CNRS Nantes University UFIP UFIP
home |  start a new run |  job status |  references&downloads |  examples |  help  

Should you encounter any unexpected behaviour,
please let us know.


***  4xv2su  ***

elNémo ID: 20012722011710675

Job options:

ID        	=	 20012722011710675
JOBID     	=	 4xv2su
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER 4xv2su

HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       26-JAN-15   4XV2              
TITLE     B-RAF KINASE V600E ONCOGENIC MUTANT IN COMPLEX WITH DABRAFENIB        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE B-RAF;                     
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 444-705;                                      
COMPND   5 SYNONYM: PROTO-ONCOGENE B-RAF,P94,V-RAF MURINE SARCOMA VIRAL ONCOGENE
COMPND   6 HOMOLOG B1;                                                          
COMPND   7 EC: 2.7.11.1;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: BRAF, BRAF1, RAFB1;                                            
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    B-RAF, BRAF, PROTO-ONCOGENE, V600E, KINASE, TRANSFERASE, TRANSFERASE- 
KEYWDS   2 TRANSFERASE INHIBITOR COMPLEX                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.ZHANG,C.ZHANG                                                       
REVDAT   2   04-NOV-15 4XV2    1       JRNL                                     
REVDAT   1   28-OCT-15 4XV2    0                                                
JRNL        AUTH   C.ZHANG,W.SPEVAK,Y.ZHANG,E.A.BURTON,Y.MA,G.HABETS,J.ZHANG,   
JRNL        AUTH 2 J.LIN,T.EWING,B.MATUSOW,G.TSANG,A.MARIMUTHU,H.CHO,G.WU,      
JRNL        AUTH 3 W.WANG,D.FONG,H.NGUYEN,S.SHI,P.WOMACK,M.NESPI,R.SHELLOOE,    
JRNL        AUTH 4 H.CARIAS,B.POWELL,E.LIGHT,L.SANFTNER,J.WALTERS,J.TSAI,       
JRNL        AUTH 5 B.L.WEST,G.VISOR,H.REZAEI,P.S.LIN,K.NOLOP,P.N.IBRAHIM,       
JRNL        AUTH 6 P.HIRTH,G.BOLLAG                                             
JRNL        TITL   RAF INHIBITORS THAT EVADE PARADOXICAL MAPK PATHWAY           
JRNL        TITL 2 ACTIVATION.                                                  
JRNL        REF    NATURE                        V. 526   583 2015              
JRNL        REFN                   ESSN 1476-4687                               
JRNL        PMID   26466569                                                     
JRNL        DOI    10.1038/NATURE14982                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7.3_928)                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 54.87                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.390                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 22263                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.213                           
REMARK   3   R VALUE            (WORKING SET) : 0.212                           
REMARK   3   FREE R VALUE                     : 0.244                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.070                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1128                            
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 54.8650 -  4.9989    1.00     2796   152  0.2160 0.2519        
REMARK   3     2  4.9989 -  3.9682    1.00     2664   144  0.1801 0.1962        
REMARK   3     3  3.9682 -  3.4667    1.00     2663   130  0.1974 0.2437        
REMARK   3     4  3.4667 -  3.1497    1.00     2611   139  0.2051 0.2447        
REMARK   3     5  3.1497 -  2.9240    1.00     2616   150  0.2265 0.2579        
REMARK   3     6  2.9240 -  2.7516    1.00     2596   148  0.2550 0.3062        
REMARK   3     7  2.7516 -  2.6138    1.00     2586   142  0.2642 0.3043        
REMARK   3     8  2.6138 -  2.5000    1.00     2603   123  0.2815 0.2996        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.20                                          
REMARK   3   SHRINKAGE RADIUS   : 0.98                                          
REMARK   3   K_SOL              : 0.37                                          
REMARK   3   B_SOL              : 47.58                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.370            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.760           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 11.26670                                             
REMARK   3    B22 (A**2) : -7.02730                                             
REMARK   3    B33 (A**2) : -4.23940                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.003           4126                                  
REMARK   3   ANGLE     :  0.737           5566                                  
REMARK   3   CHIRALITY :  0.055            592                                  
REMARK   3   PLANARITY :  0.004            704                                  
REMARK   3   DIHEDRAL  : 14.540           1558                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 449:720 )                           
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.4403 -13.3113 -19.2223              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3285 T22:   0.3061                                     
REMARK   3      T33:   0.3024 T12:  -0.0479                                     
REMARK   3      T13:  -0.0193 T23:   0.0104                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7427 L22:   6.2547                                     
REMARK   3      L33:   3.9506 L12:  -0.5449                                     
REMARK   3      L13:  -0.4682 L23:   2.7399                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0127 S12:   0.0365 S13:  -0.3618                       
REMARK   3      S21:   0.5493 S22:  -0.0245 S23:  -0.1486                       
REMARK   3      S31:   0.4846 S32:  -0.0320 S33:   0.0385                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 448:720 )                           
REMARK   3    ORIGIN FOR THE GROUP (A):   0.7577   7.9485   5.5081              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3871 T22:   0.4416                                     
REMARK   3      T33:   0.2500 T12:   0.0811                                     
REMARK   3      T13:   0.0344 T23:   0.0373                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6207 L22:   4.8358                                     
REMARK   3      L33:   4.1836 L12:   2.2658                                     
REMARK   3      L13:   0.9079 L23:   1.1296                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0027 S12:  -0.4891 S13:  -0.0371                       
REMARK   3      S21:   0.3213 S22:  -0.2003 S23:  -0.0606                       
REMARK   3      S31:   0.3440 S32:  -0.0670 S33:   0.2063                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 801:801 )                           
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.5092  -3.2835 -20.7253              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3636 T22:   0.4194                                     
REMARK   3      T33:   0.2711 T12:   0.0011                                     
REMARK   3      T13:   0.0513 T23:   0.0134                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0576 L22:   3.4588                                     
REMARK   3      L33:   2.7440 L12:   0.8256                                     
REMARK   3      L13:   1.7006 L23:   1.5510                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5433 S12:  -0.0539 S13:  -0.3070                       
REMARK   3      S21:  -0.0754 S22:  -0.1060 S23:  -0.2429                       
REMARK   3      S31:   0.0649 S32:  -0.1633 S33:  -0.3565                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 801:801 )                           
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.9137  -0.9333   6.1428              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5012 T22:   0.5564                                     
REMARK   3      T33:   0.2160 T12:   0.0473                                     
REMARK   3      T13:   0.0268 T23:  -0.0441                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3180 L22:   2.8541                                     
REMARK   3      L33:   3.6726 L12:   0.7945                                     
REMARK   3      L13:  -0.9801 L23:   2.0533                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2904 S12:  -0.0502 S13:   0.0294                       
REMARK   3      S21:  -0.1245 S22:   0.3059 S23:  -0.0906                       
REMARK   3      S31:   0.3893 S32:   0.1840 S33:  -0.5266                       
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 4XV2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JAN-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000206348.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-DEC-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.3.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.11587                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22321                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 76.114                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 6.100                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 8.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.64                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.37                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BISTRIS AT PH 6.0, 12.5% 2,5-       
REMARK 280  HEXABEDIOL, 12% PEG3350, VAPOR DIFFUSION, SITTING DROP,             
REMARK 280  TEMPERATURE 277K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       26.84450            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       54.86550            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.83300            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       54.86550            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       26.84450            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.83300            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   432                                                      
REMARK 465     LYS A   433                                                      
REMARK 465     LYS A   434                                                      
REMARK 465     GLY A   435                                                      
REMARK 465     HIS A   436                                                      
REMARK 465     HIS A   437                                                      
REMARK 465     HIS A   438                                                      
REMARK 465     HIS A   439                                                      
REMARK 465     HIS A   440                                                      
REMARK 465     HIS A   441                                                      
REMARK 465     GLY A   442                                                      
REMARK 465     SER A   443                                                      
REMARK 465     ARG A   444                                                      
REMARK 465     ASP A   445                                                      
REMARK 465     ALA A   446                                                      
REMARK 465     ALA A   447                                                      
REMARK 465     ASP A   448                                                      
REMARK 465     THR A   488                                                      
REMARK 465     ALA A   489                                                      
REMARK 465     LEU A   597                                                      
REMARK 465     ALA A   598                                                      
REMARK 465     THR A   599                                                      
REMARK 465     GLU A   600                                                      
REMARK 465     LYS A   601                                                      
REMARK 465     SER A   602                                                      
REMARK 465     ARG A   603                                                      
REMARK 465     TRP A   604                                                      
REMARK 465     SER A   605                                                      
REMARK 465     GLY A   606                                                      
REMARK 465     SER A   607                                                      
REMARK 465     HIS A   608                                                      
REMARK 465     GLN A   609                                                      
REMARK 465     PHE A   610                                                      
REMARK 465     GLU A   611                                                      
REMARK 465     GLN A   612                                                      
REMARK 465     LEU A   613                                                      
REMARK 465     SER A   614                                                      
REMARK 465     MET A   627                                                      
REMARK 465     GLN A   628                                                      
REMARK 465     ASP A   629                                                      
REMARK 465     SER A   630                                                      
REMARK 465     ASN A   631                                                      
REMARK 465     LEU A   721                                                      
REMARK 465     SER A   722                                                      
REMARK 465     GLY A   723                                                      
REMARK 465     MET B   432                                                      
REMARK 465     LYS B   433                                                      
REMARK 465     LYS B   434                                                      
REMARK 465     GLY B   435                                                      
REMARK 465     HIS B   436                                                      
REMARK 465     HIS B   437                                                      
REMARK 465     HIS B   438                                                      
REMARK 465     HIS B   439                                                      
REMARK 465     HIS B   440                                                      
REMARK 465     HIS B   441                                                      
REMARK 465     GLY B   442                                                      
REMARK 465     SER B   443                                                      
REMARK 465     ARG B   444                                                      
REMARK 465     ASP B   445                                                      
REMARK 465     ALA B   446                                                      
REMARK 465     ALA B   447                                                      
REMARK 465     THR B   546                                                      
REMARK 465     LYS B   547                                                      
REMARK 465     LEU B   597                                                      
REMARK 465     ALA B   598                                                      
REMARK 465     THR B   599                                                      
REMARK 465     GLU B   600                                                      
REMARK 465     LYS B   601                                                      
REMARK 465     SER B   602                                                      
REMARK 465     ARG B   603                                                      
REMARK 465     TRP B   604                                                      
REMARK 465     SER B   605                                                      
REMARK 465     GLY B   606                                                      
REMARK 465     SER B   607                                                      
REMARK 465     HIS B   608                                                      
REMARK 465     GLN B   609                                                      
REMARK 465     PHE B   610                                                      
REMARK 465     GLU B   611                                                      
REMARK 465     GLN B   612                                                      
REMARK 465     LEU B   613                                                      
REMARK 465     SER B   614                                                      
REMARK 465     MET B   627                                                      
REMARK 465     GLN B   628                                                      
REMARK 465     ASP B   629                                                      
REMARK 465     SER B   630                                                      
REMARK 465     LEU B   721                                                      
REMARK 465     SER B   722                                                      
REMARK 465     GLY B   723                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 522    CG   CD   CE   NZ                                   
REMARK 470     LYS B 522    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    TRP A 476       93.44   -168.99                                   
REMARK 500    ASN A 486       80.13    -65.06                                   
REMARK 500    ARG A 575       -8.24     74.38                                   
REMARK 500    ASP A 576       36.83   -153.59                                   
REMARK 500    ASP A 587       -1.02     68.45                                   
REMARK 500    TRP B 476       96.79   -161.92                                   
REMARK 500    ARG B 575       -8.52     77.27                                   
REMARK 500    ASP B 576       39.19   -150.51                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue P06 A 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue P06 B 801                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4K04   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4K0I   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4K16   RELATED DB: PDB                                   
DBREF  4XV2 A  444   705  UNP    P15056   BRAF_HUMAN     444    705             
DBREF  4XV2 B  444   705  UNP    P15056   BRAF_HUMAN     444    705             
SEQADV 4XV2 MET A  432  UNP  P15056              EXPRESSION TAG                 
SEQADV 4XV2 LYS A  433  UNP  P15056              EXPRESSION TAG                 
SEQADV 4XV2 LYS A  434  UNP  P15056              EXPRESSION TAG                 
SEQADV 4XV2 GLY A  435  UNP  P15056              EXPRESSION TAG                 
SEQADV 4XV2 HIS A  436  UNP  P15056              EXPRESSION TAG                 
SEQADV 4XV2 HIS A  437  UNP  P15056              EXPRESSION TAG                 
SEQADV 4XV2 HIS A  438  UNP  P15056              EXPRESSION TAG                 
SEQADV 4XV2 HIS A  439  UNP  P15056              EXPRESSION TAG                 
SEQADV 4XV2 HIS A  440  UNP  P15056              EXPRESSION TAG                 
SEQADV 4XV2 HIS A  441  UNP  P15056              EXPRESSION TAG                 
SEQADV 4XV2 GLY A  442  UNP  P15056              EXPRESSION TAG                 
SEQADV 4XV2 SER A  443  UNP  P15056              EXPRESSION TAG                 
SEQADV 4XV2 ALA A  446  UNP  P15056    SER   446 ENGINEERED MUTATION            
SEQADV 4XV2 ALA A  447  UNP  P15056    SER   447 ENGINEERED MUTATION            
SEQADV 4XV2 ALA A  543  UNP  P15056    ILE   543 ENGINEERED MUTATION            
SEQADV 4XV2 SER A  544  UNP  P15056    ILE   544 ENGINEERED MUTATION            
SEQADV 4XV2 LYS A  551  UNP  P15056    ILE   551 ENGINEERED MUTATION            
SEQADV 4XV2 ARG A  562  UNP  P15056    GLN   562 ENGINEERED MUTATION            
SEQADV 4XV2 ASN A  588  UNP  P15056    LEU   588 ENGINEERED MUTATION            
SEQADV 4XV2 GLU A  600  UNP  P15056    VAL   600 ENGINEERED MUTATION            
SEQADV 4XV2 SER A  630  UNP  P15056    LYS   630 ENGINEERED MUTATION            
SEQADV 4XV2 GLU A  667  UNP  P15056    PHE   667 ENGINEERED MUTATION            
SEQADV 4XV2 SER A  673  UNP  P15056    TYR   673 ENGINEERED MUTATION            
SEQADV 4XV2 ARG A  688  UNP  P15056    ALA   688 ENGINEERED MUTATION            
SEQADV 4XV2 SER A  706  UNP  P15056              EXPRESSION TAG                 
SEQADV 4XV2 PHE A  707  UNP  P15056              EXPRESSION TAG                 
SEQADV 4XV2 PRO A  708  UNP  P15056              EXPRESSION TAG                 
SEQADV 4XV2 ARG A  709  UNP  P15056              EXPRESSION TAG                 
SEQADV 4XV2 ILE A  710  UNP  P15056              EXPRESSION TAG                 
SEQADV 4XV2 LEU A  711  UNP  P15056              EXPRESSION TAG                 
SEQADV 4XV2 ALA A  712  UNP  P15056              EXPRESSION TAG                 
SEQADV 4XV2 GLU A  713  UNP  P15056              EXPRESSION TAG                 
SEQADV 4XV2 ILE A  714  UNP  P15056              EXPRESSION TAG                 
SEQADV 4XV2 GLU A  715  UNP  P15056              EXPRESSION TAG                 
SEQADV 4XV2 GLU A  716  UNP  P15056              EXPRESSION TAG                 
SEQADV 4XV2 LEU A  717  UNP  P15056              EXPRESSION TAG                 
SEQADV 4XV2 ALA A  718  UNP  P15056              EXPRESSION TAG                 
SEQADV 4XV2 ARG A  719  UNP  P15056              EXPRESSION TAG                 
SEQADV 4XV2 GLU A  720  UNP  P15056              EXPRESSION TAG                 
SEQADV 4XV2 LEU A  721  UNP  P15056              EXPRESSION TAG                 
SEQADV 4XV2 SER A  722  UNP  P15056              EXPRESSION TAG                 
SEQADV 4XV2 GLY A  723  UNP  P15056              EXPRESSION TAG                 
SEQADV 4XV2 MET B  432  UNP  P15056              EXPRESSION TAG                 
SEQADV 4XV2 LYS B  433  UNP  P15056              EXPRESSION TAG                 
SEQADV 4XV2 LYS B  434  UNP  P15056              EXPRESSION TAG                 
SEQADV 4XV2 GLY B  435  UNP  P15056              EXPRESSION TAG                 
SEQADV 4XV2 HIS B  436  UNP  P15056              EXPRESSION TAG                 
SEQADV 4XV2 HIS B  437  UNP  P15056              EXPRESSION TAG                 
SEQADV 4XV2 HIS B  438  UNP  P15056              EXPRESSION TAG                 
SEQADV 4XV2 HIS B  439  UNP  P15056              EXPRESSION TAG                 
SEQADV 4XV2 HIS B  440  UNP  P15056              EXPRESSION TAG                 
SEQADV 4XV2 HIS B  441  UNP  P15056              EXPRESSION TAG                 
SEQADV 4XV2 GLY B  442  UNP  P15056              EXPRESSION TAG                 
SEQADV 4XV2 SER B  443  UNP  P15056              EXPRESSION TAG                 
SEQADV 4XV2 ALA B  446  UNP  P15056    SER   446 ENGINEERED MUTATION            
SEQADV 4XV2 ALA B  447  UNP  P15056    SER   447 ENGINEERED MUTATION            
SEQADV 4XV2 ALA B  543  UNP  P15056    ILE   543 ENGINEERED MUTATION            
SEQADV 4XV2 SER B  544  UNP  P15056    ILE   544 ENGINEERED MUTATION            
SEQADV 4XV2 LYS B  551  UNP  P15056    ILE   551 ENGINEERED MUTATION            
SEQADV 4XV2 ARG B  562  UNP  P15056    GLN   562 ENGINEERED MUTATION            
SEQADV 4XV2 ASN B  588  UNP  P15056    LEU   588 ENGINEERED MUTATION            
SEQADV 4XV2 GLU B  600  UNP  P15056    VAL   600 ENGINEERED MUTATION            
SEQADV 4XV2 SER B  630  UNP  P15056    LYS   630 ENGINEERED MUTATION            
SEQADV 4XV2 GLU B  667  UNP  P15056    PHE   667 ENGINEERED MUTATION            
SEQADV 4XV2 SER B  673  UNP  P15056    TYR   673 ENGINEERED MUTATION            
SEQADV 4XV2 ARG B  688  UNP  P15056    ALA   688 ENGINEERED MUTATION            
SEQADV 4XV2 SER B  706  UNP  P15056              EXPRESSION TAG                 
SEQADV 4XV2 PHE B  707  UNP  P15056              EXPRESSION TAG                 
SEQADV 4XV2 PRO B  708  UNP  P15056              EXPRESSION TAG                 
SEQADV 4XV2 ARG B  709  UNP  P15056              EXPRESSION TAG                 
SEQADV 4XV2 ILE B  710  UNP  P15056              EXPRESSION TAG                 
SEQADV 4XV2 LEU B  711  UNP  P15056              EXPRESSION TAG                 
SEQADV 4XV2 ALA B  712  UNP  P15056              EXPRESSION TAG                 
SEQADV 4XV2 GLU B  713  UNP  P15056              EXPRESSION TAG                 
SEQADV 4XV2 ILE B  714  UNP  P15056              EXPRESSION TAG                 
SEQADV 4XV2 GLU B  715  UNP  P15056              EXPRESSION TAG                 
SEQADV 4XV2 GLU B  716  UNP  P15056              EXPRESSION TAG                 
SEQADV 4XV2 LEU B  717  UNP  P15056              EXPRESSION TAG                 
SEQADV 4XV2 ALA B  718  UNP  P15056              EXPRESSION TAG                 
SEQADV 4XV2 ARG B  719  UNP  P15056              EXPRESSION TAG                 
SEQADV 4XV2 GLU B  720  UNP  P15056              EXPRESSION TAG                 
SEQADV 4XV2 LEU B  721  UNP  P15056              EXPRESSION TAG                 
SEQADV 4XV2 SER B  722  UNP  P15056              EXPRESSION TAG                 
SEQADV 4XV2 GLY B  723  UNP  P15056              EXPRESSION TAG                 
SEQRES   1 A  292  MET LYS LYS GLY HIS HIS HIS HIS HIS HIS GLY SER ARG          
SEQRES   2 A  292  ASP ALA ALA ASP ASP TRP GLU ILE PRO ASP GLY GLN ILE          
SEQRES   3 A  292  THR VAL GLY GLN ARG ILE GLY SER GLY SER PHE GLY THR          
SEQRES   4 A  292  VAL TYR LYS GLY LYS TRP HIS GLY ASP VAL ALA VAL LYS          
SEQRES   5 A  292  MET LEU ASN VAL THR ALA PRO THR PRO GLN GLN LEU GLN          
SEQRES   6 A  292  ALA PHE LYS ASN GLU VAL GLY VAL LEU ARG LYS THR ARG          
SEQRES   7 A  292  HIS VAL ASN ILE LEU LEU PHE MET GLY TYR SER THR LYS          
SEQRES   8 A  292  PRO GLN LEU ALA ILE VAL THR GLN TRP CYS GLU GLY SER          
SEQRES   9 A  292  SER LEU TYR HIS HIS LEU HIS ALA SER GLU THR LYS PHE          
SEQRES  10 A  292  GLU MET LYS LYS LEU ILE ASP ILE ALA ARG GLN THR ALA          
SEQRES  11 A  292  ARG GLY MET ASP TYR LEU HIS ALA LYS SER ILE ILE HIS          
SEQRES  12 A  292  ARG ASP LEU LYS SER ASN ASN ILE PHE LEU HIS GLU ASP          
SEQRES  13 A  292  ASN THR VAL LYS ILE GLY ASP PHE GLY LEU ALA THR GLU          
SEQRES  14 A  292  LYS SER ARG TRP SER GLY SER HIS GLN PHE GLU GLN LEU          
SEQRES  15 A  292  SER GLY SER ILE LEU TRP MET ALA PRO GLU VAL ILE ARG          
SEQRES  16 A  292  MET GLN ASP SER ASN PRO TYR SER PHE GLN SER ASP VAL          
SEQRES  17 A  292  TYR ALA PHE GLY ILE VAL LEU TYR GLU LEU MET THR GLY          
SEQRES  18 A  292  GLN LEU PRO TYR SER ASN ILE ASN ASN ARG ASP GLN ILE          
SEQRES  19 A  292  ILE GLU MET VAL GLY ARG GLY SER LEU SER PRO ASP LEU          
SEQRES  20 A  292  SER LYS VAL ARG SER ASN CYS PRO LYS ARG MET LYS ARG          
SEQRES  21 A  292  LEU MET ALA GLU CYS LEU LYS LYS LYS ARG ASP GLU ARG          
SEQRES  22 A  292  PRO SER PHE PRO ARG ILE LEU ALA GLU ILE GLU GLU LEU          
SEQRES  23 A  292  ALA ARG GLU LEU SER GLY                                      
SEQRES   1 B  292  MET LYS LYS GLY HIS HIS HIS HIS HIS HIS GLY SER ARG          
SEQRES   2 B  292  ASP ALA ALA ASP ASP TRP GLU ILE PRO ASP GLY GLN ILE          
SEQRES   3 B  292  THR VAL GLY GLN ARG ILE GLY SER GLY SER PHE GLY THR          
SEQRES   4 B  292  VAL TYR LYS GLY LYS TRP HIS GLY ASP VAL ALA VAL LYS          
SEQRES   5 B  292  MET LEU ASN VAL THR ALA PRO THR PRO GLN GLN LEU GLN          
SEQRES   6 B  292  ALA PHE LYS ASN GLU VAL GLY VAL LEU ARG LYS THR ARG          
SEQRES   7 B  292  HIS VAL ASN ILE LEU LEU PHE MET GLY TYR SER THR LYS          
SEQRES   8 B  292  PRO GLN LEU ALA ILE VAL THR GLN TRP CYS GLU GLY SER          
SEQRES   9 B  292  SER LEU TYR HIS HIS LEU HIS ALA SER GLU THR LYS PHE          
SEQRES  10 B  292  GLU MET LYS LYS LEU ILE ASP ILE ALA ARG GLN THR ALA          
SEQRES  11 B  292  ARG GLY MET ASP TYR LEU HIS ALA LYS SER ILE ILE HIS          
SEQRES  12 B  292  ARG ASP LEU LYS SER ASN ASN ILE PHE LEU HIS GLU ASP          
SEQRES  13 B  292  ASN THR VAL LYS ILE GLY ASP PHE GLY LEU ALA THR GLU          
SEQRES  14 B  292  LYS SER ARG TRP SER GLY SER HIS GLN PHE GLU GLN LEU          
SEQRES  15 B  292  SER GLY SER ILE LEU TRP MET ALA PRO GLU VAL ILE ARG          
SEQRES  16 B  292  MET GLN ASP SER ASN PRO TYR SER PHE GLN SER ASP VAL          
SEQRES  17 B  292  TYR ALA PHE GLY ILE VAL LEU TYR GLU LEU MET THR GLY          
SEQRES  18 B  292  GLN LEU PRO TYR SER ASN ILE ASN ASN ARG ASP GLN ILE          
SEQRES  19 B  292  ILE GLU MET VAL GLY ARG GLY SER LEU SER PRO ASP LEU          
SEQRES  20 B  292  SER LYS VAL ARG SER ASN CYS PRO LYS ARG MET LYS ARG          
SEQRES  21 B  292  LEU MET ALA GLU CYS LEU LYS LYS LYS ARG ASP GLU ARG          
SEQRES  22 B  292  PRO SER PHE PRO ARG ILE LEU ALA GLU ILE GLU GLU LEU          
SEQRES  23 B  292  ALA ARG GLU LEU SER GLY                                      
HET    P06  A 801      35                                                       
HET    P06  B 801      35                                                       
HETNAM     P06 DABRAFENIB                                                       
HETSYN     P06 N-{3-[5-(2-AMINOPYRIMIDIN-4-YL)-2-TERT-BUTYL-1,3-                
HETSYN   2 P06  THIAZOL-4-YL]-2-FLUOROPHENYL}-2,6-                              
HETSYN   3 P06  DIFLUOROBENZENESULFONAMIDE                                      
FORMUL   3  P06    2(C23 H20 F3 N5 O2 S2)                                       
FORMUL   5  HOH   *54(H2 O)                                                     
HELIX    1 AA1 THR A  491  ARG A  506  1                                  16    
HELIX    2 AA2 SER A  536  ALA A  543  1                                   8    
HELIX    3 AA3 GLU A  549  LYS A  570  1                                  22    
HELIX    4 AA4 GLU A  586  ASN A  588  5                                   3    
HELIX    5 AA5 ALA A  621  ARG A  626  1                                   6    
HELIX    6 AA6 SER A  634  GLY A  652  1                                  19    
HELIX    7 AA7 ASN A  661  ARG A  671  1                                  11    
HELIX    8 AA8 ASP A  677  VAL A  681  5                                   5    
HELIX    9 AA9 PRO A  686  LEU A  697  1                                  12    
HELIX   10 AB1 LYS A  700  ARG A  704  5                                   5    
HELIX   11 AB2 SER A  706  ALA A  718  1                                  13    
HELIX   12 AB3 THR B  491  ARG B  506  1                                  16    
HELIX   13 AB4 SER B  536  ALA B  543  1                                   8    
HELIX   14 AB5 GLU B  549  LYS B  570  1                                  22    
HELIX   15 AB6 GLU B  586  ASN B  588  5                                   3    
HELIX   16 AB7 GLY B  615  MET B  620  5                                   6    
HELIX   17 AB8 ALA B  621  ARG B  626  1                                   6    
HELIX   18 AB9 SER B  634  GLY B  652  1                                  19    
HELIX   19 AC1 ASN B  661  ARG B  671  1                                  11    
HELIX   20 AC2 ASP B  677  VAL B  681  5                                   5    
HELIX   21 AC3 PRO B  686  LEU B  697  1                                  12    
HELIX   22 AC4 LYS B  700  ARG B  704  5                                   5    
HELIX   23 AC5 SER B  706  GLU B  720  1                                  15    
SHEET    1 AA1 5 THR A 458  SER A 465  0                                        
SHEET    2 AA1 5 THR A 470  LYS A 475 -1  O  VAL A 471   N  ILE A 463           
SHEET    3 AA1 5 ASP A 479  MET A 484 -1  O  MET A 484   N  THR A 470           
SHEET    4 AA1 5 ALA A 526  GLN A 530 -1  O  ILE A 527   N  LYS A 483           
SHEET    5 AA1 5 PHE A 516  SER A 520 -1  N  GLY A 518   O  VAL A 528           
SHEET    1 AA2 2 ILE A 582  HIS A 585  0                                        
SHEET    2 AA2 2 THR A 589  ILE A 592 -1  O  LYS A 591   N  PHE A 583           
SHEET    1 AA3 5 THR B 458  SER B 465  0                                        
SHEET    2 AA3 5 THR B 470  LYS B 475 -1  O  VAL B 471   N  ILE B 463           
SHEET    3 AA3 5 ASP B 479  LEU B 485 -1  O  VAL B 480   N  GLY B 474           
SHEET    4 AA3 5 LEU B 525  GLN B 530 -1  O  THR B 529   N  ALA B 481           
SHEET    5 AA3 5 PHE B 516  SER B 520 -1  N  GLY B 518   O  VAL B 528           
SHEET    1 AA4 2 ILE B 582  HIS B 585  0                                        
SHEET    2 AA4 2 THR B 589  ILE B 592 -1  O  THR B 589   N  HIS B 585           
CISPEP   1 LYS A  522    PRO A  523          0         4.96                     
CISPEP   2 LYS B  522    PRO B  523          0        -1.13                     
SITE     1 AC1 18 GLY A 464  SER A 465  PHE A 468  VAL A 471                    
SITE     2 AC1 18 ALA A 481  LYS A 483  LEU A 505  LEU A 514                    
SITE     3 AC1 18 ILE A 527  THR A 529  GLN A 530  TRP A 531                    
SITE     4 AC1 18 CYS A 532  PHE A 583  GLY A 593  ASP A 594                    
SITE     5 AC1 18 PHE A 595  HOH A 913                                          
SITE     1 AC2 18 SER B 465  GLY B 466  PHE B 468  VAL B 471                    
SITE     2 AC2 18 ALA B 481  LYS B 483  LEU B 505  LEU B 514                    
SITE     3 AC2 18 PHE B 516  ILE B 527  THR B 529  GLN B 530                    
SITE     4 AC2 18 TRP B 531  CYS B 532  GLY B 593  ASP B 594                    
SITE     5 AC2 18 PHE B 595  HOH B 913                                          
CRYST1   53.689  105.666  109.731  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.018626  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009464  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009113        0.00000                         
ATOM      1  N   ASP A 449     -16.130   8.418 -11.336  1.00 70.53           N  
ANISOU    1  N   ASP A 449     8482   9430   8885   1228    819  -1701       N  
ATOM      2  CA  ASP A 449     -15.729   8.054 -12.689  1.00 68.64           C  
ANISOU    2  CA  ASP A 449     8217   9220   8642   1303    514  -1572       C  
ATOM      3  C   ASP A 449     -14.210   8.112 -12.823  1.00 59.67           C  
ANISOU    3  C   ASP A 449     7475   7953   7245   1150    419  -1247       C  
ATOM      4  O   ASP A 449     -13.531   8.780 -12.043  1.00 56.49           O  
ANISOU    4  O   ASP A 449     7364   7416   6683   1078    493  -1147       O  
ATOM      5  CB  ASP A 449     -16.404   8.969 -13.716  1.00 73.37           C  
ANISOU    5  CB  ASP A 449     8730   9801   9347   1706    211  -1703       C  
ATOM      6  CG  ASP A 449     -16.532   8.320 -15.087  1.00 75.20           C  
ANISOU    6  CG  ASP A 449     8804  10126   9641   1807    -64  -1699       C  
ATOM      7  OD1 ASP A 449     -16.318   7.090 -15.191  1.00 72.34           O  
ANISOU    7  OD1 ASP A 449     8302   9874   9311   1558     20  -1655       O  
ATOM      8  OD2 ASP A 449     -16.858   9.038 -16.057  1.00 77.30           O  
ANISOU    8  OD2 ASP A 449     9121  10342   9908   2149   -373  -1746       O  
ATOM      9  N   TRP A 450     -13.679   7.407 -13.813  1.00 53.33           N  
ANISOU    9  N   TRP A 450     6658   7188   6416   1098    257  -1112       N  
ATOM     10  CA  TRP A 450     -12.237   7.287 -13.956  1.00 47.24           C  
ANISOU   10  CA  TRP A 450     6180   6317   5454    925    203   -847       C  
ATOM     11  C   TRP A 450     -11.725   7.980 -15.208  1.00 44.20           C  
ANISOU   11  C   TRP A 450     5987   5823   4983   1096    -38   -727       C  
ATOM     12  O   TRP A 450     -10.638   7.675 -15.696  1.00 42.61           O  
ANISOU   12  O   TRP A 450     5939   5570   4679    959    -85   -545       O  
ATOM     13  CB  TRP A 450     -11.828   5.813 -13.936  1.00 45.35           C  
ANISOU   13  CB  TRP A 450     5829   6177   5226    675    278   -771       C  
ATOM     14  CG  TRP A 450     -12.264   5.111 -12.683  1.00 46.26           C  
ANISOU   14  CG  TRP A 450     5858   6346   5373    486    550   -860       C  
ATOM     15  CD1 TRP A 450     -13.414   4.401 -12.500  1.00 47.85           C  
ANISOU   15  CD1 TRP A 450     5758   6669   5755    452    716  -1063       C  
ATOM     16  CD2 TRP A 450     -11.565   5.069 -11.434  1.00 43.42           C  
ANISOU   16  CD2 TRP A 450     5750   5900   4848    301    700   -764       C  
ATOM     17  NE1 TRP A 450     -13.471   3.913 -11.219  1.00 47.71           N  
ANISOU   17  NE1 TRP A 450     5830   6625   5672    239   1007  -1077       N  
ATOM     18  CE2 TRP A 450     -12.347   4.311 -10.542  1.00 44.48           C  
ANISOU   18  CE2 TRP A 450     5783   6090   5029    164    977   -888       C  
ATOM     19  CE3 TRP A 450     -10.349   5.592 -10.984  1.00 39.42           C  
ANISOU   19  CE3 TRP A 450     5552   5267   4160    235    622   -605       C  
ATOM     20  CZ2 TRP A 450     -11.954   4.063  -9.230  1.00 41.91           C  
ANISOU   20  CZ2 TRP A 450     5721   5682   4519    -11   1165   -830       C  
ATOM     21  CZ3 TRP A 450      -9.962   5.347  -9.683  1.00 37.42           C  
ANISOU   21  CZ3 TRP A 450     5506   4957   3755     78    759   -575       C  
ATOM     22  CH2 TRP A 450     -10.760   4.589  -8.821  1.00 38.92           C  
ANISOU   22  CH2 TRP A 450     5656   5189   3941    -32   1022   -672       C  
ATOM     23  N   GLU A 451     -12.508   8.921 -15.724  1.00 45.82           N  
ANISOU   23  N   GLU A 451     6207   5977   5227   1403   -179   -839       N  
ATOM     24  CA  GLU A 451     -12.071   9.698 -16.874  1.00 46.23           C  
ANISOU   24  CA  GLU A 451     6549   5872   5146   1586   -387   -715       C  
ATOM     25  C   GLU A 451     -11.044  10.749 -16.469  1.00 42.69           C  
ANISOU   25  C   GLU A 451     6486   5192   4541   1498   -315   -561       C  
ATOM     26  O   GLU A 451     -11.259  11.524 -15.536  1.00 44.83           O  
ANISOU   26  O   GLU A 451     6827   5385   4822   1530   -222   -635       O  
ATOM     27  CB  GLU A 451     -13.247  10.355 -17.593  1.00 53.40           C  
ANISOU   27  CB  GLU A 451     7400   6770   6121   1990   -611   -887       C  
ATOM     28  CG  GLU A 451     -12.816  11.152 -18.816  1.00 62.12           C  
ANISOU   28  CG  GLU A 451     8908   7668   7027   2198   -824   -738       C  
ATOM     29  CD  GLU A 451     -13.983  11.605 -19.662  1.00 72.10           C  
ANISOU   29  CD  GLU A 451    10131   8931   8332   2642  -1126   -912       C  
ATOM     30  OE1 GLU A 451     -15.138  11.303 -19.292  1.00 75.71           O  
ANISOU   30  OE1 GLU A 451    10170   9571   9026   2780  -1168  -1181       O  
ATOM     31  OE2 GLU A 451     -13.745  12.262 -20.699  1.00 75.84           O  
ANISOU   31  OE2 GLU A 451    11002   9210   8603   2858  -1320   -794       O  
ATOM     32  N   ILE A 452      -9.921  10.755 -17.175  1.00 39.01           N  
ANISOU   32  N   ILE A 452     6259   4614   3947   1370   -337   -369       N  
ATOM     33  CA  ILE A 452      -8.875  11.734 -16.947  1.00 39.02           C  
ANISOU   33  CA  ILE A 452     6609   4383   3835   1252   -259   -247       C  
ATOM     34  C   ILE A 452      -8.979  12.836 -17.992  1.00 43.46           C  
ANISOU   34  C   ILE A 452     7532   4711   4271   1498   -375   -187       C  
ATOM     35  O   ILE A 452      -8.779  12.591 -19.182  1.00 45.60           O  
ANISOU   35  O   ILE A 452     7928   4949   4449   1555   -461    -95       O  
ATOM     36  CB  ILE A 452      -7.487  11.087 -17.022  1.00 38.82           C  
ANISOU   36  CB  ILE A 452     6609   4360   3782    928   -166   -106       C  
ATOM     37  CG1 ILE A 452      -7.385   9.947 -16.005  1.00 38.57           C  
ANISOU   37  CG1 ILE A 452     6286   4529   3841    725    -88   -152       C  
ATOM     38  CG2 ILE A 452      -6.403  12.125 -16.790  1.00 38.75           C  
ANISOU   38  CG2 ILE A 452     6910   4109   3706    780    -75    -29       C  
ATOM     39  CD1 ILE A 452      -6.121   9.123 -16.123  1.00 36.97           C  
ANISOU   39  CD1 ILE A 452     6046   4357   3642    463    -50    -46       C  
ATOM     40  N   PRO A 453      -9.299  14.059 -17.545  1.00 45.32           N  
ANISOU   40  N   PRO A 453     7982   4759   4478   1654   -374   -239       N  
ATOM     41  CA  PRO A 453      -9.528  15.216 -18.418  1.00 47.55           C  
ANISOU   41  CA  PRO A 453     8676   4768   4623   1937   -493   -190       C  
ATOM     42  C   PRO A 453      -8.357  15.488 -19.350  1.00 47.38           C  
ANISOU   42  C   PRO A 453     9047   4524   4432   1770   -414     14       C  
ATOM     43  O   PRO A 453      -7.217  15.152 -19.037  1.00 45.34           O  
ANISOU   43  O   PRO A 453     8755   4271   4200   1410   -235     90       O  
ATOM     44  CB  PRO A 453      -9.693  16.372 -17.429  1.00 47.09           C  
ANISOU   44  CB  PRO A 453     8775   4533   4584   1997   -419   -271       C  
ATOM     45  CG  PRO A 453     -10.173  15.723 -16.182  1.00 45.29           C  
ANISOU   45  CG  PRO A 453     8128   4560   4519   1897   -330   -431       C  
ATOM     46  CD  PRO A 453      -9.462  14.408 -16.124  1.00 43.55           C  
ANISOU   46  CD  PRO A 453     7664   4551   4333   1576   -251   -353       C  
ATOM     47  N   ASP A 454      -8.657  16.088 -20.494  1.00 53.21           N  
ANISOU   47  N   ASP A 454    10163   5059   4997   2043   -549     85       N  
ATOM     48  CA  ASP A 454      -7.655  16.374 -21.511  1.00 55.70           C  
ANISOU   48  CA  ASP A 454    10920   5129   5116   1902   -433    275       C  
ATOM     49  C   ASP A 454      -6.562  17.287 -20.970  1.00 56.76           C  
ANISOU   49  C   ASP A 454    11332   4989   5245   1603   -170    343       C  
ATOM     50  O   ASP A 454      -6.843  18.329 -20.373  1.00 59.92           O  
ANISOU   50  O   ASP A 454    11921   5197   5648   1712   -168    292       O  
ATOM     51  CB  ASP A 454      -8.323  17.009 -22.734  1.00 62.56           C  
ANISOU   51  CB  ASP A 454    12248   5776   5746   2311   -644    332       C  
ATOM     52  CG  ASP A 454      -7.343  17.292 -23.862  1.00 67.98           C  
ANISOU   52  CG  ASP A 454    13470   6178   6181   2165   -479    535       C  
ATOM     53  OD1 ASP A 454      -6.228  16.729 -23.853  1.00 69.91           O  
ANISOU   53  OD1 ASP A 454    13605   6477   6481   1759   -223    603       O  
ATOM     54  OD2 ASP A 454      -7.696  18.073 -24.770  1.00 70.41           O  
ANISOU   54  OD2 ASP A 454    14127   6329   6296   2364   -559    521       O  
ATOM     55  N   GLY A 455      -5.313  16.881 -21.177  1.00 53.54           N  
ANISOU   55  N   GLY A 455    10923   4565   4853   1222     51    430       N  
ATOM     56  CA  GLY A 455      -4.172  17.688 -20.786  1.00 53.03           C  
ANISOU   56  CA  GLY A 455    11085   4243   4821    896    310    459       C  
ATOM     57  C   GLY A 455      -3.432  17.237 -19.539  1.00 49.63           C  
ANISOU   57  C   GLY A 455    10239   3998   4620    561    402    352       C  
ATOM     58  O   GLY A 455      -2.339  17.720 -19.265  1.00 51.66           O  
ANISOU   58  O   GLY A 455    10595   4083   4948    246    602    340       O  
ATOM     59  N   GLN A 456      -4.012  16.317 -18.777  1.00 46.10           N  
ANISOU   59  N   GLN A 456     9345   3884   4288    625    257    260       N  
ATOM     60  CA  GLN A 456      -3.377  15.868 -17.539  1.00 43.99           C  
ANISOU   60  CA  GLN A 456     8751   3776   4185    357    303    162       C  
ATOM     61  C   GLN A 456      -2.259  14.851 -17.769  1.00 43.09           C  
ANISOU   61  C   GLN A 456     8398   3803   4173     61    385    188       C  
ATOM     62  O   GLN A 456      -1.350  14.721 -16.950  1.00 40.74           O  
ANISOU   62  O   GLN A 456     7936   3539   4005   -196    433    111       O  
ATOM     63  CB  GLN A 456      -4.419  15.311 -16.568  1.00 38.09           C  
ANISOU   63  CB  GLN A 456     7694   3286   3492    525    164     56       C  
ATOM     64  CG  GLN A 456      -5.359  16.364 -16.012  1.00 39.96           C  
ANISOU   64  CG  GLN A 456     8101   3393   3689    770    118    -30       C  
ATOM     65  CD  GLN A 456      -6.158  15.859 -14.831  1.00 44.54           C  
ANISOU   65  CD  GLN A 456     8374   4206   4342    838     75   -168       C  
ATOM     66  OE1 GLN A 456      -6.003  14.713 -14.409  1.00 41.89           O  
ANISOU   66  OE1 GLN A 456     7738   4110   4067    696     77   -181       O  
ATOM     67  NE2 GLN A 456      -7.017  16.710 -14.287  1.00 40.83           N  
ANISOU   67  NE2 GLN A 456     8007   3646   3862   1057     58   -276       N  
ATOM     68  N   ILE A 457      -2.325  14.143 -18.892  1.00 45.05           N  
ANISOU   68  N   ILE A 457     8631   4125   4362    119    380    277       N  
ATOM     69  CA  ILE A 457      -1.358  13.095 -19.202  1.00 45.57           C  
ANISOU   69  CA  ILE A 457     8454   4331   4528   -118    457    288       C  
ATOM     70  C   ILE A 457      -0.301  13.549 -20.200  1.00 47.31           C  
ANISOU   70  C   ILE A 457     8934   4318   4723   -322    692    349       C  
ATOM     71  O   ILE A 457      -0.626  14.009 -21.290  1.00 50.38           O  
ANISOU   71  O   ILE A 457     9688   4528   4925   -186    749    452       O  
ATOM     72  CB  ILE A 457      -2.053  11.871 -19.807  1.00 46.30           C  
ANISOU   72  CB  ILE A 457     8341   4666   4585     45    330    323       C  
ATOM     73  CG1 ILE A 457      -3.096  11.311 -18.840  1.00 45.19           C  
ANISOU   73  CG1 ILE A 457     7919   4753   4497    199    160    243       C  
ATOM     74  CG2 ILE A 457      -1.032  10.811 -20.175  1.00 45.04           C  
ANISOU   74  CG2 ILE A 457     7960   4625   4530   -181    417    330       C  
ATOM     75  CD1 ILE A 457      -4.042  10.332 -19.496  1.00 45.56           C  
ANISOU   75  CD1 ILE A 457     7801   4995   4515    392     32    245       C  
ATOM     76  N   THR A 458       0.967  13.409 -19.830  1.00 47.36           N  
ANISOU   76  N   THR A 458     8760   4317   4916   -645    831    269       N  
ATOM     77  CA  THR A 458       2.057  13.701 -20.751  1.00 47.74           C  
ANISOU   77  CA  THR A 458     8975   4167   4996   -894   1117    284       C  
ATOM     78  C   THR A 458       2.586  12.414 -21.367  1.00 49.33           C  
ANISOU   78  C   THR A 458     8895   4570   5278   -980   1158    281       C  
ATOM     79  O   THR A 458       3.134  11.564 -20.672  1.00 51.21           O  
ANISOU   79  O   THR A 458     8717   5019   5720  -1093   1069    176       O  
ATOM     80  CB  THR A 458       3.220  14.418 -20.062  1.00 49.27           C  
ANISOU   80  CB  THR A 458     9108   4206   5405  -1225   1278    139       C  
ATOM     81  OG1 THR A 458       2.736  15.566 -19.353  1.00 51.07           O  
ANISOU   81  OG1 THR A 458     9580   4254   5571  -1150   1224    120       O  
ATOM     82  CG2 THR A 458       4.250  14.855 -21.102  1.00 44.16           C  
ANISOU   82  CG2 THR A 458     8676   3308   4796  -1503   1651    139       C  
ATOM     83  N   VAL A 459       2.427  12.283 -22.679  1.00 48.31           N  
ANISOU   83  N   VAL A 459     9031   4358   4968   -906   1282    393       N  
ATOM     84  CA  VAL A 459       2.825  11.074 -23.388  1.00 45.24           C  
ANISOU   84  CA  VAL A 459     8426   4142   4621   -956   1330    391       C  
ATOM     85  C   VAL A 459       4.311  11.088 -23.734  1.00 44.81           C  
ANISOU   85  C   VAL A 459     8281   3982   4763  -1315   1664    292       C  
ATOM     86  O   VAL A 459       4.829  12.078 -24.237  1.00 46.31           O  
ANISOU   86  O   VAL A 459     8811   3879   4906  -1488   1962    303       O  
ATOM     87  CB  VAL A 459       1.989  10.890 -24.664  1.00 47.63           C  
ANISOU   87  CB  VAL A 459     9070   4404   4621   -708   1301    529       C  
ATOM     88  CG1 VAL A 459       2.338   9.578 -25.356  1.00 47.70           C  
ANISOU   88  CG1 VAL A 459     8853   4603   4668   -748   1336    511       C  
ATOM     89  CG2 VAL A 459       0.509  10.942 -24.325  1.00 45.70           C  
ANISOU   89  CG2 VAL A 459     8859   4265   4240   -350    966    571       C  
ATOM     90  N   GLY A 460       4.992   9.983 -23.453  1.00 45.71           N  
ANISOU   90  N   GLY A 460     7933   4323   5111  -1425   1625    178       N  
ATOM     91  CA  GLY A 460       6.409   9.864 -23.743  1.00 46.90           C  
ANISOU   91  CA  GLY A 460     7890   4417   5514  -1746   1921     30       C  
ATOM     92  C   GLY A 460       6.668   8.863 -24.849  1.00 49.12           C  
ANISOU   92  C   GLY A 460     8126   4783   5756  -1742   2065     49       C  
ATOM     93  O   GLY A 460       5.876   8.744 -25.782  1.00 49.33           O  
ANISOU   93  O   GLY A 460     8493   4771   5478  -1552   2066    204       O  
ATOM     94  N   GLN A 461       7.773   8.133 -24.736  1.00 51.40           N  
ANISOU   94  N   GLN A 461     7990   5186   6355  -1931   2161   -130       N  
ATOM     95  CA  GLN A 461       8.211   7.235 -25.798  1.00 57.93           C  
ANISOU   95  CA  GLN A 461     8758   6066   7185  -1968   2363   -154       C  
ATOM     96  C   GLN A 461       7.229   6.094 -26.051  1.00 56.68           C  
ANISOU   96  C   GLN A 461     8578   6121   6837  -1669   2077    -34       C  
ATOM     97  O   GLN A 461       6.526   5.641 -25.143  1.00 52.39           O  
ANISOU   97  O   GLN A 461     7850   5753   6304  -1486   1714     -3       O  
ATOM     98  CB  GLN A 461       9.605   6.679 -25.490  1.00 68.23           C  
ANISOU   98  CB  GLN A 461     9541   7462   8921  -2203   2486   -415       C  
ATOM     99  CG  GLN A 461       9.604   5.446 -24.600  1.00 73.95           C  
ANISOU   99  CG  GLN A 461     9792   8473   9834  -2040   2091   -494       C  
ATOM    100  CD  GLN A 461      10.692   5.487 -23.546  1.00 81.89           C  
ANISOU  100  CD  GLN A 461    10332   9535  11249  -2196   1991   -751       C  
ATOM    101  OE1 GLN A 461      11.519   4.578 -23.454  1.00 84.62           O  
ANISOU  101  OE1 GLN A 461    10262  10012  11878  -2218   1947   -933       O  
ATOM    102  NE2 GLN A 461      10.692   6.542 -22.738  1.00 84.05           N  
ANISOU  102  NE2 GLN A 461    10674   9704  11558  -2285   1927   -786       N  
ATOM    103  N   ARG A 462       7.183   5.647 -27.301  1.00 60.00           N  
ANISOU  103  N   ARG A 462     9212   6507   7078  -1638   2267     21       N  
ATOM    104  CA  ARG A 462       6.364   4.510 -27.684  1.00 58.23           C  
ANISOU  104  CA  ARG A 462     8956   6470   6701  -1392   2032     93       C  
ATOM    105  C   ARG A 462       7.028   3.232 -27.193  1.00 54.20           C  
ANISOU  105  C   ARG A 462     7918   6173   6502  -1428   1929    -56       C  
ATOM    106  O   ARG A 462       8.236   3.060 -27.335  1.00 53.37           O  
ANISOU  106  O   ARG A 462     7578   6043   6656  -1635   2173   -220       O  
ATOM    107  CB  ARG A 462       6.200   4.460 -29.204  1.00 63.36           C  
ANISOU  107  CB  ARG A 462    10036   6995   7043  -1352   2267    174       C  
ATOM    108  CG  ARG A 462       5.273   3.358 -29.700  1.00 66.87           C  
ANISOU  108  CG  ARG A 462    10486   7614   7306  -1095   2008    228       C  
ATOM    109  CD  ARG A 462       5.614   2.964 -31.130  1.00 73.63           C  
ANISOU  109  CD  ARG A 462    11626   8385   7966  -1127   2289    223       C  
ATOM    110  NE  ARG A 462       6.990   2.482 -31.229  1.00 80.85           N  
ANISOU  110  NE  ARG A 462    12228   9308   9182  -1384   2618     53       N  
ATOM    111  CZ  ARG A 462       7.335   1.201 -31.317  1.00 82.68           C  
ANISOU  111  CZ  ARG A 462    12112   9713   9588  -1365   2574    -61       C  
ATOM    112  NH1 ARG A 462       6.404   0.255 -31.339  1.00 79.24           N  
ANISOU  112  NH1 ARG A 462    11622   9444   9042  -1130   2238    -14       N  
ATOM    113  NH2 ARG A 462       8.617   0.865 -31.395  1.00 85.41           N  
ANISOU  113  NH2 ARG A 462    12157  10055  10240  -1582   2877   -245       N  
ATOM    114  N   ILE A 463       6.234   2.341 -26.613  1.00 50.83           N  
ANISOU  114  N   ILE A 463     7313   5938   6062  -1225   1576    -16       N  
ATOM    115  CA  ILE A 463       6.746   1.082 -26.098  1.00 51.92           C  
ANISOU  115  CA  ILE A 463     7026   6248   6454  -1214   1436   -132       C  
ATOM    116  C   ILE A 463       6.542  -0.038 -27.116  1.00 54.83           C  
ANISOU  116  C   ILE A 463     7425   6685   6723  -1120   1476   -126       C  
ATOM    117  O   ILE A 463       7.465  -0.794 -27.412  1.00 55.29           O  
ANISOU  117  O   ILE A 463     7249   6777   6981  -1197   1606   -259       O  
ATOM    118  CB  ILE A 463       6.077   0.713 -24.756  1.00 50.28           C  
ANISOU  118  CB  ILE A 463     6641   6173   6291  -1077   1063    -99       C  
ATOM    119  CG1 ILE A 463       6.321   1.813 -23.717  1.00 49.16           C  
ANISOU  119  CG1 ILE A 463     6483   5959   6235  -1167   1016   -127       C  
ATOM    120  CG2 ILE A 463       6.575  -0.634 -24.253  1.00 49.10           C  
ANISOU  120  CG2 ILE A 463     6141   6157   6357  -1036    905   -198       C  
ATOM    121  CD1 ILE A 463       7.782   2.178 -23.527  1.00 49.75           C  
ANISOU  121  CD1 ILE A 463     6325   5967   6611  -1390   1186   -314       C  
ATOM    122  N   GLY A 464       5.331  -0.130 -27.657  1.00 55.70           N  
ANISOU  122  N   GLY A 464     7811   6814   6539   -945   1353      2       N  
ATOM    123  CA  GLY A 464       5.019  -1.127 -28.663  1.00 57.03           C  
ANISOU  123  CA  GLY A 464     8053   7039   6579   -848   1363     -3       C  
ATOM    124  C   GLY A 464       3.533  -1.402 -28.786  1.00 59.56           C  
ANISOU  124  C   GLY A 464     8521   7439   6670   -629   1081     87       C  
ATOM    125  O   GLY A 464       2.716  -0.733 -28.159  1.00 60.21           O  
ANISOU  125  O   GLY A 464     8668   7525   6683   -543    908    158       O  
ATOM    126  N   SER A 465       3.183  -2.391 -29.601  1.00 62.79           N  
ANISOU  126  N   SER A 465     8963   7911   6983   -540   1039     55       N  
ATOM    127  CA  SER A 465       1.788  -2.775 -29.788  1.00 64.20           C  
ANISOU  127  CA  SER A 465     9222   8179   6994   -345    764     83       C  
ATOM    128  C   SER A 465       1.540  -4.190 -29.283  1.00 63.50           C  
ANISOU  128  C   SER A 465     8810   8230   7086   -324    600     10       C  
ATOM    129  O   SER A 465       2.355  -5.087 -29.494  1.00 63.89           O  
ANISOU  129  O   SER A 465     8716   8290   7271   -396    710    -64       O  
ATOM    130  CB  SER A 465       1.385  -2.664 -31.262  1.00 67.72           C  
ANISOU  130  CB  SER A 465    10056   8556   7119   -234    807     93       C  
ATOM    131  OG  SER A 465       1.321  -1.311 -31.677  1.00 71.88           O  
ANISOU  131  OG  SER A 465    10974   8921   7416   -204    905    187       O  
ATOM    132  N   GLY A 466       0.407  -4.383 -28.619  1.00 62.00           N  
ANISOU  132  N   GLY A 466     8519   8130   6906   -229    360     19       N  
ATOM    133  CA  GLY A 466       0.074  -5.679 -28.059  1.00 61.73           C  
ANISOU  133  CA  GLY A 466     8233   8191   7032   -234    235    -42       C  
ATOM    134  C   GLY A 466      -1.131  -6.327 -28.710  1.00 63.14           C  
ANISOU  134  C   GLY A 466     8443   8442   7108   -122     73   -114       C  
ATOM    135  O   GLY A 466      -1.358  -6.176 -29.914  1.00 65.06           O  
ANISOU  135  O   GLY A 466     8904   8664   7151    -35     68   -144       O  
ATOM    136  N   SER A 467      -1.900  -7.056 -27.904  1.00 60.36           N  
ANISOU  136  N   SER A 467     7887   8161   6887   -131    -54   -157       N  
ATOM    137  CA  SER A 467      -3.101  -7.748 -28.370  1.00 59.26           C  
ANISOU  137  CA  SER A 467     7697   8096   6723    -61   -208   -275       C  
ATOM    138  C   SER A 467      -4.124  -6.762 -28.914  1.00 62.65           C  
ANISOU  138  C   SER A 467     8257   8562   6985    101   -360   -307       C  
ATOM    139  O   SER A 467      -4.895  -7.082 -29.820  1.00 65.17           O  
ANISOU  139  O   SER A 467     8622   8929   7211    210   -511   -427       O  
ATOM    140  CB  SER A 467      -3.715  -8.576 -27.239  1.00 55.92           C  
ANISOU  140  CB  SER A 467     7042   7711   6494   -146   -247   -317       C  
ATOM    141  OG  SER A 467      -4.913  -9.201 -27.659  1.00 54.54           O  
ANISOU  141  OG  SER A 467     6772   7606   6344   -113   -372   -470       O  
ATOM    142  N   PHE A 468      -4.128  -5.563 -28.345  1.00 63.01           N  
ANISOU  142  N   PHE A 468     8371   8577   6994    135   -347   -216       N  
ATOM    143  CA  PHE A 468      -4.906  -4.462 -28.891  1.00 64.85           C  
ANISOU  143  CA  PHE A 468     8793   8800   7046    326   -490   -226       C  
ATOM    144  C   PHE A 468      -4.357  -3.138 -28.370  1.00 61.96           C  
ANISOU  144  C   PHE A 468     8584   8332   6625    316   -382    -88       C  
ATOM    145  O   PHE A 468      -3.978  -3.029 -27.206  1.00 60.47           O  
ANISOU  145  O   PHE A 468     8243   8142   6591    192   -291    -36       O  
ATOM    146  CB  PHE A 468      -6.394  -4.613 -28.556  1.00 67.49           C  
ANISOU  146  CB  PHE A 468     8909   9253   7481    433   -704   -377       C  
ATOM    147  CG  PHE A 468      -6.748  -4.216 -27.151  1.00 70.36           C  
ANISOU  147  CG  PHE A 468     9080   9644   8011    370   -656   -357       C  
ATOM    148  CD1 PHE A 468      -6.593  -5.109 -26.102  1.00 70.53           C  
ANISOU  148  CD1 PHE A 468     8879   9692   8226    180   -534   -359       C  
ATOM    149  CD2 PHE A 468      -7.249  -2.951 -26.881  1.00 71.80           C  
ANISOU  149  CD2 PHE A 468     9347   9802   8130    514   -729   -338       C  
ATOM    150  CE1 PHE A 468      -6.921  -4.743 -24.806  1.00 69.75           C  
ANISOU  150  CE1 PHE A 468     8664   9602   8234    123   -470   -341       C  
ATOM    151  CE2 PHE A 468      -7.580  -2.579 -25.590  1.00 71.17           C  
ANISOU  151  CE2 PHE A 468     9110   9742   8188    457   -665   -335       C  
ATOM    152  CZ  PHE A 468      -7.416  -3.477 -24.551  1.00 70.55           C  
ANISOU  152  CZ  PHE A 468     8828   9698   8281    255   -527   -337       C  
ATOM    153  N   GLY A 469      -4.300  -2.143 -29.248  1.00 60.32           N  
ANISOU  153  N   GLY A 469     8721   8017   6178    446   -393    -32       N  
ATOM    154  CA  GLY A 469      -3.821  -0.825 -28.882  1.00 58.02           C  
ANISOU  154  CA  GLY A 469     8632   7592   5821    432   -279     88       C  
ATOM    155  C   GLY A 469      -2.314  -0.679 -28.952  1.00 55.72           C  
ANISOU  155  C   GLY A 469     8440   7184   5548    223     16    177       C  
ATOM    156  O   GLY A 469      -1.593  -1.646 -29.195  1.00 53.92           O  
ANISOU  156  O   GLY A 469     8088   6992   5408     98    131    143       O  
ATOM    157  N   THR A 470      -1.845   0.548 -28.734  1.00 54.34           N  
ANISOU  157  N   THR A 470     8473   6860   5314    183    144    266       N  
ATOM    158  CA  THR A 470      -0.418   0.858 -28.726  1.00 51.79           C  
ANISOU  158  CA  THR A 470     8206   6416   5058    -42    445    309       C  
ATOM    159  C   THR A 470      -0.011   1.534 -27.420  1.00 49.54           C  
ANISOU  159  C   THR A 470     7759   6103   4959   -164    486    327       C  
ATOM    160  O   THR A 470      -0.666   2.471 -26.966  1.00 52.05           O  
ANISOU  160  O   THR A 470     8194   6370   5214    -62    387    364       O  
ATOM    161  CB  THR A 470      -0.039   1.770 -29.894  1.00 52.08           C  
ANISOU  161  CB  THR A 470     8731   6236   4820    -29    638    382       C  
ATOM    162  OG1 THR A 470      -0.448   1.156 -31.122  1.00 56.33           O  
ANISOU  162  OG1 THR A 470     9474   6792   5135    109    572    359       O  
ATOM    163  CG2 THR A 470       1.465   2.005 -29.916  1.00 48.93           C  
ANISOU  163  CG2 THR A 470     8328   5716   4548   -308   1007    378       C  
ATOM    164  N   VAL A 471       1.087   1.063 -26.835  1.00 43.74           N  
ANISOU  164  N   VAL A 471     6765   5397   4456   -363    614    281       N  
ATOM    165  CA  VAL A 471       1.488   1.480 -25.498  1.00 39.08           C  
ANISOU  165  CA  VAL A 471     5984   4810   4054   -467    591    264       C  
ATOM    166  C   VAL A 471       2.588   2.533 -25.517  1.00 38.36           C  
ANISOU  166  C   VAL A 471     6011   4546   4019   -650    830    256       C  
ATOM    167  O   VAL A 471       3.563   2.413 -26.259  1.00 36.22           O  
ANISOU  167  O   VAL A 471     5764   4203   3795   -791   1068    214       O  
ATOM    168  CB  VAL A 471       1.943   0.264 -24.662  1.00 38.15           C  
ANISOU  168  CB  VAL A 471     5498   4830   4165   -533    504    193       C  
ATOM    169  CG1 VAL A 471       2.297   0.678 -23.237  1.00 36.49           C  
ANISOU  169  CG1 VAL A 471     5142   4620   4102   -607    428    168       C  
ATOM    170  CG2 VAL A 471       0.857  -0.800 -24.652  1.00 35.66           C  
ANISOU  170  CG2 VAL A 471     5087   4652   3808   -396    321    190       C  
ATOM    171  N   TYR A 472       2.408   3.564 -24.693  1.00 40.54           N  
ANISOU  171  N   TYR A 472     6355   4746   4302   -660    787    277       N  
ATOM    172  CA  TYR A 472       3.418   4.593 -24.462  1.00 45.46           C  
ANISOU  172  CA  TYR A 472     7047   5200   5026   -862    992    238       C  
ATOM    173  C   TYR A 472       3.687   4.727 -22.965  1.00 44.10           C  
ANISOU  173  C   TYR A 472     6617   5089   5050   -926    843    163       C  
ATOM    174  O   TYR A 472       2.814   4.444 -22.145  1.00 39.76           O  
ANISOU  174  O   TYR A 472     5990   4653   4463   -785    616    188       O  
ATOM    175  CB  TYR A 472       2.931   5.951 -24.969  1.00 49.67           C  
ANISOU  175  CB  TYR A 472     8029   5515   5330   -805   1090    333       C  
ATOM    176  CG  TYR A 472       2.707   6.061 -26.458  1.00 54.65           C  
ANISOU  176  CG  TYR A 472     9046   6022   5696   -726   1235    417       C  
ATOM    177  CD1 TYR A 472       1.576   5.519 -27.053  1.00 54.42           C  
ANISOU  177  CD1 TYR A 472     9121   6093   5462   -464   1021    472       C  
ATOM    178  CD2 TYR A 472       3.607   6.745 -27.265  1.00 58.24           C  
ANISOU  178  CD2 TYR A 472     9792   6242   6094   -919   1592    425       C  
ATOM    179  CE1 TYR A 472       1.363   5.634 -28.413  1.00 56.62           C  
ANISOU  179  CE1 TYR A 472     9805   6250   5457   -362   1110    540       C  
ATOM    180  CE2 TYR A 472       3.401   6.865 -28.623  1.00 59.84           C  
ANISOU  180  CE2 TYR A 472    10439   6302   5995   -839   1737    514       C  
ATOM    181  CZ  TYR A 472       2.277   6.308 -29.192  1.00 61.10           C  
ANISOU  181  CZ  TYR A 472    10721   6572   5923   -543   1469    574       C  
ATOM    182  OH  TYR A 472       2.066   6.426 -30.547  1.00 66.77           O  
ANISOU  182  OH  TYR A 472    11922   7142   6305   -433   1567    651       O  
ATOM    183  N   LYS A 473       4.888   5.174 -22.612  1.00 46.64           N  
ANISOU  183  N   LYS A 473     6817   5327   5579  -1145    981     50       N  
ATOM    184  CA  LYS A 473       5.176   5.552 -21.236  1.00 47.20           C  
ANISOU  184  CA  LYS A 473     6723   5415   5797  -1203    827    -36       C  
ATOM    185  C   LYS A 473       4.708   6.985 -21.046  1.00 49.64           C  
ANISOU  185  C   LYS A 473     7346   5542   5972  -1204    884     15       C  
ATOM    186  O   LYS A 473       4.821   7.810 -21.948  1.00 49.27           O  
ANISOU  186  O   LYS A 473     7593   5301   5826  -1273   1122     63       O  
ATOM    187  CB  LYS A 473       6.670   5.442 -20.931  1.00 50.32           C  
ANISOU  187  CB  LYS A 473     6815   5799   6504  -1425    906   -230       C  
ATOM    188  CG  LYS A 473       7.041   5.719 -19.478  1.00 49.88           C  
ANISOU  188  CG  LYS A 473     6583   5775   6596  -1461    680   -351       C  
ATOM    189  CD  LYS A 473       8.528   5.511 -19.243  1.00 53.14           C  
ANISOU  189  CD  LYS A 473     6637   6198   7355  -1648    703   -590       C  
ATOM    190  CE  LYS A 473       8.901   5.768 -17.793  1.00 56.90           C  
ANISOU  190  CE  LYS A 473     6963   6704   7953  -1654    416   -733       C  
ATOM    191  NZ  LYS A 473      10.351   5.532 -17.540  1.00 61.06           N  
ANISOU  191  NZ  LYS A 473     7088   7257   8853  -1800    370  -1014       N  
ATOM    192  N   GLY A 474       4.168   7.288 -19.876  1.00 49.73           N  
ANISOU  192  N   GLY A 474     7341   5593   5960  -1120    680      8       N  
ATOM    193  CA  GLY A 474       3.585   8.597 -19.669  1.00 48.25           C  
ANISOU  193  CA  GLY A 474     7459   5235   5638  -1077    713     53       C  
ATOM    194  C   GLY A 474       3.733   9.118 -18.263  1.00 46.15           C  
ANISOU  194  C   GLY A 474     7120   4961   5453  -1125    574    -47       C  
ATOM    195  O   GLY A 474       4.199   8.411 -17.370  1.00 44.63           O  
ANISOU  195  O   GLY A 474     6659   4908   5391  -1162    409   -142       O  
ATOM    196  N   LYS A 475       3.335  10.371 -18.076  1.00 46.40           N  
ANISOU  196  N   LYS A 475     7433   4808   5388  -1106    628    -30       N  
ATOM    197  CA  LYS A 475       3.351  10.998 -16.766  1.00 44.25           C  
ANISOU  197  CA  LYS A 475     7157   4503   5151  -1134    504   -129       C  
ATOM    198  C   LYS A 475       1.920  11.327 -16.339  1.00 42.84           C  
ANISOU  198  C   LYS A 475     7162   4343   4771   -878    395    -49       C  
ATOM    199  O   LYS A 475       1.147  11.900 -17.103  1.00 42.27           O  
ANISOU  199  O   LYS A 475     7348   4158   4555   -730    468     48       O  
ATOM    200  CB  LYS A 475       4.202  12.261 -16.781  1.00 48.96           C  
ANISOU  200  CB  LYS A 475     7909   4842   5852  -1362    680   -228       C  
ATOM    201  CG  LYS A 475       5.671  12.006 -17.113  1.00 57.61           C  
ANISOU  201  CG  LYS A 475     8756   5918   7214  -1648    818   -373       C  
ATOM    202  CD  LYS A 475       6.347  11.186 -16.024  1.00 64.18           C  
ANISOU  202  CD  LYS A 475     9200   6951   8234  -1689    560   -538       C  
ATOM    203  CE  LYS A 475       6.342  11.934 -14.689  1.00 69.84           C  
ANISOU  203  CE  LYS A 475     9970   7613   8951  -1707    382   -663       C  
ATOM    204  NZ  LYS A 475       7.038  11.168 -13.614  1.00 72.49           N  
ANISOU  204  NZ  LYS A 475     9993   8121   9430  -1718     87   -832       N  
ATOM    205  N   TRP A 476       1.572  10.920 -15.121  1.00 41.29           N  
ANISOU  205  N   TRP A 476     6839   4287   4563   -813    219   -106       N  
ATOM    206  CA  TRP A 476       0.300  11.261 -14.481  1.00 38.10           C  
ANISOU  206  CA  TRP A 476     6563   3904   4011   -607    152    -87       C  
ATOM    207  C   TRP A 476       0.348  10.866 -13.011  1.00 41.23           C  
ANISOU  207  C   TRP A 476     6858   4408   4398   -628     10   -179       C  
ATOM    208  O   TRP A 476       0.040   9.722 -12.660  1.00 41.99           O  
ANISOU  208  O   TRP A 476     6801   4684   4469   -574    -71   -155       O  
ATOM    209  CB  TRP A 476      -0.896  10.594 -15.182  1.00 35.28           C  
ANISOU  209  CB  TRP A 476     6169   3675   3560   -387    137     11       C  
ATOM    210  CG  TRP A 476      -2.228  11.120 -14.695  1.00 36.89           C  
ANISOU  210  CG  TRP A 476     6478   3878   3661   -169    106    -12       C  
ATOM    211  CD1 TRP A 476      -2.756  12.355 -14.939  1.00 40.93           C  
ANISOU  211  CD1 TRP A 476     7244   4203   4102    -34    145    -14       C  
ATOM    212  CD2 TRP A 476      -3.182  10.437 -13.866  1.00 34.56           C  
ANISOU  212  CD2 TRP A 476     6038   3757   3337    -62     54    -57       C  
ATOM    213  NE1 TRP A 476      -3.976  12.483 -14.320  1.00 40.66           N  
ANISOU  213  NE1 TRP A 476     7188   4239   4023    169    103    -77       N  
ATOM    214  CE2 TRP A 476      -4.260  11.318 -13.654  1.00 37.19           C  
ANISOU  214  CE2 TRP A 476     6497   4022   3611    135     72   -109       C  
ATOM    215  CE3 TRP A 476      -3.228   9.167 -13.282  1.00 31.72           C  
ANISOU  215  CE3 TRP A 476     5476   3581   2994   -117     16    -64       C  
ATOM    216  CZ2 TRP A 476      -5.370  10.973 -12.889  1.00 34.46           C  
ANISOU  216  CZ2 TRP A 476     6038   3805   3251    254     86   -191       C  
ATOM    217  CZ3 TRP A 476      -4.336   8.825 -12.522  1.00 32.66           C  
ANISOU  217  CZ3 TRP A 476     5539   3803   3067    -16     44   -121       C  
ATOM    218  CH2 TRP A 476      -5.389   9.724 -12.335  1.00 30.64           C  
ANISOU  218  CH2 TRP A 476     5367   3495   2780    157     94   -195       C  
ATOM    219  N   HIS A 477       0.729  11.824 -12.167  1.00 41.29           N  
ANISOU  219  N   HIS A 477     6998   4283   4408   -709    -12   -286       N  
ATOM    220  CA  HIS A 477       0.950  11.582 -10.743  1.00 39.46           C  
ANISOU  220  CA  HIS A 477     6744   4116   4134   -739   -165   -392       C  
ATOM    221  C   HIS A 477       2.003  10.494 -10.581  1.00 39.07           C  
ANISOU  221  C   HIS A 477     6460   4189   4196   -850   -308   -432       C  
ATOM    222  O   HIS A 477       1.858   9.578  -9.773  1.00 39.20           O  
ANISOU  222  O   HIS A 477     6438   4332   4126   -788   -444   -432       O  
ATOM    223  CB  HIS A 477      -0.351  11.191 -10.037  1.00 37.93           C  
ANISOU  223  CB  HIS A 477     6615   4031   3767   -554   -168   -358       C  
ATOM    224  CG  HIS A 477      -1.436  12.214 -10.153  1.00 37.66           C  
ANISOU  224  CG  HIS A 477     6762   3892   3655   -402    -50   -357       C  
ATOM    225  ND1 HIS A 477      -1.351  13.461  -9.567  1.00 38.45           N  
ANISOU  225  ND1 HIS A 477     7078   3812   3720   -420    -32   -455       N  
ATOM    226  CD2 HIS A 477      -2.638  12.173 -10.775  1.00 33.25           C  
ANISOU  226  CD2 HIS A 477     6192   3379   3062   -209     32   -296       C  
ATOM    227  CE1 HIS A 477      -2.451  14.142  -9.827  1.00 36.09           C  
ANISOU  227  CE1 HIS A 477     6906   3444   3364   -229     63   -442       C  
ATOM    228  NE2 HIS A 477      -3.250  13.384 -10.557  1.00 39.03           N  
ANISOU  228  NE2 HIS A 477     7128   3958   3743    -91     90   -355       N  
ATOM    229  N   GLY A 478       3.060  10.606 -11.377  1.00 38.83           N  
ANISOU  229  N   GLY A 478     6294   4101   4359  -1009   -260   -474       N  
ATOM    230  CA  GLY A 478       4.084   9.589 -11.456  1.00 33.97           C  
ANISOU  230  CA  GLY A 478     5409   3595   3901  -1091   -379   -532       C  
ATOM    231  C   GLY A 478       4.066   8.945 -12.828  1.00 40.22           C  
ANISOU  231  C   GLY A 478     6078   4440   4764  -1088   -226   -418       C  
ATOM    232  O   GLY A 478       3.474   9.472 -13.765  1.00 40.48           O  
ANISOU  232  O   GLY A 478     6257   4392   4734  -1055    -37   -315       O  
ATOM    233  N   ASP A 479       4.712   7.793 -12.946  1.00 40.09           N  
ANISOU  233  N   ASP A 479     5823   4549   4862  -1100   -326   -443       N  
ATOM    234  CA  ASP A 479       4.793   7.090 -14.214  1.00 36.56           C  
ANISOU  234  CA  ASP A 479     5254   4155   4483  -1103   -186   -360       C  
ATOM    235  C   ASP A 479       3.537   6.273 -14.480  1.00 36.24           C  
ANISOU  235  C   ASP A 479     5282   4227   4260   -918   -184   -196       C  
ATOM    236  O   ASP A 479       3.003   5.615 -13.586  1.00 35.22           O  
ANISOU  236  O   ASP A 479     5169   4187   4026   -815   -326   -173       O  
ATOM    237  CB  ASP A 479       6.009   6.169 -14.224  1.00 39.28           C  
ANISOU  237  CB  ASP A 479     5294   4579   5051  -1175   -296   -483       C  
ATOM    238  CG  ASP A 479       7.278   6.882 -13.834  1.00 46.38           C  
ANISOU  238  CG  ASP A 479     6042   5392   6187  -1360   -339   -710       C  
ATOM    239  OD1 ASP A 479       7.594   7.921 -14.450  1.00 49.42           O  
ANISOU  239  OD1 ASP A 479     6488   5630   6661  -1530   -104   -756       O  
ATOM    240  OD2 ASP A 479       7.959   6.404 -12.904  1.00 50.35           O  
ANISOU  240  OD2 ASP A 479     6382   5961   6789  -1332   -615   -855       O  
ATOM    241  N   VAL A 480       3.066   6.321 -15.720  1.00 34.99           N  
ANISOU  241  N   VAL A 480     5185   4050   4060   -883    -15    -98       N  
ATOM    242  CA  VAL A 480       1.954   5.486 -16.139  1.00 34.60           C  
ANISOU  242  CA  VAL A 480     5143   4116   3889   -724    -23     12       C  
ATOM    243  C   VAL A 480       2.236   4.843 -17.488  1.00 36.36           C  
ANISOU  243  C   VAL A 480     5287   4367   4160   -740     82     54       C  
ATOM    244  O   VAL A 480       3.153   5.239 -18.205  1.00 39.99           O  
ANISOU  244  O   VAL A 480     5744   4735   4717   -870    221     16       O  
ATOM    245  CB  VAL A 480       0.633   6.277 -16.243  1.00 32.03           C  
ANISOU  245  CB  VAL A 480     5021   3747   3400   -579     21     74       C  
ATOM    246  CG1 VAL A 480       0.209   6.795 -14.881  1.00 33.37           C  
ANISOU  246  CG1 VAL A 480     5273   3902   3506   -547    -56     23       C  
ATOM    247  CG2 VAL A 480       0.762   7.411 -17.263  1.00 28.15           C  
ANISOU  247  CG2 VAL A 480     4735   3084   2876   -597    169    106       C  
ATOM    248  N   ALA A 481       1.437   3.840 -17.819  1.00 33.18           N  
ANISOU  248  N   ALA A 481     4830   4084   3692   -624     40    115       N  
ATOM    249  CA  ALA A 481       1.423   3.298 -19.163  1.00 34.81           C  
ANISOU  249  CA  ALA A 481     5023   4314   3889   -601    130    155       C  
ATOM    250  C   ALA A 481       0.157   3.796 -19.836  1.00 33.12           C  
ANISOU  250  C   ALA A 481     4995   4085   3506   -442    144    220       C  
ATOM    251  O   ALA A 481      -0.926   3.728 -19.262  1.00 33.72           O  
ANISOU  251  O   ALA A 481     5060   4229   3524   -324     52    218       O  
ATOM    252  CB  ALA A 481       1.462   1.776 -19.132  1.00 34.60           C  
ANISOU  252  CB  ALA A 481     4803   4418   3926   -580     50    148       C  
ATOM    253  N   VAL A 482       0.301   4.322 -21.044  1.00 33.44           N  
ANISOU  253  N   VAL A 482     5219   4021   3464   -431    261    259       N  
ATOM    254  CA  VAL A 482      -0.845   4.824 -21.785  1.00 34.27           C  
ANISOU  254  CA  VAL A 482     5539   4092   3391   -232    220    308       C  
ATOM    255  C   VAL A 482      -1.068   3.985 -23.033  1.00 36.13           C  
ANISOU  255  C   VAL A 482     5790   4389   3550   -159    216    325       C  
ATOM    256  O   VAL A 482      -0.238   3.964 -23.939  1.00 36.85           O  
ANISOU  256  O   VAL A 482     5995   4396   3610   -252    368    347       O  
ATOM    257  CB  VAL A 482      -0.652   6.295 -22.190  1.00 34.52           C  
ANISOU  257  CB  VAL A 482     5910   3895   3310   -228    332    353       C  
ATOM    258  CG1 VAL A 482      -1.940   6.865 -22.779  1.00 32.53           C  
ANISOU  258  CG1 VAL A 482     5894   3598   2867     46    213    388       C  
ATOM    259  CG2 VAL A 482      -0.200   7.115 -20.994  1.00 34.70           C  
ANISOU  259  CG2 VAL A 482     5917   3839   3431   -347    357    310       C  
ATOM    260  N   LYS A 483      -2.186   3.278 -23.070  1.00 37.20           N  
ANISOU  260  N   LYS A 483     5803   4666   3664     -6     59    292       N  
ATOM    261  CA  LYS A 483      -2.521   2.495 -24.241  1.00 39.35           C  
ANISOU  261  CA  LYS A 483     6096   5000   3855     82     14    280       C  
ATOM    262  C   LYS A 483      -3.434   3.310 -25.127  1.00 41.31           C  
ANISOU  262  C   LYS A 483     6626   5170   3899    317    -92    293       C  
ATOM    263  O   LYS A 483      -4.593   3.544 -24.786  1.00 40.93           O  
ANISOU  263  O   LYS A 483     6511   5186   3854    496   -261    231       O  
ATOM    264  CB  LYS A 483      -3.194   1.176 -23.858  1.00 39.26           C  
ANISOU  264  CB  LYS A 483     5784   5175   3960     97   -100    203       C  
ATOM    265  CG  LYS A 483      -3.711   0.394 -25.065  1.00 41.40           C  
ANISOU  265  CG  LYS A 483     6068   5511   4150    203   -184    155       C  
ATOM    266  CD  LYS A 483      -4.185  -0.997 -24.687  1.00 40.74           C  
ANISOU  266  CD  LYS A 483     5690   5577   4213    156   -246     69       C  
ATOM    267  CE  LYS A 483      -3.018  -1.891 -24.315  1.00 41.73           C  
ANISOU  267  CE  LYS A 483     5700   5698   4458    -33   -126    101       C  
ATOM    268  NZ  LYS A 483      -3.427  -3.321 -24.280  1.00 42.61           N  
ANISOU  268  NZ  LYS A 483     5617   5904   4667    -66   -173     28       N  
ATOM    269  N   MET A 484      -2.896   3.759 -26.255  1.00 44.92           N  
ANISOU  269  N   MET A 484     7415   5476   4176    325     12    360       N  
ATOM    270  CA  MET A 484      -3.681   4.472 -27.249  1.00 50.24           C  
ANISOU  270  CA  MET A 484     8453   6041   4596    584   -117    385       C  
ATOM    271  C   MET A 484      -4.440   3.486 -28.115  1.00 54.04           C  
ANISOU  271  C   MET A 484     8864   6663   5005    745   -313    303       C  
ATOM    272  O   MET A 484      -3.841   2.597 -28.715  1.00 55.51           O  
ANISOU  272  O   MET A 484     9018   6891   5184    627   -214    298       O  
ATOM    273  CB  MET A 484      -2.766   5.276 -28.170  1.00 53.40           C  
ANISOU  273  CB  MET A 484     9319   6185   4784    511    112    497       C  
ATOM    274  CG  MET A 484      -1.973   6.350 -27.493  1.00 55.08           C  
ANISOU  274  CG  MET A 484     9648   6216   5063    332    326    556       C  
ATOM    275  SD  MET A 484      -3.043   7.503 -26.633  1.00 76.24           S  
ANISOU  275  SD  MET A 484    12401   8835   7732    557    122    548       S  
ATOM    276  CE  MET A 484      -1.868   8.789 -26.228  1.00 57.54           C  
ANISOU  276  CE  MET A 484    10299   6178   5384    304    433    620       C  
ATOM    277  N   LEU A 485      -5.755   3.664 -28.190  1.00 56.96           N  
ANISOU  277  N   LEU A 485     9201   7103   5339   1019   -596    211       N  
ATOM    278  CA  LEU A 485      -6.571   2.958 -29.167  1.00 62.91           C  
ANISOU  278  CA  LEU A 485     9949   7959   5993   1218   -837    100       C  
ATOM    279  C   LEU A 485      -6.629   3.738 -30.479  1.00 72.09           C  
ANISOU  279  C   LEU A 485    11677   8924   6791   1451   -931    169       C  
ATOM    280  O   LEU A 485      -6.960   4.927 -30.504  1.00 78.29           O  
ANISOU  280  O   LEU A 485    12770   9545   7434   1644  -1012    223       O  
ATOM    281  CB  LEU A 485      -7.986   2.715 -28.649  1.00 63.47           C  
ANISOU  281  CB  LEU A 485     9660   8212   6243   1404  -1112    -89       C  
ATOM    282  CG  LEU A 485      -8.177   1.871 -27.393  1.00 62.46           C  
ANISOU  282  CG  LEU A 485     9026   8266   6439   1197  -1022   -177       C  
ATOM    283  CD1 LEU A 485      -8.130   2.719 -26.121  1.00 61.01           C  
ANISOU  283  CD1 LEU A 485     8780   8034   6366   1138   -906   -131       C  
ATOM    284  CD2 LEU A 485      -9.492   1.132 -27.498  1.00 65.25           C  
ANISOU  284  CD2 LEU A 485     9043   8808   6942   1336  -1259   -411       C  
ATOM    285  N   ASN A 486      -6.312   3.060 -31.572  1.00 73.14           N  
ANISOU  285  N   ASN A 486    11990   9051   6748   1445   -918    168       N  
ATOM    286  CA  ASN A 486      -6.253   3.719 -32.869  1.00 77.74           C  
ANISOU  286  CA  ASN A 486    13083   9406   7050   1597   -926    228       C  
ATOM    287  C   ASN A 486      -7.607   4.246 -33.359  1.00 81.23           C  
ANISOU  287  C   ASN A 486    13593   9821   7451   1969  -1304    103       C  
ATOM    288  O   ASN A 486      -8.244   3.629 -34.199  1.00 83.18           O  
ANISOU  288  O   ASN A 486    13808  10141   7656   2124  -1530    -28       O  
ATOM    289  CB  ASN A 486      -5.642   2.771 -33.903  1.00 78.81           C  
ANISOU  289  CB  ASN A 486    13322   9550   7074   1481   -800    219       C  
ATOM    290  CG  ASN A 486      -5.348   3.448 -35.223  1.00 82.64           C  
ANISOU  290  CG  ASN A 486    14329   9759   7309   1560   -703    289       C  
ATOM    291  OD1 ASN A 486      -5.245   4.673 -35.313  1.00 84.06           O  
ANISOU  291  OD1 ASN A 486    14840   9701   7398   1618   -624    377       O  
ATOM    292  ND2 ASN A 486      -5.198   2.642 -36.260  1.00 84.27           N  
ANISOU  292  ND2 ASN A 486    14641   9981   7395   1559   -700    240       N  
ATOM    293  N   VAL A 487      -8.018   5.405 -32.852  1.00 82.72           N  
ANISOU  293  N   VAL A 487    13886   9890   7655   2115  -1369    126       N  
ATOM    294  CA  VAL A 487      -9.304   5.981 -33.208  1.00 86.38           C  
ANISOU  294  CA  VAL A 487    14394  10322   8105   2487  -1724    -22       C  
ATOM    295  C   VAL A 487      -9.425   7.403 -32.715  1.00 85.41           C  
ANISOU  295  C   VAL A 487    14510   9994   7946   2607  -1699     42       C  
ATOM    296  O   VAL A 487      -8.849   7.768 -31.722  1.00 82.06           O  
ANISOU  296  O   VAL A 487    14023   9551   7605   2421  -1489    149       O  
ATOM    297  CB  VAL A 487     -10.467   5.143 -32.619  1.00 65.37           C  
ANISOU  297  CB  VAL A 487    11151   7978   5710   2609  -2029   -263       C  
ATOM    298  CG1 VAL A 487     -10.217   4.936 -31.131  1.00 59.93           C  
ANISOU  298  CG1 VAL A 487    10088   7453   5231   2412  -1893   -235       C  
ATOM    299  CG2 VAL A 487     -11.823   5.837 -32.863  1.00 68.28           C  
ANISOU  299  CG2 VAL A 487    11504   8319   6120   2996  -2383   -463       C  
ATOM    300  N   PRO A 490     -14.318   9.231 -31.999  1.00 88.11           N  
ANISOU  300  N   PRO A 490    14228  10543   8708   3872  -2935   -779       N  
ATOM    301  CA  PRO A 490     -14.873   7.874 -32.021  1.00 86.39           C  
ANISOU  301  CA  PRO A 490    13471  10629   8726   3810  -3068   -982       C  
ATOM    302  C   PRO A 490     -16.273   7.812 -32.629  1.00 89.42           C  
ANISOU  302  C   PRO A 490    13663  11096   9214   4143  -3464  -1321       C  
ATOM    303  O   PRO A 490     -16.968   8.823 -32.697  1.00 90.58           O  
ANISOU  303  O   PRO A 490    13966  11129   9322   4438  -3659  -1434       O  
ATOM    304  CB  PRO A 490     -14.925   7.503 -30.541  1.00 82.87           C  
ANISOU  304  CB  PRO A 490    12491  10408   8589   3625  -2933  -1022       C  
ATOM    305  CG  PRO A 490     -13.792   8.268 -29.937  1.00 81.40           C  
ANISOU  305  CG  PRO A 490    12651  10029   8249   3453  -2632   -721       C  
ATOM    306  CD  PRO A 490     -13.707   9.563 -30.698  1.00 84.75           C  
ANISOU  306  CD  PRO A 490    13683  10125   8391   3662  -2673   -629       C  
ATOM    307  N   THR A 491     -16.663   6.624 -33.079  1.00 92.32           N  
ANISOU  307  N   THR A 491    13706  11655   9715   4088  -3580  -1493       N  
ATOM    308  CA  THR A 491     -18.015   6.360 -33.555  1.00 99.87           C  
ANISOU  308  CA  THR A 491    14371  12731  10845   4350  -3941  -1862       C  
ATOM    309  C   THR A 491     -18.890   6.151 -32.331  1.00101.96           C  
ANISOU  309  C   THR A 491    13964  13242  11533   4297  -3943  -2117       C  
ATOM    310  O   THR A 491     -18.382   5.761 -31.278  1.00 99.63           O  
ANISOU  310  O   THR A 491    13391  13068  11396   4011  -3666  -2009       O  
ATOM    311  CB  THR A 491     -18.037   5.087 -34.446  1.00103.90           C  
ANISOU  311  CB  THR A 491    14771  13345  11361   4260  -4022  -1954       C  
ATOM    312  OG1 THR A 491     -17.255   5.319 -35.622  1.00106.34           O  
ANISOU  312  OG1 THR A 491    15724  13411  11270   4319  -4003  -1732       O  
ATOM    313  CG2 THR A 491     -19.450   4.694 -34.867  1.00107.32           C  
ANISOU  313  CG2 THR A 491    14835  13916  12025   4493  -4383  -2373       C  
ATOM    314  N   PRO A 492     -20.198   6.441 -32.447  1.00106.75           N  
ANISOU  314  N   PRO A 492    14321  13913  12325   4572  -4242  -2467       N  
ATOM    315  CA  PRO A 492     -21.120   6.058 -31.377  1.00107.31           C  
ANISOU  315  CA  PRO A 492    13693  14232  12847   4475  -4204  -2766       C  
ATOM    316  C   PRO A 492     -20.926   4.618 -30.923  1.00104.16           C  
ANISOU  316  C   PRO A 492    12821  14053  12702   4094  -3975  -2809       C  
ATOM    317  O   PRO A 492     -20.931   4.351 -29.723  1.00102.18           O  
ANISOU  317  O   PRO A 492    12168  13941  12713   3858  -3720  -2835       O  
ATOM    318  CB  PRO A 492     -22.483   6.217 -32.040  1.00113.16           C  
ANISOU  318  CB  PRO A 492    14269  15005  13719   4802  -4595  -3168       C  
ATOM    319  CG  PRO A 492     -22.289   7.383 -32.951  1.00116.24           C  
ANISOU  319  CG  PRO A 492    15344  15116  13705   5157  -4827  -3030       C  
ATOM    320  CD  PRO A 492     -20.836   7.370 -33.398  1.00112.48           C  
ANISOU  320  CD  PRO A 492    15436  14453  12846   4990  -4595  -2592       C  
ATOM    321  N   GLN A 493     -20.732   3.709 -31.871  1.00103.44           N  
ANISOU  321  N   GLN A 493    12809  13974  12518   4033  -4053  -2814       N  
ATOM    322  CA  GLN A 493     -20.585   2.296 -31.544  1.00100.67           C  
ANISOU  322  CA  GLN A 493    12042  13810  12396   3677  -3854  -2873       C  
ATOM    323  C   GLN A 493     -19.191   1.932 -31.040  1.00 94.15           C  
ANISOU  323  C   GLN A 493    11381  12970  11422   3364  -3526  -2508       C  
ATOM    324  O   GLN A 493     -19.040   1.023 -30.223  1.00 91.27           O  
ANISOU  324  O   GLN A 493    10626  12760  11292   3045  -3288  -2539       O  
ATOM    325  CB  GLN A 493     -20.954   1.432 -32.745  1.00104.42           C  
ANISOU  325  CB  GLN A 493    12525  14305  12845   3739  -4074  -3043       C  
ATOM    326  CG  GLN A 493     -22.356   1.679 -33.246  1.00111.45           C  
ANISOU  326  CG  GLN A 493    13211  15223  13910   4047  -4426  -3450       C  
ATOM    327  CD  GLN A 493     -22.428   1.686 -34.751  1.00114.97           C  
ANISOU  327  CD  GLN A 493    14071  15536  14075   4330  -4758  -3480       C  
ATOM    328  OE1 GLN A 493     -22.492   0.634 -35.384  1.00114.84           O  
ANISOU  328  OE1 GLN A 493    13947  15585  14102   4234  -4812  -3582       O  
ATOM    329  NE2 GLN A 493     -22.408   2.878 -35.338  1.00117.64           N  
ANISOU  329  NE2 GLN A 493    14918  15670  14110   4682  -4975  -3390       N  
ATOM    330  N   GLN A 494     -18.175   2.631 -31.535  1.00 90.43           N  
