CNRS Nantes University UFIP UFIP
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***  TRANSFERASE/IMMUNE SYSTEM 29-OCT-17 6BGT  ***

elNémo ID: 19100818143855026

Job options:

ID        	=	 19100818143855026
JOBID     	=	 TRANSFERASE/IMMUNE SYSTEM 29-OCT-17 6BGT
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 3
DQMIN     	=	 -1000
DQMAX     	=	 1000
DQSTEP    	=	 50
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    TRANSFERASE/IMMUNE SYSTEM               29-OCT-17   6BGT              
TITLE     STRUCTURE OF TRASTUZUMAB FAB MUTANT IN COMPLEX WITH HER2 EXTRACELLULAR
TITLE    2 DOMAIN                                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RECEPTOR TYROSINE-PROTEIN KINASE ERBB-2;                   
COMPND   3 CHAIN: C;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 1-652;                                        
COMPND   5 SYNONYM: METASTATIC LYMPH NODE GENE 19 PROTEIN, MLN 19, PROTO-       
COMPND   6 ONCOGENE NEU, PROTO-ONCOGENE C-ERBB-2, TYROSINE KINASE-TYPE CELL     
COMPND   7 SURFACE RECEPTOR HER2, P185ERBB2;                                    
COMPND   8 EC: 2.7.10.1;                                                        
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: HERCEPTIN LIGHT CHAIN MUTANT;                              
COMPND  12 CHAIN: A;                                                            
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MOL_ID: 3;                                                           
COMPND  15 MOLECULE: HERCEPTIN HEAVY CHAIN FAB FRAGMENT MUTANT;                 
COMPND  16 CHAIN: B;                                                            
COMPND  17 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ERBB2, HER2, MLN19, NEU, NGL;                                  
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  14 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  16 MOL_ID: 3;                                                           
SOURCE  17 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  18 ORGANISM_COMMON: HUMAN;                                              
SOURCE  19 ORGANISM_TAXID: 9606;                                                
SOURCE  20 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  21 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  22 EXPRESSION_SYSTEM_TAXID: 9606                                        
KEYWDS    HERCEPTIN, ANTIBODY, TRANSFERASE-IMMUNE SYSTEM COMPLEX                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.CHRISTIE,D.CHRIST                                                   
REVDAT   1   31-OCT-18 6BGT    0                                                
JRNL        AUTH   M.CHRISTIE,R.ROUET,D.NEVOLTRIS,D.LANGLEY,P.SCHOFIELD,        
JRNL        AUTH 2 L.FABRI,K.TINGLY,D.LOWE,L.JERMUTUS,D.CHRIST                  
JRNL        TITL   STABLE HUMAN IGG ANTIBODY THERAPEUTICS WITH NATIVE FRAMEWORK 
JRNL        TITL 2 STRUCTURE                                                    
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10.1_2155: ???)                            
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.93                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 40965                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.207                           
REMARK   3   R VALUE            (WORKING SET) : 0.205                           
REMARK   3   FREE R VALUE                     : 0.248                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2007                            
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 49.9354 -  6.5030    1.00     3006   159  0.2243 0.2830        
REMARK   3     2  6.5030 -  5.1633    1.00     2888   142  0.2038 0.2131        
REMARK   3     3  5.1633 -  4.5111    1.00     2802   167  0.1552 0.2027        
REMARK   3     4  4.5111 -  4.0989    1.00     2838   141  0.1570 0.1860        
REMARK   3     5  4.0989 -  3.8052    1.00     2815   140  0.1773 0.2117        
REMARK   3     6  3.8052 -  3.5809    1.00     2819   127  0.1957 0.2278        
REMARK   3     7  3.5809 -  3.4016    1.00     2811   128  0.2194 0.2565        
REMARK   3     8  3.4016 -  3.2536    1.00     2779   148  0.2250 0.2691        
REMARK   3     9  3.2536 -  3.1284    1.00     2771   139  0.2260 0.3116        
REMARK   3    10  3.1284 -  3.0204    1.00     2755   160  0.2415 0.2930        
REMARK   3    11  3.0204 -  2.9260    1.00     2772   151  0.2637 0.3282        
REMARK   3    12  2.9260 -  2.8424    1.00     2756   153  0.2659 0.3093        
REMARK   3    13  2.8424 -  2.7675    0.98     2747   126  0.2634 0.2948        
REMARK   3    14  2.7675 -  2.7000    0.87     2399   126  0.2645 0.3255        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.300            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.570           
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) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.005           7991                                  
REMARK   3   ANGLE     :  0.831          10897                                  
REMARK   3   CHIRALITY :  0.051           1207                                  
REMARK   3   PLANARITY :  0.006           1420                                  
REMARK   3   DIHEDRAL  : 17.313           4835                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (CHAIN 'C' AND RESID 1 THROUGH 607)                    
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.8227  28.1750 -48.6228              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1640 T22:   0.1496                                     
REMARK   3      T33:   0.2369 T12:  -0.0176                                     
REMARK   3      T13:  -0.0338 T23:  -0.0048                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2161 L22:   0.4410                                     
REMARK   3      L33:   0.7284 L12:  -0.3081                                     
REMARK   3      L13:   0.2945 L23:   0.0254                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0231 S12:   0.0088 S13:   0.0862                       
REMARK   3      S21:   0.0882 S22:   0.1127 S23:  -0.0154                       
REMARK   3      S31:  -0.0153 S32:   0.0042 S33:   0.0390                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN 'A' AND RESID 1 THROUGH 211)                    
REMARK   3    ORIGIN FOR THE GROUP (A):  37.4942  53.1301   3.9364              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9336 T22:   0.4893                                     
REMARK   3      T33:   0.4920 T12:   0.0657                                     
REMARK   3      T13:   0.0236 T23:  -0.0642                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4181 L22:   0.6882                                     
REMARK   3      L33:   1.7178 L12:   0.3330                                     
REMARK   3      L13:   1.1012 L23:  -0.1944                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2236 S12:  -0.2027 S13:   0.4332                       
REMARK   3      S21:   0.4112 S22:   0.0801 S23:   0.3087                       
REMARK   3      S31:  -0.8024 S32:  -0.1897 S33:  -0.0605                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (CHAIN 'B' AND RESID 1 THROUGH 220)                    
REMARK   3    ORIGIN FOR THE GROUP (A):  30.3845  50.7722 -13.7082              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7138 T22:   0.5381                                     
REMARK   3      T33:   0.5476 T12:  -0.0161                                     
REMARK   3      T13:  -0.0409 T23:   0.1094                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7549 L22:   1.2092                                     
REMARK   3      L33:   1.6937 L12:   0.3989                                     
REMARK   3      L13:   0.5729 L23:   0.0773                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3161 S12:   0.3796 S13:   0.7080                       
REMARK   3      S21:  -0.1588 S22:   0.2297 S23:   0.4260                       
REMARK   3      S31:  -0.5992 S32:   0.1629 S33:   0.0009                       
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 6BGT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-OCT-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000230830.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-APR-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : AUSTRALIAN SYNCHROTRON             
REMARK 200  BEAMLINE                       : MX2                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9536                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 41043                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 53.200                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 10.10                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 12.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.81                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1N8Z                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.60                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.04                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MES, PH 6.5, 18% PEG3350, 10%     
REMARK 280  GLYCEROL, VAPOR DIFFUSION, TEMPERATURE 293K                         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       31.43000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      102.13950            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       57.23000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      102.13950            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       31.43000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       57.23000            
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5650 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 46100 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 C   -21                                                      
REMARK 465     GLU C   -20                                                      
REMARK 465     LEU C   -19                                                      
REMARK 465     ALA C   -18                                                      
REMARK 465     ALA C   -17                                                      
REMARK 465     LEU C   -16                                                      
REMARK 465     CYS C   -15                                                      
REMARK 465     ARG C   -14                                                      
REMARK 465     TRP C   -13                                                      
REMARK 465     GLY C   -12                                                      
REMARK 465     LEU C   -11                                                      
REMARK 465     LEU C   -10                                                      
REMARK 465     LEU C    -9                                                      
REMARK 465     ALA C    -8                                                      
REMARK 465     LEU C    -7                                                      
REMARK 465     LEU C    -6                                                      
REMARK 465     PRO C    -5                                                      
REMARK 465     PRO C    -4                                                      
REMARK 465     GLY C    -3                                                      
REMARK 465     ALA C    -2                                                      
REMARK 465     ALA C    -1                                                      
REMARK 465     SER C     0                                                      
REMARK 465     PRO C   100                                                      
REMARK 465     LEU C   101                                                      
REMARK 465     ASN C   102                                                      
REMARK 465     ASN C   103                                                      
REMARK 465     THR C   104                                                      
REMARK 465     THR C   105                                                      
REMARK 465     PRO C   106                                                      
REMARK 465     VAL C   107                                                      
REMARK 465     THR C   108                                                      
REMARK 465     GLY C   109                                                      
REMARK 465     ALA C   110                                                      
REMARK 465     GLY C   581                                                      
REMARK 465     VAL C   582                                                      
REMARK 465     LYS C   583                                                      
REMARK 465     PRO C   584                                                      
REMARK 465     ASP C   585                                                      
REMARK 465     LEU C   586                                                      
REMARK 465     SER C   587                                                      
REMARK 465     CYS C   608                                                      
REMARK 465     THR C   609                                                      
REMARK 465     HIS C   610                                                      
REMARK 465     SER C   611                                                      
REMARK 465     CYS C   612                                                      
REMARK 465     VAL C   613                                                      
REMARK 465     ASP C   614                                                      
REMARK 465     LEU C   615                                                      
REMARK 465     ASP C   616                                                      
REMARK 465     ASP C   617                                                      
REMARK 465     LYS C   618                                                      
REMARK 465     GLY C   619                                                      
REMARK 465     CYS C   620                                                      
REMARK 465     PRO C   621                                                      
REMARK 465     ALA C   622                                                      
REMARK 465     GLU C   623                                                      
REMARK 465     GLN C   624                                                      
REMARK 465     ARG C   625                                                      
REMARK 465     ALA C   626                                                      
REMARK 465     SER C   627                                                      
REMARK 465     PRO C   628                                                      
REMARK 465     LEU C   629                                                      
REMARK 465     THR C   630                                                      
REMARK 465     HIS C   631                                                      
REMARK 465     HIS C   632                                                      
REMARK 465     HIS C   633                                                      
REMARK 465     HIS C   634                                                      
REMARK 465     HIS C   635                                                      
REMARK 465     HIS C   636                                                      
REMARK 465     GLY A   212                                                      
REMARK 465     GLU A   213                                                      
REMARK 465     CYS A   214                                                      
REMARK 465     SER B   134                                                      
REMARK 465     SER B   135                                                      
REMARK 465     LYS B   136                                                      
REMARK 465     SER B   137                                                      
REMARK 465     THR B   138                                                      
REMARK 465     SER B   139                                                      
REMARK 465     GLY B   140                                                      
REMARK 465     GLY B   141                                                      
REMARK 465     GLU B   219                                                      
REMARK 465     PRO B   220                                                      
REMARK 465     LYS B   221                                                      
REMARK 465     SER B   222                                                      
REMARK 465     CYS B   223                                                      
REMARK 465     GLY B   224                                                      
REMARK 465     SER B   225                                                      
REMARK 465     HIS B   226                                                      
REMARK 465     HIS B   227                                                      
REMARK 465     HIS B   228                                                      
REMARK 465     HIS B   229                                                      
REMARK 465     HIS B   230                                                      
REMARK 465     HIS B   231                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OG   SER C   429     O    HOH C   801              1.86            
REMARK 500   OE2  GLU C    18     O    HOH C   802              2.01            
REMARK 500   OG   SER C   187     O    HOH C   803              2.03            
REMARK 500   OE1  GLU A   105     OH   TYR A   173              2.08            
REMARK 500   OE2  GLU C   117     O    HOH C   804              2.08            
REMARK 500   O    LYS C   148     NE2  GLN C   156              2.10            
REMARK 500   OE1  GLN C   156     NH2  ARG C   195              2.11            
REMARK 500   OE1  GLU A   195     N    LYS A   207              2.16            
REMARK 500   NH1  ARG C    25     O    HOH C   805              2.18            
REMARK 500   OE1  GLU C   357     O    HOH C   806              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP C   8       49.00   -157.98                                   
REMARK 500    LYS C  10     -120.43     43.55                                   
REMARK 500    ARG C 195      -42.46   -139.55                                   
REMARK 500    HIS C 215      151.45    -49.63                                   
REMARK 500    ALA C 220      -31.61     78.54                                   
REMARK 500    HIS C 235      -69.38   -133.07                                   
REMARK 500    ALA C 271       30.93    -97.93                                   
REMARK 500    ASN C 280        6.27     81.25                                   
REMARK 500    HIS C 296       35.09    -89.93                                   
REMARK 500    GLU C 326     -125.63     51.90                                   
REMARK 500    LEU C 400       46.03   -106.39                                   
REMARK 500    ARG C 495       15.45     56.65                                   
REMARK 500    GLN C 511     -103.48   -114.80                                   
REMARK 500    HIS C 567      -90.28   -130.08                                   
REMARK 500    PRO C 605       64.35   -104.33                                   
REMARK 500    ASN A  30     -127.09     60.27                                   
REMARK 500    ALA A  32       71.55    -67.15                                   
REMARK 500    ALA A  51      -51.90     76.02                                   
REMARK 500    LYS B  43     -169.21   -121.04                                   
REMARK 500    ASP B 151       78.98     69.87                                   
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 Mono-Saccharide NAG C 701 bound   
REMARK 800  to ASN C 237                                                        
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 6BFT   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6ARP   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6ARU   RELATED DB: PDB                                   
DBREF  6BGT C  -21   630  UNP    P04626   ERBB2_HUMAN      1    652             
DBREF  6BGT A    1   104  PDB    6BGT     6BGT             1    104             
DBREF  6BGT A  105   214  UNP    Q7Z3Y4   Q7Z3Y4_HUMAN   127    236             
DBREF  6BGT B    1   109  PDB    6BGT     6BGT             1    109             
DBREF  6BGT B  110   223  UNP    P0DOX5   IGG1_HUMAN     109    222             
SEQADV 6BGT HIS C  631  UNP  P04626              EXPRESSION TAG                 
SEQADV 6BGT HIS C  632  UNP  P04626              EXPRESSION TAG                 
SEQADV 6BGT HIS C  633  UNP  P04626              EXPRESSION TAG                 
SEQADV 6BGT HIS C  634  UNP  P04626              EXPRESSION TAG                 
SEQADV 6BGT HIS C  635  UNP  P04626              EXPRESSION TAG                 
SEQADV 6BGT HIS C  636  UNP  P04626              EXPRESSION TAG                 
SEQADV 6BGT GLY B  224  UNP  P0DOX5              EXPRESSION TAG                 
SEQADV 6BGT SER B  225  UNP  P0DOX5              EXPRESSION TAG                 
SEQADV 6BGT HIS B  226  UNP  P0DOX5              EXPRESSION TAG                 
SEQADV 6BGT HIS B  227  UNP  P0DOX5              EXPRESSION TAG                 
SEQADV 6BGT HIS B  228  UNP  P0DOX5              EXPRESSION TAG                 
SEQADV 6BGT HIS B  229  UNP  P0DOX5              EXPRESSION TAG                 
SEQADV 6BGT HIS B  230  UNP  P0DOX5              EXPRESSION TAG                 
SEQADV 6BGT HIS B  231  UNP  P0DOX5              EXPRESSION TAG                 
SEQRES   1 C  658  MET GLU LEU ALA ALA LEU CYS ARG TRP GLY LEU LEU LEU          
SEQRES   2 C  658  ALA LEU LEU PRO PRO GLY ALA ALA SER THR GLN VAL CYS          
SEQRES   3 C  658  THR GLY THR ASP MET LYS LEU ARG LEU PRO ALA SER PRO          
SEQRES   4 C  658  GLU THR HIS LEU ASP MET LEU ARG HIS LEU TYR GLN GLY          
SEQRES   5 C  658  CYS GLN VAL VAL GLN GLY ASN LEU GLU LEU THR TYR LEU          
SEQRES   6 C  658  PRO THR ASN ALA SER LEU SER PHE LEU GLN ASP ILE GLN          
SEQRES   7 C  658  GLU VAL GLN GLY TYR VAL LEU ILE ALA HIS ASN GLN VAL          
SEQRES   8 C  658  ARG GLN VAL PRO LEU GLN ARG LEU ARG ILE VAL ARG GLY          
SEQRES   9 C  658  THR GLN LEU PHE GLU ASP ASN TYR ALA LEU ALA VAL LEU          
SEQRES  10 C  658  ASP ASN GLY ASP PRO LEU ASN ASN THR THR PRO VAL THR          
SEQRES  11 C  658  GLY ALA SER PRO GLY GLY LEU ARG GLU LEU GLN LEU ARG          
SEQRES  12 C  658  SER LEU THR GLU ILE LEU LYS GLY GLY VAL LEU ILE GLN          
SEQRES  13 C  658  ARG ASN PRO GLN LEU CYS TYR GLN ASP THR ILE LEU TRP          
SEQRES  14 C  658  LYS ASP ILE PHE HIS LYS ASN ASN GLN LEU ALA LEU THR          
SEQRES  15 C  658  LEU ILE ASP THR ASN ARG SER ARG ALA CYS HIS PRO CYS          
SEQRES  16 C  658  SER PRO MET CYS LYS GLY SER ARG CYS TRP GLY GLU SER          
SEQRES  17 C  658  SER GLU ASP CYS GLN SER LEU THR ARG THR VAL CYS ALA          
SEQRES  18 C  658  GLY GLY CYS ALA ARG CYS LYS GLY PRO LEU PRO THR ASP          
SEQRES  19 C  658  CYS CYS HIS GLU GLN CYS ALA ALA GLY CYS THR GLY PRO          
SEQRES  20 C  658  LYS HIS SER ASP CYS LEU ALA CYS LEU HIS PHE ASN HIS          
SEQRES  21 C  658  SER GLY ILE CYS GLU LEU HIS CYS PRO ALA LEU VAL THR          
SEQRES  22 C  658  TYR ASN THR ASP THR PHE GLU SER MET PRO ASN PRO GLU          
SEQRES  23 C  658  GLY ARG TYR THR PHE GLY ALA SER CYS VAL THR ALA CYS          
SEQRES  24 C  658  PRO TYR ASN TYR LEU SER THR ASP VAL GLY SER CYS THR          
SEQRES  25 C  658  LEU VAL CYS PRO LEU HIS ASN GLN GLU VAL THR ALA GLU          
SEQRES  26 C  658  ASP GLY THR GLN ARG CYS GLU LYS CYS SER LYS PRO CYS          
SEQRES  27 C  658  ALA ARG VAL CYS TYR GLY LEU GLY MET GLU HIS LEU ARG          
SEQRES  28 C  658  GLU VAL ARG ALA VAL THR SER ALA ASN ILE GLN GLU PHE          
SEQRES  29 C  658  ALA GLY CYS LYS LYS ILE PHE GLY SER LEU ALA PHE LEU          
SEQRES  30 C  658  PRO GLU SER PHE ASP GLY ASP PRO ALA SER ASN THR ALA          
SEQRES  31 C  658  PRO LEU GLN PRO GLU GLN LEU GLN VAL PHE GLU THR LEU          
SEQRES  32 C  658  GLU GLU ILE THR GLY TYR LEU TYR ILE SER ALA TRP PRO          
SEQRES  33 C  658  ASP SER LEU PRO ASP LEU SER VAL PHE GLN ASN LEU GLN          
SEQRES  34 C  658  VAL ILE ARG GLY ARG ILE LEU HIS ASN GLY ALA TYR SER          
SEQRES  35 C  658  LEU THR LEU GLN GLY LEU GLY ILE SER TRP LEU GLY LEU          
SEQRES  36 C  658  ARG SER LEU ARG GLU LEU GLY SER GLY LEU ALA LEU ILE          
SEQRES  37 C  658  HIS HIS ASN THR HIS LEU CYS PHE VAL HIS THR VAL PRO          
SEQRES  38 C  658  TRP ASP GLN LEU PHE ARG ASN PRO HIS GLN ALA LEU LEU          
SEQRES  39 C  658  HIS THR ALA ASN ARG PRO GLU ASP GLU CYS VAL GLY GLU          
SEQRES  40 C  658  GLY LEU ALA CYS HIS GLN LEU CYS ALA ARG GLY HIS CYS          
SEQRES  41 C  658  TRP GLY PRO GLY PRO THR GLN CYS VAL ASN CYS SER GLN          
SEQRES  42 C  658  PHE LEU ARG GLY GLN GLU CYS VAL GLU GLU CYS ARG VAL          
SEQRES  43 C  658  LEU GLN GLY LEU PRO ARG GLU TYR VAL ASN ALA ARG HIS          
SEQRES  44 C  658  CYS LEU PRO CYS HIS PRO GLU CYS GLN PRO GLN ASN GLY          
SEQRES  45 C  658  SER VAL THR CYS PHE GLY PRO GLU ALA ASP GLN CYS VAL          
SEQRES  46 C  658  ALA CYS ALA HIS TYR LYS ASP PRO PRO PHE CYS VAL ALA          
SEQRES  47 C  658  ARG CYS PRO SER GLY VAL LYS PRO ASP LEU SER TYR MET          
SEQRES  48 C  658  PRO ILE TRP LYS PHE PRO ASP GLU GLU GLY ALA CYS GLN          
SEQRES  49 C  658  PRO CYS PRO ILE ASN CYS THR HIS SER CYS VAL ASP LEU          
SEQRES  50 C  658  ASP ASP LYS GLY CYS PRO ALA GLU GLN ARG ALA SER PRO          
SEQRES  51 C  658  LEU THR HIS HIS HIS HIS HIS HIS                              
SEQRES   1 A  214  ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA          
SEQRES   2 A  214  SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER          
SEQRES   3 A  214  GLN ASP VAL ASN THR ALA VAL ALA TRP TYR GLN GLN LYS          
SEQRES   4 A  214  PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA ASP          
SEQRES   5 A  214  PHE LEU TYR SER GLY VAL PRO SER ARG PHE SER GLY SER          
SEQRES   6 A  214  ARG SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU          
SEQRES   7 A  214  GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN HIS          
SEQRES   8 A  214  TYR THR THR PRO PRO THR PHE GLY GLN GLY THR LYS VAL          
SEQRES   9 A  214  GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE          
SEQRES  10 A  214  PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA          
SEQRES  11 A  214  SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU          
SEQRES  12 A  214  ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER          
SEQRES  13 A  214  GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS          
SEQRES  14 A  214  ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER          
SEQRES  15 A  214  LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU          
SEQRES  16 A  214  VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER          
SEQRES  17 A  214  PHE ASN ARG GLY GLU CYS                                      
SEQRES   1 B  231  GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN          
SEQRES   2 B  231  PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY          
SEQRES   3 B  231  PHE ASN ILE ASP ASP THR TYR ILE HIS TRP VAL ARG GLN          
SEQRES   4 B  231  ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA ARG ILE TYR          
SEQRES   5 B  231  PRO THR ASN GLY TYR THR ARG TYR ALA ASP SER VAL LYS          
SEQRES   6 B  231  GLY ARG PHE THR ILE SER ALA ASP THR SER LYS ASN THR          
SEQRES   7 B  231  ALA TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR          
SEQRES   8 B  231  ALA VAL TYR TYR CYS SER ARG TRP GLY GLY ASP GLY PHE          
SEQRES   9 B  231  TYR ALA MET ASP TYR TRP GLY GLN GLY THR LEU VAL THR          
SEQRES  10 B  231  VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO          
SEQRES  11 B  231  LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA          
SEQRES  12 B  231  ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO          
SEQRES  13 B  231  VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY          
SEQRES  14 B  231  VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU          
SEQRES  15 B  231  TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SER          
SEQRES  16 B  231  LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS          
SEQRES  17 B  231  PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS          
SEQRES  18 B  231  SER CYS GLY SER HIS HIS HIS HIS HIS HIS                      
HET    NAG  C 701      14                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
FORMUL   4  NAG    C8 H15 N O6                                                  
FORMUL   5  HOH   *29(H2 O)                                                     
HELIX    1 AA1 SER C   16  GLU C   18  5                                   3    
HELIX    2 AA2 THR C   19  GLN C   29  1                                  11    
HELIX    3 AA3 LEU C   49  GLN C   53  5                                   5    
HELIX    4 AA4 LEU C   85  ASP C   88  5                                   4    
HELIX    5 AA5 TYR C  141  ILE C  145  5                                   5    
HELIX    6 AA6 LEU C  146  PHE C  151  1                                   6    
HELIX    7 AA7 HIS C  152  GLN C  156  5                                   5    
HELIX    8 AA8 SER C  186  CYS C  190  5                                   5    
HELIX    9 AA9 LEU C  209  CYS C  213  5                                   5    
HELIX   10 AB1 MET C  325  ARG C  329  5                                   5    
HELIX   11 AB2 ASN C  338  ALA C  343  5                                   6    
HELIX   12 AB3 LEU C  355  ASP C  360  5                                   6    
HELIX   13 AB4 ASP C  362  ASN C  366  5                                   5    
HELIX   14 AB5 GLU C  373  LEU C  381  5                                   9    
HELIX   15 AB6 LEU C  400  GLN C  404  5                                   5    
HELIX   16 AB7 LEU C  414  GLY C  417  5                                   4    
HELIX   17 AB8 PRO C  459  PHE C  464  1                                   6    
HELIX   18 AB9 PRO C  478  GLU C  485  1                                   8    
HELIX   19 AC1 CYS C  493  HIS C  497  5                                   5    
HELIX   20 AC2 GLN A   79  PHE A   83  5                                   5    
HELIX   21 AC3 SER A  121  LYS A  126  1                                   6    
HELIX   22 AC4 LYS A  183  LYS A  188  1                                   6    
HELIX   23 AC5 ASN B   28  THR B   32  5                                   5    
HELIX   24 AC6 ASP B   62  LYS B   65  5                                   4    
HELIX   25 AC7 ARG B   87  THR B   91  5                                   5    
HELIX   26 AC8 SER B  163  ALA B  165  5                                   3    
SHEET    1 AA1 5 VAL C   3  THR C   5  0                                        
SHEET    2 AA1 5 VAL C  33  GLN C  35  1  O  GLN C  35   N  CYS C   4           
SHEET    3 AA1 5 GLU C  57  VAL C  58  1  O  GLU C  57   N  VAL C  34           
SHEET    4 AA1 5 ILE C  79  VAL C  80  1  O  ILE C  79   N  VAL C  58           
SHEET    5 AA1 5 GLU C 125  ILE C 126  1  O  GLU C 125   N  VAL C  80           
SHEET    1 AA2 5 LEU C  38  THR C  41  0                                        
SHEET    2 AA2 5 VAL C  62  ALA C  65  1  O  LEU C  63   N  LEU C  40           
SHEET    3 AA2 5 TYR C  90  LEU C  95  1  O  ALA C  93   N  ILE C  64           
SHEET    4 AA2 5 GLY C 130  GLN C 134  1  O  LEU C 132   N  VAL C  94           
SHEET    5 AA2 5 THR C 160  ILE C 162  1  O  LEU C 161   N  ILE C 133           
SHEET    1 AA3 2 CYS C 218  CYS C 222  0                                        
SHEET    2 AA3 2 CYS C 230  CYS C 233 -1  O  ALA C 232   N  ALA C 219           
SHEET    1 AA4 2 PHE C 236  HIS C 238  0                                        
SHEET    2 AA4 2 ILE C 241  GLU C 243 -1  O  ILE C 241   N  HIS C 238           
SHEET    1 AA5 2 VAL C 250  TYR C 252  0                                        
SHEET    2 AA5 2 SER C 259  PRO C 261 -1  O  MET C 260   N  THR C 251           
SHEET    1 AA6 2 TYR C 267  PHE C 269  0                                        
SHEET    2 AA6 2 SER C 272  VAL C 274 -1  O  VAL C 274   N  TYR C 267           
SHEET    1 AA7 4 CYS C 289  THR C 290  0                                        
SHEET    2 AA7 4 LEU C 282  THR C 284 -1  N  LEU C 282   O  THR C 290           
SHEET    3 AA7 4 GLN C 307  LYS C 311  1  O  CYS C 309   N  SER C 283           
SHEET    4 AA7 4 ASN C 297  THR C 301 -1  N  GLN C 298   O  GLU C 310           
SHEET    1 AA8 5 CYS C 320  TYR C 321  0                                        
SHEET    2 AA8 5 LYS C 347  PHE C 349  1  O  PHE C 349   N  CYS C 320           
SHEET    3 AA8 5 GLU C 383  ILE C 384  1  O  GLU C 383   N  ILE C 348           
SHEET    4 AA8 5 VAL C 408  ILE C 409  1  O  VAL C 408   N  ILE C 384           
SHEET    5 AA8 5 GLU C 438  LEU C 439  1  O  GLU C 438   N  ILE C 409           
SHEET    1 AA9 5 LEU C 352  PHE C 354  0                                        
SHEET    2 AA9 5 LEU C 388  ILE C 390  1  O  TYR C 389   N  LEU C 352           
SHEET    3 AA9 5 TYR C 419  GLN C 424  1  O  THR C 422   N  ILE C 390           
SHEET    4 AA9 5 LEU C 443  HIS C 447  1  O  LEU C 445   N  LEU C 421           
SHEET    5 AA9 5 LEU C 471  THR C 474  1  O  LEU C 472   N  ALA C 444           
SHEET    1 AB1 4 GLU C 517  VAL C 519  0                                        
SHEET    2 AB1 4 PHE C 512  ARG C 514 -1  N  ARG C 514   O  GLU C 517           
SHEET    3 AB1 4 HIS C 537  PRO C 540  1  O  CYS C 538   N  LEU C 513           
SHEET    4 AB1 4 GLU C 531  ASN C 534 -1  N  TYR C 532   O  LEU C 539           
SHEET    1 AB2 2 TYR C 568  ASP C 570  0                                        
SHEET    2 AB2 2 PHE C 573  VAL C 575 -1  O  PHE C 573   N  ASP C 570           
SHEET    1 AB3 2 LYS C 593  PRO C 595  0                                        
SHEET    2 AB3 2 CYS C 601  PRO C 603 -1  O  GLN C 602   N  PHE C 594           
SHEET    1 AB4 4 MET A   4  SER A   7  0                                        
SHEET    2 AB4 4 VAL A  19  ALA A  25 -1  O  THR A  22   N  SER A   7           
SHEET    3 AB4 4 ASP A  70  ILE A  75 -1  O  LEU A  73   N  ILE A  21           
SHEET    4 AB4 4 PHE A  62  SER A  67 -1  N  SER A  63   O  THR A  74           
SHEET    1 AB5 6 SER A  10  SER A  14  0                                        
SHEET    2 AB5 6 THR A 102  LYS A 107  1  O  LYS A 103   N  LEU A  11           
SHEET    3 AB5 6 ALA A  84  GLN A  90 -1  N  ALA A  84   O  VAL A 104           
SHEET    4 AB5 6 VAL A  33  GLN A  38 -1  N  GLN A  38   O  THR A  85           
SHEET    5 AB5 6 LYS A  45  TYR A  49 -1  O  LYS A  45   N  GLN A  37           
SHEET    6 AB5 6 PHE A  53  LEU A  54 -1  O  PHE A  53   N  TYR A  49           
SHEET    1 AB6 4 SER A  10  SER A  14  0                                        
SHEET    2 AB6 4 THR A 102  LYS A 107  1  O  LYS A 103   N  LEU A  11           
SHEET    3 AB6 4 ALA A  84  GLN A  90 -1  N  ALA A  84   O  VAL A 104           
SHEET    4 AB6 4 THR A  97  PHE A  98 -1  O  THR A  97   N  GLN A  90           
SHEET    1 AB7 4 SER A 114  PHE A 118  0                                        
SHEET    2 AB7 4 THR A 129  PHE A 139 -1  O  VAL A 133   N  PHE A 118           
SHEET    3 AB7 4 TYR A 173  SER A 182 -1  O  LEU A 181   N  ALA A 130           
SHEET    4 AB7 4 SER A 159  VAL A 163 -1  N  SER A 162   O  SER A 176           
SHEET    1 AB8 3 LYS A 145  VAL A 150  0                                        
SHEET    2 AB8 3 VAL A 191  THR A 197 -1  O  GLU A 195   N  GLN A 147           
SHEET    3 AB8 3 VAL A 205  ASN A 210 -1  O  LYS A 207   N  CYS A 194           
SHEET    1 AB9 4 GLN B   3  SER B   7  0                                        
SHEET    2 AB9 4 LEU B  18  SER B  25 -1  O  ALA B  23   N  VAL B   5           
SHEET    3 AB9 4 THR B  78  MET B  83 -1  O  MET B  83   N  LEU B  18           
SHEET    4 AB9 4 PHE B  68  ASP B  73 -1  N  THR B  69   O  GLN B  82           
SHEET    1 AC1 6 GLY B  10  VAL B  12  0                                        
SHEET    2 AC1 6 THR B 114  VAL B 118  1  O  THR B 117   N  GLY B  10           
SHEET    3 AC1 6 ALA B  92  ARG B  98 -1  N  ALA B  92   O  VAL B 116           
SHEET    4 AC1 6 ILE B  34  GLN B  39 -1  N  VAL B  37   O  TYR B  95           
SHEET    5 AC1 6 GLU B  46  ILE B  51 -1  O  GLU B  46   N  ARG B  38           
SHEET    6 AC1 6 THR B  58  TYR B  60 -1  O  ARG B  59   N  ARG B  50           
SHEET    1 AC2 4 GLY B  10  VAL B  12  0                                        
SHEET    2 AC2 4 THR B 114  VAL B 118  1  O  THR B 117   N  GLY B  10           
SHEET    3 AC2 4 ALA B  92  ARG B  98 -1  N  ALA B  92   O  VAL B 116           
SHEET    4 AC2 4 TYR B 109  TRP B 110 -1  O  TYR B 109   N  ARG B  98           
SHEET    1 AC3 4 SER B 127  LEU B 131  0                                        
SHEET    2 AC3 4 ALA B 143  TYR B 152 -1  O  GLY B 146   N  LEU B 131           
SHEET    3 AC3 4 TYR B 183  VAL B 191 -1  O  SER B 187   N  CYS B 147           
SHEET    4 AC3 4 VAL B 170  THR B 172 -1  N  HIS B 171   O  VAL B 188           
SHEET    1 AC4 4 SER B 127  LEU B 131  0                                        
SHEET    2 AC4 4 ALA B 143  TYR B 152 -1  O  GLY B 146   N  LEU B 131           
SHEET    3 AC4 4 TYR B 183  VAL B 191 -1  O  SER B 187   N  CYS B 147           
SHEET    4 AC4 4 VAL B 176  LEU B 177 -1  N  VAL B 176   O  SER B 184           
SHEET    1 AC5 3 THR B 158  TRP B 161  0                                        
SHEET    2 AC5 3 ILE B 202  HIS B 207 -1  O  ASN B 204   N  SER B 160           
SHEET    3 AC5 3 THR B 212  LYS B 217 -1  O  VAL B 214   N  VAL B 205           
SSBOND   1 CYS C    4    CYS C   31                          1555   1555  2.03  
SSBOND   2 CYS C  140    CYS C  170                          1555   1555  2.03  
SSBOND   3 CYS C  173    CYS C  182                          1555   1555  2.04  
SSBOND   4 CYS C  177    CYS C  190                          1555   1555  2.03  
SSBOND   5 CYS C  198    CYS C  205                          1555   1555  2.03  
SSBOND   6 CYS C  202    CYS C  213                          1555   1555  2.03  
SSBOND   7 CYS C  214    CYS C  222                          1555   1555  2.03  
SSBOND   8 CYS C  218    CYS C  230                          1555   1555  2.03  
SSBOND   9 CYS C  233    CYS C  242                          1555   1555  2.04  
SSBOND  10 CYS C  246    CYS C  273                          1555   1555  2.03  
SSBOND  11 CYS C  277    CYS C  289                          1555   1555  2.03  
SSBOND  12 CYS C  293    CYS C  309                          1555   1555  2.03  
SSBOND  13 CYS C  312    CYS C  316                          1555   1555  2.03  
SSBOND  14 CYS C  320    CYS C  345                          1555   1555  2.03  
SSBOND  15 CYS C  453    CYS C  482                          1555   1555  2.03  
SSBOND  16 CYS C  489    CYS C  498                          1555   1555  2.03  
SSBOND  17 CYS C  493    CYS C  506                          1555   1555  2.03  
SSBOND  18 CYS C  509    CYS C  518                          1555   1555  2.03  
SSBOND  19 CYS C  522    CYS C  538                          1555   1555  2.03  
SSBOND  20 CYS C  541    CYS C  554                          1555   1555  2.03  
SSBOND  21 CYS C  545    CYS C  562                          1555   1555  2.03  
SSBOND  22 CYS C  565    CYS C  574                          1555   1555  2.03  
SSBOND  23 CYS C  578    CYS C  601                          1555   1555  2.03  
SSBOND  24 CYS A   23    CYS A   88                          1555   1555  2.03  
SSBOND  25 CYS A  134    CYS A  194                          1555   1555  2.01  
SSBOND  26 CYS B   22    CYS B   96                          1555   1555  2.03  
SSBOND  27 CYS B  147    CYS B  203                          1555   1555  2.03  
LINK         ND2 ASN C 237                 C1  NAG C 701     1555   1555  1.48  
CISPEP   1 LEU C  528    PRO C  529          0        -0.41                     
CISPEP   2 PRO C  571    PRO C  572          0         6.92                     
CISPEP   3 SER A    7    PRO A    8          0        -0.94                     
CISPEP   4 THR A   94    PRO A   95          0         8.25                     
CISPEP   5 TYR A  140    PRO A  141          0         4.95                     
CISPEP   6 PHE B  153    PRO B  154          0        -7.35                     
CISPEP   7 GLU B  155    PRO B  156          0         3.63                     
SITE     1 AC1  3 CYS C 230  ASN C 237  GLY C 240                               
CRYST1   62.860  114.460  204.279  90.00  90.00  90.00 P 21 21 21    4          
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      0.015908  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008737  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004895        0.00000                         
ATOM      1  N   THR C   1     -16.080  31.366 -40.941  1.00103.37           N  
ANISOU    1  N   THR C   1    12741  13145  13391    220     35    337       N  
ATOM      2  CA  THR C   1     -15.471  31.622 -42.241  1.00 99.26           C  
ANISOU    2  CA  THR C   1    12233  12550  12932    174      1    323       C  
ATOM      3  C   THR C   1     -16.326  32.552 -43.095  1.00 91.82           C  
ANISOU    3  C   THR C   1    11258  11602  12029    187      7    334       C  
ATOM      4  O   THR C   1     -17.534  32.356 -43.221  1.00 97.40           O  
ANISOU    4  O   THR C   1    11918  12360  12729    189     32    384       O  
ATOM      5  CB  THR C   1     -15.235  30.312 -43.020  1.00 97.97           C  
ANISOU    5  CB  THR C   1    12067  12372  12786     96    -15    367       C  
ATOM      6  OG1 THR C   1     -14.966  30.614 -44.396  1.00 97.87           O  
ANISOU    6  OG1 THR C   1    12050  12311  12824     58    -41    363       O  
ATOM      7  CG2 THR C   1     -16.453  29.400 -42.931  1.00 95.19           C  
ANISOU    7  CG2 THR C   1    11668  12078  12421     72     12    442       C  
ATOM      8  N   GLN C   2     -15.696  33.569 -43.681  1.00 78.35           N  
ANISOU    8  N   GLN C   2     9573   9831  10364    196    -18    292       N  
ATOM      9  CA  GLN C   2     -16.405  34.423 -44.624  1.00 63.82           C  
ANISOU    9  CA  GLN C   2     7705   7976   8566    204    -19    311       C  
ATOM     10  C   GLN C   2     -15.546  34.693 -45.853  1.00 54.50           C  
ANISOU   10  C   GLN C   2     6542   6729   7435    157    -51    309       C  
ATOM     11  O   GLN C   2     -16.074  34.899 -46.950  1.00 50.78           O  
ANISOU   11  O   GLN C   2     6045   6256   6992    137    -54    348       O  
ATOM     12  CB  GLN C   2     -16.840  35.735 -43.960  1.00 62.31           C  
ANISOU   12  CB  GLN C   2     7514   7782   8379    286    -10    270       C  
ATOM     13  CG  GLN C   2     -15.816  36.850 -43.890  1.00 64.60           C  
ANISOU   13  CG  GLN C   2     7846   7992   8709    310    -40    204       C  
ATOM     14  CD  GLN C   2     -16.486  38.211 -43.790  1.00 76.19           C  
ANISOU   14  CD  GLN C   2     9303   9438  10208    381    -40    179       C  
ATOM     15  OE1 GLN C   2     -16.571  38.798 -42.712  1.00 86.33           O  
ANISOU   15  OE1 GLN C   2    10597  10733  11472    451    -36    121       O  
ATOM     16  NE2 GLN C   2     -16.973  38.715 -44.920  1.00 67.97           N  
ANISOU   16  NE2 GLN C   2     8241   8370   9214    368    -46    221       N  
ATOM     17  N   VAL C   3     -14.226  34.668 -45.688  1.00 49.34           N  
ANISOU   17  N   VAL C   3     5929   6030   6788    139    -74    265       N  
ATOM     18  CA  VAL C   3     -13.287  34.968 -46.762  1.00 47.96           C  
ANISOU   18  CA  VAL C   3     5767   5800   6656     97   -101    261       C  
ATOM     19  C   VAL C   3     -12.513  33.705 -47.112  1.00 51.10           C  
ANISOU   19  C   VAL C   3     6174   6206   7037     38   -114    267       C  
ATOM     20  O   VAL C   3     -12.115  32.938 -46.228  1.00 66.24           O  
ANISOU   20  O   VAL C   3     8110   8140   8920     40   -114    247       O  
ATOM     21  CB  VAL C   3     -12.335  36.117 -46.370  1.00 41.06           C  
ANISOU   21  CB  VAL C   3     4925   4861   5815    124   -120    202       C  
ATOM     22  CG1 VAL C   3     -11.246  36.301 -47.416  1.00 39.14           C  
ANISOU   22  CG1 VAL C   3     4690   4569   5612     71   -144    205       C  
ATOM     23  CG2 VAL C   3     -13.120  37.407 -46.195  1.00 26.79           C  
ANISOU   23  CG2 VAL C   3     3109   3033   4038    182   -114    195       C  
ATOM     24  N   CYS C   4     -12.315  33.487 -48.410  1.00 38.22           N  
ANISOU   24  N   CYS C   4     4529   4568   5426     -8   -128    296       N  
ATOM     25  CA  CYS C   4     -11.555  32.354 -48.914  1.00 35.83           C  
ANISOU   25  CA  CYS C   4     4232   4271   5111    -59   -146    294       C  
ATOM     26  C   CYS C   4     -10.853  32.784 -50.191  1.00 39.81           C  
ANISOU   26  C   CYS C   4     4730   4753   5643    -90   -163    299       C  
ATOM     27  O   CYS C   4     -11.341  33.658 -50.914  1.00 46.48           O  
ANISOU   27  O   CYS C   4     5557   5592   6512    -83   -158    330       O  
ATOM     28  CB  CYS C   4     -12.457  31.143 -49.188  1.00 33.43           C  
ANISOU   28  CB  CYS C   4     3901   4013   4788    -85   -141    334       C  
ATOM     29  SG  CYS C   4     -13.601  31.362 -50.582  1.00 49.56           S  
ANISOU   29  SG  CYS C   4     5897   6087   6848   -101   -139    388       S  
ATOM     30  N   THR C   5      -9.697  32.183 -50.459  1.00 48.43           N  
ANISOU   30  N   THR C   5     5836   5837   6730   -122   -182    273       N  
ATOM     31  CA  THR C   5      -9.056  32.436 -51.737  1.00 54.84           C  
ANISOU   31  CA  THR C   5     6634   6646   7557   -154   -194    284       C  
ATOM     32  C   THR C   5      -9.761  31.642 -52.832  1.00 62.60           C  
ANISOU   32  C   THR C   5     7586   7676   8524   -180   -199    321       C  
ATOM     33  O   THR C   5     -10.559  30.741 -52.569  1.00 61.60           O  
ANISOU   33  O   THR C   5     7451   7575   8380   -182   -198    331       O  
ATOM     34  CB  THR C   5      -7.570  32.082 -51.692  1.00 52.43           C  
ANISOU   34  CB  THR C   5     6346   6326   7250   -176   -213    240       C  
ATOM     35  OG1 THR C   5      -7.411  30.680 -51.444  1.00 57.55           O  
ANISOU   35  OG1 THR C   5     7002   6997   7869   -188   -225    221       O  
ATOM     36  CG2 THR C   5      -6.865  32.873 -50.601  1.00 51.26           C  
ANISOU   36  CG2 THR C   5     6225   6132   7120   -151   -214    197       C  
ATOM     37  N   GLY C   6      -9.467  31.992 -54.074  1.00 58.21           N  
ANISOU   37  N   GLY C   6     7010   7134   7972   -199   -205    342       N  
ATOM     38  CA  GLY C   6     -10.031  31.317 -55.220  1.00 49.05           C  
ANISOU   38  CA  GLY C   6     5820   6026   6793   -219   -215    368       C  
ATOM     39  C   GLY C   6      -9.110  30.243 -55.754  1.00 43.25           C  
ANISOU   39  C   GLY C   6     5085   5314   6035   -248   -238    333       C  
ATOM     40  O   GLY C   6      -8.342  29.621 -55.011  1.00 49.50           O  
ANISOU   40  O   GLY C   6     5900   6084   6824   -251   -247    291       O  
ATOM     41  N   THR C   7      -9.195  30.010 -57.062  1.00 36.68           N  
ANISOU   41  N   THR C   7     4223   4529   5184   -263   -250    349       N  
ATOM     42  CA  THR C   7      -8.228  29.152 -57.736  1.00 36.35           C  
ANISOU   42  CA  THR C   7     4176   4518   5119   -282   -272    311       C  
ATOM     43  C   THR C   7      -7.624  29.876 -58.927  1.00 41.30           C  
ANISOU   43  C   THR C   7     4779   5183   5730   -289   -267    335       C  
ATOM     44  O   THR C   7      -7.895  31.061 -59.148  1.00 34.51           O  
ANISOU   44  O   THR C   7     3912   4314   4886   -281   -248    385       O  
ATOM     45  CB  THR C   7      -8.861  27.837 -58.197  1.00 35.64           C  
ANISOU   45  CB  THR C   7     4070   4462   5011   -293   -299    292       C  
ATOM     46  OG1 THR C   7     -10.005  28.107 -59.018  1.00 43.10           O  
ANISOU   46  OG1 THR C   7     4981   5446   5948   -290   -298    334       O  
ATOM     47  CG2 THR C   7      -9.266  27.002 -57.013  1.00 26.34           C  
ANISOU   47  CG2 THR C   7     2914   3244   3850   -293   -304    275       C  
ATOM     48  N   ASP C   8      -6.816  29.161 -59.703  1.00 46.04           N  
ANISOU   48  N   ASP C   8     5365   5829   6299   -300   -285    302       N  
ATOM     49  CA  ASP C   8      -6.115  29.748 -60.835  1.00 48.36           C  
ANISOU   49  CA  ASP C   8     5631   6174   6569   -307   -277    326       C  
ATOM     50  C   ASP C   8      -5.736  28.645 -61.814  1.00 47.43           C  
ANISOU   50  C   ASP C   8     5489   6129   6403   -308   -303    283       C  
ATOM     51  O   ASP C   8      -4.582  28.546 -62.242  1.00 57.72           O  
ANISOU   51  O   ASP C   8     6780   7466   7684   -313   -303    258       O  
ATOM     52  CB  ASP C   8      -4.882  30.515 -60.352  1.00 52.76           C  
ANISOU   52  CB  ASP C   8     6201   6696   7151   -316   -260    322       C  
ATOM     53  CG  ASP C   8      -4.432  31.580 -61.331  1.00 66.91           C  
ANISOU   53  CG  ASP C   8     7964   8523   8937   -327   -241    381       C  
ATOM     54  OD1 ASP C   8      -4.273  31.265 -62.529  1.00 67.72           O  
ANISOU   54  OD1 ASP C   8     8033   8707   8991   -329   -245    391       O  
ATOM     55  OD2 ASP C   8      -4.230  32.733 -60.898  1.00 77.64           O  
ANISOU   55  OD2 ASP C   8     9332   9826  10340   -333   -223    417       O  
ATOM     56  N   MET C   9      -6.702  27.797 -62.153  1.00 40.59           N  
ANISOU   56  N   MET C   9     4613   5287   5523   -303   -327    268       N  
ATOM     57  CA  MET C   9      -6.499  26.705 -63.093  1.00 45.70           C  
ANISOU   57  CA  MET C   9     5237   6000   6129   -300   -360    217       C  
ATOM     58  C   MET C   9      -7.031  27.031 -64.479  1.00 47.33           C  
ANISOU   58  C   MET C   9     5402   6294   6289   -291   -363    252       C  
ATOM     59  O   MET C   9      -6.760  26.282 -65.423  1.00 40.88           O  
ANISOU   59  O   MET C   9     4559   5548   5426   -281   -389    207       O  
ATOM     60  CB  MET C   9      -7.165  25.426 -62.569  1.00 44.26           C  
ANISOU   60  CB  MET C   9     5068   5781   5967   -303   -395    169       C  
ATOM     61  CG  MET C   9      -8.678  25.529 -62.420  1.00 53.50           C  
ANISOU   61  CG  MET C   9     6230   6938   7158   -307   -395    210       C  
ATOM     62  SD  MET C   9      -9.408  24.117 -61.565  1.00 56.88           S  
ANISOU   62  SD  MET C   9     6675   7310   7628   -322   -429    170       S  
ATOM     63  CE  MET C   9      -9.299  24.661 -59.863  1.00 54.04           C  
ANISOU   63  CE  MET C   9     6358   6867   7308   -322   -392    200       C  
ATOM     64  N   LYS C  10      -7.762  28.137 -64.617  1.00 47.54           N  
ANISOU   64  N   LYS C  10     5420   6319   6324   -288   -338    328       N  
ATOM     65  CA  LYS C  10      -8.445  28.511 -65.849  1.00 47.17           C  
ANISOU   65  CA  LYS C  10     5335   6354   6235   -275   -342    372       C  
ATOM     66  C   LYS C  10      -9.135  27.296 -66.460  1.00 45.74           C  
ANISOU   66  C   LYS C  10     5132   6223   6026   -268   -386    316       C  
ATOM     67  O   LYS C  10      -9.981  26.678 -65.807  1.00 47.80           O  
ANISOU   67  O   LYS C  10     5403   6436   6324   -276   -405    294       O  
ATOM     68  CB  LYS C  10      -7.467  29.181 -66.816  1.00 46.91           C  
ANISOU   68  CB  LYS C  10     5277   6391   6156   -272   -322    407       C  
ATOM     69  CG  LYS C  10      -6.719  30.340 -66.154  1.00 52.19           C  
ANISOU   69  CG  LYS C  10     5967   6997   6868   -287   -283    457       C  
ATOM     70  CD  LYS C  10      -6.251  31.408 -67.133  1.00 54.09           C  
ANISOU   70  CD  LYS C  10     6177   7296   7079   -288   -257    536       C  
ATOM     71  CE  LYS C  10      -6.035  32.737 -66.406  1.00 60.20           C  
ANISOU   71  CE  LYS C  10     6973   7981   7920   -303   -226    601       C  
ATOM     72  NZ  LYS C  10      -6.597  33.903 -67.148  1.00 66.40           N  
ANISOU   72  NZ  LYS C  10     7740   8787   8703   -296   -209    704       N  
ATOM     73  N   LEU C  11      -8.783  26.919 -67.687  1.00 37.78           N  
ANISOU   73  N   LEU C  11     4090   5313   4953   -254   -406    291       N  
ATOM     74  CA  LEU C  11      -9.457  25.811 -68.355  1.00 35.72           C  
ANISOU   74  CA  LEU C  11     3805   5102   4667   -244   -455    230       C  
ATOM     75  C   LEU C  11      -8.629  24.530 -68.368  1.00 45.84           C  
ANISOU   75  C   LEU C  11     5093   6386   5940   -241   -491    128       C  
ATOM     76  O   LEU C  11      -8.906  23.630 -69.169  1.00 48.58           O  
ANISOU   76  O   LEU C  11     5414   6790   6254   -227   -537     66       O  
ATOM     77  CB  LEU C  11      -9.847  26.206 -69.780  1.00 32.09           C  
ANISOU   77  CB  LEU C  11     3298   4761   4135   -219   -463    262       C  
ATOM     78  CG  LEU C  11     -10.784  27.413 -69.824  1.00 39.01           C  
ANISOU   78  CG  LEU C  11     4166   5633   5022   -216   -435    362       C  
ATOM     79  CD1 LEU C  11     -11.066  27.846 -71.256  1.00 40.18           C  
ANISOU   79  CD1 LEU C  11     4270   5906   5092   -187   -441    403       C  
ATOM     80  CD2 LEU C  11     -12.067  27.097 -69.082  1.00 31.26           C  
ANISOU   80  CD2 LEU C  11     3192   4587   4099   -227   -452    358       C  
ATOM     81  N   ARG C  12      -7.638  24.418 -67.492  1.00 51.94           N  
ANISOU   81  N   ARG C  12     5897   7095   6742   -252   -476    107       N  
ATOM     82  CA  ARG C  12      -6.841  23.205 -67.418  1.00 50.89           C  
ANISOU   82  CA  ARG C  12     5773   6954   6607   -244   -512     11       C  
ATOM     83  C   ARG C  12      -7.591  22.115 -66.661  1.00 58.31           C  
ANISOU   83  C   ARG C  12     6736   7811   7607   -259   -552    -33       C  
ATOM     84  O   ARG C  12      -8.346  22.383 -65.721  1.00 59.26           O  
ANISOU   84  O   ARG C  12     6878   7858   7779   -281   -536     13       O  
ATOM     85  CB  ARG C  12      -5.492  23.495 -66.756  1.00 43.92           C  
ANISOU   85  CB  ARG C  12     4914   6040   5735   -247   -483      6       C  
ATOM     86  CG  ARG C  12      -4.532  24.256 -67.664  1.00 41.81           C  
ANISOU   86  CG  ARG C  12     4614   5867   5405   -234   -453     33       C  
ATOM     87  CD  ARG C  12      -3.253  24.664 -66.948  1.00 34.88           C  
ANISOU   87  CD  ARG C  12     3753   4953   4547   -244   -422     35       C  
ATOM     88  NE  ARG C  12      -3.325  26.040 -66.464  1.00 44.88           N  
ANISOU   88  NE  ARG C  12     5030   6178   5845   -266   -375    127       N  
ATOM     89  CZ  ARG C  12      -3.283  26.384 -65.181  1.00 41.25           C  
ANISOU   89  CZ  ARG C  12     4609   5616   5447   -284   -361    141       C  
ATOM     90  NH1 ARG C  12      -3.156  25.452 -64.248  1.00 41.82           N  
ANISOU   90  NH1 ARG C  12     4713   5623   5552   -282   -387     79       N  
ATOM     91  NH2 ARG C  12      -3.360  27.662 -64.832  1.00 35.27           N  
ANISOU   91  NH2 ARG C  12     3858   4823   4719   -299   -324    216       N  
ATOM     92  N   LEU C  13      -7.386  20.871 -67.095  1.00 59.02           N  
ANISOU   92  N   LEU C  13     6819   7916   7690   -247   -605   -124       N  
ATOM     93  CA  LEU C  13      -8.105  19.747 -66.514  1.00 55.04           C  
ANISOU   93  CA  LEU C  13     6331   7332   7248   -265   -651   -165       C  
ATOM     94  C   LEU C  13      -7.533  19.407 -65.140  1.00 48.40           C  
ANISOU   94  C   LEU C  13     5538   6387   6463   -279   -641   -167       C  
ATOM     95  O   LEU C  13      -6.318  19.475 -64.939  1.00 47.35           O  
ANISOU   95  O   LEU C  13     5420   6255   6313   -264   -628   -191       O  
ATOM     96  CB  LEU C  13      -8.024  18.518 -67.421  1.00 63.80           C  
ANISOU   96  CB  LEU C  13     7419   8480   8341   -245   -719   -267       C  
ATOM     97  CG  LEU C  13      -8.527  18.620 -68.865  1.00 72.10           C  
ANISOU   97  CG  LEU C  13     8420   9647   9327   -222   -743   -288       C  
ATOM     98  CD1 LEU C  13      -7.436  19.124 -69.803  1.00 80.45           C  
ANISOU   98  CD1 LEU C  13     9454  10818  10295   -183   -721   -301       C  
ATOM     99  CD2 LEU C  13      -9.069  17.279 -69.337  1.00 68.23           C  
ANISOU   99  CD2 LEU C  13     7915   9147   8862   -218   -822   -383       C  
ATOM    100  N   PRO C  14      -8.382  19.041 -64.183  1.00 50.98           N  
ANISOU  100  N   PRO C  14     5885   6630   6854   -308   -647   -141       N  
ATOM    101  CA  PRO C  14      -7.873  18.618 -62.873  1.00 50.88           C  
ANISOU  101  CA  PRO C  14     5918   6525   6889   -317   -641   -142       C  
ATOM    102  C   PRO C  14      -7.072  17.331 -63.003  1.00 53.29           C  
ANISOU  102  C   PRO C  14     6236   6805   7206   -302   -696   -232       C  
ATOM    103  O   PRO C  14      -7.493  16.381 -63.667  1.00 55.49           O  
ANISOU  103  O   PRO C  14     6497   7087   7498   -302   -752   -289       O  
ATOM    104  CB  PRO C  14      -9.147  18.412 -62.042  1.00 50.09           C  
ANISOU  104  CB  PRO C  14     5824   6362   6846   -350   -639    -90       C  
ATOM    105  CG  PRO C  14     -10.246  19.084 -62.818  1.00 40.88           C  
ANISOU  105  CG  PRO C  14     4616   5257   5658   -356   -628    -49       C  
ATOM    106  CD  PRO C  14      -9.851  18.984 -64.251  1.00 41.43           C  
ANISOU  106  CD  PRO C  14     4655   5415   5674   -331   -657   -105       C  
ATOM    107  N   ALA C  15      -5.901  17.309 -62.368  1.00 54.96           N  
ANISOU  107  N   ALA C  15     6478   6989   7417   -286   -684   -250       N  
ATOM    108  CA  ALA C  15      -5.054  16.124 -62.419  1.00 45.86           C  
ANISOU  108  CA  ALA C  15     5339   5808   6277   -264   -736   -336       C  
ATOM    109  C   ALA C  15      -5.654  14.954 -61.654  1.00 42.83           C  
ANISOU  109  C   ALA C  15     4983   5322   5969   -285   -780   -344       C  
ATOM    110  O   ALA C  15      -5.327  13.800 -61.951  1.00 47.96           O  
ANISOU  110  O   ALA C  15     5637   5942   6643   -270   -840   -420       O  
ATOM    111  CB  ALA C  15      -3.664  16.445 -61.869  1.00 40.35           C  
ANISOU  111  CB  ALA C  15     4663   5109   5560   -241   -712   -348       C  
ATOM    112  N   SER C  16      -6.525  15.226 -60.681  1.00 39.06           N  
ANISOU  112  N   SER C  16     4521   4790   5530   -319   -751   -264       N  
ATOM    113  CA  SER C  16      -7.179  14.201 -59.873  1.00 40.65           C  
ANISOU  113  CA  SER C  16     4744   4897   5804   -347   -784   -249       C  
ATOM    114  C   SER C  16      -8.686  14.412 -59.967  1.00 42.98           C  
ANISOU  114  C   SER C  16     5009   5196   6124   -386   -774   -191       C  
ATOM    115  O   SER C  16      -9.309  14.935 -59.031  1.00 51.26           O  
ANISOU  115  O   SER C  16     6067   6223   7187   -408   -729   -110       O  
ATOM    116  CB  SER C  16      -6.698  14.250 -58.424  1.00 37.63           C  
ANISOU  116  CB  SER C  16     4406   4451   5441   -347   -756   -203       C  
ATOM    117  OG  SER C  16      -7.479  13.407 -57.597  1.00 43.36           O  
ANISOU  117  OG  SER C  16     5148   5095   6232   -379   -775   -163       O  
ATOM    118  N   PRO C  17      -9.306  14.010 -61.081  1.00 45.58           N  
ANISOU  118  N   PRO C  17     5301   5561   6456   -393   -816   -234       N  
ATOM    119  CA  PRO C  17     -10.755  14.227 -61.232  1.00 46.22           C  
ANISOU  119  CA  PRO C  17     5347   5655   6561   -429   -810   -181       C  
ATOM    120  C   PRO C  17     -11.571  13.571 -60.136  1.00 45.59           C  
ANISOU  120  C   PRO C  17     5279   5487   6557   -473   -814   -125       C  
ATOM    121  O   PRO C  17     -12.684  14.023 -59.840  1.00 45.20           O  
ANISOU  121  O   PRO C  17     5204   5448   6521   -502   -784    -55       O  
ATOM    122  CB  PRO C  17     -11.064  13.612 -62.605  1.00 42.64           C  
ANISOU  122  CB  PRO C  17     4855   5245   6103   -423   -874   -262       C  
ATOM    123  CG  PRO C  17      -9.734  13.477 -63.291  1.00 47.80           C  
ANISOU  123  CG  PRO C  17     5517   5939   6704   -375   -893   -345       C  
ATOM    124  CD  PRO C  17      -8.738  13.249 -62.204  1.00 45.29           C  
ANISOU  124  CD  PRO C  17     5250   5553   6406   -365   -878   -338       C  
ATOM    125  N   GLU C  18     -11.037  12.519 -59.514  1.00 42.38           N  
ANISOU  125  N   GLU C  18     4907   4995   6201   -478   -850   -148       N  
ATOM    126  CA  GLU C  18     -11.739  11.853 -58.427  1.00 44.63           C  
ANISOU  126  CA  GLU C  18     5204   5196   6558   -521   -852    -83       C  
ATOM    127  C   GLU C  18     -11.853  12.732 -57.182  1.00 42.82           C  
ANISOU  127  C   GLU C  18     4994   4971   6305   -522   -776     12       C  
ATOM    128  O   GLU C  18     -12.748  12.501 -56.361  1.00 49.18           O  
ANISOU  128  O   GLU C  18     5793   5742   7153   -559   -759     86       O  
ATOM    129  CB  GLU C  18     -11.033  10.536 -58.087  1.00 54.09           C  
ANISOU  129  CB  GLU C  18     6438   6299   7813   -519   -912   -128       C  
ATOM    130  CG  GLU C  18     -10.548   9.743 -59.306  1.00 67.75           C  
ANISOU  130  CG  GLU C  18     8158   8029   9553   -496   -989   -246       C  
ATOM    131  CD  GLU C  18      -9.120  10.086 -59.704  1.00 82.44           C  
ANISOU  131  CD  GLU C  18    10041   9939  11345   -434   -984   -316       C  
ATOM    132  OE1 GLU C  18      -8.532  11.000 -59.089  1.00 81.35           O  
ANISOU  132  OE1 GLU C  18     9922   9832  11154   -415   -922   -272       O  
ATOM    133  OE2 GLU C  18      -8.586   9.442 -60.631  1.00 88.45           O  
ANISOU  133  OE2 GLU C  18    10794  10708  12104   -405  -1043   -417       O  
ATOM    134  N   THR C  19     -10.980  13.738 -57.027  1.00 33.88           N  
ANISOU  134  N   THR C  19     3882   3884   5106   -481   -731      9       N  
ATOM    135  CA  THR C  19     -10.984  14.607 -55.855  1.00 40.29           C  
ANISOU  135  CA  THR C  19     4715   4701   5892   -474   -665     82       C  
ATOM    136  C   THR C  19     -11.178  16.081 -56.188  1.00 38.87           C  
ANISOU  136  C   THR C  19     4515   4598   5655   -455   -611    104       C  
ATOM    137  O   THR C  19     -10.980  16.940 -55.309  1.00 53.22           O  
ANISOU  137  O   THR C  19     6352   6424   7446   -438   -560    146       O  
ATOM    138  CB  THR C  19      -9.688  14.442 -55.050  1.00 45.56           C  
ANISOU  138  CB  THR C  19     5433   5332   6545   -443   -663     63       C  
ATOM    139  OG1 THR C  19      -8.558  14.595 -55.916  1.00 50.54           O  
ANISOU  139  OG1 THR C  19     6067   5995   7139   -409   -683    -16       O  
ATOM    140  CG2 THR C  19      -9.640  13.066 -54.415  1.00 38.36           C  
ANISOU  140  CG2 THR C  19     4547   4334   5695   -461   -707     69       C  
ATOM    141  N   HIS C  20     -11.576  16.397 -57.421  1.00 30.03           N  
ANISOU  141  N   HIS C  20     3356   3535   4518   -456   -624     78       N  
ATOM    142  CA  HIS C  20     -11.746  17.788 -57.825  1.00 34.36           C  
ANISOU  142  CA  HIS C  20     3886   4152   5017   -436   -578    104       C  
ATOM    143  C   HIS C  20     -12.917  18.434 -57.088  1.00 43.39           C  
ANISOU  143  C   HIS C  20     5012   5301   6171   -450   -533    184       C  
ATOM    144  O   HIS C  20     -12.787  19.535 -56.533  1.00 41.40           O  
ANISOU  144  O   HIS C  20     4774   5067   5892   -428   -483    220       O  
ATOM    145  CB  HIS C  20     -11.922  17.861 -59.349  1.00 36.43           C  
ANISOU  145  CB  HIS C  20     4109   4479   5254   -431   -608     61       C  
ATOM    146  CG  HIS C  20     -12.132  19.247 -59.876  1.00 34.67           C  
ANISOU  146  CG  HIS C  20     3865   4326   4984   -411   -566     96       C  
ATOM    147  ND1 HIS C  20     -11.254  20.279 -59.628  1.00 41.93           N  
ANISOU  147  ND1 HIS C  20     4806   5258   5866   -386   -525    109       N  
ATOM    148  CD2 HIS C  20     -13.109  19.764 -60.658  1.00 37.07           C  
ANISOU  148  CD2 HIS C  20     4125   4686   5273   -414   -563    121       C  
ATOM    149  CE1 HIS C  20     -11.692  21.377 -60.217  1.00 48.23           C  
ANISOU  149  CE1 HIS C  20     5578   6110   6635   -374   -497    147       C  
ATOM    150  NE2 HIS C  20     -12.815  21.091 -60.850  1.00 46.77           N  
ANISOU  150  NE2 HIS C  20     5354   5955   6459   -388   -519    155       N  
ATOM    151  N   LEU C  21     -14.055  17.733 -57.023  1.00 39.76           N  
ANISOU  151  N   LEU C  21     4523   4827   5756   -485   -551    211       N  
ATOM    152  CA  LEU C  21     -15.252  18.318 -56.425  1.00 35.64           C  
ANISOU  152  CA  LEU C  21     3974   4326   5243   -496   -509    285       C  
ATOM    153  C   LEU C  21     -15.126  18.488 -54.914  1.00 39.33           C  
ANISOU  153  C   LEU C  21     4474   4761   5710   -489   -465    335       C  
ATOM    154  O   LEU C  21     -15.586  19.496 -54.376  1.00 44.28           O  
ANISOU  154  O   LEU C  21     5093   5419   6314   -469   -414    380       O  
ATOM    155  CB  LEU C  21     -16.486  17.488 -56.790  1.00 32.40           C  
ANISOU  155  CB  LEU C  21     3514   3913   4883   -541   -542    299       C  
ATOM    156  CG  LEU C  21     -17.805  17.923 -56.138  1.00 32.16           C  
ANISOU  156  CG  LEU C  21     3445   3908   4866   -556   -500    377       C  
ATOM    157  CD1 LEU C  21     -18.145  19.376 -56.456  1.00 34.30           C  
ANISOU  157  CD1 LEU C  21     3698   4247   5089   -518   -457    399       C  
ATOM    158  CD2 LEU C  21     -18.951  17.013 -56.552  1.00 31.74           C  
ANISOU  158  CD2 LEU C  21     3337   3851   4872   -607   -539    387       C  
ATOM    159  N   ASP C  22     -14.520  17.539 -54.203  1.00 46.57           N  
ANISOU  159  N   ASP C  22     5426   5619   6651   -499   -484    328       N  
ATOM    160  CA  ASP C  22     -14.258  17.803 -52.792  1.00 52.87           C  
ANISOU  160  CA  ASP C  22     6256   6398   7432   -481   -442    371       C  
ATOM    161  C   ASP C  22     -13.211  18.889 -52.601  1.00 48.77           C  
ANISOU  161  C   ASP C  22     5772   5898   6861   -434   -414    343       C  
ATOM    162  O   ASP C  22     -13.230  19.584 -51.577  1.00 52.63           O  
ANISOU  162  O   ASP C  22     6276   6396   7325   -410   -370    377       O  
ATOM    163  CB  ASP C  22     -13.832  16.538 -52.066  1.00 64.47           C  
ANISOU  163  CB  ASP C  22     7757   7802   8937   -500   -471    377       C  
ATOM    164  CG  ASP C  22     -12.853  15.706 -52.854  1.00 92.31           C  
ANISOU  164  CG  ASP C  22    11305  11288  12482   -500   -532    301       C  
ATOM    165  OD1 ASP C  22     -12.032  15.037 -52.210  1.00 99.49           O  
ANISOU  165  OD1 ASP C  22    12255  12147  13400   -491   -550    292       O  
ATOM    166  OD2 ASP C  22     -12.938  15.675 -54.086  1.00105.97           O  
ANISOU  166  OD2 ASP C  22    13009  13040  14216   -506   -563    252       O  
ATOM    167  N   MET C  23     -12.299  19.069 -53.561  1.00 39.17           N  
ANISOU  167  N   MET C  23     4564   4690   5628   -420   -438    281       N  
ATOM    168  CA  MET C  23     -11.445  20.255 -53.491  1.00 40.37           C  
ANISOU  168  CA  MET C  23     4736   4864   5739   -383   -409    263       C  
ATOM    169  C   MET C  23     -12.285  21.532 -53.494  1.00 40.26           C  
ANISOU  169  C   MET C  23     4697   4891   5708   -370   -364    306       C  
ATOM    170  O   MET C  23     -12.120  22.408 -52.630  1.00 36.98           O  
ANISOU  170  O   MET C  23     4301   4476   5275   -342   -327    323       O  
ATOM    171  CB  MET C  23     -10.441  20.276 -54.642  1.00 38.10           C  
ANISOU  171  CB  MET C  23     4449   4593   5434   -375   -438    200       C  
ATOM    172  CG  MET C  23      -9.478  21.445 -54.583  1.00 38.02           C  
ANISOU  172  CG  MET C  23     4456   4600   5391   -345   -410    186       C  
ATOM    173  SD  MET C  23      -9.968  22.897 -55.528  1.00 42.56           S  
ANISOU  173  SD  MET C  23     4997   5230   5944   -336   -380    213       S  
ATOM    174  CE  MET C  23      -9.740  22.263 -57.185  1.00 44.90           C  
ANISOU  174  CE  MET C  23     5262   5569   6228   -348   -423    168       C  
ATOM    175  N   LEU C  24     -13.217  21.645 -54.446  1.00 33.25           N  
ANISOU  175  N   LEU C  24     3767   4039   4829   -385   -372    319       N  
ATOM    176  CA  LEU C  24     -14.070  22.834 -54.491  1.00 29.50           C  
ANISOU  176  CA  LEU C  24     3265   3602   4341   -367   -334    361       C  
ATOM    177  C   LEU C  24     -14.907  22.975 -53.227  1.00 30.65           C  
ANISOU  177  C   LEU C  24     3408   3745   4494   -360   -297    411       C  
ATOM    178  O   LEU C  24     -15.070  24.086 -52.705  1.00 27.24           O  
ANISOU  178  O   LEU C  24     2980   3326   4043   -326   -259    430       O  
ATOM    179  CB  LEU C  24     -14.982  22.802 -55.715  1.00 25.79           C  
ANISOU  179  CB  LEU C  24     2746   3175   3877   -382   -354    368       C  
ATOM    180  CG  LEU C  24     -14.282  22.832 -57.078  1.00 27.47           C  
ANISOU  180  CG  LEU C  24     2953   3415   4070   -380   -385    322       C  
ATOM    181  CD1 LEU C  24     -15.235  22.366 -58.148  1.00 24.41           C  
ANISOU  181  CD1 LEU C  24     2517   3068   3691   -400   -418    320       C  
ATOM    182  CD2 LEU C  24     -13.795  24.233 -57.380  1.00 15.79           C  
ANISOU  182  CD2 LEU C  24     1482   1958   2561   -348   -355    334       C  
ATOM    183  N   ARG C  25     -15.452  21.865 -52.726  1.00 34.07           N  
ANISOU  183  N   ARG C  25     3831   4161   4953   -391   -308    434       N  
ATOM    184  CA  ARG C  25     -16.242  21.918 -51.501  1.00 35.34           C  
ANISOU  184  CA  ARG C  25     3983   4331   5113   -386   -270    490       C  
ATOM    185  C   ARG C  25     -15.420  22.469 -50.343  1.00 41.24           C  
ANISOU  185  C   ARG C  25     4777   5065   5828   -345   -240    483       C  
ATOM    186  O   ARG C  25     -15.848  23.402 -49.656  1.00 38.23           O  
ANISOU  186  O   ARG C  25     4391   4712   5424   -310   -200    505       O  
ATOM    187  CB  ARG C  25     -16.785  20.531 -51.164  1.00 28.63           C  
ANISOU  187  CB  ARG C  25     3118   3459   4303   -432   -290    522       C  
ATOM    188  CG  ARG C  25     -17.674  20.493 -49.927  1.00 35.90           C  
ANISOU  188  CG  ARG C  25     4019   4401   5219   -432   -246    591       C  
ATOM    189  CD  ARG C  25     -18.562  19.254 -49.906  1.00 51.21           C  
ANISOU  189  CD  ARG C  25     5919   6327   7209   -490   -265    638       C  
ATOM    190  NE  ARG C  25     -17.972  18.143 -50.646  1.00 64.79           N  
ANISOU  190  NE  ARG C  25     7657   7990   8973   -528   -327    596       N  
ATOM    191  CZ  ARG C  25     -18.449  17.674 -51.795  1.00 75.78           C  
ANISOU  191  CZ  ARG C  25     9012   9378  10404   -564   -371    572       C  
ATOM    192  NH1 ARG C  25     -17.843  16.664 -52.404  1.00 79.52           N  
ANISOU  192  NH1 ARG C  25     9504   9798  10914   -589   -430    524       N  
ATOM    193  NH2 ARG C  25     -19.533  18.214 -52.336  1.00 72.94           N  
ANISOU  193  NH2 ARG C  25     8595   9073  10046   -569   -358    591       N  
ATOM    194  N   HIS C  26     -14.228  21.909 -50.120  1.00 45.65           N  
ANISOU  194  N   HIS C  26     5379   5582   6383   -346   -265    446       N  
ATOM    195  CA  HIS C  26     -13.380  22.399 -49.037  1.00 42.18           C  
ANISOU  195  CA  HIS C  26     4983   5133   5912   -307   -244    432       C  
ATOM    196  C   HIS C  26     -13.048  23.875 -49.214  1.00 43.17           C  
ANISOU  196  C   HIS C  26     5113   5273   6015   -268   -223    405       C  
ATOM    197  O   HIS C  26     -13.021  24.633 -48.237  1.00 37.98           O  
ANISOU  197  O   HIS C  26     4470   4625   5333   -229   -192    408       O  
ATOM    198  CB  HIS C  26     -12.099  21.572 -48.953  1.00 30.18           C  
ANISOU  198  CB  HIS C  26     3503   3569   4394   -312   -280    390       C  
ATOM    199  CG  HIS C  26     -12.278  20.258 -48.263  1.00 36.95           C  
ANISOU  199  CG  HIS C  26     4370   4399   5269   -335   -295    424       C  
ATOM    200  ND1 HIS C  26     -12.460  20.154 -46.901  1.00 43.89           N  
ANISOU  200  ND1 HIS C  26     5264   5286   6125   -317   -267    468       N  
ATOM    201  CD2 HIS C  26     -12.306  18.993 -48.744  1.00 26.94           C  
ANISOU  201  CD2 HIS C  26     3098   3094   4042   -375   -338    424       C  
ATOM    202  CE1 HIS C  26     -12.592  18.881 -46.572  1.00 30.83           C  
ANISOU  202  CE1 HIS C  26     3616   3601   4499   -347   -289    503       C  
ATOM    203  NE2 HIS C  26     -12.501  18.156 -47.672  1.00 28.44           N  
ANISOU  203  NE2 HIS C  26     3302   3263   4241   -383   -334    475       N  
ATOM    204  N   LEU C  27     -12.800  24.306 -50.451  1.00 38.91           N  
ANISOU  204  N   LEU C  27     4562   4737   5485   -277   -239    380       N  
ATOM    205  CA  LEU C  27     -12.487  25.711 -50.689  1.00 33.61           C  
ANISOU  205  CA  LEU C  27     3894   4072   4804   -246   -222    365       C  
ATOM    206  C   LEU C  27     -13.649  26.619 -50.306  1.00 33.65           C  
ANISOU  206  C   LEU C  27     3874   4105   4806   -218   -186    403       C  
ATOM    207  O   LEU C  27     -13.500  27.531 -49.485  1.00 40.07           O  
ANISOU  207  O   LEU C  27     4705   4913   5607   -179   -163    394       O  
ATOM    208  CB  LEU C  27     -12.116  25.927 -52.153  1.00 40.18           C  
ANISOU  208  CB  LEU C  27     4711   4913   5643   -263   -244    346       C  
ATOM    209  CG  LEU C  27     -10.699  25.545 -52.562  1.00 46.98           C  
ANISOU  209  CG  LEU C  27     5596   5755   6499   -272   -272    297       C  
ATOM    210  CD1 LEU C  27     -10.475  26.019 -53.963  1.00 50.37           C  
ANISOU  210  CD1 LEU C  27     6002   6210   6925   -281   -282    290       C  
ATOM    211  CD2 LEU C  27      -9.696  26.184 -51.628  1.00 49.06           C  
ANISOU  211  CD2 LEU C  27     5895   5991   6753   -246   -260    270       C  
ATOM    212  N   TYR C  28     -14.823  26.378 -50.893  1.00 35.20           N  