ANISOU  330  N   GLN A 494    11500  12296  10562   3444  -3500  -2177       N  
ATOM    331  CA  GLN A 494     -16.814   2.421 -31.057  1.00 81.30           C  
ANISOU  331  CA  GLN A 494    10529  11108   9253   3164  -3198  -1843       C  
ATOM    332  C   GLN A 494     -16.704   2.833 -29.598  1.00 77.46           C  
ANISOU  332  C   GLN A 494     9794  10692   8947   3049  -2998  -1798       C  
ATOM    333  O   GLN A 494     -15.957   2.236 -28.824  1.00 71.51           O  
ANISOU  333  O   GLN A 494     8894  10026   8249   2761  -2757  -1670       O  
ATOM    334  CB  GLN A 494     -15.821   3.219 -31.898  1.00 77.91           C  
ANISOU  334  CB  GLN A 494    10799  10412   8393   3260  -3165  -1529       C  
ATOM    335  CG  GLN A 494     -15.606   2.648 -33.283  1.00 76.66           C  
ANISOU  335  CG  GLN A 494    10926  10180   8022   3298  -3268  -1515       C  
ATOM    336  CD  GLN A 494     -14.693   3.501 -34.128  1.00 73.77           C  
ANISOU  336  CD  GLN A 494    11259   9522   7248   3376  -3181  -1233       C  
ATOM    337  OE1 GLN A 494     -14.869   4.714 -34.222  1.00 74.13           O  
ANISOU  337  OE1 GLN A 494    11629   9377   7158   3598  -3250  -1185       O  
ATOM    338  NE2 GLN A 494     -13.704   2.872 -34.747  1.00 71.36           N  
ANISOU  338  NE2 GLN A 494    11194   9165   6753   3177  -3002  -1060       N  
ATOM    339  N   LEU A 495     -17.461   3.863 -29.238  1.00 80.71           N  
ANISOU  339  N   LEU A 495    10171  11057   9440   3291  -3109  -1918       N  
ATOM    340  CA  LEU A 495     -17.472   4.383 -27.881  1.00 81.02           C  
ANISOU  340  CA  LEU A 495     9990  11141   9652   3236  -2931  -1902       C  
ATOM    341  C   LEU A 495     -18.092   3.378 -26.918  1.00 79.01           C  
ANISOU  341  C   LEU A 495     9067  11138   9817   2991  -2764  -2155       C  
ATOM    342  O   LEU A 495     -17.643   3.237 -25.781  1.00 76.76           O  
ANISOU  342  O   LEU A 495     8613  10906   9647   2766  -2473  -2065       O  
ATOM    343  CB  LEU A 495     -18.228   5.710 -27.841  1.00 87.56           C  
ANISOU  343  CB  LEU A 495    10951  11848  10470   3570  -3102  -2007       C  
ATOM    344  CG  LEU A 495     -18.231   6.495 -26.529  1.00 90.46           C  
ANISOU  344  CG  LEU A 495    11194  12203  10973   3578  -2924  -1979       C  
ATOM    345  CD1 LEU A 495     -18.165   7.981 -26.825  1.00 93.19           C  
ANISOU  345  CD1 LEU A 495    12056  12289  11064   3872  -3050  -1855       C  
ATOM    346  CD2 LEU A 495     -19.470   6.178 -25.701  1.00 93.99           C  
ANISOU  346  CD2 LEU A 495    10993  12860  11858   3546  -2876  -2354       C  
ATOM    347  N   GLN A 496     -19.121   2.677 -27.382  1.00 79.94           N  
ANISOU  347  N   GLN A 496     8849  11369  10155   2995  -2893  -2469       N  
ATOM    348  CA  GLN A 496     -19.780   1.663 -26.570  1.00 79.62           C  
ANISOU  348  CA  GLN A 496     8217  11520  10515   2710  -2677  -2725       C  
ATOM    349  C   GLN A 496     -18.837   0.499 -26.309  1.00 75.53           C  
ANISOU  349  C   GLN A 496     7648  11067   9984   2346  -2433  -2559       C  
ATOM    350  O   GLN A 496     -18.729   0.011 -25.186  1.00 77.61           O  
ANISOU  350  O   GLN A 496     7612  11418  10457   2063  -2112  -2578       O  
ATOM    351  CB  GLN A 496     -21.039   1.155 -27.268  1.00 85.53           C  
ANISOU  351  CB  GLN A 496     8679  12339  11478   2791  -2881  -3097       C  
ATOM    352  CG  GLN A 496     -21.956   0.348 -26.367  1.00 89.27           C  
ANISOU  352  CG  GLN A 496     8566  12961  12390   2511  -2624  -3408       C  
ATOM    353  CD  GLN A 496     -22.777   1.226 -25.442  1.00 93.33           C  
ANISOU  353  CD  GLN A 496     8842  13498  13122   2606  -2540  -3590       C  
ATOM    354  OE1 GLN A 496     -22.263   1.787 -24.473  1.00 91.65           O  
ANISOU  354  OE1 GLN A 496     8688  13260  12876   2548  -2311  -3413       O  
ATOM    355  NE2 GLN A 496     -24.063   1.357 -25.744  1.00 97.87           N  
ANISOU  355  NE2 GLN A 496     9145  14117  13925   2763  -2729  -3962       N  
ATOM    356  N   ALA A 497     -18.154   0.059 -27.359  1.00 71.23           N  
ANISOU  356  N   ALA A 497     7424  10462   9179   2351  -2566  -2403       N  
ATOM    357  CA  ALA A 497     -17.201  -1.036 -27.250  1.00 66.12           C  
ANISOU  357  CA  ALA A 497     6778   9860   8484   2027  -2373  -2250       C  
ATOM    358  C   ALA A 497     -16.036  -0.640 -26.348  1.00 62.30           C  
ANISOU  358  C   ALA A 497     6584   9241   7846   1806  -2011  -1886       C  
ATOM    359  O   ALA A 497     -15.437  -1.481 -25.679  1.00 60.71           O  
ANISOU  359  O   ALA A 497     6320   9035   7712   1453  -1690  -1769       O  
ATOM    360  CB  ALA A 497     -16.699  -1.438 -28.628  1.00 65.22           C  
ANISOU  360  CB  ALA A 497     7025   9663   8091   2095  -2553  -2147       C  
ATOM    361  N   PHE A 498     -15.719   0.650 -26.344  1.00 60.99           N  
ANISOU  361  N   PHE A 498     6759   8941   7472   2023  -2075  -1718       N  
ATOM    362  CA  PHE A 498     -14.663   1.186 -25.501  1.00 55.77           C  
ANISOU  362  CA  PHE A 498     6370   8140   6682   1834  -1764  -1412       C  
ATOM    363  C   PHE A 498     -15.088   1.139 -24.038  1.00 55.91           C  
ANISOU  363  C   PHE A 498     6062   8221   6961   1646  -1487  -1502       C  
ATOM    364  O   PHE A 498     -14.304   0.770 -23.165  1.00 50.32           O  
ANISOU  364  O   PHE A 498     5407   7468   6244   1346  -1180  -1326       O  
ATOM    365  CB  PHE A 498     -14.343   2.625 -25.914  1.00 53.93           C  
ANISOU  365  CB  PHE A 498     6589   7724   6179   2117  -1908  -1252       C  
ATOM    366  CG  PHE A 498     -13.275   3.272 -25.080  1.00 50.25           C  
ANISOU  366  CG  PHE A 498     6387   7103   5601   1925  -1610   -979       C  
ATOM    367  CD1 PHE A 498     -11.984   2.775 -25.083  1.00 46.14           C  
ANISOU  367  CD1 PHE A 498     6054   6515   4961   1637  -1387   -747       C  
ATOM    368  CD2 PHE A 498     -13.558   4.386 -24.304  1.00 51.05           C  
ANISOU  368  CD2 PHE A 498     6535   7126   5735   2042  -1569   -984       C  
ATOM    369  CE1 PHE A 498     -10.998   3.364 -24.319  1.00 43.34           C  
ANISOU  369  CE1 PHE A 498     5900   6030   4539   1464  -1151   -543       C  
ATOM    370  CE2 PHE A 498     -12.576   4.983 -23.538  1.00 48.26           C  
ANISOU  370  CE2 PHE A 498     6421   6629   5287   1858  -1319   -763       C  
ATOM    371  CZ  PHE A 498     -11.293   4.471 -23.546  1.00 45.56           C  
ANISOU  371  CZ  PHE A 498     6237   6232   4841   1566  -1121   -550       C  
ATOM    372  N   LYS A 499     -16.336   1.513 -23.780  1.00 59.53           N  
ANISOU  372  N   LYS A 499     6193   8776   7648   1840  -1601  -1795       N  
ATOM    373  CA  LYS A 499     -16.880   1.480 -22.430  1.00 63.38           C  
ANISOU  373  CA  LYS A 499     6370   9324   8388   1671  -1306  -1926       C  
ATOM    374  C   LYS A 499     -17.006   0.055 -21.907  1.00 66.11           C  
ANISOU  374  C   LYS A 499     6414   9766   8937   1299  -1032  -2016       C  
ATOM    375  O   LYS A 499     -16.810  -0.196 -20.720  1.00 65.34           O  
ANISOU  375  O   LYS A 499     6291   9640   8895   1033   -680  -1950       O  
ATOM    376  CB  LYS A 499     -18.233   2.188 -22.384  1.00 69.61           C  
ANISOU  376  CB  LYS A 499     6835  10202   9413   1984  -1490  -2270       C  
ATOM    377  CG  LYS A 499     -18.124   3.696 -22.536  1.00 72.88           C  
ANISOU  377  CG  LYS A 499     7585  10471   9635   2334  -1680  -2166       C  
ATOM    378  CD  LYS A 499     -17.356   4.316 -21.375  1.00 70.66           C  
ANISOU  378  CD  LYS A 499     7557  10054   9237   2147  -1345  -1924       C  
ATOM    379  CE  LYS A 499     -16.816   5.691 -21.740  1.00 70.63           C  
ANISOU  379  CE  LYS A 499     8040   9841   8955   2415  -1511  -1719       C  
ATOM    380  NZ  LYS A 499     -17.853   6.570 -22.358  1.00 73.38           N  
ANISOU  380  NZ  LYS A 499     8335  10182   9365   2893  -1878  -1951       N  
ATOM    381  N   ASN A 500     -17.329  -0.878 -22.794  1.00 69.62           N  
ANISOU  381  N   ASN A 500     6678  10303   9471   1285  -1197  -2169       N  
ATOM    382  CA  ASN A 500     -17.439  -2.275 -22.402  1.00 72.46           C  
ANISOU  382  CA  ASN A 500     6795  10719  10020    927   -941  -2257       C  
ATOM    383  C   ASN A 500     -16.111  -2.864 -21.941  1.00 69.09           C  
ANISOU  383  C   ASN A 500     6702  10164   9383    638   -686  -1906       C  
ATOM    384  O   ASN A 500     -16.066  -3.610 -20.964  1.00 69.72           O  
ANISOU  384  O   ASN A 500     6710  10217   9564    338   -356  -1889       O  
ATOM    385  CB  ASN A 500     -18.018  -3.115 -23.538  1.00 76.42           C  
ANISOU  385  CB  ASN A 500     7057  11329  10651    984  -1205  -2508       C  
ATOM    386  CG  ASN A 500     -19.508  -2.915 -23.706  1.00 83.22           C  
ANISOU  386  CG  ASN A 500     7488  12308  11824   1156  -1363  -2929       C  
ATOM    387  OD1 ASN A 500     -20.033  -1.826 -23.472  1.00 86.25           O  
ANISOU  387  OD1 ASN A 500     7847  12688  12236   1401  -1455  -3008       O  
ATOM    388  ND2 ASN A 500     -20.203  -3.973 -24.106  1.00 86.02           N  
ANISOU  388  ND2 ASN A 500     7634  12681  12368    996  -1340  -3150       N  
ATOM    389  N   GLU A 501     -15.032  -2.534 -22.642  1.00 65.55           N  
ANISOU  389  N   GLU A 501     6633   9625   8648    735   -835  -1640       N  
ATOM    390  CA  GLU A 501     -13.719  -3.043 -22.264  1.00 62.98           C  
ANISOU  390  CA  GLU A 501     6584   9187   8158    500   -636  -1344       C  
ATOM    391  C   GLU A 501     -13.224  -2.374 -20.993  1.00 57.03           C  
ANISOU  391  C   GLU A 501     5989   8345   7335    409   -412  -1175       C  
ATOM    392  O   GLU A 501     -12.643  -3.023 -20.129  1.00 56.84           O  
ANISOU  392  O   GLU A 501     6040   8261   7298    166   -181  -1051       O  
ATOM    393  CB  GLU A 501     -12.706  -2.863 -23.395  1.00 66.32           C  
ANISOU  393  CB  GLU A 501     7331   9540   8329    611   -816  -1151       C  
ATOM    394  CG  GLU A 501     -12.087  -4.173 -23.866  1.00 72.31           C  
ANISOU  394  CG  GLU A 501     8110  10288   9077    425   -765  -1101       C  
ATOM    395  CD  GLU A 501     -11.162  -4.796 -22.833  1.00 75.83           C  
ANISOU  395  CD  GLU A 501     8644  10647   9522    157   -491   -915       C  
ATOM    396  OE1 GLU A 501     -10.513  -4.035 -22.086  1.00 76.45           O  
ANISOU  396  OE1 GLU A 501     8896  10650   9503    144   -396   -746       O  
ATOM    397  OE2 GLU A 501     -11.080  -6.043 -22.767  1.00 77.17           O  
ANISOU  397  OE2 GLU A 501     8729  10809   9782    -28   -390   -948       O  
ATOM    398  N   VAL A 502     -13.462  -1.072 -20.884  1.00 52.92           N  
ANISOU  398  N   VAL A 502     5549   7802   6757    624   -503  -1179       N  
ATOM    399  CA  VAL A 502     -13.114  -0.340 -19.676  1.00 49.50           C  
ANISOU  399  CA  VAL A 502     5258   7286   6263    558   -311  -1063       C  
ATOM    400  C   VAL A 502     -13.926  -0.897 -18.511  1.00 51.39           C  
ANISOU  400  C   VAL A 502     5251   7579   6697    371    -36  -1227       C  
ATOM    401  O   VAL A 502     -13.428  -1.009 -17.391  1.00 51.51           O  
ANISOU  401  O   VAL A 502     5418   7517   6637    185    196  -1102       O  
ATOM    402  CB  VAL A 502     -13.354   1.180 -19.840  1.00 45.42           C  
ANISOU  402  CB  VAL A 502     4871   6717   5667    843   -464  -1072       C  
ATOM    403  CG1 VAL A 502     -13.293   1.891 -18.497  1.00 42.45           C  
ANISOU  403  CG1 VAL A 502     4576   6275   5279    776   -254  -1035       C  
ATOM    404  CG2 VAL A 502     -12.338   1.772 -20.803  1.00 40.16           C  
ANISOU  404  CG2 VAL A 502     4564   5935   4761    957   -635   -858       C  
ATOM    405  N   GLY A 503     -15.170  -1.273 -18.793  1.00 52.01           N  
ANISOU  405  N   GLY A 503     4959   7781   7020    416    -58  -1525       N  
ATOM    406  CA  GLY A 503     -16.040  -1.863 -17.793  1.00 54.21           C  
ANISOU  406  CA  GLY A 503     4975   8103   7518    206    260  -1727       C  
ATOM    407  C   GLY A 503     -15.487  -3.157 -17.228  1.00 54.20           C  
ANISOU  407  C   GLY A 503     5091   8026   7477   -133    520  -1597       C  
ATOM    408  O   GLY A 503     -15.653  -3.445 -16.043  1.00 57.32           O  
ANISOU  408  O   GLY A 503     5535   8360   7885   -342    853  -1600       O  
ATOM    409  N   VAL A 504     -14.832  -3.940 -18.079  1.00 49.78           N  
ANISOU  409  N   VAL A 504     4614   7451   6850   -174    371  -1485       N  
ATOM    410  CA  VAL A 504     -14.191  -5.172 -17.640  1.00 50.37           C  
ANISOU  410  CA  VAL A 504     4845   7425   6869   -449    567  -1343       C  
ATOM    411  C   VAL A 504     -12.947  -4.869 -16.809  1.00 49.81           C  
ANISOU  411  C   VAL A 504     5170   7218   6538   -495    632  -1037       C  
ATOM    412  O   VAL A 504     -12.728  -5.472 -15.760  1.00 51.28           O  
ANISOU  412  O   VAL A 504     5523   7298   6665   -696    876   -956       O  
ATOM    413  CB  VAL A 504     -13.801  -6.072 -18.837  1.00 50.62           C  
ANISOU  413  CB  VAL A 504     4854   7472   6908   -452    376  -1327       C  
ATOM    414  CG1 VAL A 504     -13.130  -7.351 -18.351  1.00 49.07           C  
ANISOU  414  CG1 VAL A 504     4840   7143   6660   -709    571  -1185       C  
ATOM    415  CG2 VAL A 504     -15.025  -6.402 -19.671  1.00 51.49           C  
ANISOU  415  CG2 VAL A 504     4570   7719   7276   -401    264  -1663       C  
ATOM    416  N   LEU A 505     -12.137  -3.930 -17.285  1.00 47.39           N  
ANISOU  416  N   LEU A 505     5030   6902   6075   -308    408   -884       N  
ATOM    417  CA  LEU A 505     -10.890  -3.586 -16.617  1.00 44.58           C  
ANISOU  417  CA  LEU A 505     4996   6429   5511   -343    420   -638       C  
ATOM    418  C   LEU A 505     -11.152  -2.937 -15.260  1.00 48.73           C  
ANISOU  418  C   LEU A 505     5630   6905   5979   -384    607   -642       C  
ATOM    419  O   LEU A 505     -10.406  -3.147 -14.303  1.00 49.71           O  
ANISOU  419  O   LEU A 505     6008   6923   5957   -496    700   -496       O  
ATOM    420  CB  LEU A 505     -10.044  -2.674 -17.505  1.00 41.27           C  
ANISOU  420  CB  LEU A 505     4704   6001   4977   -165    183   -517       C  
ATOM    421  CG  LEU A 505      -9.724  -3.240 -18.892  1.00 42.49           C  
ANISOU  421  CG  LEU A 505     4812   6190   5141   -113     18   -509       C  
ATOM    422  CD1 LEU A 505      -9.013  -2.206 -19.759  1.00 44.10           C  
ANISOU  422  CD1 LEU A 505     5188   6358   5210     52   -150   -405       C  
ATOM    423  CD2 LEU A 505      -8.903  -4.524 -18.799  1.00 38.30           C  
ANISOU  423  CD2 LEU A 505     4349   5602   4602   -286     83   -410       C  
ATOM    424  N   ARG A 506     -12.230  -2.165 -15.182  1.00 50.91           N  
ANISOU  424  N   ARG A 506     5720   7256   6367   -275    649   -829       N  
ATOM    425  CA  ARG A 506     -12.615  -1.484 -13.952  1.00 52.81           C  
ANISOU  425  CA  ARG A 506     6044   7455   6565   -299    851   -875       C  
ATOM    426  C   ARG A 506     -13.002  -2.472 -12.850  1.00 53.60           C  
ANISOU  426  C   ARG A 506     6197   7496   6671   -555   1193   -916       C  
ATOM    427  O   ARG A 506     -13.156  -2.092 -11.692  1.00 53.10           O  
ANISOU  427  O   ARG A 506     6301   7366   6508   -616   1406   -921       O  
ATOM    428  CB  ARG A 506     -13.798  -0.556 -14.226  1.00 58.38           C  
ANISOU  428  CB  ARG A 506     6479   8260   7442   -104    823  -1117       C  
ATOM    429  CG  ARG A 506     -13.611   0.875 -13.763  1.00 63.48           C  
ANISOU  429  CG  ARG A 506     7298   8848   7971     63    774  -1076       C  
ATOM    430  CD  ARG A 506     -14.916   1.429 -13.218  1.00 71.23           C  
ANISOU  430  CD  ARG A 506     8046   9890   9128    143    949  -1349       C  
ATOM    431  NE  ARG A 506     -16.064   0.944 -13.976  1.00 76.39           N  
ANISOU  431  NE  ARG A 506     8268  10686  10070    204    913  -1622       N  
ATOM    432  CZ  ARG A 506     -16.766   1.682 -14.827  1.00 81.60           C  
ANISOU  432  CZ  ARG A 506     8700  11428  10878    500    663  -1805       C  
ATOM    433  NH1 ARG A 506     -16.448   2.954 -15.028  1.00 82.27           N  
ANISOU  433  NH1 ARG A 506     8987  11441  10831    754    462  -1718       N  
ATOM    434  NH2 ARG A 506     -17.793   1.146 -15.471  1.00 85.06           N  
ANISOU  434  NH2 ARG A 506     8720  12003  11595    548    602  -2089       N  
ATOM    435  N   LYS A 507     -13.165  -3.740 -13.214  1.00 55.01           N  
ANISOU  435  N   LYS A 507     6275   7676   6949   -708   1263   -949       N  
ATOM    436  CA  LYS A 507     -13.573  -4.763 -12.258  1.00 56.53           C  
ANISOU  436  CA  LYS A 507     6564   7771   7144   -973   1622   -987       C  
ATOM    437  C   LYS A 507     -12.403  -5.501 -11.611  1.00 52.18           C  
ANISOU  437  C   LYS A 507     6446   7045   6335  -1087   1632   -720       C  
ATOM    438  O   LYS A 507     -12.616  -6.406 -10.807  1.00 54.74           O  
ANISOU  438  O   LYS A 507     6963   7237   6599  -1296   1918   -707       O  
ATOM    439  CB  LYS A 507     -14.511  -5.774 -12.922  1.00 61.10           C  
ANISOU  439  CB  LYS A 507     6801   8414   7999  -1105   1733  -1208       C  
ATOM    440  CG  LYS A 507     -15.918  -5.254 -13.149  1.00 67.98           C  
ANISOU  440  CG  LYS A 507     7224   9437   9168  -1048   1825  -1553       C  
ATOM    441  CD  LYS A 507     -16.754  -6.238 -13.950  1.00 72.43           C  
ANISOU  441  CD  LYS A 507     7406  10078  10035  -1166   1858  -1805       C  
ATOM    442  CE  LYS A 507     -18.213  -5.811 -13.974  1.00 78.78           C  
ANISOU  442  CE  LYS A 507     7722  11028  11184  -1136   1989  -2208       C  
ATOM    443  NZ  LYS A 507     -18.379  -4.424 -14.499  1.00 80.18           N  
ANISOU  443  NZ  LYS A 507     7749  11337  11379   -768   1654  -2275       N  
ATOM    444  N   THR A 508     -11.177  -5.114 -11.951  1.00 45.16           N  
ANISOU  444  N   THR A 508     5720   6139   5299   -946   1326   -523       N  
ATOM    445  CA  THR A 508      -9.999  -5.790 -11.415  1.00 41.44           C  
ANISOU  445  CA  THR A 508     5609   5516   4618  -1002   1261   -306       C  
ATOM    446  C   THR A 508      -9.259  -4.973 -10.359  1.00 40.25           C  
ANISOU  446  C   THR A 508     5781   5284   4228   -939   1202   -185       C  
ATOM    447  O   THR A 508      -8.802  -3.864 -10.622  1.00 39.79           O  
ANISOU  447  O   THR A 508     5676   5287   4154   -794   1007   -165       O  
ATOM    448  CB  THR A 508      -9.004  -6.176 -12.526  1.00 39.80           C  
ANISOU  448  CB  THR A 508     5338   5334   4449   -914    968   -203       C  
ATOM    449  OG1 THR A 508      -8.515  -4.992 -13.174  1.00 40.42           O  
ANISOU  449  OG1 THR A 508     5319   5506   4533   -738    737   -182       O  
ATOM    450  CG2 THR A 508      -9.670  -7.085 -13.551  1.00 38.65           C  
ANISOU  450  CG2 THR A 508     4922   5252   4510   -979   1005   -327       C  
ATOM    451  N   ARG A 509      -9.146  -5.543  -9.164  1.00 41.63           N  
ANISOU  451  N   ARG A 509     6318   5299   4200  -1053   1374   -110       N  
ATOM    452  CA  ARG A 509      -8.342  -4.970  -8.091  1.00 39.59           C  
ANISOU  452  CA  ARG A 509     6430   4939   3674   -991   1274      1       C  
ATOM    453  C   ARG A 509      -7.535  -6.071  -7.421  1.00 38.86           C  
ANISOU  453  C   ARG A 509     6742   4657   3369  -1034   1218    158       C  
ATOM    454  O   ARG A 509      -7.965  -6.647  -6.425  1.00 43.42           O  
ANISOU  454  O   ARG A 509     7662   5077   3759  -1154   1477    180       O  
ATOM    455  CB  ARG A 509      -9.227  -4.269  -7.057  1.00 39.73           C  
ANISOU  455  CB  ARG A 509     6575   4933   3587  -1044   1563   -102       C  
ATOM    456  CG  ARG A 509      -9.697  -2.883  -7.476  1.00 38.36           C  
ANISOU  456  CG  ARG A 509     6107   4909   3557   -919   1517   -235       C  
ATOM    457  CD  ARG A 509     -10.642  -2.290  -6.436  1.00 43.05           C  
ANISOU  457  CD  ARG A 509     6811   5474   4071   -972   1844   -368       C  
ATOM    458  NE  ARG A 509     -10.976  -0.902  -6.738  1.00 45.90           N  
ANISOU  458  NE  ARG A 509     6952   5944   4545   -813   1763   -486       N  
ATOM    459  CZ  ARG A 509     -10.252   0.143  -6.351  1.00 43.70           C  
ANISOU  459  CZ  ARG A 509     6864   5627   4115   -697   1572   -428       C  
ATOM    460  NH1 ARG A 509      -9.145  -0.035  -5.643  1.00 42.07           N  
ANISOU  460  NH1 ARG A 509     7031   5301   3654   -716   1414   -276       N  
ATOM    461  NH2 ARG A 509     -10.634   1.370  -6.674  1.00 44.02           N  
ANISOU  461  NH2 ARG A 509     6724   5735   4266   -553   1521   -539       N  
ATOM    462  N   HIS A 510      -6.363  -6.361  -7.971  1.00 32.95           N  
ANISOU  462  N   HIS A 510     5971   3905   2644   -926    888    256       N  
ATOM    463  CA  HIS A 510      -5.526  -7.435  -7.459  1.00 34.04           C  
ANISOU  463  CA  HIS A 510     6462   3860   2612   -909    764    389       C  
ATOM    464  C   HIS A 510      -4.060  -7.126  -7.724  1.00 37.54           C  
ANISOU  464  C   HIS A 510     6868   4328   3066   -734    345    445       C  
ATOM    465  O   HIS A 510      -3.714  -6.576  -8.761  1.00 36.98           O  
ANISOU  465  O   HIS A 510     6437   4407   3206   -679    207    397       O  
ATOM    466  CB  HIS A 510      -5.914  -8.763  -8.113  1.00 34.32           C  
ANISOU  466  CB  HIS A 510     6420   3840   2781  -1014    901    394       C  
ATOM    467  CG  HIS A 510      -5.368  -9.966  -7.414  1.00 36.35           C  
ANISOU  467  CG  HIS A 510     7132   3849   2830  -1013    866    526       C  
ATOM    468  ND1 HIS A 510      -4.064 -10.390  -7.569  1.00 46.35           N  
ANISOU  468  ND1 HIS A 510     8489   5053   4069   -841    499    614       N  
ATOM    469  CD2 HIS A 510      -5.951 -10.848  -6.568  1.00 47.98           C  
ANISOU  469  CD2 HIS A 510     9019   5099   4113  -1154   1158    576       C  
ATOM    470  CE1 HIS A 510      -3.868 -11.474  -6.841  1.00 47.61           C  
ANISOU  470  CE1 HIS A 510     9113   4959   4018   -840    522    721       C  
ATOM    471  NE2 HIS A 510      -4.997 -11.775  -6.225  1.00 40.49           N  
ANISOU  471  NE2 HIS A 510     8448   3941   2995  -1041    934    715       N  
ATOM    472  N   VAL A 511      -3.204  -7.489  -6.776  1.00 40.06           N  
ANISOU  472  N   VAL A 511     7576   4489   3157   -645    148    529       N  
ATOM    473  CA  VAL A 511      -1.777  -7.181  -6.836  1.00 38.44           C  
ANISOU  473  CA  VAL A 511     7325   4301   2981   -476   -265    532       C  
ATOM    474  C   VAL A 511      -1.081  -7.822  -8.044  1.00 40.11           C  
ANISOU  474  C   VAL A 511     7217   4572   3452   -423   -421    526       C  
ATOM    475  O   VAL A 511      -0.099  -7.287  -8.557  1.00 40.75           O  
ANISOU  475  O   VAL A 511     7050   4745   3690   -335   -661    469       O  
ATOM    476  CB  VAL A 511      -1.070  -7.596  -5.516  1.00 46.36           C  
ANISOU  476  CB  VAL A 511     8842   5102   3669   -357   -487    600       C  
ATOM    477  CG1 VAL A 511      -1.264  -9.082  -5.239  1.00 44.79           C  
ANISOU  477  CG1 VAL A 511     8993   4694   3332   -368   -396    710       C  
ATOM    478  CG2 VAL A 511       0.408  -7.224  -5.535  1.00 47.19           C  
ANISOU  478  CG2 VAL A 511     8833   5243   3856   -174   -946    541       C  
ATOM    479  N   ASN A 512      -1.594  -8.958  -8.506  1.00 42.77           N  
ANISOU  479  N   ASN A 512     7561   4848   3844   -493   -255    565       N  
ATOM    480  CA  ASN A 512      -0.978  -9.663  -9.629  1.00 41.27           C  
ANISOU  480  CA  ASN A 512     7109   4694   3877   -440   -379    551       C  
ATOM    481  C   ASN A 512      -1.634  -9.351 -10.970  1.00 40.57           C  
ANISOU  481  C   ASN A 512     6605   4787   4023   -534   -210    475       C  
ATOM    482  O   ASN A 512      -1.318  -9.969 -11.984  1.00 40.13           O  
ANISOU  482  O   ASN A 512     6350   4762   4135   -514   -253    453       O  
ATOM    483  CB  ASN A 512      -0.957 -11.173  -9.383  1.00 41.99           C  
ANISOU  483  CB  ASN A 512     7492   4577   3886   -429   -358    630       C  
ATOM    484  CG  ASN A 512      -0.110 -11.557  -8.184  1.00 44.56           C  
ANISOU  484  CG  ASN A 512     8265   4700   3964   -266   -618    705       C  
ATOM    485  OD1 ASN A 512      -0.599 -12.170  -7.235  1.00 46.32           O  
ANISOU  485  OD1 ASN A 512     8961   4713   3924   -305   -484    797       O  
ATOM    486  ND2 ASN A 512       1.168 -11.197  -8.221  1.00 35.82           N  
ANISOU  486  ND2 ASN A 512     7025   3644   2941    -79   -992    650       N  
ATOM    487  N   ILE A 513      -2.553  -8.393 -10.968  1.00 39.12           N  
ANISOU  487  N   ILE A 513     6313   4711   3838   -612    -34    425       N  
ATOM    488  CA  ILE A 513      -3.154  -7.912 -12.204  1.00 34.80           C  
ANISOU  488  CA  ILE A 513     5409   4332   3482   -648     58    342       C  
ATOM    489  C   ILE A 513      -2.741  -6.469 -12.444  1.00 35.19           C  
ANISOU  489  C   ILE A 513     5318   4489   3563   -580    -52    309       C  
ATOM    490  O   ILE A 513      -2.791  -5.651 -11.529  1.00 36.64           O  
ANISOU  490  O   ILE A 513     5646   4650   3623   -571    -54    310       O  
ATOM    491  CB  ILE A 513      -4.683  -7.999 -12.162  1.00 32.56           C  
ANISOU  491  CB  ILE A 513     5072   4082   3219   -772    345    271       C  
ATOM    492  CG1 ILE A 513      -5.122  -9.444 -11.930  1.00 34.74           C  
ANISOU  492  CG1 ILE A 513     5502   4220   3480   -887    507    289       C  
ATOM    493  CG2 ILE A 513      -5.281  -7.466 -13.458  1.00 30.03           C  
ANISOU  493  CG2 ILE A 513     4397   3934   3082   -753    359    166       C  
ATOM    494  CD1 ILE A 513      -4.657 -10.394 -13.011  1.00 33.93           C  
ANISOU  494  CD1 ILE A 513     5258   4114   3520   -864    403    286       C  
ATOM    495  N   LEU A 514      -2.320  -6.169 -13.670  1.00 36.80           N  
ANISOU  495  N   LEU A 514     5279   4786   3916   -540   -125    276       N  
ATOM    496  CA  LEU A 514      -1.892  -4.820 -14.034  1.00 34.51           C  
ANISOU  496  CA  LEU A 514     4891   4560   3660   -497   -192    249       C  
ATOM    497  C   LEU A 514      -2.947  -3.798 -13.635  1.00 32.58           C  
ANISOU  497  C   LEU A 514     4678   4354   3348   -503    -71    213       C  
ATOM    498  O   LEU A 514      -4.105  -3.899 -14.038  1.00 32.91           O  
ANISOU  498  O   LEU A 514     4621   4456   3427   -515     62    162       O  
ATOM    499  CB  LEU A 514      -1.615  -4.731 -15.535  1.00 31.07           C  
ANISOU  499  CB  LEU A 514     4252   4197   3357   -475   -200    221       C  
ATOM    500  CG  LEU A 514      -1.120  -3.380 -16.053  1.00 31.14           C  
ANISOU  500  CG  LEU A 514     4213   4228   3392   -452   -223    202       C  
ATOM    501  CD1 LEU A 514       0.285  -3.093 -15.552  1.00 30.52           C  
ANISOU  501  CD1 LEU A 514     4147   4091   3359   -466   -349    190       C  
ATOM    502  CD2 LEU A 514      -1.166  -3.330 -17.577  1.00 30.66           C  
ANISOU  502  CD2 LEU A 514     4040   4217   3392   -430   -176    185       C  
ATOM    503  N   LEU A 515      -2.542  -2.822 -12.830  1.00 30.80           N  
ANISOU  503  N   LEU A 515     4574   4089   3039   -486   -131    213       N  
ATOM    504  CA  LEU A 515      -3.480  -1.861 -12.257  1.00 30.61           C  
ANISOU  504  CA  LEU A 515     4616   4076   2938   -477    -14    168       C  
ATOM    505  C   LEU A 515      -4.067  -0.871 -13.265  1.00 30.92           C  
ANISOU  505  C   LEU A 515     4499   4185   3062   -412     25    118       C  
ATOM    506  O   LEU A 515      -3.367  -0.006 -13.788  1.00 29.93           O  
ANISOU  506  O   LEU A 515     4364   4041   2967   -381    -59    127       O  
ATOM    507  CB  LEU A 515      -2.821  -1.091 -11.115  1.00 31.28           C  
ANISOU  507  CB  LEU A 515     4904   4083   2898   -472   -108    169       C  
ATOM    508  CG  LEU A 515      -3.779  -0.177 -10.353  1.00 34.97           C  
ANISOU  508  CG  LEU A 515     5482   4541   3263   -461     34    112       C  
ATOM    509  CD1 LEU A 515      -4.921  -0.997  -9.771  1.00 35.85           C  
ANISOU  509  CD1 LEU A 515     5664   4651   3306   -516    254     95       C  
ATOM    510  CD2 LEU A 515      -3.053   0.604  -9.264  1.00 35.02           C  
ANISOU  510  CD2 LEU A 515     5711   4462   3132   -455    -83     96       C  
ATOM    511  N   PHE A 516      -5.362  -1.004 -13.524  1.00 30.84           N  
ANISOU  511  N   PHE A 516     4382   4243   3094   -389    153     48       N  
ATOM    512  CA  PHE A 516      -6.089  -0.002 -14.289  1.00 31.96           C  
ANISOU  512  CA  PHE A 516     4419   4435   3288   -274    152    -22       C  
ATOM    513  C   PHE A 516      -6.196   1.277 -13.455  1.00 35.95           C  
ANISOU  513  C   PHE A 516     5063   4882   3714   -227    178    -49       C  
ATOM    514  O   PHE A 516      -6.500   1.216 -12.263  1.00 35.38           O  
ANISOU  514  O   PHE A 516     5099   4780   3564   -281    283    -77       O  
ATOM    515  CB  PHE A 516      -7.481  -0.523 -14.642  1.00 28.73           C  
ANISOU  515  CB  PHE A 516     3814   4121   2981   -247    251   -144       C  
ATOM    516  CG  PHE A 516      -8.451   0.555 -15.038  1.00 32.78           C  
ANISOU  516  CG  PHE A 516     4233   4679   3544    -84    235   -259       C  
ATOM    517  CD1 PHE A 516      -8.503   1.009 -16.346  1.00 33.50           C  
ANISOU  517  CD1 PHE A 516     4272   4794   3661     64     83   -268       C  
ATOM    518  CD2 PHE A 516      -9.317   1.110 -14.103  1.00 33.42           C  
ANISOU  518  CD2 PHE A 516     4305   4761   3631    -60    371   -368       C  
ATOM    519  CE1 PHE A 516      -9.397   1.998 -16.719  1.00 33.79           C  
ANISOU  519  CE1 PHE A 516     4261   4849   3729    263     21   -377       C  
ATOM    520  CE2 PHE A 516     -10.212   2.100 -14.467  1.00 33.06           C  
ANISOU  520  CE2 PHE A 516     4159   4749   3654    128    332   -497       C  
ATOM    521  CZ  PHE A 516     -10.254   2.543 -15.777  1.00 34.17           C  
ANISOU  521  CZ  PHE A 516     4257   4906   3819    305    134   -499       C  
ATOM    522  N   MET A 517      -5.956   2.429 -14.079  1.00 34.23           N  
ANISOU  522  N   MET A 517     4884   4624   3498   -131    100    -43       N  
ATOM    523  CA  MET A 517      -5.971   3.701 -13.355  1.00 33.13           C  
ANISOU  523  CA  MET A 517     4899   4401   3290    -87    117    -74       C  
ATOM    524  C   MET A 517      -6.986   4.705 -13.896  1.00 35.96           C  
ANISOU  524  C   MET A 517     5226   4756   3680     96    123   -156       C  
ATOM    525  O   MET A 517      -7.487   5.549 -13.157  1.00 36.17           O  
ANISOU  525  O   MET A 517     5333   4737   3673    159    184   -230       O  
ATOM    526  CB  MET A 517      -4.570   4.319 -13.328  1.00 29.64           C  
ANISOU  526  CB  MET A 517     4598   3849   2813   -159     24     -6       C  
ATOM    527  CG  MET A 517      -3.603   3.567 -12.433  1.00 25.64           C  
ANISOU  527  CG  MET A 517     4142   3331   2271   -290    -33     26       C  
ATOM    528  SD  MET A 517      -1.949   4.268 -12.409  1.00 33.38           S  
ANISOU  528  SD  MET A 517     5189   4203   3289   -383   -161     30       S  
ATOM    529  CE  MET A 517      -2.275   5.913 -11.772  1.00 32.36           C  
ANISOU  529  CE  MET A 517     5252   3959   3086   -344   -122    -38       C  
ATOM    530  N   GLY A 518      -7.290   4.617 -15.186  1.00 38.29           N  
ANISOU  530  N   GLY A 518     5429   5090   4029    205     43   -155       N  
ATOM    531  CA  GLY A 518      -8.266   5.509 -15.777  1.00 37.37           C  
ANISOU  531  CA  GLY A 518     5303   4963   3934    432    -14   -243       C  
ATOM    532  C   GLY A 518      -8.310   5.439 -17.286  1.00 38.84           C  
ANISOU  532  C   GLY A 518     5490   5155   4113    559   -152   -213       C  
ATOM    533  O   GLY A 518      -7.578   4.675 -17.912  1.00 38.13           O  
ANISOU  533  O   GLY A 518     5392   5085   4009    451   -170   -127       O  
ATOM    534  N   TYR A 519      -9.179   6.249 -17.877  1.00 39.90           N  
ANISOU  534  N   TYR A 519     5657   5260   4242    813   -261   -294       N  
ATOM    535  CA  TYR A 519      -9.298   6.288 -19.325  1.00 40.81           C  
ANISOU  535  CA  TYR A 519     5855   5356   4295    981   -427   -271       C  
ATOM    536  C   TYR A 519      -9.397   7.711 -19.850  1.00 45.86           C  
ANISOU  536  C   TYR A 519     6809   5807   4808   1215   -527   -238       C  
ATOM    537  O   TYR A 519      -9.841   8.621 -19.151  1.00 45.69           O  
ANISOU  537  O   TYR A 519     6840   5715   4807   1322   -509   -304       O  
ATOM    538  CB  TYR A 519     -10.503   5.469 -19.791  1.00 38.71           C  
ANISOU  538  CB  TYR A 519     5281   5270   4157   1114   -542   -449       C  
ATOM    539  CG  TYR A 519     -11.840   6.028 -19.359  1.00 41.36           C  
ANISOU  539  CG  TYR A 519     5434   5659   4621   1335   -597   -663       C  
ATOM    540  CD1 TYR A 519     -12.392   5.688 -18.131  1.00 41.93           C  
ANISOU  540  CD1 TYR A 519     5258   5826   4846   1210   -407   -791       C  
ATOM    541  CD2 TYR A 519     -12.553   6.889 -20.183  1.00 44.89           C  
ANISOU  541  CD2 TYR A 519     5974   6050   5032   1682   -832   -750       C  
ATOM    542  CE1 TYR A 519     -13.615   6.192 -17.734  1.00 44.17           C  
ANISOU  542  CE1 TYR A 519     5337   6164   5281   1404   -415  -1023       C  
ATOM    543  CE2 TYR A 519     -13.776   7.400 -19.796  1.00 47.57           C  
ANISOU  543  CE2 TYR A 519     6102   6445   5529   1915   -899   -984       C  
ATOM    544  CZ  TYR A 519     -14.303   7.046 -18.571  1.00 47.86           C  
ANISOU  544  CZ  TYR A 519     5837   6594   5756   1763   -672  -1131       C  
ATOM    545  OH  TYR A 519     -15.521   7.547 -18.181  1.00 51.12           O  
ANISOU  545  OH  TYR A 519     6002   7066   6358   1985   -697  -1398       O  
ATOM    546  N   SER A 520      -8.980   7.888 -21.096  1.00 49.75           N  
ANISOU  546  N   SER A 520     7552   6196   5152   1296   -619   -137       N  
ATOM    547  CA  SER A 520      -9.036   9.183 -21.747  1.00 52.57           C  
ANISOU  547  CA  SER A 520     8307   6326   5342   1525   -710    -80       C  
ATOM    548  C   SER A 520      -9.977   9.114 -22.936  1.00 52.66           C  
ANISOU  548  C   SER A 520     8368   6367   5274   1858   -982   -161       C  
ATOM    549  O   SER A 520      -9.988   8.132 -23.679  1.00 51.85           O  
ANISOU  549  O   SER A 520     8151   6389   5160   1831  -1054   -176       O  
ATOM    550  CB  SER A 520      -7.643   9.607 -22.207  1.00 57.72           C  
ANISOU  550  CB  SER A 520     9324   6768   5840   1325   -549    114       C  
ATOM    551  OG  SER A 520      -7.318  10.893 -21.715  1.00 65.87           O  
ANISOU  551  OG  SER A 520    10639   7571   6819   1323   -460    161       O  
ATOM    552  N   THR A 521     -10.773  10.161 -23.105  1.00 54.33           N  
ANISOU  552  N   THR A 521     8759   6455   5428   2195  -1157   -231       N  
ATOM    553  CA  THR A 521     -11.688  10.247 -24.233  1.00 55.13           C  
ANISOU  553  CA  THR A 521     8957   6557   5433   2581  -1488   -328       C  
ATOM    554  C   THR A 521     -11.168  11.278 -25.229  1.00 55.60           C  
ANISOU  554  C   THR A 521     9675   6289   5160   2746  -1545   -141       C  
ATOM    555  O   THR A 521     -11.455  11.208 -26.420  1.00 59.22           O  
ANISOU  555  O   THR A 521    10384   6696   5421   2991  -1778   -135       O  
ATOM    556  CB  THR A 521     -13.123  10.579 -23.771  1.00 57.79           C  
ANISOU  556  CB  THR A 521     8982   7005   5972   2909  -1701   -597       C  
ATOM    557  OG1 THR A 521     -14.059   9.775 -24.499  1.00 61.46           O  
ANISOU  557  OG1 THR A 521     9153   7672   6528   3112  -1982   -801       O  
ATOM    558  CG2 THR A 521     -13.447  12.054 -23.966  1.00 60.75           C  
ANISOU  558  CG2 THR A 521     9775   7108   6200   3267  -1856   -579       C  
ATOM    559  N   LYS A 522     -10.383  12.224 -24.723  1.00 58.12           N  
ANISOU  559  N   LYS A 522    10302   6371   5408   2597  -1317      4       N  
ATOM    560  CA  LYS A 522      -9.753  13.251 -25.545  1.00 62.64           C  
ANISOU  560  CA  LYS A 522    11546   6580   5673   2669  -1269    197       C  
ATOM    561  C   LYS A 522      -8.344  13.501 -25.014  1.00 63.96           C  
ANISOU  561  C   LYS A 522    11843   6605   5852   2224   -876    353       C  
ATOM    562  O   LYS A 522      -8.127  13.465 -23.802  1.00 61.80           O  
ANISOU  562  O   LYS A 522    11256   6431   5796   2011   -733    296       O  
ATOM    563  CB  LYS A 522     -10.574  14.533 -25.522  1.00 63.76           C  
ANISOU  563  CB  LYS A 522    11975   6508   5743   3057  -1462    134       C  
ATOM    564  N   PRO A 523      -7.376  13.766 -25.909  1.00 66.09           N  
ANISOU  564  N   PRO A 523    12583   6635   5892   2079   -695    530       N  
ATOM    565  CA  PRO A 523      -7.463  13.956 -27.367  1.00 68.85           C  
ANISOU  565  CA  PRO A 523    13286   6853   6022   2214   -752    539       C  
ATOM    566  C   PRO A 523      -7.876  12.711 -28.158  1.00 67.31           C  
ANISOU  566  C   PRO A 523    12852   6906   5817   2301   -936    470       C  
ATOM    567  O   PRO A 523      -8.426  12.840 -29.250  1.00 68.56           O  
ANISOU  567  O   PRO A 523    13224   7001   5824   2537  -1114    405       O  
ATOM    568  CB  PRO A 523      -6.041  14.385 -27.750  1.00 69.30           C  
ANISOU  568  CB  PRO A 523    13675   6663   5993   1840   -349    673       C  
ATOM    569  CG  PRO A 523      -5.175  13.853 -26.659  1.00 66.12           C  
ANISOU  569  CG  PRO A 523    12960   6374   5788   1484   -131    725       C  
ATOM    570  CD  PRO A 523      -5.998  13.933 -25.415  1.00 64.00           C  
ANISOU  570  CD  PRO A 523    12353   6260   5706   1630   -317    623       C  
ATOM    571  N   GLN A 524      -7.619  11.527 -27.618  1.00 65.22           N  
ANISOU  571  N   GLN A 524    12175   6909   5696   2114   -900    469       N  
ATOM    572  CA  GLN A 524      -8.107  10.305 -28.247  1.00 66.02           C  
ANISOU  572  CA  GLN A 524    12004   7263   5816   2197  -1093    370       C  
ATOM    573  C   GLN A 524      -8.442   9.255 -27.201  1.00 57.98           C  
ANISOU  573  C   GLN A 524    10324   6582   5122   2055  -1114    231       C  
ATOM    574  O   GLN A 524      -8.192   9.456 -26.012  1.00 55.23           O  
ANISOU  574  O   GLN A 524     9744   6267   4972   1867   -952    221       O  
ATOM    575  CB  GLN A 524      -7.101   9.759 -29.265  1.00 71.59           C  
ANISOU  575  CB  GLN A 524    12901   7902   6396   1957   -868    464       C  
ATOM    576  CG  GLN A 524      -5.725   9.435 -28.711  1.00 73.70           C  
ANISOU  576  CG  GLN A 524    13106   8162   6735   1536   -497    586       C  
ATOM    577  CD  GLN A 524      -4.796   8.891 -29.780  1.00 81.61           C  
ANISOU  577  CD  GLN A 524    14262   9104   7641   1334   -272    638       C  
ATOM    578  OE1 GLN A 524      -5.193   8.061 -30.600  1.00 83.52           O  
ANISOU  578  OE1 GLN A 524    14446   9469   7820   1449   -425    574       O  
ATOM    579  NE2 GLN A 524      -3.555   9.365 -29.783  1.00 85.03           N  
ANISOU  579  NE2 GLN A 524    14882   9343   8083   1028     99    727       N  
ATOM    580  N   LEU A 525      -9.030   8.149 -27.642  1.00 55.79           N  
ANISOU  580  N   LEU A 525     9752   6537   4909   2129  -1298    103       N  
ATOM    581  CA  LEU A 525      -9.351   7.058 -26.736  1.00 51.67           C  
ANISOU  581  CA  LEU A 525     8624   6304   4704   1952  -1266    -39       C  
ATOM    582  C   LEU A 525      -8.068   6.464 -26.191  1.00 45.82           C  
ANISOU  582  C   LEU A 525     7773   5582   4052   1537   -938     81       C  
ATOM    583  O   LEU A 525      -7.170   6.101 -26.950  1.00 48.49           O  
ANISOU  583  O   LEU A 525     8307   5855   4263   1396   -811    186       O  
ATOM    584  CB  LEU A 525     -10.171   5.975 -27.433  1.00 53.13           C  
ANISOU  584  CB  LEU A 525     8551   6698   4938   2086  -1510   -211       C  
ATOM    585  CG  LEU A 525     -11.621   6.305 -27.780  1.00 58.89           C  
ANISOU  585  CG  LEU A 525     9186   7493   5695   2502  -1896   -430       C  
ATOM    586  CD1 LEU A 525     -12.390   5.017 -28.024  1.00 57.04           C  
ANISOU  586  CD1 LEU A 525     8495   7523   5653   2503  -2064   -661       C  
ATOM    587  CD2 LEU A 525     -12.288   7.151 -26.693  1.00 60.99           C  
ANISOU  587  CD2 LEU A 525     9274   7755   6146   2616  -1900   -526       C  
ATOM    588  N   ALA A 526      -7.982   6.376 -24.871  1.00 38.98           N  
ANISOU  588  N   ALA A 526     6608   4800   3402   1359   -808     48       N  
ATOM    589  CA  ALA A 526      -6.789   5.849 -24.235  1.00 38.96           C  
ANISOU  589  CA  ALA A 526     6493   4815   3497   1010   -560    135       C  
ATOM    590  C   ALA A 526      -7.132   5.199 -22.909  1.00 41.03           C  
ANISOU  590  C   ALA A 526     6354   5250   3986    883   -519     41       C  
ATOM    591  O   ALA A 526      -8.087   5.591 -22.241  1.00 40.80           O  
ANISOU  591  O   ALA A 526     6199   5268   4036   1015   -588    -66       O  
ATOM    592  CB  ALA A 526      -5.760   6.949 -24.035  1.00 38.94           C  
ANISOU  592  CB  ALA A 526     6805   4579   3411    883   -374    265       C  
ATOM    593  N   ILE A 527      -6.347   4.195 -22.541  1.00 39.40           N  
ANISOU  593  N   ILE A 527     5974   5122   3874    635   -396     75       N  
ATOM    594  CA  ILE A 527      -6.463   3.571 -21.235  1.00 36.60           C  
ANISOU  594  CA  ILE A 527     5350   4879   3679    490   -327     22       C  
ATOM    595  C   ILE A 527      -5.169   3.812 -20.474  1.00 35.79           C  
ANISOU  595  C   ILE A 527     5325   4684   3590    276   -191    116       C  
ATOM    596  O   ILE A 527      -4.079   3.714 -21.037  1.00 34.81           O  
ANISOU  596  O   ILE A 527     5294   4491   3440    162   -123    190       O  
ATOM    597  CB  ILE A 527      -6.757   2.066 -21.354  1.00 37.58           C  
ANISOU  597  CB  ILE A 527     5213   5160   3906    413   -341    -43       C  
ATOM    598  CG1 ILE A 527      -8.139   1.853 -21.978  1.00 39.65           C  
ANISOU  598  CG1 ILE A 527     5334   5529   4204    615   -497   -198       C  
ATOM    599  CG2 ILE A 527      -6.699   1.397 -19.993  1.00 38.90           C  
ANISOU  599  CG2 ILE A 527     5210   5385   4187    241   -234    -62       C  
ATOM    600  CD1 ILE A 527      -8.413   0.421 -22.396  1.00 39.94           C  
ANISOU  600  CD1 ILE A 527     5152   5690   4334    538   -520   -280       C  
ATOM    601  N   VAL A 528      -5.298   4.151 -19.197  1.00 35.61           N  
ANISOU  601  N   VAL A 528     5259   4659   3614    227   -151     87       N  
ATOM    602  CA  VAL A 528      -4.145   4.440 -18.358  1.00 34.05           C  
ANISOU  602  CA  VAL A 528     5126   4379   3434     49    -78    135       C  
ATOM    603  C   VAL A 528      -3.961   3.366 -17.298  1.00 32.47           C  
ANISOU  603  C   VAL A 528     4763   4274   3301    -77    -68    115       C  
ATOM    604  O   VAL A 528      -4.902   3.006 -16.590  1.00 30.47           O  
ANISOU  604  O   VAL A 528     4423   4095   3057    -42    -51     55       O  
ATOM    605  CB  VAL A 528      -4.307   5.789 -17.650  1.00 35.55           C  
ANISOU  605  CB  VAL A 528     5481   4449   3577     97    -59    115       C  
ATOM    606  CG1 VAL A 528      -3.087   6.093 -16.794  1.00 34.33           C  
ANISOU  606  CG1 VAL A 528     5379   4211   3452    -92    -18    128       C  
ATOM    607  CG2 VAL A 528      -4.551   6.885 -18.672  1.00 37.48           C  
ANISOU  607  CG2 VAL A 528     5958   4554   3727    250    -75    145       C  
ATOM    608  N   THR A 529      -2.742   2.857 -17.189  1.00 31.30           N  
ANISOU  608  N   THR A 529     4588   4105   3200   -219    -69    153       N  
ATOM    609  CA  THR A 529      -2.422   1.878 -16.163  1.00 33.01           C  
ANISOU  609  CA  THR A 529     4726   4368   3447   -307    -98    146       C  
ATOM    610  C   THR A 529      -1.156   2.293 -15.440  1.00 32.83           C  
ANISOU  610  C   THR A 529     4759   4265   3452   -409   -150    138       C  
ATOM    611  O   THR A 529      -0.509   3.265 -15.820  1.00 33.37           O  
ANISOU  611  O   THR A 529     4886   4246   3549   -448   -126    126       O  
ATOM    612  CB  THR A 529      -2.210   0.469 -16.766  1.00 30.92           C  
ANISOU  612  CB  THR A 529     4328   4175   3246   -338   -113    164       C  
ATOM    613  OG1 THR A 529      -0.957   0.428 -17.459  1.00 32.32           O  
ANISOU  613  OG1 THR A 529     4475   4311   3495   -401   -121    178       O  
ATOM    614  CG2 THR A 529      -3.335   0.117 -17.721  1.00 28.10           C  
ANISOU  614  CG2 THR A 529     3898   3894   2885   -245    -89    139       C  
ATOM    615  N   GLN A 530      -0.806   1.548 -14.401  1.00 31.46           N  
ANISOU  615  N   GLN A 530     4581   4105   3266   -450   -228    129       N  
ATOM    616  CA  GLN A 530       0.460   1.754 -13.720  1.00 33.58           C  
ANISOU  616  CA  GLN A 530     4864   4313   3581   -520   -348     83       C  
ATOM    617  C   GLN A 530       1.613   1.457 -14.663  1.00 36.77           C  
ANISOU  617  C   GLN A 530     5105   4715   4151   -580   -362     57       C  
ATOM    618  O   GLN A 530       1.449   0.774 -15.680  1.00 36.83           O  
ANISOU  618  O   GLN A 530     5023   4771   4201   -562   -294     94       O  
ATOM    619  CB  GLN A 530       0.567   0.830 -12.512  1.00 34.75           C  
ANISOU  619  CB  GLN A 530     5090   4465   3649   -504   -469     85       C  
ATOM    620  CG  GLN A 530       0.709  -0.636 -12.879  1.00 37.13           C  
ANISOU  620  CG  GLN A 530     5303   4806   3997   -486   -499    127       C  
ATOM    621  CD  GLN A 530       0.836  -1.533 -11.670  1.00 42.65           C  
ANISOU  621  CD  GLN A 530     6170   5458   4578   -453   -622    147       C  
ATOM    622  OE1 GLN A 530       0.056  -2.468 -11.492  1.00 42.07           O  
ANISOU  622  OE1 GLN A 530     6181   5382   4421   -445   -535    206       O  
ATOM    623  NE2 GLN A 530       1.830  -1.261 -10.834  1.00 45.59           N  
ANISOU  623  NE2 GLN A 530     6612   5775   4936   -434   -828     85       N  
ATOM    624  N   TRP A 531       2.788   1.958 -14.311  1.00 35.90           N  
ANISOU  624  N   TRP A 531     4943   4547   4149   -658   -445    -35       N  
ATOM    625  CA  TRP A 531       3.994   1.624 -15.046  1.00 35.38           C  
ANISOU  625  CA  TRP A 531     4675   4480   4286   -731   -442   -110       C  
ATOM    626  C   TRP A 531       4.790   0.540 -14.325  1.00 38.51           C  
ANISOU  626  C   TRP A 531     4955   4910   4767   -684   -664   -176       C  
ATOM    627  O   TRP A 531       5.062   0.641 -13.128  1.00 40.45           O  
ANISOU  627  O   TRP A 531     5276   5130   4964   -652   -861   -232       O  
ATOM    628  CB  TRP A 531       4.858   2.862 -15.249  1.00 33.80           C  
ANISOU  628  CB  TRP A 531     4439   4185   4216   -869   -364   -218       C  
ATOM    629  CG  TRP A 531       6.113   2.573 -15.984  1.00 36.36           C  
ANISOU  629  CG  TRP A 531     4523   4506   4787   -974   -304   -335       C  
ATOM    630  CD1 TRP A 531       7.359   2.457 -15.453  1.00 38.99           C  
ANISOU  630  CD1 TRP A 531     4632   4838   5345  -1035   -453   -521       C  
ATOM    631  CD2 TRP A 531       6.250   2.354 -17.392  1.00 39.50           C  
ANISOU  631  CD2 TRP A 531     4870   4899   5241  -1024    -74   -304       C  
ATOM    632  NE1 TRP A 531       8.271   2.186 -16.443  1.00 42.87           N  
ANISOU  632  NE1 TRP A 531     4894   5330   6066  -1132   -298   -623       N  
ATOM    633  CE2 TRP A 531       7.614   2.117 -17.645  1.00 41.80           C  
ANISOU  633  CE2 TRP A 531     4887   5185   5809  -1135    -46   -480       C  
ATOM    634  CE3 TRP A 531       5.353   2.338 -18.465  1.00 41.01           C  
ANISOU  634  CE3 TRP A 531     5225   5088   5270   -973     99   -166       C  
ATOM    635  CZ2 TRP A 531       8.105   1.864 -18.923  1.00 42.64           C  
ANISOU  635  CZ2 TRP A 531     4901   5277   6024  -1217    203   -511       C  
ATOM    636  CZ3 TRP A 531       5.841   2.089 -19.736  1.00 42.90           C  
ANISOU  636  CZ3 TRP A 531     5414   5306   5578  -1040    305   -183       C  
ATOM    637  CH2 TRP A 531       7.205   1.855 -19.953  1.00 44.04           C  
ANISOU  637  CH2 TRP A 531     5306   5438   5988  -1171    382   -348       C  
ATOM    638  N   CYS A 532       5.162  -0.499 -15.063  1.00 38.21           N  
ANISOU  638  N   CYS A 532     4765   4916   4838   -658   -648   -177       N  
ATOM    639  CA  CYS A 532       5.966  -1.573 -14.502  1.00 40.17           C  
ANISOU  639  CA  CYS A 532     4908   5173   5182   -576   -875   -248       C  
ATOM    640  C   CYS A 532       7.435  -1.332 -14.793  1.00 42.07           C  
ANISOU  640  C   CYS A 532     4863   5406   5715   -642   -928   -447       C  
ATOM    641  O   CYS A 532       7.813  -1.029 -15.924  1.00 39.70           O  
ANISOU  641  O   CYS A 532     4413   5108   5562   -751   -701   -494       O  
ATOM    642  CB  CYS A 532       5.540  -2.925 -15.071  1.00 41.17           C  
ANISOU  642  CB  CYS A 532     5029   5332   5281   -497   -836   -160       C  
ATOM    643  SG  CYS A 532       3.866  -3.414 -14.633  1.00 45.89           S  
ANISOU  643  SG  CYS A 532     5901   5934   5601   -447   -767     14       S  
ATOM    644  N   GLU A 533       8.256  -1.457 -13.758  1.00 46.77           N  
ANISOU  644  N   GLU A 533     5393   5985   6393   -575  -1223   -583       N  
ATOM    645  CA  GLU A 533       9.698  -1.350 -13.906  1.00 53.47           C  
ANISOU  645  CA  GLU A 533     5899   6839   7578   -619  -1323   -833       C  
ATOM    646  C   GLU A 533      10.256  -2.723 -14.243  1.00 55.13           C  
ANISOU  646  C   GLU A 533     5932   7080   7934   -478  -1437   -884       C  
ATOM    647  O   GLU A 533       9.851  -3.722 -13.655  1.00 58.03           O  
ANISOU  647  O   GLU A 533     6488   7429   8132   -300  -1633   -776       O  
ATOM    648  CB  GLU A 533      10.331  -0.840 -12.611  1.00 59.93           C  
ANISOU  648  CB  GLU A 533     6712   7629   8431   -579  -1656   -999       C  
ATOM    649  CG  GLU A 533       9.720   0.446 -12.075  1.00 63.61           C  
ANISOU  649  CG  GLU A 533     7406   8045   8717   -689  -1582   -951       C  
ATOM    650  CD  GLU A 533      10.131   1.673 -12.867  1.00 68.11           C  
ANISOU  650  CD  GLU A 533     7814   8576   9490   -928  -1297  -1061       C  
ATOM    651  OE1 GLU A 533       9.534   2.747 -12.640  1.00 69.35           O  
ANISOU  651  OE1 GLU A 533     8183   8668   9497  -1017  -1181  -1000       O  
ATOM    652  OE2 GLU A 533      11.050   1.570 -13.708  1.00 69.89           O  
ANISOU  652  OE2 GLU A 533     7721   8814  10020  -1031  -1167  -1216       O  
ATOM    653  N   GLY A 534      11.184  -2.772 -15.189  1.00 53.97           N  
ANISOU  653  N   GLY A 534     5447   6960   8101   -562  -1286  -1055       N  
ATOM    654  CA  GLY A 534      11.798  -4.030 -15.570  1.00 54.30           C  
ANISOU  654  CA  GLY A 534     5287   7025   8321   -419  -1378  -1141       C  
ATOM    655  C   GLY A 534      11.282  -4.565 -16.891  1.00 53.59           C  
ANISOU  655  C   GLY A 534     5228   6952   8183   -469  -1043  -1013       C  
ATOM    656  O   GLY A 534      10.945  -3.801 -17.794  1.00 53.47           O  
ANISOU  656  O   GLY A 534     5254   6936   8126   -649   -704   -958       O  
ATOM    657  N   SER A 535      11.215  -5.885 -17.006  1.00 52.17           N  
ANISOU  657  N   SER A 535     5067   6767   7989   -297  -1151   -971       N  
ATOM    658  CA  SER A 535      10.819  -6.507 -18.260  1.00 49.99           C  
ANISOU  658  CA  SER A 535     4805   6505   7684   -330   -868   -891       C  
ATOM    659  C   SER A 535       9.812  -7.632 -18.059  1.00 45.89           C  
ANISOU  659  C   SER A 535     4565   5951   6919   -191   -961   -691       C  
ATOM    660  O   SER A 535       9.485  -7.996 -16.929  1.00 48.21           O  
ANISOU  660  O   SER A 535     5058   6195   7065    -68  -1223   -610       O  
ATOM    661  CB  SER A 535      12.053  -7.011 -19.007  1.00 52.85           C  
ANISOU  661  CB  SER A 535     4795   6883   8400   -314   -791  -1134       C  
ATOM    662  OG  SER A 535      13.090  -7.339 -18.103  1.00 56.22           O  
ANISOU  662  OG  SER A 535     4986   7303   9071   -157  -1145  -1345       O  
ATOM    663  N   SER A 536       9.313  -8.169 -19.165  1.00 40.19           N  
ANISOU  663  N   SER A 536     3884   5242   6144   -225   -729   -622       N  
ATOM    664  CA  SER A 536       8.391  -9.293 -19.114  1.00 38.55           C  
ANISOU  664  CA  SER A 536     3903   4992   5753   -129   -777   -474       C  
ATOM    665  C   SER A 536       9.116 -10.553 -18.661  1.00 38.46           C  
ANISOU  665  C   SER A 536     3836   4901   5876     70  -1021   -557       C  
ATOM    666  O   SER A 536      10.341 -10.626 -18.706  1.00 38.71           O  
ANISOU  666  O   SER A 536     3588   4939   6182    144  -1120   -758       O  
ATOM    667  CB  SER A 536       7.766  -9.533 -20.485  1.00 35.92           C  
ANISOU  667  CB  SER A 536     3604   4693   5352   -211   -495   -427       C  
ATOM    668  OG  SER A 536       8.728 -10.036 -21.391  1.00 36.81           O  
ANISOU  668  OG  SER A 536     3494   4807   5685   -190   -388   -587       O  
ATOM    669  N   LEU A 537       8.350 -11.543 -18.220  1.00 39.27           N  
ANISOU  669  N   LEU A 537     4208   4913   5800    158  -1114   -418       N  
ATOM    670  CA  LEU A 537       8.906 -12.842 -17.858  1.00 44.17           C  
ANISOU  670  CA  LEU A 537     4869   5411   6504    367  -1335   -466       C  
ATOM    671  C   LEU A 537       9.556 -13.511 -19.071  1.00 48.53           C  
ANISOU  671  C   LEU A 537     5174   5978   7289    402  -1199   -613       C  
ATOM    672  O   LEU A 537      10.519 -14.266 -18.932  1.00 51.37           O  
ANISOU  672  O   LEU A 537     5399   6269   7850    595  -1389   -757       O  
ATOM    673  CB  LEU A 537       7.807 -13.741 -17.289  1.00 41.41           C  
ANISOU  673  CB  LEU A 537     4915   4927   5890    396  -1362   -273       C  
ATOM    674  CG  LEU A 537       8.152 -15.205 -17.022  1.00 41.84           C  
ANISOU  674  CG  LEU A 537     5125   4798   5973    600  -1541   -279       C  
ATOM    675  CD1 LEU A 537       9.202 -15.320 -15.928  1.00 42.49           C  
ANISOU  675  CD1 LEU A 537     5235   4791   6119    844  -1935   -363       C  
ATOM    676  CD2 LEU A 537       6.895 -15.978 -16.657  1.00 40.92           C  
ANISOU  676  CD2 LEU A 537     5411   4540   5596    535  -1440    -88       C  
ATOM    677  N   TYR A 538       9.019 -13.230 -20.256  1.00 46.93           N  
ANISOU  677  N   TYR A 538     4929   5857   7045    235   -881   -590       N  
ATOM    678  CA  TYR A 538       9.565 -13.767 -21.495  1.00 50.08           C  
ANISOU  678  CA  TYR A 538     5137   6272   7620    242   -695   -731       C  
ATOM    679  C   TYR A 538      11.007 -13.323 -21.669  1.00 52.42           C  
ANISOU  679  C   TYR A 538     5057   6618   8240    272   -694   -974       C  
ATOM    680  O   TYR A 538      11.887 -14.128 -21.967  1.00 55.87           O  
ANISOU  680  O   TYR A 538     5296   7015   8916    413   -739  -1151       O  
ATOM    681  CB  TYR A 538       8.733 -13.293 -22.687  1.00 51.82           C  
ANISOU  681  CB  TYR A 538     5432   6572   7685     57   -376   -665       C  
ATOM    682  CG  TYR A 538       9.205 -13.820 -24.025  1.00 56.28           C  
ANISOU  682  CG  TYR A 538     5873   7145   8367     51   -151   -804       C  
ATOM    683  CD1 TYR A 538      10.223 -13.185 -24.728  1.00 59.67           C  
ANISOU  683  CD1 TYR A 538     6054   7631   8989    -20     58   -978       C  
ATOM    684  CD2 TYR A 538       8.626 -14.949 -24.591  1.00 57.58           C  
ANISOU  684  CD2 TYR A 538     6183   7247   8447     98   -116   -778       C  
ATOM    685  CE1 TYR A 538      10.657 -13.664 -25.948  1.00 62.55           C  
ANISOU  685  CE1 TYR A 538     6338   7990   9436    -32    306  -1114       C  
ATOM    686  CE2 TYR A 538       9.053 -15.433 -25.814  1.00 60.15           C  
ANISOU  686  CE2 TYR A 538     6426   7572   8855     98     94   -917       C  
ATOM    687  CZ  TYR A 538      10.068 -14.787 -26.486  1.00 63.26           C  
ANISOU  687  CZ  TYR A 538     6593   8026   9418     39    311  -1081       C  
ATOM    688  OH  TYR A 538      10.498 -15.262 -27.704  1.00 65.87           O  
ANISOU  688  OH  TYR A 538     6872   8347   9809     31    563  -1228       O  
ATOM    689  N   HIS A 539      11.234 -12.028 -21.488  1.00 51.48           N  
ANISOU  689  N   HIS A 539     4829   6580   8151    132   -628  -1005       N  
ATOM    690  CA  HIS A 539      12.562 -11.453 -21.629  1.00 52.80           C  
ANISOU  690  CA  HIS A 539     4609   6796   8657    100   -583  -1266       C  
ATOM    691  C   HIS A 539      13.576 -12.076 -20.673  1.00 54.60           C  
ANISOU  691  C   HIS A 539     4626   6979   9142    345   -972  -1450       C  
ATOM    692  O   HIS A 539      14.729 -12.280 -21.042  1.00 58.78           O  
ANISOU  692  O   HIS A 539     4775   7529  10028    403   -948  -1728       O  
ATOM    693  CB  HIS A 539      12.507  -9.942 -21.412  1.00 53.34           C  
ANISOU  693  CB  HIS A 539     4662   6921   8684   -103   -474  -1248       C  
ATOM    694  CG  HIS A 539      13.821  -9.262 -21.610  1.00 56.42           C  
ANISOU  694  CG  HIS A 539     4646   7349   9442   -201   -363  -1539       C  
ATOM    695  ND1 HIS A 539      14.679  -8.980 -20.568  1.00 58.95           N  
ANISOU  695  ND1 HIS A 539     4719   7679  10001   -120   -674  -1727       N  
ATOM    696  CD2 HIS A 539      14.435  -8.817 -22.732  1.00 58.95           C  
ANISOU  696  CD2 HIS A 539     4765   7690   9944   -386     41  -1700       C  
ATOM    697  CE1 HIS A 539      15.761  -8.389 -21.039  1.00 63.12           C  
ANISOU  697  CE1 HIS A 539     4855   8242  10884   -264   -466  -2013       C  
ATOM    698  NE2 HIS A 539      15.638  -8.278 -22.351  1.00 63.06           N  
ANISOU  698  NE2 HIS A 539     4881   8234  10844   -439     -1  -1994       N  
ATOM    699  N   HIS A 540      13.151 -12.371 -19.448  1.00 53.02           N  
ANISOU  699  N   HIS A 540     4679   6708   8758    498  -1331  -1312       N  
ATOM    700  CA  HIS A 540      14.050 -12.971 -18.465  1.00 56.75           C  
ANISOU  700  CA  HIS A 540     5041   7111   9411    780  -1773  -1469       C  
ATOM    701  C   HIS A 540      14.404 -14.402 -18.830  1.00 58.53           C  
ANISOU  701  C   HIS A 540     5246   7236   9758   1014  -1860  -1542       C  
ATOM    702  O   HIS A 540      15.553 -14.820 -18.706  1.00 64.14           O  
ANISOU  702  O   HIS A 540     5637   7931  10802   1225  -2080  -1811       O  
ATOM    703  CB  HIS A 540      13.425 -12.953 -17.071  1.00 57.44           C  
ANISOU  703  CB  HIS A 540     5524   7112   9187    887  -2109  -1274       C  
ATOM    704  CG  HIS A 540      13.349 -11.591 -16.460  1.00 58.10           C  
ANISOU  704  CG  HIS A 540     5593   7276   9206    730  -2133  -1271       C  
ATOM    705  ND1 HIS A 540      14.470 -10.850 -16.154  1.00 61.43           N  
ANISOU  705  ND1 HIS A 540     5640   7768   9933    735  -2292  -1550       N  
ATOM    706  CD2 HIS A 540      12.286 -10.837 -16.091  1.00 55.33           C  
ANISOU  706  CD2 HIS A 540     5544   6939   8540    564  -2016  -1049       C  
ATOM    707  CE1 HIS A 540      14.101  -9.696 -15.628  1.00 61.27           C  
ANISOU  707  CE1 HIS A 540     5724   7789   9768    571  -2272  -1485       C  
ATOM    708  NE2 HIS A 540      12.781  -9.664 -15.577  1.00 57.62           N  
ANISOU  708  NE2 HIS A 540     5673   7293   8925    477  -2105  -1178       N  
ATOM    709  N   LEU A 541      13.400 -15.149 -19.272  1.00 54.92           N  
ANISOU  709  N   LEU A 541     5117   6702   9048    982  -1697  -1324       N  
ATOM    710  CA  LEU A 541      13.564 -16.565 -19.561  1.00 55.53           C  
ANISOU  710  CA  LEU A 541     5268   6643   9189   1196  -1775  -1357       C  
ATOM    711  C   LEU A 541      14.320 -16.823 -20.855  1.00 57.02           C  
ANISOU  711  C   LEU A 541     5080   6895   9688   1172  -1500  -1597       C  
ATOM    712  O   LEU A 541      15.179 -17.700 -20.910  1.00 59.82           O  
ANISOU  712  O   LEU A 541     5256   7173  10300   1420  -1663  -1796       O  
ATOM    713  CB  LEU A 541      12.203 -17.253 -19.625  1.00 52.66           C  
ANISOU  713  CB  LEU A 541     5371   6167   8472   1125  -1660  -1073       C  
ATOM    714  CG  LEU A 541      11.405 -17.344 -18.328  1.00 53.26           C  
ANISOU  714  CG  LEU A 541     5889   6119   8228   1169  -1888   -839       C  
ATOM    715  CD1 LEU A 541      10.081 -18.047 -18.579  1.00 52.64           C  
ANISOU  715  CD1 LEU A 541     6186   5936   7878   1045  -1685   -620       C  
ATOM    716  CD2 LEU A 541      12.201 -18.068 -17.253  1.00 55.27           C  
ANISOU  716  CD2 LEU A 541     6262   6202   8538   1511  -2343   -905       C  
ATOM    717  N   HIS A 542      14.007 -16.057 -21.894  1.00 56.08           N  
ANISOU  717  N   HIS A 542     4871   6902   9534    890  -1082  -1587       N  
ATOM    718  CA  HIS A 542      14.476 -16.397 -23.231  1.00 55.40           C  
ANISOU  718  CA  HIS A 542     4565   6850   9636    838   -744  -1766       C  
ATOM    719  C   HIS A 542      15.434 -15.387 -23.855  1.00 61.01           C  
ANISOU  719  C   HIS A 542     4858   7689  10634    667   -460  -2016       C  
ATOM    720  O   HIS A 542      16.076 -15.684 -24.860  1.00 63.22           O  
ANISOU  720  O   HIS A 542     4908   7986  11129    645   -177  -2226       O  
ATOM    721  CB  HIS A 542      13.282 -16.622 -24.159  1.00 49.50           C  
ANISOU  721  CB  HIS A 542     4144   6094   8570    672   -451  -1562       C  
ATOM    722  CG  HIS A 542      12.233 -17.516 -23.580  1.00 47.86           C  
ANISOU  722  CG  HIS A 542     4335   5756   8094    764   -656  -1332       C  
ATOM    723  ND1 HIS A 542      12.478 -18.832 -23.243  1.00 49.53           N  
ANISOU  723  ND1 HIS A 542     4638   5799   8381   1011   -878  -1369       N  
ATOM    724  CD2 HIS A 542      10.933 -17.288 -23.275  1.00 45.46           C  
ANISOU  724  CD2 HIS A 542     4364   5446   7462    633   -647  -1079       C  
ATOM    725  CE1 HIS A 542      11.377 -19.372 -22.755  1.00 48.53           C  
ANISOU  725  CE1 HIS A 542     4910   5556   7974    998   -967  -1138       C  
ATOM    726  NE2 HIS A 542      10.423 -18.457 -22.766  1.00 46.24           N  
ANISOU  726  NE2 HIS A 542     4742   5374   7453    765   -823   -974       N  
ATOM    727  N   ALA A 543      15.534 -14.198 -23.273  1.00 64.01           N  
ANISOU  727  N   ALA A 543     5157   8144  11020    528   -502  -2007       N  
ATOM    728  CA  ALA A 543      16.419 -13.179 -23.827  1.00 68.82           C  
ANISOU  728  CA  ALA A 543     5397   8846  11907    319   -192  -2248       C  
ATOM    729  C   ALA A 543      17.561 -12.854 -22.875  1.00 77.33           C  
ANISOU  729  C   ALA A 543     6166   9932  13283    418   -492  -2483       C  
ATOM    730  O   ALA A 543      18.734 -12.984 -23.225  1.00 82.59           O  
ANISOU  730  O   ALA A 543     6578  10584  14218    426   -390  -2748       O  
ATOM    731  CB  ALA A 543      15.636 -11.921 -24.172  1.00 64.71           C  
ANISOU  731  CB  ALA A 543     5117   8368  11101     16     99  -2047       C  
ATOM    732  N   SER A 544      17.203 -12.426 -21.670  1.00 79.36           N  
ANISOU  732  N   SER A 544     6553  10189  13412    479   -856  -2362       N  
ATOM    733  CA  SER A 544      18.177 -12.066 -20.650  1.00 84.29           C  
ANISOU  733  CA  SER A 544     7040  10796  14189    576  -1170  -2536       C  
ATOM    734  C   SER A 544      18.934 -13.277 -20.119  1.00 90.39           C  
ANISOU  734  C   SER A 544     7759  11479  15104    922  -1552  -2684       C  
ATOM    735  O   SER A 544      20.065 -13.146 -19.647  1.00 93.82           O  
ANISOU  735  O   SER A 544     7976  11902  15770   1004  -1727  -2939       O  
ATOM    736  CB  SER A 544      17.481 -11.353 -19.491  1.00 82.68           C  
ANISOU  736  CB  SER A 544     7073  10599  13742    565  -1458  -2347       C  
ATOM    737  OG  SER A 544      18.340 -11.252 -18.370  1.00 87.29           O  
ANISOU  737  OG  SER A 544     7596  11145  14424    733  -1841  -2504       O  
ATOM    738  N   GLU A 545      18.309 -14.448 -20.198  1.00 92.00           N  
ANISOU  738  N   GLU A 545     8176  11606  15174   1127  -1683  -2536       N  
ATOM    739  CA  GLU A 545      18.855 -15.656 -19.587  1.00 97.84           C  
ANISOU  739  CA  GLU A 545     8986  12217  15971   1479  -2083  -2618       C  
ATOM    740  C   GLU A 545      19.143 -15.425 -18.110  1.00101.58           C  
ANISOU  740  C   GLU A 545     9618  12635  16343   1647  -2560  -2616       C  
ATOM    741  O   GLU A 545      20.178 -15.846 -17.593  1.00106.45           O  
ANISOU  741  O   GLU A 545    10120  13193  17133   1858  -2846  -2840       O  
ATOM    742  CB  GLU A 545      20.117 -16.130 -20.314  1.00103.14           C  
ANISOU  742  CB  GLU A 545     9295  12892  17003   1527  -1944  -2951       C  
ATOM    743  CG  GLU A 545      19.861 -16.748 -21.677  1.00103.84           C  
ANISOU  743  CG  GLU A 545     9328  12984  17142   1452  -1540  -2953       C  
ATOM    744  CD  GLU A 545      19.126 -18.073 -21.595  1.00104.26           C  
ANISOU  744  CD  GLU A 545     9698  12896  17018   1713  -1734  -2770       C  
ATOM    745  OE1 GLU A 545      19.735 -19.112 -21.927  1.00107.12           O  
ANISOU  745  OE1 GLU A 545     9988  13176  17536   1905  -1784  -2922       O  
ATOM    746  OE2 GLU A 545      17.938 -18.080 -21.207  1.00100.98           O  
ANISOU  746  OE2 GLU A 545     9618  12437  16313   1722  -1827  -2481       O  
ATOM    747  N   THR A 546      18.224 -14.729 -17.447  1.00 98.61           N  
ANISOU  747  N   THR A 546     9513  12276  15679   1550  -2638  -2376       N  
ATOM    748  CA  THR A 546      18.321 -14.487 -16.015  1.00 98.35           C  
ANISOU  748  CA  THR A 546     9726  12176  15466   1697  -3061  -2335       C  
ATOM    749  C   THR A 546      18.235 -15.814 -15.273  1.00 98.31           C  
ANISOU  749  C   THR A 546    10105  11976  15273   2044  -3447  -2236       C  
ATOM    750  O   THR A 546      17.290 -16.578 -15.466  1.00 96.67           O  
ANISOU  750  O   THR A 546    10217  11670  14843   2100  -3410  -1992       O  
ATOM    751  CB  THR A 546      17.182 -13.574 -15.527  1.00 93.63           C  
ANISOU  751  CB  THR A 546     9406  11620  14547   1514  -3025  -2067       C  
ATOM    752  OG1 THR A 546      17.229 -12.322 -16.223  1.00 92.46           O  
ANISOU  752  OG1 THR A 546     8954  11627  14548   1183  -2655  -2146       O  
ATOM    753  CG2 THR A 546      17.299 -13.325 -14.033  1.00 94.64           C  
ANISOU  753  CG2 THR A 546     9832  11667  14461   1664  -3430  -2032       C  
ATOM    754  N   LYS A 547      19.222 -16.093 -14.430  1.00 99.90           N  
ANISOU  754  N   LYS A 547    10299  12099  15558   2276  -3811  -2434       N  
ATOM    755  CA  LYS A 547      19.240 -17.353 -13.697  1.00100.35           C  
ANISOU  755  CA  LYS A 547    10764  11946  15419   2611  -4178  -2357       C  
ATOM    756  C   LYS A 547      18.413 -17.268 -12.421  1.00 97.98           C  
ANISOU  756  C   LYS A 547    11056  11516  14656   2677  -4422  -2081       C  
ATOM    757  O   LYS A 547      18.818 -16.629 -11.450  1.00101.93           O  
ANISOU  757  O   LYS A 547    11612  12019  15098   2720  -4660  -2170       O  
ATOM    758  CB  LYS A 547      20.675 -17.767 -13.371  1.00105.53           C  
ANISOU  758  CB  LYS A 547    11173  12562  16362   2858  -4483  -2714       C  
ATOM    759  CG  LYS A 547      21.527 -18.057 -14.595  1.00106.38           C  
ANISOU  759  CG  LYS A 547    10749  12762  16909   2817  -4237  -2998       C  
ATOM    760  CD  LYS A 547      22.939 -18.462 -14.203  1.00111.85           C  
ANISOU  760  CD  LYS A 547    11191  13410  17895   3075  -4573  -3375       C  
ATOM    761  CE  LYS A 547      23.789 -18.765 -15.427  1.00112.79           C  
ANISOU  761  CE  LYS A 547    10790  13614  18450   3021  -4294  -3670       C  
ATOM    762  NZ  LYS A 547      25.188 -19.123 -15.062  1.00118.67           N  
ANISOU  762  NZ  LYS A 547    11244  14324  19520   3271  -4627  -4077       N  
ATOM    763  N   PHE A 548      17.250 -17.911 -12.428  1.00 91.14           N  
ANISOU  763  N   PHE A 548    10646  10522  13460   2674  -4336  -1757       N  
ATOM    764  CA  PHE A 548      16.389 -17.933 -11.254  1.00 88.14           C  
ANISOU  764  CA  PHE A 548    10892   9989  12608   2707  -4487  -1482       C  
ATOM    765  C   PHE A 548      16.591 -19.211 -10.462  1.00 90.14           C  
ANISOU  765  C   PHE A 548    11634   9976  12641   3013  -4790  -1434       C  
ATOM    766  O   PHE A 548      16.639 -20.302 -11.026  1.00 90.08           O  
ANISOU  766  O   PHE A 548    11672   9857  12699   3136  -4757  -1423       O  
ATOM    767  CB  PHE A 548      14.914 -17.826 -11.647  1.00 84.02           C  
ANISOU  767  CB  PHE A 548    10638   9459  11826   2487  -4176  -1152       C  
ATOM    768  CG  PHE A 548      14.529 -16.499 -12.226  1.00 80.93           C  
ANISOU  768  CG  PHE A 548     9893   9309  11548   2187  -3913  -1157       C  
ATOM    769  CD1 PHE A 548      14.668 -15.338 -11.485  1.00 80.66           C  
ANISOU  769  CD1 PHE A 548     9827   9373  11447   2083  -3991  -1205       C  
ATOM    770  CD2 PHE A 548      14.001 -16.415 -13.503  1.00 77.09           C  
ANISOU  770  CD2 PHE A 548     9136   8934  11222   2011  -3585  -1117       C  
ATOM    771  CE1 PHE A 548      14.306 -14.116 -12.013  1.00 77.08           C  
ANISOU  771  CE1 PHE A 548     9084   9121  11083   1797  -3740  -1209       C  
ATOM    772  CE2 PHE A 548      13.635 -15.197 -14.037  1.00 73.97           C  
ANISOU  772  CE2 PHE A 548     8489   8745  10870   1678  -3251  -1114       C  
ATOM    773  CZ  PHE A 548      13.788 -14.044 -13.291  1.00 74.44           C  
ANISOU  773  CZ  PHE A 548     8501   8896  10885   1603  -3391  -1165       C  
ATOM    774  N   GLU A 549      16.707 -19.077  -9.148  1.00 92.62           N  
ANISOU  774  N   GLU A 549    12338  10173  12680   3137  -5075  -1412       N  
ATOM    775  CA  GLU A 549      16.705 -20.247  -8.295  1.00 95.36           C  
ANISOU  775  CA  GLU A 549    13273  10236  12723   3399  -5327  -1321       C  
ATOM    776  C   GLU A 549      15.291 -20.798  -8.359  1.00 89.94           C  
ANISOU  776  C   GLU A 549    13113   9396  11665   3248  -5030   -948       C  
ATOM    777  O   GLU A 549      14.355 -20.061  -8.664  1.00 85.34           O  
ANISOU  777  O   GLU A 549    12505   8923  10998   2973  -4729   -776       O  
ATOM    778  CB  GLU A 549      17.087 -19.873  -6.865  1.00100.19           C  
ANISOU  778  CB  GLU A 549    14210  10754  13102   3548  -5671  -1388       C  
ATOM    779  CG  GLU A 549      18.144 -18.777  -6.769  1.00102.51           C  
ANISOU  779  CG  GLU A 549    13955  11250  13743   3555  -5851  -1717       C  
ATOM    780  CD  GLU A 549      19.565 -19.276  -6.987  1.00107.70           C  
ANISOU  780  CD  GLU A 549    14218  11915  14789   3824  -6158  -2087       C  
ATOM    781  OE1 GLU A 549      19.762 -20.270  -7.718  1.00108.34           O  
ANISOU  781  OE1 GLU A 549    14208  11943  15013   3930  -6117  -2116       O  
ATOM    782  OE2 GLU A 549      20.493 -18.664  -6.418  1.00110.82           O  
ANISOU  782  OE2 GLU A 549    14386  12363  15356   3933  -6441  -2366       O  
ATOM    783  N   MET A 550      15.139 -22.089  -8.088  1.00 91.43           N  
ANISOU  783  N   MET A 550    13776   9321  11643   3420  -5101   -838       N  
ATOM    784  CA  MET A 550      13.846 -22.757  -8.212  1.00 86.42           C  
ANISOU  784  CA  MET A 550    13637   8504  10696   3260  -4776   -513       C  
ATOM    785  C   MET A 550      12.761 -22.054  -7.401  1.00 83.18           C  
ANISOU  785  C   MET A 550    13638   8068   9898   3026  -4580   -282       C  
ATOM    786  O   MET A 550      11.590 -22.044  -7.787  1.00 79.72           O  
ANISOU  786  O   MET A 550    13364   7605   9322   2769  -4205    -55       O  
ATOM    787  CB  MET A 550      13.959 -24.225  -7.789  1.00 88.22           C  
ANISOU  787  CB  MET A 550    14387   8417  10716   3489  -4910   -451       C  
ATOM    788  CG  MET A 550      12.702 -25.039  -8.045  1.00 85.45           C  
ANISOU  788  CG  MET A 550    14503   7855  10110   3299  -4526   -154       C  
ATOM    789  SD  MET A 550      12.172 -24.955  -9.764  1.00 77.50           S  
ANISOU  789  SD  MET A 550    12985   6999   9464   3076  -4145   -128       S  
ATOM    790  CE  MET A 550      13.644 -25.529 -10.601  1.00 96.28           C  
ANISOU  790  CE  MET A 550    14811   9455  12316   3389  -4420   -455       C  
ATOM    791  N   LYS A 551      13.164 -21.454  -6.285  1.00 84.14           N  
ANISOU  791  N   LYS A 551    13915   8191   9864   3115  -4828   -364       N  
ATOM    792  CA  LYS A 551      12.237 -20.752  -5.407  1.00 83.15           C  
ANISOU  792  CA  LYS A 551    14182   8037   9374   2916  -4654   -183       C  
ATOM    793  C   LYS A 551      11.566 -19.568  -6.102  1.00 76.79           C  
ANISOU  793  C   LYS A 551    12984   7492   8700   2607  -4354   -120       C  
ATOM    794  O   LYS A 551      10.373 -19.333  -5.922  1.00 75.41           O  
ANISOU  794  O   LYS A 551    13110   7281   8261   2362  -4023    101       O  
ATOM    795  CB  LYS A 551      12.950 -20.291  -4.132  1.00 89.56           C  
ANISOU  795  CB  LYS A 551    15185   8799  10043   3106  -5018   -330       C  
ATOM    796  CG  LYS A 551      12.075 -19.474  -3.191  1.00 89.73           C  
ANISOU  796  CG  LYS A 551    15584   8799   9711   2913  -4840   -179       C  
ATOM    797  CD  LYS A 551      12.695 -19.364  -1.808  1.00 94.50           C  
ANISOU  797  CD  LYS A 551    16567   9250  10089   3149  -5206   -297       C  
ATOM    798  CE  LYS A 551      11.717 -18.757  -0.816  1.00 94.39           C  
ANISOU  798  CE  LYS A 551    17034   9156   9674   2963  -4980   -128       C  
ATOM    799  NZ  LYS A 551      12.187 -18.911   0.590  1.00100.79           N  
ANISOU  799  NZ  LYS A 551    18377   9736  10182   3215  -5312   -208       N  
ATOM    800  N   LYS A 552      12.334 -18.829  -6.898  1.00 74.90           N  
ANISOU  800  N   LYS A 552    12075   7509   8875   2611  -4450   -332       N  
ATOM    801  CA  LYS A 552      11.797 -17.688  -7.636  1.00 70.91           C  
ANISOU  801  CA  LYS A 552    11178   7253   8510   2336  -4192   -297       C  
ATOM    802  C   LYS A 552      10.817 -18.138  -8.718  1.00 64.42           C  
ANISOU  802  C   LYS A 552    10348   6422   7708   2161  -3845   -111       C  
ATOM    803  O   LYS A 552       9.752 -17.549  -8.887  1.00 61.06           O  
ANISOU  803  O   LYS A 552    10008   6059   7132   1911  -3563     61       O  
ATOM    804  CB  LYS A 552      12.929 -16.887  -8.280  1.00 74.21           C  
ANISOU  804  CB  LYS A 552    10884   7924   9389   2366  -4336   -599       C  
ATOM    805  CG  LYS A 552      12.897 -15.394  -7.982  1.00 76.05           C  
ANISOU  805  CG  LYS A 552    10901   8351   9642   2186  -4302   -660       C  
ATOM    806  CD  LYS A 552      11.482 -14.830  -8.007  1.00 75.48           C  
ANISOU  806  CD  LYS A 552    11083   8314   9281   1915  -3981   -394       C  
ATOM    807  CE  LYS A 552      11.500 -13.316  -7.843  1.00 77.20           C  
ANISOU  807  CE  LYS A 552    11045   8734   9554   1735  -3941   -479       C  
ATOM    808  NZ  LYS A 552      10.362 -12.809  -7.024  1.00 77.25           N  
ANISOU  808  NZ  LYS A 552    11520   8684   9147   1581  -3774   -264       N  
ATOM    809  N   LEU A 553      11.194 -19.181  -9.449  1.00 63.37           N  
ANISOU  809  N   LEU A 553    10110   6198   7769   2301  -3872   -164       N  
ATOM    810  CA  LEU A 553      10.378 -19.708 -10.535  1.00 60.54           C  
ANISOU  810  CA  LEU A 553     9734   5792   7475   2169  -3569    -24       C  
ATOM    811  C   LEU A 553       9.015 -20.170 -10.043  1.00 58.21           C  
ANISOU  811  C   LEU A 553    10066   5276   6775   1981  -3278    269       C  
ATOM    812  O   LEU A 553       8.008 -20.015 -10.731  1.00 53.64           O  
ANISOU  812  O   LEU A 553     9394   4786   6201   1662  -2845    357       O  
ATOM    813  CB  LEU A 553      11.097 -20.869 -11.219  1.00 64.83           C  
ANISOU  813  CB  LEU A 553    10133   6227   8271   2384  -3663   -153       C  
ATOM    814  CG  LEU A 553      12.385 -20.532 -11.970  1.00 65.70           C  
ANISOU  814  CG  LEU A 553     9551   6561   8853   2515  -3823   -478       C  
ATOM    815  CD1 LEU A 553      13.063 -21.806 -12.444  1.00 67.06           C  
ANISOU  815  CD1 LEU A 553     9681   6588   9210   2745  -3912   -602       C  
ATOM    816  CD2 LEU A 553      12.091 -19.613 -13.144  1.00 60.95           C  
ANISOU  816  CD2 LEU A 553     8426   6234   8498   2235  -3487   -538       C  
ATOM    817  N   ILE A 554       8.988 -20.738  -8.844  1.00 62.67           N  
ANISOU  817  N   ILE A 554    11161   5633   7017   2068  -3363    338       N  
ATOM    818  CA  ILE A 554       7.743 -21.241  -8.283  1.00 63.29           C  
ANISOU  818  CA  ILE A 554    11826   5495   6726   1859  -3025    571       C  
ATOM    819  C   ILE A 554       6.911 -20.106  -7.685  1.00 60.56           C  
ANISOU  819  C   ILE A 554    11576   5270   6163   1615  -2822    664       C  
ATOM    820  O   ILE A 554       5.684 -20.112  -7.777  1.00 58.87           O  
ANISOU  820  O   ILE A 554    11564   5005   5800   1330  -2415    819       O  
ATOM    821  CB  ILE A 554       8.003 -22.375  -7.266  1.00 69.29           C  
ANISOU  821  CB  ILE A 554    13148   5963   7216   2042  -3157    597       C  
ATOM    822  CG1 ILE A 554       8.598 -23.587  -7.986  1.00 72.94           C  
ANISOU  822  CG1 ILE A 554    13544   6288   7882   2240  -3274    531       C  
ATOM    823  CG2 ILE A 554       6.725 -22.775  -6.544  1.00 68.41           C  
ANISOU  823  CG2 ILE A 554    13627   5644   6722   1790  -2761    799       C  
ATOM    824  CD1 ILE A 554       8.801 -24.784  -7.094  1.00 79.96           C  
ANISOU  824  CD1 ILE A 554    15018   6870   8495   2419  -3393    569       C  
ATOM    825  N   ASP A 555       7.579 -19.119  -7.097  1.00 61.38           N  
ANISOU  825  N   ASP A 555    11506   5536   6281   1713  -3084    539       N  
ATOM    826  CA  ASP A 555       6.877 -17.934  -6.626  1.00 62.78           C  
ANISOU  826  CA  ASP A 555    11708   5850   6296   1497  -2906    597       C  
ATOM    827  C   ASP A 555       6.214 -17.198  -7.789  1.00 58.15           C  
ANISOU  827  C   ASP A 555    10729   5477   5890   1261  -2656    646       C  
ATOM    828  O   ASP A 555       5.074 -16.747  -7.679  1.00 57.72           O  
ANISOU  828  O   ASP A 555    10782   5466   5682    982  -2279    749       O  
ATOM    829  CB  ASP A 555       7.816 -16.987  -5.885  1.00 68.27           C  
ANISOU  829  CB  ASP A 555    12241   6672   7026   1648  -3249    423       C  
ATOM    830  CG  ASP A 555       7.092 -15.769  -5.344  1.00 73.38           C  
ANISOU  830  CG  ASP A 555    12947   7438   7496   1436  -3061    475       C  
ATOM    831  OD1 ASP A 555       6.030 -15.951  -4.709  1.00 77.44           O  
ANISOU  831  OD1 ASP A 555    13905   7815   7702   1272  -2749    627       O  
ATOM    832  OD2 ASP A 555       7.566 -14.633  -5.568  1.00 72.66           O  
ANISOU  832  OD2 ASP A 555    12444   7574   7591   1418  -3194    345       O  
ATOM    833  N   ILE A 556       6.938 -17.076  -8.899  1.00 54.21           N  
ANISOU  833  N   ILE A 556     9637   5171   5788   1305  -2733    477       N  
ATOM    834  CA  ILE A 556       6.397 -16.450 -10.100  1.00 51.34           C  
ANISOU  834  CA  ILE A 556     8768   5071   5667   1021  -2363    423       C  
ATOM    835  C   ILE A 556       5.189 -17.233 -10.599  1.00 51.48           C  
ANISOU  835  C   ILE A 556     8957   4991   5611    800  -1953    550       C  
ATOM    836  O   ILE A 556       4.154 -16.653 -10.935  1.00 48.93           O  
ANISOU  836  O   ILE A 556     8519   4805   5269    530  -1611    585       O  
ATOM    837  CB  ILE A 556       7.450 -16.366 -11.221  1.00 50.58           C  
ANISOU  837  CB  ILE A 556     8085   5149   5983   1113  -2480    215       C  
ATOM    838  CG1 ILE A 556       8.563 -15.394 -10.828  1.00 53.40           C  
ANISOU  838  CG1 ILE A 556     8159   5644   6485   1252  -2817     35       C  
ATOM    839  CG2 ILE A 556       6.809 -15.917 -12.521  1.00 45.37           C  
ANISOU  839  CG2 ILE A 556     7037   4701   5501    838  -2083    189       C  
ATOM    840  CD1 ILE A 556       9.677 -15.290 -11.849  1.00 54.18           C  
ANISOU  840  CD1 ILE A 556     7672   5899   7014   1325  -2895   -206       C  
ATOM    841  N   ALA A 557       5.327 -18.555 -10.632  1.00 53.82           N  
ANISOU  841  N   ALA A 557     9527   5039   5883    926  -2005    598       N  
ATOM    842  CA  ALA A 557       4.233 -19.440 -11.014  1.00 51.74           C  
ANISOU  842  CA  ALA A 557     9469   4631   5558    714  -1633    696       C  
ATOM    843  C   ALA A 557       3.057 -19.277 -10.060  1.00 49.53           C  
ANISOU  843  C   ALA A 557     9634   4232   4954    501  -1357    847       C  
ATOM    844  O   ALA A 557       1.897 -19.284 -10.470  1.00 47.17           O  
ANISOU  844  O   ALA A 557     9264   3983   4675    208   -960    862       O  
ATOM    845  CB  ALA A 557       4.706 -20.892 -11.028  1.00 53.48           C  
ANISOU  845  CB  ALA A 557     9996   4544   5778    919  -1777    723       C  
ATOM    846  N   ARG A 558       3.370 -19.129  -8.780  1.00 50.81           N  
ANISOU  846  N   ARG A 558    10252   4234   4820    656  -1572    934       N  
ATOM    847  CA  ARG A 558       2.350 -18.971  -7.757  1.00 54.97           C  
ANISOU  847  CA  ARG A 558    11267   4618   5001    470  -1296   1071       C  
ATOM    848  C   ARG A 558       1.620 -17.638  -7.901  1.00 53.09           C  
ANISOU  848  C   ARG A 558    10666   4686   4822    233  -1057   1012       C  
ATOM    849  O   ARG A 558       0.397 -17.570  -7.770  1.00 52.66           O  
ANISOU  849  O   ARG A 558    10711   4616   4682    -45   -639   1051       O  
ATOM    850  CB  ARG A 558       2.989 -19.076  -6.376  1.00 64.24           C  
ANISOU  850  CB  ARG A 558    12812   5673   5924    689  -1554   1044       C  
ATOM    851  CG  ARG A 558       2.006 -19.223  -5.237  1.00 71.94           C  
ANISOU  851  CG  ARG A 558    14257   6496   6582    505  -1212   1103       C  
ATOM    852  CD  ARG A 558       2.233 -18.138  -4.213  1.00 76.39           C  
ANISOU  852  CD  ARG A 558    14894   7154   6978    572  -1360   1053       C  
ATOM    853  NE  ARG A 558       3.653 -17.932  -3.943  1.00 78.64           N  
ANISOU  853  NE  ARG A 558    15087   7473   7319    907  -1901    951       N  
ATOM    854  CZ  ARG A 558       4.259 -18.257  -2.805  1.00 81.71           C  
ANISOU  854  CZ  ARG A 558    15874   7680   7491   1122  -2154    908       C  
ATOM    855  NH1 ARG A 558       3.570 -18.804  -1.814  1.00 85.59           N  
ANISOU  855  NH1 ARG A 558    16932   7929   7660   1040  -1911    978       N  
ATOM    856  NH2 ARG A 558       5.556 -18.026  -2.658  1.00 81.72           N  
ANISOU  856  NH2 ARG A 558    15702   7738   7610   1414  -2646    771       N  
ATOM    857  N   GLN A 559       2.374 -16.580  -8.177  1.00 51.43           N  
ANISOU  857  N   GLN A 559    10028   4737   4776    342  -1314    898       N  
ATOM    858  CA  GLN A 559       1.793 -15.252  -8.326  1.00 49.46           C  
ANISOU  858  CA  GLN A 559     9460   4753   4582    159  -1132    840       C  
ATOM    859  C   GLN A 559       0.902 -15.178  -9.557  1.00 45.73           C  
ANISOU  859  C   GLN A 559     8559   4459   4356    -76   -789    780       C  
ATOM    860  O   GLN A 559      -0.179 -14.589  -9.521  1.00 44.45           O  
ANISOU  860  O   GLN A 559     8334   4395   4161   -285   -487    773       O  
ATOM    861  CB  GLN A 559       2.889 -14.193  -8.414  1.00 51.97           C  
ANISOU  861  CB  GLN A 559     9430   5272   5043    319  -1478    719       C  
ATOM    862  CG  GLN A 559       3.633 -13.955  -7.117  1.00 57.26           C  
ANISOU  862  CG  GLN A 559    10478   5816   5462    535  -1839    733       C  
ATOM    863  CD  GLN A 559       4.539 -12.749  -7.194  1.00 59.70           C  
ANISOU  863  CD  GLN A 559    10396   6341   5946    617  -2115    575       C  
ATOM    864  OE1 GLN A 559       4.081 -11.629  -7.427  1.00 58.59           O  
ANISOU  864  OE1 GLN A 559    10007   6388   5867    445  -1928    533       O  
ATOM    865  NE2 GLN A 559       5.835 -12.970  -7.011  1.00 62.45           N  
ANISOU  865  NE2 GLN A 559    10676   6654   6399    884  -2563    464       N  
ATOM    866  N   THR A 560       1.367 -15.776 -10.648  1.00 42.57           N  
ANISOU  866  N   THR A 560     7869   4102   4205    -22   -856    715       N  
ATOM    867  CA  THR A 560       0.597 -15.816 -11.880  1.00 38.62           C  
ANISOU  867  CA  THR A 560     7004   3755   3917   -210   -588    643       C  
ATOM    868  C   THR A 560      -0.692 -16.595 -11.666  1.00 37.84           C  
ANISOU  868  C   THR A 560     7155   3500   3721   -430   -236    691       C  
ATOM    869  O   THR A 560      -1.748 -16.214 -12.164  1.00 38.41           O  
ANISOU  869  O   THR A 560     6994   3716   3884   -631     28    622       O  
ATOM    870  CB  THR A 560       1.404 -16.454 -13.022  1.00 41.57           C  
ANISOU  870  CB  THR A 560     7101   4158   4534    -96   -723    560       C  
ATOM    871  OG1 THR A 560       2.630 -15.732 -13.201  1.00 41.32           O  
ANISOU  871  OG1 THR A 560     6808   4263   4629     80  -1004    481       O  
ATOM    872  CG2 THR A 560       0.609 -16.428 -14.322  1.00 40.86           C  
ANISOU  872  CG2 THR A 560     6670   4231   4622   -274   -479    473       C  
ATOM    873  N   ALA A 561      -0.600 -17.682 -10.910  1.00 38.99           N  
ANISOU  873  N   ALA A 561     7788   3337   3689   -387   -236    793       N  
ATOM    874  CA  ALA A 561      -1.775 -18.464 -10.550  1.00 45.31           C  
ANISOU  874  CA  ALA A 561     8899   3934   4384   -629    145    836       C  
ATOM    875  C   ALA A 561      -2.767 -17.649  -9.718  1.00 45.77           C  
ANISOU  875  C   ALA A 561     9070   4041   4281   -817    422    848       C  
ATOM    876  O   ALA A 561      -3.976 -17.755  -9.905  1.00 49.22           O  
ANISOU  876  O   ALA A 561     9405   4498   4796  -1083    799    774       O  
ATOM    877  CB  ALA A 561      -1.363 -19.725  -9.802  1.00 44.40           C  
ANISOU  877  CB  ALA A 561     9388   3425   4057   -522     81    968       C  
ATOM    878  N   ARG A 562      -2.248 -16.845  -8.794  1.00 43.79           N  
ANISOU  878  N   ARG A 562     9013   3804   3819   -674    232    911       N  
ATOM    879  CA  ARG A 562      -3.084 -15.970  -7.977  1.00 42.16           C  
ANISOU  879  CA  ARG A 562     8918   3651   3449   -821    477    909       C  
ATOM    880  C   ARG A 562      -3.887 -14.976  -8.818  1.00 40.93           C  
ANISOU  880  C   ARG A 562     8183   3818   3551   -965    646    758       C  
ATOM    881  O   ARG A 562      -5.077 -14.771  -8.580  1.00 41.61           O  
ANISOU  881  O   ARG A 562     8245   3926   3640  -1184   1014    692       O  
ATOM    882  CB  ARG A 562      -2.228 -15.225  -6.952  1.00 43.01           C  
ANISOU  882  CB  ARG A 562     9304   3737   3302   -607    168    977       C  
ATOM    883  CG  ARG A 562      -1.745 -16.089  -5.802  1.00 48.30           C  
ANISOU  883  CG  ARG A 562    10551   4107   3694   -456     41   1057       C  
ATOM    884  CD  ARG A 562      -0.717 -15.363  -4.954  1.00 49.72           C  
ANISOU  884  CD  ARG A 562    10849   4319   3724   -197   -367   1041       C  
ATOM    885  NE  ARG A 562      -0.515 -16.029  -3.671  1.00 57.16           N  
ANISOU  885  NE  ARG A 562    12314   5002   4401    -83   -420   1055       N  
ATOM    886  CZ  ARG A 562       0.413 -15.686  -2.783  1.00 59.30           C  
ANISOU  886  CZ  ARG A 562    12778   5230   4525    157   -790   1021       C  
ATOM    887  NH1 ARG A 562       1.246 -14.686  -3.038  1.00 57.59           N  
ANISOU  887  NH1 ARG A 562    12231   5219   4431    297  -1133    955       N  
ATOM    888  NH2 ARG A 562       0.519 -16.354  -1.642  1.00 62.33           N  
ANISOU  888  NH2 ARG A 562    13690   5349   4642    254   -817   1033       N  
ATOM    889  N   GLY A 563      -3.231 -14.362  -9.798  1.00 36.98           N  
ANISOU  889  N   GLY A 563     7231   3553   3267   -833    383    690       N  
ATOM    890  CA  GLY A 563      -3.890 -13.423 -10.688  1.00 37.71           C  
ANISOU  890  CA  GLY A 563     6831   3923   3573   -917    483    559       C  
ATOM    891  C   GLY A 563      -4.950 -14.073 -11.559  1.00 40.73           C  
ANISOU  891  C   GLY A 563     6976   4341   4157  -1104    745    448       C  
ATOM    892  O   GLY A 563      -6.041 -13.533 -11.738  1.00 39.19           O  
ANISOU  892  O   GLY A 563     6550   4280   4060  -1239    964    330       O  
ATOM    893  N   MET A 564      -4.629 -15.243 -12.099  1.00 44.37           N  
ANISOU  893  N   MET A 564     7484   4678   4696  -1101    705    461       N  
ATOM    894  CA  MET A 564      -5.548 -15.954 -12.983  1.00 41.22           C  
ANISOU  894  CA  MET A 564     6860   4299   4502  -1279    915    330       C  
ATOM    895  C   MET A 564      -6.757 -16.502 -12.232  1.00 41.53           C  
ANISOU  895  C   MET A 564     7109   4174   4498  -1543   1320    287       C  
ATOM    896  O   MET A 564      -7.876 -16.490 -12.743  1.00 40.77           O  
ANISOU  896  O   MET A 564     6705   4186   4599  -1726   1544    107       O  
ATOM    897  CB  MET A 564      -4.821 -17.080 -13.713  1.00 38.06           C  
ANISOU  897  CB  MET A 564     6493   3781   4187  -1202    769    347       C  
ATOM    898  CG  MET A 564      -3.763 -16.588 -14.679  1.00 32.48           C  
ANISOU  898  CG  MET A 564     5499   3257   3586   -989    455    331       C  
ATOM    899  SD  MET A 564      -4.444 -15.472 -15.924  1.00 44.15           S  
ANISOU  899  SD  MET A 564     6460   5071   5242  -1022    466    169       S  
ATOM    900  CE  MET A 564      -5.618 -16.541 -16.755  1.00 39.69           C  
ANISOU  900  CE  MET A 564     5749   4476   4855  -1226    679      0       C  
ATOM    901  N   ASP A 565      -6.530 -16.978 -11.016  1.00 45.05           N  
ANISOU  901  N   ASP A 565     8087   4347   4684  -1562   1418    435       N  
ATOM    902  CA  ASP A 565      -7.625 -17.454 -10.186  1.00 49.07           C  
ANISOU  902  CA  ASP A 565     8871   4661   5113  -1839   1870    404       C  
ATOM    903  C   ASP A 565      -8.566 -16.298  -9.873  1.00 48.05           C  
ANISOU  903  C   ASP A 565     8487   4740   5031  -1943   2079    277       C  
ATOM    904  O   ASP A 565      -9.785 -16.450  -9.897  1.00 51.30           O  
ANISOU  904  O   ASP A 565     8708   5175   5609  -2181   2436     94       O  
ATOM    905  CB  ASP A 565      -7.094 -18.068  -8.895  1.00 53.88           C  
ANISOU  905  CB  ASP A 565    10156   4943   5374  -1766   1876    592       C  
ATOM    906  CG  ASP A 565      -8.191 -18.684  -8.052  1.00 60.50           C  
ANISOU  906  CG  ASP A 565    11188   5631   6169  -1960   2278    483       C  
ATOM    907  OD1 ASP A 565      -9.115 -19.298  -8.631  1.00 58.57           O  
ANISOU  907  OD1 ASP A 565    10693   5394   6168  -2179   2545    314       O  
ATOM    908  OD2 ASP A 565      -8.134 -18.543  -6.812  1.00 65.18           O  
ANISOU  908  OD2 ASP A 565    12182   6093   6489  -1896   2323    543       O  
ATOM    909  N   TYR A 566      -7.985 -15.140  -9.588  1.00 46.85           N  
ANISOU  909  N   TYR A 566     8295   4743   4762  -1740   1830    339       N  
ATOM    910  CA  TYR A 566      -8.760 -13.932  -9.350  1.00 47.11           C  
ANISOU  910  CA  TYR A 566     8080   4977   4842  -1783   1973    218       C  
ATOM    911  C   TYR A 566      -9.584 -13.549 -10.578  1.00 44.44           C  
ANISOU  911  C   TYR A 566     7119   4908   4857  -1830   1989     -9       C  
ATOM    912  O   TYR A 566     -10.787 -13.311 -10.473  1.00 43.80           O  
ANISOU  912  O   TYR A 566     6818   4899   4924  -2000   2297   -198       O  
ATOM    913  CB  TYR A 566      -7.838 -12.777  -8.950  1.00 44.30           C  
ANISOU  913  CB  TYR A 566     7796   4724   4313  -1542   1651    322       C  
ATOM    914  CG  TYR A 566      -8.544 -11.443  -8.828  1.00 44.60           C  
ANISOU  914  CG  TYR A 566     7565   4969   4413  -1544   1749    195       C  
ATOM    915  CD1 TYR A 566      -9.215 -11.093  -7.660  1.00 48.09           C  
ANISOU  915  CD1 TYR A 566     8268   5322   4680  -1660   2064    171       C  
ATOM    916  CD2 TYR A 566      -8.536 -10.530  -9.877  1.00 40.62           C  
ANISOU  916  CD2 TYR A 566     6586   4725   4124  -1420   1538     98       C  
ATOM    917  CE1 TYR A 566      -9.860  -9.873  -7.543  1.00 47.32           C  
ANISOU  917  CE1 TYR A 566     7921   5403   4654  -1640   2153     37       C  
ATOM    918  CE2 TYR A 566      -9.178  -9.310  -9.769  1.00 41.36           C  
ANISOU  918  CE2 TYR A 566     6466   4977   4271  -1389   1607    -19       C  
ATOM    919  CZ  TYR A 566      -9.837  -8.987  -8.601  1.00 46.04           C  
ANISOU  919  CZ  TYR A 566     7282   5491   4721  -1494   1908    -56       C  
ATOM    920  OH  TYR A 566     -10.476  -7.775  -8.493  1.00 47.20           O  
ANISOU  920  OH  TYR A 566     7210   5786   4935  -1443   1976   -189       O  
ATOM    921  N   LEU A 567      -8.932 -13.487 -11.737  1.00 43.00           N  
ANISOU  921  N   LEU A 567     6663   4867   4807  -1667   1654     -7       N  
ATOM    922  CA  LEU A 567      -9.621 -13.167 -12.987  1.00 43.52           C  
ANISOU  922  CA  LEU A 567     6210   5169   5158  -1666   1602   -211       C  
ATOM    923  C   LEU A 567     -10.801 -14.097 -13.246  1.00 45.31           C  
ANISOU  923  C   LEU A 567     6269   5344   5600  -1921   1909   -415       C  
ATOM    924  O   LEU A 567     -11.862 -13.658 -13.688  1.00 46.50           O  
ANISOU  924  O   LEU A 567     6022   5670   5974  -1980   2002   -651       O  
ATOM    925  CB  LEU A 567      -8.661 -13.236 -14.176  1.00 41.39           C  
ANISOU  925  CB  LEU A 567     5791   4991   4946  -1481   1249   -162       C  
ATOM    926  CG  LEU A 567      -7.624 -12.129 -14.326  1.00 40.40           C  
ANISOU  926  CG  LEU A 567     5654   4980   4718  -1250    950    -47       C  
ATOM    927  CD1 LEU A 567      -6.768 -12.377 -15.557  1.00 39.00           C  
ANISOU  927  CD1 LEU A 567     5333   4866   4619  -1121    699    -32       C  
ATOM    928  CD2 LEU A 567      -8.311 -10.780 -14.413  1.00 40.87           C  
ANISOU  928  CD2 LEU A 567     5475   5229   4826  -1195    959   -151       C  
ATOM    929  N   HIS A 568     -10.611 -15.382 -12.966  1.00 44.98           N  
ANISOU  929  N   HIS A 568     6533   5051   5506  -2065   2054   -343       N  
ATOM    930  CA  HIS A 568     -11.646 -16.373 -13.243  1.00 48.07           C  
ANISOU  930  CA  HIS A 568     6786   5356   6122  -2343   2360   -547       C  
ATOM    931  C   HIS A 568     -12.772 -16.345 -12.218  1.00 52.28           C  
ANISOU  931  C   HIS A 568     7379   5814   6673  -2540   2769   -675       C  
ATOM    932  O   HIS A 568     -13.912 -16.681 -12.534  1.00 55.50           O  
ANISOU  932  O   HIS A 568     7468   6279   7340  -2668   2933   -946       O  
ATOM    933  CB  HIS A 568     -11.038 -17.773 -13.368  1.00 47.51           C  
ANISOU  933  CB  HIS A 568     7044   5014   5993  -2405   2359   -432       C  
ATOM    934  CG  HIS A 568     -10.203 -17.951 -14.595  1.00 48.27           C  
ANISOU  934  CG  HIS A 568     6959   5220   6161  -2196   1969   -410       C  
ATOM    935  ND1 HIS A 568      -9.678 -19.164 -14.980  1.00 51.76           N  
ANISOU  935  ND1 HIS A 568     7597   5459   6610  -2214   1922   -357       N  
ATOM    936  CD2 HIS A 568      -9.813 -17.057 -15.539  1.00 45.47           C  
ANISOU  936  CD2 HIS A 568     6273   5140   5865  -1968   1636   -441       C  
ATOM    937  CE1 HIS A 568      -8.996 -19.013 -16.102  1.00 50.60           C  
ANISOU  937  CE1 HIS A 568     7223   5474   6530  -2009   1588   -369       C  
ATOM    938  NE2 HIS A 568      -9.062 -17.742 -16.460  1.00 47.42           N  
ANISOU  938  NE2 HIS A 568     6515   5354   6148  -1867   1422   -413       N  
ATOM    939  N   ALA A 569     -12.455 -15.939 -10.995  1.00 53.76           N  
ANISOU  939  N   ALA A 569     7969   5881   6575  -2489   2856   -506       N  
ATOM    940  CA  ALA A 569     -13.480 -15.774  -9.972  1.00 56.56           C  
ANISOU  940  CA  ALA A 569     8392   6177   6923  -2600   3185   -640       C  
ATOM    941  C   ALA A 569     -14.386 -14.617 -10.372  1.00 56.95           C  
ANISOU  941  C   ALA A 569     7899   6520   7222  -2577   3202   -883       C  
ATOM    942  O   ALA A 569     -15.586 -14.625 -10.100  1.00 57.12           O  
ANISOU  942  O   ALA A 569     7713   6557   7434  -2701   3460  -1132       O  
ATOM    943  CB  ALA A 569     -12.845 -15.518  -8.621  1.00 55.76           C  
ANISOU  943  CB  ALA A 569     8858   5890   6438  -2515   3211   -413       C  
ATOM    944  N   LYS A 570     -13.794 -13.627 -11.033  1.00 55.95           N  
ANISOU  944  N   LYS A 570     7549   6614   7095  -2408   2921   -823       N  
ATOM    945  CA  LYS A 570     -14.536 -12.509 -11.600  1.00 59.50           C  
ANISOU  945  CA  LYS A 570     7474   7353   7780  -2323   2858  -1053       C  
ATOM    946  C   LYS A 570     -15.148 -12.896 -12.943  1.00 62.63           C  
ANISOU  946  C   LYS A 570     7367   7910   8520  -2332   2713  -1304       C  
ATOM    947  O   LYS A 570     -15.759 -12.064 -13.617  1.00 61.40           O  
ANISOU  947  O   LYS A 570     6756   7997   8575  -2207   2568  -1519       O  
ATOM    948  CB  LYS A 570     -13.611 -11.308 -11.788  1.00 57.48           C  
ANISOU  948  CB  LYS A 570     7249   7240   7351  -2026   2486   -882       C  
ATOM    949  CG  LYS A 570     -13.176 -10.644 -10.491  1.00 59.23           C  
ANISOU  949  CG  LYS A 570     7882   7356   7266  -1985   2585   -709       C  
ATOM    950  CD  LYS A 570     -14.330  -9.894  -9.860  1.00 61.69           C  
ANISOU  950  CD  LYS A 570     8010   7745   7684  -2068   2911   -929       C  
ATOM    951  CE  LYS A 570     -13.831  -8.786  -8.955  1.00 62.85           C  
ANISOU  951  CE  LYS A 570     8443   7880   7556  -1917   2851   -791       C  
ATOM    952  NZ  LYS A 570     -14.869  -7.735  -8.747  1.00 65.06           N  
ANISOU  952  NZ  LYS A 570     8406   8312   8002  -1884   3026  -1036       N  
ATOM    953  N   SER A 571     -14.979 -14.164 -13.315  1.00 65.20           N  
ANISOU  953  N   SER A 571     7807   8085   8882  -2449   2725  -1283       N  
ATOM    954  CA  SER A 571     -15.449 -14.697 -14.593  1.00 66.39           C  
ANISOU  954  CA  SER A 571     7561   8352   9314  -2455   2559  -1509       C  
ATOM    955  C   SER A 571     -14.900 -13.895 -15.772  1.00 62.52           C  
ANISOU  955  C   SER A 571     6799   8104   8850  -2208   2134  -1501       C  
ATOM    956  O   SER A 571     -15.627 -13.548 -16.702  1.00 63.01           O  
ANISOU  956  O   SER A 571     6417   8375   9149  -2121   1960  -1765       O  
ATOM    957  CB  SER A 571     -16.976 -14.773 -14.642  1.00 70.66           C  
ANISOU  957  CB  SER A 571     7735   8964  10149  -2534   2719  -1869       C  
ATOM    958  OG  SER A 571     -17.552 -13.484 -14.615  1.00 73.23           O  
ANISOU  958  OG  SER A 571     7750   9502  10573  -2383   2645  -2015       O  
ATOM    959  N   ILE A 572     -13.607 -13.598 -15.707  1.00 56.39           N  
ANISOU  959  N   ILE A 572     6357   7279   7789  -2011   1896  -1188       N  
ATOM    960  CA  ILE A 572     -12.907 -12.945 -16.798  1.00 49.84           C  
ANISOU  960  CA  ILE A 572     5417   6614   6907  -1725   1473  -1120       C  
ATOM    961  C   ILE A 572     -11.932 -13.926 -17.428  1.00 48.31           C  
ANISOU  961  C   ILE A 572     5410   6307   6640  -1708   1322   -982       C  
ATOM    962  O   ILE A 572     -11.158 -14.581 -16.734  1.00 47.71           O  
ANISOU  962  O   ILE A 572     5701   6022   6405  -1769   1410   -779       O  
ATOM    963  CB  ILE A 572     -12.124 -11.712 -16.312  1.00 47.23           C  
ANISOU  963  CB  ILE A 572     5268   6326   6350  -1516   1326   -909       C  
ATOM    964  CG1 ILE A 572     -13.080 -10.656 -15.752  1.00 47.15           C  
ANISOU  964  CG1 ILE A 572     5072   6430   6413  -1496   1456  -1057       C  
ATOM    965  CG2 ILE A 572     -11.289 -11.126 -17.446  1.00 42.39           C  
ANISOU  965  CG2 ILE A 572     4604   5833   5670  -1264    952   -824       C  
ATOM    966  CD1 ILE A 572     -12.383  -9.415 -15.232  1.00 42.16           C  
ANISOU  966  CD1 ILE A 572     4630   5821   5568  -1309   1330   -875       C  
ATOM    967  N   ILE A 573     -11.983 -14.028 -18.750  1.00 48.31           N  
ANISOU  967  N   ILE A 573     5175   6434   6746  -1604   1082  -1108       N  
ATOM    968  CA  ILE A 573     -11.053 -14.862 -19.493  1.00 44.51           C  
ANISOU  968  CA  ILE A 573     4840   5868   6204  -1559    930  -1008       C  
ATOM    969  C   ILE A 573     -10.018 -13.966 -20.154  1.00 42.16           C  
ANISOU  969  C   ILE A 573     4595   5680   5746  -1291    637   -855       C  
ATOM    970  O   ILE A 573     -10.368 -12.983 -20.800  1.00 44.25           O  
ANISOU  970  O   ILE A 573     4671   6122   6021  -1139    472   -941       O  
ATOM    971  CB  ILE A 573     -11.785 -15.673 -20.569  1.00 46.75           C  
ANISOU  971  CB  ILE A 573     4868   6199   6697  -1645    885  -1273       C  
ATOM    972  CG1 ILE A 573     -12.941 -16.452 -19.941  1.00 49.89           C  
ANISOU  972  CG1 ILE A 573     5148   6497   7310  -1952   1218  -1483       C  
ATOM    973  CG2 ILE A 573     -10.822 -16.609 -21.283  1.00 47.40           C  
ANISOU  973  CG2 ILE A 573     5130   6168   6711  -1607    767  -1179       C  
ATOM    974  CD1 ILE A 573     -13.892 -17.053 -20.956  1.00 52.39           C  
ANISOU  974  CD1 ILE A 573     5111   6900   7895  -2049   1159  -1829       C  
ATOM    975  N   HIS A 574      -8.745 -14.304 -19.984  1.00 40.33           N  
ANISOU  975  N   HIS A 574     4627   5324   5374  -1232    580   -642       N  
ATOM    976  CA  HIS A 574      -7.660 -13.475 -20.490  1.00 38.77           C  
ANISOU  976  CA  HIS A 574     4479   5201   5049  -1023    369   -508       C  
ATOM    977  C   HIS A 574      -7.555 -13.545 -22.011  1.00 42.99           C  
ANISOU  977  C   HIS A 574     4885   5840   5611   -919    198   -611       C  
ATOM    978  O   HIS A 574      -7.381 -12.517 -22.673  1.00 44.11           O  
ANISOU  978  O   HIS A 574     4980   6104   5677   -764     58   -603       O  
ATOM    979  CB  HIS A 574      -6.337 -13.903 -19.861  1.00 35.98           C  
ANISOU  979  CB  HIS A 574     4391   4689   4591   -990    351   -307       C  
ATOM    980  CG  HIS A 574      -5.196 -12.985 -20.170  1.00 36.80           C  
ANISOU  980  CG  HIS A 574     4516   4860   4606   -819    187   -197       C  
ATOM    981  ND1 HIS A 574      -4.707 -12.804 -21.447  1.00 37.65           N  
ANISOU  981  ND1 HIS A 574     4532   5052   4722   -717     73   -238       N  
ATOM    982  CD2 HIS A 574      -4.441 -12.201 -19.366  1.00 36.99           C  
ANISOU  982  CD2 HIS A 574     4652   4866   4537   -752    139    -68       C  
ATOM    983  CE1 HIS A 574      -3.705 -11.945 -21.417  1.00 35.46           C  
ANISOU  983  CE1 HIS A 574     4296   4798   4378   -617     -1   -139       C  
ATOM    984  NE2 HIS A 574      -3.523 -11.563 -20.166  1.00 37.05           N  
ANISOU  984  NE2 HIS A 574     4600   4944   4532   -635     19    -45       N  
ATOM    985  N   ARG A 575      -7.627 -14.767 -22.536  1.00 40.42           N  
ANISOU  985  N   ARG A 575     4554   5435   5369  -1004    223   -703       N  
ATOM    986  CA  ARG A 575      -7.601 -15.060 -23.974  1.00 40.59           C  
ANISOU  986  CA  ARG A 575     4492   5529   5402   -926     79   -831       C  
ATOM    987  C   ARG A 575      -6.241 -14.927 -24.652  1.00 38.69           C  
ANISOU  987  C   ARG A 575     4389   5272   5038   -781    -15   -705       C  
ATOM    988  O   ARG A 575      -6.093 -15.304 -25.812  1.00 42.46           O  
ANISOU  988  O   ARG A 575     4861   5775   5495   -726    -94   -800       O  
ATOM    989  CB  ARG A 575      -8.651 -14.249 -24.740  1.00 40.97           C  
ANISOU  989  CB  ARG A 575     4331   5765   5471   -839    -61  -1015       C  
ATOM    990  CG  ARG A 575     -10.074 -14.549 -24.338  1.00 44.67           C  
ANISOU  990  CG  ARG A 575     4566   6271   6137   -988     26  -1238       C  
ATOM    991  CD  ARG A 575     -11.054 -13.789 -25.206  1.00 47.26           C  
ANISOU  991  CD  ARG A 575     4663   6789   6505   -842   -188  -1459       C  
ATOM    992  NE  ARG A 575     -12.433 -14.095 -24.840  1.00 54.60           N  
ANISOU  992  NE  ARG A 575     5288   7769   7688   -991   -102  -1734       N  
ATOM    993  CZ  ARG A 575     -13.134 -13.413 -23.941  1.00 55.93           C  
ANISOU  993  CZ  ARG A 575     5311   7988   7950  -1023     16  -1780       C  
ATOM    994  NH1 ARG A 575     -12.586 -12.378 -23.316  1.00 52.86           N  
ANISOU  994  NH1 ARG A 575     5083   7602   7400   -908     35  -1556       N  
ATOM    995  NH2 ARG A 575     -14.384 -13.763 -23.667  1.00 57.98           N  
ANISOU  995  NH2 ARG A 575     5254   8294   8483  -1180    132  -2075       N  
ATOM    996  N   ASP A 576      -5.249 -14.405 -23.943  1.00 34.31           N  
ANISOU  996  N   ASP A 576     3953   4671   4412   -726      5   -518       N  
ATOM    997  CA  ASP A 576      -3.940 -14.216 -24.552  1.00 35.74           C  
ANISOU  997  CA  ASP A 576     4210   4843   4528   -611    -47   -439       C  
ATOM    998  C   ASP A 576      -2.799 -14.233 -23.538  1.00 33.26           C  
ANISOU  998  C   ASP A 576     3996   4421   4219   -591    -28   -287       C  
ATOM    999  O   ASP A 576      -1.829 -13.496 -23.681  1.00 32.62           O  
ANISOU  999  O   ASP A 576     3919   4372   4105   -508    -60   -225       O  
ATOM   1000  CB  ASP A 576      -3.913 -12.911 -25.354  1.00 42.23           C  
ANISOU 1000  CB  ASP A 576     5016   5798   5234   -497   -117   -439       C  
ATOM   1001  CG  ASP A 576      -2.778 -12.868 -26.353  1.00 48.27           C  
ANISOU 1001  CG  ASP A 576     5855   6549   5936   -419   -108   -423       C  
ATOM   1002  OD1 ASP A 576      -2.446 -13.925 -26.929  1.00 48.37           O  
ANISOU 1002  OD1 ASP A 576     5882   6503   5994   -430    -87   -494       O  
ATOM   1003  OD2 ASP A 576      -2.210 -11.777 -26.552  1.00 54.44           O  
ANISOU 1003  OD2 ASP A 576     6690   7364   6631   -359    -94   -352       O  
ATOM   1004  N   LEU A 577      -2.910 -15.080 -22.521  1.00 33.40           N  
ANISOU 1004  N   LEU A 577     4113   4298   4280   -666     21   -244       N  
ATOM   1005  CA  LEU A 577      -1.856 -15.203 -21.524  1.00 32.43           C  
ANISOU 1005  CA  LEU A 577     4123   4056   4143   -607    -23   -118       C  
ATOM   1006  C   LEU A 577      -0.604 -15.818 -22.128  1.00 37.52           C  
ANISOU 1006  C   LEU A 577     4759   4638   4859   -498    -89   -137       C  
ATOM   1007  O   LEU A 577      -0.664 -16.852 -22.794  1.00 42.45           O  
ANISOU 1007  O   LEU A 577     5395   5193   5542   -510    -60   -216       O  
ATOM   1008  CB  LEU A 577      -2.325 -16.058 -20.349  1.00 33.10           C  
ANISOU 1008  CB  LEU A 577     4406   3961   4207   -698     49    -62       C  
ATOM   1009  CG  LEU A 577      -1.306 -16.266 -19.228  1.00 34.02           C  
ANISOU 1009  CG  LEU A 577     4734   3925   4266   -599    -50     66       C  
ATOM   1010  CD1 LEU A 577      -1.000 -14.944 -18.539  1.00 33.59           C  
ANISOU 1010  CD1 LEU A 577     4660   3972   4132   -548   -122    133       C  
ATOM   1011  CD2 LEU A 577      -1.816 -17.294 -18.221  1.00 35.38           C  
ANISOU 1011  CD2 LEU A 577     5205   3866   4372   -689     49    127       C  
ATOM   1012  N   LYS A 578       0.530 -15.172 -21.893  1.00 39.15           N  
ANISOU 1012  N   LYS A 578     4925   4869   5082   -397   -169    -93       N  
ATOM   1013  CA  LYS A 578       1.823 -15.701 -22.304  1.00 41.20           C  
ANISOU 1013  CA  LYS A 578     5129   5070   5456   -282   -225   -144       C  
ATOM   1014  C   LYS A 578       2.925 -15.016 -21.513  1.00 40.16           C  
ANISOU 1014  C   LYS A 578     4950   4940   5371   -191   -344   -109       C  
ATOM   1015  O   LYS A 578       2.667 -14.061 -20.785  1.00 42.16           O  
ANISOU 1015  O   LYS A 578     5231   5246   5543   -227   -372    -41       O  
ATOM   1016  CB  LYS A 578       2.039 -15.532 -23.808  1.00 43.73           C  
ANISOU 1016  CB  LYS A 578     5319   5492   5805   -280   -131   -251       C  
ATOM   1017  CG  LYS A 578       1.583 -14.204 -24.350  1.00 47.72           C  
ANISOU 1017  CG  LYS A 578     5775   6150   6205   -330    -70   -242       C  
ATOM   1018  CD  LYS A 578       1.592 -14.200 -25.864  1.00 51.16           C  
ANISOU 1018  CD  LYS A 578     6193   6647   6597   -324     26   -340       C  
ATOM   1019  CE  LYS A 578       0.796 -13.026 -26.398  1.00 53.62           C  
ANISOU 1019  CE  LYS A 578     6547   7075   6752   -348     48   -322       C  
ATOM   1020  NZ  LYS A 578       1.511 -12.344 -27.508  1.00 57.15           N  
ANISOU 1020  NZ  LYS A 578     7030   7553   7131   -324    165   -357       N  
ATOM   1021  N   SER A 579       4.150 -15.506 -21.656  1.00 39.64           N  
ANISOU 1021  N   SER A 579     4792   4815   5453    -68   -424   -185       N  
ATOM   1022  CA  SER A 579       5.258 -15.038 -20.830  1.00 41.98           C  
ANISOU 1022  CA  SER A 579     5010   5098   5841     39   -590   -204       C  
ATOM   1023  C   SER A 579       5.604 -13.558 -21.022  1.00 42.98           C  
ANISOU 1023  C   SER A 579     4967   5373   5990    -33   -529   -233       C  
ATOM   1024  O   SER A 579       6.180 -12.936 -20.132  1.00 42.87           O  
ANISOU 1024  O   SER A 579     4917   5360   6010      7   -671   -237       O  
ATOM   1025  CB  SER A 579       6.492 -15.915 -21.050  1.00 41.97           C  
ANISOU 1025  CB  SER A 579     4886   5011   6048    207   -695   -333       C  
ATOM   1026  OG  SER A 579       6.714 -16.140 -22.428  1.00 44.46           O  
ANISOU 1026  OG  SER A 579     5048   5385   6461    173   -506   -448       O  
ATOM   1027  N   ASN A 580       5.262 -12.995 -22.176  1.00 45.54           N  
ANISOU 1027  N   ASN A 580     5223   5799   6280   -135   -328   -260       N  
ATOM   1028  CA  ASN A 580       5.515 -11.577 -22.410  1.00 51.58           C  
ANISOU 1028  CA  ASN A 580     5901   6660   7038   -217   -235   -272       C  
ATOM   1029  C   ASN A 580       4.338 -10.701 -21.991  1.00 50.48           C  
ANISOU 1029  C   ASN A 580     5909   6568   6702   -292   -224   -151       C  
ATOM   1030  O   ASN A 580       4.416  -9.476 -22.034  1.00 50.44           O  
ANISOU 1030  O   ASN A 580     5888   6612   6663   -350   -164   -140       O  
ATOM   1031  CB  ASN A 580       5.923 -11.311 -23.861  1.00 55.88           C  
ANISOU 1031  CB  ASN A 580     6357   7253   7623   -270    -10   -365       C  
ATOM   1032  CG  ASN A 580       5.076 -12.069 -24.849  1.00 60.30           C  
ANISOU 1032  CG  ASN A 580     7033   7815   8062   -273     76   -359       C  
ATOM   1033  OD1 ASN A 580       3.957 -11.665 -25.158  1.00 62.68           O  
ANISOU 1033  OD1 ASN A 580     7468   8165   8183   -318    103   -289       O  
ATOM   1034  ND2 ASN A 580       5.604 -13.179 -25.354  1.00 61.72           N  
ANISOU 1034  ND2 ASN A 580     7153   7941   8356   -210    100   -457       N  
ATOM   1035  N   ASN A 581       3.251 -11.348 -21.583  1.00 50.39           N  
ANISOU 1035  N   ASN A 581     6039   6527   6580   -295   -263    -78       N  
ATOM   1036  CA  ASN A 581       2.105 -10.663 -21.001  1.00 48.75           C  
ANISOU 1036  CA  ASN A 581     5940   6357   6225   -352   -253      5       C  
ATOM   1037  C   ASN A 581       2.266 -10.567 -19.490  1.00 45.02           C  
ANISOU 1037  C   ASN A 581     5570   5816   5718   -328   -381     67       C  
ATOM   1038  O   ASN A 581       1.485  -9.905 -18.808  1.00 43.50           O  
ANISOU 1038  O   ASN A 581     5472   5646   5411   -372   -364    124       O  
ATOM   1039  CB  ASN A 581       0.815 -11.420 -21.326  1.00 53.06           C  
ANISOU 1039  CB  ASN A 581     6553   6906   6704   -395   -193      6       C  
ATOM   1040  CG  ASN A 581       0.327 -11.165 -22.731  1.00 62.15           C  
ANISOU 1040  CG  ASN A 581     7650   8147   7819   -406   -110    -58       C  
ATOM   1041  OD1 ASN A 581       1.063 -10.654 -23.573  1.00 68.99           O  
ANISOU 1041  OD1 ASN A 581     8475   9044   8695   -383    -60    -90       O  
ATOM   1042  ND2 ASN A 581      -0.925 -11.514 -22.993  1.00 64.42           N  
ANISOU 1042  ND2 ASN A 581     7951   8467   8060   -443    -90    -95       N  
ATOM   1043  N   ILE A 582       3.285 -11.248 -18.978  1.00 42.03           N  
ANISOU 1043  N   ILE A 582     5190   5349   5432   -238   -522     42       N  
ATOM   1044  CA  ILE A 582       3.539 -11.315 -17.546  1.00 41.83           C  
ANISOU 1044  CA  ILE A 582     5325   5230   5338   -174   -696     93       C  
ATOM   1045  C   ILE A 582       4.723 -10.433 -17.185  1.00 41.21           C  
ANISOU 1045  C   ILE A 582     5107   5187   5366   -123   -840     14       C  
ATOM   1046  O   ILE A 582       5.876 -10.780 -17.431  1.00 44.20           O  
ANISOU 1046  O   ILE A 582     5314   5548   5930    -33   -947    -97       O  
ATOM   1047  CB  ILE A 582       3.808 -12.766 -17.092  1.00 42.74           C  
ANISOU 1047  CB  ILE A 582     5601   5182   5457    -67   -815    113       C  
ATOM   1048  CG1 ILE A 582       2.613 -13.660 -17.436  1.00 42.21           C  
ANISOU 1048  CG1 ILE A 582     5669   5059   5311   -162   -640    166       C  
ATOM   1049  CG2 ILE A 582       4.112 -12.814 -15.603  1.00 43.33           C  
ANISOU 1049  CG2 ILE A 582     5923   5135   5406     31  -1025    172       C  
ATOM   1050  CD1 ILE A 582       2.845 -15.128 -17.168  1.00 43.94           C  
ANISOU 1050  CD1 ILE A 582     6079   5079   5536    -75   -713    185       C  
ATOM   1051  N   PHE A 583       4.424  -9.282 -16.602  1.00 40.89           N  
ANISOU 1051  N   PHE A 583     5116   5190   5229   -183   -836     45       N  
ATOM   1052  CA  PHE A 583       5.444  -8.296 -16.287  1.00 41.99           C  
ANISOU 1052  CA  PHE A 583     5113   5362   5479   -177   -948    -53       C  
ATOM   1053  C   PHE A 583       5.969  -8.488 -14.869  1.00 44.93           C  
ANISOU 1053  C   PHE A 583     5632   5646   5794    -56  -1237    -66       C  
ATOM   1054  O   PHE A 583       5.200  -8.519 -13.908  1.00 45.22           O  
ANISOU 1054  O   PHE A 583     5956   5622   5602    -50  -1268     42       O  
ATOM   1055  CB  PHE A 583       4.868  -6.890 -16.461  1.00 40.94           C  
ANISOU 1055  CB  PHE A 583     4986   5300   5269   -300   -795    -26       C  
ATOM   1056  CG  PHE A 583       4.203  -6.675 -17.793  1.00 41.84           C  
ANISOU 1056  CG  PHE A 583     5047   5479   5373   -377   -555      1       C  
ATOM   1057  CD1 PHE A 583       4.872  -6.969 -18.973  1.00 43.04           C  
ANISOU 1057  CD1 PHE A 583     5029   5652   5671   -391   -453    -77       C  
ATOM   1058  CD2 PHE A 583       2.904  -6.204 -17.867  1.00 42.18           C  
ANISOU 1058  CD2 PHE A 583     5218   5557   5253   -418   -442     85       C  
ATOM   1059  CE1 PHE A 583       4.262  -6.783 -20.205  1.00 39.77           C  
ANISOU 1059  CE1 PHE A 583     4633   5281   5195   -440   -259    -52       C  
ATOM   1060  CE2 PHE A 583       2.287  -6.017 -19.098  1.00 43.40           C  
ANISOU 1060  CE2 PHE A 583     5345   5764   5379   -445   -287     92       C  
ATOM   1061  CZ  PHE A 583       2.969  -6.310 -20.269  1.00 39.23           C  
ANISOU 1061  CZ  PHE A 583     4708   5246   4952   -454   -204     33       C  
ATOM   1062  N   LEU A 584       7.283  -8.639 -14.747  1.00 46.74           N  
ANISOU 1062  N   LEU A 584     5669   5861   6228     49  -1451   -218       N  
ATOM   1063  CA  LEU A 584       7.918  -8.710 -13.439  1.00 48.53           C  
ANISOU 1063  CA  LEU A 584     6023   6010   6407    200  -1798   -271       C  
ATOM   1064  C   LEU A 584       8.267  -7.313 -12.966  1.00 46.93           C  
ANISOU 1064  C   LEU A 584     5729   5866   6234    116  -1855   -366       C  
ATOM   1065  O   LEU A 584       9.380  -6.831 -13.175  1.00 47.51           O  
ANISOU 1065  O   LEU A 584     5487   5989   6577    110  -1953   -569       O  
ATOM   1066  CB  LEU A 584       9.177  -9.570 -13.481  1.00 54.81           C  
ANISOU 1066  CB  LEU A 584     6625   6760   7440    396  -2064   -435       C  
ATOM   1067  CG  LEU A 584       9.004 -11.063 -13.751  1.00 59.15           C  
ANISOU 1067  CG  LEU A 584     7315   7200   7961    529  -2080   -360       C  
ATOM   1068  CD1 LEU A 584      10.293 -11.786 -13.409  1.00 62.43           C  
ANISOU 1068  CD1 LEU A 584     7597   7542   8581    793  -2449   -539       C  
ATOM   1069  CD2 LEU A 584       7.836 -11.634 -12.960  1.00 60.47           C  
ANISOU 1069  CD2 LEU A 584     7972   7233   7772    533  -2048   -134       C  
ATOM   1070  N   HIS A 585       7.297  -6.667 -12.333  1.00 46.39           N  
ANISOU 1070  N   HIS A 585     5931   5788   5909     38  -1771   -240       N  
ATOM   1071  CA  HIS A 585       7.473  -5.318 -11.816  1.00 50.30           C  
ANISOU 1071  CA  HIS A 585     6404   6316   6392    -46  -1809   -317       C  
ATOM   1072  C   HIS A 585       8.508  -5.280 -10.696  1.00 55.96           C  
ANISOU 1072  C   HIS A 585     7141   6980   7141    100  -2217   -471       C  
ATOM   1073  O   HIS A 585       8.353  -5.954  -9.676  1.00 57.99           O  
ANISOU 1073  O   HIS A 585     7728   7136   7168    260  -2446   -401       O  
ATOM   1074  CB  HIS A 585       6.136  -4.784 -11.315  1.00 51.07           C  
ANISOU 1074  CB  HIS A 585     6811   6399   6196   -124  -1633   -157       C  
ATOM   1075  CG  HIS A 585       6.230  -3.449 -10.655  1.00 54.49           C  
ANISOU 1075  CG  HIS A 585     7289   6837   6578   -191  -1681   -229       C  
ATOM   1076  ND1 HIS A 585       6.811  -2.357 -11.264  1.00 54.94           N  
ANISOU 1076  ND1 HIS A 585     7083   6942   6849   -314  -1600   -356       N  
ATOM   1077  CD2 HIS A 585       5.820  -3.027  -9.436  1.00 58.01           C  
ANISOU 1077  CD2 HIS A 585     8043   7225   6775   -160  -1782   -200       C  
ATOM   1078  CE1 HIS A 585       6.754  -1.320 -10.448  1.00 57.52           C  
ANISOU 1078  CE1 HIS A 585     7539   7240   7078   -355  -1667   -406       C  
ATOM   1079  NE2 HIS A 585       6.157  -1.700  -9.332  1.00 60.05           N  
ANISOU 1079  NE2 HIS A 585     8200   7504   7113   -255  -1785   -317       N  
ATOM   1080  N   GLU A 586       9.563  -4.494 -10.900  1.00 59.06           N  
ANISOU 1080  N   GLU A 586     7195   7428   7816     43  -2305   -695       N  
ATOM   1081  CA  GLU A 586      10.680  -4.418  -9.960  1.00 64.56           C  
ANISOU 1081  CA  GLU A 586     7810   8098   8624    187  -2738   -916       C  
ATOM   1082  C   GLU A 586      11.276  -5.792  -9.688  1.00 68.62           C  
ANISOU 1082  C   GLU A 586     8345   8550   9178    455  -3060   -957       C  
ATOM   1083  O   GLU A 586      11.807  -6.041  -8.606  1.00 71.55           O  
ANISOU 1083  O   GLU A 586     8880   8846   9460    659  -3433  -1036       O  
ATOM   1084  CB  GLU A 586      10.250  -3.761  -8.644  1.00 67.64           C  
ANISOU 1084  CB  GLU A 586     8570   8428   8702    214  -2915   -876       C  
ATOM   1085  CG  GLU A 586       9.828  -2.307  -8.774  1.00 69.57           C  
ANISOU 1085  CG  GLU A 586     8787   8709   8935    -17  -2663   -885       C  
ATOM   1086  CD  GLU A 586      11.005  -1.348  -8.806  1.00 75.80           C  
ANISOU 1086  CD  GLU A 586     9209   9534  10058   -116  -2796  -1187       C  
ATOM   1087  OE1 GLU A 586      12.159  -1.810  -8.936  1.00 79.27           O  
ANISOU 1087  OE1 GLU A 586     9315  10001  10802    -25  -3035  -1412       O  
ATOM   1088  OE2 GLU A 586      10.776  -0.125  -8.694  1.00 76.93           O  
ANISOU 1088  OE2 GLU A 586     9385   9666  10177   -286  -2654  -1220       O  
ATOM   1089  N   ASP A 587      11.152  -6.681 -10.673  1.00 70.74           N  
ANISOU 1089  N   ASP A 587     8496   8828   9554    464  -2862   -886       N  
ATOM   1090  CA  ASP A 587      11.728  -8.025 -10.627  1.00 74.23           C  
ANISOU 1090  CA  ASP A 587     8931   9195  10077    719  -3120   -931       C  
ATOM   1091  C   ASP A 587      11.097  -8.974  -9.610  1.00 74.14           C  
ANISOU 1091  C   ASP A 587     9481   9014   9673    919  -3324   -725       C  
ATOM   1092  O   ASP A 587      11.498 -10.132  -9.521  1.00 77.91           O  
ANISOU 1092  O   ASP A 587    10045   9386  10173   1149  -3538   -734       O  
ATOM   1093  CB  ASP A 587      13.243  -7.954 -10.402  1.00 81.64           C  
ANISOU 1093  CB  ASP A 587     9501  10156  11361    860  -3410  -1248       C  
ATOM   1094  CG  ASP A 587      14.024  -7.953 -11.695  1.00 86.20           C  
ANISOU 1094  CG  ASP A 587     9535  10837  12379    758  -3189  -1451       C  
ATOM   1095  OD1 ASP A 587      14.057  -6.906 -12.376  1.00 85.58           O  
ANISOU 1095  OD1 ASP A 587     9184  10860  12473    492  -2911  -1535       O  
ATOM   1096  OD2 ASP A 587      14.609  -9.005 -12.026  1.00 90.43           O  
ANISOU 1096  OD2 ASP A 587     9951  11331  13076    939  -3265  -1529       O  
ATOM   1097  N   ASN A 588      10.112  -8.500  -8.854  1.00 71.21           N  
ANISOU 1097  N   ASN A 588     9518   8599   8941    829  -3226   -545       N  
ATOM   1098  CA  ASN A 588       9.530  -9.312  -7.788  1.00 70.49           C  
ANISOU 1098  CA  ASN A 588    10019   8317   8445    987  -3372   -360       C  
ATOM   1099  C   ASN A 588       8.046  -9.626  -7.955  1.00 64.84           C  
ANISOU 1099  C   ASN A 588     9625   7550   7460    810  -2941    -94       C  
ATOM   1100  O   ASN A 588       7.614 -10.746  -7.696  1.00 67.43           O  
ANISOU 1100  O   ASN A 588    10315   7711   7594    898  -2922     53       O  
ATOM   1101  CB  ASN A 588       9.770  -8.667  -6.420  1.00 74.27           C  
ANISOU 1101  CB  ASN A 588    10760   8732   8726   1052  -3553   -413       C  
ATOM   1102  CG  ASN A 588      11.239  -8.615  -6.049  1.00 81.12           C  
ANISOU 1102  CG  ASN A 588    11358   9600   9864   1239  -3889   -679       C  
ATOM   1103  OD1 ASN A 588      11.850  -9.638  -5.741  1.00 84.17           O  
ANISOU 1103  OD1 ASN A 588    11851   9858  10273   1473  -4105   -722       O  
ATOM   1104  ND2 ASN A 588      11.812  -7.417  -6.068  1.00 84.11           N  
ANISOU 1104  ND2 ASN A 588    11395  10109  10452   1131  -3928   -874       N  
ATOM   1105  N   THR A 589       7.267  -8.639  -8.381  1.00 58.47           N  
ANISOU 1105  N   THR A 589     8687   6871   6658    564  -2598    -53       N  
ATOM   1106  CA  THR A 589       5.820  -8.798  -8.453  1.00 53.95           C  
ANISOU 1106  CA  THR A 589     8366   6270   5864    400  -2212    143       C  
ATOM   1107  C   THR A 589       5.309  -9.064  -9.867  1.00 51.30           C  
ANISOU 1107  C   THR A 589     7723   6034   5733    256  -1885    173       C  
ATOM   1108  O   THR A 589       5.545  -8.281 -10.788  1.00 51.52           O  
ANISOU 1108  O   THR A 589     7375   6211   5988    155  -1774     82       O  
ATOM   1109  CB  THR A 589       5.096  -7.566  -7.895  1.00 53.25           C  
ANISOU 1109  CB  THR A 589     8394   6237   5603    259  -2057    165       C  
ATOM   1110  OG1 THR A 589       5.582  -7.284  -6.579  1.00 63.31           O  
ANISOU 1110  OG1 THR A 589     9980   7414   6659    394  -2373    120       O  
ATOM   1111  CG2 THR A 589       3.599  -7.813  -7.831  1.00 49.27           C  
ANISOU 1111  CG2 THR A 589     8137   5694   4891    113  -1675    325       C  
ATOM   1112  N   VAL A 590       4.596 -10.173 -10.024  1.00 46.07           N  
ANISOU 1112  N   VAL A 590     7263   5270   4972    242  -1726    295       N  
ATOM   1113  CA  VAL A 590       3.977 -10.520 -11.293  1.00 43.44           C  
ANISOU 1113  CA  VAL A 590     6695   5018   4794    111  -1436    314       C  
ATOM   1114  C   VAL A 590       2.824  -9.577 -11.612  1.00 41.17           C  
ANISOU 1114  C   VAL A 590     6330   4855   4460    -81  -1134    345       C  
ATOM   1115  O   VAL A 590       1.962  -9.329 -10.769  1.00 39.79           O  
ANISOU 1115  O   VAL A 590     6420   4631   4069   -146  -1017    415       O  
ATOM   1116  CB  VAL A 590       3.468 -11.977 -11.281  1.00 42.94           C  
ANISOU 1116  CB  VAL A 590     6891   4786   4639    129  -1348    413       C  
ATOM   1117  CG1 VAL A 590       2.444 -12.215 -12.384  1.00 39.01           C  
ANISOU 1117  CG1 VAL A 590     6216   4371   4235    -49  -1016    427       C  
ATOM   1118  CG2 VAL A 590       4.636 -12.939 -11.404  1.00 42.98           C  
ANISOU 1118  CG2 VAL A 590     6872   4686   4771    342  -1631    356       C  
ATOM   1119  N   LYS A 591       2.818  -9.051 -12.834  1.00 36.57           N  
ANISOU 1119  N   LYS A 591     5404   4419   4072   -157  -1008    282       N  
ATOM   1120  CA  LYS A 591       1.729  -8.204 -13.298  1.00 35.79           C  
ANISOU 1120  CA  LYS A 591     5223   4430   3945   -290   -764    297       C  
ATOM   1121  C   LYS A 591       1.165  -8.747 -14.607  1.00 35.74           C  
ANISOU 1121  C   LYS A 591     5040   4487   4052   -348   -591    286       C  
ATOM   1122  O   LYS A 591       1.808  -8.654 -15.651  1.00 34.02           O  
ANISOU 1122  O   LYS A 591     4601   4334   3991   -332   -604    225       O  
ATOM   1123  CB  LYS A 591       2.217  -6.764 -13.503  1.00 37.12           C  
ANISOU 1123  CB  LYS A 591     5221   4694   4188   -311   -798    228       C  
ATOM   1124  CG  LYS A 591       2.703  -6.068 -12.242  1.00 37.96           C  
ANISOU 1124  CG  LYS A 591     5487   4750   4187   -269   -975    205       C  
ATOM   1125  CD  LYS A 591       1.561  -5.826 -11.280  1.00 39.16           C  
ANISOU 1125  CD  LYS A 591     5919   4860   4100   -312   -852    278       C  
ATOM   1126  CE  LYS A 591       2.036  -5.128 -10.021  1.00 43.37           C  
ANISOU 1126  CE  LYS A 591     6657   5334   4488   -263  -1035    246       C  
ATOM   1127  NZ  LYS A 591       0.882  -4.735  -9.165  1.00 44.18           N  
ANISOU 1127  NZ  LYS A 591     7024   5403   4359   -320   -852    297       N  
ATOM   1128  N   ILE A 592      -0.034  -9.312 -14.556  1.00 34.53           N  
ANISOU 1128  N   ILE A 592     4988   4309   3822   -426   -418    323       N  
ATOM   1129  CA  ILE A 592      -0.654  -9.841 -15.763  1.00 35.63           C  
ANISOU 1129  CA  ILE A 592     4962   4510   4065   -479   -287    281       C  
ATOM   1130  C   ILE A 592      -1.428  -8.761 -16.506  1.00 38.84           C  
ANISOU 1130  C   ILE A 592     5202   5063   4494   -516   -186    231       C  
ATOM   1131  O   ILE A 592      -2.350  -8.157 -15.963  1.00 42.37           O  
ANISOU 1131  O   ILE A 592     5694   5538   4866   -558    -93    227       O  
ATOM   1132  CB  ILE A 592      -1.597 -11.023 -15.459  1.00 34.59           C  
ANISOU 1132  CB  ILE A 592     4979   4275   3889   -565   -145    298       C  
ATOM   1133  CG1 ILE A 592      -0.820 -12.177 -14.829  1.00 34.91           C  
ANISOU 1133  CG1 ILE A 592     5253   4126   3886   -497   -259    360       C  
ATOM   1134  CG2 ILE A 592      -2.296 -11.491 -16.729  1.00 32.31           C  
ANISOU 1134  CG2 ILE A 592     4491   4064   3723   -625    -38    213       C  
ATOM   1135  CD1 ILE A 592      -1.700 -13.318 -14.374  1.00 36.54           C  
ANISOU 1135  CD1 ILE A 592     5694   4169   4019   -607    -81    394       C  
ATOM   1136  N   GLY A 593      -1.041  -8.522 -17.752  1.00 39.26           N  
ANISOU 1136  N   GLY A 593     5087   5193   4638   -485   -201    186       N  
ATOM   1137  CA  GLY A 593      -1.725  -7.555 -18.584  1.00 38.54           C  
ANISOU 1137  CA  GLY A 593     4900   5208   4534   -479   -141    146       C  
ATOM   1138  C   GLY A 593      -1.998  -8.096 -19.971  1.00 37.80           C  
ANISOU 1138  C   GLY A 593     4705   5166   4490   -466   -114     83       C  
ATOM   1139  O   GLY A 593      -1.912  -9.306 -20.201  1.00 34.26           O  
ANISOU 1139  O   GLY A 593     4246   4674   4097   -489   -108     61       O  
ATOM   1140  N   ASP A 594      -2.348  -7.189 -20.880  1.00 38.32           N  
ANISOU 1140  N   ASP A 594     4739   5306   4516   -417   -108     53       N  
ATOM   1141  CA  ASP A 594      -2.501  -7.483 -22.301  1.00 38.52           C  
ANISOU 1141  CA  ASP A 594     4729   5374   4533   -375   -109     -9       C  
ATOM   1142  C   ASP A 594      -3.629  -8.469 -22.589  1.00 41.43           C  
ANISOU 1142  C   ASP A 594     5019   5781   4942   -397   -115   -106       C  
ATOM   1143  O   ASP A 594      -3.419  -9.466 -23.273  1.00 46.11           O  
ANISOU 1143  O   ASP A 594     5590   6355   5574   -413   -114   -154       O  
ATOM   1144  CB  ASP A 594      -1.180  -7.999 -22.875  1.00 41.01           C  
ANISOU 1144  CB  ASP A 594     5042   5639   4900   -384    -85     -1       C  
ATOM   1145  CG  ASP A 594      -1.057  -7.760 -24.360  1.00 49.25           C  
ANISOU 1145  CG  ASP A 594     6133   6709   5872   -337    -46    -44       C  
ATOM   1146  OD1 ASP A 594      -1.684  -6.805 -24.871  1.00 49.99           O  
ANISOU 1146  OD1 ASP A 594     6314   6836   5846   -275    -64    -42       O  
ATOM   1147  OD2 ASP A 594      -0.320  -8.524 -25.017  1.00 52.64           O  
ANISOU 1147  OD2 ASP A 594     6543   7110   6349   -347      1    -82       O  
ATOM   1148  N   PHE A 595      -4.823  -8.185 -22.077  1.00 42.38           N  
ANISOU 1148  N   PHE A 595     5079   5949   5073   -406   -107   -162       N  
ATOM   1149  CA  PHE A 595      -5.961  -9.082 -22.273  1.00 47.15           C  
ANISOU 1149  CA  PHE A 595     5558   6591   5767   -460    -90   -301       C  
ATOM   1150  C   PHE A 595      -6.327  -9.171 -23.751  1.00 51.31           C  
ANISOU 1150  C   PHE A 595     6032   7192   6272   -368   -203   -418       C  
ATOM   1151  O   PHE A 595      -5.995  -8.284 -24.535  1.00 50.70           O  
ANISOU 1151  O   PHE A 595     6049   7141   6075   -242   -281   -384       O  
ATOM   1152  CB  PHE A 595      -7.183  -8.635 -21.459  1.00 48.85           C  
ANISOU 1152  CB  PHE A 595     5672   6855   6034   -490    -31   -384       C  
ATOM   1153  CG  PHE A 595      -6.990  -8.703 -19.964  1.00 52.88           C  
ANISOU 1153  CG  PHE A 595     6286   7276   6531   -596    106   -289       C  
ATOM   1154  CD1 PHE A 595      -5.834  -9.231 -19.415  1.00 53.24           C  
ANISOU 1154  CD1 PHE A 595     6499   7204   6525   -637    115   -149       C  
ATOM   1155  CD2 PHE A 595      -7.976  -8.238 -19.108  1.00 55.40           C  
ANISOU 1155  CD2 PHE A 595     6547   7622   6881   -636    216   -358       C  
ATOM   1156  CE1 PHE A 595      -5.658  -9.287 -18.045  1.00 52.20           C  
ANISOU 1156  CE1 PHE A 595     6526   6975   6333   -703    199    -64       C  
ATOM   1157  CE2 PHE A 595      -7.807  -8.294 -17.737  1.00 55.02           C  
ANISOU 1157  CE2 PHE A 595     6659   7475   6770   -730    355   -271       C  
ATOM   1158  CZ  PHE A 595      -6.647  -8.820 -17.206  1.00 53.05           C  
ANISOU 1158  CZ  PHE A 595     6628   7101   6430   -758    330   -116       C  
ATOM   1159  N   GLY A 596      -7.008 -10.250 -24.124  1.00 55.08           N  
ANISOU 1159  N   GLY A 596     6396   7683   6849   -435   -206   -562       N  
ATOM   1160  CA  GLY A 596      -7.415 -10.464 -25.499  1.00 57.12           C  
ANISOU 1160  CA  GLY A 596     6618   8009   7077   -345   -345   -705       C  
ATOM   1161  C   GLY A 596      -8.440  -9.452 -25.974  1.00 61.95           C  
ANISOU 1161  C   GLY A 596     7153   8735   7650   -185   -507   -825       C  
ATOM   1162  O   GLY A 596      -9.542  -9.366 -25.433  1.00 65.35           O  
ANISOU 1162  O   GLY A 596     7382   9228   8219   -211   -507   -965       O  
ATOM   1163  N   GLY A 615      -0.202 -14.242 -33.888  1.00 82.08           N  
ANISOU 1163  N   GLY A 615    10891  10757   9538   -123    216   -892       N  
ATOM   1164  CA  GLY A 615       1.207 -14.573 -33.999  1.00 81.76           C  
ANISOU 1164  CA  GLY A 615    10820  10639   9608   -158    461   -897       C  
ATOM   1165  C   GLY A 615       1.708 -15.417 -32.842  1.00 80.03           C  
ANISOU 1165  C   GLY A 615    10340  10368   9698   -204    451   -882       C  
ATOM   1166  O   GLY A 615       2.736 -16.089 -32.951  1.00 82.35           O  
ANISOU 1166  O   GLY A 615    10563  10591  10136   -197    588   -948       O  
ATOM   1167  N   SER A 616       0.975 -15.383 -31.732  1.00 73.70           N  
ANISOU 1167  N   SER A 616     9420   9591   8992   -235    290   -804       N  
ATOM   1168  CA  SER A 616       1.359 -16.101 -30.519  1.00 66.70           C  
ANISOU 1168  CA  SER A 616     8375   8628   8341   -261    256   -761       C  
ATOM   1169  C   SER A 616       0.635 -17.440 -30.378  1.00 61.50           C  
ANISOU 1169  C   SER A 616     7714   7893   7760   -294    169   -843       C  
ATOM   1170  O   SER A 616      -0.254 -17.596 -29.539  1.00 60.27           O  
ANISOU 1170  O   SER A 616     7522   7729   7649   -359     77   -803       O  
ATOM   1171  CB  SER A 616       1.081 -15.236 -29.295  1.00 68.33           C  
ANISOU 1171  CB  SER A 616     8511   8872   8577   -292    180   -620       C  
ATOM   1172  OG  SER A 616      -0.274 -14.825 -29.274  1.00 69.29           O  
ANISOU 1172  OG  SER A 616     8666   9073   8589   -317     73   -616       O  
ATOM   1173  N   ILE A 617       1.043 -18.412 -31.187  1.00 55.75           N  
ANISOU 1173  N   ILE A 617     7034   7091   7058   -264    230   -970       N  
ATOM   1174  CA  ILE A 617       0.381 -19.709 -31.220  1.00 50.15           C  
ANISOU 1174  CA  ILE A 617     6353   6281   6419   -310    170  -1075       C  
ATOM   1175  C   ILE A 617       0.941 -20.731 -30.223  1.00 45.53           C  
ANISOU 1175  C   ILE A 617     5746   5516   6036   -300    172  -1032       C  
ATOM   1176  O   ILE A 617       0.329 -21.773 -29.992  1.00 43.80           O  
ANISOU 1176  O   ILE A 617     5585   5171   5885   -367    141  -1087       O  
ATOM   1177  CB  ILE A 617       0.451 -20.320 -32.623  1.00 52.41           C  
ANISOU 1177  CB  ILE A 617     6748   6552   6612   -275    220  -1254       C  
ATOM   1178  CG1 ILE A 617       1.909 -20.524 -33.032  1.00 53.54           C  
ANISOU 1178  CG1 ILE A 617     6891   6633   6818   -184    388  -1285       C  
ATOM   1179  CG2 ILE A 617      -0.269 -19.432 -33.623  1.00 52.99           C  
ANISOU 1179  CG2 ILE A 617     6926   6772   6437   -258    163  -1305       C  
ATOM   1180  CD1 ILE A 617       2.159 -21.844 -33.721  1.00 56.93           C  
ANISOU 1180  CD1 ILE A 617     7392   6933   7305   -152    440  -1457       C  
ATOM   1181  N   LEU A 618       2.099 -20.439 -29.639  1.00 42.42           N  
ANISOU 1181  N   LEU A 618     5284   5094   5738   -211    198   -950       N  
ATOM   1182  CA  LEU A 618       2.747 -21.377 -28.725  1.00 40.56           C  
ANISOU 1182  CA  LEU A 618     5064   4674   5674   -138    146   -918       C  
ATOM   1183  C   LEU A 618       1.945 -21.616 -27.445  1.00 39.61           C  
ANISOU 1183  C   LEU A 618     5039   4458   5552   -217     57   -791       C  
ATOM   1184  O   LEU A 618       2.115 -22.639 -26.782  1.00 40.04           O  
ANISOU 1184  O   LEU A 618     5221   4304   5690   -179     16   -768       O  
ATOM   1185  CB  LEU A 618       4.157 -20.903 -28.377  1.00 39.28           C  
ANISOU 1185  CB  LEU A 618     4765   4525   5634     -5    147   -899       C  
ATOM   1186  CG  LEU A 618       5.186 -20.946 -29.504  1.00 42.11           C  
ANISOU 1186  CG  LEU A 618     5022   4918   6061     73    297  -1057       C  
ATOM   1187  CD1 LEU A 618       6.529 -20.446 -29.003  1.00 41.29           C  
ANISOU 1187  CD1 LEU A 618     4714   4832   6143    180    295  -1076       C  
ATOM   1188  CD2 LEU A 618       5.312 -22.356 -30.063  1.00 44.37           C  
ANISOU 1188  CD2 LEU A 618     5391   5046   6423    140    323  -1195       C  
ATOM   1189  N   TRP A 619       1.075 -20.672 -27.106  1.00 37.62           N  
ANISOU 1189  N   TRP A 619     4757   4339   5197   -321     46   -716       N  
ATOM   1190  CA  TRP A 619       0.279 -20.758 -25.887  1.00 36.42           C  
ANISOU 1190  CA  TRP A 619     4697   4110   5032   -418     19   -609       C  
ATOM   1191  C   TRP A 619      -1.174 -21.092 -26.208  1.00 38.10           C  
ANISOU 1191  C   TRP A 619     4915   4340   5221   -592     73   -704       C  
ATOM   1192  O   TRP A 619      -2.027 -21.109 -25.321  1.00 36.65           O  
ANISOU 1192  O   TRP A 619     4780   4110   5037   -718    112   -655       O  
ATOM   1193  CB  TRP A 619       0.360 -19.441 -25.104  1.00 33.51           C  
ANISOU 1193  CB  TRP A 619     4266   3867   4597   -407    -21   -480       C  
ATOM   1194  CG  TRP A 619       1.738 -19.123 -24.590  1.00 33.36           C  
ANISOU 1194  CG  TRP A 619     4215   3823   4639   -258    -98   -416       C  
ATOM   1195  CD1 TRP A 619       2.215 -19.361 -23.336  1.00 33.99           C  
ANISOU 1195  CD1 TRP A 619     4407   3767   4740   -185   -203   -315       C  
ATOM   1196  CD2 TRP A 619       2.814 -18.516 -25.320  1.00 34.94           C  
ANISOU 1196  CD2 TRP A 619     4256   4125   4893   -165    -79   -479       C  
ATOM   1197  NE1 TRP A 619       3.519 -18.945 -23.238  1.00 34.62           N  
ANISOU 1197  NE1 TRP A 619     4361   3878   4915    -37   -295   -335       N  
ATOM   1198  CE2 TRP A 619       3.911 -18.420 -24.442  1.00 34.26           C  
ANISOU 1198  CE2 TRP A 619     4128   3977   4911    -43   -190   -441       C  
ATOM   1199  CE3 TRP A 619       2.955 -18.043 -26.629  1.00 35.82           C  
ANISOU 1199  CE3 TRP A 619     4281   4362   4969   -178     34   -575       C  
ATOM   1200  CZ2 TRP A 619       5.134 -17.872 -24.829  1.00 34.73           C  
ANISOU 1200  CZ2 TRP A 619     3992   4110   5095     40   -172   -526       C  
ATOM   1201  CZ3 TRP A 619       4.173 -17.499 -27.013  1.00 34.35           C  
ANISOU 1201  CZ3 TRP A 619     3963   4224   4866   -109     98   -628       C  
ATOM   1202  CH2 TRP A 619       5.244 -17.419 -26.116  1.00 34.51           C  
ANISOU 1202  CH2 TRP A 619     3874   4194   5044    -14      6   -618       C  
ATOM   1203  N   MET A 620      -1.450 -21.358 -27.481  1.00 40.28           N  
ANISOU 1203  N   MET A 620     5139   4682   5484   -602     79   -866       N  
ATOM   1204  CA  MET A 620      -2.812 -21.641 -27.917  1.00 42.62           C  
ANISOU 1204  CA  MET A 620     5388   5020   5788   -751     83  -1017       C  
ATOM   1205  C   MET A 620      -3.181 -23.104 -27.703  1.00 46.37           C  
ANISOU 1205  C   MET A 620     5977   5261   6382   -876    155  -1104       C  
ATOM   1206  O   MET A 620      -2.486 -24.003 -28.171  1.00 47.66           O  
ANISOU 1206  O   MET A 620     6240   5283   6585   -807    166  -1155       O  
ATOM   1207  CB  MET A 620      -3.001 -21.252 -29.385  1.00 44.53           C  
ANISOU 1207  CB  MET A 620     5566   5427   5927   -690     15  -1171       C  
ATOM   1208  CG  MET A 620      -3.141 -19.756 -29.603  1.00 46.80           C  
ANISOU 1208  CG  MET A 620     5782   5924   6075   -614    -49  -1109       C  
ATOM   1209  SD  MET A 620      -3.292 -19.311 -31.341  1.00 58.25           S  
ANISOU 1209  SD  MET A 620     7288   7517   7329   -506   -138  -1266       S  
ATOM   1210  CE  MET A 620      -4.656 -20.350 -31.827  1.00 60.97           C  
ANISOU 1210  CE  MET A 620     7565   7841   7758   -625   -242  -1532       C  
ATOM   1211  N   ALA A 621      -4.274 -23.332 -26.981  1.00 47.38           N  
ANISOU 1211  N   ALA A 621     6096   5329   6576  -1068    231  -1130       N  
ATOM   1212  CA  ALA A 621      -4.787 -24.678 -26.761  1.00 47.81           C  
ANISOU 1212  CA  ALA A 621     6279   5137   6752  -1243    348  -1229       C  
ATOM   1213  C   ALA A 621      -5.223 -25.269 -28.095  1.00 49.46           C  
ANISOU 1213  C   ALA A 621     6397   5382   7011  -1287    297  -1490       C  
ATOM   1214  O   ALA A 621      -5.598 -24.530 -29.000  1.00 49.13           O  
ANISOU 1214  O   ALA A 621     6180   5581   6906  -1231    172  -1611       O  
ATOM   1215  CB  ALA A 621      -5.950 -24.644 -25.787  1.00 47.30           C  
ANISOU 1215  CB  ALA A 621     6189   5024   6757  -1479    496  -1239       C  
ATOM   1216  N   PRO A 622      -5.167 -26.604 -28.222  1.00 51.82           N  
ANISOU 1216  N   PRO A 622     6858   5425   7406  -1371    377  -1581       N  
ATOM   1217  CA  PRO A 622      -5.586 -27.309 -29.437  1.00 51.16           C  
ANISOU 1217  CA  PRO A 622     6722   5339   7377  -1430    329  -1855       C  
ATOM   1218  C   PRO A 622      -6.962 -26.873 -29.932  1.00 52.92           C  
ANISOU 1218  C   PRO A 622     6679   5769   7657  -1582    257  -2097       C  
ATOM   1219  O   PRO A 622      -7.137 -26.681 -31.135  1.00 54.13           O  
ANISOU 1219  O   PRO A 622     6738   6087   7744  -1499     92  -2285       O  
ATOM   1220  CB  PRO A 622      -5.642 -28.767 -28.983  1.00 51.41           C  
ANISOU 1220  CB  PRO A 622     6986   5005   7542  -1586    488  -1892       C  
ATOM   1221  CG  PRO A 622      -4.617 -28.864 -27.932  1.00 51.24           C  
ANISOU 1221  CG  PRO A 622     7204   4798   7466  -1446    538  -1608       C  
ATOM   1222  CD  PRO A 622      -4.594 -27.528 -27.226  1.00 52.79           C  
ANISOU 1222  CD  PRO A 622     7274   5216   7566  -1382    496  -1424       C  
ATOM   1223  N   GLU A 623      -7.920 -26.716 -29.021  1.00 51.90           N  
ANISOU 1223  N   GLU A 623     6442   5629   7650  -1789    374  -2109       N  
ATOM   1224  CA  GLU A 623      -9.277 -26.345 -29.411  1.00 52.79           C  
ANISOU 1224  CA  GLU A 623     6240   5935   7881  -1930    300  -2388       C  
ATOM   1225  C   GLU A 623      -9.342 -24.914 -29.942  1.00 53.68           C  
ANISOU 1225  C   GLU A 623     6174   6380   7842  -1708     69  -2370       C  
ATOM   1226  O   GLU A 623     -10.203 -24.586 -30.759  1.00 58.34           O  
ANISOU 1226  O   GLU A 623     6543   7159   8465  -1693   -121  -2631       O  
ATOM   1227  CB  GLU A 623     -10.272 -26.554 -28.261  1.00 52.51           C  
ANISOU 1227  CB  GLU A 623     6116   5791   8045  -2226    544  -2432       C  
ATOM   1228  CG  GLU A 623     -10.147 -25.577 -27.099  1.00 52.90           C  
ANISOU 1228  CG  GLU A 623     6184   5905   8012  -2182    640  -2172       C  
ATOM   1229  CD  GLU A 623      -9.269 -26.096 -25.979  1.00 53.79           C  
ANISOU 1229  CD  GLU A 623     6676   5725   8037  -2191    835  -1868       C  
ATOM   1230  OE1 GLU A 623      -8.550 -27.091 -26.200  1.00 53.32           O  
ANISOU 1230  OE1 GLU A 623     6868   5434   7957  -2156    851  -1824       O  
ATOM   1231  OE2 GLU A 623      -9.301 -25.508 -24.875  1.00 54.15           O  
ANISOU 1231  OE2 GLU A 623     6787   5764   8023  -2212    955  -1684       O  
ATOM   1232  N   VAL A 624      -8.419 -24.071 -29.487  1.00 49.56           N  
ANISOU 1232  N   VAL A 624     5766   5912   7153  -1525     70  -2074       N  
ATOM   1233  CA  VAL A 624      -8.348 -22.686 -29.952  1.00 50.88           C  
ANISOU 1233  CA  VAL A 624     5837   6342   7152  -1314   -114  -2021       C  
ATOM   1234  C   VAL A 624      -7.783 -22.610 -31.371  1.00 53.93           C  
ANISOU 1234  C   VAL A 624     6322   6811   7357  -1120   -287  -2096       C  
ATOM   1235  O   VAL A 624      -8.229 -21.812 -32.192  1.00 55.77           O  
ANISOU 1235  O   VAL A 624     6485   7239   7467   -990   -488  -2206       O  
ATOM   1236  CB  VAL A 624      -7.494 -21.810 -28.998  1.00 43.25           C  
ANISOU 1236  CB  VAL A 624     4969   5385   6079  -1208    -38  -1699       C  
ATOM   1237  CG1 VAL A 624      -7.407 -20.380 -29.508  1.00 39.99           C  
ANISOU 1237  CG1 VAL A 624     4497   5205   5493  -1009   -200  -1646       C  
ATOM   1238  CG2 VAL A 624      -8.079 -21.829 -27.590  1.00 42.51           C  
ANISOU 1238  CG2 VAL A 624     4835   5205   6112  -1390    141  -1625       C  
ATOM   1239  N   ILE A 625      -6.805 -23.462 -31.651  1.00 55.04           N  
ANISOU 1239  N   ILE A 625     6659   6785   7471  -1089   -202  -2045       N  
ATOM   1240  CA  ILE A 625      -6.177 -23.526 -32.967  1.00 55.85           C  
ANISOU 1240  CA  ILE A 625     6894   6929   7396   -926   -295  -2125       C  
ATOM   1241  C   ILE A 625      -7.161 -23.965 -34.067  1.00 61.31           C  
ANISOU 1241  C   ILE A 625     7527   7684   8083   -965   -475  -2458       C  
ATOM   1242  O   ILE A 625      -7.153 -23.397 -35.169  1.00 62.10           O  
ANISOU 1242  O   ILE A 625     7708   7926   7962   -799   -644  -2543       O  
ATOM   1243  CB  ILE A 625      -4.960 -24.467 -32.951  1.00 51.71           C  
ANISOU 1243  CB  ILE A 625     6556   6193   6899   -890   -145  -2041       C  
ATOM   1244  CG1 ILE A 625      -3.853 -23.872 -32.090  1.00 43.95           C  
ANISOU 1244  CG1 ILE A 625     5615   5189   5896   -786    -42  -1755       C  
ATOM   1245  CG2 ILE A 625      -4.456 -24.731 -34.357  1.00 52.18           C  
ANISOU 1245  CG2 ILE A 625     6754   6272   6799   -762   -192  -2186       C  
ATOM   1246  CD1 ILE A 625      -2.580 -24.688 -32.054  1.00 43.67           C  
ANISOU 1246  CD1 ILE A 625     5716   4964   5913   -696     66  -1695       C  
ATOM   1247  N   ARG A 626      -8.000 -24.961 -33.768  1.00 65.54           N  
ANISOU 1247  N   ARG A 626     7950   8102   8851  -1186   -437  -2654       N  
ATOM   1248  CA  ARG A 626      -8.928 -25.521 -34.747  1.00 70.48           C  
ANISOU 1248  CA  ARG A 626     8487   8767   9525  -1251   -618  -3019       C  
ATOM   1249  C   ARG A 626      -9.875 -24.488 -35.347  1.00 74.02           C  
ANISOU 1249  C   ARG A 626     8759   9483   9881  -1131   -912  -3189       C  
ATOM   1250  O   ARG A 626     -10.280 -23.541 -34.693  1.00 76.86           O  
ANISOU 1250  O   ARG A 626     8960   9970  10272  -1106   -933  -3088       O  
ATOM   1251  CB  ARG A 626      -9.726 -26.689 -34.143  1.00 72.54           C  
ANISOU 1251  CB  ARG A 626     8619   8838  10105  -1562   -478  -3210       C  
ATOM   1252  CG  ARG A 626      -8.890 -27.874 -33.653  1.00 71.43           C  
ANISOU 1252  CG  ARG A 626     8719   8377  10044  -1662   -224  -3080       C  
ATOM   1253  CD  ARG A 626      -9.695 -28.885 -32.883  1.00 72.37           C  
ANISOU 1253  CD  ARG A 626     8773   8269  10456  -1992    -29  -3215       C  
ATOM   1254  NE  ARG A 626      -8.892 -29.709 -31.969  1.00 71.78           N  
ANISOU 1254  NE  ARG A 626     8979   7868  10426  -2056    231  -2978       N  
ATOM   1255  CZ  ARG A 626      -9.265 -30.093 -30.752  1.00 71.74           C  
ANISOU 1255  CZ  ARG A 626     9024   7658  10574  -2283    476  -2883       C  
ATOM   1256  NH1 ARG A 626     -10.446 -29.766 -30.278  1.00 71.81           N  
ANISOU 1256  NH1 ARG A 626     8783   7799  10701  -2434    533  -2937       N  
ATOM   1257  NH2 ARG A 626      -8.443 -30.811 -30.015  1.00 71.89           N  
ANISOU 1257  NH2 ARG A 626     9373   7368  10574  -2272    653  -2655       N  
ATOM   1258  N   PRO A 632     -14.574 -21.431 -28.211  1.00 58.55           N  
ANISOU 1258  N   PRO A 632     5428   7787   9033  -1868     -1  -2946       N  
ATOM   1259  CA  PRO A 632     -13.170 -21.856 -28.234  1.00 56.91           C  
ANISOU 1259  CA  PRO A 632     5549   7418   8658  -1893     37  -2741       C  
ATOM   1260  C   PRO A 632     -12.379 -21.298 -27.049  1.00 55.00           C  
ANISOU 1260  C   PRO A 632     5522   7096   8279  -1872    227  -2382       C  
ATOM   1261  O   PRO A 632     -11.566 -22.015 -26.468  1.00 53.45           O  
ANISOU 1261  O   PRO A 632     5620   6669   8021  -1949    413  -2168       O  
ATOM   1262  CB  PRO A 632     -12.651 -21.275 -29.551  1.00 55.40           C  
ANISOU 1262  CB  PRO A 632     5418   7392   8240  -1593   -323  -2759       C  
ATOM   1263  CG  PRO A 632     -13.515 -20.088 -29.803  1.00 57.34           C  
ANISOU 1263  CG  PRO A 632     5412   7886   8488  -1412   -547  -2885       C  
ATOM   1264  CD  PRO A 632     -14.877 -20.450 -29.267  1.00 60.69           C  
ANISOU 1264  CD  PRO A 632     5558   8304   9197  -1565   -387  -3066       C  
ATOM   1265  N   TYR A 633     -12.613 -20.036 -26.701  1.00 53.61           N  
ANISOU 1265  N   TYR A 633     5226   7099   8044  -1735    156  -2313       N  
ATOM   1266  CA  TYR A 633     -11.937 -19.424 -25.562  1.00 52.09           C  
ANISOU 1266  CA  TYR A 633     5235   6845   7712  -1698    314  -1989       C  
ATOM   1267  C   TYR A 633     -12.710 -19.650 -24.273  1.00 54.74           C  
ANISOU 1267  C   TYR A 633     5511   7073   8214  -1964    642  -2027       C  
ATOM   1268  O   TYR A 633     -13.877 -19.279 -24.165  1.00 57.98           O  
ANISOU 1268  O   TYR A 633     5595   7613   8822  -2051    681  -2279       O  
ATOM   1269  CB  TYR A 633     -11.731 -17.928 -25.790  1.00 50.21           C  
ANISOU 1269  CB  TYR A 633     4951   6817   7308  -1426    102  -1884       C  
ATOM   1270  CG  TYR A 633     -10.680 -17.621 -26.825  1.00 49.03           C  
ANISOU 1270  CG  TYR A 633     4986   6714   6931  -1185   -119  -1755       C  
ATOM   1271  CD1 TYR A 633      -9.332 -17.726 -26.520  1.00 46.30           C  
ANISOU 1271  CD1 TYR A 633     4916   6244   6432  -1129    -47  -1475       C  
ATOM   1272  CD2 TYR A 633     -11.033 -17.227 -28.106  1.00 51.34           C  
ANISOU 1272  CD2 TYR A 633     5185   7164   7159  -1011   -396  -1932       C  
ATOM   1273  CE1 TYR A 633      -8.365 -17.447 -27.460  1.00 46.54           C  
ANISOU 1273  CE1 TYR A 633     5089   6310   6284   -941   -186  -1388       C  
ATOM   1274  CE2 TYR A 633     -10.073 -16.945 -29.057  1.00 50.84           C  
ANISOU 1274  CE2 TYR A 633     5341   7116   6859   -815   -536  -1815       C  
ATOM   1275  CZ  TYR A 633      -8.738 -17.056 -28.728  1.00 49.38           C  
ANISOU 1275  CZ  TYR A 633     5394   6810   6558   -798   -401  -1548       C  
ATOM   1276  OH  TYR A 633      -7.771 -16.779 -29.667  1.00 49.06           O  
ANISOU 1276  OH  TYR A 633     5547   6780   6313   -634   -479  -1461       O  
ATOM   1277  N   SER A 634     -12.049 -20.255 -23.295  1.00 51.92           N  
ANISOU 1277  N   SER A 634     5486   6470   7772  -2079    880  -1791       N  
ATOM   1278  CA  SER A 634     -12.692 -20.585 -22.032  1.00 51.66           C  
ANISOU 1278  CA  SER A 634     5516   6274   7837  -2351   1247  -1797       C  
ATOM   1279  C   SER A 634     -11.673 -20.500 -20.907  1.00 46.78           C  
ANISOU 1279  C   SER A 634     5329   5472   6973  -2292   1357  -1433       C  
ATOM   1280  O   SER A 634     -10.524 -20.133 -21.136  1.00 42.87           O  
ANISOU 1280  O   SER A 634     4996   5008   6287  -2045   1134  -1217       O  
ATOM   1281  CB  SER A 634     -13.282 -21.995 -22.099  1.00 56.52           C  
ANISOU 1281  CB  SER A 634     6168   6682   8626  -2604   1460  -1968       C  
ATOM   1282  OG  SER A 634     -12.256 -22.973 -22.182  1.00 57.35           O  
ANISOU 1282  OG  SER A 634     6633   6525   8634  -2634   1473  -1809       O  
ATOM   1283  N   PHE A 635     -12.092 -20.838 -19.693  1.00 47.68           N  
ANISOU 1283  N   PHE A 635     5637   5390   7090  -2520   1704  -1385       N  
ATOM   1284  CA  PHE A 635     -11.162 -20.886 -18.576  1.00 49.29           C  
ANISOU 1284  CA  PHE A 635     6314   5382   7032  -2457   1784  -1056       C  
ATOM   1285  C   PHE A 635     -10.129 -21.977 -18.807  1.00 48.30           C  
ANISOU 1285  C   PHE A 635     6528   5013   6812  -2386   1691   -906       C  
ATOM   1286  O   PHE A 635      -8.977 -21.849 -18.400  1.00 44.43           O  
ANISOU 1286  O   PHE A 635     6329   4441   6111  -2175   1536   -653       O  
ATOM   1287  CB  PHE A 635     -11.900 -21.138 -17.263  1.00 57.09           C  
ANISOU 1287  CB  PHE A 635     7516   6169   8005  -2727   2208  -1049       C  
ATOM   1288  CG  PHE A 635     -12.947 -20.115 -16.955  1.00 60.93           C  
ANISOU 1288  CG  PHE A 635     7667   6896   8588  -2739   2303  -1214       C  
ATOM   1289  CD1 PHE A 635     -12.591 -18.838 -16.563  1.00 58.92           C  
ANISOU 1289  CD1 PHE A 635     7389   6797   8201  -2588   2195  -1090       C  
ATOM   1290  CD2 PHE A 635     -14.289 -20.431 -17.057  1.00 66.99           C  
ANISOU 1290  CD2 PHE A 635     8148   7727   9579  -2868   2481  -1505       C  
ATOM   1291  CE1 PHE A 635     -13.552 -17.894 -16.277  1.00 62.56           C  
ANISOU 1291  CE1 PHE A 635     7549   7452   8769  -2602   2296  -1259       C  
ATOM   1292  CE2 PHE A 635     -15.258 -19.493 -16.772  1.00 69.50           C  
ANISOU 1292  CE2 PHE A 635     8157   8242  10009  -2854   2556  -1682       C  
ATOM   1293  CZ  PHE A 635     -14.889 -18.222 -16.381  1.00 67.06           C  
ANISOU 1293  CZ  PHE A 635     7833   8072   9574  -2712   2461  -1556       C  
ATOM   1294  N   GLN A 636     -10.555 -23.049 -19.466  1.00 52.04           N  
ANISOU 1294  N   GLN A 636     6942   5369   7462  -2556   1774  -1093       N  
ATOM   1295  CA  GLN A 636      -9.685 -24.184 -19.740  1.00 55.05           C  
ANISOU 1295  CA  GLN A 636     7638   5493   7786  -2498   1709   -992       C  
ATOM   1296  C   GLN A 636      -8.534 -23.823 -20.673  1.00 51.33           C  
ANISOU 1296  C   GLN A 636     7084   5187   7232  -2163   1331   -910       C  
ATOM   1297  O   GLN A 636      -7.411 -24.290 -20.484  1.00 50.88           O  
ANISOU 1297  O   GLN A 636     7330   4953   7048  -1992   1224   -723       O  
ATOM   1298  CB  GLN A 636     -10.485 -25.350 -20.323  1.00 63.34           C  
ANISOU 1298  CB  GLN A 636     8608   6391   9068  -2773   1887  -1253       C  
ATOM   1299  CG  GLN A 636     -11.493 -25.960 -19.357  1.00 72.64           C  
ANISOU 1299  CG  GLN A 636     9916   7426  10259  -2977   2244  -1283       C  
ATOM   1300  CD  GLN A 636     -12.770 -25.151 -19.248  1.00 79.12           C  
ANISOU 1300  CD  GLN A 636    10310   8526  11226  -3066   2353  -1500       C  
ATOM   1301  OE1 GLN A 636     -13.403 -24.828 -20.254  1.00 81.56           O  
ANISOU 1301  OE1 GLN A 636    10162   9092  11735  -3048   2193  -1762       O  
ATOM   1302  NE2 GLN A 636     -13.155 -24.816 -18.023  1.00 81.78           N  
ANISOU 1302  NE2 GLN A 636    10817   8805  11450  -3133   2606  -1405       N  
ATOM   1303  N   SER A 637      -8.806 -22.993 -21.678  1.00 48.64           N  
ANISOU 1303  N   SER A 637     6350   5170   6964  -2063   1136  -1063       N  
ATOM   1304  CA  SER A 637      -7.752 -22.564 -22.594  1.00 44.48           C  
ANISOU 1304  CA  SER A 637     5764   4793   6345  -1776    841   -996       C  
ATOM   1305  C   SER A 637      -6.762 -21.614 -21.915  1.00 42.58           C  
ANISOU 1305  C   SER A 637     5645   4611   5923  -1564    730   -742       C  
ATOM   1306  O   SER A 637      -5.578 -21.599 -22.254  1.00 42.31           O  
ANISOU 1306  O   SER A 637     5691   4570   5815  -1356    565   -636       O  
ATOM   1307  CB  SER A 637      -8.326 -21.962 -23.879  1.00 41.79           C  
ANISOU 1307  CB  SER A 637     5060   4739   6079  -1720    669  -1221       C  
ATOM   1308  OG  SER A 637      -9.245 -20.922 -23.622  1.00 43.50           O  
ANISOU 1308  OG  SER A 637     5035   5161   6334  -1756    680  -1302       O  
ATOM   1309  N   ASP A 638      -7.242 -20.837 -20.947  1.00 42.42           N  
ANISOU 1309  N   ASP A 638     5626   4642   5851  -1624    832   -673       N  
ATOM   1310  CA  ASP A 638      -6.348 -20.035 -20.115  1.00 42.64           C  
ANISOU 1310  CA  ASP A 638     5813   4681   5706  -1455    741   -447       C  
ATOM   1311  C   ASP A 638      -5.417 -20.943 -19.313  1.00 42.67           C  
ANISOU 1311  C   ASP A 638     6218   4387   5606  -1396    743   -269       C  
ATOM   1312  O   ASP A 638      -4.229 -20.661 -19.166  1.00 41.69           O  
ANISOU 1312  O   ASP A 638     6184   4262   5395  -1177    547   -137       O  
ATOM   1313  CB  ASP A 638      -7.142 -19.144 -19.159  1.00 45.54           C  
ANISOU 1313  CB  ASP A 638     6150   5125   6029  -1552    882   -429       C  
ATOM   1314  CG  ASP A 638      -7.510 -17.808 -19.769  1.00 46.25           C  
ANISOU 1314  CG  ASP A 638     5907   5519   6148  -1454    755   -517       C  
ATOM   1315  OD1 ASP A 638      -7.075 -17.523 -20.905  1.00 44.46           O  
ANISOU 1315  OD1 ASP A 638     5523   5432   5936  -1308    558   -564       O  
ATOM   1316  OD2 ASP A 638      -8.226 -17.035 -19.098  1.00 47.66           O  
ANISOU 1316  OD2 ASP A 638     6016   5775   6317  -1515    864   -539       O  
ATOM   1317  N   VAL A 639      -5.974 -22.032 -18.793  1.00 42.69           N  
ANISOU 1317  N   VAL A 639     6468   4124   5629  -1591    965   -284       N  
ATOM   1318  CA  VAL A 639      -5.208 -23.007 -18.024  1.00 43.37           C  
ANISOU 1318  CA  VAL A 639     7015   3871   5594  -1524    966   -118       C  
ATOM   1319  C   VAL A 639      -4.099 -23.633 -18.862  1.00 43.44           C  
ANISOU 1319  C   VAL A 639     7020   3828   5656  -1307    737   -122       C  
ATOM   1320  O   VAL A 639      -2.965 -23.778 -18.400  1.00 45.42           O  
ANISOU 1320  O   VAL A 639     7492   3956   5809  -1074    550     20       O  
ATOM   1321  CB  VAL A 639      -6.121 -24.114 -17.467  1.00 47.01           C  
ANISOU 1321  CB  VAL A 639     7769   4019   6072  -1813   1300   -155       C  
ATOM   1322  CG1 VAL A 639      -5.298 -25.286 -16.944  1.00 47.34           C  
ANISOU 1322  CG1 VAL A 639     8330   3668   5990  -1706   1264      3       C  
ATOM   1323  CG2 VAL A 639      -7.027 -23.550 -16.382  1.00 49.54           C  
ANISOU 1323  CG2 VAL A 639     8185   4332   6305  -2012   1571   -125       C  
ATOM   1324  N   TYR A 640      -4.431 -23.998 -20.095  1.00 40.72           N  
ANISOU 1324  N   TYR A 640     6417   3580   5476  -1370    742   -311       N  
ATOM   1325  CA  TYR A 640      -3.445 -24.537 -21.017  1.00 40.65           C  
ANISOU 1325  CA  TYR A 640     6371   3548   5528  -1176    565   -352       C  
ATOM   1326  C   TYR A 640      -2.313 -23.541 -21.259  1.00 40.16           C  
ANISOU 1326  C   TYR A 640     6134   3701   5423   -912    331   -283       C  
ATOM   1327  O   TYR A 640      -1.145 -23.920 -21.282  1.00 42.90           O  
ANISOU 1327  O   TYR A 640     6574   3947   5778   -695    179   -234       O  
ATOM   1328  CB  TYR A 640      -4.105 -24.905 -22.347  1.00 42.02           C  
ANISOU 1328  CB  TYR A 640     6288   3829   5850  -1298    608   -590       C  
ATOM   1329  CG  TYR A 640      -3.141 -25.499 -23.348  1.00 43.09           C  
ANISOU 1329  CG  TYR A 640     6406   3931   6037  -1113    470   -656       C  
ATOM   1330  CD1 TYR A 640      -2.369 -24.683 -24.171  1.00 36.67           C  
ANISOU 1330  CD1 TYR A 640     5361   3365   5207   -919    312   -678       C  
ATOM   1331  CD2 TYR A 640      -2.995 -26.879 -23.468  1.00 45.30           C  
ANISOU 1331  CD2 TYR A 640     6924   3909   6381  -1141    530   -706       C  
ATOM   1332  CE1 TYR A 640      -1.480 -25.221 -25.082  1.00 40.08           C  
ANISOU 1332  CE1 TYR A 640     5775   3763   5691   -762    236   -760       C  
ATOM   1333  CE2 TYR A 640      -2.108 -27.426 -24.382  1.00 43.57           C  
ANISOU 1333  CE2 TYR A 640     6683   3654   6218   -959    419   -787       C  
ATOM   1334  CZ  TYR A 640      -1.356 -26.592 -25.184  1.00 42.13           C  
ANISOU 1334  CZ  TYR A 640     6245   3740   6024   -773    283   -820       C  
ATOM   1335  OH  TYR A 640      -0.473 -27.125 -26.088  1.00 42.24           O  
ANISOU 1335  OH  TYR A 640     6234   3717   6098   -605    223   -922       O  
ATOM   1336  N   ALA A 641      -2.670 -22.276 -21.462  1.00 35.44           N  
ANISOU 1336  N   ALA A 641     5275   3390   4802   -932    310   -303       N  
ATOM   1337  CA  ALA A 641      -1.685 -21.226 -21.707  1.00 35.38           C  
ANISOU 1337  CA  ALA A 641     5102   3577   4764   -734    140   -253       C  
ATOM   1338  C   ALA A 641      -0.776 -21.064 -20.499  1.00 36.56           C  
ANISOU 1338  C   ALA A 641     5455   3606   4829   -587     23    -87       C  
ATOM   1339  O   ALA A 641       0.411 -20.757 -20.628  1.00 36.66           O  
ANISOU 1339  O   ALA A 641     5386   3666   4876   -391   -142    -73       O  
ATOM   1340  CB  ALA A 641      -2.379 -19.914 -22.023  1.00 33.28           C  
ANISOU 1340  CB  ALA A 641     4594   3584   4466   -796    158   -292       C  
ATOM   1341  N   PHE A 642      -1.355 -21.259 -19.322  1.00 37.42           N  
ANISOU 1341  N   PHE A 642     5831   3557   4829   -688    114     16       N  
ATOM   1342  CA  PHE A 642      -0.605 -21.232 -18.082  1.00 40.25           C  
ANISOU 1342  CA  PHE A 642     6477   3758   5057   -541    -19    170       C  
ATOM   1343  C   PHE A 642       0.318 -22.446 -17.995  1.00 42.42           C  
ANISOU 1343  C   PHE A 642     6996   3764   5358   -359   -156    195       C  
ATOM   1344  O   PHE A 642       1.405 -22.372 -17.425  1.00 43.73           O  
ANISOU 1344  O   PHE A 642     7263   3865   5488   -119   -396    256       O  
ATOM   1345  CB  PHE A 642      -1.565 -21.195 -16.894  1.00 43.90           C  
ANISOU 1345  CB  PHE A 642     7233   4091   5355   -716    166    267       C  
ATOM   1346  CG  PHE A 642      -0.880 -21.218 -15.565  1.00 45.38           C  
ANISOU 1346  CG  PHE A 642     7812   4085   5344   -560     20    430       C  
ATOM   1347  CD1 PHE A 642      -0.286 -20.077 -15.058  1.00 41.09           C  
ANISOU 1347  CD1 PHE A 642     7181   3702   4728   -425   -165    475       C  
ATOM   1348  CD2 PHE A 642      -0.829 -22.386 -14.820  1.00 48.52           C  
ANISOU 1348  CD2 PHE A 642     8702   4120   5612   -539     55    529       C  
ATOM   1349  CE1 PHE A 642       0.349 -20.097 -13.834  1.00 41.52           C  
ANISOU 1349  CE1 PHE A 642     7608   3582   4584   -261   -348    599       C  
ATOM   1350  CE2 PHE A 642      -0.199 -22.414 -13.597  1.00 48.93           C  
ANISOU 1350  CE2 PHE A 642     9176   3977   5438   -357   -124    676       C  
ATOM   1351  CZ  PHE A 642       0.391 -21.264 -13.100  1.00 45.76           C  
ANISOU 1351  CZ  PHE A 642     8659   3763   4965   -212   -343    703       C  
ATOM   1352  N   GLY A 643      -0.122 -23.563 -18.564  1.00 43.69           N  
ANISOU 1352  N   GLY A 643     7243   3764   5595   -459    -21    123       N  
ATOM   1353  CA  GLY A 643       0.698 -24.761 -18.623  1.00 44.90           C  
ANISOU 1353  CA  GLY A 643     7622   3646   5792   -275   -141    124       C  
ATOM   1354  C   GLY A 643       1.955 -24.547 -19.447  1.00 43.07           C  
ANISOU 1354  C   GLY A 643     7081   3565   5717    -23   -357     22       C  
ATOM   1355  O   GLY A 643       3.029 -25.030 -19.097  1.00 41.30           O  
ANISOU 1355  O   GLY A 643     6986   3184   5524    244   -576     39       O  
ATOM   1356  N   ILE A 644       1.816 -23.815 -20.547  1.00 39.31           N  
ANISOU 1356  N   ILE A 644     6209   3386   5343   -101   -290   -100       N  
ATOM   1357  CA  ILE A 644       2.951 -23.473 -21.398  1.00 39.73           C  
ANISOU 1357  CA  ILE A 644     5956   3599   5541     85   -409   -213       C  
ATOM   1358  C   ILE A 644       3.899 -22.517 -20.671  1.00 40.67           C  
ANISOU 1358  C   ILE A 644     5973   3822   5659    253   -606   -160       C  
ATOM   1359  O   ILE A 644       5.122 -22.616 -20.802  1.00 41.25           O  
ANISOU 1359  O   ILE A 644     5910   3889   5874    476   -770   -243       O  
ATOM   1360  CB  ILE A 644       2.488 -22.840 -22.725  1.00 39.03           C  
ANISOU 1360  CB  ILE A 644     5559   3776   5495    -54   -263   -338       C  
ATOM   1361  CG1 ILE A 644       1.635 -23.831 -23.524  1.00 40.48           C  
ANISOU 1361  CG1 ILE A 644     5815   3863   5703   -199   -118   -442       C  
ATOM   1362  CG2 ILE A 644       3.681 -22.388 -23.553  1.00 38.14           C  
ANISOU 1362  CG2 ILE A 644     5172   3812   5509    104   -317   -450       C  
ATOM   1363  CD1 ILE A 644       2.426 -24.967 -24.144  1.00 37.36           C  
ANISOU 1363  CD1 ILE A 644     5469   3296   5428    -49   -150   -552       C  
ATOM   1364  N   VAL A 645       3.330 -21.593 -19.903  1.00 39.44           N  
ANISOU 1364  N   VAL A 645     5862   3760   5363    142   -588    -51       N  
ATOM   1365  CA  VAL A 645       4.134 -20.693 -19.083  1.00 39.84           C  
ANISOU 1365  CA  VAL A 645     5859   3886   5394    280   -785     -7       C  
ATOM   1366  C   VAL A 645       4.899 -21.483 -18.025  1.00 45.26           C  
ANISOU 1366  C   VAL A 645     6846   4310   6041    519  -1039     51       C  
ATOM   1367  O   VAL A 645       6.082 -21.232 -17.794  1.00 48.44           O  
ANISOU 1367  O   VAL A 645     7105   4742   6557    745  -1286    -23       O  
ATOM   1368  CB  VAL A 645       3.276 -19.601 -18.409  1.00 39.10           C  
ANISOU 1368  CB  VAL A 645     5807   3915   5134    114   -703     96       C  
ATOM   1369  CG1 VAL A 645       4.089 -18.869 -17.346  1.00 39.90           C  
ANISOU 1369  CG1 VAL A 645     5950   4028   5184    264   -938    142       C  
ATOM   1370  CG2 VAL A 645       2.738 -18.630 -19.443  1.00 31.08           C  
ANISOU 1370  CG2 VAL A 645     4481   3165   4164    -43   -535     25       C  
ATOM   1371  N   LEU A 646       4.223 -22.440 -17.392  1.00 44.24           N  
ANISOU 1371  N   LEU A 646     7145   3909   5753    474   -979    166       N  
ATOM   1372  CA  LEU A 646       4.886 -23.355 -16.466  1.00 49.24           C  
ANISOU 1372  CA  LEU A 646     8173   4230   6307    728  -1224    234       C  
ATOM   1373  C   LEU A 646       6.040 -24.075 -17.152  1.00 50.78           C  
ANISOU 1373  C   LEU A 646     8188   4366   6740    995  -1410     81       C  
ATOM   1374  O   LEU A 646       7.116 -24.240 -16.576  1.00 50.90           O  
ANISOU 1374  O   LEU A 646     8254   4284   6803   1307  -1743     44       O  
ATOM   1375  CB  LEU A 646       3.902 -24.394 -15.925  1.00 53.04           C  
ANISOU 1375  CB  LEU A 646     9177   4385   6589    589  -1037    370       C  
ATOM   1376  CG  LEU A 646       2.784 -23.924 -14.995  1.00 53.10           C  
ANISOU 1376  CG  LEU A 646     9468   4362   6346    345   -829    516       C  
ATOM   1377  CD1 LEU A 646       1.882 -25.096 -14.619  1.00 55.85           C  
ANISOU 1377  CD1 LEU A 646    10313   4355   6552    174   -576    609       C  
ATOM   1378  CD2 LEU A 646       3.358 -23.256 -13.756  1.00 49.16           C  
ANISOU 1378  CD2 LEU A 646     9184   3841   5652    531  -1092    614       C  
ATOM   1379  N   TYR A 647       5.801 -24.508 -18.386  1.00 52.58           N  
ANISOU 1379  N   TYR A 647     8203   4653   7122    884  -1204    -32       N  
ATOM   1380  CA  TYR A 647       6.816 -25.199 -19.171  1.00 55.77           C  
ANISOU 1380  CA  TYR A 647     8413   5010   7765   1110  -1311   -204       C  
ATOM   1381  C   TYR A 647       8.019 -24.297 -19.388  1.00 55.07           C  
ANISOU 1381  C   TYR A 647     7875   5166   7885   1280  -1484   -357       C  
ATOM   1382  O   TYR A 647       9.157 -24.727 -19.231  1.00 56.80           O  
ANISOU 1382  O   TYR A 647     8012   5293   8277   1587  -1740   -479       O  
ATOM   1383  CB  TYR A 647       6.242 -25.641 -20.520  1.00 54.73           C  
ANISOU 1383  CB  TYR A 647     8131   4939   7726    919  -1025   -310       C  
ATOM   1384  CG  TYR A 647       7.228 -26.373 -21.405  1.00 55.90           C  
ANISOU 1384  CG  TYR A 647     8092   5035   8112   1134  -1079   -506       C  
ATOM   1385  CD1 TYR A 647       7.442 -27.738 -21.257  1.00 58.50           C  
ANISOU 1385  CD1 TYR A 647     8732   5025   8468   1311  -1165   -517       C  
ATOM   1386  CD2 TYR A 647       7.941 -25.704 -22.393  1.00 54.79           C  
ANISOU 1386  CD2 TYR A 647     7490   5163   8165   1156  -1013   -687       C  
ATOM   1387  CE1 TYR A 647       8.340 -28.415 -22.061  1.00 59.29           C  
ANISOU 1387  CE1 TYR A 647     8653   5072   8800   1526  -1207   -717       C  
ATOM   1388  CE2 TYR A 647       8.842 -26.376 -23.202  1.00 56.74           C  
ANISOU 1388  CE2 TYR A 647     7558   5361   8638   1345  -1017   -891       C  
ATOM   1389  CZ  TYR A 647       9.036 -27.730 -23.031  1.00 58.27           C  
ANISOU 1389  CZ  TYR A 647     8032   5235   8873   1539  -1124   -912       C  
ATOM   1390  OH  TYR A 647       9.930 -28.405 -23.831  1.00 59.30           O  
ANISOU 1390  OH  TYR A 647     7977   5311   9243   1744  -1122  -1136       O  
ATOM   1391  N   GLU A 648       7.757 -23.046 -19.750  1.00 52.59           N  
ANISOU 1391  N   GLU A 648     7265   5147   7570   1079  -1337   -370       N  
ATOM   1392  CA  GLU A 648       8.819 -22.067 -19.926  1.00 55.14           C  
ANISOU 1392  CA  GLU A 648     7169   5691   8090   1170  -1439   -518       C  
ATOM   1393  C   GLU A 648       9.652 -21.906 -18.666  1.00 57.40           C  
ANISOU 1393  C   GLU A 648     7530   5894   8387   1424  -1818   -517       C  
ATOM   1394  O   GLU A 648      10.878 -21.906 -18.725  1.00 58.32           O  
ANISOU 1394  O   GLU A 648     7355   6043   8762   1654  -2023   -715       O  
ATOM   1395  CB  GLU A 648       8.238 -20.714 -20.322  1.00 53.83           C  
ANISOU 1395  CB  GLU A 648     6805   5796   7853    900  -1221   -483       C  
ATOM   1396  CG  GLU A 648       7.649 -20.682 -21.710  1.00 54.54           C  
ANISOU 1396  CG  GLU A 648     6763   6007   7954    703   -907   -538       C  
ATOM   1397  CD  GLU A 648       7.120 -19.318 -22.066  1.00 54.94           C  
ANISOU 1397  CD  GLU A 648     6669   6292   7914    489   -738   -500       C  
ATOM   1398  OE1 GLU A 648       7.941 -18.424 -22.355  1.00 57.39           O  
ANISOU 1398  OE1 GLU A 648     6701   6747   8357    498   -717   -603       O  
ATOM   1399  OE2 GLU A 648       5.887 -19.134 -22.042  1.00 53.45           O  
ANISOU 1399  OE2 GLU A 648     6644   6129   7537    314   -622   -382       O  
ATOM   1400  N   LEU A 649       8.978 -21.766 -17.529  1.00 59.31           N  
ANISOU 1400  N   LEU A 649     8158   6027   8349   1384  -1909   -319       N  
ATOM   1401  CA  LEU A 649       9.656 -21.573 -16.253  1.00 63.44           C  
ANISOU 1401  CA  LEU A 649     8840   6458   8807   1627  -2295   -304       C  
ATOM   1402  C   LEU A 649      10.579 -22.738 -15.910  1.00 71.67           C  
ANISOU 1402  C   LEU A 649    10038   7243   9950   2011  -2637   -388       C  
ATOM   1403  O   LEU A 649      11.728 -22.529 -15.531  1.00 75.67           O  
ANISOU 1403  O   LEU A 649    10326   7783  10642   2287  -2989   -560       O  
ATOM   1404  CB  LEU A 649       8.642 -21.369 -15.125  1.00 61.79           C  
ANISOU 1404  CB  LEU A 649     9123   6132   8223   1502  -2272    -61       C  
ATOM   1405  CG  LEU A 649       7.830 -20.072 -15.110  1.00 58.81           C  
ANISOU 1405  CG  LEU A 649     8620   5992   7733   1199  -2037     10       C  
ATOM   1406  CD1 LEU A 649       6.684 -20.182 -14.117  1.00 59.93           C  
ANISOU 1406  CD1 LEU A 649     9279   5972   7519   1061  -1924    231       C  
ATOM   1407  CD2 LEU A 649       8.718 -18.887 -14.772  1.00 57.22           C  
ANISOU 1407  CD2 LEU A 649     8103   5988   7652   1279  -2255   -115       C  
ATOM   1408  N   MET A 650      10.080 -23.962 -16.048  1.00 73.42           N  
ANISOU 1408  N   MET A 650    10631   7197  10067   2037  -2545   -290       N  