ANISOU  212  N   TYR C  28     4027   4333   5015   -236   -185    440       N  
ATOM    213  CA  TYR C  28     -15.898  27.360 -50.888  1.00 28.60           C  
ANISOU  213  CA  TYR C  28     3159   3528   4179   -207   -156    472       C  
ATOM    214  C   TYR C  28     -16.965  27.128 -49.825  1.00 29.49           C  
ANISOU  214  C   TYR C  28     3249   3672   4283   -195   -125    510       C  
ATOM    215  O   TYR C  28     -17.842  27.986 -49.667  1.00 38.77           O  
ANISOU  215  O   TYR C  28     4397   4878   5456   -160    -99    531       O  
ATOM    216  CB  TYR C  28     -16.561  27.404 -52.269  1.00 20.91           C  
ANISOU  216  CB  TYR C  28     2143   2581   3220   -228   -174    489       C  
ATOM    217  CG  TYR C  28     -15.614  27.828 -53.367  1.00 26.88           C  
ANISOU  217  CG  TYR C  28     2914   3323   3975   -232   -197    461       C  
ATOM    218  CD1 TYR C  28     -15.313  26.974 -54.418  1.00 29.70           C  
ANISOU  218  CD1 TYR C  28     3261   3690   4333   -268   -232    444       C  
ATOM    219  CD2 TYR C  28     -15.013  29.081 -53.347  1.00 28.08           C  
ANISOU  219  CD2 TYR C  28     3089   3456   4126   -200   -184    451       C  
ATOM    220  CE1 TYR C  28     -14.445  27.359 -55.426  1.00 31.65           C  
ANISOU  220  CE1 TYR C  28     3515   3940   4570   -270   -249    422       C  
ATOM    221  CE2 TYR C  28     -14.144  29.474 -54.346  1.00 24.38           C  
ANISOU  221  CE2 TYR C  28     2627   2979   3656   -209   -201    437       C  
ATOM    222  CZ  TYR C  28     -13.863  28.610 -55.382  1.00 32.66           C  
ANISOU  222  CZ  TYR C  28     3662   4051   4696   -242   -230    425       C  
ATOM    223  OH  TYR C  28     -12.999  29.002 -56.380  1.00 42.08           O  
ANISOU  223  OH  TYR C  28     4856   5252   5879   -248   -242    414       O  
ATOM    224  N   GLN C  29     -16.923  26.010 -49.101  1.00 33.00           N  
ANISOU  224  N   GLN C  29     3700   4112   4724   -219   -127    524       N  
ATOM    225  CA  GLN C  29     -17.932  25.756 -48.078  1.00 40.08           C  
ANISOU  225  CA  GLN C  29     4570   5050   5610   -209    -92    572       C  
ATOM    226  C   GLN C  29     -17.937  26.879 -47.050  1.00 35.37           C  
ANISOU  226  C   GLN C  29     3988   4473   4979   -143    -55    561       C  
ATOM    227  O   GLN C  29     -16.920  27.148 -46.404  1.00 43.80           O  
ANISOU  227  O   GLN C  29     5103   5514   6025   -117    -57    522       O  
ATOM    228  CB  GLN C  29     -17.678  24.413 -47.395  1.00 41.16           C  
ANISOU  228  CB  GLN C  29     4721   5170   5748   -245   -101    594       C  
ATOM    229  CG  GLN C  29     -18.632  24.115 -46.247  1.00 48.21           C  
ANISOU  229  CG  GLN C  29     5584   6111   6621   -237    -61    654       C  
ATOM    230  CD  GLN C  29     -19.989  23.627 -46.723  1.00 58.98           C  
ANISOU  230  CD  GLN C  29     6881   7511   8018   -277    -55    709       C  
ATOM    231  OE1 GLN C  29     -20.083  22.689 -47.514  1.00 68.18           O  
ANISOU  231  OE1 GLN C  29     8031   8647   9225   -335    -92    715       O  
ATOM    232  NE2 GLN C  29     -21.048  24.272 -46.248  1.00 56.60           N  
ANISOU  232  NE2 GLN C  29     6535   7274   7697   -245    -13    743       N  
ATOM    233  N   GLY C  30     -19.085  27.543 -46.913  1.00 35.20           N  
ANISOU  233  N   GLY C  30     3923   4499   4951   -113    -25    588       N  
ATOM    234  CA  GLY C  30     -19.222  28.655 -46.000  1.00 38.96           C  
ANISOU  234  CA  GLY C  30     4407   4999   5398    -42      7    569       C  
ATOM    235  C   GLY C  30     -18.590  29.949 -46.459  1.00 39.96           C  
ANISOU  235  C   GLY C  30     4563   5084   5537     -4     -7    519       C  
ATOM    236  O   GLY C  30     -18.768  30.974 -45.788  1.00 43.36           O  
ANISOU  236  O   GLY C  30     4997   5525   5952     59     13    495       O  
ATOM    237  N   CYS C  31     -17.866  29.944 -47.575  1.00 38.19           N  
ANISOU  237  N   CYS C  31     4355   4814   5341    -39    -41    501       N  
ATOM    238  CA  CYS C  31     -17.221  31.158 -48.056  1.00 45.56           C  
ANISOU  238  CA  CYS C  31     5313   5704   6292    -12    -53    465       C  
ATOM    239  C   CYS C  31     -18.261  32.145 -48.574  1.00 44.06           C  
ANISOU  239  C   CYS C  31     5086   5535   6120     22    -42    487       C  
ATOM    240  O   CYS C  31     -19.208  31.761 -49.268  1.00 49.76           O  
ANISOU  240  O   CYS C  31     5762   6295   6850      0    -42    528       O  
ATOM    241  CB  CYS C  31     -16.213  30.818 -49.153  1.00 42.31           C  
ANISOU  241  CB  CYS C  31     4921   5255   5901    -60    -88    450       C  
ATOM    242  SG  CYS C  31     -15.245  32.222 -49.768  1.00 47.12           S  
ANISOU  242  SG  CYS C  31     5558   5808   6537    -40   -103    418       S  
ATOM    243  N   GLN C  32     -18.090  33.419 -48.219  1.00 38.43           N  
ANISOU  243  N   GLN C  32     4392   4795   5417     78    -37    458       N  
ATOM    244  CA  GLN C  32     -18.952  34.492 -48.700  1.00 36.92           C  
ANISOU  244  CA  GLN C  32     4172   4609   5248    119    -31    475       C  
ATOM    245  C   GLN C  32     -18.243  35.479 -49.612  1.00 32.94           C  
ANISOU  245  C   GLN C  32     3691   4042   4784    119    -56    466       C  
ATOM    246  O   GLN C  32     -18.897  36.093 -50.460  1.00 32.62           O  
ANISOU  246  O   GLN C  32     3624   4005   4765    133    -61    499       O  
ATOM    247  CB  GLN C  32     -19.575  35.268 -47.528  1.00 25.32           C  
ANISOU  247  CB  GLN C  32     2697   3160   3764    196     -5    452       C  
ATOM    248  CG  GLN C  32     -19.870  34.452 -46.279  1.00 30.14           C  
ANISOU  248  CG  GLN C  32     3299   3828   4325    206     23    451       C  
ATOM    249  CD  GLN C  32     -20.613  35.261 -45.221  1.00 40.04           C  
ANISOU  249  CD  GLN C  32     4537   5121   5556    290     52    428       C  
ATOM    250  OE1 GLN C  32     -21.783  35.594 -45.395  1.00 46.45           O  
ANISOU  250  OE1 GLN C  32     5299   5978   6370    322     69    456       O  
ATOM    251  NE2 GLN C  32     -19.938  35.568 -44.122  1.00 40.16           N  
ANISOU  251  NE2 GLN C  32     4590   5123   5546    332     54    373       N  
ATOM    252  N   VAL C  33     -16.929  35.643 -49.464  1.00 21.15           N  
ANISOU  252  N   VAL C  33     2243   2493   3300    104    -73    427       N  
ATOM    253  CA  VAL C  33     -16.143  36.566 -50.275  1.00 31.57           C  
ANISOU  253  CA  VAL C  33     3582   3751   4660     97    -94    425       C  
ATOM    254  C   VAL C  33     -14.968  35.788 -50.853  1.00 37.07           C  
ANISOU  254  C   VAL C  33     4298   4436   5351     34   -113    418       C  
ATOM    255  O   VAL C  33     -14.074  35.363 -50.111  1.00 48.60           O  
ANISOU  255  O   VAL C  33     5788   5880   6799     24   -117    375       O  
ATOM    256  CB  VAL C  33     -15.652  37.775 -49.469  1.00 38.86           C  
ANISOU  256  CB  VAL C  33     4539   4612   5615    146    -99    376       C  
ATOM    257  CG1 VAL C  33     -14.735  38.643 -50.319  1.00 29.97           C  
ANISOU  257  CG1 VAL C  33     3431   3417   4540    125   -122    383       C  
ATOM    258  CG2 VAL C  33     -16.834  38.585 -48.940  1.00 18.40           C  
ANISOU  258  CG2 VAL C  33     1927   2034   3029    219    -84    376       C  
ATOM    259  N   VAL C  34     -14.969  35.602 -52.168  1.00 30.87           N  
ANISOU  259  N   VAL C  34     3493   3666   4571     -3   -125    457       N  
ATOM    260  CA  VAL C  34     -13.885  34.922 -52.865  1.00 33.14           C  
ANISOU  260  CA  VAL C  34     3791   3951   4850    -56   -142    449       C  
ATOM    261  C   VAL C  34     -12.826  35.965 -53.199  1.00 37.83           C  
ANISOU  261  C   VAL C  34     4406   4488   5479    -59   -152    442       C  
ATOM    262  O   VAL C  34     -13.056  36.851 -54.024  1.00 33.86           O  
ANISOU  262  O   VAL C  34     3890   3973   5002    -52   -155    483       O  
ATOM    263  CB  VAL C  34     -14.388  34.217 -54.129  1.00 31.94           C  
ANISOU  263  CB  VAL C  34     3603   3853   4680    -89   -152    488       C  
ATOM    264  CG1 VAL C  34     -13.228  33.595 -54.892  1.00 31.00           C  
ANISOU  264  CG1 VAL C  34     3492   3738   4548   -134   -171    473       C  
ATOM    265  CG2 VAL C  34     -15.436  33.173 -53.771  1.00 33.78           C  
ANISOU  265  CG2 VAL C  34     3811   4135   4891    -93   -146    496       C  
ATOM    266  N   GLN C  35     -11.667  35.873 -52.550  1.00 46.19           N  
ANISOU  266  N   GLN C  35     5496   5513   6542    -70   -159    394       N  
ATOM    267  CA  GLN C  35     -10.574  36.809 -52.816  1.00 44.59           C  
ANISOU  267  CA  GLN C  35     5309   5255   6379    -82   -171    385       C  
ATOM    268  C   GLN C  35      -9.672  36.230 -53.906  1.00 35.31           C  
ANISOU  268  C   GLN C  35     4121   4105   5188   -134   -181    400       C  
ATOM    269  O   GLN C  35      -8.531  35.816 -53.686  1.00 42.64           O  
ANISOU  269  O   GLN C  35     5064   5026   6112   -158   -190    361       O  
ATOM    270  CB  GLN C  35      -9.818  37.129 -51.534  1.00 53.68           C  
ANISOU  270  CB  GLN C  35     6492   6357   7545    -63   -176    320       C  
ATOM    271  CG  GLN C  35     -10.286  38.437 -50.908  1.00 67.46           C  
ANISOU  271  CG  GLN C  35     8248   8048   9335    -12   -176    309       C  
ATOM    272  CD  GLN C  35      -9.624  38.739 -49.582  1.00 78.83           C  
ANISOU  272  CD  GLN C  35     9719   9448  10784     15   -186    233       C  
ATOM    273  OE1 GLN C  35     -10.162  39.491 -48.768  1.00 85.18           O  
ANISOU  273  OE1 GLN C  35    10532  10226  11605     70   -186    204       O  
ATOM    274  NE2 GLN C  35      -8.453  38.158 -49.356  1.00 78.16           N  
ANISOU  274  NE2 GLN C  35     9648   9362  10687    -17   -198    197       N  
ATOM    275  N   GLY C  36     -10.228  36.221 -55.108  1.00 29.91           N  
ANISOU  275  N   GLY C  36     3408   3462   4494   -146   -179    455       N  
ATOM    276  CA  GLY C  36      -9.601  35.653 -56.287  1.00 33.25           C  
ANISOU  276  CA  GLY C  36     3812   3931   4890   -185   -187    473       C  
ATOM    277  C   GLY C  36     -10.663  35.337 -57.326  1.00 36.49           C  
ANISOU  277  C   GLY C  36     4188   4403   5272   -183   -188    521       C  
ATOM    278  O   GLY C  36     -11.726  35.957 -57.350  1.00 41.85           O  
ANISOU  278  O   GLY C  36     4856   5079   5966   -154   -181    557       O  
ATOM    279  N   ASN C  37     -10.356  34.355 -58.164  1.00 31.03           N  
ANISOU  279  N   ASN C  37     3479   3770   4540   -211   -199    515       N  
ATOM    280  CA  ASN C  37     -11.249  33.931 -59.231  1.00 28.78           C  
ANISOU  280  CA  ASN C  37     3159   3554   4223   -212   -208    549       C  
ATOM    281  C   ASN C  37     -12.082  32.750 -58.759  1.00 30.42           C  
ANISOU  281  C   ASN C  37     3361   3785   4414   -212   -217    518       C  
ATOM    282  O   ASN C  37     -11.550  31.809 -58.162  1.00 30.86           O  
ANISOU  282  O   ASN C  37     3433   3829   4462   -228   -225    468       O  
ATOM    283  CB  ASN C  37     -10.455  33.549 -60.479  1.00 38.42           C  
ANISOU  283  CB  ASN C  37     4359   4833   5406   -237   -219    554       C  
ATOM    284  CG  ASN C  37      -9.404  34.575 -60.831  1.00 38.91           C  
ANISOU  284  CG  ASN C  37     4425   4872   5487   -248   -207    584       C  
ATOM    285  OD1 ASN C  37      -9.655  35.777 -60.781  1.00 38.45           O  
ANISOU  285  OD1 ASN C  37     4371   4772   5467   -233   -196    634       O  
ATOM    286  ND2 ASN C  37      -8.216  34.105 -61.195  1.00 48.49           N  
ANISOU  286  ND2 ASN C  37     5634   6112   6677   -273   -211    557       N  
ATOM    287  N   LEU C  38     -13.386  32.808 -59.016  1.00 29.09           N  
ANISOU  287  N   LEU C  38     3164   3645   4243   -195   -217    550       N  
ATOM    288  CA  LEU C  38     -14.277  31.675 -58.793  1.00 28.70           C  
ANISOU  288  CA  LEU C  38     3096   3626   4181   -204   -228    532       C  
ATOM    289  C   LEU C  38     -14.318  30.854 -60.076  1.00 28.79           C  
ANISOU  289  C   LEU C  38     3077   3703   4159   -226   -256    527       C  
ATOM    290  O   LEU C  38     -14.926  31.270 -61.066  1.00 24.36           O  
ANISOU  290  O   LEU C  38     2484   3189   3582   -215   -263    565       O  
ATOM    291  CB  LEU C  38     -15.671  32.151 -58.392  1.00 32.54           C  
ANISOU  291  CB  LEU C  38     3562   4119   4685   -174   -214    567       C  
ATOM    292  CG  LEU C  38     -16.728  31.058 -58.226  1.00 25.15           C  
ANISOU  292  CG  LEU C  38     2594   3219   3743   -188   -224    561       C  
ATOM    293  CD1 LEU C  38     -16.344  30.126 -57.095  1.00 28.34           C  
ANISOU  293  CD1 LEU C  38     3024   3591   4152   -207   -220    522       C  
ATOM    294  CD2 LEU C  38     -18.103  31.659 -57.981  1.00 29.48           C  
ANISOU  294  CD2 LEU C  38     3110   3786   4304   -156   -208    600       C  
ATOM    295  N   GLU C  39     -13.663  29.694 -60.069  1.00 30.93           N  
ANISOU  295  N   GLU C  39     3358   3978   4417   -252   -276    476       N  
ATOM    296  CA  GLU C  39     -13.548  28.845 -61.252  1.00 33.62           C  
ANISOU  296  CA  GLU C  39     3672   4378   4724   -269   -309    453       C  
ATOM    297  C   GLU C  39     -14.261  27.525 -60.990  1.00 42.71           C  
ANISOU  297  C   GLU C  39     4809   5532   5886   -289   -336    419       C  
ATOM    298  O   GLU C  39     -13.830  26.735 -60.142  1.00 50.90           O  
ANISOU  298  O   GLU C  39     5874   6526   6941   -304   -341    384       O  
ATOM    299  CB  GLU C  39     -12.085  28.610 -61.626  1.00 36.38           C  
ANISOU  299  CB  GLU C  39     4039   4733   5052   -279   -316    415       C  
ATOM    300  CG  GLU C  39     -11.318  29.878 -61.964  1.00 40.88           C  
ANISOU  300  CG  GLU C  39     4615   5301   5616   -269   -291    454       C  
ATOM    301  CD  GLU C  39      -9.874  29.602 -62.326  1.00 48.35           C  
ANISOU  301  CD  GLU C  39     5569   6263   6540   -281   -296    418       C  
ATOM    302  OE1 GLU C  39      -9.299  28.645 -61.770  1.00 55.48           O  
ANISOU  302  OE1 GLU C  39     6490   7142   7446   -291   -311    359       O  
ATOM    303  OE2 GLU C  39      -9.316  30.342 -63.163  1.00 48.55           O  
ANISOU  303  OE2 GLU C  39     5578   6325   6543   -279   -285    453       O  
ATOM    304  N   LEU C  40     -15.345  27.294 -61.725  1.00 40.46           N  
ANISOU  304  N   LEU C  40     4482   5297   5594   -290   -355    434       N  
ATOM    305  CA  LEU C  40     -16.152  26.082 -61.644  1.00 34.32           C  
ANISOU  305  CA  LEU C  40     3681   4525   4835   -315   -386    408       C  
ATOM    306  C   LEU C  40     -16.092  25.395 -63.003  1.00 43.20           C  
ANISOU  306  C   LEU C  40     4775   5711   5928   -322   -433    369       C  
ATOM    307  O   LEU C  40     -16.675  25.882 -63.984  1.00 42.11           O  
ANISOU  307  O   LEU C  40     4601   5637   5763   -305   -441    393       O  
ATOM    308  CB  LEU C  40     -17.585  26.420 -61.241  1.00 31.08           C  
ANISOU  308  CB  LEU C  40     3238   4123   4449   -309   -372    455       C  
ATOM    309  CG  LEU C  40     -17.652  27.269 -59.967  1.00 29.93           C  
ANISOU  309  CG  LEU C  40     3120   3929   4324   -289   -324    490       C  
ATOM    310  CD1 LEU C  40     -19.003  27.957 -59.815  1.00 25.19           C  
ANISOU  310  CD1 LEU C  40     2482   3355   3736   -266   -306    540       C  
ATOM    311  CD2 LEU C  40     -17.332  26.419 -58.743  1.00 26.29           C  
ANISOU  311  CD2 LEU C  40     2688   3414   3886   -310   -319    467       C  
ATOM    312  N   THR C  41     -15.364  24.278 -63.067  1.00 44.52           N  
ANISOU  312  N   THR C  41     4957   5862   6098   -340   -465    305       N  
ATOM    313  CA  THR C  41     -15.083  23.605 -64.326  1.00 43.37           C  
ANISOU  313  CA  THR C  41     4787   5774   5916   -339   -511    251       C  
ATOM    314  C   THR C  41     -15.126  22.093 -64.151  1.00 43.81           C  
ANISOU  314  C   THR C  41     4844   5795   6008   -366   -560    185       C  
ATOM    315  O   THR C  41     -14.847  21.566 -63.070  1.00 44.13           O  
ANISOU  315  O   THR C  41     4918   5761   6090   -385   -554    178       O  
ATOM    316  CB  THR C  41     -13.711  24.009 -64.896  1.00 44.05           C  
ANISOU  316  CB  THR C  41     4892   5892   5954   -318   -501    233       C  
ATOM    317  OG1 THR C  41     -12.682  23.695 -63.947  1.00 50.59           O  
ANISOU  317  OG1 THR C  41     5765   6653   6805   -326   -489    206       O  
ATOM    318  CG2 THR C  41     -13.667  25.503 -65.228  1.00 39.75           C  
ANISOU  318  CG2 THR C  41     4342   5381   5380   -295   -458    305       C  
ATOM    319  N   TYR C  42     -15.485  21.406 -65.239  1.00 45.07           N  
ANISOU  319  N   TYR C  42     4967   6008   6151   -367   -612    136       N  
ATOM    320  CA  TYR C  42     -15.402  19.946 -65.338  1.00 43.79           C  
ANISOU  320  CA  TYR C  42     4803   5813   6022   -389   -672     58       C  
ATOM    321  C   TYR C  42     -16.220  19.254 -64.252  1.00 39.30           C  
ANISOU  321  C   TYR C  42     4237   5163   5531   -431   -677     79       C  
ATOM    322  O   TYR C  42     -15.774  18.287 -63.630  1.00 47.79           O  
ANISOU  322  O   TYR C  42     5340   6166   6650   -451   -699     45       O  
ATOM    323  CB  TYR C  42     -13.944  19.480 -65.317  1.00 42.09           C  
ANISOU  323  CB  TYR C  42     4626   5576   5789   -375   -681     -1       C  
ATOM    324  CG  TYR C  42     -13.144  20.055 -66.462  1.00 45.27           C  
ANISOU  324  CG  TYR C  42     5017   6072   6113   -337   -677    -22       C  
ATOM    325  CD1 TYR C  42     -12.252  21.100 -66.259  1.00 48.68           C  
ANISOU  325  CD1 TYR C  42     5471   6516   6509   -319   -623     21       C  
ATOM    326  CD2 TYR C  42     -13.314  19.581 -67.755  1.00 45.05           C  
ANISOU  326  CD2 TYR C  42     4950   6124   6042   -319   -727    -82       C  
ATOM    327  CE1 TYR C  42     -11.534  21.640 -67.311  1.00 49.36           C  
ANISOU  327  CE1 TYR C  42     5539   6691   6523   -288   -615     15       C  
ATOM    328  CE2 TYR C  42     -12.602  20.113 -68.811  1.00 46.90           C  
ANISOU  328  CE2 TYR C  42     5169   6458   6195   -281   -719    -93       C  
ATOM    329  CZ  TYR C  42     -11.714  21.142 -68.585  1.00 49.94           C  
ANISOU  329  CZ  TYR C  42     5574   6853   6548   -268   -660    -39       C  
ATOM    330  OH  TYR C  42     -11.006  21.672 -69.637  1.00 49.01           O  
ANISOU  330  OH  TYR C  42     5434   6838   6349   -236   -649    -38       O  
ATOM    331  N   LEU C  43     -17.441  19.751 -64.031  1.00 34.34           N  
ANISOU  331  N   LEU C  43     3576   4551   4922   -443   -657    141       N  
ATOM    332  CA  LEU C  43     -18.334  19.207 -63.015  1.00 40.31           C  
ANISOU  332  CA  LEU C  43     4322   5246   5746   -483   -653    175       C  
ATOM    333  C   LEU C  43     -19.394  18.328 -63.651  1.00 42.45           C  
ANISOU  333  C   LEU C  43     4539   5535   6057   -515   -712    146       C  
ATOM    334  O   LEU C  43     -20.086  18.777 -64.574  1.00 47.05           O  
ANISOU  334  O   LEU C  43     5075   6192   6609   -501   -726    147       O  
ATOM    335  CB  LEU C  43     -18.998  20.339 -62.235  1.00 41.01           C  
ANISOU  335  CB  LEU C  43     4405   5344   5831   -472   -589    261       C  
ATOM    336  CG  LEU C  43     -18.024  21.394 -61.690  1.00 38.53           C  
ANISOU  336  CG  LEU C  43     4140   5018   5480   -437   -534    288       C  
ATOM    337  CD1 LEU C  43     -18.763  22.595 -61.111  1.00 39.59           C  
ANISOU  337  CD1 LEU C  43     4263   5168   5610   -416   -479    361       C  
ATOM    338  CD2 LEU C  43     -17.103  20.779 -60.660  1.00 35.74           C  
ANISOU  338  CD2 LEU C  43     3839   4589   5151   -449   -527    270       C  
ATOM    339  N   PRO C  44     -19.558  17.093 -63.186  1.00 41.06           N  
ANISOU  339  N   PRO C  44     4364   5287   5950   -559   -751    121       N  
ATOM    340  CA  PRO C  44     -20.515  16.182 -63.819  1.00 40.73           C  
ANISOU  340  CA  PRO C  44     4268   5251   5958   -596   -817     83       C  
ATOM    341  C   PRO C  44     -21.953  16.563 -63.498  1.00 43.14           C  
ANISOU  341  C   PRO C  44     4515   5583   6291   -621   -794    155       C  
ATOM    342  O   PRO C  44     -22.235  17.478 -62.722  1.00 49.69           O  
ANISOU  342  O   PRO C  44     5350   6424   7105   -608   -727    232       O  
ATOM    343  CB  PRO C  44     -20.143  14.822 -63.227  1.00 32.62           C  
ANISOU  343  CB  PRO C  44     3267   4121   5006   -637   -858     49       C  
ATOM    344  CG  PRO C  44     -19.616  15.154 -61.875  1.00 37.20           C  
ANISOU  344  CG  PRO C  44     3899   4647   5589   -635   -794    114       C  
ATOM    345  CD  PRO C  44     -18.899  16.478 -62.020  1.00 41.14           C  
ANISOU  345  CD  PRO C  44     4424   5204   6001   -578   -738    130       C  
ATOM    346  N   THR C  45     -22.875  15.820 -64.115  1.00 47.48           N  
ANISOU  346  N   THR C  45     5007   6144   6887   -657   -855    122       N  
ATOM    347  CA  THR C  45     -24.292  16.171 -64.056  1.00 50.88           C  
ANISOU  347  CA  THR C  45     5370   6621   7342   -678   -842    178       C  
ATOM    348  C   THR C  45     -24.836  16.104 -62.633  1.00 57.23           C  
ANISOU  348  C   THR C  45     6171   7372   8201   -717   -790    265       C  
ATOM    349  O   THR C  45     -25.569  17.001 -62.198  1.00 63.77           O  
ANISOU  349  O   THR C  45     6971   8247   9011   -702   -734    336       O  
ATOM    350  CB  THR C  45     -25.090  15.251 -64.983  1.00 53.70           C  
ANISOU  350  CB  THR C  45     5663   6995   7746   -714   -928    115       C  
ATOM    351  OG1 THR C  45     -24.698  15.485 -66.342  1.00 60.10           O  
ANISOU  351  OG1 THR C  45     6468   7881   8487   -666   -970     40       O  
ATOM    352  CG2 THR C  45     -26.576  15.503 -64.846  1.00 59.24           C  
ANISOU  352  CG2 THR C  45     6286   7740   8482   -743   -918    173       C  
ATOM    353  N   ASN C  46     -24.486  15.056 -61.888  1.00 59.56           N  
ANISOU  353  N   ASN C  46     6495   7575   8561   -761   -806    263       N  
ATOM    354  CA  ASN C  46     -25.039  14.820 -60.562  1.00 65.97           C  
ANISOU  354  CA  ASN C  46     7297   8341   9426   -803   -761    349       C  
ATOM    355  C   ASN C  46     -24.234  15.489 -59.450  1.00 59.67           C  
ANISOU  355  C   ASN C  46     6565   7523   8584   -767   -686    399       C  
ATOM    356  O   ASN C  46     -24.307  15.049 -58.296  1.00 65.92           O  
ANISOU  356  O   ASN C  46     7369   8263   9414   -798   -658    457       O  
ATOM    357  CB  ASN C  46     -25.142  13.315 -60.300  1.00 78.52           C  
ANISOU  357  CB  ASN C  46     8881   9838  11116   -874   -819    332       C  
ATOM    358  CG  ASN C  46     -26.147  12.632 -61.210  1.00 85.53           C  
ANISOU  358  CG  ASN C  46     9693  10740  12065   -920   -893    291       C  
ATOM    359  OD1 ASN C  46     -26.994  13.286 -61.820  1.00 84.01           O  
ANISOU  359  OD1 ASN C  46     9441  10635  11844   -906   -889    296       O  
ATOM    360  ND2 ASN C  46     -26.058  11.309 -61.307  1.00 84.06           N  
ANISOU  360  ND2 ASN C  46     9518  10468  11953   -964   -954    244       N  
ATOM    361  N   ALA C  47     -23.484  16.545 -59.764  1.00 48.16           N  
ANISOU  361  N   ALA C  47     5146   6107   7047   -704   -656    381       N  
ATOM    362  CA  ALA C  47     -22.599  17.170 -58.789  1.00 46.90           C  
ANISOU  362  CA  ALA C  47     5049   5924   6847   -668   -596    413       C  
ATOM    363  C   ALA C  47     -23.387  18.043 -57.819  1.00 43.29           C  
ANISOU  363  C   ALA C  47     4570   5502   6376   -655   -524    497       C  
ATOM    364  O   ALA C  47     -24.138  18.930 -58.236  1.00 41.39           O  
ANISOU  364  O   ALA C  47     4287   5330   6109   -630   -505    517       O  
ATOM    365  CB  ALA C  47     -21.530  18.003 -59.497  1.00 34.65           C  
ANISOU  365  CB  ALA C  47     3540   4402   5224   -611   -591    366       C  
ATOM    366  N   SER C  48     -23.205  17.793 -56.523  1.00 41.24           N  
ANISOU  366  N   SER C  48     4339   5200   6132   -666   -486    545       N  
ATOM    367  CA  SER C  48     -23.849  18.585 -55.479  1.00 40.75           C  
ANISOU  367  CA  SER C  48     4259   5175   6048   -645   -415    619       C  
ATOM    368  C   SER C  48     -23.015  19.835 -55.221  1.00 45.67           C  
ANISOU  368  C   SER C  48     4935   5813   6603   -577   -372    609       C  
ATOM    369  O   SER C  48     -21.901  19.750 -54.694  1.00 47.50           O  
ANISOU  369  O   SER C  48     5230   5999   6818   -561   -365    590       O  
ATOM    370  CB  SER C  48     -24.010  17.757 -54.207  1.00 41.63           C  
ANISOU  370  CB  SER C  48     4376   5245   6198   -684   -394    677       C  
ATOM    371  OG  SER C  48     -24.469  18.555 -53.130  1.00 49.41           O  
ANISOU  371  OG  SER C  48     5351   6275   7148   -652   -323    740       O  
ATOM    372  N   LEU C  49     -23.557  20.998 -55.583  1.00 44.45           N  
ANISOU  372  N   LEU C  49     4753   5721   6417   -535   -346    621       N  
ATOM    373  CA  LEU C  49     -22.848  22.268 -55.488  1.00 38.07           C  
ANISOU  373  CA  LEU C  49     3988   4921   5555   -472   -311    611       C  
ATOM    374  C   LEU C  49     -23.480  23.206 -54.462  1.00 35.68           C  
ANISOU  374  C   LEU C  49     3673   4651   5233   -432   -249    662       C  
ATOM    375  O   LEU C  49     -23.411  24.429 -54.607  1.00 34.98           O  
ANISOU  375  O   LEU C  49     3593   4585   5113   -379   -226    660       O  
ATOM    376  CB  LEU C  49     -22.792  22.936 -56.861  1.00 37.65           C  
ANISOU  376  CB  LEU C  49     3923   4906   5478   -448   -338    580       C  
ATOM    377  CG  LEU C  49     -22.249  22.059 -57.992  1.00 39.15           C  
ANISOU  377  CG  LEU C  49     4117   5083   5677   -478   -401    521       C  
ATOM    378  CD1 LEU C  49     -22.436  22.739 -59.337  1.00 46.79           C  
ANISOU  378  CD1 LEU C  49     5057   6108   6612   -451   -423    504       C  
ATOM    379  CD2 LEU C  49     -20.783  21.743 -57.753  1.00 46.43           C  
ANISOU  379  CD2 LEU C  49     5108   5949   6586   -475   -408    480       C  
ATOM    380  N   SER C  50     -24.090  22.644 -53.415  1.00 37.93           N  
ANISOU  380  N   SER C  50     3934   4940   5536   -455   -223    708       N  
ATOM    381  CA  SER C  50     -24.748  23.478 -52.415  1.00 39.13           C  
ANISOU  381  CA  SER C  50     4066   5136   5663   -412   -164    752       C  
ATOM    382  C   SER C  50     -23.756  24.373 -51.682  1.00 34.47           C  
ANISOU  382  C   SER C  50     3544   4523   5031   -354   -132    730       C  
ATOM    383  O   SER C  50     -24.126  25.452 -51.205  1.00 29.86           O  
ANISOU  383  O   SER C  50     2953   3974   4420   -297    -93    742       O  
ATOM    384  CB  SER C  50     -25.507  22.601 -51.418  1.00 47.71           C  
ANISOU  384  CB  SER C  50     5115   6239   6774   -451   -140    811       C  
ATOM    385  OG  SER C  50     -24.623  21.757 -50.701  1.00 64.73           O  
ANISOU  385  OG  SER C  50     7323   8338   8934   -476   -145    811       O  
ATOM    386  N   PHE C  51     -22.491  23.958 -51.601  1.00 34.36           N  
ANISOU  386  N   PHE C  51     3593   4450   5011   -364   -153    694       N  
ATOM    387  CA  PHE C  51     -21.489  24.709 -50.854  1.00 32.14           C  
ANISOU  387  CA  PHE C  51     3373   4144   4694   -315   -128    669       C  
ATOM    388  C   PHE C  51     -21.203  26.086 -51.444  1.00 33.00           C  
ANISOU  388  C   PHE C  51     3496   4257   4785   -265   -124    641       C  
ATOM    389  O   PHE C  51     -20.454  26.854 -50.831  1.00 41.79           O  
ANISOU  389  O   PHE C  51     4654   5348   5875   -222   -106    618       O  
ATOM    390  CB  PHE C  51     -20.190  23.901 -50.765  1.00 32.81           C  
ANISOU  390  CB  PHE C  51     3516   4169   4783   -340   -158    634       C  
ATOM    391  CG  PHE C  51     -19.666  23.437 -52.096  1.00 29.79           C  
ANISOU  391  CG  PHE C  51     3138   3761   4420   -372   -210    592       C  
ATOM    392  CD1 PHE C  51     -18.845  24.254 -52.856  1.00 23.39           C  
ANISOU  392  CD1 PHE C  51     2354   2943   3590   -345   -221    551       C  
ATOM    393  CD2 PHE C  51     -19.985  22.179 -52.584  1.00 28.37           C  
ANISOU  393  CD2 PHE C  51     2933   3567   4278   -428   -249    594       C  
ATOM    394  CE1 PHE C  51     -18.360  23.829 -54.080  1.00 24.50           C  
ANISOU  394  CE1 PHE C  51     2495   3076   3738   -368   -266    513       C  
ATOM    395  CE2 PHE C  51     -19.502  21.749 -53.807  1.00 27.40           C  
ANISOU  395  CE2 PHE C  51     2814   3429   4167   -448   -300    546       C  
ATOM    396  CZ  PHE C  51     -18.689  22.574 -54.555  1.00 26.48           C  
ANISOU  396  CZ  PHE C  51     2722   3319   4020   -416   -306    506       C  
ATOM    397  N   LEU C  52     -21.766  26.413 -52.609  1.00 30.58           N  
ANISOU  397  N   LEU C  52     3152   3977   4490   -268   -144    643       N  
ATOM    398  CA  LEU C  52     -21.635  27.740 -53.200  1.00 34.43           C  
ANISOU  398  CA  LEU C  52     3646   4469   4965   -220   -140    633       C  
ATOM    399  C   LEU C  52     -22.728  28.701 -52.757  1.00 34.41           C  
ANISOU  399  C   LEU C  52     3607   4509   4958   -170   -104    664       C  
ATOM    400  O   LEU C  52     -22.726  29.854 -53.205  1.00 42.18           O  
ANISOU  400  O   LEU C  52     4595   5492   5939   -126   -102    661       O  
ATOM    401  CB  LEU C  52     -21.649  27.657 -54.734  1.00 32.53           C  
ANISOU  401  CB  LEU C  52     3386   4243   4732   -241   -180    623       C  
ATOM    402  CG  LEU C  52     -20.605  26.826 -55.498  1.00 34.56           C  
ANISOU  402  CG  LEU C  52     3671   4471   4988   -282   -221    583       C  
ATOM    403  CD1 LEU C  52     -20.969  26.762 -56.978  1.00 30.58           C  
ANISOU  403  CD1 LEU C  52     3129   4007   4482   -294   -258    579       C  
ATOM    404  CD2 LEU C  52     -19.200  27.382 -55.323  1.00 36.18           C  
ANISOU  404  CD2 LEU C  52     3938   4632   5178   -261   -216    552       C  
ATOM    405  N   GLN C  53     -23.652  28.249 -51.900  1.00 38.20           N  
ANISOU  405  N   GLN C  53     4047   5028   5438   -174    -77    696       N  
ATOM    406  CA  GLN C  53     -24.818  29.052 -51.528  1.00 38.39           C  
ANISOU  406  CA  GLN C  53     4022   5107   5457   -124    -44    725       C  
ATOM    407  C   GLN C  53     -24.438  30.460 -51.086  1.00 38.32           C  
ANISOU  407  C   GLN C  53     4051   5078   5432    -49    -23    701       C  
ATOM    408  O   GLN C  53     -25.107  31.437 -51.444  1.00 45.16           O  
ANISOU  408  O   GLN C  53     4890   5968   6303     -1    -18    710       O  
ATOM    409  CB  GLN C  53     -25.581  28.377 -50.389  1.00 39.97           C  
ANISOU  409  CB  GLN C  53     4184   5352   5650   -135     -8    761       C  
ATOM    410  CG  GLN C  53     -26.595  27.329 -50.774  1.00 48.61           C  
ANISOU  410  CG  GLN C  53     5208   6488   6772   -196    -20    802       C  
ATOM    411  CD  GLN C  53     -26.978  26.476 -49.576  1.00 62.84           C  
ANISOU  411  CD  GLN C  53     6989   8317   8570   -222     13    845       C  
ATOM    412  OE1 GLN C  53     -26.722  26.855 -48.432  1.00 67.29           O  
ANISOU  412  OE1 GLN C  53     7579   8891   9098   -178     53    846       O  
ATOM    413  NE2 GLN C  53     -27.605  25.331 -49.831  1.00 71.08           N  
ANISOU  413  NE2 GLN C  53     7981   9374   9650   -293     -3    881       N  
ATOM    414  N   ASP C  54     -23.370  30.583 -50.306  1.00 29.23           N  
ANISOU  414  N   ASP C  54     2961   3881   4265    -35    -15    668       N  
ATOM    415  CA  ASP C  54     -23.109  31.786 -49.527  1.00 33.45           C  
ANISOU  415  CA  ASP C  54     3525   4398   4785     37      8    640       C  
ATOM    416  C   ASP C  54     -22.217  32.801 -50.232  1.00 36.92           C  
ANISOU  416  C   ASP C  54     4009   4775   5244     57    -17    610       C  
ATOM    417  O   ASP C  54     -21.972  33.873 -49.670  1.00 41.25           O  
ANISOU  417  O   ASP C  54     4584   5297   5793    116     -6    582       O  
ATOM    418  CB  ASP C  54     -22.484  31.404 -48.180  1.00 41.94           C  
ANISOU  418  CB  ASP C  54     4638   5467   5832     45     29    620       C  
ATOM    419  CG  ASP C  54     -23.384  30.498 -47.361  1.00 53.40           C  
ANISOU  419  CG  ASP C  54     6044   6985   7262     30     60    662       C  
ATOM    420  OD1 ASP C  54     -24.617  30.556 -47.555  1.00 60.26           O  
ANISOU  420  OD1 ASP C  54     6847   7912   8136     38     75    699       O  
ATOM    421  OD2 ASP C  54     -22.863  29.732 -46.524  1.00 56.92           O  
ANISOU  421  OD2 ASP C  54     6516   7426   7686     11     68    664       O  
ATOM    422  N   ILE C  55     -21.734  32.506 -51.437  1.00 36.16           N  
ANISOU  422  N   ILE C  55     3919   4656   5162     12    -50    614       N  
ATOM    423  CA  ILE C  55     -20.861  33.441 -52.140  1.00 36.57           C  
ANISOU  423  CA  ILE C  55     4009   4656   5232     24    -69    597       C  
ATOM    424  C   ILE C  55     -21.646  34.701 -52.484  1.00 36.41           C  
ANISOU  424  C   ILE C  55     3965   4641   5229     82    -64    618       C  
ATOM    425  O   ILE C  55     -22.683  34.639 -53.158  1.00 43.38           O  
ANISOU  425  O   ILE C  55     4796   5572   6113     84    -68    654       O  
ATOM    426  CB  ILE C  55     -20.265  32.800 -53.399  1.00 31.85           C  
ANISOU  426  CB  ILE C  55     3413   4052   4635    -33   -102    602       C  
ATOM    427  CG1 ILE C  55     -19.345  31.635 -53.026  1.00 30.13           C  
ANISOU  427  CG1 ILE C  55     3225   3817   4406    -81   -112    573       C  
ATOM    428  CG2 ILE C  55     -19.499  33.833 -54.210  1.00 18.31           C  
ANISOU  428  CG2 ILE C  55     1725   2297   2936    -20   -117    601       C  
ATOM    429  CD1 ILE C  55     -18.807  30.880 -54.222  1.00 24.16           C  
ANISOU  429  CD1 ILE C  55     2467   3064   3648   -131   -146    568       C  
ATOM    430  N   GLN C  56     -21.158  35.850 -52.011  1.00 31.33           N  
ANISOU  430  N   GLN C  56     3357   3943   4602    131    -60    592       N  
ATOM    431  CA  GLN C  56     -21.734  37.143 -52.357  1.00 35.68           C  
ANISOU  431  CA  GLN C  56     3896   4480   5181    190    -62    609       C  
ATOM    432  C   GLN C  56     -20.846  37.988 -53.250  1.00 36.43           C  
ANISOU  432  C   GLN C  56     4024   4508   5308    183    -87    617       C  
ATOM    433  O   GLN C  56     -21.360  38.759 -54.061  1.00 41.55           O  
ANISOU  433  O   GLN C  56     4654   5156   5978    209    -98    656       O  
ATOM    434  CB  GLN C  56     -22.037  37.966 -51.100  1.00 31.79           C  
ANISOU  434  CB  GLN C  56     3414   3973   4692    263    -41    572       C  
ATOM    435  CG  GLN C  56     -22.906  37.308 -50.052  1.00 45.57           C  
ANISOU  435  CG  GLN C  56     5123   5790   6400    282     -9    567       C  
ATOM    436  CD  GLN C  56     -23.153  38.245 -48.888  1.00 54.24           C  
ANISOU  436  CD  GLN C  56     6231   6880   7496    367     10    524       C  
ATOM    437  OE1 GLN C  56     -23.003  39.461 -49.021  1.00 52.79           O  
ANISOU  437  OE1 GLN C  56     6069   6638   7349    417     -6    504       O  
ATOM    438  NE2 GLN C  56     -23.520  37.690 -47.740  1.00 56.64           N  
ANISOU  438  NE2 GLN C  56     6520   7244   7757    384     41    509       N  
ATOM    439  N   GLU C  57     -19.531  37.889 -53.096  1.00 38.31           N  
ANISOU  439  N   GLU C  57     4310   4696   5552    150    -95    587       N  
ATOM    440  CA  GLU C  57     -18.593  38.732 -53.819  1.00 38.43           C  
ANISOU  440  CA  GLU C  57     4354   4646   5601    140   -115    597       C  
ATOM    441  C   GLU C  57     -17.455  37.887 -54.371  1.00 36.61           C  
ANISOU  441  C   GLU C  57     4141   4418   5353     71   -127    591       C  
ATOM    442  O   GLU C  57     -16.936  36.998 -53.689  1.00 30.94           O  
ANISOU  442  O   GLU C  57     3438   3706   4611     46   -122    552       O  
ATOM    443  CB  GLU C  57     -18.027  39.838 -52.921  1.00 33.36           C  
ANISOU  443  CB  GLU C  57     3751   3923   4999    182   -116    555       C  
ATOM    444  CG  GLU C  57     -18.979  40.317 -51.832  1.00 50.26           C  
ANISOU  444  CG  GLU C  57     5882   6074   7141    256   -100    526       C  
ATOM    445  CD  GLU C  57     -18.507  41.592 -51.162  1.00 65.31           C  
ANISOU  445  CD  GLU C  57     7825   7893   9097    306   -111    482       C  
ATOM    446  OE1 GLU C  57     -19.340  42.286 -50.532  1.00 62.74           O  
ANISOU  446  OE1 GLU C  57     7489   7568   8784    379   -105    462       O  
ATOM    447  OE2 GLU C  57     -17.301  41.920 -51.276  1.00 72.77           O  
ANISOU  447  OE2 GLU C  57     8806   8771  10074    274   -129    464       O  
ATOM    448  N   VAL C  58     -17.083  38.157 -55.617  1.00 31.32           N  
ANISOU  448  N   VAL C  58     3464   3746   4690     46   -142    632       N  
ATOM    449  CA  VAL C  58     -15.902  37.576 -56.245  1.00 32.51           C  
ANISOU  449  CA  VAL C  58     3628   3898   4825    -10   -154    626       C  
ATOM    450  C   VAL C  58     -14.981  38.729 -56.613  1.00 35.60           C  
ANISOU  450  C   VAL C  58     4043   4225   5258    -11   -160    645       C  
ATOM    451  O   VAL C  58     -15.377  39.635 -57.358  1.00 37.54           O  
ANISOU  451  O   VAL C  58     4276   4461   5528      9   -165    700       O  
ATOM    452  CB  VAL C  58     -16.258  36.733 -57.480  1.00 30.07           C  
ANISOU  452  CB  VAL C  58     3283   3665   4477    -42   -166    659       C  
ATOM    453  CG1 VAL C  58     -14.996  36.321 -58.231  1.00 29.48           C  
ANISOU  453  CG1 VAL C  58     3220   3597   4385    -89   -177    652       C  
ATOM    454  CG2 VAL C  58     -17.058  35.508 -57.072  1.00 21.41           C  
ANISOU  454  CG2 VAL C  58     2163   2620   3351    -52   -164    637       C  
ATOM    455  N   GLN C  59     -13.762  38.708 -56.074  1.00 41.24           N  
ANISOU  455  N   GLN C  59     4789   4894   5986    -35   -162    602       N  
ATOM    456  CA  GLN C  59     -12.827  39.798 -56.324  1.00 35.00           C  
ANISOU  456  CA  GLN C  59     4018   4035   5246    -43   -170    618       C  
ATOM    457  C   GLN C  59     -12.194  39.700 -57.706  1.00 27.81           C  
ANISOU  457  C   GLN C  59     3088   3159   4319    -87   -174    671       C  
ATOM    458  O   GLN C  59     -11.876  40.729 -58.314  1.00 35.51           O  
ANISOU  458  O   GLN C  59     4062   4095   5334    -91   -178    723       O  
ATOM    459  CB  GLN C  59     -11.745  39.818 -55.241  1.00 35.04           C  
ANISOU  459  CB  GLN C  59     4057   3985   5272    -53   -173    549       C  
ATOM    460  CG  GLN C  59     -10.696  40.902 -55.419  1.00 54.00           C  
ANISOU  460  CG  GLN C  59     6474   6310   7735    -71   -184    559       C  
ATOM    461  CD  GLN C  59      -9.489  40.683 -54.535  1.00 66.49           C  
ANISOU  461  CD  GLN C  59     8081   7857   9327    -92   -192    489       C  
ATOM    462  OE1 GLN C  59      -8.504  40.074 -54.952  1.00 66.35           O  
ANISOU  462  OE1 GLN C  59     8058   7866   9287   -138   -193    483       O  
ATOM    463  NE2 GLN C  59      -9.557  41.179 -53.306  1.00 75.25           N  
ANISOU  463  NE2 GLN C  59     9216   8912  10466    -52   -198    430       N  
ATOM    464  N   GLY C  60     -12.020  38.489 -58.224  1.00 19.20           N  
ANISOU  464  N   GLY C  60     1981   2142   3171   -119   -176    660       N  
ATOM    465  CA  GLY C  60     -11.444  38.315 -59.542  1.00 29.85           C  
ANISOU  465  CA  GLY C  60     3307   3542   4491   -154   -180    703       C  
ATOM    466  C   GLY C  60     -12.500  38.196 -60.618  1.00 34.82           C  
ANISOU  466  C   GLY C  60     3901   4242   5086   -139   -184    758       C  
ATOM    467  O   GLY C  60     -13.293  39.120 -60.819  1.00 32.69           O  
ANISOU  467  O   GLY C  60     3625   3954   4843   -106   -183    810       O  
ATOM    468  N   TYR C  61     -12.527  37.066 -61.316  1.00 39.76           N  
ANISOU  468  N   TYR C  61     4504   4950   5653   -160   -193    744       N  
ATOM    469  CA  TYR C  61     -13.553  36.793 -62.308  1.00 39.04           C  
ANISOU  469  CA  TYR C  61     4375   4935   5522   -146   -204    783       C  
ATOM    470  C   TYR C  61     -14.271  35.497 -61.961  1.00 40.08           C  
ANISOU  470  C   TYR C  61     4494   5108   5626   -150   -215    730       C  
ATOM    471  O   TYR C  61     -13.821  34.707 -61.128  1.00 40.32           O  
ANISOU  471  O   TYR C  61     4545   5115   5659   -168   -215    670       O  
ATOM    472  CB  TYR C  61     -12.958  36.711 -63.722  1.00 32.98           C  
ANISOU  472  CB  TYR C  61     3582   4241   4708   -166   -210    822       C  
ATOM    473  CG  TYR C  61     -11.909  35.634 -63.884  1.00 29.76           C  
ANISOU  473  CG  TYR C  61     3176   3870   4262   -201   -216    764       C  
ATOM    474  CD1 TYR C  61     -12.271  34.309 -64.097  1.00 22.28           C  
ANISOU  474  CD1 TYR C  61     2212   2983   3272   -208   -237    710       C  
ATOM    475  CD2 TYR C  61     -10.556  35.943 -63.832  1.00 35.07           C  
ANISOU  475  CD2 TYR C  61     3862   4516   4945   -226   -205    760       C  
ATOM    476  CE1 TYR C  61     -11.316  33.322 -64.239  1.00 29.62           C  
ANISOU  476  CE1 TYR C  61     3144   3940   4170   -233   -247    652       C  
ATOM    477  CE2 TYR C  61      -9.594  34.964 -63.983  1.00 27.02           C  
ANISOU  477  CE2 TYR C  61     2841   3536   3891   -251   -212    704       C  
ATOM    478  CZ  TYR C  61      -9.980  33.655 -64.181  1.00 33.37           C  
ANISOU  478  CZ  TYR C  61     3632   4394   4651   -252   -234    648       C  
ATOM    479  OH  TYR C  61      -9.026  32.676 -64.325  1.00 37.00           O  
ANISOU  479  OH  TYR C  61     4091   4887   5080   -270   -245    587       O  
ATOM    480  N   VAL C  62     -15.400  35.286 -62.628  1.00 33.78           N  
ANISOU  480  N   VAL C  62     3660   4371   4805   -134   -227    756       N  
ATOM    481  CA  VAL C  62     -16.171  34.056 -62.534  1.00 35.38           C  
ANISOU  481  CA  VAL C  62     3838   4619   4984   -144   -244    716       C  
ATOM    482  C   VAL C  62     -16.000  33.309 -63.847  1.00 33.88           C  
ANISOU  482  C   VAL C  62     3619   4514   4741   -162   -270    710       C  
ATOM    483  O   VAL C  62     -16.341  33.829 -64.916  1.00 43.43           O  
ANISOU  483  O   VAL C  62     4800   5777   5923   -144   -278    760       O  
ATOM    484  CB  VAL C  62     -17.654  34.337 -62.249  1.00 28.83           C  
ANISOU  484  CB  VAL C  62     2982   3799   4172   -112   -242    741       C  
ATOM    485  CG1 VAL C  62     -18.450  33.046 -62.290  1.00 27.00           C  
ANISOU  485  CG1 VAL C  62     2717   3619   3923   -132   -262    707       C  
ATOM    486  CG2 VAL C  62     -17.816  35.024 -60.903  1.00 19.74           C  
ANISOU  486  CG2 VAL C  62     1859   2575   3068    -87   -216    736       C  
ATOM    487  N   LEU C  63     -15.456  32.100 -63.769  1.00 30.60           N  
ANISOU  487  N   LEU C  63     3209   4111   4308   -193   -287    647       N  
ATOM    488  CA  LEU C  63     -15.303  31.218 -64.917  1.00 38.08           C  
ANISOU  488  CA  LEU C  63     4127   5137   5203   -205   -318    619       C  
ATOM    489  C   LEU C  63     -16.144  29.978 -64.664  1.00 37.33           C  
ANISOU  489  C   LEU C  63     4013   5056   5116   -221   -346    570       C  
ATOM    490  O   LEU C  63     -15.942  29.285 -63.665  1.00 31.00           O  
ANISOU  490  O   LEU C  63     3235   4200   4344   -241   -344    529       O  
ATOM    491  CB  LEU C  63     -13.834  30.846 -65.135  1.00 39.78           C  
ANISOU  491  CB  LEU C  63     4363   5356   5396   -225   -318    581       C  
ATOM    492  CG  LEU C  63     -13.519  29.879 -66.278  1.00 40.26           C  
ANISOU  492  CG  LEU C  63     4396   5502   5399   -231   -352    538       C  
ATOM    493  CD1 LEU C  63     -13.939  30.473 -67.612  1.00 40.04           C  
ANISOU  493  CD1 LEU C  63     4329   5564   5320   -208   -359    592       C  
ATOM    494  CD2 LEU C  63     -12.039  29.524 -66.290  1.00 41.07           C  
ANISOU  494  CD2 LEU C  63     4518   5602   5484   -246   -349    495       C  
ATOM    495  N   ILE C  64     -17.102  29.719 -65.547  1.00 35.08           N  
ANISOU  495  N   ILE C  64     3682   4840   4806   -213   -374    579       N  
ATOM    496  CA  ILE C  64     -17.996  28.570 -65.456  1.00 29.18           C  
ANISOU  496  CA  ILE C  64     2906   4108   4072   -232   -406    536       C  
ATOM    497  C   ILE C  64     -17.890  27.851 -66.792  1.00 31.21           C  
ANISOU  497  C   ILE C  64     3130   4448   4278   -234   -452    497       C  
ATOM    498  O   ILE C  64     -18.392  28.350 -67.810  1.00 30.82           O  
ANISOU  498  O   ILE C  64     3047   4474   4190   -209   -464    530       O  
ATOM    499  CB  ILE C  64     -19.444  28.984 -65.159  1.00 32.64           C  
ANISOU  499  CB  ILE C  64     3310   4554   4537   -217   -400    580       C  
ATOM    500  CG1 ILE C  64     -19.499  29.822 -63.880  1.00 31.48           C  
ANISOU  500  CG1 ILE C  64     3194   4333   4432   -203   -354    614       C  
ATOM    501  CG2 ILE C  64     -20.345  27.763 -65.041  1.00 22.59           C  
ANISOU  501  CG2 ILE C  64     2002   3295   3288   -247   -434    539       C  
ATOM    502  CD1 ILE C  64     -20.856  30.420 -63.589  1.00 25.04           C  
ANISOU  502  CD1 ILE C  64     2345   3532   3639   -176   -342    659       C  
ATOM    503  N   ALA C  65     -17.222  26.699 -66.806  1.00 36.78           N  
ANISOU  503  N   ALA C  65     3848   5145   4982   -259   -480    424       N  
ATOM    504  CA  ALA C  65     -16.853  26.160 -68.108  1.00 37.14           C  
ANISOU  504  CA  ALA C  65     3868   5275   4969   -250   -520    378       C  
ATOM    505  C   ALA C  65     -16.711  24.646 -68.067  1.00 42.14           C  
ANISOU  505  C   ALA C  65     4500   5891   5620   -276   -568    287       C  
ATOM    506  O   ALA C  65     -16.340  24.069 -67.044  1.00 38.39           O  
ANISOU  506  O   ALA C  65     4059   5334   5193   -301   -562    261       O  
ATOM    507  CB  ALA C  65     -15.553  26.794 -68.612  1.00 30.19           C  
ANISOU  507  CB  ALA C  65     3009   4424   4040   -232   -495    393       C  
ATOM    508  N   HIS C  66     -17.006  24.021 -69.210  1.00 44.38           N  
ANISOU  508  N   HIS C  66     4743   6254   5864   -267   -620    237       N  
ATOM    509  CA  HIS C  66     -16.805  22.585 -69.429  1.00 47.32           C  
ANISOU  509  CA  HIS C  66     5111   6618   6249   -285   -678    138       C  
ATOM    510  C   HIS C  66     -17.513  21.743 -68.372  1.00 45.73           C  
ANISOU  510  C   HIS C  66     4916   6325   6136   -328   -693    123       C  
ATOM    511  O   HIS C  66     -16.982  20.747 -67.878  1.00 53.72           O  
ANISOU  511  O   HIS C  66     5953   7273   7186   -350   -716     66       O  
ATOM    512  CB  HIS C  66     -15.315  22.242 -69.501  1.00 56.21           C  
ANISOU  512  CB  HIS C  66     6272   7738   7348   -275   -675     87       C  
ATOM    513  CG  HIS C  66     -14.625  22.804 -70.706  1.00 62.00           C  
ANISOU  513  CG  HIS C  66     6988   8581   7990   -236   -669     89       C  
ATOM    514  ND1 HIS C  66     -14.859  22.337 -71.982  1.00 66.63           N  
ANISOU  514  ND1 HIS C  66     7530   9270   8516   -210   -719     35       N  
ATOM    515  CD2 HIS C  66     -13.711  23.795 -70.830  1.00 62.38           C  
ANISOU  515  CD2 HIS C  66     7051   8655   7996   -218   -619    143       C  
ATOM    516  CE1 HIS C  66     -14.120  23.017 -72.840  1.00 66.55           C  
ANISOU  516  CE1 HIS C  66     7510   9353   8422   -176   -696     61       C  
ATOM    517  NE2 HIS C  66     -13.413  23.907 -72.166  1.00 65.81           N  
ANISOU  517  NE2 HIS C  66     7450   9211   8342   -183   -635    130       N  
ATOM    518  N   ASN C  67     -18.737  22.134 -68.036  1.00 42.37           N  
ANISOU  518  N   ASN C  67     4461   5895   5742   -338   -682    179       N  
ATOM    519  CA  ASN C  67     -19.537  21.427 -67.051  1.00 39.48           C  
ANISOU  519  CA  ASN C  67     4089   5456   5456   -381   -690    181       C  
ATOM    520  C   ASN C  67     -20.692  20.704 -67.727  1.00 44.34           C  
ANISOU  520  C   ASN C  67     4644   6112   6093   -400   -750    147       C  
ATOM    521  O   ASN C  67     -21.180  21.122 -68.781  1.00 49.11           O  
ANISOU  521  O   ASN C  67     5205   6806   6647   -372   -770    148       O  
ATOM    522  CB  ASN C  67     -20.092  22.385 -65.991  1.00 45.83           C  
ANISOU  522  CB  ASN C  67     4901   6225   6286   -381   -627    269       C  
ATOM    523  CG  ASN C  67     -19.006  23.144 -65.268  1.00 48.01           C  
ANISOU  523  CG  ASN C  67     5235   6456   6549   -363   -572    299       C  
ATOM    524  OD1 ASN C  67     -18.210  22.556 -64.542  1.00 50.72           O  
ANISOU  524  OD1 ASN C  67     5619   6735   6915   -380   -569    270       O  
ATOM    525  ND2 ASN C  67     -18.980  24.458 -65.442  1.00 45.08           N  
ANISOU  525  ND2 ASN C  67     4867   6116   6144   -328   -532    357       N  
ATOM    526  N   GLN C  68     -21.124  19.609 -67.107  1.00 41.53           N  
ANISOU  526  N   GLN C  68     4280   5687   5811   -448   -780    119       N  
ATOM    527  CA  GLN C  68     -22.356  18.937 -67.489  1.00 43.98           C  
ANISOU  527  CA  GLN C  68     4528   6018   6165   -479   -833     97       C  
ATOM    528  C   GLN C  68     -23.488  19.203 -66.508  1.00 46.87           C  
ANISOU  528  C   GLN C  68     4866   6356   6588   -509   -797    175       C  
ATOM    529  O   GLN C  68     -24.632  18.832 -66.790  1.00 46.48           O  
ANISOU  529  O   GLN C  68     4753   6333   6574   -535   -832    172       O  
ATOM    530  CB  GLN C  68     -22.128  17.424 -67.609  1.00 54.41           C  
ANISOU  530  CB  GLN C  68     5850   7282   7541   -517   -905      8       C  
ATOM    531  CG  GLN C  68     -20.999  17.029 -68.551  1.00 65.11           C  
ANISOU  531  CG  GLN C  68     7230   8668   8842   -482   -946    -83       C  
ATOM    532  CD  GLN C  68     -21.353  17.222 -70.015  1.00 78.18           C  
ANISOU  532  CD  GLN C  68     8835  10441  10429   -446   -992   -129       C  
ATOM    533  OE1 GLN C  68     -22.486  17.560 -70.356  1.00 81.48           O  
ANISOU  533  OE1 GLN C  68     9199  10913  10848   -449  -1001    -99       O  
ATOM    534  NE2 GLN C  68     -20.376  17.008 -70.889  1.00 85.36           N  
ANISOU  534  NE2 GLN C  68     9760  11400  11274   -406  -1020   -203       N  
ATOM    535  N   VAL C  69     -23.193  19.838 -65.370  1.00 46.99           N  
ANISOU  535  N   VAL C  69     4921   6323   6609   -504   -727    241       N  
ATOM    536  CA  VAL C  69     -24.217  20.095 -64.370  1.00 45.40           C  
ANISOU  536  CA  VAL C  69     4692   6104   6454   -525   -687    312       C  
ATOM    537  C   VAL C  69     -25.251  21.066 -64.938  1.00 44.18           C  
ANISOU  537  C   VAL C  69     4482   6035   6269   -493   -677    355       C  
ATOM    538  O   VAL C  69     -24.940  21.945 -65.754  1.00 45.46           O  
ANISOU  538  O   VAL C  69     4651   6257   6367   -444   -671    358       O  
ATOM    539  CB  VAL C  69     -23.579  20.624 -63.072  1.00 47.71           C  
ANISOU  539  CB  VAL C  69     5044   6338   6747   -515   -618    362       C  
ATOM    540  CG1 VAL C  69     -23.393  22.138 -63.114  1.00 42.75           C  
ANISOU  540  CG1 VAL C  69     4432   5750   6062   -457   -565    409       C  
ATOM    541  CG2 VAL C  69     -24.392  20.197 -61.859  1.00 53.72           C  
ANISOU  541  CG2 VAL C  69     5783   7057   7570   -555   -593    413       C  
ATOM    542  N   ARG C  70     -26.504  20.874 -64.534  1.00 46.32           N  
ANISOU  542  N   ARG C  70     4693   6317   6588   -522   -676    390       N  
ATOM    543  CA  ARG C  70     -27.612  21.609 -65.124  1.00 48.15           C  
ANISOU  543  CA  ARG C  70     4861   6634   6800   -494   -678    422       C  
ATOM    544  C   ARG C  70     -27.865  22.943 -64.452  1.00 48.21           C  
ANISOU  544  C   ARG C  70     4878   6657   6784   -447   -606    499       C  
ATOM    545  O   ARG C  70     -28.658  23.737 -64.966  1.00 46.34           O  
ANISOU  545  O   ARG C  70     4596   6489   6522   -409   -604    529       O  
ATOM    546  CB  ARG C  70     -28.887  20.769 -65.079  1.00 49.11           C  
ANISOU  546  CB  ARG C  70     4902   6769   6988   -548   -715    419       C  
ATOM    547  CG  ARG C  70     -28.793  19.548 -65.944  1.00 50.55           C  
ANISOU  547  CG  ARG C  70     5064   6944   7197   -588   -800    334       C  
ATOM    548  CD  ARG C  70     -30.127  18.866 -66.099  1.00 48.79           C  
ANISOU  548  CD  ARG C  70     4751   6746   7039   -639   -845    330       C  
ATOM    549  NE  ARG C  70     -29.966  17.596 -66.794  1.00 50.84           N  
ANISOU  549  NE  ARG C  70     4998   6978   7340   -682   -932    240       N  
ATOM    550  CZ  ARG C  70     -29.753  16.439 -66.180  1.00 57.35           C  
ANISOU  550  CZ  ARG C  70     5838   7708   8245   -747   -955    219       C  
ATOM    551  NH1 ARG C  70     -29.687  16.393 -64.856  1.00 56.38           N  
ANISOU  551  NH1 ARG C  70     5741   7518   8162   -775   -894    289       N  
ATOM    552  NH2 ARG C  70     -29.611  15.327 -66.887  1.00 65.71           N  
ANISOU  552  NH2 ARG C  70     6884   8738   9344   -779  -1041    128       N  
ATOM    553  N   GLN C  71     -27.222  23.208 -63.322  1.00 46.80           N  
ANISOU  553  N   GLN C  71     4756   6414   6612   -443   -551    526       N  
ATOM    554  CA  GLN C  71     -27.430  24.468 -62.626  1.00 46.70           C  
ANISOU  554  CA  GLN C  71     4755   6408   6581   -394   -488    588       C  
ATOM    555  C   GLN C  71     -26.352  24.675 -61.577  1.00 47.75           C  
ANISOU  555  C   GLN C  71     4964   6469   6711   -387   -442    594       C  
ATOM    556  O   GLN C  71     -26.085  23.777 -60.771  1.00 57.56           O  
ANISOU  556  O   GLN C  71     6224   7657   7987   -430   -439    584       O  
ATOM    557  CB  GLN C  71     -28.812  24.538 -61.960  1.00 57.57           C  
ANISOU  557  CB  GLN C  71     6063   7816   7994   -402   -464    636       C  
ATOM    558  CG  GLN C  71     -28.927  25.699 -60.974  1.00 85.70           C  
ANISOU  558  CG  GLN C  71     9646  11373  11543   -349   -396    688       C  
ATOM    559  CD  GLN C  71     -28.719  27.074 -61.597  1.00 99.94           C  
ANISOU  559  CD  GLN C  71    11468  13203  13300   -278   -385    705       C  
ATOM    560  OE1 GLN C  71     -28.206  27.205 -62.708  1.00110.55           O  
ANISOU  560  OE1 GLN C  71    12826  14564  14612   -267   -420    682       O  
ATOM    561  NE2 GLN C  71     -29.060  28.118 -60.836  1.00103.11           N  
ANISOU  561  NE2 GLN C  71    11873  13604  13699   -227   -335    746       N  
ATOM    562  N   VAL C  72     -25.772  25.864 -61.566  1.00 40.06           N  
ANISOU  562  N   VAL C  72     4031   5491   5699   -334   -408    614       N  
ATOM    563  CA  VAL C  72     -24.819  26.277 -60.537  1.00 42.40           C  
ANISOU  563  CA  VAL C  72     4394   5724   5991   -319   -364    620       C  
ATOM    564  C   VAL C  72     -25.496  27.303 -59.646  1.00 39.03           C  
ANISOU  564  C   VAL C  72     3957   5304   5568   -275   -312    669       C  
ATOM    565  O   VAL C  72     -25.977  28.340 -60.136  1.00 41.76           O  
ANISOU  565  O   VAL C  72     4281   5686   5897   -228   -305    696       O  
ATOM    566  CB  VAL C  72     -23.506  26.803 -61.153  1.00 43.90           C  
ANISOU  566  CB  VAL C  72     4640   5895   6143   -296   -368    597       C  
ATOM    567  CG1 VAL C  72     -22.991  25.834 -62.213  1.00 42.45           C  
ANISOU  567  CG1 VAL C  72     4453   5728   5946   -327   -423    543       C  
ATOM    568  CG2 VAL C  72     -23.627  28.193 -61.764  1.00 55.73           C  
ANISOU  568  CG2 VAL C  72     6136   7427   7613   -241   -354    634       C  
ATOM    569  N   PRO C  73     -25.632  27.043 -58.345  1.00 38.73           N  
ANISOU  569  N   PRO C  73     3928   5238   5551   -285   -276    683       N  
ATOM    570  CA  PRO C  73     -26.416  27.938 -57.489  1.00 36.49           C  
ANISOU  570  CA  PRO C  73     3623   4975   5267   -238   -229    722       C  
ATOM    571  C   PRO C  73     -25.611  29.103 -56.936  1.00 41.18           C  
ANISOU  571  C   PRO C  73     4277   5527   5841   -183   -195    720       C  
ATOM    572  O   PRO C  73     -24.959  28.990 -55.894  1.00 54.93           O  
ANISOU  572  O   PRO C  73     6063   7226   7581   -183   -170    709       O  
ATOM    573  CB  PRO C  73     -26.901  27.010 -56.373  1.00 38.21           C  
ANISOU  573  CB  PRO C  73     3817   5190   5509   -277   -208    739       C  
ATOM    574  CG  PRO C  73     -25.830  25.984 -56.261  1.00 38.14           C  
ANISOU  574  CG  PRO C  73     3860   5124   5509   -326   -230    706       C  
ATOM    575  CD  PRO C  73     -25.258  25.795 -57.650  1.00 40.57           C  
ANISOU  575  CD  PRO C  73     4177   5428   5808   -340   -282    666       C  
ATOM    576  N   LEU C  74     -25.661  30.234 -57.629  1.00 34.35           N  
ANISOU  576  N   LEU C  74     3413   4673   4964   -135   -198    733       N  
ATOM    577  CA  LEU C  74     -25.025  31.472 -57.199  1.00 21.32           C  
ANISOU  577  CA  LEU C  74     1813   2979   3308    -81   -172    733       C  
ATOM    578  C   LEU C  74     -26.042  32.601 -57.101  1.00 29.68           C  
ANISOU  578  C   LEU C  74     2837   4068   4373    -15   -154    766       C  
ATOM    579  O   LEU C  74     -25.774  33.740 -57.488  1.00 28.35           O  
ANISOU  579  O   LEU C  74     2692   3875   4206     31   -155    777       O  
ATOM    580  CB  LEU C  74     -23.889  31.858 -58.142  1.00 25.37           C  
ANISOU  580  CB  LEU C  74     2371   3460   3808    -84   -195    721       C  
ATOM    581  CG  LEU C  74     -22.855  30.765 -58.471  1.00 29.96           C  
ANISOU  581  CG  LEU C  74     2981   4023   4380   -141   -220    684       C  
ATOM    582  CD1 LEU C  74     -22.194  31.032 -59.818  1.00 25.98           C  
ANISOU  582  CD1 LEU C  74     2487   3532   3854   -144   -249    683       C  
ATOM    583  CD2 LEU C  74     -21.810  30.655 -57.376  1.00 17.83           C  
ANISOU  583  CD2 LEU C  74     1504   2424   2848   -147   -198    656       C  
ATOM    584  N   GLN C  75     -27.228  32.291 -56.572  1.00 27.45           N  
ANISOU  584  N   GLN C  75     2495   3837   4097    -10   -137    783       N  
ATOM    585  CA  GLN C  75     -28.297  33.282 -56.482  1.00 28.72           C  
ANISOU  585  CA  GLN C  75     2612   4036   4262     57   -121    810       C  
ATOM    586  C   GLN C  75     -27.947  34.447 -55.567  1.00 28.93           C  
ANISOU  586  C   GLN C  75     2683   4016   4292    125    -90    799       C  
ATOM    587  O   GLN C  75     -28.639  35.469 -55.593  1.00 30.39           O  
ANISOU  587  O   GLN C  75     2846   4216   4485    193    -83    814       O  
ATOM    588  CB  GLN C  75     -29.598  32.635 -55.991  1.00 26.79           C  
ANISOU  588  CB  GLN C  75     2290   3865   4024     45   -105    829       C  
ATOM    589  CG  GLN C  75     -30.228  31.657 -56.963  1.00 34.06           C  
ANISOU  589  CG  GLN C  75     3150   4838   4953    -13   -143    839       C  
ATOM    590  CD  GLN C  75     -29.678  30.251 -56.823  1.00 46.64           C  
ANISOU  590  CD  GLN C  75     4758   6408   6555    -96   -158    820       C  
ATOM    591  OE1 GLN C  75     -28.663  30.031 -56.162  1.00 57.02           O  
ANISOU  591  OE1 GLN C  75     6136   7664   7864   -110   -143    800       O  
ATOM    592  NE2 GLN C  75     -30.349  29.290 -57.447  1.00 47.21           N  
ANISOU  592  NE2 GLN C  75     4771   6523   6645   -150   -191    824       N  
ATOM    593  N   ARG C  76     -26.896  34.318 -54.764  1.00 29.59           N  
ANISOU  593  N   ARG C  76     2829   4042   4371    113    -75    767       N  
ATOM    594  CA  ARG C  76     -26.524  35.332 -53.788  1.00 32.47           C  
ANISOU  594  CA  ARG C  76     3236   4362   4740    175    -49    744       C  
ATOM    595  C   ARG C  76     -25.305  36.145 -54.198  1.00 34.51           C  
ANISOU  595  C   ARG C  76     3561   4538   5012    184    -67    727       C  
ATOM    596  O   ARG C  76     -24.951  37.094 -53.495  1.00 40.17           O  
ANISOU  596  O   ARG C  76     4315   5206   5742    236    -55    703       O  
ATOM    597  CB  ARG C  76     -26.282  34.668 -52.431  1.00 23.98           C  
ANISOU  597  CB  ARG C  76     2176   3290   3646    162    -18    720       C  
ATOM    598  CG  ARG C  76     -27.454  33.824 -51.985  1.00 39.22           C  
ANISOU  598  CG  ARG C  76     4036   5302   5564    145      4    748       C  
ATOM    599  CD  ARG C  76     -28.141  34.451 -50.798  1.00 56.96           C  
ANISOU  599  CD  ARG C  76     6260   7587   7795    218     46    742       C  
ATOM    600  NE  ARG C  76     -27.172  34.749 -49.751  1.00 63.90           N  
ANISOU  600  NE  ARG C  76     7204   8418   8658    244     62    700       N  
ATOM    601  CZ  ARG C  76     -26.795  33.870 -48.833  1.00 81.93           C  
ANISOU  601  CZ  ARG C  76     9502  10712  10915    211     82    695       C  
ATOM    602  NH1 ARG C  76     -25.906  34.207 -47.910  1.00 87.42           N  
ANISOU  602  NH1 ARG C  76    10256  11368  11593    242     92    652       N  
ATOM    603  NH2 ARG C  76     -27.313  32.650 -48.842  1.00 89.09           N  
ANISOU  603  NH2 ARG C  76    10364  11667  11818    148     88    735       N  
ATOM    604  N   LEU C  77     -24.666  35.805 -55.313  1.00 26.78           N  
ANISOU  604  N   LEU C  77     2596   3547   4032    135    -97    738       N  
ATOM    605  CA  LEU C  77     -23.513  36.552 -55.802  1.00 33.80           C  
ANISOU  605  CA  LEU C  77     3539   4367   4935    137   -112    733       C  
ATOM    606  C   LEU C  77     -23.957  37.954 -56.202  1.00 29.08           C  
ANISOU  606  C   LEU C  77     2937   3748   4364    202   -117    763       C  
ATOM    607  O   LEU C  77     -24.737  38.126 -57.146  1.00 37.96           O  
ANISOU  607  O   LEU C  77     4019   4918   5486    214   -133    805       O  
ATOM    608  CB  LEU C  77     -22.869  35.816 -56.976  1.00 18.92           C  
ANISOU  608  CB  LEU C  77     1657   2496   3034     75   -140    742       C  
ATOM    609  CG  LEU C  77     -21.856  36.601 -57.831  1.00 21.69           C  
ANISOU  609  CG  LEU C  77     2046   2802   3395     74   -156    758       C  
ATOM    610  CD1 LEU C  77     -20.756  37.210 -56.971  1.00 18.64           C  
ANISOU  610  CD1 LEU C  77     1718   2334   3032     83   -144    726       C  
ATOM    611  CD2 LEU C  77     -21.263  35.719 -58.910  1.00 18.56           C  
ANISOU  611  CD2 LEU C  77     1644   2440   2969     17   -181    759       C  
ATOM    612  N   ARG C  78     -23.462  38.959 -55.483  1.00 24.93           N  
ANISOU  612  N   ARG C  78     2453   3151   3867    245   -108    740       N  
ATOM    613  CA  ARG C  78     -23.901  40.330 -55.695  1.00 29.85           C  
ANISOU  613  CA  ARG C  78     3075   3738   4527    314   -115    764       C  
ATOM    614  C   ARG C  78     -22.944  41.153 -56.544  1.00 41.42           C  
ANISOU  614  C   ARG C  78     4580   5133   6024    303   -138    793       C  
ATOM    615  O   ARG C  78     -23.402  41.996 -57.321  1.00 39.47           O  
ANISOU  615  O   ARG C  78     4320   4878   5800    338   -153    843       O  
ATOM    616  CB  ARG C  78     -24.103  41.037 -54.352  1.00 32.84           C  
ANISOU  616  CB  ARG C  78     3471   4080   4926    380    -96    717       C  
ATOM    617  CG  ARG C  78     -25.007  42.252 -54.434  1.00 49.01           C  
ANISOU  617  CG  ARG C  78     5499   6114   7008    465   -103    735       C  
ATOM    618  CD  ARG C  78     -26.437  41.885 -54.061  1.00 60.22           C  
ANISOU  618  CD  ARG C  78     6851   7628   8400    504    -83    739       C  
ATOM    619  NE  ARG C  78     -27.424  42.480 -54.958  1.00 62.92           N  
ANISOU  619  NE  ARG C  78     7150   8000   8758    548   -100    790       N  
ATOM    620  CZ  ARG C  78     -28.736  42.446 -54.747  1.00 66.50           C  
ANISOU  620  CZ  ARG C  78     7539   8530   9197    596    -87    797       C  
ATOM    621  NH1 ARG C  78     -29.218  41.852 -53.663  1.00 65.44           N  
ANISOU  621  NH1 ARG C  78     7376   8455   9034    605    -54    761       N  
ATOM    622  NH2 ARG C  78     -29.568  43.007 -55.614  1.00 78.34           N  
ANISOU  622  NH2 ARG C  78     8999  10055  10711    638   -108    844       N  
ATOM    623  N   ILE C  79     -21.634  40.946 -56.426  1.00 42.15           N  
ANISOU  623  N   ILE C  79     4719   5176   6120    255   -140    768       N  
ATOM    624  CA  ILE C  79     -20.681  41.821 -57.104  1.00 37.96           C  
ANISOU  624  CA  ILE C  79     4222   4575   5626    244   -157    799       C  
ATOM    625  C   ILE C  79     -19.480  41.010 -57.570  1.00 32.09           C  
ANISOU  625  C   ILE C  79     3498   3839   4857    168   -160    792       C  
ATOM    626  O   ILE C  79     -18.945  40.182 -56.826  1.00 31.45           O  
ANISOU  626  O   ILE C  79     3433   3762   4756    138   -151    738       O  
ATOM    627  CB  ILE C  79     -20.240  42.989 -56.197  1.00 39.18           C  
ANISOU  627  CB  ILE C  79     4418   4627   5841    288   -158    764       C  
ATOM    628  CG1 ILE C  79     -19.150  43.818 -56.880  1.00 36.06           C  
ANISOU  628  CG1 ILE C  79     4056   4153   5493    261   -176    800       C  
ATOM    629  CG2 ILE C  79     -19.776  42.481 -54.835  1.00 36.48           C  
ANISOU  629  CG2 ILE C  79     4102   4273   5486    284   -143    684       C  
ATOM    630  CD1 ILE C  79     -18.863  45.134 -56.196  1.00 32.83           C  
ANISOU  630  CD1 ILE C  79     3682   3632   5160    308   -188    777       C  
ATOM    631  N   VAL C  80     -19.067  41.249 -58.813  1.00 34.26           N  
ANISOU  631  N   VAL C  80     3767   4122   5128    143   -174    849       N  
ATOM    632  CA  VAL C  80     -17.807  40.755 -59.358  1.00 36.61           C  
ANISOU  632  CA  VAL C  80     4081   4421   5406     81   -178    847       C  
ATOM    633  C   VAL C  80     -16.917  41.967 -59.612  1.00 37.52           C  
ANISOU  633  C   VAL C  80     4226   4454   5576     80   -184    883       C  
ATOM    634  O   VAL C  80     -17.299  42.880 -60.355  1.00 41.61           O  
ANISOU  634  O   VAL C  80     4733   4957   6118    106   -193    952       O  
ATOM    635  CB  VAL C  80     -18.022  39.945 -60.646  1.00 30.07           C  
ANISOU  635  CB  VAL C  80     3215   3688   4520     50   -189    884       C  
ATOM    636  CG1 VAL C  80     -16.685  39.571 -61.264  1.00 23.02           C  
ANISOU  636  CG1 VAL C  80     2338   2803   3607     -5   -192    883       C  
ATOM    637  CG2 VAL C  80     -18.859  38.706 -60.359  1.00 19.57           C  
ANISOU  637  CG2 VAL C  80     1856   2429   3151     42   -189    845       C  
ATOM    638  N   ARG C  81     -15.734  41.984 -58.997  1.00 36.63           N  
ANISOU  638  N   ARG C  81     4147   4284   5486     49   -181    839       N  
ATOM    639  CA  ARG C  81     -14.882  43.166 -59.063  1.00 41.67           C  
ANISOU  639  CA  ARG C  81     4811   4830   6190     44   -188    866       C  
ATOM    640  C   ARG C  81     -13.955  43.172 -60.269  1.00 42.13           C  
ANISOU  640  C   ARG C  81     4860   4913   6235     -9   -189    927       C  
ATOM    641  O   ARG C  81     -13.654  44.247 -60.801  1.00 48.78           O  
ANISOU  641  O   ARG C  81     5706   5701   7127     -9   -195    993       O  
ATOM    642  CB  ARG C  81     -14.056  43.295 -57.781  1.00 34.65           C  
ANISOU  642  CB  ARG C  81     3960   3867   5339     39   -188    786       C  
ATOM    643  CG  ARG C  81     -14.905  43.551 -56.553  1.00 30.23           C  
ANISOU  643  CG  ARG C  81     3411   3278   4797    101   -186    729       C  
ATOM    644  CD  ARG C  81     -14.071  43.959 -55.357  1.00 29.44           C  
ANISOU  644  CD  ARG C  81     3348   3096   4740    106   -192    654       C  
ATOM    645  NE  ARG C  81     -14.893  44.060 -54.156  1.00 36.49           N  
ANISOU  645  NE  ARG C  81     4248   3984   5631    170   -188    593       N  
ATOM    646  CZ  ARG C  81     -15.555  45.155 -53.796  1.00 35.33           C  
ANISOU  646  CZ  ARG C  81     4107   3781   5537    235   -198    589       C  
ATOM    647  NH1 ARG C  81     -15.493  46.247 -54.547  1.00 40.04           N  
ANISOU  647  NH1 ARG C  81     4706   4308   6199    241   -216    647       N  
ATOM    648  NH2 ARG C  81     -16.282  45.157 -52.688  1.00 30.93           N  
ANISOU  648  NH2 ARG C  81     3550   3236   4965    297   -191    528       N  
ATOM    649  N   GLY C  82     -13.498  42.006 -60.712  1.00 37.39           N  
ANISOU  649  N   GLY C  82     4245   4394   5569    -51   -184    908       N  
ATOM    650  CA  GLY C  82     -12.654  41.954 -61.887  1.00 42.30           C  
ANISOU  650  CA  GLY C  82     4850   5059   6164    -94   -182    963       C  
ATOM    651  C   GLY C  82     -11.267  42.530 -61.709  1.00 47.16           C  
ANISOU  651  C   GLY C  82     5484   5606   6827   -134   -179    964       C  
ATOM    652  O   GLY C  82     -10.717  43.095 -62.659  1.00 52.37           O  
ANISOU  652  O   GLY C  82     6130   6274   7495   -158   -176   1041       O  
ATOM    653  N   THR C  83     -10.685  42.412 -60.512  1.00 42.06           N  
ANISOU  653  N   THR C  83     4868   4899   6215   -141   -180    884       N  
ATOM    654  CA  THR C  83      -9.289  42.803 -60.343  1.00 42.47           C  
ANISOU  654  CA  THR C  83     4931   4897   6308   -185   -180    875       C  
ATOM    655  C   THR C  83      -8.379  41.958 -61.225  1.00 42.48           C  
ANISOU  655  C   THR C  83     4906   4987   6247   -233   -171    886       C  
ATOM    656  O   THR C  83      -7.324  42.429 -61.665  1.00 46.11           O  
ANISOU  656  O   THR C  83     5356   5432   6732   -273   -166    922       O  
ATOM    657  CB  THR C  83      -8.882  42.693 -58.873  1.00 39.60           C  
ANISOU  657  CB  THR C  83     4601   4468   5978   -177   -187    777       C  
ATOM    658  OG1 THR C  83      -8.849  41.314 -58.485  1.00 50.45           O  
ANISOU  658  OG1 THR C  83     5974   5910   7283   -183   -183    710       O  
ATOM    659  CG2 THR C  83      -9.877  43.435 -57.996  1.00 27.38           C  
ANISOU  659  CG2 THR C  83     3074   2851   4477   -118   -196    756       C  
ATOM    660  N   GLN C  84      -8.768  40.711 -61.480  1.00 43.99           N  
ANISOU  660  N   GLN C  84     5084   5270   6361   -230   -170    852       N  
ATOM    661  CA  GLN C  84      -8.256  39.907 -62.578  1.00 45.79           C  
ANISOU  661  CA  GLN C  84     5280   5601   6517   -258   -166    869       C  
ATOM    662  C   GLN C  84      -9.406  39.617 -63.534  1.00 43.77           C  
ANISOU  662  C   GLN C  84     4998   5427   6207   -232   -170    915       C  
ATOM    663  O   GLN C  84     -10.577  39.643 -63.152  1.00 45.81           O  
ANISOU  663  O   GLN C  84     5262   5672   6473   -195   -176    909       O  
ATOM    664  CB  GLN C  84      -7.653  38.586 -62.094  1.00 45.26           C  
ANISOU  664  CB  GLN C  84     5218   5569   6407   -276   -170    777       C  
ATOM    665  CG  GLN C  84      -6.730  38.688 -60.901  1.00 55.95           C  
ANISOU  665  CG  GLN C  84     6602   6847   7809   -290   -172    713       C  
ATOM    666  CD  GLN C  84      -6.428  37.324 -60.313  1.00 63.27           C  
ANISOU  666  CD  GLN C  84     7539   7806   8694   -294   -181    626       C  
ATOM    667  OE1 GLN C  84      -6.812  37.022 -59.182  1.00 65.67           O  
ANISOU  667  OE1 GLN C  84     7870   8069   9011   -274   -186    572       O  
ATOM    668  NE2 GLN C  84      -5.752  36.484 -61.088  1.00 65.17           N  
ANISOU  668  NE2 GLN C  84     7757   8125   8882   -316   -182    614       N  
ATOM    669  N   LEU C  85      -9.069  39.338 -64.789  1.00 36.26           N  
ANISOU  669  N   LEU C  85     4012   4568   5196   -248   -167    959       N  
ATOM    670  CA  LEU C  85     -10.072  39.063 -65.809  1.00 35.17           C  
ANISOU  670  CA  LEU C  85     3844   4520   4998   -222   -175   1001       C  
ATOM    671  C   LEU C  85      -9.644  37.895 -66.678  1.00 38.18           C  
ANISOU  671  C   LEU C  85     4196   5018   5292   -237   -181    968       C  
ATOM    672  O   LEU C  85      -8.485  37.806 -67.089  1.00 46.43           O  
ANISOU  672  O   LEU C  85     5229   6096   6316   -265   -171    970       O  
ATOM    673  CB  LEU C  85     -10.336  40.286 -66.703  1.00 31.27           C  
ANISOU  673  CB  LEU C  85     3334   4029   4519   -209   -168   1118       C  
ATOM    674  CG  LEU C  85     -10.545  41.649 -66.020  1.00 33.51           C  
ANISOU  674  CG  LEU C  85     3646   4186   4899   -195   -165   1162       C  
ATOM    675  CD1 LEU C  85     -10.402  42.787 -67.018  1.00 36.62           C  
ANISOU  675  CD1 LEU C  85     4023   4581   5310   -197   -158   1287       C  
ATOM    676  CD2 LEU C  85     -11.908  41.692 -65.356  1.00 33.01           C  
ANISOU  676  CD2 LEU C  85     3595   4090   4859   -147   -178   1136       C  
ATOM    677  N   PHE C  86     -10.595  37.004 -66.946  1.00 40.56           N  
ANISOU  677  N   PHE C  86     4482   5383   5547   -216   -201    933       N  
ATOM    678  CA  PHE C  86     -10.349  35.872 -67.829  1.00 40.42           C  
ANISOU  678  CA  PHE C  86     4434   5475   5447   -221   -216    892       C  
ATOM    679  C   PHE C  86     -10.038  36.360 -69.238  1.00 43.42           C  
ANISOU  679  C   PHE C  86     4778   5951   5770   -217   -208    972       C  
ATOM    680  O   PHE C  86     -10.757  37.200 -69.787  1.00 44.23           O  