ATOM   1409  CA  MET A 650      10.858 -25.136 -15.662  1.00 80.80           C  
ANISOU 1409  CA  MET A 650    11816   7829  11055   2428  -2877   -343       C  
ATOM   1410  C   MET A 650      11.868 -25.567 -16.725  1.00 84.04           C  
ANISOU 1410  C   MET A 650    11750   8311  11869   2615  -2910   -622       C  
ATOM   1411  O   MET A 650      12.956 -26.039 -16.401  1.00 89.17           O  
ANISOU 1411  O   MET A 650    12335   8858  12689   2992  -3277   -780       O  
ATOM   1412  CB  MET A 650       9.937 -26.302 -15.290  1.00 83.51           C  
ANISOU 1412  CB  MET A 650    12823   7797  11111   2380  -2754   -122       C  
ATOM   1413  CG  MET A 650       9.022 -26.000 -14.106  1.00 84.22           C  
ANISOU 1413  CG  MET A 650    13448   7760  10794   2225  -2709    136       C  
ATOM   1414  SD  MET A 650       9.919 -25.246 -12.733  1.00 83.69           S  
ANISOU 1414  SD  MET A 650    13445   7768  10585   2489  -3175    112       S  
ATOM   1415  CE  MET A 650       8.784 -25.531 -11.373  1.00116.50           C  
ANISOU 1415  CE  MET A 650    18387  11685  14193   2292  -2995    402       C  
ATOM   1416  N   THR A 651      11.508 -25.402 -17.991  1.00 81.73           N  
ANISOU 1416  N   THR A 651    11131   8208  11715   2347  -2518   -697       N  
ATOM   1417  CA  THR A 651      12.383 -25.804 -19.084  1.00 84.63           C  
ANISOU 1417  CA  THR A 651    11074   8642  12438   2481  -2462   -966       C  
ATOM   1418  C   THR A 651      13.408 -24.720 -19.415  1.00 82.70           C  
ANISOU 1418  C   THR A 651    10210   8710  12504   2505  -2502  -1214       C  
ATOM   1419  O   THR A 651      14.568 -25.014 -19.701  1.00 85.82           O  
ANISOU 1419  O   THR A 651    10255   9114  13238   2772  -2660  -1486       O  
ATOM   1420  CB  THR A 651      11.564 -26.169 -20.344  1.00 86.31           C  
ANISOU 1420  CB  THR A 651    11268   8894  12631   2194  -2023   -956       C  
ATOM   1421  OG1 THR A 651      10.736 -27.308 -20.064  1.00 88.03           O  
ANISOU 1421  OG1 THR A 651    12027   8787  12632   2178  -1987   -784       O  
ATOM   1422  CG2 THR A 651      12.479 -26.481 -21.521  1.00 90.79           C  
ANISOU 1422  CG2 THR A 651    11405   9547  13543   2310  -1914  -1248       C  
ATOM   1423  N   GLY A 652      12.978 -23.466 -19.357  1.00 78.76           N  
ANISOU 1423  N   GLY A 652     9572   8450  11903   2222  -2345  -1137       N  
ATOM   1424  CA  GLY A 652      13.843 -22.355 -19.706  1.00 76.94           C  
ANISOU 1424  CA  GLY A 652     8789   8494  11949   2171  -2308  -1361       C  
ATOM   1425  C   GLY A 652      13.725 -22.047 -21.182  1.00 74.68           C  
ANISOU 1425  C   GLY A 652     8200   8391  11786   1914  -1847  -1466       C  
ATOM   1426  O   GLY A 652      14.304 -21.082 -21.683  1.00 73.46           O  
ANISOU 1426  O   GLY A 652     7630   8451  11831   1789  -1685  -1634       O  
ATOM   1427  N   GLN A 653      12.952 -22.874 -21.878  1.00 73.66           N  
ANISOU 1427  N   GLN A 653     8318   8153  11517   1826  -1628  -1370       N  
ATOM   1428  CA  GLN A 653      12.830 -22.779 -23.323  1.00 72.22           C  
ANISOU 1428  CA  GLN A 653     7935   8102  11405   1630  -1224  -1479       C  
ATOM   1429  C   GLN A 653      11.383 -22.590 -23.740  1.00 65.75           C  
ANISOU 1429  C   GLN A 653     7407   7318  10258   1327   -973  -1257       C  
ATOM   1430  O   GLN A 653      10.471 -22.752 -22.934  1.00 62.91           O  
ANISOU 1430  O   GLN A 653     7395   6851   9656   1274  -1079  -1038       O  
ATOM   1431  CB  GLN A 653      13.353 -24.056 -23.971  1.00 76.84           C  
ANISOU 1431  CB  GLN A 653     8495   8525  12177   1839  -1207  -1655       C  
ATOM   1432  CG  GLN A 653      14.768 -24.430 -23.578  1.00 84.32           C  
ANISOU 1432  CG  GLN A 653     9140   9410  13487   2199  -1494  -1914       C  
ATOM   1433  CD  GLN A 653      15.217 -25.707 -24.255  1.00 91.58           C  
ANISOU 1433  CD  GLN A 653    10053  10156  14589   2418  -1458  -2094       C  
ATOM   1434  OE1 GLN A 653      15.126 -25.840 -25.476  1.00 92.94           O  
ANISOU 1434  OE1 GLN A 653    10116  10396  14800   2268  -1093  -2202       O  
ATOM   1435  NE2 GLN A 653      15.685 -26.664 -23.463  1.00 94.84           N  
ANISOU 1435  NE2 GLN A 653    10628  10319  15087   2789  -1846  -2125       N  
ATOM   1436  N   LEU A 654      11.180 -22.255 -25.009  1.00 63.46           N  
ANISOU 1436  N   LEU A 654     6979   7170   9962   1137   -637  -1335       N  
ATOM   1437  CA  LEU A 654       9.846 -22.243 -25.588  1.00 59.46           C  
ANISOU 1437  CA  LEU A 654     6720   6691   9181    900   -436  -1189       C  
ATOM   1438  C   LEU A 654       9.526 -23.647 -26.081  1.00 58.31           C  
ANISOU 1438  C   LEU A 654     6780   6350   9026    967   -403  -1232       C  
ATOM   1439  O   LEU A 654      10.433 -24.425 -26.379  1.00 60.10           O  
ANISOU 1439  O   LEU A 654     6896   6471   9466   1170   -435  -1409       O  
ATOM   1440  CB  LEU A 654       9.767 -21.240 -26.740  1.00 59.73           C  
ANISOU 1440  CB  LEU A 654     6586   6941   9168    698   -130  -1255       C  
ATOM   1441  CG  LEU A 654       9.773 -19.757 -26.364  1.00 59.53           C  
ANISOU 1441  CG  LEU A 654     6442   7088   9089    566   -107  -1178       C  
ATOM   1442  CD1 LEU A 654       9.939 -18.907 -27.613  1.00 59.17           C  
ANISOU 1442  CD1 LEU A 654     6276   7192   9013    407    220  -1271       C  
ATOM   1443  CD2 LEU A 654       8.498 -19.375 -25.614  1.00 55.68           C  
ANISOU 1443  CD2 LEU A 654     6209   6607   8340    445   -207   -942       C  
ATOM   1444  N   PRO A 655       8.233 -23.985 -26.150  1.00 55.59           N  
ANISOU 1444  N   PRO A 655     6719   5946   8458    796   -340  -1097       N  
ATOM   1445  CA  PRO A 655       7.850 -25.322 -26.612  1.00 55.20           C  
ANISOU 1445  CA  PRO A 655     6881   5691   8401    822   -297  -1151       C  
ATOM   1446  C   PRO A 655       8.217 -25.531 -28.071  1.00 54.75           C  
ANISOU 1446  C   PRO A 655     6674   5710   8420    813    -77  -1361       C  
ATOM   1447  O   PRO A 655       8.299 -24.562 -28.827  1.00 54.66           O  
ANISOU 1447  O   PRO A 655     6487   5918   8362    699     96  -1411       O  
ATOM   1448  CB  PRO A 655       6.327 -25.320 -26.467  1.00 53.63           C  
ANISOU 1448  CB  PRO A 655     6924   5481   7973    573   -232  -1004       C  
ATOM   1449  CG  PRO A 655       6.032 -24.245 -25.486  1.00 53.16           C  
ANISOU 1449  CG  PRO A 655     6850   5538   7811    501   -317   -836       C  
ATOM   1450  CD  PRO A 655       7.074 -23.200 -25.695  1.00 51.97           C  
ANISOU 1450  CD  PRO A 655     6387   5586   7774    581   -319   -911       C  
ATOM   1451  N   TYR A 656       8.432 -26.789 -28.445  1.00 55.59           N  
ANISOU 1451  N   TYR A 656     6894   5610   8618    935    -73  -1479       N  
ATOM   1452  CA  TYR A 656       8.675 -27.179 -29.832  1.00 56.03           C  
ANISOU 1452  CA  TYR A 656     6880   5696   8712    928    147  -1690       C  
ATOM   1453  C   TYR A 656       9.873 -26.452 -30.430  1.00 61.09           C  
ANISOU 1453  C   TYR A 656     7180   6513   9519   1008    297  -1861       C  
ATOM   1454  O   TYR A 656       9.814 -25.967 -31.559  1.00 59.64           O  
ANISOU 1454  O   TYR A 656     6944   6478   9239    879    551  -1956       O  
ATOM   1455  CB  TYR A 656       7.428 -26.945 -30.691  1.00 50.77           C  
ANISOU 1455  CB  TYR A 656     6357   5137   7795    667    299  -1666       C  
ATOM   1456  CG  TYR A 656       6.125 -27.139 -29.946  1.00 47.20           C  
ANISOU 1456  CG  TYR A 656     6135   4603   7195    506    187  -1491       C  
ATOM   1457  CD1 TYR A 656       5.754 -28.386 -29.460  1.00 48.69           C  
ANISOU 1457  CD1 TYR A 656     6573   4504   7421    530    107  -1473       C  
ATOM   1458  CD2 TYR A 656       5.265 -26.070 -29.728  1.00 44.17           C  
ANISOU 1458  CD2 TYR A 656     5726   4410   6646    322    188  -1359       C  
ATOM   1459  CE1 TYR A 656       4.561 -28.562 -28.780  1.00 46.55           C  
ANISOU 1459  CE1 TYR A 656     6507   4144   7035    341     72  -1337       C  
ATOM   1460  CE2 TYR A 656       4.072 -26.237 -29.046  1.00 41.37           C  
ANISOU 1460  CE2 TYR A 656     5539   3988   6193    162    127  -1237       C  
ATOM   1461  CZ  TYR A 656       3.726 -27.485 -28.577  1.00 44.83           C  
ANISOU 1461  CZ  TYR A 656     6210   4145   6680    155     90  -1232       C  
ATOM   1462  OH  TYR A 656       2.539 -27.654 -27.902  1.00 46.00           O  
ANISOU 1462  OH  TYR A 656     6519   4210   6748    -43     94  -1134       O  
ATOM   1463  N   SER A 657      10.958 -26.389 -29.665  1.00 68.94           N  
ANISOU 1463  N   SER A 657     7958   7476  10761   1220    140  -1915       N  
ATOM   1464  CA  SER A 657      12.159 -25.679 -30.087  1.00 76.37           C  
ANISOU 1464  CA  SER A 657     8512   8576  11929   1277    291  -2114       C  
ATOM   1465  C   SER A 657      12.810 -26.338 -31.298  1.00 80.38           C  
ANISOU 1465  C   SER A 657     8917   9046  12578   1353    552  -2387       C  
ATOM   1466  O   SER A 657      13.317 -25.655 -32.189  1.00 80.38           O  
ANISOU 1466  O   SER A 657     8722   9203  12616   1248    865  -2536       O  
ATOM   1467  CB  SER A 657      13.160 -25.596 -28.935  1.00 80.83           C  
ANISOU 1467  CB  SER A 657     8842   9102  12770   1517      2  -2161       C  
ATOM   1468  OG  SER A 657      13.580 -26.887 -28.534  1.00 86.96           O  
ANISOU 1468  OG  SER A 657     9707   9627  13708   1815   -225  -2243       O  
ATOM   1469  N   ASN A 658      12.792 -27.665 -31.335  1.00 84.78           N  
ANISOU 1469  N   ASN A 658     9641   9373  13199   1529    452  -2457       N  
ATOM   1470  CA  ASN A 658      13.395 -28.388 -32.450  1.00 91.80           C  
ANISOU 1470  CA  ASN A 658    10456  10201  14223   1623    694  -2733       C  
ATOM   1471  C   ASN A 658      12.555 -28.350 -33.724  1.00 90.48           C  
ANISOU 1471  C   ASN A 658    10524  10099  13754   1383    988  -2743       C  
ATOM   1472  O   ASN A 658      12.982 -28.829 -34.773  1.00 93.98           O  
ANISOU 1472  O   ASN A 658    10952  10512  14245   1424   1240  -2973       O  
ATOM   1473  CB  ASN A 658      13.728 -29.829 -32.051  1.00 98.87           C  
ANISOU 1473  CB  ASN A 658    11464  10800  15303   1924    473  -2823       C  
ATOM   1474  CG  ASN A 658      14.845 -29.903 -31.023  1.00105.41           C  
ANISOU 1474  CG  ASN A 658    12015  11564  16470   2244    180  -2910       C  
ATOM   1475  OD1 ASN A 658      16.026 -29.803 -31.361  1.00109.27           O  
ANISOU 1475  OD1 ASN A 658    12112  12132  17273   2395    283  -3184       O  
ATOM   1476  ND2 ASN A 658      14.474 -30.070 -29.759  1.00106.39           N  
ANISOU 1476  ND2 ASN A 658    12354  11553  16519   2340   -188  -2684       N  
ATOM   1477  N   ILE A 659      11.360 -27.775 -33.626  1.00 85.39           N  
ANISOU 1477  N   ILE A 659    10102   9543  12798   1151    942  -2513       N  
ATOM   1478  CA  ILE A 659      10.517 -27.565 -34.797  1.00 82.49           C  
ANISOU 1478  CA  ILE A 659     9954   9265  12122    942   1154  -2527       C  
ATOM   1479  C   ILE A 659      10.303 -26.084 -35.074  1.00 82.58           C  
ANISOU 1479  C   ILE A 659     9916   9518  11942    750   1296  -2422       C  
ATOM   1480  O   ILE A 659       9.499 -25.435 -34.403  1.00 80.77           O  
ANISOU 1480  O   ILE A 659     9753   9365  11572    636   1127  -2204       O  
ATOM   1481  CB  ILE A 659       9.139 -28.217 -34.638  1.00 78.26           C  
ANISOU 1481  CB  ILE A 659     9740   8617  11379    833    976  -2398       C  
ATOM   1482  CG1 ILE A 659       9.268 -29.689 -34.243  1.00 78.92           C  
ANISOU 1482  CG1 ILE A 659     9943   8407  11635   1002    834  -2468       C  
ATOM   1483  CG2 ILE A 659       8.340 -28.071 -35.928  1.00 76.96           C  
ANISOU 1483  CG2 ILE A 659     9780   8545  10916    663   1142  -2474       C  
ATOM   1484  CD1 ILE A 659       7.937 -30.382 -34.082  1.00 78.03           C  
ANISOU 1484  CD1 ILE A 659    10138   8153  11358    852    711  -2374       C  
ATOM   1485  N   ASN A 660      11.025 -25.545 -36.052  1.00 83.80           N  
ANISOU 1485  N   ASN A 660     9980   9773  12088    711   1629  -2583       N  
ATOM   1486  CA  ASN A 660      10.842 -24.141 -36.395  1.00 79.28           C  
ANISOU 1486  CA  ASN A 660     9436   9383  11304    528   1796  -2482       C  
ATOM   1487  C   ASN A 660       9.961 -23.960 -37.614  1.00 77.59           C  
ANISOU 1487  C   ASN A 660     9582   9213  10685    398   1937  -2480       C  
ATOM   1488  O   ASN A 660      10.400 -23.454 -38.632  1.00 77.93           O  
ANISOU 1488  O   ASN A 660     9713   9305  10590    333   2271  -2589       O  
ATOM   1489  CB  ASN A 660      12.173 -23.425 -36.609  1.00 79.47           C  
ANISOU 1489  CB  ASN A 660     9163   9480  11551    523   2105  -2638       C  
ATOM   1490  CG  ASN A 660      12.034 -21.915 -36.528  1.00 76.73           C  
ANISOU 1490  CG  ASN A 660     8825   9280  11050    339   2211  -2487       C  
ATOM   1491  OD1 ASN A 660      11.093 -21.398 -35.929  1.00 73.74           O  
ANISOU 1491  OD1 ASN A 660     8575   8953  10490    271   1967  -2253       O  
ATOM   1492  ND2 ASN A 660      12.974 -21.201 -37.128  1.00 77.95           N  
ANISOU 1492  ND2 ASN A 660     8848   9483  11285    248   2602  -2635       N  
ATOM   1493  N   ASN A 661       8.707 -24.367 -37.482  1.00 74.56           N  
ANISOU 1493  N   ASN A 661     9417   8801  10110    359   1678  -2369       N  
ATOM   1494  CA  ASN A 661       7.745 -24.278 -38.563  1.00 72.11           C  
ANISOU 1494  CA  ASN A 661     9441   8531   9425    269   1706  -2393       C  
ATOM   1495  C   ASN A 661       6.337 -24.037 -38.040  1.00 69.78           C  
ANISOU 1495  C   ASN A 661     9251   8291   8971    184   1391  -2219       C  
ATOM   1496  O   ASN A 661       5.696 -24.950 -37.524  1.00 69.45           O  
ANISOU 1496  O   ASN A 661     9215   8150   9024    187   1178  -2216       O  
ATOM   1497  CB  ASN A 661       7.801 -25.528 -39.435  1.00 72.95           C  
ANISOU 1497  CB  ASN A 661     9702   8504   9513    339   1784  -2619       C  
ATOM   1498  CG  ASN A 661       7.043 -25.354 -40.742  1.00 73.66           C  
ANISOU 1498  CG  ASN A 661    10157   8642   9188    271   1846  -2698       C  
ATOM   1499  OD1 ASN A 661       5.812 -25.365 -40.764  1.00 72.39           O  
ANISOU 1499  OD1 ASN A 661    10151   8517   8838    210   1585  -2639       O  
ATOM   1500  ND2 ASN A 661       7.777 -25.188 -41.839  1.00 75.94           N  
ANISOU 1500  ND2 ASN A 661    10591   8928   9334    286   2191  -2853       N  
ATOM   1501  N   ARG A 662       5.873 -22.798 -38.174  1.00 68.94           N  
ANISOU 1501  N   ARG A 662     9231   8327   8637    103   1386  -2088       N  
ATOM   1502  CA  ARG A 662       4.579 -22.386 -37.637  1.00 66.00           C  
ANISOU 1502  CA  ARG A 662     8902   8029   8146     34   1104  -1941       C  
ATOM   1503  C   ARG A 662       3.396 -23.218 -38.145  1.00 63.08           C  
ANISOU 1503  C   ARG A 662     8701   7623   7642      8    911  -2056       C  
ATOM   1504  O   ARG A 662       2.558 -23.658 -37.357  1.00 61.77           O  
ANISOU 1504  O   ARG A 662     8451   7427   7592    -48    698  -2011       O  
ATOM   1505  CB  ARG A 662       4.356 -20.902 -37.927  1.00 68.63           C  
ANISOU 1505  CB  ARG A 662     9348   8499   8230     -9   1150  -1819       C  
ATOM   1506  CG  ARG A 662       2.912 -20.450 -37.888  1.00 73.34           C  
ANISOU 1506  CG  ARG A 662    10059   9186   8622    -43    876  -1747       C  
ATOM   1507  CD  ARG A 662       2.792 -19.014 -38.358  1.00 77.58           C  
ANISOU 1507  CD  ARG A 662    10783   9817   8878    -40    933  -1643       C  
ATOM   1508  NE  ARG A 662       3.355 -18.078 -37.392  1.00 80.13           N  
ANISOU 1508  NE  ARG A 662    10921  10174   9352    -80   1008  -1472       N  
ATOM   1509  CZ  ARG A 662       2.634 -17.414 -36.495  1.00 82.45           C  
ANISOU 1509  CZ  ARG A 662    11116  10537   9674   -103    809  -1328       C  
ATOM   1510  NH1 ARG A 662       3.223 -16.578 -35.651  1.00 82.55           N  
ANISOU 1510  NH1 ARG A 662    10980  10568   9815   -140    883  -1195       N  
ATOM   1511  NH2 ARG A 662       1.319 -17.581 -36.445  1.00 83.43           N  
ANISOU 1511  NH2 ARG A 662    11275  10712   9711    -93    541  -1347       N  
ATOM   1512  N   ASP A 663       3.333 -23.429 -39.457  1.00 62.61           N  
ANISOU 1512  N   ASP A 663     8889   7560   7341     35   1001  -2222       N  
ATOM   1513  CA  ASP A 663       2.245 -24.190 -40.062  1.00 63.71           C  
ANISOU 1513  CA  ASP A 663     9188   7672   7349     13    800  -2381       C  
ATOM   1514  C   ASP A 663       2.174 -25.597 -39.491  1.00 62.66           C  
ANISOU 1514  C   ASP A 663     8933   7371   7505    -14    732  -2471       C  
ATOM   1515  O   ASP A 663       1.089 -26.135 -39.270  1.00 63.22           O  
ANISOU 1515  O   ASP A 663     8995   7412   7614    -99    520  -2532       O  
ATOM   1516  CB  ASP A 663       2.423 -24.258 -41.578  1.00 69.55           C  
ANISOU 1516  CB  ASP A 663    10253   8406   7766     72    930  -2563       C  
ATOM   1517  CG  ASP A 663       1.956 -22.999 -42.274  1.00 73.81           C  
ANISOU 1517  CG  ASP A 663    11048   9077   7919     99    882  -2496       C  
ATOM   1518  OD1 ASP A 663       1.508 -22.062 -41.579  1.00 71.76           O  
ANISOU 1518  OD1 ASP A 663    10677   8917   7671     75    748  -2316       O  
ATOM   1519  OD2 ASP A 663       2.046 -22.942 -43.518  1.00 79.62           O  
ANISOU 1519  OD2 ASP A 663    12133   9798   8320    158    978  -2624       O  
ATOM   1520  N   GLN A 664       3.343 -26.178 -39.251  1.00 61.44           N  
ANISOU 1520  N   GLN A 664     8687   7091   7567     62    922  -2494       N  
ATOM   1521  CA  GLN A 664       3.468 -27.534 -38.740  1.00 61.68           C  
ANISOU 1521  CA  GLN A 664     8665   6911   7860     81    880  -2572       C  
ATOM   1522  C   GLN A 664       2.895 -27.640 -37.328  1.00 57.23           C  
ANISOU 1522  C   GLN A 664     7963   6295   7488      6    696  -2396       C  
ATOM   1523  O   GLN A 664       2.049 -28.486 -37.050  1.00 56.66           O  
ANISOU 1523  O   GLN A 664     7946   6096   7485    -90    573  -2452       O  
ATOM   1524  CB  GLN A 664       4.941 -27.921 -38.736  1.00 66.03           C  
ANISOU 1524  CB  GLN A 664     9119   7358   8610    230   1100  -2632       C  
ATOM   1525  CG  GLN A 664       5.217 -29.399 -38.820  1.00 72.74           C  
ANISOU 1525  CG  GLN A 664    10030   7966   9641    308   1112  -2802       C  
ATOM   1526  CD  GLN A 664       6.700 -29.683 -38.891  1.00 79.35           C  
ANISOU 1526  CD  GLN A 664    10731   8724  10694    492   1323  -2900       C  
ATOM   1527  OE1 GLN A 664       7.246 -30.396 -38.051  1.00 81.75           O  
ANISOU 1527  OE1 GLN A 664    10925   8857  11281    617   1251  -2884       O  
ATOM   1528  NE2 GLN A 664       7.366 -29.112 -39.891  1.00 81.53           N  
ANISOU 1528  NE2 GLN A 664    11025   9116  10839    517   1591  -3016       N  
ATOM   1529  N   ILE A 665       3.362 -26.762 -36.448  1.00 52.69           N  
ANISOU 1529  N   ILE A 665     7226   5805   6990     34    701  -2197       N  
ATOM   1530  CA  ILE A 665       2.895 -26.711 -35.070  1.00 49.55           C  
ANISOU 1530  CA  ILE A 665     6736   5363   6727    -28    553  -2015       C  
ATOM   1531  C   ILE A 665       1.389 -26.488 -35.003  1.00 49.77           C  
ANISOU 1531  C   ILE A 665     6801   5470   6637   -199    407  -2006       C  
ATOM   1532  O   ILE A 665       0.696 -27.117 -34.206  1.00 49.65           O  
ANISOU 1532  O   ILE A 665     6796   5328   6740   -305    329  -1976       O  
ATOM   1533  CB  ILE A 665       3.624 -25.598 -34.300  1.00 48.81           C  
ANISOU 1533  CB  ILE A 665     6476   5385   6684     30    574  -1831       C  
ATOM   1534  CG1 ILE A 665       5.117 -25.921 -34.224  1.00 50.84           C  
ANISOU 1534  CG1 ILE A 665     6622   5555   7141    203    690  -1887       C  
ATOM   1535  CG2 ILE A 665       3.044 -25.421 -32.903  1.00 45.27           C  
ANISOU 1535  CG2 ILE A 665     5983   4907   6311    -39    424  -1641       C  
ATOM   1536  CD1 ILE A 665       5.984 -24.726 -33.924  1.00 51.06           C  
ANISOU 1536  CD1 ILE A 665     6460   5729   7211    245    767  -1802       C  
ATOM   1537  N   ILE A 666       0.886 -25.601 -35.853  1.00 51.59           N  
ANISOU 1537  N   ILE A 666     7064   5897   6639   -221    379  -2050       N  
ATOM   1538  CA  ILE A 666      -0.545 -25.336 -35.920  1.00 53.31           C  
ANISOU 1538  CA  ILE A 666     7275   6216   6765   -345    205  -2099       C  
ATOM   1539  C   ILE A 666      -1.318 -26.606 -36.267  1.00 55.13           C  
ANISOU 1539  C   ILE A 666     7570   6306   7072   -449    137  -2317       C  
ATOM   1540  O   ILE A 666      -2.311 -26.938 -35.619  1.00 54.96           O  
ANISOU 1540  O   ILE A 666     7466   6240   7177   -603     53  -2341       O  
ATOM   1541  CB  ILE A 666      -0.858 -24.232 -36.949  1.00 53.65           C  
ANISOU 1541  CB  ILE A 666     7406   6464   6514   -286    148  -2137       C  
ATOM   1542  CG1 ILE A 666      -0.389 -22.876 -36.417  1.00 51.42           C  
ANISOU 1542  CG1 ILE A 666     7055   6306   6178   -238    202  -1913       C  
ATOM   1543  CG2 ILE A 666      -2.345 -24.189 -37.268  1.00 42.94           C  
ANISOU 1543  CG2 ILE A 666     6034   5200   5082   -365    -87  -2284       C  
ATOM   1544  CD1 ILE A 666      -0.497 -21.750 -37.423  1.00 50.55           C  
ANISOU 1544  CD1 ILE A 666     7114   6341   5752   -160    189  -1917       C  
ATOM   1545  N   GLU A 667      -0.845 -27.318 -37.284  1.00 55.33           N  
ANISOU 1545  N   GLU A 667     7743   6248   7032   -381    204  -2494       N  
ATOM   1546  CA  GLU A 667      -1.490 -28.549 -37.721  1.00 59.26           C  
ANISOU 1546  CA  GLU A 667     8324   6593   7599   -479    147  -2733       C  
ATOM   1547  C   GLU A 667      -1.389 -29.649 -36.669  1.00 56.05           C  
ANISOU 1547  C   GLU A 667     7907   5916   7472   -564    214  -2682       C  
ATOM   1548  O   GLU A 667      -2.377 -30.314 -36.357  1.00 55.20           O  
ANISOU 1548  O   GLU A 667     7787   5700   7487   -750    157  -2787       O  
ATOM   1549  CB  GLU A 667      -0.880 -29.025 -39.042  1.00 66.60           C  
ANISOU 1549  CB  GLU A 667     9451   7482   8374   -366    227  -2931       C  
ATOM   1550  CG  GLU A 667      -1.376 -30.385 -39.515  1.00 76.67           C  
ANISOU 1550  CG  GLU A 667    10837   8564   9732   -456    184  -3197       C  
ATOM   1551  CD  GLU A 667      -2.819 -30.369 -39.989  1.00 82.99           C  
ANISOU 1551  CD  GLU A 667    11610   9466  10458   -598    -53  -3409       C  
ATOM   1552  OE1 GLU A 667      -3.350 -29.272 -40.276  1.00 84.40           O  
ANISOU 1552  OE1 GLU A 667    11741   9882  10447   -562   -203  -3381       O  
ATOM   1553  OE2 GLU A 667      -3.418 -31.463 -40.078  1.00 85.15           O  
ANISOU 1553  OE2 GLU A 667    11907   9569  10876   -739    -99  -3624       O  
ATOM   1554  N   MET A 668      -0.195 -29.831 -36.118  1.00 53.43           N  
ANISOU 1554  N   MET A 668     7592   5465   7246   -425    337  -2535       N  
ATOM   1555  CA  MET A 668       0.056 -30.947 -35.215  1.00 53.42           C  
ANISOU 1555  CA  MET A 668     7673   5159   7466   -441    381  -2486       C  
ATOM   1556  C   MET A 668      -0.504 -30.741 -33.808  1.00 47.83           C  
ANISOU 1556  C   MET A 668     6920   4397   6855   -566    346  -2281       C  
ATOM   1557  O   MET A 668      -1.042 -31.674 -33.216  1.00 52.59           O  
ANISOU 1557  O   MET A 668     7646   4752   7583   -708    374  -2300       O  
ATOM   1558  CB  MET A 668       1.547 -31.277 -35.175  1.00 49.70           C  
ANISOU 1558  CB  MET A 668     7232   4567   7083   -199    477  -2447       C  
ATOM   1559  CG  MET A 668       2.148 -31.413 -36.558  1.00 51.22           C  
ANISOU 1559  CG  MET A 668     7472   4818   7173    -85    577  -2658       C  
ATOM   1560  SD  MET A 668       3.704 -32.307 -36.602  1.00 60.06           S  
ANISOU 1560  SD  MET A 668     8623   5710   8489    178    708  -2734       S  
ATOM   1561  CE  MET A 668       4.621 -31.446 -35.345  1.00 64.08           C  
ANISOU 1561  CE  MET A 668     8920   6294   9134    319    670  -2475       C  
ATOM   1562  N   VAL A 669      -0.381 -29.531 -33.272  1.00 45.43           N  
ANISOU 1562  N   VAL A 669     6475   4302   6486   -528    312  -2093       N  
ATOM   1563  CA  VAL A 669      -0.976 -29.235 -31.972  1.00 44.34           C  
ANISOU 1563  CA  VAL A 669     6311   4132   6404   -652    293  -1912       C  
ATOM   1564  C   VAL A 669      -2.499 -29.235 -32.088  1.00 47.91           C  
ANISOU 1564  C   VAL A 669     6694   4649   6860   -906    267  -2046       C  
ATOM   1565  O   VAL A 669      -3.202 -29.718 -31.202  1.00 48.94           O  
ANISOU 1565  O   VAL A 669     6880   4616   7100  -1091    331  -2013       O  
ATOM   1566  CB  VAL A 669      -0.474 -27.886 -31.391  1.00 47.84           C  
ANISOU 1566  CB  VAL A 669     6618   4786   6775   -548    258  -1700       C  
ATOM   1567  CG1 VAL A 669      -1.212 -27.537 -30.105  1.00 40.88           C  
ANISOU 1567  CG1 VAL A 669     5730   3885   5919   -687    250  -1538       C  
ATOM   1568  CG2 VAL A 669       1.023 -27.941 -31.133  1.00 41.78           C  
ANISOU 1568  CG2 VAL A 669     5863   3943   6070   -313    273  -1609       C  
ATOM   1569  N   GLY A 670      -2.997 -28.712 -33.203  1.00 48.95           N  
ANISOU 1569  N   GLY A 670     6717   5009   6873   -910    177  -2217       N  
ATOM   1570  CA  GLY A 670      -4.426 -28.623 -33.443  1.00 50.19           C  
ANISOU 1570  CA  GLY A 670     6744   5269   7056  -1108     94  -2404       C  
ATOM   1571  C   GLY A 670      -5.128 -29.964 -33.542  1.00 57.33           C  
ANISOU 1571  C   GLY A 670     7716   5936   8130  -1318    145  -2629       C  
ATOM   1572  O   GLY A 670      -6.255 -30.116 -33.068  1.00 61.05           O  
ANISOU 1572  O   GLY A 670     8070   6386   8742  -1554    168  -2730       O  
ATOM   1573  N   ARG A 671      -4.469 -30.940 -34.161  1.00 59.06           N  
ANISOU 1573  N   ARG A 671     8118   5966   8354  -1245    186  -2729       N  
ATOM   1574  CA  ARG A 671      -5.042 -32.278 -34.302  1.00 62.63           C  
ANISOU 1574  CA  ARG A 671     8676   6151   8970  -1444    249  -2953       C  
ATOM   1575  C   ARG A 671      -4.691 -33.175 -33.116  1.00 64.80           C  
ANISOU 1575  C   ARG A 671     9165   6060   9395  -1517    432  -2780       C  
ATOM   1576  O   ARG A 671      -5.203 -34.289 -32.994  1.00 66.98           O  
ANISOU 1576  O   ARG A 671     9576   6051   9821  -1722    536  -2925       O  
ATOM   1577  CB  ARG A 671      -4.588 -32.933 -35.609  1.00 64.50           C  
ANISOU 1577  CB  ARG A 671     9043   6340   9126  -1331    200  -3180       C  
ATOM   1578  CG  ARG A 671      -3.129 -33.343 -35.627  1.00 54.88           C  
ANISOU 1578  CG  ARG A 671     8017   4958   7878  -1086    301  -3043       C  
ATOM   1579  CD  ARG A 671      -2.691 -33.762 -37.016  1.00 56.59           C  
ANISOU 1579  CD  ARG A 671     8341   5186   7976   -960    276  -3280       C  
ATOM   1580  NE  ARG A 671      -1.267 -34.071 -37.052  1.00 56.56           N  
ANISOU 1580  NE  ARG A 671     8460   5052   7977   -712    392  -3182       N  
ATOM   1581  CZ  ARG A 671      -0.614 -34.455 -38.141  1.00 58.15           C  
ANISOU 1581  CZ  ARG A 671     8774   5231   8088   -566    440  -3361       C  
ATOM   1582  NH1 ARG A 671      -1.259 -34.580 -39.290  1.00 72.10           N  
ANISOU 1582  NH1 ARG A 671    10597   7088   9709   -638    360  -3631       N  
ATOM   1583  NH2 ARG A 671       0.684 -34.716 -38.082  1.00 59.88           N  
ANISOU 1583  NH2 ARG A 671     9048   5337   8367   -337    561  -3295       N  
ATOM   1584  N   GLY A 672      -3.814 -32.684 -32.246  1.00 64.33           N  
ANISOU 1584  N   GLY A 672     9166   5991   9285  -1344    462  -2478       N  
ATOM   1585  CA  GLY A 672      -3.467 -33.399 -31.030  1.00 64.78           C  
ANISOU 1585  CA  GLY A 672     9480   5705   9429  -1363    587  -2284       C  
ATOM   1586  C   GLY A 672      -2.273 -34.336 -31.117  1.00 64.99           C  
ANISOU 1586  C   GLY A 672     9763   5447   9483  -1130    596  -2247       C  
ATOM   1587  O   GLY A 672      -1.993 -35.063 -30.166  1.00 68.94           O  
ANISOU 1587  O   GLY A 672    10547   5609  10038  -1114    667  -2102       O  
ATOM   1588  N   SER A 673      -1.557 -34.321 -32.237  1.00 60.06           N  
ANISOU 1588  N   SER A 673     9066   4942   8811   -934    529  -2383       N  
ATOM   1589  CA  SER A 673      -0.411 -35.213 -32.400  1.00 60.05           C  
ANISOU 1589  CA  SER A 673     9262   4683   8870   -690    544  -2398       C  
ATOM   1590  C   SER A 673       0.871 -34.686 -31.744  1.00 58.24           C  
ANISOU 1590  C   SER A 673     8999   4493   8637   -383    478  -2177       C  
ATOM   1591  O   SER A 673       1.840 -35.432 -31.573  1.00 56.31           O  
ANISOU 1591  O   SER A 673     8911   4002   8482   -148    461  -2167       O  
ATOM   1592  CB  SER A 673      -0.165 -35.523 -33.877  1.00 57.10           C  
ANISOU 1592  CB  SER A 673     8846   4391   8460   -617    543  -2673       C  
ATOM   1593  OG  SER A 673       0.193 -34.359 -34.594  1.00 54.99           O  
ANISOU 1593  OG  SER A 673     8348   4498   8047   -501    497  -2679       O  
ATOM   1594  N   LEU A 674       0.878 -33.410 -31.376  1.00 51.81           N  
ANISOU 1594  N   LEU A 674     7970   3977   7737   -373    426  -2024       N  
ATOM   1595  CA  LEU A 674       2.072 -32.798 -30.800  1.00 52.02           C  
ANISOU 1595  CA  LEU A 674     7910   4075   7779   -104    349  -1856       C  
ATOM   1596  C   LEU A 674       1.784 -32.096 -29.477  1.00 50.51           C  
ANISOU 1596  C   LEU A 674     7731   3919   7540   -162    293  -1605       C  
ATOM   1597  O   LEU A 674       0.782 -31.393 -29.333  1.00 48.62           O  
ANISOU 1597  O   LEU A 674     7395   3860   7220   -384    323  -1567       O  
ATOM   1598  CB  LEU A 674       2.706 -31.815 -31.791  1.00 49.14           C  
ANISOU 1598  CB  LEU A 674     7271   4048   7354     11    362  -1942       C  
ATOM   1599  CG  LEU A 674       4.019 -31.152 -31.373  1.00 48.42           C  
ANISOU 1599  CG  LEU A 674     7016   4051   7330    265    313  -1842       C  
ATOM   1600  CD1 LEU A 674       5.164 -32.157 -31.390  1.00 51.08           C  
ANISOU 1600  CD1 LEU A 674     7425   4140   7845    536    293  -1940       C  
ATOM   1601  CD2 LEU A 674       4.331 -29.950 -32.253  1.00 46.81           C  
ANISOU 1601  CD2 LEU A 674     6566   4189   7029    268    389  -1898       C  
ATOM   1602  N   SER A 675       2.678 -32.297 -28.516  1.00 50.73           N  
ANISOU 1602  N   SER A 675     7886   3770   7618     60    194  -1455       N  
ATOM   1603  CA  SER A 675       2.586 -31.650 -27.217  1.00 48.70           C  
ANISOU 1603  CA  SER A 675     7690   3526   7289     54    118  -1220       C  
ATOM   1604  C   SER A 675       4.002 -31.338 -26.733  1.00 48.92           C  
ANISOU 1604  C   SER A 675     7637   3566   7383    398    -61  -1151       C  
ATOM   1605  O   SER A 675       4.965 -31.914 -27.236  1.00 50.62           O  
ANISOU 1605  O   SER A 675     7812   3689   7730    634   -109  -1282       O  
ATOM   1606  CB  SER A 675       1.845 -32.549 -26.222  1.00 50.74           C  
ANISOU 1606  CB  SER A 675     8354   3419   7507    -94    179  -1105       C  
ATOM   1607  OG  SER A 675       2.739 -33.400 -25.531  1.00 79.06           O  
ANISOU 1607  OG  SER A 675    12252   6660  11127    177     55  -1021       O  
ATOM   1608  N   PRO A 676       4.138 -30.402 -25.779  1.00 47.46           N  
ANISOU 1608  N   PRO A 676     7400   3505   7127    429   -163   -978       N  
ATOM   1609  CA  PRO A 676       5.454 -30.013 -25.256  1.00 50.13           C  
ANISOU 1609  CA  PRO A 676     7619   3878   7551    744   -370   -945       C  
ATOM   1610  C   PRO A 676       6.251 -31.193 -24.695  1.00 54.80           C  
ANISOU 1610  C   PRO A 676     8495   4098   8231   1043   -544   -945       C  
ATOM   1611  O   PRO A 676       5.691 -32.064 -24.032  1.00 53.19           O  
ANISOU 1611  O   PRO A 676     8720   3562   7928    992   -539   -833       O  
ATOM   1612  CB  PRO A 676       5.101 -29.031 -24.133  1.00 48.96           C  
ANISOU 1612  CB  PRO A 676     7504   3838   7260    663   -444   -743       C  
ATOM   1613  CG  PRO A 676       3.819 -28.434 -24.561  1.00 43.97           C  
ANISOU 1613  CG  PRO A 676     6785   3403   6517    325   -243   -734       C  
ATOM   1614  CD  PRO A 676       3.067 -29.540 -25.247  1.00 45.36           C  
ANISOU 1614  CD  PRO A 676     7121   3396   6716    169    -91   -847       C  
ATOM   1615  N   ASP A 677       7.552 -31.210 -24.967  1.00 57.63           N  
ANISOU 1615  N   ASP A 677     8619   4498   8781   1356   -687  -1085       N  
ATOM   1616  CA  ASP A 677       8.436 -32.285 -24.523  1.00 60.61           C  
ANISOU 1616  CA  ASP A 677     9213   4538   9279   1714   -904  -1129       C  
ATOM   1617  C   ASP A 677       8.774 -32.131 -23.045  1.00 65.72           C  
ANISOU 1617  C   ASP A 677    10106   5036   9830   1918  -1204   -943       C  
ATOM   1618  O   ASP A 677       9.603 -31.304 -22.677  1.00 66.84           O  
ANISOU 1618  O   ASP A 677     9958   5377  10063   2094  -1398   -977       O  
ATOM   1619  CB  ASP A 677       9.726 -32.262 -25.344  1.00 60.70           C  
ANISOU 1619  CB  ASP A 677     8809   4683   9572   1984   -946  -1394       C  
ATOM   1620  CG  ASP A 677      10.569 -33.511 -25.160  1.00 67.41           C  
ANISOU 1620  CG  ASP A 677     9848   5177  10587   2370  -1146  -1504       C  
ATOM   1621  OD1 ASP A 677      10.236 -34.363 -24.306  1.00 70.43           O  
ANISOU 1621  OD1 ASP A 677    10736   5186  10839   2459  -1288  -1345       O  
ATOM   1622  OD2 ASP A 677      11.581 -33.634 -25.879  1.00 69.43           O  
ANISOU 1622  OD2 ASP A 677     9760   5515  11106   2591  -1146  -1759       O  
ATOM   1623  N   LEU A 678       8.145 -32.940 -22.201  1.00 70.07           N  
ANISOU 1623  N   LEU A 678    11217   5216  10190   1890  -1235   -759       N  
ATOM   1624  CA  LEU A 678       8.348 -32.847 -20.758  1.00 73.35           C  
ANISOU 1624  CA  LEU A 678    11991   5445  10433   2073  -1507   -559       C  
ATOM   1625  C   LEU A 678       9.702 -33.392 -20.302  1.00 77.80           C  
ANISOU 1625  C   LEU A 678    12617   5803  11139   2600  -1914   -648       C  
ATOM   1626  O   LEU A 678      10.084 -33.219 -19.147  1.00 79.81           O  
ANISOU 1626  O   LEU A 678    13058   6029  11237   2769  -2180   -513       O  
ATOM   1627  CB  LEU A 678       7.222 -33.564 -20.013  1.00 75.04           C  
ANISOU 1627  CB  LEU A 678    12851   5289  10371   1853  -1352   -336       C  
ATOM   1628  CG  LEU A 678       5.819 -32.992 -20.208  1.00 71.25           C  
ANISOU 1628  CG  LEU A 678    12315   4996   9761   1348   -986   -260       C  
ATOM   1629  CD1 LEU A 678       4.815 -33.767 -19.376  1.00 75.20           C  
ANISOU 1629  CD1 LEU A 678    13456   5091  10027   1134   -805    -72       C  
ATOM   1630  CD2 LEU A 678       5.792 -31.524 -19.844  1.00 66.30           C  
ANISOU 1630  CD2 LEU A 678    11358   4759   9072   1266  -1035   -200       C  
ATOM   1631  N   SER A 679      10.425 -34.047 -21.205  1.00 78.05           N  
ANISOU 1631  N   SER A 679    12415   5809  11433   2797  -1920   -879       N  
ATOM   1632  CA  SER A 679      11.737 -34.590 -20.872  1.00 80.07           C  
ANISOU 1632  CA  SER A 679    12550   6058  11814   3191  -2219   -979       C  
ATOM   1633  C   SER A 679      12.737 -33.461 -20.641  1.00 83.03           C  
ANISOU 1633  C   SER A 679    12400   6786  12363   3363  -2458  -1112       C  
ATOM   1634  O   SER A 679      13.791 -33.660 -20.036  1.00 86.41           O  
ANISOU 1634  O   SER A 679    12738   7243  12849   3661  -2776  -1180       O  
ATOM   1635  CB  SER A 679      12.236 -35.527 -21.979  1.00 77.77           C  
ANISOU 1635  CB  SER A 679    12086   5694  11768   3313  -2098  -1210       C  
ATOM   1636  OG  SER A 679      12.639 -34.811 -23.135  1.00 74.03           O  
ANISOU 1636  OG  SER A 679    11019   5529  11579   3273  -1941  -1477       O  
ATOM   1637  N   LYS A 680      12.387 -32.271 -21.117  1.00 81.82           N  
ANISOU 1637  N   LYS A 680    11902   6894  12294   3155  -2303  -1165       N  
ATOM   1638  CA  LYS A 680      13.284 -31.126 -21.069  1.00 84.92           C  
ANISOU 1638  CA  LYS A 680    11736   7639  12891   3245  -2444  -1323       C  
ATOM   1639  C   LYS A 680      13.203 -30.315 -19.775  1.00 82.79           C  
ANISOU 1639  C   LYS A 680    11616   7434  12406   3245  -2697  -1138       C  
ATOM   1640  O   LYS A 680      13.953 -29.354 -19.603  1.00 81.52           O  
ANISOU 1640  O   LYS A 680    11018   7554  12401   3299  -2837  -1270       O  
ATOM   1641  CB  LYS A 680      13.034 -30.216 -22.273  1.00 86.31           C  
ANISOU 1641  CB  LYS A 680    11427   8177  13188   2913  -2054  -1447       C  
ATOM   1642  CG  LYS A 680      13.474 -30.803 -23.605  1.00 90.83           C  
ANISOU 1642  CG  LYS A 680    11726   8773  14013   2952  -1821  -1709       C  
ATOM   1643  CD  LYS A 680      12.895 -29.990 -24.752  1.00 90.84           C  
ANISOU 1643  CD  LYS A 680    11456   9093  13967   2548  -1390  -1742       C  
ATOM   1644  CE  LYS A 680      13.742 -30.094 -26.007  1.00 94.08           C  
ANISOU 1644  CE  LYS A 680    11443   9633  14670   2616  -1171  -2063       C  
ATOM   1645  NZ  LYS A 680      15.072 -29.446 -25.813  1.00 97.23           N  
ANISOU 1645  NZ  LYS A 680    11335  10205  15401   2836  -1315  -2294       N  
ATOM   1646  N   VAL A 681      12.301 -30.690 -18.871  1.00 82.65           N  
ANISOU 1646  N   VAL A 681    12216   7162  12023   3151  -2720   -849       N  
ATOM   1647  CA  VAL A 681      12.238 -30.016 -17.578  1.00 83.53           C  
ANISOU 1647  CA  VAL A 681    12537   7320  11881   3156  -2945   -678       C  
ATOM   1648  C   VAL A 681      13.524 -30.289 -16.817  1.00 91.34           C  
ANISOU 1648  C   VAL A 681    13449   8340  12914   3497  -3352   -802       C  
ATOM   1649  O   VAL A 681      14.084 -31.383 -16.896  1.00 96.01           O  
ANISOU 1649  O   VAL A 681    14154   8762  13565   3718  -3464   -880       O  
ATOM   1650  CB  VAL A 681      11.028 -30.453 -16.719  1.00 82.76           C  
ANISOU 1650  CB  VAL A 681    13152   6938  11356   2957  -2818   -358       C  
ATOM   1651  CG1 VAL A 681       9.723 -30.071 -17.393  1.00 77.37           C  
ANISOU 1651  CG1 VAL A 681    12484   6295  10618   2538  -2393   -265       C  
ATOM   1652  CG2 VAL A 681      11.075 -31.946 -16.434  1.00 89.47           C  
ANISOU 1652  CG2 VAL A 681    14473   7452  12071   3087  -2845   -291       C  
ATOM   1653  N   ARG A 682      13.997 -29.283 -16.091  1.00 93.12           N  
ANISOU 1653  N   ARG A 682    13483   8778  13120   3535  -3583   -842       N  
ATOM   1654  CA  ARG A 682      15.231 -29.410 -15.332  1.00 99.36           C  
ANISOU 1654  CA  ARG A 682    14177   9610  13966   3836  -3998  -1011       C  
ATOM   1655  C   ARG A 682      15.062 -30.373 -14.163  1.00100.99           C  
ANISOU 1655  C   ARG A 682    15094   9495  13784   3997  -4216   -824       C  
ATOM   1656  O   ARG A 682      13.945 -30.626 -13.709  1.00 99.46           O  
ANISOU 1656  O   ARG A 682    15456   9098  13238   3813  -4029   -541       O  
ATOM   1657  CB  ARG A 682      15.707 -28.037 -14.857  1.00103.15           C  
ANISOU 1657  CB  ARG A 682    14288  10383  14521   3787  -4160  -1125       C  
ATOM   1658  CG  ARG A 682      16.102 -27.112 -16.000  1.00104.94           C  
ANISOU 1658  CG  ARG A 682    13780  10931  15161   3643  -3944  -1358       C  
ATOM   1659  CD  ARG A 682      16.616 -25.769 -15.508  1.00108.92           C  
ANISOU 1659  CD  ARG A 682    13931  11702  15751   3568  -4083  -1484       C  
ATOM   1660  NE  ARG A 682      16.908 -24.868 -16.621  1.00110.40           N  
ANISOU 1660  NE  ARG A 682    13465  12179  16303   3374  -3798  -1688       N  
ATOM   1661  CZ  ARG A 682      17.323 -23.613 -16.479  1.00112.15           C  
ANISOU 1661  CZ  ARG A 682    13305  12648  16661   3234  -3802  -1820       C  
ATOM   1662  NH1 ARG A 682      17.496 -23.105 -15.266  1.00113.97           N  
ANISOU 1662  NH1 ARG A 682    13725  12873  16705   3286  -4103  -1784       N  
ATOM   1663  NH2 ARG A 682      17.563 -22.866 -17.549  1.00110.59           N  
ANISOU 1663  NH2 ARG A 682    12567  12684  16768   3026  -3477  -1996       N  
ATOM   1664  N   SER A 683      16.180 -30.915 -13.692  1.00104.38           N  
ANISOU 1664  N   SER A 683    15504   9872  14284   4331  -4593  -1004       N  
ATOM   1665  CA  SER A 683      16.178 -31.902 -12.619  1.00107.24           C  
ANISOU 1665  CA  SER A 683    16544   9914  14287   4538  -4837   -869       C  
ATOM   1666  C   SER A 683      15.664 -31.335 -11.299  1.00105.00           C  
ANISOU 1666  C   SER A 683    16736   9581  13579   4453  -4943   -680       C  
ATOM   1667  O   SER A 683      14.935 -32.006 -10.568  1.00105.78           O  
ANISOU 1667  O   SER A 683    17530   9392  13271   4412  -4872   -439       O  
ATOM   1668  CB  SER A 683      17.585 -32.464 -12.423  1.00113.94           C  
ANISOU 1668  CB  SER A 683    17206  10747  15341   4943  -5268  -1155       C  
ATOM   1669  OG  SER A 683      18.499 -31.429 -12.105  1.00115.38           O  
ANISOU 1669  OG  SER A 683    16906  11207  15728   5021  -5543  -1410       O  
ATOM   1670  N   ASN A 684      16.046 -30.097 -11.001  1.00102.03           N  
ANISOU 1670  N   ASN A 684    15989   9478  13299   4408  -5081   -806       N  
ATOM   1671  CA  ASN A 684      15.654 -29.445  -9.754  1.00102.42           C  
ANISOU 1671  CA  ASN A 684    16439   9503  12972   4337  -5190   -672       C  
ATOM   1672  C   ASN A 684      14.164 -29.143  -9.663  1.00 96.69           C  
ANISOU 1672  C   ASN A 684    16083   8714  11940   3968  -4764   -351       C  
ATOM   1673  O   ASN A 684      13.656 -28.808  -8.592  1.00 97.10           O  
ANISOU 1673  O   ASN A 684    16591   8686  11618   3885  -4774   -203       O  
ATOM   1674  CB  ASN A 684      16.460 -28.161  -9.550  1.00103.90           C  
ANISOU 1674  CB  ASN A 684    16090   9998  13389   4362  -5418   -915       C  
ATOM   1675  CG  ASN A 684      16.829 -27.496 -10.859  1.00101.72           C  
ANISOU 1675  CG  ASN A 684    15013  10026  13609   4235  -5230  -1112       C  
ATOM   1676  OD1 ASN A 684      16.957 -28.160 -11.888  1.00101.27           O  
ANISOU 1676  OD1 ASN A 684    14726   9953  13798   4264  -5073  -1176       O  
ATOM   1677  ND2 ASN A 684      17.011 -26.181 -10.828  1.00100.29           N  
ANISOU 1677  ND2 ASN A 684    14422  10113  13571   4085  -5222  -1221       N  
ATOM   1678  N   CYS A 685      13.468 -29.253 -10.789  1.00 91.83           N  
ANISOU 1678  N   CYS A 685    15268   8128  11493   3743  -4382   -270       N  
ATOM   1679  CA  CYS A 685      12.033 -29.007 -10.817  1.00 89.02           C  
ANISOU 1679  CA  CYS A 685    15217   7707  10898   3377  -3960     -2       C  
ATOM   1680  C   CYS A 685      11.300 -30.046  -9.977  1.00 91.19           C  
ANISOU 1680  C   CYS A 685    16279   7626  10745   3329  -3833    224       C  
ATOM   1681  O   CYS A 685      11.429 -31.244 -10.225  1.00 91.98           O  
ANISOU 1681  O   CYS A 685    16604   7491  10854   3451  -3826    230       O  
ATOM   1682  CB  CYS A 685      11.504 -29.013 -12.255  1.00 85.96           C  
ANISOU 1682  CB  CYS A 685    14465   7390  10805   3174  -3608    -11       C  
ATOM   1683  SG  CYS A 685       9.699 -29.038 -12.379  1.00 88.95           S  
ANISOU 1683  SG  CYS A 685    15260   7615  10921   2717  -3070    278       S  
ATOM   1684  N   PRO A 686      10.541 -29.584  -8.965  1.00 92.28           N  
ANISOU 1684  N   PRO A 686    16838   7716  10508   3145  -3712    393       N  
ATOM   1685  CA  PRO A 686       9.733 -30.463  -8.113  1.00 95.40           C  
ANISOU 1685  CA  PRO A 686    17989   7781  10478   3037  -3507    596       C  
ATOM   1686  C   PRO A 686       8.801 -31.319  -8.954  1.00 95.74           C  
ANISOU 1686  C   PRO A 686    18146   7650  10582   2782  -3067    712       C  
ATOM   1687  O   PRO A 686       8.250 -30.832  -9.939  1.00 92.21           O  
ANISOU 1687  O   PRO A 686    17302   7358  10375   2538  -2796    709       O  
ATOM   1688  CB  PRO A 686       8.910 -29.480  -7.280  1.00 92.24           C  
ANISOU 1688  CB  PRO A 686    17787   7466   9794   2779  -3314    716       C  
ATOM   1689  CG  PRO A 686       9.755 -28.273  -7.201  1.00 90.83           C  
ANISOU 1689  CG  PRO A 686    17120   7592   9800   2928  -3652    549       C  
ATOM   1690  CD  PRO A 686      10.447 -28.177  -8.540  1.00 88.87           C  
ANISOU 1690  CD  PRO A 686    16186   7541  10041   3029  -3751    377       C  
ATOM   1691  N   LYS A 687       8.630 -32.576  -8.565  1.00101.64           N  
ANISOU 1691  N   LYS A 687    19444   8063  11113   2833  -3002    797       N  
ATOM   1692  CA  LYS A 687       7.848 -33.520  -9.353  1.00102.78           C  
ANISOU 1692  CA  LYS A 687    19699   8010  11341   2604  -2608    869       C  
ATOM   1693  C   LYS A 687       6.353 -33.215  -9.320  1.00100.29           C  
ANISOU 1693  C   LYS A 687    19532   7685  10890   2112  -2066   1012       C  
ATOM   1694  O   LYS A 687       5.622 -33.598 -10.234  1.00 98.23           O  
ANISOU 1694  O   LYS A 687    19135   7374  10813   1844  -1714   1013       O  
ATOM   1695  CB  LYS A 687       8.111 -34.950  -8.880  1.00109.82           C  
ANISOU 1695  CB  LYS A 687    21166   8531  12029   2799  -2696    913       C  
ATOM   1696  CG  LYS A 687       9.588 -35.330  -8.896  1.00114.59           C  
ANISOU 1696  CG  LYS A 687    21623   9135  12781   3299  -3240    743       C  
ATOM   1697  CD  LYS A 687       9.786 -36.813  -8.596  1.00121.76           C  
ANISOU 1697  CD  LYS A 687    23097   9652  13513   3488  -3302    788       C  
ATOM   1698  CE  LYS A 687      11.236 -37.122  -8.265  1.00126.89           C  
ANISOU 1698  CE  LYS A 687    23705  10287  14220   4011  -3893    615       C  
ATOM   1699  NZ  LYS A 687      11.412 -38.544  -7.874  1.00133.47           N  
ANISOU 1699  NZ  LYS A 687    25163  10716  14834   4218  -3976    671       N  
ATOM   1700  N   ARG A 688       5.900 -32.532  -8.272  1.00100.68           N  
ANISOU 1700  N   ARG A 688    19841   7781  10633   1990  -1994   1098       N  
ATOM   1701  CA  ARG A 688       4.489 -32.172  -8.158  1.00 99.08           C  
ANISOU 1701  CA  ARG A 688    19733   7597  10317   1527  -1471   1196       C  
ATOM   1702  C   ARG A 688       4.097 -31.136  -9.206  1.00 91.99           C  
ANISOU 1702  C   ARG A 688    18201   7007   9746   1309  -1321   1137       C  
ATOM   1703  O   ARG A 688       2.954 -31.105  -9.669  1.00 88.86           O  
ANISOU 1703  O   ARG A 688    17721   6622   9420    920   -875   1157       O  
ATOM   1704  CB  ARG A 688       4.174 -31.650  -6.755  1.00103.39           C  
ANISOU 1704  CB  ARG A 688    20700   8121  10462   1482  -1438   1271       C  
ATOM   1705  CG  ARG A 688       4.252 -32.703  -5.660  1.00112.37           C  
ANISOU 1705  CG  ARG A 688    22591   8898  11205   1612  -1465   1340       C  
ATOM   1706  CD  ARG A 688       3.879 -32.125  -4.300  1.00117.06           C  
ANISOU 1706  CD  ARG A 688    23616   9459  11404   1550  -1393   1387       C  
ATOM   1707  NE  ARG A 688       3.953 -33.122  -3.233  1.00127.22           N  
ANISOU 1707  NE  ARG A 688    25692  10367  12277   1683  -1414   1444       N  
ATOM   1708  CZ  ARG A 688       3.739 -32.858  -1.947  1.00131.48           C  
ANISOU 1708  CZ  ARG A 688    26757  10782  12415   1688  -1380   1472       C  
ATOM   1709  NH1 ARG A 688       3.441 -31.624  -1.564  1.00127.96           N  
ANISOU 1709  NH1 ARG A 688    26101  10571  11948   1565  -1324   1447       N  
ATOM   1710  NH2 ARG A 688       3.826 -33.825  -1.043  1.00138.24           N  
ANISOU 1710  NH2 ARG A 688    28379  11261  12886   1823  -1398   1519       N  
ATOM   1711  N   MET A 689       5.057 -30.294  -9.569  1.00 89.29           N  
ANISOU 1711  N   MET A 689    17406   6910   9609   1563  -1701   1038       N  
ATOM   1712  CA  MET A 689       4.852 -29.268 -10.577  1.00 84.24           C  
ANISOU 1712  CA  MET A 689    16190   6548   9268   1414  -1618    971       C  
ATOM   1713  C   MET A 689       4.856 -29.888 -11.971  1.00 81.71           C  
ANISOU 1713  C   MET A 689    15579   6179   9288   1378  -1511    870       C  
ATOM   1714  O   MET A 689       4.149 -29.423 -12.865  1.00 76.71           O  
ANISOU 1714  O   MET A 689    14649   5658   8839   1106  -1246    830       O  
ATOM   1715  CB  MET A 689       5.944 -28.201 -10.462  1.00 85.08           C  
ANISOU 1715  CB  MET A 689    15919   6920   9488   1703  -2056    870       C  
ATOM   1716  CG  MET A 689       5.689 -26.931 -11.266  1.00 81.04           C  
ANISOU 1716  CG  MET A 689    14887   6697   9207   1544  -1974    822       C  
ATOM   1717  SD  MET A 689       4.413 -25.870 -10.560  1.00 97.97           S  
ANISOU 1717  SD  MET A 689    17179   8956  11088   1161  -1626    961       S  
ATOM   1718  CE  MET A 689       5.398 -24.478 -10.010  1.00103.95           C  
ANISOU 1718  CE  MET A 689    17641  10003  11852   1401  -2054    886       C  
ATOM   1719  N   LYS A 690       5.659 -30.933 -12.154  1.00 86.13           N  
ANISOU 1719  N   LYS A 690    16234   6566   9925   1659  -1724    807       N  
ATOM   1720  CA  LYS A 690       5.695 -31.655 -13.424  1.00 86.99           C  
ANISOU 1720  CA  LYS A 690    16119   6595  10337   1643  -1616    689       C  
ATOM   1721  C   LYS A 690       4.340 -32.283 -13.718  1.00 83.97           C  
ANISOU 1721  C   LYS A 690    15965   6039   9902   1214  -1118    749       C  
ATOM   1722  O   LYS A 690       3.855 -32.237 -14.849  1.00 81.33           O  
ANISOU 1722  O   LYS A 690    15331   5761   9811   1004   -901    638       O  
ATOM   1723  CB  LYS A 690       6.781 -32.731 -13.416  1.00 93.99           C  
ANISOU 1723  CB  LYS A 690    17117   7309  11286   2028  -1922    612       C  
ATOM   1724  CG  LYS A 690       8.185 -32.183 -13.266  1.00 98.45           C  
ANISOU 1724  CG  LYS A 690    17336   8078  11993   2440  -2410    472       C  
ATOM   1725  CD  LYS A 690       9.231 -33.282 -13.344  1.00105.46           C  
ANISOU 1725  CD  LYS A 690    18284   8804  12981   2810  -2692    359       C  
ATOM   1726  CE  LYS A 690      10.616 -32.745 -13.011  1.00108.07           C  
ANISOU 1726  CE  LYS A 690    18268   9347  13444   3192  -3178    184       C  
ATOM   1727  NZ  LYS A 690      11.655 -33.810 -13.073  1.00112.75           N  
ANISOU 1727  NZ  LYS A 690    18897   9791  14152   3561  -3464     48       N  
ATOM   1728  N   ARG A 691       3.731 -32.864 -12.689  1.00 83.74           N  
ANISOU 1728  N   ARG A 691    16454   5807   9555   1077   -935    891       N  
ATOM   1729  CA  ARG A 691       2.393 -33.425 -12.814  1.00 82.69           C  
ANISOU 1729  CA  ARG A 691    16504   5536   9379    639   -436    919       C  
ATOM   1730  C   ARG A 691       1.371 -32.338 -13.110  1.00 76.09           C  
ANISOU 1730  C   ARG A 691    15342   4951   8619    263   -136    890       C  
ATOM   1731  O   ARG A 691       0.541 -32.488 -14.002  1.00 74.57           O  
ANISOU 1731  O   ARG A 691    14913   4789   8630    -51    168    780       O  
ATOM   1732  CB  ARG A 691       2.002 -34.177 -11.541  1.00 88.36           C  
ANISOU 1732  CB  ARG A 691    17857   5994   9722    586   -293   1058       C  
ATOM   1733  CG  ARG A 691       2.678 -35.524 -11.396  1.00 95.50           C  
ANISOU 1733  CG  ARG A 691    19149   6580  10555    854   -468   1076       C  
ATOM   1734  CD  ARG A 691       2.398 -36.137 -10.039  1.00102.19           C  
ANISOU 1734  CD  ARG A 691    20689   7164  10975    845   -369   1212       C  
ATOM   1735  NE  ARG A 691       3.634 -36.477  -9.341  1.00107.48           N  
ANISOU 1735  NE  ARG A 691    21667   7711  11458   1324   -854   1244       N  
ATOM   1736  CZ  ARG A 691       3.880 -36.186  -8.068  1.00111.45           C  
ANISOU 1736  CZ  ARG A 691    22579   8172  11594   1474  -1022   1321       C  
ATOM   1737  NH1 ARG A 691       2.974 -35.546  -7.342  1.00110.32           N  
ANISOU 1737  NH1 ARG A 691    22596   8092  11228   1182   -714   1384       N  
ATOM   1738  NH2 ARG A 691       5.035 -36.536  -7.519  1.00115.78           N  
ANISOU 1738  NH2 ARG A 691    23373   8612  12005   1923  -1501   1307       N  
ATOM   1739  N   LEU A 692       1.442 -31.244 -12.357  1.00 72.46           N  
ANISOU 1739  N   LEU A 692    14858   4676   7998    303   -240    965       N  
ATOM   1740  CA  LEU A 692       0.507 -30.136 -12.519  1.00 68.77           C  
ANISOU 1740  CA  LEU A 692    14096   4454   7580    -24     24    942       C  
ATOM   1741  C   LEU A 692       0.625 -29.513 -13.901  1.00 63.12           C  
ANISOU 1741  C   LEU A 692    12843   3934   7203    -64    -26    799       C  
ATOM   1742  O   LEU A 692      -0.376 -29.157 -14.519  1.00 59.55           O  
ANISOU 1742  O   LEU A 692    12086   3650   6890   -414    285    697       O  
ATOM   1743  CB  LEU A 692       0.737 -29.070 -11.449  1.00 69.30           C  
ANISOU 1743  CB  LEU A 692    14248   4673   7409     84   -133   1039       C  
ATOM   1744  CG  LEU A 692      -0.179 -27.851 -11.538  1.00 65.29           C  
ANISOU 1744  CG  LEU A 692    13440   4426   6942   -222    121   1018       C  
ATOM   1745  CD1 LEU A 692      -1.633 -28.260 -11.375  1.00 65.31           C  
ANISOU 1745  CD1 LEU A 692    13525   4375   6914   -649    646    978       C  
ATOM   1746  CD2 LEU A 692       0.208 -26.819 -10.497  1.00 66.66           C  
ANISOU 1746  CD2 LEU A 692    13705   4738   6884    -67    -85   1100       C  
ATOM   1747  N   MET A 693       1.858 -29.387 -14.374  1.00 62.66           N  
ANISOU 1747  N   MET A 693    12559   3960   7289    304   -422    736       N  
ATOM   1748  CA  MET A 693       2.120 -28.875 -15.710  1.00 60.47           C  
ANISOU 1748  CA  MET A 693    11576   4079   7322    297   -462    532       C  
ATOM   1749  C   MET A 693       1.478 -29.771 -16.764  1.00 61.34           C  
ANISOU 1749  C   MET A 693    11595   4101   7609     74   -197    396       C  
ATOM   1750  O   MET A 693       0.883 -29.289 -17.724  1.00 59.30           O  
ANISOU 1750  O   MET A 693    10872   4147   7510   -150    -30    251       O  
ATOM   1751  CB  MET A 693       3.624 -28.796 -15.942  1.00 60.20           C  
ANISOU 1751  CB  MET A 693    11328   4123   7424    731   -886    456       C  
ATOM   1752  CG  MET A 693       4.020 -28.282 -17.304  1.00 55.03           C  
ANISOU 1752  CG  MET A 693    10004   3842   7064    733   -893    245       C  
ATOM   1753  SD  MET A 693       5.761 -28.599 -17.624  1.00 78.42           S  
ANISOU 1753  SD  MET A 693    12760   6789  10248   1220  -1302    102       S  
ATOM   1754  CE  MET A 693       6.519 -27.854 -16.185  1.00 70.02           C  
ANISOU 1754  CE  MET A 693    11870   5720   9015   1495  -1684    218       C  
ATOM   1755  N   ALA A 694       1.601 -31.079 -16.571  1.00 62.69           N  
ANISOU 1755  N   ALA A 694    12247   3836   7737    150   -180    438       N  
ATOM   1756  CA  ALA A 694       1.030 -32.048 -17.498  1.00 64.55           C  
ANISOU 1756  CA  ALA A 694    12463   3928   8136    -59     61    298       C  
ATOM   1757  C   ALA A 694      -0.495 -32.037 -17.451  1.00 67.59           C  
ANISOU 1757  C   ALA A 694    12876   4306   8501   -552    495    271       C  
ATOM   1758  O   ALA A 694      -1.155 -32.283 -18.458  1.00 66.02           O  
ANISOU 1758  O   ALA A 694    12373   4214   8495   -793    682     78       O  
ATOM   1759  CB  ALA A 694       1.560 -33.444 -17.204  1.00 64.87           C  
ANISOU 1759  CB  ALA A 694    12980   3545   8124    154    -29    351       C  
ATOM   1760  N   GLU A 695      -1.050 -31.765 -16.275  1.00 71.57           N  
ANISOU 1760  N   GLU A 695    13664   4756   8775   -685    643    430       N  
ATOM   1761  CA  GLU A 695      -2.498 -31.700 -16.121  1.00 74.89           C  
ANISOU 1761  CA  GLU A 695    13993   5262   9200  -1129   1062    367       C  
ATOM   1762  C   GLU A 695      -3.057 -30.466 -16.823  1.00 70.70           C  
ANISOU 1762  C   GLU A 695    12928   5097   8839  -1325   1127    226       C  
ATOM   1763  O   GLU A 695      -4.154 -30.499 -17.381  1.00 71.62           O  
ANISOU 1763  O   GLU A 695    12765   5327   9121  -1664   1400     44       O  
ATOM   1764  CB  GLU A 695      -2.884 -31.689 -14.641  1.00 80.36           C  
ANISOU 1764  CB  GLU A 695    15082   5868   9584  -1178   1208    542       C  
ATOM   1765  CG  GLU A 695      -2.509 -32.960 -13.903  1.00 88.42           C  
ANISOU 1765  CG  GLU A 695    16659   6538  10397  -1027   1187    659       C  
ATOM   1766  CD  GLU A 695      -3.250 -34.172 -14.426  1.00 96.81           C  
ANISOU 1766  CD  GLU A 695    17772   7415  11596  -1285   1483    536       C  
ATOM   1767  OE1 GLU A 695      -2.595 -35.194 -14.728  1.00 99.71           O  
ANISOU 1767  OE1 GLU A 695    18353   7543  11992  -1093   1336    545       O  
ATOM   1768  OE2 GLU A 695      -4.492 -34.103 -14.529  1.00 99.36           O  
ANISOU 1768  OE2 GLU A 695    17901   7838  12012  -1671   1855    410       O  
ATOM   1769  N   CYS A 696      -2.290 -29.382 -16.800  1.00 65.37           N  
ANISOU 1769  N   CYS A 696    11971   4743   8125  -1060    828    278       N  
ATOM   1770  CA  CYS A 696      -2.696 -28.143 -17.450  1.00 61.23           C  
ANISOU 1770  CA  CYS A 696    10846   4696   7721  -1149    819    153       C  
ATOM   1771  C   CYS A 696      -2.598 -28.255 -18.965  1.00 56.78           C  
ANISOU 1771  C   CYS A 696     9829   4350   7394  -1132    742    -61       C  
ATOM   1772  O   CYS A 696      -3.352 -27.610 -19.689  1.00 53.07           O  
ANISOU 1772  O   CYS A 696     8943   4181   7038  -1303    825   -216       O  
ATOM   1773  CB  CYS A 696      -1.835 -26.975 -16.966  1.00 60.02           C  
ANISOU 1773  CB  CYS A 696    10575   4776   7455   -881    538    270       C  
ATOM   1774  SG  CYS A 696      -2.036 -26.566 -15.217  1.00 67.29           S  
ANISOU 1774  SG  CYS A 696    11993   5517   8058   -902    609    496       S  
ATOM   1775  N   LEU A 697      -1.673 -29.086 -19.434  1.00 58.11           N  
ANISOU 1775  N   LEU A 697    10107   4351   7621   -907    575    -82       N  
ATOM   1776  CA  LEU A 697      -1.394 -29.193 -20.861  1.00 56.12           C  
ANISOU 1776  CA  LEU A 697     9478   4290   7554   -847    492   -281       C  
ATOM   1777  C   LEU A 697      -2.217 -30.267 -21.547  1.00 56.73           C  
ANISOU 1777  C   LEU A 697     9610   4187   7757  -1094    703   -455       C  
ATOM   1778  O   LEU A 697      -1.929 -30.640 -22.686  1.00 56.37           O  
ANISOU 1778  O   LEU A 697     9374   4208   7838  -1027    636   -623       O  
ATOM   1779  CB  LEU A 697       0.092 -29.455 -21.093  1.00 55.89           C  
ANISOU 1779  CB  LEU A 697     9467   4208   7560   -462    214   -260       C  
ATOM   1780  CG  LEU A 697       1.010 -28.272 -20.797  1.00 53.46           C  
ANISOU 1780  CG  LEU A 697     8932   4167   7214   -224    -18   -183       C  
ATOM   1781  CD1 LEU A 697       2.460 -28.685 -20.959  1.00 55.02           C  
ANISOU 1781  CD1 LEU A 697     9130   4274   7503    146   -275   -212       C  
ATOM   1782  CD2 LEU A 697       0.672 -27.100 -21.702  1.00 48.72           C  
ANISOU 1782  CD2 LEU A 697     7846   3989   6674   -334     24   -294       C  
ATOM   1783  N   LYS A 698      -3.238 -30.758 -20.852  1.00 60.61           N  
ANISOU 1783  N   LYS A 698    10371   4442   8216  -1395    977   -433       N  
ATOM   1784  CA  LYS A 698      -4.111 -31.791 -21.396  1.00 62.38           C  
ANISOU 1784  CA  LYS A 698    10649   4465   8587  -1687   1211   -626       C  
ATOM   1785  C   LYS A 698      -4.744 -31.317 -22.692  1.00 61.44           C  
ANISOU 1785  C   LYS A 698     9988   4716   8639  -1813   1187   -898       C  
ATOM   1786  O   LYS A 698      -5.297 -30.218 -22.760  1.00 57.80           O  
ANISOU 1786  O   LYS A 698     9183   4595   8182  -1886   1178   -939       O  
ATOM   1787  CB  LYS A 698      -5.203 -32.156 -20.394  1.00 63.07           C  
ANISOU 1787  CB  LYS A 698    11027   4306   8631  -2037   1563   -582       C  
ATOM   1788  CG  LYS A 698      -5.126 -33.576 -19.889  1.00 68.03           C  
ANISOU 1788  CG  LYS A 698    12102   4565   9182  -2021   1668   -490       C  
ATOM   1789  CD  LYS A 698      -3.868 -33.804 -19.080  1.00 69.41           C  
ANISOU 1789  CD  LYS A 698    12742   4487   9142  -1650   1444   -226       C  
ATOM   1790  CE  LYS A 698      -3.818 -35.222 -18.540  1.00 73.46           C  
ANISOU 1790  CE  LYS A 698    13725   4633   9553  -1625   1541   -136       C  
ATOM   1791  NZ  LYS A 698      -4.937 -35.504 -17.593  1.00 76.42           N  
ANISOU 1791  NZ  LYS A 698    14292   4941   9802  -1931   1900    -89       N  
ATOM   1792  N   LYS A 699      -4.654 -32.156 -23.717  1.00 63.67           N  
ANISOU 1792  N   LYS A 699    10231   4915   9047  -1816   1159  -1088       N  
ATOM   1793  CA  LYS A 699      -5.167 -31.822 -25.038  1.00 63.40           C  
ANISOU 1793  CA  LYS A 699     9756   5198   9135  -1891   1089  -1360       C  
ATOM   1794  C   LYS A 699      -6.684 -31.704 -25.009  1.00 62.67           C  
ANISOU 1794  C   LYS A 699     9451   5186   9174  -2274   1292  -1560       C  
ATOM   1795  O   LYS A 699      -7.266 -30.858 -25.688  1.00 59.92           O  
ANISOU 1795  O   LYS A 699     8693   5199   8876  -2306   1191  -1725       O  
ATOM   1796  CB  LYS A 699      -4.720 -32.875 -26.055  1.00 65.90           C  
ANISOU 1796  CB  LYS A 699    10153   5351   9535  -1813   1031  -1528       C  
ATOM   1797  CG  LYS A 699      -3.287 -33.343 -25.833  1.00 68.99           C  
ANISOU 1797  CG  LYS A 699    10830   5533   9852  -1463    896  -1355       C  
ATOM   1798  CD  LYS A 699      -2.698 -34.034 -27.052  1.00 73.99           C  
ANISOU 1798  CD  LYS A 699    11423   6129  10561  -1314    804  -1546       C  
ATOM   1799  CE  LYS A 699      -1.343 -34.644 -26.711  1.00 78.28           C  
ANISOU 1799  CE  LYS A 699    12252   6409  11082   -969    689  -1408       C  
ATOM   1800  NZ  LYS A 699      -0.661 -35.254 -27.890  1.00 79.60           N  
ANISOU 1800  NZ  LYS A 699    12361   6553  11331   -791    619  -1605       N  
ATOM   1801  N   LYS A 700      -7.319 -32.550 -24.207  1.00 65.26           N  
ANISOU 1801  N   LYS A 700    10044   5209   9543  -2520   1559  -1533       N  
ATOM   1802  CA  LYS A 700      -8.762 -32.497 -24.046  1.00 68.78           C  
ANISOU 1802  CA  LYS A 700    10215   5820  10101  -2801   1746  -1683       C  
ATOM   1803  C   LYS A 700      -9.119 -31.465 -22.988  1.00 69.10           C  
ANISOU 1803  C   LYS A 700    10207   5997  10052  -2846   1855  -1533       C  
ATOM   1804  O   LYS A 700      -8.705 -31.566 -21.834  1.00 69.66           O  
ANISOU 1804  O   LYS A 700    10668   5847   9952  -2801   1970  -1271       O  
ATOM   1805  CB  LYS A 700      -9.323 -33.879 -23.702  1.00 74.75           C  
ANISOU 1805  CB  LYS A 700    11214   6280  10907  -2991   1989  -1710       C  
ATOM   1806  CG  LYS A 700      -9.108 -34.898 -24.810  1.00 79.14           C  
ANISOU 1806  CG  LYS A 700    11782   6717  11570  -2969   1885  -1893       C  
ATOM   1807  CD  LYS A 700      -9.726 -36.246 -24.487  1.00 85.99           C  
ANISOU 1807  CD  LYS A 700    12879   7290  12501  -3184   2139  -1937       C  
ATOM   1808  CE  LYS A 700      -9.551 -37.214 -25.650  1.00 88.91           C  
ANISOU 1808  CE  LYS A 700    13239   7557  12984  -3165   2020  -2141       C  
ATOM   1809  NZ  LYS A 700     -10.105 -38.564 -25.349  1.00 94.45           N  
ANISOU 1809  NZ  LYS A 700    14189   7945  13754  -3382   2272  -2185       N  
ATOM   1810  N   ARG A 701      -9.887 -30.467 -23.409  1.00 70.92           N  
ANISOU 1810  N   ARG A 701     9971   6594  10381  -2904   1792  -1710       N  
ATOM   1811  CA  ARG A 701     -10.185 -29.289 -22.599  1.00 71.31           C  
ANISOU 1811  CA  ARG A 701     9904   6830  10361  -2908   1847  -1605       C  
ATOM   1812  C   ARG A 701     -10.781 -29.603 -21.224  1.00 74.32           C  
ANISOU 1812  C   ARG A 701    10539   7034  10665  -3068   2183  -1473       C  
ATOM   1813  O   ARG A 701     -10.418 -28.979 -20.229  1.00 74.36           O  
ANISOU 1813  O   ARG A 701    10756   7004  10493  -3000   2233  -1248       O  
ATOM   1814  CB  ARG A 701     -11.102 -28.347 -23.386  1.00 70.75           C  
ANISOU 1814  CB  ARG A 701     9272   7169  10439  -2927   1714  -1870       C  
ATOM   1815  CG  ARG A 701     -12.174 -27.675 -22.562  1.00 74.96           C  
ANISOU 1815  CG  ARG A 701     9609   7856  11018  -3047   1907  -1907       C  
ATOM   1816  CD  ARG A 701     -13.492 -27.636 -23.309  1.00 79.88           C  
ANISOU 1816  CD  ARG A 701     9758   8720  11872  -3136   1879  -2257       C  
ATOM   1817  NE  ARG A 701     -13.594 -26.487 -24.202  1.00 80.05           N  
ANISOU 1817  NE  ARG A 701     9397   9096  11922  -2949   1552  -2390       N  
ATOM   1818  CZ  ARG A 701     -14.744 -26.022 -24.678  1.00 83.41           C  
ANISOU 1818  CZ  ARG A 701     9401   9779  12513  -2941   1467  -2663       C  
ATOM   1819  NH1 ARG A 701     -15.884 -26.608 -24.343  1.00 87.53           N  
ANISOU 1819  NH1 ARG A 701     9787  10249  13220  -3138   1711  -2857       N  
ATOM   1820  NH2 ARG A 701     -14.759 -24.970 -25.483  1.00 82.52           N  
ANISOU 1820  NH2 ARG A 701     9019   9960  12374  -2723   1137  -2753       N  
ATOM   1821  N   ASP A 702     -11.680 -30.580 -21.165  1.00 77.97           N  
ANISOU 1821  N   ASP A 702    11005   7376  11243  -3280   2419  -1623       N  
ATOM   1822  CA  ASP A 702     -12.395 -30.862 -19.924  1.00 81.57           C  
ANISOU 1822  CA  ASP A 702    11678   7685  11631  -3460   2786  -1561       C  
ATOM   1823  C   ASP A 702     -11.599 -31.672 -18.910  1.00 76.99           C  
ANISOU 1823  C   ASP A 702    11755   6707  10793  -3404   2911  -1260       C  
ATOM   1824  O   ASP A 702     -12.063 -31.909 -17.796  1.00 77.68           O  
ANISOU 1824  O   ASP A 702    12121   6643  10753  -3527   3215  -1182       O  
ATOM   1825  CB  ASP A 702     -13.740 -31.527 -20.209  1.00 91.10           C  
ANISOU 1825  CB  ASP A 702    12616   8921  13076  -3726   3025  -1874       C  
ATOM   1826  CG  ASP A 702     -14.850 -30.518 -20.375  1.00 95.91           C  
ANISOU 1826  CG  ASP A 702    12684   9888  13868  -3788   3041  -2124       C  
ATOM   1827  OD1 ASP A 702     -15.272 -29.942 -19.351  1.00 97.79           O  
ANISOU 1827  OD1 ASP A 702    12972  10152  14031  -3841   3260  -2066       O  
ATOM   1828  OD2 ASP A 702     -15.291 -30.288 -21.521  1.00 97.48           O  
ANISOU 1828  OD2 ASP A 702    12431  10336  14272  -3757   2816  -2385       O  
ATOM   1829  N   GLU A 703     -10.399 -32.086 -19.290  1.00 71.54           N  
ANISOU 1829  N   GLU A 703    11326   5842  10014  -3193   2667  -1108       N  
ATOM   1830  CA  GLU A 703      -9.550 -32.838 -18.382  1.00 74.37           C  
ANISOU 1830  CA  GLU A 703    12312   5826  10119  -3059   2698   -826       C  
ATOM   1831  C   GLU A 703      -8.533 -31.937 -17.696  1.00 71.72           C  
ANISOU 1831  C   GLU A 703    12195   5505   9550  -2788   2489   -557       C  
ATOM   1832  O   GLU A 703      -7.650 -32.415 -16.986  1.00 73.83           O  
ANISOU 1832  O   GLU A 703    12967   5497   9590  -2585   2402   -320       O  
ATOM   1833  CB  GLU A 703      -8.854 -33.976 -19.122  1.00 79.29           C  
ANISOU 1833  CB  GLU A 703    13127   6204  10796  -2954   2556   -840       C  
ATOM   1834  CG  GLU A 703      -9.808 -35.060 -19.580  1.00 86.20           C  
ANISOU 1834  CG  GLU A 703    13915   6981  11854  -3226   2789  -1071       C  
ATOM   1835  CD  GLU A 703      -9.098 -36.202 -20.267  1.00 92.01           C  
ANISOU 1835  CD  GLU A 703    14875   7454  12631  -3111   2652  -1081       C  
ATOM   1836  OE1 GLU A 703      -9.788 -37.125 -20.750  1.00 96.16           O  
ANISOU 1836  OE1 GLU A 703    15335   7888  13315  -3323   2809  -1279       O  
ATOM   1837  OE2 GLU A 703      -7.851 -36.177 -20.324  1.00 91.90           O  
ANISOU 1837  OE2 GLU A 703    15093   7322  12503  -2799   2385   -910       O  
ATOM   1838  N   ARG A 704      -8.668 -30.631 -17.909  1.00 68.02           N  
ANISOU 1838  N   ARG A 704    11344   5363   9138  -2770   2386   -606       N  
ATOM   1839  CA  ARG A 704      -7.791 -29.652 -17.277  1.00 62.61           C  
ANISOU 1839  CA  ARG A 704    10818   4722   8251  -2540   2194   -377       C  
ATOM   1840  C   ARG A 704      -8.366 -29.181 -15.950  1.00 62.78           C  
ANISOU 1840  C   ARG A 704    11020   4755   8078  -2626   2423   -269       C  
ATOM   1841  O   ARG A 704      -9.575 -28.992 -15.825  1.00 64.84           O  
ANISOU 1841  O   ARG A 704    11021   5162   8453  -2870   2696   -447       O  
ATOM   1842  CB  ARG A 704      -7.573 -28.451 -18.196  1.00 59.62           C  
ANISOU 1842  CB  ARG A 704     9967   4673   8013  -2476   1970   -485       C  
ATOM   1843  CG  ARG A 704      -6.674 -28.730 -19.380  1.00 58.37           C  
ANISOU 1843  CG  ARG A 704     9659   4577   7943  -2244   1662   -547       C  
ATOM   1844  CD  ARG A 704      -6.663 -27.559 -20.344  1.00 54.37           C  
ANISOU 1844  CD  ARG A 704     8591   4547   7520  -2112   1427   -670       C  
ATOM   1845  NE  ARG A 704      -6.467 -28.012 -21.717  1.00 56.90           N  
ANISOU 1845  NE  ARG A 704     8683   4955   7983  -2048   1278   -861       N  
ATOM   1846  CZ  ARG A 704      -6.978 -27.413 -22.785  1.00 54.82           C  
ANISOU 1846  CZ  ARG A 704     7975   5019   7833  -2069   1175  -1075       C  
ATOM   1847  NH1 ARG A 704      -7.714 -26.320 -22.645  1.00 53.21           N  
ANISOU 1847  NH1 ARG A 704     7482   5091   7645  -2135   1189  -1127       N  
ATOM   1848  NH2 ARG A 704      -6.753 -27.908 -23.993  1.00 53.05           N  
ANISOU 1848  NH2 ARG A 704     7631   4834   7692  -2003   1047  -1242       N  
ATOM   1849  N   PRO A 705      -7.494 -28.984 -14.952  1.00 61.53           N  
ANISOU 1849  N   PRO A 705    11307   4445   7627  -2400   2295     -4       N  
ATOM   1850  CA  PRO A 705      -7.912 -28.525 -13.624  1.00 60.02           C  
ANISOU 1850  CA  PRO A 705    11362   4247   7197  -2443   2485     99       C  
ATOM   1851  C   PRO A 705      -8.300 -27.050 -13.622  1.00 59.26           C  
ANISOU 1851  C   PRO A 705    10866   4491   7161  -2482   2474     40       C  
ATOM   1852  O   PRO A 705      -7.879 -26.298 -14.501  1.00 54.94           O  
ANISOU 1852  O   PRO A 705     9965   4152   6759  -2396   2235      2       O  
ATOM   1853  CB  PRO A 705      -6.657 -28.739 -12.776  1.00 60.76           C  
ANISOU 1853  CB  PRO A 705    12011   4106   6969  -2115   2220    373       C  
ATOM   1854  CG  PRO A 705      -5.532 -28.629 -13.746  1.00 60.37           C  
ANISOU 1854  CG  PRO A 705    11809   4083   7045  -1867   1831    405       C  
ATOM   1855  CD  PRO A 705      -6.042 -29.227 -15.025  1.00 59.80           C  
ANISOU 1855  CD  PRO A 705    11384   4049   7288  -2057   1933    181       C  
ATOM   1856  N   SER A 706      -9.104 -26.647 -12.644  1.00 61.88           N  
ANISOU 1856  N   SER A 706    11270   4864   7379  -2611   2743     18       N  
ATOM   1857  CA  SER A 706      -9.469 -25.246 -12.492  1.00 60.30           C  
ANISOU 1857  CA  SER A 706    10741   4961   7210  -2623   2739    -30       C  
ATOM   1858  C   SER A 706      -8.387 -24.509 -11.714  1.00 59.01           C  
ANISOU 1858  C   SER A 706    10901   4768   6750  -2353   2475    225       C  
ATOM   1859  O   SER A 706      -7.624 -25.119 -10.966  1.00 60.86           O  
ANISOU 1859  O   SER A 706    11660   4744   6720  -2180   2365    409       O  
ATOM   1860  CB  SER A 706     -10.823 -25.109 -11.791  1.00 66.52           C  
ANISOU 1860  CB  SER A 706    11446   5796   8032  -2862   3144   -204       C  
ATOM   1861  OG  SER A 706     -10.789 -25.658 -10.483  1.00 73.29           O  
ANISOU 1861  OG  SER A 706    12897   6370   8582  -2862   3339    -76       O  
ATOM   1862  N   PHE A 707      -8.316 -23.196 -11.901  1.00 58.11           N  
ANISOU 1862  N   PHE A 707    10471   4926   6680  -2299   2347    217       N  
ATOM   1863  CA  PHE A 707      -7.317 -22.382 -11.207  1.00 54.99           C  
ANISOU 1863  CA  PHE A 707    10331   4538   6024  -2047   2077    430       C  
ATOM   1864  C   PHE A 707      -7.334 -22.429  -9.673  1.00 57.27           C  
ANISOU 1864  C   PHE A 707    11126   4660   5976  -1983   2177    541       C  
ATOM   1865  O   PHE A 707      -6.273 -22.349  -9.058  1.00 57.71           O  
ANISOU 1865  O   PHE A 707    11540   4605   5781  -1718   1879    719       O  
ATOM   1866  CB  PHE A 707      -7.311 -20.938 -11.725  1.00 49.39           C  
ANISOU 1866  CB  PHE A 707     9156   4180   5431  -2004   1934    375       C  
ATOM   1867  CG  PHE A 707      -6.314 -20.711 -12.818  1.00 46.91           C  
ANISOU 1867  CG  PHE A 707     8500   4074   5249  -1732   1505    362       C  
ATOM   1868  CD1 PHE A 707      -4.959 -20.724 -12.537  1.00 42.51           C  
ANISOU 1868  CD1 PHE A 707     8178   3440   4535  -1427   1147    525       C  
ATOM   1869  CD2 PHE A 707      -6.725 -20.516 -14.126  1.00 45.09           C  
ANISOU 1869  CD2 PHE A 707     7729   4103   5301  -1778   1463    166       C  
ATOM   1870  CE1 PHE A 707      -4.029 -20.539 -13.537  1.00 48.94           C  
ANISOU 1870  CE1 PHE A 707     8665   4433   5496  -1205    815    486       C  
ATOM   1871  CE2 PHE A 707      -5.799 -20.326 -15.138  1.00 43.93           C  
ANISOU 1871  CE2 PHE A 707     7324   4122   5246  -1546   1124    155       C  
ATOM   1872  CZ  PHE A 707      -4.449 -20.339 -14.845  1.00 44.73           C  
ANISOU 1872  CZ  PHE A 707     7636   4145   5215  -1276    830    311       C  
ATOM   1873  N   PRO A 708      -8.522 -22.551  -9.050  1.00 60.00           N  
ANISOU 1873  N   PRO A 708    11495   4981   6320  -2213   2577    406       N  
ATOM   1874  CA  PRO A 708      -8.506 -22.730  -7.594  1.00 64.22           C  
ANISOU 1874  CA  PRO A 708    12587   5301   6512  -2163   2691    496       C  
ATOM   1875  C   PRO A 708      -7.712 -23.962  -7.174  1.00 67.12           C  
ANISOU 1875  C   PRO A 708    13515   5336   6650  -2011   2558    644       C  
ATOM   1876  O   PRO A 708      -6.967 -23.903  -6.200  1.00 66.55           O  
ANISOU 1876  O   PRO A 708    13904   5124   6260  -1790   2358    785       O  
ATOM   1877  CB  PRO A 708      -9.983 -22.922  -7.255  1.00 65.67           C  
ANISOU 1877  CB  PRO A 708    12669   5470   6812  -2478   3193    281       C  
ATOM   1878  CG  PRO A 708     -10.696 -22.145  -8.291  1.00 63.78           C  
ANISOU 1878  CG  PRO A 708    11735   5560   6938  -2608   3238     87       C  
ATOM   1879  CD  PRO A 708      -9.888 -22.308  -9.550  1.00 59.87           C  
ANISOU 1879  CD  PRO A 708    10987   5155   6604  -2492   2904    145       C  
ATOM   1880  N   ARG A 709      -7.871 -25.057  -7.910  1.00 70.09           N  
ANISOU 1880  N   ARG A 709    13849   5591   7193  -2113   2648    591       N  
ATOM   1881  CA  ARG A 709      -7.118 -26.273  -7.637  1.00 75.58           C  
ANISOU 1881  CA  ARG A 709    15051   5968   7698  -1954   2512    720       C  
ATOM   1882  C   ARG A 709      -5.640 -26.064  -7.943  1.00 71.17           C  
ANISOU 1882  C   ARG A 709    14535   5425   7082  -1583   1972    879       C  
ATOM   1883  O   ARG A 709      -4.771 -26.506  -7.190  1.00 72.17           O  
ANISOU 1883  O   ARG A 709    15142   5347   6934  -1322   1725   1009       O  
ATOM   1884  CB  ARG A 709      -7.661 -27.433  -8.471  1.00 82.46           C  
ANISOU 1884  CB  ARG A 709    15807   6722   8803  -2160   2733    603       C  
ATOM   1885  CG  ARG A 709      -9.132 -27.753  -8.233  1.00 90.25           C  
ANISOU 1885  CG  ARG A 709    16713   7683   9894  -2529   3264    400       C  
ATOM   1886  CD  ARG A 709      -9.299 -29.079  -7.500  1.00 99.55           C  
ANISOU 1886  CD  ARG A 709    18493   8478  10852  -2603   3513    435       C  
ATOM   1887  NE  ARG A 709     -10.652 -29.617  -7.629  1.00105.65           N  
ANISOU 1887  NE  ARG A 709    19106   9211  11825  -2976   4013    200       N  
ATOM   1888  CZ  ARG A 709     -10.994 -30.597  -8.462  1.00109.41           C  
ANISOU 1888  CZ  ARG A 709    19435   9606  12532  -3136   4134     84       C  
ATOM   1889  NH1 ARG A 709     -10.082 -31.161  -9.243  1.00107.49           N  
ANISOU 1889  NH1 ARG A 709    19203   9296  12342  -2952   3803    190       N  
ATOM   1890  NH2 ARG A 709     -12.250 -31.021  -8.510  1.00114.19           N  
ANISOU 1890  NH2 ARG A 709    19874  10185  13327  -3475   4586   -160       N  
ATOM   1891  N   ILE A 710      -5.369 -25.393  -9.058  1.00 65.88           N  
ANISOU 1891  N   ILE A 710    13355   4996   6681  -1556   1786    839       N  
ATOM   1892  CA  ILE A 710      -4.006 -25.093  -9.481  1.00 62.00           C  
ANISOU 1892  CA  ILE A 710    12818   4541   6199  -1220   1294    946       C  
ATOM   1893  C   ILE A 710      -3.267 -24.298  -8.413  1.00 60.55           C  
ANISOU 1893  C   ILE A 710    12878   4394   5733   -963   1012   1057       C  
ATOM   1894  O   ILE A 710      -2.135 -24.620  -8.054  1.00 60.83           O  
ANISOU 1894  O   ILE A 710    13179   4305   5629   -637    629   1143       O  
ATOM   1895  CB  ILE A 710      -4.005 -24.283 -10.794  1.00 59.71           C  
ANISOU 1895  CB  ILE A 710    11947   4514   6226  -1286   1215    859       C  
ATOM   1896  CG1 ILE A 710      -4.634 -25.101 -11.925  1.00 59.09           C  
ANISOU 1896  CG1 ILE A 710    11609   4403   6439  -1514   1428    704       C  
ATOM   1897  CG2 ILE A 710      -2.592 -23.835 -11.156  1.00 49.95           C  
ANISOU 1897  CG2 ILE A 710    10618   3351   5009   -924    714    932       C  
ATOM   1898  CD1 ILE A 710      -4.736 -24.352 -13.237  1.00 55.73           C  
ANISOU 1898  CD1 ILE A 710    10519   4338   6317  -1548   1329    537       C  
ATOM   1899  N   LEU A 711      -3.925 -23.263  -7.905  1.00 60.87           N  
ANISOU 1899  N   LEU A 711    12802   4614   5713  -1103   1190   1021       N  
ATOM   1900  CA  LEU A 711      -3.335 -22.388  -6.901  1.00 61.08           C  
ANISOU 1900  CA  LEU A 711    13020   4698   5491   -894    945   1090       C  
ATOM   1901  C   LEU A 711      -2.978 -23.158  -5.634  1.00 68.71           C  
ANISOU 1901  C   LEU A 711    14616   5376   6116   -738    878   1154       C  
ATOM   1902  O   LEU A 711      -1.902 -22.973  -5.070  1.00 70.43           O  
ANISOU 1902  O   LEU A 711    15039   5556   6165   -424    462   1210       O  
ATOM   1903  CB  LEU A 711      -4.293 -21.243  -6.571  1.00 57.38           C  
ANISOU 1903  CB  LEU A 711    12333   4440   5028  -1107   1225   1015       C  
ATOM   1904  CG  LEU A 711      -3.824 -20.246  -5.511  1.00 58.76           C  
ANISOU 1904  CG  LEU A 711    12690   4678   4958   -930   1016   1057       C  
ATOM   1905  CD1 LEU A 711      -2.494 -19.634  -5.918  1.00 57.35           C  
ANISOU 1905  CD1 LEU A 711    12333   4635   4823   -627    492   1114       C  
ATOM   1906  CD2 LEU A 711      -4.871 -19.164  -5.297  1.00 56.81           C  
ANISOU 1906  CD2 LEU A 711    12196   4629   4758  -1152   1332    962       C  
ATOM   1907  N   ALA A 712      -3.883 -24.030  -5.201  1.00 71.58           N  
ANISOU 1907  N   ALA A 712    15279   5531   6388   -959   1283   1121       N  
ATOM   1908  CA  ALA A 712      -3.675 -24.815  -3.990  1.00 75.83           C  
ANISOU 1908  CA  ALA A 712    16487   5754   6569   -847   1284   1176       C  
ATOM   1909  C   ALA A 712      -2.434 -25.704  -4.067  1.00 80.44           C  
ANISOU 1909  C   ALA A 712    17342   6153   7070   -508    851   1259       C  
ATOM   1910  O   ALA A 712      -1.615 -25.703  -3.151  1.00 84.41           O  
ANISOU 1910  O   ALA A 712    18235   6535   7301   -227    528   1304       O  
ATOM   1911  CB  ALA A 712      -4.907 -25.649  -3.682  1.00 76.95           C  
ANISOU 1911  CB  ALA A 712    16872   5697   6669  -1175   1839   1106       C  
ATOM   1912  N   GLU A 713      -2.292 -26.452  -5.158  1.00 80.15           N  
ANISOU 1912  N   GLU A 713    17084   6090   7279   -523    830   1255       N  
ATOM   1913  CA  GLU A 713      -1.155 -27.358  -5.305  1.00 84.89           C  
ANISOU 1913  CA  GLU A 713    17903   6507   7842   -195    436   1309       C  
ATOM   1914  C   GLU A 713       0.179 -26.622  -5.376  1.00 82.27           C  
ANISOU 1914  C   GLU A 713    17361   6341   7556    184   -141   1313       C  
ATOM   1915  O   GLU A 713       1.184 -27.100  -4.856  1.00 83.45           O  
ANISOU 1915  O   GLU A 713    17814   6342   7552    518   -525   1329       O  
ATOM   1916  CB  GLU A 713      -1.332 -28.279  -6.514  1.00 87.68           C  
ANISOU 1916  CB  GLU A 713    18037   6795   8484   -305    560   1279       C  
ATOM   1917  CG  GLU A 713      -1.607 -29.733  -6.138  1.00 97.06           C  
ANISOU 1917  CG  GLU A 713    19749   7625   9505   -358    766   1307       C  
ATOM   1918  CD  GLU A 713      -0.338 -30.527  -5.864  1.00103.79           C  
ANISOU 1918  CD  GLU A 713    20959   8264  10212     60    309   1369       C  
ATOM   1919  OE1 GLU A 713      -0.051 -30.824  -4.683  1.00108.80           O  
ANISOU 1919  OE1 GLU A 713    22163   8693  10481    221    207   1421       O  
ATOM   1920  OE2 GLU A 713       0.368 -30.865  -6.838  1.00103.33           O  
ANISOU 1920  OE2 GLU A 713    20614   8234  10413    235     50   1344       O  
ATOM   1921  N   ILE A 714       0.187 -25.461  -6.020  1.00 79.70           N  
ANISOU 1921  N   ILE A 714    16505   6322   7453    132   -204   1276       N  
ATOM   1922  CA  ILE A 714       1.373 -24.616  -6.018  1.00 80.94           C  
ANISOU 1922  CA  ILE A 714    16426   6659   7667    452   -710   1248       C  
ATOM   1923  C   ILE A 714       1.583 -24.044  -4.621  1.00 88.06           C  
ANISOU 1923  C   ILE A 714    17672   7539   8250    567   -848   1250       C  
ATOM   1924  O   ILE A 714       2.711 -23.941  -4.138  1.00 89.34           O  
ANISOU 1924  O   ILE A 714    17917   7687   8340    901  -1311   1208       O  
ATOM   1925  CB  ILE A 714       1.249 -23.466  -7.020  1.00 74.08           C  
ANISOU 1925  CB  ILE A 714    14955   6106   7086    341   -702   1210       C  
ATOM   1926  CG1 ILE A 714       0.947 -24.011  -8.413  1.00 71.20           C  
ANISOU 1926  CG1 ILE A 714    14287   5735   7031    202   -536   1186       C  
ATOM   1927  CG2 ILE A 714       2.525 -22.650  -7.052  1.00 71.93           C  
ANISOU 1927  CG2 ILE A 714    14412   6015   6904    666  -1219   1152       C  
ATOM   1928  CD1 ILE A 714       0.758 -22.938  -9.454  1.00 65.14           C  
ANISOU 1928  CD1 ILE A 714    12990   5237   6523     77   -505   1142       C  
ATOM   1929  N   GLU A 715       0.482 -23.678  -3.975  1.00 92.60           N  
ANISOU 1929  N   GLU A 715    18428   8102   8654    288   -438   1267       N  
ATOM   1930  CA  GLU A 715       0.533 -23.133  -2.629  1.00 99.15           C  
ANISOU 1930  CA  GLU A 715    19625   8875   9173    362   -502   1258       C  
ATOM   1931  C   GLU A 715       1.024 -24.202  -1.656  1.00104.51           C  
ANISOU 1931  C   GLU A 715    20963   9211   9537    578   -662   1283       C  
ATOM   1932  O   GLU A 715       1.852 -23.928  -0.788  1.00107.32           O  
ANISOU 1932  O   GLU A 715    21566   9510   9701    852  -1040   1250       O  
ATOM   1933  CB  GLU A 715      -0.849 -22.627  -2.214  1.00103.68           C  
ANISOU 1933  CB  GLU A 715    20245   9483   9667      3     32   1248       C  
ATOM   1934  CG  GLU A 715      -0.838 -21.458  -1.247  1.00109.23           C  
ANISOU 1934  CG  GLU A 715    21026  10280  10196     41    -39   1215       C  
ATOM   1935  CD  GLU A 715      -0.415 -20.154  -1.899  1.00110.04           C  
ANISOU 1935  CD  GLU A 715    20547  10729  10534     95   -277   1178       C  
ATOM   1936  OE1 GLU A 715       0.805 -19.921  -2.024  1.00112.65           O  
ANISOU 1936  OE1 GLU A 715    20744  11131  10926    390   -774   1155       O  
ATOM   1937  OE2 GLU A 715      -1.302 -19.357  -2.280  1.00107.48           O  
ANISOU 1937  OE2 GLU A 715    19894  10602  10343   -156     35   1152       O  
ATOM   1938  N   GLU A 716       0.516 -25.421  -1.811  1.00106.98           N  
ANISOU 1938  N   GLU A 716    21565   9285   9797    455   -380   1327       N  
ATOM   1939  CA  GLU A 716       0.924 -26.536  -0.961  1.00113.65           C  
ANISOU 1939  CA  GLU A 716    23085   9772  10324    651   -502   1360       C  
ATOM   1940  C   GLU A 716       2.399 -26.869  -1.142  1.00112.26           C  
ANISOU 1940  C   GLU A 716    22866   9579  10208   1088  -1122   1329       C  
ATOM   1941  O   GLU A 716       3.117 -27.102  -0.172  1.00114.99           O  
ANISOU 1941  O   GLU A 716    23671   9741  10279   1374  -1452   1306       O  
ATOM   1942  CB  GLU A 716       0.078 -27.776  -1.253  1.00119.74           C  
ANISOU 1942  CB  GLU A 716    24116  10302  11076    408    -56   1404       C  
ATOM   1943  CG  GLU A 716      -1.376 -27.662  -0.823  1.00124.44           C  
ANISOU 1943  CG  GLU A 716    24865  10841  11575     -6    575   1387       C  
ATOM   1944  CD  GLU A 716      -2.193 -28.883  -1.202  1.00130.02           C  
ANISOU 1944  CD  GLU A 716    25752  11325  12322   -266   1017   1392       C  
ATOM   1945  OE1 GLU A 716      -3.437 -28.820  -1.111  1.00131.83           O  
ANISOU 1945  OE1 GLU A 716    25950  11550  12589   -641   1561   1332       O  
ATOM   1946  OE2 GLU A 716      -1.590 -29.908  -1.589  1.00131.95           O  
ANISOU 1946  OE2 GLU A 716    26155  11399  12582    -95    821   1436       O  
ATOM   1947  N   LEU A 717       2.841 -26.889  -2.395  1.00108.97           N  
ANISOU 1947  N   LEU A 717    21893   9346  10165   1142  -1277   1304       N  
ATOM   1948  CA  LEU A 717       4.220 -27.220  -2.734  1.00110.76           C  
ANISOU 1948  CA  LEU A 717    21965   9583  10537   1543  -1832   1233       C  
ATOM   1949  C   LEU A 717       5.174 -26.108  -2.307  1.00109.86           C  
ANISOU 1949  C   LEU A 717    21604   9678  10460   1792  -2292   1122       C  
ATOM   1950  O   LEU A 717       6.377 -26.326  -2.152  1.00111.73           O  
ANISOU 1950  O   LEU A 717    21821   9889  10743   2157  -2791   1015       O  
ATOM   1951  CB  LEU A 717       4.334 -27.467  -4.241  1.00108.29           C  
ANISOU 1951  CB  LEU A 717    21097   9407  10640   1499  -1806   1215       C  
ATOM   1952  CG  LEU A 717       5.683 -27.915  -4.801  1.00110.90           C  
ANISOU 1952  CG  LEU A 717    21182   9752  11202   1886  -2305   1111       C  
ATOM   1953  CD1 LEU A 717       6.125 -29.206  -4.126  1.00117.99           C  
ANISOU 1953  CD1 LEU A 717    22678  10304  11847   2127  -2474   1127       C  
ATOM   1954  CD2 LEU A 717       5.605 -28.084  -6.312  1.00107.10           C  
ANISOU 1954  CD2 LEU A 717    20174   9390  11127   1789  -2185   1087       C  
ATOM   1955  N   ALA A 718       4.620 -24.918  -2.103  1.00107.68           N  
ANISOU 1955  N   ALA A 718    21130   9606  10179   1587  -2116   1125       N  
ATOM   1956  CA  ALA A 718       5.410 -23.738  -1.766  1.00107.55           C  
ANISOU 1956  CA  ALA A 718    20826   9806  10231   1763  -2494   1012       C  
ATOM   1957  C   ALA A 718       5.958 -23.770  -0.344  1.00114.01           C  
ANISOU 1957  C   ALA A 718    22183  10427  10710   2007  -2791    956       C  
ATOM   1958  O   ALA A 718       6.910 -23.055  -0.029  1.00113.82           O  
ANISOU 1958  O   ALA A 718    21955  10527  10765   2239  -3220    820       O  
ATOM   1959  CB  ALA A 718       4.590 -22.476  -1.983  1.00102.83           C  
ANISOU 1959  CB  ALA A 718    19889   9465   9717   1464  -2192   1037       C  
ATOM   1960  N   ARG A 719       5.343 -24.585   0.508  1.00121.35           N  
ANISOU 1960  N   ARG A 719    23804  11035  11266   1945  -2551   1046       N  
ATOM   1961  CA  ARG A 719       5.732 -24.688   1.912  1.00131.18           C  
ANISOU 1961  CA  ARG A 719    25682  12033  12129   2166  -2789   1006       C  
ATOM   1962  C   ARG A 719       7.229 -24.921   2.079  1.00135.89           C  
ANISOU 1962  C   ARG A 719    26237  12600  12797   2620  -3453    854       C  
ATOM   1963  O   ARG A 719       7.872 -24.316   2.939  1.00138.73           O  
ANISOU 1963  O   ARG A 719    26722  12950  13040   2832  -3808    741       O  
ATOM   1964  CB  ARG A 719       4.977 -25.830   2.588  1.00138.79           C  
ANISOU 1964  CB  ARG A 719    27417  12609  12707   2066  -2446   1118       C  
ATOM   1965  CG  ARG A 719       3.481 -25.627   2.719  1.00139.64           C  
ANISOU 1965  CG  ARG A 719    27656  12694  12705   1623  -1774   1217       C  
ATOM   1966  CD  ARG A 719       2.867 -26.838   3.403  1.00147.12           C  
ANISOU 1966  CD  ARG A 719    29385  13230  13285   1544  -1451   1295       C  
ATOM   1967  NE  ARG A 719       1.415 -26.756   3.518  1.00147.81           N  
ANISOU 1967  NE  ARG A 719    29578  13276  13307   1105   -771   1349       N  
ATOM   1968  CZ  ARG A 719       0.656 -27.720   4.030  1.00152.91           C  
ANISOU 1968  CZ  ARG A 719    30838  13583  13678    936   -354   1400       C  
ATOM   1969  NH1 ARG A 719       1.212 -28.840   4.472  1.00158.02           N  
ANISOU 1969  NH1 ARG A 719    32095  13890  14055   1181   -559   1430       N  
ATOM   1970  NH2 ARG A 719      -0.660 -27.567   4.099  1.00152.93           N  
ANISOU 1970  NH2 ARG A 719    30844  13577  13685    526    271   1402       N  
ATOM   1971  N   GLU A 720       7.771 -25.805   1.249  1.00136.76           N  
ANISOU 1971  N   GLU A 720    26156  12688  13117   2770  -3615    832       N  
ATOM   1972  CA  GLU A 720       9.187 -26.145   1.287  1.00140.38           C  
ANISOU 1972  CA  GLU A 720    26514  13122  13702   3204  -4226    656       C  
ATOM   1973  C   GLU A 720      10.061 -24.922   1.035  1.00137.69           C  
ANISOU 1973  C   GLU A 720    25500  13114  13701   3320  -4585    463       C  
ATOM   1974  O   GLU A 720      11.003 -24.974   0.246  1.00136.68           O  
ANISOU 1974  O   GLU A 720    24835  13148  13950   3509  -4894    309       O  
ATOM   1975  CB  GLU A 720       9.487 -27.223   0.248  1.00140.62           C  
ANISOU 1975  CB  GLU A 720    26350  13112  13968   3291  -4251    664       C  
ATOM   1976  CG  GLU A 720       8.640 -28.472   0.399  1.00144.74           C  
ANISOU 1976  CG  GLU A 720    27501  13299  14193   3157  -3876    845       C  
ATOM   1977  CD  GLU A 720       8.810 -29.430  -0.759  1.00145.66           C  
ANISOU 1977  CD  GLU A 720    27357  13398  14588   3188  -3837    864       C  
ATOM   1978  OE1 GLU A 720       9.303 -28.996  -1.822  1.00142.54           O  
ANISOU 1978  OE1 GLU A 720    26240  13287  14633   3216  -3965    766       O  
ATOM   1979  OE2 GLU A 720       8.453 -30.618  -0.608  1.00149.39           O  
ANISOU 1979  OE2 GLU A 720    28361  13559  14843   3181  -3665    968       O  
TER    1980      GLU A 720                                                      
ATOM   1981  N   ASP B 448     -18.122  -3.243 -10.645  1.00102.75           N  
ANISOU 1981  N   ASP B 448    13481  13716  11843  -2826   -910   -618       N  
ATOM   1982  CA  ASP B 448     -18.769  -2.064 -10.084  1.00102.62           C  
ANISOU 1982  CA  ASP B 448    12967  13926  12098  -2617  -1068   -621       C  
ATOM   1983  C   ASP B 448     -19.144  -2.290  -8.624  1.00 99.27           C  
ANISOU 1983  C   ASP B 448    12253  13619  11845  -2610   -776   -680       C  
ATOM   1984  O   ASP B 448     -19.340  -1.338  -7.869  1.00 99.04           O  
ANISOU 1984  O   ASP B 448    11869  13739  12022  -2376   -771   -704       O  
ATOM   1985  CB  ASP B 448     -20.011  -1.692 -10.895  1.00108.62           C  
ANISOU 1985  CB  ASP B 448    13429  14862  12981  -2767  -1485   -676       C  
ATOM   1986  CG  ASP B 448     -20.610  -0.368 -10.466  1.00110.14           C  
ANISOU 1986  CG  ASP B 448    13110  15240  13497  -2488  -1697   -693       C  
ATOM   1987  OD1 ASP B 448     -21.475  -0.370  -9.563  1.00111.99           O  
ANISOU 1987  OD1 ASP B 448    12900  15669  13984  -2513  -1593   -818       O  
ATOM   1988  OD2 ASP B 448     -20.211   0.675 -11.028  1.00108.74           O  
ANISOU 1988  OD2 ASP B 448    12985  15005  13326  -2253  -1957   -594       O  
ATOM   1989  N   ASP B 449     -19.248  -3.552  -8.226  1.00 96.30           N  
ANISOU 1989  N   ASP B 449    12054  13166  11370  -2890   -529   -710       N  
ATOM   1990  CA  ASP B 449     -19.513  -3.869  -6.829  1.00 92.79           C  
ANISOU 1990  CA  ASP B 449    11426  12817  11012  -2947   -227   -739       C  
ATOM   1991  C   ASP B 449     -18.370  -4.674  -6.220  1.00 85.31           C  
ANISOU 1991  C   ASP B 449    10920  11611   9884  -2915     77   -629       C  
ATOM   1992  O   ASP B 449     -17.940  -5.688  -6.771  1.00 83.97           O  
ANISOU 1992  O   ASP B 449    11159  11195   9551  -3073    123   -601       O  
ATOM   1993  CB  ASP B 449     -20.847  -4.596  -6.665  1.00 97.30           C  
ANISOU 1993  CB  ASP B 449    11741  13562  11667  -3351   -212   -861       C  
ATOM   1994  CG  ASP B 449     -21.560  -4.206  -5.386  1.00100.28           C  
ANISOU 1994  CG  ASP B 449    11654  14215  12232  -3359    -19   -956       C  
ATOM   1995  OD1 ASP B 449     -21.220  -3.144  -4.819  1.00 98.59           O  
ANISOU 1995  OD1 ASP B 449    11240  14088  12130  -3018      9   -958       O  
ATOM   1996  OD2 ASP B 449     -22.461  -4.954  -4.951  1.00103.86           O  
ANISOU 1996  OD2 ASP B 449    11947  14803  12714  -3728    120  -1044       O  
ATOM   1997  N   TRP B 450     -17.882  -4.209  -5.076  1.00 77.99           N  
ANISOU 1997  N   TRP B 450     9906  10731   8997  -2702    268   -578       N  
ATOM   1998  CA  TRP B 450     -16.692  -4.787  -4.469  1.00 70.74           C  
ANISOU 1998  CA  TRP B 450     9373   9570   7936  -2601    490   -449       C  
ATOM   1999  C   TRP B 450     -16.998  -5.582  -3.209  1.00 72.10           C  
ANISOU 1999  C   TRP B 450     9574   9759   8062  -2832    746   -414       C  
ATOM   2000  O   TRP B 450     -16.122  -5.808  -2.375  1.00 71.46           O  
ANISOU 2000  O   TRP B 450     9716   9541   7896  -2715    906   -291       O  
ATOM   2001  CB  TRP B 450     -15.672  -3.688  -4.189  1.00 63.04           C  
ANISOU 2001  CB  TRP B 450     8369   8595   6988  -2194    479   -382       C  
ATOM   2002  CG  TRP B 450     -15.279  -2.975  -5.433  1.00 59.97           C  
ANISOU 2002  CG  TRP B 450     8027   8161   6599  -2017    243   -386       C  
ATOM   2003  CD1 TRP B 450     -15.685  -1.738  -5.834  1.00 58.64           C  
ANISOU 2003  CD1 TRP B 450     7561   8161   6560  -1860     15   -429       C  
ATOM   2004  CD2 TRP B 450     -14.422  -3.473  -6.467  1.00 56.77           C  
ANISOU 2004  CD2 TRP B 450     8010   7516   6043  -2006    212   -351       C  
ATOM   2005  NE1 TRP B 450     -15.120  -1.428  -7.047  1.00 57.24           N  
ANISOU 2005  NE1 TRP B 450     7595   7866   6287  -1781   -169   -388       N  
ATOM   2006  CE2 TRP B 450     -14.340  -2.479  -7.456  1.00 55.60           C  
ANISOU 2006  CE2 TRP B 450     7798   7430   5897  -1877    -27   -358       C  
ATOM   2007  CE3 TRP B 450     -13.709  -4.663  -6.645  1.00 55.15           C  
ANISOU 2007  CE3 TRP B 450     8205   7038   5711  -2090    369   -326       C  
ATOM   2008  CZ2 TRP B 450     -13.574  -2.634  -8.606  1.00 55.14           C  
ANISOU 2008  CZ2 TRP B 450     8066   7211   5674  -1872    -80   -348       C  
ATOM   2009  CZ3 TRP B 450     -12.950  -4.816  -7.784  1.00 54.56           C  
ANISOU 2009  CZ3 TRP B 450     8417   6796   5518  -2044    326   -351       C  
ATOM   2010  CH2 TRP B 450     -12.887  -3.809  -8.751  1.00 55.10           C  
ANISOU 2010  CH2 TRP B 450     8418   6971   5547  -1956    120   -366       C  
ATOM   2011  N   GLU B 451     -18.246  -6.010  -3.076  1.00 73.48           N  
ANISOU 2011  N   GLU B 451     9527  10106   8284  -3186    773   -515       N  
ATOM   2012  CA  GLU B 451     -18.627  -6.839  -1.948  1.00 75.42           C  
ANISOU 2012  CA  GLU B 451     9833  10375   8447  -3497   1026   -477       C  
ATOM   2013  C   GLU B 451     -18.124  -8.259  -2.148  1.00 74.68           C  
ANISOU 2013  C   GLU B 451    10277   9902   8196  -3705   1088   -355       C  
ATOM   2014  O   GLU B 451     -18.499  -8.933  -3.106  1.00 76.22           O  
ANISOU 2014  O   GLU B 451    10606   9973   8380  -3920    980   -414       O  
ATOM   2015  CB  GLU B 451     -20.141  -6.844  -1.757  1.00 81.04           C  
ANISOU 2015  CB  GLU B 451    10103  11417   9273  -3844   1059   -647       C  
ATOM   2016  CG  GLU B 451     -20.605  -7.846  -0.721  1.00 87.00           C  
ANISOU 2016  CG  GLU B 451    10970  12188   9897  -4274   1335   -606       C  
ATOM   2017  CD  GLU B 451     -21.651  -7.274   0.204  1.00 93.49           C  
ANISOU 2017  CD  GLU B 451    11267  13438  10818  -4434   1514   -772       C  
ATOM   2018  OE1 GLU B 451     -21.946  -7.918   1.233  1.00 97.29           O  
ANISOU 2018  OE1 GLU B 451    11835  13979  11150  -4782   1784   -732       O  
ATOM   2019  OE2 GLU B 451     -22.174  -6.179  -0.095  1.00 94.58           O  
ANISOU 2019  OE2 GLU B 451    10910  13843  11184  -4217   1386   -949       O  
ATOM   2020  N   ILE B 452     -17.263  -8.703  -1.241  1.00 71.58           N  
ANISOU 2020  N   ILE B 452    10200   9309   7689  -3636   1242   -188       N  
ATOM   2021  CA  ILE B 452     -16.770 -10.069  -1.264  1.00 71.07           C  
ANISOU 2021  CA  ILE B 452    10652   8839   7514  -3808   1294    -60       C  
ATOM   2022  C   ILE B 452     -17.673 -10.939  -0.407  1.00 79.03           C  
ANISOU 2022  C   ILE B 452    11709   9890   8429  -4301   1459    -18       C  
ATOM   2023  O   ILE B 452     -17.733 -10.758   0.808  1.00 81.96           O  
ANISOU 2023  O   ILE B 452    12014  10411   8716  -4370   1616     66       O  
ATOM   2024  CB  ILE B 452     -15.346 -10.154  -0.705  1.00 64.11           C  
ANISOU 2024  CB  ILE B 452    10094   7685   6580  -3474   1328    124       C  
ATOM   2025  CG1 ILE B 452     -14.409  -9.251  -1.507  1.00 58.71           C  
ANISOU 2025  CG1 ILE B 452     9342   6987   5980  -3017   1198     76       C  
ATOM   2026  CG2 ILE B 452     -14.862 -11.598  -0.702  1.00 63.35           C  
ANISOU 2026  CG2 ILE B 452    10527   7124   6420  -3623   1353    253       C  
ATOM   2027  CD1 ILE B 452     -12.986  -9.243  -1.006  1.00 55.11           C  
ANISOU 2027  CD1 ILE B 452     9124   6304   5511  -2671   1218    231       C  
ATOM   2028  N   PRO B 453     -18.391 -11.878  -1.040  1.00 83.91           N  
ANISOU 2028  N   PRO B 453    12455  10389   9038  -4683   1430    -85       N  
ATOM   2029  CA  PRO B 453     -19.275 -12.792  -0.309  1.00 88.80           C  
ANISOU 2029  CA  PRO B 453    13153  11029   9560  -5223   1590    -43       C  
ATOM   2030  C   PRO B 453     -18.518 -13.578   0.755  1.00 91.12           C  
ANISOU 2030  C   PRO B 453    13925  11001   9696  -5275   1710    215       C  
ATOM   2031  O   PRO B 453     -17.481 -14.176   0.456  1.00 88.93           O  
ANISOU 2031  O   PRO B 453    14094  10279   9417  -5057   1621    337       O  
ATOM   2032  CB  PRO B 453     -19.781 -13.728  -1.406  1.00 90.23           C  
ANISOU 2032  CB  PRO B 453    13523  10998   9761  -5532   1481   -140       C  
ATOM   2033  CG  PRO B 453     -19.759 -12.885  -2.634  1.00 87.48           C  
ANISOU 2033  CG  PRO B 453    12913  10790   9536  -5237   1270   -310       C  
ATOM   2034  CD  PRO B 453     -18.512 -12.053  -2.498  1.00 83.72           C  
ANISOU 2034  CD  PRO B 453    12481  10251   9079  -4677   1242   -222       C  
ATOM   2035  N   ASP B 454     -19.030 -13.569   1.982  1.00 96.56           N  
ANISOU 2035  N   ASP B 454    14504  11922  10262  -5516   1883    278       N  
ATOM   2036  CA  ASP B 454     -18.314 -14.196   3.087  1.00 99.28           C  
ANISOU 2036  CA  ASP B 454    15252  12019  10452  -5441   1902    519       C  
ATOM   2037  C   ASP B 454     -18.210 -15.704   2.931  1.00 96.25           C  
ANISOU 2037  C   ASP B 454    15368  11176  10028  -5612   1810    636       C  
ATOM   2038  O   ASP B 454     -19.098 -16.351   2.377  1.00 97.37           O  
ANISOU 2038  O   ASP B 454    15490  11316  10191  -5931   1804    517       O  
ATOM   2039  CB  ASP B 454     -18.923 -13.856   4.450  1.00108.25           C  
ANISOU 2039  CB  ASP B 454    16155  13531  11444  -5604   2067    518       C  
ATOM   2040  CG  ASP B 454     -18.017 -14.274   5.600  1.00114.21           C  
ANISOU 2040  CG  ASP B 454    17308  14056  12032  -5479   2033    781       C  
ATOM   2041  OD1 ASP B 454     -16.815 -14.503   5.335  1.00115.02           O  
ANISOU 2041  OD1 ASP B 454    17750  13771  12180  -5162   1883    949       O  
ATOM   2042  OD2 ASP B 454     -18.496 -14.366   6.748  1.00116.94           O  
ANISOU 2042  OD2 ASP B 454    17618  14606  12207  -5695   2145    808       O  
ATOM   2043  N   GLY B 455     -17.114 -16.253   3.443  1.00 92.51           N  
ANISOU 2043  N   GLY B 455    15325  10314   9509  -5386   1721    866       N  
ATOM   2044  CA  GLY B 455     -16.826 -17.667   3.313  1.00 93.18           C  
ANISOU 2044  CA  GLY B 455    15902   9903   9597  -5466   1607    987       C  
ATOM   2045  C   GLY B 455     -15.687 -17.888   2.339  1.00 89.78           C  
ANISOU 2045  C   GLY B 455    15748   9027   9338  -5088   1471    992       C  
ATOM   2046  O   GLY B 455     -15.081 -18.958   2.304  1.00 90.45           O  
ANISOU 2046  O   GLY B 455    16254   8637   9476  -5001   1358   1106       O  
ATOM   2047  N   GLN B 456     -15.404 -16.866   1.538  1.00 85.75           N  
ANISOU 2047  N   GLN B 456    14990   8666   8923  -4862   1487    852       N  
ATOM   2048  CA  GLN B 456     -14.278 -16.906   0.619  1.00 81.39           C  
ANISOU 2048  CA  GLN B 456    14664   7738   8522  -4483   1395    820       C  
ATOM   2049  C   GLN B 456     -13.017 -16.444   1.339  1.00 78.64           C  
ANISOU 2049  C   GLN B 456    14399   7283   8197  -4056   1349   1014       C  
ATOM   2050  O   GLN B 456     -11.907 -16.869   1.013  1.00 79.04           O  
ANISOU 2050  O   GLN B 456    14731   6916   8385  -3715   1253   1060       O  
ATOM   2051  CB  GLN B 456     -14.548 -16.020  -0.596  1.00 78.81           C  
ANISOU 2051  CB  GLN B 456    13993   7677   8275  -4379   1389    557       C  
ATOM   2052  CG  GLN B 456     -15.812 -16.365  -1.363  1.00 83.06           C  
ANISOU 2052  CG  GLN B 456    14423   8344   8791  -4832   1400    366       C  
ATOM   2053  CD  GLN B 456     -15.897 -15.617  -2.677  1.00 83.57           C  
ANISOU 2053  CD  GLN B 456    14205   8614   8932  -4636   1304    120       C  
ATOM   2054  OE1 GLN B 456     -14.877 -15.352  -3.313  1.00 83.51           O  
ANISOU 2054  OE1 GLN B 456    14291   8447   8992  -4225   1245     71       O  
ATOM   2055  NE2 GLN B 456     -17.109 -15.257  -3.084  1.00 84.07           N  
ANISOU 2055  NE2 GLN B 456    13915   9043   8984  -4943   1278    -33       N  
ATOM   2056  N   ILE B 457     -13.197 -15.586   2.338  1.00 76.29           N  
ANISOU 2056  N   ILE B 457    13835   7376   7774  -4069   1415   1106       N  
ATOM   2057  CA  ILE B 457     -12.066 -15.005   3.048  1.00 76.44           C  
ANISOU 2057  CA  ILE B 457    13866   7384   7796  -3669   1351   1269       C  
ATOM   2058  C   ILE B 457     -11.633 -15.827   4.257  1.00 81.87           C  
ANISOU 2058  C   ILE B 457    14856   7847   8403  -3680   1242   1532       C  
ATOM   2059  O   ILE B 457     -12.412 -16.058   5.180  1.00 73.68           O  
ANISOU 2059  O   ILE B 457    13783   7020   7193  -4008   1297   1594       O  
ATOM   2060  CB  ILE B 457     -12.373 -13.578   3.523  1.00 76.38           C  
ANISOU 2060  CB  ILE B 457    13366   7944   7713  -3581   1435   1183       C  
ATOM   2061  CG1 ILE B 457     -13.052 -12.773   2.414  1.00 76.56           C  
ANISOU 2061  CG1 ILE B 457    12958   8285   7846  -3540   1466    886       C  
ATOM   2062  CG2 ILE B 457     -11.095 -12.894   3.987  1.00 74.75           C  
ANISOU 2062  CG2 ILE B 457    13131   7726   7546  -3105   1335   1294       C  
ATOM   2063  CD1 ILE B 457     -13.326 -11.329   2.795  1.00 74.13           C  
ANISOU 2063  CD1 ILE B 457    12165   8479   7523  -3399   1523    779       C  
ATOM   2064  N   THR B 458     -10.376 -16.252   4.251  1.00 83.57           N  
ANISOU 2064  N   THR B 458    15342   7651   8759  -3304   1077   1669       N  
ATOM   2065  CA  THR B 458      -9.815 -16.995   5.371  1.00 87.37           C  
ANISOU 2065  CA  THR B 458    16090   7906   9202  -3252    910   1934       C  
ATOM   2066  C   THR B 458      -8.920 -16.101   6.221  1.00 87.15           C  
ANISOU 2066  C   THR B 458    15937   8053   9124  -2949    828   2082       C  
ATOM   2067  O   THR B 458      -7.736 -15.941   5.928  1.00 85.77           O  
ANISOU 2067  O   THR B 458    15809   7646   9132  -2516    699   2125       O  
ATOM   2068  CB  THR B 458      -8.994 -18.193   4.883  1.00 90.87           C  
ANISOU 2068  CB  THR B 458    16894   7748   9883  -3020    735   1990       C  
ATOM   2069  OG1 THR B 458      -9.817 -19.030   4.062  1.00 94.79           O  
ANISOU 2069  OG1 THR B 458    17521   8080  10415  -3309    808   1830       O  
ATOM   2070  CG2 THR B 458      -8.468 -18.998   6.062  1.00 94.42           C  
ANISOU 2070  CG2 THR B 458    17611   7958  10306  -2988    526   2286       C  
ATOM   2071  N   VAL B 459      -9.492 -15.524   7.273  1.00 88.68           N  
ANISOU 2071  N   VAL B 459    15957   8663   9073  -3181    908   2133       N  
ATOM   2072  CA  VAL B 459      -8.752 -14.630   8.161  1.00 86.19           C  
ANISOU 2072  CA  VAL B 459    15515   8566   8669  -2951    838   2249       C  
ATOM   2073  C   VAL B 459      -7.700 -15.399   8.953  1.00 87.20           C  
ANISOU 2073  C   VAL B 459    15952   8341   8841  -2754    562   2530       C  
ATOM   2074  O   VAL B 459      -7.795 -16.614   9.105  1.00 90.27           O  
ANISOU 2074  O   VAL B 459    16646   8390   9262  -2893    455   2652       O  
ATOM   2075  CB  VAL B 459      -9.693 -13.891   9.129  1.00 86.04           C  
ANISOU 2075  CB  VAL B 459    15245   9072   8376  -3273   1013   2186       C  
ATOM   2076  CG1 VAL B 459     -10.791 -13.180   8.352  1.00 81.02           C  
ANISOU 2076  CG1 VAL B 459    14252   8785   7749  -3458   1261   1897       C  
ATOM   2077  CG2 VAL B 459     -10.297 -14.866  10.129  1.00 94.51           C  
ANISOU 2077  CG2 VAL B 459    16558  10094   9258  -3661    994   2325       C  
ATOM   2078  N   GLY B 460      -6.698 -14.685   9.453  1.00 85.26           N  
ANISOU 2078  N   GLY B 460    15614   8176   8604  -2432    431   2632       N  
ATOM   2079  CA  GLY B 460      -5.594 -15.319  10.150  1.00 89.08           C  
ANISOU 2079  CA  GLY B 460    16331   8342   9174  -2196    130   2893       C  
ATOM   2080  C   GLY B 460      -5.056 -14.492  11.300  1.00 91.00           C  
ANISOU 2080  C   GLY B 460    16458   8883   9237  -2117     29   3020       C  
ATOM   2081  O   GLY B 460      -5.816 -13.842  12.016  1.00 91.84           O  
ANISOU 2081  O   GLY B 460    16428   9408   9059  -2412    194   2959       O  
ATOM   2082  N   GLN B 461      -3.737 -14.512  11.466  1.00 92.79           N  
ANISOU 2082  N   GLN B 461    16715   8894   9646  -1712   -239   3168       N  
ATOM   2083  CA  GLN B 461      -3.077 -13.853  12.590  1.00 96.64           C  
ANISOU 2083  CA  GLN B 461    17126   9613   9977  -1626   -396   3311       C  
ATOM   2084  C   GLN B 461      -3.334 -12.351  12.641  1.00 90.82           C  
ANISOU 2084  C   GLN B 461    16058   9378   9071  -1641   -198   3125       C  
ATOM   2085  O   GLN B 461      -3.282 -11.668  11.618  1.00 87.32           O  
ANISOU 2085  O   GLN B 461    15403   9003   8771  -1449    -68   2934       O  
ATOM   2086  CB  GLN B 461      -1.574 -14.116  12.535  1.00103.70           C  
ANISOU 2086  CB  GLN B 461    18038  10187  11177  -1143   -724   3460       C  
ATOM   2087  CG  GLN B 461      -0.989 -13.964  11.145  1.00106.78           C  
ANISOU 2087  CG  GLN B 461    18272  10366  11935   -744   -689   3279       C  
ATOM   2088  CD  GLN B 461       0.504 -14.208  11.113  1.00113.20           C  
ANISOU 2088  CD  GLN B 461    19023  10895  13095   -252   -992   3381       C  
ATOM   2089  OE1 GLN B 461       1.187 -14.076  12.129  1.00117.25           O  
ANISOU 2089  OE1 GLN B 461    19519  11486  13544   -176  -1229   3573       O  
ATOM   2090  NE2 GLN B 461       1.021 -14.567   9.943  1.00113.18           N  
ANISOU 2090  NE2 GLN B 461    18963  10571  13469     82   -976   3223       N  
ATOM   2091  N   ARG B 462      -3.612 -11.846  13.840  1.00 90.61           N  
ANISOU 2091  N   ARG B 462    16004   9688   8735  -1875   -173   3169       N  
ATOM   2092  CA  ARG B 462      -3.843 -10.420  14.042  1.00 87.36           C  
ANISOU 2092  CA  ARG B 462    15283   9748   8163  -1891      6   2978       C  
ATOM   2093  C   ARG B 462      -2.524  -9.653  14.013  1.00 83.79           C  
ANISOU 2093  C   ARG B 462    14687   9306   7842  -1472   -204   3026       C  
ATOM   2094  O   ARG B 462      -1.508 -10.137  14.508  1.00 84.63           O  
ANISOU 2094  O   ARG B 462    14933   9188   8034  -1279   -510   3246       O  
ATOM   2095  CB  ARG B 462      -4.572 -10.175  15.365  1.00 91.48           C  
ANISOU 2095  CB  ARG B 462    15835  10601   8320  -2283    117   2969       C  
ATOM   2096  CG  ARG B 462      -4.931  -8.716  15.611  1.00 90.28           C  
ANISOU 2096  CG  ARG B 462    15354  10927   8021  -2314    333   2719       C  
ATOM   2097  CD  ARG B 462      -5.521  -8.507  16.998  1.00 95.64           C  
ANISOU 2097  CD  ARG B 462    16088  11896   8355  -2676    432   2693       C  
ATOM   2098  NE  ARG B 462      -6.938  -8.852  17.058  1.00100.04           N  
ANISOU 2098  NE  ARG B 462    16621  12594   8794  -3082    718   2538       N  
ATOM   2099  CZ  ARG B 462      -7.519  -9.447  18.096  1.00105.43           C  
ANISOU 2099  CZ  ARG B 462    17520  13326   9215  -3474    759   2610       C  
ATOM   2100  NH1 ARG B 462      -6.800  -9.773  19.162  1.00108.55           N  
ANISOU 2100  NH1 ARG B 462    18193  13626   9423  -3516    519   2848       N  
ATOM   2101  NH2 ARG B 462      -8.816  -9.722  18.065  1.00106.53           N  
ANISOU 2101  NH2 ARG B 462    17593  13610   9274  -3837   1029   2442       N  
ATOM   2102  N   ILE B 463      -2.546  -8.457  13.432  1.00 79.82           N  
ANISOU 2102  N   ILE B 463    13895   9069   7365  -1335    -51   2813       N  
ATOM   2103  CA  ILE B 463      -1.334  -7.657  13.268  1.00 78.81           C  
ANISOU 2103  CA  ILE B 463    13608   8964   7372   -949   -231   2825       C  
ATOM   2104  C   ILE B 463      -1.348  -6.401  14.138  1.00 76.96           C  
ANISOU 2104  C   ILE B 463    13189   9164   6887  -1036   -176   2726       C  
ATOM   2105  O   ILE B 463      -0.298  -5.919  14.566  1.00 77.82           O  
ANISOU 2105  O   ILE B 463    13236   9311   7019   -819   -400   2808       O  
ATOM   2106  CB  ILE B 463      -1.127  -7.280  11.785  1.00 78.43           C  
ANISOU 2106  CB  ILE B 463    13349   8829   7623   -646   -127   2623       C  
ATOM   2107  CG1 ILE B 463      -0.956  -8.544  10.946  1.00 80.13           C  
ANISOU 2107  CG1 ILE B 463    13758   8578   8109   -522   -193   2690       C  
ATOM   2108  CG2 ILE B 463       0.076  -6.359  11.602  1.00 77.28           C  
ANISOU 2108  CG2 ILE B 463    12902   8786   7675   -250   -269   2545       C  
ATOM   2109  CD1 ILE B 463      -1.775  -8.535   9.689  1.00 78.97           C  
ANISOU 2109  CD1 ILE B 463    13444   8454   8106   -562     75   2412       C  
ATOM   2110  N   GLY B 464      -2.538  -5.876  14.409  1.00 75.07           N  
ANISOU 2110  N   GLY B 464    12839   9250   6432  -1350    121   2524       N  
ATOM   2111  CA  GLY B 464      -2.660  -4.697  15.244  1.00 75.21           C  
ANISOU 2111  CA  GLY B 464    12685   9662   6230  -1441    211   2374       C  
ATOM   2112  C   GLY B 464      -3.838  -3.820  14.877  1.00 75.98           C  
ANISOU 2112  C   GLY B 464    12509  10082   6278  -1597    564   2042       C  
ATOM   2113  O   GLY B 464      -4.699  -4.213  14.092  1.00 77.11           O  
ANISOU 2113  O   GLY B 464    12604  10175   6519  -1701    743   1944       O  
ATOM   2114  N   SER B 465      -3.867  -2.622  15.454  1.00 75.53           N  
ANISOU 2114  N   SER B 465    12261  10347   6092  -1605    649   1854       N  
ATOM   2115  CA  SER B 465      -4.946  -1.671  15.218  1.00 72.83           C  
ANISOU 2115  CA  SER B 465    11611  10313   5748  -1708    964   1504       C  
ATOM   2116  C   SER B 465      -4.401  -0.312  14.784  1.00 72.16           C  
ANISOU 2116  C   SER B 465    11275  10381   5762  -1438    950   1322       C  
ATOM   2117  O   SER B 465      -3.504   0.237  15.421  1.00 72.11           O  
ANISOU 2117  O   SER B 465    11314  10431   5653  -1340    783   1380       O  
ATOM   2118  CB  SER B 465      -5.798  -1.515  16.479  1.00 72.00           C  
ANISOU 2118  CB  SER B 465    11500  10455   5402  -2034   1141   1369       C  
ATOM   2119  OG  SER B 465      -6.431  -2.735  16.826  1.00 73.48           O  
ANISOU 2119  OG  SER B 465    11901  10520   5497  -2325   1178   1508       O  
ATOM   2120  N   GLY B 466      -4.946   0.224  13.695  1.00 71.20           N  
ANISOU 2120  N   GLY B 466    10828  10288   5937  -1272   1078   1075       N  
ATOM   2121  CA  GLY B 466      -4.529   1.520  13.189  1.00 69.44           C  
ANISOU 2121  CA  GLY B 466    10304  10147   5934   -971   1038    867       C  
ATOM   2122  C   GLY B 466      -5.477   2.635  13.591  1.00 72.00           C  
ANISOU 2122  C   GLY B 466    10374  10778   6204  -1078   1271    530       C  
ATOM   2123  O   GLY B 466      -6.058   2.600  14.679  1.00 74.39           O  
ANISOU 2123  O   GLY B 466    10767  11291   6206  -1382   1440    467       O  
ATOM   2124  N   SER B 467      -5.632   3.626  12.714  1.00 69.23           N  
ANISOU 2124  N   SER B 467     9714  10443   6146   -834   1280    307       N  
ATOM   2125  CA  SER B 467      -6.527   4.752  12.977  1.00 71.21           C  
ANISOU 2125  CA  SER B 467     9686  10932   6437   -864   1471    -42       C  
ATOM   2126  C   SER B 467      -7.953   4.274  13.226  1.00 73.33           C  
ANISOU 2126  C   SER B 467     9862  11373   6628  -1158   1743   -191       C  
ATOM   2127  O   SER B 467      -8.624   4.745  14.143  1.00 74.96           O  
ANISOU 2127  O   SER B 467     9976  11835   6671  -1349   1965   -422       O  
ATOM   2128  CB  SER B 467      -6.506   5.749  11.819  1.00 70.52           C  
ANISOU 2128  CB  SER B 467     9318  10760   6716   -550   1380   -203       C  
ATOM   2129  OG  SER B 467      -5.221   6.313  11.650  1.00 71.48           O  
ANISOU 2129  OG  SER B 467     9498  10763   6899   -324   1168   -101       O  
ATOM   2130  N   PHE B 468      -8.408   3.339  12.397  1.00 72.28           N  
ANISOU 2130  N   PHE B 468     9743  11108   6612  -1209   1739    -83       N  
ATOM   2131  CA  PHE B 468      -9.690   2.678  12.614  1.00 72.53           C  
ANISOU 2131  CA  PHE B 468     9712  11289   6558  -1539   1982   -179       C  
ATOM   2132  C   PHE B 468      -9.579   1.193  12.273  1.00 69.60           C  
ANISOU 2132  C   PHE B 468     9640  10695   6111  -1702   1910    123       C  
ATOM   2133  O   PHE B 468      -8.776   0.804  11.427  1.00 66.55           O  
ANISOU 2133  O   PHE B 468     9376  10032   5878  -1476   1691    312       O  
ATOM   2134  CB  PHE B 468     -10.808   3.354  11.807  1.00 72.15           C  
ANISOU 2134  CB  PHE B 468     9229  11355   6832  -1442   2080   -494       C  
ATOM   2135  CG  PHE B 468     -10.603   3.307  10.316  1.00 71.02           C  
ANISOU 2135  CG  PHE B 468     9006  10975   7001  -1177   1860   -417       C  
ATOM   2136  CD1 PHE B 468      -9.813   4.252   9.679  1.00 68.96           C  
ANISOU 2136  CD1 PHE B 468     8675  10591   6937   -827   1658   -429       C  
ATOM   2137  CD2 PHE B 468     -11.212   2.325   9.551  1.00 71.92           C  
ANISOU 2137  CD2 PHE B 468     9139  10999   7189  -1317   1864   -342       C  
ATOM   2138  CE1 PHE B 468      -9.626   4.212   8.306  1.00 67.21           C  
ANISOU 2138  CE1 PHE B 468     8414  10173   6951   -633   1474   -360       C  
ATOM   2139  CE2 PHE B 468     -11.030   2.278   8.178  1.00 69.60           C  
ANISOU 2139  CE2 PHE B 468     8804  10505   7136  -1109   1670   -287       C  
ATOM   2140  CZ  PHE B 468     -10.236   3.224   7.555  1.00 67.18           C  
ANISOU 2140  CZ  PHE B 468     8438  10091   6995   -772   1481   -294       C  
ATOM   2141  N   GLY B 469     -10.367   0.368  12.958  1.00 70.33           N  
ANISOU 2141  N   GLY B 469     9849  10876   5999  -2080   2083    154       N  
ATOM   2142  CA  GLY B 469     -10.398  -1.062  12.703  1.00 68.37           C  
ANISOU 2142  CA  GLY B 469     9895  10390   5693  -2269   2019    419       C  
ATOM   2143  C   GLY B 469      -9.187  -1.826  13.204  1.00 66.97           C  
ANISOU 2143  C   GLY B 469    10150   9943   5354  -2226   1783    779       C  
ATOM   2144  O   GLY B 469      -8.230  -1.239  13.706  1.00 65.60           O  
ANISOU 2144  O   GLY B 469    10044   9781   5101  -2047   1651    842       O  
ATOM   2145  N   THR B 470      -9.244  -3.148  13.064  1.00 68.88           N  
ANISOU 2145  N   THR B 470    10673   9930   5568  -2389   1713   1005       N  
ATOM   2146  CA  THR B 470      -8.155  -4.045  13.449  1.00 69.31           C  
ANISOU 2146  CA  THR B 470    11130   9669   5536  -2328   1455   1354       C  
ATOM   2147  C   THR B 470      -7.789  -4.932  12.260  1.00 68.23           C  
ANISOU 2147  C   THR B 470    11166   9171   5589  -2203   1335   1511       C  
ATOM   2148  O   THR B 470      -8.673  -5.453  11.583  1.00 69.77           O  
ANISOU 2148  O   THR B 470    11316   9326   5868  -2377   1462   1427       O  
ATOM   2149  CB  THR B 470      -8.562  -4.941  14.640  1.00 69.69           C  
ANISOU 2149  CB  THR B 470    11425   9695   5358  -2675   1461   1487       C  
ATOM   2150  OG1 THR B 470      -8.864  -4.122  15.775  1.00 70.08           O  
ANISOU 2150  OG1 THR B 470    11349  10064   5213  -2804   1583   1325       O  
ATOM   2151  CG2 THR B 470      -7.440  -5.908  15.000  1.00 69.91           C  
ANISOU 2151  CG2 THR B 470    11853   9368   5341  -2586   1152   1851       C  
ATOM   2152  N   VAL B 471      -6.496  -5.108  12.000  1.00 65.24           N  
ANISOU 2152  N   VAL B 471    10974   8521   5294  -1902   1089   1717       N  
ATOM   2153  CA  VAL B 471      -6.081  -5.837  10.804  1.00 64.74           C  
ANISOU 2153  CA  VAL B 471    10970   8098   5530  -1670    969   1765       C  
ATOM   2154  C   VAL B 471      -5.505  -7.232  11.071  1.00 67.85           C  
ANISOU 2154  C   VAL B 471    11815   8070   5894  -1719    773   2089       C  
ATOM   2155  O   VAL B 471      -4.778  -7.451  12.042  1.00 69.12           O  
ANISOU 2155  O   VAL B 471    12147   8162   5954  -1679    576   2296       O  
ATOM   2156  CB  VAL B 471      -5.133  -4.993   9.904  1.00 66.85           C  
ANISOU 2156  CB  VAL B 471    10968   8343   6089  -1202    856   1638       C  
ATOM   2157  CG1 VAL B 471      -5.437  -3.511  10.062  1.00 64.61           C  
ANISOU 2157  CG1 VAL B 471    10325   8442   5781  -1146    969   1396       C  
ATOM   2158  CG2 VAL B 471      -3.673  -5.263  10.218  1.00 67.77           C  
ANISOU 2158  CG2 VAL B 471    11254   8224   6273   -920    588   1861       C  
ATOM   2159  N   TYR B 472      -5.862  -8.171  10.198  1.00 68.84           N  
ANISOU 2159  N   TYR B 472    12061   7917   6180  -1769    798   2084       N  
ATOM   2160  CA  TYR B 472      -5.348  -9.535  10.240  1.00 72.42           C  
ANISOU 2160  CA  TYR B 472    12906   7903   6708  -1756    603   2335       C  
ATOM   2161  C   TYR B 472      -4.813  -9.901   8.855  1.00 71.23           C  
ANISOU 2161  C   TYR B 472    12721   7435   6907  -1425    551   2230       C  
ATOM   2162  O   TYR B 472      -5.264  -9.352   7.850  1.00 67.98           O  
ANISOU 2162  O   TYR B 472    12016   7188   6625  -1363    704   1960       O  
ATOM   2163  CB  TYR B 472      -6.460 -10.528  10.595  1.00 76.92           C  
ANISOU 2163  CB  TYR B 472    13632   8433   7161  -2185    701   2355       C  
ATOM   2164  CG  TYR B 472      -7.376 -10.141  11.737  1.00 80.42           C  
ANISOU 2164  CG  TYR B 472    13958   9277   7319  -2545    855   2293       C  
ATOM   2165  CD1 TYR B 472      -8.434  -9.259  11.541  1.00 79.24           C  
ANISOU 2165  CD1 TYR B 472    13467   9534   7106  -2721   1130   2016       C  
ATOM   2166  CD2 TYR B 472      -7.214 -10.696  12.999  1.00 86.14           C  
ANISOU 2166  CD2 TYR B 472    14914   9961   7855  -2711    728   2493       C  
ATOM   2167  CE1 TYR B 472      -9.284  -8.916  12.577  1.00 82.63           C  
ANISOU 2167  CE1 TYR B 472    13770  10315   7312  -3029   1294   1913       C  
ATOM   2168  CE2 TYR B 472      -8.058 -10.362  14.042  1.00 90.17           C  
ANISOU 2168  CE2 TYR B 472    15343  10824   8093  -3055    895   2407       C  
ATOM   2169  CZ  TYR B 472      -9.091  -9.471  13.826  1.00 89.45           C  
ANISOU 2169  CZ  TYR B 472    14893  11128   7964  -3205   1189   2104       C  
ATOM   2170  OH  TYR B 472      -9.934  -9.140  14.864  1.00 93.15           O  
ANISOU 2170  OH  TYR B 472    15261  11936   8194  -3530   1373   1980       O  
ATOM   2171  N   LYS B 473      -3.861 -10.827   8.792  1.00 72.27           N  
ANISOU 2171  N   LYS B 473    13129   7119   7211  -1205    328   2419       N  
ATOM   2172  CA  LYS B 473      -3.443 -11.353   7.500  1.00 70.35           C  
ANISOU 2172  CA  LYS B 473    12871   6558   7299   -934    321   2272       C  
ATOM   2173  C   LYS B 473      -4.479 -12.374   7.063  1.00 71.19           C  
ANISOU 2173  C   LYS B 473    13228   6451   7369  -1285    438   2247       C  
ATOM   2174  O   LYS B 473      -4.974 -13.149   7.879  1.00 71.93           O  
ANISOU 2174  O   LYS B 473    13598   6439   7293  -1607    393   2439       O  
ATOM   2175  CB  LYS B 473      -2.054 -11.990   7.560  1.00 73.55           C  
ANISOU 2175  CB  LYS B 473    13439   6545   7960   -541     54   2433       C  
ATOM   2176  CG  LYS B 473      -1.580 -12.516   6.211  1.00 76.04           C  
ANISOU 2176  CG  LYS B 473    13721   6545   8626   -252     95   2223       C  
ATOM   2177  CD  LYS B 473      -0.103 -12.888   6.220  1.00 78.93           C  
ANISOU 2177  CD  LYS B 473    14100   6582   9309    215   -139   2303       C  
ATOM   2178  CE  LYS B 473       0.345 -13.359   4.842  1.00 79.72           C  
ANISOU 2178  CE  LYS B 473    14138   6406   9745    485    -33   2029       C  
ATOM   2179  NZ  LYS B 473       1.802 -13.651   4.778  1.00 82.51           N  
ANISOU 2179  NZ  LYS B 473    14414   6477  10461    971   -220   2040       N  
ATOM   2180  N   GLY B 474      -4.826 -12.363   5.782  1.00 68.59           N  
ANISOU 2180  N   GLY B 474    12749   6112   7201  -1238    578   1978       N  
ATOM   2181  CA  GLY B 474      -5.896 -13.214   5.294  1.00 69.36           C  
ANISOU 2181  CA  GLY B 474    13037   6064   7254  -1606    695   1913       C  
ATOM   2182  C   GLY B 474      -5.559 -13.962   4.021  1.00 68.09           C  
ANISOU 2182  C   GLY B 474    12994   5523   7354  -1429    694   1746       C  
ATOM   2183  O   GLY B 474      -4.496 -13.765   3.431  1.00 65.37           O  
ANISOU 2183  O   GLY B 474    12542   5059   7237  -1007    638   1647       O  
ATOM   2184  N   LYS B 475      -6.480 -14.823   3.598  1.00 69.61           N  
ANISOU 2184  N   LYS B 475    13402   5540   7506  -1780    774   1694       N  
ATOM   2185  CA  LYS B 475      -6.308 -15.590   2.375  1.00 71.26           C  
ANISOU 2185  CA  LYS B 475    13763   5387   7924  -1685    797   1500       C  
ATOM   2186  C   LYS B 475      -7.500 -15.349   1.446  1.00 69.75           C  
ANISOU 2186  C   LYS B 475    13401   5460   7642  -2002    962   1248       C  
ATOM   2187  O   LYS B 475      -8.636 -15.640   1.797  1.00 73.70           O  
ANISOU 2187  O   LYS B 475    13963   6070   7970  -2455   1027   1295       O  
ATOM   2188  CB  LYS B 475      -6.175 -17.080   2.686  1.00 78.14           C  
ANISOU 2188  CB  LYS B 475    15140   5672   8876  -1799    677   1677       C  
ATOM   2189  CG  LYS B 475      -5.192 -17.820   1.796  1.00 84.36           C  
ANISOU 2189  CG  LYS B 475    16085   5976   9992  -1419    617   1528       C  
ATOM   2190  CD  LYS B 475      -3.779 -17.294   1.991  1.00 88.48           C  
ANISOU 2190  CD  LYS B 475    16435   6468  10717   -877    504   1567       C  
ATOM   2191  CE  LYS B 475      -2.878 -17.708   0.841  1.00 92.87           C  
ANISOU 2191  CE  LYS B 475    16991   6696  11600   -492    547   1290       C  
ATOM   2192  NZ  LYS B 475      -1.587 -18.276   1.318  1.00 96.75           N  
ANISOU 2192  NZ  LYS B 475    17538   6822  12402    -55    330   1413       N  
ATOM   2193  N   TRP B 476      -7.235 -14.788   0.269  1.00 64.15           N  
ANISOU 2193  N   TRP B 476    12465   4873   7038  -1781   1022    983       N  
ATOM   2194  CA  TRP B 476      -8.268 -14.550  -0.748  1.00 63.16           C  
ANISOU 2194  CA  TRP B 476    12187   4974   6838  -2047   1120    745       C  
ATOM   2195  C   TRP B 476      -7.667 -14.318  -2.142  1.00 63.09           C  
ANISOU 2195  C   TRP B 476    12109   4915   6949  -1786   1155    480       C  
ATOM   2196  O   TRP B 476      -7.250 -13.198  -2.471  1.00 60.72           O  
ANISOU 2196  O   TRP B 476    11500   4917   6653  -1546   1166    398       O  
ATOM   2197  CB  TRP B 476      -9.185 -13.374  -0.349  1.00 61.20           C  
ANISOU 2197  CB  TRP B 476    11535   5286   6431  -2221   1165    736       C  
ATOM   2198  CG  TRP B 476     -10.432 -13.290  -1.207  1.00 62.41           C  
ANISOU 2198  CG  TRP B 476    11542   5651   6520  -2559   1213    538       C  
ATOM   2199  CD1 TRP B 476     -11.462 -14.187  -1.239  1.00 64.34           C  
ANISOU 2199  CD1 TRP B 476    11956   5796   6695  -3008   1245    527       C  
ATOM   2200  CD2 TRP B 476     -10.747 -12.287  -2.183  1.00 58.92           C  
ANISOU 2200  CD2 TRP B 476    10769   5534   6083  -2485   1198    335       C  
ATOM   2201  NE1 TRP B 476     -12.404 -13.799  -2.164  1.00 62.65           N  
ANISOU 2201  NE1 TRP B 476    11503   5847   6455  -3207   1244    318       N  
ATOM   2202  CE2 TRP B 476     -11.989 -12.635  -2.757  1.00 60.20           C  
ANISOU 2202  CE2 TRP B 476    10896   5790   6187  -2885   1200    209       C  
ATOM   2203  CE3 TRP B 476     -10.104 -11.127  -2.625  1.00 56.77           C  
ANISOU 2203  CE3 TRP B 476    10240   5473   5855  -2140   1164    261       C  
ATOM   2204  CZ2 TRP B 476     -12.599 -11.862  -3.746  1.00 57.18           C  
ANISOU 2204  CZ2 TRP B 476    10231   5700   5795  -2926   1134     26       C  
ATOM   2205  CZ3 TRP B 476     -10.710 -10.360  -3.608  1.00 52.16           C  
ANISOU 2205  CZ3 TRP B 476     9412   5160   5248  -2197   1114     90       C  
ATOM   2206  CH2 TRP B 476     -11.944 -10.732  -4.157  1.00 54.10           C  
ANISOU 2206  CH2 TRP B 476     9628   5488   5440  -2575   1083    -20       C  
ATOM   2207  N   HIS B 477      -7.623 -15.380  -2.943  1.00 62.72           N  
ANISOU 2207  N   HIS B 477    12373   4478   6981  -1862   1182    341       N  
ATOM   2208  CA  HIS B 477      -6.967 -15.339  -4.245  1.00 65.44           C  
ANISOU 2208  CA  HIS B 477    12723   4725   7415  -1642   1249     69       C  
ATOM   2209  C   HIS B 477      -5.534 -14.884  -4.056  1.00 63.56           C  
ANISOU 2209  C   HIS B 477    12361   4444   7346  -1146   1248     92       C  
ATOM   2210  O   HIS B 477      -4.998 -14.104  -4.839  1.00 59.05           O  
ANISOU 2210  O   HIS B 477    11580   4075   6781   -947   1316    -79       O  
ATOM   2211  CB  HIS B 477      -7.711 -14.418  -5.211  1.00 64.83           C  
ANISOU 2211  CB  HIS B 477    12382   5073   7179  -1811   1279   -116       C  
ATOM   2212  CG  HIS B 477      -9.144 -14.792  -5.416  1.00 67.19           C  
ANISOU 2212  CG  HIS B 477    12728   5464   7338  -2297   1254   -152       C  
ATOM   2213  ND1 HIS B 477      -9.535 -16.045  -5.839  1.00 65.34           N  
ANISOU 2213  ND1 HIS B 477    12856   4861   7111  -2567   1274   -245       N  
ATOM   2214  CD2 HIS B 477     -10.283 -14.073  -5.267  1.00 60.44           C  
ANISOU 2214  CD2 HIS B 477    11581   5028   6357  -2562   1207   -126       C  
ATOM   2215  CE1 HIS B 477     -10.852 -16.082  -5.941  1.00 71.88           C  
ANISOU 2215  CE1 HIS B 477    13607   5899   7807  -3004   1237   -265       C  
ATOM   2216  NE2 HIS B 477     -11.329 -14.898  -5.601  1.00 68.50           N  
ANISOU 2216  NE2 HIS B 477    12763   5955   7309  -2996   1197   -199       N  
ATOM   2217  N   GLY B 478      -4.928 -15.377  -2.985  1.00 63.75           N  
ANISOU 2217  N   GLY B 478    12520   4207   7496   -977   1154    319       N  
ATOM   2218  CA  GLY B 478      -3.588 -14.985  -2.609  1.00 63.72           C  
ANISOU 2218  CA  GLY B 478    12371   4169   7673   -520   1107    378       C  
ATOM   2219  C   GLY B 478      -3.629 -14.310  -1.256  1.00 63.15           C  
ANISOU 2219  C   GLY B 478    12140   4353   7499   -515    986    673       C  
ATOM   2220  O   GLY B 478      -4.647 -14.347  -0.570  1.00 64.53           O  
ANISOU 2220  O   GLY B 478    12373   4663   7484   -862    961    827       O  
ATOM   2221  N   ASP B 479      -2.526 -13.683  -0.873  1.00 60.42           N  
ANISOU 2221  N   ASP B 479    11588   4097   7273   -146    926    732       N  
ATOM   2222  CA  ASP B 479      -2.461 -12.986   0.401  1.00 58.03           C  
ANISOU 2222  CA  ASP B 479    11144   4046   6857   -133    806    989       C  
ATOM   2223  C   ASP B 479      -3.257 -11.691   0.365  1.00 58.35           C  
ANISOU 2223  C   ASP B 479    10869   4621   6679   -315    889    929       C  
ATOM   2224  O   ASP B 479      -3.251 -10.970  -0.634  1.00 58.18           O  
ANISOU 2224  O   ASP B 479    10635   4810   6662   -255    988    713       O  
ATOM   2225  CB  ASP B 479      -1.011 -12.681   0.766  1.00 57.97           C  
ANISOU 2225  CB  ASP B 479    10989   3981   7057    310    695   1050       C  
ATOM   2226  CG  ASP B 479      -0.169 -13.927   0.896  1.00 65.00           C  
ANISOU 2226  CG  ASP B 479    12148   4323   8225    551    568   1116       C  
ATOM   2227  OD1 ASP B 479      -0.625 -14.892   1.543  1.00 69.98           O  
ANISOU 2227  OD1 ASP B 479    13130   4643   8817    359    450   1321       O  
ATOM   2228  OD2 ASP B 479       0.953 -13.940   0.351  1.00 66.91           O  
ANISOU 2228  OD2 ASP B 479    12249   4437   8739    929    586    958       O  
ATOM   2229  N   VAL B 480      -3.951 -11.407   1.461  1.00 58.63           N  
ANISOU 2229  N   VAL B 480    10889   4864   6523   -547    847   1116       N  
ATOM   2230  CA  VAL B 480      -4.645 -10.139   1.630  1.00 55.90           C  
ANISOU 2230  CA  VAL B 480    10220   5006   6013   -671    910   1058       C  
ATOM   2231  C   VAL B 480      -4.523  -9.666   3.070  1.00 57.98           C  
ANISOU 2231  C   VAL B 480    10436   5450   6143   -690    834   1271       C  
ATOM   2232  O   VAL B 480      -4.240 -10.451   3.973  1.00 61.05           O  
ANISOU 2232  O   VAL B 480    11095   5605   6497   -734    728   1497       O  
ATOM   2233  CB  VAL B 480      -6.143 -10.240   1.286  1.00 56.11           C  
ANISOU 2233  CB  VAL B 480    10226   5193   5902  -1077   1012    957       C  
ATOM   2234  CG1 VAL B 480      -6.345 -10.557  -0.191  1.00 57.17           C  
ANISOU 2234  CG1 VAL B 480    10393   5209   6118  -1099   1069    729       C  
ATOM   2235  CG2 VAL B 480      -6.824 -11.278   2.167  1.00 58.22           C  
ANISOU 2235  CG2 VAL B 480    10786   5286   6048  -1421   1008   1138       C  
ATOM   2236  N   ALA B 481      -4.736  -8.372   3.274  1.00 56.06           N  
ANISOU 2236  N   ALA B 481     9874   5611   5816   -665    873   1197       N  
ATOM   2237  CA  ALA B 481      -4.853  -7.821   4.614  1.00 53.40           C  
ANISOU 2237  CA  ALA B 481     9479   5508   5302   -756    845   1340       C  
ATOM   2238  C   ALA B 481      -6.324  -7.533   4.867  1.00 52.70           C  
ANISOU 2238  C   ALA B 481     9271   5712   5041  -1130    990   1252       C  
ATOM   2239  O   ALA B 481      -7.012  -6.996   4.003  1.00 54.04           O  
ANISOU 2239  O   ALA B 481     9209   6058   5266  -1170   1069   1046       O  
ATOM   2240  CB  ALA B 481      -4.026  -6.562   4.750  1.00 49.58           C  
ANISOU 2240  CB  ALA B 481     8721   5253   4864   -465    793   1292       C  
ATOM   2241  N   VAL B 482      -6.806  -7.903   6.048  1.00 52.25           N  
ANISOU 2241  N   VAL B 482     9370   5710   4774  -1416   1020   1406       N  
ATOM   2242  CA  VAL B 482      -8.214  -7.733   6.383  1.00 54.08           C  
ANISOU 2242  CA  VAL B 482     9470   6232   4848  -1806   1196   1304       C  
ATOM   2243  C   VAL B 482      -8.397  -6.830   7.598  1.00 57.78           C  
ANISOU 2243  C   VAL B 482     9783   7052   5117  -1891   1268   1307       C  
ATOM   2244  O   VAL B 482      -8.048  -7.205   8.719  1.00 59.16           O  
ANISOU 2244  O   VAL B 482    10211   7176   5090  -2013   1224   1520       O  
ATOM   2245  CB  VAL B 482      -8.882  -9.083   6.699  1.00 58.36           C  
ANISOU 2245  CB  VAL B 482    10354   6555   5265  -2207   1243   1444       C  
ATOM   2246  CG1 VAL B 482     -10.392  -8.917   6.786  1.00 58.70           C  
ANISOU 2246  CG1 VAL B 482    10182   6922   5201  -2618   1451   1279       C  
ATOM   2247  CG2 VAL B 482      -8.511 -10.126   5.658  1.00 60.20           C  
ANISOU 2247  CG2 VAL B 482    10833   6354   5687  -2110   1152   1462       C  
ATOM   2248  N   LYS B 483      -8.951  -5.644   7.378  1.00 56.90           N  
ANISOU 2248  N   LYS B 483     9276   7285   5057  -1836   1366   1067       N  
ATOM   2249  CA  LYS B 483      -9.275  -4.749   8.480  1.00 56.52           C  
ANISOU 2249  CA  LYS B 483     9054   7584   4836  -1937   1478    996       C  
ATOM   2250  C   LYS B 483     -10.741  -4.896   8.877  1.00 59.57           C  
ANISOU 2250  C   LYS B 483     9305   8231   5098  -2363   1714    857       C  
ATOM   2251  O   LYS B 483     -11.638  -4.622   8.081  1.00 60.58           O  
ANISOU 2251  O   LYS B 483     9139   8489   5392  -2402   1785    641       O  
ATOM   2252  CB  LYS B 483      -8.962  -3.299   8.113  1.00 51.74           C  
ANISOU 2252  CB  LYS B 483     8096   7176   4387  -1605   1441    801       C  
ATOM   2253  CG  LYS B 483      -9.479  -2.285   9.119  1.00 51.64           C  
ANISOU 2253  CG  LYS B 483     7856   7527   4239  -1706   1588    641       C  
ATOM   2254  CD  LYS B 483      -9.086  -0.871   8.731  1.00 50.25           C  
ANISOU 2254  CD  LYS B 483     7380   7471   4242  -1364   1517    465       C  
ATOM   2255  CE  LYS B 483      -7.587  -0.665   8.841  1.00 50.67           C  
ANISOU 2255  CE  LYS B 483     7598   7356   4299  -1077   1323    635       C  
ATOM   2256  NZ  LYS B 483      -7.218   0.760   8.616  1.00 49.42           N  
ANISOU 2256  NZ  LYS B 483     7175   7325   4277   -807   1268    468       N  
ATOM   2257  N   MET B 484     -10.976  -5.334  10.111  1.00 61.22           N  
ANISOU 2257  N   MET B 484     9726   8526   5009  -2700   1827    981       N  
ATOM   2258  CA  MET B 484     -12.336  -5.531  10.605  1.00 64.07           C  
ANISOU 2258  CA  MET B 484     9916   9135   5293  -3086   2041    818       C  
ATOM   2259  C   MET B 484     -12.640  -4.646  11.803  1.00 62.69           C  
ANISOU 2259  C   MET B 484     9535   9297   4987  -3133   2168    655       C  
ATOM   2260  O   MET B 484     -11.758  -4.341  12.605  1.00 61.32           O  
ANISOU 2260  O   MET B 484     9521   9099   4678  -2997   2064    775       O  
ATOM   2261  CB  MET B 484     -12.567  -6.991  11.008  1.00 68.08           C  
ANISOU 2261  CB  MET B 484    10788   9392   5685  -3395   1994   1024       C  
ATOM   2262  CG  MET B 484     -11.738  -8.016  10.241  1.00 69.56           C  
ANISOU 2262  CG  MET B 484    11355   9109   5964  -3269   1787   1274       C  
ATOM   2263  SD  MET B 484     -12.267  -9.702  10.607  1.00 92.10           S  
ANISOU 2263  SD  MET B 484    14590  11679   8724  -3665   1750   1449       S  
ATOM   2264  CE  MET B 484     -13.821  -9.768   9.716  1.00115.73           C  
ANISOU 2264  CE  MET B 484    17261  14884  11827  -3984   1969   1165       C  
ATOM   2265  N   LEU B 485     -13.897  -4.235  11.912  1.00 64.29           N  
ANISOU 2265  N   LEU B 485     9373   9810   5244  -3328   2387    363       N  
ATOM   2266  CA  LEU B 485     -14.392  -3.572  13.105  1.00 68.83           C  
ANISOU 2266  CA  LEU B 485     9774  10683   5695  -3442   2548    170       C  
ATOM   2267  C   LEU B 485     -15.022  -4.632  13.996  1.00 74.47           C  
ANISOU 2267  C   LEU B 485    10715  11388   6193  -3871   2633    257       C  
ATOM   2268  O   LEU B 485     -16.114  -5.122  13.707  1.00 71.08           O  
ANISOU 2268  O   LEU B 485    10137  11047   5823  -4142   2768    132       O  
ATOM   2269  CB  LEU B 485     -15.429  -2.513  12.729  1.00 71.37           C  
ANISOU 2269  CB  LEU B 485     9542  11333   6243  -3384   2733   -228       C  
ATOM   2270  CG  LEU B 485     -16.334  -1.967  13.838  1.00 79.21           C  
ANISOU 2270  CG  LEU B 485    10291  12639   7165  -3568   2958   -510       C  
ATOM   2271  CD1 LEU B 485     -15.544  -1.191  14.892  1.00 80.29           C  
ANISOU 2271  CD1 LEU B 485    10548  12827   7130  -3427   2935   -509       C  
ATOM   2272  CD2 LEU B 485     -17.439  -1.111  13.236  1.00 80.45           C  
ANISOU 2272  CD2 LEU B 485     9875  13056   7636  -3481   3097   -898       C  
ATOM   2273  N   ASN B 486     -14.329  -5.009  15.066  1.00 77.33           N  
ANISOU 2273  N   ASN B 486    11440  11644   6298  -3950   2537    477       N  
ATOM   2274  CA  ASN B 486     -14.856  -6.056  15.932  1.00 86.38           C  
ANISOU 2274  CA  ASN B 486    12853  12760   7208  -4376   2595    586       C  
ATOM   2275  C   ASN B 486     -15.805  -5.533  17.002  1.00 89.98           C  
ANISOU 2275  C   ASN B 486    13095  13584   7509  -4654   2857    309       C  
ATOM   2276  O   ASN B 486     -15.402  -5.099  18.081  1.00 91.94           O  
ANISOU 2276  O   ASN B 486    13455  13933   7547  -4679   2863    315       O  
ATOM   2277  CB  ASN B 486     -13.754  -6.942  16.525  1.00 90.44           C  
ANISOU 2277  CB  ASN B 486    13894  12945   7523  -4382   2336    981       C  
ATOM   2278  CG  ASN B 486     -12.813  -6.183  17.424  1.00 90.40           C  
ANISOU 2278  CG  ASN B 486    13971  13008   7367  -4200   2235   1039       C  
ATOM   2279  OD1 ASN B 486     -12.575  -4.991  17.228  1.00 88.40           O  
ANISOU 2279  OD1 ASN B 486    13432  12932   7225  -3925   2279    849       O  
ATOM   2280  ND2 ASN B 486     -12.273  -6.868  18.425  1.00 92.17           N  
ANISOU 2280  ND2 ASN B 486    14595  13090   7335  -4365   2082   1301       N  
ATOM   2281  N   VAL B 487     -17.081  -5.567  16.655  1.00 90.04           N  
ANISOU 2281  N   VAL B 487    12780  13796   7635  -4864   3074     48       N  
ATOM   2282  CA  VAL B 487     -18.152  -5.276  17.576  1.00 92.33           C  
ANISOU 2282  CA  VAL B 487    12857  14425   7802  -5179   3350   -237       C  
ATOM   2283  C   VAL B 487     -19.163  -6.379  17.357  1.00 94.53           C  
ANISOU 2283  C   VAL B 487    13168  14697   8052  -5581   3450   -235       C  
ATOM   2284  O   VAL B 487     -19.180  -7.006  16.298  1.00 92.61           O  
ANISOU 2284  O   VAL B 487    12961  14251   7976  -5538   3335   -118       O  
ATOM   2285  CB  VAL B 487     -18.788  -3.917  17.270  1.00 91.14           C  
ANISOU 2285  CB  VAL B 487    12130  14582   7916  -4950   3524   -656       C  
ATOM   2286  CG1 VAL B 487     -17.841  -2.794  17.666  1.00 88.72           C  
ANISOU 2286  CG1 VAL B 487    11817  14295   7598  -4604   3446   -685       C  
ATOM   2287  CG2 VAL B 487     -19.137  -3.821  15.793  1.00 86.40           C  
ANISOU 2287  CG2 VAL B 487    11215  13939   7673  -4742   3468   -740       C  
ATOM   2288  N   THR B 488     -19.990  -6.632  18.359  1.00 99.33           N  
ANISOU 2288  N   THR B 488    13783  15523   8434  -5994   3666   -368       N  
ATOM   2289  CA  THR B 488     -20.995  -7.674  18.256  1.00102.55           C  
ANISOU 2289  CA  THR B 488    14226  15954   8784  -6423   3779   -381       C  
ATOM   2290  C   THR B 488     -22.011  -7.305  17.182  1.00101.51           C  
ANISOU 2290  C   THR B 488    13554  16010   9006  -6345   3900   -686       C  
ATOM   2291  O   THR B 488     -22.413  -8.140  16.374  1.00101.98           O  
ANISOU 2291  O   THR B 488    13645  15939   9163  -6486   3845   -607       O  
ATOM   2292  CB  THR B 488     -21.698  -7.873  19.598  1.00106.01           C  
ANISOU 2292  CB  THR B 488    14743  16640   8894  -6892   4019   -505       C  
ATOM   2293  OG1 THR B 488     -20.721  -8.179  20.601  1.00107.16           O  
ANISOU 2293  OG1 THR B 488    15394  16614   8707  -6967   3871   -211       O  
ATOM   2294  CG2 THR B 488     -22.710  -8.999  19.510  1.00117.14           C  
ANISOU 2294  CG2 THR B 488    16219  18069  10220  -7366   4133   -505       C  
ATOM   2295  N   ALA B 489     -22.411  -6.040  17.176  1.00 97.65           N  
ANISOU 2295  N   ALA B 489    12572  15813   8718  -6112   4044  -1039       N  
ATOM   2296  CA  ALA B 489     -23.328  -5.531  16.167  1.00101.76           C  
ANISOU 2296  CA  ALA B 489    12530  16516   9618  -5972   4117  -1341       C  
ATOM   2297  C   ALA B 489     -23.110  -4.038  15.992  1.00 99.05           C  
ANISOU 2297  C   ALA B 489    11789  16313   9530  -5513   4118  -1593       C  
ATOM   2298  O   ALA B 489     -23.205  -3.273  16.955  1.00101.14           O  
ANISOU 2298  O   ALA B 489    11947  16772   9707  -5499   4275  -1800       O  
ATOM   2299  CB  ALA B 489     -24.767  -5.818  16.552  1.00103.05           C  
ANISOU 2299  CB  ALA B 489    12402  16985   9768  -6374   4390  -1627       C  
ATOM   2300  N   PRO B 490     -22.816  -3.620  14.753  1.00 94.82           N  
ANISOU 2300  N   PRO B 490    11049  15668   9309  -5151   3939  -1583       N  
ATOM   2301  CA  PRO B 490     -22.465  -2.233  14.444  1.00 92.50           C  
ANISOU 2301  CA  PRO B 490    10431  15441   9272  -4682   3881  -1775       C  
ATOM   2302  C   PRO B 490     -23.613  -1.274  14.704  1.00 98.87           C  
ANISOU 2302  C   PRO B 490    10665  16577  10326  -4625   4081  -2236       C  
ATOM   2303  O   PRO B 490     -24.737  -1.499  14.253  1.00 92.26           O  
ANISOU 2303  O   PRO B 490     9470  15895   9689  -4765   4161  -2430       O  
ATOM   2304  CB  PRO B 490     -22.131  -2.275  12.949  1.00 86.80           C  
ANISOU 2304  CB  PRO B 490     9620  14541   8818  -4427   3652  -1657       C  
ATOM   2305  CG  PRO B 490     -22.813  -3.492  12.433  1.00 88.83           C  
ANISOU 2305  CG  PRO B 490     9947  14750   9056  -4784   3656  -1560       C  
ATOM   2306  CD  PRO B 490     -22.799  -4.477  13.555  1.00 92.69           C  
ANISOU 2306  CD  PRO B 490    10871  15190   9156  -5194   3771  -1387       C  
ATOM   2307  N   THR B 491     -23.321  -0.215  15.449  1.00101.29           N  
ANISOU 2307  N   THR B 491    10890  16972  10624  -4418   4152  -2413       N  
ATOM   2308  CA  THR B 491     -24.282   0.848  15.667  1.00107.41           C  
ANISOU 2308  CA  THR B 491    11127  18002  11682  -4276   4313  -2866       C  
ATOM   2309  C   THR B 491     -24.430   1.575  14.340  1.00108.57           C  
ANISOU 2309  C   THR B 491    10859  18093  12300  -3848   4107  -2978       C  
ATOM   2310  O   THR B 491     -23.468   1.657  13.577  1.00105.97           O  
ANISOU 2310  O   THR B 491    10708  17544  12013  -3596   3871  -2740       O  
ATOM   2311  CB  THR B 491     -23.786   1.826  16.743  1.00107.86           C  
ANISOU 2311  CB  THR B 491    11257  18111  11612  -4142   4407  -3009       C  
ATOM   2312  OG1 THR B 491     -22.771   2.678  16.195  1.00102.80           O  
ANISOU 2312  OG1 THR B 491    10653  17282  11126  -3687   4176  -2920       O  
ATOM   2313  CG2 THR B 491     -23.222   1.060  17.937  1.00109.37           C  
ANISOU 2313  CG2 THR B 491    11986  18277  11292  -4523   4499  -2772       C  
ATOM   2314  N   PRO B 492     -25.636   2.094  14.052  1.00112.39           N  
ANISOU 2314  N   PRO B 492    10788  18770  13144  -3768   4179  -3338       N  
ATOM   2315  CA  PRO B 492     -25.927   2.812  12.803  1.00110.88           C  
ANISOU 2315  CA  PRO B 492    10163  18528  13439  -3365   3942  -3458       C  
ATOM   2316  C   PRO B 492     -24.851   3.835  12.435  1.00106.60           C  
ANISOU 2316  C   PRO B 492     9698  17784  13020  -2899   3720  -3390       C  
ATOM   2317  O   PRO B 492     -24.611   4.067  11.252  1.00102.94           O  
ANISOU 2317  O   PRO B 492     9107  17186  12821  -2626   3450  -3301       O  
ATOM   2318  CB  PRO B 492     -27.243   3.522  13.118  1.00115.77           C  
ANISOU 2318  CB  PRO B 492    10227  19385  14376  -3307   4097  -3906       C  
ATOM   2319  CG  PRO B 492     -27.915   2.622  14.082  1.00120.49           C  
ANISOU 2319  CG  PRO B 492    10927  20193  14660  -3825   4415  -3966       C  
ATOM   2320  CD  PRO B 492     -26.823   2.005  14.920  1.00118.42           C  
ANISOU 2320  CD  PRO B 492    11302  19816  13878  -4070   4482  -3652       C  
ATOM   2321  N   GLN B 493     -24.216   4.429  13.441  1.00107.36           N  
ANISOU 2321  N   GLN B 493    10009  17865  12917  -2834   3826  -3431       N  
ATOM   2322  CA  GLN B 493     -23.095   5.335  13.225  1.00105.03           C  
ANISOU 2322  CA  GLN B 493     9855  17375  12676  -2444   3633  -3344       C  
ATOM   2323  C   GLN B 493     -21.952   4.612  12.523  1.00 99.67           C  
ANISOU 2323  C   GLN B 493     9578  16487  11804  -2444   3441  -2926       C  
ATOM   2324  O   GLN B 493     -21.363   5.129  11.573  1.00 95.67           O  
ANISOU 2324  O   GLN B 493     9020  15825  11505  -2108   3201  -2850       O  
ATOM   2325  CB  GLN B 493     -22.610   5.897  14.564  1.00109.56           C  
ANISOU 2325  CB  GLN B 493    10649  17988  12993  -2479   3800  -3436       C  
ATOM   2326  CG  GLN B 493     -21.164   6.376  14.569  1.00108.28           C  
ANISOU 2326  CG  GLN B 493    10834  17618  12691  -2235   3627  -3215       C  
ATOM   2327  CD  GLN B 493     -20.626   6.571  15.974  1.00112.56           C  
ANISOU 2327  CD  GLN B 493    11686  18212  12871  -2399   3788  -3224       C  
ATOM   2328  OE1 GLN B 493     -20.155   7.652  16.328  1.00112.87           O  
ANISOU 2328  OE1 GLN B 493    11711  18199  12974  -2152   3752  -3363       O  
ATOM   2329  NE2 GLN B 493     -20.694   5.520  16.784  1.00115.08           N  
ANISOU 2329  NE2 GLN B 493    12300  18622  12802  -2831   3947  -3070       N  
ATOM   2330  N   GLN B 494     -21.650   3.408  12.997  1.00 99.07           N  
ANISOU 2330  N   GLN B 494     9913  16394  11336  -2827   3540  -2659       N  
ATOM   2331  CA  GLN B 494     -20.539   2.624  12.474  1.00 92.52           C  
ANISOU 2331  CA  GLN B 494     9520  15338  10295  -2853   3376  -2254       C  
ATOM   2332  C   GLN B 494     -20.817   2.117  11.066  1.00 89.77           C  
ANISOU 2332  C   GLN B 494     9018  14922  10170  -2833   3218  -2167       C  
ATOM   2333  O   GLN B 494     -19.920   2.077  10.226  1.00 84.37           O  
ANISOU 2333  O   GLN B 494     8500  14056   9500  -2652   3030  -1956       O  
ATOM   2334  CB  GLN B 494     -20.236   1.458  13.416  1.00 92.31           C  
ANISOU 2334  CB  GLN B 494     9981  15270   9825  -3262   3487  -1994       C  
ATOM   2335  CG  GLN B 494     -19.845   1.913  14.812  1.00 92.40           C  
ANISOU 2335  CG  GLN B 494    10185  15347   9576  -3314   3607  -2046       C  
ATOM   2336  CD  GLN B 494     -19.814   0.781  15.815  1.00 92.75           C  
ANISOU 2336  CD  GLN B 494    10645  15386   9211  -3759   3713  -1837       C  
ATOM   2337  OE1 GLN B 494     -20.765   0.010  15.930  1.00 94.01           O  
ANISOU 2337  OE1 GLN B 494    10740  15654   9326  -4100   3854  -1892       O  
ATOM   2338  NE2 GLN B 494     -18.714   0.675  16.548  1.00 90.90           N  
ANISOU 2338  NE2 GLN B 494    10840  15020   8680  -3761   3625  -1591       N  
ATOM   2339  N   LEU B 495     -22.063   1.730  10.814  1.00 93.54           N  
ANISOU 2339  N   LEU B 495     9175  15555  10812  -3037   3297  -2339       N  
ATOM   2340  CA  LEU B 495     -22.460   1.248   9.498  1.00 93.41           C  
ANISOU 2340  CA  LEU B 495     8976  15498  11018  -3065   3131  -2283       C  
ATOM   2341  C   LEU B 495     -22.385   2.373   8.475  1.00 92.56           C  
ANISOU 2341  C   LEU B 495     8488  15361  11321  -2613   2884  -2423       C  
ATOM   2342  O   LEU B 495     -21.993   2.162   7.327  1.00 89.40           O  
ANISOU 2342  O   LEU B 495     8105  14840  11022  -2537   2666  -2271       O  
ATOM   2343  CB  LEU B 495     -23.878   0.683   9.544  1.00 97.78           C  
ANISOU 2343  CB  LEU B 495     9231  16248  11674  -3378   3256  -2466       C  
ATOM   2344  CG  LEU B 495     -24.461   0.211   8.213  1.00 97.44           C  
ANISOU 2344  CG  LEU B 495     8949  16190  11885  -3440   3060  -2444       C  
ATOM   2345  CD1 LEU B 495     -23.683  -0.981   7.682  1.00 94.48           C  
ANISOU 2345  CD1 LEU B 495     9075  15580  11244  -3686   2979  -2076       C  
ATOM   2346  CD2 LEU B 495     -25.929  -0.130   8.374  1.00102.63           C  
ANISOU 2346  CD2 LEU B 495     9238  17075  12680  -3699   3186  -2679       C  
ATOM   2347  N   GLN B 496     -22.764   3.571   8.904  1.00 95.02           N  
ANISOU 2347  N   GLN B 496     8476  15762  11867  -2325   2900  -2714       N  
ATOM   2348  CA  GLN B 496     -22.748   4.736   8.035  1.00 92.68           C  
ANISOU 2348  CA  GLN B 496     7839  15388  11988  -1865   2621  -2850       C  
ATOM   2349  C   GLN B 496     -21.321   5.138   7.693  1.00 83.96           C  
ANISOU 2349  C   GLN B 496     7040  14083  10779  -1608   2466  -2640       C  
ATOM   2350  O   GLN B 496     -21.001   5.390   6.534  1.00 81.29           O  
ANISOU 2350  O   GLN B 496     6696  13555  10636  -1363   2124  -2513       O  
ATOM   2351  CB  GLN B 496     -23.485   5.899   8.699  1.00 98.79           C  
ANISOU 2351  CB  GLN B 496     8263  16250  13023  -1633   2687  -3205       C  
ATOM   2352  CG  GLN B 496     -24.623   6.462   7.866  1.00103.72           C  
ANISOU 2352  CG  GLN B 496     8353  16908  14149  -1416   2466  -3424       C  
ATOM   2353  CD  GLN B 496     -24.131   7.318   6.719  1.00101.91           C  
ANISOU 2353  CD  GLN B 496     8032  16455  14235   -982   2049  -3348       C  
ATOM   2354  OE1 GLN B 496     -24.445   7.062   5.557  1.00102.53           O  
ANISOU 2354  OE1 GLN B 496     7945  16489  14522   -950   1756  -3256       O  
ATOM   2355  NE2 GLN B 496     -23.356   8.348   7.043  1.00 99.26           N  
ANISOU 2355  NE2 GLN B 496     7827  15965  13923   -667   1994  -3379       N  
ATOM   2356  N   ALA B 497     -20.465   5.185   8.708  1.00 79.40           N  
ANISOU 2356  N   ALA B 497     6837  13465   9867  -1648   2632  -2547       N  
ATOM   2357  CA  ALA B 497     -19.069   5.557   8.516  1.00 73.12           C  
ANISOU 2357  CA  ALA B 497     6380  12462   8940  -1406   2481  -2334       C  
ATOM   2358  C   ALA B 497     -18.367   4.529   7.648  1.00 70.97           C  
ANISOU 2358  C   ALA B 497     6541  11919   8506  -1480   2255  -1928       C  
ATOM   2359  O   ALA B 497     -17.449   4.855   6.896  1.00 69.24           O  
ANISOU 2359  O   ALA B 497     6545  11432   8333  -1198   1965  -1730       O  
ATOM   2360  CB  ALA B 497     -18.365   5.683   9.854  1.00 71.94           C  
ANISOU 2360  CB  ALA B 497     6558  12332   8444  -1490   2678  -2298       C  
ATOM   2361  N   PHE B 498     -18.800   3.280   7.769  1.00 72.09           N  
ANISOU 2361  N   PHE B 498     6805  12129   8455  -1879   2408  -1824       N  
ATOM   2362  CA  PHE B 498     -18.221   2.193   6.998  1.00 70.10           C  
ANISOU 2362  CA  PHE B 498     6966  11609   8060  -1977   2230  -1482       C  
ATOM   2363  C   PHE B 498     -18.484   2.394   5.517  1.00 69.95           C  
ANISOU 2363  C   PHE B 498     6790  11445   8342  -1773   1896  -1468       C  
ATOM   2364  O   PHE B 498     -17.577   2.273   4.701  1.00 67.01           O  
ANISOU 2364  O   PHE B 498     6730  10796   7935  -1595   1656  -1238       O  
ATOM   2365  CB  PHE B 498     -18.795   0.853   7.451  1.00 70.65           C  
ANISOU 2365  CB  PHE B 498     7177  11773   7894  -2478   2464  -1408       C  
ATOM   2366  CG  PHE B 498     -18.185  -0.326   6.761  1.00 67.14           C  
ANISOU 2366  CG  PHE B 498     7192  11015   7304  -2587   2302  -1078       C  
ATOM   2367  CD1 PHE B 498     -16.876  -0.690   7.019  1.00 62.65           C  
ANISOU 2367  CD1 PHE B 498     7116  10185   6503  -2487   2231   -792       C  
ATOM   2368  CD2 PHE B 498     -18.920  -1.073   5.856  1.00 68.18           C  
ANISOU 2368  CD2 PHE B 498     7251  11107   7548  -2784   2215  -1075       C  
ATOM   2369  CE1 PHE B 498     -16.309  -1.776   6.388  1.00 62.01           C  
ANISOU 2369  CE1 PHE B 498     7436   9793   6331  -2555   2094   -529       C  
ATOM   2370  CE2 PHE B 498     -18.359  -2.162   5.219  1.00 65.72           C  
ANISOU 2370  CE2 PHE B 498     7377  10483   7110  -2882   2084   -810       C  
ATOM   2371  CZ  PHE B 498     -17.052  -2.515   5.484  1.00 63.19           C  
ANISOU 2371  CZ  PHE B 498     7537   9888   6585  -2753   2033   -546       C  
ATOM   2372  N   LYS B 499     -19.733   2.701   5.180  1.00 73.94           N  
ANISOU 2372  N   LYS B 499     6803  12152   9137  -1813   1882  -1724       N  
ATOM   2373  CA  LYS B 499     -20.117   2.980   3.803  1.00 74.37           C  
ANISOU 2373  CA  LYS B 499     6675  12101   9481  -1636   1524  -1723       C  
ATOM   2374  C   LYS B 499     -19.346   4.170   3.244  1.00 71.03           C  
ANISOU 2374  C   LYS B 499     6295  11481   9212  -1184   1234  -1676       C  
ATOM   2375  O   LYS B 499     -18.930   4.160   2.087  1.00 68.39           O  
ANISOU 2375  O   LYS B 499     6148  10928   8910  -1058    927  -1498       O  
ATOM   2376  CB  LYS B 499     -21.618   3.250   3.712  1.00 80.66           C  
ANISOU 2376  CB  LYS B 499     6858  13180  10608  -1725   1544  -2039       C  
ATOM   2377  CG  LYS B 499     -22.484   2.066   4.094  1.00 86.19           C  
ANISOU 2377  CG  LYS B 499     7477  14088  11181  -2223   1810  -2093       C  
ATOM   2378  CD  LYS B 499     -23.958   2.421   4.007  1.00 92.34           C  
ANISOU 2378  CD  LYS B 499     7569  15180  12335  -2291   1830  -2440       C  
ATOM   2379  CE  LYS B 499     -24.837   1.250   4.414  1.00 96.95           C  
ANISOU 2379  CE  LYS B 499     8072  15982  12781  -2831   2113  -2499       C  
ATOM   2380  NZ  LYS B 499     -26.285   1.600   4.350  1.00102.20           N  
ANISOU 2380  NZ  LYS B 499     8205  16835  13793  -2794   2063  -2777       N  
ATOM   2381  N   ASN B 500     -19.156   5.193   4.072  1.00 70.67           N  
ANISOU 2381  N   ASN B 500     6099  11513   9240   -971   1343  -1843       N  
ATOM   2382  CA  ASN B 500     -18.451   6.394   3.644  1.00 69.59           C  
ANISOU 2382  CA  ASN B 500     6003  11182   9256   -568   1082  -1812       C  
ATOM   2383  C   ASN B 500     -16.990   6.149   3.281  1.00 67.03           C  
ANISOU 2383  C   ASN B 500     6210  10588   8669   -491    970  -1487       C  
ATOM   2384  O   ASN B 500     -16.532   6.579   2.224  1.00 65.98           O  
ANISOU 2384  O   ASN B 500     6195  10251   8625   -296    665  -1352       O  
ATOM   2385  CB  ASN B 500     -18.540   7.491   4.706  1.00 71.89           C  
ANISOU 2385  CB  ASN B 500     6048  11601   9666   -388   1254  -2087       C  
ATOM   2386  CG  ASN B 500     -19.930   8.080   4.821  1.00 79.50           C  
ANISOU 2386  CG  ASN B 500     6404  12782  11021   -325   1287  -2460       C  
ATOM   2387  OD1 ASN B 500     -20.787   7.854   3.966  1.00 82.61           O  
ANISOU 2387  OD1 ASN B 500     6535  13207  11646   -357   1090  -2488       O  
ATOM   2388  ND2 ASN B 500     -20.160   8.852   5.878  1.00 82.21           N  
ANISOU 2388  ND2 ASN B 500     6505  13280  11452   -234   1531  -2769       N  
ATOM   2389  N   GLU B 501     -16.259   5.468   4.159  1.00 66.08           N  
ANISOU 2389  N   GLU B 501     6406  10473   8229   -654   1210  -1363       N  
ATOM   2390  CA  GLU B 501     -14.833   5.250   3.932  1.00 64.97           C  
ANISOU 2390  CA  GLU B 501     6713  10095   7879   -558   1119  -1086       C  
ATOM   2391  C   GLU B 501     -14.586   4.329   2.746  1.00 60.14           C  
ANISOU 2391  C   GLU B 501     6347   9295   7209   -642    956   -875       C  
ATOM   2392  O   GLU B 501     -13.645   4.532   1.982  1.00 56.14           O  
ANISOU 2392  O   GLU B 501     6068   8584   6678   -474    777   -718       O  
ATOM   2393  CB  GLU B 501     -14.147   4.705   5.186  1.00 71.07           C  
ANISOU 2393  CB  GLU B 501     7749  10912   8344   -708   1367   -996       C  
ATOM   2394  CG  GLU B 501     -14.052   5.710   6.328  1.00 80.37           C  
ANISOU 2394  CG  GLU B 501     8786  12240   9512   -608   1508  -1185       C  
ATOM   2395  CD  GLU B 501     -13.314   6.989   5.946  1.00 84.46           C  
ANISOU 2395  CD  GLU B 501     9288  12615  10190   -257   1293  -1201       C  
ATOM   2396  OE1 GLU B 501     -12.333   6.916   5.173  1.00 84.24           O  
ANISOU 2396  OE1 GLU B 501     9512  12368  10128   -132   1098   -976       O  
ATOM   2397  OE2 GLU B 501     -13.720   8.071   6.424  1.00 86.18           O  
ANISOU 2397  OE2 GLU B 501     9239  12933  10572   -118   1332  -1455       O  
ATOM   2398  N   VAL B 502     -15.438   3.320   2.596  1.00 58.92           N  
ANISOU 2398  N   VAL B 502     6147   9215   7024   -927   1037   -893       N  
ATOM   2399  CA  VAL B 502     -15.354   2.413   1.461  1.00 56.99           C  
ANISOU 2399  CA  VAL B 502     6127   8798   6729  -1041    895   -743       C  
ATOM   2400  C   VAL B 502     -15.562   3.192   0.169  1.00 55.53           C  
ANISOU 2400  C   VAL B 502     5807   8544   6748   -852    574   -769       C  
ATOM   2401  O   VAL B 502     -14.849   2.989  -0.812  1.00 51.55           O  
ANISOU 2401  O   VAL B 502     5582   7840   6163   -797    416   -617       O  
ATOM   2402  CB  VAL B 502     -16.388   1.275   1.572  1.00 57.57           C  
ANISOU 2402  CB  VAL B 502     6136   8980   6756  -1418   1032   -792       C  
ATOM   2403  CG1 VAL B 502     -16.504   0.517   0.260  1.00 55.59           C  
ANISOU 2403  CG1 VAL B 502     6057   8565   6499  -1532    844   -700       C  
ATOM   2404  CG2 VAL B 502     -16.009   0.333   2.699  1.00 57.89           C  
ANISOU 2404  CG2 VAL B 502     6450   9010   6534  -1646   1306   -684       C  
ATOM   2405  N   GLY B 503     -16.530   4.104   0.188  1.00 56.87           N  
ANISOU 2405  N   GLY B 503     5551   8874   7182   -753    474   -969       N  
ATOM   2406  CA  GLY B 503     -16.798   4.958  -0.953  1.00 55.14           C  
ANISOU 2406  CA  GLY B 503     5196   8579   7176   -563    117   -978       C  
ATOM   2407  C   GLY B 503     -15.604   5.823  -1.306  1.00 51.87           C  
ANISOU 2407  C   GLY B 503     5026   7965   6717   -295    -30   -841       C  
ATOM   2408  O   GLY B 503     -15.402   6.167  -2.470  1.00 53.90           O  
ANISOU 2408  O   GLY B 503     5402   8081   6997   -221   -316   -734       O  
ATOM   2409  N   VAL B 504     -14.815   6.176  -0.297  1.00 45.91           N  
ANISOU 2409  N   VAL B 504     4356   7209   5877   -184    164   -842       N  
ATOM   2410  CA  VAL B 504     -13.594   6.946  -0.509  1.00 45.60           C  
ANISOU 2410  CA  VAL B 504     4548   6998   5782     31     63   -716       C  
ATOM   2411  C   VAL B 504     -12.467   6.062  -1.049  1.00 48.66           C  
ANISOU 2411  C   VAL B 504     5352   7226   5912    -55    103   -497       C  
ATOM   2412  O   VAL B 504     -11.763   6.436  -1.989  1.00 48.02           O  
ANISOU 2412  O   VAL B 504     5457   6994   5794     32    -69   -380       O  
ATOM   2413  CB  VAL B 504     -13.137   7.636   0.794  1.00 43.22           C  
ANISOU 2413  CB  VAL B 504     4181   6763   5478    161    243   -812       C  
ATOM   2414  CG1 VAL B 504     -11.796   8.320   0.606  1.00 37.16           C  
ANISOU 2414  CG1 VAL B 504     3662   5823   4634    335    151   -672       C  
ATOM   2415  CG2 VAL B 504     -14.184   8.634   1.255  1.00 44.99           C  
ANISOU 2415  CG2 VAL B 504     3986   7115   5992    289    210  -1076       C  
ATOM   2416  N   LEU B 505     -12.310   4.884  -0.453  1.00 50.64           N  
ANISOU 2416  N   LEU B 505     5749   7503   5991   -236    334   -452       N  
ATOM   2417  CA  LEU B 505     -11.236   3.965  -0.817  1.00 49.02           C  
ANISOU 2417  CA  LEU B 505     5913   7126   5587   -286    396   -278       C  
ATOM   2418  C   LEU B 505     -11.392   3.403  -2.228  1.00 48.48           C  
ANISOU 2418  C   LEU B 505     5994   6943   5483   -394    253   -227       C  
ATOM   2419  O   LEU B 505     -10.403   3.141  -2.913  1.00 45.63           O  
ANISOU 2419  O   LEU B 505     5901   6425   5011   -355    238   -124       O  
ATOM   2420  CB  LEU B 505     -11.156   2.821   0.193  1.00 51.32           C  
ANISOU 2420  CB  LEU B 505     6333   7437   5731   -457    635   -234       C  
ATOM   2421  CG  LEU B 505     -10.861   3.229   1.636  1.00 50.79           C  
ANISOU 2421  CG  LEU B 505     6202   7484   5613   -402    787   -260       C  
ATOM   2422  CD1 LEU B 505     -11.078   2.049   2.568  1.00 51.10           C  
ANISOU 2422  CD1 LEU B 505     6377   7555   5485   -647    990   -204       C  
ATOM   2423  CD2 LEU B 505      -9.449   3.780   1.769  1.00 47.89           C  
ANISOU 2423  CD2 LEU B 505     5992   7007   5196   -183    741   -153       C  
ATOM   2424  N   ARG B 506     -12.635   3.226  -2.663  1.00 51.01           N  
ANISOU 2424  N   ARG B 506     6128   7356   5897   -543    152   -319       N  
ATOM   2425  CA  ARG B 506     -12.897   2.667  -3.983  1.00 52.43           C  
ANISOU 2425  CA  ARG B 506     6457   7447   6017   -691     -3   -286       C  
ATOM   2426  C   ARG B 506     -12.598   3.685  -5.081  1.00 50.11           C  
ANISOU 2426  C   ARG B 506     6205   7085   5751   -554   -276   -237       C  
ATOM   2427  O   ARG B 506     -12.692   3.378  -6.266  1.00 49.38           O  
ANISOU 2427  O   ARG B 506     6279   6920   5562   -680   -429   -200       O  
ATOM   2428  CB  ARG B 506     -14.343   2.178  -4.091  1.00 57.76           C  
ANISOU 2428  CB  ARG B 506     6897   8260   6788   -918    -57   -399       C  
ATOM   2429  CG  ARG B 506     -15.369   3.287  -4.203  1.00 63.78           C  
ANISOU 2429  CG  ARG B 506     7250   9177   7806   -813   -287   -517       C  
ATOM   2430  CD  ARG B 506     -16.691   2.754  -4.728  1.00 72.26           C  
ANISOU 2430  CD  ARG B 506     8112  10368   8973  -1052   -420   -612       C  
ATOM   2431  NE  ARG B 506     -16.507   1.878  -5.885  1.00 78.25           N  
ANISOU 2431  NE  ARG B 506     9203  10992   9539  -1257   -523   -522       N  
ATOM   2432  CZ  ARG B 506     -16.289   2.303  -7.129  1.00 81.05           C  
ANISOU 2432  CZ  ARG B 506     9716  11248   9833  -1221   -812   -444       C  
ATOM   2433  NH1 ARG B 506     -16.215   3.603  -7.393  1.00 80.23           N  
ANISOU 2433  NH1 ARG B 506     9484  11137   9862   -982  -1057   -412       N  
ATOM   2434  NH2 ARG B 506     -16.136   1.424  -8.111  1.00 81.89           N  
ANISOU 2434  NH2 ARG B 506    10140  11246   9729  -1445   -857   -400       N  
ATOM   2435  N   LYS B 507     -12.236   4.898  -4.680  1.00 49.55           N  
ANISOU 2435  N   LYS B 507     6011   7027   5789   -324   -341   -235       N  
ATOM   2436  CA  LYS B 507     -11.877   5.938  -5.633  1.00 49.16           C  
ANISOU 2436  CA  LYS B 507     6039   6885   5754   -211   -604   -159       C  
ATOM   2437  C   LYS B 507     -10.367   6.030  -5.817  1.00 46.02           C  
ANISOU 2437  C   LYS B 507     5942   6362   5183   -142   -490    -46       C  
ATOM   2438  O   LYS B 507      -9.878   6.877  -6.560  1.00 44.89           O  
ANISOU 2438  O   LYS B 507     5912   6137   5005    -86   -661     34       O  
ATOM   2439  CB  LYS B 507     -12.447   7.288  -5.197  1.00 50.85           C  
ANISOU 2439  CB  LYS B 507     5942   7149   6229     -7   -785   -235       C  
ATOM   2440  CG  LYS B 507     -13.946   7.400  -5.396  1.00 56.22           C  
ANISOU 2440  CG  LYS B 507     6288   7938   7133    -48   -991   -353       C  
ATOM   2441  CD  LYS B 507     -14.499   8.679  -4.800  1.00 60.73           C  
ANISOU 2441  CD  LYS B 507     6514   8544   8019    197  -1125   -479       C  
ATOM   2442  CE  LYS B 507     -15.959   8.857  -5.186  1.00 67.01           C  
ANISOU 2442  CE  LYS B 507     6942   9432   9087    189  -1392   -597       C  
ATOM   2443  NZ  LYS B 507     -16.770   7.647  -4.859  1.00 69.68           N  
ANISOU 2443  NZ  LYS B 507     7117   9962   9397    -53  -1191   -708       N  
ATOM   2444  N   THR B 508      -9.634   5.145  -5.151  1.00 43.55           N  
ANISOU 2444  N   THR B 508     5753   6029   4765   -160   -212    -34       N  
ATOM   2445  CA  THR B 508      -8.179   5.144  -5.241  1.00 40.22           C  
ANISOU 2445  CA  THR B 508     5554   5507   4221    -81    -88     48       C  
ATOM   2446  C   THR B 508      -7.649   4.027  -6.141  1.00 39.32           C  
ANISOU 2446  C   THR B 508     5721   5285   3934   -221     16     69       C  
ATOM   2447  O   THR B 508      -7.892   2.850  -5.891  1.00 33.63           O  
ANISOU 2447  O   THR B 508     5067   4531   3180   -323    151     38       O  
ATOM   2448  CB  THR B 508      -7.527   5.029  -3.844  1.00 38.97           C  
ANISOU 2448  CB  THR B 508     5338   5380   4090     41    113     51       C  
ATOM   2449  OG1 THR B 508      -7.952   3.817  -3.207  1.00 37.70           O  
ANISOU 2449  OG1 THR B 508     5196   5234   3896    -74    272     30       O  
ATOM   2450  CG2 THR B 508      -7.918   6.212  -2.974  1.00 39.52           C  
ANISOU 2450  CG2 THR B 508     5159   5550   4306    175     40     -8       C  
ATOM   2451  N   ARG B 509      -6.932   4.412  -7.193  1.00 36.87           N  
ANISOU 2451  N   ARG B 509     5589   4911   3508   -242    -40    109       N  
ATOM   2452  CA  ARG B 509      -6.207   3.465  -8.037  1.00 37.42           C  
ANISOU 2452  CA  ARG B 509     5926   4881   3411   -352    111     85       C  
ATOM   2453  C   ARG B 509      -4.846   4.042  -8.411  1.00 38.58           C  
ANISOU 2453  C   ARG B 509     6176   4999   3483   -276    198    119       C  
ATOM   2454  O   ARG B 509      -4.709   4.711  -9.434  1.00 42.64           O  
ANISOU 2454  O   ARG B 509     6809   5520   3873   -378     81    150       O  
ATOM   2455  CB  ARG B 509      -6.997   3.138  -9.310  1.00 40.92           C  
ANISOU 2455  CB  ARG B 509     6519   5313   3717   -585    -37     53       C  
ATOM   2456  CG  ARG B 509      -8.099   2.090  -9.147  1.00 36.77           C  
ANISOU 2456  CG  ARG B 509     5958   4789   3223   -730    -41    -14       C  
ATOM   2457  CD  ARG B 509      -8.924   1.979 -10.433  1.00 38.97           C  
ANISOU 2457  CD  ARG B 509     6360   5082   3366   -972   -258    -40       C  
ATOM   2458  NE  ARG B 509      -9.893   0.886 -10.412  1.00 40.48           N  
ANISOU 2458  NE  ARG B 509     6546   5268   3566  -1161   -251   -119       N  
ATOM   2459  CZ  ARG B 509      -9.596  -0.380 -10.691  1.00 44.44           C  
ANISOU 2459  CZ  ARG B 509     7290   5640   3957  -1294    -55   -200       C  
ATOM   2460  NH1 ARG B 509      -8.352  -0.723 -11.004  1.00 43.75           N  
ANISOU 2460  NH1 ARG B 509     7433   5427   3765  -1228    161   -234       N  
ATOM   2461  NH2 ARG B 509     -10.541  -1.311 -10.650  1.00 45.08           N  
ANISOU 2461  NH2 ARG B 509     7369   5708   4052  -1497    -71   -266       N  
ATOM   2462  N   HIS B 510      -3.842   3.780  -7.583  1.00 35.43           N  
ANISOU 2462  N   HIS B 510     5733   4575   3154   -120    390    119       N  
ATOM   2463  CA  HIS B 510      -2.508   4.325  -7.800  1.00 34.14           C  
ANISOU 2463  CA  HIS B 510     5601   4412   2959    -47    488    134       C  
ATOM   2464  C   HIS B 510      -1.490   3.391  -7.161  1.00 37.54           C  
ANISOU 2464  C   HIS B 510     6022   4775   3466     91    716     95       C  
ATOM   2465  O   HIS B 510      -1.762   2.789  -6.123  1.00 38.32           O  
ANISOU 2465  O   HIS B 510     6049   4844   3665    178    737    118       O  
ATOM   2466  CB  HIS B 510      -2.407   5.723  -7.184  1.00 30.48           C  
ANISOU 2466  CB  HIS B 510     4974   4023   2584     59    345    212       C  
ATOM   2467  CG  HIS B 510      -1.176   6.476  -7.579  1.00 30.51           C  
ANISOU 2467  CG  HIS B 510     5015   4041   2535     63    405    237       C  
ATOM   2468  ND1 HIS B 510       0.044   6.285  -6.963  1.00 30.16           N  
ANISOU 2468  ND1 HIS B 510     4888   4009   2561    190    581    219       N  
ATOM   2469  CD2 HIS B 510      -0.978   7.434  -8.515  1.00 31.32           C  
ANISOU 2469  CD2 HIS B 510     5228   4152   2522    -68    301    286       C  
ATOM   2470  CE1 HIS B 510       0.941   7.083  -7.513  1.00 30.51           C  
ANISOU 2470  CE1 HIS B 510     4961   4090   2543    128    611    234       C  
ATOM   2471  NE2 HIS B 510       0.347   7.795  -8.454  1.00 31.29           N  
ANISOU 2471  NE2 HIS B 510     5198   4180   2512    -42    450    283       N  
ATOM   2472  N   VAL B 511      -0.317   3.276  -7.775  1.00 38.14           N  
ANISOU 2472  N   VAL B 511     6165   4828   3499    101    878     35       N  
ATOM   2473  CA  VAL B 511       0.696   2.317  -7.332  1.00 41.38           C  
ANISOU 2473  CA  VAL B 511     6550   5147   4024    256   1076    -24       C  
ATOM   2474  C   VAL B 511       1.226   2.611  -5.922  1.00 40.62           C  
ANISOU 2474  C   VAL B 511     6257   5086   4090    462   1033     70       C  
ATOM   2475  O   VAL B 511       1.701   1.713  -5.223  1.00 41.35           O  
ANISOU 2475  O   VAL B 511     6327   5079   4304    605   1100     74       O  
ATOM   2476  CB  VAL B 511       1.874   2.220  -8.348  1.00 38.30           C  
ANISOU 2476  CB  VAL B 511     6218   4756   3579    224   1286   -154       C  
ATOM   2477  CG1 VAL B 511       2.796   3.429  -8.233  1.00 35.93           C  
ANISOU 2477  CG1 VAL B 511     5766   4592   3294    257   1282   -106       C  
ATOM   2478  CG2 VAL B 511       2.651   0.926  -8.154  1.00 35.92           C  
ANISOU 2478  CG2 VAL B 511     5917   4304   3428    384   1482   -270       C  
ATOM   2479  N   ASN B 512       1.129   3.865  -5.499  1.00 38.06           N  
ANISOU 2479  N   ASN B 512     5811   4885   3764    468    897    148       N  
ATOM   2480  CA  ASN B 512       1.687   4.261  -4.213  1.00 37.36           C  
ANISOU 2480  CA  ASN B 512     5554   4850   3789    627    851    220       C  
ATOM   2481  C   ASN B 512       0.635   4.371  -3.119  1.00 36.81           C  
ANISOU 2481  C   ASN B 512     5436   4817   3735    637    727    282       C  
ATOM   2482  O   ASN B 512       0.929   4.771  -1.994  1.00 38.44           O  
ANISOU 2482  O   ASN B 512     5531   5085   3990    730    675    335       O  
ATOM   2483  CB  ASN B 512       2.490   5.555  -4.350  1.00 37.10           C  
ANISOU 2483  CB  ASN B 512     5419   4922   3757    625    817    234       C  
ATOM   2484  CG  ASN B 512       3.723   5.380  -5.220  1.00 38.66           C  
ANISOU 2484  CG  ASN B 512     5615   5122   3953    608    993    154       C  
ATOM   2485  OD1 ASN B 512       3.887   6.057  -6.234  1.00 39.08           O  
ANISOU 2485  OD1 ASN B 512     5738   5220   3890    451   1021    127       O  
ATOM   2486  ND2 ASN B 512       4.592   4.459  -4.828  1.00 40.65           N  
ANISOU 2486  ND2 ASN B 512     5786   5322   4337    763   1110    112       N  
ATOM   2487  N   ILE B 513      -0.593   4.005  -3.461  1.00 34.73           N  
ANISOU 2487  N   ILE B 513     5248   4530   3417    518    690    260       N  
ATOM   2488  CA  ILE B 513      -1.663   3.930  -2.482  1.00 33.81           C  