ANISOU  680  O   PHE C  86     4868   6067   5872   -194   -206   1057       O  
ATOM    681  CB  PHE C  86     -11.572  34.951 -67.841  1.00 37.48           C  
ANISOU  681  CB  PHE C  86     4049   5140   5050   -201   -244    845       C  
ATOM    682  CG  PHE C  86     -11.389  33.706 -68.652  1.00 38.52           C  
ANISOU  682  CG  PHE C  86     4154   5374   5110   -204   -269    785       C  
ATOM    683  CD1 PHE C  86     -10.673  32.636 -68.145  1.00 40.00           C  
ANISOU  683  CD1 PHE C  86     4355   5547   5295   -224   -280    695       C  
ATOM    684  CD2 PHE C  86     -11.938  33.603 -69.919  1.00 42.62           C  
ANISOU  684  CD2 PHE C  86     4632   6000   5560   -181   -287    815       C  
ATOM    685  CE1 PHE C  86     -10.502  31.486 -68.891  1.00 40.11           C  
ANISOU  685  CE1 PHE C  86     4345   5647   5248   -222   -309    632       C  
ATOM    686  CE2 PHE C  86     -11.772  32.454 -70.668  1.00 41.12           C  
ANISOU  686  CE2 PHE C  86     4416   5905   5303   -179   -316    748       C  
ATOM    687  CZ  PHE C  86     -11.053  31.395 -70.153  1.00 38.48           C  
ANISOU  687  CZ  PHE C  86     4098   5548   4975   -199   -328    654       C  
ATOM    688  N   GLU C  87      -8.956  35.834 -69.819  1.00 46.91           N  
ANISOU  688  N   GLU C  87     5201   6464   6158   -235   -203    948       N  
ATOM    689  CA  GLU C  87      -8.465  36.271 -71.132  1.00 45.08           C  
ANISOU  689  CA  GLU C  87     4930   6337   5862   -233   -189   1026       C  
ATOM    690  C   GLU C  87      -8.289  37.789 -71.180  1.00 44.90           C  
ANISOU  690  C   GLU C  87     4912   6253   5893   -243   -162   1146       C  
ATOM    691  O   GLU C  87      -8.422  38.416 -72.234  1.00 48.94           O  
ANISOU  691  O   GLU C  87     5395   6837   6364   -230   -153   1244       O  
ATOM    692  CB  GLU C  87      -9.378  35.771 -72.257  1.00 41.32           C  
ANISOU  692  CB  GLU C  87     4418   5983   5300   -196   -214   1032       C  
ATOM    693  CG  GLU C  87      -9.235  34.270 -72.507  1.00 50.12           C  
ANISOU  693  CG  GLU C  87     5517   7175   6352   -190   -244    917       C  
ATOM    694  CD  GLU C  87     -10.308  33.700 -73.419  1.00 59.27           C  
ANISOU  694  CD  GLU C  87     6643   8435   7441   -154   -280    901       C  
ATOM    695  OE1 GLU C  87     -11.091  34.484 -73.994  1.00 56.82           O  
ANISOU  695  OE1 GLU C  87     6316   8155   7117   -130   -279    988       O  
ATOM    696  OE2 GLU C  87     -10.368  32.459 -73.556  1.00 62.92           O  
ANISOU  696  OE2 GLU C  87     7095   8944   7868   -148   -313    799       O  
ATOM    697  N   ASP C  88      -7.990  38.375 -70.018  1.00 43.56           N  
ANISOU  697  N   ASP C  88     4780   5951   5819   -264   -152   1137       N  
ATOM    698  CA  ASP C  88      -7.717  39.804 -69.849  1.00 56.06           C  
ANISOU  698  CA  ASP C  88     6375   7446   7479   -279   -132   1234       C  
ATOM    699  C   ASP C  88      -8.867  40.689 -70.328  1.00 55.35           C  
ANISOU  699  C   ASP C  88     6282   7347   7401   -243   -138   1329       C  
ATOM    700  O   ASP C  88      -8.668  41.875 -70.603  1.00 57.78           O  
ANISOU  700  O   ASP C  88     6588   7609   7755   -251   -125   1433       O  
ATOM    701  CB  ASP C  88      -6.412  40.204 -70.547  1.00 66.35           C  
ANISOU  701  CB  ASP C  88     7649   8797   8765   -317   -105   1297       C  
ATOM    702  CG  ASP C  88      -5.209  39.467 -69.994  1.00 78.12           C  
ANISOU  702  CG  ASP C  88     9141  10286  10255   -350    -99   1206       C  
ATOM    703  OD1 ASP C  88      -5.152  39.249 -68.765  1.00 82.25           O  
ANISOU  703  OD1 ASP C  88     9701  10710  10839   -356   -110   1125       O  
ATOM    704  OD2 ASP C  88      -4.315  39.110 -70.790  1.00 80.35           O  
ANISOU  704  OD2 ASP C  88     9384  10672  10472   -366    -84   1216       O  
ATOM    705  N   ASN C  89     -10.083  40.148 -70.410  1.00 57.53           N  
ANISOU  705  N   ASN C  89     6555   7661   7643   -204   -161   1296       N  
ATOM    706  CA  ASN C  89     -11.220  40.926 -70.893  1.00 54.07           C  
ANISOU  706  CA  ASN C  89     6108   7225   7210   -163   -171   1381       C  
ATOM    707  C   ASN C  89     -12.508  40.738 -70.106  1.00 49.58           C  
ANISOU  707  C   ASN C  89     5557   6607   6676   -127   -191   1329       C  
ATOM    708  O   ASN C  89     -13.384  41.604 -70.201  1.00 49.09           O  
ANISOU  708  O   ASN C  89     5495   6510   6646    -92   -198   1396       O  
ATOM    709  CB  ASN C  89     -11.507  40.603 -72.367  1.00 57.91           C  
ANISOU  709  CB  ASN C  89     6548   7867   7588   -141   -178   1432       C  
ATOM    710  CG  ASN C  89     -10.496  41.220 -73.313  1.00 63.85           C  
ANISOU  710  CG  ASN C  89     7277   8676   8309   -164   -152   1533       C  
ATOM    711  OD1 ASN C  89     -10.102  42.375 -73.150  1.00 67.58           O  
ANISOU  711  OD1 ASN C  89     7762   9061   8853   -181   -134   1622       O  
ATOM    712  ND2 ASN C  89     -10.084  40.457 -74.320  1.00 60.36           N  
ANISOU  712  ND2 ASN C  89     6795   8381   7759   -162   -151   1521       N  
ATOM    713  N   TYR C  90     -12.673  39.669 -69.329  1.00 45.59           N  
ANISOU  713  N   TYR C  90     5063   6095   6166   -134   -202   1218       N  
ATOM    714  CA  TYR C  90     -13.997  39.250 -68.892  1.00 38.97           C  
ANISOU  714  CA  TYR C  90     4221   5254   5332   -101   -221   1176       C  
ATOM    715  C   TYR C  90     -14.052  39.024 -67.388  1.00 42.24           C  
ANISOU  715  C   TYR C  90     4672   5567   5812   -108   -217   1097       C  
ATOM    716  O   TYR C  90     -13.238  38.283 -66.829  1.00 33.75           O  
ANISOU  716  O   TYR C  90     3612   4476   4734   -140   -213   1025       O  
ATOM    717  CB  TYR C  90     -14.415  37.986 -69.645  1.00 37.77           C  
ANISOU  717  CB  TYR C  90     4033   5224   5094    -98   -245   1125       C  
ATOM    718  CG  TYR C  90     -14.429  38.200 -71.139  1.00 48.43           C  
ANISOU  718  CG  TYR C  90     5345   6689   6367    -81   -252   1198       C  
ATOM    719  CD1 TYR C  90     -15.120  39.274 -71.694  1.00 50.24           C  
ANISOU  719  CD1 TYR C  90     5562   6924   6604    -46   -253   1302       C  
ATOM    720  CD2 TYR C  90     -13.729  37.351 -71.991  1.00 58.06           C  
ANISOU  720  CD2 TYR C  90     6540   8017   7505    -96   -259   1165       C  
ATOM    721  CE1 TYR C  90     -15.129  39.483 -73.059  1.00 61.89           C  
ANISOU  721  CE1 TYR C  90     7001   8513   8002    -27   -258   1376       C  
ATOM    722  CE2 TYR C  90     -13.736  37.555 -73.357  1.00 56.44           C  
ANISOU  722  CE2 TYR C  90     6296   7931   7219    -75   -263   1232       C  
ATOM    723  CZ  TYR C  90     -14.435  38.620 -73.884  1.00 61.13           C  
ANISOU  723  CZ  TYR C  90     6878   8531   7816    -42   -262   1341       C  
ATOM    724  OH  TYR C  90     -14.439  38.822 -75.244  1.00 65.99           O  
ANISOU  724  OH  TYR C  90     7455   9274   8343    -18   -267   1415       O  
ATOM    725  N   ALA C  91     -15.026  39.665 -66.744  1.00 39.91           N  
ANISOU  725  N   ALA C  91     4386   5209   5568    -73   -219   1111       N  
ATOM    726  CA  ALA C  91     -15.362  39.372 -65.358  1.00 31.89           C  
ANISOU  726  CA  ALA C  91     3396   4124   4598    -68   -215   1037       C  
ATOM    727  C   ALA C  91     -16.241  38.138 -65.226  1.00 33.99           C  
ANISOU  727  C   ALA C  91     3638   4454   4824    -65   -230    978       C  
ATOM    728  O   ALA C  91     -16.268  37.530 -64.154  1.00 33.03           O  
ANISOU  728  O   ALA C  91     3534   4295   4722    -75   -225    910       O  
ATOM    729  CB  ALA C  91     -16.068  40.569 -64.713  1.00 25.73           C  
ANISOU  729  CB  ALA C  91     2631   3259   3887    -24   -211   1072       C  
ATOM    730  N   LEU C  92     -16.952  37.753 -66.285  1.00 30.64           N  
ANISOU  730  N   LEU C  92     3172   4124   4346    -53   -249   1002       N  
ATOM    731  CA  LEU C  92     -17.830  36.589 -66.262  1.00 32.32           C  
ANISOU  731  CA  LEU C  92     3355   4396   4528    -56   -269    948       C  
ATOM    732  C   LEU C  92     -17.692  35.847 -67.584  1.00 35.33           C  
ANISOU  732  C   LEU C  92     3702   4887   4835    -67   -294    945       C  
ATOM    733  O   LEU C  92     -17.864  36.438 -68.654  1.00 40.61           O  
ANISOU  733  O   LEU C  92     4347   5614   5468    -45   -301   1011       O  
ATOM    734  CB  LEU C  92     -19.289  37.003 -66.019  1.00 27.85           C  
ANISOU  734  CB  LEU C  92     2764   3832   3985    -13   -274    974       C  
ATOM    735  CG  LEU C  92     -20.383  35.932 -66.107  1.00 33.43           C  
ANISOU  735  CG  LEU C  92     3426   4607   4667    -16   -298    933       C  
ATOM    736  CD1 LEU C  92     -20.197  34.878 -65.033  1.00 33.83           C  
ANISOU  736  CD1 LEU C  92     3494   4623   4738    -52   -292    857       C  
ATOM    737  CD2 LEU C  92     -21.753  36.572 -65.978  1.00 32.34           C  
ANISOU  737  CD2 LEU C  92     3258   4478   4552     32   -300    972       C  
ATOM    738  N   ALA C  93     -17.375  34.557 -67.507  1.00 30.43           N  
ANISOU  738  N   ALA C  93     3078   4295   4190    -99   -310    867       N  
ATOM    739  CA  ALA C  93     -17.144  33.733 -68.688  1.00 39.78           C  
ANISOU  739  CA  ALA C  93     4231   5580   5302   -108   -338    842       C  
ATOM    740  C   ALA C  93     -17.885  32.417 -68.516  1.00 46.30           C  
ANISOU  740  C   ALA C  93     5034   6434   6125   -123   -371    767       C  
ATOM    741  O   ALA C  93     -17.554  31.632 -67.623  1.00 49.89           O  
ANISOU  741  O   ALA C  93     5511   6834   6611   -152   -370    705       O  
ATOM    742  CB  ALA C  93     -15.649  33.482 -68.907  1.00 37.02           C  
ANISOU  742  CB  ALA C  93     3903   5236   4928   -134   -328    818       C  
ATOM    743  N   VAL C  94     -18.877  32.175 -69.367  1.00 43.73           N  
ANISOU  743  N   VAL C  94     4660   6189   5765   -104   -403    773       N  
ATOM    744  CA  VAL C  94     -19.671  30.951 -69.346  1.00 39.00           C  
ANISOU  744  CA  VAL C  94     4029   5620   5168   -121   -441    705       C  
ATOM    745  C   VAL C  94     -19.428  30.244 -70.672  1.00 41.80           C  
ANISOU  745  C   VAL C  94     4352   6080   5450   -118   -483    666       C  
ATOM    746  O   VAL C  94     -19.876  30.719 -71.723  1.00 42.40           O  
ANISOU  746  O   VAL C  94     4394   6243   5475    -85   -499    709       O  
ATOM    747  CB  VAL C  94     -21.163  31.242 -69.134  1.00 39.55           C  
ANISOU  747  CB  VAL C  94     4062   5698   5266   -101   -449    737       C  
ATOM    748  CG1 VAL C  94     -21.948  29.948 -68.968  1.00 38.47           C  
ANISOU  748  CG1 VAL C  94     3890   5579   5148   -131   -487    669       C  
ATOM    749  CG2 VAL C  94     -21.359  32.158 -67.931  1.00 37.47           C  
ANISOU  749  CG2 VAL C  94     3829   5345   5064    -89   -405    780       C  
ATOM    750  N   LEU C  95     -18.723  29.110 -70.633  1.00 40.08           N  
ANISOU  750  N   LEU C  95     4145   5858   5225   -147   -504    583       N  
ATOM    751  CA  LEU C  95     -18.229  28.483 -71.854  1.00 42.09           C  
ANISOU  751  CA  LEU C  95     4376   6211   5405   -137   -541    535       C  
ATOM    752  C   LEU C  95     -18.452  26.977 -71.849  1.00 43.44           C  
ANISOU  752  C   LEU C  95     4532   6384   5590   -163   -594    429       C  
ATOM    753  O   LEU C  95     -18.174  26.309 -70.852  1.00 48.01           O  
ANISOU  753  O   LEU C  95     5140   6874   6226   -196   -590    386       O  
ATOM    754  CB  LEU C  95     -16.725  28.742 -72.043  1.00 43.07           C  
ANISOU  754  CB  LEU C  95     4531   6339   5494   -138   -512    539       C  
ATOM    755  CG  LEU C  95     -16.166  30.163 -72.010  1.00 43.70           C  
ANISOU  755  CG  LEU C  95     4633   6401   5571   -124   -460    638       C  
ATOM    756  CD1 LEU C  95     -14.647  30.110 -72.025  1.00 44.70           C  
ANISOU  756  CD1 LEU C  95     4785   6524   5677   -138   -437    620       C  
ATOM    757  CD2 LEU C  95     -16.685  30.954 -73.193  1.00 49.30           C  
ANISOU  757  CD2 LEU C  95     5304   7210   6218    -85   -465    714       C  
ATOM    758  N   ASP C  96     -18.933  26.451 -72.979  1.00 41.75           N  
ANISOU  758  N   ASP C  96     4270   6270   5322   -145   -646    388       N  
ATOM    759  CA  ASP C  96     -18.827  25.026 -73.314  1.00 46.29           C  
ANISOU  759  CA  ASP C  96     4831   6864   5895   -161   -706    275       C  
ATOM    760  C   ASP C  96     -19.407  24.132 -72.218  1.00 44.33           C  
ANISOU  760  C   ASP C  96     4590   6511   5741   -208   -723    232       C  
ATOM    761  O   ASP C  96     -18.788  23.157 -71.785  1.00 55.46           O  
ANISOU  761  O   ASP C  96     6026   7864   7184   -234   -741    162       O  
ATOM    762  CB  ASP C  96     -17.378  24.634 -73.599  1.00 55.69           C  
ANISOU  762  CB  ASP C  96     6048   8069   7042   -155   -702    222       C  
ATOM    763  CG  ASP C  96     -16.840  25.259 -74.869  1.00 65.72           C  
ANISOU  763  CG  ASP C  96     7296   9467   8206   -109   -695    252       C  
ATOM    764  OD1 ASP C  96     -17.263  24.847 -75.970  1.00 72.27           O  
ANISOU  764  OD1 ASP C  96     8082  10405   8973    -81   -745    208       O  
ATOM    765  OD2 ASP C  96     -15.977  26.155 -74.763  1.00 63.33           O  
ANISOU  765  OD2 ASP C  96     7019   9160   7884   -102   -641    319       O  
ATOM    766  N   ASN C  97     -20.614  24.464 -71.768  1.00 43.58           N  
ANISOU  766  N   ASN C  97     4471   6396   5692   -217   -717    281       N  
ATOM    767  CA  ASN C  97     -21.292  23.709 -70.717  1.00 48.71           C  
ANISOU  767  CA  ASN C  97     5118   6958   6430   -263   -726    260       C  
ATOM    768  C   ASN C  97     -22.431  22.910 -71.356  1.00 53.81           C  
ANISOU  768  C   ASN C  97     5700   7654   7089   -276   -794    210       C  
ATOM    769  O   ASN C  97     -23.584  23.339 -71.382  1.00 56.05           O  
ANISOU  769  O   ASN C  97     5941   7968   7387   -271   -794    255       O  
ATOM    770  CB  ASN C  97     -21.787  24.619 -69.607  1.00 51.12           C  
ANISOU  770  CB  ASN C  97     5438   7202   6782   -266   -667    346       C  
ATOM    771  CG  ASN C  97     -20.676  25.481 -69.028  1.00 50.96           C  
ANISOU  771  CG  ASN C  97     5478   7133   6751   -252   -607    389       C  
ATOM    772  OD1 ASN C  97     -20.527  26.652 -69.376  1.00 57.42           O  
ANISOU  772  OD1 ASN C  97     6301   7983   7533   -217   -575    453       O  
ATOM    773  ND2 ASN C  97     -19.871  24.888 -68.149  1.00 35.92           N  
ANISOU  773  ND2 ASN C  97     3617   5148   4882   -281   -595    354       N  
ATOM    774  N   GLY C  98     -22.098  21.726 -71.858  1.00 55.46           N  
ANISOU  774  N   GLY C  98     5903   7871   7298   -291   -854    112       N  
ATOM    775  CA  GLY C  98     -23.072  20.884 -72.539  1.00 60.52           C  
ANISOU  775  CA  GLY C  98     6482   8557   7955   -304   -929     48       C  
ATOM    776  C   GLY C  98     -22.373  19.747 -73.266  1.00 72.78           C  
ANISOU  776  C   GLY C  98     8038  10127   9487   -302   -996    -70       C  
ATOM    777  O   GLY C  98     -21.269  19.329 -72.887  1.00 79.77           O  
ANISOU  777  O   GLY C  98     8974  10956  10381   -308   -985   -106       O  
ATOM    778  N   ASP C  99     -23.030  19.252 -74.307  1.00 80.99           N  
ANISOU  778  N   ASP C  99     9021  11248  10502   -290  -1068   -136       N  
ATOM    779  CA  ASP C  99     -22.460  18.211 -75.151  1.00 85.80           C  
ANISOU  779  CA  ASP C  99     9624  11891  11083   -276  -1141   -261       C  
ATOM    780  C   ASP C  99     -22.020  16.987 -74.349  1.00 78.29           C  
ANISOU  780  C   ASP C  99     8708  10811  10228   -326  -1169   -330       C  
ATOM    781  O   ASP C  99     -21.056  16.310 -74.708  1.00 73.43           O  
ANISOU  781  O   ASP C  99     8117  10193   9590   -307  -1201   -418       O  
ATOM    782  CB  ASP C  99     -21.271  18.758 -75.950  1.00 93.05           C  
ANISOU  782  CB  ASP C  99    10567  12900  11886   -215  -1116   -267       C  
ATOM    783  CG  ASP C  99     -21.687  19.767 -77.001  1.00 92.25           C  
ANISOU  783  CG  ASP C  99    10427  12942  11683   -161  -1107   -213       C  
ATOM    784  OD1 ASP C  99     -22.797  20.327 -76.883  1.00 88.10           O  
ANISOU  784  OD1 ASP C  99     9867  12430  11179   -168  -1099   -146       O  
ATOM    785  OD2 ASP C  99     -20.908  19.993 -77.953  1.00 91.16           O  
ANISOU  785  OD2 ASP C  99    10288  12909  11440   -108  -1109   -236       O  
ATOM    786  N   SER C 111     -32.322  12.984 -70.131  1.00 77.35           N  
ANISOU  786  N   SER C 111     8185  10342  10863   -831  -1272   -140       N  
ATOM    787  CA  SER C 111     -32.277  14.429 -70.330  1.00 78.23           C  
ANISOU  787  CA  SER C 111     8278  10551  10894   -766  -1234    -79       C  
ATOM    788  C   SER C 111     -30.844  14.899 -70.560  1.00 78.62           C  
ANISOU  788  C   SER C 111     8393  10601  10877   -714  -1229    -93       C  
ATOM    789  O   SER C 111     -29.924  14.462 -69.869  1.00 86.36           O  
ANISOU  789  O   SER C 111     9437  11486  11888   -734  -1212    -93       O  
ATOM    790  CB  SER C 111     -32.888  15.158 -69.131  1.00 76.45           C  
ANISOU  790  CB  SER C 111     8032  10312  10702   -784  -1152     46       C  
ATOM    791  OG  SER C 111     -32.984  16.552 -69.374  1.00 79.68           O  
ANISOU  791  OG  SER C 111     8420  10817  11037   -719  -1117    108       O  
ATOM    792  N   PRO C 112     -30.655  15.791 -71.530  1.00 74.66           N  
ANISOU  792  N   PRO C 112     7874  10210  10282   -647  -1245   -101       N  
ATOM    793  CA  PRO C 112     -29.301  16.254 -71.847  1.00 72.38           C  
ANISOU  793  CA  PRO C 112     7658   9935   9909   -590  -1225   -116       C  
ATOM    794  C   PRO C 112     -28.715  17.100 -70.729  1.00 66.73           C  
ANISOU  794  C   PRO C 112     7006   9168   9180   -577  -1122    -17       C  
ATOM    795  O   PRO C 112     -29.427  17.781 -69.987  1.00 71.71           O  
ANISOU  795  O   PRO C 112     7615   9799   9830   -583  -1064     74       O  
ATOM    796  CB  PRO C 112     -29.498  17.080 -73.123  1.00 70.74           C  
ANISOU  796  CB  PRO C 112     7417   9870   9592   -517  -1244   -129       C  
ATOM    797  CG  PRO C 112     -30.914  17.541 -73.047  1.00 71.65           C  
ANISOU  797  CG  PRO C 112     7453  10037   9733   -527  -1240    -70       C  
ATOM    798  CD  PRO C 112     -31.672  16.420 -72.390  1.00 73.20           C  
ANISOU  798  CD  PRO C 112     7617  10148  10048   -610  -1266    -95       C  
ATOM    799  N   GLY C 113     -27.388  17.047 -70.614  1.00 55.23           N  
ANISOU  799  N   GLY C 113     5626   7670   7689   -556  -1102    -41       N  
ATOM    800  CA  GLY C 113     -26.680  17.820 -69.619  1.00 50.22           C  
ANISOU  800  CA  GLY C 113     5057   6987   7039   -541  -1012     38       C  
ATOM    801  C   GLY C 113     -26.382  19.230 -70.092  1.00 53.37           C  
ANISOU  801  C   GLY C 113     5471   7470   7338   -470   -962     92       C  
ATOM    802  O   GLY C 113     -26.635  19.608 -71.235  1.00 59.41           O  
ANISOU  802  O   GLY C 113     6201   8336   8037   -429   -994     72       O  
ATOM    803  N   GLY C 114     -25.836  20.017 -69.184  1.00 42.75           N  
ANISOU  803  N   GLY C 114     4179   6080   5985   -457   -885    162       N  
ATOM    804  CA  GLY C 114     -25.487  21.378 -69.526  1.00 42.86           C  
ANISOU  804  CA  GLY C 114     4212   6152   5919   -395   -835    220       C  
ATOM    805  C   GLY C 114     -26.364  22.389 -68.807  1.00 49.63           C  
ANISOU  805  C   GLY C 114     5051   7012   6795   -383   -778    314       C  
ATOM    806  O   GLY C 114     -27.535  22.134 -68.492  1.00 47.00           O  
ANISOU  806  O   GLY C 114     4662   6684   6513   -410   -789    331       O  
ATOM    807  N   LEU C 115     -25.789  23.563 -68.558  1.00 51.95           N  
ANISOU  807  N   LEU C 115     5389   7303   7048   -340   -719    373       N  
ATOM    808  CA  LEU C 115     -26.477  24.623 -67.833  1.00 49.55           C  
ANISOU  808  CA  LEU C 115     5076   6993   6759   -317   -663    457       C  
ATOM    809  C   LEU C 115     -27.730  25.068 -68.581  1.00 50.41           C  
ANISOU  809  C   LEU C 115     5111   7191   6851   -290   -688    483       C  
ATOM    810  O   LEU C 115     -27.690  25.321 -69.790  1.00 45.70           O  
ANISOU  810  O   LEU C 115     4495   6674   6194   -256   -723    470       O  
ATOM    811  CB  LEU C 115     -25.518  25.799 -67.641  1.00 43.64           C  
ANISOU  811  CB  LEU C 115     4388   6223   5970   -273   -608    503       C  
ATOM    812  CG  LEU C 115     -25.711  26.805 -66.508  1.00 46.63           C  
ANISOU  812  CG  LEU C 115     4790   6552   6374   -252   -543    572       C  
ATOM    813  CD1 LEU C 115     -25.257  26.211 -65.188  1.00 43.87           C  
ANISOU  813  CD1 LEU C 115     4481   6115   6074   -291   -514    557       C  
ATOM    814  CD2 LEU C 115     -24.929  28.069 -66.816  1.00 45.39           C  
ANISOU  814  CD2 LEU C 115     4676   6397   6174   -202   -510    615       C  
ATOM    815  N   ARG C 116     -28.850  25.155 -67.859  1.00 50.43           N  
ANISOU  815  N   ARG C 116     5069   7189   6904   -302   -670    520       N  
ATOM    816  CA  ARG C 116     -30.113  25.634 -68.415  1.00 47.83           C  
ANISOU  816  CA  ARG C 116     4665   6943   6566   -273   -689    550       C  
ATOM    817  C   ARG C 116     -30.351  27.115 -68.154  1.00 44.39           C  
ANISOU  817  C   ARG C 116     4240   6520   6107   -208   -636    629       C  
ATOM    818  O   ARG C 116     -30.887  27.815 -69.018  1.00 37.64           O  
ANISOU  818  O   ARG C 116     3349   5741   5212   -159   -654    657       O  
ATOM    819  CB  ARG C 116     -31.295  24.843 -67.842  1.00 45.08           C  
ANISOU  819  CB  ARG C 116     4246   6593   6289   -324   -705    544       C  
ATOM    820  CG  ARG C 116     -31.166  23.331 -67.906  1.00 44.52           C  
ANISOU  820  CG  ARG C 116     4163   6486   6265   -397   -759    471       C  
ATOM    821  CD  ARG C 116     -32.422  22.656 -67.361  1.00 40.83           C  
ANISOU  821  CD  ARG C 116     3618   6022   5875   -451   -771    481       C  
ATOM    822  NE  ARG C 116     -33.333  22.239 -68.424  1.00 43.18           N  
ANISOU  822  NE  ARG C 116     3833   6399   6175   -459   -845    440       N  
ATOM    823  CZ  ARG C 116     -34.556  22.729 -68.606  1.00 44.10           C  
ANISOU  823  CZ  ARG C 116     3869   6590   6295   -439   -848    476       C  
ATOM    824  NH1 ARG C 116     -35.032  23.663 -67.794  1.00 47.78           N  
ANISOU  824  NH1 ARG C 116     4328   7062   6763   -405   -781    553       N  
ATOM    825  NH2 ARG C 116     -35.306  22.280 -69.603  1.00 51.76           N  
ANISOU  825  NH2 ARG C 116     4765   7634   7267   -448   -923    429       N  
ATOM    826  N   GLU C 117     -29.975  27.599 -66.973  1.00 42.30           N  
ANISOU  826  N   GLU C 117     4022   6182   5868   -203   -574    664       N  
ATOM    827  CA  GLU C 117     -30.222  28.970 -66.554  1.00 39.45           C  
ANISOU  827  CA  GLU C 117     3674   5817   5500   -142   -525    731       C  
ATOM    828  C   GLU C 117     -29.029  29.453 -65.742  1.00 42.50           C  
ANISOU  828  C   GLU C 117     4145   6116   5888   -135   -475    741       C  
ATOM    829  O   GLU C 117     -28.374  28.665 -65.055  1.00 47.82           O  
ANISOU  829  O   GLU C 117     4854   6731   6584   -181   -466    707       O  
ATOM    830  CB  GLU C 117     -31.493  29.077 -65.702  1.00 42.75           C  
ANISOU  830  CB  GLU C 117     4032   6248   5963   -138   -502    761       C  
ATOM    831  CG  GLU C 117     -32.776  28.586 -66.350  1.00 50.35           C  
ANISOU  831  CG  GLU C 117     4900   7296   6937   -150   -549    752       C  
ATOM    832  CD  GLU C 117     -33.917  28.493 -65.352  1.00 54.66           C  
ANISOU  832  CD  GLU C 117     5384   7852   7533   -161   -520    778       C  
ATOM    833  OE1 GLU C 117     -33.647  28.585 -64.133  1.00 53.05           O  
ANISOU  833  OE1 GLU C 117     5214   7588   7352   -167   -465    795       O  
ATOM    834  OE2 GLU C 117     -35.089  28.337 -65.771  1.00 59.90           O  
ANISOU  834  OE2 GLU C 117     5960   8590   8208   -160   -550    783       O  
ATOM    835  N   LEU C 118     -28.751  30.756 -65.819  1.00 40.85           N  
ANISOU  835  N   LEU C 118     3967   5896   5657    -76   -447    789       N  
ATOM    836  CA  LEU C 118     -27.678  31.327 -65.008  1.00 36.58           C  
ANISOU  836  CA  LEU C 118     3503   5272   5126    -68   -402    798       C  
ATOM    837  C   LEU C 118     -28.141  31.592 -63.578  1.00 38.14           C  
ANISOU  837  C   LEU C 118     3702   5423   5366    -58   -356    811       C  
ATOM    838  O   LEU C 118     -27.403  31.320 -62.624  1.00 45.87           O  
ANISOU  838  O   LEU C 118     4730   6338   6362    -81   -329    790       O  
ATOM    839  CB  LEU C 118     -27.155  32.616 -65.648  1.00 40.26           C  
ANISOU  839  CB  LEU C 118     4001   5734   5562    -14   -393    845       C  
ATOM    840  CG  LEU C 118     -26.376  32.498 -66.963  1.00 42.51           C  
ANISOU  840  CG  LEU C 118     4296   6061   5793    -20   -426    841       C  
ATOM    841  CD1 LEU C 118     -26.049  33.880 -67.504  1.00 46.93           C  
ANISOU  841  CD1 LEU C 118     4881   6618   6334     33   -412    909       C  
ATOM    842  CD2 LEU C 118     -25.110  31.687 -66.764  1.00 42.21           C  
ANISOU  842  CD2 LEU C 118     4307   5981   5750    -69   -424    788       C  
ATOM    843  N   GLN C 119     -29.360  32.121 -63.420  1.00 35.64           N  
ANISOU  843  N   GLN C 119     3331   5148   5063    -18   -348    844       N  
ATOM    844  CA  GLN C 119     -29.973  32.393 -62.113  1.00 47.52           C  
ANISOU  844  CA  GLN C 119     4824   6633   6600      2   -304    856       C  
ATOM    845  C   GLN C 119     -29.105  33.280 -61.226  1.00 43.77           C  
ANISOU  845  C   GLN C 119     4422   6078   6132     36   -262    860       C  
ATOM    846  O   GLN C 119     -29.140  33.163 -59.998  1.00 56.74           O  
ANISOU  846  O   GLN C 119     6075   7691   7792     35   -226    849       O  
ATOM    847  CB  GLN C 119     -30.322  31.099 -61.374  1.00 55.74           C  
ANISOU  847  CB  GLN C 119     5835   7679   7666    -62   -300    830       C  
ATOM    848  CG  GLN C 119     -31.379  30.243 -62.054  1.00 68.64           C  
ANISOU  848  CG  GLN C 119     7384   9386   9309    -98   -341    825       C  
ATOM    849  CD  GLN C 119     -32.025  29.242 -61.107  1.00 77.62           C  
ANISOU  849  CD  GLN C 119     8477  10529  10484   -151   -326    821       C  
ATOM    850  OE1 GLN C 119     -32.190  29.510 -59.912  1.00 87.04           O  
ANISOU  850  OE1 GLN C 119     9677  11704  11690   -135   -276    841       O  
ATOM    851  NE2 GLN C 119     -32.375  28.075 -61.635  1.00 73.16           N  
ANISOU  851  NE2 GLN C 119     7867   9990   9940   -216   -371    797       N  
ATOM    852  N   LEU C 120     -28.331  34.175 -61.839  1.00 37.35           N  
ANISOU  852  N   LEU C 120     3655   5233   5305     67   -268    877       N  
ATOM    853  CA  LEU C 120     -27.554  35.179 -61.114  1.00 38.90           C  
ANISOU  853  CA  LEU C 120     3914   5349   5516    103   -237    882       C  
ATOM    854  C   LEU C 120     -28.455  36.352 -60.715  1.00 38.62           C  
ANISOU  854  C   LEU C 120     3857   5315   5502    181   -219    913       C  
ATOM    855  O   LEU C 120     -28.287  37.489 -61.155  1.00 45.40           O  
ANISOU  855  O   LEU C 120     4738   6144   6368    230   -224    946       O  
ATOM    856  CB  LEU C 120     -26.384  35.641 -61.973  1.00 34.63           C  
ANISOU  856  CB  LEU C 120     3425   4775   4960     98   -252    894       C  
ATOM    857  CG  LEU C 120     -25.391  34.552 -62.377  1.00 29.45           C  
ANISOU  857  CG  LEU C 120     2792   4119   4280     31   -269    856       C  
ATOM    858  CD1 LEU C 120     -24.398  35.071 -63.408  1.00 27.67           C  
ANISOU  858  CD1 LEU C 120     2598   3886   4029     32   -283    879       C  
ATOM    859  CD2 LEU C 120     -24.665  34.026 -61.153  1.00 31.85           C  
ANISOU  859  CD2 LEU C 120     3139   4362   4601      0   -243    813       C  
ATOM    860  N   ARG C 121     -29.422  36.056 -59.842  1.00 38.43           N  
ANISOU  860  N   ARG C 121     3788   5324   5488    192   -197    903       N  
ATOM    861  CA  ARG C 121     -30.501  36.998 -59.563  1.00 41.40           C  
ANISOU  861  CA  ARG C 121     4124   5727   5880    269   -185    927       C  
ATOM    862  C   ARG C 121     -30.095  38.138 -58.634  1.00 39.28           C  
ANISOU  862  C   ARG C 121     3907   5382   5634    332   -156    918       C  
ATOM    863  O   ARG C 121     -30.875  39.083 -58.473  1.00 50.23           O  
ANISOU  863  O   ARG C 121     5269   6778   7037    407   -151    934       O  
ATOM    864  CB  ARG C 121     -31.718  36.255 -58.991  1.00 40.76           C  
ANISOU  864  CB  ARG C 121     3964   5722   5800    259   -170    923       C  
ATOM    865  CG  ARG C 121     -31.475  35.472 -57.710  1.00 45.76           C  
ANISOU  865  CG  ARG C 121     4610   6341   6435    221   -134    893       C  
ATOM    866  CD  ARG C 121     -32.751  34.781 -57.215  1.00 45.33           C  
ANISOU  866  CD  ARG C 121     4468   6371   6384    208   -117    903       C  
ATOM    867  NE  ARG C 121     -33.185  33.682 -58.081  1.00 42.08           N  
ANISOU  867  NE  ARG C 121     4003   6013   5974    138   -154    910       N  
ATOM    868  CZ  ARG C 121     -33.798  32.583 -57.645  1.00 41.01           C  
ANISOU  868  CZ  ARG C 121     3810   5921   5850     81   -146    912       C  
ATOM    869  NH1 ARG C 121     -34.048  32.427 -56.352  1.00 28.52           N  
ANISOU  869  NH1 ARG C 121     2218   4349   4271     86    -98    916       N  
ATOM    870  NH2 ARG C 121     -34.156  31.635 -58.501  1.00 44.07           N  
ANISOU  870  NH2 ARG C 121     4150   6347   6247     18   -188    911       N  
ATOM    871  N   SER C 122     -28.908  38.092 -58.033  1.00 34.66           N  
ANISOU  871  N   SER C 122     3391   4724   5054    306   -142    887       N  
ATOM    872  CA  SER C 122     -28.396  39.206 -57.241  1.00 29.16           C  
ANISOU  872  CA  SER C 122     2748   3947   4383    363   -125    869       C  
ATOM    873  C   SER C 122     -27.246  39.945 -57.907  1.00 31.47           C  
ANISOU  873  C   SER C 122     3104   4161   4695    357   -145    884       C  
ATOM    874  O   SER C 122     -26.769  40.938 -57.355  1.00 34.34           O  
ANISOU  874  O   SER C 122     3511   4446   5091    400   -138    870       O  
ATOM    875  CB  SER C 122     -27.953  38.725 -55.851  1.00 27.12           C  
ANISOU  875  CB  SER C 122     2517   3668   4119    348    -92    819       C  
ATOM    876  OG  SER C 122     -28.909  37.851 -55.264  1.00 24.67           O  
ANISOU  876  OG  SER C 122     2147   3437   3788    335    -71    816       O  
ATOM    877  N   LEU C 123     -26.799  39.498 -59.074  1.00 28.92           N  
ANISOU  877  N   LEU C 123     2781   3857   4352    307   -170    911       N  
ATOM    878  CA  LEU C 123     -25.621  40.072 -59.721  1.00 28.26           C  
ANISOU  878  CA  LEU C 123     2750   3709   4279    291   -184    931       C  
ATOM    879  C   LEU C 123     -25.986  41.434 -60.302  1.00 32.88           C  
ANISOU  879  C   LEU C 123     3334   4264   4894    356   -198    986       C  
ATOM    880  O   LEU C 123     -26.578  41.530 -61.380  1.00 43.65           O  
ANISOU  880  O   LEU C 123     4660   5684   6240    369   -220   1036       O  
ATOM    881  CB  LEU C 123     -25.083  39.130 -60.794  1.00 26.82           C  
ANISOU  881  CB  LEU C 123     2561   3574   4056    224   -204    941       C  
ATOM    882  CG  LEU C 123     -23.898  39.685 -61.600  1.00 32.99           C  
ANISOU  882  CG  LEU C 123     3386   4310   4839    206   -216    972       C  
ATOM    883  CD1 LEU C 123     -22.750  40.018 -60.668  1.00 21.05           C  
ANISOU  883  CD1 LEU C 123     1934   2705   3359    193   -197    936       C  
ATOM    884  CD2 LEU C 123     -23.445  38.704 -62.660  1.00 35.20           C  
ANISOU  884  CD2 LEU C 123     3651   4655   5069    149   -236    974       C  
ATOM    885  N   THR C 124     -25.629  42.501 -59.584  1.00 31.24           N  
ANISOU  885  N   THR C 124     3170   3965   4736    401   -190    975       N  
ATOM    886  CA  THR C 124     -25.950  43.858 -60.009  1.00 35.16           C  
ANISOU  886  CA  THR C 124     3670   4412   5275    467   -206   1025       C  
ATOM    887  C   THR C 124     -24.729  44.766 -60.113  1.00 38.15           C  
ANISOU  887  C   THR C 124     4112   4680   5702    457   -214   1042       C  
ATOM    888  O   THR C 124     -24.897  45.987 -60.207  1.00 42.89           O  
ANISOU  888  O   THR C 124     4727   5212   6357    514   -228   1076       O  
ATOM    889  CB  THR C 124     -26.971  44.492 -59.055  1.00 39.56           C  
ANISOU  889  CB  THR C 124     4208   4959   5862    551   -197    996       C  
ATOM    890  OG1 THR C 124     -26.428  44.527 -57.729  1.00 46.90           O  
ANISOU  890  OG1 THR C 124     5176   5832   6811    555   -175    924       O  
ATOM    891  CG2 THR C 124     -28.279  43.705 -59.043  1.00 39.52           C  
ANISOU  891  CG2 THR C 124     4130   5071   5816    564   -189    992       C  
ATOM    892  N   GLU C 125     -23.510  44.226 -60.101  1.00 35.06           N  
ANISOU  892  N   GLU C 125     3755   4267   5298    387   -208   1022       N  
ATOM    893  CA  GLU C 125     -22.338  45.088 -60.252  1.00 37.74           C  
ANISOU  893  CA  GLU C 125     4145   4506   5687    370   -215   1044       C  
ATOM    894  C   GLU C 125     -21.165  44.297 -60.807  1.00 44.60           C  
ANISOU  894  C   GLU C 125     5029   5399   6519    287   -212   1047       C  
ATOM    895  O   GLU C 125     -20.776  43.277 -60.233  1.00 36.99           O  
ANISOU  895  O   GLU C 125     4069   4461   5522    246   -199    985       O  
ATOM    896  CB  GLU C 125     -21.962  45.734 -58.919  1.00 31.00           C  
ANISOU  896  CB  GLU C 125     3334   3553   4892    401   -209    978       C  
ATOM    897  CG  GLU C 125     -20.926  46.842 -59.060  1.00 26.85           C  
ANISOU  897  CG  GLU C 125     2855   2910   4439    393   -224   1004       C  
ATOM    898  CD  GLU C 125     -21.542  48.221 -59.156  1.00 35.77           C  
ANISOU  898  CD  GLU C 125     3989   3963   5639    468   -246   1044       C  
ATOM    899  OE1 GLU C 125     -21.298  48.913 -60.177  1.00 46.46           O  
ANISOU  899  OE1 GLU C 125     5347   5283   7024    460   -263   1133       O  
ATOM    900  OE2 GLU C 125     -22.286  48.635 -58.227  1.00 46.56           O  
ANISOU  900  OE2 GLU C 125     5354   5305   7032    539   -246    990       O  
ATOM    901  N   ILE C 126     -20.610  44.765 -61.920  1.00 43.51           N  
ANISOU  901  N   ILE C 126     4895   5253   6385    266   -224   1121       N  
ATOM    902  CA  ILE C 126     -19.322  44.310 -62.426  1.00 38.19           C  
ANISOU  902  CA  ILE C 126     4237   4586   5687    195   -219   1129       C  
ATOM    903  C   ILE C 126     -18.437  45.546 -62.533  1.00 42.00           C  
ANISOU  903  C   ILE C 126     4755   4962   6241    191   -225   1176       C  
ATOM    904  O   ILE C 126     -18.674  46.422 -63.375  1.00 43.45           O  
ANISOU  904  O   ILE C 126     4931   5131   6447    214   -237   1265       O  
ATOM    905  CB  ILE C 126     -19.446  43.583 -63.772  1.00 33.83           C  
ANISOU  905  CB  ILE C 126     3647   4149   5059    167   -227   1176       C  
ATOM    906  CG1 ILE C 126     -19.947  42.146 -63.558  1.00 33.31           C  
ANISOU  906  CG1 ILE C 126     3553   4172   4932    148   -225   1110       C  
ATOM    907  CG2 ILE C 126     -18.111  43.565 -64.503  1.00 32.11           C  
ANISOU  907  CG2 ILE C 126     3443   3932   4826    111   -223   1211       C  
ATOM    908  CD1 ILE C 126     -20.815  41.617 -64.681  1.00 21.45           C  
ANISOU  908  CD1 ILE C 126     1998   2782   3368    156   -243   1146       C  
ATOM    909  N   LEU C 127     -17.436  45.633 -61.654  1.00 41.08           N  
ANISOU  909  N   LEU C 127     4675   4768   6164    162   -218   1119       N  
ATOM    910  CA  LEU C 127     -16.605  46.832 -61.596  1.00 37.41           C  
ANISOU  910  CA  LEU C 127     4242   4188   5783    155   -227   1154       C  
ATOM    911  C   LEU C 127     -15.705  46.948 -62.817  1.00 41.12           C  
ANISOU  911  C   LEU C 127     4703   4682   6238     99   -224   1241       C  
ATOM    912  O   LEU C 127     -15.519  48.045 -63.354  1.00 45.97           O  
ANISOU  912  O   LEU C 127     5323   5232   6910    105   -234   1325       O  
ATOM    913  CB  LEU C 127     -15.768  46.832 -60.316  1.00 22.33           C  
ANISOU  913  CB  LEU C 127     2370   2199   3916    138   -224   1061       C  
ATOM    914  CG  LEU C 127     -16.574  46.990 -59.018  1.00 25.29           C  
ANISOU  914  CG  LEU C 127     2756   2537   4314    202   -226    979       C  
ATOM    915  CD1 LEU C 127     -15.659  47.181 -57.820  1.00 29.80           C  
ANISOU  915  CD1 LEU C 127     3366   3025   4932    190   -229    893       C  
ATOM    916  CD2 LEU C 127     -17.538  48.151 -59.133  1.00 23.20           C  
ANISOU  916  CD2 LEU C 127     2490   2218   4107    274   -243   1022       C  
ATOM    917  N   LYS C 128     -15.135  45.834 -63.262  1.00 40.24           N  
ANISOU  917  N   LYS C 128     4574   4663   6050     48   -211   1223       N  
ATOM    918  CA  LYS C 128     -14.264  45.810 -64.425  1.00 45.09           C  
ANISOU  918  CA  LYS C 128     5173   5326   6634     -1   -205   1298       C  
ATOM    919  C   LYS C 128     -14.479  44.505 -65.176  1.00 39.05           C  
ANISOU  919  C   LYS C 128     4373   4703   5760    -17   -200   1283       C  
ATOM    920  O   LYS C 128     -14.791  43.472 -64.578  1.00 34.81           O  
ANISOU  920  O   LYS C 128     3834   4205   5187    -17   -199   1197       O  
ATOM    921  CB  LYS C 128     -12.784  45.962 -64.028  1.00 52.31           C  
ANISOU  921  CB  LYS C 128     6108   6176   7589    -59   -197   1273       C  
ATOM    922  CG  LYS C 128     -12.433  47.352 -63.516  1.00 71.03           C  
ANISOU  922  CG  LYS C 128     8509   8402  10076    -53   -208   1301       C  
ATOM    923  CD  LYS C 128     -11.059  47.407 -62.869  1.00 85.69           C  
ANISOU  923  CD  LYS C 128    10386  10194  11980   -108   -205   1251       C  
ATOM    924  CE  LYS C 128     -10.762  48.817 -62.370  1.00 88.47           C  
ANISOU  924  CE  LYS C 128    10765  10392  12457   -102   -224   1273       C  
ATOM    925  NZ  LYS C 128      -9.340  49.001 -61.973  1.00 86.29           N  
ANISOU  925  NZ  LYS C 128    10497  10054  12234   -165   -224   1244       N  
ATOM    926  N   GLY C 129     -14.328  44.560 -66.494  1.00 34.09           N  
ANISOU  926  N   GLY C 129     3716   4154   5082    -29   -199   1368       N  
ATOM    927  CA  GLY C 129     -14.411  43.374 -67.312  1.00 34.99           C  
ANISOU  927  CA  GLY C 129     3796   4406   5094    -43   -200   1350       C  
ATOM    928  C   GLY C 129     -15.782  43.196 -67.958  1.00 43.21           C  
ANISOU  928  C   GLY C 129     4804   5527   6086      6   -217   1379       C  
ATOM    929  O   GLY C 129     -16.779  43.800 -67.546  1.00 39.47           O  
ANISOU  929  O   GLY C 129     4334   5005   5656     54   -227   1392       O  
ATOM    930  N   GLY C 130     -15.809  42.346 -68.970  1.00 45.05           N  
ANISOU  930  N   GLY C 130     5002   5887   6228     -4   -224   1383       N  
ATOM    931  CA  GLY C 130     -17.022  42.089 -69.739  1.00 43.17           C  
ANISOU  931  CA  GLY C 130     4725   5744   5934     38   -245   1408       C  
ATOM    932  C   GLY C 130     -17.592  40.710 -69.489  1.00 44.60           C  
ANISOU  932  C   GLY C 130     4886   5992   6069     32   -260   1307       C  
ATOM    933  O   GLY C 130     -17.203  39.985 -68.573  1.00 43.92           O  
ANISOU  933  O   GLY C 130     4820   5867   6001      3   -253   1220       O  
ATOM    934  N   VAL C 131     -18.550  40.350 -70.344  1.00 43.58           N  
ANISOU  934  N   VAL C 131     4713   5964   5880     61   -284   1324       N  
ATOM    935  CA  VAL C 131     -19.280  39.094 -70.236  1.00 40.03           C  
ANISOU  935  CA  VAL C 131     4236   5580   5393     57   -306   1238       C  
ATOM    936  C   VAL C 131     -19.058  38.289 -71.510  1.00 41.21           C  
ANISOU  936  C   VAL C 131     4348   5861   5447     48   -328   1230       C  
ATOM    937  O   VAL C 131     -19.241  38.805 -72.621  1.00 49.70           O  
ANISOU  937  O   VAL C 131     5398   7012   6473     77   -337   1308       O  
ATOM    938  CB  VAL C 131     -20.780  39.331 -69.986  1.00 43.51           C  
ANISOU  938  CB  VAL C 131     4650   6024   5858    104   -322   1247       C  
ATOM    939  CG1 VAL C 131     -21.537  38.014 -69.991  1.00 36.98           C  
ANISOU  939  CG1 VAL C 131     3785   5270   4995     92   -347   1167       C  
ATOM    940  CG2 VAL C 131     -20.980  40.061 -68.668  1.00 44.05           C  
ANISOU  940  CG2 VAL C 131     4753   5970   6014    120   -300   1240       C  
ATOM    941  N   LEU C 132     -18.669  37.027 -71.341  1.00 35.68           N  
ANISOU  941  N   LEU C 132     3646   5190   4720     12   -338   1135       N  
ATOM    942  CA  LEU C 132     -18.384  36.116 -72.445  1.00 41.94           C  
ANISOU  942  CA  LEU C 132     4405   6104   5424      5   -363   1102       C  
ATOM    943  C   LEU C 132     -19.195  34.847 -72.230  1.00 48.20           C  
ANISOU  943  C   LEU C 132     5173   6929   6211     -4   -398   1006       C  
ATOM    944  O   LEU C 132     -18.912  34.077 -71.307  1.00 52.07           O  
ANISOU  944  O   LEU C 132     5686   7358   6740    -39   -395    931       O  
ATOM    945  CB  LEU C 132     -16.891  35.799 -72.521  1.00 42.04           C  
ANISOU  945  CB  LEU C 132     4441   6117   5416    -31   -344   1075       C  
ATOM    946  CG  LEU C 132     -16.478  34.688 -73.484  1.00 40.74           C  
ANISOU  946  CG  LEU C 132     4245   6071   5162    -37   -371   1013       C  
ATOM    947  CD1 LEU C 132     -16.597  35.160 -74.921  1.00 45.27           C  
ANISOU  947  CD1 LEU C 132     4780   6770   5649     -2   -380   1088       C  
ATOM    948  CD2 LEU C 132     -15.066  34.214 -73.184  1.00 37.30           C  
ANISOU  948  CD2 LEU C 132     3835   5612   4725    -74   -353    962       C  
ATOM    949  N   ILE C 133     -20.202  34.626 -73.072  1.00 46.05           N  
ANISOU  949  N   ILE C 133     4852   6751   5893     25   -434   1012       N  
ATOM    950  CA  ILE C 133     -21.076  33.462 -72.965  1.00 46.61           C  
ANISOU  950  CA  ILE C 133     4890   6854   5965     13   -474    927       C  
ATOM    951  C   ILE C 133     -21.101  32.766 -74.319  1.00 46.75           C  
ANISOU  951  C   ILE C 133     4864   7007   5892     26   -519    894       C  
ATOM    952  O   ILE C 133     -21.590  33.336 -75.302  1.00 45.06           O  
ANISOU  952  O   ILE C 133     4617   6881   5623     68   -534    955       O  
ATOM    953  CB  ILE C 133     -22.497  33.847 -72.520  1.00 45.26           C  
ANISOU  953  CB  ILE C 133     4692   6664   5841     38   -481    955       C  
ATOM    954  CG1 ILE C 133     -22.441  34.694 -71.247  1.00 41.16           C  
ANISOU  954  CG1 ILE C 133     4215   6021   5402     39   -436    990       C  
ATOM    955  CG2 ILE C 133     -23.341  32.605 -72.295  1.00 40.82           C  
ANISOU  955  CG2 ILE C 133     4093   6125   5293     14   -519    869       C  
ATOM    956  CD1 ILE C 133     -23.798  35.079 -70.703  1.00 36.66           C  
ANISOU  956  CD1 ILE C 133     3618   5434   4878     69   -438   1011       C  
ATOM    957  N   GLN C 134     -20.571  31.543 -74.375  1.00 42.94           N  
ANISOU  957  N   GLN C 134     4382   6543   5392     -5   -543    796       N  
ATOM    958  CA  GLN C 134     -20.362  30.862 -75.646  1.00 50.45           C  
ANISOU  958  CA  GLN C 134     5297   7621   6252     11   -585    749       C  
ATOM    959  C   GLN C 134     -20.628  29.369 -75.510  1.00 51.08           C  
ANISOU  959  C   GLN C 134     5358   7703   6346    -18   -635    625       C  
ATOM    960  O   GLN C 134     -20.245  28.749 -74.514  1.00 47.67           O  
ANISOU  960  O   GLN C 134     4959   7174   5978    -59   -625    572       O  
ATOM    961  CB  GLN C 134     -18.932  31.068 -76.164  1.00 56.71           C  
ANISOU  961  CB  GLN C 134     6112   8451   6986     12   -558    765       C  
ATOM    962  CG  GLN C 134     -18.509  32.516 -76.312  1.00 62.69           C  
ANISOU  962  CG  GLN C 134     6887   9197   7736     31   -509    892       C  
ATOM    963  CD  GLN C 134     -18.821  33.077 -77.681  1.00 71.89           C  
ANISOU  963  CD  GLN C 134     8011  10496   8808     80   -523    965       C  
ATOM    964  OE1 GLN C 134     -19.867  33.690 -77.891  1.00 72.06           O  
ANISOU  964  OE1 GLN C 134     8010  10535   8834    112   -535   1026       O  
ATOM    965  NE2 GLN C 134     -17.907  32.875 -78.622  1.00 78.44           N  
ANISOU  965  NE2 GLN C 134     8827  11431   9547     91   -522    960       N  
ATOM    966  N   ARG C 135     -21.283  28.807 -76.529  1.00 49.85           N  
ANISOU  966  N   ARG C 135     5150   7657   6134      4   -692    580       N  
ATOM    967  CA  ARG C 135     -21.370  27.359 -76.730  1.00 47.85           C  
ANISOU  967  CA  ARG C 135     4875   7425   5881    -18   -752    454       C  
ATOM    968  C   ARG C 135     -22.005  26.655 -75.531  1.00 50.12           C  
ANISOU  968  C   ARG C 135     5170   7597   6276    -67   -761    410       C  
ATOM    969  O   ARG C 135     -21.457  25.704 -74.970  1.00 54.14           O  
ANISOU  969  O   ARG C 135     5705   8040   6827   -105   -771    334       O  
ATOM    970  CB  ARG C 135     -19.988  26.786 -77.056  1.00 49.33           C  
ANISOU  970  CB  ARG C 135     5088   7633   6021    -21   -751    392       C  
ATOM    971  CG  ARG C 135     -19.349  27.472 -78.261  1.00 50.42           C  
ANISOU  971  CG  ARG C 135     5211   7900   6045     28   -738    443       C  
ATOM    972  CD  ARG C 135     -17.986  26.904 -78.631  1.00 46.40           C  
ANISOU  972  CD  ARG C 135     4719   7430   5483     30   -735    379       C  
ATOM    973  NE  ARG C 135     -16.968  27.175 -77.618  1.00 49.12           N  
ANISOU  973  NE  ARG C 135     5118   7663   5885     -4   -679    404       N  
ATOM    974  CZ  ARG C 135     -16.354  28.345 -77.463  1.00 54.99           C  
ANISOU  974  CZ  ARG C 135     5884   8388   6623     -2   -617    511       C  
ATOM    975  NH1 ARG C 135     -16.660  29.371 -78.247  1.00 62.14           N  
ANISOU  975  NH1 ARG C 135     6766   9373   7470     33   -600    613       N  
ATOM    976  NH2 ARG C 135     -15.438  28.492 -76.516  1.00 47.84           N  
ANISOU  976  NH2 ARG C 135     5024   7379   5773    -35   -574    517       N  
ATOM    977  N   ASN C 136     -23.194  27.126 -75.154  1.00 44.90           N  
ANISOU  977  N   ASN C 136     4483   6919   5659    -65   -757    461       N  
ATOM    978  CA  ASN C 136     -23.976  26.570 -74.051  1.00 42.57           C  
ANISOU  978  CA  ASN C 136     4182   6533   5460   -109   -760    437       C  
ATOM    979  C   ASN C 136     -25.311  26.111 -74.624  1.00 51.60           C  
ANISOU  979  C   ASN C 136     5253   7747   6606   -106   -821    407       C  
ATOM    980  O   ASN C 136     -26.297  26.865 -74.611  1.00 49.79           O  
ANISOU  980  O   ASN C 136     4990   7543   6384    -82   -811    472       O  
ATOM    981  CB  ASN C 136     -24.159  27.605 -72.943  1.00 42.64           C  
ANISOU  981  CB  ASN C 136     4221   6457   5524   -108   -695    526       C  
ATOM    982  CG  ASN C 136     -22.837  28.056 -72.348  1.00 39.37           C  
ANISOU  982  CG  ASN C 136     3876   5971   5114   -114   -641    550       C  
ATOM    983  OD1 ASN C 136     -22.034  27.238 -71.900  1.00 47.99           O  
ANISOU  983  OD1 ASN C 136     4999   7010   6225   -149   -643    488       O  
ATOM    984  ND2 ASN C 136     -22.594  29.362 -72.363  1.00 36.17           N  
ANISOU  984  ND2 ASN C 136     3491   5560   4692    -81   -596    639       N  
ATOM    985  N   PRO C 137     -25.386  24.882 -75.144  1.00 52.40           N  
ANISOU  985  N   PRO C 137     5326   7881   6705   -128   -887    304       N  
ATOM    986  CA  PRO C 137     -26.575  24.477 -75.917  1.00 49.44           C  
ANISOU  986  CA  PRO C 137     4875   7591   6319   -119   -955    266       C  
ATOM    987  C   PRO C 137     -27.877  24.492 -75.134  1.00 50.94           C  
ANISOU  987  C   PRO C 137     5024   7739   6593   -148   -953    298       C  
ATOM    988  O   PRO C 137     -28.934  24.744 -75.727  1.00 54.43           O  
ANISOU  988  O   PRO C 137     5403   8262   7017   -123   -986    313       O  
ATOM    989  CB  PRO C 137     -26.225  23.055 -76.385  1.00 49.20           C  
ANISOU  989  CB  PRO C 137     4833   7569   6290   -146  -1026    137       C  
ATOM    990  CG  PRO C 137     -25.002  22.653 -75.607  1.00 47.35           C  
ANISOU  990  CG  PRO C 137     4669   7233   6088   -176   -991    113       C  
ATOM    991  CD  PRO C 137     -24.290  23.907 -75.255  1.00 48.64           C  
ANISOU  991  CD  PRO C 137     4882   7380   6219   -148   -909    214       C  
ATOM    992  N   GLN C 138     -27.848  24.226 -73.830  1.00 49.52           N  
ANISOU  992  N   GLN C 138     4873   7443   6501   -197   -914    310       N  
ATOM    993  CA  GLN C 138     -29.069  24.159 -73.036  1.00 41.08           C  
ANISOU  993  CA  GLN C 138     3759   6340   5511   -228   -908    340       C  
ATOM    994  C   GLN C 138     -29.410  25.471 -72.343  1.00 41.62           C  
ANISOU  994  C   GLN C 138     3839   6389   5585   -194   -837    446       C  
ATOM    995  O   GLN C 138     -30.415  25.531 -71.627  1.00 47.42           O  
ANISOU  995  O   GLN C 138     4535   7105   6379   -210   -823    477       O  
ATOM    996  CB  GLN C 138     -28.959  23.041 -71.993  1.00 45.76           C  
ANISOU  996  CB  GLN C 138     4366   6825   6195   -301   -910    296       C  
ATOM    997  CG  GLN C 138     -28.872  21.644 -72.584  1.00 49.71           C  
ANISOU  997  CG  GLN C 138     4843   7329   6714   -340   -991    186       C  
ATOM    998  CD  GLN C 138     -30.128  21.260 -73.338  1.00 57.79           C  
ANISOU  998  CD  GLN C 138     5777   8432   7749   -346  -1061    150       C  
ATOM    999  OE1 GLN C 138     -31.224  21.251 -72.777  1.00 61.29           O  
ANISOU  999  OE1 GLN C 138     6167   8863   8255   -375  -1055    187       O  
ATOM   1000  NE2 GLN C 138     -29.977  20.950 -74.620  1.00 61.73           N  
ANISOU 1000  NE2 GLN C 138     6252   9019   8182   -315  -1128     77       N  
ATOM   1001  N   LEU C 139     -28.616  26.519 -72.544  1.00 46.15           N  
ANISOU 1001  N   LEU C 139     4463   6969   6103   -146   -794    501       N  
ATOM   1002  CA  LEU C 139     -28.774  27.745 -71.775  1.00 47.07           C  
ANISOU 1002  CA  LEU C 139     4603   7044   6238   -115   -728    592       C  
ATOM   1003  C   LEU C 139     -29.872  28.622 -72.363  1.00 52.23           C  
ANISOU 1003  C   LEU C 139     5201   7779   6866    -60   -739    650       C  
ATOM   1004  O   LEU C 139     -29.997  28.754 -73.584  1.00 56.23           O  
ANISOU 1004  O   LEU C 139     5678   8383   7305    -25   -781    647       O  
ATOM   1005  CB  LEU C 139     -27.453  28.512 -71.731  1.00 51.61           C  
ANISOU 1005  CB  LEU C 139     5254   7580   6777    -91   -682    629       C  
ATOM   1006  CG  LEU C 139     -27.424  29.793 -70.899  1.00 53.05           C  
ANISOU 1006  CG  LEU C 139     5471   7701   6984    -60   -618    713       C  
ATOM   1007  CD1 LEU C 139     -27.787  29.491 -69.455  1.00 55.15           C  
ANISOU 1007  CD1 LEU C 139     5745   7881   7328    -94   -585    705       C  
ATOM   1008  CD2 LEU C 139     -26.050  30.433 -70.983  1.00 43.81           C  
ANISOU 1008  CD2 LEU C 139     4369   6495   5783    -47   -583    740       C  
ATOM   1009  N   CYS C 140     -30.670  29.222 -71.480  1.00 55.63           N  
ANISOU 1009  N   CYS C 140     5614   8175   7346    -48   -702    702       N  
ATOM   1010  CA  CYS C 140     -31.760  30.103 -71.868  1.00 57.62           C  
ANISOU 1010  CA  CYS C 140     5813   8494   7585      9   -709    760       C  
ATOM   1011  C   CYS C 140     -31.683  31.401 -71.076  1.00 50.91           C  
ANISOU 1011  C   CYS C 140     5003   7582   6757     54   -645    839       C  
ATOM   1012  O   CYS C 140     -31.121  31.445 -69.978  1.00 58.10           O  
ANISOU 1012  O   CYS C 140     5965   8400   7709     31   -597    839       O  
ATOM   1013  CB  CYS C 140     -33.134  29.443 -71.642  1.00 62.13           C  
ANISOU 1013  CB  CYS C 140     6297   9103   8204    -17   -740    733       C  
ATOM   1014  SG  CYS C 140     -33.726  28.370 -72.981  1.00 62.48           S  
ANISOU 1014  SG  CYS C 140     6264   9260   8216    -37   -836    656       S  
ATOM   1015  N   TYR C 141     -32.249  32.458 -71.659  1.00 45.59           N  
ANISOU 1015  N   TYR C 141     4306   6962   6054    123   -649    903       N  
ATOM   1016  CA  TYR C 141     -32.519  33.773 -71.069  1.00 52.49           C  
ANISOU 1016  CA  TYR C 141     5199   7791   6953    181   -604    978       C  
ATOM   1017  C   TYR C 141     -31.298  34.688 -70.984  1.00 53.42           C  
ANISOU 1017  C   TYR C 141     5402   7837   7060    202   -565   1024       C  
ATOM   1018  O   TYR C 141     -31.426  35.787 -70.431  1.00 52.51           O  
ANISOU 1018  O   TYR C 141     5309   7667   6975    249   -531   1079       O  
ATOM   1019  CB  TYR C 141     -33.139  33.676 -69.664  1.00 50.02           C  
ANISOU 1019  CB  TYR C 141     4872   7421   6712    166   -566    968       C  
ATOM   1020  CG  TYR C 141     -34.344  32.766 -69.583  1.00 55.81           C  
ANISOU 1020  CG  TYR C 141     5517   8217   7471    135   -597    930       C  
ATOM   1021  CD1 TYR C 141     -34.236  31.481 -69.064  1.00 53.84           C  
ANISOU 1021  CD1 TYR C 141     5258   7943   7255     55   -603    868       C  
ATOM   1022  CD2 TYR C 141     -35.589  33.189 -70.027  1.00 52.04           C  
ANISOU 1022  CD2 TYR C 141     4963   7821   6989    184   -622    958       C  
ATOM   1023  CE1 TYR C 141     -35.332  30.645 -68.990  1.00 54.32           C  
ANISOU 1023  CE1 TYR C 141     5234   8055   7349     19   -632    838       C  
ATOM   1024  CE2 TYR C 141     -36.691  32.363 -69.954  1.00 58.41           C  
ANISOU 1024  CE2 TYR C 141     5681   8687   7824    150   -651    924       C  
ATOM   1025  CZ  TYR C 141     -36.558  31.091 -69.436  1.00 57.60           C  
ANISOU 1025  CZ  TYR C 141     5570   8556   7760     64   -656    865       C  
ATOM   1026  OH  TYR C 141     -37.659  30.265 -69.366  1.00 45.35           O  
ANISOU 1026  OH  TYR C 141     3926   7058   6247     24   -687    837       O  
ATOM   1027  N   GLN C 142     -30.131  34.298 -71.507  1.00 50.67           N  
ANISOU 1027  N   GLN C 142     5097   7486   6672    171   -571   1002       N  
ATOM   1028  CA  GLN C 142     -28.963  35.166 -71.374  1.00 50.59           C  
ANISOU 1028  CA  GLN C 142     5160   7405   6658    184   -532   1049       C  
ATOM   1029  C   GLN C 142     -29.023  36.348 -72.335  1.00 60.11           C  
ANISOU 1029  C   GLN C 142     6364   8651   7823    248   -539   1139       C  
ATOM   1030  O   GLN C 142     -28.469  37.412 -72.037  1.00 64.91           O  
ANISOU 1030  O   GLN C 142     7022   9187   8456    273   -505   1200       O  
ATOM   1031  CB  GLN C 142     -27.673  34.373 -71.591  1.00 42.55           C  
ANISOU 1031  CB  GLN C 142     4183   6375   5610    131   -533    998       C  
ATOM   1032  CG  GLN C 142     -27.428  33.930 -73.025  1.00 44.31           C  
ANISOU 1032  CG  GLN C 142     4379   6708   5750    135   -578    986       C  
ATOM   1033  CD  GLN C 142     -28.049  32.585 -73.341  1.00 48.65           C  
ANISOU 1033  CD  GLN C 142     4874   7323   6288    101   -630    899       C  
ATOM   1034  OE1 GLN C 142     -29.133  32.257 -72.857  1.00 54.00           O  
ANISOU 1034  OE1 GLN C 142     5507   8001   7011     94   -642    879       O  
ATOM   1035  NE2 GLN C 142     -27.363  31.797 -74.160  1.00 41.10           N  
ANISOU 1035  NE2 GLN C 142     3918   6424   5275     81   -662    844       N  
ATOM   1036  N   ASP C 143     -29.685  36.187 -73.483  1.00 58.70           N  
ANISOU 1036  N   ASP C 143     6129   8588   7585    276   -586   1150       N  
ATOM   1037  CA  ASP C 143     -29.906  37.288 -74.415  1.00 58.60           C  
ANISOU 1037  CA  ASP C 143     6108   8627   7532    343   -597   1244       C  
ATOM   1038  C   ASP C 143     -30.815  38.362 -73.841  1.00 59.63           C  
ANISOU 1038  C   ASP C 143     6228   8709   7719    401   -582   1304       C  
ATOM   1039  O   ASP C 143     -30.969  39.423 -74.456  1.00 66.23           O  
ANISOU 1039  O   ASP C 143     7066   9562   8538    462   -587   1393       O  
ATOM   1040  CB  ASP C 143     -30.528  36.756 -75.703  1.00 63.95           C  
ANISOU 1040  CB  ASP C 143     6719   9449   8129    362   -657   1230       C  
ATOM   1041  CG  ASP C 143     -31.745  35.889 -75.438  1.00 74.73           C  
ANISOU 1041  CG  ASP C 143     8015  10859   9521    348   -692   1159       C  
ATOM   1042  OD1 ASP C 143     -31.686  35.053 -74.511  1.00 75.82           O  
ANISOU 1042  OD1 ASP C 143     8158  10938   9711    290   -679   1087       O  
ATOM   1043  OD2 ASP C 143     -32.763  36.050 -76.144  1.00 78.75           O  
ANISOU 1043  OD2 ASP C 143     8460  11462   9998    393   -733   1179       O  
ATOM   1044  N   THR C 144     -31.407  38.104 -72.683  1.00 54.58           N  
ANISOU 1044  N   THR C 144     5577   8015   7146    387   -564   1258       N  
ATOM   1045  CA  THR C 144     -32.495  38.885 -72.123  1.00 51.00           C  
ANISOU 1045  CA  THR C 144     5094   7543   6742    446   -556   1292       C  
ATOM   1046  C   THR C 144     -32.030  39.924 -71.107  1.00 52.78           C  
ANISOU 1046  C   THR C 144     5383   7640   7032    471   -508   1326       C  
ATOM   1047  O   THR C 144     -32.660  40.982 -70.980  1.00 53.78           O  
ANISOU 1047  O   THR C 144     5502   7743   7189    541   -505   1380       O  
ATOM   1048  CB  THR C 144     -33.500  37.904 -71.497  1.00 50.52           C  
ANISOU 1048  CB  THR C 144     4969   7518   6708    416   -565   1220       C  
ATOM   1049  OG1 THR C 144     -34.513  37.563 -72.453  1.00 52.36           O  
ANISOU 1049  OG1 THR C 144     5121   7873   6900    438   -618   1218       O  
ATOM   1050  CG2 THR C 144     -34.120  38.439 -70.263  1.00 46.83           C  
ANISOU 1050  CG2 THR C 144     4498   6988   6309    446   -529   1223       C  
ATOM   1051  N   ILE C 145     -30.913  39.663 -70.426  1.00 53.69           N  
ANISOU 1051  N   ILE C 145     5560   7671   7169    418   -474   1292       N  
ATOM   1052  CA  ILE C 145     -30.406  40.559 -69.396  1.00 49.67           C  
ANISOU 1052  CA  ILE C 145     5111   7039   6723    436   -433   1308       C  
ATOM   1053  C   ILE C 145     -29.919  41.863 -70.016  1.00 52.32           C  
ANISOU 1053  C   ILE C 145     5486   7331   7064    483   -434   1400       C  
ATOM   1054  O   ILE C 145     -29.240  41.868 -71.052  1.00 52.87           O  
ANISOU 1054  O   ILE C 145     5567   7440   7082    467   -448   1441       O  
ATOM   1055  CB  ILE C 145     -29.275  39.863 -68.618  1.00 45.99           C  
ANISOU 1055  CB  ILE C 145     4697   6506   6270    365   -404   1246       C  
ATOM   1056  CG1 ILE C 145     -29.813  38.628 -67.896  1.00 37.59           C  
ANISOU 1056  CG1 ILE C 145     3596   5472   5214    320   -402   1166       C  
ATOM   1057  CG2 ILE C 145     -28.603  40.822 -67.642  1.00 39.92           C  
ANISOU 1057  CG2 ILE C 145     3993   5611   5563    382   -367   1258       C  
ATOM   1058  CD1 ILE C 145     -30.914  38.938 -66.902  1.00 27.94           C  
ANISOU 1058  CD1 ILE C 145     2340   4237   4038    361   -384   1158       C  
ATOM   1059  N   LEU C 146     -30.268  42.982 -69.382  1.00 51.15           N  
ANISOU 1059  N   LEU C 146     5355   7102   6977    543   -420   1433       N  
ATOM   1060  CA  LEU C 146     -29.671  44.279 -69.701  1.00 46.41           C  
ANISOU 1060  CA  LEU C 146     4805   6422   6408    580   -417   1518       C  
ATOM   1061  C   LEU C 146     -28.322  44.330 -68.994  1.00 43.60           C  
ANISOU 1061  C   LEU C 146     4518   5959   6087    526   -385   1490       C  
ATOM   1062  O   LEU C 146     -28.196  44.827 -67.874  1.00 43.06           O  
ANISOU 1062  O   LEU C 146     4484   5790   6086    541   -363   1459       O  
ATOM   1063  CB  LEU C 146     -30.581  45.425 -69.269  1.00 44.42           C  
ANISOU 1063  CB  LEU C 146     4544   6117   6216    668   -422   1553       C  
ATOM   1064  CG  LEU C 146     -30.206  46.841 -69.721  1.00 44.82           C  
ANISOU 1064  CG  LEU C 146     4636   6084   6308    718   -431   1653       C  
ATOM   1065  CD1 LEU C 146     -30.200  46.936 -71.243  1.00 42.72           C  
ANISOU 1065  CD1 LEU C 146     4347   5910   5974    726   -460   1745       C  
ATOM   1066  CD2 LEU C 146     -31.156  47.871 -69.121  1.00 41.03           C  
ANISOU 1066  CD2 LEU C 146     4149   5544   5897    810   -438   1666       C  
ATOM   1067  N   TRP C 147     -27.299  43.790 -69.662  1.00 49.47           N  
ANISOU 1067  N   TRP C 147     5279   6735   6782    465   -383   1496       N  
ATOM   1068  CA  TRP C 147     -25.964  43.703 -69.075  1.00 49.40           C  
ANISOU 1068  CA  TRP C 147     5329   6641   6800    408   -355   1466       C  
ATOM   1069  C   TRP C 147     -25.423  45.066 -68.677  1.00 43.33           C  
ANISOU 1069  C   TRP C 147     4612   5742   6108    435   -342   1520       C  
ATOM   1070  O   TRP C 147     -24.612  45.172 -67.750  1.00 43.54           O  
ANISOU 1070  O   TRP C 147     4685   5675   6184    405   -320   1476       O  
ATOM   1071  CB  TRP C 147     -25.018  43.039 -70.067  1.00 45.81           C  
ANISOU 1071  CB  TRP C 147     4875   6256   6274    353   -359   1477       C  
ATOM   1072  CG  TRP C 147     -25.329  41.622 -70.170  1.00 46.48           C  
ANISOU 1072  CG  TRP C 147     4923   6435   6304    316   -372   1397       C  
ATOM   1073  CD1 TRP C 147     -26.015  41.000 -71.165  1.00 48.56           C  
ANISOU 1073  CD1 TRP C 147     5130   6823   6498    326   -405   1399       C  
ATOM   1074  CD2 TRP C 147     -25.027  40.626 -69.198  1.00 45.16           C  
ANISOU 1074  CD2 TRP C 147     4767   6240   6151    266   -357   1301       C  
ATOM   1075  NE1 TRP C 147     -26.140  39.663 -70.881  1.00 49.37           N  
ANISOU 1075  NE1 TRP C 147     5210   6969   6578    280   -413   1306       N  
ATOM   1076  CE2 TRP C 147     -25.534  39.408 -69.680  1.00 47.69           C  
ANISOU 1076  CE2 TRP C 147     5039   6664   6416    242   -382   1250       C  
ATOM   1077  CE3 TRP C 147     -24.361  40.644 -67.970  1.00 42.59           C  
ANISOU 1077  CE3 TRP C 147     4489   5812   5879    240   -326   1253       C  
ATOM   1078  CZ2 TRP C 147     -25.396  38.215 -68.978  1.00 48.10           C  
ANISOU 1078  CZ2 TRP C 147     5092   6712   6473    191   -378   1161       C  
ATOM   1079  CZ3 TRP C 147     -24.224  39.462 -67.275  1.00 42.90           C  
ANISOU 1079  CZ3 TRP C 147     4528   5859   5914    193   -320   1167       C  
ATOM   1080  CH2 TRP C 147     -24.740  38.263 -67.780  1.00 47.30           C  
ANISOU 1080  CH2 TRP C 147     5039   6512   6422    168   -345   1125       C  
ATOM   1081  N   LYS C 148     -25.860  46.115 -69.367  1.00 48.23           N  
ANISOU 1081  N   LYS C 148     5226   6355   6744    492   -361   1615       N  
ATOM   1082  CA  LYS C 148     -25.359  47.460 -69.131  1.00 56.88           C  
ANISOU 1082  CA  LYS C 148     6370   7321   7923    518   -356   1678       C  
ATOM   1083  C   LYS C 148     -25.820  48.033 -67.794  1.00 51.43           C  
ANISOU 1083  C   LYS C 148     5700   6523   7317    563   -350   1620       C  
ATOM   1084  O   LYS C 148     -25.156  48.927 -67.258  1.00 58.79           O  
ANISOU 1084  O   LYS C 148     6682   7327   8328    566   -344   1631       O  
ATOM   1085  CB  LYS C 148     -25.757  48.370 -70.305  1.00 70.38           C  
ANISOU 1085  CB  LYS C 148     8063   9055   9622    569   -382   1804       C  
ATOM   1086  CG  LYS C 148     -25.543  47.741 -71.699  1.00 86.28           C  
ANISOU 1086  CG  LYS C 148    10043  11210  11530    540   -392   1858       C  
ATOM   1087  CD  LYS C 148     -26.755  46.930 -72.196  1.00 91.25           C  
ANISOU 1087  CD  LYS C 148    10607  11981  12084    572   -417   1827       C  
ATOM   1088  CE  LYS C 148     -26.462  45.923 -73.301  1.00 91.33           C  
ANISOU 1088  CE  LYS C 148    10582  12136  11984    531   -428   1825       C  
ATOM   1089  NZ  LYS C 148     -27.698  45.149 -73.616  1.00 92.69           N  
ANISOU 1089  NZ  LYS C 148    10689  12429  12100    560   -458   1779       N  
ATOM   1090  N   ASP C 149     -26.920  47.535 -67.229  1.00 44.46           N  
ANISOU 1090  N   ASP C 149     4778   5693   6422    598   -351   1555       N  
ATOM   1091  CA  ASP C 149     -27.269  47.932 -65.871  1.00 40.19           C  
ANISOU 1091  CA  ASP C 149     4255   5068   5948    639   -339   1487       C  
ATOM   1092  C   ASP C 149     -26.304  47.331 -64.858  1.00 40.95           C  
ANISOU 1092  C   ASP C 149     4389   5114   6054    576   -311   1401       C  
ATOM   1093  O   ASP C 149     -26.106  47.894 -63.775  1.00 35.25           O  
ANISOU 1093  O   ASP C 149     3703   4294   5397    601   -301   1353       O  
ATOM   1094  CB  ASP C 149     -28.699  47.506 -65.557  1.00 42.31           C  
ANISOU 1094  CB  ASP C 149     4461   5421   6192    690   -343   1446       C  
ATOM   1095  CG  ASP C 149     -29.170  48.000 -64.213  1.00 47.29           C  
ANISOU 1095  CG  ASP C 149     5103   5983   6884    747   -329   1381       C  
ATOM   1096  OD1 ASP C 149     -28.944  47.289 -63.214  1.00 48.78           O  
ANISOU 1096  OD1 ASP C 149     5298   6172   7065    713   -303   1298       O  
ATOM   1097  OD2 ASP C 149     -29.763  49.096 -64.161  1.00 49.03           O  
ANISOU 1097  OD2 ASP C 149     5323   6151   7157    830   -346   1414       O  
ATOM   1098  N   ILE C 150     -25.694  46.196 -65.195  1.00 39.93           N  
ANISOU 1098  N   ILE C 150     4255   5054   5863    500   -301   1376       N  
ATOM   1099  CA  ILE C 150     -24.829  45.508 -64.246  1.00 34.99           C  
ANISOU 1099  CA  ILE C 150     3661   4392   5240    443   -277   1294       C  
ATOM   1100  C   ILE C 150     -23.442  46.136 -64.225  1.00 41.90           C  
ANISOU 1100  C   ILE C 150     4594   5167   6160    407   -271   1315       C  
ATOM   1101  O   ILE C 150     -22.841  46.298 -63.157  1.00 41.51           O  
ANISOU 1101  O   ILE C 150     4583   5033   6155    397   -258   1256       O  
ATOM   1102  CB  ILE C 150     -24.774  44.006 -64.580  1.00 37.50           C  
ANISOU 1102  CB  ILE C 150     3949   4819   5482    381   -273   1254       C  
ATOM   1103  CG1 ILE C 150     -26.178  43.397 -64.511  1.00 32.43           C  
ANISOU 1103  CG1 ILE C 150     3245   4268   4810    411   -280   1231       C  
ATOM   1104  CG2 ILE C 150     -23.847  43.282 -63.623  1.00 39.50           C  
ANISOU 1104  CG2 ILE C 150     4237   5032   5738    325   -251   1176       C  
ATOM   1105  CD1 ILE C 150     -26.241  41.966 -64.989  1.00 27.91           C  
ANISOU 1105  CD1 ILE C 150     2635   3797   4171    352   -287   1198       C  
ATOM   1106  N   PHE C 151     -22.917  46.512 -65.390  1.00 44.64           N  
ANISOU 1106  N   PHE C 151     4944   5526   6493    387   -282   1402       N  
ATOM   1107  CA  PHE C 151     -21.593  47.119 -65.444  1.00 45.03           C  
ANISOU 1107  CA  PHE C 151     5038   5484   6586    346   -276   1433       C  
ATOM   1108  C   PHE C 151     -21.568  48.415 -64.644  1.00 49.37           C  
ANISOU 1108  C   PHE C 151     5626   5892   7241    392   -283   1436       C  
ATOM   1109  O   PHE C 151     -22.550  49.160 -64.602  1.00 48.59           O  
ANISOU 1109  O   PHE C 151     5516   5768   7178    465   -299   1462       O  
ATOM   1110  CB  PHE C 151     -21.189  47.397 -66.894  1.00 40.05           C  
ANISOU 1110  CB  PHE C 151     4394   4903   5920    327   -284   1544       C  
ATOM   1111  CG  PHE C 151     -21.061  46.162 -67.739  1.00 38.57           C  
ANISOU 1111  CG  PHE C 151     4171   4855   5628    284   -282   1534       C  
ATOM   1112  CD1 PHE C 151     -21.427  46.181 -69.075  1.00 35.94           C  
ANISOU 1112  CD1 PHE C 151     3802   4621   5232    299   -297   1618       C  
ATOM   1113  CD2 PHE C 151     -20.559  44.987 -67.203  1.00 44.03           C  
ANISOU 1113  CD2 PHE C 151     4866   5578   6285    232   -268   1439       C  
ATOM   1114  CE1 PHE C 151     -21.310  45.046 -69.857  1.00 40.29           C  
ANISOU 1114  CE1 PHE C 151     4320   5303   5686    265   -300   1597       C  
ATOM   1115  CE2 PHE C 151     -20.437  43.849 -67.981  1.00 44.89           C  
ANISOU 1115  CE2 PHE C 151     4943   5807   6305    197   -272   1422       C  
ATOM   1116  CZ  PHE C 151     -20.813  43.879 -69.310  1.00 45.30           C  
ANISOU 1116  CZ  PHE C 151     4958   5959   6294    214   -289   1496       C  
ATOM   1117  N   HIS C 152     -20.441  48.674 -63.989  1.00 47.54           N  
ANISOU 1117  N   HIS C 152     5437   5565   7061    351   -274   1400       N  
ATOM   1118  CA  HIS C 152     -20.245  49.960 -63.336  1.00 44.47           C  
ANISOU 1118  CA  HIS C 152     5087   5029   6781    387   -288   1403       C  
ATOM   1119  C   HIS C 152     -20.090  51.050 -64.395  1.00 49.14           C  
ANISOU 1119  C   HIS C 152     5682   5571   7418    396   -307   1532       C  
ATOM   1120  O   HIS C 152     -19.694  50.784 -65.534  1.00 49.38           O  
ANISOU 1120  O   HIS C 152     5694   5674   7395    353   -301   1614       O  
ATOM   1121  CB  HIS C 152     -19.022  49.900 -62.416  1.00 35.33           C  
ANISOU 1121  CB  HIS C 152     3969   3790   5665    336   -279   1329       C  
ATOM   1122  CG  HIS C 152     -18.817  51.122 -61.573  1.00 39.27           C  
ANISOU 1122  CG  HIS C 152     4508   4135   6277    373   -298   1304       C  
ATOM   1123  ND1 HIS C 152     -18.065  52.196 -61.996  1.00 45.87           N  
ANISOU 1123  ND1 HIS C 152     5368   4861   7200    352   -316   1378       N  
ATOM   1124  CD2 HIS C 152     -19.223  51.421 -60.316  1.00 46.84           C  
ANISOU 1124  CD2 HIS C 152     5485   5033   7279    429   -305   1208       C  
ATOM   1125  CE1 HIS C 152     -18.036  53.114 -61.046  1.00 48.03           C  
ANISOU 1125  CE1 HIS C 152     5675   5003   7572    393   -338   1324       C  
ATOM   1126  NE2 HIS C 152     -18.731  52.668 -60.016  1.00 52.57           N  
ANISOU 1126  NE2 HIS C 152     6247   5610   8118    444   -332   1217       N  
ATOM   1127  N   LYS C 153     -20.440  52.286 -64.017  1.00 55.18           N  
ANISOU 1127  N   LYS C 153     6470   6214   8281    456   -330   1550       N  
ATOM   1128  CA  LYS C 153     -20.398  53.399 -64.966  1.00 63.89           C  
ANISOU 1128  CA  LYS C 153     7579   7256   9441    471   -352   1682       C  
ATOM   1129  C   LYS C 153     -19.016  53.540 -65.594  1.00 69.71           C  
ANISOU 1129  C   LYS C 153     8330   7965  10193    383   -342   1754       C  
ATOM   1130  O   LYS C 153     -18.895  53.834 -66.791  1.00 71.74           O  
ANISOU 1130  O   LYS C 153     8570   8260  10427    368   -343   1880       O  
ATOM   1131  CB  LYS C 153     -20.820  54.707 -64.285  1.00 67.54           C  
ANISOU 1131  CB  LYS C 153     8071   7565  10025    545   -383   1673       C  
ATOM   1132  CG  LYS C 153     -20.492  55.972 -65.090  1.00 75.89           C  
ANISOU 1132  CG  LYS C 153     9147   8516  11172    548   -409   1808       C  
ATOM   1133  CD  LYS C 153     -21.146  55.912 -66.468  1.00 81.09           C  
ANISOU 1133  CD  LYS C 153     9767   9284  11758    568   -412   1936       C  
ATOM   1134  CE  LYS C 153     -21.378  57.280 -67.076  1.00 86.92           C  
ANISOU 1134  CE  LYS C 153    10527   9940  12556    598   -435   2018       C  
ATOM   1135  NZ  LYS C 153     -21.882  58.259 -66.067  1.00 94.93           N  
ANISOU 1135  NZ  LYS C 153    11578  10816  13676    670   -464   1940       N  
ATOM   1136  N   ASN C 154     -17.960  53.314 -64.812  1.00 68.53           N  
ANISOU 1136  N   ASN C 154     8206   7759  10074    326   -330   1677       N  
ATOM   1137  CA  ASN C 154     -16.608  53.379 -65.349  1.00 70.14           C  
ANISOU 1137  CA  ASN C 154     8415   7945  10289    238   -317   1737       C  
ATOM   1138  C   ASN C 154     -16.218  52.131 -66.141  1.00 71.42           C  
ANISOU 1138  C   ASN C 154     8543   8270  10323    183   -288   1748       C  
ATOM   1139  O   ASN C 154     -15.061  52.024 -66.566  1.00 74.67           O  
ANISOU 1139  O   ASN C 154     8952   8690  10728    110   -272   1786       O  
ATOM   1140  CB  ASN C 154     -15.603  53.606 -64.219  1.00 70.85           C  
ANISOU 1140  CB  ASN C 154     8541   7917  10461    199   -320   1646       C  
ATOM   1141  CG  ASN C 154     -15.938  54.818 -63.375  1.00 73.73           C  
ANISOU 1141  CG  ASN C 154     8942   8118  10956    257   -355   1616       C  
ATOM   1142  OD1 ASN C 154     -16.663  55.713 -63.806  1.00 77.91           O  
ANISOU 1142  OD1 ASN C 154     9472   8594  11535    314   -378   1694       O  
ATOM   1143  ND2 ASN C 154     -15.397  54.857 -62.162  1.00 69.15           N  
ANISOU 1143  ND2 ASN C 154     8390   7455  10428    248   -362   1499       N  
ATOM   1144  N   ASN C 155     -17.149  51.195 -66.362  1.00 70.52           N  
ANISOU 1144  N   ASN C 155     8400   8285  10111    215   -282   1714       N  
ATOM   1145  CA  ASN C 155     -16.852  49.945 -67.054  1.00 77.14           C  
ANISOU 1145  CA  ASN C 155     9206   9274  10830    170   -261   1705       C  
ATOM   1146  C   ASN C 155     -17.879  49.656 -68.147  1.00 87.23           C  
ANISOU 1146  C   ASN C 155    10442  10678  12023    211   -270   1771       C  
ATOM   1147  O   ASN C 155     -18.111  48.499 -68.497  1.00 85.69           O  
ANISOU 1147  O   ASN C 155    10217  10612  11730    198   -263   1728       O  
ATOM   1148  CB  ASN C 155     -16.801  48.786 -66.057  1.00 70.77           C  
ANISOU 1148  CB  ASN C 155     8403   8502   9984    153   -249   1564       C  
ATOM   1149  CG  ASN C 155     -16.349  47.472 -66.687  1.00 71.81           C  
ANISOU 1149  CG  ASN C 155     8507   8771  10009    103   -233   1542       C  
ATOM   1150  OD1 ASN C 155     -15.521  47.455 -67.593  1.00 79.40           O  
ANISOU 1150  OD1 ASN C 155     9455   9776  10937     59   -224   1608       O  
ATOM   1151  ND2 ASN C 155     -16.944  46.367 -66.239  1.00 70.40           N  
ANISOU 1151  ND2 ASN C 155     8314   8661   9772    112   -232   1451       N  
ATOM   1152  N   GLN C 156     -18.507  50.680 -68.722  1.00 90.80           N  
ANISOU 1152  N   GLN C 156    10890  11097  12513    262   -289   1874       N  
ATOM   1153  CA  GLN C 156     -19.678  50.437 -69.563  1.00 91.77           C  
ANISOU 1153  CA  GLN C 156    10973  11335  12561    317   -303   1919       C  
ATOM   1154  C   GLN C 156     -19.387  50.378 -71.058  1.00 89.95           C  
ANISOU 1154  C   GLN C 156    10711  11216  12249    298   -300   2037       C  
ATOM   1155  O   GLN C 156     -20.314  50.223 -71.852  1.00 83.26           O  
ANISOU 1155  O   GLN C 156     9828  10471  11335    344   -317   2081       O  
ATOM   1156  CB  GLN C 156     -20.769  51.473 -69.304  1.00 94.18           C  
ANISOU 1156  CB  GLN C 156    11284  11561  12939    402   -330   1953       C  
ATOM   1157  CG  GLN C 156     -22.140  50.954 -69.695  1.00104.29           C  
ANISOU 1157  CG  GLN C 156    12519  12961  14145    463   -345   1942       C  
ATOM   1158  CD  GLN C 156     -23.087  51.066 -68.553  1.00113.01           C  
ANISOU 1158  CD  GLN C 156    13627  14011  15300    523   -353   1851       C  
ATOM   1159  OE1 GLN C 156     -22.862  51.867 -67.657  1.00117.76           O  
ANISOU 1159  OE1 GLN C 156    14267  14474  16000    540   -357   1823       O  
ATOM   1160  NE2 GLN C 156     -24.118  50.234 -68.534  1.00118.10           N  
ANISOU 1160  NE2 GLN C 156    14228  14767  15878    552   -357   1796       N  
ATOM   1161  N   LEU C 157     -18.138  50.469 -71.480  1.00 90.57           N  
ANISOU 1161  N   LEU C 157    10798  11290  12325    232   -280   2088       N  
ATOM   1162  CA  LEU C 157     -17.801  49.974 -72.808  1.00 88.78           C  
ANISOU 1162  CA  LEU C 157    10532  11214  11985    209   -270   2162       C  
ATOM   1163  C   LEU C 157     -17.098  48.628 -72.723  1.00 81.43           C  
ANISOU 1163  C   LEU C 157     9589  10378  10974    153   -251   2059       C  
ATOM   1164  O   LEU C 157     -16.356  48.242 -73.632  1.00 78.91           O  
ANISOU 1164  O   LEU C 157     9245  10161  10576    116   -235   2103       O  
ATOM   1165  CB  LEU C 157     -16.983  51.000 -73.592  1.00 92.17           C  
ANISOU 1165  CB  LEU C 157    10966  11605  12448    182   -260   2314       C  
ATOM   1166  CG  LEU C 157     -17.881  52.200 -73.966  1.00 95.91           C  
ANISOU 1166  CG  LEU C 157    11445  12017  12979    250   -287   2432       C  
ATOM   1167  CD1 LEU C 157     -17.131  53.246 -74.775  1.00 98.33           C  
ANISOU 1167  CD1 LEU C 157    11756  12290  13314    216   -271   2551       C  
ATOM   1168  CD2 LEU C 157     -19.140  51.750 -74.712  1.00 96.17           C  
ANISOU 1168  CD2 LEU C 157    11438  12190  12911    319   -309   2444       C  
ATOM   1169  N   ALA C 158     -17.345  47.903 -71.633  1.00 78.34           N  
ANISOU 1169  N   ALA C 158     9211   9956  10599    150   -252   1923       N  
ATOM   1170  CA  ALA C 158     -16.798  46.568 -71.458  1.00 78.26           C  
ANISOU 1170  CA  ALA C 158     9190  10024  10519    104   -239   1818       C  
ATOM   1171  C   ALA C 158     -17.374  45.624 -72.501  1.00 75.81           C  
ANISOU 1171  C   ALA C 158     8832   9884  10087    122   -252   1814       C  
ATOM   1172  O   ALA C 158     -18.560  45.687 -72.839  1.00 74.13           O  
ANISOU 1172  O   ALA C 158     8597   9719   9851    177   -275   1834       O  
ATOM   1173  CB  ALA C 158     -17.099  46.043 -70.054  1.00 77.73           C  
ANISOU 1173  CB  ALA C 158     9147   9888  10499    106   -241   1686       C  
ATOM   1174  N   LEU C 159     -16.521  44.744 -73.008  1.00 73.07           N  
ANISOU 1174  N   LEU C 159     8468   9631   9663     78   -240   1783       N  
ATOM   1175  CA  LEU C 159     -16.906  43.868 -74.100  1.00 78.10           C  
ANISOU 1175  CA  LEU C 159     9059  10434  10180     93   -255   1777       C  
ATOM   1176  C   LEU C 159     -18.008  42.910 -73.663  1.00 76.83           C  
ANISOU 1176  C   LEU C 159     8883  10308  10000    118   -281   1671       C  
ATOM   1177  O   LEU C 159     -18.111  42.532 -72.495  1.00 78.67           O  
ANISOU 1177  O   LEU C 159     9141  10461  10291    104   -278   1580       O  
ATOM   1178  CB  LEU C 159     -15.692  43.090 -74.605  1.00 82.44           C  
ANISOU 1178  CB  LEU C 159     9597  11068  10659     45   -238   1747       C  
ATOM   1179  CG  LEU C 159     -14.435  43.929 -74.847  1.00 87.79           C  
ANISOU 1179  CG  LEU C 159    10286  11705  11366      5   -206   1840       C  
ATOM   1180  CD1 LEU C 159     -13.365  43.087 -75.520  1.00 85.35           C  
ANISOU 1180  CD1 LEU C 159     9950  11515  10965    -31   -190   1811       C  
ATOM   1181  CD2 LEU C 159     -14.746  45.176 -75.673  1.00 88.74           C  
ANISOU 1181  CD2 LEU C 159    10396  11826  11495     36   -206   1999       C  
ATOM   1182  N   THR C 160     -18.849  42.530 -74.619  1.00 70.28           N  
ANISOU 1182  N   THR C 160     8010   9604   9089    155   -308   1687       N  
ATOM   1183  CA  THR C 160     -19.978  41.649 -74.339  1.00 59.85           C  
ANISOU 1183  CA  THR C 160     6664   8325   7751    176   -337   1597       C  
ATOM   1184  C   THR C 160     -20.166  40.754 -75.554  1.00 67.91           C  
ANISOU 1184  C   THR C 160     7636   9513   8656    185   -364   1578       C  
ATOM   1185  O   THR C 160     -20.640  41.216 -76.596  1.00 76.34           O  
ANISOU 1185  O   THR C 160     8673  10667   9666    227   -381   1661       O  
ATOM   1186  CB  THR C 160     -21.239  42.459 -74.035  1.00 52.29           C  
ANISOU 1186  CB  THR C 160     5700   7320   6847    233   -351   1641       C  
ATOM   1187  OG1 THR C 160     -21.129  43.043 -72.731  1.00 57.40           O  
ANISOU 1187  OG1 THR C 160     6391   7817   7600    227   -331   1620       O  
ATOM   1188  CG2 THR C 160     -22.469  41.584 -74.079  1.00 49.18           C  
ANISOU 1188  CG2 THR C 160     5262   7006   6419    257   -384   1570       C  
ATOM   1189  N   LEU C 161     -19.777  39.487 -75.428  1.00 65.46           N  
ANISOU 1189  N   LEU C 161     7318   9244   8308    148   -372   1468       N  
ATOM   1190  CA  LEU C 161     -19.855  38.527 -76.528  1.00 64.05           C  
ANISOU 1190  CA  LEU C 161     7094   9219   8021    155   -404   1426       C  
ATOM   1191  C   LEU C 161     -20.758  37.388 -76.070  1.00 59.77           C  
ANISOU 1191  C   LEU C 161     6531   8689   7490    150   -438   1310       C  
ATOM   1192  O   LEU C 161     -20.339  36.527 -75.288  1.00 61.13           O  
ANISOU 1192  O   LEU C 161     6723   8809   7694    107   -434   1216       O  
ATOM   1193  CB  LEU C 161     -18.470  38.028 -76.925  1.00 70.47           C  
ANISOU 1193  CB  LEU C 161     7915  10078   8781    119   -386   1400       C  
ATOM   1194  CG  LEU C 161     -18.320  37.625 -78.392  1.00 74.41           C  
ANISOU 1194  CG  LEU C 161     8368  10751   9153    144   -407   1413       C  
ATOM   1195  CD1 LEU C 161     -18.238  38.861 -79.281  1.00 75.85           C  
ANISOU 1195  CD1 LEU C 161     8540  10982   9298    178   -390   1566       C  
ATOM   1196  CD2 LEU C 161     -17.109  36.728 -78.595  1.00 71.32           C  
ANISOU 1196  CD2 LEU C 161     7978  10411   8711    110   -399   1337       C  
ATOM   1197  N   ILE C 162     -21.996  37.382 -76.558  1.00 56.29           N  
ANISOU 1197  N   ILE C 162     6047   8316   7024    191   -474   1322       N  
ATOM   1198  CA  ILE C 162     -23.054  36.538 -76.014  1.00 55.00           C  
ANISOU 1198  CA  ILE C 162     5858   8148   6893    186   -505   1234       C  
ATOM   1199  C   ILE C 162     -23.643  35.698 -77.138  1.00 57.83           C  
ANISOU 1199  C   ILE C 162     6157   8653   7163    205   -560   1188       C  
ATOM   1200  O   ILE C 162     -24.353  36.216 -78.011  1.00 61.24           O  
ANISOU 1200  O   ILE C 162     6552   9172   7546    256   -583   1251       O  
ATOM   1201  CB  ILE C 162     -24.133  37.371 -75.318  1.00 52.60           C  
ANISOU 1201  CB  ILE C 162     5551   7773   6661    219   -499   1282       C  
ATOM   1202  CG1 ILE C 162     -23.540  38.006 -74.057  1.00 51.72           C  
ANISOU 1202  CG1 ILE C 162     5498   7512   6641    197   -451   1295       C  
ATOM   1203  CG2 ILE C 162     -25.334  36.514 -74.974  1.00 53.40           C  
ANISOU 1203  CG2 ILE C 162     5607   7900   6782    217   -533   1204       C  
ATOM   1204  CD1 ILE C 162     -24.508  38.835 -73.311  1.00 54.55           C  
ANISOU 1204  CD1 ILE C 162     5857   7799   7071    235   -443   1332       C  
ATOM   1205  N   ASP C 163     -23.339  34.403 -77.116  1.00 58.32           N  
ANISOU 1205  N   ASP C 163     6210   8742   7207    167   -583   1075       N  
ATOM   1206  CA  ASP C 163     -23.892  33.450 -78.066  1.00 62.85           C  
ANISOU 1206  CA  ASP C 163     6728   9442   7709    180   -644   1005       C  
ATOM   1207  C   ASP C 163     -25.285  33.029 -77.611  1.00 62.00           C  
ANISOU 1207  C   ASP C 163     6581   9322   7656    179   -678    962       C  
ATOM   1208  O   ASP C 163     -25.482  32.660 -76.449  1.00 57.30           O  
ANISOU 1208  O   ASP C 163     6003   8623   7146    140   -663    920       O  
ATOM   1209  CB  ASP C 163     -22.960  32.240 -78.177  1.00 68.12           C  
ANISOU 1209  CB  ASP C 163     7406  10129   8348    142   -658    897       C  
ATOM   1210  CG  ASP C 163     -23.538  31.109 -79.010  1.00 73.06           C  
ANISOU 1210  CG  ASP C 163     7976  10865   8917    150   -729    798       C  
ATOM   1211  OD1 ASP C 163     -24.539  31.316 -79.727  1.00 82.82           O  
ANISOU 1211  OD1 ASP C 163     9162  12191  10115    190   -767    821       O  
ATOM   1212  OD2 ASP C 163     -22.969  29.998 -78.949  1.00 71.52           O  
ANISOU 1212  OD2 ASP C 163     7787  10666   8720    118   -751    693       O  
ATOM   1213  N   THR C 164     -26.250  33.083 -78.530  1.00 67.50           N  
ANISOU 1213  N   THR C 164     7218  10129   8298    223   -724    975       N  
ATOM   1214  CA  THR C 164     -27.637  32.746 -78.234  1.00 65.06           C  
ANISOU 1214  CA  THR C 164     6858   9826   8036    225   -760    942       C  
ATOM   1215  C   THR C 164     -28.094  31.469 -78.927  1.00 64.25           C  
ANISOU 1215  C   THR C 164     6700   9820   7894    211   -832    832       C  
ATOM   1216  O   THR C 164     -29.283  31.141 -78.874  1.00 70.59           O  
ANISOU 1216  O   THR C 164     7447  10649   8727    213   -871    802       O  
ATOM   1217  CB  THR C 164     -28.559  33.903 -78.624  1.00 66.27           C  
ANISOU 1217  CB  THR C 164     6982  10021   8175    290   -762   1045       C  
ATOM   1218  OG1 THR C 164     -28.391  34.200 -80.016  1.00 69.90           O  
ANISOU 1218  OG1 THR C 164     7419  10615   8525    340   -790   1087       O  
ATOM   1219  CG2 THR C 164     -28.226  35.140 -77.812  1.00 67.36           C  
ANISOU 1219  CG2 THR C 164     7175  10045   8374    303   -699   1142       C  
ATOM   1220  N   ASN C 165     -27.188  30.746 -79.580  1.00 63.01           N  
ANISOU 1220  N   ASN C 165     6552   9717   7672    200   -852    767       N  
ATOM   1221  CA  ASN C 165     -27.560  29.504 -80.244  1.00 63.05           C  
ANISOU 1221  CA  ASN C 165     6506   9805   7643    190   -927    649       C  
ATOM   1222  C   ASN C 165     -27.875  28.434 -79.205  1.00 61.77           C  
ANISOU 1222  C   ASN C 165     6344   9540   7587    121   -941    557       C  
ATOM   1223  O   ASN C 165     -27.090  28.206 -78.279  1.00 64.35           O  
ANISOU 1223  O   ASN C 165     6725   9755   7970     78   -899    544       O  
ATOM   1224  CB  ASN C 165     -26.433  29.040 -81.165  1.00 65.70           C  
ANISOU 1224  CB  ASN C 165     6855  10224   7883    202   -942    598       C  
ATOM   1225  CG  ASN C 165     -26.033  30.098 -82.178  1.00 73.78           C  
ANISOU 1225  CG  ASN C 165     7879  11356   8799    266   -920    702       C  
ATOM   1226  OD1 ASN C 165     -26.813  30.995 -82.498  1.00 83.96           O  
ANISOU 1226  OD1 ASN C 165     9143  12688  10070    310   -920    793       O  
ATOM   1227  ND2 ASN C 165     -24.806  30.003 -82.680  1.00 68.03           N  
ANISOU 1227  ND2 ASN C 165     7177  10673   7998    272   -901    694       N  
ATOM   1228  N   ARG C 166     -29.029  27.780 -79.350  1.00 63.06           N  
ANISOU 1228  N   ARG C 166     6441   9739   7778    110  -1001    499       N  
ATOM   1229  CA  ARG C 166     -29.477  26.795 -78.375  1.00 63.00           C  
ANISOU 1229  CA  ARG C 166     6424   9637   7878     42  -1015    429       C  
ATOM   1230  C   ARG C 166     -29.954  25.526 -79.066  1.00 69.36           C  
ANISOU 1230  C   ARG C 166     7171  10505   8677     21  -1106    307       C  
ATOM   1231  O   ARG C 166     -30.156  25.480 -80.283  1.00 75.16           O  
ANISOU 1231  O   ARG C 166     7885  11342   9331     67  -1149    271       O  
ATOM   1232  CB  ARG C 166     -30.621  27.321 -77.500  1.00 58.54           C  
ANISOU 1232  CB  ARG C 166     5829   9021   7391     34   -989    492       C  
ATOM   1233  CG  ARG C 166     -30.765  28.816 -77.435  1.00 58.59           C  
ANISOU 1233  CG  ARG C 166     5853   9035   7375     92   -936    616       C  
ATOM   1234  CD  ARG C 166     -32.090  29.165 -76.784  1.00 63.91           C  
ANISOU 1234  CD  ARG C 166     6477   9690   8116     95   -929    654       C  
ATOM   1235  NE  ARG C 166     -32.237  30.595 -76.543  1.00 72.60           N  
ANISOU 1235  NE  ARG C 166     7599  10774   9212    152   -877    767       N  
ATOM   1236  CZ  ARG C 166     -31.577  31.262 -75.603  1.00 74.41           C  
ANISOU 1236  CZ  ARG C 166     7895  10897   9482    147   -809    820       C  
ATOM   1237  NH1 ARG C 166     -30.714  30.629 -74.822  1.00 69.16           N  
ANISOU 1237  NH1 ARG C 166     7280  10141   8855     91   -782    773       N  
ATOM   1238  NH2 ARG C 166     -31.775  32.563 -75.446  1.00 80.40           N  
ANISOU 1238  NH2 ARG C 166     8669  11638  10242    203   -771    916       N  
ATOM   1239  N   SER C 167     -30.162  24.496 -78.243  1.00 65.22           N  
ANISOU 1239  N   SER C 167     6642   9886   8251    -48  -1123    239       N  
ATOM   1240  CA  SER C 167     -30.733  23.226 -78.673  1.00 62.17           C  
ANISOU 1240  CA  SER C 167     6210   9513   7898    -82  -1206    120       C  
ATOM   1241  C   SER C 167     -32.060  22.939 -77.977  1.00 58.18           C  
ANISOU 1241  C   SER C 167     5650   8959   7496   -128  -1217    126       C  
ATOM   1242  O   SER C 167     -32.458  21.776 -77.863  1.00 56.40           O  
ANISOU 1242  O   SER C 167     5401   8685   7344   -182  -1270     38       O  
ATOM   1243  CB  SER C 167     -29.745  22.085 -78.424  1.00 66.93           C  
ANISOU 1243  CB  SER C 167     6848  10051   8531   -129  -1230     24       C  
ATOM   1244  OG  SER C 167     -28.499  22.346 -79.044  1.00 70.15           O  
ANISOU 1244  OG  SER C 167     7304  10506   8843    -84  -1213     16       O  
ATOM   1245  N   ARG C 168     -32.743  23.976 -77.495  1.00 53.98           N  
ANISOU 1245  N   ARG C 168     5099   8436   6976   -106  -1169    231       N  
ATOM   1246  CA  ARG C 168     -34.058  23.818 -76.888  1.00 49.72           C  
ANISOU 1246  CA  ARG C 168     4502   7867   6523   -139  -1172    243       C  
ATOM   1247  C   ARG C 168     -34.787  25.150 -76.958  1.00 56.57           C  
ANISOU 1247  C   ARG C 168     5349   8790   7357    -75  -1133    344       C  
ATOM   1248  O   ARG C 168     -34.171  26.208 -77.108  1.00 58.63           O  
ANISOU 1248  O   ARG C 168     5647   9077   7553    -20  -1090    423       O  
ATOM   1249  CB  ARG C 168     -33.963  23.330 -75.436  1.00 45.42           C  
ANISOU 1249  CB  ARG C 168     3964   7209   6084   -216  -1135    261       C  
ATOM   1250  CG  ARG C 168     -33.640  24.417 -74.411  1.00 52.59           C  
ANISOU 1250  CG  ARG C 168     4928   8053   7002   -194  -1038    367       C  
ATOM   1251  CD  ARG C 168     -33.591  23.843 -72.998  1.00 54.37           C  
ANISOU 1251  CD  ARG C 168     5175   8158   7326   -264   -996    372       C  
ATOM   1252  NE  ARG C 168     -33.155  24.818 -72.000  1.00 51.60           N  
ANISOU 1252  NE  ARG C 168     4884   7743   6979   -241   -907    456       N  
ATOM   1253  CZ  ARG C 168     -33.970  25.447 -71.158  1.00 57.42           C  
ANISOU 1253  CZ  ARG C 168     5593   8468   7754   -231   -860    524       C  
ATOM   1254  NH1 ARG C 168     -35.274  25.208 -71.187  1.00 62.58           N  
ANISOU 1254  NH1 ARG C 168     6157   9174   8448   -246   -888    525       N  
ATOM   1255  NH2 ARG C 168     -33.479  26.315 -70.283  1.00 61.12           N  
ANISOU 1255  NH2 ARG C 168     6122   8876   8224   -205   -785    587       N  
ATOM   1256  N   ALA C 169     -36.110  25.083 -76.863  1.00 57.12           N  
ANISOU 1256  N   ALA C 169     5356   8874   7474    -81  -1150    342       N  
ATOM   1257  CA  ALA C 169     -36.927  26.278 -76.734  1.00 57.76           C  
ANISOU 1257  CA  ALA C 169     5412   8993   7542    -24  -1112    434       C  
ATOM   1258  C   ALA C 169     -36.979  26.695 -75.271  1.00 63.23           C  
ANISOU 1258  C   ALA C 169     6111   9606   8307    -50  -1040    509       C  
ATOM   1259  O   ALA C 169     -36.779  25.878 -74.369  1.00 69.23           O  
ANISOU 1259  O   ALA C 169     6874  10288   9140   -122  -1029    481       O  
ATOM   1260  CB  ALA C 169     -38.338  26.032 -77.269  1.00 55.40           C  
ANISOU 1260  CB  ALA C 169     5039   8750   7261    -17  -1162    396       C  
ATOM   1261  N   CYS C 170     -37.233  27.977 -75.040  1.00 62.13           N  
ANISOU 1261  N   CYS C 170     5977   9484   8147     14   -993    603       N  
ATOM   1262  CA  CYS C 170     -37.325  28.516 -73.693  1.00 63.20           C  
ANISOU 1262  CA  CYS C 170     6118   9551   8344      8   -924    673       C  
ATOM   1263  C   CYS C 170     -38.767  28.906 -73.396  1.00 65.13           C  
ANISOU 1263  C   CYS C 170     6296   9826   8623     32   -914    699       C  
ATOM   1264  O   CYS C 170     -39.467  29.442 -74.258  1.00 71.08           O  
ANISOU 1264  O   CYS C 170     7021  10654   9333     91   -942    708       O  
ATOM   1265  CB  CYS C 170     -36.421  29.738 -73.509  1.00 65.75           C  
ANISOU 1265  CB  CYS C 170     6522   9833   8628     66   -865    750       C  
ATOM   1266  SG  CYS C 170     -34.755  29.602 -74.226  1.00 81.73           S  
ANISOU 1266  SG  CYS C 170     8637  11836  10579     63   -869    725       S  
ATOM   1267  N   HIS C 171     -39.217  28.630 -72.178  1.00 57.52           N  
ANISOU 1267  N   HIS C 171     5308   8810   7737    -11   -874    710       N  
ATOM   1268  CA  HIS C 171     -40.451  29.238 -71.683  1.00 54.09           C  
ANISOU 1268  CA  HIS C 171     4817   8403   7332     24   -846    751       C  
ATOM   1269  C   HIS C 171     -40.238  30.744 -71.534  1.00 54.00           C  
ANISOU 1269  C   HIS C 171     4839   8391   7285    117   -801    837       C  
ATOM   1270  O   HIS C 171     -39.108  31.208 -71.370  1.00 56.39           O  
ANISOU 1270  O   HIS C 171     5212   8646   7569    133   -775    871       O  
ATOM   1271  CB  HIS C 171     -40.849  28.626 -70.340  1.00 58.54           C  
ANISOU 1271  CB  HIS C 171     5353   8912   7978    -41   -803    751       C  
ATOM   1272  CG  HIS C 171     -41.153  27.160 -70.401  1.00 68.19           C  
ANISOU 1272  CG  HIS C 171     6539  10120   9249   -135   -845    675       C  
ATOM   1273  ND1 HIS C 171     -40.319  26.206 -69.863  1.00 77.25           N  
ANISOU 1273  ND1 HIS C 171     7726  11190  10436   -212   -841    646       N  
ATOM   1274  CD2 HIS C 171     -42.208  26.487 -70.920  1.00 68.54           C  
ANISOU 1274  CD2 HIS C 171     6514  10210   9318   -163   -894    622       C  
ATOM   1275  CE1 HIS C 171     -40.845  25.008 -70.047  1.00 77.95           C  
ANISOU 1275  CE1 HIS C 171     7772  11272  10574   -284   -886    580       C  
ATOM   1276  NE2 HIS C 171     -41.989  25.150 -70.692  1.00 76.74           N  
ANISOU 1276  NE2 HIS C 171     7551  11194  10415   -257   -920    563       N  
ATOM   1277  N   PRO C 172     -41.303  31.535 -71.600  1.00 52.64           N  
ANISOU 1277  N   PRO C 172     4623   8266   7110    181   -794    871       N  
ATOM   1278  CA  PRO C 172     -41.146  32.975 -71.361  1.00 51.84           C  
ANISOU 1278  CA  PRO C 172     4556   8150   6991    273   -753    951       C  
ATOM   1279  C   PRO C 172     -40.725  33.254 -69.928  1.00 55.58           C  
ANISOU 1279  C   PRO C 172     5055   8545   7517    265   -686    985       C  
ATOM   1280  O   PRO C 172     -40.866  32.411 -69.035  1.00 57.34           O  
ANISOU 1280  O   PRO C 172     5255   8742   7791    197   -663    956       O  
ATOM   1281  CB  PRO C 172     -42.548  33.554 -71.651  1.00 45.94           C  
ANISOU 1281  CB  PRO C 172     3746   7470   6240    334   -766    963       C  
ATOM   1282  CG  PRO C 172     -43.333  32.451 -72.257  1.00 49.99           C  
ANISOU 1282  CG  PRO C 172     4193   8041   6757    278   -820    891       C  
ATOM   1283  CD  PRO C 172     -42.713  31.162 -71.831  1.00 50.08           C  
ANISOU 1283  CD  PRO C 172     4216   8005   6806    175   -824    836       C  
ATOM   1284  N   CYS C 173     -40.171  34.456 -69.725  1.00 57.79           N  
ANISOU 1284  N   CYS C 173     5404   8772   7782    336   -648   1038       N  
ATOM   1285  CA  CYS C 173     -39.941  34.931 -68.364  1.00 57.64           C  
ANISOU 1285  CA  CYS C 173     5429   8667   7805    347   -578   1054       C  
ATOM   1286  C   CYS C 173     -41.263  34.949 -67.601  1.00 50.40           C  
ANISOU 1286  C   CYS C 173     4419   7802   6930    367   -559   1059       C  
ATOM   1287  O   CYS C 173     -42.351  34.980 -68.188  1.00 47.95           O  
ANISOU 1287  O   CYS C 173     4031   7578   6611    393   -593   1059       O  
ATOM   1288  CB  CYS C 173     -39.338  36.331 -68.357  1.00 69.13           C  
ANISOU 1288  CB  CYS C 173     6960  10059   9246    430   -551   1107       C  
ATOM   1289  SG  CYS C 173     -37.623  36.548 -68.957  1.00 86.05           S  
ANISOU 1289  SG  CYS C 173     9221  12124  11349    411   -552   1117       S  
ATOM   1290  N   SER C 174     -41.162  34.937 -66.284  1.00 43.81           N  
ANISOU 1290  N   SER C 174     3604   6911   6131    354   -498   1055       N  
ATOM   1291  CA  SER C 174     -42.352  35.008 -65.453  1.00 38.00           C  
ANISOU 1291  CA  SER C 174     2780   6228   5428    377   -469   1064       C  
ATOM   1292  C   SER C 174     -43.135  36.281 -65.770  1.00 40.36           C  
ANISOU 1292  C   SER C 174     3044   6573   5717    493   -476   1104       C  
ATOM   1293  O   SER C 174     -42.531  37.325 -66.045  1.00 43.30           O  
ANISOU 1293  O   SER C 174     3491   6889   6071    560   -474   1132       O  
ATOM   1294  CB  SER C 174     -41.970  34.982 -63.968  1.00 40.30           C  
ANISOU 1294  CB  SER C 174     3113   6452   5747    362   -398   1058       C  
ATOM   1295  OG  SER C 174     -43.068  35.333 -63.151  1.00 48.98           O  
ANISOU 1295  OG  SER C 174     4134   7609   6867    410   -362   1073       O  
ATOM   1296  N   PRO C 175     -44.476  36.234 -65.763  1.00 46.48           N  
ANISOU 1296  N   PRO C 175     3742   7422   6498    510   -480   1090       N  
ATOM   1297  CA  PRO C 175     -45.264  37.466 -65.938  1.00 48.59           C  
ANISOU 1297  CA  PRO C 175     3992   7716   6754    622   -480   1115       C  
ATOM   1298  C   PRO C 175     -44.896  38.526 -64.908  1.00 53.00           C  
ANISOU 1298  C   PRO C 175     4593   8211   7333    703   -427   1142       C  
ATOM   1299  O   PRO C 175     -45.219  39.707 -65.070  1.00 56.14           O  
ANISOU 1299  O   PRO C 175     5004   8599   7727    805   -431   1166       O  
ATOM   1300  CB  PRO C 175     -46.715  36.998 -65.759  1.00 38.22           C  
ANISOU 1300  CB  PRO C 175     2579   6488   5453    607   -480   1087       C  
ATOM   1301  CG  PRO C 175     -46.693  35.503 -65.790  1.00 36.40           C  
ANISOU 1301  CG  PRO C 175     2316   6275   5237    483   -494   1049       C  
ATOM   1302  CD  PRO C 175     -45.284  35.015 -65.921  1.00 41.36           C  
ANISOU 1302  CD  PRO C 175     3021   6833   5862    424   -501   1048       C  
ATOM   1303  N   MET C 176     -44.211  38.097 -63.844  1.00 53.36           N  
ANISOU 1303  N   MET C 176     4662   8211   7402    659   -381   1135       N  
ATOM   1304  CA  MET C 176     -43.730  39.022 -62.825  1.00 51.51           C  
ANISOU 1304  CA  MET C 176     4496   7895   7180    724   -329   1136       C  
ATOM   1305  C   MET C 176     -42.708  40.000 -63.395  1.00 54.20           C  
ANISOU 1305  C   MET C 176     4946   8138   7512    772   -347   1157       C  
ATOM   1306  O   MET C 176     -42.687  41.176 -63.012  1.00 52.05           O  
ANISOU 1306  O   MET C 176     4708   7814   7254    865   -331   1170       O  
ATOM   1307  CB  MET C 176     -43.127  38.230 -61.665  1.00 52.76           C  
ANISOU 1307  CB  MET C 176     4690   8009   7349    649   -277   1105       C  
ATOM   1308  CG  MET C 176     -42.488  39.080 -60.589  1.00 60.43           C  
ANISOU 1308  CG  MET C 176     5741   8894   8327    707   -227   1093       C  
ATOM   1309  SD  MET C 176     -43.599  39.344 -59.198  1.00 67.62           S  
ANISOU 1309  SD  MET C 176     6568   9877   9248    773   -167   1081       S  
ATOM   1310  CE  MET C 176     -42.752  38.417 -57.926  1.00 59.05           C  
ANISOU 1310  CE  MET C 176     5533   8746   8157    686   -111   1053       C  
ATOM   1311  N   CYS C 177     -41.850  39.536 -64.301  1.00 55.20           N  
ANISOU 1311  N   CYS C 177     5122   8235   7615    708   -381   1161       N  
ATOM   1312  CA  CYS C 177     -40.815  40.381 -64.889  1.00 56.62           C  
ANISOU 1312  CA  CYS C 177     5400   8328   7785    740   -396   1190       C  
ATOM   1313  C   CYS C 177     -41.449  41.246 -65.970  1.00 66.22           C  
ANISOU 1313  C   CYS C 177     6583   9591   8986    823   -443   1242       C  
ATOM   1314  O   CYS C 177     -41.748  40.757 -67.064  1.00 74.44           O  
ANISOU 1314  O   CYS C 177     7579  10710   9993    798   -490   1253       O  
ATOM   1315  CB  CYS C 177     -39.692  39.528 -65.472  1.00 54.47           C  
ANISOU 1315  CB  CYS C 177     5184   8025   7486    644   -413   1176       C  
ATOM   1316  SG  CYS C 177     -39.230  38.091 -64.482  1.00 55.16           S  
ANISOU 1316  SG  CYS C 177     5278   8094   7585    530   -377   1117       S  
ATOM   1317  N   LYS C 178     -41.650  42.534 -65.681  1.00 66.16           N  
ANISOU 1317  N   LYS C 178     6597   9535   9004    926   -433   1271       N  
ATOM   1318  CA  LYS C 178     -42.376  43.377 -66.624  1.00 64.01           C  
ANISOU 1318  CA  LYS C 178     6287   9310   8723   1015   -478   1324       C  
ATOM   1319  C   LYS C 178     -41.497  43.938 -67.732  1.00 58.51           C  
ANISOU 1319  C   LYS C 178     5664   8563   8003   1023   -512   1383       C  
ATOM   1320  O   LYS C 178     -42.029  44.396 -68.749  1.00 59.25           O  
ANISOU 1320  O   LYS C 178     5743   8700   8067   1067   -551   1417       O  
ATOM   1321  CB  LYS C 178     -43.085  44.520 -65.892  1.00 66.90           C  
ANISOU 1321  CB  LYS C 178     6646   9646   9129   1126   -458   1325       C  
ATOM   1322  CG  LYS C 178     -44.459  44.141 -65.328  1.00 73.83           C  
ANISOU 1322  CG  LYS C 178     7428  10619  10005   1140   -442   1278       C  
ATOM   1323  CD  LYS C 178     -45.039  42.887 -65.996  1.00 83.24           C  
ANISOU 1323  CD  LYS C 178     8549  11920  11160   1051   -467   1256       C  
ATOM   1324  CE  LYS C 178     -45.656  43.162 -67.371  1.00 88.93           C  
ANISOU 1324  CE  LYS C 178     9250  12697  11843   1080   -524   1279       C  
ATOM   1325  NZ  LYS C 178     -45.953  41.883 -68.080  1.00 89.65           N  
ANISOU 1325  NZ  LYS C 178     9287  12877  11900    986   -555   1249       N  
ATOM   1326  N   GLY C 179     -40.180  43.920 -67.567  1.00 45.02           N  
ANISOU 1326  N   GLY C 179     4050   6756   6298    970   -491   1380       N  
ATOM   1327  CA  GLY C 179     -39.300  44.212 -68.675  1.00 44.71           C  
ANISOU 1327  CA  GLY C 179     4069   6691   6228    957   -519   1435       C  
ATOM   1328  C   GLY C 179     -38.938  43.004 -69.502  1.00 54.06           C  
ANISOU 1328  C   GLY C 179     5235   7952   7353    867   -543   1415       C  
ATOM   1329  O   GLY C 179     -38.146  43.118 -70.443  1.00 57.07           O  
ANISOU 1329  O   GLY C 179     5660   8328   7696    850   -563   1456       O  
ATOM   1330  N   SER C 180     -39.510  41.843 -69.174  1.00 53.29           N  
ANISOU 1330  N   SER C 180     5071   7927   7248    809   -542   1352       N  
ATOM   1331  CA  SER C 180     -39.146  40.566 -69.785  1.00 50.49           C  
ANISOU 1331  CA  SER C 180     4702   7632   6850    717   -565   1313       C  
ATOM   1332  C   SER C 180     -37.652  40.286 -69.642  1.00 50.44           C  
ANISOU 1332  C   SER C 180     4790   7538   6838    651   -541   1298       C  
ATOM   1333  O   SER C 180     -37.044  39.647 -70.506  1.00 47.04           O  
ANISOU 1333  O   SER C 180     4371   7142   6359    601   -568   1289       O  
ATOM   1334  CB  SER C 180     -39.573  40.509 -71.255  1.00 51.78           C  
ANISOU 1334  CB  SER C 180     4816   7903   6954    740   -627   1345       C  
ATOM   1335  OG  SER C 180     -40.974  40.682 -71.377  1.00 59.41           O  
ANISOU 1335  OG  SER C 180     5707   8942   7922    789   -646   1338       O  
ATOM   1336  N   ARG C 181     -37.058  40.761 -68.545  1.00 50.51           N  
ANISOU 1336  N   ARG C 181     4862   7437   6892    654   -492   1291       N  
ATOM   1337  CA  ARG C 181     -35.640  40.587 -68.252  1.00 40.54           C  
ANISOU 1337  CA  ARG C 181     3687   6084   5631    597   -466   1275       C  
ATOM   1338  C   ARG C 181     -35.494  39.682 -67.034  1.00 37.24           C  
ANISOU 1338  C   ARG C 181     3272   5635   5241    534   -430   1205       C  
ATOM   1339  O   ARG C 181     -35.931  40.043 -65.935  1.00 45.25           O  
ANISOU 1339  O   ARG C 181     4281   6616   6297    567   -396   1191       O  
ATOM   1340  CB  ARG C 181     -34.959  41.935 -68.014  1.00 47.26           C  
ANISOU 1340  CB  ARG C 181     4614   6827   6515    652   -446   1325       C  
ATOM   1341  CG  ARG C 181     -34.986  42.874 -69.211  1.00 49.16           C  
ANISOU 1341  CG  ARG C 181     4860   7087   6733    711   -480   1410       C  
ATOM   1342  CD  ARG C 181     -34.031  44.035 -68.991  1.00 48.14           C  
ANISOU 1342  CD  ARG C 181     4815   6831   6644    738   -460   1459       C  
ATOM   1343  NE  ARG C 181     -34.071  45.016 -70.071  1.00 51.82           N  
ANISOU 1343  NE  ARG C 181     5288   7306   7097    797   -490   1555       N  
ATOM   1344  CZ  ARG C 181     -33.532  44.839 -71.273  1.00 53.71           C  
ANISOU 1344  CZ  ARG C 181     5533   7600   7275    771   -513   1604       C  
ATOM   1345  NH1 ARG C 181     -32.904  43.707 -71.568  1.00 47.59           N  
ANISOU 1345  NH1 ARG C 181     4757   6876   6448    691   -512   1556       N  
ATOM   1346  NH2 ARG C 181     -33.620  45.798 -72.184  1.00 56.48           N  
ANISOU 1346  NH2 ARG C 181     5888   7957   7613    831   -537   1702       N  
ATOM   1347  N   CYS C 182     -34.875  38.516 -67.223  1.00 40.05           N  
ANISOU 1347  N   CYS C 182     3638   6005   5574    449   -437   1162       N  
ATOM   1348  CA  CYS C 182     -34.869  37.501 -66.180  1.00 40.92           C  
ANISOU 1348  CA  CYS C 182     3740   6100   5709    385   -410   1103       C  
ATOM   1349  C   CYS C 182     -33.646  36.601 -66.315  1.00 41.06           C  
ANISOU 1349  C   CYS C 182     3812   6081   5708    304   -413   1065       C  
ATOM   1350  O   CYS C 182     -33.052  36.477 -67.390  1.00 44.00           O  
ANISOU 1350  O   CYS C 182     4203   6476   6040    290   -444   1074       O  
ATOM   1351  CB  CYS C 182     -36.167  36.673 -66.212  1.00 38.98           C  
ANISOU 1351  CB  CYS C 182     3393   5951   5467    366   -431   1081       C  
ATOM   1352  SG  CYS C 182     -36.399  35.576 -67.649  1.00 49.93           S  
ANISOU 1352  SG  CYS C 182     4724   7438   6810    312   -500   1058       S  
ATOM   1353  N   TRP C 183     -33.275  35.978 -65.192  1.00 33.56           N  
ANISOU 1353  N   TRP C 183     2886   5079   4785    257   -379   1024       N  
ATOM   1354  CA  TRP C 183     -32.175  35.021 -65.101  1.00 32.72           C  
ANISOU 1354  CA  TRP C 183     2829   4934   4671    182   -378    982       C  
ATOM   1355  C   TRP C 183     -32.655  33.577 -65.166  1.00 39.13           C  
ANISOU 1355  C   TRP C 183     3585   5797   5486    111   -404    937       C  
ATOM   1356  O   TRP C 183     -31.851  32.652 -65.002  1.00 38.95           O  
ANISOU 1356  O   TRP C 183     3597   5740   5464     49   -407    896       O  
ATOM   1357  CB  TRP C 183     -31.395  35.234 -63.802  1.00 31.50           C  
ANISOU 1357  CB  TRP C 183     2739   4684   4544    175   -329    966       C  
ATOM   1358  CG  TRP C 183     -30.745  36.570 -63.690  1.00 35.65           C  
ANISOU 1358  CG  TRP C 183     3326   5141   5077    232   -309    999       C  
ATOM   1359  CD1 TRP C 183     -31.227  37.664 -63.036  1.00 36.95           C  
ANISOU 1359  CD1 TRP C 183     3493   5276   5271    303   -284   1022       C  
ATOM   1360  CD2 TRP C 183     -29.483  36.954 -64.243  1.00 38.27           C  
ANISOU 1360  CD2 TRP C 183     3724   5423   5393    222   -314   1011       C  
ATOM   1361  NE1 TRP C 183     -30.344  38.711 -63.152  1.00 38.52           N  
ANISOU 1361  NE1 TRP C 183     3758   5399   5480    334   -278   1047       N  
ATOM   1362  CE2 TRP C 183     -29.264  38.299 -63.889  1.00 42.29           C  
ANISOU 1362  CE2 TRP C 183     4273   5865   5931    283   -294   1045       C  
ATOM   1363  CE3 TRP C 183     -28.516  36.291 -65.006  1.00 35.46           C  
ANISOU 1363  CE3 TRP C 183     3394   5075   5004    170   -335    994       C  
ATOM   1364  CZ2 TRP C 183     -28.120  38.995 -64.270  1.00 35.18           C  
ANISOU 1364  CZ2 TRP C 183     3434   4901   5031    284   -293   1071       C  
ATOM   1365  CZ3 TRP C 183     -27.381  36.983 -65.385  1.00 30.81           C  
ANISOU 1365  CZ3 TRP C 183     2864   4436   4407    176   -329   1020       C  
ATOM   1366  CH2 TRP C 183     -27.193  38.321 -65.016  1.00 31.23           C  
ANISOU 1366  CH2 TRP C 183     2953   4419   4494    228   -308   1062       C  
ATOM   1367  N   GLY C 184     -33.944  33.373 -65.392  1.00 44.86           N  
ANISOU 1367  N   GLY C 184     4225   6601   6220    121   -425    944       N  
ATOM   1368  CA  GLY C 184     -34.556  32.064 -65.327  1.00 46.68           C  
ANISOU 1368  CA  GLY C 184     4393   6873   6471     53   -448    906       C  
ATOM   1369  C   GLY C 184     -36.052  32.237 -65.455  1.00 46.37           C  
ANISOU 1369  C   GLY C 184     4255   6919   6445     84   -462    927       C  
ATOM   1370  O   GLY C 184     -36.557  33.353 -65.587  1.00 47.16           O  
ANISOU 1370  O   GLY C 184     4340   7042   6535    162   -452    968       O  
ATOM   1371  N   GLU C 185     -36.762  31.116 -65.409  1.00 40.75           N  
ANISOU 1371  N   GLU C 185     3473   6250   5761     21   -486    900       N  
ATOM   1372  CA  GLU C 185     -38.199  31.187 -65.634  1.00 38.32           C  
ANISOU 1372  CA  GLU C 185     3059   6034   5467     43   -505    916       C  
ATOM   1373  C   GLU C 185     -39.004  31.415 -64.358  1.00 36.46           C  
ANISOU 1373  C   GLU C 185     2779   5805   5269     58   -449    943       C  
ATOM   1374  O   GLU C 185     -40.214  31.646 -64.445  1.00 38.55           O  
ANISOU 1374  O   GLU C 185     2954   6149   5545     88   -456    962       O  
ATOM   1375  CB  GLU C 185     -38.689  29.923 -66.349  1.00 44.24           C  
ANISOU 1375  CB  GLU C 185     3738   6837   6232    -31   -568    873       C  
ATOM   1376  CG  GLU C 185     -38.582  28.639 -65.557  1.00 52.70           C  
ANISOU 1376  CG  GLU C 185     4802   7865   7357   -127   -559    843       C  
ATOM   1377  CD  GLU C 185     -39.373  27.517 -66.201  1.00 66.43           C  
ANISOU 1377  CD  GLU C 185     6451   9661   9129   -193   -625    805       C  
ATOM   1378  OE1 GLU C 185     -40.367  27.819 -66.896  1.00 68.74           O  
ANISOU 1378  OE1 GLU C 185     6669  10039   9411   -159   -658    809       O  
ATOM   1379  OE2 GLU C 185     -39.001  26.340 -66.021  1.00 75.29           O  
ANISOU 1379  OE2 GLU C 185     7583  10736  10289   -277   -645    767       O  
ATOM   1380  N   SER C 186     -38.369  31.388 -63.189  1.00 39.06           N  
ANISOU 1380  N   SER C 186     3167   6061   5612     43   -393    944       N  
ATOM   1381  CA  SER C 186     -39.083  31.612 -61.940  1.00 42.79           C  
ANISOU 1381  CA  SER C 186     3598   6550   6108     64   -336    968       C  
ATOM   1382  C   SER C 186     -39.435  33.090 -61.764  1.00 42.39           C  
ANISOU 1382  C   SER C 186     3552   6512   6040    176   -309    998       C  
ATOM   1383  O   SER C 186     -38.887  33.976 -62.427  1.00 45.44           O  
ANISOU 1383  O   SER C 186     3996   6868   6402    231   -326   1005       O  
ATOM   1384  CB  SER C 186     -38.249  31.130 -60.753  1.00 49.63           C  
ANISOU 1384  CB  SER C 186     4529   7341   6987     20   -288    959       C  
ATOM   1385  OG  SER C 186     -38.813  31.561 -59.529  1.00 58.14           O  
ANISOU 1385  OG  SER C 186     5579   8439   8072     60   -227    983       O  
ATOM   1386  N   SER C 187     -40.367  33.349 -60.842  1.00 35.03           N  
ANISOU 1386  N   SER C 187     2558   5628   5124    211   -266   1016       N  
ATOM   1387  CA  SER C 187     -40.812  34.717 -60.598  1.00 39.34           C  
ANISOU 1387  CA  SER C 187     3100   6188   5660    324   -243   1036       C  
ATOM   1388  C   SER C 187     -39.782  35.532 -59.829  1.00 46.02           C  
ANISOU 1388  C   SER C 187     4051   6938   6497    370   -203   1028       C  
ATOM   1389  O   SER C 187     -39.813  36.764 -59.893  1.00 55.00           O  
ANISOU 1389  O   SER C 187     5214   8054   7630    464   -199   1039       O  
ATOM   1390  CB  SER C 187     -42.142  34.728 -59.843  1.00 38.68           C  
ANISOU 1390  CB  SER C 187     2909   6196   5592    352   -209   1052       C  
ATOM   1391  OG  SER C 187     -41.965  34.369 -58.485  1.00 43.33           O  
ANISOU 1391  OG  SER C 187     3509   6769   6186    328   -148   1048       O  
ATOM   1392  N   GLU C 188     -38.877  34.879 -59.104  1.00 39.60           N  
ANISOU 1392  N   GLU C 188     3297   6063   5685    309   -176   1008       N  
ATOM   1393  CA  GLU C 188     -37.786  35.560 -58.419  1.00 44.71           C  
ANISOU 1393  CA  GLU C 188     4046   6617   6325    343   -146    993       C  
ATOM   1394  C   GLU C 188     -36.521  35.651 -59.261  1.00 38.98           C  
ANISOU 1394  C   GLU C 188     3411   5812   5590    318   -179    984       C  
ATOM   1395  O   GLU C 188     -35.485  36.086 -58.750  1.00 33.89           O  
ANISOU 1395  O   GLU C 188     2851   5083   4943    330   -159    968       O  
ATOM   1396  CB  GLU C 188     -37.450  34.872 -57.092  1.00 47.78           C  
ANISOU 1396  CB  GLU C 188     4453   6987   6715    300    -96    978       C  
ATOM   1397  CG  GLU C 188     -38.617  34.248 -56.359  1.00 64.35           C  
ANISOU 1397  CG  GLU C 188     6451   9178   8820    283    -64    995       C  
ATOM   1398  CD  GLU C 188     -38.192  33.692 -55.015  1.00 73.63           C  
ANISOU 1398  CD  GLU C 188     7653  10334   9988    250    -13    989       C  
ATOM   1399  OE1 GLU C 188     -38.083  32.451 -54.875  1.00 73.57           O  
ANISOU 1399  OE1 GLU C 188     7629  10330   9993    156    -15    998       O  
ATOM   1400  OE2 GLU C 188     -37.952  34.494 -54.076  1.00 77.13           O  
ANISOU 1400  OE2 GLU C 188     8134  10758  10413    322     28    975       O  
ATOM   1401  N   ASP C 189     -36.578  35.253 -60.530  1.00 41.32           N  
ANISOU 1401  N   ASP C 189     3685   6137   5877    284   -231    991       N  
ATOM   1402  CA  ASP C 189     -35.434  35.335 -61.425  1.00 40.59           C  
ANISOU 1402  CA  ASP C 189     3667   5989   5767    263   -262    986       C  
ATOM   1403  C   ASP C 189     -35.454  36.585 -62.296  1.00 41.99           C  
ANISOU 1403  C   ASP C 189     3861   6162   5933    341   -285   1021       C  
ATOM   1404  O   ASP C 189     -34.598  36.728 -63.172  1.00 35.47           O  
ANISOU 1404  O   ASP C 189     3084   5305   5086    329   -311   1029       O  
ATOM   1405  CB  ASP C 189     -35.363  34.083 -62.298  1.00 49.94           C  
ANISOU 1405  CB  ASP C 189     4823   7212   6942    180   -307    967       C  
ATOM   1406  CG  ASP C 189     -34.836  32.879 -61.543  1.00 66.86           C  
ANISOU 1406  CG  ASP C 189     6985   9318   9099     96   -291    934       C  
ATOM   1407  OD1 ASP C 189     -35.235  31.747 -61.884  1.00 74.70           O  
ANISOU 1407  OD1 ASP C 189     7928  10352  10104     29   -321    917       O  
ATOM   1408  OD2 ASP C 189     -34.021  33.063 -60.613  1.00 69.02           O  
ANISOU 1408  OD2 ASP C 189     7327   9523   9377     98   -252    924       O  
ATOM   1409  N   CYS C 190     -36.406  37.489 -62.073  1.00 39.99           N  
ANISOU 1409  N   CYS C 190     3563   5939   5691    423   -275   1044       N  
ATOM   1410  CA  CYS C 190     -36.420  38.761 -62.782  1.00 40.11           C  
ANISOU 1410  CA  CYS C 190     3600   5935   5704    504   -295   1084       C  
ATOM   1411  C   CYS C 190     -35.150  39.543 -62.475  1.00 43.62           C  
ANISOU 1411  C   CYS C 190     4149   6266   6161    520   -278   1085       C  
ATOM   1412  O   CYS C 190     -34.623  39.495 -61.359  1.00 46.05           O  
ANISOU 1412  O   CYS C 190     4498   6514   6484    509   -240   1052       O  
ATOM   1413  CB  CYS C 190     -37.637  39.590 -62.370  1.00 47.48           C  
ANISOU 1413  CB  CYS C 190     4473   6912   6657    596   -284   1100       C  
ATOM   1414  SG  CYS C 190     -39.241  38.776 -62.574  1.00 61.52           S  
ANISOU 1414  SG  CYS C 190     6115   8831   8430    583   -300   1100       S  
ATOM   1415  N   GLN C 191     -34.658  40.275 -63.468  1.00 39.10           N  
ANISOU 1415  N   GLN C 191     3612   5663   5579    546   -306   1126       N  
ATOM   1416  CA  GLN C 191     -33.493  41.117 -63.236  1.00 40.94           C  
ANISOU 1416  CA  GLN C 191     3937   5786   5833    561   -292   1136       C  
ATOM   1417  C   GLN C 191     -33.912  42.418 -62.566  1.00 43.48           C  
ANISOU 1417  C   GLN C 191     4270   6053   6198    657   -278   1147       C  
ATOM   1418  O   GLN C 191     -34.784  43.134 -63.060  1.00 46.63           O  
ANISOU 1418  O   GLN C 191     4628   6485   6604    728   -299   1186       O  
ATOM   1419  CB  GLN C 191     -32.740  41.436 -64.527  1.00 39.15           C  
ANISOU 1419  CB  GLN C 191     3745   5546   5583    549   -325   1185       C  
ATOM   1420  CG  GLN C 191     -31.847  42.656 -64.329  1.00 40.67           C  
ANISOU 1420  CG  GLN C 191     4015   5623   5814    586   -314   1213       C  
ATOM   1421  CD  GLN C 191     -30.942  43.003 -65.506  1.00 46.15           C  
ANISOU 1421  CD  GLN C 191     4749   6300   6488    566   -337   1271       C  
ATOM   1422  OE1 GLN C 191     -29.976  43.755 -65.354  1.00 51.60           O  
ANISOU 1422  OE1 GLN C 191     5503   6892   7210    568   -327   1291       O  
ATOM   1423  NE2 GLN C 191     -31.246  42.449 -66.680  1.00 48.40           N  
ANISOU 1423  NE2 GLN C 191     4990   6682   6717    547   -368   1297       N  
ATOM   1424  N   SER C 192     -33.273  42.733 -61.448  1.00 46.97           N  
ANISOU 1424  N   SER C 192     4767   6411   6670    663   -246   1108       N  
ATOM   1425  CA  SER C 192     -33.458  44.011 -60.777  1.00 48.10           C  
ANISOU 1425  CA  SER C 192     4934   6483   6859    754   -236   1106       C  
ATOM   1426  C   SER C 192     -32.463  45.015 -61.351  1.00 51.07           C  
ANISOU 1426  C   SER C 192     5384   6754   7267    767   -257   1147       C  
ATOM   1427  O   SER C 192     -31.249  44.779 -61.338  1.00 49.94           O  
ANISOU 1427  O   SER C 192     5301   6552   7124    705   -251   1137       O  
ATOM   1428  CB  SER C 192     -33.261  43.851 -59.274  1.00 44.87           C  
ANISOU 1428  CB  SER C 192     4545   6042   6462    758   -195   1038       C  
ATOM   1429  OG  SER C 192     -32.267  42.897 -59.002  1.00 59.34           O  
ANISOU 1429  OG  SER C 192     6416   7857   8273    667   -180   1009       O  
ATOM   1430  N   LEU C 193     -32.976  46.128 -61.862  1.00 53.32           N  
ANISOU 1430  N   LEU C 193     5661   7015   7581    847   -282   1197       N  
ATOM   1431  CA  LEU C 193     -32.133  47.183 -62.412  1.00 43.76           C  
ANISOU 1431  CA  LEU C 193     4516   5699   6412    864   -303   1250       C  
ATOM   1432  C   LEU C 193     -31.755  48.162 -61.313  1.00 46.61           C  
ANISOU 1432  C   LEU C 193     4930   5937   6841    916   -291   1208       C  
ATOM   1433  O   LEU C 193     -32.621  48.650 -60.585  1.00 51.21           O  
ANISOU 1433  O   LEU C 193     5486   6522   7448    999   -286   1174       O  
ATOM   1434  CB  LEU C 193     -32.835  47.917 -63.557  1.00 41.60           C  
ANISOU 1434  CB  LEU C 193     4212   5453   6141    925   -340   1334       C  
ATOM   1435  CG  LEU C 193     -33.530  47.023 -64.605  1.00 39.80           C  
ANISOU 1435  CG  LEU C 193     3913   5366   5843    896   -359   1365       C  
ATOM   1436  CD1 LEU C 193     -34.169  47.842 -65.728  1.00 31.21           C  
ANISOU 1436  CD1 LEU C 193     2800   4305   4755    965   -399   1453       C  
ATOM   1437  CD2 LEU C 193     -32.536  46.035 -65.181  1.00 35.40           C  
ANISOU 1437  CD2 LEU C 193     3378   4836   5236    792   -356   1365       C  
ATOM   1438  N   THR C 194     -30.463  48.444 -61.190  1.00 43.73           N  
ANISOU 1438  N   THR C 194     4638   5470   6507    872   -289   1205       N  
ATOM   1439  CA  THR C 194     -29.994  49.311 -60.129  1.00 44.21           C  
ANISOU 1439  CA  THR C 194     4751   5411   6635    913   -284   1154       C  
ATOM   1440  C   THR C 194     -29.347  50.593 -60.622  1.00 43.82           C  
ANISOU 1440  C   THR C 194     4757   5232   6661    938   -314   1212       C  
ATOM   1441  O   THR C 194     -28.935  51.407 -59.792  1.00 44.39           O  
ANISOU 1441  O   THR C 194     4875   5191   6801    975   -319   1167       O  
ATOM   1442  CB  THR C 194     -29.004  48.556 -59.225  1.00 49.81           C  
ANISOU 1442  CB  THR C 194     5498   6100   7328    842   -255   1081       C  
ATOM   1443  OG1 THR C 194     -28.118  47.764 -60.022  1.00 50.62           O  
ANISOU 1443  OG1 THR C 194     5615   6228   7391    744   -254   1115       O  
ATOM   1444  CG2 THR C 194     -29.770  47.649 -58.267  1.00 45.25           C  
ANISOU 1444  CG2 THR C 194     4873   5617   6702    849   -223   1012       C  
ATOM   1445  N   ARG C 195     -29.283  50.822 -61.913  1.00 47.66           N  
ANISOU 1445  N   ARG C 195     5237   5731   7139    923   -337   1310       N  
ATOM   1446  CA  ARG C 195     -28.496  51.978 -62.325  1.00 53.36           C  
ANISOU 1446  CA  ARG C 195     6015   6322   7937    930   -361   1374       C  
ATOM   1447  C   ARG C 195     -29.130  52.772 -63.456  1.00 59.05           C  
ANISOU 1447  C   ARG C 195     6716   7047   8675    986   -395   1483       C  
ATOM   1448  O   ARG C 195     -29.122  54.004 -63.405  1.00 62.37           O  
ANISOU 1448  O   ARG C 195     7168   7348   9181   1047   -422   1517       O  
ATOM   1449  CB  ARG C 195     -27.088  51.524 -62.728  1.00 52.68           C  
ANISOU 1449  CB  ARG C 195     5967   6213   7834    823   -350   1396       C  
ATOM   1450  CG  ARG C 195     -26.171  52.672 -63.059  1.00 60.88           C  
ANISOU 1450  CG  ARG C 195     7060   7112   8958    816   -371   1461       C  
ATOM   1451  CD  ARG C 195     -24.776  52.213 -63.351  1.00 53.37           C  
ANISOU 1451  CD  ARG C 195     6140   6147   7991    712   -355   1475       C  
ATOM   1452  NE  ARG C 195     -24.334  52.887 -64.570  1.00 59.45           N  
ANISOU 1452  NE  ARG C 195     6920   6888   8782    694   -373   1604       N  
ATOM   1453  CZ  ARG C 195     -24.723  52.527 -65.788  1.00 60.53           C  
ANISOU 1453  CZ  ARG C 195     7018   7137   8845    687   -377   1688       C  
ATOM   1454  NH1 ARG C 195     -25.521  51.481 -65.936  1.00 64.30           N  
ANISOU 1454  NH1 ARG C 195     7445   7753   9232    692   -368   1650       N  
ATOM   1455  NH2 ARG C 195     -24.285  53.201 -66.845  1.00 59.87           N  
ANISOU 1455  NH2 ARG C 195     6943   7026   8777    674   -391   1811       N  
ATOM   1456  N   THR C 196     -29.680  52.105 -64.472  1.00 61.02           N  
ANISOU 1456  N   THR C 196     6914   7427   8845    971   -399   1538       N  
ATOM   1457  CA  THR C 196     -30.383  52.800 -65.544  1.00 62.41           C  
ANISOU 1457  CA  THR C 196     7064   7626   9024   1032   -433   1641       C  
ATOM   1458  C   THR C 196     -31.746  53.331 -65.112  1.00 68.73           C  
ANISOU 1458  C   THR C 196     7824   8439   9852   1145   -449   1616       C  
ATOM   1459  O   THR C 196     -32.401  54.031 -65.893  1.00 69.46           O  
ANISOU 1459  O   THR C 196     7896   8538   9957   1213   -482   1699       O  
ATOM   1460  CB  THR C 196     -30.561  51.872 -66.747  1.00 61.17           C  
ANISOU 1460  CB  THR C 196     6860   7618   8765    984   -436   1695       C  
ATOM   1461  OG1 THR C 196     -31.314  50.719 -66.354  1.00 65.97           O  
ANISOU 1461  OG1 THR C 196     7410   8347   9308    972   -420   1614       O  
ATOM   1462  CG2 THR C 196     -29.212  51.420 -67.282  1.00 57.84           C  
ANISOU 1462  CG2 THR C 196     6474   7190   8312    883   -421   1726       C  
ATOM   1463  N   VAL C 197     -32.178  53.023 -63.888  1.00 74.16           N  
ANISOU 1463  N   VAL C 197     8497   9135  10546   1171   -427   1507       N  
ATOM   1464  CA  VAL C 197     -33.501  53.388 -63.388  1.00 72.95           C  
ANISOU 1464  CA  VAL C 197     8293   9017  10407   1278   -436   1471       C  
ATOM   1465  C   VAL C 197     -33.469  54.662 -62.539  1.00 71.42           C  
ANISOU 1465  C   VAL C 197     8145   8676  10316   1366   -451   1435       C  
ATOM   1466  O   VAL C 197     -34.528  55.270 -62.302  1.00 73.46           O  
ANISOU 1466  O   VAL C 197     8368   8942  10601   1475   -469   1422       O  
ATOM   1467  CB  VAL C 197     -34.086  52.179 -62.612  1.00 69.52           C  
ANISOU 1467  CB  VAL C 197     7801   8706   9905   1253   -398   1379       C  
ATOM   1468  CG1 VAL C 197     -35.125  52.559 -61.569  1.00 71.36           C  
ANISOU 1468  CG1 VAL C 197     7997   8953  10164   1355   -391   1306       C  
ATOM   1469  CG2 VAL C 197     -34.658  51.159 -63.584  1.00 64.94           C  
ANISOU 1469  CG2 VAL C 197     7155   8280   9241   1209   -402   1419       C  
ATOM   1470  N   CYS C 198     -32.286  55.132 -62.158  1.00 70.08           N  
ANISOU 1470  N   CYS C 198     8049   8370  10208   1326   -452   1422       N  
ATOM   1471  CA  CYS C 198     -32.109  56.037 -61.032  1.00 69.52           C  
ANISOU 1471  CA  CYS C 198     8021   8166  10226   1391   -461   1344       C  
ATOM   1472  C   CYS C 198     -32.446  57.486 -61.368  1.00 74.78           C  
ANISOU 1472  C   CYS C 198     8710   8710  10991   1490   -510   1402       C  
ATOM   1473  O   CYS C 198     -32.229  57.956 -62.488  1.00 73.93           O  
ANISOU 1473  O   CYS C 198     8626   8574  10891   1465   -534   1505       O  
ATOM   1474  CB  CYS C 198     -30.671  55.947 -60.528  1.00 67.44           C  
ANISOU 1474  CB  CYS C 198     7826   7804   9993   1304   -447   1306       C  
ATOM   1475  SG  CYS C 198     -30.267  54.273 -60.036  1.00 74.79           S  
ANISOU 1475  SG  CYS C 198     8734   8865  10815   1199   -394   1235       S  
ATOM   1476  N   ALA C 199     -32.962  58.194 -60.361  1.00 78.71           N  
ANISOU 1476  N   ALA C 199     9213   9145  11549   1592   -523   1315       N  
ATOM   1477  CA  ALA C 199     -33.285  59.608 -60.502  1.00 81.15           C  
ANISOU 1477  CA  ALA C 199     9568   9338  11927   1672   -568   1318       C  
ATOM   1478  C   ALA C 199     -32.025  60.454 -60.400  1.00 86.30           C  
ANISOU 1478  C   ALA C 199    10311   9810  12667   1621   -589   1321       C  
ATOM   1479  O   ALA C 199     -31.101  60.138 -59.644  1.00 89.69           O  
ANISOU 1479  O   ALA C 199    10768  10188  13123   1569   -573   1262       O  
ATOM   1480  CB  ALA C 199     -34.288  60.039 -59.436  1.00 79.89           C  
ANISOU 1480  CB  ALA C 199     9381   9187  11787   1801   -574   1207       C  
ATOM   1481  N   GLY C 200     -32.000  61.552 -61.153  1.00 87.51           N  
ANISOU 1481  N   GLY C 200    10512   9871  12868   1637   -627   1390       N  
ATOM   1482  CA  GLY C 200     -30.780  62.325 -61.229  1.00 91.14           C  
ANISOU 1482  CA  GLY C 200    11051  10172  13407   1572   -644   1413       C  
ATOM   1483  C   GLY C 200     -29.671  61.513 -61.876  1.00 93.87           C  
ANISOU 1483  C   GLY C 200    11399  10551  13717   1436   -616   1489       C  
ATOM   1484  O   GLY C 200     -29.894  60.719 -62.794  1.00 98.00           O  
ANISOU 1484  O   GLY C 200    11877  11203  14157   1395   -597   1572       O  
ATOM   1485  N   GLY C 201     -28.456  61.703 -61.372  1.00 90.64           N  
ANISOU 1485  N   GLY C 201    11040  10030  13367   1367   -614   1454       N  
ATOM   1486  CA  GLY C 201     -27.310  61.017 -61.933  1.00 91.90           C  
ANISOU 1486  CA  GLY C 201    11206  10213  13500   1240   -588   1520       C  
ATOM   1487  C   GLY C 201     -26.654  60.039 -60.982  1.00 85.97           C  
ANISOU 1487  C   GLY C 201    10446   9485  12735   1193   -559   1432       C  
ATOM   1488  O   GLY C 201     -25.446  59.802 -61.068  1.00 89.13           O  
ANISOU 1488  O   GLY C 201    10872   9843  13149   1095   -547   1450       O  
ATOM   1489  N   CYS C 202     -27.441  59.462 -60.075  1.00 78.55           N  
ANISOU 1489  N   CYS C 202     9465   8616  11764   1264   -546   1338       N  
ATOM   1490  CA  CYS C 202     -26.897  58.546 -59.082  1.00 77.36           C  
ANISOU 1490  CA  CYS C 202     9313   8504  11577   1219   -513   1234       C  
ATOM   1491  C   CYS C 202     -26.298  57.317 -59.754  1.00 71.04           C  
ANISOU 1491  C   CYS C 202     8495   7824  10674   1101   -474   1283       C  
ATOM   1492  O   CYS C 202     -26.762  56.865 -60.803  1.00 72.75           O  
ANISOU 1492  O   CYS C 202     8672   8145  10823   1085   -465   1373       O  
ATOM   1493  CB  CYS C 202     -27.984  58.112 -58.101  1.00 84.81           C  
ANISOU 1493  CB  CYS C 202    10214   9546  12462   1303   -493   1122       C  
ATOM   1494  SG  CYS C 202     -28.791  59.453 -57.210  1.00101.44           S  
ANISOU 1494  SG  CYS C 202    12333  11538  14672   1460   -537   1041       S  
ATOM   1495  N   ALA C 203     -25.249  56.774 -59.132  1.00 56.40           N  
ANISOU 1495  N   ALA C 203     6668   5954   8807   1023   -452   1216       N  
ATOM   1496  CA  ALA C 203     -24.657  55.541 -59.637  1.00 55.58           C  
ANISOU 1496  CA  ALA C 203     6548   5964   8607    917   -416   1242       C  
ATOM   1497  C   ALA C 203     -25.569  54.342 -59.403  1.00 53.79           C  
ANISOU 1497  C   ALA C 203     6267   5904   8267    928   -382   1194       C  
ATOM   1498  O   ALA C 203     -25.634  53.447 -60.251  1.00 52.52           O  
ANISOU 1498  O   ALA C 203     6073   5857   8024    873   -365   1249       O  
ATOM   1499  CB  ALA C 203     -23.290  55.307 -58.992  1.00 42.73           C  
ANISOU 1499  CB  ALA C 203     4963   4272   7002    837   -406   1180       C  
ATOM   1500  N   ARG C 204     -26.269  54.298 -58.267  1.00 49.70           N  
ANISOU 1500  N   ARG C 204     5736   5405   7744    999   -374   1092       N  
ATOM   1501  CA  ARG C 204     -27.124  53.167 -57.926  1.00 48.05           C  
ANISOU 1501  CA  ARG C 204     5472   5350   7436   1005   -340   1047       C  
ATOM   1502  C   ARG C 204     -28.318  53.650 -57.110  1.00 50.00           C  
ANISOU 1502  C   ARG C 204     5689   5612   7697   1123   -343    984       C  
ATOM   1503  O   ARG C 204     -28.229  54.629 -56.366  1.00 55.54           O  
ANISOU 1503  O   ARG C 204     6424   6203   8474   1191   -365    927       O  
ATOM   1504  CB  ARG C 204     -26.370  52.068 -57.147  1.00 42.09           C  
ANISOU 1504  CB  ARG C 204     4729   4639   6624    929   -305    971       C  
ATOM   1505  CG  ARG C 204     -25.173  51.448 -57.879  1.00 39.25           C  
ANISOU 1505  CG  ARG C 204     4392   4280   6240    814   -299   1019       C  
ATOM   1506  CD  ARG C 204     -25.595  50.225 -58.738  1.00 41.88           C  
ANISOU 1506  CD  ARG C 204     4676   4761   6478    761   -279   1066       C  
ATOM   1507  NE  ARG C 204     -24.489  49.781 -59.605  1.00 42.37           N  
ANISOU 1507  NE  ARG C 204     4757   4824   6519    666   -278   1119       N  
ATOM   1508  CZ  ARG C 204     -24.645  49.086 -60.740  1.00 37.92           C  
ANISOU 1508  CZ  ARG C 204     4160   4358   5892    623   -277   1184       C  
ATOM   1509  NH1 ARG C 204     -25.859  48.753 -61.170  1.00 45.63           N  
ANISOU 1509  NH1 ARG C 204     5081   5435   6824    661   -279   1207       N  
ATOM   1510  NH2 ARG C 204     -23.572  48.728 -61.440  1.00 32.74           N  
ANISOU 1510  NH2 ARG C 204     3521   3703   5215    543   -274   1222       N  
ATOM   1511  N   CYS C 205     -29.438  52.943 -57.251  1.00 53.36           N  
ANISOU 1511  N   CYS C 205     6048   6178   8050   1147   -323    991       N  
ATOM   1512  CA  CYS C 205     -30.656  53.282 -56.527  1.00 62.65           C  
ANISOU 1512  CA  CYS C 205     7182   7397   9227   1258   -320    935       C  
ATOM   1513  C   CYS C 205     -31.468  52.023 -56.242  1.00 67.18           C  
ANISOU 1513  C   CYS C 205     7684   8138   9702   1238   -279    911       C  
ATOM   1514  O   CYS C 205     -31.243  50.960 -56.829  1.00 72.08           O  
ANISOU 1514  O   CYS C 205     8287   8838  10263   1146   -262    949       O  
ATOM   1515  CB  CYS C 205     -31.510  54.285 -57.307  1.00 62.55           C  
ANISOU 1515  CB  CYS C 205     7147   7355   9262   1346   -358   1004       C  
ATOM   1516  SG  CYS C 205     -31.893  53.712 -58.966  1.00 64.43           S  
ANISOU 1516  SG  CYS C 205     7340   7695   9444   1291   -366   1134       S  
ATOM   1517  N   LYS C 206     -32.420  52.167 -55.319  1.00 63.34           N  
ANISOU 1517  N   LYS C 206     7157   7705   9205   1328   -264    844       N  
ATOM   1518  CA  LYS C 206     -33.384  51.134 -54.960  1.00 56.51           C  
ANISOU 1518  CA  LYS C 206     6214   6999   8259   1325   -225    825       C  
ATOM   1519  C   LYS C 206     -34.750  51.382 -55.593  1.00 66.92           C  
ANISOU 1519  C   LYS C 206     7456   8399   9570   1398   -238    872       C  
ATOM   1520  O   LYS C 206     -35.714  50.675 -55.278  1.00 64.21           O  
ANISOU 1520  O   LYS C 206     7037   8190   9171   1410   -208    856       O  
ATOM   1521  CB  LYS C 206     -33.521  51.069 -53.439  1.00 47.89           C  
ANISOU 1521  CB  LYS C 206     5117   5931   7147   1376   -192    720       C  
ATOM   1522  CG  LYS C 206     -34.339  52.231 -52.912  1.00 68.47           C  
ANISOU 1522  CG  LYS C 206     7707   8509   9798   1519   -209    673       C  
ATOM   1523  CD  LYS C 206     -34.061  52.599 -51.470  1.00 81.38           C  
ANISOU 1523  CD  LYS C 206     9371  10111  11439   1581   -195    560       C  
ATOM   1524  CE  LYS C 206     -34.373  51.468 -50.522  1.00 89.88           C  
ANISOU 1524  CE  LYS C 206    10400  11328  12423   1554   -137    516       C  
ATOM   1525  NZ  LYS C 206     -34.186  51.915 -49.117  1.00 95.91           N  
ANISOU 1525  NZ  LYS C 206    11186  12072  13183   1632   -126    405       N  
ATOM   1526  N   GLY C 207     -34.851  52.375 -56.472  1.00 69.67           N  
ANISOU 1526  N   GLY C 207     7822   8672   9977   1446   -282    933       N  
ATOM   1527  CA  GLY C 207     -36.111  52.788 -57.036  1.00 72.59           C  
ANISOU 1527  CA  GLY C 207     8126   9105  10349   1531   -302    975       C  
ATOM   1528  C   GLY C 207     -35.951  54.060 -57.842  1.00 78.17           C  
ANISOU 1528  C   GLY C 207     8876   9689  11136   1588   -355   1039       C  
ATOM   1529  O   GLY C 207     -34.851  54.607 -57.968  1.00 85.10           O  
ANISOU 1529  O   GLY C 207     9833  10431  12070   1554   -374   1054       O  
ATOM   1530  N   PRO C 208     -37.056  54.570 -58.392  1.00 77.53           N  
ANISOU 1530  N   PRO C 208     8742   9652  11065   1677   -380   1082       N  
ATOM   1531  CA  PRO C 208     -36.970  55.683 -59.343  1.00 74.26           C  
ANISOU 1531  CA  PRO C 208     8362   9132  10721   1725   -433   1167       C  
ATOM   1532  C   PRO C 208     -36.943  57.072 -58.720  1.00 69.09           C  
ANISOU 1532  C   PRO C 208     7755   8329  10168   1837   -466   1124       C  
ATOM   1533  O   PRO C 208     -36.626  58.037 -59.427  1.00 61.69           O  
ANISOU 1533  O   PRO C 208     6868   7273   9298   1858   -510   1191       O  
ATOM   1534  CB  PRO C 208     -38.240  55.497 -60.174  1.00 78.94           C  
ANISOU 1534  CB  PRO C 208     8868   9855  11271   1773   -447   1226       C  
ATOM   1535  CG  PRO C 208     -39.227  54.979 -59.179  1.00 80.55           C  
ANISOU 1535  CG  PRO C 208     8996  10180  11430   1822   -411   1138       C  
ATOM   1536  CD  PRO C 208     -38.444  54.111 -58.212  1.00 79.25           C  
ANISOU 1536  CD  PRO C 208     8858  10024  11229   1734   -362   1062       C  
ATOM   1537  N   LEU C 209     -37.245  57.209 -57.440  1.00 73.17           N  
ANISOU 1537  N   LEU C 209     8261   8849  10690   1905   -446   1010       N  
ATOM   1538  CA  LEU C 209     -37.153  58.493 -56.758  1.00 81.70           C  
ANISOU 1538  CA  LEU C 209     9390   9783  11869   2013   -481    949       C  
ATOM   1539  C   LEU C 209     -35.724  58.773 -56.297  1.00 87.67           C  
ANISOU 1539  C   LEU C 209    10239  10389  12682   1947   -487    912       C  
ATOM   1540  O   LEU C 209     -34.935  57.848 -56.086  1.00 91.53           O  
ANISOU 1540  O   LEU C 209    10745  10915  13118   1835   -451    897       O  
ATOM   1541  CB  LEU C 209     -38.102  58.502 -55.560  1.00 83.96           C  
ANISOU 1541  CB  LEU C 209     9619  10154  12126   2121   -456    834       C  
ATOM   1542  CG  LEU C 209     -39.544  58.004 -55.802  1.00 82.73           C  
ANISOU 1542  CG  LEU C 209     9354  10180  11900   2175   -437    853       C  
ATOM   1543  CD1 LEU C 209     -40.441  58.234 -54.590  1.00 75.30           C  
ANISOU 1543  CD1 LEU C 209     8361   9308  10941   2295   -416    736       C  
ATOM   1544  CD2 LEU C 209     -40.173  58.606 -57.054  1.00 84.75           C  
ANISOU 1544  CD2 LEU C 209     9605  10425  12170   2199   -488    936       C  
ATOM   1545  N   PRO C 210     -35.361  60.052 -56.139  1.00 89.63           N  
ANISOU 1545  N   PRO C 210    10553  10465  13036   2010   -536    892       N  
ATOM   1546  CA  PRO C 210     -34.034  60.385 -55.597  1.00 93.35           C  
ANISOU 1546  CA  PRO C 210    11106  10788  13573   1955   -547    845       C  
ATOM   1547  C   PRO C 210     -33.836  60.038 -54.130  1.00 91.86           C  
ANISOU 1547  C   PRO C 210    10918  10627  13358   1977   -517    700       C  
ATOM   1548  O   PRO C 210     -32.677  60.038 -53.668  1.00 92.28           O  
ANISOU 1548  O   PRO C 210    11033  10589  13442   1910   -519    657       O  
ATOM   1549  CB  PRO C 210     -33.926  61.911 -55.804  1.00 94.79           C  
ANISOU 1549  CB  PRO C 210    11367  10809  13839   2011   -604    841       C  
ATOM   1550  CG  PRO C 210     -35.032  62.266 -56.698  1.00 93.16           C  
ANISOU 1550  CG  PRO C 210    11126  10662  13609   2074   -623    915       C  
ATOM   1551  CD  PRO C 210     -36.112  61.260 -56.476  1.00 89.85           C  
ANISOU 1551  CD  PRO C 210    10601  10435  13103   2113   -584    896       C  
ATOM   1552  N   THR C 211     -34.910  59.810 -53.359  1.00 89.74           N  
ANISOU 1552  N   THR C 211    10585  10481  13030   2071   -491    621       N  
ATOM   1553  CA  THR C 211     -34.706  59.253 -52.026  1.00 84.58           C  
ANISOU 1553  CA  THR C 211     9928   9892  12317   2072   -450    497       C  
ATOM   1554  C   THR C 211     -34.325  57.787 -52.101  1.00 78.49           C  
ANISOU 1554  C   THR C 211     9135   9250  11440   1938   -393    528       C  
ATOM   1555  O   THR C 211     -33.818  57.233 -51.121  1.00 74.82           O  
ANISOU 1555  O   THR C 211     8682   8818  10928   1906   -360    446       O  
ATOM   1556  CB  THR C 211     -35.958  59.411 -51.162  1.00 81.70           C  
ANISOU 1556  CB  THR C 211     9494   9635  11912   2211   -434    408       C  
ATOM   1557  OG1 THR C 211     -37.105  58.909 -51.849  1.00 78.12           O  
ANISOU 1557  OG1 THR C 211     8956   9328  11399   2225   -412    484       O  
ATOM   1558  CG2 THR C 211     -36.187  60.873 -50.756  1.00 83.16           C  
ANISOU 1558  CG2 THR C 211     9710   9680  12206   2357   -493    336       C  
ATOM   1559  N   ASP C 212     -34.566  57.153 -53.248  1.00 76.71           N  
ANISOU 1559  N   ASP C 212     8875   9097  11175   1864   -383    642       N  
ATOM   1560  CA  ASP C 212     -34.147  55.781 -53.481  1.00 81.32           C  
ANISOU 1560  CA  ASP C 212     9443   9785  11671   1733   -338    677       C  
ATOM   1561  C   ASP C 212     -32.662  55.662 -53.802  1.00 78.16           C  
ANISOU 1561  C   ASP C 212     9119   9276  11301   1618   -348    705       C  
ATOM   1562  O   ASP C 212     -32.157  54.540 -53.901  1.00 71.88           O  
ANISOU 1562  O   ASP C 212     8321   8553  10439   1510   -315    721       O  
ATOM   1563  CB  ASP C 212     -34.962  55.173 -54.627  1.00 87.56           C  
ANISOU 1563  CB  ASP C 212    10166  10693  12410   1702   -332    780       C  
ATOM   1564  CG  ASP C 212     -36.420  54.962 -54.264  1.00 94.40           C  
ANISOU 1564  CG  ASP C 212    10940  11703  13227   1791   -309    752       C  
ATOM   1565  OD1 ASP C 212     -37.286  55.161 -55.142  1.00 96.64           O  
ANISOU 1565  OD1 ASP C 212    11173  12033  13511   1830   -330    821       O  
ATOM   1566  OD2 ASP C 212     -36.700  54.584 -53.106  1.00 95.33           O  
ANISOU 1566  OD2 ASP C 212    11029  11893  13299   1821   -271    664       O  
ATOM   1567  N   CYS C 213     -31.957  56.781 -53.962  1.00 76.50           N  
ANISOU 1567  N   CYS C 213     8977   8896  11195   1638   -395    711       N  
ATOM   1568  CA  CYS C 213     -30.570  56.745 -54.404  1.00 73.10           C  
ANISOU 1568  CA  CYS C 213     8611   8364  10801   1527   -407    752       C  
ATOM   1569  C   CYS C 213     -29.653  56.196 -53.316  1.00 69.34           C  
ANISOU 1569  C   CYS C 213     8168   7882  10297   1474   -382    654       C  
ATOM   1570  O   CYS C 213     -29.908  56.341 -52.117  1.00 71.65           O  
ANISOU 1570  O   CYS C 213     8457   8187  10581   1546   -373    543       O  
ATOM   1571  CB  CYS C 213     -30.100  58.140 -54.814  1.00 76.18           C  
ANISOU 1571  CB  CYS C 213     9058   8567  11320   1563   -466    788       C  
ATOM   1572  SG  CYS C 213     -30.494  58.595 -56.515  1.00 80.97           S  
ANISOU 1572  SG  CYS C 213     9649   9157  11957   1557   -496    956       S  
ATOM   1573  N   CYS C 214     -28.562  55.575 -53.753  1.00 59.42           N  
ANISOU 1573  N   CYS C 214     6942   6612   9023   1352   -371    696       N  
ATOM   1574  CA  CYS C 214     -27.601  54.950 -52.858  1.00 57.54           C  
ANISOU 1574  CA  CYS C 214     6735   6374   8754   1290   -348    617       C  
ATOM   1575  C   CYS C 214     -26.406  55.865 -52.629  1.00 52.24           C  
ANISOU 1575  C   CYS C 214     6134   5529   8185   1272   -388    586       C  
ATOM   1576  O   CYS C 214     -25.995  56.608 -53.527  1.00 52.45           O  
ANISOU 1576  O   CYS C 214     6189   5448   8292   1249   -423    667       O  
ATOM   1577  CB  CYS C 214     -27.125  53.608 -53.417  1.00 59.96           C  
ANISOU 1577  CB  CYS C 214     7027   6780   8977   1168   -312    671       C  
ATOM   1578  SG  CYS C 214     -28.459  52.443 -53.766  1.00 59.99           S  
ANISOU 1578  SG  CYS C 214     6944   6980   8871   1170   -271    710       S  
ATOM   1579  N   HIS C 215     -25.857  55.799 -51.414  1.00 48.46           N  
ANISOU 1579  N   HIS C 215     5683   5028   7702   1282   -384    471       N  
ATOM   1580  CA  HIS C 215     -24.665  56.550 -51.045  1.00 50.34           C  
ANISOU 1580  CA  HIS C 215     5983   5110   8033   1258   -423    423       C  
ATOM   1581  C   HIS C 215     -23.567  56.360 -52.085  1.00 54.48           C  
ANISOU 1581  C   HIS C 215     6534   5581   8586   1134   -428    523       C  
ATOM   1582  O   HIS C 215     -23.495  55.330 -52.762  1.00 53.08           O  
ANISOU 1582  O   HIS C 215     6331   5509   8328   1055   -392    592       O  
ATOM   1583  CB  HIS C 215     -24.183  56.087 -49.665  1.00 53.81           C  
ANISOU 1583  CB  HIS C 215     6438   5583   8425   1264   -406    293       C  
ATOM   1584  CG  HIS C 215     -23.142  56.967 -49.045  1.00 59.12           C  
ANISOU 1584  CG  HIS C 215     7168   6100   9196   1268   -454    211       C  
ATOM   1585  ND1 HIS C 215     -21.799  56.846 -49.327  1.00 56.48           N  
ANISOU 1585  ND1 HIS C 215     6871   5691   8898   1160   -465    234       N  
ATOM   1586  CD2 HIS C 215     -23.246  57.964 -48.134  1.00 55.62           C  
ANISOU 1586  CD2 HIS C 215     6748   5565   8821   1368   -495    100       C  
ATOM   1587  CE1 HIS C 215     -21.121  57.739 -48.628  1.00 57.33           C  
ANISOU 1587  CE1 HIS C 215     7021   5665   9099   1187   -513    144       C  
ATOM   1588  NE2 HIS C 215     -21.976  58.430 -47.896  1.00 54.16           N  
ANISOU 1588  NE2 HIS C 215     6613   5246   8717   1314   -534     58       N  
ATOM   1589  N   GLU C 216     -22.707  57.375 -52.215  1.00 54.13           N  
ANISOU 1589  N   GLU C 216     6537   5371   8658   1117   -474    528       N  
ATOM   1590  CA  GLU C 216     -21.639  57.324 -53.211  1.00 56.30           C  
ANISOU 1590  CA  GLU C 216     6832   5592   8969   1003   -479    628       C  
ATOM   1591  C   GLU C 216     -20.726  56.119 -53.009  1.00 46.86           C  
ANISOU 1591  C   GLU C 216     5636   4479   7688    901   -441    606       C  
ATOM   1592  O   GLU C 216     -20.192  55.577 -53.984  1.00 41.61           O  
ANISOU 1592  O   GLU C 216     4964   3852   6994    809   -424    700       O  
ATOM   1593  CB  GLU C 216     -20.822  58.618 -53.175  1.00 69.64           C  
ANISOU 1593  CB  GLU C 216     8570   7084  10807   1000   -535    624       C  
ATOM   1594  CG  GLU C 216     -21.022  59.519 -54.386  1.00 86.35           C  
ANISOU 1594  CG  GLU C 216    10689   9110  13009   1001   -565    760       C  
ATOM   1595  CD  GLU C 216     -20.295  60.847 -54.261  1.00100.87           C  
ANISOU 1595  CD  GLU C 216    12580  10777  14967    986   -613    740       C  
ATOM   1596  OE1 GLU C 216     -20.284  61.423 -53.152  1.00105.54           O  
ANISOU 1596  OE1 GLU C 216    13199  11303  15598   1046   -640    607       O  
ATOM   1597  OE2 GLU C 216     -19.733  61.314 -55.274  1.00105.24           O  
ANISOU 1597  OE2 GLU C 216    13147  11282  15557    909   -619    851       O  
ATOM   1598  N   GLN C 217     -20.544  55.680 -51.764  1.00 43.84           N  
ANISOU 1598  N   GLN C 217     5261   4131   7263    922   -430    483       N  
ATOM   1599  CA  GLN C 217     -19.626  54.589 -51.457  1.00 40.99           C  
ANISOU 1599  CA  GLN C 217     4906   3837   6831    834   -400    453       C  
ATOM   1600  C   GLN C 217     -20.234  53.205 -51.652  1.00 43.62           C  
ANISOU 1600  C   GLN C 217     5196   4343   7034    809   -348    482       C  
ATOM   1601  O   GLN C 217     -19.552  52.210 -51.384  1.00 48.68           O  
ANISOU 1601  O   GLN C 217     5839   5045   7611    741   -324    458       O  
ATOM   1602  CB  GLN C 217     -19.115  54.726 -50.020  1.00 40.10           C  
ANISOU 1602  CB  GLN C 217     4821   3687   6728    868   -414    311       C  
ATOM   1603  CG  GLN C 217     -18.252  55.950 -49.799  1.00 41.83           C  
ANISOU 1603  CG  GLN C 217     5083   3729   7080    870   -471    271       C  
ATOM   1604  CD  GLN C 217     -17.090  56.007 -50.768  1.00 45.44           C  
ANISOU 1604  CD  GLN C 217     5554   4118   7592    754   -480    363       C  
ATOM   1605  OE1 GLN C 217     -16.264  55.095 -50.818  1.00 50.11           O  
ANISOU 1605  OE1 GLN C 217     6143   4770   8124    670   -454    367       O  
ATOM   1606  NE2 GLN C 217     -17.027  57.073 -51.556  1.00 50.49           N  
ANISOU 1606  NE2 GLN C 217     6205   4634   8343    751   -515    441       N  
ATOM   1607  N   CYS C 218     -21.483  53.109 -52.103  1.00 41.49           N  
ANISOU 1607  N   CYS C 218     4886   4150   6729    860   -334    531       N  
ATOM   1608  CA  CYS C 218     -22.110  51.817 -52.342  1.00 40.64           C  
ANISOU 1608  CA  CYS C 218     4732   4199   6509    832   -290    560       C  
ATOM   1609  C   CYS C 218     -21.790  51.309 -53.741  1.00 42.03           C  
ANISOU 1609  C   CYS C 218     4896   4410   6664    744   -284    673       C  
ATOM   1610  O   CYS C 218     -21.680  52.088 -54.693  1.00 47.67           O  
ANISOU 1610  O   CYS C 218     5617   5055   7439    739   -308    754       O  
ATOM   1611  CB  CYS C 218     -23.631  51.891 -52.184  1.00 40.15           C  
ANISOU 1611  CB  CYS C 218     4623   4217   6415    925   -278    558       C  
ATOM   1612  SG  CYS C 218     -24.292  52.371 -50.570  1.00 51.72           S  
ANISOU 1612  SG  CYS C 218     6085   5687   7878   1047   -277    426       S  
ATOM   1613  N   ALA C 219     -21.653  49.994 -53.855  1.00 38.26           N  
ANISOU 1613  N   ALA C 219     4398   4042   6098    679   -252    679       N  
ATOM   1614  CA  ALA C 219     -21.724  49.298 -55.127  1.00 40.46           C  
ANISOU 1614  CA  ALA C 219     4648   4395   6331    616   -242    771       C  
ATOM   1615  C   ALA C 219     -22.938  48.376 -55.115  1.00 41.98           C  
ANISOU 1615  C   ALA C 219     4785   4722   6443    638   -216    774       C  
ATOM   1616  O   ALA C 219     -23.396  47.951 -54.050  1.00 33.03           O  
ANISOU 1616  O   ALA C 219     3639   3636   5274    672   -196    703       O  