ANISOU 2488  CA  ILE B 513     5067   4465   3315    492    626    283       C  
ATOM   2489  C   ILE B 513      -2.021   2.470  -2.265  1.00 35.73           C  
ANISOU 2489  C   ILE B 513     5435   4598   3545    436    713    293       C  
ATOM   2490  O   ILE B 513      -2.203   1.728  -3.225  1.00 35.31           O  
ANISOU 2490  O   ILE B 513     5519   4442   3457    348    764    242       O  
ATOM   2491  CB  ILE B 513      -2.919   4.694  -2.938  1.00 32.55           C  
ANISOU 2491  CB  ILE B 513     4843   4379   3147    389    494    239       C  
ATOM   2492  CG1 ILE B 513      -2.562   6.126  -3.326  1.00 31.73           C  
ANISOU 2492  CG1 ILE B 513     4674   4318   3062    433    376    245       C  
ATOM   2493  CG2 ILE B 513      -3.969   4.698  -1.834  1.00 31.81           C  
ANISOU 2493  CG2 ILE B 513     4618   4377   3092    366    474    217       C  
ATOM   2494  CD1 ILE B 513      -1.996   6.934  -2.179  1.00 32.08           C  
ANISOU 2494  CD1 ILE B 513     4591   4430   3169    557    363    261       C  
ATOM   2495  N   LEU B 514      -2.101   2.068  -1.000  1.00 36.73           N  
ANISOU 2495  N   LEU B 514     5543   4735   3680    464    725    359       N  
ATOM   2496  CA  LEU B 514      -2.464   0.706  -0.629  1.00 36.10           C  
ANISOU 2496  CA  LEU B 514     5613   4525   3578    384    787    403       C  
ATOM   2497  C   LEU B 514      -3.714   0.270  -1.380  1.00 36.36           C  
ANISOU 2497  C   LEU B 514     5700   4545   3569    184    795    329       C  
ATOM   2498  O   LEU B 514      -4.705   0.998  -1.428  1.00 38.14           O  
ANISOU 2498  O   LEU B 514     5783   4924   3786     95    732    275       O  
ATOM   2499  CB  LEU B 514      -2.698   0.625   0.878  1.00 35.28           C  
ANISOU 2499  CB  LEU B 514     5484   4494   3427    360    773    494       C  
ATOM   2500  CG  LEU B 514      -3.058  -0.735   1.467  1.00 37.10           C  
ANISOU 2500  CG  LEU B 514     5907   4582   3607    238    816    585       C  
ATOM   2501  CD1 LEU B 514      -1.876  -1.697   1.367  1.00 34.52           C  
ANISOU 2501  CD1 LEU B 514     5745   4005   3364    392    809    668       C  
ATOM   2502  CD2 LEU B 514      -3.518  -0.571   2.909  1.00 34.03           C  
ANISOU 2502  CD2 LEU B 514     5492   4336   3104    135    815    657       C  
ATOM   2503  N   LEU B 515      -3.658  -0.914  -1.976  1.00 34.53           N  
ANISOU 2503  N   LEU B 515     5664   4124   3333    119    861    313       N  
ATOM   2504  CA  LEU B 515      -4.723  -1.355  -2.867  1.00 37.51           C  
ANISOU 2504  CA  LEU B 515     6111   4479   3660    -91    854    228       C  
ATOM   2505  C   LEU B 515      -5.967  -1.864  -2.144  1.00 38.61           C  
ANISOU 2505  C   LEU B 515     6230   4671   3768   -297    857    248       C  
ATOM   2506  O   LEU B 515      -5.948  -2.914  -1.504  1.00 40.24           O  
ANISOU 2506  O   LEU B 515     6596   4734   3960   -366    921    321       O  
ATOM   2507  CB  LEU B 515      -4.212  -2.421  -3.838  1.00 40.06           C  
ANISOU 2507  CB  LEU B 515     6670   4570   3980   -110    939    162       C  
ATOM   2508  CG  LEU B 515      -5.213  -2.857  -4.907  1.00 43.69           C  
ANISOU 2508  CG  LEU B 515     7234   5006   4358   -351    916     57       C  
ATOM   2509  CD1 LEU B 515      -5.486  -1.718  -5.879  1.00 42.13           C  
ANISOU 2509  CD1 LEU B 515     6929   4983   4096   -389    805      1       C  
ATOM   2510  CD2 LEU B 515      -4.714  -4.099  -5.638  1.00 48.70           C  
ANISOU 2510  CD2 LEU B 515     8140   5373   4989   -380   1032    -31       C  
ATOM   2511  N   PHE B 516      -7.049  -1.107  -2.265  1.00 38.24           N  
ANISOU 2511  N   PHE B 516     5982   4824   3723   -403    780    182       N  
ATOM   2512  CA  PHE B 516      -8.357  -1.559  -1.828  1.00 39.19           C  
ANISOU 2512  CA  PHE B 516     6029   5034   3829   -641    801    151       C  
ATOM   2513  C   PHE B 516      -8.815  -2.673  -2.763  1.00 41.75           C  
ANISOU 2513  C   PHE B 516     6549   5202   4115   -848    807    105       C  
ATOM   2514  O   PHE B 516      -8.768  -2.518  -3.983  1.00 37.97           O  
ANISOU 2514  O   PHE B 516     6120   4685   3620   -854    728     36       O  
ATOM   2515  CB  PHE B 516      -9.338  -0.390  -1.876  1.00 36.17           C  
ANISOU 2515  CB  PHE B 516     5327   4897   3518   -654    696     54       C  
ATOM   2516  CG  PHE B 516     -10.775  -0.799  -1.778  1.00 39.12           C  
ANISOU 2516  CG  PHE B 516     5557   5392   3914   -913    703    -30       C  
ATOM   2517  CD1 PHE B 516     -11.339  -1.104  -0.549  1.00 39.41           C  
ANISOU 2517  CD1 PHE B 516     5503   5546   3926  -1052    843    -33       C  
ATOM   2518  CD2 PHE B 516     -11.567  -0.865  -2.913  1.00 39.27           C  
ANISOU 2518  CD2 PHE B 516     5526   5428   3965  -1046    566   -109       C  
ATOM   2519  CE1 PHE B 516     -12.664  -1.478  -0.452  1.00 41.68           C  
ANISOU 2519  CE1 PHE B 516     5621   5975   4242  -1321    879   -130       C  
ATOM   2520  CE2 PHE B 516     -12.896  -1.237  -2.827  1.00 56.76           C  
ANISOU 2520  CE2 PHE B 516     7563   7777   6227  -1296    560   -198       C  
ATOM   2521  CZ  PHE B 516     -13.447  -1.543  -1.594  1.00 57.75           C  
ANISOU 2521  CZ  PHE B 516     7564   8028   6349  -1435    732   -217       C  
ATOM   2522  N   MET B 517      -9.254  -3.793  -2.197  1.00 42.83           N  
ANISOU 2522  N   MET B 517     6824   5239   4213  -1047    897    145       N  
ATOM   2523  CA  MET B 517      -9.654  -4.944  -3.007  1.00 45.20           C  
ANISOU 2523  CA  MET B 517     7347   5349   4476  -1266    910     95       C  
ATOM   2524  C   MET B 517     -11.126  -5.320  -2.849  1.00 46.26           C  
ANISOU 2524  C   MET B 517     7365   5616   4594  -1605    908     39       C  
ATOM   2525  O   MET B 517     -11.730  -5.872  -3.766  1.00 45.31           O  
ANISOU 2525  O   MET B 517     7327   5437   4453  -1812    857    -48       O  
ATOM   2526  CB  MET B 517      -8.766  -6.153  -2.704  1.00 42.86           C  
ANISOU 2526  CB  MET B 517     7391   4721   4174  -1223   1004    185       C  
ATOM   2527  CG  MET B 517      -7.343  -6.013  -3.217  1.00 41.72           C  
ANISOU 2527  CG  MET B 517     7353   4418   4082   -917   1015    177       C  
ATOM   2528  SD  MET B 517      -6.286  -7.380  -2.709  1.00 44.15           S  
ANISOU 2528  SD  MET B 517     7994   4317   4463   -795   1086    278       S  
ATOM   2529  CE  MET B 517      -7.068  -8.756  -3.550  1.00 46.60           C  
ANISOU 2529  CE  MET B 517     8601   4363   4743  -1104   1125    169       C  
ATOM   2530  N   GLY B 518     -11.701  -5.026  -1.689  1.00 45.99           N  
ANISOU 2530  N   GLY B 518     7133   5778   4562  -1685    974     71       N  
ATOM   2531  CA  GLY B 518     -13.110  -5.294  -1.473  1.00 47.91           C  
ANISOU 2531  CA  GLY B 518     7193   6200   4809  -2017   1005    -10       C  
ATOM   2532  C   GLY B 518     -13.538  -5.166  -0.028  1.00 50.10           C  
ANISOU 2532  C   GLY B 518     7325   6667   5044  -2132   1155     25       C  
ATOM   2533  O   GLY B 518     -12.723  -4.881   0.845  1.00 51.48           O  
ANISOU 2533  O   GLY B 518     7573   6822   5164  -1956   1212    129       O  
ATOM   2534  N   TYR B 519     -14.824  -5.380   0.223  1.00 53.32           N  
ANISOU 2534  N   TYR B 519     7520   7276   5463  -2455   1223    -75       N  
ATOM   2535  CA  TYR B 519     -15.363  -5.286   1.574  1.00 57.17           C  
ANISOU 2535  CA  TYR B 519     7855   7988   5880  -2636   1414    -83       C  
ATOM   2536  C   TYR B 519     -16.386  -6.381   1.856  1.00 64.00           C  
ANISOU 2536  C   TYR B 519     8774   8878   6664  -3119   1547    -94       C  
ATOM   2537  O   TYR B 519     -16.913  -7.001   0.934  1.00 64.67           O  
ANISOU 2537  O   TYR B 519     8900   8873   6799  -3307   1464   -147       O  
ATOM   2538  CB  TYR B 519     -16.008  -3.915   1.795  1.00 56.24           C  
ANISOU 2538  CB  TYR B 519     7234   8226   5908  -2497   1409   -275       C  
ATOM   2539  CG  TYR B 519     -17.295  -3.701   1.028  1.00 58.37           C  
ANISOU 2539  CG  TYR B 519     7126   8694   6356  -2647   1317   -472       C  
ATOM   2540  CD1 TYR B 519     -18.525  -3.997   1.603  1.00 62.98           C  
ANISOU 2540  CD1 TYR B 519     7433   9534   6962  -3001   1483   -608       C  
ATOM   2541  CD2 TYR B 519     -17.281  -3.200  -0.267  1.00 56.23           C  
ANISOU 2541  CD2 TYR B 519     6771   8368   6228  -2455   1054   -520       C  
ATOM   2542  CE1 TYR B 519     -19.702  -3.804   0.909  1.00 65.59           C  
ANISOU 2542  CE1 TYR B 519     7369  10060   7492  -3130   1372   -796       C  
ATOM   2543  CE2 TYR B 519     -18.454  -3.002  -0.968  1.00 57.82           C  
ANISOU 2543  CE2 TYR B 519     6625   8746   6598  -2588    911   -680       C  
ATOM   2544  CZ  TYR B 519     -19.661  -3.307  -0.374  1.00 62.97           C  
ANISOU 2544  CZ  TYR B 519     6962   9651   7311  -2910   1062   -822       C  
ATOM   2545  OH  TYR B 519     -20.835  -3.114  -1.062  1.00 66.38           O  
ANISOU 2545  OH  TYR B 519     7000  10275   7949  -3035    896   -990       O  
ATOM   2546  N   SER B 520     -16.662  -6.606   3.137  1.00 70.58           N  
ANISOU 2546  N   SER B 520     9622   9844   7351  -3354   1757    -48       N  
ATOM   2547  CA  SER B 520     -17.715  -7.523   3.562  1.00 79.20           C  
ANISOU 2547  CA  SER B 520    10725  11022   8346  -3872   1926    -69       C  
ATOM   2548  C   SER B 520     -18.419  -6.960   4.793  1.00 81.92           C  
ANISOU 2548  C   SER B 520    10751  11762   8613  -4060   2175   -188       C  
ATOM   2549  O   SER B 520     -17.832  -6.183   5.547  1.00 79.87           O  
ANISOU 2549  O   SER B 520    10455  11600   8291  -3824   2225   -173       O  
ATOM   2550  CB  SER B 520     -17.146  -8.910   3.857  1.00 84.56           C  
ANISOU 2550  CB  SER B 520    11985  11309   8834  -4090   1948    187       C  
ATOM   2551  OG  SER B 520     -16.247  -8.875   4.950  1.00 88.01           O  
ANISOU 2551  OG  SER B 520    12682  11661   9097  -3977   2002    383       O  
ATOM   2552  N   THR B 521     -19.674  -7.357   4.995  1.00 87.86           N  
ANISOU 2552  N   THR B 521    11267  12752   9363  -4506   2343   -328       N  
ATOM   2553  CA  THR B 521     -20.513  -6.764   6.035  1.00 91.34           C  
ANISOU 2553  CA  THR B 521    11308  13629   9769  -4704   2619   -528       C  
ATOM   2554  C   THR B 521     -20.904  -7.751   7.134  1.00 96.65           C  
ANISOU 2554  C   THR B 521    12267  14260  10198  -5041   2748   -437       C  
ATOM   2555  O   THR B 521     -21.344  -7.345   8.210  1.00 99.15           O  
ANISOU 2555  O   THR B 521    12408  14834  10430  -5096   2918   -567       O  
ATOM   2556  CB  THR B 521     -21.810  -6.181   5.436  1.00 92.43           C  
ANISOU 2556  CB  THR B 521    10797  14113  10208  -4762   2619   -859       C  
ATOM   2557  OG1 THR B 521     -22.698  -7.251   5.089  1.00 96.06           O  
ANISOU 2557  OG1 THR B 521    11302  14534  10665  -5159   2611   -869       O  
ATOM   2558  CG2 THR B 521     -21.504  -5.355   4.196  1.00 88.20           C  
ANISOU 2558  CG2 THR B 521    10075  13479   9959  -4272   2278   -922       C  
ATOM   2559  N   LYS B 522     -20.753  -9.043   6.863  1.00 98.45           N  
ANISOU 2559  N   LYS B 522    12943  14151  10312  -5275   2663   -228       N  
ATOM   2560  CA  LYS B 522     -21.104 -10.064   7.846  1.00103.15           C  
ANISOU 2560  CA  LYS B 522    13843  14677  10673  -5620   2754   -120       C  
ATOM   2561  C   LYS B 522     -19.977 -11.080   8.039  1.00104.26           C  
ANISOU 2561  C   LYS B 522    14647  14328  10639  -5584   2599    231       C  
ATOM   2562  O   LYS B 522     -19.307 -11.447   7.076  1.00102.37           O  
ANISOU 2562  O   LYS B 522    14646  13753  10496  -5431   2430    353       O  
ATOM   2563  CB  LYS B 522     -22.400 -10.761   7.451  1.00105.86           C  
ANISOU 2563  CB  LYS B 522    14005  15138  11080  -6019   2815   -269       C  
ATOM   2564  N   PRO B 523     -19.755 -11.531   9.290  1.00108.62           N  
ANISOU 2564  N   PRO B 523    15497  14829  10946  -5717   2642    384       N  
ATOM   2565  CA  PRO B 523     -20.492 -11.109  10.489  1.00112.46           C  
ANISOU 2565  CA  PRO B 523    15753  15695  11281  -5921   2856    231       C  
ATOM   2566  C   PRO B 523     -20.038  -9.746  10.992  1.00108.07           C  
ANISOU 2566  C   PRO B 523    14930  15387  10745  -5589   2914    117       C  
ATOM   2567  O   PRO B 523     -20.799  -9.051  11.665  1.00109.19           O  
ANISOU 2567  O   PRO B 523    14713  15907  10867  -5680   3114   -133       O  
ATOM   2568  CB  PRO B 523     -20.116 -12.180  11.517  1.00116.47           C  
ANISOU 2568  CB  PRO B 523    16802  15953  11499  -6159   2807    504       C  
ATOM   2569  CG  PRO B 523     -18.747 -12.588  11.118  1.00113.61           C  
ANISOU 2569  CG  PRO B 523    16868  15128  11169  -5846   2546    801       C  
ATOM   2570  CD  PRO B 523     -18.767 -12.578   9.611  1.00110.17           C  
ANISOU 2570  CD  PRO B 523    16302  14558  10998  -5695   2464    721       C  
ATOM   2571  N   GLN B 524     -18.804  -9.379  10.667  1.00102.34           N  
ANISOU 2571  N   GLN B 524    14382  14437  10065  -5204   2742    284       N  
ATOM   2572  CA  GLN B 524     -18.271  -8.076  11.025  1.00 97.92           C  
ANISOU 2572  CA  GLN B 524    13593  14077   9534  -4863   2767    184       C  
ATOM   2573  C   GLN B 524     -18.019  -7.278   9.762  1.00 90.53           C  
ANISOU 2573  C   GLN B 524    12375  13157   8867  -4535   2691     75       C  
ATOM   2574  O   GLN B 524     -17.792  -7.846   8.695  1.00 90.33           O  
ANISOU 2574  O   GLN B 524    12499  12877   8946  -4517   2564    179       O  
ATOM   2575  CB  GLN B 524     -16.962  -8.222  11.802  1.00 98.92           C  
ANISOU 2575  CB  GLN B 524    14155  13960   9469  -4683   2615    474       C  
ATOM   2576  CG  GLN B 524     -17.106  -8.863  13.166  1.00107.21           C  
ANISOU 2576  CG  GLN B 524    15491  15018  10227  -4998   2664    591       C  
ATOM   2577  CD  GLN B 524     -15.944  -9.777  13.492  1.00110.94           C  
ANISOU 2577  CD  GLN B 524    16521  15069  10564  -4929   2416    974       C  
ATOM   2578  OE1 GLN B 524     -15.808 -10.854  12.912  1.00113.77           O  
ANISOU 2578  OE1 GLN B 524    17169  15086  10973  -5004   2287   1149       O  
ATOM   2579  NE2 GLN B 524     -15.093  -9.348  14.416  1.00110.86           N  
ANISOU 2579  NE2 GLN B 524    16655  15068  10400  -4776   2331   1094       N  
ATOM   2580  N   LEU B 525     -18.063  -5.959   9.886  1.00 83.83           N  
ANISOU 2580  N   LEU B 525    11131  12596   8124  -4287   2764   -145       N  
ATOM   2581  CA  LEU B 525     -17.713  -5.093   8.777  1.00 74.33           C  
ANISOU 2581  CA  LEU B 525     9674  11415   7152  -3957   2675   -237       C  
ATOM   2582  C   LEU B 525     -16.226  -5.250   8.521  1.00 69.35           C  
ANISOU 2582  C   LEU B 525     9473  10439   6440  -3676   2482     53       C  
ATOM   2583  O   LEU B 525     -15.425  -5.184   9.452  1.00 69.87           O  
ANISOU 2583  O   LEU B 525     9790  10431   6328  -3574   2445    203       O  
ATOM   2584  CB  LEU B 525     -18.034  -3.643   9.117  1.00 71.08           C  
ANISOU 2584  CB  LEU B 525     8777  11351   6878  -3726   2776   -539       C  
ATOM   2585  CG  LEU B 525     -19.472  -3.380   9.550  1.00 73.12           C  
ANISOU 2585  CG  LEU B 525     8585  11948   7249  -3936   2966   -862       C  
ATOM   2586  CD1 LEU B 525     -19.666  -1.903   9.840  1.00 71.92           C  
ANISOU 2586  CD1 LEU B 525     7986  12056   7282  -3628   3028  -1166       C  
ATOM   2587  CD2 LEU B 525     -20.442  -3.856   8.481  1.00 73.45           C  
ANISOU 2587  CD2 LEU B 525     8365  12037   7506  -4126   2936   -965       C  
ATOM   2588  N   ALA B 526     -15.855  -5.468   7.266  1.00 64.24           N  
ANISOU 2588  N   ALA B 526     8886   9523   6001  -3434   2250    102       N  
ATOM   2589  CA  ALA B 526     -14.456  -5.695   6.937  1.00 59.88           C  
ANISOU 2589  CA  ALA B 526     8701   8604   5448  -3101   2031    333       C  
ATOM   2590  C   ALA B 526     -14.037  -5.007   5.642  1.00 57.42           C  
ANISOU 2590  C   ALA B 526     8211   8204   5403  -2688   1825    235       C  
ATOM   2591  O   ALA B 526     -14.843  -4.809   4.732  1.00 57.59           O  
ANISOU 2591  O   ALA B 526     7962   8321   5599  -2719   1785     61       O  
ATOM   2592  CB  ALA B 526     -14.164  -7.187   6.867  1.00 61.01           C  
ANISOU 2592  CB  ALA B 526     9333   8372   5474  -3328   1981    583       C  
ATOM   2593  N   ILE B 527     -12.766  -4.638   5.572  1.00 53.32           N  
ANISOU 2593  N   ILE B 527     7846   7511   4901  -2325   1684    353       N  
ATOM   2594  CA  ILE B 527     -12.208  -4.096   4.346  1.00 50.93           C  
ANISOU 2594  CA  ILE B 527     7458   7093   4800  -1976   1504    297       C  
ATOM   2595  C   ILE B 527     -10.982  -4.900   3.939  1.00 50.89           C  
ANISOU 2595  C   ILE B 527     7840   6706   4788  -1809   1386    492       C  
ATOM   2596  O   ILE B 527     -10.043  -5.063   4.717  1.00 52.93           O  
ANISOU 2596  O   ILE B 527     8308   6848   4954  -1700   1361    662       O  
ATOM   2597  CB  ILE B 527     -11.838  -2.613   4.492  1.00 47.08           C  
ANISOU 2597  CB  ILE B 527     6688   6800   4401  -1662   1455    186       C  
ATOM   2598  CG1 ILE B 527     -13.079  -1.795   4.848  1.00 47.38           C  
ANISOU 2598  CG1 ILE B 527     6306   7189   4507  -1783   1569    -54       C  
ATOM   2599  CG2 ILE B 527     -11.220  -2.094   3.205  1.00 42.25           C  
ANISOU 2599  CG2 ILE B 527     6040   6055   3959  -1355   1270    158       C  
ATOM   2600  CD1 ILE B 527     -12.791  -0.341   5.146  1.00 46.06           C  
ANISOU 2600  CD1 ILE B 527     5883   7185   4432  -1494   1534   -182       C  
ATOM   2601  N   VAL B 528     -11.003  -5.406   2.714  1.00 47.39           N  
ANISOU 2601  N   VAL B 528     7483   6072   4451  -1792   1308    452       N  
ATOM   2602  CA  VAL B 528      -9.908  -6.222   2.212  1.00 46.99           C  
ANISOU 2602  CA  VAL B 528     7771   5649   4433  -1630   1228    575       C  
ATOM   2603  C   VAL B 528      -8.947  -5.394   1.373  1.00 45.21           C  
ANISOU 2603  C   VAL B 528     7448   5402   4329  -1259   1128    514       C  
ATOM   2604  O   VAL B 528      -9.361  -4.642   0.490  1.00 44.59           O  
ANISOU 2604  O   VAL B 528     7150   5472   4321  -1214   1081    367       O  
ATOM   2605  CB  VAL B 528     -10.430  -7.397   1.371  1.00 48.77           C  
ANISOU 2605  CB  VAL B 528     8209   5643   4677  -1865   1233    543       C  
ATOM   2606  CG1 VAL B 528      -9.281  -8.273   0.914  1.00 48.09           C  
ANISOU 2606  CG1 VAL B 528     8472   5146   4654  -1675   1175    631       C  
ATOM   2607  CG2 VAL B 528     -11.436  -8.207   2.173  1.00 50.88           C  
ANISOU 2607  CG2 VAL B 528     8573   5942   4818  -2291   1341    604       C  
ATOM   2608  N   THR B 529      -7.658  -5.533   1.656  1.00 42.39           N  
ANISOU 2608  N   THR B 529     7252   4860   3995  -1009   1084    636       N  
ATOM   2609  CA  THR B 529      -6.635  -4.851   0.881  1.00 43.65           C  
ANISOU 2609  CA  THR B 529     7332   4990   4263   -691   1020    579       C  
ATOM   2610  C   THR B 529      -5.561  -5.833   0.445  1.00 46.45           C  
ANISOU 2610  C   THR B 529     7954   4992   4704   -534   1005    633       C  
ATOM   2611  O   THR B 529      -5.575  -7.002   0.838  1.00 48.30           O  
ANISOU 2611  O   THR B 529     8451   4974   4928   -641   1011    738       O  
ATOM   2612  CB  THR B 529      -5.966  -3.720   1.688  1.00 42.13           C  
ANISOU 2612  CB  THR B 529     6957   4987   4064   -483    981    625       C  
ATOM   2613  OG1 THR B 529      -5.097  -4.284   2.680  1.00 42.41           O  
ANISOU 2613  OG1 THR B 529     7176   4871   4068   -399    946    806       O  
ATOM   2614  CG2 THR B 529      -7.013  -2.853   2.363  1.00 43.14           C  
ANISOU 2614  CG2 THR B 529     6840   5431   4119   -631   1021    554       C  
ATOM   2615  N   GLN B 530      -4.628  -5.351  -0.366  1.00 45.28           N  
ANISOU 2615  N   GLN B 530     7737   4817   4650   -286    991    552       N  
ATOM   2616  CA  GLN B 530      -3.476  -6.150  -0.747  1.00 47.86           C  
ANISOU 2616  CA  GLN B 530     8243   4839   5103    -83   1001    556       C  
ATOM   2617  C   GLN B 530      -2.594  -6.380   0.470  1.00 51.26           C  
ANISOU 2617  C   GLN B 530     8723   5168   5585     91    919    746       C  
ATOM   2618  O   GLN B 530      -2.668  -5.646   1.460  1.00 50.85           O  
ANISOU 2618  O   GLN B 530     8542   5333   5447     83    866    847       O  
ATOM   2619  CB  GLN B 530      -2.671  -5.451  -1.843  1.00 45.80           C  
ANISOU 2619  CB  GLN B 530     7852   4638   4911    109   1040    406       C  
ATOM   2620  CG  GLN B 530      -1.946  -4.201  -1.375  1.00 44.23           C  
ANISOU 2620  CG  GLN B 530     7410   4665   4731    300    989    450       C  
ATOM   2621  CD  GLN B 530      -1.101  -3.572  -2.465  1.00 44.77           C  
ANISOU 2621  CD  GLN B 530     7377   4783   4851    440   1047    313       C  
ATOM   2622  OE1 GLN B 530      -1.271  -2.399  -2.800  1.00 43.97           O  
ANISOU 2622  OE1 GLN B 530     7113   4908   4685    414   1019    274       O  
ATOM   2623  NE2 GLN B 530      -0.174  -4.345  -3.015  1.00 45.45           N  
ANISOU 2623  NE2 GLN B 530     7563   4648   5058    583   1132    231       N  
ATOM   2624  N   TRP B 531      -1.752  -7.401   0.392  1.00 53.43           N  
ANISOU 2624  N   TRP B 531     9190   5102   6008    251    895    784       N  
ATOM   2625  CA  TRP B 531      -0.809  -7.663   1.462  1.00 55.20           C  
ANISOU 2625  CA  TRP B 531     9462   5197   6314    449    758    977       C  
ATOM   2626  C   TRP B 531       0.571  -7.117   1.113  1.00 55.11           C  
ANISOU 2626  C   TRP B 531     9240   5211   6488    796    740    901       C  
ATOM   2627  O   TRP B 531       1.133  -7.439   0.069  1.00 60.61           O  
ANISOU 2627  O   TRP B 531     9928   5760   7342    940    837    724       O  
ATOM   2628  CB  TRP B 531      -0.732  -9.156   1.765  1.00 59.68           C  
ANISOU 2628  CB  TRP B 531    10371   5336   6970    429    687   1101       C  
ATOM   2629  CG  TRP B 531       0.239  -9.459   2.842  1.00 65.70           C  
ANISOU 2629  CG  TRP B 531    11200   5938   7827    639    486   1328       C  
ATOM   2630  CD1 TRP B 531       1.481  -9.993   2.694  1.00 69.44           C  
ANISOU 2630  CD1 TRP B 531    11680   6123   8583    987    387   1329       C  
ATOM   2631  CD2 TRP B 531       0.067  -9.219   4.244  1.00 67.48           C  
ANISOU 2631  CD2 TRP B 531    11481   6296   7862    514    343   1581       C  
ATOM   2632  NE1 TRP B 531       2.091 -10.114   3.916  1.00 72.03           N  
ANISOU 2632  NE1 TRP B 531    12063   6380   8924   1097    145   1593       N  
ATOM   2633  CE2 TRP B 531       1.243  -9.645   4.885  1.00 70.54           C  
ANISOU 2633  CE2 TRP B 531    11933   6452   8418    791    116   1758       C  
ATOM   2634  CE3 TRP B 531      -0.971  -8.691   5.018  1.00 67.06           C  
ANISOU 2634  CE3 TRP B 531    11423   6542   7513    187    389   1656       C  
ATOM   2635  CZ2 TRP B 531       1.415  -9.562   6.264  1.00 71.26           C  
ANISOU 2635  CZ2 TRP B 531    12126   6600   8349    726    -92   2035       C  
ATOM   2636  CZ3 TRP B 531      -0.800  -8.609   6.387  1.00 67.91           C  
ANISOU 2636  CZ3 TRP B 531    11632   6718   7454    113    235   1898       C  
ATOM   2637  CH2 TRP B 531       0.384  -9.043   6.996  1.00 69.39           C  
ANISOU 2637  CH2 TRP B 531    11925   6669   7772    369    -16   2100       C  
ATOM   2638  N   CYS B 532       1.108  -6.281   1.993  1.00 50.43           N  
ANISOU 2638  N   CYS B 532     8473   4822   5865    902    632   1015       N  
ATOM   2639  CA  CYS B 532       2.438  -5.721   1.800  1.00 48.66           C  
ANISOU 2639  CA  CYS B 532     8018   4653   5819   1200    600    958       C  
ATOM   2640  C   CYS B 532       3.483  -6.586   2.482  1.00 52.54           C  
ANISOU 2640  C   CYS B 532     8585   4861   6516   1446    422   1107       C  
ATOM   2641  O   CYS B 532       3.315  -6.994   3.628  1.00 53.64           O  
ANISOU 2641  O   CYS B 532     8893   4918   6568   1380    244   1343       O  
ATOM   2642  CB  CYS B 532       2.509  -4.293   2.344  1.00 40.88           C  
ANISOU 2642  CB  CYS B 532     6794   4032   4707   1177    556    984       C  
ATOM   2643  SG  CYS B 532       1.429  -3.132   1.492  1.00 59.08           S  
ANISOU 2643  SG  CYS B 532     8969   6635   6843    961    707    808       S  
ATOM   2644  N   GLU B 533       4.560  -6.867   1.761  1.00 57.06           N  
ANISOU 2644  N   GLU B 533     9032   5285   7364   1724    466    962       N  
ATOM   2645  CA  GLU B 533       5.667  -7.634   2.303  1.00 63.39           C  
ANISOU 2645  CA  GLU B 533     9832   5809   8443   2025    274   1070       C  
ATOM   2646  C   GLU B 533       6.731  -6.677   2.814  1.00 64.19           C  
ANISOU 2646  C   GLU B 533     9606   6160   8626   2210    152   1109       C  
ATOM   2647  O   GLU B 533       7.081  -5.708   2.144  1.00 64.68           O  
ANISOU 2647  O   GLU B 533     9401   6486   8689   2226    307    927       O  
ATOM   2648  CB  GLU B 533       6.257  -8.538   1.222  1.00 69.55           C  
ANISOU 2648  CB  GLU B 533    10621   6277   9528   2243    413    838       C  
ATOM   2649  CG  GLU B 533       5.255  -9.490   0.596  1.00 74.47           C  
ANISOU 2649  CG  GLU B 533    11577   6640  10077   2044    543    759       C  
ATOM   2650  CD  GLU B 533       5.148 -10.807   1.343  1.00 83.54           C  
ANISOU 2650  CD  GLU B 533    13060   7343  11339   2085    332    971       C  
ATOM   2651  OE1 GLU B 533       4.230 -11.596   1.030  1.00 85.18           O  
ANISOU 2651  OE1 GLU B 533    13578   7332  11455   1864    405    952       O  
ATOM   2652  OE2 GLU B 533       5.984 -11.058   2.238  1.00 87.98           O  
ANISOU 2652  OE2 GLU B 533    13586   7762  12080   2323     72   1166       O  
ATOM   2653  N   GLY B 534       7.244  -6.949   4.006  1.00 66.77           N  
ANISOU 2653  N   GLY B 534     9972   6396   9004   2323   -146   1360       N  
ATOM   2654  CA  GLY B 534       8.263  -6.104   4.595  1.00 67.75           C  
ANISOU 2654  CA  GLY B 534     9794   6747   9202   2479   -309   1414       C  
ATOM   2655  C   GLY B 534       7.732  -5.323   5.775  1.00 66.43           C  
ANISOU 2655  C   GLY B 534     9701   6845   8693   2240   -456   1621       C  
ATOM   2656  O   GLY B 534       6.772  -5.735   6.422  1.00 67.41           O  
ANISOU 2656  O   GLY B 534    10135   6905   8572   2007   -506   1789       O  
ATOM   2657  N   SER B 535       8.358  -4.187   6.055  1.00 64.41           N  
ANISOU 2657  N   SER B 535     9164   6895   8414   2275   -507   1589       N  
ATOM   2658  CA  SER B 535       7.948  -3.366   7.181  1.00 64.70           C  
ANISOU 2658  CA  SER B 535     9257   7194   8132   2057   -634   1738       C  
ATOM   2659  C   SER B 535       7.703  -1.915   6.776  1.00 60.55           C  
ANISOU 2659  C   SER B 535     8514   7021   7471   1925   -444   1549       C  
ATOM   2660  O   SER B 535       7.900  -1.534   5.621  1.00 59.31           O  
ANISOU 2660  O   SER B 535     8174   6912   7450   1987   -236   1334       O  
ATOM   2661  CB  SER B 535       8.972  -3.460   8.316  1.00 69.97           C  
ANISOU 2661  CB  SER B 535     9874   7845   8867   2201  -1002   1957       C  
ATOM   2662  OG  SER B 535      10.292  -3.549   7.814  1.00 72.40           O  
ANISOU 2662  OG  SER B 535     9858   8085   9564   2530  -1074   1860       O  
ATOM   2663  N   SER B 536       7.252  -1.115   7.734  1.00 57.53           N  
ANISOU 2663  N   SER B 536     8180   6869   6808   1726   -517   1627       N  
ATOM   2664  CA  SER B 536       6.934   0.278   7.472  1.00 51.19           C  
ANISOU 2664  CA  SER B 536     7211   6357   5883   1599   -371   1458       C  
ATOM   2665  C   SER B 536       8.211   1.091   7.353  1.00 50.48           C  
ANISOU 2665  C   SER B 536     6813   6402   5965   1753   -456   1390       C  
ATOM   2666  O   SER B 536       9.297   0.611   7.682  1.00 50.36           O  
ANISOU 2666  O   SER B 536     6694   6299   6141   1946   -656   1487       O  
ATOM   2667  CB  SER B 536       6.071   0.847   8.593  1.00 46.29           C  
ANISOU 2667  CB  SER B 536     6735   5924   4929   1348   -407   1522       C  
ATOM   2668  OG  SER B 536       6.847   1.067   9.753  1.00 47.45           O  
ANISOU 2668  OG  SER B 536     6875   6158   4996   1363   -666   1668       O  
ATOM   2669  N   LEU B 537       8.072   2.325   6.880  1.00 47.02           N  
ANISOU 2669  N   LEU B 537     6225   6168   5473   1660   -320   1227       N  
ATOM   2670  CA  LEU B 537       9.201   3.238   6.766  1.00 45.93           C  
ANISOU 2670  CA  LEU B 537     5805   6181   5464   1734   -378   1153       C  
ATOM   2671  C   LEU B 537       9.735   3.571   8.157  1.00 47.99           C  
ANISOU 2671  C   LEU B 537     6052   6562   5619   1707   -657   1294       C  
ATOM   2672  O   LEU B 537      10.920   3.852   8.330  1.00 49.79           O  
ANISOU 2672  O   LEU B 537     6047   6863   6006   1815   -808   1302       O  
ATOM   2673  CB  LEU B 537       8.775   4.507   6.022  1.00 43.33           C  
ANISOU 2673  CB  LEU B 537     5398   6005   5061   1593   -195    978       C  
ATOM   2674  CG  LEU B 537       9.817   5.600   5.781  1.00 44.34           C  
ANISOU 2674  CG  LEU B 537     5266   6290   5292   1595   -216    888       C  
ATOM   2675  CD1 LEU B 537      11.049   5.032   5.100  1.00 47.52           C  
ANISOU 2675  CD1 LEU B 537     5436   6639   5982   1779   -186    845       C  
ATOM   2676  CD2 LEU B 537       9.215   6.726   4.952  1.00 40.19           C  
ANISOU 2676  CD2 LEU B 537     4748   5839   4682   1439    -49    747       C  
ATOM   2677  N   TYR B 538       8.849   3.525   9.147  1.00 48.14           N  
ANISOU 2677  N   TYR B 538     6317   6618   5355   1537   -720   1393       N  
ATOM   2678  CA  TYR B 538       9.222   3.789  10.529  1.00 49.59           C  
ANISOU 2678  CA  TYR B 538     6561   6924   5357   1455   -981   1529       C  
ATOM   2679  C   TYR B 538      10.221   2.755  11.027  1.00 54.03           C  
ANISOU 2679  C   TYR B 538     7115   7338   6075   1639  -1279   1742       C  
ATOM   2680  O   TYR B 538      11.244   3.103  11.613  1.00 55.87           O  
ANISOU 2680  O   TYR B 538     7190   7672   6365   1696  -1531   1804       O  
ATOM   2681  CB  TYR B 538       7.980   3.784  11.422  1.00 50.49           C  
ANISOU 2681  CB  TYR B 538     6970   7102   5112   1207   -933   1573       C  
ATOM   2682  CG  TYR B 538       8.258   4.151  12.863  1.00 55.24           C  
ANISOU 2682  CG  TYR B 538     7682   7862   5446   1058  -1169   1683       C  
ATOM   2683  CD1 TYR B 538       8.674   3.191  13.781  1.00 58.32           C  
ANISOU 2683  CD1 TYR B 538     8259   8156   5743   1061  -1454   1949       C  
ATOM   2684  CD2 TYR B 538       8.101   5.458  13.309  1.00 54.25           C  
ANISOU 2684  CD2 TYR B 538     7500   7963   5148    902  -1124   1520       C  
ATOM   2685  CE1 TYR B 538       8.931   3.523  15.096  1.00 59.64           C  
ANISOU 2685  CE1 TYR B 538     8561   8482   5618    889  -1691   2060       C  
ATOM   2686  CE2 TYR B 538       8.355   5.798  14.624  1.00 55.70           C  
ANISOU 2686  CE2 TYR B 538     7808   8302   5053    737  -1330   1594       C  
ATOM   2687  CZ  TYR B 538       8.770   4.827  15.512  1.00 60.42           C  
ANISOU 2687  CZ  TYR B 538     8598   8833   5526    718  -1614   1869       C  
ATOM   2688  OH  TYR B 538       9.023   5.159  16.821  1.00 65.40           O  
ANISOU 2688  OH  TYR B 538     9387   9630   5832    518  -1841   1954       O  
ATOM   2689  N   HIS B 539       9.912   1.483  10.797  1.00 56.88           N  
ANISOU 2689  N   HIS B 539     7650   7443   6519   1731  -1274   1855       N  
ATOM   2690  CA  HIS B 539      10.779   0.392  11.222  1.00 59.80           C  
ANISOU 2690  CA  HIS B 539     8042   7598   7082   1939  -1581   2068       C  
ATOM   2691  C   HIS B 539      12.161   0.486  10.586  1.00 62.56           C  
ANISOU 2691  C   HIS B 539     7987   7938   7843   2229  -1657   1970       C  
ATOM   2692  O   HIS B 539      13.174   0.332  11.267  1.00 66.38           O  
ANISOU 2692  O   HIS B 539     8340   8423   8457   2364  -1996   2109       O  
ATOM   2693  CB  HIS B 539      10.142  -0.955  10.883  1.00 61.08           C  
ANISOU 2693  CB  HIS B 539     8469   7438   7300   1986  -1516   2162       C  
ATOM   2694  CG  HIS B 539      10.976  -2.134  11.280  1.00 68.06           C  
ANISOU 2694  CG  HIS B 539     9410   8029   8422   2227  -1853   2386       C  
ATOM   2695  ND1 HIS B 539      12.025  -2.595  10.513  1.00 71.20           N  
ANISOU 2695  ND1 HIS B 539     9515   8258   9280   2576  -1893   2294       N  
ATOM   2696  CD2 HIS B 539      10.915  -2.946  12.361  1.00 71.86           C  
ANISOU 2696  CD2 HIS B 539    10209   8339   8755   2169  -2177   2696       C  
ATOM   2697  CE1 HIS B 539      12.576  -3.638  11.108  1.00 75.71           C  
ANISOU 2697  CE1 HIS B 539    10200   8546  10019   2763  -2249   2533       C  
ATOM   2698  NE2 HIS B 539      11.923  -3.872  12.231  1.00 76.22           N  
ANISOU 2698  NE2 HIS B 539    10645   8606   9708   2501  -2426   2794       N  
ATOM   2699  N   HIS B 540      12.198   0.737   9.281  1.00 61.12           N  
ANISOU 2699  N   HIS B 540     7603   7762   7859   2306  -1344   1728       N  
ATOM   2700  CA  HIS B 540      13.463   0.844   8.561  1.00 63.02           C  
ANISOU 2700  CA  HIS B 540     7437   8027   8482   2542  -1330   1584       C  
ATOM   2701  C   HIS B 540      14.316   1.995   9.082  1.00 62.69           C  
ANISOU 2701  C   HIS B 540     7122   8273   8425   2477  -1488   1560       C  
ATOM   2702  O   HIS B 540      15.534   1.879   9.193  1.00 67.55           O  
ANISOU 2702  O   HIS B 540     7419   8914   9334   2671  -1684   1565       O  
ATOM   2703  CB  HIS B 540      13.214   1.031   7.064  1.00 62.74           C  
ANISOU 2703  CB  HIS B 540     7295   7987   8556   2541   -924   1320       C  
ATOM   2704  CG  HIS B 540      12.664  -0.184   6.386  1.00 66.01           C  
ANISOU 2704  CG  HIS B 540     7908   8103   9070   2644   -776   1296       C  
ATOM   2705  ND1 HIS B 540      11.331  -0.316   6.058  1.00 65.20           N  
ANISOU 2705  ND1 HIS B 540     8113   7941   8719   2448   -580   1281       N  
ATOM   2706  CD2 HIS B 540      13.266  -1.326   5.975  1.00 67.84           C  
ANISOU 2706  CD2 HIS B 540     8067   8068   9640   2922   -800   1266       C  
ATOM   2707  CE1 HIS B 540      11.137  -1.485   5.474  1.00 65.42           C  
ANISOU 2707  CE1 HIS B 540     8272   7682   8902   2572   -492   1252       C  
ATOM   2708  NE2 HIS B 540      12.295  -2.117   5.410  1.00 66.35           N  
ANISOU 2708  NE2 HIS B 540     8175   7655   9378   2868   -616   1235       N  
ATOM   2709  N   LEU B 541      13.662   3.104   9.401  1.00 58.26           N  
ANISOU 2709  N   LEU B 541     6673   7921   7542   2204  -1406   1517       N  
ATOM   2710  CA  LEU B 541      14.354   4.309   9.832  1.00 57.08           C  
ANISOU 2710  CA  LEU B 541     6306   8034   7348   2091  -1522   1463       C  
ATOM   2711  C   LEU B 541      14.746   4.284  11.309  1.00 60.66           C  
ANISOU 2711  C   LEU B 541     6840   8561   7647   2043  -1933   1675       C  
ATOM   2712  O   LEU B 541      15.842   4.711  11.673  1.00 62.94           O  
ANISOU 2712  O   LEU B 541     6852   8991   8073   2085  -2162   1681       O  
ATOM   2713  CB  LEU B 541      13.490   5.540   9.545  1.00 53.24           C  
ANISOU 2713  CB  LEU B 541     5924   7699   6606   1832  -1277   1309       C  
ATOM   2714  CG  LEU B 541      13.757   6.335   8.265  1.00 51.96           C  
ANISOU 2714  CG  LEU B 541     5539   7611   6592   1800   -997   1089       C  
ATOM   2715  CD1 LEU B 541      14.098   5.428   7.090  1.00 53.59           C  
ANISOU 2715  CD1 LEU B 541     5611   7668   7085   1999   -807   1010       C  
ATOM   2716  CD2 LEU B 541      12.553   7.207   7.934  1.00 47.30           C  
ANISOU 2716  CD2 LEU B 541     5160   7056   5757   1589   -784    986       C  
ATOM   2717  N   HIS B 542      13.857   3.783  12.160  1.00 59.39           N  
ANISOU 2717  N   HIS B 542     7061   8319   7184   1926  -2030   1847       N  
ATOM   2718  CA  HIS B 542      14.036   3.952  13.597  1.00 59.75           C  
ANISOU 2718  CA  HIS B 542     7267   8480   6957   1779  -2382   2034       C  
ATOM   2719  C   HIS B 542      14.226   2.657  14.383  1.00 65.66           C  
ANISOU 2719  C   HIS B 542     8225   9019   7702   1889  -2733   2340       C  
ATOM   2720  O   HIS B 542      14.760   2.680  15.489  1.00 67.02           O  
ANISOU 2720  O   HIS B 542     8461   9272   7732   1824  -3116   2523       O  
ATOM   2721  CB  HIS B 542      12.862   4.740  14.181  1.00 55.93           C  
ANISOU 2721  CB  HIS B 542     7078   8149   6024   1453  -2218   1964       C  
ATOM   2722  CG  HIS B 542      12.532   5.982  13.414  1.00 54.74           C  
ANISOU 2722  CG  HIS B 542     6776   8137   5884   1355  -1902   1683       C  
ATOM   2723  ND1 HIS B 542      13.452   6.982  13.188  1.00 54.72           N  
ANISOU 2723  ND1 HIS B 542     6474   8289   6028   1354  -1948   1554       N  
ATOM   2724  CD2 HIS B 542      11.384   6.383  12.818  1.00 53.64           C  
ANISOU 2724  CD2 HIS B 542     6751   7990   5641   1250  -1563   1520       C  
ATOM   2725  CE1 HIS B 542      12.886   7.947  12.486  1.00 53.44           C  
ANISOU 2725  CE1 HIS B 542     6285   8182   5838   1247  -1657   1339       C  
ATOM   2726  NE2 HIS B 542      11.631   7.609  12.249  1.00 52.85           N  
ANISOU 2726  NE2 HIS B 542     6448   8009   5622   1200  -1434   1315       N  
ATOM   2727  N   ALA B 543      13.791   1.534  13.825  1.00 68.98           N  
ANISOU 2727  N   ALA B 543     8783   9158   8268   2037  -2623   2401       N  
ATOM   2728  CA  ALA B 543      13.858   0.271  14.552  1.00 74.83           C  
ANISOU 2728  CA  ALA B 543     9791   9650   8993   2114  -2929   2694       C  
ATOM   2729  C   ALA B 543      14.792  -0.732  13.892  1.00 82.17           C  
ANISOU 2729  C   ALA B 543    10470  10326  10425   2493  -2987   2684       C  
ATOM   2730  O   ALA B 543      14.700  -1.931  14.148  1.00 84.88           O  
ANISOU 2730  O   ALA B 543    11029  10402  10820   2573  -3071   2846       O  
ATOM   2731  CB  ALA B 543      12.467  -0.324  14.712  1.00 71.67           C  
ANISOU 2731  CB  ALA B 543     9848   9109   8276   1900  -2760   2794       C  
ATOM   2732  N   SER B 544      15.698  -0.248  13.051  1.00 85.85           N  
ANISOU 2732  N   SER B 544    10475  10880  11265   2706  -2921   2478       N  
ATOM   2733  CA  SER B 544      16.546  -1.155  12.288  1.00 92.43           C  
ANISOU 2733  CA  SER B 544    11036  11498  12585   3059  -2882   2394       C  
ATOM   2734  C   SER B 544      17.928  -0.602  11.969  1.00 95.48           C  
ANISOU 2734  C   SER B 544    10884  12085  13308   3235  -2927   2215       C  
ATOM   2735  O   SER B 544      18.209   0.580  12.160  1.00 94.28           O  
ANISOU 2735  O   SER B 544    10543  12233  13046   3078  -2961   2132       O  
ATOM   2736  CB  SER B 544      15.844  -1.567  10.993  1.00 92.72           C  
ANISOU 2736  CB  SER B 544    11117  11318  12794   3158  -2534   2229       C  
ATOM   2737  OG  SER B 544      16.723  -2.279  10.143  1.00 97.39           O  
ANISOU 2737  OG  SER B 544    11397  11748  13857   3479  -2423   2067       O  
ATOM   2738  N   GLU B 545      18.785  -1.484  11.471  1.00101.21           N  
ANISOU 2738  N   GLU B 545    11367  12642  14448   3545  -2912   2142       N  
ATOM   2739  CA  GLU B 545      20.153  -1.132  11.129  1.00107.25           C  
ANISOU 2739  CA  GLU B 545    11596  13592  15562   3718  -2924   1959       C  
ATOM   2740  C   GLU B 545      20.257  -0.753   9.658  1.00106.87           C  
ANISOU 2740  C   GLU B 545    11228  13602  15775   3788  -2490   1626       C  
ATOM   2741  O   GLU B 545      21.138  -1.239   8.948  1.00110.65           O  
ANISOU 2741  O   GLU B 545    11373  14037  16632   4025  -2348   1442       O  
ATOM   2742  CB  GLU B 545      21.084  -2.307  11.424  1.00113.86           C  
ANISOU 2742  CB  GLU B 545    12323  14226  16711   4017  -3142   2047       C  
ATOM   2743  CG  GLU B 545      20.845  -2.961  12.774  1.00118.32           C  
ANISOU 2743  CG  GLU B 545    13286  14644  17026   3953  -3542   2393       C  
ATOM   2744  CD  GLU B 545      21.661  -4.225  12.954  1.00126.01           C  
ANISOU 2744  CD  GLU B 545    14184  15346  18348   4272  -3758   2484       C  
ATOM   2745  OE1 GLU B 545      22.562  -4.472  12.124  1.00129.03           O  
ANISOU 2745  OE1 GLU B 545    14145  15712  19170   4548  -3619   2260       O  
ATOM   2746  OE2 GLU B 545      21.400  -4.975  13.919  1.00129.18           O  
ANISOU 2746  OE2 GLU B 545    14951  15549  18583   4236  -4059   2772       O  
ATOM   2747  N   PHE B 548      19.732   3.266   4.707  1.00 82.09           N  
ANISOU 2747  N   PHE B 548     7385  11293  12512   3009   -669    455       N  
ATOM   2748  CA  PHE B 548      19.385   3.647   3.342  1.00 80.18           C  
ANISOU 2748  CA  PHE B 548     7186  11108  12172   2831   -199    223       C  
ATOM   2749  C   PHE B 548      20.318   4.720   2.796  1.00 81.26           C  
ANISOU 2749  C   PHE B 548     6940  11551  12383   2639    -19     36       C  
ATOM   2750  O   PHE B 548      20.623   5.698   3.479  1.00 81.83           O  
ANISOU 2750  O   PHE B 548     6923  11818  12351   2464   -215    122       O  
ATOM   2751  CB  PHE B 548      17.939   4.144   3.268  1.00 74.54           C  
ANISOU 2751  CB  PHE B 548     6964  10349  11011   2567   -106    321       C  
ATOM   2752  CG  PHE B 548      16.918   3.044   3.261  1.00 72.82           C  
ANISOU 2752  CG  PHE B 548     7114   9840  10713   2684   -100    410       C  
ATOM   2753  CD1 PHE B 548      17.193   1.831   2.653  1.00 75.66           C  
ANISOU 2753  CD1 PHE B 548     7409   9983  11354   2939     23    295       C  
ATOM   2754  CD2 PHE B 548      15.683   3.224   3.863  1.00 68.08           C  
ANISOU 2754  CD2 PHE B 548     6917   9183   9770   2527   -204    586       C  
ATOM   2755  CE1 PHE B 548      16.255   0.815   2.643  1.00 74.29           C  
ANISOU 2755  CE1 PHE B 548     7597   9523  11107   3015     22    376       C  
ATOM   2756  CE2 PHE B 548      14.739   2.212   3.858  1.00 66.56           C  
ANISOU 2756  CE2 PHE B 548     7051   8738   9502   2592   -189    665       C  
ATOM   2757  CZ  PHE B 548      15.026   1.005   3.246  1.00 69.70           C  
ANISOU 2757  CZ  PHE B 548     7411   8904  10168   2826    -86    572       C  
ATOM   2758  N   GLU B 549      20.769   4.532   1.561  1.00 81.19           N  
ANISOU 2758  N   GLU B 549     6723  11586  12538   2641    369   -232       N  
ATOM   2759  CA  GLU B 549      21.568   5.546   0.889  1.00 80.87           C  
ANISOU 2759  CA  GLU B 549     6368  11842  12519   2386    612   -420       C  
ATOM   2760  C   GLU B 549      20.661   6.656   0.385  1.00 75.87           C  
ANISOU 2760  C   GLU B 549     6110  11274  11443   1986    780   -378       C  
ATOM   2761  O   GLU B 549      19.462   6.448   0.209  1.00 73.99           O  
ANISOU 2761  O   GLU B 549     6311  10857  10947   1949    814   -287       O  
ATOM   2762  CB  GLU B 549      22.374   4.930  -0.251  1.00 85.15           C  
ANISOU 2762  CB  GLU B 549     6560  12424  13368   2499    999   -744       C  
ATOM   2763  CG  GLU B 549      23.610   4.193   0.229  1.00 91.75           C  
ANISOU 2763  CG  GLU B 549     6959  13259  14644   2818    822   -777       C  
ATOM   2764  CD  GLU B 549      24.227   3.334  -0.850  1.00 97.00           C  
ANISOU 2764  CD  GLU B 549     7504  13873  15480   2935   1185  -1025       C  
ATOM   2765  OE1 GLU B 549      23.899   3.545  -2.037  1.00 96.11           O  
ANISOU 2765  OE1 GLU B 549     7531  13812  15175   2708   1610  -1222       O  
ATOM   2766  OE2 GLU B 549      25.030   2.440  -0.510  1.00101.82           O  
ANISOU 2766  OE2 GLU B 549     7902  14391  16395   3245   1033  -1025       O  
ATOM   2767  N   MET B 550      21.238   7.831   0.162  1.00 74.43           N  
ANISOU 2767  N   MET B 550     5749  11338  11194   1687    865   -441       N  
ATOM   2768  CA  MET B 550      20.468   9.027  -0.165  1.00 69.56           C  
ANISOU 2768  CA  MET B 550     5482  10757  10191   1313    937   -369       C  
ATOM   2769  C   MET B 550      19.528   8.818  -1.350  1.00 66.33           C  
ANISOU 2769  C   MET B 550     5433  10219   9551   1199   1244   -432       C  
ATOM   2770  O   MET B 550      18.372   9.235  -1.315  1.00 62.86           O  
ANISOU 2770  O   MET B 550     5407   9659   8820   1077   1168   -295       O  
ATOM   2771  CB  MET B 550      21.406  10.209  -0.431  1.00 70.39           C  
ANISOU 2771  CB  MET B 550     5316  11125  10306    990   1032   -460       C  
ATOM   2772  CG  MET B 550      20.689  11.531  -0.657  1.00 67.38           C  
ANISOU 2772  CG  MET B 550     5303  10737   9561    612   1037   -362       C  
ATOM   2773  SD  MET B 550      19.579  11.949   0.701  1.00 73.76           S  
ANISOU 2773  SD  MET B 550     6485  11382  10158    674    618   -115       S  
ATOM   2774  CE  MET B 550      20.710  11.913   2.086  1.00 98.63           C  
ANISOU 2774  CE  MET B 550     9223  14691  13562    815    267    -74       C  
ATOM   2775  N   LYS B 551      20.026   8.154  -2.388  1.00 67.58           N  
ANISOU 2775  N   LYS B 551     5420  10408   9849   1241   1583   -656       N  
ATOM   2776  CA  LYS B 551      19.252   7.932  -3.605  1.00 66.71           C  
ANISOU 2776  CA  LYS B 551     5641  10203   9502   1095   1886   -742       C  
ATOM   2777  C   LYS B 551      17.972   7.142  -3.331  1.00 62.46           C  
ANISOU 2777  C   LYS B 551     5494   9391   8845   1282   1741   -606       C  
ATOM   2778  O   LYS B 551      16.941   7.377  -3.962  1.00 60.33           O  
ANISOU 2778  O   LYS B 551     5606   9036   8280   1098   1818   -560       O  
ATOM   2779  CB  LYS B 551      20.112   7.237  -4.668  1.00 72.27           C  
ANISOU 2779  CB  LYS B 551     6064  10998  10398   1128   2293  -1054       C  
ATOM   2780  CG  LYS B 551      19.354   6.819  -5.919  1.00 74.32           C  
ANISOU 2780  CG  LYS B 551     6677  11154  10407    990   2604  -1170       C  
ATOM   2781  CD  LYS B 551      20.296   6.523  -7.078  1.00 82.28           C  
ANISOU 2781  CD  LYS B 551     7417  12333  11513    878   3075  -1515       C  
ATOM   2782  CE  LYS B 551      19.551   5.883  -8.247  1.00 84.64           C  
ANISOU 2782  CE  LYS B 551     8096  12500  11563    780   3348  -1642       C  
ATOM   2783  NZ  LYS B 551      20.104   6.312  -9.570  1.00 88.54           N  
ANISOU 2783  NZ  LYS B 551     8657  13167  11818    401   3663  -1785       N  
ATOM   2784  N   LYS B 552      18.037   6.215  -2.383  1.00 62.55           N  
ANISOU 2784  N   LYS B 552     5411   9266   9089   1628   1509   -532       N  
ATOM   2785  CA  LYS B 552      16.853   5.470  -1.971  1.00 60.73           C  
ANISOU 2785  CA  LYS B 552     5543   8785   8745   1772   1352   -383       C  
ATOM   2786  C   LYS B 552      15.929   6.368  -1.160  1.00 55.74           C  
ANISOU 2786  C   LYS B 552     5179   8157   7842   1619   1091   -154       C  
ATOM   2787  O   LYS B 552      14.709   6.317  -1.314  1.00 52.68           O  
ANISOU 2787  O   LYS B 552     5145   7645   7227   1543   1082    -75       O  
ATOM   2788  CB  LYS B 552      17.242   4.247  -1.142  1.00 66.54           C  
ANISOU 2788  CB  LYS B 552     6130   9356   9796   2156   1153   -341       C  
ATOM   2789  CG  LYS B 552      16.056   3.414  -0.677  1.00 68.32           C  
ANISOU 2789  CG  LYS B 552     6741   9317   9901   2267    998   -177       C  
ATOM   2790  CD  LYS B 552      15.402   2.694  -1.846  1.00 72.48           C  
ANISOU 2790  CD  LYS B 552     7504   9688  10348   2233   1291   -329       C  
ATOM   2791  CE  LYS B 552      15.507   1.181  -1.693  1.00 78.63           C  
ANISOU 2791  CE  LYS B 552     8298  10183  11397   2555   1254   -366       C  
ATOM   2792  NZ  LYS B 552      14.573   0.652  -0.653  1.00 78.42           N  
ANISOU 2792  NZ  LYS B 552     8574   9953  11267   2627    953   -103       N  
ATOM   2793  N   LEU B 553      16.517   7.189  -0.296  1.00 55.79           N  
ANISOU 2793  N   LEU B 553     4998   8313   7887   1571    882    -73       N  
ATOM   2794  CA  LEU B 553      15.745   8.110   0.531  1.00 53.06           C  
ANISOU 2794  CA  LEU B 553     4878   7978   7304   1428    652     96       C  
ATOM   2795  C   LEU B 553      14.954   9.093  -0.328  1.00 50.87           C  
ANISOU 2795  C   LEU B 553     4860   7706   6761   1137    797     77       C  
ATOM   2796  O   LEU B 553      13.785   9.369  -0.054  1.00 47.49           O  
ANISOU 2796  O   LEU B 553     4727   7181   6138   1086    695    175       O  
ATOM   2797  CB  LEU B 553      16.663   8.862   1.495  1.00 54.41           C  
ANISOU 2797  CB  LEU B 553     4789   8319   7565   1392    426    144       C  
ATOM   2798  CG  LEU B 553      17.369   8.015   2.557  1.00 56.71           C  
ANISOU 2798  CG  LEU B 553     4855   8601   8093   1670    166    220       C  
ATOM   2799  CD1 LEU B 553      18.416   8.835   3.294  1.00 58.51           C  
ANISOU 2799  CD1 LEU B 553     4779   9036   8415   1586    -39    232       C  
ATOM   2800  CD2 LEU B 553      16.365   7.426   3.537  1.00 54.71           C  
ANISOU 2800  CD2 LEU B 553     4916   8182   7691   1785    -61    405       C  
ATOM   2801  N   ILE B 554      15.595   9.610  -1.372  1.00 51.16           N  
ANISOU 2801  N   ILE B 554     4783   7859   6798    941   1030    -50       N  
ATOM   2802  CA  ILE B 554      14.930  10.514  -2.301  1.00 49.54           C  
ANISOU 2802  CA  ILE B 554     4848   7637   6337    648   1144    -45       C  
ATOM   2803  C   ILE B 554      13.782   9.793  -2.997  1.00 48.20           C  
ANISOU 2803  C   ILE B 554     4984   7303   6027    685   1238    -43       C  
ATOM   2804  O   ILE B 554      12.671  10.314  -3.080  1.00 49.51           O  
ANISOU 2804  O   ILE B 554     5437   7375   6000    581   1135     51       O  
ATOM   2805  CB  ILE B 554      15.900  11.063  -3.369  1.00 54.48           C  
ANISOU 2805  CB  ILE B 554     5319   8424   6956    387   1407   -180       C  
ATOM   2806  CG1 ILE B 554      17.108  11.737  -2.714  1.00 58.25           C  
ANISOU 2806  CG1 ILE B 554     5447   9086   7598    323   1324   -201       C  
ATOM   2807  CG2 ILE B 554      15.186  12.045  -4.286  1.00 51.95           C  
ANISOU 2807  CG2 ILE B 554     5339   8055   6343     59   1461   -123       C  
ATOM   2808  CD1 ILE B 554      16.764  12.987  -1.939  1.00 57.96           C  
ANISOU 2808  CD1 ILE B 554     5553   9030   7438    170   1058    -61       C  
ATOM   2809  N   ASP B 555      14.052   8.587  -3.486  1.00 48.58           N  
ANISOU 2809  N   ASP B 555     4954   7307   6196    841   1422   -163       N  
ATOM   2810  CA  ASP B 555      13.052   7.813  -4.215  1.00 49.98           C  
ANISOU 2810  CA  ASP B 555     5414   7332   6245    853   1526   -189       C  
ATOM   2811  C   ASP B 555      11.830   7.486  -3.366  1.00 46.18           C  
ANISOU 2811  C   ASP B 555     5148   6698   5701    979   1290    -35       C  
ATOM   2812  O   ASP B 555      10.705   7.467  -3.865  1.00 44.47           O  
ANISOU 2812  O   ASP B 555     5204   6389   5303    881   1289     -2       O  
ATOM   2813  CB  ASP B 555      13.655   6.521  -4.764  1.00 56.42           C  
ANISOU 2813  CB  ASP B 555     6094   8102   7243   1023   1762   -375       C  
ATOM   2814  CG  ASP B 555      12.700   5.785  -5.680  1.00 59.58           C  
ANISOU 2814  CG  ASP B 555     6803   8354   7480    971   1900   -436       C  
ATOM   2815  OD1 ASP B 555      12.189   6.413  -6.633  1.00 60.68           O  
ANISOU 2815  OD1 ASP B 555     7166   8534   7354    690   1990   -442       O  
ATOM   2816  OD2 ASP B 555      12.445   4.586  -5.440  1.00 61.18           O  
ANISOU 2816  OD2 ASP B 555     7046   8387   7813   1196   1891   -467       O  
ATOM   2817  N   ILE B 556      12.061   7.216  -2.085  1.00 45.25           N  
ANISOU 2817  N   ILE B 556     4900   6569   5725   1177   1088     56       N  
ATOM   2818  CA  ILE B 556      10.973   6.984  -1.143  1.00 40.89           C  
ANISOU 2818  CA  ILE B 556     4537   5912   5089   1253    883    196       C  
ATOM   2819  C   ILE B 556      10.145   8.250  -0.974  1.00 37.48           C  
ANISOU 2819  C   ILE B 556     4252   5524   4465   1067    768    264       C  
ATOM   2820  O   ILE B 556       8.917   8.201  -0.948  1.00 37.11           O  
ANISOU 2820  O   ILE B 556     4413   5393   4293   1032    718    308       O  
ATOM   2821  CB  ILE B 556      11.510   6.537   0.230  1.00 44.29           C  
ANISOU 2821  CB  ILE B 556     4819   6344   5666   1453    675    293       C  
ATOM   2822  CG1 ILE B 556      12.142   5.145   0.120  1.00 47.03           C  
ANISOU 2822  CG1 ILE B 556     5057   6570   6243   1689    734    244       C  
ATOM   2823  CG2 ILE B 556      10.399   6.534   1.266  1.00 41.44           C  
ANISOU 2823  CG2 ILE B 556     4665   5927   5153   1449    488    430       C  
ATOM   2824  CD1 ILE B 556      12.821   4.670   1.391  1.00 47.14           C  
ANISOU 2824  CD1 ILE B 556     4917   6568   6426   1896    482    363       C  
ATOM   2825  N   ALA B 557      10.826   9.384  -0.867  1.00 34.01           N  
ANISOU 2825  N   ALA B 557     3689   5204   4028    947    724    258       N  
ATOM   2826  CA  ALA B 557      10.150  10.671  -0.760  1.00 35.70           C  
ANISOU 2826  CA  ALA B 557     4042   5420   4102    782    608    302       C  
ATOM   2827  C   ALA B 557       9.308  10.951  -2.002  1.00 35.47           C  
ANISOU 2827  C   ALA B 557     4237   5311   3931    625    695    287       C  
ATOM   2828  O   ALA B 557       8.181  11.437  -1.904  1.00 33.04           O  
ANISOU 2828  O   ALA B 557     4097   4923   3534    590    575    331       O  
ATOM   2829  CB  ALA B 557      11.160  11.783  -0.547  1.00 36.59           C  
ANISOU 2829  CB  ALA B 557     3998   5650   4255    652    558    289       C  
ATOM   2830  N   ARG B 558       9.872  10.647  -3.168  1.00 38.43           N  
ANISOU 2830  N   ARG B 558     4602   5713   4288    527    901    214       N  
ATOM   2831  CA  ARG B 558       9.188  10.850  -4.439  1.00 40.38           C  
ANISOU 2831  CA  ARG B 558     5087   5898   4359    340    975    209       C  
ATOM   2832  C   ARG B 558       7.916  10.017  -4.557  1.00 38.02           C  
ANISOU 2832  C   ARG B 558     4964   5479   4002    428    935    226       C  
ATOM   2833  O   ARG B 558       6.863  10.537  -4.917  1.00 37.78           O  
ANISOU 2833  O   ARG B 558     5121   5377   3858    332    811    283       O  
ATOM   2834  CB  ARG B 558      10.127  10.539  -5.607  1.00 47.33           C  
ANISOU 2834  CB  ARG B 558     5922   6862   5201    197   1248     95       C  
ATOM   2835  CG  ARG B 558       9.430  10.438  -6.956  1.00 51.24           C  
ANISOU 2835  CG  ARG B 558     6699   7299   5473     -3   1340     79       C  
ATOM   2836  CD  ARG B 558      10.436  10.345  -8.087  1.00 58.07           C  
ANISOU 2836  CD  ARG B 558     7532   8282   6250   -213   1641    -54       C  
ATOM   2837  NE  ARG B 558      11.435   9.311  -7.840  1.00 63.18           N  
ANISOU 2837  NE  ARG B 558     7891   9001   7114    -15   1859   -223       N  
ATOM   2838  CZ  ARG B 558      12.547   9.161  -8.553  1.00 67.61           C  
ANISOU 2838  CZ  ARG B 558     8292   9703   7695   -134   2160   -397       C  
ATOM   2839  NH1 ARG B 558      12.804   9.983  -9.559  1.00 70.65           N  
ANISOU 2839  NH1 ARG B 558     8814  10188   7842   -497   2293   -407       N  
ATOM   2840  NH2 ARG B 558      13.404   8.195  -8.257  1.00 68.92           N  
ANISOU 2840  NH2 ARG B 558     8158   9906   8123    105   2323   -564       N  
ATOM   2841  N   GLN B 559       8.016   8.727  -4.251  1.00 38.14           N  
ANISOU 2841  N   GLN B 559     4914   5462   4116    607   1022    177       N  
ATOM   2842  CA  GLN B 559       6.868   7.832  -4.341  1.00 37.97           C  
ANISOU 2842  CA  GLN B 559     5056   5325   4045    661   1001    185       C  
ATOM   2843  C   GLN B 559       5.752   8.255  -3.399  1.00 36.66           C  
ANISOU 2843  C   GLN B 559     4937   5131   3862    702    789    278       C  
ATOM   2844  O   GLN B 559       4.572   8.133  -3.724  1.00 38.18           O  
ANISOU 2844  O   GLN B 559     5272   5262   3974    646    731    290       O  
ATOM   2845  CB  GLN B 559       7.280   6.391  -4.034  1.00 37.78           C  
ANISOU 2845  CB  GLN B 559     4964   5232   4158    850   1110    130       C  
ATOM   2846  CG  GLN B 559       8.199   5.775  -5.066  1.00 39.20           C  
ANISOU 2846  CG  GLN B 559     5099   5415   4381    834   1361    -25       C  
ATOM   2847  CD  GLN B 559       8.465   4.309  -4.797  1.00 41.42           C  
ANISOU 2847  CD  GLN B 559     5343   5560   4834   1051   1440    -91       C  
ATOM   2848  OE1 GLN B 559       7.536   3.511  -4.670  1.00 40.04           O  
ANISOU 2848  OE1 GLN B 559     5343   5245   4625   1082   1392    -59       O  
ATOM   2849  NE2 GLN B 559       9.739   3.946  -4.706  1.00 43.51           N  
ANISOU 2849  NE2 GLN B 559     5371   5853   5308   1200   1550   -188       N  
ATOM   2850  N   THR B 560       6.135   8.745  -2.226  1.00 34.52           N  
ANISOU 2850  N   THR B 560     4530   4918   3667    789    680    322       N  
ATOM   2851  CA  THR B 560       5.169   9.195  -1.238  1.00 33.86           C  
ANISOU 2851  CA  THR B 560     4470   4833   3563    819    520    365       C  
ATOM   2852  C   THR B 560       4.494  10.475  -1.712  1.00 34.81           C  
ANISOU 2852  C   THR B 560     4667   4933   3626    697    411    364       C  
ATOM   2853  O   THR B 560       3.300  10.673  -1.500  1.00 35.82           O  
ANISOU 2853  O   THR B 560     4847   5023   3740    702    317    357       O  
ATOM   2854  CB  THR B 560       5.835   9.425   0.132  1.00 34.98           C  
ANISOU 2854  CB  THR B 560     4474   5053   3763    912    433    396       C  
ATOM   2855  OG1 THR B 560       6.545   8.241   0.518  1.00 35.03           O  
ANISOU 2855  OG1 THR B 560     4413   5049   3848   1041    483    424       O  
ATOM   2856  CG2 THR B 560       4.794   9.747   1.189  1.00 33.69           C  
ANISOU 2856  CG2 THR B 560     4349   4903   3547    924    321    402       C  
ATOM   2857  N   ALA B 561       5.265  11.337  -2.366  1.00 37.13           N  
ANISOU 2857  N   ALA B 561     4961   5242   3903    581    419    368       N  
ATOM   2858  CA  ALA B 561       4.721  12.573  -2.914  1.00 35.25           C  
ANISOU 2858  CA  ALA B 561     4839   4935   3620    455    280    395       C  
ATOM   2859  C   ALA B 561       3.732  12.261  -4.032  1.00 36.84           C  
ANISOU 2859  C   ALA B 561     5210   5057   3731    375    258    413       C  
ATOM   2860  O   ALA B 561       2.685  12.896  -4.135  1.00 37.84           O  
ANISOU 2860  O   ALA B 561     5406   5101   3870    367     79    434       O  
ATOM   2861  CB  ALA B 561       5.839  13.470  -3.418  1.00 34.56           C  
ANISOU 2861  CB  ALA B 561     4751   4874   3507    297    306    416       C  
ATOM   2862  N   ARG B 562       4.074  11.281  -4.866  1.00 35.64           N  
ANISOU 2862  N   ARG B 562     5114   4926   3500    319    430    389       N  
ATOM   2863  CA  ARG B 562       3.201  10.843  -5.954  1.00 33.38           C  
ANISOU 2863  CA  ARG B 562     5007   4581   3095    212    414    393       C  
ATOM   2864  C   ARG B 562       1.854  10.374  -5.428  1.00 33.44           C  
ANISOU 2864  C   ARG B 562     4997   4548   3162    318    302    385       C  
ATOM   2865  O   ARG B 562       0.810  10.742  -5.957  1.00 34.99           O  
ANISOU 2865  O   ARG B 562     5282   4687   3325    253    134    414       O  
ATOM   2866  CB  ARG B 562       3.854   9.709  -6.738  1.00 32.33           C  
ANISOU 2866  CB  ARG B 562     4923   4478   2882    156    660    317       C  
ATOM   2867  CG  ARG B 562       4.985  10.143  -7.639  1.00 34.63           C  
ANISOU 2867  CG  ARG B 562     5258   4833   3068    -26    809    293       C  
ATOM   2868  CD  ARG B 562       5.708   8.939  -8.193  1.00 33.56           C  
ANISOU 2868  CD  ARG B 562     5104   4736   2913    -24   1097    155       C  
ATOM   2869  NE  ARG B 562       6.725   9.316  -9.164  1.00 43.60           N  
ANISOU 2869  NE  ARG B 562     6411   6100   4057   -242   1292     93       N  
ATOM   2870  CZ  ARG B 562       7.499   8.447  -9.804  1.00 47.09           C  
ANISOU 2870  CZ  ARG B 562     6819   6596   4477   -274   1590    -76       C  
ATOM   2871  NH1 ARG B 562       7.373   7.149  -9.567  1.00 47.73           N  
ANISOU 2871  NH1 ARG B 562     6852   6606   4678    -78   1692   -183       N  
ATOM   2872  NH2 ARG B 562       8.398   8.874 -10.680  1.00 48.22           N  
ANISOU 2872  NH2 ARG B 562     6982   6855   4484   -512   1796   -150       N  
ATOM   2873  N   GLY B 563       1.887   9.551  -4.387  1.00 34.24           N  
ANISOU 2873  N   GLY B 563     4978   4683   3350    467    385    349       N  
ATOM   2874  CA  GLY B 563       0.672   9.061  -3.766  1.00 34.13           C  
ANISOU 2874  CA  GLY B 563     4930   4658   3378    529    322    331       C  
ATOM   2875  C   GLY B 563      -0.154  10.185  -3.171  1.00 33.87           C  
ANISOU 2875  C   GLY B 563     4813   4630   3424    569    139    323       C  
ATOM   2876  O   GLY B 563      -1.358  10.266  -3.409  1.00 36.24           O  
ANISOU 2876  O   GLY B 563     5109   4908   3753    548     26    300       O  
ATOM   2877  N   MET B 564       0.492  11.059  -2.403  1.00 29.21           N  
ANISOU 2877  N   MET B 564     4142   4068   2890    629    106    322       N  
ATOM   2878  CA  MET B 564      -0.202  12.191  -1.792  1.00 27.02           C  
ANISOU 2878  CA  MET B 564     3787   3770   2710    684    -50    273       C  
ATOM   2879  C   MET B 564      -0.753  13.158  -2.833  1.00 27.97           C  
ANISOU 2879  C   MET B 564     3997   3771   2859    620   -248    306       C  
ATOM   2880  O   MET B 564      -1.863  13.666  -2.688  1.00 34.86           O  
ANISOU 2880  O   MET B 564     4803   4597   3848    682   -399    250       O  
ATOM   2881  CB  MET B 564       0.721  12.934  -0.829  1.00 26.92           C  
ANISOU 2881  CB  MET B 564     3704   3794   2728    730    -48    254       C  
ATOM   2882  CG  MET B 564       1.160  12.104   0.355  1.00 30.53           C  
ANISOU 2882  CG  MET B 564     4083   4363   3154    795     75    239       C  
ATOM   2883  SD  MET B 564      -0.247  11.507   1.310  1.00 40.37           S  
ANISOU 2883  SD  MET B 564     5263   5673   4403    838    111    153       S  
ATOM   2884  CE  MET B 564      -1.012  13.057   1.780  1.00 30.27           C  
ANISOU 2884  CE  MET B 564     3895   4365   3242    886    -23     10       C  
ATOM   2885  N   ASP B 565       0.032  13.409  -3.877  1.00 29.08           N  
ANISOU 2885  N   ASP B 565     4286   3864   2898    488   -252    396       N  
ATOM   2886  CA  ASP B 565      -0.394  14.266  -4.976  1.00 31.09           C  
ANISOU 2886  CA  ASP B 565     4694   3990   3128    379   -466    475       C  
ATOM   2887  C   ASP B 565      -1.611  13.668  -5.659  1.00 33.39           C  
ANISOU 2887  C   ASP B 565     5022   4263   3403    357   -567    478       C  
ATOM   2888  O   ASP B 565      -2.541  14.377  -6.045  1.00 33.36           O  
ANISOU 2888  O   ASP B 565     5038   4152   3486    372   -829    507       O  
ATOM   2889  CB  ASP B 565       0.738  14.423  -5.989  1.00 34.91           C  
ANISOU 2889  CB  ASP B 565     5357   4470   3439    177   -387    567       C  
ATOM   2890  CG  ASP B 565       0.367  15.332  -7.142  1.00 45.37           C  
ANISOU 2890  CG  ASP B 565     6905   5650   4684     13   -630    690       C  
ATOM   2891  OD1 ASP B 565      -0.177  16.433  -6.891  1.00 44.87           O  
ANISOU 2891  OD1 ASP B 565     6844   5440   4763     82   -884    719       O  
ATOM   2892  OD2 ASP B 565       0.616  14.940  -8.304  1.00 52.27           O  
ANISOU 2892  OD2 ASP B 565     7969   6544   5348   -191   -574    753       O  
ATOM   2893  N   TYR B 566      -1.595  12.350  -5.804  1.00 34.54           N  
ANISOU 2893  N   TYR B 566     5172   4498   3455    324   -379    446       N  
ATOM   2894  CA  TYR B 566      -2.712  11.641  -6.393  1.00 34.55           C  
ANISOU 2894  CA  TYR B 566     5201   4498   3428    273   -455    433       C  
ATOM   2895  C   TYR B 566      -3.955  11.785  -5.521  1.00 32.37           C  
ANISOU 2895  C   TYR B 566     4705   4242   3351    416   -566    346       C  
ATOM   2896  O   TYR B 566      -5.031  12.087  -6.021  1.00 31.80           O  
ANISOU 2896  O   TYR B 566     4603   4124   3354    406   -793    349       O  
ATOM   2897  CB  TYR B 566      -2.362  10.164  -6.593  1.00 35.07           C  
ANISOU 2897  CB  TYR B 566     5326   4627   3372    211   -207    393       C  
ATOM   2898  CG  TYR B 566      -3.541   9.328  -7.015  1.00 30.58           C  
ANISOU 2898  CG  TYR B 566     4771   4063   2783    143   -267    358       C  
ATOM   2899  CD1 TYR B 566      -3.942   9.279  -8.343  1.00 32.13           C  
ANISOU 2899  CD1 TYR B 566     5154   4219   2835    -37   -404    403       C  
ATOM   2900  CD2 TYR B 566      -4.268   8.601  -6.084  1.00 30.07           C  
ANISOU 2900  CD2 TYR B 566     4547   4053   2824    221   -197    283       C  
ATOM   2901  CE1 TYR B 566      -5.026   8.525  -8.732  1.00 33.89           C  
ANISOU 2901  CE1 TYR B 566     5380   4455   3040   -122   -483    365       C  
ATOM   2902  CE2 TYR B 566      -5.356   7.844  -6.465  1.00 33.16           C  
ANISOU 2902  CE2 TYR B 566     4936   4459   3206    124   -251    245       C  
ATOM   2903  CZ  TYR B 566      -5.728   7.810  -7.790  1.00 35.39           C  
ANISOU 2903  CZ  TYR B 566     5381   4699   3364    -39   -402    281       C  
ATOM   2904  OH  TYR B 566      -6.810   7.056  -8.174  1.00 38.48           O  
ANISOU 2904  OH  TYR B 566     5763   5114   3746   -157   -477    237       O  
ATOM   2905  N   LEU B 567      -3.804  11.559  -4.219  1.00 32.87           N  
ANISOU 2905  N   LEU B 567     4608   4386   3495    536   -409    262       N  
ATOM   2906  CA  LEU B 567      -4.924  11.688  -3.285  1.00 35.39           C  
ANISOU 2906  CA  LEU B 567     4705   4762   3980    643   -446    140       C  
ATOM   2907  C   LEU B 567      -5.547  13.083  -3.287  1.00 38.23           C  
ANISOU 2907  C   LEU B 567     4965   5026   4534    748   -697     95       C  
ATOM   2908  O   LEU B 567      -6.771  13.226  -3.296  1.00 42.93           O  
ANISOU 2908  O   LEU B 567     5394   5627   5290    803   -831      8       O  
ATOM   2909  CB  LEU B 567      -4.492  11.330  -1.866  1.00 28.81           C  
ANISOU 2909  CB  LEU B 567     3773   4034   3139    711   -234     71       C  
ATOM   2910  CG  LEU B 567      -4.197   9.860  -1.576  1.00 32.15           C  
ANISOU 2910  CG  LEU B 567     4257   4526   3434    644    -22    101       C  
ATOM   2911  CD1 LEU B 567      -3.749   9.694  -0.129  1.00 30.24           C  
ANISOU 2911  CD1 LEU B 567     3949   4374   3169    701    119     67       C  
ATOM   2912  CD2 LEU B 567      -5.413   8.987  -1.873  1.00 30.25           C  
ANISOU 2912  CD2 LEU B 567     3972   4319   3202    555    -16     59       C  
ATOM   2913  N   HIS B 568      -4.706  14.108  -3.278  1.00 34.92           N  
ANISOU 2913  N   HIS B 568     4637   4508   4125    777   -768    144       N  
ATOM   2914  CA  HIS B 568      -5.199  15.478  -3.215  1.00 38.17           C  
ANISOU 2914  CA  HIS B 568     4985   4772   4745    894  -1016     97       C  
ATOM   2915  C   HIS B 568      -5.935  15.894  -4.481  1.00 40.90           C  
ANISOU 2915  C   HIS B 568     5420   4972   5148    855  -1336    201       C  
ATOM   2916  O   HIS B 568      -6.877  16.679  -4.428  1.00 42.79           O  
ANISOU 2916  O   HIS B 568     5522   5102   5636    996  -1576    129       O  
ATOM   2917  CB  HIS B 568      -4.060  16.442  -2.895  1.00 37.96           C  
ANISOU 2917  CB  HIS B 568     5069   4654   4699    894  -1015    133       C  
ATOM   2918  CG  HIS B 568      -3.623  16.391  -1.467  1.00 40.85           C  
ANISOU 2918  CG  HIS B 568     5305   5140   5077    971   -805     -5       C  
ATOM   2919  ND1 HIS B 568      -2.741  17.295  -0.917  1.00 43.31           N  
ANISOU 2919  ND1 HIS B 568     5664   5389   5401    981   -810    -24       N  
ATOM   2920  CD2 HIS B 568      -3.964  15.542  -0.463  1.00 40.00           C  
ANISOU 2920  CD2 HIS B 568     5044   5211   4944   1010   -598   -123       C  
ATOM   2921  CE1 HIS B 568      -2.551  17.006   0.358  1.00 43.77           C  
ANISOU 2921  CE1 HIS B 568     5605   5594   5434   1029   -627   -151       C  
ATOM   2922  NE2 HIS B 568      -3.282  15.946   0.657  1.00 43.11           N  
ANISOU 2922  NE2 HIS B 568     5409   5656   5316   1043   -495   -204       N  
ATOM   2923  N   ALA B 569      -5.509  15.352  -5.616  1.00 40.51           N  
ANISOU 2923  N   ALA B 569     5600   4921   4872    664  -1346    360       N  
ATOM   2924  CA  ALA B 569      -6.182  15.617  -6.882  1.00 41.42           C  
ANISOU 2924  CA  ALA B 569     5849   4918   4970    574  -1665    485       C  
ATOM   2925  C   ALA B 569      -7.591  15.021  -6.887  1.00 44.86           C  
ANISOU 2925  C   ALA B 569     6062   5432   5551    637  -1769    388       C  
ATOM   2926  O   ALA B 569      -8.469  15.492  -7.609  1.00 47.81           O  
ANISOU 2926  O   ALA B 569     6426   5697   6041    652  -2119    445       O  
ATOM   2927  CB  ALA B 569      -5.360  15.082  -8.044  1.00 38.83           C  
ANISOU 2927  CB  ALA B 569     5833   4609   4313    313  -1592    641       C  
ATOM   2928  N   LYS B 570      -7.798  13.990  -6.073  1.00 44.64           N  
ANISOU 2928  N   LYS B 570     5854   5588   5520    658  -1481    249       N  
ATOM   2929  CA  LYS B 570      -9.111  13.376  -5.914  1.00 47.24           C  
ANISOU 2929  CA  LYS B 570     5933   6025   5991    685  -1521    129       C  
ATOM   2930  C   LYS B 570      -9.886  14.016  -4.765  1.00 48.60           C  
ANISOU 2930  C   LYS B 570     5758   6229   6478    905  -1522    -77       C  
ATOM   2931  O   LYS B 570     -10.943  13.519  -4.377  1.00 51.02           O  
ANISOU 2931  O   LYS B 570     5792   6670   6924    925  -1479   -225       O  
ATOM   2932  CB  LYS B 570      -8.959  11.882  -5.639  1.00 49.48           C  
ANISOU 2932  CB  LYS B 570     6236   6473   6091    549  -1200     91       C  
ATOM   2933  CG  LYS B 570      -7.974  11.183  -6.551  1.00 49.17           C  
ANISOU 2933  CG  LYS B 570     6524   6405   5752    362  -1095    229       C  
ATOM   2934  CD  LYS B 570      -8.613  10.780  -7.860  1.00 48.69           C  
ANISOU 2934  CD  LYS B 570     6596   6320   5583    186  -1306    301       C  
ATOM   2935  CE  LYS B 570      -9.762   9.831  -7.616  1.00 49.43           C  
ANISOU 2935  CE  LYS B 570     6490   6532   5760    136  -1274    187       C  
ATOM   2936  NZ  LYS B 570     -10.024   8.964  -8.796  1.00 51.75           N  
ANISOU 2936  NZ  LYS B 570     6987   6826   5848   -100  -1347    240       N  
ATOM   2937  N   SER B 571      -9.355  15.112  -4.227  1.00 47.34           N  
ANISOU 2937  N   SER B 571     5609   5954   6425   1047  -1553   -107       N  
ATOM   2938  CA  SER B 571      -9.956  15.801  -3.086  1.00 46.91           C  
ANISOU 2938  CA  SER B 571     5253   5918   6654   1256  -1514   -345       C  
ATOM   2939  C   SER B 571     -10.042  14.903  -1.853  1.00 48.51           C  
ANISOU 2939  C   SER B 571     5287   6366   6779   1219  -1126   -514       C  
ATOM   2940  O   SER B 571     -11.028  14.930  -1.118  1.00 50.72           O  
ANISOU 2940  O   SER B 571     5254   6761   7258   1306  -1050   -740       O  
ATOM   2941  CB  SER B 571     -11.336  16.353  -3.441  1.00 47.70           C  
ANISOU 2941  CB  SER B 571     5081   5945   7097   1407  -1828   -450       C  
ATOM   2942  OG  SER B 571     -11.241  17.324  -4.466  1.00 50.91           O  
ANISOU 2942  OG  SER B 571     5675   6083   7586   1453  -2235   -274       O  
ATOM   2943  N   ILE B 572      -9.000  14.108  -1.640  1.00 44.81           N  
ANISOU 2943  N   ILE B 572     5027   5974   6023   1082   -886   -403       N  
ATOM   2944  CA  ILE B 572      -8.939  13.216  -0.493  1.00 42.94           C  
ANISOU 2944  CA  ILE B 572     4712   5936   5667   1018   -556   -503       C  
ATOM   2945  C   ILE B 572      -7.836  13.647   0.468  1.00 42.16           C  
ANISOU 2945  C   ILE B 572     4709   5841   5468   1058   -409   -516       C  
ATOM   2946  O   ILE B 572      -6.677  13.798   0.079  1.00 37.48           O  
ANISOU 2946  O   ILE B 572     4337   5158   4747   1027   -439   -359       O  
ATOM   2947  CB  ILE B 572      -8.698  11.759  -0.926  1.00 41.04           C  
ANISOU 2947  CB  ILE B 572     4626   5769   5196    830   -417   -367       C  
ATOM   2948  CG1 ILE B 572      -9.824  11.284  -1.844  1.00 41.26           C  
ANISOU 2948  CG1 ILE B 572     4563   5812   5303    751   -566   -369       C  
ATOM   2949  CG2 ILE B 572      -8.584  10.847   0.289  1.00 39.27           C  
ANISOU 2949  CG2 ILE B 572     4372   5709   4839    752   -115   -428       C  
ATOM   2950  CD1 ILE B 572      -9.670   9.849  -2.305  1.00 38.23           C  
ANISOU 2950  CD1 ILE B 572     4350   5470   4705    554   -434   -266       C  
ATOM   2951  N   ILE B 573      -8.210  13.857   1.726  1.00 44.05           N  
ANISOU 2951  N   ILE B 573     4774   6203   5762   1107   -247   -721       N  
ATOM   2952  CA  ILE B 573      -7.252  14.211   2.764  1.00 41.38           C  
ANISOU 2952  CA  ILE B 573     4523   5897   5302   1116   -114   -754       C  
ATOM   2953  C   ILE B 573      -6.910  12.973   3.579  1.00 40.60           C  
ANISOU 2953  C   ILE B 573     4497   5978   4952    967    136   -700       C  
ATOM   2954  O   ILE B 573      -7.801  12.268   4.044  1.00 44.51           O  
ANISOU 2954  O   ILE B 573     4867   6620   5424    881    285   -797       O  
ATOM   2955  CB  ILE B 573      -7.819  15.293   3.697  1.00 41.35           C  
ANISOU 2955  CB  ILE B 573     4323   5905   5481   1243    -93  -1034       C  
ATOM   2956  CG1 ILE B 573      -8.277  16.502   2.881  1.00 40.19           C  
ANISOU 2956  CG1 ILE B 573     4102   5529   5639   1418   -386  -1084       C  
ATOM   2957  CG2 ILE B 573      -6.782  15.711   4.734  1.00 40.43           C  
ANISOU 2957  CG2 ILE B 573     4331   5820   5210   1221     15  -1069       C  
ATOM   2958  CD1 ILE B 573      -8.974  17.562   3.705  1.00 41.97           C  
ANISOU 2958  CD1 ILE B 573     4103   5726   6119   1585   -374  -1407       C  
ATOM   2959  N   HIS B 574      -5.621  12.708   3.745  1.00 38.20           N  
ANISOU 2959  N   HIS B 574     4392   5653   4470    927    168   -541       N  
ATOM   2960  CA  HIS B 574      -5.173  11.530   4.481  1.00 38.44           C  
ANISOU 2960  CA  HIS B 574     4526   5802   4277    807    342   -448       C  
ATOM   2961  C   HIS B 574      -5.502  11.607   5.972  1.00 41.22           C  
ANISOU 2961  C   HIS B 574     4811   6325   4526    746    504   -608       C  
ATOM   2962  O   HIS B 574      -6.073  10.671   6.530  1.00 43.91           O  
ANISOU 2962  O   HIS B 574     5147   6793   4744    610    661   -618       O  
ATOM   2963  CB  HIS B 574      -3.672  11.335   4.290  1.00 37.04           C  
ANISOU 2963  CB  HIS B 574     4529   5554   3990    816    299   -257       C  
ATOM   2964  CG  HIS B 574      -3.159  10.040   4.830  1.00 40.30           C  
ANISOU 2964  CG  HIS B 574     5063   6025   4224    730    410   -123       C  
ATOM   2965  ND1 HIS B 574      -3.171   9.731   6.176  1.00 38.97           N  
ANISOU 2965  ND1 HIS B 574     4920   5987   3902    652    510   -151       N  
ATOM   2966  CD2 HIS B 574      -2.609   8.969   4.208  1.00 40.09           C  
ANISOU 2966  CD2 HIS B 574     5160   5922   4152    710    423     40       C  
ATOM   2967  CE1 HIS B 574      -2.658   8.530   6.355  1.00 39.71           C  
ANISOU 2967  CE1 HIS B 574     5155   6061   3871    594    545     21       C  
ATOM   2968  NE2 HIS B 574      -2.306   8.046   5.177  1.00 41.78           N  
ANISOU 2968  NE2 HIS B 574     5467   6189   4219    646    500    124       N  
ATOM   2969  N   ARG B 575      -5.105  12.712   6.600  1.00 40.72           N  
ANISOU 2969  N   ARG B 575     4725   6259   4489    816    470   -730       N  
ATOM   2970  CA  ARG B 575      -5.374  13.011   8.014  1.00 42.62           C  
ANISOU 2970  CA  ARG B 575     4918   6664   4612    747    625   -930       C  
ATOM   2971  C   ARG B 575      -4.505  12.281   9.045  1.00 41.53           C  
ANISOU 2971  C   ARG B 575     4971   6643   4168    603    704   -795       C  
ATOM   2972  O   ARG B 575      -4.560  12.604  10.228  1.00 43.71           O  
ANISOU 2972  O   ARG B 575     5260   7057   4290    515    810   -944       O  
ATOM   2973  CB  ARG B 575      -6.865  12.858   8.360  1.00 45.17           C  
ANISOU 2973  CB  ARG B 575     5027   7127   5008    694    795  -1164       C  
ATOM   2974  CG  ARG B 575      -7.776  13.879   7.687  1.00 47.98           C  
ANISOU 2974  CG  ARG B 575     5141   7380   5710    874    689  -1373       C  
ATOM   2975  CD  ARG B 575      -9.215  13.727   8.151  1.00 51.63           C  
ANISOU 2975  CD  ARG B 575     5326   8020   6272    824    881  -1647       C  
ATOM   2976  NE  ARG B 575     -10.141  14.506   7.333  1.00 57.87           N  
ANISOU 2976  NE  ARG B 575     5852   8693   7444   1021    723  -1807       N  
ATOM   2977  CZ  ARG B 575     -10.761  14.032   6.256  1.00 59.68           C  
ANISOU 2977  CZ  ARG B 575     5985   8871   7820   1036    590  -1701       C  
ATOM   2978  NH1 ARG B 575     -10.551  12.781   5.868  1.00 58.99           N  
ANISOU 2978  NH1 ARG B 575     6054   8831   7529    862    629  -1461       N  
ATOM   2979  NH2 ARG B 575     -11.592  14.807   5.568  1.00 58.91           N  
ANISOU 2979  NH2 ARG B 575     5646   8658   8079   1225    395  -1838       N  
ATOM   2980  N   ASP B 576      -3.702  11.315   8.611  1.00 39.02           N  
ANISOU 2980  N   ASP B 576     4804   6261   3762    578    640   -524       N  
ATOM   2981  CA  ASP B 576      -2.879  10.559   9.555  1.00 42.03           C  
ANISOU 2981  CA  ASP B 576     5363   6719   3887    466    654   -366       C  
ATOM   2982  C   ASP B 576      -1.585  10.058   8.925  1.00 41.60           C  
ANISOU 2982  C   ASP B 576     5415   6533   3857    548    506   -115       C  
ATOM   2983  O   ASP B 576      -1.138   8.946   9.200  1.00 41.56           O  
ANISOU 2983  O   ASP B 576     5545   6518   3729    494    496     74       O  
ATOM   2984  CB  ASP B 576      -3.668   9.387  10.146  1.00 48.27           C  
ANISOU 2984  CB  ASP B 576     6224   7621   4496    278    815   -327       C  
ATOM   2985  CG  ASP B 576      -3.041   8.841  11.416  1.00 56.58           C  
ANISOU 2985  CG  ASP B 576     7482   8774   5243    123    817   -200       C  
ATOM   2986  OD1 ASP B 576      -2.461   9.635  12.190  1.00 59.57           O  
ANISOU 2986  OD1 ASP B 576     7885   9227   5520    118    764   -274       O  
ATOM   2987  OD2 ASP B 576      -3.126   7.615  11.638  1.00 59.28           O  
ANISOU 2987  OD2 ASP B 576     7980   9104   5440     -7    849    -18       O  
ATOM   2988  N   LEU B 577      -0.980  10.892   8.088  1.00 42.51           N  
ANISOU 2988  N   LEU B 577     5470   6541   4142    674    391   -121       N  
ATOM   2989  CA  LEU B 577       0.246  10.516   7.403  1.00 41.27           C  
ANISOU 2989  CA  LEU B 577     5362   6283   4034    745    290     66       C  
ATOM   2990  C   LEU B 577       1.431  10.494   8.360  1.00 43.23           C  
ANISOU 2990  C   LEU B 577     5664   6599   4162    728    199    158       C  
ATOM   2991  O   LEU B 577       1.808  11.520   8.923  1.00 43.86           O  
ANISOU 2991  O   LEU B 577     5713   6735   4218    712    136     60       O  
ATOM   2992  CB  LEU B 577       0.520  11.467   6.238  1.00 38.90           C  
ANISOU 2992  CB  LEU B 577     4995   5871   3915    825    213     29       C  
ATOM   2993  CG  LEU B 577       1.762  11.151   5.407  1.00 38.90           C  
ANISOU 2993  CG  LEU B 577     5015   5796   3970    870    162    177       C  
ATOM   2994  CD1 LEU B 577       1.619   9.804   4.717  1.00 37.41           C  
ANISOU 2994  CD1 LEU B 577     4886   5544   3784    881    237    283       C  
ATOM   2995  CD2 LEU B 577       2.012  12.254   4.394  1.00 38.71           C  
ANISOU 2995  CD2 LEU B 577     4960   5681   4067    880     94    139       C  
ATOM   2996  N   LYS B 578       2.001   9.306   8.541  1.00 46.54           N  
ANISOU 2996  N   LYS B 578     6168   6995   4518    733    169    343       N  
ATOM   2997  CA  LYS B 578       3.191   9.104   9.362  1.00 44.38           C  
ANISOU 2997  CA  LYS B 578     5933   6768   4163    740     26    472       C  
ATOM   2998  C   LYS B 578       4.101   8.145   8.618  1.00 44.34           C  
ANISOU 2998  C   LYS B 578     5911   6637   4300    866    -30    637       C  
ATOM   2999  O   LYS B 578       3.663   7.476   7.686  1.00 43.67           O  
ANISOU 2999  O   LYS B 578     5847   6440   4308    906     68    652       O  
ATOM   3000  CB  LYS B 578       2.816   8.476  10.703  1.00 43.30           C  
ANISOU 3000  CB  LYS B 578     5954   6730   3769    601     20    537       C  
ATOM   3001  CG  LYS B 578       1.746   9.222  11.479  1.00 44.28           C  
ANISOU 3001  CG  LYS B 578     6094   6999   3733    453    147    329       C  
ATOM   3002  CD  LYS B 578       1.342   8.466  12.741  1.00 46.78           C  
ANISOU 3002  CD  LYS B 578     6603   7430   3744    255    181    404       C  
ATOM   3003  CE  LYS B 578       0.290   7.396  12.461  1.00 47.30           C  
ANISOU 3003  CE  LYS B 578     6741   7450   3782    171    337    453       C  
ATOM   3004  NZ  LYS B 578       0.063   6.558  13.678  1.00 49.62           N  
ANISOU 3004  NZ  LYS B 578     7271   7832   3749    -61    347    584       N  
ATOM   3005  N   SER B 579       5.359   8.053   9.038  1.00 46.57           N  
ANISOU 3005  N   SER B 579     6146   6939   4612    928   -190    743       N  
ATOM   3006  CA  SER B 579       6.262   7.046   8.486  1.00 49.42           C  
ANISOU 3006  CA  SER B 579     6460   7177   5140   1076   -245    877       C  
ATOM   3007  C   SER B 579       5.783   5.654   8.888  1.00 52.10           C  
ANISOU 3007  C   SER B 579     6990   7406   5401   1071   -254   1024       C  
ATOM   3008  O   SER B 579       6.194   4.647   8.313  1.00 51.97           O  
ANISOU 3008  O   SER B 579     6980   7227   5541   1200   -259   1107       O  
ATOM   3009  CB  SER B 579       7.690   7.269   8.980  1.00 49.83           C  
ANISOU 3009  CB  SER B 579     6374   7292   5266   1149   -447    949       C  
ATOM   3010  OG  SER B 579       7.755   7.160  10.387  1.00 52.70           O  
ANISOU 3010  OG  SER B 579     6858   7743   5422   1061   -623   1053       O  
ATOM   3011  N   ASN B 580       4.910   5.624   9.888  1.00 56.82           N  
ANISOU 3011  N   ASN B 580     7750   8085   5752    903   -243   1040       N  
ATOM   3012  CA  ASN B 580       4.285   4.409  10.381  1.00 61.69           C  
ANISOU 3012  CA  ASN B 580     8591   8612   6235    815   -235   1184       C  
ATOM   3013  C   ASN B 580       3.263   3.878   9.377  1.00 58.79           C  
ANISOU 3013  C   ASN B 580     8258   8134   5946    793    -32   1111       C  
ATOM   3014  O   ASN B 580       3.038   2.672   9.284  1.00 59.04           O  
ANISOU 3014  O   ASN B 580     8447   8001   5984    782    -27   1235       O  
ATOM   3015  CB  ASN B 580       3.589   4.719  11.706  1.00 68.66           C  
ANISOU 3015  CB  ASN B 580     9623   9670   6794    580   -227   1175       C  
ATOM   3016  CG  ASN B 580       3.507   3.520  12.618  1.00 79.71           C  
ANISOU 3016  CG  ASN B 580    11295  10995   7995    458   -336   1411       C  
ATOM   3017  OD1 ASN B 580       4.457   2.743  12.732  1.00 85.03           O  
ANISOU 3017  OD1 ASN B 580    12029  11516   8762    589   -557   1620       O  
ATOM   3018  ND2 ASN B 580       2.367   3.360  13.281  1.00 83.75           N  
ANISOU 3018  ND2 ASN B 580    11971  11610   8240    200   -187   1378       N  
ATOM   3019  N   ASN B 581       2.650   4.798   8.634  1.00 57.45           N  
ANISOU 3019  N   ASN B 581     7951   8039   5838    778    109    915       N  
ATOM   3020  CA  ASN B 581       1.608   4.479   7.662  1.00 56.09           C  
ANISOU 3020  CA  ASN B 581     7785   7797   5729    736    269    827       C  
ATOM   3021  C   ASN B 581       2.158   4.239   6.257  1.00 51.98           C  
ANISOU 3021  C   ASN B 581     7197   7131   5424    883    293    809       C  
ATOM   3022  O   ASN B 581       1.397   4.014   5.320  1.00 50.44           O  
ANISOU 3022  O   ASN B 581     7014   6874   5275    843    399    735       O  
ATOM   3023  CB  ASN B 581       0.581   5.619   7.596  1.00 59.02           C  
ANISOU 3023  CB  ASN B 581     8040   8315   6069    649    369    626       C  
ATOM   3024  CG  ASN B 581      -0.091   5.886   8.926  1.00 65.26           C  
ANISOU 3024  CG  ASN B 581     8878   9275   6644    482    414    573       C  
ATOM   3025  OD1 ASN B 581       0.343   5.397   9.965  1.00 71.21           O  
ANISOU 3025  OD1 ASN B 581     9772  10060   7225    410    341    706       O  
ATOM   3026  ND2 ASN B 581      -1.167   6.661   8.896  1.00 66.83           N  
ANISOU 3026  ND2 ASN B 581     8960   9584   6849    415    530    369       N  
ATOM   3027  N   ILE B 582       3.476   4.310   6.111  1.00 48.27           N  