ATOM   1617  CB  ALA C 219     -20.451  48.491 -55.400  1.00 39.82           C  
ANISOU 1617  CB  ALA C 219     4587   4323   6221    515   -232    776       C  
ATOM   1618  N   ALA C 220     -23.482  48.120 -56.310  1.00 45.14           N  
ANISOU 1618  N   ALA C 220     5149   5186   6816    621   -219    857       N  
ATOM   1619  CA  ALA C 220     -24.504  47.103 -56.564  1.00 47.19           C  
ANISOU 1619  CA  ALA C 220     5350   5577   7001    618   -200    871       C  
ATOM   1620  C   ALA C 220     -25.919  47.515 -56.158  1.00 47.96           C  
ANISOU 1620  C   ALA C 220     5405   5716   7102    712   -197    859       C  
ATOM   1621  O   ALA C 220     -26.888  47.079 -56.788  1.00 45.18           O  
ANISOU 1621  O   ALA C 220     4998   5458   6711    720   -195    901       O  
ATOM   1622  CB  ALA C 220     -24.133  45.783 -55.877  1.00 48.94           C  
ANISOU 1622  CB  ALA C 220     5570   5863   7163    560   -172    815       C  
ATOM   1623  N   GLY C 221     -26.064  48.329 -55.127  1.00 46.29           N  
ANISOU 1623  N   GLY C 221     5213   5442   6933    786   -199    798       N  
ATOM   1624  CA  GLY C 221     -27.381  48.743 -54.683  1.00 42.05           C  
ANISOU 1624  CA  GLY C 221     4632   4949   6396    883   -195    778       C  
ATOM   1625  C   GLY C 221     -27.390  48.992 -53.188  1.00 49.80           C  
ANISOU 1625  C   GLY C 221     5629   5911   7382    942   -180    678       C  
ATOM   1626  O   GLY C 221     -26.370  48.908 -52.513  1.00 50.08           O  
ANISOU 1626  O   GLY C 221     5711   5891   7424    909   -178    624       O  
ATOM   1627  N   CYS C 222     -28.582  49.301 -52.681  1.00 47.45           N  
ANISOU 1627  N   CYS C 222     5285   5668   7075   1034   -171    651       N  
ATOM   1628  CA  CYS C 222     -28.725  49.655 -51.277  1.00 47.16           C  
ANISOU 1628  CA  CYS C 222     5256   5625   7037   1110   -158    553       C  
ATOM   1629  C   CYS C 222     -30.131  49.343 -50.782  1.00 42.69           C  
ANISOU 1629  C   CYS C 222     4614   5190   6418   1180   -127    538       C  
ATOM   1630  O   CYS C 222     -31.088  49.271 -51.556  1.00 49.91           O  
ANISOU 1630  O   CYS C 222     5472   6167   7323   1196   -129    599       O  
ATOM   1631  CB  CYS C 222     -28.417  51.137 -51.039  1.00 55.56           C  
ANISOU 1631  CB  CYS C 222     6369   6549   8193   1190   -200    513       C  
ATOM   1632  SG  CYS C 222     -29.437  52.278 -51.998  1.00 59.08           S  
ANISOU 1632  SG  CYS C 222     6788   6956   8704   1278   -237    578       S  
ATOM   1633  N   THR C 223     -30.236  49.155 -49.467  1.00 36.48           N  
ANISOU 1633  N   THR C 223     3821   4448   5592   1223    -99    457       N  
ATOM   1634  CA  THR C 223     -31.513  49.093 -48.769  1.00 37.97           C  
ANISOU 1634  CA  THR C 223     3938   4753   5734   1309    -68    428       C  
ATOM   1635  C   THR C 223     -31.884  50.425 -48.135  1.00 53.76           C  
ANISOU 1635  C   THR C 223     5949   6696   7782   1444    -90    354       C  
ATOM   1636  O   THR C 223     -32.925  50.517 -47.477  1.00 57.96           O  
ANISOU 1636  O   THR C 223     6421   7324   8277   1533    -66    319       O  
ATOM   1637  CB  THR C 223     -31.485  48.008 -47.687  1.00 41.68           C  
ANISOU 1637  CB  THR C 223     4387   5330   6121   1278    -17    391       C  
ATOM   1638  OG1 THR C 223     -30.776  48.492 -46.538  1.00 49.71           O  
ANISOU 1638  OG1 THR C 223     5456   6293   7140   1326    -20    295       O  
ATOM   1639  CG2 THR C 223     -30.802  46.752 -48.213  1.00 44.45           C  
ANISOU 1639  CG2 THR C 223     4749   5700   6440   1141     -5    447       C  
ATOM   1640  N   GLY C 224     -31.069  51.459 -48.331  1.00 57.93           N  
ANISOU 1640  N   GLY C 224     6547   7069   8394   1462   -138    331       N  
ATOM   1641  CA  GLY C 224     -31.309  52.762 -47.757  1.00 59.39           C  
ANISOU 1641  CA  GLY C 224     6751   7175   8640   1588   -171    254       C  
ATOM   1642  C   GLY C 224     -30.269  53.761 -48.217  1.00 69.97           C  
ANISOU 1642  C   GLY C 224     8171   8328  10087   1573   -228    254       C  
ATOM   1643  O   GLY C 224     -29.319  53.418 -48.928  1.00 81.96           O  
ANISOU 1643  O   GLY C 224     9728   9790  11624   1464   -237    313       O  
ATOM   1644  N   PRO C 225     -30.422  55.021 -47.810  1.00 63.56           N  
ANISOU 1644  N   PRO C 225     7382   7417   9350   1684   -269    187       N  
ATOM   1645  CA  PRO C 225     -29.560  56.078 -48.353  1.00 58.20           C  
ANISOU 1645  CA  PRO C 225     6773   6549   8792   1672   -330    201       C  
ATOM   1646  C   PRO C 225     -28.238  56.228 -47.615  1.00 54.23           C  
ANISOU 1646  C   PRO C 225     6338   5948   8321   1631   -348    121       C  
ATOM   1647  O   PRO C 225     -27.321  56.887 -48.116  1.00 54.33           O  
ANISOU 1647  O   PRO C 225     6406   5809   8429   1586   -392    145       O  
ATOM   1648  CB  PRO C 225     -30.431  57.329 -48.204  1.00 60.16           C  
ANISOU 1648  CB  PRO C 225     7011   6737   9111   1817   -369    160       C  
ATOM   1649  CG  PRO C 225     -31.214  57.059 -46.955  1.00 63.62           C  
ANISOU 1649  CG  PRO C 225     7401   7305   9466   1913   -333     54       C  
ATOM   1650  CD  PRO C 225     -31.447  55.560 -46.899  1.00 66.15           C  
ANISOU 1650  CD  PRO C 225     7669   7802   9662   1828   -264     99       C  
ATOM   1651  N   LYS C 226     -28.124  55.629 -46.433  1.00 54.74           N  
ANISOU 1651  N   LYS C 226     6394   6099   8305   1645   -315     28       N  
ATOM   1652  CA  LYS C 226     -26.903  55.754 -45.652  1.00 58.46           C  
ANISOU 1652  CA  LYS C 226     6925   6489   8799   1615   -335    -59       C  
ATOM   1653  C   LYS C 226     -25.776  54.924 -46.259  1.00 61.54           C  
ANISOU 1653  C   LYS C 226     7344   6864   9177   1465   -323     12       C  
ATOM   1654  O   LYS C 226     -25.990  54.026 -47.078  1.00 56.08           O  
ANISOU 1654  O   LYS C 226     6621   6254   8432   1387   -290    113       O  
ATOM   1655  CB  LYS C 226     -27.127  55.306 -44.206  1.00 59.72           C  
ANISOU 1655  CB  LYS C 226     7064   6763   8863   1679   -302   -173       C  
ATOM   1656  CG  LYS C 226     -28.305  55.935 -43.501  1.00 58.10           C  
ANISOU 1656  CG  LYS C 226     6818   6615   8643   1832   -301   -250       C  
ATOM   1657  CD  LYS C 226     -28.186  55.756 -41.996  1.00 65.08           C  
ANISOU 1657  CD  LYS C 226     7701   7576   9450   1899   -283   -381       C  
ATOM   1658  CE  LYS C 226     -29.227  56.580 -41.264  1.00 68.28           C  
ANISOU 1658  CE  LYS C 226     8070   8020   9851   2065   -293   -477       C  
ATOM   1659  NZ  LYS C 226     -29.552  57.821 -42.027  1.00 74.24           N  
ANISOU 1659  NZ  LYS C 226     8843   8630  10736   2126   -353   -462       N  
ATOM   1660  N   HIS C 227     -24.556  55.230 -45.828  1.00 61.59           N  
ANISOU 1660  N   HIS C 227     7406   6763   9231   1428   -354    -48       N  
ATOM   1661  CA  HIS C 227     -23.399  54.409 -46.152  1.00 58.70           C  
ANISOU 1661  CA  HIS C 227     7065   6393   8844   1297   -342     -7       C  
ATOM   1662  C   HIS C 227     -23.318  53.154 -45.296  1.00 57.44           C  
ANISOU 1662  C   HIS C 227     6887   6376   8561   1270   -291    -47       C  
ATOM   1663  O   HIS C 227     -22.273  52.495 -45.274  1.00 50.51           O  
ANISOU 1663  O   HIS C 227     6036   5494   7663   1178   -285    -42       O  
ATOM   1664  CB  HIS C 227     -22.113  55.236 -46.023  1.00 49.75           C  
ANISOU 1664  CB  HIS C 227     5994   5094   7816   1266   -396    -55       C  
ATOM   1665  CG  HIS C 227     -21.828  55.722 -44.635  1.00 53.96           C  
ANISOU 1665  CG  HIS C 227     6551   5594   8356   1345   -422   -206       C  
ATOM   1666  ND1 HIS C 227     -22.619  55.410 -43.551  1.00 58.54           N  
ANISOU 1666  ND1 HIS C 227     7102   6298   8845   1439   -392   -291       N  
ATOM   1667  CD2 HIS C 227     -20.837  56.513 -44.160  1.00 56.39           C  
ANISOU 1667  CD2 HIS C 227     6907   5766   8752   1346   -476   -290       C  
ATOM   1668  CE1 HIS C 227     -22.122  55.978 -42.467  1.00 60.13           C  
ANISOU 1668  CE1 HIS C 227     7334   6445   9069   1499   -428   -424       C  
ATOM   1669  NE2 HIS C 227     -21.041  56.654 -42.809  1.00 58.64           N  
ANISOU 1669  NE2 HIS C 227     7192   6094   8992   1443   -481   -429       N  
ATOM   1670  N   SER C 228     -24.392  52.825 -44.577  1.00 54.70           N  
ANISOU 1670  N   SER C 228     6493   6156   8133   1351   -256    -83       N  
ATOM   1671  CA  SER C 228     -24.514  51.569 -43.847  1.00 44.84           C  
ANISOU 1671  CA  SER C 228     5216   5056   6763   1325   -201    -96       C  
ATOM   1672  C   SER C 228     -25.642  50.708 -44.401  1.00 39.05           C  
ANISOU 1672  C   SER C 228     4417   4458   5963   1308   -153     -4       C  
ATOM   1673  O   SER C 228     -25.996  49.690 -43.792  1.00 42.68           O  
ANISOU 1673  O   SER C 228     4841   5051   6326   1297   -105     -5       O  
ATOM   1674  CB  SER C 228     -24.738  51.832 -42.356  1.00 42.08           C  
ANISOU 1674  CB  SER C 228     4864   4759   6365   1432   -196   -222       C  
ATOM   1675  OG  SER C 228     -25.810  52.731 -42.153  1.00 53.76           O  
ANISOU 1675  OG  SER C 228     6313   6244   7868   1556   -206   -261       O  
ATOM   1676  N   ASP C 229     -26.224  51.100 -45.535  1.00 38.81           N  
ANISOU 1676  N   ASP C 229     4365   4397   5983   1306   -167     76       N  
ATOM   1677  CA  ASP C 229     -27.298  50.352 -46.174  1.00 39.27           C  
ANISOU 1677  CA  ASP C 229     4357   4577   5988   1288   -130    162       C  
ATOM   1678  C   ASP C 229     -26.876  49.816 -47.534  1.00 39.44           C  
ANISOU 1678  C   ASP C 229     4384   4574   6026   1174   -136    269       C  
ATOM   1679  O   ASP C 229     -27.725  49.389 -48.318  1.00 46.00           O  
ANISOU 1679  O   ASP C 229     5164   5480   6834   1159   -121    345       O  
ATOM   1680  CB  ASP C 229     -28.542  51.227 -46.318  1.00 48.14           C  
ANISOU 1680  CB  ASP C 229     5437   5713   7140   1401   -140    162       C  
ATOM   1681  CG  ASP C 229     -28.970  51.854 -45.009  1.00 55.96           C  
ANISOU 1681  CG  ASP C 229     6420   6727   8115   1527   -138     47       C  
ATOM   1682  OD1 ASP C 229     -28.822  51.200 -43.957  1.00 56.09           O  
ANISOU 1682  OD1 ASP C 229     6430   6830   8052   1529   -103     -9       O  
ATOM   1683  OD2 ASP C 229     -29.452  53.007 -45.035  1.00 56.39           O  
ANISOU 1683  OD2 ASP C 229     6475   6715   8234   1628   -173     12       O  
ATOM   1684  N   CYS C 230     -25.582  49.845 -47.835  1.00 34.83           N  
ANISOU 1684  N   CYS C 230     3858   3893   5482   1097   -160    274       N  
ATOM   1685  CA  CYS C 230     -25.103  49.309 -49.097  1.00 38.79           C  
ANISOU 1685  CA  CYS C 230     4364   4384   5991    992   -164    369       C  
ATOM   1686  C   CYS C 230     -25.262  47.793 -49.131  1.00 39.17           C  
ANISOU 1686  C   CYS C 230     4377   4558   5948    918   -122    401       C  
ATOM   1687  O   CYS C 230     -25.157  47.106 -48.110  1.00 35.56           O  
ANISOU 1687  O   CYS C 230     3917   4162   5432    917    -95    349       O  
ATOM   1688  CB  CYS C 230     -23.631  49.655 -49.316  1.00 38.90           C  
ANISOU 1688  CB  CYS C 230     4442   4275   6063    928   -195    361       C  
ATOM   1689  SG  CYS C 230     -23.159  51.398 -49.192  1.00 45.57           S  
ANISOU 1689  SG  CYS C 230     5338   4943   7034    993   -252    318       S  
ATOM   1690  N   LEU C 231     -25.525  47.272 -50.327  1.00 32.88           N  
ANISOU 1690  N   LEU C 231     3553   3800   5141    859   -121    489       N  
ATOM   1691  CA  LEU C 231     -25.422  45.839 -50.556  1.00 30.60           C  
ANISOU 1691  CA  LEU C 231     3240   3600   4784    771    -94    522       C  
ATOM   1692  C   LEU C 231     -23.986  45.410 -50.812  1.00 38.23           C  
ANISOU 1692  C   LEU C 231     4259   4509   5758    681   -106    521       C  
ATOM   1693  O   LEU C 231     -23.657  44.234 -50.615  1.00 51.63           O  
ANISOU 1693  O   LEU C 231     5951   6263   7401    618    -86    519       O  
ATOM   1694  CB  LEU C 231     -26.319  45.432 -51.727  1.00 33.65           C  
ANISOU 1694  CB  LEU C 231     3572   4058   5155    749    -94    604       C  
ATOM   1695  CG  LEU C 231     -27.797  45.793 -51.500  1.00 45.95           C  
ANISOU 1695  CG  LEU C 231     5068   5686   6704    837    -82    607       C  
ATOM   1696  CD1 LEU C 231     -28.641  45.565 -52.748  1.00 24.60           C  
ANISOU 1696  CD1 LEU C 231     2311   3042   3995    821    -92    687       C  
ATOM   1697  CD2 LEU C 231     -28.358  45.012 -50.320  1.00 24.51           C  
ANISOU 1697  CD2 LEU C 231     2315   3070   3926    854    -40    563       C  
ATOM   1698  N   ALA C 232     -23.132  46.344 -51.226  1.00 37.89           N  
ANISOU 1698  N   ALA C 232     4262   4353   5782    676   -138    525       N  
ATOM   1699  CA  ALA C 232     -21.712  46.097 -51.425  1.00 33.75           C  
ANISOU 1699  CA  ALA C 232     3783   3769   5272    597   -149    520       C  
ATOM   1700  C   ALA C 232     -20.975  47.421 -51.292  1.00 38.07           C  
ANISOU 1700  C   ALA C 232     4376   4182   5906    625   -184    493       C  
ATOM   1701  O   ALA C 232     -21.549  48.488 -51.522  1.00 34.64           O  
ANISOU 1701  O   ALA C 232     3939   3695   5528    689   -204    509       O  
ATOM   1702  CB  ALA C 232     -21.433  45.457 -52.790  1.00 31.17           C  
ANISOU 1702  CB  ALA C 232     3443   3473   4928    516   -152    602       C  
ATOM   1703  N   CYS C 233     -19.702  47.344 -50.913  1.00 43.32           N  
ANISOU 1703  N   CYS C 233     5083   4791   6587    578   -193    452       N  
ATOM   1704  CA  CYS C 233     -18.858  48.524 -50.767  1.00 41.05           C  
ANISOU 1704  CA  CYS C 233     4837   4369   6389    589   -229    423       C  
ATOM   1705  C   CYS C 233     -18.029  48.718 -52.028  1.00 40.47           C  
ANISOU 1705  C   CYS C 233     4774   4243   6359    511   -244    506       C  
ATOM   1706  O   CYS C 233     -17.406  47.770 -52.518  1.00 36.55           O  
ANISOU 1706  O   CYS C 233     4273   3798   5815    433   -230    535       O  
ATOM   1707  CB  CYS C 233     -17.935  48.401 -49.552  1.00 49.03           C  
ANISOU 1707  CB  CYS C 233     5883   5350   7397    586   -235    323       C  
ATOM   1708  SG  CYS C 233     -18.757  48.457 -47.942  1.00 66.95           S  
ANISOU 1708  SG  CYS C 233     8146   7671   9622    692   -222    215       S  
ATOM   1709  N   LEU C 234     -18.015  49.949 -52.548  1.00 41.01           N  
ANISOU 1709  N   LEU C 234     4855   4209   6517    534   -275    546       N  
ATOM   1710  CA  LEU C 234     -17.221  50.238 -53.735  1.00 38.56           C  
ANISOU 1710  CA  LEU C 234     4553   3850   6250    463   -287    635       C  
ATOM   1711  C   LEU C 234     -15.728  50.244 -53.433  1.00 41.38           C  
ANISOU 1711  C   LEU C 234     4940   4142   6641    395   -298    598       C  
ATOM   1712  O   LEU C 234     -14.921  50.060 -54.350  1.00 44.20           O  
ANISOU 1712  O   LEU C 234     5294   4499   7002    319   -296    666       O  
ATOM   1713  CB  LEU C 234     -17.638  51.581 -54.341  1.00 45.65           C  
ANISOU 1713  CB  LEU C 234     5455   4651   7239    507   -318    698       C  
ATOM   1714  CG  LEU C 234     -16.998  51.960 -55.680  1.00 43.67           C  
ANISOU 1714  CG  LEU C 234     5204   4360   7029    441   -327    815       C  
ATOM   1715  CD1 LEU C 234     -17.447  51.005 -56.781  1.00 35.87           C  
ANISOU 1715  CD1 LEU C 234     4177   3505   5948    406   -299    897       C  
ATOM   1716  CD2 LEU C 234     -17.308  53.405 -56.053  1.00 41.03           C  
ANISOU 1716  CD2 LEU C 234     4883   3904   6803    489   -363    870       C  
ATOM   1717  N   HIS C 235     -15.339  50.445 -52.174  1.00 41.21           N  
ANISOU 1717  N   HIS C 235     4944   4073   6640    424   -311    490       N  
ATOM   1718  CA  HIS C 235     -13.928  50.388 -51.820  1.00 35.21           C  
ANISOU 1718  CA  HIS C 235     4209   3260   5908    362   -325    446       C  
ATOM   1719  C   HIS C 235     -13.694  49.543 -50.571  1.00 32.27           C  
ANISOU 1719  C   HIS C 235     3845   2947   5467    375   -312    339       C  
ATOM   1720  O   HIS C 235     -13.127  48.454 -50.682  1.00 36.04           O  
ANISOU 1720  O   HIS C 235     4316   3498   5879    315   -291    344       O  
ATOM   1721  CB  HIS C 235     -13.360  51.800 -51.652  1.00 30.26           C  
ANISOU 1721  CB  HIS C 235     3609   2476   5410    373   -370    428       C  
ATOM   1722  CG  HIS C 235     -13.583  52.690 -52.840  1.00 36.11           C  
ANISOU 1722  CG  HIS C 235     4344   3150   6225    362   -384    543       C  
ATOM   1723  ND1 HIS C 235     -13.031  52.432 -54.083  1.00 35.03           N  
ANISOU 1723  ND1 HIS C 235     4190   3039   6080    280   -370    653       N  
ATOM   1724  CD2 HIS C 235     -14.289  53.839 -52.973  1.00 33.91           C  
ANISOU 1724  CD2 HIS C 235     4073   2783   6029    427   -413    567       C  
ATOM   1725  CE1 HIS C 235     -13.394  53.378 -54.933  1.00 28.68           C  
ANISOU 1725  CE1 HIS C 235     3383   2168   5346    293   -387    747       C  
ATOM   1726  NE2 HIS C 235     -14.156  54.244 -54.284  1.00 30.94           N  
ANISOU 1726  NE2 HIS C 235     3685   2378   5692    381   -414    698       N  
ATOM   1727  N   PHE C 236     -14.117  49.994 -49.384  1.00 26.07           N  
ANISOU 1727  N   PHE C 236     3075   2137   4693    455   -326    244       N  
ATOM   1728  CA  PHE C 236     -13.812  49.226 -48.179  1.00 33.99           C  
ANISOU 1728  CA  PHE C 236     4087   3200   5626    468   -315    148       C  
ATOM   1729  C   PHE C 236     -14.978  49.153 -47.187  1.00 35.14           C  
ANISOU 1729  C   PHE C 236     4222   3411   5718    566   -299     88       C  
ATOM   1730  O   PHE C 236     -15.682  50.135 -46.940  1.00 32.22           O  
ANISOU 1730  O   PHE C 236     3853   2991   5397    645   -318     62       O  
ATOM   1731  CB  PHE C 236     -12.540  49.769 -47.494  1.00 23.75           C  
ANISOU 1731  CB  PHE C 236     2823   1809   4393    449   -353     66       C  
ATOM   1732  CG  PHE C 236     -11.326  49.803 -48.404  1.00 40.21           C  
ANISOU 1732  CG  PHE C 236     4910   3840   6529    349   -364    125       C  
ATOM   1733  CD1 PHE C 236     -10.431  48.745 -48.428  1.00 42.52           C  
ANISOU 1733  CD1 PHE C 236     5200   4195   6762    281   -348    122       C  
ATOM   1734  CD2 PHE C 236     -11.067  50.903 -49.209  1.00 42.08           C  
ANISOU 1734  CD2 PHE C 236     5150   3965   6874    326   -392    184       C  
ATOM   1735  CE1 PHE C 236      -9.323  48.773 -49.250  1.00 42.45           C  
ANISOU 1735  CE1 PHE C 236     5186   4149   6795    194   -355    173       C  
ATOM   1736  CE2 PHE C 236      -9.956  50.931 -50.032  1.00 39.63           C  
ANISOU 1736  CE2 PHE C 236     4836   3618   6606    233   -397    244       C  
ATOM   1737  CZ  PHE C 236      -9.083  49.868 -50.051  1.00 44.58           C  
ANISOU 1737  CZ  PHE C 236     5454   4317   7167    169   -378    236       C  
ATOM   1738  N   ASN C 237     -15.135  47.956 -46.613  1.00 41.59           N  
ANISOU 1738  N   ASN C 237     5027   4343   6433    560   -265     67       N  
ATOM   1739  CA  ASN C 237     -16.179  47.531 -45.670  1.00 52.75           C  
ANISOU 1739  CA  ASN C 237     6420   5854   7768    636   -237     25       C  
ATOM   1740  C   ASN C 237     -15.576  47.749 -44.278  1.00 53.98           C  
ANISOU 1740  C   ASN C 237     6605   5994   7913    681   -255    -93       C  
ATOM   1741  O   ASN C 237     -14.889  46.877 -43.740  1.00 60.29           O  
ANISOU 1741  O   ASN C 237     7413   6841   8653    646   -245   -121       O  
ATOM   1742  CB  ASN C 237     -16.510  46.073 -46.023  1.00 66.94           C  
ANISOU 1742  CB  ASN C 237     8189   7770   9474    582   -194     89       C  
ATOM   1743  CG  ASN C 237     -17.605  45.351 -45.159  1.00 69.98           C  
ANISOU 1743  CG  ASN C 237     8543   8278   9769    638   -154     72       C  
ATOM   1744  OD1 ASN C 237     -17.630  44.122 -45.227  1.00 76.40           O  
ANISOU 1744  OD1 ASN C 237     9341   9173  10517    587   -126    109       O  
ATOM   1745  ND2 ASN C 237     -18.486  46.039 -44.422  1.00 70.51           N  
ANISOU 1745  ND2 ASN C 237     8596   8360   9832    736   -151     24       N  
ATOM   1746  N   HIS C 238     -15.755  48.959 -43.734  1.00 51.20           N  
ANISOU 1746  N   HIS C 238     6267   5564   7622    761   -289   -166       N  
ATOM   1747  CA  HIS C 238     -15.231  49.350 -42.417  1.00 44.30           C  
ANISOU 1747  CA  HIS C 238     5419   4668   6744    818   -316   -293       C  
ATOM   1748  C   HIS C 238     -16.309  49.066 -41.374  1.00 51.85           C  
ANISOU 1748  C   HIS C 238     6352   5742   7608    916   -284   -343       C  
ATOM   1749  O   HIS C 238     -17.099  49.933 -40.997  1.00 47.19           O  
ANISOU 1749  O   HIS C 238     5754   5135   7042   1011   -296   -391       O  
ATOM   1750  CB  HIS C 238     -14.805  50.826 -42.412  1.00 40.33           C  
ANISOU 1750  CB  HIS C 238     4944   4013   6368    850   -377   -352       C  
ATOM   1751  CG  HIS C 238     -14.227  51.302 -41.108  1.00 40.68           C  
ANISOU 1751  CG  HIS C 238     5014   4026   6417    909   -415   -494       C  
ATOM   1752  ND1 HIS C 238     -14.191  52.635 -40.755  1.00 40.52           N  
ANISOU 1752  ND1 HIS C 238     5013   3887   6496    976   -471   -578       N  
ATOM   1753  CD2 HIS C 238     -13.650  50.629 -40.083  1.00 36.83           C  
ANISOU 1753  CD2 HIS C 238     4536   3609   5850    915   -410   -568       C  
ATOM   1754  CE1 HIS C 238     -13.625  52.761 -39.568  1.00 43.03           C  
ANISOU 1754  CE1 HIS C 238     5350   4209   6792   1020   -500   -706       C  
ATOM   1755  NE2 HIS C 238     -13.287  51.559 -39.138  1.00 42.89           N  
ANISOU 1755  NE2 HIS C 238     5326   4309   6662    986   -463   -699       N  
ATOM   1756  N   SER C 239     -16.346  47.806 -40.930  1.00 55.02           N  
ANISOU 1756  N   SER C 239     6739   6264   7902    891   -242   -325       N  
ATOM   1757  CA  SER C 239     -17.226  47.356 -39.849  1.00 50.77           C  
ANISOU 1757  CA  SER C 239     6175   5855   7261    971   -205   -363       C  
ATOM   1758  C   SER C 239     -18.684  47.732 -40.102  1.00 51.13           C  
ANISOU 1758  C   SER C 239     6178   5945   7303   1040   -181   -328       C  
ATOM   1759  O   SER C 239     -19.414  48.120 -39.189  1.00 51.87           O  
ANISOU 1759  O   SER C 239     6255   6096   7356   1144   -172   -395       O  
ATOM   1760  CB  SER C 239     -16.753  47.901 -38.501  1.00 53.11           C  
ANISOU 1760  CB  SER C 239     6496   6143   7539   1052   -235   -498       C  
ATOM   1761  OG  SER C 239     -15.445  47.448 -38.198  1.00 65.92           O  
ANISOU 1761  OG  SER C 239     8152   7742   9154    991   -256   -530       O  
ATOM   1762  N   GLY C 240     -19.117  47.622 -41.355  1.00 44.25           N  
ANISOU 1762  N   GLY C 240     5288   5056   6471    986   -171   -226       N  
ATOM   1763  CA  GLY C 240     -20.476  47.938 -41.734  1.00 49.59           C  
ANISOU 1763  CA  GLY C 240     5919   5775   7147   1043   -151   -183       C  
ATOM   1764  C   GLY C 240     -20.639  49.238 -42.495  1.00 52.22           C  
ANISOU 1764  C   GLY C 240     6264   5985   7592   1074   -193   -177       C  
ATOM   1765  O   GLY C 240     -21.685  49.447 -43.119  1.00 59.94           O  
ANISOU 1765  O   GLY C 240     7205   6989   8581   1103   -181   -120       O  
ATOM   1766  N   ILE C 241     -19.640  50.116 -42.462  1.00 45.19           N  
ANISOU 1766  N   ILE C 241     5422   4961   6789   1068   -245   -233       N  
ATOM   1767  CA  ILE C 241     -19.689  51.399 -43.153  1.00 46.39           C  
ANISOU 1767  CA  ILE C 241     5589   4978   7060   1093   -291   -223       C  
ATOM   1768  C   ILE C 241     -18.844  51.302 -44.412  1.00 45.41           C  
ANISOU 1768  C   ILE C 241     5483   4774   6998    977   -305   -128       C  
ATOM   1769  O   ILE C 241     -17.660  50.960 -44.340  1.00 49.80           O  
ANISOU 1769  O   ILE C 241     6066   5296   7559    904   -316   -143       O  
ATOM   1770  CB  ILE C 241     -19.175  52.529 -42.245  1.00 47.33           C  
ANISOU 1770  CB  ILE C 241     5746   4991   7247   1166   -345   -351       C  
ATOM   1771  CG1 ILE C 241     -19.998  52.630 -40.951  1.00 45.13           C  
ANISOU 1771  CG1 ILE C 241     5447   4806   6894   1291   -331   -455       C  
ATOM   1772  CG2 ILE C 241     -19.175  53.841 -42.983  1.00 47.61           C  
ANISOU 1772  CG2 ILE C 241     5800   4871   7419   1184   -397   -334       C  
ATOM   1773  CD1 ILE C 241     -21.474  52.766 -41.165  1.00 47.68           C  
ANISOU 1773  CD1 ILE C 241     5721   5204   7190   1369   -302   -417       C  
ATOM   1774  N   CYS C 242     -19.436  51.605 -45.565  1.00 39.49           N  
ANISOU 1774  N   CYS C 242     4714   4001   6290    965   -305    -31       N  
ATOM   1775  CA  CYS C 242     -18.662  51.627 -46.799  1.00 45.65           C  
ANISOU 1775  CA  CYS C 242     5508   4710   7127    864   -318     62       C  
ATOM   1776  C   CYS C 242     -17.903  52.946 -46.905  1.00 51.20           C  
ANISOU 1776  C   CYS C 242     6250   5243   7960    869   -376     35       C  
ATOM   1777  O   CYS C 242     -18.497  54.025 -46.803  1.00 51.12           O  
ANISOU 1777  O   CYS C 242     6244   5159   8020    952   -407     10       O  
ATOM   1778  CB  CYS C 242     -19.566  51.429 -48.014  1.00 59.27           C  
ANISOU 1778  CB  CYS C 242     7196   6483   8840    850   -298    180       C  
ATOM   1779  SG  CYS C 242     -20.291  49.775 -48.172  1.00 76.16           S  
ANISOU 1779  SG  CYS C 242     9285   8806  10845    812   -237    231       S  
ATOM   1780  N   GLU C 243     -16.588  52.857 -47.106  1.00 52.21           N  
ANISOU 1780  N   GLU C 243     6404   5308   8124    781   -393     39       N  
ATOM   1781  CA  GLU C 243     -15.717  54.023 -47.078  1.00 47.08           C  
ANISOU 1781  CA  GLU C 243     5790   4497   7602    772   -449      5       C  
ATOM   1782  C   GLU C 243     -14.684  53.934 -48.195  1.00 45.22           C  
ANISOU 1782  C   GLU C 243     5559   4210   7413    654   -452    104       C  
ATOM   1783  O   GLU C 243     -14.393  52.857 -48.724  1.00 51.73           O  
ANISOU 1783  O   GLU C 243     6366   5128   8159    580   -414    164       O  
ATOM   1784  CB  GLU C 243     -15.015  54.166 -45.719  1.00 49.72           C  
ANISOU 1784  CB  GLU C 243     6150   4802   7939    802   -476   -138       C  
ATOM   1785  CG  GLU C 243     -15.945  54.591 -44.590  1.00 64.67           C  
ANISOU 1785  CG  GLU C 243     8041   6722   9808    933   -484   -248       C  
ATOM   1786  CD  GLU C 243     -15.209  54.895 -43.299  1.00 76.42           C  
ANISOU 1786  CD  GLU C 243     9557   8171  11308    970   -522   -395       C  
ATOM   1787  OE1 GLU C 243     -15.767  55.631 -42.457  1.00 76.01           O  
ANISOU 1787  OE1 GLU C 243     9511   8094  11274   1080   -549   -497       O  
ATOM   1788  OE2 GLU C 243     -14.077  54.397 -43.123  1.00 79.43           O  
ANISOU 1788  OE2 GLU C 243     9952   8552  11677    893   -526   -414       O  
ATOM   1789  N   LEU C 244     -14.125  55.100 -48.531  1.00 40.98           N  
ANISOU 1789  N   LEU C 244     5044   3520   7008    638   -500    118       N  
ATOM   1790  CA  LEU C 244     -13.165  55.236 -49.622  1.00 38.55           C  
ANISOU 1790  CA  LEU C 244     4736   3153   6760    532   -505    221       C  
ATOM   1791  C   LEU C 244     -11.776  54.741 -49.236  1.00 38.63           C  
ANISOU 1791  C   LEU C 244     4755   3160   6762    451   -509    172       C  
ATOM   1792  O   LEU C 244     -11.017  54.293 -50.104  1.00 34.51           O  
ANISOU 1792  O   LEU C 244     4220   2661   6230    356   -490    256       O  
ATOM   1793  CB  LEU C 244     -13.109  56.700 -50.065  1.00 38.32           C  
ANISOU 1793  CB  LEU C 244     4723   2954   6881    545   -556    261       C  
ATOM   1794  CG  LEU C 244     -11.937  57.201 -50.924  1.00 41.19           C  
ANISOU 1794  CG  LEU C 244     5091   3215   7344    440   -576    348       C  
ATOM   1795  CD1 LEU C 244     -11.986  56.587 -52.312  1.00 28.88           C  
ANISOU 1795  CD1 LEU C 244     3504   1744   5727    371   -532    500       C  
ATOM   1796  CD2 LEU C 244     -11.963  58.715 -51.006  1.00 30.97           C  
ANISOU 1796  CD2 LEU C 244     3818   1746   6202    469   -633    356       C  
ATOM   1797  N   HIS C 245     -11.432  54.807 -47.953  1.00 32.88           N  
ANISOU 1797  N   HIS C 245     4046   2415   6034    491   -533     36       N  
ATOM   1798  CA  HIS C 245     -10.163  54.292 -47.466  1.00 32.80           C  
ANISOU 1798  CA  HIS C 245     4042   2413   6007    426   -539    -23       C  
ATOM   1799  C   HIS C 245     -10.331  53.922 -46.002  1.00 34.07           C  
ANISOU 1799  C   HIS C 245     4215   2632   6098    501   -543   -166       C  
ATOM   1800  O   HIS C 245     -11.271  54.361 -45.334  1.00 35.66           O  
ANISOU 1800  O   HIS C 245     4422   2833   6292    602   -553   -229       O  
ATOM   1801  CB  HIS C 245      -9.029  55.311 -47.642  1.00 35.88           C  
ANISOU 1801  CB  HIS C 245     4444   2647   6540    367   -591    -28       C  
ATOM   1802  CG  HIS C 245      -9.233  56.582 -46.875  1.00 39.61           C  
ANISOU 1802  CG  HIS C 245     4942   2983   7124    443   -653   -124       C  
ATOM   1803  ND1 HIS C 245      -9.047  56.669 -45.512  1.00 47.49           N  
ANISOU 1803  ND1 HIS C 245     5957   3975   8110    505   -684   -281       N  
ATOM   1804  CD2 HIS C 245      -9.613  57.816 -47.282  1.00 41.59           C  
ANISOU 1804  CD2 HIS C 245     5203   3097   7501    472   -692    -88       C  
ATOM   1805  CE1 HIS C 245      -9.301  57.902 -45.112  1.00 45.65           C  
ANISOU 1805  CE1 HIS C 245     5744   3619   7982    567   -739   -345       C  
ATOM   1806  NE2 HIS C 245      -9.646  58.619 -46.167  1.00 43.19           N  
ANISOU 1806  NE2 HIS C 245     5429   3247   7735    541   -738   -227       N  
ATOM   1807  N   CYS C 246      -9.408  53.106 -45.511  1.00 37.29           N  
ANISOU 1807  N   CYS C 246     4624   3096   6448    454   -536   -214       N  
ATOM   1808  CA  CYS C 246      -9.420  52.708 -44.115  1.00 41.11           C  
ANISOU 1808  CA  CYS C 246     5119   3642   6858    519   -541   -343       C  
ATOM   1809  C   CYS C 246      -8.770  53.786 -43.254  1.00 51.49           C  
ANISOU 1809  C   CYS C 246     6458   4835   8273    552   -609   -466       C  
ATOM   1810  O   CYS C 246      -7.996  54.606 -43.753  1.00 52.40           O  
ANISOU 1810  O   CYS C 246     6578   4821   8512    495   -649   -446       O  
ATOM   1811  CB  CYS C 246      -8.689  51.380 -43.945  1.00 40.03           C  
ANISOU 1811  CB  CYS C 246     4975   3615   6620    459   -510   -341       C  
ATOM   1812  SG  CYS C 246      -9.435  50.016 -44.871  1.00 59.69           S  
ANISOU 1812  SG  CYS C 246     7438   6248   8995    421   -438   -215       S  
ATOM   1813  N   PRO C 247      -9.081  53.822 -41.959  1.00 51.77           N  
ANISOU 1813  N   PRO C 247     6505   4908   8257    646   -624   -594       N  
ATOM   1814  CA  PRO C 247      -8.393  54.771 -41.073  1.00 43.78           C  
ANISOU 1814  CA  PRO C 247     5514   3787   7332    679   -695   -729       C  
ATOM   1815  C   PRO C 247      -6.910  54.438 -40.988  1.00 46.22           C  
ANISOU 1815  C   PRO C 247     5824   4076   7662    587   -717   -753       C  
ATOM   1816  O   PRO C 247      -6.526  53.280 -40.808  1.00 49.08           O  
ANISOU 1816  O   PRO C 247     6177   4555   7916    553   -680   -742       O  
ATOM   1817  CB  PRO C 247      -9.101  54.586 -39.725  1.00 43.48           C  
ANISOU 1817  CB  PRO C 247     5482   3844   7195    802   -692   -852       C  
ATOM   1818  CG  PRO C 247     -10.369  53.844 -40.033  1.00 50.65           C  
ANISOU 1818  CG  PRO C 247     6369   4880   7994    838   -623   -768       C  
ATOM   1819  CD  PRO C 247     -10.080  53.015 -41.238  1.00 47.51           C  
ANISOU 1819  CD  PRO C 247     5956   4518   7578    726   -579   -623       C  
ATOM   1820  N   ALA C 248      -6.078  55.466 -41.131  1.00 48.31           N  
ANISOU 1820  N   ALA C 248     6096   4189   8072    546   -779   -785       N  
ATOM   1821  CA  ALA C 248      -4.638  55.261 -41.163  1.00 42.29           C  
ANISOU 1821  CA  ALA C 248     5325   3397   7346    451   -802   -800       C  
ATOM   1822  C   ALA C 248      -4.132  54.782 -39.809  1.00 47.40           C  
ANISOU 1822  C   ALA C 248     5980   4117   7912    498   -825   -944       C  
ATOM   1823  O   ALA C 248      -4.752  55.015 -38.768  1.00 49.55           O  
ANISOU 1823  O   ALA C 248     6269   4418   8141    607   -843  -1056       O  
ATOM   1824  CB  ALA C 248      -3.922  56.549 -41.568  1.00 45.99           C  
ANISOU 1824  CB  ALA C 248     5788   3739   7946    387   -849   -781       C  
ATOM   1825  N   LEU C 249      -2.987  54.098 -39.832  1.00 51.29           N  
ANISOU 1825  N   LEU C 249     6460   4648   8379    419   -823   -941       N  
ATOM   1826  CA  LEU C 249      -2.450  53.530 -38.601  1.00 56.36           C  
ANISOU 1826  CA  LEU C 249     7108   5372   8933    459   -842  -1066       C  
ATOM   1827  C   LEU C 249      -1.830  54.594 -37.704  1.00 56.61           C  
ANISOU 1827  C   LEU C 249     7144   5342   9024    483   -913  -1191       C  
ATOM   1828  O   LEU C 249      -1.816  54.432 -36.478  1.00 58.36           O  
ANISOU 1828  O   LEU C 249     7375   5634   9165    561   -934  -1312       O  
ATOM   1829  CB  LEU C 249      -1.431  52.439 -38.925  1.00 54.65           C  
ANISOU 1829  CB  LEU C 249     6872   5234   8658    369   -815  -1015       C  
ATOM   1830  CG  LEU C 249      -2.071  51.146 -39.436  1.00 52.66           C  
ANISOU 1830  CG  LEU C 249     6614   5120   8274    359   -735   -904       C  
ATOM   1831  CD1 LEU C 249      -1.022  50.164 -39.924  1.00 52.93           C  
ANISOU 1831  CD1 LEU C 249     6629   5212   8272    266   -714   -849       C  
ATOM   1832  CD2 LEU C 249      -2.926  50.527 -38.340  1.00 45.18           C  
ANISOU 1832  CD2 LEU C 249     5683   4294   7191    465   -712   -968       C  
ATOM   1833  N   VAL C 250      -1.316  55.680 -38.280  1.00 53.27           N  
ANISOU 1833  N   VAL C 250     6708   4809   8723    416   -944  -1151       N  
ATOM   1834  CA  VAL C 250      -0.768  56.783 -37.500  1.00 60.93           C  
ANISOU 1834  CA  VAL C 250     7675   5723   9750    432  -1010  -1254       C  
ATOM   1835  C   VAL C 250      -1.459  58.075 -37.914  1.00 61.37           C  
ANISOU 1835  C   VAL C 250     7739   5670   9907    452  -1030  -1223       C  
ATOM   1836  O   VAL C 250      -1.776  58.279 -39.092  1.00 67.99           O  
ANISOU 1836  O   VAL C 250     8574   6450  10809    400  -1001  -1094       O  
ATOM   1837  CB  VAL C 250       0.769  56.903 -37.650  1.00 67.62           C  
ANISOU 1837  CB  VAL C 250     8493   6541  10658    329  -1040  -1252       C  
ATOM   1838  CG1 VAL C 250       1.439  55.544 -37.485  1.00 63.20           C  
ANISOU 1838  CG1 VAL C 250     7924   6087  10003    299  -1014  -1256       C  
ATOM   1839  CG2 VAL C 250       1.162  57.543 -38.978  1.00 69.29           C  
ANISOU 1839  CG2 VAL C 250     8684   6651  10992    223  -1032  -1119       C  
ATOM   1840  N   THR C 251      -1.719  58.931 -36.933  1.00 60.02           N  
ANISOU 1840  N   THR C 251     7580   5478   9746    533  -1079  -1342       N  
ATOM   1841  CA  THR C 251      -2.151  60.298 -37.162  1.00 69.13           C  
ANISOU 1841  CA  THR C 251     8741   6516  11009    550  -1116  -1337       C  
ATOM   1842  C   THR C 251      -1.052  61.246 -36.700  1.00 72.63           C  
ANISOU 1842  C   THR C 251     9169   6883  11545    510  -1187  -1411       C  
ATOM   1843  O   THR C 251      -0.204  60.894 -35.875  1.00 73.06           O  
ANISOU 1843  O   THR C 251     9211   6992  11555    507  -1213  -1502       O  
ATOM   1844  CB  THR C 251      -3.460  60.607 -36.424  1.00 67.62           C  
ANISOU 1844  CB  THR C 251     8573   6358  10761    685  -1118  -1417       C  
ATOM   1845  OG1 THR C 251      -3.234  60.584 -35.009  1.00 67.87           O  
ANISOU 1845  OG1 THR C 251     8607   6460  10719    761  -1157  -1573       O  
ATOM   1846  CG2 THR C 251      -4.534  59.586 -36.777  1.00 65.21           C  
ANISOU 1846  CG2 THR C 251     8276   6143  10357    732  -1047  -1351       C  
ATOM   1847  N   TYR C 252      -1.068  62.458 -37.243  1.00 70.62           N  
ANISOU 1847  N   TYR C 252     8912   6499  11421    480  -1220  -1370       N  
ATOM   1848  CA  TYR C 252      -0.029  63.444 -36.986  1.00 66.71           C  
ANISOU 1848  CA  TYR C 252     8398   5911  11038    430  -1287  -1421       C  
ATOM   1849  C   TYR C 252      -0.567  64.545 -36.085  1.00 67.90           C  
ANISOU 1849  C   TYR C 252     8565   6007  11226    526  -1351  -1545       C  
ATOM   1850  O   TYR C 252      -1.663  65.066 -36.315  1.00 67.93           O  
ANISOU 1850  O   TYR C 252     8591   5971  11249    587  -1345  -1524       O  
ATOM   1851  CB  TYR C 252       0.507  64.029 -38.294  1.00 68.61           C  
ANISOU 1851  CB  TYR C 252     8620   6042  11407    314  -1281  -1276       C  
ATOM   1852  CG  TYR C 252       1.071  62.973 -39.216  1.00 77.44           C  
ANISOU 1852  CG  TYR C 252     9717   7220  12486    219  -1219  -1154       C  
ATOM   1853  CD1 TYR C 252       0.416  62.623 -40.391  1.00 70.69           C  
ANISOU 1853  CD1 TYR C 252     8868   6368  11624    190  -1159  -1007       C  
ATOM   1854  CD2 TYR C 252       2.244  62.301 -38.889  1.00 82.06           C  
ANISOU 1854  CD2 TYR C 252    10276   7866  13036    164  -1222  -1189       C  
ATOM   1855  CE1 TYR C 252       0.927  61.649 -41.225  1.00 65.46           C  
ANISOU 1855  CE1 TYR C 252     8185   5766  10923    107  -1104   -900       C  
ATOM   1856  CE2 TYR C 252       2.759  61.325 -39.717  1.00 81.23           C  
ANISOU 1856  CE2 TYR C 252    10150   7820  12893     82  -1167  -1084       C  
ATOM   1857  CZ  TYR C 252       2.096  61.002 -40.884  1.00 76.67           C  
ANISOU 1857  CZ  TYR C 252     9578   7243  12309     53  -1109   -941       C  
ATOM   1858  OH  TYR C 252       2.606  60.028 -41.712  1.00 86.50           O  
ANISOU 1858  OH  TYR C 252    10800   8552  13513    -26  -1056   -839       O  
ATOM   1859  N   ASN C 253       0.204  64.881 -35.053  1.00 72.84           N  
ANISOU 1859  N   ASN C 253     9178   6637  11861    543  -1413  -1676       N  
ATOM   1860  CA  ASN C 253      -0.126  66.008 -34.190  1.00 75.27           C  
ANISOU 1860  CA  ASN C 253     9494   6884  12219    625  -1485  -1801       C  
ATOM   1861  C   ASN C 253      -0.226  67.278 -35.024  1.00 76.98           C  
ANISOU 1861  C   ASN C 253     9713   6937  12600    580  -1515  -1728       C  
ATOM   1862  O   ASN C 253       0.726  67.655 -35.711  1.00 74.36           O  
ANISOU 1862  O   ASN C 253     9358   6520  12377    471  -1529  -1653       O  
ATOM   1863  CB  ASN C 253       0.935  66.155 -33.098  1.00 76.41           C  
ANISOU 1863  CB  ASN C 253     9617   7053  12364    629  -1550  -1938       C  
ATOM   1864  CG  ASN C 253       0.629  67.279 -32.135  1.00 82.86           C  
ANISOU 1864  CG  ASN C 253    10440   7816  13227    719  -1630  -2080       C  
ATOM   1865  OD1 ASN C 253       1.378  68.251 -32.039  1.00 88.36           O  
ANISOU 1865  OD1 ASN C 253    11118   8403  14051    679  -1698  -2119       O  
ATOM   1866  ND2 ASN C 253      -0.482  67.157 -31.419  1.00 83.41           N  
ANISOU 1866  ND2 ASN C 253    10533   7964  13195    843  -1622  -2158       N  
ATOM   1867  N   THR C 254      -1.387  67.936 -34.966  1.00 75.85           N  
ANISOU 1867  N   THR C 254     9596   6753  12471    667  -1525  -1748       N  
ATOM   1868  CA  THR C 254      -1.668  69.049 -35.867  1.00 77.34           C  
ANISOU 1868  CA  THR C 254     9791   6791  12803    632  -1544  -1659       C  
ATOM   1869  C   THR C 254      -0.688  70.206 -35.710  1.00 76.71           C  
ANISOU 1869  C   THR C 254     9692   6579  12875    577  -1626  -1704       C  
ATOM   1870  O   THR C 254      -0.561  71.023 -36.629  1.00 79.42           O  
ANISOU 1870  O   THR C 254    10033   6793  13350    511  -1638  -1601       O  
ATOM   1871  CB  THR C 254      -3.096  69.549 -35.647  1.00 78.44           C  
ANISOU 1871  CB  THR C 254     9961   6920  12922    752  -1547  -1697       C  
ATOM   1872  OG1 THR C 254      -3.186  70.199 -34.372  1.00 85.57           O  
ANISOU 1872  OG1 THR C 254    10868   7822  13823    847  -1618  -1873       O  
ATOM   1873  CG2 THR C 254      -4.071  68.380 -35.684  1.00 65.55           C  
ANISOU 1873  CG2 THR C 254     8343   5428  11135    814  -1467  -1665       C  
ATOM   1874  N   ASP C 255       0.007  70.296 -34.577  1.00 74.96           N  
ANISOU 1874  N   ASP C 255     9455   6387  12639    604  -1684  -1851       N  
ATOM   1875  CA  ASP C 255       0.965  71.368 -34.332  1.00 77.70           C  
ANISOU 1875  CA  ASP C 255     9780   6612  13131    557  -1767  -1907       C  
ATOM   1876  C   ASP C 255       2.400  70.973 -34.650  1.00 74.54           C  
ANISOU 1876  C   ASP C 255     9341   6215  12766    434  -1763  -1856       C  
ATOM   1877  O   ASP C 255       3.125  71.753 -35.275  1.00 77.29           O  
ANISOU 1877  O   ASP C 255     9668   6439  13258    342  -1792  -1790       O  
ATOM   1878  CB  ASP C 255       0.881  71.835 -32.873  1.00 87.38           C  
ANISOU 1878  CB  ASP C 255    11008   7861  14332    665  -1844  -2107       C  
ATOM   1879  CG  ASP C 255      -0.423  72.543 -32.561  1.00 98.90           C  
ANISOU 1879  CG  ASP C 255    12499   9287  15792    783  -1867  -2167       C  
ATOM   1880  OD1 ASP C 255      -1.242  71.974 -31.808  1.00102.71           O  
ANISOU 1880  OD1 ASP C 255    12997   9895  16133    893  -1844  -2248       O  
ATOM   1881  OD2 ASP C 255      -0.634  73.665 -33.075  1.00102.30           O  
ANISOU 1881  OD2 ASP C 255    12938   9568  16364    768  -1906  -2130       O  
ATOM   1882  N   THR C 256       2.830  69.780 -34.233  1.00 76.08           N  
ANISOU 1882  N   THR C 256     9525   6551  12832    432  -1726  -1885       N  
ATOM   1883  CA  THR C 256       4.208  69.345 -34.416  1.00 78.88           C  
ANISOU 1883  CA  THR C 256     9839   6923  13207    327  -1723  -1853       C  
ATOM   1884  C   THR C 256       4.380  68.297 -35.504  1.00 77.63           C  
ANISOU 1884  C   THR C 256     9675   6828  12993    242  -1634  -1696       C  
ATOM   1885  O   THR C 256       5.512  68.071 -35.944  1.00 79.40           O  
ANISOU 1885  O   THR C 256     9864   7048  13258    140  -1626  -1638       O  
ATOM   1886  CB  THR C 256       4.768  68.785 -33.101  1.00 77.97           C  
ANISOU 1886  CB  THR C 256     9711   6921  12993    381  -1756  -2008       C  
ATOM   1887  OG1 THR C 256       4.234  67.475 -32.872  1.00 75.17           O  
ANISOU 1887  OG1 THR C 256     9373   6721  12466    432  -1690  -2005       O  
ATOM   1888  CG2 THR C 256       4.381  69.688 -31.937  1.00 78.98           C  
ANISOU 1888  CG2 THR C 256     9849   7016  13143    489  -1839  -2175       C  
ATOM   1889  N   PHE C 257       3.294  67.655 -35.936  1.00 72.32           N  
ANISOU 1889  N   PHE C 257     9031   6216  12230    285  -1569  -1629       N  
ATOM   1890  CA  PHE C 257       3.322  66.623 -36.974  1.00 68.64           C  
ANISOU 1890  CA  PHE C 257     8561   5815  11705    216  -1485  -1482       C  
ATOM   1891  C   PHE C 257       4.247  65.468 -36.608  1.00 73.86           C  
ANISOU 1891  C   PHE C 257     9198   6594  12271    181  -1462  -1512       C  
ATOM   1892  O   PHE C 257       4.904  64.878 -37.469  1.00 72.13           O  
ANISOU 1892  O   PHE C 257     8956   6398  12053     85  -1417  -1400       O  
ATOM   1893  CB  PHE C 257       3.680  67.219 -38.337  1.00 55.78           C  
ANISOU 1893  CB  PHE C 257     6915   4078  10203    105  -1468  -1321       C  
ATOM   1894  CG  PHE C 257       2.529  67.928 -38.984  1.00 61.62           C  
ANISOU 1894  CG  PHE C 257     7683   4735  10993    141  -1458  -1246       C  
ATOM   1895  CD1 PHE C 257       2.361  69.294 -38.830  1.00 70.36           C  
ANISOU 1895  CD1 PHE C 257     8798   5709  12227    162  -1524  -1284       C  
ATOM   1896  CD2 PHE C 257       1.584  67.220 -39.705  1.00 60.84           C  
ANISOU 1896  CD2 PHE C 257     7604   4696  10815    160  -1387  -1145       C  
ATOM   1897  CE1 PHE C 257       1.287  69.944 -39.409  1.00 64.48           C  
ANISOU 1897  CE1 PHE C 257     8081   4891  11528    201  -1517  -1217       C  
ATOM   1898  CE2 PHE C 257       0.508  67.863 -40.287  1.00 58.66           C  
ANISOU 1898  CE2 PHE C 257     7353   4351  10582    199  -1379  -1077       C  
ATOM   1899  CZ  PHE C 257       0.360  69.227 -40.139  1.00 53.27           C  
ANISOU 1899  CZ  PHE C 257     6680   3536  10024    220  -1444  -1113       C  
ATOM   1900  N   GLU C 258       4.291  65.143 -35.321  1.00 78.72           N  
ANISOU 1900  N   GLU C 258     9818   7291  12799    263  -1495  -1662       N  
ATOM   1901  CA  GLU C 258       4.897  63.905 -34.862  1.00 84.43           C  
ANISOU 1901  CA  GLU C 258    10529   8148  13403    257  -1468  -1696       C  
ATOM   1902  C   GLU C 258       3.903  62.764 -35.031  1.00 83.10           C  
ANISOU 1902  C   GLU C 258    10389   8088  13097    308  -1396  -1652       C  
ATOM   1903  O   GLU C 258       2.698  62.939 -34.827  1.00 85.88           O  
ANISOU 1903  O   GLU C 258    10773   8446  13412    395  -1387  -1673       O  
ATOM   1904  CB  GLU C 258       5.308  64.025 -33.396  1.00 91.43           C  
ANISOU 1904  CB  GLU C 258    11409   9085  14244    332  -1533  -1870       C  
ATOM   1905  CG  GLU C 258       6.437  65.004 -33.138  1.00 97.00           C  
ANISOU 1905  CG  GLU C 258    12080   9696  15079    279  -1608  -1926       C  
ATOM   1906  CD  GLU C 258       6.637  65.282 -31.662  1.00102.85           C  
ANISOU 1906  CD  GLU C 258    12817  10480  15781    370  -1680  -2106       C  
ATOM   1907  OE1 GLU C 258       6.491  64.340 -30.846  1.00107.25           O  
ANISOU 1907  OE1 GLU C 258    13383  11175  16191    439  -1664  -2176       O  
ATOM   1908  OE2 GLU C 258       6.938  66.445 -31.299  1.00103.30           O  
ANISOU 1908  OE2 GLU C 258    12862  10435  15953    376  -1754  -2178       O  
ATOM   1909  N   SER C 259       4.410  61.599 -35.422  1.00 76.73           N  
ANISOU 1909  N   SER C 259     9569   7367  12219    253  -1346  -1589       N  
ATOM   1910  CA  SER C 259       3.550  60.435 -35.565  1.00 68.52           C  
ANISOU 1910  CA  SER C 259     8554   6431  11051    296  -1279  -1549       C  
ATOM   1911  C   SER C 259       3.035  59.984 -34.205  1.00 69.87           C  
ANISOU 1911  C   SER C 259     8745   6707  11093    416  -1294  -1687       C  
ATOM   1912  O   SER C 259       3.765  59.997 -33.210  1.00 70.45           O  
ANISOU 1912  O   SER C 259     8806   6823  11139    440  -1341  -1798       O  
ATOM   1913  CB  SER C 259       4.308  59.290 -36.240  1.00 68.36           C  
ANISOU 1913  CB  SER C 259     8511   6475  10986    209  -1230  -1461       C  
ATOM   1914  OG  SER C 259       4.287  59.417 -37.650  1.00 71.33           O  
ANISOU 1914  OG  SER C 259     8877   6789  11437    120  -1189  -1307       O  
ATOM   1915  N   MET C 260       1.762  59.595 -34.161  1.00 74.97           N  
ANISOU 1915  N   MET C 260     9422   7404  11659    496  -1253  -1676       N  
ATOM   1916  CA  MET C 260       1.219  58.918 -32.996  1.00 80.96           C  
ANISOU 1916  CA  MET C 260    10199   8290  12273    607  -1248  -1780       C  
ATOM   1917  C   MET C 260       0.276  57.826 -33.478  1.00 79.29           C  
ANISOU 1917  C   MET C 260    10006   8156  11965    631  -1171  -1699       C  
ATOM   1918  O   MET C 260      -0.485  58.038 -34.437  1.00 79.43           O  
ANISOU 1918  O   MET C 260    10033   8115  12033    614  -1136  -1599       O  
ATOM   1919  CB  MET C 260       0.485  59.862 -32.031  1.00 89.01           C  
ANISOU 1919  CB  MET C 260    11233   9298  13290    718  -1295  -1898       C  
ATOM   1920  CG  MET C 260      -0.285  60.997 -32.675  1.00 97.52           C  
ANISOU 1920  CG  MET C 260    12321  10252  14479    724  -1305  -1853       C  
ATOM   1921  SD  MET C 260      -0.893  62.143 -31.420  1.00105.33           S  
ANISOU 1921  SD  MET C 260    13322  11229  15471    852  -1375  -2014       S  
ATOM   1922  CE  MET C 260      -2.110  63.072 -32.347  1.00100.68           C  
ANISOU 1922  CE  MET C 260    12752  10525  14976    872  -1360  -1932       C  
ATOM   1923  N   PRO C 261       0.317  56.652 -32.847  1.00 73.54           N  
ANISOU 1923  N   PRO C 261     9283   7558  11101    670  -1145  -1736       N  
ATOM   1924  CA  PRO C 261      -0.490  55.521 -33.325  1.00 69.29           C  
ANISOU 1924  CA  PRO C 261     8758   7092  10475    686  -1072  -1657       C  
ATOM   1925  C   PRO C 261      -1.979  55.799 -33.174  1.00 67.84           C  
ANISOU 1925  C   PRO C 261     8595   6925  10256    789  -1047  -1663       C  
ATOM   1926  O   PRO C 261      -2.448  56.199 -32.106  1.00 71.27           O  
ANISOU 1926  O   PRO C 261     9037   7408  10633    891  -1072  -1771       O  
ATOM   1927  CB  PRO C 261      -0.036  54.359 -32.434  1.00 69.58           C  
ANISOU 1927  CB  PRO C 261     8797   7266  10377    719  -1064  -1719       C  
ATOM   1928  CG  PRO C 261       0.486  55.017 -31.197  1.00 71.19           C  
ANISOU 1928  CG  PRO C 261     8994   7491  10565    773  -1130  -1855       C  
ATOM   1929  CD  PRO C 261       1.111  56.303 -31.657  1.00 72.71           C  
ANISOU 1929  CD  PRO C 261     9168   7541  10916    704  -1182  -1851       C  
ATOM   1930  N   ASN C 262      -2.716  55.580 -34.259  1.00 62.49           N  
ANISOU 1930  N   ASN C 262     7921   6212   9610    764   -997  -1545       N  
ATOM   1931  CA  ASN C 262      -4.150  55.825 -34.304  1.00 61.68           C  
ANISOU 1931  CA  ASN C 262     7831   6123   9484    854   -968  -1531       C  
ATOM   1932  C   ASN C 262      -4.893  54.645 -33.690  1.00 63.36           C  
ANISOU 1932  C   ASN C 262     8048   6484   9543    941   -917  -1553       C  
ATOM   1933  O   ASN C 262      -4.844  53.532 -34.229  1.00 61.87           O  
ANISOU 1933  O   ASN C 262     7855   6342   9311    901   -870  -1474       O  
ATOM   1934  CB  ASN C 262      -4.598  56.063 -35.749  1.00 60.41           C  
ANISOU 1934  CB  ASN C 262     7666   5868   9419    791   -938  -1388       C  
ATOM   1935  CG  ASN C 262      -6.084  56.354 -35.869  1.00 61.89           C  
ANISOU 1935  CG  ASN C 262     7861   6067   9590    884   -909  -1366       C  
ATOM   1936  OD1 ASN C 262      -6.781  56.541 -34.871  1.00 64.08           O  
ANISOU 1936  OD1 ASN C 262     8143   6412   9793    996   -915  -1463       O  
ATOM   1937  ND2 ASN C 262      -6.576  56.399 -37.102  1.00 60.59           N  
ANISOU 1937  ND2 ASN C 262     7691   5843   9489    840   -878  -1235       N  
ATOM   1938  N   PRO C 263      -5.592  54.848 -32.570  1.00 66.99           N  
ANISOU 1938  N   PRO C 263     8512   7027   9913   1061   -922  -1654       N  
ATOM   1939  CA  PRO C 263      -6.339  53.736 -31.958  1.00 63.72           C  
ANISOU 1939  CA  PRO C 263     8097   6769   9344   1149   -867  -1666       C  
ATOM   1940  C   PRO C 263      -7.430  53.172 -32.849  1.00 56.82           C  
ANISOU 1940  C   PRO C 263     7211   5937   8442   1142   -792  -1528       C  
ATOM   1941  O   PRO C 263      -7.841  52.022 -32.646  1.00 60.76           O  
ANISOU 1941  O   PRO C 263     7698   6587   8801   1148   -726  -1464       O  
ATOM   1942  CB  PRO C 263      -6.922  54.365 -30.684  1.00 66.22           C  
ANISOU 1942  CB  PRO C 263     8414   7160   9586   1272   -890  -1789       C  
ATOM   1943  CG  PRO C 263      -6.965  55.839 -30.975  1.00 67.60           C  
ANISOU 1943  CG  PRO C 263     8593   7197   9895   1259   -944  -1811       C  
ATOM   1944  CD  PRO C 263      -5.756  56.108 -31.823  1.00 65.65           C  
ANISOU 1944  CD  PRO C 263     8346   6819   9778   1124   -978  -1757       C  
ATOM   1945  N   GLU C 264      -7.912  53.939 -33.825  1.00 57.97           N  
ANISOU 1945  N   GLU C 264     7355   5966   8704   1119   -796  -1463       N  
ATOM   1946  CA  GLU C 264      -8.935  53.482 -34.753  1.00 59.30           C  
ANISOU 1946  CA  GLU C 264     7506   6182   8842   1098   -725  -1315       C  
ATOM   1947  C   GLU C 264      -8.362  52.979 -36.072  1.00 54.80           C  
ANISOU 1947  C   GLU C 264     6930   5569   8323    958   -699  -1169       C  
ATOM   1948  O   GLU C 264      -9.133  52.630 -36.971  1.00 55.86           O  
ANISOU 1948  O   GLU C 264     7049   5733   8441    930   -647  -1045       O  
ATOM   1949  CB  GLU C 264      -9.935  54.611 -35.026  1.00 68.63           C  
ANISOU 1949  CB  GLU C 264     8688   7278  10109   1172   -744  -1328       C  
ATOM   1950  CG  GLU C 264     -10.654  55.130 -33.789  1.00 79.14           C  
ANISOU 1950  CG  GLU C 264    10021   8662  11386   1324   -765  -1472       C  
ATOM   1951  CD  GLU C 264     -11.718  54.174 -33.284  1.00 87.03           C  
ANISOU 1951  CD  GLU C 264    10995   9858  12215   1391   -688  -1438       C  
ATOM   1952  OE1 GLU C 264     -11.360  53.100 -32.754  1.00 89.55           O  
ANISOU 1952  OE1 GLU C 264    11309  10304  12412   1371   -653  -1429       O  
ATOM   1953  OE2 GLU C 264     -12.916  54.495 -33.423  1.00 88.61           O  
ANISOU 1953  OE2 GLU C 264    11177  10085  12404   1465   -662  -1416       O  
ATOM   1954  N   GLY C 265      -7.038  52.933 -36.209  1.00 48.74           N  
ANISOU 1954  N   GLY C 265     6169   4740   7610    872   -735  -1185       N  
ATOM   1955  CA  GLY C 265      -6.439  52.559 -37.472  1.00 44.71           C  
ANISOU 1955  CA  GLY C 265     5648   4187   7151    745   -713  -1054       C  
ATOM   1956  C   GLY C 265      -6.735  51.124 -37.862  1.00 48.40           C  
ANISOU 1956  C   GLY C 265     6100   4796   7492    704   -639   -946       C  
ATOM   1957  O   GLY C 265      -6.989  50.254 -37.030  1.00 50.18           O  
ANISOU 1957  O   GLY C 265     6325   5150   7590    751   -610   -977       O  
ATOM   1958  N   ARG C 266      -6.705  50.878 -39.170  1.00 39.08           N  
ANISOU 1958  N   ARG C 266     4908   3591   6351    615   -609   -813       N  
ATOM   1959  CA  ARG C 266      -6.998  49.560 -39.709  1.00 29.60           C  
ANISOU 1959  CA  ARG C 266     3691   2509   5048    570   -544   -707       C  
ATOM   1960  C   ARG C 266      -6.046  49.246 -40.850  1.00 37.59           C  
ANISOU 1960  C   ARG C 266     4692   3481   6109    451   -540   -618       C  
ATOM   1961  O   ARG C 266      -5.451  50.137 -41.460  1.00 41.47           O  
ANISOU 1961  O   ARG C 266     5182   3854   6719    402   -575   -603       O  
ATOM   1962  CB  ARG C 266      -8.441  49.444 -40.219  1.00 35.23           C  
ANISOU 1962  CB  ARG C 266     4390   3271   5724    609   -496   -625       C  
ATOM   1963  CG  ARG C 266      -9.509  49.625 -39.163  1.00 40.07           C  
ANISOU 1963  CG  ARG C 266     5003   3949   6272    728   -488   -698       C  
ATOM   1964  CD  ARG C 266      -9.532  48.461 -38.191  1.00 45.14           C  
ANISOU 1964  CD  ARG C 266     5643   4733   6774    756   -456   -730       C  
ATOM   1965  NE  ARG C 266     -10.624  48.600 -37.234  1.00 46.95           N  
ANISOU 1965  NE  ARG C 266     5865   5043   6931    871   -439   -786       N  
ATOM   1966  CZ  ARG C 266     -10.480  49.090 -36.008  1.00 48.41           C  
ANISOU 1966  CZ  ARG C 266     6063   5238   7092    958   -472   -916       C  
ATOM   1967  NH1 ARG C 266      -9.284  49.482 -35.587  1.00 41.90           N  
ANISOU 1967  NH1 ARG C 266     5260   4342   6316    940   -529  -1006       N  
ATOM   1968  NH2 ARG C 266     -11.529  49.188 -35.203  1.00 52.94           N  
ANISOU 1968  NH2 ARG C 266     6624   5900   7592   1065   -450   -960       N  
ATOM   1969  N   TYR C 267      -5.921  47.954 -41.126  1.00 38.90           N  
ANISOU 1969  N   TYR C 267     4847   3750   6182    407   -497   -556       N  
ATOM   1970  CA  TYR C 267      -5.212  47.458 -42.291  1.00 36.72           C  
ANISOU 1970  CA  TYR C 267     4555   3469   5928    304   -481   -462       C  
ATOM   1971  C   TYR C 267      -6.200  47.219 -43.421  1.00 41.55           C  
ANISOU 1971  C   TYR C 267     5150   4110   6526    287   -437   -342       C  
ATOM   1972  O   TYR C 267      -7.331  46.777 -43.190  1.00 39.98           O  
ANISOU 1972  O   TYR C 267     4948   3987   6255    340   -404   -325       O  
ATOM   1973  CB  TYR C 267      -4.481  46.156 -41.963  1.00 38.19           C  
ANISOU 1973  CB  TYR C 267     4739   3748   6022    271   -466   -472       C  
ATOM   1974  CG  TYR C 267      -3.337  46.341 -41.005  1.00 36.79           C  
ANISOU 1974  CG  TYR C 267     4573   3546   5861    276   -513   -582       C  
ATOM   1975  CD1 TYR C 267      -3.562  46.430 -39.640  1.00 34.81           C  
ANISOU 1975  CD1 TYR C 267     4340   3328   5558    362   -532   -688       C  
ATOM   1976  CD2 TYR C 267      -2.030  46.429 -41.463  1.00 33.86           C  
ANISOU 1976  CD2 TYR C 267     4189   3124   5550    197   -538   -581       C  
ATOM   1977  CE1 TYR C 267      -2.520  46.608 -38.757  1.00 40.37           C  
ANISOU 1977  CE1 TYR C 267     5052   4014   6272    371   -580   -795       C  
ATOM   1978  CE2 TYR C 267      -0.979  46.604 -40.589  1.00 35.14           C  
ANISOU 1978  CE2 TYR C 267     4356   3266   5729    201   -585   -685       C  
ATOM   1979  CZ  TYR C 267      -1.230  46.693 -39.236  1.00 40.84           C  
ANISOU 1979  CZ  TYR C 267     5098   4019   6399    289   -608   -794       C  
ATOM   1980  OH  TYR C 267      -0.185  46.868 -38.360  1.00 44.86           O  
ANISOU 1980  OH  TYR C 267     5611   4513   6920    296   -660   -902       O  
ATOM   1981  N   THR C 268      -5.773  47.522 -44.642  1.00 39.90           N  
ANISOU 1981  N   THR C 268     4927   3847   6386    212   -437   -258       N  
ATOM   1982  CA  THR C 268      -6.540  47.129 -45.812  1.00 33.75           C  
ANISOU 1982  CA  THR C 268     4129   3112   5582    186   -397   -142       C  
ATOM   1983  C   THR C 268      -6.322  45.646 -46.068  1.00 36.46           C  
ANISOU 1983  C   THR C 268     4461   3567   5826    144   -362   -106       C  
ATOM   1984  O   THR C 268      -5.198  45.144 -45.980  1.00 39.94           O  
ANISOU 1984  O   THR C 268     4901   4019   6257     96   -371   -131       O  
ATOM   1985  CB  THR C 268      -6.136  47.943 -47.042  1.00 32.00           C  
ANISOU 1985  CB  THR C 268     3894   2805   5458    124   -408    -58       C  
ATOM   1986  OG1 THR C 268      -4.747  47.733 -47.321  1.00 37.43           O  
ANISOU 1986  OG1 THR C 268     4573   3478   6172     45   -420    -59       O  
ATOM   1987  CG2 THR C 268      -6.378  49.425 -46.812  1.00 23.33           C  
ANISOU 1987  CG2 THR C 268     2810   1581   4471    165   -447    -88       C  
ATOM   1988  N   PHE C 269      -7.412  44.939 -46.360  1.00 37.12           N  
ANISOU 1988  N   PHE C 269     4533   3731   5839    165   -324    -53       N  
ATOM   1989  CA  PHE C 269      -7.364  43.503 -46.624  1.00 31.07           C  
ANISOU 1989  CA  PHE C 269     3756   3064   4985    130   -294    -18       C  
ATOM   1990  C   PHE C 269      -8.490  43.215 -47.611  1.00 35.56           C  
ANISOU 1990  C   PHE C 269     4302   3680   5531    127   -264     73       C  
ATOM   1991  O   PHE C 269      -9.660  43.151 -47.218  1.00 42.59           O  
ANISOU 1991  O   PHE C 269     5188   4609   6387    183   -246     75       O  
ATOM   1992  CB  PHE C 269      -7.511  42.690 -45.345  1.00 29.67           C  
ANISOU 1992  CB  PHE C 269     3592   2954   4727    175   -287    -85       C  
ATOM   1993  CG  PHE C 269      -7.717  41.215 -45.582  1.00 34.21           C  
ANISOU 1993  CG  PHE C 269     4156   3623   5219    147   -257    -42       C  
ATOM   1994  CD1 PHE C 269      -6.759  40.461 -46.234  1.00 38.98           C  
ANISOU 1994  CD1 PHE C 269     4755   4243   5814     80   -260    -19       C  
ATOM   1995  CD2 PHE C 269      -8.868  40.586 -45.148  1.00 35.61           C  
ANISOU 1995  CD2 PHE C 269     4326   3874   5331    188   -228    -25       C  
ATOM   1996  CE1 PHE C 269      -6.950  39.114 -46.446  1.00 39.25           C  
ANISOU 1996  CE1 PHE C 269     4781   4353   5781     57   -239     14       C  
ATOM   1997  CE2 PHE C 269      -9.059  39.242 -45.358  1.00 35.92           C  
ANISOU 1997  CE2 PHE C 269     4355   3987   5306    158   -206     15       C  
ATOM   1998  CZ  PHE C 269      -8.100  38.502 -46.009  1.00 36.84           C  
ANISOU 1998  CZ  PHE C 269     4470   4108   5419     93   -214     32       C  
ATOM   1999  N   GLY C 270      -8.128  43.047 -48.880  1.00 27.75           N  
ANISOU 1999  N   GLY C 270     3295   2694   4556     64   -258    147       N  
ATOM   2000  CA  GLY C 270      -9.141  43.005 -49.918  1.00 24.57           C  
ANISOU 2000  CA  GLY C 270     2869   2325   4143     63   -238    233       C  
ATOM   2001  C   GLY C 270      -9.920  44.303 -49.908  1.00 39.32           C  
ANISOU 2001  C   GLY C 270     4740   4126   6075    115   -248    245       C  
ATOM   2002  O   GLY C 270      -9.349  45.400 -49.910  1.00 40.60           O  
ANISOU 2002  O   GLY C 270     4914   4193   6320    112   -275    233       O  
ATOM   2003  N   ALA C 271     -11.245  44.184 -49.876  1.00 35.51           N  
ANISOU 2003  N   ALA C 271     4243   3691   5559    165   -230    267       N  
ATOM   2004  CA  ALA C 271     -12.135  45.329 -49.746  1.00 31.35           C  
ANISOU 2004  CA  ALA C 271     3717   3111   5084    230   -240    270       C  
ATOM   2005  C   ALA C 271     -12.595  45.537 -48.305  1.00 35.87           C  
ANISOU 2005  C   ALA C 271     4303   3685   5640    308   -242    178       C  
ATOM   2006  O   ALA C 271     -13.706  46.025 -48.069  1.00 31.69           O  
ANISOU 2006  O   ALA C 271     3763   3163   5113    377   -237    177       O  
ATOM   2007  CB  ALA C 271     -13.337  45.168 -50.677  1.00 26.59           C  
ANISOU 2007  CB  ALA C 271     3082   2564   4457    242   -220    353       C  
ATOM   2008  N   SER C 272     -11.759  45.178 -47.332  1.00 43.74           N  
ANISOU 2008  N   SER C 272     5321   4683   6615    304   -251    100       N  
ATOM   2009  CA  SER C 272     -12.118  45.266 -45.924  1.00 47.61           C  
ANISOU 2009  CA  SER C 272     5824   5195   7072    379   -252     11       C  
ATOM   2010  C   SER C 272     -11.080  46.074 -45.158  1.00 42.21           C  
ANISOU 2010  C   SER C 272     5170   4422   6446    392   -294    -80       C  
ATOM   2011  O   SER C 272      -9.911  46.144 -45.548  1.00 45.86           O  
ANISOU 2011  O   SER C 272     5641   4832   6952    326   -314    -77       O  
ATOM   2012  CB  SER C 272     -12.241  43.871 -45.293  1.00 56.54           C  
ANISOU 2012  CB  SER C 272     6948   6436   8099    374   -222      0       C  
ATOM   2013  OG  SER C 272     -13.001  43.000 -46.110  1.00 70.92           O  
ANISOU 2013  OG  SER C 272     8739   8330   9876    342   -190     84       O  
ATOM   2014  N   CYS C 273     -11.526  46.696 -44.069  1.00 41.69           N  
ANISOU 2014  N   CYS C 273     5115   4345   6381    478   -307   -164       N  
ATOM   2015  CA  CYS C 273     -10.642  47.279 -43.068  1.00 41.59           C  
ANISOU 2015  CA  CYS C 273     5129   4272   6402    504   -348   -273       C  
ATOM   2016  C   CYS C 273     -10.666  46.378 -41.842  1.00 46.34           C  
ANISOU 2016  C   CYS C 273     5735   4977   6896    544   -331   -338       C  
ATOM   2017  O   CYS C 273     -11.743  46.065 -41.324  1.00 59.64           O  
ANISOU 2017  O   CYS C 273     7404   6745   8510    607   -299   -338       O  
ATOM   2018  CB  CYS C 273     -11.083  48.696 -42.697  1.00 32.54           C  
ANISOU 2018  CB  CYS C 273     3993   3034   5336    581   -384   -334       C  
ATOM   2019  SG  CYS C 273     -11.298  49.812 -44.101  1.00 36.07           S  
ANISOU 2019  SG  CYS C 273     4435   3360   5909    549   -403   -243       S  
ATOM   2020  N   VAL C 274      -9.489  45.945 -41.389  1.00 35.59           N  
ANISOU 2020  N   VAL C 274     4389   3615   5519    506   -349   -385       N  
ATOM   2021  CA  VAL C 274      -9.405  44.951 -40.324  1.00 38.17           C  
ANISOU 2021  CA  VAL C 274     4720   4044   5739    534   -332   -428       C  
ATOM   2022  C   VAL C 274      -8.400  45.391 -39.267  1.00 42.34           C  
ANISOU 2022  C   VAL C 274     5272   4538   6279    564   -378   -547       C  
ATOM   2023  O   VAL C 274      -7.462  46.143 -39.544  1.00 39.35           O  
ANISOU 2023  O   VAL C 274     4903   4056   5991    527   -423   -581       O  
ATOM   2024  CB  VAL C 274      -9.039  43.551 -40.872  1.00 34.32           C  
ANISOU 2024  CB  VAL C 274     4223   3623   5193    457   -302   -351       C  
ATOM   2025  CG1 VAL C 274     -10.080  43.082 -41.880  1.00 27.65           C  
ANISOU 2025  CG1 VAL C 274     3352   2819   4334    431   -261   -244       C  
ATOM   2026  CG2 VAL C 274      -7.646  43.560 -41.494  1.00 33.47           C  
ANISOU 2026  CG2 VAL C 274     4124   3449   5143    375   -331   -349       C  
ATOM   2027  N   THR C 275      -8.600  44.897 -38.042  1.00 45.79           N  
ANISOU 2027  N   THR C 275     5714   5065   6619    629   -369   -607       N  
ATOM   2028  CA  THR C 275      -7.751  45.295 -36.922  1.00 47.40           C  
ANISOU 2028  CA  THR C 275     5939   5254   6819    672   -415   -729       C  
ATOM   2029  C   THR C 275      -6.369  44.655 -37.012  1.00 46.83           C  
ANISOU 2029  C   THR C 275     5875   5171   6746    598   -436   -734       C  
ATOM   2030  O   THR C 275      -5.362  45.288 -36.672  1.00 41.64           O  
ANISOU 2030  O   THR C 275     5229   4445   6146    592   -489   -819       O  
ATOM   2031  CB  THR C 275      -8.441  44.936 -35.604  1.00 46.41           C  
ANISOU 2031  CB  THR C 275     5812   5244   6576    771   -394   -784       C  
ATOM   2032  OG1 THR C 275      -9.558  45.811 -35.398  1.00 48.00           O  
ANISOU 2032  OG1 THR C 275     6005   5442   6793    854   -389   -811       O  
ATOM   2033  CG2 THR C 275      -7.486  45.057 -34.424  1.00 45.81           C  
ANISOU 2033  CG2 THR C 275     5756   5181   6468    812   -440   -904       C  
ATOM   2034  N   ALA C 276      -6.299  43.409 -37.474  1.00 49.97           N  
ANISOU 2034  N   ALA C 276     6265   5635   7086    541   -399   -648       N  
ATOM   2035  CA  ALA C 276      -5.035  42.706 -37.633  1.00 48.99           C  
ANISOU 2035  CA  ALA C 276     6145   5510   6958    474   -416   -647       C  
ATOM   2036  C   ALA C 276      -5.074  41.906 -38.925  1.00 50.10           C  
ANISOU 2036  C   ALA C 276     6271   5658   7107    389   -382   -531       C  
ATOM   2037  O   ALA C 276      -6.132  41.409 -39.321  1.00 51.29           O  
ANISOU 2037  O   ALA C 276     6410   5859   7220    392   -339   -455       O  
ATOM   2038  CB  ALA C 276      -4.753  41.774 -36.448  1.00 44.72           C  
ANISOU 2038  CB  ALA C 276     5616   5067   6307    515   -413   -689       C  
ATOM   2039  N   CYS C 277      -3.925  41.795 -39.582  1.00 46.57           N  
ANISOU 2039  N   CYS C 277     5820   5165   6709    315   -404   -522       N  
ATOM   2040  CA  CYS C 277      -3.848  40.976 -40.781  1.00 49.40           C  
ANISOU 2040  CA  CYS C 277     6163   5541   7067    240   -376   -425       C  
ATOM   2041  C   CYS C 277      -4.128  39.520 -40.420  1.00 42.04           C  
ANISOU 2041  C   CYS C 277     5234   4708   6033    246   -347   -391       C  
ATOM   2042  O   CYS C 277      -3.641  39.030 -39.394  1.00 46.51           O  
ANISOU 2042  O   CYS C 277     5814   5315   6542    278   -360   -445       O  
ATOM   2043  CB  CYS C 277      -2.475  41.104 -41.443  1.00 57.51           C  
ANISOU 2043  CB  CYS C 277     7180   6515   8156    167   -404   -430       C  
ATOM   2044  SG  CYS C 277      -2.155  42.723 -42.189  1.00 70.76           S  
ANISOU 2044  SG  CYS C 277     8847   8068   9971    134   -433   -432       S  
ATOM   2045  N   PRO C 278      -4.911  38.805 -41.223  1.00 36.31           N  
ANISOU 2045  N   PRO C 278     4493   4018   5283    218   -309   -302       N  
ATOM   2046  CA  PRO C 278      -5.255  37.421 -40.881  1.00 38.67           C  
ANISOU 2046  CA  PRO C 278     4795   4401   5498    221   -284   -265       C  
ATOM   2047  C   PRO C 278      -4.041  36.505 -40.963  1.00 41.73           C  
ANISOU 2047  C   PRO C 278     5188   4798   5868    178   -303   -275       C  
ATOM   2048  O   PRO C 278      -2.968  36.871 -41.448  1.00 27.89           O  
ANISOU 2048  O   PRO C 278     3431   2997   4167    138   -330   -301       O  
ATOM   2049  CB  PRO C 278      -6.312  37.048 -41.923  1.00 38.33           C  
ANISOU 2049  CB  PRO C 278     4730   4377   5458    191   -249   -173       C  
ATOM   2050  CG  PRO C 278      -6.027  37.944 -43.079  1.00 42.73           C  
ANISOU 2050  CG  PRO C 278     5274   4864   6096    150   -261   -154       C  
ATOM   2051  CD  PRO C 278      -5.529  39.235 -42.489  1.00 40.98           C  
ANISOU 2051  CD  PRO C 278     5066   4578   5928    183   -292   -230       C  
ATOM   2052  N   TYR C 279      -4.234  35.282 -40.472  1.00 47.40           N  
ANISOU 2052  N   TYR C 279     5914   5581   6515    187   -289   -250       N  
ATOM   2053  CA  TYR C 279      -3.138  34.327 -40.375  1.00 38.32           C  
ANISOU 2053  CA  TYR C 279     4773   4445   5341    160   -310   -264       C  
ATOM   2054  C   TYR C 279      -2.535  34.054 -41.749  1.00 38.16           C  
ANISOU 2054  C   TYR C 279     4736   4395   5369     89   -316   -230       C  
ATOM   2055  O   TYR C 279      -3.259  33.849 -42.728  1.00 33.92           O  
ANISOU 2055  O   TYR C 279     4182   3860   4846     58   -292   -165       O  
ATOM   2056  CB  TYR C 279      -3.627  33.024 -39.739  1.00 35.17           C  
ANISOU 2056  CB  TYR C 279     4385   4113   4866    179   -291   -224       C  
ATOM   2057  CG  TYR C 279      -2.521  32.032 -39.446  1.00 40.97           C  
ANISOU 2057  CG  TYR C 279     5133   4861   5572    167   -318   -243       C  
ATOM   2058  CD1 TYR C 279      -1.932  31.974 -38.189  1.00 39.98           C  
ANISOU 2058  CD1 TYR C 279     5027   4763   5398    217   -340   -300       C  
ATOM   2059  CD2 TYR C 279      -2.069  31.152 -40.423  1.00 39.17           C  
ANISOU 2059  CD2 TYR C 279     4897   4623   5363    112   -324   -207       C  
ATOM   2060  CE1 TYR C 279      -0.921  31.070 -37.915  1.00 43.21           C  
ANISOU 2060  CE1 TYR C 279     5449   5186   5783    212   -367   -315       C  
ATOM   2061  CE2 TYR C 279      -1.059  30.250 -40.159  1.00 42.86           C  
ANISOU 2061  CE2 TYR C 279     5377   5101   5807    107   -351   -227       C  
ATOM   2062  CZ  TYR C 279      -0.490  30.211 -38.904  1.00 47.60           C  
ANISOU 2062  CZ  TYR C 279     5997   5725   6363    157   -372   -279       C  
ATOM   2063  OH  TYR C 279       0.514  29.311 -38.638  1.00 58.27           O  
ANISOU 2063  OH  TYR C 279     7360   7089   7692    157   -402   -297       O  
ATOM   2064  N   ASN C 280      -1.201  34.065 -41.807  1.00 30.74           N  
ANISOU 2064  N   ASN C 280     3796   3434   4451     66   -347   -276       N  
ATOM   2065  CA  ASN C 280      -0.345  33.786 -42.969  1.00 42.67           C  
ANISOU 2065  CA  ASN C 280     5287   4929   5998      5   -357   -259       C  
ATOM   2066  C   ASN C 280      -0.196  34.982 -43.903  1.00 42.29           C  
ANISOU 2066  C   ASN C 280     5216   4827   6024    -31   -356   -249       C  
ATOM   2067  O   ASN C 280       0.418  34.841 -44.974  1.00 47.62           O  
ANISOU 2067  O   ASN C 280     5868   5499   6726    -82   -357   -224       O  
ATOM   2068  CB  ASN C 280      -0.816  32.578 -43.788  1.00 47.22           C  
ANISOU 2068  CB  ASN C 280     5856   5540   6546    -24   -337   -193       C  
ATOM   2069  CG  ASN C 280       0.327  31.870 -44.487  1.00 48.29           C  
ANISOU 2069  CG  ASN C 280     5979   5684   6687    -63   -356   -203       C  
ATOM   2070  OD1 ASN C 280       1.394  31.671 -43.908  1.00 53.87           O  
ANISOU 2070  OD1 ASN C 280     6691   6393   7386    -54   -384   -256       O  
ATOM   2071  ND2 ASN C 280       0.113  31.496 -45.744  1.00 45.17           N  
ANISOU 2071  ND2 ASN C 280     5561   5297   6303   -103   -344   -154       N  
ATOM   2072  N   TYR C 281      -0.713  36.150 -43.544  1.00 42.00           N  
ANISOU 2072  N   TYR C 281     5184   4751   6023     -3   -356   -266       N  
ATOM   2073  CA  TYR C 281      -0.467  37.363 -44.308  1.00 40.65           C  
ANISOU 2073  CA  TYR C 281     4995   4517   5934    -36   -363   -257       C  
ATOM   2074  C   TYR C 281       0.577  38.228 -43.612  1.00 39.06           C  
ANISOU 2074  C   TYR C 281     4796   4266   5781    -31   -402   -338       C  
ATOM   2075  O   TYR C 281       0.850  38.083 -42.418  1.00 40.35           O  
ANISOU 2075  O   TYR C 281     4979   4445   5909     14   -424   -408       O  
ATOM   2076  CB  TYR C 281      -1.759  38.159 -44.515  1.00 42.60           C  
ANISOU 2076  CB  TYR C 281     5244   4740   6204    -11   -342   -218       C  
ATOM   2077  CG  TYR C 281      -2.650  37.589 -45.595  1.00 51.66           C  
ANISOU 2077  CG  TYR C 281     6376   5923   7331    -35   -309   -131       C  
ATOM   2078  CD1 TYR C 281      -3.441  36.475 -45.351  1.00 50.41           C  
ANISOU 2078  CD1 TYR C 281     6223   5827   7103    -16   -287   -105       C  
ATOM   2079  CD2 TYR C 281      -2.690  38.157 -46.862  1.00 57.46           C  
ANISOU 2079  CD2 TYR C 281     7086   6630   8115    -77   -301    -72       C  
ATOM   2080  CE1 TYR C 281      -4.253  35.946 -46.336  1.00 55.32           C  
ANISOU 2080  CE1 TYR C 281     6827   6480   7710    -39   -263    -33       C  
ATOM   2081  CE2 TYR C 281      -3.500  37.637 -47.854  1.00 56.81           C  
ANISOU 2081  CE2 TYR C 281     6988   6588   8009    -95   -275      1       C  
ATOM   2082  CZ  TYR C 281      -4.278  36.530 -47.584  1.00 60.45           C  
ANISOU 2082  CZ  TYR C 281     7454   7108   8405    -76   -259     16       C  
ATOM   2083  OH  TYR C 281      -5.086  36.004 -48.565  1.00 66.82           O  
ANISOU 2083  OH  TYR C 281     8242   7953   9193    -95   -239     81       O  
ATOM   2084  N   LEU C 282       1.168  39.131 -44.385  1.00 31.28           N  
ANISOU 2084  N   LEU C 282     3787   3222   4875    -78   -414   -326       N  
ATOM   2085  CA  LEU C 282       2.190  40.038 -43.888  1.00 44.08           C  
ANISOU 2085  CA  LEU C 282     5403   4784   6563    -88   -455   -398       C  
ATOM   2086  C   LEU C 282       1.593  41.415 -43.630  1.00 47.89           C  
ANISOU 2086  C   LEU C 282     5894   5186   7115    -61   -468   -416       C  
ATOM   2087  O   LEU C 282       0.816  41.928 -44.440  1.00 51.12           O  
ANISOU 2087  O   LEU C 282     6298   5566   7560    -73   -446   -347       O  
ATOM   2088  CB  LEU C 282       3.341  40.148 -44.888  1.00 50.40           C  
ANISOU 2088  CB  LEU C 282     6165   5570   7416   -164   -461   -370       C  
ATOM   2089  CG  LEU C 282       4.082  38.850 -45.219  1.00 50.28           C  
ANISOU 2089  CG  LEU C 282     6135   5630   7340   -188   -453   -361       C  
ATOM   2090  CD1 LEU C 282       4.739  38.944 -46.586  1.00 46.33           C  
ANISOU 2090  CD1 LEU C 282     5591   5133   6878   -259   -439   -299       C  
ATOM   2091  CD2 LEU C 282       5.119  38.552 -44.151  1.00 51.10           C  
ANISOU 2091  CD2 LEU C 282     6243   5747   7427   -168   -492   -453       C  
ATOM   2092  N   SER C 283       1.951  42.005 -42.494  1.00 48.30           N  
ANISOU 2092  N   SER C 283     5961   5204   7188    -21   -507   -513       N  
ATOM   2093  CA  SER C 283       1.597  43.391 -42.235  1.00 45.55           C  
ANISOU 2093  CA  SER C 283     5619   4765   6922      2   -532   -548       C  
ATOM   2094  C   SER C 283       2.626  44.316 -42.872  1.00 46.80           C  
ANISOU 2094  C   SER C 283     5750   4836   7198    -69   -562   -545       C  
ATOM   2095  O   SER C 283       3.778  43.938 -43.100  1.00 52.68           O  
ANISOU 2095  O   SER C 283     6469   5596   7949   -121   -574   -552       O  
ATOM   2096  CB  SER C 283       1.499  43.655 -40.732  1.00 51.90           C  
ANISOU 2096  CB  SER C 283     6450   5573   7698     83   -567   -663       C  
ATOM   2097  OG  SER C 283       0.490  42.852 -40.145  1.00 61.15           O  
ANISOU 2097  OG  SER C 283     7642   6830   8761    148   -534   -654       O  
ATOM   2098  N   THR C 284       2.193  45.536 -43.172  1.00 55.67           N  
ANISOU 2098  N   THR C 284     6874   5865   8415    -70   -575   -530       N  
ATOM   2099  CA  THR C 284       3.027  46.512 -43.852  1.00 56.93           C  
ANISOU 2099  CA  THR C 284     7005   5929   8697   -142   -600   -507       C  
ATOM   2100  C   THR C 284       3.033  47.798 -43.038  1.00 60.58           C  
ANISOU 2100  C   THR C 284     7483   6281   9255   -107   -656   -597       C  
ATOM   2101  O   THR C 284       2.082  48.086 -42.309  1.00 61.48           O  
ANISOU 2101  O   THR C 284     7628   6388   9346    -26   -662   -647       O  
ATOM   2102  CB  THR C 284       2.512  46.771 -45.285  1.00 56.33           C  
ANISOU 2102  CB  THR C 284     6912   5834   8656   -190   -561   -373       C  
ATOM   2103  OG1 THR C 284       2.428  45.527 -45.991  1.00 54.50           O  
ANISOU 2103  OG1 THR C 284     6668   5711   8328   -212   -514   -303       O  
ATOM   2104  CG2 THR C 284       3.451  47.679 -46.054  1.00 64.10           C  
ANISOU 2104  CG2 THR C 284     7861   6732   9762   -274   -581   -330       C  
ATOM   2105  N   ASP C 285       4.130  48.553 -43.136  1.00 70.11           N  
ANISOU 2105  N   ASP C 285     8663   7405  10570   -168   -698   -625       N  
ATOM   2106  CA  ASP C 285       4.133  49.906 -42.588  1.00 74.23           C  
ANISOU 2106  CA  ASP C 285     9195   7798  11211   -147   -757   -700       C  
ATOM   2107  C   ASP C 285       3.097  50.774 -43.284  1.00 64.60           C  
ANISOU 2107  C   ASP C 285     7988   6498  10059   -137   -743   -620       C  
ATOM   2108  O   ASP C 285       2.481  51.640 -42.655  1.00 66.83           O  
ANISOU 2108  O   ASP C 285     8296   6703  10392    -72   -778   -687       O  
ATOM   2109  CB  ASP C 285       5.523  50.528 -42.722  1.00 89.73           C  
ANISOU 2109  CB  ASP C 285    11120   9682  13291   -231   -803   -726       C  
ATOM   2110  CG  ASP C 285       6.586  49.750 -41.971  1.00107.63           C  
ANISOU 2110  CG  ASP C 285    13371  12026  15497   -235   -825   -815       C  
ATOM   2111  OD1 ASP C 285       6.235  49.005 -41.035  1.00114.09           O  
ANISOU 2111  OD1 ASP C 285    14219  12930  16202   -157   -823   -887       O  
ATOM   2112  OD2 ASP C 285       7.778  49.885 -42.327  1.00110.71           O  
ANISOU 2112  OD2 ASP C 285    13718  12422  15926   -308   -832   -795       O  
ATOM   2113  N   VAL C 286       2.883  50.537 -44.579  1.00 60.85           N  
ANISOU 2113  N   VAL C 286     7493   6045   9580   -193   -693   -481       N  
ATOM   2114  CA  VAL C 286       1.875  51.244 -45.359  1.00 55.84           C  
ANISOU 2114  CA  VAL C 286     6868   5351   8997   -183   -676   -389       C  
ATOM   2115  C   VAL C 286       0.456  50.948 -44.884  1.00 47.49           C  
ANISOU 2115  C   VAL C 286     5846   4347   7852    -83   -653   -408       C  
ATOM   2116  O   VAL C 286      -0.482  51.667 -45.250  1.00 50.53           O  
ANISOU 2116  O   VAL C 286     6243   4674   8284    -50   -650   -362       O  
ATOM   2117  CB  VAL C 286       2.157  50.885 -46.838  1.00 59.09           C  
ANISOU 2117  CB  VAL C 286     7244   5803   9403   -269   -628   -240       C  
ATOM   2118  CG1 VAL C 286       0.942  51.058 -47.743  1.00 66.86           C  
ANISOU 2118  CG1 VAL C 286     8237   6791  10375   -248   -589   -129       C  
ATOM   2119  CG2 VAL C 286       3.347  51.690 -47.348  1.00 56.59           C  
ANISOU 2119  CG2 VAL C 286     6891   5395   9217   -363   -656   -208       C  
ATOM   2120  N   GLY C 287       0.276  49.936 -44.040  1.00 48.52           N  
ANISOU 2120  N   GLY C 287     5990   4585   7860    -30   -638   -475       N  
ATOM   2121  CA  GLY C 287      -1.043  49.635 -43.524  1.00 45.01           C  
ANISOU 2121  CA  GLY C 287     5571   4199   7331     62   -614   -493       C  
ATOM   2122  C   GLY C 287      -1.831  48.650 -44.353  1.00 43.05           C  
ANISOU 2122  C   GLY C 287     5315   4053   6989     54   -550   -384       C  
ATOM   2123  O   GLY C 287      -3.064  48.723 -44.386  1.00 39.04           O  
ANISOU 2123  O   GLY C 287     4818   3565   6450    111   -528   -357       O  
ATOM   2124  N   SER C 288      -1.156  47.723 -45.023  1.00 43.06           N  
ANISOU 2124  N   SER C 288     5296   4122   6945    -15   -523   -326       N  
ATOM   2125  CA  SER C 288      -1.799  46.746 -45.886  1.00 43.65           C  
ANISOU 2125  CA  SER C 288     5359   4289   6935    -30   -470   -228       C  
ATOM   2126  C   SER C 288      -1.443  45.336 -45.432  1.00 44.59           C  
ANISOU 2126  C   SER C 288     5479   4518   6944    -29   -451   -258       C  
ATOM   2127  O   SER C 288      -0.507  45.120 -44.657  1.00 52.24           O  
ANISOU 2127  O   SER C 288     6451   5491   7905    -32   -479   -338       O  
ATOM   2128  CB  SER C 288      -1.392  46.948 -47.352  1.00 47.27           C  
ANISOU 2128  CB  SER C 288     5788   4728   7445   -112   -453   -116       C  
ATOM   2129  OG  SER C 288       0.013  46.867 -47.514  1.00 52.65           O  
ANISOU 2129  OG  SER C 288     6447   5398   8160   -181   -470   -129       O  
ATOM   2130  N   CYS C 289      -2.219  44.374 -45.925  1.00 42.79           N  
ANISOU 2130  N   CYS C 289     5247   4377   6634    -25   -409   -193       N  
ATOM   2131  CA  CYS C 289      -1.985  42.952 -45.700  1.00 39.03           C  
ANISOU 2131  CA  CYS C 289     4771   4000   6059    -30   -389   -201       C  
ATOM   2132  C   CYS C 289      -1.700  42.324 -47.058  1.00 42.62           C  
ANISOU 2132  C   CYS C 289     5199   4494   6500    -98   -364   -111       C  
ATOM   2133  O   CYS C 289      -2.579  42.296 -47.926  1.00 47.31           O  
ANISOU 2133  O   CYS C 289     5783   5107   7085   -101   -337    -33       O  
ATOM   2134  CB  CYS C 289      -3.191  42.289 -45.032  1.00 40.70           C  
ANISOU 2134  CB  CYS C 289     5000   4279   6186     36   -365   -207       C  
ATOM   2135  SG  CYS C 289      -3.712  43.021 -43.460  1.00 49.26           S  
ANISOU 2135  SG  CYS C 289     6111   5340   7267    131   -388   -310       S  
ATOM   2136  N   THR C 290      -0.478  41.829 -47.247  1.00 47.93           N  
ANISOU 2136  N   THR C 290     5857   5187   7169   -146   -373   -126       N  
ATOM   2137  CA  THR C 290      -0.046  41.298 -48.534  1.00 51.60           C  
ANISOU 2137  CA  THR C 290     6290   5693   7621   -207   -353    -52       C  
ATOM   2138  C   THR C 290       0.548  39.904 -48.357  1.00 51.07           C  
ANISOU 2138  C   THR C 290     6221   5707   7477   -215   -349    -80       C  
ATOM   2139  O   THR C 290       0.709  39.400 -47.242  1.00 39.75           O  
ANISOU 2139  O   THR C 290     4809   4289   6004   -178   -364   -150       O  
ATOM   2140  CB  THR C 290       0.973  42.227 -49.206  1.00 52.10           C  
ANISOU 2140  CB  THR C 290     6324   5698   7772   -268   -367    -27       C  
ATOM   2141  OG1 THR C 290       2.063  42.475 -48.309  1.00 52.09           O  
ANISOU 2141  OG1 THR C 290     6324   5662   7806   -274   -403   -114       O  
ATOM   2142  CG2 THR C 290       0.321  43.547 -49.597  1.00 59.49           C  
ANISOU 2142  CG2 THR C 290     7262   6551   8790   -265   -369     22       C  
ATOM   2143  N   LEU C 291       0.870  39.278 -49.489  1.00 60.84           N  
ANISOU 2143  N   LEU C 291     7431   6996   8690   -259   -331    -24       N  
ATOM   2144  CA  LEU C 291       1.519  37.975 -49.533  1.00 54.91           C  
ANISOU 2144  CA  LEU C 291     6673   6314   7875   -270   -331    -47       C  
ATOM   2145  C   LEU C 291       2.959  38.050 -50.014  1.00 61.67           C  
ANISOU 2145  C   LEU C 291     7494   7177   8760   -320   -342    -57       C  
ATOM   2146  O   LEU C 291       3.634  37.017 -50.069  1.00 67.45           O  
ANISOU 2146  O   LEU C 291     8217   7966   9445   -326   -346    -83       O  
ATOM   2147  CB  LEU C 291       0.728  37.018 -50.435  1.00 41.82           C  
ANISOU 2147  CB  LEU C 291     5008   4723   6159   -272   -304     12       C  
ATOM   2148  CG  LEU C 291      -0.728  36.710 -50.039  1.00 41.99           C  
ANISOU 2148  CG  LEU C 291     5055   4755   6144   -227   -290     29       C  
ATOM   2149  CD1 LEU C 291      -1.507  36.181 -51.233  1.00 47.74           C  
ANISOU 2149  CD1 LEU C 291     5765   5534   6842   -242   -268     98       C  
ATOM   2150  CD2 LEU C 291      -0.771  35.706 -48.900  1.00 38.90           C  
ANISOU 2150  CD2 LEU C 291     4690   4390   5699   -191   -299    -26       C  
ATOM   2151  N   VAL C 292       3.434  39.241 -50.376  1.00 62.55           N  
ANISOU 2151  N   VAL C 292     7583   7232   8951   -357   -348    -35       N  
ATOM   2152  CA  VAL C 292       4.829  39.486 -50.719  1.00 66.09           C  
ANISOU 2152  CA  VAL C 292     7991   7681   9438   -409   -360    -45       C  
ATOM   2153  C   VAL C 292       5.199  40.869 -50.201  1.00 71.86           C  
ANISOU 2153  C   VAL C 292     8720   8313  10269   -425   -386    -69       C  
ATOM   2154  O   VAL C 292       4.361  41.773 -50.136  1.00 73.43           O  
ANISOU 2154  O   VAL C 292     8938   8447  10515   -409   -386    -43       O  
ATOM   2155  CB  VAL C 292       5.096  39.383 -52.239  1.00 70.39           C  
ANISOU 2155  CB  VAL C 292     8491   8280   9974   -459   -330     42       C  
ATOM   2156  CG1 VAL C 292       5.163  37.926 -52.669  1.00 75.78           C  
ANISOU 2156  CG1 VAL C 292     9167   9062  10565   -447   -317     35       C  
ATOM   2157  CG2 VAL C 292       4.019  40.123 -53.018  1.00 71.31           C  
ANISOU 2157  CG2 VAL C 292     8610   8370  10115   -461   -308    130       C  
ATOM   2158  N   CYS C 293       6.460  41.029 -49.816  1.00 73.09           N  
ANISOU 2158  N   CYS C 293     8851   8458  10462   -454   -412   -123       N  
ATOM   2159  CA  CYS C 293       6.900  42.299 -49.267  1.00 79.54           C  
ANISOU 2159  CA  CYS C 293     9663   9176  11383   -473   -446   -158       C  
ATOM   2160  C   CYS C 293       7.088  43.326 -50.376  1.00 93.85           C  
ANISOU 2160  C   CYS C 293    11438  10942  13280   -538   -432    -64       C  
ATOM   2161  O   CYS C 293       7.190  42.974 -51.555  1.00 98.29           O  
ANISOU 2161  O   CYS C 293    11967  11567  13811   -574   -396     20       O  
ATOM   2162  CB  CYS C 293       8.210  42.125 -48.505  1.00 70.83           C  
ANISOU 2162  CB  CYS C 293     8540   8079  10295   -486   -483   -248       C  
ATOM   2163  SG  CYS C 293       8.042  41.525 -46.810  1.00 72.14           S  
ANISOU 2163  SG  CYS C 293     8756   8254  10399   -403   -519   -372       S  
ATOM   2164  N   PRO C 294       7.131  44.615 -50.023  1.00 96.36           N  
ANISOU 2164  N   PRO C 294    11758  11148  13706   -553   -461    -74       N  
ATOM   2165  CA  PRO C 294       7.609  45.617 -50.984  1.00 97.34           C  
ANISOU 2165  CA  PRO C 294    11839  11220  13927   -627   -455     14       C  
ATOM   2166  C   PRO C 294       9.071  45.373 -51.323  1.00100.53           C  
ANISOU 2166  C   PRO C 294    12181  11671  14346   -694   -456     12       C  
ATOM   2167  O   PRO C 294       9.707  44.487 -50.743  1.00100.21           O  
ANISOU 2167  O   PRO C 294    12136  11693  14246   -676   -468    -68       O  
ATOM   2168  CB  PRO C 294       7.398  46.948 -50.250  1.00 97.28           C  
ANISOU 2168  CB  PRO C 294    11854  11071  14038   -619   -500    -26       C  
ATOM   2169  CG  PRO C 294       6.391  46.647 -49.181  1.00 95.88           C  
ANISOU 2169  CG  PRO C 294    11737  10889  13804   -527   -514   -109       C  
ATOM   2170  CD  PRO C 294       6.641  45.230 -48.778  1.00 95.96           C  
ANISOU 2170  CD  PRO C 294    11752  11013  13693   -497   -501   -162       C  
ATOM   2171  N   LEU C 295       9.627  46.156 -52.243  1.00103.80           N  
ANISOU 2171  N   LEU C 295    12545  12056  14838   -769   -444    102       N  
ATOM   2172  CA  LEU C 295      10.906  45.783 -52.833  1.00109.01           C  
ANISOU 2172  CA  LEU C 295    13135  12793  15490   -832   -429    124       C  
ATOM   2173  C   LEU C 295      12.105  46.177 -51.972  1.00106.64           C  
ANISOU 2173  C   LEU C 295    12804  12444  15270   -867   -477     33       C  
ATOM   2174  O   LEU C 295      13.104  45.446 -51.939  1.00104.83           O  
ANISOU 2174  O   LEU C 295    12534  12299  14999   -883   -476     -7       O  
ATOM   2175  CB  LEU C 295      11.010  46.387 -54.232  1.00112.51           C  
ANISOU 2175  CB  LEU C 295    13529  13247  15972   -900   -389    270       C  
ATOM   2176  CG  LEU C 295       9.858  45.823 -55.073  1.00106.70           C  
ANISOU 2176  CG  LEU C 295    12820  12582  15138   -857   -345    346       C  
ATOM   2177  CD1 LEU C 295       9.534  46.699 -56.275  1.00 99.76           C  
ANISOU 2177  CD1 LEU C 295    11916  11682  14308   -903   -315    493       C  
ATOM   2178  CD2 LEU C 295      10.157  44.389 -55.500  1.00103.46           C  
ANISOU 2178  CD2 LEU C 295    12391  12323  14598   -837   -316    327       C  
ATOM   2179  N   HIS C 296      12.038  47.310 -51.263  1.00105.55           N  
ANISOU 2179  N   HIS C 296    12685  12171  15249   -875   -523     -6       N  
ATOM   2180  CA  HIS C 296      13.076  47.686 -50.308  1.00111.32           C  
ANISOU 2180  CA  HIS C 296    13404  12872  16022   -880   -569   -109       C  
ATOM   2181  C   HIS C 296      12.800  47.155 -48.903  1.00104.81           C  
ANISOU 2181  C   HIS C 296    12629  12038  15156   -804   -614   -252       C  
ATOM   2182  O   HIS C 296      13.125  47.830 -47.917  1.00104.12           O  
ANISOU 2182  O   HIS C 296    12559  11887  15114   -781   -661   -341       O  
ATOM   2183  CB  HIS C 296      13.233  49.205 -50.260  1.00123.68           C  
ANISOU 2183  CB  HIS C 296    14972  14324  17695   -907   -590    -83       C  
ATOM   2184  CG  HIS C 296      13.902  49.788 -51.470  1.00129.09           C  
ANISOU 2184  CG  HIS C 296    15600  15025  18424   -990   -554     43       C  
ATOM   2185  ND1 HIS C 296      13.524  49.470 -52.767  1.00132.23           N  
ANISOU 2185  ND1 HIS C 296    15973  15487  18781  -1019   -497    173       N  
ATOM   2186  CD2 HIS C 296      14.915  50.682 -51.581  1.00126.82           C  
ANISOU 2186  CD2 HIS C 296    15271  14702  18214  -1050   -566     61       C  
ATOM   2187  CE1 HIS C 296      14.277  50.137 -53.624  1.00131.86           C  
ANISOU 2187  CE1 HIS C 296    15874  15448  18778  -1089   -473    268       C  
ATOM   2188  NE2 HIS C 296      15.129  50.878 -52.931  1.00128.48           N  
ANISOU 2188  NE2 HIS C 296    15434  14956  18426  -1113   -514    203       N  
ATOM   2189  N   ASN C 297      12.214  45.965 -48.783  1.00 97.84           N  
ANISOU 2189  N   ASN C 297    11777  11242  14155   -745   -592   -271       N  
ATOM   2190  CA  ASN C 297      11.714  45.476 -47.510  1.00 84.54           C  
ANISOU 2190  CA  ASN C 297    10152   9562  12407   -658   -622   -383       C  
ATOM   2191  C   ASN C 297      12.181  44.053 -47.248  1.00 72.13           C  
ANISOU 2191  C   ASN C 297     8577   8113  10717   -625   -612   -429       C  
ATOM   2192  O   ASN C 297      12.574  43.319 -48.158  1.00 65.27           O  
ANISOU 2192  O   ASN C 297     7672   7331   9797   -655   -574   -368       O  
ATOM   2193  CB  ASN C 297      10.183  45.528 -47.459  1.00 83.65           C  
ANISOU 2193  CB  ASN C 297    10102   9427  12254   -594   -600   -352       C  
ATOM   2194  CG  ASN C 297       9.659  46.920 -47.189  1.00 90.10           C  
ANISOU 2194  CG  ASN C 297    10940  10109  13185   -593   -631   -357       C  
ATOM   2195  OD1 ASN C 297       9.181  47.211 -46.094  1.00 92.19           O  
ANISOU 2195  OD1 ASN C 297    11248  10326  13453   -528   -667   -449       O  
ATOM   2196  ND2 ASN C 297       9.763  47.795 -48.182  1.00 90.80           N  
ANISOU 2196  ND2 ASN C 297    10996  10136  13367   -661   -618   -257       N  
ATOM   2197  N   GLN C 298      12.125  43.673 -45.972  1.00 68.44           N  
ANISOU 2197  N   GLN C 298     8149   7652  10205   -558   -649   -539       N  
ATOM   2198  CA  GLN C 298      12.423  42.315 -45.547  1.00 60.67           C  
ANISOU 2198  CA  GLN C 298     7173   6771   9107   -514   -646   -585       C  
ATOM   2199  C   GLN C 298      11.357  41.855 -44.563  1.00 61.41           C  
ANISOU 2199  C   GLN C 298     7337   6874   9122   -423   -651   -632       C  
ATOM   2200  O   GLN C 298      10.680  42.665 -43.921  1.00 67.44           O  
ANISOU 2200  O   GLN C 298     8135   7565   9923   -390   -671   -666       O  
ATOM   2201  CB  GLN C 298      13.814  42.214 -44.912  1.00 63.61           C  
ANISOU 2201  CB  GLN C 298     7505   7163   9502   -530   -693   -675       C  
ATOM   2202  CG  GLN C 298      14.016  43.132 -43.718  1.00 77.94           C  
ANISOU 2202  CG  GLN C 298     9333   8895  11385   -509   -756   -781       C  
ATOM   2203  CD  GLN C 298      15.402  43.008 -43.118  1.00 85.65           C  
ANISOU 2203  CD  GLN C 298    10263   9898  12381   -525   -806   -872       C  
ATOM   2204  OE1 GLN C 298      15.557  42.632 -41.956  1.00 87.08           O  
ANISOU 2204  OE1 GLN C 298    10472  10106  12508   -460   -844   -970       O  
ATOM   2205  NE2 GLN C 298      16.421  43.327 -43.909  1.00 88.65           N  
ANISOU 2205  NE2 GLN C 298    10577  10290  12815   -601   -792   -824       N  
ATOM   2206  N   GLU C 299      11.216  40.535 -44.459  1.00 51.57           N  
ANISOU 2206  N   GLU C 299     6110   5718   7767   -383   -632   -632       N  
ATOM   2207  CA  GLU C 299      10.265  39.941 -43.532  1.00 43.27           C  
ANISOU 2207  CA  GLU C 299     5118   4690   6631   -301   -632   -665       C  
ATOM   2208  C   GLU C 299      10.886  39.810 -42.148  1.00 46.02           C  
ANISOU 2208  C   GLU C 299     5479   5049   6956   -252   -684   -780       C  
ATOM   2209  O   GLU C 299      12.079  39.526 -42.008  1.00 56.10           O  
ANISOU 2209  O   GLU C 299     6720   6356   8239   -272   -712   -825       O  
ATOM   2210  CB  GLU C 299       9.809  38.569 -44.033  1.00 38.51           C  
ANISOU 2210  CB  GLU C 299     4530   4171   5931   -282   -592   -609       C  
ATOM   2211  CG  GLU C 299       9.238  38.579 -45.441  1.00 46.26           C  
ANISOU 2211  CG  GLU C 299     5495   5159   6922   -326   -543   -502       C  
ATOM   2212  CD  GLU C 299       8.514  37.294 -45.794  1.00 63.42           C  
ANISOU 2212  CD  GLU C 299     7692   7402   9004   -297   -511   -457       C  
ATOM   2213  OE1 GLU C 299       8.137  37.128 -46.973  1.00 71.79           O  
ANISOU 2213  OE1 GLU C 299     8735   8483  10059   -329   -476   -378       O  
ATOM   2214  OE2 GLU C 299       8.320  36.451 -44.893  1.00 67.55           O  
ANISOU 2214  OE2 GLU C 299     8249   7958   9460   -243   -523   -499       O  
ATOM   2215  N   VAL C 300      10.071  40.040 -41.121  1.00 50.65           N  
ANISOU 2215  N   VAL C 300     6113   5619   7512   -184   -698   -827       N  
ATOM   2216  CA  VAL C 300      10.507  39.945 -39.731  1.00 57.25           C  
ANISOU 2216  CA  VAL C 300     6966   6475   8313   -124   -747   -936       C  
ATOM   2217  C   VAL C 300       9.446  39.179 -38.959  1.00 62.95           C  
ANISOU 2217  C   VAL C 300     7742   7251   8925    -43   -727   -933       C  
ATOM   2218  O   VAL C 300       8.254  39.478 -39.073  1.00 65.54           O  
ANISOU 2218  O   VAL C 300     8096   7558   9247    -21   -696   -890       O  
ATOM   2219  CB  VAL C 300      10.737  41.332 -39.099  1.00 63.02           C  
ANISOU 2219  CB  VAL C 300     7690   7119   9134   -122   -798  -1021       C  
ATOM   2220  CG1 VAL C 300      11.464  41.197 -37.771  1.00 65.27           C  
ANISOU 2220  CG1 VAL C 300     7980   7437   9382    -69   -856  -1142       C  
ATOM   2221  CG2 VAL C 300      11.516  42.225 -40.044  1.00 67.07           C  
ANISOU 2221  CG2 VAL C 300     8150   7562   9772   -215   -807   -993       C  
ATOM   2222  N   THR C 301       9.872  38.191 -38.178  1.00 64.48           N  
ANISOU 2222  N   THR C 301     7948   7517   9034      3   -744   -972       N  
ATOM   2223  CA  THR C 301       8.957  37.350 -37.419  1.00 68.16           C  
ANISOU 2223  CA  THR C 301     8460   8044   9393     76   -724   -958       C  
ATOM   2224  C   THR C 301       9.041  37.705 -35.943  1.00 74.62           C  
ANISOU 2224  C   THR C 301     9300   8879  10172    151   -769  -1061       C  
ATOM   2225  O   THR C 301      10.138  37.881 -35.401  1.00 76.02           O  
ANISOU 2225  O   THR C 301     9458   9061  10365    155   -821  -1144       O  
ATOM   2226  CB  THR C 301       9.259  35.865 -37.627  1.00 65.94           C  
ANISOU 2226  CB  THR C 301     8183   7834   9038     78   -709   -913       C  
ATOM   2227  OG1 THR C 301       9.498  35.615 -39.018  1.00 61.50           O  
ANISOU 2227  OG1 THR C 301     7588   7259   8518      6   -680   -843       O  
ATOM   2228  CG2 THR C 301       8.078  35.022 -37.166  1.00 65.31           C  
ANISOU 2228  CG2 THR C 301     8147   7803   8867    133   -674   -862       C  
ATOM   2229  N   ALA C 302       7.881  37.804 -35.302  1.00 85.65           N  
ANISOU 2229  N   ALA C 302    10734  10294  11516    214   -749  -1056       N  
ATOM   2230  CA  ALA C 302       7.792  38.257 -33.928  1.00 95.73           C  
ANISOU 2230  CA  ALA C 302    12030  11593  12749    294   -786  -1153       C  
ATOM   2231  C   ALA C 302       7.735  37.067 -32.973  1.00102.57           C  
ANISOU 2231  C   ALA C 302    12923  12561  13488    361   -784  -1150       C  
ATOM   2232  O   ALA C 302       7.745  35.902 -33.380  1.00105.07           O  
ANISOU 2232  O   ALA C 302    13245  12919  13760    343   -755  -1073       O  
ATOM   2233  CB  ALA C 302       6.577  39.168 -33.755  1.00 97.38           C  
ANISOU 2233  CB  ALA C 302    12258  11767  12976    330   -767  -1156       C  
ATOM   2234  N   GLU C 303       7.687  37.386 -31.677  1.00105.76           N  
ANISOU 2234  N   GLU C 303    13345  13006  13835    443   -818  -1238       N  
ATOM   2235  CA  GLU C 303       7.557  36.382 -30.626  1.00108.50           C  
ANISOU 2235  CA  GLU C 303    13717  13456  14052    517   -816  -1234       C  
ATOM   2236  C   GLU C 303       6.442  35.384 -30.925  1.00107.38           C  
ANISOU 2236  C   GLU C 303    13597  13357  13844    521   -748  -1110       C  
ATOM   2237  O   GLU C 303       6.611  34.172 -30.762  1.00107.23           O  
ANISOU 2237  O   GLU C 303    13590  13395  13757    530   -738  -1056       O  
ATOM   2238  CB  GLU C 303       7.305  37.083 -29.283  1.00114.83           C  
ANISOU 2238  CB  GLU C 303    14533  14298  14798    611   -850  -1338       C  
ATOM   2239  CG  GLU C 303       6.014  37.929 -29.205  1.00121.77           C  
ANISOU 2239  CG  GLU C 303    15425  15156  15686    645   -818  -1337       C  
ATOM   2240  CD  GLU C 303       5.963  39.079 -30.200  1.00123.99           C  
ANISOU 2240  CD  GLU C 303    15687  15318  16108    578   -823  -1347       C  
ATOM   2241  OE1 GLU C 303       4.840  39.513 -30.555  1.00121.50           O  
ANISOU 2241  OE1 GLU C 303    15378  14976  15810    584   -782  -1302       O  
ATOM   2242  OE2 GLU C 303       7.040  39.555 -30.634  1.00124.97           O  
ANISOU 2242  OE2 GLU C 303    15785  15375  16325    520   -866  -1394       O  
ATOM   2243  N   ASP C 304       5.298  35.882 -31.384  1.00106.87           N  
ANISOU 2243  N   ASP C 304    13537  13262  13808    512   -705  -1063       N  
ATOM   2244  CA  ASP C 304       4.081  35.089 -31.479  1.00105.80           C  
ANISOU 2244  CA  ASP C 304    13419  13174  13608    525   -644   -958       C  
ATOM   2245  C   ASP C 304       4.006  34.254 -32.749  1.00103.00           C  
ANISOU 2245  C   ASP C 304    13055  12791  13290    446   -609   -853       C  
ATOM   2246  O   ASP C 304       3.202  33.318 -32.810  1.00106.12           O  
ANISOU 2246  O   ASP C 304    13463  13229  13631    451   -566   -764       O  
ATOM   2247  CB  ASP C 304       2.866  36.017 -31.411  1.00107.13           C  
ANISOU 2247  CB  ASP C 304    13588  13326  13789    556   -615   -960       C  
ATOM   2248  CG  ASP C 304       3.119  37.347 -32.097  1.00105.24           C  
ANISOU 2248  CG  ASP C 304    13332  12985  13670    515   -639  -1013       C  
ATOM   2249  OD1 ASP C 304       3.931  37.371 -33.046  1.00100.47           O  
ANISOU 2249  OD1 ASP C 304    12708  12320  13145    438   -652   -999       O  
ATOM   2250  OD2 ASP C 304       2.510  38.359 -31.695  1.00107.62           O  
ANISOU 2250  OD2 ASP C 304    13636  13267  13989    561   -644  -1067       O  
ATOM   2251  N   GLY C 305       4.823  34.562 -33.753  1.00 97.40           N  
ANISOU 2251  N   GLY C 305    12322  12016  12671    376   -626   -862       N  
ATOM   2252  CA  GLY C 305       4.704  33.985 -35.074  1.00 93.03           C  
ANISOU 2252  CA  GLY C 305    11756  11435  12158    303   -594   -773       C  
ATOM   2253  C   GLY C 305       4.284  34.981 -36.132  1.00 89.59           C  
ANISOU 2253  C   GLY C 305    11300  10927  11813    252   -575   -751       C  
ATOM   2254  O   GLY C 305       4.419  34.692 -37.328  1.00 89.48           O  
ANISOU 2254  O   GLY C 305    11268  10888  11843    187   -557   -693       O  
ATOM   2255  N   THR C 306       3.770  36.140 -35.717  1.00 85.60           N  
ANISOU 2255  N   THR C 306    10798  10390  11335    283   -581   -797       N  
ATOM   2256  CA  THR C 306       3.452  37.226 -36.635  1.00 79.64           C  
ANISOU 2256  CA  THR C 306    10026   9557  10676    240   -572   -782       C  
ATOM   2257  C   THR C 306       4.642  37.537 -37.533  1.00 77.62           C  
ANISOU 2257  C   THR C 306     9739   9247  10505    165   -597   -791       C  
ATOM   2258  O   THR C 306       5.796  37.494 -37.099  1.00 80.30           O  
ANISOU 2258  O   THR C 306    10067   9591  10850    162   -639   -858       O  
ATOM   2259  CB  THR C 306       3.047  38.474 -35.837  1.00 80.08           C  
ANISOU 2259  CB  THR C 306    10091   9581  10756    296   -594   -861       C  
ATOM   2260  OG1 THR C 306       1.671  38.376 -35.447  1.00 79.51           O  
ANISOU 2260  OG1 THR C 306    10037   9551  10624    351   -555   -825       O  
ATOM   2261  CG2 THR C 306       3.272  39.761 -36.631  1.00 78.27           C  
ANISOU 2261  CG2 THR C 306     9842   9248  10650    247   -612   -875       C  
ATOM   2262  N   GLN C 307       4.356  37.830 -38.799  1.00 67.44           N  
ANISOU 2262  N   GLN C 307     8431   7915   9278    104   -569   -720       N  
ATOM   2263  CA  GLN C 307       5.370  38.254 -39.753  1.00 61.23           C  
ANISOU 2263  CA  GLN C 307     7608   7080   8575     30   -584   -714       C  
ATOM   2264  C   GLN C 307       4.969  39.595 -40.355  1.00 62.33           C  
ANISOU 2264  C   GLN C 307     7736   7135   8810      2   -581   -697       C  
ATOM   2265  O   GLN C 307       3.827  39.769 -40.796  1.00 61.54           O  
ANISOU 2265  O   GLN C 307     7647   7027   8709     10   -546   -636       O  
ATOM   2266  CB  GLN C 307       5.571  37.197 -40.843  1.00 51.66           C  
ANISOU 2266  CB  GLN C 307     6379   5908   7340    -20   -554   -635       C  
ATOM   2267  CG  GLN C 307       6.301  35.955 -40.347  1.00 58.84           C  
ANISOU 2267  CG  GLN C 307     7294   6884   8180     -1   -569   -660       C  
ATOM   2268  CD  GLN C 307       6.558  34.938 -41.444  1.00 71.96           C  
ANISOU 2268  CD  GLN C 307     8937   8579   9825    -46   -546   -595       C  
ATOM   2269  OE1 GLN C 307       5.674  34.167 -41.814  1.00 72.65           O  
ANISOU 2269  OE1 GLN C 307     9040   8694   9870    -40   -513   -532       O  
ATOM   2270  NE2 GLN C 307       7.779  34.933 -41.969  1.00 77.84           N  
ANISOU 2270  NE2 GLN C 307     9645   9324  10606    -89   -565   -615       N  
ATOM   2271  N   ARG C 308       5.907  40.540 -40.358  1.00 62.13           N  
ANISOU 2271  N   ARG C 308     7687   7046   8872    -32   -621   -751       N  
ATOM   2272  CA  ARG C 308       5.709  41.872 -40.905  1.00 58.57           C  
ANISOU 2272  CA  ARG C 308     7224   6500   8530    -65   -628   -736       C  
ATOM   2273  C   ARG C 308       6.702  42.117 -42.035  1.00 58.05           C  
ANISOU 2273  C   ARG C 308     7111   6403   8541   -156   -629   -688       C  
ATOM   2274  O   ARG C 308       7.740  41.456 -42.133  1.00 58.02           O  
ANISOU 2274  O   ARG C 308     7083   6446   8518   -186   -638   -703       O  
ATOM   2275  CB  ARG C 308       5.884  42.955 -39.828  1.00 64.96           C  
ANISOU 2275  CB  ARG C 308     8045   7246   9392    -23   -683   -846       C  
ATOM   2276  CG  ARG C 308       5.059  42.741 -38.568  1.00 71.92           C  
ANISOU 2276  CG  ARG C 308     8966   8174  10187     76   -687   -908       C  
ATOM   2277  CD  ARG C 308       4.972  44.012 -37.725  1.00 77.42           C  
ANISOU 2277  CD  ARG C 308     9673   8797  10947    122   -737  -1011       C  
ATOM   2278  NE  ARG C 308       3.750  44.769 -37.992  1.00 83.32           N  
ANISOU 2278  NE  ARG C 308    10436   9493  11728    151   -716   -977       N  
ATOM   2279  CZ  ARG C 308       3.686  45.848 -38.766  1.00 86.69           C  
ANISOU 2279  CZ  ARG C 308    10850   9813  12274    106   -726   -945       C  
ATOM   2280  NH1 ARG C 308       4.780  46.314 -39.354  1.00 88.40           N  
ANISOU 2280  NH1 ARG C 308    11034   9963  12589     25   -753   -940       N  
ATOM   2281  NH2 ARG C 308       2.527  46.466 -38.951  1.00 86.38           N  
ANISOU 2281  NH2 ARG C 308    10826   9735  12257    144   -708   -915       N  
ATOM   2282  N   CYS C 309       6.367  43.078 -42.894  1.00 59.05           N  
ANISOU 2282  N   CYS C 309     7225   6457   8755   -198   -617   -628       N  
ATOM   2283  CA  CYS C 309       7.263  43.557 -43.946  1.00 62.05           C  
ANISOU 2283  CA  CYS C 309     7557   6800   9221   -286   -617   -576       C  
ATOM   2284  C   CYS C 309       7.808  44.903 -43.488  1.00 72.91           C  
ANISOU 2284  C   CYS C 309     8921   8067  10717   -305   -670   -640       C  
ATOM   2285  O   CYS C 309       7.123  45.924 -43.592  1.00 82.71           O  
ANISOU 2285  O   CYS C 309    10176   9221  12029   -297   -677   -624       O  
ATOM   2286  CB  CYS C 309       6.536  43.697 -45.281  1.00 60.28           C  
ANISOU 2286  CB  CYS C 309     7323   6570   9011   -323   -569   -451       C  
ATOM   2287  SG  CYS C 309       6.220  42.161 -46.175  1.00 72.01           S  
ANISOU 2287  SG  CYS C 309     8803   8176  10380   -328   -514   -371       S  
ATOM   2288  N   GLU C 310       9.035  44.919 -42.977  1.00 78.15           N  
ANISOU 2288  N   GLU C 310     9557   8731  11408   -328   -713   -717       N  
ATOM   2289  CA  GLU C 310       9.618  46.170 -42.520  1.00 84.21           C  
ANISOU 2289  CA  GLU C 310    10307   9390  12297   -351   -771   -787       C  
ATOM   2290  C   GLU C 310      10.760  46.579 -43.440  1.00 95.84           C  
ANISOU 2290  C   GLU C 310    11716  10833  13866   -455   -774   -735       C  
ATOM   2291  O   GLU C 310      11.496  45.732 -43.963  1.00 96.60           O  
ANISOU 2291  O   GLU C 310    11776  11013  13914   -493   -750   -701       O  
ATOM   2292  CB  GLU C 310      10.065  46.088 -41.053  1.00 84.26           C  
ANISOU 2292  CB  GLU C 310    10331   9411  12275   -290   -829   -933       C  
ATOM   2293  CG  GLU C 310      11.493  45.673 -40.768  1.00 93.77           C  
ANISOU 2293  CG  GLU C 310    11491  10657  13479   -325   -862   -992       C  
ATOM   2294  CD  GLU C 310      11.725  45.485 -39.276  1.00105.17           C  
ANISOU 2294  CD  GLU C 310    12961  12141  14859   -243   -910  -1123       C  
ATOM   2295  OE1 GLU C 310      10.734  45.548 -38.515  1.00108.44           O  
ANISOU 2295  OE1 GLU C 310    13425  12549  15230   -163   -918  -1172       O  
ATOM   2296  OE2 GLU C 310      12.883  45.269 -38.863  1.00108.64           O  
ANISOU 2296  OE2 GLU C 310    13368  12626  15283   -253   -937  -1172       O  
ATOM   2297  N   LYS C 311      10.861  47.888 -43.657  1.00106.30           N  
ANISOU 2297  N   LYS C 311    13029  12057  15302   -490   -792   -715       N  
ATOM   2298  CA  LYS C 311      11.774  48.448 -44.643  1.00111.28           C  
ANISOU 2298  CA  LYS C 311    13603  12672  16006   -581   -776   -629       C  
ATOM   2299  C   LYS C 311      13.218  48.176 -44.251  1.00111.63           C  
ANISOU 2299  C   LYS C 311    13603  12769  16041   -610   -800   -690       C  
ATOM   2300  O   LYS C 311      13.618  48.414 -43.107  1.00106.44           O  
ANISOU 2300  O   LYS C 311    12957  12102  15382   -567   -849   -802       O  
ATOM   2301  CB  LYS C 311      11.522  49.952 -44.764  1.00114.18           C  
ANISOU 2301  CB  LYS C 311    13978  12923  16482   -595   -793   -601       C  
ATOM   2302  CG  LYS C 311      12.044  50.609 -46.029  1.00114.70           C  
ANISOU 2302  CG  LYS C 311    13996  12961  16624   -687   -764   -473       C  
ATOM   2303  CD  LYS C 311      11.346  51.946 -46.265  1.00113.87           C  
ANISOU 2303  CD  LYS C 311    13913  12739  16612   -684   -774   -425       C  
ATOM   2304  CE  LYS C 311      11.258  52.771 -44.984  1.00113.20           C  
ANISOU 2304  CE  LYS C 311    13860  12578  16572   -624   -838   -552       C  
ATOM   2305  NZ  LYS C 311      10.606  54.093 -45.206  1.00111.97           N  
ANISOU 2305  NZ  LYS C 311    13724  12306  16513   -618   -853   -511       N  
ATOM   2306  N   CYS C 312      13.994  47.658 -45.200  1.00119.74           N  
ANISOU 2306  N   CYS C 312    14576  13862  17059   -679   -766   -617       N  
ATOM   2307  CA  CYS C 312      15.422  47.471 -44.984  1.00128.44           C  
ANISOU 2307  CA  CYS C 312    15626  15015  18161   -713   -785   -662       C  
ATOM   2308  C   CYS C 312      16.056  48.791 -44.576  1.00134.64           C  
ANISOU 2308  C   CYS C 312    16396  15715  19047   -740   -825   -694       C  
ATOM   2309  O   CYS C 312      16.034  49.762 -45.337  1.00136.03           O  
ANISOU 2309  O   CYS C 312    16554  15822  19310   -796   -810   -608       O  
ATOM   2310  CB  CYS C 312      16.087  46.937 -46.256  1.00129.77           C  
ANISOU 2310  CB  CYS C 312    15730  15259  18317   -789   -736   -562       C  
ATOM   2311  SG  CYS C 312      15.573  45.291 -46.808  1.00128.49           S  
ANISOU 2311  SG  CYS C 312    15571  15211  18039   -764   -695   -531       S  
ATOM   2312  N   SER C 313      16.601  48.833 -43.358  1.00137.02           N  
ANISOU 2312  N   SER C 313    16704  16020  19338   -695   -877   -818       N  
ATOM   2313  CA  SER C 313      17.280  50.038 -42.896  1.00135.17           C  
ANISOU 2313  CA  SER C 313    16451  15708  19201   -719   -923   -861       C  
ATOM   2314  C   SER C 313      18.515  50.349 -43.729  1.00138.37           C  
ANISOU 2314  C   SER C 313    16781  16125  19667   -819   -907   -794       C  
ATOM   2315  O   SER C 313      18.979  51.494 -43.731  1.00140.49           O  
ANISOU 2315  O   SER C 313    17028  16312  20038   -862   -933   -788       O  
ATOM   2316  CB  SER C 313      17.666  49.891 -41.423  1.00129.13           C  
ANISOU 2316  CB  SER C 313    15703  14965  18397   -648   -982  -1009       C  
ATOM   2317  OG  SER C 313      18.641  48.878 -41.252  1.00124.78           O  
ANISOU 2317  OG  SER C 313    15116  14518  17777   -652   -982  -1044       O  
ATOM   2318  N   LYS C 314      19.043  49.358 -44.440  1.00138.29           N  
ANISOU 2318  N   LYS C 314    16729  16216  19596   -854   -867   -744       N  
ATOM   2319  CA  LYS C 314      20.242  49.471 -45.258  1.00137.16           C  
ANISOU 2319  CA  LYS C 314    16509  16114  19493   -944   -846   -680       C  
ATOM   2320  C   LYS C 314      19.999  48.671 -46.538  1.00137.97           C  
ANISOU 2320  C   LYS C 314    16586  16296  19540   -979   -778   -566       C  
ATOM   2321  O   LYS C 314      18.854  48.270 -46.782  1.00137.09           O  
ANISOU 2321  O   LYS C 314    16522  16183  19384   -940   -754   -533       O  
ATOM   2322  CB  LYS C 314      21.454  48.981 -44.459  1.00131.67           C  
ANISOU 2322  CB  LYS C 314    15776  15485  18766   -934   -883   -783       C  
ATOM   2323  CG  LYS C 314      21.436  47.506 -44.114  1.00126.74           C  
ANISOU 2323  CG  LYS C 314    15163  14973  18018   -873   -877   -836       C  
ATOM   2324  CD  LYS C 314      22.745  47.107 -43.455  1.00125.04           C  
ANISOU 2324  CD  LYS C 314    14902  14825  17781   -869   -913   -922       C  
ATOM   2325  CE  LYS C 314      22.760  45.638 -43.076  1.00124.74           C  
ANISOU 2325  CE  LYS C 314    14878  14896  17620   -801   -911   -975       C  
ATOM   2326  NZ  LYS C 314      24.061  45.250 -42.464  1.00123.70           N  
ANISOU 2326  NZ  LYS C 314    14701  14834  17467   -794   -946  -1053       N  
ATOM   2327  N   PRO C 315      20.995  48.450 -47.401  1.00137.35           N  
ANISOU 2327  N   PRO C 315    16433  16292  19464  -1051   -746   -502       N  
ATOM   2328  CA  PRO C 315      20.778  47.534 -48.531  1.00132.50           C  
ANISOU 2328  CA  PRO C 315    15791  15775  18780  -1069   -685   -411       C  
ATOM   2329  C   PRO C 315      20.316  46.158 -48.065  1.00122.13           C  
ANISOU 2329  C   PRO C 315    14511  14537  17357   -992   -689   -480       C  
ATOM   2330  O   PRO C 315      20.915  45.550 -47.175  1.00117.50           O  
ANISOU 2330  O   PRO C 315    13923  13995  16728   -951   -725   -585       O  
ATOM   2331  CB  PRO C 315      22.152  47.475 -49.202  1.00134.44           C  
ANISOU 2331  CB  PRO C 315    15942  16102  19037  -1146   -664   -371       C  
ATOM   2332  CG  PRO C 315      22.719  48.818 -48.955  1.00137.46           C  
ANISOU 2332  CG  PRO C 315    16308  16388  19531  -1198   -693   -369       C  
ATOM   2333  CD  PRO C 315      22.223  49.250 -47.598  1.00138.41           C  
ANISOU 2333  CD  PRO C 315    16499  16411  19678  -1129   -757   -485       C  
ATOM   2334  N   CYS C 316      19.235  45.674 -48.678  1.00116.02           N  
ANISOU 2334  N   CYS C 316    13767  13776  16538   -971   -652   -417       N  
ATOM   2335  CA  CYS C 316      18.666  44.385 -48.302  1.00109.89           C  
ANISOU 2335  CA  CYS C 316    13027  13063  15664   -901   -655   -472       C  
ATOM   2336  C   CYS C 316      19.648  43.260 -48.603  1.00103.50           C  
ANISOU 2336  C   CYS C 316    12157  12381  14788   -907   -644   -493       C  
ATOM   2337  O   CYS C 316      20.188  43.167 -49.710  1.00107.83           O  
ANISOU 2337  O   CYS C 316    12636  12995  15337   -965   -603   -411       O  
ATOM   2338  CB  CYS C 316      17.355  44.135 -49.050  1.00109.10           C  
ANISOU 2338  CB  CYS C 316    12961  12954  15538   -889   -615   -388       C  
ATOM   2339  SG  CYS C 316      15.997  45.317 -48.796  1.00108.67           S  
ANISOU 2339  SG  CYS C 316    12980  12759  15551   -868   -623   -357       S  
ATOM   2340  N   ALA C 317      19.871  42.397 -47.615  1.00 91.59           N  
ANISOU 2340  N   ALA C 317    10672  10913  13215   -841   -681   -602       N  
ATOM   2341  CA  ALA C 317      20.752  41.257 -47.802  1.00 84.12           C  
ANISOU 2341  CA  ALA C 317     9675  10086  12200   -830   -678   -634       C  
ATOM   2342  C   ALA C 317      20.145  40.263 -48.790  1.00 81.58           C  
ANISOU 2342  C   ALA C 317     9360   9846  11789   -809   -625   -563       C  
ATOM   2343  O   ALA C 317      18.939  40.257 -49.054  1.00 86.62           O  
ANISOU 2343  O   ALA C 317    10061  10454  12397   -783   -597   -509       O  
ATOM   2344  CB  ALA C 317      21.030  40.569 -46.465  1.00 81.40           C  
ANISOU 2344  CB  ALA C 317     9369   9762  11796   -750   -730   -759       C  
ATOM   2345  N   ARG C 318      21.009  39.411 -49.337  1.00 71.27           N  
ANISOU 2345  N   ARG C 318     7997   8655  10430   -812   -607   -563       N  
ATOM   2346  CA  ARG C 318      20.590  38.445 -50.343  1.00 62.63           C  
ANISOU 2346  CA  ARG C 318     6907   7652   9237   -786   -555   -500       C  
ATOM   2347  C   ARG C 318      19.586  37.454 -49.761  1.00 57.05           C  
ANISOU 2347  C   ARG C 318     6294   6945   8437   -695   -563   -539       C  
ATOM   2348  O   ARG C 318      19.635  37.105 -48.579  1.00 56.88           O  
ANISOU 2348  O   ARG C 318     6314   6901   8396   -641   -608   -628       O  
ATOM   2349  CB  ARG C 318      21.809  37.700 -50.888  1.00 55.44           C  
ANISOU 2349  CB  ARG C 318     5913   6864   8287   -794   -545   -516       C  
ATOM   2350  CG  ARG C 318      21.578  36.981 -52.201  1.00 56.28           C  
ANISOU 2350  CG  ARG C 318     5999   7073   8314   -787   -488   -441       C  
ATOM   2351  CD  ARG C 318      22.161  35.580 -52.164  1.00 57.67           C  
ANISOU 2351  CD  ARG C 318     6161   7353   8396   -723   -498   -509       C  
ATOM   2352  NE  ARG C 318      21.638  34.751 -53.245  1.00 61.84           N  
ANISOU 2352  NE  ARG C 318     6697   7963   8837   -694   -454   -458       N  
ATOM   2353  CZ  ARG C 318      21.674  33.423 -53.253  1.00 70.99           C  
ANISOU 2353  CZ  ARG C 318     7875   9189   9908   -622   -463   -510       C  
ATOM   2354  NH1 ARG C 318      21.174  32.749 -54.280  1.00 63.26           N  
ANISOU 2354  NH1 ARG C 318     6901   8278   8858   -598   -428   -467       N  
ATOM   2355  NH2 ARG C 318      22.202  32.767 -52.228  1.00 78.66           N  
ANISOU 2355  NH2 ARG C 318     8865  10159  10864   -570   -513   -606       N  
ATOM   2356  N   VAL C 319      18.659  37.003 -50.609  1.00 47.55           N  
ANISOU 2356  N   VAL C 319     5120   5770   7174   -678   -518   -466       N  
ATOM   2357  CA  VAL C 319      17.685  35.984 -50.237  1.00 43.32           C  
ANISOU 2357  CA  VAL C 319     4664   5243   6552   -601   -519   -487       C  
ATOM   2358  C   VAL C 319      17.558  34.978 -51.374  1.00 41.54           C  
ANISOU 2358  C   VAL C 319     4422   5114   6247   -587   -481   -442       C  
ATOM   2359  O   VAL C 319      17.825  35.279 -52.539  1.00 45.60           O  
ANISOU 2359  O   VAL C 319     4878   5678   6769   -634   -443   -373       O  
ATOM   2360  CB  VAL C 319      16.296  36.574 -49.899  1.00 44.66           C  
ANISOU 2360  CB  VAL C 319     4907   5321   6739   -587   -513   -454       C  
ATOM   2361  CG1 VAL C 319      16.377  37.492 -48.687  1.00 41.03           C  
ANISOU 2361  CG1 VAL C 319     4469   4769   6350   -587   -558   -516       C  
ATOM   2362  CG2 VAL C 319      15.728  37.310 -51.094  1.00 48.64           C  
ANISOU 2362  CG2 VAL C 319     5391   5813   7275   -639   -467   -345       C  
ATOM   2363  N   CYS C 320      17.146  33.765 -51.014  1.00 30.99           N  
ANISOU 2363  N   CYS C 320     3136   3805   4832   -518   -493   -483       N  
ATOM   2364  CA  CYS C 320      16.925  32.699 -51.981  1.00 34.85           C  
ANISOU 2364  CA  CYS C 320     3620   4376   5246   -492   -467   -457       C  
ATOM   2365  C   CYS C 320      15.500  32.797 -52.514  1.00 36.83           C  
ANISOU 2365  C   CYS C 320     3919   4597   5478   -490   -436   -385       C  
ATOM   2366  O   CYS C 320      14.536  32.667 -51.751  1.00 40.09           O  
ANISOU 2366  O   CYS C 320     4403   4949   5883   -455   -449   -395       O  
ATOM   2367  CB  CYS C 320      17.161  31.329 -51.349  1.00 46.32           C  
ANISOU 2367  CB  CYS C 320     5103   5861   6635   -422   -501   -533       C  
ATOM   2368  SG  CYS C 320      18.841  31.036 -50.760  1.00 66.64           S  
ANISOU 2368  SG  CYS C 320     7617   8484   9219   -411   -542   -623       S  
ATOM   2369  N   TYR C 321      15.370  33.026 -53.816  1.00 31.85           N  
ANISOU 2369  N   TYR C 321     3247   4017   4838   -524   -395   -312       N  
ATOM   2370  CA  TYR C 321      14.073  33.117 -54.468  1.00 23.61           C  
ANISOU 2370  CA  TYR C 321     2239   2959   3772   -522   -366   -241       C  
ATOM   2371  C   TYR C 321      13.725  31.792 -55.132  1.00 25.86           C  
ANISOU 2371  C   TYR C 321     2533   3319   3972   -477   -361   -251       C  
ATOM   2372  O   TYR C 321      14.592  31.121 -55.698  1.00 27.25           O  
ANISOU 2372  O   TYR C 321     2661   3582   4110   -468   -360   -279       O  
ATOM   2373  CB  TYR C 321      14.054  34.249 -55.499  1.00 19.26           C  
ANISOU 2373  CB  TYR C 321     1640   2416   3263   -585   -327   -146       C  
ATOM   2374  CG  TYR C 321      13.924  35.624 -54.879  1.00 31.98           C  
ANISOU 2374  CG  TYR C 321     3262   3922   4968   -625   -335   -122       C  
ATOM   2375  CD1 TYR C 321      14.984  36.522 -54.897  1.00 29.36           C  
ANISOU 2375  CD1 TYR C 321     2868   3578   4708   -684   -337   -113       C  
ATOM   2376  CD2 TYR C 321      12.746  36.011 -54.255  1.00 31.54           C  
ANISOU 2376  CD2 TYR C 321     3275   3777   4933   -603   -343   -114       C  
ATOM   2377  CE1 TYR C 321      14.865  37.779 -54.326  1.00 32.97           C  
ANISOU 2377  CE1 TYR C 321     3336   3928   5261   -720   -352    -98       C  
ATOM   2378  CE2 TYR C 321      12.618  37.259 -53.679  1.00 32.89           C  
ANISOU 2378  CE2 TYR C 321     3457   3848   5191   -632   -356   -103       C  
ATOM   2379  CZ  TYR C 321      13.678  38.139 -53.714  1.00 40.46           C  
ANISOU 2379  CZ  TYR C 321     4358   4787   6227   -690   -363    -98       C  
ATOM   2380  OH  TYR C 321      13.547  39.381 -53.137  1.00 50.47           O  
ANISOU 2380  OH  TYR C 321     5639   5945   7592   -718   -382    -93       O  
ATOM   2381  N   GLY C 322      12.447  31.413 -55.050  1.00 24.39           N  
ANISOU 2381  N   GLY C 322     2408   3098   3760   -448   -359   -233       N  
ATOM   2382  CA  GLY C 322      11.969  30.205 -55.685  1.00 26.68           C  
ANISOU 2382  CA  GLY C 322     2710   3445   3981   -410   -359   -242       C  
ATOM   2383  C   GLY C 322      11.397  30.475 -57.063  1.00 30.91           C  
ANISOU 2383  C   GLY C 322     3218   4035   4492   -431   -322   -167       C  
ATOM   2384  O   GLY C 322      11.440  31.590 -57.579  1.00 25.03           O  
ANISOU 2384  O   GLY C 322     2440   3289   3781   -477   -294    -99       O  
ATOM   2385  N   LEU C 323      10.856  29.416 -57.667  1.00 31.20           N  
ANISOU 2385  N   LEU C 323     3267   4120   4469   -396   -327   -179       N  
ATOM   2386  CA  LEU C 323      10.157  29.557 -58.938  1.00 32.80           C  
ANISOU 2386  CA  LEU C 323     3448   4378   4636   -406   -298   -115       C  
ATOM   2387  C   LEU C 323       8.987  30.523 -58.789  1.00 34.38           C  
ANISOU 2387  C   LEU C 323     3683   4505   4874   -428   -281    -43       C  
ATOM   2388  O   LEU C 323       8.377  30.634 -57.721  1.00 37.34           O  
ANISOU 2388  O   LEU C 323     4113   4794   5282   -417   -297    -57       O  
ATOM   2389  CB  LEU C 323       9.656  28.198 -59.432  1.00 30.64           C  
ANISOU 2389  CB  LEU C 323     3191   4151   4301   -360   -317   -156       C  
ATOM   2390  CG  LEU C 323      10.628  27.017 -59.452  1.00 29.76           C  
ANISOU 2390  CG  LEU C 323     3060   4095   4153   -321   -346   -243       C  
ATOM   2391  CD1 LEU C 323       9.969  25.819 -60.111  1.00 31.29           C  
ANISOU 2391  CD1 LEU C 323     3268   4325   4294   -281   -366   -275       C  
ATOM   2392  CD2 LEU C 323      11.923  27.373 -60.168  1.00 28.32           C  
ANISOU 2392  CD2 LEU C 323     2799   4008   3954   -339   -325   -243       C  
ATOM   2393  N   GLY C 324       8.671  31.224 -59.875  1.00 34.07           N  
ANISOU 2393  N   GLY C 324     3610   4509   4825   -455   -249     37       N  
ATOM   2394  CA  GLY C 324       7.629  32.232 -59.838  1.00 33.11           C  
ANISOU 2394  CA  GLY C 324     3514   4323   4743   -474   -233    111       C  
ATOM   2395  C   GLY C 324       8.021  33.505 -59.131  1.00 38.96           C  
ANISOU 2395  C   GLY C 324     4256   4982   5567   -511   -228    137       C  
ATOM   2396  O   GLY C 324       7.145  34.292 -58.756  1.00 40.92           O  
ANISOU 2396  O   GLY C 324     4538   5152   5858   -516   -225    177       O  
ATOM   2397  N   MET C 325       9.318  33.739 -58.948  1.00 36.89           N  
ANISOU 2397  N   MET C 325     3953   4734   5330   -537   -230    112       N  
ATOM   2398  CA  MET C 325       9.802  34.866 -58.165  1.00 30.77           C  
ANISOU 2398  CA  MET C 325     3177   3874   4641   -573   -237    117       C  
ATOM   2399  C   MET C 325      11.079  35.411 -58.787  1.00 31.88           C  
ANISOU 2399  C   MET C 325     3241   4068   4805   -624   -218    148       C  
ATOM   2400  O   MET C 325      12.006  34.647 -59.071  1.00 30.59           O  
ANISOU 2400  O   MET C 325     3036   3990   4598   -616   -220    104       O  
ATOM   2401  CB  MET C 325      10.066  34.442 -56.716  1.00 39.28           C  
ANISOU 2401  CB  MET C 325     4296   4890   5738   -544   -275     22       C  
ATOM   2402  CG  MET C 325       9.625  35.447 -55.682  1.00 46.41           C  
ANISOU 2402  CG  MET C 325     5240   5678   6715   -550   -289     20       C  
ATOM   2403  SD  MET C 325       7.835  35.547 -55.575  1.00 57.36           S  
ANISOU 2403  SD  MET C 325     6690   7015   8090   -516   -282     60       S  
ATOM   2404  CE  MET C 325       7.641  37.268 -55.125  1.00 53.85           C  
ANISOU 2404  CE  MET C 325     6252   6457   7750   -548   -284     99       C  
ATOM   2405  N   GLU C 326      11.114  36.728 -59.002  1.00 36.38           N  
ANISOU 2405  N   GLU C 326     3789   4585   5447   -675   -202    226       N  
ATOM   2406  CA  GLU C 326      12.315  37.484 -59.402  1.00 40.00           C  
ANISOU 2406  CA  GLU C 326     4175   5069   5955   -737   -187    266       C  
ATOM   2407  C   GLU C 326      12.943  36.815 -60.626  1.00 38.43           C  
ANISOU 2407  C   GLU C 326     3909   5020   5674   -738   -156    291       C  
ATOM   2408  O   GLU C 326      12.247  36.615 -61.630  1.00 37.13           O  
ANISOU 2408  O   GLU C 326     3740   4919   5447   -723   -130    351       O  
ATOM   2409  CB  GLU C 326      13.230  37.631 -58.195  1.00 44.54           C  
ANISOU 2409  CB  GLU C 326     4748   5582   6592   -748   -223    180       C  
ATOM   2410  CG  GLU C 326      12.666  38.500 -57.076  1.00 53.46           C  
ANISOU 2410  CG  GLU C 326     5935   6569   7807   -749   -253    160       C  
ATOM   2411  CD  GLU C 326      12.287  39.899 -57.538  1.00 57.05           C  
ANISOU 2411  CD  GLU C 326     6380   6952   8345   -800   -236    263       C  
ATOM   2412  OE1 GLU C 326      11.415  40.520 -56.893  1.00 58.36           O  
ANISOU 2412  OE1 GLU C 326     6602   7011   8560   -784   -254    260       O  
ATOM   2413  OE2 GLU C 326      12.864  40.386 -58.534  1.00 54.81           O  
ANISOU 2413  OE2 GLU C 326     6030   6718   8076   -854   -205    348       O  
ATOM   2414  N   HIS C 327      14.229  36.458 -60.590  1.00 33.46           N  
ANISOU 2414  N   HIS C 327     3220   4456   5036   -751   -158    244       N  
ATOM   2415  CA  HIS C 327      14.892  35.903 -61.766  1.00 41.53           C  
ANISOU 2415  CA  HIS C 327     4170   5631   5980   -750   -126    267       C  
ATOM   2416  C   HIS C 327      14.369  34.521 -62.134  1.00 44.81           C  
ANISOU 2416  C   HIS C 327     4613   6124   6289   -677   -134    208       C  
ATOM   2417  O   HIS C 327      14.575  34.078 -63.268  1.00 48.69           O  
ANISOU 2417  O   HIS C 327     5054   6744   6702   -664   -107    233       O  
ATOM   2418  CB  HIS C 327      16.406  35.849 -61.540  1.00 48.61           C  
ANISOU 2418  CB  HIS C 327     4994   6577   6898   -777   -130    222       C  
ATOM   2419  CG  HIS C 327      16.807  35.148 -60.279  1.00 52.73           C  
ANISOU 2419  CG  HIS C 327     5552   7050   7433   -739   -179     96       C  
ATOM   2420  ND1 HIS C 327      16.812  35.772 -59.050  1.00 52.92           N  
ANISOU 2420  ND1 HIS C 327     5616   6946   7545   -756   -213     60       N  
ATOM   2421  CD2 HIS C 327      17.223  33.878 -60.057  1.00 55.08           C  
ANISOU 2421  CD2 HIS C 327     5852   7411   7665   -680   -201     -2       C  
ATOM   2422  CE1 HIS C 327      17.209  34.916 -58.125  1.00 56.76           C  
ANISOU 2422  CE1 HIS C 327     6127   7427   8014   -710   -253    -49       C  
ATOM   2423  NE2 HIS C 327      17.465  33.760 -58.710  1.00 57.27           N  
ANISOU 2423  NE2 HIS C 327     6171   7601   7989   -664   -247    -86       N  
ATOM   2424  N   LEU C 328      13.701  33.833 -61.209  1.00 40.60           N  
ANISOU 2424  N   LEU C 328     4157   5518   5752   -629   -172    130       N  
ATOM   2425  CA  LEU C 328      13.085  32.542 -61.479  1.00 48.29           C  
ANISOU 2425  CA  LEU C 328     5164   6542   6643   -565   -186     76       C  
ATOM   2426  C   LEU C 328      11.592  32.666 -61.764  1.00 55.87           C  
ANISOU 2426  C   LEU C 328     6177   7461   7589   -551   -181    128       C  
ATOM   2427  O   LEU C 328      10.856  31.684 -61.623  1.00 59.19           O  
ANISOU 2427  O   LEU C 328     6644   7879   7968   -503   -203     78       O  
ATOM   2428  CB  LEU C 328      13.316  31.590 -60.306  1.00 43.60           C  
ANISOU 2428  CB  LEU C 328     4615   5900   6052   -521   -232    -35       C  
ATOM   2429  CG  LEU C 328      14.766  31.227 -59.978  1.00 40.22           C  
ANISOU 2429  CG  LEU C 328     4137   5519   5626   -519   -246   -104       C  
ATOM   2430  CD1 LEU C 328      14.822  30.342 -58.746  1.00 32.88           C  
ANISOU 2430  CD1 LEU C 328     3263   4529   4700   -470   -294   -203       C  
ATOM   2431  CD2 LEU C 328      15.432  30.543 -61.160  1.00 37.44           C  
ANISOU 2431  CD2 LEU C 328     3716   5313   5196   -499   -227   -114       C  
ATOM   2432  N   ARG C 329      11.137  33.855 -62.169  1.00 53.95           N  
ANISOU 2432  N   ARG C 329     5927   7186   7387   -593   -153    229       N  
ATOM   2433  CA  ARG C 329       9.705  34.102 -62.316  1.00 51.06           C  
ANISOU 2433  CA  ARG C 329     5610   6770   7018   -580   -151    279       C  
ATOM   2434  C   ARG C 329       9.098  33.255 -63.429  1.00 44.45           C  
ANISOU 2434  C   ARG C 329     4763   6039   6086   -542   -143    286       C  
ATOM   2435  O   ARG C 329       7.980  32.747 -63.290  1.00 42.67           O  
ANISOU 2435  O   ARG C 329     4589   5784   5841   -508   -160    269       O  
ATOM   2436  CB  ARG C 329       9.465  35.591 -62.574  1.00 52.17           C  
ANISOU 2436  CB  ARG C 329     5739   6856   7226   -630   -126    388       C  
ATOM   2437  CG  ARG C 329       8.008  36.014 -62.656  1.00 59.31           C  
ANISOU 2437  CG  ARG C 329     6693   7703   8140   -615   -125    443       C  
ATOM   2438  CD  ARG C 329       7.892  37.532 -62.747  1.00 63.03           C  
ANISOU 2438  CD  ARG C 329     7155   8098   8694   -663   -108    544       C  
ATOM   2439  NE  ARG C 329       8.677  38.075 -63.854  1.00 71.94           N  
ANISOU 2439  NE  ARG C 329     8211   9310   9813   -707    -73    633       N  
ATOM   2440  CZ  ARG C 329       9.602  39.022 -63.723  1.00 77.86           C  
ANISOU 2440  CZ  ARG C 329     8921  10021  10640   -766    -63    675       C  
ATOM   2441  NH1 ARG C 329       9.857  39.543 -62.531  1.00 75.10           N  
ANISOU 2441  NH1 ARG C 329     8601   9548  10386   -784    -91    627       N  
ATOM   2442  NH2 ARG C 329      10.269  39.453 -64.786  1.00 79.20           N  
ANISOU 2442  NH2 ARG C 329     9019  10279  10794   -807    -27    767       N  
ATOM   2443  N   GLU C 330       9.822  33.079 -64.533  1.00 44.34           N  
ANISOU 2443  N   GLU C 330     4681   6153   6012   -547   -119    309       N  
ATOM   2444  CA  GLU C 330       9.307  32.370 -65.697  1.00 43.17           C  
ANISOU 2444  CA  GLU C 330     4516   6119   5770   -509   -112    316       C  
ATOM   2445  C   GLU C 330       9.724  30.904 -65.743  1.00 40.28           C  
ANISOU 2445  C   GLU C 330     4145   5820   5338   -457   -140    201       C  
ATOM   2446  O   GLU C 330       9.460  30.232 -66.745  1.00 45.98           O  
ANISOU 2446  O   GLU C 330     4844   6647   5978   -421   -140    188       O  
ATOM   2447  CB  GLU C 330       9.772  33.061 -66.983  1.00 53.38           C  
ANISOU 2447  CB  GLU C 330     5733   7527   7022   -537    -67    414       C  
ATOM   2448  CG  GLU C 330       9.638  34.582 -67.010  1.00 67.80           C  
ANISOU 2448  CG  GLU C 330     7551   9288   8922   -597    -38    538       C  
ATOM   2449  CD  GLU C 330       8.202  35.077 -67.029  1.00 80.93           C  
ANISOU 2449  CD  GLU C 330     9268  10877  10606   -589    -43    597       C  
ATOM   2450  OE1 GLU C 330       8.010  36.313 -67.051  1.00 84.07           O  
ANISOU 2450  OE1 GLU C 330     9665  11211  11069   -630    -24    697       O  
ATOM   2451  OE2 GLU C 330       7.264  34.250 -67.031  1.00 84.26           O  
ANISOU 2451  OE2 GLU C 330     9730  11302  10982   -541    -67    546       O  
ATOM   2452  N   VAL C 331      10.361  30.393 -64.695  1.00 33.02           N  
ANISOU 2452  N   VAL C 331     3246   4845   4454   -447   -168    116       N  
ATOM   2453  CA  VAL C 331      11.004  29.084 -64.746  1.00 39.77           C  
ANISOU 2453  CA  VAL C 331     4089   5765   5258   -398   -196     11       C  
ATOM   2454  C   VAL C 331      10.002  28.013 -64.334  1.00 37.50           C  
ANISOU 2454  C   VAL C 331     3869   5422   4959   -353   -238    -55       C  
ATOM   2455  O   VAL C 331       9.449  28.055 -63.230  1.00 36.79           O  
ANISOU 2455  O   VAL C 331     3840   5214   4924   -357   -258    -66       O  
ATOM   2456  CB  VAL C 331      12.255  29.047 -63.858  1.00 38.51           C  
ANISOU 2456  CB  VAL C 331     3912   5579   5140   -408   -208    -46       C  
ATOM   2457  CG1 VAL C 331      12.859  27.653 -63.855  1.00 32.19           C  
ANISOU 2457  CG1 VAL C 331     3104   4836   4291   -349   -242   -157       C  
ATOM   2458  CG2 VAL C 331      13.273  30.071 -64.344  1.00 25.88           C  
ANISOU 2458  CG2 VAL C 331     2234   4042   3555   -459   -166     21       C  
ATOM   2459  N   ARG C 332       9.788  27.039 -65.222  1.00 35.91           N  
ANISOU 2459  N   ARG C 332     3652   5308   4684   -309   -253    -99       N  
ATOM   2460  CA  ARG C 332       8.798  25.995 -64.975  1.00 38.90           C  
ANISOU 2460  CA  ARG C 332     4087   5637   5056   -271   -295   -155       C  
ATOM   2461  C   ARG C 332       9.224  25.061 -63.849  1.00 41.95           C  
ANISOU 2461  C   ARG C 332     4515   5949   5476   -244   -338   -246       C  
ATOM   2462  O   ARG C 332       8.405  24.698 -62.998  1.00 42.81           O  
ANISOU 2462  O   ARG C 332     4686   5956   5623   -239   -364   -259       O  
ATOM   2463  CB  ARG C 332       8.552  25.195 -66.255  1.00 49.11           C  
ANISOU 2463  CB  ARG C 332     5348   7045   6266   -229   -307   -190       C  
ATOM   2464  CG  ARG C 332       7.440  25.735 -67.141  1.00 59.88           C  
ANISOU 2464  CG  ARG C 332     6707   8444   7599   -240   -287   -112       C  
ATOM   2465  CD  ARG C 332       7.480  25.106 -68.531  1.00 69.74           C  
ANISOU 2465  CD  ARG C 332     7907   9839   8753   -197   -293   -146       C  
ATOM   2466  NE  ARG C 332       7.217  23.667 -68.512  1.00 75.67           N  
ANISOU 2466  NE  ARG C 332     8682  10581   9487   -146   -351   -259       N  
ATOM   2467  CZ  ARG C 332       6.012  23.121 -68.379  1.00 79.44           C  
ANISOU 2467  CZ  ARG C 332     9206  10994   9982   -137   -386   -278       C  
ATOM   2468  NH1 ARG C 332       4.937  23.889 -68.250  1.00 80.92           N  
ANISOU 2468  NH1 ARG C 332     9419  11129  10198   -171   -369   -193       N  
ATOM   2469  NH2 ARG C 332       5.880  21.801 -68.376  1.00 77.49           N  
ANISOU 2469  NH2 ARG C 332     8979  10735   9730    -94   -442   -381       N  
ATOM   2470  N   ALA C 333      10.491  24.650 -63.826  1.00 42.71           N  
ANISOU 2470  N   ALA C 333     4573   6099   5557   -224   -345   -307       N  
ATOM   2471  CA  ALA C 333      10.878  23.555 -62.950  1.00 43.78           C  
ANISOU 2471  CA  ALA C 333     4744   6179   5711   -185   -393   -400       C  
ATOM   2472  C   ALA C 333      12.325  23.702 -62.505  1.00 46.64           C  
ANISOU 2472  C   ALA C 333     5068   6568   6086   -184   -390   -435       C  
ATOM   2473  O   ALA C 333      13.134  24.383 -63.141  1.00 50.48           O  
ANISOU 2473  O   ALA C 333     5485   7143   6551   -206   -354   -404       O  
ATOM   2474  CB  ALA C 333      10.681  22.201 -63.640  1.00 45.66           C  
ANISOU 2474  CB  ALA C 333     4982   6466   5900   -127   -433   -480       C  
ATOM   2475  N   VAL C 334      12.631  23.044 -61.387  1.00 41.45           N  
ANISOU 2475  N   VAL C 334     4452   5833   5463   -159   -430   -496       N  
ATOM   2476  CA  VAL C 334      14.010  22.882 -60.945  1.00 34.16           C  
ANISOU 2476  CA  VAL C 334     3494   4939   4547   -143   -441   -552       C  
ATOM   2477  C   VAL C 334      14.733  21.953 -61.907  1.00 32.16           C  
ANISOU 2477  C   VAL C 334     3187   4800   4231    -89   -456   -625       C  
ATOM   2478  O   VAL C 334      14.255  20.852 -62.203  1.00 37.49           O  
ANISOU 2478  O   VAL C 334     3891   5471   4883    -42   -493   -680       O  
ATOM   2479  CB  VAL C 334      14.050  22.325 -59.514  1.00 28.89           C  
ANISOU 2479  CB  VAL C 334     2890   4163   3925   -121   -485   -597       C  
ATOM   2480  CG1 VAL C 334      15.484  22.217 -59.022  1.00 24.85           C  
ANISOU 2480  CG1 VAL C 334     2339   3683   3420   -102   -500   -655       C  
ATOM   2481  CG2 VAL C 334      13.212  23.181 -58.580  1.00 17.40           C  
ANISOU 2481  CG2 VAL C 334     1488   2603   2520   -164   -472   -533       C  
ATOM   2482  N   THR C 335      15.880  22.393 -62.416  1.00 35.22           N  
ANISOU 2482  N   THR C 335     3495   5293   4595    -97   -428   -626       N  
ATOM   2483  CA  THR C 335      16.691  21.561 -63.291  1.00 39.17           C  
ANISOU 2483  CA  THR C 335     3935   5916   5031    -40   -439   -702       C  
ATOM   2484  C   THR C 335      18.146  21.661 -62.862  1.00 44.68           C  
ANISOU 2484  C   THR C 335     4577   6659   5741    -33   -439   -742       C  
ATOM   2485  O   THR C 335      18.505  22.432 -61.968  1.00 48.62           O  
ANISOU 2485  O   THR C 335     5080   7097   6296    -78   -430   -709       O  
ATOM   2486  CB  THR C 335      16.560  21.961 -64.769  1.00 36.86           C  
ANISOU 2486  CB  THR C 335     3578   5758   4669    -48   -394   -657       C  
ATOM   2487  OG1 THR C 335      17.205  23.220 -64.986  1.00 42.79           O  
ANISOU 2487  OG1 THR C 335     4263   6566   5428   -109   -337   -575       O  
ATOM   2488  CG2 THR C 335      15.099  22.059 -65.184  1.00 20.33           C  
ANISOU 2488  CG2 THR C 335     1534   3622   2567    -63   -391   -605       C  
ATOM   2489  N   SER C 336      18.989  20.864 -63.522  1.00 51.92           N  
ANISOU 2489  N   SER C 336     5436   7687   6603     28   -452   -821       N  
ATOM   2490  CA  SER C 336      20.429  20.993 -63.347  1.00 52.71           C  
ANISOU 2490  CA  SER C 336     5462   7864   6703     36   -446   -858       C  
ATOM   2491  C   SER C 336      20.925  22.381 -63.720  1.00 48.79           C  
ANISOU 2491  C   SER C 336     4890   7436   6214    -41   -380   -763       C  
ATOM   2492  O   SER C 336      22.011  22.778 -63.283  1.00 54.76           O  
ANISOU 2492  O   SER C 336     5592   8219   6997    -60   -373   -772       O  
ATOM   2493  CB  SER C 336      21.149  19.939 -64.186  1.00 48.76           C  
ANISOU 2493  CB  SER C 336     4905   7490   6132    120   -465   -956       C  
ATOM   2494  OG  SER C 336      20.780  20.050 -65.550  1.00 53.29           O  
ANISOU 2494  OG  SER C 336     5435   8182   6632    124   -430   -928       O  
ATOM   2495  N   ALA C 337      20.152  23.125 -64.516  1.00 43.91           N  
ANISOU 2495  N   ALA C 337     4265   6843   5574    -87   -335   -671       N  
ATOM   2496  CA  ALA C 337      20.555  24.474 -64.892  1.00 43.65           C  
ANISOU 2496  CA  ALA C 337     4165   6864   5557   -165   -274   -567       C  
ATOM   2497  C   ALA C 337      20.428  25.453 -63.731  1.00 37.09           C  
ANISOU 2497  C   ALA C 337     3374   5895   4824   -234   -274   -513       C  
ATOM   2498  O   ALA C 337      21.162  26.446 -63.685  1.00 44.52           O  
ANISOU 2498  O   ALA C 337     4253   6860   5803   -296   -241   -457       O  
ATOM   2499  CB  ALA C 337      19.728  24.957 -66.083  1.00 22.80           C  
ANISOU 2499  CB  ALA C 337     1510   4290   2865   -187   -230   -479       C  
ATOM   2500  N   ASN C 338      19.521  25.197 -62.785  1.00 27.30           N  
ANISOU 2500  N   ASN C 338     2235   4511   3628   -226   -313   -530       N  
ATOM   2501  CA  ASN C 338      19.256  26.145 -61.710  1.00 27.84           C  
ANISOU 2501  CA  ASN C 338     2346   4451   3781   -284   -314   -483       C  
ATOM   2502  C   ASN C 338      19.348  25.560 -60.306  1.00 28.00           C  
ANISOU 2502  C   ASN C 338     2431   4364   3843   -251   -369   -559       C  
ATOM   2503  O   ASN C 338      19.016  26.262 -59.346  1.00 39.43           O  
ANISOU 2503  O   ASN C 338     3923   5703   5353   -288   -376   -531       O  
ATOM   2504  CB  ASN C 338      17.869  26.787 -61.892  1.00 28.51           C  
ANISOU 2504  CB  ASN C 338     2488   4462   3881   -319   -294   -396       C  
ATOM   2505  CG  ASN C 338      16.732  25.770 -61.873  1.00 38.31           C  
ANISOU 2505  CG  ASN C 338     3807   5658   5091   -266   -326   -434       C  
ATOM   2506  OD1 ASN C 338      16.652  24.914 -60.991  1.00 39.19           O  
ANISOU 2506  OD1 ASN C 338     3974   5701   5217   -224   -373   -505       O  
ATOM   2507  ND2 ASN C 338      15.839  25.872 -62.850  1.00 43.68           N  
ANISOU 2507  ND2 ASN C 338     4490   6376   5731   -270   -303   -381       N  
ATOM   2508  N   ILE C 339      19.778  24.307 -60.148  1.00 29.35           N  
ANISOU 2508  N   ILE C 339     2610   4562   3980   -178   -411   -654       N  
ATOM   2509  CA  ILE C 339      19.791  23.704 -58.816  1.00 38.22           C  
ANISOU 2509  CA  ILE C 339     3800   5584   5138   -143   -465   -716       C  
ATOM   2510  C   ILE C 339      20.767  24.441 -57.902  1.00 40.04           C  
ANISOU 2510  C   ILE C 339     3999   5792   5422   -176   -471   -725       C  
ATOM   2511  O   ILE C 339      20.488  24.656 -56.713  1.00 45.21           O  
ANISOU 2511  O   ILE C 339     4713   6342   6123   -182   -497   -730       O  
ATOM   2512  CB  ILE C 339      20.108  22.198 -58.914  1.00 40.22           C  
ANISOU 2512  CB  ILE C 339     4064   5870   5349    -56   -512   -813       C  
ATOM   2513  CG1 ILE C 339      20.047  21.549 -57.532  1.00 33.41           C  
ANISOU 2513  CG1 ILE C 339     3276   4898   4520    -18   -568   -863       C  
ATOM   2514  CG2 ILE C 339      21.464  21.955 -59.581  1.00 20.81           C  
ANISOU 2514  CG2 ILE C 339     1506   3548   2852    -28   -505   -866       C  
ATOM   2515  CD1 ILE C 339      18.668  21.066 -57.153  1.00 40.31           C  
ANISOU 2515  CD1 ILE C 339     4246   5667   5403     -8   -587   -841       C  
ATOM   2516  N   GLN C 340      21.908  24.875 -58.450  1.00 37.37           N  
ANISOU 2516  N   GLN C 340     3562   5558   5079   -199   -445   -725       N  
ATOM   2517  CA  GLN C 340      22.898  25.607 -57.664  1.00 48.27           C  
ANISOU 2517  CA  GLN C 340     4899   6925   6516   -236   -453   -736       C  
ATOM   2518  C   GLN C 340      22.295  26.834 -56.995  1.00 44.07           C  
ANISOU 2518  C   GLN C 340     4407   6283   6054   -306   -441   -669       C  
ATOM   2519  O   GLN C 340      22.791  27.281 -55.953  1.00 38.66           O  
ANISOU 2519  O   GLN C 340     3725   5542   5424   -323   -468   -697       O  
ATOM   2520  CB  GLN C 340      24.076  26.028 -58.549  1.00 55.92           C  
ANISOU 2520  CB  GLN C 340     5746   8031   7472   -265   -415   -724       C  
ATOM   2521  CG  GLN C 340      24.305  25.159 -59.783  1.00 69.82           C  
ANISOU 2521  CG  GLN C 340     7456   9926   9146   -212   -398   -750       C  
ATOM   2522  CD  GLN C 340      23.380  25.517 -60.936  1.00 77.19           C  
ANISOU 2522  CD  GLN C 340     8392  10896  10042   -239   -350   -666       C  
ATOM   2523  OE1 GLN C 340      23.161  26.693 -61.229  1.00 82.49           O  
ANISOU 2523  OE1 GLN C 340     9040  11557  10747   -317   -306   -569       O  
ATOM   2524  NE2 GLN C 340      22.830  24.501 -61.591  1.00 75.72           N  
ANISOU 2524  NE2 GLN C 340     8233  10749   9788   -174   -361   -703       N  
ATOM   2525  N   GLU C 341      21.219  27.380 -57.571  1.00 45.07           N  
ANISOU 2525  N   GLU C 341     4564   6380   6181   -341   -406   -587       N  
ATOM   2526  CA  GLU C 341      20.565  28.562 -57.021  1.00 43.80           C  
ANISOU 2526  CA  GLU C 341     4441   6114   6088   -402   -395   -523       C  
ATOM   2527  C   GLU C 341      20.098  28.359 -55.588  1.00 39.62           C  
ANISOU 2527  C   GLU C 341     3998   5467   5588   -373   -442   -570       C  
ATOM   2528  O   GLU C 341      19.841  29.344 -54.887  1.00 42.33           O  
ANISOU 2528  O   GLU C 341     4364   5725   5993   -414   -444   -544       O  
ATOM   2529  CB  GLU C 341      19.367  28.943 -57.890  1.00 42.68           C  
ANISOU 2529  CB  GLU C 341     4325   5961   5928   -425   -356   -436       C  
ATOM   2530  CG  GLU C 341      19.178  30.427 -58.088  1.00 53.23           C  
ANISOU 2530  CG  GLU C 341     5639   7257   7329   -505   -321   -342       C  
ATOM   2531  CD  GLU C 341      20.274  31.029 -58.932  1.00 58.49           C  
ANISOU 2531  CD  GLU C 341     6197   8023   8003   -556   -284   -301       C  
ATOM   2532  OE1 GLU C 341      20.940  31.967 -58.452  1.00 63.00           O  
ANISOU 2532  OE1 GLU C 341     6730   8556   8650   -612   -286   -286       O  
ATOM   2533  OE2 GLU C 341      20.474  30.556 -60.071  1.00 59.99           O  
ANISOU 2533  OE2 GLU C 341     6336   8335   8123   -539   -255   -284       O  
ATOM   2534  N   PHE C 342      19.976  27.113 -55.137  1.00 32.20           N  
ANISOU 2534  N   PHE C 342     3107   4521   4607   -301   -480   -638       N  
ATOM   2535  CA  PHE C 342      19.411  26.833 -53.827  1.00 36.92           C  
ANISOU 2535  CA  PHE C 342     3790   5018   5221   -269   -520   -669       C  
ATOM   2536  C   PHE C 342      20.456  26.400 -52.809  1.00 37.26           C  
ANISOU 2536  C   PHE C 342     3823   5062   5271   -231   -568   -752       C  
ATOM   2537  O   PHE C 342      20.097  26.075 -51.674  1.00 33.54           O  
ANISOU 2537  O   PHE C 342     3420   4520   4804   -196   -603   -781       O  
ATOM   2538  CB  PHE C 342      18.309  25.778 -53.960  1.00 33.85           C  
ANISOU 2538  CB  PHE C 342     3473   4602   4788   -220   -529   -668       C  
ATOM   2539  CG  PHE C 342      17.282  26.127 -55.002  1.00 30.15           C  
ANISOU 2539  CG  PHE C 342     3009   4142   4305   -251   -487   -593       C  
ATOM   2540  CD1 PHE C 342      17.238  25.450 -56.212  1.00 33.06           C  
ANISOU 2540  CD1 PHE C 342     3347   4593   4622   -231   -473   -593       C  
ATOM   2541  CD2 PHE C 342      16.387  27.164 -54.787  1.00 30.49           C  
ANISOU 2541  CD2 PHE C 342     3083   4115   4386   -296   -463   -526       C  
ATOM   2542  CE1 PHE C 342      16.302  25.785 -57.180  1.00 34.41           C  
ANISOU 2542  CE1 PHE C 342     3519   4779   4775   -256   -437   -525       C  
ATOM   2543  CE2 PHE C 342      15.450  27.504 -55.749  1.00 32.75           C  
ANISOU 2543  CE2 PHE C 342     3372   4412   4660   -321   -427   -455       C  
ATOM   2544  CZ  PHE C 342      15.407  26.814 -56.948  1.00 37.85           C  
ANISOU 2544  CZ  PHE C 342     3987   5144   5250   -302   -413   -453       C  
ATOM   2545  N   ALA C 343      21.733  26.413 -53.177  1.00 32.17           N  
ANISOU 2545  N   ALA C 343     3093   4502   4627   -236   -568   -787       N  
ATOM   2546  CA  ALA C 343      22.807  26.050 -52.261  1.00 26.10           C  
ANISOU 2546  CA  ALA C 343     2305   3746   3866   -200   -616   -867       C  
ATOM   2547  C   ALA C 343      22.817  26.955 -51.039  1.00 32.36           C  
ANISOU 2547  C   ALA C 343     3124   4457   4716   -228   -639   -874       C  
ATOM   2548  O   ALA C 343      22.903  28.181 -51.159  1.00 40.40           O  
ANISOU 2548  O   ALA C 343     4106   5455   5789   -299   -615   -834       O  
ATOM   2549  CB  ALA C 343      24.154  26.114 -52.984  1.00 32.22           C  
ANISOU 2549  CB  ALA C 343     2969   4636   4639   -213   -604   -893       C  
ATOM   2550  N   GLY C 344      22.716  26.339 -49.861  1.00 32.51           N  
ANISOU 2550  N   GLY C 344     3206   4426   4721   -170   -687   -926       N  
ATOM   2551  CA  GLY C 344      22.833  27.032 -48.596  1.00 34.82           C  
ANISOU 2551  CA  GLY C 344     3522   4655   5052   -178   -719   -953       C  
ATOM   2552  C   GLY C 344      21.561  27.649 -48.054  1.00 40.17           C  
ANISOU 2552  C   GLY C 344     4277   5238   5746   -195   -708   -908       C  