ANISOU 3027  N   ILE B 582     6643   6623   5075   1033    199    859       N  
ATOM   3028  CA  ILE B 582       4.110   4.162   4.807  1.00 44.57           C  
ANISOU 3028  CA  ILE B 582     6091   6052   4791   1150    262    806       C  
ATOM   3029  C   ILE B 582       4.838   2.822   4.689  1.00 48.95           C  
ANISOU 3029  C   ILE B 582     6708   6416   5473   1287    232    905       C  
ATOM   3030  O   ILE B 582       5.953   2.661   5.182  1.00 52.56           O  
ANISOU 3030  O   ILE B 582     7081   6859   6029   1421    101    984       O  
ATOM   3031  CB  ILE B 582       5.085   5.326   4.530  1.00 41.08           C  
ANISOU 3031  CB  ILE B 582     5458   5719   4432   1205    223    738       C  
ATOM   3032  CG1 ILE B 582       4.353   6.666   4.647  1.00 38.43           C  
ANISOU 3032  CG1 ILE B 582     5089   5512   4001   1088    228    636       C  
ATOM   3033  CG2 ILE B 582       5.712   5.183   3.159  1.00 40.75           C  
ANISOU 3033  CG2 ILE B 582     5339   5603   4541   1273    333    664       C  
ATOM   3034  CD1 ILE B 582       5.243   7.874   4.467  1.00 36.39           C  
ANISOU 3034  CD1 ILE B 582     4686   5335   3804   1097    174    581       C  
ATOM   3035  N   PHE B 583       4.193   1.860   4.036  1.00 48.31           N  
ANISOU 3035  N   PHE B 583     6769   6176   5412   1257    336    890       N  
ATOM   3036  CA  PHE B 583       4.730   0.507   3.950  1.00 53.14           C  
ANISOU 3036  CA  PHE B 583     7481   6549   6161   1388    307    968       C  
ATOM   3037  C   PHE B 583       5.653   0.333   2.747  1.00 55.19           C  
ANISOU 3037  C   PHE B 583     7610   6723   6638   1547    413    835       C  
ATOM   3038  O   PHE B 583       5.264   0.600   1.613  1.00 55.03           O  
ANISOU 3038  O   PHE B 583     7587   6725   6598   1469    575    690       O  
ATOM   3039  CB  PHE B 583       3.599  -0.525   3.875  1.00 54.04           C  
ANISOU 3039  CB  PHE B 583     7840   6505   6189   1251    373   1005       C  
ATOM   3040  CG  PHE B 583       2.459  -0.259   4.818  1.00 52.74           C  
ANISOU 3040  CG  PHE B 583     7774   6475   5789   1027    357   1069       C  
ATOM   3041  CD1 PHE B 583       2.664  -0.221   6.188  1.00 53.24           C  
ANISOU 3041  CD1 PHE B 583     7898   6606   5725    990    212   1222       C  
ATOM   3042  CD2 PHE B 583       1.175  -0.068   4.332  1.00 51.84           C  
ANISOU 3042  CD2 PHE B 583     7684   6434   5578    841    489    962       C  
ATOM   3043  CE1 PHE B 583       1.612   0.017   7.054  1.00 51.89           C  
ANISOU 3043  CE1 PHE B 583     7815   6586   5316    755    248   1243       C  
ATOM   3044  CE2 PHE B 583       0.120   0.172   5.192  1.00 51.10           C  
ANISOU 3044  CE2 PHE B 583     7631   6489   5298    636    511    978       C  
ATOM   3045  CZ  PHE B 583       0.338   0.214   6.555  1.00 51.93           C  
ANISOU 3045  CZ  PHE B 583     7801   6672   5259    585    416   1106       C  
ATOM   3046  N   LEU B 584       6.876  -0.120   3.000  1.00 57.22           N  
ANISOU 3046  N   LEU B 584     7755   6890   7098   1761    318    876       N  
ATOM   3047  CA  LEU B 584       7.816  -0.417   1.927  1.00 58.27           C  
ANISOU 3047  CA  LEU B 584     7734   6941   7464   1923    453    715       C  
ATOM   3048  C   LEU B 584       7.592  -1.827   1.406  1.00 59.81           C  
ANISOU 3048  C   LEU B 584     8116   6833   7777   2002    532    675       C  
ATOM   3049  O   LEU B 584       8.199  -2.783   1.888  1.00 63.93           O  
ANISOU 3049  O   LEU B 584     8659   7136   8497   2202    402    757       O  
ATOM   3050  CB  LEU B 584       9.256  -0.260   2.408  1.00 62.66           C  
ANISOU 3050  CB  LEU B 584     8020   7547   8242   2137    317    740       C  
ATOM   3051  CG  LEU B 584       9.831   1.151   2.313  1.00 65.31           C  
ANISOU 3051  CG  LEU B 584     8106   8168   8541   2065    337    670       C  
ATOM   3052  CD1 LEU B 584      11.059   1.276   3.189  1.00 68.74           C  
ANISOU 3052  CD1 LEU B 584     8297   8669   9153   2233    117    753       C  
ATOM   3053  CD2 LEU B 584      10.172   1.481   0.868  1.00 67.25           C  
ANISOU 3053  CD2 LEU B 584     8230   8472   8850   2025    610    444       C  
ATOM   3054  N   HIS B 585       6.711  -1.945   0.421  1.00 58.30           N  
ANISOU 3054  N   HIS B 585     8070   6613   7469   1839    721    549       N  
ATOM   3055  CA  HIS B 585       6.350  -3.239  -0.141  1.00 61.01           C  
ANISOU 3055  CA  HIS B 585     8629   6664   7886   1859    811    484       C  
ATOM   3056  C   HIS B 585       7.497  -3.849  -0.940  1.00 65.16           C  
ANISOU 3056  C   HIS B 585     9027   7035   8697   2093    942    292       C  
ATOM   3057  O   HIS B 585       7.951  -3.273  -1.933  1.00 65.08           O  
ANISOU 3057  O   HIS B 585     8861   7174   8694   2068   1140     91       O  
ATOM   3058  CB  HIS B 585       5.109  -3.101  -1.017  1.00 58.99           C  
ANISOU 3058  CB  HIS B 585     8542   6457   7413   1594    958    387       C  
ATOM   3059  CG  HIS B 585       4.727  -4.362  -1.723  1.00 63.14           C  
ANISOU 3059  CG  HIS B 585     9299   6697   7993   1570   1067    284       C  
ATOM   3060  ND1 HIS B 585       4.642  -5.580  -1.084  1.00 66.53           N  
ANISOU 3060  ND1 HIS B 585     9923   6821   8532   1647    962    398       N  
ATOM   3061  CD2 HIS B 585       4.400  -4.593  -3.017  1.00 64.45           C  
ANISOU 3061  CD2 HIS B 585     9564   6821   8104   1454   1260     76       C  
ATOM   3062  CE1 HIS B 585       4.282  -6.508  -1.952  1.00 67.53           C  
ANISOU 3062  CE1 HIS B 585    10250   6717   8693   1590   1095    249       C  
ATOM   3063  NE2 HIS B 585       4.130  -5.935  -3.133  1.00 68.01           N  
ANISOU 3063  NE2 HIS B 585    10252   6944   8643   1470   1281     44       N  
ATOM   3064  N   GLU B 586       7.959  -5.014  -0.490  1.00 68.82           N  
ANISOU 3064  N   GLU B 586     9561   7190   9396   2312    831    349       N  
ATOM   3065  CA  GLU B 586       9.144  -5.667  -1.043  1.00 73.88           C  
ANISOU 3065  CA  GLU B 586    10030   7653  10388   2604    925    155       C  
ATOM   3066  C   GLU B 586      10.345  -4.737  -0.943  1.00 73.62           C  
ANISOU 3066  C   GLU B 586     9593   7884  10496   2743    919     98       C  
ATOM   3067  O   GLU B 586      11.306  -4.866  -1.703  1.00 73.08           O  
ANISOU 3067  O   GLU B 586     9286   7813  10667   2907   1104   -148       O  
ATOM   3068  CB  GLU B 586       8.921  -6.089  -2.498  1.00 75.94           C  
ANISOU 3068  CB  GLU B 586    10389   7825  10640   2524   1247   -150       C  
ATOM   3069  CG  GLU B 586       7.657  -6.896  -2.735  1.00 78.70           C  
ANISOU 3069  CG  GLU B 586    11131   7953  10819   2322   1270   -123       C  
ATOM   3070  CD  GLU B 586       7.844  -8.382  -2.487  1.00 86.44           C  
ANISOU 3070  CD  GLU B 586    12304   8471  12067   2528   1187   -116       C  
ATOM   3071  OE1 GLU B 586       8.893  -8.774  -1.933  1.00 90.36           O  
ANISOU 3071  OE1 GLU B 586    12632   8810  12891   2854   1044    -76       O  
ATOM   3072  OE2 GLU B 586       6.938  -9.162  -2.854  1.00 87.35           O  
ANISOU 3072  OE2 GLU B 586    12741   8365  12081   2361   1243   -149       O  
ATOM   3073  N   ASP B 587      10.261  -3.792  -0.008  1.00 73.65           N  
ANISOU 3073  N   ASP B 587     9518   8126  10341   2650    723    305       N  
ATOM   3074  CA  ASP B 587      11.296  -2.790   0.225  1.00 79.48           C  
ANISOU 3074  CA  ASP B 587     9895   9136  11169   2720    678    283       C  
ATOM   3075  C   ASP B 587      11.488  -1.831  -0.950  1.00 78.89           C  
ANISOU 3075  C   ASP B 587     9662   9316  10996   2555    974     50       C  
ATOM   3076  O   ASP B 587      12.406  -1.014  -0.943  1.00 80.39           O  
ANISOU 3076  O   ASP B 587     9545   9728  11271   2578    989     -6       O  
ATOM   3077  CB  ASP B 587      12.625  -3.463   0.585  1.00 89.18           C  
ANISOU 3077  CB  ASP B 587    10853  10217  12813   3077    541    258       C  
ATOM   3078  CG  ASP B 587      12.493  -4.418   1.754  1.00 97.12           C  
ANISOU 3078  CG  ASP B 587    12054  10937  13909   3233    193    528       C  
ATOM   3079  OD1 ASP B 587      12.058  -5.570   1.542  1.00 99.63           O  
ANISOU 3079  OD1 ASP B 587    12632  10914  14310   3304    211    524       O  
ATOM   3080  OD2 ASP B 587      12.821  -4.011   2.887  1.00100.14           O  
ANISOU 3080  OD2 ASP B 587    12358  11429  14260   3257   -108    751       O  
ATOM   3081  N   ASN B 588      10.619  -1.917  -1.950  1.00 76.80           N  
ANISOU 3081  N   ASN B 588     9622   9022  10535   2358   1193    -71       N  
ATOM   3082  CA  ASN B 588      10.825  -1.158  -3.179  1.00 75.04           C  
ANISOU 3082  CA  ASN B 588     9311   9001  10200   2182   1471   -285       C  
ATOM   3083  C   ASN B 588       9.693  -0.217  -3.568  1.00 68.90           C  
ANISOU 3083  C   ASN B 588     8735   8381   9062   1860   1487   -222       C  
ATOM   3084  O   ASN B 588       9.917   0.776  -4.256  1.00 70.11           O  
ANISOU 3084  O   ASN B 588     8807   8742   9089   1688   1610   -302       O  
ATOM   3085  CB  ASN B 588      11.150  -2.101  -4.339  1.00 77.61           C  
ANISOU 3085  CB  ASN B 588     9668   9164  10657   2249   1759   -569       C  
ATOM   3086  CG  ASN B 588      12.602  -2.026  -4.753  1.00 81.91           C  
ANISOU 3086  CG  ASN B 588     9835   9811  11477   2412   1943   -796       C  
ATOM   3087  OD1 ASN B 588      13.441  -1.502  -4.020  1.00 81.32           O  
ANISOU 3087  OD1 ASN B 588     9457   9877  11564   2533   1797   -713       O  
ATOM   3088  ND2 ASN B 588      12.907  -2.545  -5.937  1.00 86.04           N  
ANISOU 3088  ND2 ASN B 588    10362  10281  12050   2397   2275  -1106       N  
ATOM   3089  N   THR B 589       8.481  -0.528  -3.132  1.00 62.06           N  
ANISOU 3089  N   THR B 589     8128   7409   8044   1773   1355    -77       N  
ATOM   3090  CA  THR B 589       7.331   0.287  -3.486  1.00 56.43           C  
ANISOU 3090  CA  THR B 589     7574   6823   7044   1505   1342    -30       C  
ATOM   3091  C   THR B 589       6.647   0.857  -2.255  1.00 53.13           C  
ANISOU 3091  C   THR B 589     7173   6484   6529   1468   1108    180       C  
ATOM   3092  O   THR B 589       6.170   0.115  -1.400  1.00 53.37           O  
ANISOU 3092  O   THR B 589     7317   6384   6577   1521    989    300       O  
ATOM   3093  CB  THR B 589       6.299  -0.509  -4.299  1.00 58.06           C  
ANISOU 3093  CB  THR B 589     8056   6876   7126   1368   1438   -108       C  
ATOM   3094  OG1 THR B 589       6.933  -1.076  -5.451  1.00 64.01           O  
ANISOU 3094  OG1 THR B 589     8821   7554   7946   1386   1683   -342       O  
ATOM   3095  CG2 THR B 589       5.158   0.393  -4.746  1.00 53.90           C  
ANISOU 3095  CG2 THR B 589     7646   6494   6340   1107   1390    -67       C  
ATOM   3096  N   VAL B 590       6.608   2.183  -2.176  1.00 49.71           N  
ANISOU 3096  N   VAL B 590     6644   6257   5989   1357   1053    212       N  
ATOM   3097  CA  VAL B 590       5.878   2.874  -1.127  1.00 44.65           C  
ANISOU 3097  CA  VAL B 590     6018   5708   5240   1297    872    351       C  
ATOM   3098  C   VAL B 590       4.385   2.620  -1.275  1.00 43.85           C  
ANISOU 3098  C   VAL B 590     6113   5557   4992   1150    860    369       C  
ATOM   3099  O   VAL B 590       3.821   2.780  -2.356  1.00 42.85           O  
ANISOU 3099  O   VAL B 590     6074   5430   4776   1017    938    286       O  
ATOM   3100  CB  VAL B 590       6.160   4.392  -1.153  1.00 39.32           C  
ANISOU 3100  CB  VAL B 590     5213   5223   4505   1210    825    346       C  
ATOM   3101  CG1 VAL B 590       5.059   5.171  -0.439  1.00 35.21           C  
ANISOU 3101  CG1 VAL B 590     4750   4774   3856   1113    688    415       C  
ATOM   3102  CG2 VAL B 590       7.519   4.685  -0.542  1.00 38.72           C  
ANISOU 3102  CG2 VAL B 590     4913   5227   4570   1335    773    364       C  
ATOM   3103  N   LYS B 591       3.758   2.208  -0.181  1.00 42.95           N  
ANISOU 3103  N   LYS B 591     6065   5412   4842   1153    757    478       N  
ATOM   3104  CA  LYS B 591       2.316   2.038  -0.135  1.00 42.13           C  
ANISOU 3104  CA  LYS B 591     6089   5303   4614    995    749    487       C  
ATOM   3105  C   LYS B 591       1.774   2.844   1.034  1.00 41.05           C  
ANISOU 3105  C   LYS B 591     5883   5319   4393    946    643    550       C  
ATOM   3106  O   LYS B 591       2.125   2.595   2.186  1.00 42.42           O  
ANISOU 3106  O   LYS B 591     6060   5501   4556    998    570    650       O  
ATOM   3107  CB  LYS B 591       1.951   0.562   0.029  1.00 46.64           C  
ANISOU 3107  CB  LYS B 591     6840   5676   5203    985    781    531       C  
ATOM   3108  CG  LYS B 591       2.289  -0.310  -1.172  1.00 49.01           C  
ANISOU 3108  CG  LYS B 591     7241   5800   5582   1013    909    419       C  
ATOM   3109  CD  LYS B 591       1.288  -0.117  -2.295  1.00 47.61           C  
ANISOU 3109  CD  LYS B 591     7145   5658   5285    819    972    313       C  
ATOM   3110  CE  LYS B 591       1.635  -0.991  -3.485  1.00 48.45           C  
ANISOU 3110  CE  LYS B 591     7384   5597   5427    814   1117    174       C  
ATOM   3111  NZ  LYS B 591       0.638  -0.868  -4.587  1.00 47.22           N  
ANISOU 3111  NZ  LYS B 591     7343   5479   5121    591   1142     82       N  
ATOM   3112  N   ILE B 592       0.928   3.820   0.734  1.00 37.35           N  
ANISOU 3112  N   ILE B 592     5359   4964   3866    845    624    482       N  
ATOM   3113  CA  ILE B 592       0.342   4.654   1.771  1.00 33.69           C  
ANISOU 3113  CA  ILE B 592     4814   4643   3344    805    556    480       C  
ATOM   3114  C   ILE B 592      -0.979   4.064   2.233  1.00 33.35           C  
ANISOU 3114  C   ILE B 592     4827   4617   3225    672    593    470       C  
ATOM   3115  O   ILE B 592      -1.854   3.761   1.421  1.00 32.63           O  
ANISOU 3115  O   ILE B 592     4766   4490   3140    579    626    415       O  
ATOM   3116  CB  ILE B 592       0.120   6.092   1.273  1.00 32.64           C  
ANISOU 3116  CB  ILE B 592     4571   4595   3236    793    497    394       C  
ATOM   3117  CG1 ILE B 592       1.460   6.756   0.959  1.00 32.54           C  
ANISOU 3117  CG1 ILE B 592     4501   4587   3277    872    471    409       C  
ATOM   3118  CG2 ILE B 592      -0.639   6.904   2.305  1.00 33.31           C  
ANISOU 3118  CG2 ILE B 592     4565   4801   3290    763    451    336       C  
ATOM   3119  CD1 ILE B 592       1.329   8.057   0.201  1.00 31.77           C  
ANISOU 3119  CD1 ILE B 592     4364   4511   3197    827    405    354       C  
ATOM   3120  N   GLY B 593      -1.115   3.894   3.543  1.00 33.03           N  
ANISOU 3120  N   GLY B 593     4806   4648   3097    632    589    523       N  
ATOM   3121  CA  GLY B 593      -2.332   3.346   4.102  1.00 32.40           C  
ANISOU 3121  CA  GLY B 593     4771   4618   2923    459    660    508       C  
ATOM   3122  C   GLY B 593      -2.721   4.009   5.401  1.00 38.88           C  
ANISOU 3122  C   GLY B 593     5519   5624   3630    387    676    462       C  
ATOM   3123  O   GLY B 593      -2.190   5.063   5.760  1.00 38.60           O  
ANISOU 3123  O   GLY B 593     5387   5673   3607    478    617    413       O  
ATOM   3124  N   ASP B 594      -3.663   3.380   6.096  1.00 43.78           N  
ANISOU 3124  N   ASP B 594     6198   6310   4127    195    772    461       N  
ATOM   3125  CA  ASP B 594      -4.097   3.807   7.416  1.00 45.08           C  
ANISOU 3125  CA  ASP B 594     6330   6668   4131     68    840    400       C  
ATOM   3126  C   ASP B 594      -4.596   5.251   7.427  1.00 47.78           C  
ANISOU 3126  C   ASP B 594     6428   7167   4560    130    861    172       C  
ATOM   3127  O   ASP B 594      -4.044   6.105   8.118  1.00 48.58           O  
ANISOU 3127  O   ASP B 594     6498   7348   4613    192    821    126       O  
ATOM   3128  CB  ASP B 594      -2.969   3.607   8.432  1.00 45.96           C  
ANISOU 3128  CB  ASP B 594     6603   6763   4096     95    746    566       C  
ATOM   3129  CG  ASP B 594      -3.469   3.596   9.857  1.00 50.33           C  
ANISOU 3129  CG  ASP B 594     7236   7500   4389   -129    834    551       C  
ATOM   3130  OD1 ASP B 594      -4.685   3.390  10.061  1.00 51.49           O  
ANISOU 3130  OD1 ASP B 594     7339   7761   4464   -333   1006    439       O  
ATOM   3131  OD2 ASP B 594      -2.644   3.785  10.774  1.00 53.48           O  
ANISOU 3131  OD2 ASP B 594     7736   7941   4642   -123    734    644       O  
ATOM   3132  N   PHE B 595      -5.651   5.515   6.665  1.00 49.60           N  
ANISOU 3132  N   PHE B 595     6489   7425   4933    115    901     25       N  
ATOM   3133  CA  PHE B 595      -6.224   6.852   6.617  1.00 55.81           C  
ANISOU 3133  CA  PHE B 595     7034   8312   5858    203    890   -197       C  
ATOM   3134  C   PHE B 595      -6.984   7.140   7.905  1.00 61.78           C  
ANISOU 3134  C   PHE B 595     7691   9284   6498     63   1060   -375       C  
ATOM   3135  O   PHE B 595      -7.167   6.258   8.742  1.00 64.35           O  
ANISOU 3135  O   PHE B 595     8148   9695   6609   -146   1189   -307       O  
ATOM   3136  CB  PHE B 595      -7.187   7.000   5.434  1.00 60.51           C  
ANISOU 3136  CB  PHE B 595     7465   8868   6657    231    838   -291       C  
ATOM   3137  CG  PHE B 595      -6.545   6.829   4.085  1.00 64.67           C  
ANISOU 3137  CG  PHE B 595     8099   9207   7265    331    689   -154       C  
ATOM   3138  CD1 PHE B 595      -5.176   6.664   3.955  1.00 66.49           C  
ANISOU 3138  CD1 PHE B 595     8504   9325   7433    418    636      2       C  
ATOM   3139  CD2 PHE B 595      -7.322   6.842   2.940  1.00 66.95           C  
ANISOU 3139  CD2 PHE B 595     8302   9449   7688    323    603   -198       C  
ATOM   3140  CE1 PHE B 595      -4.598   6.505   2.712  1.00 66.32           C  
ANISOU 3140  CE1 PHE B 595     8570   9159   7470    481    551     88       C  
ATOM   3141  CE2 PHE B 595      -6.749   6.688   1.695  1.00 67.34           C  
ANISOU 3141  CE2 PHE B 595     8481   9346   7760    371    488    -88       C  
ATOM   3142  CZ  PHE B 595      -5.386   6.520   1.580  1.00 65.91           C  
ANISOU 3142  CZ  PHE B 595     8474   9065   7503    444    486     42       C  
ATOM   3143  N   GLY B 596      -7.433   8.382   8.050  1.00 62.92           N  
ANISOU 3143  N   GLY B 596     7618   9507   6784    166   1063   -612       N  
ATOM   3144  CA  GLY B 596      -8.288   8.757   9.158  1.00 63.23           C  
ANISOU 3144  CA  GLY B 596     7508   9764   6752     43   1265   -862       C  
ATOM   3145  C   GLY B 596      -9.747   8.672   8.758  1.00 65.35           C  
ANISOU 3145  C   GLY B 596     7496  10130   7206    -14   1365  -1059       C  
ATOM   3146  O   GLY B 596     -10.580   8.157   9.504  1.00 68.52           O  
ANISOU 3146  O   GLY B 596     7823  10728   7483   -243   1595  -1177       O  
ATOM   3147  N   GLY B 615      -0.121   8.935  19.324  1.00 87.58           N  
ANISOU 3147  N   GLY B 615    12620  13566   7090  -1031    481     79       N  
ATOM   3148  CA  GLY B 615       1.273   8.879  18.922  1.00 85.84           C  
ANISOU 3148  CA  GLY B 615    12381  13186   7047   -813    125    327       C  
ATOM   3149  C   GLY B 615       1.567   9.706  17.685  1.00 79.77           C  
ANISOU 3149  C   GLY B 615    11310  12274   6726   -500    109    192       C  
ATOM   3150  O   GLY B 615       2.725   9.945  17.345  1.00 78.58           O  
ANISOU 3150  O   GLY B 615    11086  12032   6738   -339   -137    314       O  
ATOM   3151  N   SER B 616       0.509  10.164  17.024  1.00 75.79           N  
ANISOU 3151  N   SER B 616    10625  11755   6416   -434    363    -61       N  
ATOM   3152  CA  SER B 616       0.635  10.893  15.770  1.00 73.44           C  
ANISOU 3152  CA  SER B 616    10082  11300   6521   -169    344   -163       C  
ATOM   3153  C   SER B 616       1.027  12.346  15.998  1.00 68.36           C  
ANISOU 3153  C   SER B 616     9355  10686   5933   -131    296   -402       C  
ATOM   3154  O   SER B 616       1.096  13.131  15.055  1.00 64.65           O  
ANISOU 3154  O   SER B 616     8717  10081   5767     50    273   -503       O  
ATOM   3155  CB  SER B 616      -0.680  10.827  14.996  1.00 76.33           C  
ANISOU 3155  CB  SER B 616    10298  11629   7076   -118    578   -324       C  
ATOM   3156  OG  SER B 616      -1.256   9.538  15.098  1.00 78.57           O  
ANISOU 3156  OG  SER B 616    10695  11931   7226   -250    673   -164       O  
ATOM   3157  N   ILE B 617       1.287  12.688  17.256  1.00 66.58           N  
ANISOU 3157  N   ILE B 617     9280  10626   5392   -328    268   -483       N  
ATOM   3158  CA  ILE B 617       1.615  14.055  17.655  1.00 64.09           C  
ANISOU 3158  CA  ILE B 617     8930  10342   5081   -341    233   -744       C  
ATOM   3159  C   ILE B 617       2.776  14.673  16.863  1.00 56.48           C  
ANISOU 3159  C   ILE B 617     7851   9219   4391   -165     -7   -647       C  
ATOM   3160  O   ILE B 617       2.722  15.843  16.491  1.00 52.98           O  
ANISOU 3160  O   ILE B 617     7305   8681   4145    -84     11   -871       O  
ATOM   3161  CB  ILE B 617       1.907  14.127  19.169  1.00 72.06           C  
ANISOU 3161  CB  ILE B 617    10172  11566   5643   -623    195   -793       C  
ATOM   3162  CG1 ILE B 617       0.732  13.547  19.955  1.00 77.81           C  
ANISOU 3162  CG1 ILE B 617    11025  12476   6063   -854    478   -908       C  
ATOM   3163  CG2 ILE B 617       2.165  15.559  19.608  1.00 74.05           C  
ANISOU 3163  CG2 ILE B 617    10406  11838   5890   -659    182  -1111       C  
ATOM   3164  CD1 ILE B 617      -0.578  14.252  19.682  1.00 78.51           C  
ANISOU 3164  CD1 ILE B 617    10920  12576   6336   -795    811  -1311       C  
ATOM   3165  N   LEU B 618       3.812  13.881  16.597  1.00 53.80           N  
ANISOU 3165  N   LEU B 618     7524   8840   4077   -111   -226   -323       N  
ATOM   3166  CA  LEU B 618       5.003  14.371  15.906  1.00 50.86           C  
ANISOU 3166  CA  LEU B 618     7018   8364   3944     15   -432   -231       C  
ATOM   3167  C   LEU B 618       4.719  14.844  14.477  1.00 50.57           C  
ANISOU 3167  C   LEU B 618     6808   8140   4267    201   -342   -297       C  
ATOM   3168  O   LEU B 618       5.419  15.714  13.954  1.00 51.79           O  
ANISOU 3168  O   LEU B 618     6868   8210   4598    245   -440   -337       O  
ATOM   3169  CB  LEU B 618       6.095  13.298  15.898  1.00 50.23           C  
ANISOU 3169  CB  LEU B 618     6940   8286   3858     61   -662    105       C  
ATOM   3170  CG  LEU B 618       6.608  12.841  17.266  1.00 55.67           C  
ANISOU 3170  CG  LEU B 618     7815   9135   4201   -121   -859    240       C  
ATOM   3171  CD1 LEU B 618       7.653  11.747  17.118  1.00 55.09           C  
ANISOU 3171  CD1 LEU B 618     7706   9010   4217     -9  -1120    578       C  
ATOM   3172  CD2 LEU B 618       7.173  14.016  18.047  1.00 59.23           C  
ANISOU 3172  CD2 LEU B 618     8291   9702   4513   -272   -983     65       C  
ATOM   3173  N   TRP B 619       3.692  14.274  13.853  1.00 47.24           N  
ANISOU 3173  N   TRP B 619     6360   7655   3932    278   -167   -300       N  
ATOM   3174  CA  TRP B 619       3.361  14.590  12.467  1.00 41.62           C  
ANISOU 3174  CA  TRP B 619     5518   6771   3523    434   -112   -328       C  
ATOM   3175  C   TRP B 619       2.199  15.567  12.367  1.00 41.88           C  
ANISOU 3175  C   TRP B 619     5505   6751   3657    457     24   -617       C  
ATOM   3176  O   TRP B 619       1.694  15.834  11.275  1.00 40.55           O  
ANISOU 3176  O   TRP B 619     5248   6435   3723    575     50   -644       O  
ATOM   3177  CB  TRP B 619       3.030  13.312  11.694  1.00 37.03           C  
ANISOU 3177  CB  TRP B 619     4928   6135   3009    511    -47   -140       C  
ATOM   3178  CG  TRP B 619       4.189  12.388  11.541  1.00 37.81           C  
ANISOU 3178  CG  TRP B 619     5034   6220   3112    555   -186    121       C  
ATOM   3179  CD1 TRP B 619       5.052  12.322  10.486  1.00 37.46           C  
ANISOU 3179  CD1 TRP B 619     4882   6075   3276    667   -251    226       C  
ATOM   3180  CD2 TRP B 619       4.619  11.391  12.474  1.00 39.65           C  
ANISOU 3180  CD2 TRP B 619     5384   6536   3148    490   -281    300       C  
ATOM   3181  NE1 TRP B 619       5.995  11.347  10.707  1.00 38.70           N  
ANISOU 3181  NE1 TRP B 619     5037   6246   3420    710   -370    429       N  
ATOM   3182  CE2 TRP B 619       5.749  10.758  11.922  1.00 38.91           C  
ANISOU 3182  CE2 TRP B 619     5212   6365   3206    613   -420    497       C  
ATOM   3183  CE3 TRP B 619       4.158  10.970  13.726  1.00 42.82           C  
ANISOU 3183  CE3 TRP B 619     5957   7065   3249    327   -267    313       C  
ATOM   3184  CZ2 TRP B 619       6.426   9.734  12.576  1.00 41.07           C  
ANISOU 3184  CZ2 TRP B 619     5563   6654   3390    620   -587    715       C  
ATOM   3185  CZ3 TRP B 619       4.831   9.950  14.375  1.00 44.26           C  
ANISOU 3185  CZ3 TRP B 619     6264   7265   3288    291   -439    562       C  
ATOM   3186  CH2 TRP B 619       5.951   9.344  13.799  1.00 43.66           C  
ANISOU 3186  CH2 TRP B 619     6095   7078   3414    458   -617    766       C  
ATOM   3187  N   MET B 620       1.778  16.096  13.511  1.00 41.83           N  
ANISOU 3187  N   MET B 620     5558   6861   3476    344    100   -843       N  
ATOM   3188  CA  MET B 620       0.644  17.011  13.555  1.00 44.78           C  
ANISOU 3188  CA  MET B 620     5857   7185   3973    389    243  -1169       C  
ATOM   3189  C   MET B 620       1.061  18.459  13.347  1.00 46.18           C  
ANISOU 3189  C   MET B 620     6019   7198   4331    445    125  -1336       C  
ATOM   3190  O   MET B 620       1.959  18.956  14.023  1.00 48.28           O  
ANISOU 3190  O   MET B 620     6375   7507   4461    335     19  -1359       O  
ATOM   3191  CB  MET B 620      -0.088  16.892  14.888  1.00 49.53           C  
ANISOU 3191  CB  MET B 620     6523   7997   4299    226    436  -1391       C  
ATOM   3192  CG  MET B 620      -0.883  15.618  15.043  1.00 50.39           C  
ANISOU 3192  CG  MET B 620     6641   8243   4264    145    603  -1292       C  
ATOM   3193  SD  MET B 620      -1.846  15.639  16.564  1.00 68.43           S  
ANISOU 3193  SD  MET B 620     8993  10795   6211   -100    890  -1607       S  
ATOM   3194  CE  MET B 620      -2.685  14.065  16.445  1.00 75.67           C  
ANISOU 3194  CE  MET B 620     9921  11823   7006   -214   1053  -1413       C  
ATOM   3195  N   ALA B 621       0.393  19.135  12.418  1.00 45.36           N  
ANISOU 3195  N   ALA B 621     5813   6891   4530    602    121  -1444       N  
ATOM   3196  CA  ALA B 621       0.621  20.556  12.192  1.00 43.48           C  
ANISOU 3196  CA  ALA B 621     5591   6439   4491    657      1  -1610       C  
ATOM   3197  C   ALA B 621       0.200  21.339  13.428  1.00 46.10           C  
ANISOU 3197  C   ALA B 621     5959   6830   4728    593    111  -1979       C  
ATOM   3198  O   ALA B 621      -0.640  20.875  14.194  1.00 44.98           O  
ANISOU 3198  O   ALA B 621     5778   6873   4441    548    320  -2150       O  
ATOM   3199  CB  ALA B 621      -0.153  21.027  10.974  1.00 40.57           C  
ANISOU 3199  CB  ALA B 621     5129   5826   4462    841    -55  -1629       C  
ATOM   3200  N   PRO B 622       0.789  22.528  13.630  1.00 48.77           N  
ANISOU 3200  N   PRO B 622     6382   7014   5135    562    -13  -2119       N  
ATOM   3201  CA  PRO B 622       0.430  23.394  14.757  1.00 53.03           C  
ANISOU 3201  CA  PRO B 622     6977   7571   5602    503     92  -2519       C  
ATOM   3202  C   PRO B 622      -1.076  23.613  14.910  1.00 57.45           C  
ANISOU 3202  C   PRO B 622     7386   8104   6337    655    307  -2864       C  
ATOM   3203  O   PRO B 622      -1.564  23.599  16.037  1.00 62.72           O  
ANISOU 3203  O   PRO B 622     8064   8966   6802    551    525  -3161       O  
ATOM   3204  CB  PRO B 622       1.116  24.712  14.404  1.00 53.26           C  
ANISOU 3204  CB  PRO B 622     7099   7306   5831    514   -115  -2582       C  
ATOM   3205  CG  PRO B 622       2.319  24.301  13.648  1.00 49.64           C  
ANISOU 3205  CG  PRO B 622     6674   6847   5340    436   -306  -2180       C  
ATOM   3206  CD  PRO B 622       1.933  23.067  12.872  1.00 47.63           C  
ANISOU 3206  CD  PRO B 622     6304   6691   5102    534   -244  -1912       C  
ATOM   3207  N   GLU B 623      -1.798  23.803  13.809  1.00 57.23           N  
ANISOU 3207  N   GLU B 623     7215   7858   6672    880    246  -2836       N  
ATOM   3208  CA  GLU B 623      -3.238  24.044  13.894  1.00 61.66           C  
ANISOU 3208  CA  GLU B 623     7570   8389   7470   1054    419  -3176       C  
ATOM   3209  C   GLU B 623      -4.011  22.785  14.292  1.00 63.03           C  
ANISOU 3209  C   GLU B 623     7614   8895   7441    972    678  -3168       C  
ATOM   3210  O   GLU B 623      -5.107  22.875  14.843  1.00 66.98           O  
ANISOU 3210  O   GLU B 623     7941   9501   8007   1014    917  -3523       O  
ATOM   3211  CB  GLU B 623      -3.790  24.616  12.583  1.00 60.97           C  
ANISOU 3211  CB  GLU B 623     7365   7960   7839   1318    216  -3123       C  
ATOM   3212  CG  GLU B 623      -3.860  23.626  11.429  1.00 58.48           C  
ANISOU 3212  CG  GLU B 623     6992   7674   7552   1350    121  -2733       C  
ATOM   3213  CD  GLU B 623      -2.584  23.575  10.616  1.00 57.25           C  
ANISOU 3213  CD  GLU B 623     7028   7405   7319   1259   -107  -2341       C  
ATOM   3214  OE1 GLU B 623      -1.547  24.079  11.096  1.00 56.68           O  
ANISOU 3214  OE1 GLU B 623     7120   7311   7107   1126   -170  -2332       O  
ATOM   3215  OE2 GLU B 623      -2.620  23.032   9.491  1.00 57.85           O  
ANISOU 3215  OE2 GLU B 623     7083   7427   7470   1303   -214  -2059       O  
ATOM   3216  N   VAL B 624      -3.439  21.617  14.017  1.00 59.76           N  
ANISOU 3216  N   VAL B 624     7278   8635   6792    847    639  -2778       N  
ATOM   3217  CA  VAL B 624      -4.068  20.352  14.385  1.00 60.72           C  
ANISOU 3217  CA  VAL B 624     7334   9041   6696    727    858  -2719       C  
ATOM   3218  C   VAL B 624      -3.880  20.080  15.876  1.00 63.70           C  
ANISOU 3218  C   VAL B 624     7854   9704   6645    464   1057  -2866       C  
ATOM   3219  O   VAL B 624      -4.764  19.542  16.542  1.00 66.18           O  
ANISOU 3219  O   VAL B 624     8095  10250   6800    343   1331  -3042       O  
ATOM   3220  CB  VAL B 624      -3.498  19.181  13.553  1.00 58.34           C  
ANISOU 3220  CB  VAL B 624     7096   8756   6314    696    730  -2256       C  
ATOM   3221  CG1 VAL B 624      -4.024  17.846  14.062  1.00 60.19           C  
ANISOU 3221  CG1 VAL B 624     7328   9256   6284    528    938  -2174       C  
ATOM   3222  CG2 VAL B 624      -3.840  19.361  12.086  1.00 55.27           C  
ANISOU 3222  CG2 VAL B 624     6584   8126   6292    909    567  -2132       C  
ATOM   3223  N   ILE B 625      -2.722  20.473  16.392  1.00 64.45           N  
ANISOU 3223  N   ILE B 625     8158   9791   6539    347    913  -2794       N  
ATOM   3224  CA  ILE B 625      -2.412  20.306  17.805  1.00 69.44           C  
ANISOU 3224  CA  ILE B 625     8975  10683   6727     71   1037  -2910       C  
ATOM   3225  C   ILE B 625      -3.341  21.132  18.696  1.00 79.22           C  
ANISOU 3225  C   ILE B 625    10148  11996   7954     35   1315  -3449       C  
ATOM   3226  O   ILE B 625      -3.708  20.702  19.789  1.00 83.95           O  
ANISOU 3226  O   ILE B 625    10835  12813   8251   -201   1515  -3499       O  
ATOM   3227  CB  ILE B 625      -0.939  20.652  18.100  1.00 66.84           C  
ANISOU 3227  CB  ILE B 625     8856  10316   6226    -40    772  -2728       C  
ATOM   3228  CG1 ILE B 625      -0.033  19.546  17.568  1.00 60.79           C  
ANISOU 3228  CG1 ILE B 625     8145   9579   5373    -61    568  -2229       C  
ATOM   3229  CG2 ILE B 625      -0.706  20.831  19.588  1.00 72.30           C  
ANISOU 3229  CG2 ILE B 625     9748  11241   6483   -323    870  -2939       C  
ATOM   3230  CD1 ILE B 625       1.387  19.633  18.060  1.00 60.68           C  
ANISOU 3230  CD1 ILE B 625     8298   9615   5143   -208    322  -2043       C  
ATOM   3231  N   ARG B 626      -3.740  22.308  18.225  1.00 82.44           N  
ANISOU 3231  N   ARG B 626    10414  12139   8770    273   1284  -3740       N  
ATOM   3232  CA  ARG B 626      -4.653  23.140  19.000  1.00 89.50           C  
ANISOU 3232  CA  ARG B 626    11219  12990   9796    284   1494  -4125       C  
ATOM   3233  C   ARG B 626      -6.067  22.564  19.027  1.00 93.34           C  
ANISOU 3233  C   ARG B 626    11451  13593  10420    311   1742  -4187       C  
ATOM   3234  O   ARG B 626      -6.262  21.354  19.148  1.00 93.78           O  
ANISOU 3234  O   ARG B 626    11520  13879  10234    146   1844  -3960       O  
ATOM   3235  CB  ARG B 626      -4.680  24.561  18.448  1.00 90.35           C  
ANISOU 3235  CB  ARG B 626    11258  12724  10348    549   1342  -4373       C  
ATOM   3236  CG  ARG B 626      -3.308  25.131  18.169  1.00 87.27           C  
ANISOU 3236  CG  ARG B 626    11092  12174   9893    527   1056  -4299       C  
ATOM   3237  CD  ARG B 626      -3.409  26.542  17.630  1.00 86.56           C  
ANISOU 3237  CD  ARG B 626    10970  11656  10263    770    892  -4523       C  
ATOM   3238  NE  ARG B 626      -2.223  26.908  16.866  1.00 83.11           N  
ANISOU 3238  NE  ARG B 626    10699  10980   9898    760    542  -4174       N  
ATOM   3239  CZ  ARG B 626      -2.239  27.259  15.585  1.00 79.90           C  
ANISOU 3239  CZ  ARG B 626    10235  10252   9873    970    306  -3963       C  
ATOM   3240  NH1 ARG B 626      -3.385  27.307  14.920  1.00 79.07           N  
ANISOU 3240  NH1 ARG B 626     9905  10008  10131   1235    337  -4065       N  
ATOM   3241  NH2 ARG B 626      -1.108  27.574  14.971  1.00 78.39           N  
ANISOU 3241  NH2 ARG B 626    10207   9887   9692    894     31  -3653       N  
ATOM   3242  N   ASN B 631     -12.783  21.250  12.831  1.00 81.22           N  
ANISOU 3242  N   ASN B 631     7970  11571  11317   1535   1398  -4081       N  
ATOM   3243  CA  ASN B 631     -11.991  20.526  11.843  1.00 77.46           C  
ANISOU 3243  CA  ASN B 631     7648  11050  10732   1550   1209  -3727       C  
ATOM   3244  C   ASN B 631     -10.767  21.313  11.382  1.00 74.06           C  
ANISOU 3244  C   ASN B 631     7469  10337  10334   1704    943  -3613       C  
ATOM   3245  O   ASN B 631     -10.878  22.213  10.551  1.00 74.96           O  
ANISOU 3245  O   ASN B 631     7537  10128  10816   1950    647  -3604       O  
ATOM   3246  CB  ASN B 631     -12.855  20.143  10.636  1.00 79.06           C  
ANISOU 3246  CB  ASN B 631     7607  11187  11246   1687   1024  -3611       C  
ATOM   3247  CG  ASN B 631     -12.104  19.295   9.621  1.00 76.29           C  
ANISOU 3247  CG  ASN B 631     7406  10819  10763   1683    860  -3261       C  
ATOM   3248  OD1 ASN B 631     -11.062  18.713   9.926  1.00 73.61           O  
ANISOU 3248  OD1 ASN B 631     7352  10573  10043   1509    933  -3055       O  
ATOM   3249  ND2 ASN B 631     -12.637  19.217   8.407  1.00 76.70           N  
ANISOU 3249  ND2 ASN B 631     7307  10732  11105   1837    599  -3133       N  
ATOM   3250  N   PRO B 632      -9.590  20.972  11.925  1.00 71.18           N  
ANISOU 3250  N   PRO B 632     7385  10087   9571   1538   1026  -3511       N  
ATOM   3251  CA  PRO B 632      -8.326  21.599  11.531  1.00 68.54           C  
ANISOU 3251  CA  PRO B 632     7340   9500   9202   1580    756  -3295       C  
ATOM   3252  C   PRO B 632      -7.611  20.842  10.407  1.00 64.44           C  
ANISOU 3252  C   PRO B 632     6987   8910   8588   1529    532  -2796       C  
ATOM   3253  O   PRO B 632      -6.504  21.223  10.025  1.00 62.88           O  
ANISOU 3253  O   PRO B 632     7021   8540   8329   1511    330  -2571       O  
ATOM   3254  CB  PRO B 632      -7.503  21.516  12.814  1.00 67.51           C  
ANISOU 3254  CB  PRO B 632     7430   9569   8651   1341    947  -3366       C  
ATOM   3255  CG  PRO B 632      -7.954  20.234  13.434  1.00 67.73           C  
ANISOU 3255  CG  PRO B 632     7410   9962   8363   1113   1234  -3337       C  
ATOM   3256  CD  PRO B 632      -9.419  20.079  13.086  1.00 70.29           C  
ANISOU 3256  CD  PRO B 632     7391  10322   8995   1217   1337  -3508       C  
ATOM   3257  N   TYR B 633      -8.233  19.787   9.889  1.00 62.10           N  
ANISOU 3257  N   TYR B 633     6568   8750   8278   1486    583  -2650       N  
ATOM   3258  CA  TYR B 633      -7.604  18.968   8.854  1.00 60.79           C  
ANISOU 3258  CA  TYR B 633     6562   8533   8002   1422    416  -2221       C  
ATOM   3259  C   TYR B 633      -7.810  19.518   7.447  1.00 59.82           C  
ANISOU 3259  C   TYR B 633     6409   8120   8198   1605     98  -2085       C  
ATOM   3260  O   TYR B 633      -8.915  19.909   7.071  1.00 62.31           O  
ANISOU 3260  O   TYR B 633     6483   8355   8836   1771     21  -2262       O  
ATOM   3261  CB  TYR B 633      -8.093  17.522   8.934  1.00 61.70           C  
ANISOU 3261  CB  TYR B 633     6619   8902   7922   1255    606  -2111       C  
ATOM   3262  CG  TYR B 633      -7.677  16.839  10.210  1.00 63.46           C  
ANISOU 3262  CG  TYR B 633     6972   9382   7757   1024    861  -2128       C  
ATOM   3263  CD1 TYR B 633      -6.415  16.278  10.337  1.00 60.51           C  
ANISOU 3263  CD1 TYR B 633     6872   9022   7097    899    802  -1829       C  
ATOM   3264  CD2 TYR B 633      -8.541  16.768  11.295  1.00 68.47           C  
ANISOU 3264  CD2 TYR B 633     7453  10250   8312    920   1152  -2446       C  
ATOM   3265  CE1 TYR B 633      -6.026  15.657  11.506  1.00 63.07           C  
ANISOU 3265  CE1 TYR B 633     7340   9560   7065    687    973  -1811       C  
ATOM   3266  CE2 TYR B 633      -8.162  16.150  12.469  1.00 69.74           C  
ANISOU 3266  CE2 TYR B 633     7784  10645   8068    667   1362  -2435       C  
ATOM   3267  CZ  TYR B 633      -6.904  15.597  12.568  1.00 68.64           C  
ANISOU 3267  CZ  TYR B 633     7943  10489   7648    556   1245  -2099       C  
ATOM   3268  OH  TYR B 633      -6.522  14.980  13.735  1.00 71.50           O  
ANISOU 3268  OH  TYR B 633     8497  11063   7606    303   1394  -2054       O  
ATOM   3269  N   SER B 634      -6.734  19.534   6.670  1.00 55.61           N  
ANISOU 3269  N   SER B 634     6120   7440   7568   1559    -91  -1770       N  
ATOM   3270  CA  SER B 634      -6.768  20.089   5.329  1.00 54.41           C  
ANISOU 3270  CA  SER B 634     6023   7012   7640   1670   -402  -1601       C  
ATOM   3271  C   SER B 634      -5.654  19.477   4.500  1.00 49.88           C  
ANISOU 3271  C   SER B 634     5692   6424   6837   1521   -476  -1236       C  
ATOM   3272  O   SER B 634      -4.912  18.620   4.981  1.00 45.45           O  
ANISOU 3272  O   SER B 634     5219   6049   6000   1378   -302  -1130       O  
ATOM   3273  CB  SER B 634      -6.588  21.606   5.384  1.00 56.37           C  
ANISOU 3273  CB  SER B 634     6325   6969   8123   1811   -594  -1742       C  
ATOM   3274  OG  SER B 634      -5.323  21.945   5.926  1.00 54.90           O  
ANISOU 3274  OG  SER B 634     6355   6776   7729   1685   -553  -1686       O  
ATOM   3275  N   PHE B 635      -5.541  19.924   3.253  1.00 48.71           N  
ANISOU 3275  N   PHE B 635     5655   6048   6805   1553   -738  -1050       N  
ATOM   3276  CA  PHE B 635      -4.433  19.526   2.401  1.00 44.42           C  
ANISOU 3276  CA  PHE B 635     5342   5479   6056   1400   -789   -746       C  
ATOM   3277  C   PHE B 635      -3.134  20.039   2.999  1.00 42.14           C  
ANISOU 3277  C   PHE B 635     5195   5180   5638   1313   -742   -725       C  
ATOM   3278  O   PHE B 635      -2.095  19.394   2.894  1.00 40.30           O  
ANISOU 3278  O   PHE B 635     5063   5059   5190   1178   -649   -556       O  
ATOM   3279  CB  PHE B 635      -4.612  20.089   0.991  1.00 51.78           C  
ANISOU 3279  CB  PHE B 635     6398   6164   7114   1412  -1088   -572       C  
ATOM   3280  CG  PHE B 635      -5.738  19.458   0.223  1.00 57.42           C  
ANISOU 3280  CG  PHE B 635     6999   6906   7912   1452  -1177   -538       C  
ATOM   3281  CD1 PHE B 635      -6.046  18.117   0.392  1.00 57.01           C  
ANISOU 3281  CD1 PHE B 635     6848   7099   7712   1379   -962   -537       C  
ATOM   3282  CD2 PHE B 635      -6.489  20.206  -0.667  1.00 61.50           C  
ANISOU 3282  CD2 PHE B 635     7519   7189   8660   1551  -1504   -499       C  
ATOM   3283  CE1 PHE B 635      -7.082  17.535  -0.313  1.00 58.47           C  
ANISOU 3283  CE1 PHE B 635     6928   7317   7972   1385  -1051   -516       C  
ATOM   3284  CE2 PHE B 635      -7.527  19.631  -1.377  1.00 63.17           C  
ANISOU 3284  CE2 PHE B 635     7611   7440   8949   1574  -1622   -467       C  
ATOM   3285  CZ  PHE B 635      -7.826  18.293  -1.197  1.00 62.21           C  
ANISOU 3285  CZ  PHE B 635     7378   7586   8673   1481  -1384   -486       C  
ATOM   3286  N   GLN B 636      -3.202  21.202   3.639  1.00 47.50           N  
ANISOU 3286  N   GLN B 636     5862   5719   6469   1396   -812   -920       N  
ATOM   3287  CA  GLN B 636      -2.021  21.821   4.225  1.00 49.90           C  
ANISOU 3287  CA  GLN B 636     6297   5995   6666   1294   -799   -924       C  
ATOM   3288  C   GLN B 636      -1.463  21.039   5.411  1.00 47.43           C  
ANISOU 3288  C   GLN B 636     5940   5973   6107   1201   -562   -981       C  
ATOM   3289  O   GLN B 636      -0.250  20.997   5.611  1.00 46.80           O  
ANISOU 3289  O   GLN B 636     5960   5954   5867   1070   -550   -865       O  
ATOM   3290  CB  GLN B 636      -2.308  23.266   4.631  1.00 57.63           C  
ANISOU 3290  CB  GLN B 636     7296   6720   7880   1402   -939  -1148       C  
ATOM   3291  CG  GLN B 636      -2.408  24.229   3.458  1.00 66.06           C  
ANISOU 3291  CG  GLN B 636     8509   7432   9158   1441  -1247  -1014       C  
ATOM   3292  CD  GLN B 636      -3.785  24.251   2.832  1.00 74.78           C  
ANISOU 3292  CD  GLN B 636     9478   8413  10522   1639  -1398  -1062       C  
ATOM   3293  OE1 GLN B 636      -4.796  24.113   3.523  1.00 79.42           O  
ANISOU 3293  OE1 GLN B 636     9826   9093  11258   1803  -1289  -1329       O  
ATOM   3294  NE2 GLN B 636      -3.835  24.429   1.517  1.00 76.66           N  
ANISOU 3294  NE2 GLN B 636     9863   8455  10810   1605  -1653   -808       N  
ATOM   3295  N   SER B 637      -2.340  20.416   6.193  1.00 45.81           N  
ANISOU 3295  N   SER B 637     5586   5951   5868   1251   -386  -1150       N  
ATOM   3296  CA  SER B 637      -1.885  19.601   7.316  1.00 46.32           C  
ANISOU 3296  CA  SER B 637     5654   6284   5664   1136   -189  -1168       C  
ATOM   3297  C   SER B 637      -1.243  18.295   6.840  1.00 45.03           C  
ANISOU 3297  C   SER B 637     5544   6247   5320   1045   -143   -881       C  
ATOM   3298  O   SER B 637      -0.307  17.795   7.465  1.00 45.95           O  
ANISOU 3298  O   SER B 637     5723   6499   5236    946    -93   -788       O  
ATOM   3299  CB  SER B 637      -3.019  19.334   8.311  1.00 47.35           C  
ANISOU 3299  CB  SER B 637     5636   6580   5775   1163      8  -1436       C  
ATOM   3300  OG  SER B 637      -4.148  18.764   7.679  1.00 49.23           O  
ANISOU 3300  OG  SER B 637     5727   6832   6146   1238     41  -1438       O  
ATOM   3301  N   ASP B 638      -1.740  17.749   5.733  1.00 41.12           N  
ANISOU 3301  N   ASP B 638     5025   5692   4905   1083   -178   -753       N  
ATOM   3302  CA  ASP B 638      -1.108  16.592   5.110  1.00 39.55           C  
ANISOU 3302  CA  ASP B 638     4893   5561   4573   1011   -138   -510       C  
ATOM   3303  C   ASP B 638       0.304  16.946   4.662  1.00 36.62           C  
ANISOU 3303  C   ASP B 638     4626   5126   4162    946   -224   -357       C  
ATOM   3304  O   ASP B 638       1.237  16.164   4.838  1.00 36.25           O  
ANISOU 3304  O   ASP B 638     4601   5188   3985    890   -162   -230       O  
ATOM   3305  CB  ASP B 638      -1.915  16.111   3.904  1.00 43.34           C  
ANISOU 3305  CB  ASP B 638     5354   5967   5145   1041   -180   -430       C  
ATOM   3306  CG  ASP B 638      -3.008  15.138   4.282  1.00 45.66           C  
ANISOU 3306  CG  ASP B 638     5541   6396   5409   1038    -42   -504       C  
ATOM   3307  OD1 ASP B 638      -3.040  14.696   5.450  1.00 47.59           O  
ANISOU 3307  OD1 ASP B 638     5760   6801   5523    990    108   -581       O  
ATOM   3308  OD2 ASP B 638      -3.828  14.804   3.401  1.00 44.07           O  
ANISOU 3308  OD2 ASP B 638     5297   6149   5298   1053    -90   -477       O  
ATOM   3309  N   VAL B 639       0.445  18.133   4.079  1.00 35.54           N  
ANISOU 3309  N   VAL B 639     4544   4805   4155    949   -375   -372       N  
ATOM   3310  CA  VAL B 639       1.736  18.630   3.616  1.00 33.18           C  
ANISOU 3310  CA  VAL B 639     4336   4447   3825    841   -446   -247       C  
ATOM   3311  C   VAL B 639       2.720  18.766   4.776  1.00 37.11           C  
ANISOU 3311  C   VAL B 639     4807   5072   4219    780   -411   -296       C  
ATOM   3312  O   VAL B 639       3.901  18.435   4.641  1.00 39.31           O  
ANISOU 3312  O   VAL B 639     5080   5434   4424    693   -393   -170       O  
ATOM   3313  CB  VAL B 639       1.582  19.986   2.902  1.00 33.64           C  
ANISOU 3313  CB  VAL B 639     4498   4250   4035    826   -636   -258       C  
ATOM   3314  CG1 VAL B 639       2.939  20.642   2.676  1.00 32.66           C  
ANISOU 3314  CG1 VAL B 639     4465   4082   3863    662   -688   -163       C  
ATOM   3315  CG2 VAL B 639       0.832  19.812   1.589  1.00 32.11           C  
ANISOU 3315  CG2 VAL B 639     4364   3934   3905    846   -725   -146       C  
ATOM   3316  N   TYR B 640       2.229  19.240   5.917  1.00 35.19           N  
ANISOU 3316  N   TYR B 640     4537   4858   3974    818   -400   -494       N  
ATOM   3317  CA  TYR B 640       3.072  19.361   7.095  1.00 35.94           C  
ANISOU 3317  CA  TYR B 640     4632   5090   3933    736   -389   -550       C  
ATOM   3318  C   TYR B 640       3.544  17.988   7.568  1.00 36.31           C  
ANISOU 3318  C   TYR B 640     4638   5354   3805    714   -300   -415       C  
ATOM   3319  O   TYR B 640       4.704  17.821   7.937  1.00 38.13           O  
ANISOU 3319  O   TYR B 640     4853   5680   3953    639   -350   -324       O  
ATOM   3320  CB  TYR B 640       2.342  20.092   8.230  1.00 38.35           C  
ANISOU 3320  CB  TYR B 640     4941   5396   4236    761   -364   -826       C  
ATOM   3321  CG  TYR B 640       3.215  20.300   9.448  1.00 40.22           C  
ANISOU 3321  CG  TYR B 640     5215   5774   4292    637   -380   -892       C  
ATOM   3322  CD1 TYR B 640       3.369  19.298  10.399  1.00 40.51           C  
ANISOU 3322  CD1 TYR B 640     5247   6049   4098    582   -300   -848       C  
ATOM   3323  CD2 TYR B 640       3.904  21.488   9.638  1.00 43.54           C  
ANISOU 3323  CD2 TYR B 640     5701   6080   4761    550   -503   -980       C  
ATOM   3324  CE1 TYR B 640       4.179  19.475  11.504  1.00 41.69           C  
ANISOU 3324  CE1 TYR B 640     5449   6334   4058    449   -360   -886       C  
ATOM   3325  CE2 TYR B 640       4.715  21.677  10.745  1.00 38.80           C  
ANISOU 3325  CE2 TYR B 640     5138   5622   3982    412   -544  -1043       C  
ATOM   3326  CZ  TYR B 640       4.847  20.667  11.671  1.00 38.87           C  
ANISOU 3326  CZ  TYR B 640     5133   5883   3751    365   -482   -993       C  
ATOM   3327  OH  TYR B 640       5.650  20.842  12.772  1.00 43.14           O  
ANISOU 3327  OH  TYR B 640     5728   6572   4091    211   -566  -1036       O  
ATOM   3328  N   ALA B 641       2.638  17.016   7.574  1.00 34.73           N  
ANISOU 3328  N   ALA B 641     4415   5215   3565    775   -189   -402       N  
ATOM   3329  CA  ALA B 641       2.980  15.661   7.994  1.00 34.90           C  
ANISOU 3329  CA  ALA B 641     4438   5386   3436    757   -124   -257       C  
ATOM   3330  C   ALA B 641       4.029  15.085   7.057  1.00 35.56           C  
ANISOU 3330  C   ALA B 641     4497   5440   3575    770   -158    -58       C  
ATOM   3331  O   ALA B 641       4.952  14.384   7.480  1.00 38.09           O  
ANISOU 3331  O   ALA B 641     4794   5853   3825    761   -187     59       O  
ATOM   3332  CB  ALA B 641       1.750  14.782   8.013  1.00 34.14           C  
ANISOU 3332  CB  ALA B 641     4338   5326   3306    788      5   -281       C  
ATOM   3333  N   PHE B 642       3.872  15.386   5.775  1.00 32.70           N  
ANISOU 3333  N   PHE B 642     4138   4946   3340    788   -158    -29       N  
ATOM   3334  CA  PHE B 642       4.821  14.953   4.769  1.00 34.51           C  
ANISOU 3334  CA  PHE B 642     4343   5155   3614    772   -144    111       C  
ATOM   3335  C   PHE B 642       6.184  15.589   5.023  1.00 36.61           C  
ANISOU 3335  C   PHE B 642     4545   5472   3894    694   -221    131       C  
ATOM   3336  O   PHE B 642       7.222  14.960   4.816  1.00 39.52           O  
ANISOU 3336  O   PHE B 642     4822   5913   4281    696   -197    224       O  
ATOM   3337  CB  PHE B 642       4.307  15.308   3.371  1.00 34.90           C  
ANISOU 3337  CB  PHE B 642     4455   5063   3743    751   -140    128       C  
ATOM   3338  CG  PHE B 642       5.250  14.935   2.276  1.00 35.26           C  
ANISOU 3338  CG  PHE B 642     4493   5104   3799    692    -81    234       C  
ATOM   3339  CD1 PHE B 642       5.289  13.640   1.796  1.00 34.74           C  
ANISOU 3339  CD1 PHE B 642     4419   5070   3712    741     37    296       C  
ATOM   3340  CD2 PHE B 642       6.105  15.876   1.731  1.00 37.15           C  
ANISOU 3340  CD2 PHE B 642     4741   5308   4068    567   -123    253       C  
ATOM   3341  CE1 PHE B 642       6.160  13.287   0.789  1.00 34.33           C  
ANISOU 3341  CE1 PHE B 642     4347   5024   3673    686    131    344       C  
ATOM   3342  CE2 PHE B 642       6.980  15.530   0.725  1.00 38.31           C  
ANISOU 3342  CE2 PHE B 642     4864   5485   4207    481    -21    319       C  
ATOM   3343  CZ  PHE B 642       7.008  14.231   0.252  1.00 35.18           C  
ANISOU 3343  CZ  PHE B 642     4440   5133   3795    550    117    349       C  
ATOM   3344  N   GLY B 643       6.172  16.840   5.473  1.00 34.24           N  
ANISOU 3344  N   GLY B 643     4277   5127   3607    626   -314     25       N  
ATOM   3345  CA  GLY B 643       7.396  17.537   5.827  1.00 34.55           C  
ANISOU 3345  CA  GLY B 643     4259   5218   3652    514   -403     23       C  
ATOM   3346  C   GLY B 643       8.154  16.849   6.949  1.00 35.46           C  
ANISOU 3346  C   GLY B 643     4280   5515   3676    527   -450     63       C  
ATOM   3347  O   GLY B 643       9.384  16.791   6.937  1.00 35.20           O  
ANISOU 3347  O   GLY B 643     4119   5571   3683    473   -504    128       O  
ATOM   3348  N   ILE B 644       7.416  16.328   7.924  1.00 35.32           N  
ANISOU 3348  N   ILE B 644     4323   5560   3536    583   -440     26       N  
ATOM   3349  CA  ILE B 644       8.022  15.590   9.027  1.00 38.72           C  
ANISOU 3349  CA  ILE B 644     4723   6148   3843    581   -522    100       C  
ATOM   3350  C   ILE B 644       8.597  14.264   8.535  1.00 39.47           C  
ANISOU 3350  C   ILE B 644     4726   6265   4008    688   -500    277       C  
ATOM   3351  O   ILE B 644       9.661  13.834   8.982  1.00 41.50           O  
ANISOU 3351  O   ILE B 644     4874   6615   4280    703   -622    372       O  
ATOM   3352  CB  ILE B 644       7.015  15.342  10.178  1.00 39.45           C  
ANISOU 3352  CB  ILE B 644     4947   6305   3737    563   -492     21       C  
ATOM   3353  CG1 ILE B 644       6.550  16.674  10.770  1.00 39.96           C  
ANISOU 3353  CG1 ILE B 644     5082   6350   3752    471   -502   -207       C  
ATOM   3354  CG2 ILE B 644       7.644  14.491  11.274  1.00 35.95           C  
ANISOU 3354  CG2 ILE B 644     4525   6008   3127    534   -614    150       C  
ATOM   3355  CD1 ILE B 644       7.649  17.428  11.500  1.00 37.11           C  
ANISOU 3355  CD1 ILE B 644     4705   6068   3329    342   -668   -243       C  
ATOM   3356  N   VAL B 645       7.891  13.618   7.609  1.00 36.61           N  
ANISOU 3356  N   VAL B 645     4401   5805   3706    769   -360    307       N  
ATOM   3357  CA  VAL B 645       8.383  12.378   7.016  1.00 37.15           C  
ANISOU 3357  CA  VAL B 645     4399   5851   3864    879   -312    434       C  
ATOM   3358  C   VAL B 645       9.693  12.617   6.269  1.00 39.67           C  
ANISOU 3358  C   VAL B 645     4532   6198   4344    872   -316    449       C  
ATOM   3359  O   VAL B 645      10.613  11.802   6.343  1.00 42.58           O  
ANISOU 3359  O   VAL B 645     4760   6609   4809    966   -358    526       O  
ATOM   3360  CB  VAL B 645       7.336  11.725   6.084  1.00 36.22           C  
ANISOU 3360  CB  VAL B 645     4378   5619   3766    929   -154    434       C  
ATOM   3361  CG1 VAL B 645       7.973  10.637   5.228  1.00 36.09           C  
ANISOU 3361  CG1 VAL B 645     4291   5551   3872   1028    -78    512       C  
ATOM   3362  CG2 VAL B 645       6.183  11.158   6.898  1.00 34.15           C  
ANISOU 3362  CG2 VAL B 645     4252   5363   3362    928   -133    435       C  
ATOM   3363  N   LEU B 646       9.778  13.743   5.562  1.00 38.01           N  
ANISOU 3363  N   LEU B 646     4315   5957   4171    755   -278    370       N  
ATOM   3364  CA  LEU B 646      11.018  14.131   4.899  1.00 37.59           C  
ANISOU 3364  CA  LEU B 646     4085   5959   4240    678   -257    366       C  
ATOM   3365  C   LEU B 646      12.126  14.292   5.925  1.00 39.44           C  
ANISOU 3365  C   LEU B 646     4146   6337   4503    656   -429    382       C  
ATOM   3366  O   LEU B 646      13.267  13.891   5.696  1.00 41.75           O  
ANISOU 3366  O   LEU B 646     4203   6720   4938    688   -431    407       O  
ATOM   3367  CB  LEU B 646      10.845  15.445   4.141  1.00 40.39           C  
ANISOU 3367  CB  LEU B 646     4526   6235   4586    500   -225    302       C  
ATOM   3368  CG  LEU B 646       9.943  15.464   2.911  1.00 39.46           C  
ANISOU 3368  CG  LEU B 646     4568   5977   4447    480   -101    304       C  
ATOM   3369  CD1 LEU B 646       9.901  16.870   2.330  1.00 39.88           C  
ANISOU 3369  CD1 LEU B 646     4733   5929   4492    289   -146    276       C  
ATOM   3370  CD2 LEU B 646      10.433  14.469   1.879  1.00 37.44           C  
ANISOU 3370  CD2 LEU B 646     4228   5751   4246    515     71    336       C  
ATOM   3371  N   TYR B 647      11.778  14.888   7.059  1.00 37.98           N  
ANISOU 3371  N   TYR B 647     4064   6181   4185    596   -574    349       N  
ATOM   3372  CA  TYR B 647      12.733  15.091   8.132  1.00 40.48           C  
ANISOU 3372  CA  TYR B 647     4258   6641   4483    543   -779    366       C  
ATOM   3373  C   TYR B 647      13.259  13.759   8.649  1.00 43.38           C  
ANISOU 3373  C   TYR B 647     4509   7077   4895    710   -884    499       C  
ATOM   3374  O   TYR B 647      14.444  13.631   8.950  1.00 44.18           O  
ANISOU 3374  O   TYR B 647     4380   7295   5112    720  -1034    541       O  
ATOM   3375  CB  TYR B 647      12.094  15.885   9.269  1.00 43.04           C  
ANISOU 3375  CB  TYR B 647     4770   6976   4607    436   -888    279       C  
ATOM   3376  CG  TYR B 647      13.055  16.217  10.387  1.00 44.91           C  
ANISOU 3376  CG  TYR B 647     4917   7367   4779    331  -1123    283       C  
ATOM   3377  CD1 TYR B 647      13.820  17.375  10.347  1.00 47.09           C  
ANISOU 3377  CD1 TYR B 647     5105   7680   5108    147  -1199    194       C  
ATOM   3378  CD2 TYR B 647      13.203  15.370  11.478  1.00 43.68           C  
ANISOU 3378  CD2 TYR B 647     4786   7315   4496    388  -1293    390       C  
ATOM   3379  CE1 TYR B 647      14.703  17.681  11.362  1.00 49.50           C  
ANISOU 3379  CE1 TYR B 647     5321   8137   5347     27  -1435    190       C  
ATOM   3380  CE2 TYR B 647      14.087  15.667  12.496  1.00 44.76           C  
ANISOU 3380  CE2 TYR B 647     4852   7602   4553    275  -1551    407       C  
ATOM   3381  CZ  TYR B 647      14.832  16.823  12.433  1.00 50.52           C  
ANISOU 3381  CZ  TYR B 647     5468   8383   5344     97  -1620    297       C  
ATOM   3382  OH  TYR B 647      15.710  17.124  13.445  1.00 48.81           O  
ANISOU 3382  OH  TYR B 647     5176   8326   5042    -39  -1897    306       O  
ATOM   3383  N   GLU B 648      12.376  12.770   8.752  1.00 44.43           N  
ANISOU 3383  N   GLU B 648     4800   7127   4956    836   -825    568       N  
ATOM   3384  CA  GLU B 648      12.789  11.434   9.158  1.00 47.34           C  
ANISOU 3384  CA  GLU B 648     5111   7493   5383   1004   -936    716       C  
ATOM   3385  C   GLU B 648      13.739  10.825   8.136  1.00 46.31           C  
ANISOU 3385  C   GLU B 648     4719   7339   5538   1145   -854    722       C  
ATOM   3386  O   GLU B 648      14.750  10.234   8.500  1.00 46.62           O  
ANISOU 3386  O   GLU B 648     4551   7430   5734   1265  -1024    798       O  
ATOM   3387  CB  GLU B 648      11.579  10.520   9.318  1.00 49.41           C  
ANISOU 3387  CB  GLU B 648     5622   7640   5512   1070   -853    781       C  
ATOM   3388  CG  GLU B 648      10.566  10.995  10.321  1.00 51.62           C  
ANISOU 3388  CG  GLU B 648     6138   7964   5510    927   -878    741       C  
ATOM   3389  CD  GLU B 648       9.421  10.025  10.462  1.00 53.17           C  
ANISOU 3389  CD  GLU B 648     6546   8073   5585    957   -776    804       C  
ATOM   3390  OE1 GLU B 648       9.610   8.984  11.125  1.00 55.05           O  
ANISOU 3390  OE1 GLU B 648     6864   8289   5763   1008   -911    971       O  
ATOM   3391  OE2 GLU B 648       8.338  10.298   9.901  1.00 51.08           O  
ANISOU 3391  OE2 GLU B 648     6366   7751   5292    921   -581    695       O  
ATOM   3392  N   LEU B 649      13.402  10.967   6.858  1.00 43.66           N  
ANISOU 3392  N   LEU B 649     4389   6929   5272   1128   -599    631       N  
ATOM   3393  CA  LEU B 649      14.221  10.410   5.790  1.00 47.21           C  
ANISOU 3393  CA  LEU B 649     4609   7368   5961   1230   -452    587       C  
ATOM   3394  C   LEU B 649      15.603  11.045   5.733  1.00 51.50           C  
ANISOU 3394  C   LEU B 649     4821   8077   6670   1157   -509    526       C  
ATOM   3395  O   LEU B 649      16.600  10.352   5.540  1.00 57.49           O  
ANISOU 3395  O   LEU B 649     5292   8879   7672   1305   -518    513       O  
ATOM   3396  CB  LEU B 649      13.529  10.579   4.440  1.00 46.72           C  
ANISOU 3396  CB  LEU B 649     4672   7214   5864   1155   -173    497       C  
ATOM   3397  CG  LEU B 649      12.257   9.768   4.217  1.00 44.77           C  
ANISOU 3397  CG  LEU B 649     4687   6810   5512   1232    -84    535       C  
ATOM   3398  CD1 LEU B 649      11.553  10.250   2.960  1.00 43.20           C  
ANISOU 3398  CD1 LEU B 649     4623   6548   5241   1104    123    453       C  
ATOM   3399  CD2 LEU B 649      12.583   8.285   4.125  1.00 44.30           C  
ANISOU 3399  CD2 LEU B 649     4567   6656   5611   1452    -65    579       C  
ATOM   3400  N   MET B 650      15.663  12.362   5.908  1.00 49.15           N  
ANISOU 3400  N   MET B 650     4550   7861   6263    929   -549    474       N  
ATOM   3401  CA  MET B 650      16.917  13.093   5.747  1.00 49.33           C  
ANISOU 3401  CA  MET B 650     4270   8046   6426    789   -575    403       C  
ATOM   3402  C   MET B 650      17.801  13.110   6.994  1.00 50.31           C  
ANISOU 3402  C   MET B 650     4193   8313   6608    814   -894    460       C  
ATOM   3403  O   MET B 650      19.016  13.271   6.888  1.00 52.99           O  
ANISOU 3403  O   MET B 650     4176   8806   7150    776   -940    411       O  
ATOM   3404  CB  MET B 650      16.646  14.522   5.274  1.00 48.78           C  
ANISOU 3404  CB  MET B 650     4340   7965   6227    501   -484    326       C  
ATOM   3405  CG  MET B 650      15.961  14.602   3.918  1.00 47.75           C  
ANISOU 3405  CG  MET B 650     4383   7712   6048    439   -210    285       C  
ATOM   3406  SD  MET B 650      16.913  13.839   2.590  1.00 67.43           S  
ANISOU 3406  SD  MET B 650     6589  10287   8746    472     76    203       S  
ATOM   3407  CE  MET B 650      15.971  12.347   2.290  1.00 69.40           C  
ANISOU 3407  CE  MET B 650     7006  10373   8991    758    175    241       C  
ATOM   3408  N   THR B 651      17.199  12.949   8.167  1.00 49.25           N  
ANISOU 3408  N   THR B 651     4280   8147   6286    853  -1115    558       N  
ATOM   3409  CA  THR B 651      17.963  12.947   9.411  1.00 51.76           C  
ANISOU 3409  CA  THR B 651     4467   8600   6599    848  -1460    634       C  
ATOM   3410  C   THR B 651      18.146  11.538   9.952  1.00 53.99           C  
ANISOU 3410  C   THR B 651     4705   8833   6977   1117  -1649    793       C  
ATOM   3411  O   THR B 651      19.152  11.234  10.589  1.00 58.36           O  
ANISOU 3411  O   THR B 651     5008   9492   7674   1193  -1936    867       O  
ATOM   3412  CB  THR B 651      17.284  13.800  10.498  1.00 51.03           C  
ANISOU 3412  CB  THR B 651     4676   8527   6186    655  -1610    629       C  
ATOM   3413  OG1 THR B 651      16.015  13.225  10.836  1.00 49.98           O  
ANISOU 3413  OG1 THR B 651     4881   8265   5846    735  -1551    690       O  
ATOM   3414  CG2 THR B 651      17.083  15.231  10.011  1.00 48.61           C  
ANISOU 3414  CG2 THR B 651     4445   8211   5815    405  -1461    472       C  
ATOM   3415  N   GLY B 652      17.168  10.678   9.693  1.00 54.08           N  
ANISOU 3415  N   GLY B 652     4963   8668   6918   1256  -1513    853       N  
ATOM   3416  CA  GLY B 652      17.182   9.332  10.232  1.00 57.60           C  
ANISOU 3416  CA  GLY B 652     5456   9007   7424   1487  -1699   1025       C  
ATOM   3417  C   GLY B 652      16.645   9.327  11.646  1.00 59.22           C  
ANISOU 3417  C   GLY B 652     5963   9234   7304   1383  -1967   1171       C  
ATOM   3418  O   GLY B 652      16.736   8.326  12.354  1.00 61.25           O  
ANISOU 3418  O   GLY B 652     6306   9415   7551   1515  -2210   1360       O  
ATOM   3419  N   GLN B 653      16.077  10.456  12.054  1.00 59.25           N  
ANISOU 3419  N   GLN B 653     6148   9330   7033   1133  -1919   1075       N  
ATOM   3420  CA  GLN B 653      15.609  10.630  13.421  1.00 61.53           C  
ANISOU 3420  CA  GLN B 653     6719   9686   6972    977  -2131   1156       C  
ATOM   3421  C   GLN B 653      14.173  11.121  13.466  1.00 59.22           C  
ANISOU 3421  C   GLN B 653     6753   9346   6400    829  -1880   1043       C  
ATOM   3422  O   GLN B 653      13.667  11.681  12.496  1.00 56.93           O  
ANISOU 3422  O   GLN B 653     6446   8993   6191    813  -1603    892       O  
ATOM   3423  CB  GLN B 653      16.493  11.637  14.162  1.00 65.31           C  
ANISOU 3423  CB  GLN B 653     7064  10363   7390    792  -2379   1104       C  
ATOM   3424  CG  GLN B 653      17.963  11.281  14.184  1.00 72.77           C  
ANISOU 3424  CG  GLN B 653     7618  11396   8636    919  -2659   1191       C  
ATOM   3425  CD  GLN B 653      18.668  11.801  15.421  1.00 80.01           C  
ANISOU 3425  CD  GLN B 653     8514  12500   9386    739  -3052   1244       C  
ATOM   3426  OE1 GLN B 653      18.395  12.906  15.889  1.00 79.53           O  
ANISOU 3426  OE1 GLN B 653     8607  12537   9075    474  -3033   1110       O  
ATOM   3427  NE2 GLN B 653      19.572  10.994  15.968  1.00 85.98           N  
ANISOU 3427  NE2 GLN B 653     9090  13293  10285    885  -3433   1435       N  
ATOM   3428  N   LEU B 654      13.523  10.908  14.605  1.00 60.52           N  
ANISOU 3428  N   LEU B 654     7211   9548   6237    711  -1988   1115       N  
ATOM   3429  CA  LEU B 654      12.234  11.524  14.881  1.00 58.52           C  
ANISOU 3429  CA  LEU B 654     7221   9302   5713    543  -1768    959       C  
ATOM   3430  C   LEU B 654      12.478  12.933  15.402  1.00 56.97           C  
ANISOU 3430  C   LEU B 654     7018   9237   5391    337  -1823    771       C  
ATOM   3431  O   LEU B 654      13.463  13.176  16.098  1.00 59.37           O  
ANISOU 3431  O   LEU B 654     7239   9666   5653    255  -2105    824       O  
ATOM   3432  CB  LEU B 654      11.461  10.709  15.917  1.00 62.47           C  
ANISOU 3432  CB  LEU B 654     8034   9814   5886    455  -1823   1088       C  
ATOM   3433  CG  LEU B 654      10.831   9.402  15.438  1.00 63.35           C  
ANISOU 3433  CG  LEU B 654     8245   9759   6065    598  -1705   1236       C  
ATOM   3434  CD1 LEU B 654      10.282   8.610  16.616  1.00 64.28           C  
ANISOU 3434  CD1 LEU B 654     8691   9903   5828    449  -1818   1405       C  
ATOM   3435  CD2 LEU B 654       9.736   9.683  14.418  1.00 60.84           C  
ANISOU 3435  CD2 LEU B 654     7927   9351   5837    626  -1339   1054       C  
ATOM   3436  N   PRO B 655      11.585  13.871  15.064  1.00 53.75           N  
ANISOU 3436  N   PRO B 655     6695   8784   4942    256  -1576    546       N  
ATOM   3437  CA  PRO B 655      11.754  15.258  15.509  1.00 54.32           C  
ANISOU 3437  CA  PRO B 655     6790   8927   4923     68  -1614    337       C  
ATOM   3438  C   PRO B 655      11.573  15.387  17.013  1.00 57.65           C  
ANISOU 3438  C   PRO B 655     7443   9499   4964   -135  -1756    299       C  
ATOM   3439  O   PRO B 655      10.917  14.542  17.620  1.00 58.67           O  
ANISOU 3439  O   PRO B 655     7765   9661   4866   -153  -1729    393       O  
ATOM   3440  CB  PRO B 655      10.629  15.998  14.779  1.00 51.51           C  
ANISOU 3440  CB  PRO B 655     6502   8432   4637     84  -1320    125       C  
ATOM   3441  CG  PRO B 655       9.597  14.953  14.525  1.00 52.00           C  
ANISOU 3441  CG  PRO B 655     6661   8432   4665    202  -1146    204       C  
ATOM   3442  CD  PRO B 655      10.368  13.693  14.254  1.00 51.76           C  
ANISOU 3442  CD  PRO B 655     6521   8398   4749    342  -1276    468       C  
ATOM   3443  N   TYR B 656      12.154  16.436  17.591  1.00 61.16           N  
ANISOU 3443  N   TYR B 656     7886  10033   5320   -317  -1899    159       N  
ATOM   3444  CA  TYR B 656      12.021  16.733  19.017  1.00 67.10           C  
ANISOU 3444  CA  TYR B 656     8881  10942   5673   -558  -2025     72       C  
ATOM   3445  C   TYR B 656      12.575  15.614  19.898  1.00 73.61           C  
ANISOU 3445  C   TYR B 656     9784  11900   6285   -593  -2326    360       C  
ATOM   3446  O   TYR B 656      11.903  15.142  20.813  1.00 76.23           O  
ANISOU 3446  O   TYR B 656    10396  12312   6256   -725  -2308    390       O  
ATOM   3447  CB  TYR B 656      10.559  17.018  19.375  1.00 64.85           C  
ANISOU 3447  CB  TYR B 656     8838  10633   5170   -631  -1717   -164       C  
ATOM   3448  CG  TYR B 656       9.830  17.813  18.320  1.00 61.28           C  
ANISOU 3448  CG  TYR B 656     8294   9991   4997   -507  -1437   -383       C  
ATOM   3449  CD1 TYR B 656      10.368  18.988  17.811  1.00 60.55           C  
ANISOU 3449  CD1 TYR B 656     8089   9800   5116   -533  -1477   -528       C  
ATOM   3450  CD2 TYR B 656       8.614  17.376  17.813  1.00 59.77           C  
ANISOU 3450  CD2 TYR B 656     8137   9708   4864   -379  -1162   -426       C  
ATOM   3451  CE1 TYR B 656       9.710  19.712  16.841  1.00 58.13           C  
ANISOU 3451  CE1 TYR B 656     7738   9289   5060   -427  -1273   -690       C  
ATOM   3452  CE2 TYR B 656       7.949  18.094  16.840  1.00 58.12           C  
ANISOU 3452  CE2 TYR B 656     7846   9317   4920   -258   -965   -601       C  
ATOM   3453  CZ  TYR B 656       8.502  19.261  16.358  1.00 58.41           C  
ANISOU 3453  CZ  TYR B 656     7801   9237   5154   -277  -1033   -722       C  
ATOM   3454  OH  TYR B 656       7.841  19.979  15.390  1.00 60.53           O  
ANISOU 3454  OH  TYR B 656     8025   9293   5679   -164   -885   -863       O  
ATOM   3455  N   SER B 657      13.807  15.202  19.615  1.00 77.84           N  
ANISOU 3455  N   SER B 657    10068  12455   7052   -484  -2609    570       N  
ATOM   3456  CA  SER B 657      14.465  14.139  20.368  1.00 83.98           C  
ANISOU 3456  CA  SER B 657    10883  13316   7709   -471  -2972    873       C  
ATOM   3457  C   SER B 657      14.814  14.550  21.796  1.00 91.34           C  
ANISOU 3457  C   SER B 657    12030  14420   8254   -756  -3245    849       C  
ATOM   3458  O   SER B 657      14.856  13.714  22.695  1.00 94.72           O  
ANISOU 3458  O   SER B 657    12656  14825   8508   -768  -3388   1022       O  
ATOM   3459  CB  SER B 657      15.722  13.663  19.637  1.00 84.85           C  
ANISOU 3459  CB  SER B 657    10598  13392   8248   -241  -3192   1051       C  
ATOM   3460  OG  SER B 657      15.386  12.872  18.513  1.00 82.71           O  
ANISOU 3460  OG  SER B 657    10206  12943   8279     32  -2961   1123       O  
ATOM   3461  N   ASN B 658      15.069  15.836  22.004  1.00 95.39           N  
ANISOU 3461  N   ASN B 658    12517  15022   8704   -954  -3246    595       N  
ATOM   3462  CA  ASN B 658      15.413  16.315  23.336  1.00102.90           C  
ANISOU 3462  CA  ASN B 658    13671  16058   9370  -1190  -3411    503       C  
ATOM   3463  C   ASN B 658      14.204  16.749  24.149  1.00102.44           C  
ANISOU 3463  C   ASN B 658    13992  16023   8909  -1401  -3128    262       C  
ATOM   3464  O   ASN B 658      14.343  17.379  25.194  1.00105.65           O  
ANISOU 3464  O   ASN B 658    14576  16506   9063  -1627  -3188    108       O  
ATOM   3465  CB  ASN B 658      16.441  17.444  23.262  1.00109.66           C  
ANISOU 3465  CB  ASN B 658    14307  16981  10376  -1314  -3587    352       C  
ATOM   3466  CG  ASN B 658      17.826  16.943  22.911  1.00116.72           C  
ANISOU 3466  CG  ASN B 658    14825  17900  11624  -1152  -3916    581       C  
ATOM   3467  OD1 ASN B 658      18.117  15.752  23.031  1.00120.34           O  
ANISOU 3467  OD1 ASN B 658    15237  18319  12166   -956  -4076    846       O  
ATOM   3468  ND2 ASN B 658      18.692  17.852  22.480  1.00118.56           N  
ANISOU 3468  ND2 ASN B 658    14778  18187  12084  -1237  -4009    460       N  
ATOM   3469  N   ILE B 659      13.015  16.411  23.665  1.00 99.46           N  
ANISOU 3469  N   ILE B 659    13715  15587   8489  -1327  -2801    209       N  
ATOM   3470  CA  ILE B 659      11.797  16.676  24.417  1.00 99.58           C  
ANISOU 3470  CA  ILE B 659    14038  15629   8169  -1500  -2486    -31       C  
ATOM   3471  C   ILE B 659      11.004  15.391  24.600  1.00 99.86           C  
ANISOU 3471  C   ILE B 659    14236  15630   8078  -1442  -2354    175       C  
ATOM   3472  O   ILE B 659      10.436  14.854  23.649  1.00 97.16           O  
ANISOU 3472  O   ILE B 659    13802  15211   7902  -1270  -2187    248       O  
ATOM   3473  CB  ILE B 659      10.924  17.748  23.741  1.00 96.18           C  
ANISOU 3473  CB  ILE B 659    13572  15161   7812  -1508  -2147   -409       C  
ATOM   3474  CG1 ILE B 659      11.744  19.018  23.505  1.00 96.16           C  
ANISOU 3474  CG1 ILE B 659    13428  15150   7959  -1586  -2292   -603       C  
ATOM   3475  CG2 ILE B 659       9.697  18.042  24.590  1.00 97.45           C  
ANISOU 3475  CG2 ILE B 659    13996  15347   7684  -1662  -1804   -701       C  
ATOM   3476  CD1 ILE B 659      10.913  20.254  23.264  1.00 95.36           C  
ANISOU 3476  CD1 ILE B 659    13373  14922   7937  -1609  -1969  -1031       C  
ATOM   3477  N   ASN B 660      10.976  14.899  25.832  1.00104.18           N  
ANISOU 3477  N   ASN B 660    15030  16233   8321  -1609  -2434    274       N  
ATOM   3478  CA  ASN B 660      10.340  13.625  26.130  1.00105.71           C  
ANISOU 3478  CA  ASN B 660    15402  16383   8381  -1603  -2353    502       C  
ATOM   3479  C   ASN B 660       8.973  13.784  26.777  1.00104.68           C  
ANISOU 3479  C   ASN B 660    15503  16317   7953  -1812  -1947    257       C  
ATOM   3480  O   ASN B 660       8.387  12.817  27.259  1.00108.53           O  
ANISOU 3480  O   ASN B 660    16175  16794   8267  -1897  -1859    415       O  
ATOM   3481  CB  ASN B 660      11.253  12.785  27.023  1.00111.85           C  
ANISOU 3481  CB  ASN B 660    16287  17164   9045  -1647  -2742    830       C  
ATOM   3482  CG  ASN B 660      12.605  12.536  26.390  1.00112.59           C  
ANISOU 3482  CG  ASN B 660    16091  17192   9496  -1404  -3132   1057       C  
ATOM   3483  OD1 ASN B 660      13.381  13.469  26.171  1.00111.74           O  
ANISOU 3483  OD1 ASN B 660    15782  17143   9530  -1399  -3269    924       O  
ATOM   3484  ND2 ASN B 660      12.897  11.275  26.092  1.00113.67           N  
ANISOU 3484  ND2 ASN B 660    16189  17197   9803  -1204  -3300   1384       N  
ATOM   3485  N   ASN B 661       8.463  15.008  26.783  1.00 99.30           N  
ANISOU 3485  N   ASN B 661    14797  15691   7242  -1897  -1694   -143       N  
ATOM   3486  CA  ASN B 661       7.163  15.263  27.376  1.00 96.04           C  
ANISOU 3486  CA  ASN B 661    14536  15342   6613  -2068  -1282   -434       C  
ATOM   3487  C   ASN B 661       6.126  15.578  26.306  1.00 89.35           C  
ANISOU 3487  C   ASN B 661    13514  14426   6007  -1903   -921   -674       C  
ATOM   3488  O   ASN B 661       6.307  16.495  25.505  1.00 83.23           O  
ANISOU 3488  O   ASN B 661    12561  13597   5466  -1771   -906   -876       O  
ATOM   3489  CB  ASN B 661       7.254  16.391  28.399  1.00 98.84           C  
ANISOU 3489  CB  ASN B 661    15013  15797   6744  -2294  -1241   -750       C  
ATOM   3490  CG  ASN B 661       6.128  16.349  29.402  1.00102.72           C  
ANISOU 3490  CG  ASN B 661    15701  16390   6938  -2530   -894   -955       C  
ATOM   3491  OD1 ASN B 661       5.171  17.115  29.310  1.00101.60           O  
ANISOU 3491  OD1 ASN B 661    15498  16250   6855  -2530   -527  -1345       O  
ATOM   3492  ND2 ASN B 661       6.226  15.435  30.361  1.00108.10           N  
ANISOU 3492  ND2 ASN B 661    16607  17148   7318  -2732  -1011   -696       N  
ATOM   3493  N   ARG B 662       5.046  14.802  26.298  1.00 90.03           N  
ANISOU 3493  N   ARG B 662    13650  14514   6045  -1924   -644   -649       N  
ATOM   3494  CA  ARG B 662       4.012  14.920  25.277  1.00 87.82           C  
ANISOU 3494  CA  ARG B 662    13184  14172   6010  -1760   -318   -841       C  
ATOM   3495  C   ARG B 662       3.374  16.302  25.298  1.00 86.80           C  
ANISOU 3495  C   ARG B 662    12955  14052   5972  -1757    -44  -1336       C  
ATOM   3496  O   ARG B 662       3.141  16.904  24.252  1.00 82.46           O  
ANISOU 3496  O   ARG B 662    12200  13412   5719  -1555     48  -1518       O  
ATOM   3497  CB  ARG B 662       2.936  13.848  25.477  1.00 91.76           C  
ANISOU 3497  CB  ARG B 662    13758  14689   6418  -1843    -70   -744       C  
ATOM   3498  CG  ARG B 662       2.119  13.539  24.227  1.00 92.87           C  
ANISOU 3498  CG  ARG B 662    13691  14746   6850  -1639    147   -781       C  
ATOM   3499  CD  ARG B 662       0.947  12.614  24.541  1.00 98.50           C  
ANISOU 3499  CD  ARG B 662    14463  15491   7472  -1774    422   -749       C  
ATOM   3500  NE  ARG B 662       0.208  12.223  23.341  1.00 98.31           N  
ANISOU 3500  NE  ARG B 662    14239  15384   7729  -1591    595   -756       N  
ATOM   3501  CZ  ARG B 662       0.364  11.064  22.709  1.00 99.05           C  
ANISOU 3501  CZ  ARG B 662    14367  15379   7890  -1516    478   -414       C  
ATOM   3502  NH1 ARG B 662       1.232  10.168  23.160  1.00100.81           N  
ANISOU 3502  NH1 ARG B 662    14801  15548   7954  -1578    177    -36       N  
ATOM   3503  NH2 ARG B 662      -0.352  10.797  21.625  1.00 97.60           N  
ANISOU 3503  NH2 ARG B 662    13999  15132   7954  -1369    650   -456       N  
ATOM   3504  N   ASP B 663       3.106  16.807  26.496  1.00 91.82           N  
ANISOU 3504  N   ASP B 663    13741  14784   6364  -1978     75  -1558       N  
ATOM   3505  CA  ASP B 663       2.440  18.095  26.644  1.00 92.28           C  
ANISOU 3505  CA  ASP B 663    13717  14822   6526  -1968    347  -2048       C  
ATOM   3506  C   ASP B 663       3.355  19.276  26.354  1.00 88.49           C  
ANISOU 3506  C   ASP B 663    13194  14248   6178  -1895    135  -2206       C  
ATOM   3507  O   ASP B 663       2.883  20.368  26.044  1.00 87.35           O  
ANISOU 3507  O   ASP B 663    12938  13997   6255  -1789    313  -2591       O  
ATOM   3508  CB  ASP B 663       1.815  18.222  28.031  1.00 99.67           C  
ANISOU 3508  CB  ASP B 663    14820  15897   7151  -2243    568  -2247       C  
ATOM   3509  CG  ASP B 663       0.515  17.459  28.146  1.00103.10           C  
ANISOU 3509  CG  ASP B 663    15204  16402   7568  -2303    910  -2277       C  
ATOM   3510  OD1 ASP B 663       0.558  16.248  28.452  1.00103.75           O  
ANISOU 3510  OD1 ASP B 663    15424  16550   7448  -2440    831  -1931       O  
ATOM   3511  OD2 ASP B 663      -0.552  18.069  27.921  1.00105.06           O  
ANISOU 3511  OD2 ASP B 663    15261  16624   8031  -2211   1243  -2646       O  
ATOM   3512  N   GLN B 664       4.660  19.056  26.454  1.00 87.15           N  
ANISOU 3512  N   GLN B 664    13103  14103   5909  -1949   -260  -1909       N  
ATOM   3513  CA  GLN B 664       5.623  20.098  26.137  1.00 86.90           C  
ANISOU 3513  CA  GLN B 664    13013  13991   6015  -1915   -495  -2018       C  
ATOM   3514  C   GLN B 664       5.591  20.371  24.637  1.00 80.44           C  
ANISOU 3514  C   GLN B 664    11955  13032   5578  -1660   -487  -2052       C  
ATOM   3515  O   GLN B 664       5.442  21.512  24.201  1.00 79.48           O  
ANISOU 3515  O   GLN B 664    11752  12774   5674  -1585   -406  -2382       O  
ATOM   3516  CB  GLN B 664       7.022  19.676  26.574  1.00 91.41           C  
ANISOU 3516  CB  GLN B 664    13661  14637   6432  -2025   -935  -1662       C  
ATOM   3517  CG  GLN B 664       7.901  20.832  27.012  1.00 98.40           C  
ANISOU 3517  CG  GLN B 664    14586  15508   7295  -2151  -1137  -1845       C  
ATOM   3518  CD  GLN B 664       9.284  20.380  27.432  1.00103.52           C  
ANISOU 3518  CD  GLN B 664    15252  16241   7839  -2242  -1587  -1490       C  
ATOM   3519  OE1 GLN B 664       9.464  19.264  27.922  1.00105.96           O  
ANISOU 3519  OE1 GLN B 664    15649  16636   7976  -2279  -1722  -1165       O  
ATOM   3520  NE2 GLN B 664      10.272  21.243  27.231  1.00104.32           N  
ANISOU 3520  NE2 GLN B 664    15257  16301   8077  -2275  -1831  -1554       N  
ATOM   3521  N   ILE B 665       5.721  19.301  23.860  1.00 74.51           N  
ANISOU 3521  N   ILE B 665    11104  12298   4910  -1530   -577  -1707       N  
ATOM   3522  CA  ILE B 665       5.620  19.357  22.409  1.00 69.97           C  
ANISOU 3522  CA  ILE B 665    10266  11516   4804  -1225   -544  -1641       C  
ATOM   3523  C   ILE B 665       4.283  19.933  21.958  1.00 70.92           C  
ANISOU 3523  C   ILE B 665    10283  11512   5150  -1082   -181  -1998       C  
ATOM   3524  O   ILE B 665       4.239  20.796  21.083  1.00 69.38           O  
ANISOU 3524  O   ILE B 665     9932  11082   5346   -886   -173  -2131       O  
ATOM   3525  CB  ILE B 665       5.789  17.954  21.800  1.00 66.75           C  
ANISOU 3525  CB  ILE B 665     9782  11099   4480  -1088   -637  -1206       C  
ATOM   3526  CG1 ILE B 665       7.204  17.443  22.063  1.00 68.63           C  
ANISOU 3526  CG1 ILE B 665    10043  11406   4626  -1147  -1042   -853       C  
ATOM   3527  CG2 ILE B 665       5.497  17.969  20.310  1.00 61.01           C  
ANISOU 3527  CG2 ILE B 665     8803  10136   4242   -778   -543  -1154       C  
ATOM   3528  CD1 ILE B 665       7.398  15.982  21.746  1.00 68.40           C  
ANISOU 3528  CD1 ILE B 665     9998  11368   4622  -1040  -1156   -445       C  
ATOM   3529  N   ILE B 666       3.199  19.451  22.557  1.00 73.69           N  
ANISOU 3529  N   ILE B 666    10719  12021   5261  -1191    106  -2147       N  
ATOM   3530  CA  ILE B 666       1.865  19.953  22.250  1.00 74.66           C  
ANISOU 3530  CA  ILE B 666    10700  12064   5602  -1060    457  -2522       C  
ATOM   3531  C   ILE B 666       1.780  21.456  22.473  1.00 78.27           C  
ANISOU 3531  C   ILE B 666    11149  12382   6208  -1035    514  -2960       C  
ATOM   3532  O   ILE B 666       1.335  22.200  21.599  1.00 76.98           O  
ANISOU 3532  O   ILE B 666    10803  11973   6473   -784    569  -3142       O  
ATOM   3533  CB  ILE B 666       0.793  19.254  23.104  1.00 77.02           C  
ANISOU 3533  CB  ILE B 666    11060  12492   5711  -1198    747  -2553       C  
ATOM   3534  CG1 ILE B 666       0.497  17.860  22.546  1.00 73.55           C  
ANISOU 3534  CG1 ILE B 666    10579  12107   5261  -1159    764  -2207       C  
ATOM   3535  CG2 ILE B 666      -0.484  20.086  23.154  1.00 77.81           C  
ANISOU 3535  CG2 ILE B 666    10996  12508   6061  -1094   1082  -2999       C  
ATOM   3536  CD1 ILE B 666      -0.577  17.114  23.318  1.00 75.22           C  
ANISOU 3536  CD1 ILE B 666    10838  12428   5313  -1323   1037  -2215       C  
ATOM   3537  N   GLU B 667       2.214  21.899  23.647  1.00 83.21           N  
ANISOU 3537  N   GLU B 667    11972  13073   6569  -1257    461  -3048       N  
ATOM   3538  CA  GLU B 667       2.235  23.320  23.949  1.00 87.41           C  
ANISOU 3538  CA  GLU B 667    12536  13445   7231  -1253    490  -3441       C  
ATOM   3539  C   GLU B 667       3.161  24.057  22.991  1.00 83.65           C  
ANISOU 3539  C   GLU B 667    12000  12783   7000  -1150    215  -3439       C  
ATOM   3540  O   GLU B 667       2.731  24.965  22.291  1.00 84.97           O  
ANISOU 3540  O   GLU B 667    12045  12670   7570   -935    275  -3675       O  
ATOM   3541  CB  GLU B 667       2.664  23.560  25.397  1.00 96.22           C  
ANISOU 3541  CB  GLU B 667    13895  14696   7969  -1540    448  -3496       C  
ATOM   3542  CG  GLU B 667       2.903  25.023  25.738  1.00103.73           C  
ANISOU 3542  CG  GLU B 667    14919  15472   9023  -1565    425  -3871       C  
ATOM   3543  CD  GLU B 667       1.649  25.873  25.633  1.00109.32           C  
ANISOU 3543  CD  GLU B 667    15500  15992  10045  -1375    753  -4313       C  
ATOM   3544  OE1 GLU B 667       1.786  27.087  25.369  1.00111.28           O  
ANISOU 3544  OE1 GLU B 667    15750  15977  10554  -1275    700  -4591       O  
ATOM   3545  OE2 GLU B 667       0.535  25.338  25.822  1.00111.35           O  
ANISOU 3545  OE2 GLU B 667    15647  16351  10309  -1329   1047  -4374       O  
ATOM   3546  N   MET B 668       4.424  23.645  22.944  1.00 80.39           N  
ANISOU 3546  N   MET B 668    11641  12443   6460  -1258   -116  -3063       N  
ATOM   3547  CA  MET B 668       5.434  24.364  22.166  1.00 76.28           C  
ANISOU 3547  CA  MET B 668    11039  11691   6252  -1176   -394  -2936       C  
ATOM   3548  C   MET B 668       5.195  24.400  20.655  1.00 69.62           C  
ANISOU 3548  C   MET B 668     9970  10571   5910   -861   -392  -2775       C  
ATOM   3549  O   MET B 668       5.311  25.460  20.042  1.00 69.68           O  
ANISOU 3549  O   MET B 668     9944  10297   6234   -769   -453  -2912       O  
ATOM   3550  CB  MET B 668       6.840  23.843  22.471  1.00 76.26           C  
ANISOU 3550  CB  MET B 668    11082  11859   6034  -1357   -742  -2573       C  
ATOM   3551  CG  MET B 668       7.228  23.958  23.939  1.00 80.26           C  
ANISOU 3551  CG  MET B 668    11843  12620   6030  -1705   -831  -2713       C  
ATOM   3552  SD  MET B 668       9.005  23.812  24.184  1.00112.53           S  
ANISOU 3552  SD  MET B 668    15923  16827  10007  -1890  -1324  -2359       S  
ATOM   3553  CE  MET B 668       9.567  25.357  23.470  1.00 95.75           C  
ANISOU 3553  CE  MET B 668    13706  14398   8278  -1865  -1415  -2584       C  
ATOM   3554  N   VAL B 669       4.880  23.258  20.048  1.00 64.39           N  
ANISOU 3554  N   VAL B 669     9185   9972   5306   -720   -339  -2478       N  
ATOM   3555  CA  VAL B 669       4.574  23.245  18.618  1.00 59.88           C  
ANISOU 3555  CA  VAL B 669     8429   9161   5163   -449   -328  -2337       C  
ATOM   3556  C   VAL B 669       3.313  24.064  18.344  1.00 62.14           C  
ANISOU 3556  C   VAL B 669     8661   9239   5710   -279   -115  -2705       C  
ATOM   3557  O   VAL B 669       3.266  24.855  17.401  1.00 60.32           O  
ANISOU 3557  O   VAL B 669     8365   8711   5841   -120   -194  -2735       O  
ATOM   3558  CB  VAL B 669       4.425  21.810  18.052  1.00 55.22           C  
ANISOU 3558  CB  VAL B 669     7736   8678   4567   -346   -300  -1980       C  
ATOM   3559  CG1 VAL B 669       3.967  21.849  16.593  1.00 51.04           C  
ANISOU 3559  CG1 VAL B 669     7043   7910   4441    -95   -268  -1884       C  
ATOM   3560  CG2 VAL B 669       5.737  21.051  18.171  1.00 53.01           C  
ANISOU 3560  CG2 VAL B 669     7467   8539   4135   -448   -549  -1617       C  
ATOM   3561  N   GLY B 670       2.301  23.879  19.187  1.00 67.92           N  
ANISOU 3561  N   GLY B 670     9420  10130   6258   -325    146  -2989       N  
ATOM   3562  CA  GLY B 670       1.066  24.635  19.089  1.00 71.84           C  
ANISOU 3562  CA  GLY B 670     9819  10463   7015   -154    365  -3398       C  
ATOM   3563  C   GLY B 670       1.255  26.115  19.370  1.00 77.45           C  
ANISOU 3563  C   GLY B 670    10624  10932   7870   -159    306  -3759       C  
ATOM   3564  O   GLY B 670       0.622  26.956  18.733  1.00 78.54           O  
ANISOU 3564  O   GLY B 670    10666  10760   8415     71    318  -3965       O  
ATOM   3565  N   ARG B 671       2.132  26.431  20.323  1.00 82.53           N  
ANISOU 3565  N   ARG B 671    11469  11700   8189   -427    214  -3829       N  
ATOM   3566  CA  ARG B 671       2.445  27.815  20.685  1.00 90.68           C  
ANISOU 3566  CA  ARG B 671    12637  12505   9313   -488    141  -4173       C  