ATOM   2553  O   GLY C 344      21.617  28.318 -47.014  1.00 43.05           O  
ANISOU 2553  O   GLY C 344     4661   5554   6144   -200   -734   -935       O  
ATOM   2554  N   CYS C 345      20.418  27.430 -48.699  1.00 36.01           N  
ANISOU 2554  N   CYS C 345     3793   4690   5198   -199   -673   -846       N  
ATOM   2555  CA  CYS C 345      19.210  28.178 -48.374  1.00 36.18           C  
ANISOU 2555  CA  CYS C 345     3874   4632   5242   -224   -653   -795       C  
ATOM   2556  C   CYS C 345      18.450  27.546 -47.213  1.00 32.11           C  
ANISOU 2556  C   CYS C 345     3444   4064   4692   -164   -682   -812       C  
ATOM   2557  O   CYS C 345      18.169  26.344 -47.222  1.00 44.91           O  
ANISOU 2557  O   CYS C 345     5102   5698   6266   -114   -694   -817       O  
ATOM   2558  CB  CYS C 345      18.304  28.271 -49.602  1.00 54.36           C  
ANISOU 2558  CB  CYS C 345     6177   6941   7535   -255   -603   -717       C  
ATOM   2559  SG  CYS C 345      19.087  29.042 -51.036  1.00 71.92           S  
ANISOU 2559  SG  CYS C 345     8298   9238   9788   -326   -560   -676       S  
ATOM   2560  N   LYS C 346      18.126  28.367 -46.212  1.00 33.75           N  
ANISOU 2560  N   LYS C 346     3684   4213   4927   -168   -695   -822       N  
ATOM   2561  CA  LYS C 346      17.199  27.999 -45.147  1.00 33.90           C  
ANISOU 2561  CA  LYS C 346     3783   4186   4912   -119   -710   -821       C  
ATOM   2562  C   LYS C 346      15.759  28.358 -45.481  1.00 37.49           C  
ANISOU 2562  C   LYS C 346     4281   4594   5369   -139   -670   -750       C  
ATOM   2563  O   LYS C 346      14.832  27.690 -45.003  1.00 40.38           O  
ANISOU 2563  O   LYS C 346     4707   4939   5695   -100   -669   -728       O  
ATOM   2564  CB  LYS C 346      17.581  28.690 -43.835  1.00 32.39           C  
ANISOU 2564  CB  LYS C 346     3602   3968   4738   -103   -748   -878       C  
ATOM   2565  CG  LYS C 346      18.723  28.052 -43.061  1.00 52.33           C  
ANISOU 2565  CG  LYS C 346     6111   6534   7238    -54   -801   -953       C  
ATOM   2566  CD  LYS C 346      18.975  28.817 -41.769  1.00 68.06           C  
ANISOU 2566  CD  LYS C 346     8115   8502   9244    -37   -839  -1012       C  
ATOM   2567  CE  LYS C 346      17.801  28.676 -40.804  1.00 81.11           C  
ANISOU 2567  CE  LYS C 346     9849  10118  10852     10   -838   -992       C  
ATOM   2568  NZ  LYS C 346      17.335  29.977 -40.237  1.00 88.50           N  
ANISOU 2568  NZ  LYS C 346    10795  11004  11825     -9   -838  -1007       N  
ATOM   2569  N   LYS C 347      15.556  29.398 -46.289  1.00 38.67           N  
ANISOU 2569  N   LYS C 347     4397   4728   5566   -199   -636   -709       N  
ATOM   2570  CA  LYS C 347      14.231  29.947 -46.548  1.00 37.74           C  
ANISOU 2570  CA  LYS C 347     4316   4565   5459   -218   -601   -644       C  
ATOM   2571  C   LYS C 347      14.153  30.343 -48.011  1.00 37.85           C  
ANISOU 2571  C   LYS C 347     4283   4601   5496   -273   -560   -584       C  
ATOM   2572  O   LYS C 347      14.980  31.128 -48.484  1.00 37.67           O  
ANISOU 2572  O   LYS C 347     4202   4591   5520   -320   -555   -584       O  
ATOM   2573  CB  LYS C 347      13.956  31.153 -45.645  1.00 36.53           C  
ANISOU 2573  CB  LYS C 347     4181   4350   5350   -225   -611   -662       C  
ATOM   2574  CG  LYS C 347      12.541  31.696 -45.729  1.00 51.81           C  
ANISOU 2574  CG  LYS C 347     6157   6237   7293   -230   -579   -604       C  
ATOM   2575  CD  LYS C 347      12.328  32.826 -44.731  1.00 56.91           C  
ANISOU 2575  CD  LYS C 347     6822   6823   7978   -224   -597   -637       C  
ATOM   2576  CE  LYS C 347      10.942  33.439 -44.871  1.00 59.21           C  
ANISOU 2576  CE  LYS C 347     7147   7068   8281   -226   -566   -581       C  
ATOM   2577  NZ  LYS C 347      10.664  34.446 -43.807  1.00 59.37           N  
ANISOU 2577  NZ  LYS C 347     7192   7034   8334   -204   -587   -626       N  
ATOM   2578  N   ILE C 348      13.163  29.812 -48.722  1.00 30.87           N  
ANISOU 2578  N   ILE C 348     3423   3725   4580   -268   -532   -530       N  
ATOM   2579  CA  ILE C 348      12.985  30.068 -50.147  1.00 26.28           C  
ANISOU 2579  CA  ILE C 348     2802   3178   4006   -311   -494   -471       C  
ATOM   2580  C   ILE C 348      11.755  30.943 -50.333  1.00 31.00           C  
ANISOU 2580  C   ILE C 348     3427   3723   4629   -333   -465   -405       C  
ATOM   2581  O   ILE C 348      10.650  30.578 -49.911  1.00 32.93           O  
ANISOU 2581  O   ILE C 348     3725   3938   4850   -303   -463   -390       O  
ATOM   2582  CB  ILE C 348      12.864  28.762 -50.946  1.00 19.94           C  
ANISOU 2582  CB  ILE C 348     1997   2433   3146   -285   -491   -468       C  
ATOM   2583  CG1 ILE C 348      14.236  28.099 -51.078  1.00 23.75           C  
ANISOU 2583  CG1 ILE C 348     2433   2979   3611   -269   -514   -527       C  
ATOM   2584  CG2 ILE C 348      12.263  29.020 -52.317  1.00 16.62           C  
ANISOU 2584  CG2 ILE C 348     1552   2044   2718   -318   -451   -399       C  
ATOM   2585  CD1 ILE C 348      14.188  26.722 -51.701  1.00 30.92           C  
ANISOU 2585  CD1 ILE C 348     3345   3936   4466   -230   -523   -544       C  
ATOM   2586  N   PHE C 349      11.952  32.099 -50.962  1.00 28.33           N  
ANISOU 2586  N   PHE C 349     3048   3374   4342   -385   -444   -363       N  
ATOM   2587  CA  PHE C 349      10.864  33.016 -51.289  1.00 26.28           C  
ANISOU 2587  CA  PHE C 349     2807   3066   4114   -407   -417   -296       C  
ATOM   2588  C   PHE C 349      10.384  32.667 -52.690  1.00 34.32           C  
ANISOU 2588  C   PHE C 349     3803   4141   5097   -422   -383   -230       C  
ATOM   2589  O   PHE C 349      10.991  33.066 -53.687  1.00 36.61           O  
ANISOU 2589  O   PHE C 349     4036   4476   5399   -462   -363   -192       O  
ATOM   2590  CB  PHE C 349      11.331  34.462 -51.189  1.00 30.58           C  
ANISOU 2590  CB  PHE C 349     3322   3558   4740   -454   -417   -283       C  
ATOM   2591  CG  PHE C 349      11.631  34.904 -49.785  1.00 31.23           C  
ANISOU 2591  CG  PHE C 349     3430   3579   4858   -435   -456   -354       C  
ATOM   2592  CD1 PHE C 349      12.834  34.570 -49.181  1.00 31.49           C  
ANISOU 2592  CD1 PHE C 349     3438   3636   4891   -428   -489   -428       C  
ATOM   2593  CD2 PHE C 349      10.714  35.655 -49.068  1.00 21.60           C  
ANISOU 2593  CD2 PHE C 349     2255   2284   3668   -418   -461   -353       C  
ATOM   2594  CE1 PHE C 349      13.115  34.972 -47.889  1.00 35.29           C  
ANISOU 2594  CE1 PHE C 349     3941   4069   5398   -405   -528   -499       C  
ATOM   2595  CE2 PHE C 349      10.991  36.063 -47.772  1.00 33.60           C  
ANISOU 2595  CE2 PHE C 349     3797   3756   5214   -393   -499   -427       C  
ATOM   2596  CZ  PHE C 349      12.193  35.721 -47.184  1.00 38.95           C  
ANISOU 2596  CZ  PHE C 349     4451   4460   5888   -387   -533   -500       C  
ATOM   2597  N   GLY C 350       9.291  31.913 -52.765  1.00 26.06           N  
ANISOU 2597  N   GLY C 350     2798   3098   4005   -389   -378   -214       N  
ATOM   2598  CA  GLY C 350       8.810  31.329 -53.994  1.00 20.40           C  
ANISOU 2598  CA  GLY C 350     2065   2442   3244   -391   -356   -171       C  
ATOM   2599  C   GLY C 350       8.479  29.872 -53.775  1.00 25.11           C  
ANISOU 2599  C   GLY C 350     2694   3062   3787   -346   -376   -211       C  
ATOM   2600  O   GLY C 350       8.237  29.434 -52.644  1.00 24.00           O  
ANISOU 2600  O   GLY C 350     2598   2878   3642   -314   -399   -249       O  
ATOM   2601  N   SER C 351       8.487  29.104 -54.862  1.00 22.51           N  
ANISOU 2601  N   SER C 351     2339   2800   3413   -342   -370   -204       N  
ATOM   2602  CA  SER C 351       8.046  27.720 -54.826  1.00 30.44           C  
ANISOU 2602  CA  SER C 351     3372   3818   4376   -303   -392   -237       C  
ATOM   2603  C   SER C 351       9.087  26.815 -55.471  1.00 27.29           C  
ANISOU 2603  C   SER C 351     2935   3492   3942   -287   -408   -287       C  
ATOM   2604  O   SER C 351      10.066  27.268 -56.070  1.00 25.34           O  
ANISOU 2604  O   SER C 351     2632   3300   3695   -307   -395   -289       O  
ATOM   2605  CB  SER C 351       6.693  27.553 -55.529  1.00 27.96           C  
ANISOU 2605  CB  SER C 351     3072   3507   4043   -305   -377   -186       C  
ATOM   2606  OG  SER C 351       5.712  28.383 -54.931  1.00 26.62           O  
ANISOU 2606  OG  SER C 351     2935   3275   3904   -313   -362   -142       O  
ATOM   2607  N   LEU C 352       8.855  25.513 -55.329  1.00 19.50           N  
ANISOU 2607  N   LEU C 352     1976   2505   2927   -249   -437   -328       N  
ATOM   2608  CA  LEU C 352       9.687  24.476 -55.929  1.00 28.06           C  
ANISOU 2608  CA  LEU C 352     3031   3652   3978   -220   -460   -386       C  
ATOM   2609  C   LEU C 352       8.789  23.499 -56.669  1.00 26.14           C  
ANISOU 2609  C   LEU C 352     2802   3424   3706   -201   -473   -388       C  
ATOM   2610  O   LEU C 352       7.856  22.940 -56.083  1.00 24.46           O  
ANISOU 2610  O   LEU C 352     2640   3149   3504   -189   -490   -381       O  
ATOM   2611  CB  LEU C 352      10.521  23.732 -54.879  1.00 25.32           C  
ANISOU 2611  CB  LEU C 352     2705   3279   3637   -184   -499   -453       C  
ATOM   2612  CG  LEU C 352      11.384  24.561 -53.912  1.00 32.22           C  
ANISOU 2612  CG  LEU C 352     3572   4130   4542   -195   -500   -466       C  
ATOM   2613  CD1 LEU C 352      12.054  23.673 -52.867  1.00 16.07           C  
ANISOU 2613  CD1 LEU C 352     1552   2061   2492   -149   -544   -530       C  
ATOM   2614  CD2 LEU C 352      12.422  25.356 -54.677  1.00 34.59           C  
ANISOU 2614  CD2 LEU C 352     3798   4498   4845   -227   -476   -464       C  
ATOM   2615  N   ALA C 353       9.071  23.298 -57.951  1.00 20.00           N  
ANISOU 2615  N   ALA C 353     1977   2731   2892   -198   -465   -397       N  
ATOM   2616  CA  ALA C 353       8.349  22.344 -58.779  1.00 24.53           C  
ANISOU 2616  CA  ALA C 353     2554   3330   3435   -176   -484   -414       C  
ATOM   2617  C   ALA C 353       9.340  21.373 -59.405  1.00 32.71           C  
ANISOU 2617  C   ALA C 353     3556   4437   4436   -134   -513   -494       C  
ATOM   2618  O   ALA C 353      10.311  21.791 -60.048  1.00 32.36           O  
ANISOU 2618  O   ALA C 353     3452   4478   4365   -136   -492   -503       O  
ATOM   2619  CB  ALA C 353       7.541  23.054 -59.866  1.00 16.30           C  
ANISOU 2619  CB  ALA C 353     1486   2335   2371   -203   -450   -351       C  
ATOM   2620  N   PHE C 354       9.095  20.081 -59.210  1.00 33.12           N  
ANISOU 2620  N   PHE C 354     3642   4453   4491    -96   -560   -550       N  
ATOM   2621  CA  PHE C 354       9.883  19.014 -59.811  1.00 30.19           C  
ANISOU 2621  CA  PHE C 354     3244   4138   4090    -45   -597   -636       C  
ATOM   2622  C   PHE C 354       8.991  18.295 -60.815  1.00 34.69           C  
ANISOU 2622  C   PHE C 354     3814   4731   4638    -31   -618   -655       C  
ATOM   2623  O   PHE C 354       8.057  17.582 -60.433  1.00 34.40           O  
ANISOU 2623  O   PHE C 354     3825   4614   4632    -28   -650   -656       O  
ATOM   2624  CB  PHE C 354      10.424  18.062 -58.748  1.00 24.27           C  
ANISOU 2624  CB  PHE C 354     2533   3319   3371     -7   -645   -693       C  
ATOM   2625  CG  PHE C 354      11.348  18.726 -57.768  1.00 29.57           C  
ANISOU 2625  CG  PHE C 354     3201   3976   4060    -16   -631   -685       C  
ATOM   2626  CD1 PHE C 354      10.852  19.322 -56.620  1.00 31.56           C  
ANISOU 2626  CD1 PHE C 354     3497   4146   4346    -45   -618   -631       C  
ATOM   2627  CD2 PHE C 354      12.712  18.771 -58.005  1.00 30.07           C  
ANISOU 2627  CD2 PHE C 354     3210   4113   4101      7   -631   -735       C  
ATOM   2628  CE1 PHE C 354      11.700  19.938 -55.721  1.00 28.02           C  
ANISOU 2628  CE1 PHE C 354     3044   3688   3914    -50   -611   -634       C  
ATOM   2629  CE2 PHE C 354      13.565  19.386 -57.111  1.00 27.86           C  
ANISOU 2629  CE2 PHE C 354     2922   3822   3842     -4   -623   -733       C  
ATOM   2630  CZ  PHE C 354      13.059  19.971 -55.967  1.00 28.75           C  
ANISOU 2630  CZ  PHE C 354     3083   3849   3991    -32   -616   -685       C  
ATOM   2631  N   LEU C 355       9.270  18.510 -62.087  1.00 36.12           N  
ANISOU 2631  N   LEU C 355     3936   5025   4763    -22   -600   -667       N  
ATOM   2632  CA  LEU C 355       8.532  17.960 -63.205  1.00 34.64           C  
ANISOU 2632  CA  LEU C 355     3736   4886   4542     -5   -619   -691       C  
ATOM   2633  C   LEU C 355       9.366  16.877 -63.876  1.00 40.86           C  
ANISOU 2633  C   LEU C 355     4492   5742   5293     60   -661   -799       C  
ATOM   2634  O   LEU C 355      10.568  16.769 -63.616  1.00 40.27           O  
ANISOU 2634  O   LEU C 355     4393   5697   5211     86   -663   -842       O  
ATOM   2635  CB  LEU C 355       8.198  19.077 -64.207  1.00 30.85           C  
ANISOU 2635  CB  LEU C 355     3209   4499   4015    -37   -565   -619       C  
ATOM   2636  CG  LEU C 355       6.953  19.953 -63.988  1.00 32.01           C  
ANISOU 2636  CG  LEU C 355     3383   4590   4188    -88   -535   -522       C  
ATOM   2637  CD1 LEU C 355       6.829  20.438 -62.552  1.00 37.03           C  
ANISOU 2637  CD1 LEU C 355     4069   5112   4888   -119   -524   -477       C  
ATOM   2638  CD2 LEU C 355       6.990  21.143 -64.936  1.00 27.79           C  
ANISOU 2638  CD2 LEU C 355     2797   4155   3609   -114   -481   -449       C  
ATOM   2639  N   PRO C 356       8.762  16.027 -64.713  1.00 44.38           N  
ANISOU 2639  N   PRO C 356     4936   6210   5718     90   -701   -854       N  
ATOM   2640  CA  PRO C 356       9.581  15.066 -65.475  1.00 43.82           C  
ANISOU 2640  CA  PRO C 356     4828   6217   5604    160   -741   -966       C  
ATOM   2641  C   PRO C 356      10.771  15.714 -66.167  1.00 42.74           C  
ANISOU 2641  C   PRO C 356     4614   6226   5397    176   -696   -971       C  
ATOM   2642  O   PRO C 356      11.887  15.174 -66.128  1.00 46.71           O  
ANISOU 2642  O   PRO C 356     5092   6770   5888    226   -716  -1048       O  
ATOM   2643  CB  PRO C 356       8.570  14.481 -66.469  1.00 37.68           C  
ANISOU 2643  CB  PRO C 356     4047   5465   4803    176   -776  -1002       C  
ATOM   2644  CG  PRO C 356       7.277  14.506 -65.712  1.00 30.25           C  
ANISOU 2644  CG  PRO C 356     3170   4394   3931    126   -785   -938       C  
ATOM   2645  CD  PRO C 356       7.318  15.770 -64.874  1.00 38.10           C  
ANISOU 2645  CD  PRO C 356     4175   5357   4946     69   -721   -828       C  
ATOM   2646  N   GLU C 357      10.567  16.897 -66.753  1.00 45.65           N  
ANISOU 2646  N   GLU C 357     4944   6674   5725    133   -634   -884       N  
ATOM   2647  CA  GLU C 357      11.653  17.620 -67.403  1.00 45.25           C  
ANISOU 2647  CA  GLU C 357     4816   6764   5613    136   -583   -867       C  
ATOM   2648  C   GLU C 357      12.772  17.984 -66.435  1.00 47.95           C  
ANISOU 2648  C   GLU C 357     5150   7075   5993    122   -566   -859       C  
ATOM   2649  O   GLU C 357      13.881  18.299 -66.882  1.00 44.82           O  
ANISOU 2649  O   GLU C 357     4684   6792   5552    135   -537   -871       O  
ATOM   2650  CB  GLU C 357      11.113  18.885 -68.071  1.00 44.49           C  
ANISOU 2650  CB  GLU C 357     4690   6733   5483     83   -521   -753       C  
ATOM   2651  CG  GLU C 357      10.436  19.855 -67.116  1.00 57.27           C  
ANISOU 2651  CG  GLU C 357     6356   8232   7171     12   -492   -648       C  
ATOM   2652  CD  GLU C 357       9.766  21.006 -67.837  1.00 66.68           C  
ANISOU 2652  CD  GLU C 357     7524   9477   8334    -32   -440   -540       C  
ATOM   2653  OE1 GLU C 357      10.477  21.945 -68.247  1.00 69.23           O  
ANISOU 2653  OE1 GLU C 357     7791   9884   8629    -57   -388   -479       O  
ATOM   2654  OE2 GLU C 357       8.528  20.966 -68.002  1.00 70.27           O  
ANISOU 2654  OE2 GLU C 357     8014   9890   8796    -42   -453   -512       O  
ATOM   2655  N   SER C 358      12.513  17.954 -65.123  1.00 42.40           N  
ANISOU 2655  N   SER C 358     4513   6228   5367     97   -584   -841       N  
ATOM   2656  CA  SER C 358      13.586  18.194 -64.165  1.00 38.93           C  
ANISOU 2656  CA  SER C 358     4068   5760   4962     92   -579   -848       C  
ATOM   2657  C   SER C 358      14.716  17.196 -64.338  1.00 49.18           C  
ANISOU 2657  C   SER C 358     5333   7118   6235    164   -617   -959       C  
ATOM   2658  O   SER C 358      15.881  17.532 -64.102  1.00 61.55           O  
ANISOU 2658  O   SER C 358     6852   8736   7797    167   -599   -970       O  
ATOM   2659  CB  SER C 358      13.065  18.122 -62.729  1.00 29.90           C  
ANISOU 2659  CB  SER C 358     3005   4460   3896     68   -602   -823       C  
ATOM   2660  OG  SER C 358      12.103  19.127 -62.475  1.00 26.41           O  
ANISOU 2660  OG  SER C 358     2590   3965   3480      6   -564   -724       O  
ATOM   2661  N   PHE C 359      14.399  15.972 -64.756  1.00 53.87           N  
ANISOU 2661  N   PHE C 359     5947   7705   6817    224   -673  -1045       N  
ATOM   2662  CA  PHE C 359      15.377  14.895 -64.771  1.00 59.21           C  
ANISOU 2662  CA  PHE C 359     6604   8410   7482    302   -722  -1160       C  
ATOM   2663  C   PHE C 359      15.759  14.493 -66.192  1.00 65.37           C  
ANISOU 2663  C   PHE C 359     7314   9345   8178    359   -724  -1232       C  
ATOM   2664  O   PHE C 359      16.154  13.352 -66.442  1.00 64.20           O  
ANISOU 2664  O   PHE C 359     7163   9211   8020    437   -781  -1345       O  
ATOM   2665  CB  PHE C 359      14.847  13.718 -63.956  1.00 23.75           C  
ANISOU 2665  CB  PHE C 359     2196   3772   3057    333   -796  -1211       C  
ATOM   2666  CG  PHE C 359      14.500  14.100 -62.542  1.00 20.17           C  
ANISOU 2666  CG  PHE C 359     1806   3183   2673    283   -791  -1138       C  
ATOM   2667  CD1 PHE C 359      13.182  14.329 -62.171  1.00 34.14           C  
ANISOU 2667  CD1 PHE C 359     3635   4857   4480    232   -786  -1066       C  
ATOM   2668  CD2 PHE C 359      15.500  14.295 -61.599  1.00 22.40           C  
ANISOU 2668  CD2 PHE C 359     2086   3448   2979    289   -790  -1143       C  
ATOM   2669  CE1 PHE C 359      12.864  14.711 -60.870  1.00 30.73           C  
ANISOU 2669  CE1 PHE C 359     3258   4314   4103    191   -778  -1001       C  
ATOM   2670  CE2 PHE C 359      15.191  14.677 -60.298  1.00 25.85           C  
ANISOU 2670  CE2 PHE C 359     2579   3772   3470    249   -786  -1080       C  
ATOM   2671  CZ  PHE C 359      13.871  14.886 -59.934  1.00 26.21           C  
ANISOU 2671  CZ  PHE C 359     2684   3726   3549    202   -779  -1010       C  
ATOM   2672  N   ASP C 360      15.641  15.437 -67.126  1.00 74.63           N  
ANISOU 2672  N   ASP C 360     8430  10637   9289    325   -663  -1167       N  
ATOM   2673  CA  ASP C 360      16.158  15.313 -68.486  1.00 83.06           C  
ANISOU 2673  CA  ASP C 360     9415  11885  10261    375   -647  -1217       C  
ATOM   2674  C   ASP C 360      17.026  16.538 -68.742  1.00 88.53           C  
ANISOU 2674  C   ASP C 360    10027  12695  10915    331   -568  -1135       C  
ATOM   2675  O   ASP C 360      16.523  17.666 -68.740  1.00 93.86           O  
ANISOU 2675  O   ASP C 360    10703  13359  11600    255   -515  -1016       O  
ATOM   2676  CB  ASP C 360      15.030  15.229 -69.515  1.00 88.17           C  
ANISOU 2676  CB  ASP C 360    10066  12574  10860    378   -651  -1208       C  
ATOM   2677  CG  ASP C 360      13.898  14.317 -69.079  1.00 91.97           C  
ANISOU 2677  CG  ASP C 360    10635  12906  11405    386   -720  -1249       C  
ATOM   2678  OD1 ASP C 360      12.746  14.573 -69.489  1.00 94.30           O  
ANISOU 2678  OD1 ASP C 360    10951  13184  11694    354   -715  -1200       O  
ATOM   2679  OD2 ASP C 360      14.151  13.342 -68.344  1.00 89.91           O  
ANISOU 2679  OD2 ASP C 360    10417  12545  11201    425   -780  -1326       O  
ATOM   2680  N   GLY C 361      18.322  16.323 -68.962  1.00 87.69           N  
ANISOU 2680  N   GLY C 361     9849  12699  10770    377   -562  -1196       N  
ATOM   2681  CA  GLY C 361      19.261  17.415 -69.102  1.00 87.66           C  
ANISOU 2681  CA  GLY C 361     9764  12800  10744    332   -491  -1121       C  
ATOM   2682  C   GLY C 361      19.191  18.105 -70.450  1.00 89.14           C  
ANISOU 2682  C   GLY C 361     9873  13158  10837    318   -430  -1058       C  
ATOM   2683  O   GLY C 361      18.368  17.794 -71.311  1.00 96.37           O  
ANISOU 2683  O   GLY C 361    10799  14118  11699    345   -441  -1071       O  
ATOM   2684  N   ASP C 362      20.088  19.078 -70.627  1.00 81.15           N  
ANISOU 2684  N   ASP C 362     8780  12246   9807    274   -365   -983       N  
ATOM   2685  CA  ASP C 362      20.186  19.854 -71.860  1.00 80.80           C  
ANISOU 2685  CA  ASP C 362     8651  12375   9674    253   -296   -902       C  
ATOM   2686  C   ASP C 362      21.479  19.490 -72.580  1.00 85.56           C  
ANISOU 2686  C   ASP C 362     9143  13172  10193    317   -277   -970       C  
ATOM   2687  O   ASP C 362      22.543  20.056 -72.285  1.00 80.24           O  
ANISOU 2687  O   ASP C 362     8404  12547   9538    283   -239   -935       O  
ATOM   2688  CB  ASP C 362      20.131  21.356 -71.569  1.00 74.52           C  
ANISOU 2688  CB  ASP C 362     7842  11543   8929    143   -231   -744       C  
ATOM   2689  CG  ASP C 362      20.012  22.186 -72.831  1.00 74.75           C  
ANISOU 2689  CG  ASP C 362     7798  11730   8873    117   -163   -638       C  
ATOM   2690  OD1 ASP C 362      18.895  22.658 -73.134  1.00 83.48           O  
ANISOU 2690  OD1 ASP C 362     8947  12793   9977     83   -153   -559       O  
ATOM   2691  OD2 ASP C 362      21.033  22.359 -73.528  1.00 69.88           O  
ANISOU 2691  OD2 ASP C 362     7076  11286   8188    131   -120   -631       O  
ATOM   2692  N   PRO C 363      21.442  18.556 -73.535  1.00 90.44           N  
ANISOU 2692  N   PRO C 363     9735  13911  10718    411   -304  -1072       N  
ATOM   2693  CA  PRO C 363      22.681  18.156 -74.222  1.00 91.21           C  
ANISOU 2693  CA  PRO C 363     9723  14203  10727    483   -288  -1148       C  
ATOM   2694  C   PRO C 363      23.266  19.228 -75.128  1.00 94.72           C  
ANISOU 2694  C   PRO C 363    10054  14842  11094    439   -194  -1031       C  
ATOM   2695  O   PRO C 363      24.429  19.097 -75.530  1.00 98.72           O  
ANISOU 2695  O   PRO C 363    10458  15509  11540    480   -168  -1071       O  
ATOM   2696  CB  PRO C 363      22.253  16.923 -75.030  1.00 85.75           C  
ANISOU 2696  CB  PRO C 363     9046  13576   9958    595   -346  -1286       C  
ATOM   2697  CG  PRO C 363      20.773  17.074 -75.197  1.00 84.29           C  
ANISOU 2697  CG  PRO C 363     8943  13294   9788    559   -362  -1233       C  
ATOM   2698  CD  PRO C 363      20.288  17.738 -73.944  1.00 85.44           C  
ANISOU 2698  CD  PRO C 363     9171  13232  10061    461   -360  -1138       C  
ATOM   2699  N   ALA C 364      22.507  20.273 -75.471  1.00 90.45           N  
ANISOU 2699  N   ALA C 364     9524  14293  10551    358   -144   -886       N  
ATOM   2700  CA  ALA C 364      23.047  21.333 -76.318  1.00 85.63           C  
ANISOU 2700  CA  ALA C 364     8805  13857   9873    310    -54   -757       C  
ATOM   2701  C   ALA C 364      24.235  22.011 -75.647  1.00 89.15           C  
ANISOU 2701  C   ALA C 364     9187  14301  10384    246    -15   -704       C  
ATOM   2702  O   ALA C 364      25.272  22.248 -76.278  1.00 89.58           O  
ANISOU 2702  O   ALA C 364     9141  14525  10370    253     37   -681       O  
ATOM   2703  CB  ALA C 364      21.956  22.352 -76.648  1.00 76.32           C  
ANISOU 2703  CB  ALA C 364     7663  12633   8701    232    -17   -604       C  
ATOM   2704  N   SER C 365      24.099  22.326 -74.363  1.00 87.09           N  
ANISOU 2704  N   SER C 365     8999  13835  10255    182    -41   -684       N  
ATOM   2705  CA  SER C 365      25.177  22.885 -73.562  1.00 86.74           C  
ANISOU 2705  CA  SER C 365     8907  13763  10289    124    -21   -655       C  
ATOM   2706  C   SER C 365      25.959  21.820 -72.808  1.00 87.46           C  
ANISOU 2706  C   SER C 365     9004  13821  10406    198    -82   -809       C  
ATOM   2707  O   SER C 365      26.760  22.162 -71.931  1.00 93.72           O  
ANISOU 2707  O   SER C 365     9774  14558  11277    156    -82   -804       O  
ATOM   2708  CB  SER C 365      24.611  23.907 -72.575  1.00 83.07           C  
ANISOU 2708  CB  SER C 365     8515  13100   9949     15    -17   -547       C  
ATOM   2709  OG  SER C 365      23.381  23.451 -72.048  1.00 82.13           O  
ANISOU 2709  OG  SER C 365     8522  12812   9871     32    -73   -583       O  
ATOM   2710  N   ASN C 366      25.746  20.544 -73.132  1.00 83.14           N  
ANISOU 2710  N   ASN C 366     8486  13304   9800    309   -138   -947       N  
ATOM   2711  CA  ASN C 366      26.355  19.425 -72.415  1.00 87.54           C  
ANISOU 2711  CA  ASN C 366     9065  13810  10387    389   -207  -1098       C  
ATOM   2712  C   ASN C 366      26.085  19.526 -70.915  1.00 87.43           C  
ANISOU 2712  C   ASN C 366     9149  13565  10504    339   -253  -1092       C  
ATOM   2713  O   ASN C 366      26.977  19.355 -70.080  1.00 86.67           O  
ANISOU 2713  O   ASN C 366     9036  13435  10461    347   -275  -1141       O  
ATOM   2714  CB  ASN C 366      27.855  19.332 -72.701  1.00 94.11           C  
ANISOU 2714  CB  ASN C 366     9821  14770  11168    419   -174  -1130       C  
ATOM   2715  CG  ASN C 366      28.158  19.184 -74.178  1.00102.13           C  
ANISOU 2715  CG  ASN C 366    10767  15998  12039    472   -129  -1133       C  
ATOM   2716  OD1 ASN C 366      29.057  19.837 -74.708  1.00101.25           O  
ANISOU 2716  OD1 ASN C 366    10576  16016  11880    438    -63  -1060       O  
ATOM   2717  ND2 ASN C 366      27.400  18.327 -74.854  1.00107.19           N  
ANISOU 2717  ND2 ASN C 366    11441  16675  12611    556   -167  -1218       N  
ATOM   2718  N   THR C 367      24.833  19.815 -70.575  1.00 90.79           N  
ANISOU 2718  N   THR C 367     9677  13840  10979    290   -265  -1031       N  
ATOM   2719  CA  THR C 367      24.393  19.885 -69.188  1.00 88.98           C  
ANISOU 2719  CA  THR C 367     9549  13397  10864    249   -308  -1023       C  
ATOM   2720  C   THR C 367      23.690  18.581 -68.835  1.00 91.13           C  
ANISOU 2720  C   THR C 367     9919  13559  11148    327   -389  -1135       C  
ATOM   2721  O   THR C 367      22.629  18.273 -69.389  1.00 94.38           O  
ANISOU 2721  O   THR C 367    10379  13951  11529    343   -402  -1134       O  
ATOM   2722  CB  THR C 367      23.468  21.080 -68.960  1.00 82.79           C  
ANISOU 2722  CB  THR C 367     8812  12513  10133    144   -270   -882       C  
ATOM   2723  OG1 THR C 367      24.158  22.291 -69.291  1.00 85.75           O  
ANISOU 2723  OG1 THR C 367     9094  12979  10507     68   -198   -774       O  
ATOM   2724  CG2 THR C 367      23.035  21.141 -67.505  1.00 78.32           C  
ANISOU 2724  CG2 THR C 367     8346  11738   9675    109   -313   -881       C  
ATOM   2725  N   ALA C 368      24.287  17.819 -67.923  1.00 88.24           N  
ANISOU 2725  N   ALA C 368     9578  13120  10829    375   -445  -1228       N  
ATOM   2726  CA  ALA C 368      23.741  16.528 -67.544  1.00 84.16           C  
ANISOU 2726  CA  ALA C 368     9150  12495  10333    451   -526  -1332       C  
ATOM   2727  C   ALA C 368      22.397  16.700 -66.833  1.00 82.07           C  
ANISOU 2727  C   ALA C 368     9001  12046  10138    396   -546  -1269       C  
ATOM   2728  O   ALA C 368      22.126  17.752 -66.248  1.00 85.22           O  
ANISOU 2728  O   ALA C 368     9418  12375  10586    308   -509  -1165       O  
ATOM   2729  CB  ALA C 368      24.720  15.785 -66.637  1.00 81.71           C  
ANISOU 2729  CB  ALA C 368     8840  12143  10064    509   -580  -1427       C  
ATOM   2730  N   PRO C 369      21.535  15.686 -66.881  1.00 77.28           N  
ANISOU 2730  N   PRO C 369     8468  11359   9536    446   -605  -1333       N  
ATOM   2731  CA  PRO C 369      20.252  15.772 -66.173  1.00 63.02           C  
ANISOU 2731  CA  PRO C 369     6767   9382   7797    396   -624  -1275       C  
ATOM   2732  C   PRO C 369      20.451  15.874 -64.670  1.00 58.07           C  
ANISOU 2732  C   PRO C 369     6196   8612   7255    369   -647  -1257       C  
ATOM   2733  O   PRO C 369      21.509  15.545 -64.128  1.00 63.12           O  
ANISOU 2733  O   PRO C 369     6810   9263   7909    406   -670  -1315       O  
ATOM   2734  CB  PRO C 369      19.543  14.465 -66.550  1.00 61.48           C  
ANISOU 2734  CB  PRO C 369     6622   9143   7592    468   -692  -1369       C  
ATOM   2735  CG  PRO C 369      20.244  13.983 -67.784  1.00 67.08           C  
ANISOU 2735  CG  PRO C 369     7248  10030   8211    545   -692  -1456       C  
ATOM   2736  CD  PRO C 369      21.661  14.433 -67.646  1.00 73.92           C  
ANISOU 2736  CD  PRO C 369     8029  11000   9058    550   -656  -1460       C  
ATOM   2737  N   LEU C 370      19.406  16.346 -63.994  1.00 53.05           N  
ANISOU 2737  N   LEU C 370     5637   7847   6674    306   -642  -1177       N  
ATOM   2738  CA  LEU C 370      19.470  16.513 -62.548  1.00 46.67           C  
ANISOU 2738  CA  LEU C 370     4886   6907   5940    279   -661  -1153       C  
ATOM   2739  C   LEU C 370      19.662  15.160 -61.879  1.00 44.36           C  
ANISOU 2739  C   LEU C 370     4646   6534   5676    355   -738  -1248       C  
ATOM   2740  O   LEU C 370      18.861  14.240 -62.072  1.00 55.03           O  
ANISOU 2740  O   LEU C 370     6050   7824   7034    389   -782  -1284       O  
ATOM   2741  CB  LEU C 370      18.205  17.195 -62.032  1.00 38.36           C  
ANISOU 2741  CB  LEU C 370     3903   5741   4930    208   -642  -1056       C  
ATOM   2742  CG  LEU C 370      18.280  17.654 -60.576  1.00 36.88           C  
ANISOU 2742  CG  LEU C 370     3765   5440   4809    172   -648  -1019       C  
ATOM   2743  CD1 LEU C 370      19.523  18.507 -60.367  1.00 40.62           C  
ANISOU 2743  CD1 LEU C 370     4166   5984   5284    147   -616  -1009       C  
ATOM   2744  CD2 LEU C 370      17.028  18.420 -60.180  1.00 35.21           C  
ANISOU 2744  CD2 LEU C 370     3611   5135   4631    106   -622   -924       C  
ATOM   2745  N   GLN C 371      20.712  15.041 -61.119  1.00 38.57           N  
ANISOU 2745  N   GLN C 371     3894   5798   4962    380   -757  -1285       N  
ATOM   2746  CA  GLN C 371      21.105  13.785 -60.504  1.00 39.77           C  
ANISOU 2746  CA  GLN C 371     4084   5886   5139    460   -831  -1375       C  
ATOM   2747  C   GLN C 371      20.643  13.728 -59.053  1.00 41.43           C  
ANISOU 2747  C   GLN C 371     4383   5942   5415    438   -860  -1333       C  
ATOM   2748  O   GLN C 371      20.628  14.756 -58.366  1.00 41.57           O  
ANISOU 2748  O   GLN C 371     4405   5935   5455    374   -823  -1261       O  
ATOM   2749  CB  GLN C 371      22.623  13.612 -60.572  1.00 34.89           C  
ANISOU 2749  CB  GLN C 371     3386   5374   4496    515   -839  -1449       C  
ATOM   2750  CG  GLN C 371      23.168  13.552 -61.997  1.00 42.38           C  
ANISOU 2750  CG  GLN C 371     4240   6493   5371    550   -812  -1499       C  
ATOM   2751  CD  GLN C 371      22.758  12.286 -62.731  1.00 58.82           C  
ANISOU 2751  CD  GLN C 371     6346   8574   7429    632   -866  -1590       C  
ATOM   2752  OE1 GLN C 371      22.919  11.179 -62.217  1.00 66.02           O  
ANISOU 2752  OE1 GLN C 371     7311   9399   8375    701   -928  -1659       O  
ATOM   2753  NE2 GLN C 371      22.229  12.444 -63.941  1.00 59.89           N  
ANISOU 2753  NE2 GLN C 371     6450   8797   7508    624   -836  -1583       N  
ATOM   2754  N   PRO C 372      20.265  12.539 -58.579  1.00 38.73           N  
ANISOU 2754  N   PRO C 372     4112   5498   5106    491   -926  -1376       N  
ATOM   2755  CA  PRO C 372      19.710  12.424 -57.217  1.00 31.43           C  
ANISOU 2755  CA  PRO C 372     3274   4432   4237    472   -951  -1326       C  
ATOM   2756  C   PRO C 372      20.602  12.996 -56.130  1.00 41.33           C  
ANISOU 2756  C   PRO C 372     4515   5684   5505    464   -946  -1313       C  
ATOM   2757  O   PRO C 372      20.095  13.439 -55.091  1.00 45.28           O  
ANISOU 2757  O   PRO C 372     5070   6100   6036    424   -940  -1248       O  
ATOM   2758  CB  PRO C 372      19.528  10.909 -57.048  1.00 29.33           C  
ANISOU 2758  CB  PRO C 372     3063   4082   4001    546  -1029  -1391       C  
ATOM   2759  CG  PRO C 372      19.416  10.381 -58.441  1.00 32.05           C  
ANISOU 2759  CG  PRO C 372     3369   4499   4310    581  -1038  -1457       C  
ATOM   2760  CD  PRO C 372      20.293  11.247 -59.285  1.00 33.44           C  
ANISOU 2760  CD  PRO C 372     3444   4836   4425    571   -982  -1472       C  
ATOM   2761  N   GLU C 373      21.919  13.001 -56.337  1.00 48.62           N  
ANISOU 2761  N   GLU C 373     5364   6706   6404    504   -951  -1377       N  
ATOM   2762  CA  GLU C 373      22.827  13.544 -55.333  1.00 50.69           C  
ANISOU 2762  CA  GLU C 373     5606   6974   6681    498   -951  -1373       C  
ATOM   2763  C   GLU C 373      22.702  15.058 -55.222  1.00 50.43           C  
ANISOU 2763  C   GLU C 373     5543   6967   6651    405   -885  -1294       C  
ATOM   2764  O   GLU C 373      22.872  15.615 -54.132  1.00 48.73           O  
ANISOU 2764  O   GLU C 373     5348   6704   6463    380   -887  -1265       O  
ATOM   2765  CB  GLU C 373      24.272  13.160 -55.662  1.00 51.85           C  
ANISOU 2765  CB  GLU C 373     5670   7228   6802    565   -973  -1464       C  
ATOM   2766  CG  GLU C 373      24.527  11.663 -55.847  1.00 70.20           C  
ANISOU 2766  CG  GLU C 373     8021   9527   9125    667  -1034  -1548       C  
ATOM   2767  CD  GLU C 373      23.968  11.105 -57.148  1.00 81.80           C  
ANISOU 2767  CD  GLU C 373     9481  11031  10566    688  -1031  -1581       C  
ATOM   2768  OE1 GLU C 373      23.467  11.898 -57.974  1.00 86.04           O  
ANISOU 2768  OE1 GLU C 373     9981  11635  11076    628   -981  -1541       O  
ATOM   2769  OE2 GLU C 373      24.027   9.873 -57.343  1.00 82.91           O  
ANISOU 2769  OE2 GLU C 373     9654  11132  10715    769  -1080  -1646       O  
ATOM   2770  N   GLN C 374      22.406  15.738 -56.333  1.00 43.01           N  
ANISOU 2770  N   GLN C 374     4554   6102   5685    357   -829  -1259       N  
ATOM   2771  CA  GLN C 374      22.309  17.193 -56.312  1.00 40.60           C  
ANISOU 2771  CA  GLN C 374     4218   5818   5391    269   -769  -1181       C  
ATOM   2772  C   GLN C 374      21.166  17.667 -55.419  1.00 37.85           C  
ANISOU 2772  C   GLN C 374     3955   5345   5080    220   -763  -1107       C  
ATOM   2773  O   GLN C 374      21.246  18.752 -54.830  1.00 35.43           O  
ANISOU 2773  O   GLN C 374     3641   5019   4800    164   -737  -1060       O  
ATOM   2774  CB  GLN C 374      22.144  17.713 -57.743  1.00 37.67           C  
ANISOU 2774  CB  GLN C 374     3782   5551   4980    235   -713  -1151       C  
ATOM   2775  CG  GLN C 374      23.003  16.961 -58.765  1.00 32.96           C  
ANISOU 2775  CG  GLN C 374     3112   5081   4331    301   -723  -1232       C  
ATOM   2776  CD  GLN C 374      23.264  17.755 -60.034  1.00 41.23           C  
ANISOU 2776  CD  GLN C 374     4068   6266   5333    261   -658  -1195       C  
ATOM   2777  OE1 GLN C 374      22.829  17.372 -61.123  1.00 42.81           O  
ANISOU 2777  OE1 GLN C 374     4254   6528   5484    284   -648  -1207       O  
ATOM   2778  NE2 GLN C 374      23.988  18.860 -59.902  1.00 41.26           N  
ANISOU 2778  NE2 GLN C 374     4005   6321   5352    202   -616  -1150       N  
ATOM   2779  N   LEU C 375      20.113  16.855 -55.279  1.00 33.42           N  
ANISOU 2779  N   LEU C 375     3473   4700   4526    243   -790  -1099       N  
ATOM   2780  CA  LEU C 375      18.966  17.232 -54.458  1.00 30.00           C  
ANISOU 2780  CA  LEU C 375     3117   4159   4123    201   -783  -1028       C  
ATOM   2781  C   LEU C 375      19.332  17.457 -52.997  1.00 36.28           C  
ANISOU 2781  C   LEU C 375     3946   4894   4945    207   -806  -1026       C  
ATOM   2782  O   LEU C 375      18.608  18.172 -52.293  1.00 45.75           O  
ANISOU 2782  O   LEU C 375     5187   6030   6164    164   -786   -967       O  
ATOM   2783  CB  LEU C 375      17.873  16.167 -54.557  1.00 32.50           C  
ANISOU 2783  CB  LEU C 375     3504   4401   4445    229   -813  -1025       C  
ATOM   2784  CG  LEU C 375      17.285  15.941 -55.949  1.00 37.43           C  
ANISOU 2784  CG  LEU C 375     4105   5075   5043    223   -796  -1027       C  
ATOM   2785  CD1 LEU C 375      16.212  14.864 -55.911  1.00 36.44           C  
ANISOU 2785  CD1 LEU C 375     4049   4862   4936    246   -836  -1029       C  
ATOM   2786  CD2 LEU C 375      16.727  17.243 -56.501  1.00 43.45           C  
ANISOU 2786  CD2 LEU C 375     4840   5873   5796    149   -731   -951       C  
ATOM   2787  N   GLN C 376      20.438  16.877 -52.523  1.00 41.68           N  
ANISOU 2787  N   GLN C 376     4610   5600   5626    263   -849  -1093       N  
ATOM   2788  CA  GLN C 376      20.893  17.143 -51.163  1.00 44.50           C  
ANISOU 2788  CA  GLN C 376     4990   5917   6001    272   -873  -1097       C  
ATOM   2789  C   GLN C 376      21.134  18.624 -50.909  1.00 37.10           C  
ANISOU 2789  C   GLN C 376     4014   5003   5080    204   -831  -1063       C  
ATOM   2790  O   GLN C 376      21.238  19.028 -49.743  1.00 37.48           O  
ANISOU 2790  O   GLN C 376     4089   5007   5144    201   -847  -1057       O  
ATOM   2791  CB  GLN C 376      22.164  16.346 -50.868  1.00 56.05           C  
ANISOU 2791  CB  GLN C 376     6421   7421   7455    346   -925  -1179       C  
ATOM   2792  CG  GLN C 376      21.883  14.928 -50.409  1.00 72.24           C  
ANISOU 2792  CG  GLN C 376     8541   9399   9507    419   -985  -1202       C  
ATOM   2793  CD  GLN C 376      22.767  13.902 -51.085  1.00 83.24           C  
ANISOU 2793  CD  GLN C 376     9893  10849  10886    493  -1024  -1286       C  
ATOM   2794  OE1 GLN C 376      23.973  14.101 -51.232  1.00 87.62           O  
ANISOU 2794  OE1 GLN C 376    10373  11491  11429    515  -1028  -1342       O  
ATOM   2795  NE2 GLN C 376      22.167  12.795 -51.507  1.00 83.18           N  
ANISOU 2795  NE2 GLN C 376     9929  10792  10883    532  -1054  -1300       N  
ATOM   2796  N   VAL C 377      21.202  19.436 -51.967  1.00 28.53           N  
ANISOU 2796  N   VAL C 377     2864   3982   3992    150   -781  -1038       N  
ATOM   2797  CA  VAL C 377      21.280  20.885 -51.816  1.00 31.80           C  
ANISOU 2797  CA  VAL C 377     3246   4402   4434     77   -741   -994       C  
ATOM   2798  C   VAL C 377      20.163  21.407 -50.921  1.00 37.47           C  
ANISOU 2798  C   VAL C 377     4042   5020   5176     49   -735   -938       C  
ATOM   2799  O   VAL C 377      20.317  22.444 -50.262  1.00 39.58           O  
ANISOU 2799  O   VAL C 377     4302   5264   5473     10   -726   -924       O  
ATOM   2800  CB  VAL C 377      21.252  21.551 -53.208  1.00 36.79           C  
ANISOU 2800  CB  VAL C 377     3810   5109   5057     25   -685   -955       C  
ATOM   2801  CG1 VAL C 377      19.823  21.641 -53.749  1.00 39.12           C  
ANISOU 2801  CG1 VAL C 377     4158   5361   5346     -2   -656   -888       C  
ATOM   2802  CG2 VAL C 377      21.893  22.903 -53.158  1.00 33.35           C  
ANISOU 2802  CG2 VAL C 377     3311   4702   4657    -42   -655   -929       C  
ATOM   2803  N   PHE C 378      19.034  20.695 -50.862  1.00 32.01           N  
ANISOU 2803  N   PHE C 378     3422   4268   4472     69   -742   -911       N  
ATOM   2804  CA  PHE C 378      17.878  21.141 -50.094  1.00 29.57           C  
ANISOU 2804  CA  PHE C 378     3182   3875   4178     45   -731   -854       C  
ATOM   2805  C   PHE C 378      17.902  20.694 -48.640  1.00 29.44           C  
ANISOU 2805  C   PHE C 378     3224   3802   4160     90   -773   -873       C  
ATOM   2806  O   PHE C 378      16.910  20.914 -47.939  1.00 26.84           O  
ANISOU 2806  O   PHE C 378     2953   3410   3834     81   -766   -828       O  
ATOM   2807  CB  PHE C 378      16.579  20.644 -50.738  1.00 25.94           C  
ANISOU 2807  CB  PHE C 378     2764   3383   3707     39   -714   -807       C  
ATOM   2808  CG  PHE C 378      16.306  21.231 -52.090  1.00 28.50           C  
ANISOU 2808  CG  PHE C 378     3041   3760   4028     -7   -668   -774       C  
ATOM   2809  CD1 PHE C 378      16.258  20.422 -53.212  1.00 29.30           C  
ANISOU 2809  CD1 PHE C 378     3122   3910   4102     15   -671   -793       C  
ATOM   2810  CD2 PHE C 378      16.100  22.593 -52.240  1.00 23.51           C  
ANISOU 2810  CD2 PHE C 378     2385   3128   3417    -68   -625   -724       C  
ATOM   2811  CE1 PHE C 378      16.009  20.957 -54.460  1.00 31.20           C  
ANISOU 2811  CE1 PHE C 378     3316   4209   4327    -23   -629   -760       C  
ATOM   2812  CE2 PHE C 378      15.853  23.136 -53.485  1.00 24.84           C  
ANISOU 2812  CE2 PHE C 378     2510   3348   3579   -108   -583   -683       C  
ATOM   2813  CZ  PHE C 378      15.806  22.316 -54.598  1.00 27.85           C  
ANISOU 2813  CZ  PHE C 378     2870   3789   3924    -85   -583   -699       C  
ATOM   2814  N   GLU C 379      18.979  20.074 -48.159  1.00 35.58           N  
ANISOU 2814  N   GLU C 379     3985   4605   4928    141   -818   -935       N  
ATOM   2815  CA  GLU C 379      18.918  19.519 -46.812  1.00 43.09           C  
ANISOU 2815  CA  GLU C 379     4996   5506   5869    191   -861   -944       C  
ATOM   2816  C   GLU C 379      19.023  20.576 -45.718  1.00 41.10           C  
ANISOU 2816  C   GLU C 379     4752   5238   5627    172   -859   -942       C  
ATOM   2817  O   GLU C 379      18.764  20.260 -44.551  1.00 44.62           O  
ANISOU 2817  O   GLU C 379     5253   5645   6056    211   -887   -937       O  
ATOM   2818  CB  GLU C 379      19.993  18.442 -46.640  1.00 55.44           C  
ANISOU 2818  CB  GLU C 379     6545   7100   7418    261   -914  -1010       C  
ATOM   2819  CG  GLU C 379      19.533  17.095 -47.186  1.00 63.89           C  
ANISOU 2819  CG  GLU C 379     7651   8144   8481    302   -935  -1008       C  
ATOM   2820  CD  GLU C 379      20.613  16.035 -47.171  1.00 72.89           C  
ANISOU 2820  CD  GLU C 379     8770   9312   9611    376   -990  -1078       C  
ATOM   2821  OE1 GLU C 379      21.734  16.323 -46.700  1.00 76.41           O  
ANISOU 2821  OE1 GLU C 379     9174   9806  10053    397  -1011  -1127       O  
ATOM   2822  OE2 GLU C 379      20.333  14.907 -47.627  1.00 74.01           O  
ANISOU 2822  OE2 GLU C 379     8938   9427   9755    414  -1016  -1087       O  
ATOM   2823  N   THR C 380      19.364  21.815 -46.059  1.00 33.83           N  
ANISOU 2823  N   THR C 380     3776   4344   4733    116   -830   -944       N  
ATOM   2824  CA  THR C 380      19.298  22.923 -45.115  1.00 37.08           C  
ANISOU 2824  CA  THR C 380     4197   4729   5164     92   -828   -943       C  
ATOM   2825  C   THR C 380      17.977  23.679 -45.194  1.00 42.82           C  
ANISOU 2825  C   THR C 380     4963   5403   5904     48   -785   -877       C  
ATOM   2826  O   THR C 380      17.750  24.588 -44.391  1.00 36.77           O  
ANISOU 2826  O   THR C 380     4211   4606   5152     34   -785   -877       O  
ATOM   2827  CB  THR C 380      20.459  23.900 -45.353  1.00 39.44           C  
ANISOU 2827  CB  THR C 380     4413   5075   5498     52   -827   -985       C  
ATOM   2828  OG1 THR C 380      20.134  24.769 -46.443  1.00 49.78           O  
ANISOU 2828  OG1 THR C 380     5683   6391   6839    -18   -776   -939       O  
ATOM   2829  CG2 THR C 380      21.733  23.152 -45.688  1.00 37.01           C  
ANISOU 2829  CG2 THR C 380     4048   4837   5178     88   -858  -1045       C  
ATOM   2830  N   LEU C 381      17.107  23.319 -46.134  1.00 44.15           N  
ANISOU 2830  N   LEU C 381     5145   5562   6067     30   -753   -826       N  
ATOM   2831  CA  LEU C 381      15.870  24.052 -46.375  1.00 29.94           C  
ANISOU 2831  CA  LEU C 381     3372   3722   4282    -12   -711   -762       C  
ATOM   2832  C   LEU C 381      14.898  23.856 -45.217  1.00 31.27           C  
ANISOU 2832  C   LEU C 381     3615   3837   4431     18   -719   -737       C  
ATOM   2833  O   LEU C 381      14.562  22.718 -44.861  1.00 36.82           O  
ANISOU 2833  O   LEU C 381     4360   4526   5104     61   -740   -728       O  
ATOM   2834  CB  LEU C 381      15.244  23.583 -47.687  1.00 24.01           C  
ANISOU 2834  CB  LEU C 381     2612   2985   3523    -32   -682   -721       C  
ATOM   2835  CG  LEU C 381      13.851  24.118 -48.050  1.00 31.19           C  
ANISOU 2835  CG  LEU C 381     3551   3858   4442    -68   -641   -650       C  
ATOM   2836  CD1 LEU C 381      13.835  25.639 -48.060  1.00 23.00           C  
ANISOU 2836  CD1 LEU C 381     2488   2808   3443   -118   -613   -630       C  
ATOM   2837  CD2 LEU C 381      13.415  23.556 -49.385  1.00 31.40           C  
ANISOU 2837  CD2 LEU C 381     3562   3913   4457    -80   -621   -624       C  
ATOM   2838  N   GLU C 382      14.446  24.969 -44.631  1.00 30.02           N  
ANISOU 2838  N   GLU C 382     3468   3649   4290     -3   -704   -724       N  
ATOM   2839  CA  GLU C 382      13.511  24.922 -43.519  1.00 38.13           C  
ANISOU 2839  CA  GLU C 382     4557   4639   5292     27   -706   -701       C  
ATOM   2840  C   GLU C 382      12.169  25.579 -43.804  1.00 42.33           C  
ANISOU 2840  C   GLU C 382     5111   5137   5837     -5   -662   -639       C  
ATOM   2841  O   GLU C 382      11.196  25.268 -43.112  1.00 40.81           O  
ANISOU 2841  O   GLU C 382     4967   4922   5617     21   -655   -605       O  
ATOM   2842  CB  GLU C 382      14.122  25.579 -42.273  1.00 38.19           C  
ANISOU 2842  CB  GLU C 382     4567   4647   5298     53   -736   -755       C  
ATOM   2843  CG  GLU C 382      15.465  25.015 -41.872  1.00 47.72           C  
ANISOU 2843  CG  GLU C 382     5749   5891   6490     89   -784   -820       C  
ATOM   2844  CD  GLU C 382      16.092  25.781 -40.730  1.00 64.49           C  
ANISOU 2844  CD  GLU C 382     7868   8021   8616    109   -817   -881       C  
ATOM   2845  OE1 GLU C 382      15.427  26.692 -40.197  1.00 69.55           O  
ANISOU 2845  OE1 GLU C 382     8529   8632   9264    101   -804   -875       O  
ATOM   2846  OE2 GLU C 382      17.250  25.479 -40.371  1.00 71.33           O  
ANISOU 2846  OE2 GLU C 382     8706   8922   9475    137   -859   -941       O  
ATOM   2847  N   GLU C 383      12.083  26.469 -44.789  1.00 31.81           N  
ANISOU 2847  N   GLU C 383     3740   3803   4544    -58   -631   -619       N  
ATOM   2848  CA  GLU C 383      10.819  27.139 -45.064  1.00 29.72           C  
ANISOU 2848  CA  GLU C 383     3493   3505   4293    -84   -593   -561       C  
ATOM   2849  C   GLU C 383      10.655  27.384 -46.559  1.00 29.36           C  
ANISOU 2849  C   GLU C 383     3409   3474   4271   -133   -561   -520       C  
ATOM   2850  O   GLU C 383      11.605  27.767 -47.246  1.00 30.39           O  
ANISOU 2850  O   GLU C 383     3488   3634   4427   -163   -560   -539       O  
ATOM   2851  CB  GLU C 383      10.711  28.469 -44.308  1.00 37.48           C  
ANISOU 2851  CB  GLU C 383     4480   4455   5305    -90   -591   -578       C  
ATOM   2852  CG  GLU C 383       9.443  29.255 -44.619  1.00 49.47           C  
ANISOU 2852  CG  GLU C 383     6013   5939   6844   -112   -553   -522       C  
ATOM   2853  CD  GLU C 383       9.285  30.490 -43.756  1.00 57.28           C  
ANISOU 2853  CD  GLU C 383     7012   6890   7862   -105   -559   -549       C  
ATOM   2854  OE1 GLU C 383       8.402  31.318 -44.061  1.00 51.30           O  
ANISOU 2854  OE1 GLU C 383     6259   6101   7133   -124   -532   -511       O  
ATOM   2855  OE2 GLU C 383      10.039  30.630 -42.770  1.00 67.74           O  
ANISOU 2855  OE2 GLU C 383     8340   8218   9182    -78   -594   -614       O  
ATOM   2856  N   ILE C 384       9.436  27.161 -47.047  1.00 26.14           N  
ANISOU 2856  N   ILE C 384     3023   3054   3854   -140   -534   -462       N  
ATOM   2857  CA  ILE C 384       9.031  27.491 -48.409  1.00 26.71           C  
ANISOU 2857  CA  ILE C 384     3064   3142   3941   -182   -502   -415       C  
ATOM   2858  C   ILE C 384       7.815  28.401 -48.308  1.00 26.52           C  
ANISOU 2858  C   ILE C 384     3061   3079   3936   -196   -473   -364       C  
ATOM   2859  O   ILE C 384       6.764  27.981 -47.805  1.00 30.69           O  
ANISOU 2859  O   ILE C 384     3630   3589   4444   -173   -467   -339       O  
ATOM   2860  CB  ILE C 384       8.698  26.234 -49.228  1.00 30.60           C  
ANISOU 2860  CB  ILE C 384     3559   3664   4402   -173   -503   -401       C  
ATOM   2861  CG1 ILE C 384       9.943  25.369 -49.432  1.00 34.57           C  
ANISOU 2861  CG1 ILE C 384     4037   4209   4890   -153   -534   -456       C  
ATOM   2862  CG2 ILE C 384       8.089  26.618 -50.570  1.00 29.69           C  
ANISOU 2862  CG2 ILE C 384     3416   3571   4294   -209   -471   -349       C  
ATOM   2863  CD1 ILE C 384       9.667  24.091 -50.193  1.00 24.47           C  
ANISOU 2863  CD1 ILE C 384     2762   2952   3585   -137   -545   -456       C  
ATOM   2864  N   THR C 385       7.952  29.644 -48.778  1.00 26.84           N  
ANISOU 2864  N   THR C 385     3072   3107   4020   -233   -454   -345       N  
ATOM   2865  CA  THR C 385       6.832  30.576 -48.702  1.00 25.22           C  
ANISOU 2865  CA  THR C 385     2884   2859   3838   -241   -430   -300       C  
ATOM   2866  C   THR C 385       5.744  30.250 -49.717  1.00 26.83           C  
ANISOU 2866  C   THR C 385     3088   3081   4025   -253   -403   -236       C  
ATOM   2867  O   THR C 385       4.564  30.514 -49.459  1.00 32.11           O  
ANISOU 2867  O   THR C 385     3783   3724   4694   -242   -387   -201       O  
ATOM   2868  CB  THR C 385       7.313  32.014 -48.903  1.00 24.72           C  
ANISOU 2868  CB  THR C 385     2790   2765   3836   -278   -424   -296       C  
ATOM   2869  OG1 THR C 385       7.855  32.159 -50.221  1.00 29.80           O  
ANISOU 2869  OG1 THR C 385     3384   3448   4493   -321   -408   -262       O  
ATOM   2870  CG2 THR C 385       8.379  32.364 -47.872  1.00 32.27           C  
ANISOU 2870  CG2 THR C 385     3744   3704   4815   -268   -458   -368       C  
ATOM   2871  N   GLY C 386       6.113  29.685 -50.863  1.00 24.21           N  
ANISOU 2871  N   GLY C 386     2723   2798   3676   -272   -398   -224       N  
ATOM   2872  CA  GLY C 386       5.135  29.283 -51.853  1.00 19.86           C  
ANISOU 2872  CA  GLY C 386     2169   2272   3104   -279   -379   -174       C  
ATOM   2873  C   GLY C 386       4.651  27.862 -51.646  1.00 29.73           C  
ANISOU 2873  C   GLY C 386     3447   3533   4316   -250   -396   -188       C  
ATOM   2874  O   GLY C 386       4.301  27.477 -50.526  1.00 26.41           O  
ANISOU 2874  O   GLY C 386     3066   3081   3889   -223   -408   -202       O  
ATOM   2875  N   TYR C 387       4.632  27.068 -52.712  1.00 14.78           N  
ANISOU 2875  N   TYR C 387     1533   1685   2398   -256   -399   -184       N  
ATOM   2876  CA  TYR C 387       4.152  25.695 -52.652  1.00 24.15           C  
ANISOU 2876  CA  TYR C 387     2743   2873   3560   -233   -421   -198       C  
ATOM   2877  C   TYR C 387       5.275  24.724 -52.999  1.00 24.58           C  
ANISOU 2877  C   TYR C 387     2780   2963   3595   -218   -451   -255       C  
ATOM   2878  O   TYR C 387       6.363  25.113 -53.428  1.00 22.48           O  
ANISOU 2878  O   TYR C 387     2476   2734   3329   -226   -449   -280       O  
ATOM   2879  CB  TYR C 387       2.955  25.484 -53.593  1.00 19.40           C  
ANISOU 2879  CB  TYR C 387     2134   2288   2950   -246   -408   -153       C  
ATOM   2880  CG  TYR C 387       3.244  25.725 -55.063  1.00 20.45           C  
ANISOU 2880  CG  TYR C 387     2219   2483   3067   -265   -397   -143       C  
ATOM   2881  CD1 TYR C 387       3.788  24.724 -55.860  1.00 17.36           C  
ANISOU 2881  CD1 TYR C 387     1807   2141   2648   -253   -420   -184       C  
ATOM   2882  CD2 TYR C 387       2.965  26.953 -55.654  1.00 18.50           C  
ANISOU 2882  CD2 TYR C 387     1948   2249   2832   -290   -365    -90       C  
ATOM   2883  CE1 TYR C 387       4.052  24.941 -57.201  1.00 25.07           C  
ANISOU 2883  CE1 TYR C 387     2737   3190   3599   -265   -408   -176       C  
ATOM   2884  CE2 TYR C 387       3.225  27.178 -56.994  1.00 17.05           C  
ANISOU 2884  CE2 TYR C 387     1720   2132   2627   -305   -353    -71       C  
ATOM   2885  CZ  TYR C 387       3.768  26.169 -57.763  1.00 29.06           C  
ANISOU 2885  CZ  TYR C 387     3218   3714   4111   -292   -372   -114       C  
ATOM   2886  OH  TYR C 387       4.028  26.391 -59.096  1.00 31.78           O  
ANISOU 2886  OH  TYR C 387     3514   4139   4422   -301   -358    -96       O  
ATOM   2887  N   LEU C 388       4.993  23.440 -52.802  1.00 31.80           N  
ANISOU 2887  N   LEU C 388     3719   3864   4498   -194   -479   -276       N  
ATOM   2888  CA  LEU C 388       5.888  22.365 -53.207  1.00 24.33           C  
ANISOU 2888  CA  LEU C 388     2761   2947   3537   -171   -513   -333       C  
ATOM   2889  C   LEU C 388       5.110  21.405 -54.095  1.00 24.06           C  
ANISOU 2889  C   LEU C 388     2726   2923   3493   -169   -528   -331       C  
ATOM   2890  O   LEU C 388       4.127  20.796 -53.652  1.00 25.80           O  
ANISOU 2890  O   LEU C 388     2981   3098   3726   -167   -539   -307       O  
ATOM   2891  CB  LEU C 388       6.474  21.640 -51.993  1.00 18.42           C  
ANISOU 2891  CB  LEU C 388     2047   2160   2791   -137   -546   -370       C  
ATOM   2892  CG  LEU C 388       7.348  20.411 -52.296  1.00 19.83           C  
ANISOU 2892  CG  LEU C 388     2219   2357   2959   -103   -589   -433       C  
ATOM   2893  CD1 LEU C 388       8.537  20.799 -53.159  1.00 21.42           C  
ANISOU 2893  CD1 LEU C 388     2364   2630   3147   -104   -584   -474       C  
ATOM   2894  CD2 LEU C 388       7.815  19.768 -51.007  1.00 15.30           C  
ANISOU 2894  CD2 LEU C 388     1683   1740   2389    -67   -622   -456       C  
ATOM   2895  N   TYR C 389       5.547  21.279 -55.345  1.00 21.69           N  
ANISOU 2895  N   TYR C 389     2382   2687   3171   -169   -530   -356       N  
ATOM   2896  CA  TYR C 389       4.895  20.439 -56.342  1.00 28.07           C  
ANISOU 2896  CA  TYR C 389     3182   3518   3967   -165   -549   -368       C  
ATOM   2897  C   TYR C 389       5.910  19.415 -56.828  1.00 38.40           C  
ANISOU 2897  C   TYR C 389     4472   4862   5258   -128   -588   -447       C  
ATOM   2898  O   TYR C 389       6.965  19.788 -57.349  1.00 43.44           O  
ANISOU 2898  O   TYR C 389     5067   5567   5872   -121   -577   -475       O  
ATOM   2899  CB  TYR C 389       4.367  21.299 -57.495  1.00 26.59           C  
ANISOU 2899  CB  TYR C 389     2956   3389   3759   -191   -514   -325       C  
ATOM   2900  CG  TYR C 389       3.735  20.553 -58.657  1.00 23.93           C  
ANISOU 2900  CG  TYR C 389     2600   3092   3399   -184   -535   -343       C  
ATOM   2901  CD1 TYR C 389       2.356  20.408 -58.750  1.00 24.64           C  
ANISOU 2901  CD1 TYR C 389     2706   3152   3503   -200   -536   -304       C  
ATOM   2902  CD2 TYR C 389       4.516  20.033 -59.680  1.00 23.91           C  
ANISOU 2902  CD2 TYR C 389     2558   3165   3360   -159   -553   -402       C  
ATOM   2903  CE1 TYR C 389       1.776  19.741 -59.818  1.00 24.26           C  
ANISOU 2903  CE1 TYR C 389     2639   3142   3437   -194   -561   -327       C  
ATOM   2904  CE2 TYR C 389       3.948  19.366 -60.748  1.00 29.36           C  
ANISOU 2904  CE2 TYR C 389     3231   3897   4027   -147   -576   -428       C  
ATOM   2905  CZ  TYR C 389       2.579  19.223 -60.814  1.00 32.36           C  
ANISOU 2905  CZ  TYR C 389     3629   4241   4425   -166   -582   -392       C  
ATOM   2906  OH  TYR C 389       2.010  18.560 -61.879  1.00 27.30           O  
ANISOU 2906  OH  TYR C 389     2967   3642   3762   -154   -612   -425       O  
ATOM   2907  N   ILE C 390       5.605  18.133 -56.641  1.00 34.69           N  
ANISOU 2907  N   ILE C 390     4031   4346   4803   -104   -633   -481       N  
ATOM   2908  CA  ILE C 390       6.478  17.039 -57.063  1.00 31.96           C  
ANISOU 2908  CA  ILE C 390     3674   4022   4448    -61   -680   -563       C  
ATOM   2909  C   ILE C 390       5.650  16.072 -57.904  1.00 25.76           C  
ANISOU 2909  C   ILE C 390     2889   3230   3668    -54   -715   -589       C  
ATOM   2910  O   ILE C 390       4.770  15.369 -57.380  1.00 26.43           O  
ANISOU 2910  O   ILE C 390     3015   3236   3792    -62   -741   -570       O  
ATOM   2911  CB  ILE C 390       7.135  16.314 -55.877  1.00 35.24           C  
ANISOU 2911  CB  ILE C 390     4128   4374   4889    -29   -715   -592       C  
ATOM   2912  CG1 ILE C 390       7.824  17.313 -54.945  1.00 27.95           C  
ANISOU 2912  CG1 ILE C 390     3205   3453   3963    -38   -684   -568       C  
ATOM   2913  CG2 ILE C 390       8.154  15.300 -56.376  1.00 35.03           C  
ANISOU 2913  CG2 ILE C 390     4082   4375   4851     22   -762   -682       C  
ATOM   2914  CD1 ILE C 390       8.601  16.665 -53.812  1.00 25.50           C  
ANISOU 2914  CD1 ILE C 390     2926   3097   3666      0   -720   -600       C  
ATOM   2915  N   SER C 391       5.925  16.047 -59.210  1.00 20.69           N  
ANISOU 2915  N   SER C 391     2200   2676   2986    -40   -717   -631       N  
ATOM   2916  CA  SER C 391       5.311  15.109 -60.142  1.00 19.77           C  
ANISOU 2916  CA  SER C 391     2075   2568   2867    -24   -758   -677       C  
ATOM   2917  C   SER C 391       6.344  14.202 -60.803  1.00 27.97           C  
ANISOU 2917  C   SER C 391     3089   3656   3883     34   -803   -782       C  
ATOM   2918  O   SER C 391       6.002  13.456 -61.730  1.00 28.91           O  
ANISOU 2918  O   SER C 391     3193   3800   3993     56   -841   -839       O  
ATOM   2919  CB  SER C 391       4.511  15.866 -61.205  1.00 18.61           C  
ANISOU 2919  CB  SER C 391     1893   2493   2685    -52   -725   -638       C  
ATOM   2920  OG  SER C 391       5.352  16.290 -62.261  1.00 31.55           O  
ANISOU 2920  OG  SER C 391     3474   4251   4261    -31   -705   -669       O  
ATOM   2921  N   ALA C 392       7.598  14.252 -60.357  1.00 30.41           N  
ANISOU 2921  N   ALA C 392     3389   3984   4183     62   -801   -813       N  
ATOM   2922  CA  ALA C 392       8.636  13.338 -60.809  1.00 29.79           C  
ANISOU 2922  CA  ALA C 392     3287   3944   4087    125   -846   -916       C  
ATOM   2923  C   ALA C 392       9.714  13.286 -59.739  1.00 34.17           C  
ANISOU 2923  C   ALA C 392     3857   4466   4660    147   -852   -928       C  
ATOM   2924  O   ALA C 392       9.997  14.289 -59.079  1.00 38.63           O  
ANISOU 2924  O   ALA C 392     4420   5035   5222    115   -806   -870       O  
ATOM   2925  CB  ALA C 392       9.233  13.762 -62.154  1.00 18.81           C  
ANISOU 2925  CB  ALA C 392     1824   2699   2623    145   -821   -954       C  
ATOM   2926  N   TRP C 393      10.310  12.102 -59.574  1.00 27.12           N  
ANISOU 2926  N   TRP C 393     2979   3538   3787    204   -913  -1009       N  
ATOM   2927  CA  TRP C 393      11.289  11.897 -58.518  1.00 29.66           C  
ANISOU 2927  CA  TRP C 393     3318   3822   4128    233   -930  -1024       C  
ATOM   2928  C   TRP C 393      12.133  10.693 -58.891  1.00 40.20           C  
ANISOU 2928  C   TRP C 393     4642   5168   5465    311   -994  -1134       C  
ATOM   2929  O   TRP C 393      11.597   9.745 -59.483  1.00 43.96           O  
ANISOU 2929  O   TRP C 393     5131   5611   5959    334  -1043  -1183       O  
ATOM   2930  CB  TRP C 393      10.596  11.677 -57.168  1.00 24.93           C  
ANISOU 2930  CB  TRP C 393     2791   3096   3586    208   -942   -958       C  
ATOM   2931  CG  TRP C 393      11.433  12.011 -55.970  1.00 34.28           C  
ANISOU 2931  CG  TRP C 393     3989   4259   4774    219   -934   -940       C  
ATOM   2932  CD1 TRP C 393      11.913  11.136 -55.039  1.00 31.19           C  
ANISOU 2932  CD1 TRP C 393     3638   3797   4415    262   -984   -963       C  
ATOM   2933  CD2 TRP C 393      11.888  13.312 -55.569  1.00 35.63           C  
ANISOU 2933  CD2 TRP C 393     4135   4481   4920    186   -878   -897       C  
ATOM   2934  NE1 TRP C 393      12.634  11.808 -54.084  1.00 28.24           N  
ANISOU 2934  NE1 TRP C 393     3264   3436   4031    262   -963   -940       N  
ATOM   2935  CE2 TRP C 393      12.637  13.144 -54.386  1.00 26.06           C  
ANISOU 2935  CE2 TRP C 393     2947   3230   3722    214   -899   -903       C  
ATOM   2936  CE3 TRP C 393      11.737  14.599 -56.095  1.00 30.84           C  
ANISOU 2936  CE3 TRP C 393     3488   3945   4285    138   -816   -853       C  
ATOM   2937  CZ2 TRP C 393      13.233  14.216 -53.719  1.00 24.63           C  
ANISOU 2937  CZ2 TRP C 393     2750   3080   3528    194   -863   -877       C  
ATOM   2938  CZ3 TRP C 393      12.331  15.663 -55.430  1.00 32.18           C  
ANISOU 2938  CZ3 TRP C 393     3643   4135   4450    115   -780   -822       C  
ATOM   2939  CH2 TRP C 393      13.068  15.464 -54.256  1.00 26.99           C  
ANISOU 2939  CH2 TRP C 393     3009   3440   3807    142   -805   -838       C  
ATOM   2940  N   PRO C 394      13.431  10.687 -58.586  1.00 39.80           N  
ANISOU 2940  N   PRO C 394     4565   5160   5397    354  -1000  -1180       N  
ATOM   2941  CA  PRO C 394      14.276   9.561 -59.006  1.00 36.04           C  
ANISOU 2941  CA  PRO C 394     4072   4704   4920    437  -1062  -1292       C  
ATOM   2942  C   PRO C 394      13.834   8.265 -58.343  1.00 37.54           C  
ANISOU 2942  C   PRO C 394     4332   4751   5179    468  -1137  -1311       C  
ATOM   2943  O   PRO C 394      13.674   8.194 -57.122  1.00 35.96           O  
ANISOU 2943  O   PRO C 394     4185   4455   5021    452  -1144  -1252       O  
ATOM   2944  CB  PRO C 394      15.681   9.980 -58.555  1.00 34.17           C  
ANISOU 2944  CB  PRO C 394     3794   4533   4657    466  -1046  -1315       C  
ATOM   2945  CG  PRO C 394      15.597  11.457 -58.317  1.00 33.81           C  
ANISOU 2945  CG  PRO C 394     3725   4533   4588    393   -969  -1226       C  
ATOM   2946  CD  PRO C 394      14.199  11.711 -57.859  1.00 30.00           C  
ANISOU 2946  CD  PRO C 394     3303   3955   4140    331   -954  -1137       C  
ATOM   2947  N   ASP C 395      13.635   7.231 -59.166  1.00 41.25           N  
ANISOU 2947  N   ASP C 395     4801   5208   5663    513  -1194  -1395       N  
ATOM   2948  CA  ASP C 395      13.182   5.943 -58.652  1.00 46.75           C  
ANISOU 2948  CA  ASP C 395     5564   5760   6439    539  -1269  -1411       C  
ATOM   2949  C   ASP C 395      14.156   5.339 -57.651  1.00 42.25           C  
ANISOU 2949  C   ASP C 395     5021   5134   5899    597  -1311  -1433       C  
ATOM   2950  O   ASP C 395      13.765   4.456 -56.880  1.00 40.01           O  
ANISOU 2950  O   ASP C 395     4801   4716   5686    605  -1367  -1413       O  
ATOM   2951  CB  ASP C 395      12.947   4.964 -59.805  1.00 54.89           C  
ANISOU 2951  CB  ASP C 395     6583   6796   7478    588  -1302  -1485       C  
ATOM   2952  CG  ASP C 395      11.742   5.332 -60.641  1.00 72.71           C  
ANISOU 2952  CG  ASP C 395     8829   9075   9721    531  -1278  -1458       C  
ATOM   2953  OD1 ASP C 395      11.825   5.233 -61.883  1.00 77.51           O  
ANISOU 2953  OD1 ASP C 395     9391   9777  10283    563  -1270  -1520       O  
ATOM   2954  OD2 ASP C 395      10.713   5.728 -60.055  1.00 79.09           O  
ANISOU 2954  OD2 ASP C 395     9673   9814  10563    457  -1269  -1375       O  
ATOM   2955  N   SER C 396      15.405   5.801 -57.630  1.00 39.46           N  
ANISOU 2955  N   SER C 396     4617   4879   5495    635  -1288  -1470       N  
ATOM   2956  CA  SER C 396      16.360   5.312 -56.648  1.00 39.54           C  
ANISOU 2956  CA  SER C 396     4648   4846   5528    691  -1328  -1490       C  
ATOM   2957  C   SER C 396      16.146   5.911 -55.264  1.00 41.67           C  
ANISOU 2957  C   SER C 396     4963   5055   5814    641  -1301  -1384       C  
ATOM   2958  O   SER C 396      16.808   5.477 -54.315  1.00 49.32           O  
ANISOU 2958  O   SER C 396     5958   5977   6804    685  -1337  -1387       O  
ATOM   2959  CB  SER C 396      17.786   5.605 -57.114  1.00 42.90           C  
ANISOU 2959  CB  SER C 396     4999   5408   5896    749  -1304  -1560       C  
ATOM   2960  OG  SER C 396      17.842   6.786 -57.897  1.00 44.89           O  
ANISOU 2960  OG  SER C 396     5184   5793   6081    701  -1231  -1546       O  
ATOM   2961  N   LEU C 397      15.244   6.884 -55.109  1.00 36.55           N  
ANISOU 2961  N   LEU C 397     4323   4410   5154    557  -1237  -1291       N  
ATOM   2962  CA  LEU C 397      15.092   7.569 -53.823  1.00 38.44           C  
ANISOU 2962  CA  LEU C 397     4597   4611   5398    516  -1204  -1196       C  
ATOM   2963  C   LEU C 397      13.878   7.049 -53.079  1.00 38.14           C  
ANISOU 2963  C   LEU C 397     4634   4444   5415    481  -1222  -1115       C  
ATOM   2964  O   LEU C 397      12.752   7.173 -53.582  1.00 33.51           O  
ANISOU 2964  O   LEU C 397     4055   3836   4841    429  -1202  -1077       O  
ATOM   2965  CB  LEU C 397      14.977   9.073 -54.026  1.00 39.42           C  
ANISOU 2965  CB  LEU C 397     4679   4825   5474    451  -1121  -1146       C  
ATOM   2966  CG  LEU C 397      16.334   9.753 -54.331  1.00 32.80           C  
ANISOU 2966  CG  LEU C 397     3767   4108   4586    475  -1096  -1200       C  
ATOM   2967  CD1 LEU C 397      16.160  11.256 -54.464  1.00 27.10           C  
ANISOU 2967  CD1 LEU C 397     3009   3456   3833    403  -1018  -1139       C  
ATOM   2968  CD2 LEU C 397      17.343   9.396 -53.253  1.00 22.65           C  
ANISOU 2968  CD2 LEU C 397     2495   2799   3311    528  -1134  -1223       C  
ATOM   2969  N   PRO C 398      14.060   6.464 -51.896  1.00 35.04           N  
ANISOU 2969  N   PRO C 398     4293   3967   5053    509  -1259  -1082       N  
ATOM   2970  CA  PRO C 398      12.915   5.888 -51.178  1.00 32.66           C  
ANISOU 2970  CA  PRO C 398     4059   3544   4806    477  -1277   -996       C  
ATOM   2971  C   PRO C 398      11.870   6.912 -50.763  1.00 34.94           C  
ANISOU 2971  C   PRO C 398     4358   3840   5078    397  -1207   -894       C  
ATOM   2972  O   PRO C 398      10.691   6.554 -50.662  1.00 37.93           O  
ANISOU 2972  O   PRO C 398     4771   4144   5496    355  -1209   -832       O  
ATOM   2973  CB  PRO C 398      13.563   5.240 -49.937  1.00 29.80           C  
ANISOU 2973  CB  PRO C 398     3741   3120   4463    530  -1322   -977       C  
ATOM   2974  CG  PRO C 398      15.047   5.524 -50.031  1.00 24.86           C  
ANISOU 2974  CG  PRO C 398     3067   2585   3793    591  -1329  -1061       C  
ATOM   2975  CD  PRO C 398      15.344   5.908 -51.437  1.00 30.22           C  
ANISOU 2975  CD  PRO C 398     3678   3362   4441    589  -1308  -1143       C  
ATOM   2976  N   ASP C 399      12.249   8.168 -50.521  1.00 38.45           N  
ANISOU 2976  N   ASP C 399     4772   4368   5469    374  -1148   -877       N  
ATOM   2977  CA  ASP C 399      11.353   9.115 -49.858  1.00 35.13           C  
ANISOU 2977  CA  ASP C 399     4369   3943   5034    312  -1089   -781       C  
ATOM   2978  C   ASP C 399      11.689  10.540 -50.295  1.00 36.00           C  
ANISOU 2978  C   ASP C 399     4425   4156   5095    281  -1026   -791       C  
ATOM   2979  O   ASP C 399      12.398  10.762 -51.281  1.00 38.01           O  
ANISOU 2979  O   ASP C 399     4626   4487   5328    294  -1022   -860       O  
ATOM   2980  CB  ASP C 399      11.462   8.948 -48.338  1.00 43.52           C  
ANISOU 2980  CB  ASP C 399     5481   4956   6099    331  -1100   -722       C  
ATOM   2981  CG  ASP C 399      12.900   9.032 -47.853  1.00 47.36           C  
ANISOU 2981  CG  ASP C 399     5950   5488   6557    390  -1123   -779       C  
ATOM   2982  OD1 ASP C 399      13.793   9.292 -48.690  1.00 51.19           O  
ANISOU 2982  OD1 ASP C 399     6381   6046   7022    410  -1123   -860       O  
ATOM   2983  OD2 ASP C 399      13.143   8.841 -46.645  1.00 40.86           O  
ANISOU 2983  OD2 ASP C 399     5163   4633   5727    418  -1140   -742       O  
ATOM   2984  N   LEU C 400      11.169  11.513 -49.550  1.00 37.44           N  
ANISOU 2984  N   LEU C 400     4621   4342   5262    239   -977   -720       N  
ATOM   2985  CA  LEU C 400      11.484  12.922 -49.750  1.00 32.18           C  
ANISOU 2985  CA  LEU C 400     3910   3755   4561    207   -922   -720       C  
ATOM   2986  C   LEU C 400      12.404  13.444 -48.650  1.00 38.89           C  
ANISOU 2986  C   LEU C 400     4761   4624   5390    231   -922   -727       C  
ATOM   2987  O   LEU C 400      12.194  14.532 -48.113  1.00 35.36           O  
ANISOU 2987  O   LEU C 400     4313   4194   4928    200   -881   -689       O  
ATOM   2988  CB  LEU C 400      10.207  13.756 -49.810  1.00 32.10           C  
ANISOU 2988  CB  LEU C 400     3909   3736   4551    145   -869   -645       C  
ATOM   2989  CG  LEU C 400       9.098  13.242 -50.730  1.00 27.15           C  
ANISOU 2989  CG  LEU C 400     3285   3083   3947    118   -871   -627       C  
ATOM   2990  CD1 LEU C 400       7.902  14.178 -50.693  1.00 23.16           C  
ANISOU 2990  CD1 LEU C 400     2783   2578   3439     61   -817   -552       C  
ATOM   2991  CD2 LEU C 400       9.616  13.076 -52.148  1.00 23.78           C  
ANISOU 2991  CD2 LEU C 400     2808   2719   3509    130   -881   -699       C  
ATOM   2992  N   SER C 401      13.455  12.690 -48.324  1.00 43.77           N  
ANISOU 2992  N   SER C 401     5381   5242   6008    291   -972   -781       N  
ATOM   2993  CA  SER C 401      14.261  13.009 -47.152  1.00 34.71           C  
ANISOU 2993  CA  SER C 401     4241   4106   4842    321   -983   -787       C  
ATOM   2994  C   SER C 401      15.305  14.093 -47.402  1.00 35.10           C  
ANISOU 2994  C   SER C 401     4226   4242   4869    311   -958   -836       C  
ATOM   2995  O   SER C 401      15.890  14.598 -46.447  1.00 39.31           O  
ANISOU 2995  O   SER C 401     4759   4791   5387    325   -962   -841       O  
ATOM   2996  CB  SER C 401      14.939  11.746 -46.611  1.00 28.35           C  
ANISOU 2996  CB  SER C 401     3463   3262   4047    393  -1050   -819       C  
ATOM   2997  OG  SER C 401      15.660  11.068 -47.620  1.00 42.78           O  
ANISOU 2997  OG  SER C 401     5255   5116   5885    428  -1083   -897       O  
ATOM   2998  N   VAL C 402      15.559  14.501 -48.645  1.00 28.82           N  
ANISOU 2998  N   VAL C 402     3372   3507   4069    287   -933   -869       N  
ATOM   2999  CA  VAL C 402      16.379  15.697 -48.805  1.00 32.91           C  
ANISOU 2999  CA  VAL C 402     3830   4101   4575    261   -901   -893       C  
ATOM   3000  C   VAL C 402      15.612  16.914 -48.309  1.00 38.92           C  
ANISOU 3000  C   VAL C 402     4606   4844   5338    204   -854   -829       C  
ATOM   3001  O   VAL C 402      16.202  17.987 -48.119  1.00 36.65           O  
ANISOU 3001  O   VAL C 402     4280   4596   5050    179   -833   -839       O  
ATOM   3002  CB  VAL C 402      16.868  15.889 -50.257  1.00 34.59           C  
ANISOU 3002  CB  VAL C 402     3970   4394   4777    247   -880   -933       C  
ATOM   3003  CG1 VAL C 402      17.500  14.616 -50.786  1.00 37.23           C  
ANISOU 3003  CG1 VAL C 402     4292   4745   5107    312   -930  -1003       C  
ATOM   3004  CG2 VAL C 402      15.739  16.357 -51.164  1.00 26.43           C  
ANISOU 3004  CG2 VAL C 402     2937   3361   3746    192   -835   -881       C  
ATOM   3005  N   PHE C 403      14.303  16.758 -48.074  1.00 31.69           N  
ANISOU 3005  N   PHE C 403     3744   3868   4430    183   -840   -765       N  
ATOM   3006  CA  PHE C 403      13.466  17.738 -47.400  1.00 32.94           C  
ANISOU 3006  CA  PHE C 403     3927   4000   4589    144   -803   -706       C  
ATOM   3007  C   PHE C 403      13.195  17.369 -45.939  1.00 30.26           C  
ANISOU 3007  C   PHE C 403     3646   3612   4239    178   -826   -679       C  
ATOM   3008  O   PHE C 403      12.173  17.795 -45.390  1.00 29.51           O  
ANISOU 3008  O   PHE C 403     3584   3485   4141    155   -799   -620       O  
ATOM   3009  CB  PHE C 403      12.138  17.902 -48.147  1.00 34.92           C  
ANISOU 3009  CB  PHE C 403     4188   4229   4849    100   -766   -649       C  
ATOM   3010  CG  PHE C 403      12.272  18.464 -49.539  1.00 28.76           C  
ANISOU 3010  CG  PHE C 403     3352   3506   4071     64   -736   -660       C  
ATOM   3011  CD1 PHE C 403      11.941  17.702 -50.652  1.00 26.63           C  
ANISOU 3011  CD1 PHE C 403     3071   3248   3801     67   -744   -671       C  
ATOM   3012  CD2 PHE C 403      12.723  19.756 -49.731  1.00 20.44           C  
ANISOU 3012  CD2 PHE C 403     2254   2494   3019     29   -702   -659       C  
ATOM   3013  CE1 PHE C 403      12.058  18.227 -51.933  1.00 16.35           C  
ANISOU 3013  CE1 PHE C 403     1715   2011   2488     39   -715   -678       C  
ATOM   3014  CE2 PHE C 403      12.846  20.284 -51.002  1.00 18.63           C  
ANISOU 3014  CE2 PHE C 403     1970   2320   2787     -4   -671   -657       C  
ATOM   3015  CZ  PHE C 403      12.514  19.520 -52.106  1.00 24.58           C  
ANISOU 3015  CZ  PHE C 403     2713   3098   3529      3   -676   -665       C  
ATOM   3016  N   GLN C 404      14.078  16.576 -45.306  1.00 39.30           N  
ANISOU 3016  N   GLN C 404     4802   4755   5375    234   -875   -718       N  
ATOM   3017  CA  GLN C 404      13.906  16.235 -43.889  1.00 40.24           C  
ANISOU 3017  CA  GLN C 404     4975   4840   5476    271   -898   -688       C  
ATOM   3018  C   GLN C 404      13.704  17.456 -43.012  1.00 35.62           C  
ANISOU 3018  C   GLN C 404     4393   4270   4872    253   -869   -671       C  
ATOM   3019  O   GLN C 404      12.977  17.387 -42.017  1.00 32.80           O  
ANISOU 3019  O   GLN C 404     4083   3886   4495    266   -865   -621       O  
ATOM   3020  CB  GLN C 404      15.113  15.486 -43.317  1.00 50.38           C  
ANISOU 3020  CB  GLN C 404     6258   6136   6748    337   -955   -741       C  