ATOM   3567  C   ARG B 671       3.101  28.537  19.516  1.00 92.32           C  
ANISOU 3567  C   ARG B 671    12817  12346   9913   -363   -135  -3970       C  
ATOM   3568  O   ARG B 671       3.053  29.764  19.419  1.00 94.69           O  
ANISOU 3568  O   ARG B 671    13197  12321  10460   -314   -194  -4246       O  
ATOM   3569  CB  ARG B 671       3.372  27.844  21.905  1.00 96.92           C  
ANISOU 3569  CB  ARG B 671    13657  13546   9622   -849     51  -4219       C  
ATOM   3570  CG  ARG B 671       3.709  29.223  22.446  1.00104.82           C  
ANISOU 3570  CG  ARG B 671    14835  14338  10652   -971    -11  -4599       C  
ATOM   3571  CD  ARG B 671       4.538  29.106  23.720  1.00108.94           C  
ANISOU 3571  CD  ARG B 671    15571  15118  10704  -1311   -111  -4523       C  
ATOM   3572  NE  ARG B 671       4.912  30.404  24.270  1.00114.67           N  
ANISOU 3572  NE  ARG B 671    16475  15626  11469  -1427   -189  -4811       N  
ATOM   3573  CZ  ARG B 671       5.552  30.562  25.424  1.00120.78           C  
ANISOU 3573  CZ  ARG B 671    17441  16568  11882  -1703   -281  -4828       C  
ATOM   3574  NH1 ARG B 671       5.885  29.500  26.146  1.00122.28           N  
ANISOU 3574  NH1 ARG B 671    17670  17126  11663  -1881   -323  -4553       N  
ATOM   3575  NH2 ARG B 671       5.858  31.777  25.860  1.00124.08           N  
ANISOU 3575  NH2 ARG B 671    18021  16766  12359  -1797   -351  -5109       N  
ATOM   3576  N   GLY B 672       3.705  27.760  18.622  1.00 90.73           N  
ANISOU 3576  N   GLY B 672    12519  12189   9765   -325   -295  -3495       N  
ATOM   3577  CA  GLY B 672       4.384  28.302  17.462  1.00 87.92           C  
ANISOU 3577  CA  GLY B 672    12142  11541   9721   -262   -529  -3260       C  
ATOM   3578  C   GLY B 672       5.880  28.390  17.682  1.00 87.40           C  
ANISOU 3578  C   GLY B 672    12157  11578   9472   -529   -764  -3052       C  
ATOM   3579  O   GLY B 672       6.636  28.732  16.773  1.00 88.24           O  
ANISOU 3579  O   GLY B 672    12237  11512   9777   -550   -946  -2826       O  
ATOM   3580  N   SER B 673       6.311  28.071  18.897  1.00 86.96           N  
ANISOU 3580  N   SER B 673    12194  11823   9026   -755   -765  -3127       N  
ATOM   3581  CA  SER B 673       7.719  28.177  19.251  1.00 87.06           C  
ANISOU 3581  CA  SER B 673    12257  11962   8858  -1022  -1018  -2964       C  
ATOM   3582  C   SER B 673       8.578  27.100  18.590  1.00 83.84           C  
ANISOU 3582  C   SER B 673    11671  11729   8457  -1004  -1161  -2487       C  
ATOM   3583  O   SER B 673       9.614  27.399  17.997  1.00 87.17           O  
ANISOU 3583  O   SER B 673    12018  12084   9020  -1092  -1353  -2300       O  
ATOM   3584  CB  SER B 673       7.895  28.132  20.773  1.00 89.76           C  
ANISOU 3584  CB  SER B 673    12772  12581   8753  -1283  -1014  -3178       C  
ATOM   3585  OG  SER B 673       7.401  26.919  21.313  1.00 89.53           O  
ANISOU 3585  OG  SER B 673    12728  12856   8434  -1268   -880  -3068       O  
ATOM   3586  N   LEU B 674       8.138  25.850  18.680  1.00 75.58           N  
ANISOU 3586  N   LEU B 674    10550  10897   7271   -898  -1054  -2309       N  
ATOM   3587  CA  LEU B 674       9.005  24.724  18.354  1.00 68.76           C  
ANISOU 3587  CA  LEU B 674     9540  10226   6361   -895  -1201  -1900       C  
ATOM   3588  C   LEU B 674       8.830  24.174  16.943  1.00 65.07           C  
ANISOU 3588  C   LEU B 674     8895   9628   6202   -661  -1138  -1648       C  
ATOM   3589  O   LEU B 674       7.712  23.957  16.475  1.00 62.65           O  
ANISOU 3589  O   LEU B 674     8577   9216   6011   -474   -944  -1708       O  
ATOM   3590  CB  LEU B 674       8.822  23.609  19.384  1.00 67.23           C  
ANISOU 3590  CB  LEU B 674     9417  10334   5791   -966  -1180  -1812       C  
ATOM   3591  CG  LEU B 674       9.726  22.386  19.262  1.00 64.77           C  
ANISOU 3591  CG  LEU B 674     8979  10207   5422   -951  -1373  -1404       C  
ATOM   3592  CD1 LEU B 674      11.186  22.755  19.478  1.00 65.68           C  
ANISOU 3592  CD1 LEU B 674     9019  10404   5531  -1127  -1686  -1299       C  
ATOM   3593  CD2 LEU B 674       9.282  21.321  20.249  1.00 65.81           C  
ANISOU 3593  CD2 LEU B 674     9250  10569   5184  -1018  -1338  -1322       C  
ATOM   3594  N   SER B 675       9.958  23.949  16.277  1.00 63.24           N  
ANISOU 3594  N   SER B 675     8513   9420   6096   -690  -1302  -1384       N  
ATOM   3595  CA  SER B 675       9.974  23.344  14.953  1.00 59.34           C  
ANISOU 3595  CA  SER B 675     7859   8842   5846   -513  -1242  -1142       C  
ATOM   3596  C   SER B 675      11.187  22.419  14.852  1.00 56.35           C  
ANISOU 3596  C   SER B 675     7294   8667   5450   -542  -1394   -853       C  
ATOM   3597  O   SER B 675      12.157  22.589  15.593  1.00 57.09           O  
ANISOU 3597  O   SER B 675     7356   8911   5424   -716  -1593   -840       O  
ATOM   3598  CB  SER B 675      10.004  24.425  13.863  1.00 60.00           C  
ANISOU 3598  CB  SER B 675     7949   8638   6212   -514  -1238  -1195       C  
ATOM   3599  OG  SER B 675      11.320  24.888  13.624  1.00 63.46           O  
ANISOU 3599  OG  SER B 675     8299   9099   6713   -704  -1402  -1100       O  
ATOM   3600  N   PRO B 676      11.125  21.423  13.953  1.00 52.67           N  
ANISOU 3600  N   PRO B 676     6696   8202   5116   -365  -1311   -636       N  
ATOM   3601  CA  PRO B 676      12.201  20.440  13.774  1.00 51.69           C  
ANISOU 3601  CA  PRO B 676     6363   8240   5037   -331  -1431   -386       C  
ATOM   3602  C   PRO B 676      13.564  21.082  13.517  1.00 53.60           C  
ANISOU 3602  C   PRO B 676     6425   8528   5411   -493  -1589   -358       C  
ATOM   3603  O   PRO B 676      13.646  22.138  12.888  1.00 54.09           O  
ANISOU 3603  O   PRO B 676     6512   8436   5602   -601  -1545   -459       O  
ATOM   3604  CB  PRO B 676      11.746  19.655  12.542  1.00 49.81           C  
ANISOU 3604  CB  PRO B 676     6046   7900   4978   -129  -1252   -252       C  
ATOM   3605  CG  PRO B 676      10.266  19.731  12.588  1.00 48.84           C  
ANISOU 3605  CG  PRO B 676     6108   7660   4789    -43  -1079   -383       C  
ATOM   3606  CD  PRO B 676       9.952  21.104  13.119  1.00 51.02           C  
ANISOU 3606  CD  PRO B 676     6525   7840   5019   -177  -1102   -639       C  
ATOM   3607  N   ASP B 677      14.620  20.440  14.005  1.00 53.94           N  
ANISOU 3607  N   ASP B 677     6285   8776   5432   -518  -1787   -215       N  
ATOM   3608  CA  ASP B 677      15.976  20.968  13.891  1.00 54.28           C  
ANISOU 3608  CA  ASP B 677     6099   8920   5606   -690  -1954   -199       C  
ATOM   3609  C   ASP B 677      16.626  20.534  12.584  1.00 53.80           C  
ANISOU 3609  C   ASP B 677     5757   8854   5832   -598  -1839    -74       C  
ATOM   3610  O   ASP B 677      17.078  19.401  12.454  1.00 55.53           O  
ANISOU 3610  O   ASP B 677     5771   9181   6148   -427  -1875     80       O  
ATOM   3611  CB  ASP B 677      16.818  20.506  15.084  1.00 56.03           C  
ANISOU 3611  CB  ASP B 677     6224   9377   5686   -759  -2263   -116       C  
ATOM   3612  CG  ASP B 677      18.256  20.999  15.021  1.00 58.31           C  
ANISOU 3612  CG  ASP B 677     6216   9807   6133   -942  -2462   -106       C  
ATOM   3613  OD1 ASP B 677      18.559  21.924  14.238  1.00 56.82           O  
ANISOU 3613  OD1 ASP B 677     5961   9527   6100  -1091  -2353   -202       O  
ATOM   3614  OD2 ASP B 677      19.090  20.454  15.772  1.00 60.29           O  
ANISOU 3614  OD2 ASP B 677     6297  10259   6351   -952  -2748      6       O  
ATOM   3615  N   LEU B 678      16.688  21.453  11.627  1.00 53.73           N  
ANISOU 3615  N   LEU B 678     5754   8708   5953   -728  -1703   -150       N  
ATOM   3616  CA  LEU B 678      17.169  21.139  10.286  1.00 52.03           C  
ANISOU 3616  CA  LEU B 678     5327   8483   5959   -691  -1532    -64       C  
ATOM   3617  C   LEU B 678      18.687  20.981  10.213  1.00 54.41           C  
ANISOU 3617  C   LEU B 678     5236   9008   6427   -798  -1640    -17       C  
ATOM   3618  O   LEU B 678      19.219  20.550   9.193  1.00 55.55           O  
ANISOU 3618  O   LEU B 678     5146   9202   6759   -760  -1479     32       O  
ATOM   3619  CB  LEU B 678      16.691  22.193   9.284  1.00 50.15           C  
ANISOU 3619  CB  LEU B 678     5276   8014   5763   -835  -1369   -135       C  
ATOM   3620  CG  LEU B 678      15.176  22.313   9.102  1.00 48.90           C  
ANISOU 3620  CG  LEU B 678     5437   7621   5521   -690  -1256   -182       C  
ATOM   3621  CD1 LEU B 678      14.837  23.260   7.962  1.00 49.67           C  
ANISOU 3621  CD1 LEU B 678     5696   7478   5700   -818  -1149   -202       C  
ATOM   3622  CD2 LEU B 678      14.558  20.948   8.857  1.00 47.31           C  
ANISOU 3622  CD2 LEU B 678     5202   7458   5314   -412  -1138    -76       C  
ATOM   3623  N   SER B 679      19.381  21.322  11.295  1.00 55.31           N  
ANISOU 3623  N   SER B 679     5266   9273   6476   -940  -1908    -52       N  
ATOM   3624  CA  SER B 679      20.829  21.155  11.350  1.00 58.66           C  
ANISOU 3624  CA  SER B 679     5266   9938   7084  -1033  -2058    -17       C  
ATOM   3625  C   SER B 679      21.176  19.673  11.468  1.00 60.19           C  
ANISOU 3625  C   SER B 679     5201  10263   7408   -721  -2130    126       C  
ATOM   3626  O   SER B 679      22.319  19.267  11.256  1.00 62.38           O  
ANISOU 3626  O   SER B 679     5053  10722   7927   -698  -2202    155       O  
ATOM   3627  CB  SER B 679      21.420  21.935  12.527  1.00 62.68           C  
ANISOU 3627  CB  SER B 679     5778  10570   7469  -1286  -2370    -92       C  
ATOM   3628  OG  SER B 679      21.090  21.335  13.769  1.00 61.26           O  
ANISOU 3628  OG  SER B 679     5735  10460   7083  -1161  -2609    -34       O  
ATOM   3629  N   LYS B 680      20.167  18.873  11.801  1.00 59.86           N  
ANISOU 3629  N   LYS B 680     5409  10112   7221   -484  -2108    205       N  
ATOM   3630  CA  LYS B 680      20.326  17.438  11.989  1.00 63.15           C  
ANISOU 3630  CA  LYS B 680     5676  10581   7736   -183  -2198    357       C  
ATOM   3631  C   LYS B 680      20.354  16.660  10.672  1.00 63.85           C  
ANISOU 3631  C   LYS B 680     5587  10600   8071     19  -1909    377       C  
ATOM   3632  O   LYS B 680      20.621  15.459  10.671  1.00 65.56           O  
ANISOU 3632  O   LYS B 680     5637  10832   8442    283  -1966    480       O  
ATOM   3633  CB  LYS B 680      19.200  16.907  12.879  1.00 63.72           C  
ANISOU 3633  CB  LYS B 680     6126  10561   7524    -69  -2273    434       C  
ATOM   3634  CG  LYS B 680      19.643  16.456  14.260  1.00 69.46           C  
ANISOU 3634  CG  LYS B 680     6854  11430   8109    -68  -2665    552       C  
ATOM   3635  CD  LYS B 680      18.690  16.951  15.337  1.00 71.28           C  
ANISOU 3635  CD  LYS B 680     7511  11636   7937   -229  -2726    495       C  
ATOM   3636  CE  LYS B 680      18.813  16.117  16.606  1.00 76.58           C  
ANISOU 3636  CE  LYS B 680     8292  12409   8394   -192  -3067    671       C  
ATOM   3637  NZ  LYS B 680      18.057  16.718  17.746  1.00 78.05           N  
ANISOU 3637  NZ  LYS B 680     8873  12631   8150   -424  -3122    573       N  
ATOM   3638  N   VAL B 681      20.079  17.336   9.558  1.00 62.37           N  
ANISOU 3638  N   VAL B 681     5462  10322   7915   -113  -1612    278       N  
ATOM   3639  CA  VAL B 681      20.089  16.672   8.254  1.00 63.42           C  
ANISOU 3639  CA  VAL B 681     5464  10402   8229     24  -1313    272       C  
ATOM   3640  C   VAL B 681      21.482  16.146   7.921  1.00 69.83           C  
ANISOU 3640  C   VAL B 681     5767  11408   9359     87  -1324    248       C  
ATOM   3641  O   VAL B 681      22.485  16.676   8.399  1.00 72.51           O  
ANISOU 3641  O   VAL B 681     5833  11928   9789    -74  -1511    211       O  
ATOM   3642  CB  VAL B 681      19.606  17.597   7.111  1.00 60.86           C  
ANISOU 3642  CB  VAL B 681     5328   9955   7841   -190  -1028    188       C  
ATOM   3643  CG1 VAL B 681      18.195  18.095   7.380  1.00 56.03           C  
ANISOU 3643  CG1 VAL B 681     5170   9135   6983   -204  -1025    189       C  
ATOM   3644  CG2 VAL B 681      20.567  18.764   6.914  1.00 65.58           C  
ANISOU 3644  CG2 VAL B 681     5751  10668   8498   -529  -1041    102       C  
ATOM   3645  N   ARG B 682      21.541  15.097   7.107  1.00 72.56           N  
ANISOU 3645  N   ARG B 682     5966  11716   9887    320  -1122    245       N  
ATOM   3646  CA  ARG B 682      22.823  14.532   6.704  1.00 79.24           C  
ANISOU 3646  CA  ARG B 682     6290  12735  11082    421  -1084    173       C  
ATOM   3647  C   ARG B 682      23.553  15.477   5.758  1.00 80.33           C  
ANISOU 3647  C   ARG B 682     6207  13019  11297     96   -830     21       C  
ATOM   3648  O   ARG B 682      22.937  16.331   5.123  1.00 78.40           O  
ANISOU 3648  O   ARG B 682     6268  12677  10842   -155   -632     -6       O  
ATOM   3649  CB  ARG B 682      22.633  13.164   6.050  1.00 82.97           C  
ANISOU 3649  CB  ARG B 682     6699  13095  11731    758   -904    171       C  
ATOM   3650  CG  ARG B 682      21.962  12.145   6.949  1.00 86.37           C  
ANISOU 3650  CG  ARG B 682     7356  13364  12097   1055  -1154    340       C  
ATOM   3651  CD  ARG B 682      21.827  10.802   6.253  1.00 91.65           C  
ANISOU 3651  CD  ARG B 682     7968  13886  12967   1373   -975    322       C  
ATOM   3652  NE  ARG B 682      20.651  10.076   6.722  1.00 93.21           N  
ANISOU 3652  NE  ARG B 682     8590  13861  12966   1528  -1062    475       N  
ATOM   3653  CZ  ARG B 682      20.343   8.835   6.363  1.00 95.85           C  
ANISOU 3653  CZ  ARG B 682     8979  14012  13426   1800   -977    499       C  
ATOM   3654  NH1 ARG B 682      21.133   8.167   5.529  1.00 98.22           N  
ANISOU 3654  NH1 ARG B 682     8933  14317  14068   1981   -797    357       N  
ATOM   3655  NH2 ARG B 682      19.246   8.262   6.841  1.00 94.36           N  
ANISOU 3655  NH2 ARG B 682     9192  13635  13028   1877  -1058    645       N  
ATOM   3656  N   SER B 683      24.870  15.321   5.677  1.00 83.97           N  
ANISOU 3656  N   SER B 683     6130  13709  12065     90   -851    -75       N  
ATOM   3657  CA  SER B 683      25.701  16.190   4.853  1.00 85.29           C  
ANISOU 3657  CA  SER B 683     6033  14061  12314   -266   -605   -228       C  
ATOM   3658  C   SER B 683      25.356  16.086   3.372  1.00 85.40           C  
ANISOU 3658  C   SER B 683     6165  14008  12275   -353   -130   -326       C  
ATOM   3659  O   SER B 683      25.334  17.090   2.664  1.00 86.52           O  
ANISOU 3659  O   SER B 683     6454  14165  12255   -737     77   -371       O  
ATOM   3660  CB  SER B 683      27.180  15.871   5.066  1.00 89.05           C  
ANISOU 3660  CB  SER B 683     5833  14823  13179   -214   -708   -336       C  
ATOM   3661  OG  SER B 683      27.456  14.513   4.778  1.00 90.24           O  
ANISOU 3661  OG  SER B 683     5689  14963  13634    199   -631   -387       O  
ATOM   3662  N   ASN B 684      25.081  14.872   2.908  1.00 85.16           N  
ANISOU 3662  N   ASN B 684     6103  13889  12365    -16     26   -353       N  
ATOM   3663  CA  ASN B 684      24.809  14.644   1.492  1.00 85.01           C  
ANISOU 3663  CA  ASN B 684     6185  13827  12289    -95    477   -469       C  
ATOM   3664  C   ASN B 684      23.384  14.984   1.069  1.00 80.68           C  
ANISOU 3664  C   ASN B 684     6260  13021  11372   -188    558   -355       C  
ATOM   3665  O   ASN B 684      23.071  14.981  -0.123  1.00 82.42           O  
ANISOU 3665  O   ASN B 684     6643  13200  11472   -328    894   -423       O  
ATOM   3666  CB  ASN B 684      25.150  13.205   1.102  1.00 87.59           C  
ANISOU 3666  CB  ASN B 684     6212  14153  12916    291    632   -589       C  
ATOM   3667  CG  ASN B 684      24.538  12.189   2.037  1.00 88.04           C  
ANISOU 3667  CG  ASN B 684     6421  14004  13025    718    314   -434       C  
ATOM   3668  OD1 ASN B 684      24.149  12.514   3.160  1.00 87.96           O  
ANISOU 3668  OD1 ASN B 684     6608  13933  12879    734    -53   -255       O  
ATOM   3669  ND2 ASN B 684      24.459  10.946   1.584  1.00 88.92           N  
ANISOU 3669  ND2 ASN B 684     6460  14002  13323   1044    463   -511       N  
ATOM   3670  N   CYS B 685      22.525  15.271   2.043  1.00 75.16           N  
ANISOU 3670  N   CYS B 685     5897  12163  10496   -118    247   -193       N  
ATOM   3671  CA  CYS B 685      21.154  15.676   1.755  1.00 68.50           C  
ANISOU 3671  CA  CYS B 685     5595  11084   9347   -191    282    -98       C  
ATOM   3672  C   CYS B 685      21.162  16.960   0.933  1.00 67.26           C  
ANISOU 3672  C   CYS B 685     5615  10923   9018   -620    440   -122       C  
ATOM   3673  O   CYS B 685      21.744  17.959   1.350  1.00 70.20           O  
ANISOU 3673  O   CYS B 685     5901  11382   9388   -877    314   -128       O  
ATOM   3674  CB  CYS B 685      20.366  15.875   3.052  1.00 65.70           C  
ANISOU 3674  CB  CYS B 685     5501  10605   8857    -74    -63     32       C  
ATOM   3675  SG  CYS B 685      18.797  16.756   2.859  1.00 73.96           S  
ANISOU 3675  SG  CYS B 685     7128  11390   9582   -212    -64    104       S  
ATOM   3676  N   PRO B 686      20.532  16.927  -0.251  1.00 63.94           N  
ANISOU 3676  N   PRO B 686     5461  10391   8442   -719    699   -127       N  
ATOM   3677  CA  PRO B 686      20.528  18.061  -1.182  1.00 63.41           C  
ANISOU 3677  CA  PRO B 686     5610  10294   8188  -1146    849   -119       C  
ATOM   3678  C   PRO B 686      19.889  19.298  -0.568  1.00 62.70           C  
ANISOU 3678  C   PRO B 686     5859  10018   7945  -1305    577     -7       C  
ATOM   3679  O   PRO B 686      18.899  19.182   0.152  1.00 60.85           O  
ANISOU 3679  O   PRO B 686     5854   9613   7652  -1075    369     64       O  
ATOM   3680  CB  PRO B 686      19.671  17.555  -2.347  1.00 62.41           C  
ANISOU 3680  CB  PRO B 686     5781  10034   7895  -1124   1077   -106       C  
ATOM   3681  CG  PRO B 686      19.744  16.071  -2.261  1.00 63.03           C  
ANISOU 3681  CG  PRO B 686     5633  10166   8150   -743   1171   -188       C  
ATOM   3682  CD  PRO B 686      19.809  15.766  -0.795  1.00 62.63           C  
ANISOU 3682  CD  PRO B 686     5422  10116   8260   -452    849   -134       C  
ATOM   3683  N   LYS B 687      20.455  20.467  -0.854  1.00 64.96           N  
ANISOU 3683  N   LYS B 687     6176  10334   8174  -1708    592     -8       N  
ATOM   3684  CA  LYS B 687      19.946  21.718  -0.306  1.00 64.52           C  
ANISOU 3684  CA  LYS B 687     6442  10068   8006  -1876    337     70       C  
ATOM   3685  C   LYS B 687      18.527  22.017  -0.774  1.00 63.41           C  
ANISOU 3685  C   LYS B 687     6797   9612   7684  -1822    282    175       C  
ATOM   3686  O   LYS B 687      17.754  22.636  -0.049  1.00 63.22           O  
ANISOU 3686  O   LYS B 687     7016   9381   7624  -1745     40    209       O  
ATOM   3687  CB  LYS B 687      20.871  22.885  -0.657  1.00 69.08           C  
ANISOU 3687  CB  LYS B 687     6979  10709   8560  -2361    381     54       C  
ATOM   3688  CG  LYS B 687      22.242  22.822  -0.001  1.00 73.85           C  
ANISOU 3688  CG  LYS B 687     7073  11620   9366  -2446    357    -58       C  
ATOM   3689  CD  LYS B 687      23.020  24.106  -0.259  1.00 78.71           C  
ANISOU 3689  CD  LYS B 687     7704  12265   9937  -2973    371    -66       C  
ATOM   3690  CE  LYS B 687      24.471  23.987   0.177  1.00 82.49           C  
ANISOU 3690  CE  LYS B 687     7605  13103  10636  -3104    394   -196       C  
ATOM   3691  NZ  LYS B 687      25.235  25.234  -0.120  1.00 86.21           N  
ANISOU 3691  NZ  LYS B 687     8089  13610  11055  -3672    430   -208       N  
ATOM   3692  N   ARG B 688      18.187  21.581  -1.984  1.00 64.11           N  
ANISOU 3692  N   ARG B 688     7021   9672   7666  -1865    504    209       N  
ATOM   3693  CA  ARG B 688      16.834  21.761  -2.499  1.00 63.64           C  
ANISOU 3693  CA  ARG B 688     7396   9331   7452  -1800    427    315       C  
ATOM   3694  C   ARG B 688      15.843  20.990  -1.646  1.00 60.20           C  
ANISOU 3694  C   ARG B 688     6980   8817   7076  -1368    282    307       C  
ATOM   3695  O   ARG B 688      14.731  21.451  -1.393  1.00 59.10           O  
ANISOU 3695  O   ARG B 688     7126   8442   6887  -1271     96    359       O  
ATOM   3696  CB  ARG B 688      16.729  21.289  -3.947  1.00 68.22           C  
ANISOU 3696  CB  ARG B 688     8100   9939   7883  -1940    689    343       C  
ATOM   3697  CG  ARG B 688      17.513  22.123  -4.934  1.00 76.68           C  
ANISOU 3697  CG  ARG B 688     9256  11063   8817  -2438    850    375       C  
ATOM   3698  CD  ARG B 688      17.161  21.734  -6.357  1.00 81.88           C  
ANISOU 3698  CD  ARG B 688    10151  11710   9251  -2599   1071    419       C  
ATOM   3699  NE  ARG B 688      15.896  22.316  -6.797  1.00 84.17           N  
ANISOU 3699  NE  ARG B 688    10934  11673   9375  -2623    838    596       N  
ATOM   3700  CZ  ARG B 688      15.324  22.054  -7.969  1.00 86.20           C  
ANISOU 3700  CZ  ARG B 688    11482  11864   9406  -2746    926    673       C  
ATOM   3701  NH1 ARG B 688      15.900  21.211  -8.814  1.00 88.81           N  
ANISOU 3701  NH1 ARG B 688    11679  12437   9630  -2865   1283    565       N  
ATOM   3702  NH2 ARG B 688      14.175  22.629  -8.296  1.00 85.31           N  
ANISOU 3702  NH2 ARG B 688    11787  11445   9182  -2746    650    845       N  
ATOM   3703  N   MET B 689      16.255  19.804  -1.214  1.00 58.73           N  
ANISOU 3703  N   MET B 689     6482   8824   7009  -1114    371    236       N  
ATOM   3704  CA  MET B 689      15.435  18.989  -0.336  1.00 53.86           C  
ANISOU 3704  CA  MET B 689     5876   8157   6433   -746    246    239       C  
ATOM   3705  C   MET B 689      15.268  19.673   1.012  1.00 49.85           C  
ANISOU 3705  C   MET B 689     5395   7600   5948   -700    -19    228       C  
ATOM   3706  O   MET B 689      14.189  19.650   1.603  1.00 48.78           O  
ANISOU 3706  O   MET B 689     5445   7326   5763   -523   -147    238       O  
ATOM   3707  CB  MET B 689      16.071  17.614  -0.141  1.00 54.96           C  
ANISOU 3707  CB  MET B 689     5685   8484   6712   -512    365    183       C  
ATOM   3708  CG  MET B 689      15.277  16.717   0.784  1.00 53.97           C  
ANISOU 3708  CG  MET B 689     5599   8299   6606   -175    231    213       C  
ATOM   3709  SD  MET B 689      13.605  16.462   0.163  1.00 63.81           S  
ANISOU 3709  SD  MET B 689     7225   9319   7700    -82    264    267       S  
ATOM   3710  CE  MET B 689      13.928  15.382  -1.227  1.00 44.10           C  
ANISOU 3710  CE  MET B 689     4660   6880   5215    -77    569    224       C  
ATOM   3711  N   LYS B 690      16.348  20.281   1.490  1.00 49.91           N  
ANISOU 3711  N   LYS B 690     5205   7736   6022   -881    -86    187       N  
ATOM   3712  CA  LYS B 690      16.344  20.946   2.785  1.00 50.65           C  
ANISOU 3712  CA  LYS B 690     5320   7809   6116   -882   -333    150       C  
ATOM   3713  C   LYS B 690      15.419  22.156   2.758  1.00 51.90           C  
ANISOU 3713  C   LYS B 690     5848   7688   6182   -999   -450    150       C  
ATOM   3714  O   LYS B 690      14.677  22.401   3.709  1.00 51.24           O  
ANISOU 3714  O   LYS B 690     5900   7505   6066   -865   -605     98       O  
ATOM   3715  CB  LYS B 690      17.763  21.362   3.171  1.00 52.57           C  
ANISOU 3715  CB  LYS B 690     5261   8259   6455  -1097   -385    101       C  
ATOM   3716  CG  LYS B 690      17.915  21.810   4.610  1.00 54.76           C  
ANISOU 3716  CG  LYS B 690     5516   8571   6720  -1089   -652     52       C  
ATOM   3717  CD  LYS B 690      19.383  21.843   5.013  1.00 61.10           C  
ANISOU 3717  CD  LYS B 690     5927   9639   7649  -1242   -723     12       C  
ATOM   3718  CE  LYS B 690      19.562  22.348   6.438  1.00 62.74           C  
ANISOU 3718  CE  LYS B 690     6145   9890   7805  -1284  -1017    -39       C  
ATOM   3719  NZ  LYS B 690      20.988  22.313   6.877  1.00 65.93           N  
ANISOU 3719  NZ  LYS B 690     6133  10571   8346  -1422  -1137    -69       N  
ATOM   3720  N   ARG B 691      15.465  22.903   1.659  1.00 54.09           N  
ANISOU 3720  N   ARG B 691     6295   7835   6421  -1254   -374    201       N  
ATOM   3721  CA  ARG B 691      14.585  24.050   1.473  1.00 56.27           C  
ANISOU 3721  CA  ARG B 691     6939   7791   6649  -1349   -514    222       C  
ATOM   3722  C   ARG B 691      13.129  23.613   1.396  1.00 51.72           C  
ANISOU 3722  C   ARG B 691     6553   7048   6049  -1057   -546    237       C  
ATOM   3723  O   ARG B 691      12.257  24.210   2.028  1.00 50.70           O  
ANISOU 3723  O   ARG B 691     6595   6723   5945   -946   -706    171       O  
ATOM   3724  CB  ARG B 691      14.957  24.807   0.201  1.00 63.38           C  
ANISOU 3724  CB  ARG B 691     8010   8581   7488  -1703   -440    321       C  
ATOM   3725  CG  ARG B 691      16.333  25.439   0.229  1.00 72.69           C  
ANISOU 3725  CG  ARG B 691     9024   9905   8690  -2065   -403    297       C  
ATOM   3726  CD  ARG B 691      16.698  25.954  -1.149  1.00 81.48           C  
ANISOU 3726  CD  ARG B 691    10308  10957   9696  -2446   -265    409       C  
ATOM   3727  NE  ARG B 691      18.019  26.569  -1.184  1.00 92.09           N  
ANISOU 3727  NE  ARG B 691    11477  12457  11057  -2845   -198    380       N  
ATOM   3728  CZ  ARG B 691      18.556  27.107  -2.274  1.00101.65           C  
ANISOU 3728  CZ  ARG B 691    12811  13659  12153  -3274    -54    465       C  
ATOM   3729  NH1 ARG B 691      17.881  27.102  -3.417  1.00103.06           N  
ANISOU 3729  NH1 ARG B 691    13315  13673  12172  -3349     12    598       N  
ATOM   3730  NH2 ARG B 691      19.764  27.653  -2.225  1.00107.31           N  
ANISOU 3730  NH2 ARG B 691    13332  14545  12897  -3657     18    420       N  
ATOM   3731  N   LEU B 692      12.876  22.569   0.613  1.00 50.48           N  
ANISOU 3731  N   LEU B 692     6350   6975   5856   -943   -383    300       N  
ATOM   3732  CA  LEU B 692      11.530  22.030   0.446  1.00 50.25           C  
ANISOU 3732  CA  LEU B 692     6466   6821   5806   -693   -401    317       C  
ATOM   3733  C   LEU B 692      10.945  21.591   1.783  1.00 50.92           C  
ANISOU 3733  C   LEU B 692     6466   6953   5927   -424   -480    218       C  
ATOM   3734  O   LEU B 692       9.762  21.796   2.057  1.00 50.41           O  
ANISOU 3734  O   LEU B 692     6547   6731   5877   -275   -569    173       O  
ATOM   3735  CB  LEU B 692      11.548  20.849  -0.524  1.00 48.14           C  
ANISOU 3735  CB  LEU B 692     6133   6674   5485   -641   -196    376       C  
ATOM   3736  CG  LEU B 692      10.255  20.037  -0.605  1.00 44.93           C  
ANISOU 3736  CG  LEU B 692     5816   6194   5061   -386   -199    383       C  
ATOM   3737  CD1 LEU B 692       9.120  20.881  -1.164  1.00 43.23           C  
ANISOU 3737  CD1 LEU B 692     5888   5709   4828   -416   -359    432       C  
ATOM   3738  CD2 LEU B 692      10.465  18.792  -1.441  1.00 45.17           C  
ANISOU 3738  CD2 LEU B 692     5764   6356   5043   -349     15    409       C  
ATOM   3739  N   MET B 693      11.792  20.986   2.607  1.00 51.40           N  
ANISOU 3739  N   MET B 693     6287   7241   6003   -378   -452    183       N  
ATOM   3740  CA  MET B 693      11.409  20.545   3.936  1.00 50.07           C  
ANISOU 3740  CA  MET B 693     6061   7148   5815   -186   -532    111       C  
ATOM   3741  C   MET B 693      10.946  21.732   4.771  1.00 52.59           C  
ANISOU 3741  C   MET B 693     6533   7324   6124   -238   -690     -9       C  
ATOM   3742  O   MET B 693       9.897  21.685   5.409  1.00 52.68           O  
ANISOU 3742  O   MET B 693     6638   7269   6108    -83   -721    -97       O  
ATOM   3743  CB  MET B 693      12.605  19.878   4.606  1.00 50.85           C  
ANISOU 3743  CB  MET B 693     5891   7496   5936   -180   -541    125       C  
ATOM   3744  CG  MET B 693      12.261  18.889   5.695  1.00 49.58           C  
ANISOU 3744  CG  MET B 693     5678   7441   5721     32   -591    125       C  
ATOM   3745  SD  MET B 693      13.775  18.234   6.414  1.00 73.15           S  
ANISOU 3745  SD  MET B 693     8345  10681   8768     35   -687    171       S  
ATOM   3746  CE  MET B 693      14.689  17.803   4.937  1.00 53.52           C  
ANISOU 3746  CE  MET B 693     5643   8252   6440    -12   -484    215       C  
ATOM   3747  N   ALA B 694      11.735  22.802   4.750  1.00 54.39           N  
ANISOU 3747  N   ALA B 694     6784   7502   6381   -471   -773    -34       N  
ATOM   3748  CA  ALA B 694      11.417  24.010   5.503  1.00 52.83           C  
ANISOU 3748  CA  ALA B 694     6749   7134   6192   -544   -924   -174       C  
ATOM   3749  C   ALA B 694      10.126  24.653   5.007  1.00 53.32           C  
ANISOU 3749  C   ALA B 694     7054   6887   6320   -449   -966   -215       C  
ATOM   3750  O   ALA B 694       9.358  25.203   5.794  1.00 54.54           O  
ANISOU 3750  O   ALA B 694     7310   6912   6501   -351  -1043   -382       O  
ATOM   3751  CB  ALA B 694      12.565  24.998   5.431  1.00 52.08           C  
ANISOU 3751  CB  ALA B 694     6642   7022   6123   -851  -1004   -177       C  
ATOM   3752  N   GLU B 695       9.892  24.590   3.701  1.00 53.19           N  
ANISOU 3752  N   GLU B 695     7124   6754   6332   -482   -923    -73       N  
ATOM   3753  CA  GLU B 695       8.655  25.115   3.133  1.00 55.81           C  
ANISOU 3753  CA  GLU B 695     7668   6792   6747   -374  -1011    -78       C  
ATOM   3754  C   GLU B 695       7.445  24.298   3.583  1.00 53.50           C  
ANISOU 3754  C   GLU B 695     7308   6552   6466    -79   -958   -164       C  
ATOM   3755  O   GLU B 695       6.388  24.855   3.874  1.00 54.90           O  
ANISOU 3755  O   GLU B 695     7575   6535   6751     65  -1048   -294       O  
ATOM   3756  CB  GLU B 695       8.728  25.156   1.605  1.00 58.18           C  
ANISOU 3756  CB  GLU B 695     8098   6984   7025   -517   -999    119       C  
ATOM   3757  CG  GLU B 695       9.689  26.191   1.052  1.00 65.72           C  
ANISOU 3757  CG  GLU B 695     9189   7818   7964   -857  -1065    205       C  
ATOM   3758  CD  GLU B 695       9.283  27.614   1.393  1.00 74.98           C  
ANISOU 3758  CD  GLU B 695    10595   8634   9259   -900  -1294    124       C  
ATOM   3759  OE1 GLU B 695      10.182  28.471   1.523  1.00 78.38           O  
ANISOU 3759  OE1 GLU B 695    11095   9001   9687  -1172  -1351    122       O  
ATOM   3760  OE2 GLU B 695       8.068  27.879   1.525  1.00 77.96           O  
ANISOU 3760  OE2 GLU B 695    11078   8787   9758   -662  -1418     48       O  
ATOM   3761  N   CYS B 696       7.606  22.979   3.644  1.00 48.14           N  
ANISOU 3761  N   CYS B 696     6465   6129   5697      6   -808   -102       N  
ATOM   3762  CA  CYS B 696       6.522  22.096   4.065  1.00 46.78           C  
ANISOU 3762  CA  CYS B 696     6233   6029   5511    235   -737   -164       C  
ATOM   3763  C   CYS B 696       6.189  22.246   5.550  1.00 46.12           C  
ANISOU 3763  C   CYS B 696     6109   6020   5395    315   -745   -361       C  
ATOM   3764  O   CYS B 696       5.077  21.946   5.977  1.00 41.74           O  
ANISOU 3764  O   CYS B 696     5540   5467   4853    470   -698   -474       O  
ATOM   3765  CB  CYS B 696       6.865  20.633   3.757  1.00 45.74           C  
ANISOU 3765  CB  CYS B 696     5972   6115   5292    281   -586    -40       C  
ATOM   3766  SG  CYS B 696       6.773  20.179   2.010  1.00 51.39           S  
ANISOU 3766  SG  CYS B 696     6760   6760   6005    226   -518    130       S  
ATOM   3767  N   LEU B 697       7.154  22.721   6.329  1.00 49.59           N  
ANISOU 3767  N   LEU B 697     6527   6537   5779    181   -798   -415       N  
ATOM   3768  CA  LEU B 697       7.004  22.782   7.777  1.00 49.35           C  
ANISOU 3768  CA  LEU B 697     6481   6621   5650    204   -801   -596       C  
ATOM   3769  C   LEU B 697       6.617  24.164   8.291  1.00 53.80           C  
ANISOU 3769  C   LEU B 697     7176   6972   6293    170   -895   -826       C  
ATOM   3770  O   LEU B 697       6.745  24.435   9.483  1.00 58.84           O  
ANISOU 3770  O   LEU B 697     7831   7702   6824    118   -905  -1001       O  
ATOM   3771  CB  LEU B 697       8.290  22.311   8.460  1.00 46.89           C  
ANISOU 3771  CB  LEU B 697     6057   6554   5205     81   -832   -521       C  
ATOM   3772  CG  LEU B 697       8.647  20.838   8.253  1.00 43.42           C  
ANISOU 3772  CG  LEU B 697     5476   6317   4706    162   -750   -335       C  
ATOM   3773  CD1 LEU B 697      10.004  20.511   8.853  1.00 37.95           C  
ANISOU 3773  CD1 LEU B 697     4642   5830   3946     59   -840   -258       C  
ATOM   3774  CD2 LEU B 697       7.570  19.949   8.845  1.00 40.70           C  
ANISOU 3774  CD2 LEU B 697     5157   6044   4261    312   -657   -375       C  
ATOM   3775  N   LYS B 698       6.142  25.029   7.399  1.00 52.74           N  
ANISOU 3775  N   LYS B 698     7156   6541   6343    194   -977   -830       N  
ATOM   3776  CA  LYS B 698       5.730  26.374   7.788  1.00 55.23           C  
ANISOU 3776  CA  LYS B 698     7611   6582   6793    196  -1087  -1056       C  
ATOM   3777  C   LYS B 698       4.652  26.341   8.864  1.00 58.01           C  
ANISOU 3777  C   LYS B 698     7924   6976   7142    366   -991  -1349       C  
ATOM   3778  O   LYS B 698       3.672  25.604   8.751  1.00 57.89           O  
ANISOU 3778  O   LYS B 698     7811   7037   7149    540   -884  -1364       O  
ATOM   3779  CB  LYS B 698       5.228  27.163   6.578  1.00 55.28           C  
ANISOU 3779  CB  LYS B 698     7757   6228   7019    237  -1226   -974       C  
ATOM   3780  CG  LYS B 698       6.321  27.588   5.622  1.00 55.38           C  
ANISOU 3780  CG  LYS B 698     7878   6149   7017    -14  -1322   -741       C  
ATOM   3781  CD  LYS B 698       7.253  28.592   6.263  1.00 59.17           C  
ANISOU 3781  CD  LYS B 698     8450   6551   7482   -237  -1412   -845       C  
ATOM   3782  CE  LYS B 698       8.412  28.926   5.338  1.00 62.34           C  
ANISOU 3782  CE  LYS B 698     8922   6918   7846   -539  -1467   -614       C  
ATOM   3783  NZ  LYS B 698       9.248  30.039   5.878  1.00 66.35           N  
ANISOU 3783  NZ  LYS B 698     9543   7302   8366   -792  -1582   -718       N  
ATOM   3784  N   LYS B 699       4.846  27.145   9.905  1.00 60.44           N  
ANISOU 3784  N   LYS B 699     8307   7246   7413    287  -1016  -1600       N  
ATOM   3785  CA  LYS B 699       3.901  27.210  11.012  1.00 63.88           C  
ANISOU 3785  CA  LYS B 699     8715   7742   7814    402   -887  -1933       C  
ATOM   3786  C   LYS B 699       2.509  27.607  10.529  1.00 64.95           C  
ANISOU 3786  C   LYS B 699     8814   7625   8238    658   -875  -2094       C  
ATOM   3787  O   LYS B 699       1.511  27.018  10.941  1.00 64.80           O  
ANISOU 3787  O   LYS B 699     8663   7753   8206    800   -706  -2243       O  
ATOM   3788  CB  LYS B 699       4.390  28.189  12.085  1.00 69.11           C  
ANISOU 3788  CB  LYS B 699     9506   8353   8398    247   -931  -2205       C  
ATOM   3789  CG  LYS B 699       4.604  27.556  13.455  1.00 72.78           C  
ANISOU 3789  CG  LYS B 699     9946   9180   8526    128   -802  -2332       C  
ATOM   3790  CD  LYS B 699       6.054  27.142  13.666  1.00 73.80           C  
ANISOU 3790  CD  LYS B 699    10075   9534   8432   -109   -917  -2089       C  
ATOM   3791  CE  LYS B 699       6.154  25.813  14.407  1.00 72.28           C  
ANISOU 3791  CE  LYS B 699     9800   9725   7938   -142   -822  -1975       C  
ATOM   3792  NZ  LYS B 699       5.435  25.806  15.711  1.00 71.52           N  
ANISOU 3792  NZ  LYS B 699     9779   9776   7618   -176   -674  -2284       N  
ATOM   3793  N   LYS B 700       2.447  28.601   9.650  1.00 66.77           N  
ANISOU 3793  N   LYS B 700     9159   7475   8737    704  -1069  -2054       N  
ATOM   3794  CA  LYS B 700       1.171  29.033   9.093  1.00 68.21           C  
ANISOU 3794  CA  LYS B 700     9297   7376   9242    969  -1134  -2174       C  
ATOM   3795  C   LYS B 700       0.823  28.176   7.880  1.00 63.58           C  
ANISOU 3795  C   LYS B 700     8631   6837   8690   1045  -1171  -1858       C  
ATOM   3796  O   LYS B 700       1.652  27.969   6.997  1.00 61.73           O  
ANISOU 3796  O   LYS B 700     8491   6598   8366    889  -1264  -1537       O  
ATOM   3797  CB  LYS B 700       1.205  30.526   8.758  1.00 73.83           C  
ANISOU 3797  CB  LYS B 700    10207   7608  10238    993  -1374  -2274       C  
ATOM   3798  CG  LYS B 700       1.419  31.394   9.995  1.00 80.19           C  
ANISOU 3798  CG  LYS B 700    11100   8341  11028    930  -1323  -2651       C  
ATOM   3799  CD  LYS B 700       1.429  32.881   9.683  1.00 87.01           C  
ANISOU 3799  CD  LYS B 700    12186   8674  12201    959  -1571  -2765       C  
ATOM   3800  CE  LYS B 700       1.583  33.699  10.960  1.00 92.58           C  
ANISOU 3800  CE  LYS B 700    12982   9310  12884    896  -1494  -3193       C  
ATOM   3801  NZ  LYS B 700       1.606  35.165  10.697  1.00 97.93           N  
ANISOU 3801  NZ  LYS B 700    13906   9420  13883    922  -1744  -3323       N  
ATOM   3802  N   ARG B 701      -0.404  27.667   7.852  1.00 62.98           N  
ANISOU 3802  N   ARG B 701     8372   6824   8732   1261  -1082  -1972       N  
ATOM   3803  CA  ARG B 701      -0.771  26.631   6.890  1.00 62.42           C  
ANISOU 3803  CA  ARG B 701     8208   6878   8631   1303  -1075  -1705       C  
ATOM   3804  C   ARG B 701      -0.803  27.094   5.436  1.00 62.69           C  
ANISOU 3804  C   ARG B 701     8376   6602   8841   1321  -1347  -1445       C  
ATOM   3805  O   ARG B 701      -0.383  26.362   4.539  1.00 59.68           O  
ANISOU 3805  O   ARG B 701     8036   6326   8313   1208  -1358  -1142       O  
ATOM   3806  CB  ARG B 701      -2.089  25.953   7.283  1.00 63.88           C  
ANISOU 3806  CB  ARG B 701     8148   7234   8890   1490   -906  -1907       C  
ATOM   3807  CG  ARG B 701      -3.315  26.844   7.289  1.00 69.24           C  
ANISOU 3807  CG  ARG B 701     8709   7644   9955   1751  -1003  -2202       C  
ATOM   3808  CD  ARG B 701      -4.471  26.102   7.932  1.00 73.07           C  
ANISOU 3808  CD  ARG B 701     8907   8396  10462   1870   -754  -2453       C  
ATOM   3809  NE  ARG B 701      -5.753  26.414   7.313  1.00 79.39           N  
ANISOU 3809  NE  ARG B 701     9507   9004  11654   2133   -892  -2570       N  
ATOM   3810  CZ  ARG B 701      -6.813  25.614   7.362  1.00 82.95           C  
ANISOU 3810  CZ  ARG B 701     9680   9676  12163   2220   -743  -2674       C  
ATOM   3811  NH1 ARG B 701      -6.737  24.453   7.999  1.00 80.99           N  
ANISOU 3811  NH1 ARG B 701     9366   9822  11584   2048   -444  -2657       N  
ATOM   3812  NH2 ARG B 701      -7.946  25.967   6.772  1.00 86.85           N  
ANISOU 3812  NH2 ARG B 701     9961   9987  13052   2467   -913  -2783       N  
ATOM   3813  N   ASP B 702      -1.275  28.313   5.202  1.00 65.82           N  
ANISOU 3813  N   ASP B 702     8863   6605   9542   1449  -1573  -1564       N  
ATOM   3814  CA  ASP B 702      -1.394  28.819   3.839  1.00 66.87           C  
ANISOU 3814  CA  ASP B 702     9166   6408   9832   1454  -1880  -1300       C  
ATOM   3815  C   ASP B 702      -0.055  29.256   3.249  1.00 65.30           C  
ANISOU 3815  C   ASP B 702     9248   6101   9460   1150  -1986  -1023       C  
ATOM   3816  O   ASP B 702      -0.003  29.801   2.149  1.00 66.12           O  
ANISOU 3816  O   ASP B 702     9564   5915   9642   1079  -2243   -787       O  
ATOM   3817  CB  ASP B 702      -2.422  29.948   3.771  1.00 71.77           C  
ANISOU 3817  CB  ASP B 702     9787   6603  10878   1723  -2132  -1505       C  
ATOM   3818  CG  ASP B 702      -3.842  29.444   3.927  1.00 75.08           C  
ANISOU 3818  CG  ASP B 702     9888   7127  11513   2016  -2073  -1712       C  
ATOM   3819  OD1 ASP B 702      -4.112  28.301   3.506  1.00 72.83           O  
ANISOU 3819  OD1 ASP B 702     9471   7131  11070   1984  -1966  -1554       O  
ATOM   3820  OD2 ASP B 702      -4.687  30.183   4.470  1.00 81.84           O  
ANISOU 3820  OD2 ASP B 702    10611   7776  12708   2272  -2123  -2053       O  
ATOM   3821  N   GLU B 703       1.025  29.006   3.980  1.00 63.22           N  
ANISOU 3821  N   GLU B 703     8983   6084   8952    949  -1794  -1048       N  
ATOM   3822  CA  GLU B 703       2.361  29.280   3.474  1.00 62.69           C  
ANISOU 3822  CA  GLU B 703     9109   5997   8711    633  -1842   -808       C  
ATOM   3823  C   GLU B 703       3.035  27.999   2.996  1.00 56.86           C  
ANISOU 3823  C   GLU B 703     8274   5631   7698    486  -1658   -572       C  
ATOM   3824  O   GLU B 703       4.154  28.027   2.481  1.00 57.03           O  
ANISOU 3824  O   GLU B 703     8394   5707   7569    221  -1646   -376       O  
ATOM   3825  CB  GLU B 703       3.217  29.948   4.547  1.00 66.06           C  
ANISOU 3825  CB  GLU B 703     9585   6431   9083    487  -1796   -994       C  
ATOM   3826  CG  GLU B 703       2.672  31.278   5.031  1.00 72.52           C  
ANISOU 3826  CG  GLU B 703    10533   6845  10179    611  -1967  -1261       C  
ATOM   3827  CD  GLU B 703       3.721  32.106   5.748  1.00 77.16           C  
ANISOU 3827  CD  GLU B 703    11261   7363  10693    369  -1985  -1373       C  
ATOM   3828  OE1 GLU B 703       3.349  33.106   6.395  1.00 81.97           O  
ANISOU 3828  OE1 GLU B 703    11964   7680  11499    462  -2073  -1661       O  
ATOM   3829  OE2 GLU B 703       4.919  31.761   5.661  1.00 76.20           O  
ANISOU 3829  OE2 GLU B 703    11144   7476  10334     83  -1913  -1191       O  
ATOM   3830  N   ARG B 704       2.354  26.874   3.166  1.00 51.71           N  
ANISOU 3830  N   ARG B 704     7423   5229   6996    652  -1502   -609       N  
ATOM   3831  CA  ARG B 704       2.928  25.595   2.777  1.00 49.59           C  
ANISOU 3831  CA  ARG B 704     7062   5281   6498    551  -1324   -420       C  
ATOM   3832  C   ARG B 704       2.637  25.302   1.306  1.00 50.19           C  
ANISOU 3832  C   ARG B 704     7242   5264   6564    509  -1415   -177       C  
ATOM   3833  O   ARG B 704       1.597  25.707   0.783  1.00 51.16           O  
ANISOU 3833  O   ARG B 704     7423   5157   6860    646  -1599   -178       O  
ATOM   3834  CB  ARG B 704       2.416  24.485   3.701  1.00 46.90           C  
ANISOU 3834  CB  ARG B 704     6503   5238   6080    703  -1117   -560       C  
ATOM   3835  CG  ARG B 704       2.467  24.887   5.171  1.00 48.62           C  
ANISOU 3835  CG  ARG B 704     6660   5524   6288    736  -1049   -827       C  
ATOM   3836  CD  ARG B 704       2.526  23.691   6.103  1.00 47.59           C  
ANISOU 3836  CD  ARG B 704     6378   5746   5960    752   -838   -874       C  
ATOM   3837  NE  ARG B 704       1.221  23.328   6.642  1.00 47.33           N  
ANISOU 3837  NE  ARG B 704     6225   5774   5985    929   -734  -1070       N  
ATOM   3838  CZ  ARG B 704       0.802  23.647   7.860  1.00 48.25           C  
ANISOU 3838  CZ  ARG B 704     6295   5955   6084    969   -643  -1353       C  
ATOM   3839  NH1 ARG B 704       1.583  24.342   8.677  1.00 48.64           N  
ANISOU 3839  NH1 ARG B 704     6431   6001   6050    851   -670  -1468       N  
ATOM   3840  NH2 ARG B 704      -0.403  23.270   8.264  1.00 50.14           N  
ANISOU 3840  NH2 ARG B 704     6397   6277   6375   1102   -513  -1539       N  
ATOM   3841  N   PRO B 705       3.570  24.617   0.628  1.00 50.87           N  
ANISOU 3841  N   PRO B 705     7348   5531   6451    313  -1296     19       N  
ATOM   3842  CA  PRO B 705       3.424  24.307  -0.798  1.00 50.65           C  
ANISOU 3842  CA  PRO B 705     7452   5446   6345    212  -1350    239       C  
ATOM   3843  C   PRO B 705       2.387  23.220  -1.022  1.00 48.86           C  
ANISOU 3843  C   PRO B 705     7106   5341   6119    395  -1289    227       C  
ATOM   3844  O   PRO B 705       2.126  22.421  -0.124  1.00 48.98           O  
ANISOU 3844  O   PRO B 705     6921   5561   6127    538  -1126     91       O  
ATOM   3845  CB  PRO B 705       4.807  23.766  -1.193  1.00 50.09           C  
ANISOU 3845  CB  PRO B 705     7368   5600   6065    -36  -1154    363       C  
ATOM   3846  CG  PRO B 705       5.700  24.000  -0.017  1.00 51.59           C  
ANISOU 3846  CG  PRO B 705     7426   5915   6261    -70  -1070    236       C  
ATOM   3847  CD  PRO B 705       4.819  24.076   1.182  1.00 51.20           C  
ANISOU 3847  CD  PRO B 705     7270   5847   6335    179  -1103     23       C  
ATOM   3848  N   SER B 706       1.804  23.193  -2.213  1.00 48.01           N  
ANISOU 3848  N   SER B 706     7139   5104   5998    357  -1433    378       N  
ATOM   3849  CA  SER B 706       0.907  22.115  -2.595  1.00 45.98           C  
ANISOU 3849  CA  SER B 706     6786   4971   5714    471  -1383    385       C  
ATOM   3850  C   SER B 706       1.707  20.972  -3.191  1.00 42.50           C  
ANISOU 3850  C   SER B 706     6352   4765   5029    307  -1147    495       C  
ATOM   3851  O   SER B 706       2.834  21.165  -3.639  1.00 40.89           O  
ANISOU 3851  O   SER B 706     6254   4594   4689     87  -1069    593       O  
ATOM   3852  CB  SER B 706      -0.129  22.610  -3.598  1.00 52.97           C  
ANISOU 3852  CB  SER B 706     7817   5610   6701    503  -1689    491       C  
ATOM   3853  OG  SER B 706      -1.107  23.401  -2.947  1.00 58.35           O  
ANISOU 3853  OG  SER B 706     8396   6096   7676    746  -1881    328       O  
ATOM   3854  N   PHE B 707       1.120  19.780  -3.193  1.00 42.53           N  
ANISOU 3854  N   PHE B 707     6236   4930   4995    406  -1023    457       N  
ATOM   3855  CA  PHE B 707       1.805  18.590  -3.700  1.00 41.23           C  
ANISOU 3855  CA  PHE B 707     6067   4962   4635    293   -789    519       C  
ATOM   3856  C   PHE B 707       2.246  18.607  -5.172  1.00 41.86           C  
ANISOU 3856  C   PHE B 707     6374   5002   4529     44   -800    680       C  
ATOM   3857  O   PHE B 707       3.265  18.005  -5.499  1.00 43.32           O  
ANISOU 3857  O   PHE B 707     6553   5336   4571    -90   -573    696       O  
ATOM   3858  CB  PHE B 707       1.040  17.307  -3.348  1.00 38.25           C  
ANISOU 3858  CB  PHE B 707     5544   4726   4264    438   -665    441       C  
ATOM   3859  CG  PHE B 707       1.392  16.766  -1.993  1.00 37.10           C  
ANISOU 3859  CG  PHE B 707     5210   4737   4150    559   -495    327       C  
ATOM   3860  CD1 PHE B 707       2.595  16.114  -1.790  1.00 34.31           C  
ANISOU 3860  CD1 PHE B 707     4809   4524   3703    505   -306    351       C  
ATOM   3861  CD2 PHE B 707       0.541  16.942  -0.915  1.00 39.12           C  
ANISOU 3861  CD2 PHE B 707     5336   5001   4527    715   -532    190       C  
ATOM   3862  CE1 PHE B 707       2.939  15.634  -0.542  1.00 35.68           C  
ANISOU 3862  CE1 PHE B 707     4838   4826   3893    606   -208    281       C  
ATOM   3863  CE2 PHE B 707       0.876  16.463   0.341  1.00 38.60           C  
ANISOU 3863  CE2 PHE B 707     5145   5086   4434    780   -389    105       C  
ATOM   3864  CZ  PHE B 707       2.077  15.807   0.528  1.00 37.46           C  
ANISOU 3864  CZ  PHE B 707     4986   5063   4185    724   -253    171       C  
ATOM   3865  N   PRO B 708       1.490  19.279  -6.062  1.00 39.62           N  
ANISOU 3865  N   PRO B 708     6289   4520   4244    -24  -1067    791       N  
ATOM   3866  CA  PRO B 708       2.023  19.409  -7.424  1.00 43.34           C  
ANISOU 3866  CA  PRO B 708     7029   4961   4477   -327  -1075    955       C  
ATOM   3867  C   PRO B 708       3.388  20.096  -7.458  1.00 47.11           C  
ANISOU 3867  C   PRO B 708     7580   5453   4867   -550   -963   1001       C  
ATOM   3868  O   PRO B 708       4.279  19.625  -8.160  1.00 50.23           O  
ANISOU 3868  O   PRO B 708     8035   5996   5053   -778   -734   1032       O  
ATOM   3869  CB  PRO B 708       0.969  20.262  -8.130  1.00 41.64           C  
ANISOU 3869  CB  PRO B 708     7024   4483   4315   -341  -1470   1088       C  
ATOM   3870  CG  PRO B 708      -0.298  19.896  -7.450  1.00 39.96           C  
ANISOU 3870  CG  PRO B 708     6586   4264   4333    -33  -1575    959       C  
ATOM   3871  CD  PRO B 708       0.070  19.672  -5.998  1.00 37.96           C  
ANISOU 3871  CD  PRO B 708     6057   4145   4222    157  -1350    769       C  
ATOM   3872  N   ARG B 709       3.557  21.176  -6.701  1.00 47.86           N  
ANISOU 3872  N   ARG B 709     7655   5403   5126   -499  -1102    980       N  
ATOM   3873  CA  ARG B 709       4.866  21.811  -6.601  1.00 51.24           C  
ANISOU 3873  CA  ARG B 709     8115   5862   5491   -725   -991   1004       C  
ATOM   3874  C   ARG B 709       5.846  20.940  -5.818  1.00 46.07           C  
ANISOU 3874  C   ARG B 709     7165   5498   4840   -664   -670    863       C  
ATOM   3875  O   ARG B 709       7.030  20.881  -6.147  1.00 46.16           O  
ANISOU 3875  O   ARG B 709     7149   5652   4738   -888   -471    876       O  
ATOM   3876  CB  ARG B 709       4.768  23.192  -5.955  1.00 60.61           C  
ANISOU 3876  CB  ARG B 709     9374   6794   6863   -692  -1240   1000       C  
ATOM   3877  CG  ARG B 709       6.079  23.965  -6.000  1.00 72.12           C  
ANISOU 3877  CG  ARG B 709    10911   8252   8240   -995  -1164   1050       C  
ATOM   3878  CD  ARG B 709       6.221  24.908  -4.812  1.00 82.62           C  
ANISOU 3878  CD  ARG B 709    12168   9445   9780   -891  -1284    933       C  
ATOM   3879  NE  ARG B 709       7.574  24.883  -4.258  1.00 88.74           N  
ANISOU 3879  NE  ARG B 709    12773  10434  10511  -1052  -1068    862       N  
ATOM   3880  CZ  ARG B 709       7.978  25.614  -3.223  1.00 90.53           C  
ANISOU 3880  CZ  ARG B 709    12927  10605  10867  -1035  -1130    750       C  
ATOM   3881  NH1 ARG B 709       7.136  26.444  -2.619  1.00 90.95           N  
ANISOU 3881  NH1 ARG B 709    13072  10379  11105   -856  -1371    671       N  
ATOM   3882  NH2 ARG B 709       9.228  25.518  -2.792  1.00 90.87           N  
ANISOU 3882  NH2 ARG B 709    12790  10871  10865  -1199   -953    696       N  
ATOM   3883  N   ILE B 710       5.354  20.265  -4.784  1.00 42.55           N  
ANISOU 3883  N   ILE B 710     6494   5141   4531   -371   -627    730       N  
ATOM   3884  CA  ILE B 710       6.204  19.388  -3.983  1.00 41.85           C  
ANISOU 3884  CA  ILE B 710     6145   5296   4458   -286   -386    625       C  
ATOM   3885  C   ILE B 710       6.745  18.233  -4.820  1.00 44.48           C  
ANISOU 3885  C   ILE B 710     6444   5804   4654   -371   -135    636       C  
ATOM   3886  O   ILE B 710       7.932  17.914  -4.757  1.00 45.84           O  
ANISOU 3886  O   ILE B 710     6466   6142   4810   -453     61    595       O  
ATOM   3887  CB  ILE B 710       5.457  18.824  -2.753  1.00 37.11           C  
ANISOU 3887  CB  ILE B 710     5370   4745   3983      8   -402    506       C  
ATOM   3888  CG1 ILE B 710       5.093  19.944  -1.780  1.00 36.91           C  
ANISOU 3888  CG1 ILE B 710     5344   4584   4095     90   -587    429       C  
ATOM   3889  CG2 ILE B 710       6.305  17.797  -2.031  1.00 32.89           C  
ANISOU 3889  CG2 ILE B 710     4615   4437   3446     88   -199    445       C  
ATOM   3890  CD1 ILE B 710       4.246  19.476  -0.610  1.00 36.57           C  
ANISOU 3890  CD1 ILE B 710     5155   4601   4139    332   -581    292       C  
ATOM   3891  N   LEU B 711       5.871  17.614  -5.608  1.00 45.39           N  
ANISOU 3891  N   LEU B 711     6683   5879   4685   -351   -147    671       N  
ATOM   3892  CA  LEU B 711       6.269  16.499  -6.458  1.00 47.63           C  
ANISOU 3892  CA  LEU B 711     6969   6297   4831   -433     96    648       C  
ATOM   3893  C   LEU B 711       7.245  16.945  -7.535  1.00 52.28           C  
ANISOU 3893  C   LEU B 711     7688   6934   5243   -766    225    698       C  
ATOM   3894  O   LEU B 711       8.205  16.242  -7.843  1.00 55.44           O  
ANISOU 3894  O   LEU B 711     7963   7506   5594   -838    508    611       O  
ATOM   3895  CB  LEU B 711       5.049  15.839  -7.103  1.00 45.59           C  
ANISOU 3895  CB  LEU B 711     6851   5971   4499   -383     23    670       C  
ATOM   3896  CG  LEU B 711       5.362  14.653  -8.019  1.00 44.95           C  
ANISOU 3896  CG  LEU B 711     6813   6004   4264   -477    274    616       C  
ATOM   3897  CD1 LEU B 711       6.209  13.628  -7.283  1.00 43.54           C  
ANISOU 3897  CD1 LEU B 711     6371   5969   4203   -307    523    488       C  
ATOM   3898  CD2 LEU B 711       4.082  14.017  -8.542  1.00 44.62           C  
ANISOU 3898  CD2 LEU B 711     6906   5891   4157   -437    167    631       C  
ATOM   3899  N   ALA B 712       6.996  18.120  -8.099  1.00 53.95           N  
ANISOU 3899  N   ALA B 712     8150   6983   5366   -975     19    832       N  
ATOM   3900  CA  ALA B 712       7.843  18.646  -9.156  1.00 55.10           C  
ANISOU 3900  CA  ALA B 712     8477   7162   5295  -1361    130    907       C  
ATOM   3901  C   ALA B 712       9.267  18.851  -8.656  1.00 56.54           C  
ANISOU 3901  C   ALA B 712     8419   7514   5549  -1458    346    821       C  
ATOM   3902  O   ALA B 712      10.224  18.471  -9.320  1.00 58.80           O  
ANISOU 3902  O   ALA B 712     8647   7986   5709  -1674    639    756       O  
ATOM   3903  CB  ALA B 712       7.274  19.950  -9.689  1.00 55.65           C  
ANISOU 3903  CB  ALA B 712     8886   6973   5284  -1555   -198   1101       C  
ATOM   3904  N   GLU B 713       9.396  19.447  -7.477  1.00 57.12           N  
ANISOU 3904  N   GLU B 713     8338   7536   5828  -1305    204    798       N  
ATOM   3905  CA  GLU B 713      10.704  19.726  -6.894  1.00 60.56           C  
ANISOU 3905  CA  GLU B 713     8529   8130   6352  -1398    345    722       C  
ATOM   3906  C   GLU B 713      11.509  18.467  -6.597  1.00 59.12           C  
ANISOU 3906  C   GLU B 713     7997   8209   6255  -1245    633    565       C  
ATOM   3907  O   GLU B 713      12.701  18.407  -6.893  1.00 61.82           O  
ANISOU 3907  O   GLU B 713     8163   8740   6587  -1432    864    492       O  
ATOM   3908  CB  GLU B 713      10.553  20.559  -5.623  1.00 62.82           C  
ANISOU 3908  CB  GLU B 713     8745   8298   6825  -1252    106    712       C  
ATOM   3909  CG  GLU B 713      10.479  22.049  -5.880  1.00 68.76           C  
ANISOU 3909  CG  GLU B 713     9773   8814   7538  -1504   -116    832       C  
ATOM   3910  CD  GLU B 713      11.848  22.677  -6.028  1.00 75.98           C  
ANISOU 3910  CD  GLU B 713    10617   9844   8407  -1853     17    831       C  
ATOM   3911  OE1 GLU B 713      12.751  22.322  -5.241  1.00 77.91           O  
ANISOU 3911  OE1 GLU B 713    10523  10307   8771  -1786    151    706       O  
ATOM   3912  OE2 GLU B 713      12.022  23.526  -6.928  1.00 79.57           O  
ANISOU 3912  OE2 GLU B 713    11355  10172   8705  -2212    -27    964       O  
ATOM   3913  N   ILE B 714      10.862  17.468  -6.007  1.00 55.66           N  
ANISOU 3913  N   ILE B 714     7454   7776   5921   -908    613    509       N  
ATOM   3914  CA  ILE B 714      11.539  16.216  -5.690  1.00 57.42           C  
ANISOU 3914  CA  ILE B 714     7377   8183   6255   -722    834    378       C  
ATOM   3915  C   ILE B 714      11.966  15.484  -6.955  1.00 62.30           C  
ANISOU 3915  C   ILE B 714     8020   8907   6744   -876   1134    301       C  
ATOM   3916  O   ILE B 714      13.123  15.086  -7.091  1.00 63.40           O  
ANISOU 3916  O   ILE B 714     7901   9230   6958   -922   1378    176       O  
ATOM   3917  CB  ILE B 714      10.650  15.279  -4.859  1.00 54.38           C  
ANISOU 3917  CB  ILE B 714     6946   7742   5975   -371    737    362       C  
ATOM   3918  CG1 ILE B 714      10.312  15.922  -3.518  1.00 52.73           C  
ANISOU 3918  CG1 ILE B 714     6688   7472   5874   -231    492    393       C  
ATOM   3919  CG2 ILE B 714      11.348  13.950  -4.633  1.00 54.23           C  
ANISOU 3919  CG2 ILE B 714     6668   7857   6081   -182    934    251       C  
ATOM   3920  CD1 ILE B 714       9.359  15.103  -2.675  1.00 50.77           C  
ANISOU 3920  CD1 ILE B 714     6427   7180   5685     50    408    383       C  
ATOM   3921  N   GLU B 715      11.025  15.312  -7.875  1.00 65.14           N  
ANISOU 3921  N   GLU B 715     8680   9156   6915   -958   1113    356       N  
ATOM   3922  CA  GLU B 715      11.294  14.599  -9.113  1.00 68.58           C  
ANISOU 3922  CA  GLU B 715     9198   9682   7176  -1128   1399    264       C  
ATOM   3923  C   GLU B 715      12.409  15.284  -9.896  1.00 70.85           C  
ANISOU 3923  C   GLU B 715     9481  10114   7325  -1515   1613    233       C  
ATOM   3924  O   GLU B 715      13.236  14.622 -10.521  1.00 72.99           O  
ANISOU 3924  O   GLU B 715     9609  10561   7561  -1613   1958     60       O  
ATOM   3925  CB  GLU B 715      10.022  14.484  -9.953  1.00 71.99           C  
ANISOU 3925  CB  GLU B 715     9996   9965   7393  -1203   1268    357       C  
ATOM   3926  CG  GLU B 715       9.927  13.184 -10.730  1.00 79.67           C  
ANISOU 3926  CG  GLU B 715    11004  10997   8268  -1181   1519    211       C  
ATOM   3927  CD  GLU B 715       8.597  12.479 -10.536  1.00 83.13           C  
ANISOU 3927  CD  GLU B 715    11562  11293   8729   -960   1336    247       C  
ATOM   3928  OE1 GLU B 715       7.576  13.166 -10.317  1.00 84.22           O  
ANISOU 3928  OE1 GLU B 715    11857  11289   8853   -940   1018    403       O  
ATOM   3929  OE2 GLU B 715       8.574  11.233 -10.600  1.00 84.27           O  
ANISOU 3929  OE2 GLU B 715    11633  11459   8926   -809   1512    107       O  
ATOM   3930  N   GLU B 716      12.439  16.611  -9.841  1.00 72.58           N  
ANISOU 3930  N   GLU B 716     9851  10251   7475  -1743   1421    385       N  
ATOM   3931  CA  GLU B 716      13.508  17.372 -10.476  1.00 78.82           C  
ANISOU 3931  CA  GLU B 716    10645  11172   8130  -2160   1608    379       C  
ATOM   3932  C   GLU B 716      14.849  17.091  -9.825  1.00 78.56           C  
ANISOU 3932  C   GLU B 716    10136  11377   8338  -2089   1832    200       C  
ATOM   3933  O   GLU B 716      15.788  16.646 -10.484  1.00 80.51           O  
ANISOU 3933  O   GLU B 716    10203  11845   8544  -2262   2196     30       O  
ATOM   3934  CB  GLU B 716      13.224  18.870 -10.399  1.00 85.01           C  
ANISOU 3934  CB  GLU B 716    11704  11762   8833  -2394   1302    593       C  
ATOM   3935  CG  GLU B 716      12.232  19.358 -11.429  1.00 92.52           C  
ANISOU 3935  CG  GLU B 716    13151  12507   9497  -2618   1111    786       C  
ATOM   3936  CD  GLU B 716      11.903  20.827 -11.271  1.00 98.47           C  
ANISOU 3936  CD  GLU B 716    14179  13001  10234  -2789    757   1001       C  
ATOM   3937  OE1 GLU B 716      12.502  21.482 -10.390  1.00100.92           O  
ANISOU 3937  OE1 GLU B 716    14304  13308  10733  -2770    699    980       O  
ATOM   3938  OE2 GLU B 716      11.047  21.326 -12.031  1.00 99.88           O  
ANISOU 3938  OE2 GLU B 716    14767  12964  10220  -2941    515   1191       O  
ATOM   3939  N   LEU B 717      14.928  17.354  -8.525  1.00 75.25           N  
ANISOU 3939  N   LEU B 717     9502  10918   8170  -1838   1610    225       N  
ATOM   3940  CA  LEU B 717      16.182  17.233  -7.795  1.00 73.45           C  
ANISOU 3940  CA  LEU B 717     8820  10903   8184  -1777   1728     89       C  
ATOM   3941  C   LEU B 717      16.708  15.799  -7.803  1.00 73.56           C  
ANISOU 3941  C   LEU B 717     8491  11082   8375  -1506   1990   -117       C  
ATOM   3942  O   LEU B 717      17.907  15.575  -7.644  1.00 76.03           O  
ANISOU 3942  O   LEU B 717     8401  11614   8873  -1519   2181   -273       O  
ATOM   3943  CB  LEU B 717      16.032  17.771  -6.364  1.00 68.81           C  
ANISOU 3943  CB  LEU B 717     8131  10225   7788  -1568   1395    165       C  
ATOM   3944  CG  LEU B 717      15.438  16.885  -5.266  1.00 62.81           C  
ANISOU 3944  CG  LEU B 717     7250   9405   7210  -1105   1227    152       C  
ATOM   3945  CD1 LEU B 717      16.530  16.098  -4.558  1.00 64.10           C  
ANISOU 3945  CD1 LEU B 717     6948   9776   7632   -901   1320     16       C  
ATOM   3946  CD2 LEU B 717      14.659  17.723  -4.266  1.00 59.11           C  
ANISOU 3946  CD2 LEU B 717     6948   8754   6756  -1017    881    268       C  
ATOM   3947  N   ALA B 718      15.814  14.832  -7.990  1.00 71.64           N  
ANISOU 3947  N   ALA B 718     8398  10722   8100  -1261   1986   -127       N  
ATOM   3948  CA  ALA B 718      16.221  13.434  -8.095  1.00 74.57           C  
ANISOU 3948  CA  ALA B 718     8510  11184   8640  -1003   2226   -326       C  
ATOM   3949  C   ALA B 718      17.093  13.231  -9.328  1.00 84.38           C  
ANISOU 3949  C   ALA B 718     9662  12622   9776  -1291   2654   -527       C  
ATOM   3950  O   ALA B 718      17.980  12.379  -9.340  1.00 87.11           O  
ANISOU 3950  O   ALA B 718     9634  13114  10349  -1133   2906   -754       O  
ATOM   3951  CB  ALA B 718      15.008  12.525  -8.148  1.00 70.01           C  
ANISOU 3951  CB  ALA B 718     8178  10416   8008   -757   2135   -288       C  
ATOM   3952  N   ARG B 719      16.830  14.020 -10.363  1.00 90.18           N  
ANISOU 3952  N   ARG B 719    10746  13352  10166  -1718   2730   -448       N  
ATOM   3953  CA  ARG B 719      17.649  14.007 -11.565  1.00 97.57           C  
ANISOU 3953  CA  ARG B 719    11650  14500  10922  -2094   3156   -630       C  
ATOM   3954  C   ARG B 719      18.873  14.890 -11.366  1.00 99.13           C  
ANISOU 3954  C   ARG B 719    11545  14910  11208  -2366   3264   -670       C  
ATOM   3955  O   ARG B 719      20.009  14.435 -11.492  1.00102.04           O  
ANISOU 3955  O   ARG B 719    11510  15469  11791  -2318   3519   -902       O  
ATOM   3956  CB  ARG B 719      16.836  14.494 -12.761  1.00102.73           C  
ANISOU 3956  CB  ARG B 719    12858  15046  11129  -2473   3141   -491       C  
ATOM   3957  CG  ARG B 719      15.630  13.628 -13.073  1.00105.96           C  
ANISOU 3957  CG  ARG B 719    13559  15281  11421  -2273   3056   -470       C  
ATOM   3958  CD  ARG B 719      14.843  14.191 -14.240  1.00112.36           C  
ANISOU 3958  CD  ARG B 719    14894  15944  11853  -2599   2895   -302       C  
ATOM   3959  NE  ARG B 719      13.737  13.322 -14.630  1.00115.92           N  
ANISOU 3959  NE  ARG B 719    15592  16251  12202  -2436   2807   -304       N  
ATOM   3960  CZ  ARG B 719      12.873  13.607 -15.599  1.00120.71           C  
ANISOU 3960  CZ  ARG B 719    16625  16719  12519  -2651   2614   -169       C  
ATOM   3961  NH1 ARG B 719      12.985  14.742 -16.275  1.00124.40           N  
ANISOU 3961  NH1 ARG B 719    17343  17151  12771  -3023   2482    -15       N  
ATOM   3962  NH2 ARG B 719      11.896  12.759 -15.890  1.00120.37           N  
ANISOU 3962  NH2 ARG B 719    16755  16565  12414  -2502   2531   -189       N  
ATOM   3963  N   GLU B 720      18.628  16.156 -11.047  1.00 97.14           N  
ANISOU 3963  N   GLU B 720    11511  14552  10845  -2588   2976   -430       N  
ATOM   3964  CA  GLU B 720      19.697  17.122 -10.836  1.00 98.95           C  
ANISOU 3964  CA  GLU B 720    11513  14950  11133  -2904   3033   -437       C  
ATOM   3965  C   GLU B 720      20.445  16.840  -9.538  1.00 97.38           C  
ANISOU 3965  C   GLU B 720    10777  14859  11364  -2553   2920   -534       C  
ATOM   3966  O   GLU B 720      21.352  16.008  -9.502  1.00 99.15           O  
ANISOU 3966  O   GLU B 720    10531  15304  11836  -2395   3184   -781       O  
ATOM   3967  CB  GLU B 720      19.127  18.540 -10.817  1.00 98.67           C  
ANISOU 3967  CB  GLU B 720    11916  14699  10875  -3213   2710   -147       C  
ATOM   3968  CG  GLU B 720      20.129  19.619 -10.456  1.00102.04           C  
ANISOU 3968  CG  GLU B 720    12155  15245  11371  -3544   2700   -127       C  
ATOM   3969  CD  GLU B 720      19.606  20.541  -9.376  1.00 99.77           C  
ANISOU 3969  CD  GLU B 720    12013  14706  11190  -3420   2233     76       C  
ATOM   3970  OE1 GLU B 720      18.895  20.046  -8.475  1.00 96.94           O  
ANISOU 3970  OE1 GLU B 720    11613  14210  11012  -2950   1982    100       O  
ATOM   3971  OE2 GLU B 720      19.895  21.755  -9.430  1.00100.35           O  
ANISOU 3971  OE2 GLU B 720    12257  14712  11160  -3811   2129    199       O  
TER    3972      GLU B 720                                                      
HETATM 3973  C1  P06 A 801       4.855  -1.379 -18.689  1.00 35.06           C  
ANISOU 3973  C1  P06 A 801     4394   4884   4042   -128    748   -153       C  
HETATM 3974  C2  P06 A 801       3.131  -2.184 -20.021  1.00 36.67           C  
ANISOU 3974  C2  P06 A 801     4674   5159   4098    -14    707    -87       C  
HETATM 3975  N3  P06 A 801       4.453  -1.924 -19.865  1.00 35.32           N  
ANISOU 3975  N3  P06 A 801     4435   4930   4057    -23    755   -194       N  
HETATM 3976  C4  P06 A 801       2.208  -1.928 -19.020  1.00 36.22           C  
ANISOU 3976  C4  P06 A 801     4659   5168   3935   -117    674     44       C  
HETATM 3977  N6  P06 A 801       4.012  -1.088 -17.672  1.00 34.37           N  
ANISOU 3977  N6  P06 A 801     4377   4847   3836   -227    712    -16       N  
HETATM 3978  C7  P06 A 801       2.708  -1.371 -17.865  1.00 35.30           C  
ANISOU 3978  C7  P06 A 801     4543   5042   3828   -222    689     72       C  
HETATM 3979  N9  P06 A 801       6.201  -1.099 -18.519  1.00 36.89           N  
ANISOU 3979  N9  P06 A 801     4538   5055   4425   -140    783   -271       N  
HETATM 3980  C12 P06 A 801       2.772  -2.790 -21.310  1.00 35.09           C  
ANISOU 3980  C12 P06 A 801     4494   4952   3887    104    692   -138       C  
HETATM 3981  S13 P06 A 801       4.038  -3.420 -22.297  1.00 39.50           S  
ANISOU 3981  S13 P06 A 801     4975   5430   4602    203    689   -331       S  
HETATM 3982  C14 P06 A 801       2.915  -3.928 -23.495  1.00 36.98           C  
ANISOU 3982  C14 P06 A 801     4753   5129   4168    309    657   -303       C  
HETATM 3983  N15 P06 A 801       1.665  -3.653 -23.194  1.00 34.32           N  
ANISOU 3983  N15 P06 A 801     4482   4853   3704    276    638   -163       N  
HETATM 3984  C16 P06 A 801       1.571  -3.020 -21.970  1.00 33.33           C  
ANISOU 3984  C16 P06 A 801     4336   4772   3555    161    667    -78       C  
HETATM 3985  C17 P06 A 801       3.358  -4.625 -24.782  1.00 38.81           C  
ANISOU 3985  C17 P06 A 801     4986   5313   4448    433    652   -449       C  
HETATM 3986  C18 P06 A 801       3.111  -3.712 -25.997  1.00 30.54           C  
ANISOU 3986  C18 P06 A 801     4075   4302   3227    502    910   -479       C  
HETATM 3987  C22 P06 A 801       2.534  -5.916 -24.976  1.00 38.07           C  
ANISOU 3987  C22 P06 A 801     4915   5174   4375    471    374   -399       C  
HETATM 3988  C26 P06 A 801       4.841  -5.035 -24.730  1.00 37.86           C  
ANISOU 3988  C26 P06 A 801     4722   5139   4523    449    637   -633       C  
HETATM 3989  C30 P06 A 801       0.237  -2.653 -21.530  1.00 33.46           C  
ANISOU 3989  C30 P06 A 801     4390   4881   3443    118    670     42       C  
HETATM 3990  C31 P06 A 801      -2.030  -3.330 -20.975  1.00 32.46           C  
ANISOU 3990  C31 P06 A 801     4240   4887   3207     22    492    200       C  
HETATM 3991  C32 P06 A 801      -0.735  -3.643 -21.375  1.00 33.89           C  
ANISOU 3991  C32 P06 A 801     4427   4957   3493     72    475    116       C  
HETATM 3992  C33 P06 A 801      -2.379  -2.001 -20.725  1.00 29.50           C  
ANISOU 3992  C33 P06 A 801     3885   4593   2733     47    688    201       C  
HETATM 3993  C35 P06 A 801      -0.122  -1.318 -21.287  1.00 31.73           C  
ANISOU 3993  C35 P06 A 801     4218   4730   3108    122    862     69       C  
HETATM 3994  C37 P06 A 801      -1.420  -1.000 -20.884  1.00 27.27           C  
ANISOU 3994  C37 P06 A 801     3653   4265   2442    100    860    144       C  
HETATM 3995  F39 P06 A 801      -0.433  -4.927 -21.607  1.00 37.45           F  
ANISOU 3995  F39 P06 A 801     4859   5321   4048     72    260     92       F  
HETATM 3996  N40 P06 A 801      -2.939  -4.430 -20.841  1.00 28.38           N  
ANISOU 3996  N40 P06 A 801     3692   4394   2697    -57    294    266       N  
HETATM 3997  S42 P06 A 801      -4.635  -4.209 -20.945  1.00 33.77           S  
ANISOU 3997  S42 P06 A 801     4329   5218   3283    -63    315    311       S  
HETATM 3998  C43 P06 A 801      -5.065  -3.771 -19.280  1.00 38.49           C  
ANISOU 3998  C43 P06 A 801     4863   5952   3809   -276    386    379       C  
HETATM 3999  C44 P06 A 801      -5.913  -2.250 -17.601  1.00 37.82           C  
ANISOU 3999  C44 P06 A 801     4701   6100   3570   -415    641    385       C  
HETATM 4000  C46 P06 A 801      -5.584  -2.525 -18.928  1.00 37.21           C  
ANISOU 4000  C46 P06 A 801     4668   5907   3562   -240    579    348       C  
HETATM 4001  C47 P06 A 801      -5.721  -3.220 -16.614  1.00 38.76           C  
ANISOU 4001  C47 P06 A 801     4837   6206   3684   -651    506    470       C  
HETATM 4002  C49 P06 A 801      -4.879  -4.733 -18.289  1.00 39.40           C  
ANISOU 4002  C49 P06 A 801     4986   6045   3940   -492    227    458       C  
HETATM 4003  C50 P06 A 801      -5.202  -4.468 -16.960  1.00 38.81           C  
ANISOU 4003  C50 P06 A 801     4896   6073   3777   -691    283    513       C  
HETATM 4004  F52 P06 A 801      -4.380  -5.935 -18.606  1.00 43.34           F  
ANISOU 4004  F52 P06 A 801     5531   6410   4527   -513      3    476       F  
HETATM 4005  F53 P06 A 801      -5.786  -1.565 -19.836  1.00 34.71           F  
ANISOU 4005  F53 P06 A 801     4384   5586   3219    -41    695    275       F  
HETATM 4006  O54 P06 A 801      -4.959  -3.126 -21.852  1.00 36.32           O  
ANISOU 4006  O54 P06 A 801     4694   5560   3545    119    473    246       O  
HETATM 4007  O55 P06 A 801      -5.266  -5.497 -21.163  1.00 34.49           O  
ANISOU 4007  O55 P06 A 801     4399   5292   3414   -130     95    356       O  
HETATM 4008  C1  P06 B 801       0.357  -5.140   5.577  1.00 46.32           C  
ANISOU 4008  C1  P06 B 801     6856   7097   3645   1074   -314  -1150       C  
HETATM 4009  C2  P06 B 801      -1.167  -3.610   6.430  1.00 45.82           C  
ANISOU 4009  C2  P06 B 801     6711   7093   3606    835   -124   -872       C  
HETATM 4010  N3  P06 B 801      -0.086  -4.404   6.627  1.00 47.01           N  
ANISOU 4010  N3  P06 B 801     6874   7249   3739   1010   -261  -1057       N  
HETATM 4011  C4  P06 B 801      -1.812  -3.530   5.209  1.00 43.93           C  
ANISOU 4011  C4  P06 B 801     6531   6797   3364    736    -64   -771       C  
HETATM 4012  N6  P06 B 801      -0.221  -5.120   4.357  1.00 45.92           N  
ANISOU 4012  N6  P06 B 801     6877   6985   3586    955   -240  -1062       N  
HETATM 4013  C7  P06 B 801      -1.292  -4.316   4.206  1.00 44.81           C  
ANISOU 4013  C7  P06 B 801     6726   6852   3448    793   -129   -870       C  
HETATM 4014  N9  P06 B 801       1.460  -5.959   5.760  1.00 45.68           N  
ANISOU 4014  N9  P06 B 801     6775   7018   3565   1281   -458  -1354       N  
HETATM 4015  C12 P06 B 801      -1.577  -2.840   7.608  1.00 44.51           C  
ANISOU 4015  C12 P06 B 801     6463   6992   3459    771    -53   -802       C  
HETATM 4016  S13 P06 B 801      -0.502  -2.791   8.958  1.00 48.07           S  
ANISOU 4016  S13 P06 B 801     6816   7553   3895    899   -115   -987       S  
HETATM 4017  C14 P06 B 801      -1.591  -1.782   9.832  1.00 48.17           C  
ANISOU 4017  C14 P06 B 801     6780   7592   3931    720     37   -813       C  
HETATM 4018  N15 P06 B 801      -2.691  -1.489   9.173  1.00 46.93           N  
ANISOU 4018  N15 P06 B 801     6656   7368   3806    595    121   -636       N  
HETATM 4019  C16 P06 B 801      -2.697  -2.077   7.922  1.00 44.09           C  
ANISOU 4019  C16 P06 B 801     6380   6938   3434    624     61   -624       C  
HETATM 4020  C17 P06 B 801      -1.290  -1.279  11.243  1.00 47.87           C  
ANISOU 4020  C17 P06 B 801     6658   7655   3875    712     65   -879       C  
HETATM 4021  C18 P06 B 801      -0.012  -1.915  11.817  1.00 49.44           C  
ANISOU 4021  C18 P06 B 801     6842   7930   4011    905   -116  -1084       C  
HETATM 4022  C22 P06 B 801      -2.457  -1.650  12.183  1.00 47.86           C  
ANISOU 4022  C22 P06 B 801     6807   7570   3807    602      2   -667       C  
HETATM 4023  C26 P06 B 801      -1.142   0.253  11.243  1.00 44.68           C  
ANISOU 4023  C26 P06 B 801     6048   7360   3569    607    348   -962       C  
HETATM 4024  C30 P06 B 801      -3.865  -1.828   7.097  1.00 42.67           C  
ANISOU 4024  C30 P06 B 801     6235   6704   3272    508    115   -443       C  
HETATM 4025  C31 P06 B 801      -5.273  -0.191   5.969  1.00 42.58           C  
ANISOU 4025  C31 P06 B 801     6129   6698   3350    369    349   -240       C  
HETATM 4026  C32 P06 B 801      -4.161  -0.512   6.742  1.00 43.36           C  
ANISOU 4026  C32 P06 B 801     6206   6836   3433    442    320   -411       C  
HETATM 4027  C33 P06 B 801      -6.121  -1.212   5.533  1.00 42.24           C  
ANISOU 4027  C33 P06 B 801     6201   6599   3250    330    180   -118       C  
HETATM 4028  C35 P06 B 801      -4.724  -2.846   6.664  1.00 42.72           C  
ANISOU 4028  C35 P06 B 801     6395   6617   3217    463    -32   -305       C  
HETATM 4029  C37 P06 B 801      -5.843  -2.536   5.884  1.00 41.82           C  
ANISOU 4029  C37 P06 B 801     6277   6493   3122    359      6   -155       C  
HETATM 4030  F39 P06 B 801      -3.357   0.484   7.146  1.00 44.60           F  
ANISOU 4030  F39 P06 B 801     6233   7072   3643    456    493   -555       F  
HETATM 4031  N40 P06 B 801      -5.456   1.203   5.665  1.00 40.82           N  
ANISOU 4031  N40 P06 B 801     5817   6498   3197    342    557   -214       N  
HETATM 4032  S42 P06 B 801      -6.975   1.862   5.216  1.00 46.34           S  
ANISOU 4032  S42 P06 B 801     6495   7172   3941    291    588      5       S  
HETATM 4033  C43 P06 B 801      -7.041   1.517   3.475  1.00 47.46           C  
ANISOU 4033  C43 P06 B 801     6768   7267   3995    314    503     51       C  
HETATM 4034  C44 P06 B 801      -7.993   0.364   1.571  1.00 47.37           C  
ANISOU 4034  C44 P06 B 801     6931   7226   3843    284    248    194       C  
HETATM 4035  C46 P06 B 801      -7.957   0.613   2.942  1.00 47.17           C  
ANISOU 4035  C46 P06 B 801     6793   7224   3904    280    314    166       C  
HETATM 4036  C47 P06 B 801      -7.102   1.017   0.717  1.00 47.73           C  
ANISOU 4036  C47 P06 B 801     7050   7237   3850    317    383    111       C  
HETATM 4037  C49 P06 B 801      -6.155   2.169   2.616  1.00 48.30           C  
ANISOU 4037  C49 P06 B 801     6932   7348   4073    341    646    -45       C  
HETATM 4038  C50 P06 B 801      -6.182   1.923   1.244  1.00 48.29           C  
ANISOU 4038  C50 P06 B 801     7064   7306   3979    339    592    -14       C  
HETATM 4039  F52 P06 B 801      -5.260   3.045   3.094  1.00 49.98           F  
ANISOU 4039  F52 P06 B 801     7083   7576   4332    344    852   -185       F  
HETATM 4040  F53 P06 B 801      -8.827  -0.033   3.727  1.00 48.53           F  
ANISOU 4040  F53 P06 B 801     6927   7417   4094    219    205    236       F  
HETATM 4041  O54 P06 B 801      -8.054   1.158   5.884  1.00 44.79           O  
ANISOU 4041  O54 P06 B 801     6286   6983   3750    228    454    117       O  
HETATM 4042  O55 P06 B 801      -6.902   3.307   5.324  1.00 47.12           O  
ANISOU 4042  O55 P06 B 801     6517   7271   4116    297    817     -2       O  
HETATM 4043  O   HOH A 901      -3.971  -6.178 -24.982  1.00 47.35           O  
HETATM 4044  O   HOH A 902      11.566  -7.205 -14.309  1.00 41.69           O  
HETATM 4045  O   HOH A 903     -10.295  -7.300  -5.598  1.00 37.05           O  
HETATM 4046  O   HOH A 904      -0.287 -24.367 -29.434  1.00 35.68           O  
HETATM 4047  O   HOH A 905     -12.647 -23.704 -33.652  1.00 67.00           O  
HETATM 4048  O   HOH A 906      -4.568 -21.462 -24.854  1.00 33.17           O  
HETATM 4049  O   HOH A 907     -11.505 -23.803 -24.564  1.00 56.18           O  
HETATM 4050  O   HOH A 908       3.872   0.057 -32.084  1.00 69.87           O  
HETATM 4051  O   HOH A 909      -5.548  14.461 -11.418  1.00 40.83           O  
HETATM 4052  O   HOH A 910      -6.410  -3.436 -12.594  1.00 41.55           O  
HETATM 4053  O   HOH A 911       9.835  -1.129 -17.713  1.00 41.54           O  
HETATM 4054  O   HOH A 912      -1.275  -3.152 -26.895  1.00 58.87           O  
HETATM 4055  O   HOH A 913      -0.809  -4.248 -24.525  1.00 30.99           O  
HETATM 4056  O   HOH A 914       1.105 -25.359 -27.533  1.00 35.46           O  
HETATM 4057  O   HOH A 915       7.420 -31.861 -28.479  1.00 44.08           O  
HETATM 4058  O   HOH A 916       2.761   3.439 -11.908  1.00 30.87           O  
HETATM 4059  O   HOH A 917       0.244  -9.893 -27.557  1.00 42.04           O  
HETATM 4060  O   HOH A 918      -7.804 -18.570 -23.494  1.00 38.60           O  
HETATM 4061  O   HOH A 919       8.524 -29.154 -26.575  1.00 42.60           O  
HETATM 4062  O   HOH A 920      -3.160   1.040 -31.750  1.00 56.53           O  
HETATM 4063  O   HOH A 921      16.072 -18.782 -16.707  1.00 83.94           O  
HETATM 4064  O   HOH A 922     -10.146 -21.915 -13.628  1.00 54.21           O  
HETATM 4065  O   HOH A 923     -10.883  12.649 -21.546  1.00 49.51           O  
HETATM 4066  O   HOH A 924      -9.464  15.875 -12.668  1.00 61.99           O  
HETATM 4067  O   HOH A 925       1.304   6.938 -11.381  1.00 47.60           O  
HETATM 4068  O   HOH A 926       8.419   7.401 -29.537  1.00 52.70           O  
HETATM 4069  O   HOH A 927      -5.621 -18.569 -24.924  1.00 45.96           O  
HETATM 4070  O   HOH A 928       3.112  -2.834  -7.050  1.00 64.67           O  
HETATM 4071  O   HOH B 901     -18.228  -5.228  12.671  1.00 59.99           O  
HETATM 4072  O   HOH B 902      -4.758  22.511   8.438  1.00 46.86           O  
HETATM 4073  O   HOH B 903      -0.220  17.281  10.360  1.00 36.65           O  
HETATM 4074  O   HOH B 904      -2.536  17.194  -6.087  1.00 47.61           O  
HETATM 4075  O   HOH B 905      -1.586  13.656   7.346  1.00 40.41           O  
HETATM 4076  O   HOH B 906      -1.775  -0.142  -5.406  1.00 46.41           O  
HETATM 4077  O   HOH B 907      -6.444   1.462  -3.380  1.00 33.83           O  
HETATM 4078  O   HOH B 908       5.787   5.579  -8.100  1.00 48.96           O  
HETATM 4079  O   HOH B 909      11.748   2.334  -3.051  1.00 63.09           O  
HETATM 4080  O   HOH B 910      -3.820  16.087   7.820  1.00 51.31           O  
HETATM 4081  O   HOH B 911      -4.309 -11.709  -3.008  1.00 51.17           O  
HETATM 4082  O   HOH B 912      -6.290   6.444 -10.856  1.00 34.43           O  
HETATM 4083  O   HOH B 913      -4.675   0.560   9.628  1.00 48.99           O  
HETATM 4084  O   HOH B 914       1.298  -3.300  -5.754  1.00 61.89           O  
HETATM 4085  O   HOH B 915      24.795  16.272   9.903  1.00 69.89           O  
HETATM 4086  O   HOH B 916      -1.564  19.523  -2.157  1.00 43.17           O  
HETATM 4087  O   HOH B 917      -1.402  -9.103  -1.894  1.00 38.91           O  
HETATM 4088  O   HOH B 918       6.975  29.087   9.879  1.00 57.66           O  
HETATM 4089  O   HOH B 919      -4.316   1.819  -5.204  1.00 37.31           O  
HETATM 4090  O   HOH B 920      -1.787 -12.229  -3.275  1.00 38.87           O  
HETATM 4091  O   HOH B 921       0.148  26.028  -1.733  1.00 59.67           O  
HETATM 4092  O   HOH B 922       0.473   4.221 -10.482  1.00 40.44           O  
HETATM 4093  O   HOH B 923       4.828  30.260   8.990  1.00 56.30           O  
HETATM 4094  O   HOH B 924     -11.888  -2.677  15.459  1.00 45.61           O  
HETATM 4095  O   HOH B 925     -12.666   0.742  -9.222  1.00 34.75           O  
HETATM 4096  O   HOH B 926      14.299  18.305  16.311  1.00 33.14           O  
CONECT 3973 3975 3977 3979                                                      
CONECT 3974 3975 3976 3980                                                      
CONECT 3975 3973 3974                                                           
CONECT 3976 3974 3978                                                           
CONECT 3977 3973 3978                                                           
CONECT 3978 3976 3977                                                           
CONECT 3979 3973                                                                
CONECT 3980 3974 3981 3984                                                      
CONECT 3981 3980 3982                                                           
CONECT 3982 3981 3983 3985                                                      
CONECT 3983 3982 3984                                                           
CONECT 3984 3980 3983 3989                                                      
CONECT 3985 3982 3986 3987 3988                                                 
CONECT 3986 3985                                                                
CONECT 3987 3985                                                                
CONECT 3988 3985                                                                
CONECT 3989 3984 3991 3993                                                      
CONECT 3990 3991 3992 3996                                                      
CONECT 3991 3989 3990 3995                                                      
CONECT 3992 3990 3994                                                           
CONECT 3993 3989 3994                                                           
CONECT 3994 3992 3993                                                           
CONECT 3995 3991                                                                
CONECT 3996 3990 3997                                                           
CONECT 3997 3996 3998 4006 4007                                                 
CONECT 3998 3997 4000 4002                                                      
CONECT 3999 4000 4001                                                           
CONECT 4000 3998 3999 4005                                                      
CONECT 4001 3999 4003                                                           
CONECT 4002 3998 4003 4004                                                      
CONECT 4003 4001 4002                                                           
CONECT 4004 4002                                                                
CONECT 4005 4000                                                                
CONECT 4006 3997                                                                
CONECT 4007 3997                                                                
CONECT 4008 4010 4012 4014                                                      
CONECT 4009 4010 4011 4015                                                      
CONECT 4010 4008 4009                                                           
CONECT 4011 4009 4013                                                           
CONECT 4012 4008 4013                                                           
CONECT 4013 4011 4012                                                           
CONECT 4014 4008                                                                
CONECT 4015 4009 4016 4019                                                      
CONECT 4016 4015 4017                                                           
CONECT 4017 4016 4018 4020                                                      
CONECT 4018 4017 4019                                                           
CONECT 4019 4015 4018 4024                                                      
CONECT 4020 4017 4021 4022 4023                                                 
CONECT 4021 4020                                                                
CONECT 4022 4020                                                                
CONECT 4023 4020                                                                
CONECT 4024 4019 4026 4028                                                      
CONECT 4025 4026 4027 4031                                                      
CONECT 4026 4024 4025 4030                                                      
CONECT 4027 4025 4029                                                           
CONECT 4028 4024 4029                                                           
CONECT 4029 4027 4028                                                           
CONECT 4030 4026                                                                
CONECT 4031 4025 4032                                                           
CONECT 4032 4031 4033 4041 4042                                                 
CONECT 4033 4032 4035 4037                                                      
CONECT 4034 4035 4036                                                           
CONECT 4035 4033 4034 4040                                                      
CONECT 4036 4034 4038                                                           
CONECT 4037 4033 4038 4039                                                      
CONECT 4038 4036 4037                                                           
CONECT 4039 4037                                                                
CONECT 4040 4035                                                                
CONECT 4041 4032                                                                
CONECT 4042 4032                                                                
MASTER      397    0    2   23   14    0   10    6 4094    2   70   46          
END                                                                             



If you find results from this site helpful for your research, please cite one of our papers:

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