ATOM   3021  CG  GLN C 404      15.355  14.067 -43.747  1.00 55.15           C  
ANISOU 3021  CG  GLN C 404     6876   6709   7369    380  -1001   -758       C  
ATOM   3022  CD  GLN C 404      16.679  13.556 -43.217  1.00 57.01           C  
ANISOU 3022  CD  GLN C 404     7099   6969   7592    447  -1056   -819       C  
ATOM   3023  OE1 GLN C 404      17.715  14.200 -43.391  1.00 44.25           O  
ANISOU 3023  OE1 GLN C 404     5428   5417   5967    451  -1056   -882       O  
ATOM   3024  NE2 GLN C 404      16.661  12.381 -42.600  1.00 68.42           N  
ANISOU 3024  NE2 GLN C 404     8594   8363   9041    501  -1104   -798       N  
ATOM   3025  N   ASN C 405      14.378  18.557 -43.325  1.00 37.54           N  
ANISOU 3025  N   ASN C 405     4585   4557   5123    227   -852   -715       N  
ATOM   3026  CA  ASN C 405      14.439  19.713 -42.446  1.00 42.39           C  
ANISOU 3026  CA  ASN C 405     5197   5182   5726    218   -839   -721       C  
ATOM   3027  C   ASN C 405      13.409  20.775 -42.792  1.00 42.12           C  
ANISOU 3027  C   ASN C 405     5162   5134   5708    163   -787   -678       C  
ATOM   3028  O   ASN C 405      13.381  21.823 -42.140  1.00 44.22           O  
ANISOU 3028  O   ASN C 405     5425   5402   5973    154   -776   -687       O  
ATOM   3029  CB  ASN C 405      15.849  20.311 -42.477  1.00 41.57           C  
ANISOU 3029  CB  ASN C 405     5035   5127   5631    222   -860   -797       C  
ATOM   3030  CG  ASN C 405      16.883  19.379 -41.873  1.00 36.74           C  
ANISOU 3030  CG  ASN C 405     4426   4534   4998    287   -917   -844       C  
ATOM   3031  OD1 ASN C 405      16.639  18.750 -40.844  1.00 36.63           O  
ANISOU 3031  OD1 ASN C 405     4464   4500   4954    335   -943   -823       O  
ATOM   3032  ND2 ASN C 405      18.040  19.276 -42.518  1.00 36.58           N  
ANISOU 3032  ND2 ASN C 405     4348   4559   4992    292   -935   -904       N  
ATOM   3033  N   LEU C 406      12.570  20.530 -43.797  1.00 37.91           N  
ANISOU 3033  N   LEU C 406     4629   4584   5191    129   -758   -635       N  
ATOM   3034  CA  LEU C 406      11.496  21.452 -44.137  1.00 34.18           C  
ANISOU 3034  CA  LEU C 406     4158   4096   4733     82   -710   -587       C  
ATOM   3035  C   LEU C 406      10.517  21.548 -42.976  1.00 35.66           C  
ANISOU 3035  C   LEU C 406     4397   4256   4897    100   -700   -542       C  
ATOM   3036  O   LEU C 406       9.962  20.536 -42.540  1.00 32.87           O  
ANISOU 3036  O   LEU C 406     4084   3881   4526    126   -712   -504       O  
ATOM   3037  CB  LEU C 406      10.790  20.971 -45.406  1.00 26.19           C  
ANISOU 3037  CB  LEU C 406     3138   3078   3736     52   -690   -552       C  
ATOM   3038  CG  LEU C 406       9.624  21.785 -45.963  1.00 30.54           C  
ANISOU 3038  CG  LEU C 406     3686   3617   4301      5   -643   -498       C  
ATOM   3039  CD1 LEU C 406      10.033  23.234 -46.170  1.00 34.52           C  
ANISOU 3039  CD1 LEU C 406     4152   4139   4825    -28   -619   -513       C  
ATOM   3040  CD2 LEU C 406       9.152  21.170 -47.271  1.00 26.26           C  
ANISOU 3040  CD2 LEU C 406     3128   3081   3767    -16   -635   -479       C  
ATOM   3041  N   GLN C 407      10.326  22.760 -42.456  1.00 32.00           N  
ANISOU 3041  N   GLN C 407     3929   3794   4435     89   -681   -547       N  
ATOM   3042  CA  GLN C 407       9.427  22.996 -41.332  1.00 34.30           C  
ANISOU 3042  CA  GLN C 407     4261   4073   4697    112   -668   -513       C  
ATOM   3043  C   GLN C 407       8.081  23.561 -41.769  1.00 40.03           C  
ANISOU 3043  C   GLN C 407     4992   4779   5437     77   -621   -456       C  
ATOM   3044  O   GLN C 407       7.035  23.070 -41.337  1.00 39.79           O  
ANISOU 3044  O   GLN C 407     4994   4739   5384     89   -606   -399       O  
ATOM   3045  CB  GLN C 407      10.078  23.944 -40.317  1.00 38.41           C  
ANISOU 3045  CB  GLN C 407     4777   4610   5206    137   -685   -570       C  
ATOM   3046  CG  GLN C 407      11.127  23.288 -39.432  1.00 40.44           C  
ANISOU 3046  CG  GLN C 407     5044   4892   5431    190   -734   -616       C  
ATOM   3047  CD  GLN C 407      11.866  24.289 -38.563  1.00 46.45           C  
ANISOU 3047  CD  GLN C 407     5790   5673   6186    210   -757   -685       C  
ATOM   3048  OE1 GLN C 407      11.293  25.284 -38.118  1.00 53.27           O  
ANISOU 3048  OE1 GLN C 407     6660   6529   7050    206   -739   -688       O  
ATOM   3049  NE2 GLN C 407      13.143  24.027 -38.313  1.00 43.10           N  
ANISOU 3049  NE2 GLN C 407     5344   5275   5758    235   -802   -746       N  
ATOM   3050  N   VAL C 408       8.085  24.588 -42.615  1.00 43.08           N  
ANISOU 3050  N   VAL C 408     5344   5163   5862     34   -598   -464       N  
ATOM   3051  CA  VAL C 408       6.863  25.247 -43.056  1.00 38.32           C  
ANISOU 3051  CA  VAL C 408     4742   4543   5274      5   -557   -412       C  
ATOM   3052  C   VAL C 408       6.799  25.227 -44.576  1.00 35.51           C  
ANISOU 3052  C   VAL C 408     4353   4190   4950    -42   -540   -392       C  
ATOM   3053  O   VAL C 408       7.806  25.451 -45.257  1.00 35.73           O  
ANISOU 3053  O   VAL C 408     4343   4235   4998    -61   -550   -428       O  
ATOM   3054  CB  VAL C 408       6.771  26.699 -42.541  1.00 41.54           C  
ANISOU 3054  CB  VAL C 408     5145   4940   5699      4   -545   -434       C  
ATOM   3055  CG1 VAL C 408       5.357  27.006 -42.078  1.00 46.85           C  
ANISOU 3055  CG1 VAL C 408     5843   5602   6356     16   -513   -385       C  
ATOM   3056  CG2 VAL C 408       7.773  26.950 -41.426  1.00 43.62           C  
ANISOU 3056  CG2 VAL C 408     5412   5214   5946     41   -581   -502       C  
ATOM   3057  N   ILE C 409       5.614  24.937 -45.100  1.00 33.37           N  
ANISOU 3057  N   ILE C 409     4091   3910   4679    -58   -515   -334       N  
ATOM   3058  CA  ILE C 409       5.216  25.340 -46.442  1.00 32.12           C  
ANISOU 3058  CA  ILE C 409     3901   3757   4547   -101   -490   -306       C  
ATOM   3059  C   ILE C 409       4.067  26.318 -46.252  1.00 38.76           C  
ANISOU 3059  C   ILE C 409     4749   4579   5398   -109   -456   -264       C  
ATOM   3060  O   ILE C 409       2.957  25.918 -45.881  1.00 45.57           O  
ANISOU 3060  O   ILE C 409     5636   5435   6245    -99   -443   -222       O  
ATOM   3061  CB  ILE C 409       4.803  24.153 -47.321  1.00 30.30           C  
ANISOU 3061  CB  ILE C 409     3669   3535   4310   -110   -496   -283       C  
ATOM   3062  CG1 ILE C 409       5.965  23.173 -47.486  1.00 30.90           C  
ANISOU 3062  CG1 ILE C 409     3738   3627   4377    -92   -533   -333       C  
ATOM   3063  CG2 ILE C 409       4.336  24.645 -48.682  1.00 26.80           C  
ANISOU 3063  CG2 ILE C 409     3192   3109   3883   -148   -470   -254       C  
ATOM   3064  CD1 ILE C 409       5.586  21.903 -48.215  1.00 27.37           C  
ANISOU 3064  CD1 ILE C 409     3294   3178   3927    -92   -550   -322       C  
ATOM   3065  N   ARG C 410       4.338  27.604 -46.473  1.00 30.91           N  
ANISOU 3065  N   ARG C 410     3734   3577   4434   -128   -444   -274       N  
ATOM   3066  CA  ARG C 410       3.359  28.632 -46.144  1.00 35.31           C  
ANISOU 3066  CA  ARG C 410     4301   4111   5006   -126   -419   -246       C  
ATOM   3067  C   ARG C 410       2.195  28.655 -47.123  1.00 37.85           C  
ANISOU 3067  C   ARG C 410     4611   4435   5334   -149   -390   -183       C  
ATOM   3068  O   ARG C 410       1.058  28.925 -46.719  1.00 31.16           O  
ANISOU 3068  O   ARG C 410     3779   3578   4481   -135   -370   -150       O  
ATOM   3069  CB  ARG C 410       4.041  30.000 -46.090  1.00 31.46           C  
ANISOU 3069  CB  ARG C 410     3793   3600   4561   -139   -421   -278       C  
ATOM   3070  CG  ARG C 410       5.213  30.045 -45.124  1.00 34.14           C  
ANISOU 3070  CG  ARG C 410     4137   3939   4897   -117   -455   -348       C  
ATOM   3071  CD  ARG C 410       5.108  31.229 -44.189  1.00 37.37           C  
ANISOU 3071  CD  ARG C 410     4558   4315   5328    -97   -461   -381       C  
ATOM   3072  NE  ARG C 410       6.194  31.263 -43.214  1.00 44.63           N  
ANISOU 3072  NE  ARG C 410     5479   5237   6240    -72   -498   -454       N  
ATOM   3073  CZ  ARG C 410       6.061  30.924 -41.936  1.00 45.83           C  
ANISOU 3073  CZ  ARG C 410     5664   5404   6346    -18   -514   -485       C  
ATOM   3074  NH1 ARG C 410       4.883  30.526 -41.472  1.00 42.02           N  
ANISOU 3074  NH1 ARG C 410     5212   4932   5821     13   -492   -444       N  
ATOM   3075  NH2 ARG C 410       7.105  30.987 -41.121  1.00 43.80           N  
ANISOU 3075  NH2 ARG C 410     5405   5155   6081      5   -552   -555       N  
ATOM   3076  N   GLY C 411       2.447  28.368 -48.395  1.00 40.41           N  
ANISOU 3076  N   GLY C 411     4906   4781   5666   -181   -387   -168       N  
ATOM   3077  CA  GLY C 411       1.370  28.362 -49.364  1.00 40.32           C  
ANISOU 3077  CA  GLY C 411     4883   4781   5658   -201   -365   -112       C  
ATOM   3078  C   GLY C 411       0.813  29.728 -49.687  1.00 37.95           C  
ANISOU 3078  C   GLY C 411     4569   4461   5388   -213   -340    -78       C  
ATOM   3079  O   GLY C 411      -0.373  29.843 -50.013  1.00 43.37           O  
ANISOU 3079  O   GLY C 411     5255   5150   6073   -214   -321    -31       O  
ATOM   3080  N   ARG C 412       1.633  30.778 -49.588  1.00 34.92           N  
ANISOU 3080  N   ARG C 412     4173   4056   5038   -223   -343    -99       N  
ATOM   3081  CA  ARG C 412       1.196  32.092 -50.040  1.00 33.13           C  
ANISOU 3081  CA  ARG C 412     3933   3803   4853   -239   -324    -62       C  
ATOM   3082  C   ARG C 412       1.015  32.127 -51.549  1.00 29.75           C  
ANISOU 3082  C   ARG C 412     3471   3408   4425   -272   -308     -9       C  
ATOM   3083  O   ARG C 412       0.287  32.984 -52.061  1.00 38.22           O  
ANISOU 3083  O   ARG C 412     4534   4466   5521   -280   -289     41       O  
ATOM   3084  CB  ARG C 412       2.196  33.155 -49.590  1.00 30.15           C  
ANISOU 3084  CB  ARG C 412     3547   3386   4521   -248   -336    -99       C  
ATOM   3085  CG  ARG C 412       2.474  33.094 -48.099  1.00 32.32           C  
ANISOU 3085  CG  ARG C 412     3853   3639   4787   -210   -358   -162       C  
ATOM   3086  CD  ARG C 412       3.093  34.367 -47.575  1.00 33.55           C  
ANISOU 3086  CD  ARG C 412     4004   3743   4998   -213   -373   -200       C  
ATOM   3087  NE  ARG C 412       3.321  34.291 -46.136  1.00 34.98           N  
ANISOU 3087  NE  ARG C 412     4216   3915   5162   -169   -397   -267       N  
ATOM   3088  CZ  ARG C 412       4.497  34.494 -45.554  1.00 39.04           C  
ANISOU 3088  CZ  ARG C 412     4722   4418   5692   -169   -428   -331       C  
ATOM   3089  NH1 ARG C 412       5.561  34.796 -46.288  1.00 32.89           N  
ANISOU 3089  NH1 ARG C 412     3905   3638   4955   -217   -436   -335       N  
ATOM   3090  NH2 ARG C 412       4.607  34.404 -44.236  1.00 43.55           N  
ANISOU 3090  NH2 ARG C 412     5321   4990   6237   -122   -451   -392       N  
ATOM   3091  N   ILE C 413       1.671  31.215 -52.261  1.00 21.13           N  
ANISOU 3091  N   ILE C 413     2359   2364   3305   -286   -316    -21       N  
ATOM   3092  CA  ILE C 413       1.397  30.921 -53.660  1.00 24.19           C  
ANISOU 3092  CA  ILE C 413     2715   2802   3672   -307   -305     20       C  
ATOM   3093  C   ILE C 413       1.049  29.443 -53.739  1.00 35.08           C  
ANISOU 3093  C   ILE C 413     4106   4214   5009   -291   -320      0       C  
ATOM   3094  O   ILE C 413       1.783  28.600 -53.210  1.00 37.01           O  
ANISOU 3094  O   ILE C 413     4362   4460   5239   -278   -343    -51       O  
ATOM   3095  CB  ILE C 413       2.600  31.251 -54.562  1.00 28.74           C  
ANISOU 3095  CB  ILE C 413     3249   3417   4255   -337   -302     20       C  
ATOM   3096  CG1 ILE C 413       3.210  32.597 -54.165  1.00 28.40           C  
ANISOU 3096  CG1 ILE C 413     3197   3325   4267   -356   -297     26       C  
ATOM   3097  CG2 ILE C 413       2.178  31.269 -56.026  1.00 27.87           C  
ANISOU 3097  CG2 ILE C 413     3105   3364   4121   -353   -285     76       C  
ATOM   3098  CD1 ILE C 413       4.647  32.774 -54.606  1.00 40.65           C  
ANISOU 3098  CD1 ILE C 413     4708   4908   5831   -385   -300      9       C  
ATOM   3099  N   LEU C 414      -0.074  29.132 -54.374  1.00 37.62           N  
ANISOU 3099  N   LEU C 414     4424   4555   5316   -291   -313     39       N  
ATOM   3100  CA  LEU C 414      -0.568  27.767 -54.470  1.00 28.41           C  
ANISOU 3100  CA  LEU C 414     3267   3407   4122   -281   -331     23       C  
ATOM   3101  C   LEU C 414      -0.537  27.302 -55.915  1.00 28.12           C  
ANISOU 3101  C   LEU C 414     3195   3432   4058   -293   -337     28       C  
ATOM   3102  O   LEU C 414      -0.845  28.073 -56.826  1.00 21.76           O  
ANISOU 3102  O   LEU C 414     2362   2655   3251   -307   -318     73       O  
ATOM   3103  CB  LEU C 414      -1.995  27.661 -53.927  1.00 23.01           C  
ANISOU 3103  CB  LEU C 414     2602   2697   3442   -271   -323     57       C  
ATOM   3104  CG  LEU C 414      -2.220  28.274 -52.532  1.00 26.33           C  
ANISOU 3104  CG  LEU C 414     3054   3071   3880   -251   -312     56       C  
ATOM   3105  CD1 LEU C 414      -3.701  28.496 -52.259  1.00 14.41           C  
ANISOU 3105  CD1 LEU C 414     1548   1552   2373   -241   -293    102       C  
ATOM   3106  CD2 LEU C 414      -1.613  27.375 -51.475  1.00 23.74           C  
ANISOU 3106  CD2 LEU C 414     2754   2726   3540   -233   -333     12       C  
ATOM   3107  N   HIS C 415      -0.156  26.043 -56.125  1.00 31.74           N  
ANISOU 3107  N   HIS C 415     3654   3911   4496   -284   -365    -18       N  
ATOM   3108  CA  HIS C 415      -0.240  25.478 -57.464  1.00 35.05           C  
ANISOU 3108  CA  HIS C 415     4040   4393   4885   -288   -376    -25       C  
ATOM   3109  C   HIS C 415      -1.697  25.408 -57.905  1.00 35.97           C  
ANISOU 3109  C   HIS C 415     4154   4515   5000   -293   -373     18       C  
ATOM   3110  O   HIS C 415      -2.563  24.930 -57.164  1.00 22.50           O  
ANISOU 3110  O   HIS C 415     2473   2766   3312   -290   -381     25       O  
ATOM   3111  CB  HIS C 415       0.392  24.088 -57.522  1.00 35.04           C  
ANISOU 3111  CB  HIS C 415     4043   4402   4868   -270   -415    -92       C  
ATOM   3112  CG  HIS C 415       0.447  23.523 -58.906  1.00 34.60           C  
ANISOU 3112  CG  HIS C 415     3951   4418   4776   -266   -431   -116       C  
ATOM   3113  ND1 HIS C 415      -0.482  22.622 -59.380  1.00 34.16           N  
ANISOU 3113  ND1 HIS C 415     3895   4367   4716   -262   -457   -126       N  
ATOM   3114  CD2 HIS C 415       1.296  23.763 -59.933  1.00 34.25           C  
ANISOU 3114  CD2 HIS C 415     3865   4450   4698   -263   -424   -131       C  
ATOM   3115  CE1 HIS C 415      -0.198  22.319 -60.633  1.00 36.82           C  
ANISOU 3115  CE1 HIS C 415     4196   4781   5015   -252   -470   -155       C  
ATOM   3116  NE2 HIS C 415       0.877  22.997 -60.993  1.00 38.83           N  
ANISOU 3116  NE2 HIS C 415     4424   5085   5246   -251   -447   -156       N  
ATOM   3117  N   ASN C 416      -1.965  25.907 -59.113  1.00 39.72           N  
ANISOU 3117  N   ASN C 416     4592   5047   5452   -300   -361     49       N  
ATOM   3118  CA  ASN C 416      -3.325  26.049 -59.635  1.00 35.84           C  
ANISOU 3118  CA  ASN C 416     4090   4571   4957   -304   -357     94       C  
ATOM   3119  C   ASN C 416      -4.216  26.841 -58.682  1.00 37.49           C  
ANISOU 3119  C   ASN C 416     4321   4721   5201   -305   -334    142       C  
ATOM   3120  O   ASN C 416      -5.444  26.721 -58.722  1.00 41.01           O  
ANISOU 3120  O   ASN C 416     4765   5166   5653   -305   -334    171       O  
ATOM   3121  CB  ASN C 416      -3.951  24.684 -59.945  1.00 29.20           C  
ANISOU 3121  CB  ASN C 416     3247   3740   4106   -299   -394     57       C  
ATOM   3122  CG  ASN C 416      -3.327  24.018 -61.156  1.00 36.24           C  
ANISOU 3122  CG  ASN C 416     4108   4705   4957   -290   -420      9       C  
ATOM   3123  OD1 ASN C 416      -2.793  24.685 -62.041  1.00 44.17           O  
ANISOU 3123  OD1 ASN C 416     5082   5774   5928   -289   -402     26       O  
ATOM   3124  ND2 ASN C 416      -3.397  22.692 -61.203  1.00 43.88           N  
ANISOU 3124  ND2 ASN C 416     5082   5663   5926   -282   -462    -50       N  
ATOM   3125  N   GLY C 417      -3.606  27.646 -57.812  1.00 31.55           N  
ANISOU 3125  N   GLY C 417     3589   3926   4474   -304   -315    146       N  
ATOM   3126  CA  GLY C 417      -4.329  28.442 -56.846  1.00 26.71           C  
ANISOU 3126  CA  GLY C 417     2998   3260   3891   -296   -295    179       C  
ATOM   3127  C   GLY C 417      -4.937  27.684 -55.687  1.00 31.82           C  
ANISOU 3127  C   GLY C 417     3675   3870   4547   -285   -304    163       C  
ATOM   3128  O   GLY C 417      -5.627  28.300 -54.867  1.00 38.07           O  
ANISOU 3128  O   GLY C 417     4479   4628   5355   -272   -285    188       O  
ATOM   3129  N   ALA C 418      -4.699  26.381 -55.572  1.00 36.37           N  
ANISOU 3129  N   ALA C 418     4259   4448   5112   -286   -330    124       N  
ATOM   3130  CA  ALA C 418      -5.362  25.583 -54.548  1.00 34.72           C  
ANISOU 3130  CA  ALA C 418     4074   4206   4912   -280   -338    124       C  
ATOM   3131  C   ALA C 418      -4.412  24.790 -53.664  1.00 39.80           C  
ANISOU 3131  C   ALA C 418     4747   4820   5554   -270   -358     79       C  
ATOM   3132  O   ALA C 418      -4.613  24.741 -52.447  1.00 41.15           O  
ANISOU 3132  O   ALA C 418     4946   4960   5731   -257   -350     86       O  
ATOM   3133  CB  ALA C 418      -6.362  24.620 -55.205  1.00 32.67           C  
ANISOU 3133  CB  ALA C 418     3796   3966   4652   -294   -357    135       C  
ATOM   3134  N   TYR C 419      -3.378  24.171 -54.228  1.00 34.07           N  
ANISOU 3134  N   TYR C 419     4016   4110   4818   -271   -384     32       N  
ATOM   3135  CA  TYR C 419      -2.600  23.156 -53.525  1.00 36.52           C  
ANISOU 3135  CA  TYR C 419     4352   4395   5128   -259   -412    -11       C  
ATOM   3136  C   TYR C 419      -1.244  23.709 -53.107  1.00 31.94           C  
ANISOU 3136  C   TYR C 419     3779   3814   4543   -245   -410    -47       C  
ATOM   3137  O   TYR C 419      -0.473  24.182 -53.948  1.00 33.24           O  
ANISOU 3137  O   TYR C 419     3917   4014   4700   -252   -407    -65       O  
ATOM   3138  CB  TYR C 419      -2.422  21.914 -54.397  1.00 36.62           C  
ANISOU 3138  CB  TYR C 419     4354   4423   5138   -262   -451    -48       C  
ATOM   3139  CG  TYR C 419      -3.730  21.354 -54.902  1.00 28.96           C  
ANISOU 3139  CG  TYR C 419     3370   3453   4179   -280   -460    -20       C  
ATOM   3140  CD1 TYR C 419      -4.177  21.637 -56.185  1.00 28.68           C  
ANISOU 3140  CD1 TYR C 419     3299   3468   4131   -290   -459    -14       C  
ATOM   3141  CD2 TYR C 419      -4.528  20.560 -54.089  1.00 22.15           C  
ANISOU 3141  CD2 TYR C 419     2528   2546   3340   -286   -471      4       C  
ATOM   3142  CE1 TYR C 419      -5.371  21.135 -56.651  1.00 27.91           C  
ANISOU 3142  CE1 TYR C 419     3184   3374   4045   -306   -472      6       C  
ATOM   3143  CE2 TYR C 419      -5.730  20.051 -54.547  1.00 25.65           C  
ANISOU 3143  CE2 TYR C 419     2953   2991   3802   -308   -481     30       C  
ATOM   3144  CZ  TYR C 419      -6.145  20.344 -55.829  1.00 33.21           C  
ANISOU 3144  CZ  TYR C 419     3874   3997   4749   -317   -484     26       C  
ATOM   3145  OH  TYR C 419      -7.339  19.844 -56.293  1.00 48.97           O  
ANISOU 3145  OH  TYR C 419     5846   5996   6763   -339   -499     46       O  
ATOM   3146  N   SER C 420      -0.955  23.631 -51.807  1.00 18.35           N  
ANISOU 3146  N   SER C 420     2090   2058   2824   -227   -413    -56       N  
ATOM   3147  CA  SER C 420       0.356  23.973 -51.273  1.00 28.08           C  
ANISOU 3147  CA  SER C 420     3329   3287   4053   -212   -420    -99       C  
ATOM   3148  C   SER C 420       1.332  22.806 -51.306  1.00 32.35           C  
ANISOU 3148  C   SER C 420     3876   3830   4586   -197   -459   -151       C  
ATOM   3149  O   SER C 420       2.548  23.033 -51.309  1.00 43.60           O  
ANISOU 3149  O   SER C 420     5289   5270   6006   -188   -468   -194       O  
ATOM   3150  CB  SER C 420       0.228  24.472 -49.828  1.00 26.45           C  
ANISOU 3150  CB  SER C 420     3154   3050   3847   -191   -409    -92       C  
ATOM   3151  OG  SER C 420      -0.574  23.594 -49.057  1.00 26.86           O  
ANISOU 3151  OG  SER C 420     3232   3082   3892   -179   -414    -66       O  
ATOM   3152  N   LEU C 421       0.831  21.571 -51.325  1.00 26.78           N  
ANISOU 3152  N   LEU C 421     3185   3108   3884   -193   -483   -148       N  
ATOM   3153  CA  LEU C 421       1.669  20.378 -51.362  1.00 27.70           C  
ANISOU 3153  CA  LEU C 421     3309   3216   3999   -173   -526   -197       C  
ATOM   3154  C   LEU C 421       1.051  19.390 -52.335  1.00 31.31           C  
ANISOU 3154  C   LEU C 421     3756   3674   4467   -185   -550   -201       C  
ATOM   3155  O   LEU C 421      -0.079  18.942 -52.125  1.00 29.99           O  
ANISOU 3155  O   LEU C 421     3601   3477   4316   -199   -551   -159       O  
ATOM   3156  CB  LEU C 421       1.796  19.749 -49.971  1.00 22.99           C  
ANISOU 3156  CB  LEU C 421     2756   2576   3404   -148   -544   -192       C  
ATOM   3157  CG  LEU C 421       2.562  18.425 -49.909  1.00 26.50           C  
ANISOU 3157  CG  LEU C 421     3214   2999   3854   -123   -593   -236       C  
ATOM   3158  CD1 LEU C 421       4.042  18.645 -50.187  1.00 28.67           C  
ANISOU 3158  CD1 LEU C 421     3469   3309   4116   -101   -608   -302       C  
ATOM   3159  CD2 LEU C 421       2.354  17.734 -48.568  1.00 26.48           C  
ANISOU 3159  CD2 LEU C 421     3256   2950   3855   -103   -608   -206       C  
ATOM   3160  N   THR C 422       1.784  19.045 -53.391  1.00 37.58           N  
ANISOU 3160  N   THR C 422     4523   4506   5251   -177   -572   -254       N  
ATOM   3161  CA  THR C 422       1.292  18.094 -54.378  1.00 37.69           C  
ANISOU 3161  CA  THR C 422     4524   4525   5273   -181   -603   -275       C  
ATOM   3162  C   THR C 422       2.343  17.024 -54.619  1.00 36.46           C  
ANISOU 3162  C   THR C 422     4368   4367   5117   -148   -651   -349       C  
ATOM   3163  O   THR C 422       3.509  17.342 -54.860  1.00 34.02           O  
ANISOU 3163  O   THR C 422     4038   4102   4784   -129   -649   -392       O  
ATOM   3164  CB  THR C 422       0.938  18.789 -55.695  1.00 35.85           C  
ANISOU 3164  CB  THR C 422     4247   4358   5018   -200   -581   -267       C  
ATOM   3165  OG1 THR C 422      -0.080  19.770 -55.460  1.00 44.06           O  
ANISOU 3165  OG1 THR C 422     5286   5392   6061   -225   -539   -198       O  
ATOM   3166  CG2 THR C 422       0.443  17.774 -56.717  1.00 28.54           C  
ANISOU 3166  CG2 THR C 422     3305   3442   4096   -198   -619   -301       C  
ATOM   3167  N   LEU C 423       1.928  15.762 -54.540  1.00 35.87           N  
ANISOU 3167  N   LEU C 423     4316   4240   5074   -142   -696   -363       N  
ATOM   3168  CA  LEU C 423       2.784  14.620 -54.837  1.00 27.13           C  
ANISOU 3168  CA  LEU C 423     3212   3122   3976   -105   -751   -439       C  
ATOM   3169  C   LEU C 423       1.998  13.700 -55.749  1.00 24.02           C  
ANISOU 3169  C   LEU C 423     2808   2712   3607   -113   -791   -463       C  
ATOM   3170  O   LEU C 423       0.929  13.218 -55.357  1.00 25.62           O  
ANISOU 3170  O   LEU C 423     3032   2853   3850   -139   -802   -417       O  
ATOM   3171  CB  LEU C 423       3.189  13.882 -53.559  1.00 19.80           C  
ANISOU 3171  CB  LEU C 423     2329   2121   3074    -82   -779   -433       C  
ATOM   3172  CG  LEU C 423       3.878  14.741 -52.489  1.00 29.67           C  
ANISOU 3172  CG  LEU C 423     3591   3381   4299    -71   -747   -410       C  
ATOM   3173  CD1 LEU C 423       4.014  13.968 -51.193  1.00 29.08           C  
ANISOU 3173  CD1 LEU C 423     3565   3238   4246    -49   -774   -389       C  
ATOM   3174  CD2 LEU C 423       5.238  15.225 -52.966  1.00 27.41           C  
ANISOU 3174  CD2 LEU C 423     3271   3162   3981    -46   -744   -473       C  
ATOM   3175  N   GLN C 424       2.497  13.471 -56.962  1.00 26.45           N  
ANISOU 3175  N   GLN C 424     3081   3080   3890    -91   -813   -535       N  
ATOM   3176  CA  GLN C 424       1.723  12.632 -57.866  1.00 33.38           C  
ANISOU 3176  CA  GLN C 424     3946   3946   4789    -96   -855   -569       C  
ATOM   3177  C   GLN C 424       2.623  11.856 -58.818  1.00 36.67           C  
ANISOU 3177  C   GLN C 424     4340   4403   5190    -46   -905   -676       C  
ATOM   3178  O   GLN C 424       3.602  12.391 -59.345  1.00 47.46           O  
ANISOU 3178  O   GLN C 424     5674   5857   6503    -20   -884   -714       O  
ATOM   3179  CB  GLN C 424       0.701  13.465 -58.652  1.00 32.52           C  
ANISOU 3179  CB  GLN C 424     3805   3894   4657   -132   -819   -526       C  
ATOM   3180  CG  GLN C 424       1.297  14.472 -59.614  1.00 37.70           C  
ANISOU 3180  CG  GLN C 424     4415   4663   5246   -121   -781   -541       C  
ATOM   3181  CD  GLN C 424       0.235  15.307 -60.297  1.00 42.26           C  
ANISOU 3181  CD  GLN C 424     4965   5289   5802   -154   -746   -487       C  
ATOM   3182  OE1 GLN C 424      -0.748  15.712 -59.675  1.00 44.35           O  
ANISOU 3182  OE1 GLN C 424     5247   5510   6094   -189   -721   -414       O  
ATOM   3183  NE2 GLN C 424       0.420  15.559 -61.587  1.00 39.28           N  
ANISOU 3183  NE2 GLN C 424     4543   5009   5374   -140   -744   -521       N  
ATOM   3184  N   GLY C 425       2.277  10.586 -59.026  1.00 34.08           N  
ANISOU 3184  N   GLY C 425     4027   4010   4911    -34   -972   -725       N  
ATOM   3185  CA  GLY C 425       2.960   9.753 -59.999  1.00 28.55           C  
ANISOU 3185  CA  GLY C 425     3305   3344   4200     18  -1028   -838       C  
ATOM   3186  C   GLY C 425       4.372   9.357 -59.632  1.00 26.44           C  
ANISOU 3186  C   GLY C 425     3046   3077   3924     75  -1049   -898       C  
ATOM   3187  O   GLY C 425       5.176   9.072 -60.524  1.00 26.28           O  
ANISOU 3187  O   GLY C 425     2990   3128   3865    125  -1073   -991       O  
ATOM   3188  N   LEU C 426       4.695   9.311 -58.344  1.00 22.07           N  
ANISOU 3188  N   LEU C 426     2533   2453   3400     72  -1043   -850       N  
ATOM   3189  CA  LEU C 426       6.050   9.049 -57.879  1.00 26.62           C  
ANISOU 3189  CA  LEU C 426     3115   3033   3965    126  -1060   -898       C  
ATOM   3190  C   LEU C 426       6.225   7.583 -57.496  1.00 31.82           C  
ANISOU 3190  C   LEU C 426     3814   3586   4691    165  -1140   -947       C  
ATOM   3191  O   LEU C 426       5.263   6.823 -57.375  1.00 32.10           O  
ANISOU 3191  O   LEU C 426     3877   3528   4789    139  -1179   -926       O  
ATOM   3192  CB  LEU C 426       6.390   9.935 -56.678  1.00 24.97           C  
ANISOU 3192  CB  LEU C 426     2926   2820   3743    107  -1007   -821       C  
ATOM   3193  CG  LEU C 426       6.074  11.427 -56.785  1.00 23.56           C  
ANISOU 3193  CG  LEU C 426     2720   2714   3518     61   -930   -755       C  
ATOM   3194  CD1 LEU C 426       6.448  12.136 -55.494  1.00 25.13           C  
ANISOU 3194  CD1 LEU C 426     2943   2893   3714     51   -893   -696       C  
ATOM   3195  CD2 LEU C 426       6.797  12.047 -57.964  1.00 26.48           C  
ANISOU 3195  CD2 LEU C 426     3028   3206   3826     78   -906   -807       C  
ATOM   3196  N   GLY C 427       7.481   7.199 -57.292  1.00 33.66           N  
ANISOU 3196  N   GLY C 427     4046   3831   4914    226  -1168  -1011       N  
ATOM   3197  CA  GLY C 427       7.801   5.843 -56.891  1.00 21.92           C  
ANISOU 3197  CA  GLY C 427     2597   2241   3490    273  -1247  -1058       C  
ATOM   3198  C   GLY C 427       8.130   5.718 -55.419  1.00 27.80           C  
ANISOU 3198  C   GLY C 427     3390   2910   4262    277  -1247   -991       C  
ATOM   3199  O   GLY C 427       8.347   4.607 -54.924  1.00 39.28           O  
ANISOU 3199  O   GLY C 427     4883   4266   5775    313  -1312  -1009       O  
ATOM   3200  N   ILE C 428       8.164   6.852 -54.712  1.00 31.91           N  
ANISOU 3200  N   ILE C 428     3909   3475   4741    243  -1178   -914       N  
ATOM   3201  CA  ILE C 428       8.535   6.901 -53.300  1.00 30.59           C  
ANISOU 3201  CA  ILE C 428     3782   3260   4581    252  -1172   -853       C  
ATOM   3202  C   ILE C 428       7.700   5.908 -52.504  1.00 33.76           C  
ANISOU 3202  C   ILE C 428     4241   3529   5055    235  -1213   -790       C  
ATOM   3203  O   ILE C 428       6.554   5.611 -52.862  1.00 24.86           O  
ANISOU 3203  O   ILE C 428     3120   2356   3969    190  -1219   -758       O  
ATOM   3204  CB  ILE C 428       8.375   8.322 -52.725  1.00 30.96           C  
ANISOU 3204  CB  ILE C 428     3819   3367   4579    208  -1092   -778       C  
ATOM   3205  CG1 ILE C 428       6.955   8.842 -52.959  1.00 29.32           C  
ANISOU 3205  CG1 ILE C 428     3611   3152   4379    138  -1050   -705       C  
ATOM   3206  CG2 ILE C 428       9.404   9.265 -53.325  1.00 23.92           C  
ANISOU 3206  CG2 ILE C 428     2871   2593   3625    225  -1057   -833       C  
ATOM   3207  CD1 ILE C 428       6.628  10.102 -52.185  1.00 31.72           C  
ANISOU 3207  CD1 ILE C 428     3917   3487   4649     99   -981   -624       C  
ATOM   3208  N   SER C 429       8.275   5.380 -51.422  1.00 35.05           N  
ANISOU 3208  N   SER C 429     4445   3635   5238    273  -1243   -767       N  
ATOM   3209  CA  SER C 429       7.591   4.417 -50.572  1.00 28.20           C  
ANISOU 3209  CA  SER C 429     3632   2643   4439    260  -1281   -693       C  
ATOM   3210  C   SER C 429       7.113   5.003 -49.252  1.00 33.82           C  
ANISOU 3210  C   SER C 429     4374   3347   5130    226  -1230   -573       C  
ATOM   3211  O   SER C 429       6.211   4.429 -48.635  1.00 40.66           O  
ANISOU 3211  O   SER C 429     5275   4128   6046    193  -1240   -487       O  
ATOM   3212  CB  SER C 429       8.507   3.218 -50.291  1.00 22.77           C  
ANISOU 3212  CB  SER C 429     2973   1884   3794    333  -1361   -746       C  
ATOM   3213  OG  SER C 429       8.945   2.637 -51.507  1.00 27.15           O  
ANISOU 3213  OG  SER C 429     3499   2449   4366    373  -1412   -866       O  
ATOM   3214  N   TRP C 430       7.698   6.112 -48.804  1.00 30.82           N  
ANISOU 3214  N   TRP C 430     3977   3054   4679    233  -1177   -568       N  
ATOM   3215  CA  TRP C 430       7.154   6.904 -47.710  1.00 34.11           C  
ANISOU 3215  CA  TRP C 430     4411   3485   5063    200  -1120   -468       C  
ATOM   3216  C   TRP C 430       7.519   8.362 -47.962  1.00 31.36           C  
ANISOU 3216  C   TRP C 430     4022   3246   4649    187  -1058   -493       C  
ATOM   3217  O   TRP C 430       8.200   8.689 -48.938  1.00 29.12           O  
ANISOU 3217  O   TRP C 430     3695   3023   4344    202  -1058   -576       O  
ATOM   3218  CB  TRP C 430       7.656   6.410 -46.349  1.00 39.98           C  
ANISOU 3218  CB  TRP C 430     5200   4186   5805    242  -1146   -421       C  
ATOM   3219  CG  TRP C 430       9.146   6.396 -46.206  1.00 41.46           C  
ANISOU 3219  CG  TRP C 430     5378   4414   5962    312  -1176   -500       C  
ATOM   3220  CD1 TRP C 430       9.934   7.401 -45.727  1.00 38.79           C  
ANISOU 3220  CD1 TRP C 430     5020   4159   5560    331  -1142   -519       C  
ATOM   3221  CD2 TRP C 430      10.029   5.318 -46.539  1.00 38.02           C  
ANISOU 3221  CD2 TRP C 430     4948   3936   5561    374  -1249   -574       C  
ATOM   3222  NE1 TRP C 430      11.253   7.017 -45.743  1.00 34.43           N  
ANISOU 3222  NE1 TRP C 430     4457   3625   5000    398  -1188   -597       N  
ATOM   3223  CE2 TRP C 430      11.338   5.741 -46.236  1.00 34.97           C  
ANISOU 3223  CE2 TRP C 430     4542   3620   5126    429  -1253   -633       C  
ATOM   3224  CE3 TRP C 430       9.839   4.033 -47.058  1.00 37.28           C  
ANISOU 3224  CE3 TRP C 430     4873   3750   5540    391  -1316   -600       C  
ATOM   3225  CZ2 TRP C 430      12.453   4.929 -46.441  1.00 32.28           C  
ANISOU 3225  CZ2 TRP C 430     4197   3266   4801    503  -1318   -715       C  
ATOM   3226  CZ3 TRP C 430      10.946   3.227 -47.261  1.00 28.74           C  
ANISOU 3226  CZ3 TRP C 430     3793   2650   4478    467  -1383   -685       C  
ATOM   3227  CH2 TRP C 430      12.236   3.678 -46.953  1.00 26.32           C  
ANISOU 3227  CH2 TRP C 430     3464   2422   4116    524  -1382   -741       C  
ATOM   3228  N   LEU C 431       7.055   9.244 -47.078  1.00 31.12           N  
ANISOU 3228  N   LEU C 431     4000   3239   4584    161  -1005   -420       N  
ATOM   3229  CA  LEU C 431       7.265  10.678 -47.259  1.00 24.71           C  
ANISOU 3229  CA  LEU C 431     3152   2514   3721    142   -947   -435       C  
ATOM   3230  C   LEU C 431       8.605  11.128 -46.682  1.00 35.42           C  
ANISOU 3230  C   LEU C 431     4501   3920   5039    189   -953   -482       C  
ATOM   3231  O   LEU C 431       9.485  11.587 -47.417  1.00 37.59           O  
ANISOU 3231  O   LEU C 431     4733   4255   5296    201   -950   -555       O  
ATOM   3232  CB  LEU C 431       6.114  11.464 -46.621  1.00 34.21           C  
ANISOU 3232  CB  LEU C 431     4367   3721   4910     97   -891   -345       C  
ATOM   3233  CG  LEU C 431       4.718  11.211 -47.193  1.00 36.43           C  
ANISOU 3233  CG  LEU C 431     4646   3968   5226     45   -877   -295       C  
ATOM   3234  CD1 LEU C 431       3.669  11.995 -46.425  1.00 39.24           C  
ANISOU 3234  CD1 LEU C 431     5010   4337   5563     10   -821   -209       C  
ATOM   3235  CD2 LEU C 431       4.662  11.554 -48.669  1.00 35.55           C  
ANISOU 3235  CD2 LEU C 431     4490   3899   5118     23   -870   -353       C  
ATOM   3236  N   GLY C 432       8.769  11.008 -45.367  1.00 35.79           N  
ANISOU 3236  N   GLY C 432     4583   3945   5068    215   -960   -439       N  
ATOM   3237  CA  GLY C 432      10.010  11.374 -44.722  1.00 27.42           C  
ANISOU 3237  CA  GLY C 432     3516   2929   3972    262   -972   -484       C  
ATOM   3238  C   GLY C 432      10.181  12.846 -44.433  1.00 40.59           C  
ANISOU 3238  C   GLY C 432     5157   4665   5599    242   -922   -489       C  
ATOM   3239  O   GLY C 432      11.302  13.274 -44.137  1.00 52.01           O  
ANISOU 3239  O   GLY C 432     6582   6157   7021    273   -933   -543       O  
ATOM   3240  N   LEU C 433       9.114  13.641 -44.520  1.00 40.58           N  
ANISOU 3240  N   LEU C 433     5153   4670   5593    191   -870   -437       N  
ATOM   3241  CA  LEU C 433       9.171  15.056 -44.151  1.00 37.54           C  
ANISOU 3241  CA  LEU C 433     4749   4336   5178    173   -825   -438       C  
ATOM   3242  C   LEU C 433       9.006  15.178 -42.637  1.00 42.71           C  
ANISOU 3242  C   LEU C 433     5443   4987   5799    201   -823   -394       C  
ATOM   3243  O   LEU C 433       8.024  15.711 -42.120  1.00 55.53           O  
ANISOU 3243  O   LEU C 433     7081   6609   7408    179   -785   -336       O  
ATOM   3244  CB  LEU C 433       8.110  15.857 -44.894  1.00 33.82           C  
ANISOU 3244  CB  LEU C 433     4259   3874   4716    116   -774   -404       C  
ATOM   3245  CG  LEU C 433       7.877  15.526 -46.380  1.00 29.18           C  
ANISOU 3245  CG  LEU C 433     3642   3288   4157     88   -776   -426       C  
ATOM   3246  CD1 LEU C 433       6.546  16.083 -46.871  1.00 20.49           C  
ANISOU 3246  CD1 LEU C 433     2535   2184   3066     37   -732   -371       C  
ATOM   3247  CD2 LEU C 433       9.014  16.044 -47.243  1.00 30.74           C  
ANISOU 3247  CD2 LEU C 433     3789   3544   4348     92   -777   -500       C  
ATOM   3248  N   ARG C 434      10.011  14.673 -41.922  1.00 39.35           N  
ANISOU 3248  N   ARG C 434     5030   4565   5356    255   -867   -425       N  
ATOM   3249  CA  ARG C 434       9.904  14.507 -40.476  1.00 44.98           C  
ANISOU 3249  CA  ARG C 434     5783   5276   6031    293   -875   -380       C  
ATOM   3250  C   ARG C 434       9.815  15.832 -39.732  1.00 47.02           C  
ANISOU 3250  C   ARG C 434     6033   5583   6249    289   -839   -385       C  
ATOM   3251  O   ARG C 434       9.341  15.856 -38.590  1.00 54.27           O  
ANISOU 3251  O   ARG C 434     6984   6509   7129    313   -831   -335       O  
ATOM   3252  CB  ARG C 434      11.102  13.716 -39.944  1.00 47.53           C  
ANISOU 3252  CB  ARG C 434     6117   5598   6342    357   -935   -420       C  
ATOM   3253  CG  ARG C 434      11.634  12.665 -40.891  1.00 60.45           C  
ANISOU 3253  CG  ARG C 434     7745   7201   8023    370   -978   -459       C  
ATOM   3254  CD  ARG C 434      13.046  12.295 -40.491  1.00 65.67           C  
ANISOU 3254  CD  ARG C 434     8397   7884   8668    435  -1031   -524       C  
ATOM   3255  NE  ARG C 434      13.808  13.491 -40.143  1.00 63.36           N  
ANISOU 3255  NE  ARG C 434     8069   7662   8341    438  -1016   -579       N  
ATOM   3256  CZ  ARG C 434      15.054  13.481 -39.683  1.00 67.99           C  
ANISOU 3256  CZ  ARG C 434     8638   8287   8907    490  -1056   -641       C  
ATOM   3257  NH1 ARG C 434      15.688  12.330 -39.505  1.00 66.05           N  
ANISOU 3257  NH1 ARG C 434     8410   8018   8669    548  -1112   -654       N  
ATOM   3258  NH2 ARG C 434      15.664  14.622 -39.395  1.00 71.95           N  
ANISOU 3258  NH2 ARG C 434     9103   8848   9386    484  -1043   -691       N  
ATOM   3259  N   SER C 435      10.268  16.930 -40.337  1.00 32.10           N  
ANISOU 3259  N   SER C 435     4101   3728   4368    263   -820   -444       N  
ATOM   3260  CA  SER C 435      10.216  18.228 -39.679  1.00 35.13           C  
ANISOU 3260  CA  SER C 435     4475   4146   4725    260   -794   -458       C  
ATOM   3261  C   SER C 435       9.011  19.063 -40.082  1.00 33.82           C  
ANISOU 3261  C   SER C 435     4304   3974   4572    210   -739   -416       C  
ATOM   3262  O   SER C 435       8.688  20.025 -39.378  1.00 33.48           O  
ANISOU 3262  O   SER C 435     4264   3951   4506    215   -717   -415       O  
ATOM   3263  CB  SER C 435      11.491  19.029 -39.971  1.00 32.12           C  
ANISOU 3263  CB  SER C 435     4048   3802   4354    260   -809   -546       C  
ATOM   3264  OG  SER C 435      12.654  18.277 -39.657  1.00 29.20           O  
ANISOU 3264  OG  SER C 435     3676   3446   3974    309   -861   -592       O  
ATOM   3265  N   LEU C 436       8.348  18.725 -41.188  1.00 29.53           N  
ANISOU 3265  N   LEU C 436     3751   3405   4065    169   -721   -386       N  
ATOM   3266  CA  LEU C 436       7.208  19.502 -41.658  1.00 27.18           C  
ANISOU 3266  CA  LEU C 436     3444   3103   3780    124   -672   -346       C  
ATOM   3267  C   LEU C 436       6.094  19.494 -40.622  1.00 33.62           C  
ANISOU 3267  C   LEU C 436     4294   3916   4566    136   -648   -278       C  
ATOM   3268  O   LEU C 436       5.555  18.436 -40.288  1.00 45.26           O  
ANISOU 3268  O   LEU C 436     5796   5367   6035    146   -656   -221       O  
ATOM   3269  CB  LEU C 436       6.704  18.939 -42.987  1.00 22.44           C  
ANISOU 3269  CB  LEU C 436     2828   2481   3217     85   -666   -326       C  
ATOM   3270  CG  LEU C 436       5.579  19.746 -43.638  1.00 28.35           C  
ANISOU 3270  CG  LEU C 436     3561   3231   3982     39   -619   -288       C  
ATOM   3271  CD1 LEU C 436       6.109  21.090 -44.114  1.00 25.05           C  
ANISOU 3271  CD1 LEU C 436     3106   2839   3572     19   -600   -330       C  
ATOM   3272  CD2 LEU C 436       4.944  18.971 -44.782  1.00 29.87           C  
ANISOU 3272  CD2 LEU C 436     3743   3402   4203      8   -620   -263       C  
ATOM   3273  N   ARG C 437       5.748  20.678 -40.108  1.00 34.61           N  
ANISOU 3273  N   ARG C 437     4414   4064   4673    138   -618   -283       N  
ATOM   3274  CA  ARG C 437       4.740  20.788 -39.061  1.00 47.47           C  
ANISOU 3274  CA  ARG C 437     6069   5706   6263    159   -592   -227       C  
ATOM   3275  C   ARG C 437       3.720  21.890 -39.318  1.00 44.96           C  
ANISOU 3275  C   ARG C 437     5735   5394   5954    132   -545   -208       C  
ATOM   3276  O   ARG C 437       2.909  22.176 -38.431  1.00 42.47           O  
ANISOU 3276  O   ARG C 437     5434   5101   5602    155   -520   -173       O  
ATOM   3277  CB  ARG C 437       5.402  21.004 -37.691  1.00 53.55           C  
ANISOU 3277  CB  ARG C 437     6857   6510   6978    217   -614   -260       C  
ATOM   3278  CG  ARG C 437       5.739  19.699 -36.983  1.00 71.86           C  
ANISOU 3278  CG  ARG C 437     9207   8828   9266    256   -647   -227       C  
ATOM   3279  CD  ARG C 437       6.941  19.813 -36.045  1.00 83.74           C  
ANISOU 3279  CD  ARG C 437    10720  10368  10731    313   -688   -289       C  
ATOM   3280  NE  ARG C 437       8.067  20.483 -36.696  1.00 98.26           N  
ANISOU 3280  NE  ARG C 437    12524  12206  12604    299   -711   -380       N  
ATOM   3281  CZ  ARG C 437       9.322  20.434 -36.244  1.00100.50           C  
ANISOU 3281  CZ  ARG C 437    12802  12512  12872    337   -756   -445       C  
ATOM   3282  NH1 ARG C 437       9.617  19.721 -35.159  1.00101.90           N  
ANISOU 3282  NH1 ARG C 437    13010  12712  12997    396   -786   -430       N  
ATOM   3283  NH2 ARG C 437      10.274  21.086 -36.892  1.00104.00           N  
ANISOU 3283  NH2 ARG C 437    13205  12958  13352    316   -770   -521       N  
ATOM   3284  N   GLU C 438       3.745  22.529 -40.484  1.00 39.50           N  
ANISOU 3284  N   GLU C 438     5012   4688   5306     90   -533   -230       N  
ATOM   3285  CA  GLU C 438       2.697  23.484 -40.817  1.00 36.62           C  
ANISOU 3285  CA  GLU C 438     4634   4324   4956     66   -491   -203       C  
ATOM   3286  C   GLU C 438       2.575  23.605 -42.326  1.00 36.26           C  
ANISOU 3286  C   GLU C 438     4558   4261   4958     15   -482   -198       C  
ATOM   3287  O   GLU C 438       3.573  23.827 -43.018  1.00 40.02           O  
ANISOU 3287  O   GLU C 438     5012   4735   5457      0   -500   -246       O  
ATOM   3288  CB  GLU C 438       2.960  24.867 -40.210  1.00 32.00           C  
ANISOU 3288  CB  GLU C 438     4043   3751   4364     87   -484   -252       C  
ATOM   3289  CG  GLU C 438       2.076  25.945 -40.823  1.00 29.94           C  
ANISOU 3289  CG  GLU C 438     3762   3479   4134     60   -448   -234       C  
ATOM   3290  CD  GLU C 438       2.309  27.315 -40.227  1.00 40.23           C  
ANISOU 3290  CD  GLU C 438     5062   4781   5441     83   -448   -287       C  
ATOM   3291  OE1 GLU C 438       2.871  27.395 -39.116  1.00 45.37           O  
ANISOU 3291  OE1 GLU C 438     5730   5452   6058    127   -470   -332       O  
ATOM   3292  OE2 GLU C 438       1.925  28.313 -40.873  1.00 52.06           O  
ANISOU 3292  OE2 GLU C 438     6542   6259   6981     58   -429   -286       O  
ATOM   3293  N   LEU C 439       1.354  23.442 -42.824  1.00 30.48           N  
ANISOU 3293  N   LEU C 439     3821   3522   4237    -10   -454   -139       N  
ATOM   3294  CA  LEU C 439       0.959  23.946 -44.134  1.00 32.21           C  
ANISOU 3294  CA  LEU C 439     4010   3737   4492    -52   -436   -129       C  
ATOM   3295  C   LEU C 439       0.140  25.206 -43.867  1.00 37.46           C  
ANISOU 3295  C   LEU C 439     4668   4406   5159    -49   -401   -113       C  
ATOM   3296  O   LEU C 439      -1.029  25.127 -43.479  1.00 36.95           O  
ANISOU 3296  O   LEU C 439     4610   4349   5081    -42   -376    -63       O  
ATOM   3297  CB  LEU C 439       0.170  22.903 -44.917  1.00 26.80           C  
ANISOU 3297  CB  LEU C 439     3319   3043   3820    -80   -436    -83       C  
ATOM   3298  CG  LEU C 439       0.904  21.610 -45.294  1.00 42.15           C  
ANISOU 3298  CG  LEU C 439     5270   4975   5772    -81   -476   -104       C  
ATOM   3299  CD1 LEU C 439      -0.081  20.567 -45.795  1.00 38.63           C  
ANISOU 3299  CD1 LEU C 439     4823   4510   5343   -105   -480    -56       C  
ATOM   3300  CD2 LEU C 439       1.967  21.891 -46.342  1.00 46.35           C  
ANISOU 3300  CD2 LEU C 439     5774   5519   6319    -94   -492   -160       C  
ATOM   3301  N   GLY C 440       0.769  26.370 -44.055  1.00 33.35           N  
ANISOU 3301  N   GLY C 440     4133   3880   4659    -52   -401   -155       N  
ATOM   3302  CA  GLY C 440       0.136  27.621 -43.663  1.00 38.19           C  
ANISOU 3302  CA  GLY C 440     4744   4487   5279    -39   -376   -152       C  
ATOM   3303  C   GLY C 440      -1.220  27.833 -44.308  1.00 44.28           C  
ANISOU 3303  C   GLY C 440     5502   5260   6063    -57   -344    -92       C  
ATOM   3304  O   GLY C 440      -2.163  28.291 -43.658  1.00 48.68           O  
ANISOU 3304  O   GLY C 440     6066   5825   6606    -32   -321    -71       O  
ATOM   3305  N   SER C 441      -1.337  27.497 -45.589  1.00 44.61           N  
ANISOU 3305  N   SER C 441     5522   5302   6127    -97   -342    -67       N  
ATOM   3306  CA  SER C 441      -2.612  27.563 -46.290  1.00 34.95           C  
ANISOU 3306  CA  SER C 441     4281   4086   4913   -115   -317    -11       C  
ATOM   3307  C   SER C 441      -2.560  26.594 -47.462  1.00 28.75           C  
ANISOU 3307  C   SER C 441     3479   3310   4135   -150   -330      4       C  
ATOM   3308  O   SER C 441      -1.524  25.994 -47.752  1.00 32.33           O  
ANISOU 3308  O   SER C 441     3934   3764   4587   -157   -356    -31       O  
ATOM   3309  CB  SER C 441      -2.924  28.985 -46.764  1.00 36.53           C  
ANISOU 3309  CB  SER C 441     4463   4272   5143   -119   -298     -4       C  
ATOM   3310  OG  SER C 441      -2.216  29.291 -47.952  1.00 45.32           O  
ANISOU 3310  OG  SER C 441     5554   5384   6283   -153   -306    -11       O  
ATOM   3311  N   GLY C 442      -3.700  26.445 -48.131  1.00 29.24           N  
ANISOU 3311  N   GLY C 442     3524   3383   4204   -167   -314     52       N  
ATOM   3312  CA  GLY C 442      -3.805  25.567 -49.276  1.00 24.47           C  
ANISOU 3312  CA  GLY C 442     2901   2791   3606   -197   -330     61       C  
ATOM   3313  C   GLY C 442      -4.082  24.125 -48.890  1.00 29.64           C  
ANISOU 3313  C   GLY C 442     3571   3439   4254   -199   -350     71       C  
ATOM   3314  O   GLY C 442      -4.039  23.730 -47.724  1.00 36.01           O  
ANISOU 3314  O   GLY C 442     4403   4234   5046   -178   -351     75       O  
ATOM   3315  N   LEU C 443      -4.374  23.324 -49.909  1.00 28.38           N  
ANISOU 3315  N   LEU C 443     3393   3286   4105   -224   -368     76       N  
ATOM   3316  CA  LEU C 443      -4.663  21.909 -49.739  1.00 38.79           C  
ANISOU 3316  CA  LEU C 443     4721   4585   5431   -234   -394     85       C  
ATOM   3317  C   LEU C 443      -3.445  21.063 -50.093  1.00 43.27           C  
ANISOU 3317  C   LEU C 443     5299   5142   6001   -229   -435     30       C  
ATOM   3318  O   LEU C 443      -2.519  21.510 -50.775  1.00 44.09           O  
ANISOU 3318  O   LEU C 443     5389   5266   6098   -225   -441    -13       O  
ATOM   3319  CB  LEU C 443      -5.852  21.489 -50.607  1.00 42.37           C  
ANISOU 3319  CB  LEU C 443     5147   5049   5905   -263   -396    119       C  
ATOM   3320  CG  LEU C 443      -7.149  22.275 -50.425  1.00 40.29           C  
ANISOU 3320  CG  LEU C 443     4863   4803   5641   -267   -358    174       C  
ATOM   3321  CD1 LEU C 443      -8.175  21.824 -51.426  1.00 46.20           C  
ANISOU 3321  CD1 LEU C 443     5578   5567   6409   -297   -368    196       C  
ATOM   3322  CD2 LEU C 443      -7.678  22.066 -49.043  1.00 42.83           C  
ANISOU 3322  CD2 LEU C 443     5204   5114   5955   -254   -339    213       C  
ATOM   3323  N   ALA C 444      -3.458  19.824 -49.613  1.00 36.41           N  
ANISOU 3323  N   ALA C 444     4450   4240   5143   -227   -464     33       N  
ATOM   3324  CA  ALA C 444      -2.449  18.833 -49.954  1.00 30.50           C  
ANISOU 3324  CA  ALA C 444     3712   3475   4403   -217   -509    -20       C  
ATOM   3325  C   ALA C 444      -3.098  17.763 -50.818  1.00 31.32           C  
ANISOU 3325  C   ALA C 444     3802   3561   4538   -242   -541    -19       C  
ATOM   3326  O   ALA C 444      -4.133  17.205 -50.444  1.00 34.70           O  
ANISOU 3326  O   ALA C 444     4233   3962   4990   -262   -541     32       O  
ATOM   3327  CB  ALA C 444      -1.835  18.209 -48.699  1.00 23.90           C  
ANISOU 3327  CB  ALA C 444     2914   2606   3561   -190   -527    -20       C  
ATOM   3328  N   LEU C 445      -2.498  17.490 -51.972  1.00 30.12           N  
ANISOU 3328  N   LEU C 445     3629   3428   4385   -240   -569    -77       N  
ATOM   3329  CA  LEU C 445      -3.019  16.512 -52.918  1.00 34.54           C  
ANISOU 3329  CA  LEU C 445     4173   3977   4973   -258   -607    -96       C  
ATOM   3330  C   LEU C 445      -1.967  15.435 -53.129  1.00 42.65           C  
ANISOU 3330  C   LEU C 445     5214   4979   6012   -232   -661   -164       C  
ATOM   3331  O   LEU C 445      -0.875  15.720 -53.634  1.00 50.39           O  
ANISOU 3331  O   LEU C 445     6182   5999   6965   -208   -666   -221       O  
ATOM   3332  CB  LEU C 445      -3.395  17.180 -54.244  1.00 25.80           C  
ANISOU 3332  CB  LEU C 445     3023   2929   3848   -271   -594   -107       C  
ATOM   3333  CG  LEU C 445      -3.703  16.296 -55.454  1.00 32.57           C  
ANISOU 3333  CG  LEU C 445     3857   3797   4722   -280   -639   -151       C  
ATOM   3334  CD1 LEU C 445      -4.952  15.457 -55.223  1.00 35.68           C  
ANISOU 3334  CD1 LEU C 445     4253   4140   5164   -311   -661   -113       C  
ATOM   3335  CD2 LEU C 445      -3.862  17.152 -56.700  1.00 31.39           C  
ANISOU 3335  CD2 LEU C 445     3666   3725   4537   -283   -620   -160       C  
ATOM   3336  N   ILE C 446      -2.293  14.206 -52.739  1.00 41.92           N  
ANISOU 3336  N   ILE C 446     5143   4821   5963   -237   -702   -156       N  
ATOM   3337  CA  ILE C 446      -1.392  13.065 -52.850  1.00 35.76           C  
ANISOU 3337  CA  ILE C 446     4381   4002   5205   -209   -760   -219       C  
ATOM   3338  C   ILE C 446      -2.151  11.949 -53.562  1.00 32.35           C  
ANISOU 3338  C   ILE C 446     3940   3526   4826   -230   -811   -236       C  
ATOM   3339  O   ILE C 446      -3.136  11.410 -53.028  1.00 39.33           O  
ANISOU 3339  O   ILE C 446     4835   4354   5756   -263   -817   -175       O  
ATOM   3340  CB  ILE C 446      -0.866  12.611 -51.481  1.00 33.13           C  
ANISOU 3340  CB  ILE C 446     4092   3616   4880   -186   -769   -192       C  
ATOM   3341  CG1 ILE C 446      -0.108  13.769 -50.819  1.00 31.70           C  
ANISOU 3341  CG1 ILE C 446     3914   3483   4646   -164   -725   -187       C  
ATOM   3342  CG2 ILE C 446       0.048  11.423 -51.634  1.00 39.58           C  
ANISOU 3342  CG2 ILE C 446     4927   4389   5725   -152   -834   -257       C  
ATOM   3343  CD1 ILE C 446       0.331  13.513 -49.395  1.00 27.81           C  
ANISOU 3343  CD1 ILE C 446     3463   2955   4149   -139   -727   -156       C  
ATOM   3344  N   HIS C 447      -1.714  11.617 -54.775  1.00 21.97           N  
ANISOU 3344  N   HIS C 447     2601   2241   3506   -213   -847   -319       N  
ATOM   3345  CA  HIS C 447      -2.497  10.712 -55.597  1.00 23.93           C  
ANISOU 3345  CA  HIS C 447     2834   2459   3801   -233   -897   -347       C  
ATOM   3346  C   HIS C 447      -1.612  10.017 -56.619  1.00 31.35           C  
ANISOU 3346  C   HIS C 447     3761   3415   4736   -191   -954   -459       C  
ATOM   3347  O   HIS C 447      -0.682  10.619 -57.159  1.00 30.15           O  
ANISOU 3347  O   HIS C 447     3589   3342   4526   -158   -936   -508       O  
ATOM   3348  CB  HIS C 447      -3.652  11.455 -56.289  1.00 21.76           C  
ANISOU 3348  CB  HIS C 447     2519   2237   3511   -271   -864   -312       C  
ATOM   3349  CG  HIS C 447      -3.230  12.314 -57.440  1.00 27.09           C  
ANISOU 3349  CG  HIS C 447     3157   3014   4122   -252   -844   -359       C  
ATOM   3350  ND1 HIS C 447      -3.173  11.847 -58.736  1.00 28.53           N  
ANISOU 3350  ND1 HIS C 447     3308   3236   4296   -237   -887   -438       N  
ATOM   3351  CD2 HIS C 447      -2.851  13.613 -57.492  1.00 26.68           C  
ANISOU 3351  CD2 HIS C 447     3091   3034   4012   -245   -785   -334       C  
ATOM   3352  CE1 HIS C 447      -2.775  12.820 -59.536  1.00 27.59           C  
ANISOU 3352  CE1 HIS C 447     3157   3216   4109   -221   -852   -453       C  
ATOM   3353  NE2 HIS C 447      -2.573  13.903 -58.806  1.00 21.71           N  
ANISOU 3353  NE2 HIS C 447     2422   2487   3339   -229   -790   -388       N  
ATOM   3354  N   HIS C 448      -1.912   8.735 -56.853  1.00 31.81           N  
ANISOU 3354  N   HIS C 448     3828   3397   4860   -193  -1024   -498       N  
ATOM   3355  CA  HIS C 448      -1.274   7.918 -57.889  1.00 31.69           C  
ANISOU 3355  CA  HIS C 448     3800   3391   4851   -151  -1090   -615       C  
ATOM   3356  C   HIS C 448       0.211   7.693 -57.614  1.00 32.13           C  
ANISOU 3356  C   HIS C 448     3873   3452   4883    -90  -1106   -673       C  
ATOM   3357  O   HIS C 448       1.047   7.772 -58.515  1.00 36.09           O  
ANISOU 3357  O   HIS C 448     4347   4029   5337    -45  -1118   -761       O  
ATOM   3358  CB  HIS C 448      -1.490   8.512 -59.281  1.00 36.63           C  
ANISOU 3358  CB  HIS C 448     4373   4125   5419   -147  -1079   -666       C  
ATOM   3359  CG  HIS C 448      -2.860   8.266 -59.835  1.00 41.10           C  
ANISOU 3359  CG  HIS C 448     4917   4676   6024   -192  -1100   -650       C  
ATOM   3360  ND1 HIS C 448      -3.848   9.226 -59.837  1.00 39.81           N  
ANISOU 3360  ND1 HIS C 448     4731   4556   5838   -236  -1044   -570       N  
ATOM   3361  CD2 HIS C 448      -3.407   7.163 -60.401  1.00 40.13           C  
ANISOU 3361  CD2 HIS C 448     4787   4496   5963   -199  -1175   -709       C  
ATOM   3362  CE1 HIS C 448      -4.943   8.728 -60.383  1.00 40.17           C  
ANISOU 3362  CE1 HIS C 448     4756   4581   5928   -269  -1081   -578       C  
ATOM   3363  NE2 HIS C 448      -4.703   7.478 -60.733  1.00 42.34           N  
ANISOU 3363  NE2 HIS C 448     5038   4792   6256   -250  -1162   -662       N  
ATOM   3364  N   ASN C 449       0.539   7.386 -56.363  1.00 19.41           N  
ANISOU 3364  N   ASN C 449     2306   1767   3302    -86  -1106   -623       N  
ATOM   3365  CA  ASN C 449       1.879   6.956 -55.967  1.00 19.59           C  
ANISOU 3365  CA  ASN C 449     2350   1776   3317    -26  -1134   -676       C  
ATOM   3366  C   ASN C 449       1.746   5.501 -55.514  1.00 33.57           C  
ANISOU 3366  C   ASN C 449     4160   3417   5178    -17  -1210   -685       C  
ATOM   3367  O   ASN C 449       1.441   5.224 -54.353  1.00 44.17           O  
ANISOU 3367  O   ASN C 449     5542   4681   6559    -38  -1206   -599       O  
ATOM   3368  CB  ASN C 449       2.448   7.854 -54.871  1.00 26.49           C  
ANISOU 3368  CB  ASN C 449     3240   2677   4147    -22  -1074   -612       C  
ATOM   3369  CG  ASN C 449       2.301   9.340 -55.194  1.00 36.28           C  
ANISOU 3369  CG  ASN C 449     4445   4021   5318    -46   -998   -581       C  
ATOM   3370  OD1 ASN C 449       1.343   9.990 -54.774  1.00 36.96           O  
ANISOU 3370  OD1 ASN C 449     4534   4105   5404    -92   -952   -497       O  
ATOM   3371  ND2 ASN C 449       3.251   9.879 -55.946  1.00 34.54           N  
ANISOU 3371  ND2 ASN C 449     4190   3892   5042    -14   -985   -646       N  
ATOM   3372  N   THR C 450       1.997   4.572 -56.444  1.00 29.41           N  
ANISOU 3372  N   THR C 450     3623   2868   4683     17  -1283   -790       N  
ATOM   3373  CA  THR C 450       1.561   3.186 -56.268  1.00 36.04           C  
ANISOU 3373  CA  THR C 450     4494   3573   5628     11  -1364   -800       C  
ATOM   3374  C   THR C 450       2.166   2.548 -55.023  1.00 42.83           C  
ANISOU 3374  C   THR C 450     5406   4338   6528     37  -1387   -756       C  
ATOM   3375  O   THR C 450       1.502   1.759 -54.339  1.00 42.18           O  
ANISOU 3375  O   THR C 450     5358   4140   6530      3  -1419   -687       O  
ATOM   3376  CB  THR C 450       1.919   2.353 -57.504  1.00 35.45           C  
ANISOU 3376  CB  THR C 450     4397   3501   5570     61  -1438   -938       C  
ATOM   3377  OG1 THR C 450       3.346   2.272 -57.634  1.00 58.11           O  
ANISOU 3377  OG1 THR C 450     7265   6422   8392    143  -1448  -1018       O  
ATOM   3378  CG2 THR C 450       1.353   2.977 -58.755  1.00 25.47           C  
ANISOU 3378  CG2 THR C 450     3079   2346   4250     45  -1409   -976       C  
ATOM   3379  N   HIS C 451       3.422   2.866 -54.717  1.00 35.73           N  
ANISOU 3379  N   HIS C 451     4512   3492   5573     96  -1373   -790       N  
ATOM   3380  CA  HIS C 451       4.126   2.227 -53.612  1.00 30.64           C  
ANISOU 3380  CA  HIS C 451     3914   2768   4959    134  -1404   -761       C  
ATOM   3381  C   HIS C 451       4.105   3.046 -52.331  1.00 28.94           C  
ANISOU 3381  C   HIS C 451     3719   2575   4701    111  -1334   -646       C  
ATOM   3382  O   HIS C 451       4.692   2.620 -51.332  1.00 36.13           O  
ANISOU 3382  O   HIS C 451     4668   3433   5625    144  -1354   -612       O  
ATOM   3383  CB  HIS C 451       5.579   1.937 -54.016  1.00 31.47           C  
ANISOU 3383  CB  HIS C 451     4009   2913   5035    222  -1443   -879       C  
ATOM   3384  CG  HIS C 451       5.703   1.017 -55.193  1.00 40.22           C  
ANISOU 3384  CG  HIS C 451     5101   3998   6185    261  -1521  -1004       C  
ATOM   3385  ND1 HIS C 451       6.077   1.459 -56.450  1.00 36.57           N  
ANISOU 3385  ND1 HIS C 451     4582   3661   5654    291  -1502  -1098       N  
ATOM   3386  CD2 HIS C 451       5.492  -0.317 -55.310  1.00 39.01           C  
ANISOU 3386  CD2 HIS C 451     4968   3741   6114    282  -1590  -1022       C  
ATOM   3387  CE1 HIS C 451       6.096   0.438 -57.289  1.00 39.27           C  
ANISOU 3387  CE1 HIS C 451     4911   3982   6027    335  -1552  -1170       C  
ATOM   3388  NE2 HIS C 451       5.746  -0.651 -56.622  1.00 47.57           N  
ANISOU 3388  NE2 HIS C 451     6007   4893   7173    330  -1608  -1128       N  
ATOM   3389  N   LEU C 452       3.434   4.192 -52.328  1.00 30.19           N  
ANISOU 3389  N   LEU C 452     3854   2809   4809     60  -1258   -587       N  
ATOM   3390  CA  LEU C 452       3.464   5.098 -51.187  1.00 33.37           C  
ANISOU 3390  CA  LEU C 452     4270   3246   5161     46  -1191   -495       C  
ATOM   3391  C   LEU C 452       2.587   4.572 -50.055  1.00 31.57           C  
ANISOU 3391  C   LEU C 452     4083   2927   4985      8  -1191   -377       C  
ATOM   3392  O   LEU C 452       1.362   4.487 -50.194  1.00 36.52           O  
ANISOU 3392  O   LEU C 452     4702   3524   5650    -52  -1180   -319       O  
ATOM   3393  CB  LEU C 452       3.010   6.492 -51.607  1.00 27.97           C  
ANISOU 3393  CB  LEU C 452     3548   2668   4413      9  -1114   -476       C  
ATOM   3394  CG  LEU C 452       2.963   7.539 -50.497  1.00 27.74           C  
ANISOU 3394  CG  LEU C 452     3529   2678   4332     -5  -1045   -393       C  
ATOM   3395  CD1 LEU C 452       4.346   7.746 -49.905  1.00 29.85           C  
ANISOU 3395  CD1 LEU C 452     3807   2977   4558     53  -1049   -430       C  
ATOM   3396  CD2 LEU C 452       2.419   8.841 -51.038  1.00 26.38           C  
ANISOU 3396  CD2 LEU C 452     3319   2594   4112    -42   -979   -378       C  
ATOM   3397  N   CYS C 453       3.214   4.209 -48.940  1.00 29.71           N  
ANISOU 3397  N   CYS C 453     3887   2653   4749     44  -1205   -337       N  
ATOM   3398  CA  CYS C 453       2.532   3.974 -47.679  1.00 36.94           C  
ANISOU 3398  CA  CYS C 453     4837   3513   5684     16  -1187   -210       C  
ATOM   3399  C   CYS C 453       2.793   5.170 -46.770  1.00 34.30           C  
ANISOU 3399  C   CYS C 453     4502   3268   5261     25  -1116   -163       C  
ATOM   3400  O   CYS C 453       3.354   6.187 -47.197  1.00 35.08           O  
ANISOU 3400  O   CYS C 453     4572   3458   5297     40  -1080   -224       O  
ATOM   3401  CB  CYS C 453       3.000   2.661 -47.046  1.00 47.16           C  
ANISOU 3401  CB  CYS C 453     6178   4700   7042     53  -1259   -191       C  
ATOM   3402  SG  CYS C 453       2.347   1.153 -47.813  1.00 63.53           S  
ANISOU 3402  SG  CYS C 453     8260   6633   9246     25  -1347   -212       S  
ATOM   3403  N   PHE C 454       2.381   5.046 -45.509  1.00 34.72           N  
ANISOU 3403  N   PHE C 454     4586   3295   5310     16  -1095    -53       N  
ATOM   3404  CA  PHE C 454       2.640   6.058 -44.483  1.00 33.19           C  
ANISOU 3404  CA  PHE C 454     4398   3179   5033     34  -1037    -10       C  
ATOM   3405  C   PHE C 454       2.006   7.403 -44.836  1.00 39.49           C  
ANISOU 3405  C   PHE C 454     5158   4064   5782     -5   -965     -9       C  
ATOM   3406  O   PHE C 454       2.593   8.465 -44.614  1.00 49.96           O  
ANISOU 3406  O   PHE C 454     6473   5469   7042     19   -928    -40       O  
ATOM   3407  CB  PHE C 454       4.141   6.219 -44.226  1.00 38.04           C  
ANISOU 3407  CB  PHE C 454     5021   3829   5602    106  -1060    -86       C  
ATOM   3408  CG  PHE C 454       4.801   4.982 -43.686  1.00 38.30           C  
ANISOU 3408  CG  PHE C 454     5095   3783   5675    154  -1129    -78       C  
ATOM   3409  CD1 PHE C 454       5.486   4.125 -44.529  1.00 38.13           C  
ANISOU 3409  CD1 PHE C 454     5072   3710   5704    188  -1198   -168       C  
ATOM   3410  CD2 PHE C 454       4.737   4.679 -42.336  1.00 37.66           C  
ANISOU 3410  CD2 PHE C 454     5052   3680   5577    172  -1127     20       C  
ATOM   3411  CE1 PHE C 454       6.095   2.989 -44.036  1.00 41.26           C  
ANISOU 3411  CE1 PHE C 454     5508   4027   6143    237  -1266   -162       C  
ATOM   3412  CE2 PHE C 454       5.342   3.544 -41.837  1.00 35.65           C  
ANISOU 3412  CE2 PHE C 454     4836   3349   5360    220  -1192     35       C  
ATOM   3413  CZ  PHE C 454       6.023   2.697 -42.688  1.00 39.81           C  
ANISOU 3413  CZ  PHE C 454     5364   3815   5946    252  -1263    -56       C  
ATOM   3414  N   VAL C 455       0.804   7.360 -45.397  1.00 39.77           N  
ANISOU 3414  N   VAL C 455     5173   4083   5856    -64   -948     27       N  
ATOM   3415  CA  VAL C 455      -0.024   8.549 -45.580  1.00 35.24           C  
ANISOU 3415  CA  VAL C 455     4566   3580   5242   -102   -880     53       C  
ATOM   3416  C   VAL C 455      -1.049   8.672 -44.465  1.00 40.50           C  
ANISOU 3416  C   VAL C 455     5243   4248   5898   -129   -835    173       C  
ATOM   3417  O   VAL C 455      -1.240   9.746 -43.895  1.00 46.04           O  
ANISOU 3417  O   VAL C 455     5937   5020   6538   -124   -778    199       O  
ATOM   3418  CB  VAL C 455      -0.708   8.522 -46.965  1.00 30.79           C  
ANISOU 3418  CB  VAL C 455     3966   3015   4719   -145   -888     11       C  
ATOM   3419  CG1 VAL C 455      -1.623   9.732 -47.132  1.00 28.80           C  
ANISOU 3419  CG1 VAL C 455     3680   2833   4430   -181   -820     46       C  
ATOM   3420  CG2 VAL C 455       0.332   8.473 -48.069  1.00 25.94           C  
ANISOU 3420  CG2 VAL C 455     3336   2420   4100   -111   -926   -108       C  
ATOM   3421  N   HIS C 456      -1.715   7.559 -44.149  1.00 47.70           N  
ANISOU 3421  N   HIS C 456     6170   5082   6872   -158   -863    246       N  
ATOM   3422  CA  HIS C 456      -2.619   7.494 -43.008  1.00 54.60           C  
ANISOU 3422  CA  HIS C 456     7052   5959   7736   -181   -824    372       C  
ATOM   3423  C   HIS C 456      -1.904   7.830 -41.705  1.00 52.42           C  
ANISOU 3423  C   HIS C 456     6806   5724   7385   -125   -803    403       C  
ATOM   3424  O   HIS C 456      -2.521   8.365 -40.775  1.00 46.47           O  
ANISOU 3424  O   HIS C 456     6050   5025   6581   -129   -748    482       O  
ATOM   3425  CB  HIS C 456      -3.226   6.090 -42.947  1.00 66.43           C  
ANISOU 3425  CB  HIS C 456     8562   7352   9326   -220   -870    442       C  
ATOM   3426  CG  HIS C 456      -4.493   5.997 -42.157  1.00 82.46           C  
ANISOU 3426  CG  HIS C 456    10579   9387  11364   -269   -825    576       C  
ATOM   3427  ND1 HIS C 456      -4.573   5.324 -40.957  1.00 88.94           N  
ANISOU 3427  ND1 HIS C 456    11429  10178  12186   -262   -825    686       N  
ATOM   3428  CD2 HIS C 456      -5.737   6.467 -42.409  1.00 87.71           C  
ANISOU 3428  CD2 HIS C 456    11201  10089  12035   -324   -778    621       C  
ATOM   3429  CE1 HIS C 456      -5.809   5.394 -40.497  1.00 92.02           C  
ANISOU 3429  CE1 HIS C 456    11792  10591  12580   -313   -776    795       C  
ATOM   3430  NE2 HIS C 456      -6.535   6.083 -41.359  1.00 92.21           N  
ANISOU 3430  NE2 HIS C 456    11772  10655  12610   -350   -747    755       N  
ATOM   3431  N   THR C 457      -0.604   7.537 -41.624  1.00 55.30           N  
ANISOU 3431  N   THR C 457     7199   6074   7739    -69   -848    337       N  
ATOM   3432  CA  THR C 457       0.159   7.701 -40.393  1.00 51.48           C  
ANISOU 3432  CA  THR C 457     6746   5626   7190    -11   -843    361       C  
ATOM   3433  C   THR C 457       0.518   9.149 -40.092  1.00 46.54           C  
ANISOU 3433  C   THR C 457     6104   5102   6476     16   -792    315       C  
ATOM   3434  O   THR C 457       0.997   9.431 -38.989  1.00 47.55           O  
ANISOU 3434  O   THR C 457     6252   5273   6540     63   -781    336       O  
ATOM   3435  CB  THR C 457       1.443   6.870 -40.455  1.00 50.48           C  
ANISOU 3435  CB  THR C 457     6649   5447   7086     42   -914    300       C  
ATOM   3436  OG1 THR C 457       2.219   7.273 -41.589  1.00 53.53           O  
ANISOU 3436  OG1 THR C 457     7011   5852   7476     55   -934    174       O  
ATOM   3437  CG2 THR C 457       1.117   5.391 -40.584  1.00 45.15           C  
ANISOU 3437  CG2 THR C 457     5996   4658   6502     21   -972    352       C  
ATOM   3438  N   VAL C 458       0.313  10.065 -41.033  1.00 42.85           N  
ANISOU 3438  N   VAL C 458     5601   4673   6006     -9   -764    253       N  
ATOM   3439  CA  VAL C 458       0.629  11.475 -40.818  1.00 39.61           C  
ANISOU 3439  CA  VAL C 458     5175   4348   5528     12   -720    208       C  
ATOM   3440  C   VAL C 458      -0.579  12.163 -40.191  1.00 44.50           C  
ANISOU 3440  C   VAL C 458     5782   5013   6113    -11   -656    287       C  
ATOM   3441  O   VAL C 458      -1.711  11.975 -40.660  1.00 52.95           O  
ANISOU 3441  O   VAL C 458     6831   6064   7222    -62   -637    336       O  
ATOM   3442  CB  VAL C 458       1.040  12.166 -42.129  1.00 33.84           C  
ANISOU 3442  CB  VAL C 458     4411   3637   4811     -2   -721    111       C  
ATOM   3443  CG1 VAL C 458       1.330  13.642 -41.887  1.00 31.00           C  
ANISOU 3443  CG1 VAL C 458     4035   3351   4393     13   -677     73       C  
ATOM   3444  CG2 VAL C 458       2.252  11.476 -42.735  1.00 28.38           C  
ANISOU 3444  CG2 VAL C 458     3726   2913   4146     27   -781     30       C  
ATOM   3445  N   PRO C 459      -0.395  12.943 -39.138  1.00 47.75           N  
ANISOU 3445  N   PRO C 459     6201   5487   6453     28   -625    296       N  
ATOM   3446  CA  PRO C 459      -1.512  13.708 -38.542  1.00 45.32           C  
ANISOU 3446  CA  PRO C 459     5878   5236   6106     17   -563    358       C  
ATOM   3447  C   PRO C 459      -1.750  15.030 -39.270  1.00 42.12           C  
ANISOU 3447  C   PRO C 459     5440   4870   5695      1   -528    298       C  
ATOM   3448  O   PRO C 459      -1.360  16.116 -38.840  1.00 37.98           O  
ANISOU 3448  O   PRO C 459     4913   4397   5121     35   -508    253       O  
ATOM   3449  CB  PRO C 459      -1.038  13.918 -37.103  1.00 47.87           C  
ANISOU 3449  CB  PRO C 459     6227   5611   6352     78   -555    378       C  
ATOM   3450  CG  PRO C 459       0.453  14.017 -37.234  1.00 45.83           C  
ANISOU 3450  CG  PRO C 459     5984   5346   6085    119   -602    281       C  
ATOM   3451  CD  PRO C 459       0.842  13.068 -38.345  1.00 48.49           C  
ANISOU 3451  CD  PRO C 459     6320   5606   6498     91   -650    252       C  
ATOM   3452  N   TRP C 460      -2.433  14.934 -40.414  1.00 42.53           N  
ANISOU 3452  N   TRP C 460     5465   4894   5801    -50   -525    299       N  
ATOM   3453  CA  TRP C 460      -2.558  16.081 -41.310  1.00 34.01           C  
ANISOU 3453  CA  TRP C 460     4355   3843   4726    -66   -501    243       C  
ATOM   3454  C   TRP C 460      -3.289  17.248 -40.663  1.00 41.52           C  
ANISOU 3454  C   TRP C 460     5292   4854   5630    -53   -445    267       C  
ATOM   3455  O   TRP C 460      -3.060  18.403 -41.040  1.00 44.32           O  
ANISOU 3455  O   TRP C 460     5632   5234   5974    -46   -429    212       O  
ATOM   3456  CB  TRP C 460      -3.260  15.660 -42.599  1.00 26.01           C  
ANISOU 3456  CB  TRP C 460     3314   2795   3772   -120   -509    248       C  
ATOM   3457  CG  TRP C 460      -2.474  14.658 -43.360  1.00 34.65           C  
ANISOU 3457  CG  TRP C 460     4419   3837   4911   -125   -567    202       C  
ATOM   3458  CD1 TRP C 460      -2.656  13.307 -43.373  1.00 35.76           C  
ANISOU 3458  CD1 TRP C 460     4573   3916   5098   -142   -606    237       C  
ATOM   3459  CD2 TRP C 460      -1.349  14.923 -44.202  1.00 40.39           C  
ANISOU 3459  CD2 TRP C 460     5139   4567   5640   -110   -594    109       C  
ATOM   3460  NE1 TRP C 460      -1.719  12.714 -44.186  1.00 40.65           N  
ANISOU 3460  NE1 TRP C 460     5198   4500   5748   -132   -659    163       N  
ATOM   3461  CE2 TRP C 460      -0.904  13.686 -44.707  1.00 43.91           C  
ANISOU 3461  CE2 TRP C 460     5595   4958   6129   -112   -650     85       C  
ATOM   3462  CE3 TRP C 460      -0.677  16.089 -44.584  1.00 42.97           C  
ANISOU 3462  CE3 TRP C 460     5449   4939   5939    -97   -577     46       C  
ATOM   3463  CZ2 TRP C 460       0.182  13.581 -45.574  1.00 45.05           C  
ANISOU 3463  CZ2 TRP C 460     5732   5103   6282    -94   -685     -3       C  
ATOM   3464  CZ3 TRP C 460       0.399  15.983 -45.444  1.00 43.82           C  
ANISOU 3464  CZ3 TRP C 460     5546   5046   6057    -87   -610    -31       C  
ATOM   3465  CH2 TRP C 460       0.819  14.737 -45.930  1.00 40.27           C  
ANISOU 3465  CH2 TRP C 460     5105   4553   5642    -83   -662    -57       C  
ATOM   3466  N   ASP C 461      -4.163  16.980 -39.692  1.00 45.50           N  
ANISOU 3466  N   ASP C 461     5799   5381   6107    -48   -416    349       N  
ATOM   3467  CA  ASP C 461      -4.909  18.068 -39.070  1.00 54.67           C  
ANISOU 3467  CA  ASP C 461     6944   6606   7221    -27   -363    367       C  
ATOM   3468  C   ASP C 461      -4.003  18.992 -38.262  1.00 53.02           C  
ANISOU 3468  C   ASP C 461     6754   6437   6954     32   -363    303       C  
ATOM   3469  O   ASP C 461      -4.280  20.193 -38.166  1.00 54.94           O  
ANISOU 3469  O   ASP C 461     6982   6717   7176     50   -333    271       O  
ATOM   3470  CB  ASP C 461      -6.034  17.507 -38.197  1.00 66.43           C  
ANISOU 3470  CB  ASP C 461     8427   8125   8690    -33   -330    474       C  
ATOM   3471  CG  ASP C 461      -5.607  16.290 -37.400  1.00 88.31           C  
ANISOU 3471  CG  ASP C 461    11230  10873  11451    -21   -357    528       C  
ATOM   3472  OD1 ASP C 461      -4.993  15.376 -37.990  1.00 94.43           O  
ANISOU 3472  OD1 ASP C 461    12021  11580  12277    -42   -406    512       O  
ATOM   3473  OD2 ASP C 461      -5.890  16.245 -36.185  1.00 94.61           O  
ANISOU 3473  OD2 ASP C 461    12036  11724  12188     14   -331    587       O  
ATOM   3474  N   GLN C 462      -2.917  18.467 -37.692  1.00 52.60           N  
ANISOU 3474  N   GLN C 462     6731   6373   6879     65   -400    279       N  
ATOM   3475  CA  GLN C 462      -1.994  19.317 -36.947  1.00 50.65           C  
ANISOU 3475  CA  GLN C 462     6499   6165   6582    121   -408    209       C  
ATOM   3476  C   GLN C 462      -1.088  20.135 -37.856  1.00 44.33           C  
ANISOU 3476  C   GLN C 462     5687   5343   5815    112   -429    112       C  
ATOM   3477  O   GLN C 462      -0.488  21.112 -37.394  1.00 45.95           O  
ANISOU 3477  O   GLN C 462     5892   5575   5991    147   -431     49       O  
ATOM   3478  CB  GLN C 462      -1.143  18.478 -35.993  1.00 56.56           C  
ANISOU 3478  CB  GLN C 462     7281   6917   7292    164   -443    219       C  
ATOM   3479  CG  GLN C 462      -1.934  17.456 -35.193  1.00 74.26           C  
ANISOU 3479  CG  GLN C 462     9535   9171   9510    165   -428    331       C  
ATOM   3480  CD  GLN C 462      -3.224  18.022 -34.621  1.00 88.26           C  
ANISOU 3480  CD  GLN C 462    11287  11005  11242    169   -368    390       C  
ATOM   3481  OE1 GLN C 462      -3.236  19.097 -34.020  1.00 93.55           O  
ANISOU 3481  OE1 GLN C 462    11951  11734  11858    213   -346    347       O  
ATOM   3482  NE2 GLN C 462      -4.318  17.293 -34.802  1.00 88.29           N  
ANISOU 3482  NE2 GLN C 462    11275  10995  11275    125   -345    487       N  
ATOM   3483  N   LEU C 463      -0.975  19.761 -39.131  1.00 39.51           N  
ANISOU 3483  N   LEU C 463     5062   4688   5264     65   -445    100       N  
ATOM   3484  CA  LEU C 463      -0.221  20.568 -40.083  1.00 38.30           C  
ANISOU 3484  CA  LEU C 463     4889   4523   5140     51   -456     22       C  
ATOM   3485  C   LEU C 463      -1.033  21.756 -40.588  1.00 39.96           C  
ANISOU 3485  C   LEU C 463     5072   4746   5363     31   -417     23       C  
ATOM   3486  O   LEU C 463      -0.460  22.807 -40.896  1.00 31.10           O  
ANISOU 3486  O   LEU C 463     3938   3627   4251     33   -417    -36       O  
ATOM   3487  CB  LEU C 463       0.233  19.705 -41.265  1.00 36.37           C  
ANISOU 3487  CB  LEU C 463     4637   4238   4944     17   -489      7       C  
ATOM   3488  CG  LEU C 463       1.525  18.882 -41.180  1.00 41.12           C  
ANISOU 3488  CG  LEU C 463     5255   4822   5547     40   -539    -37       C  
ATOM   3489  CD1 LEU C 463       1.629  18.090 -39.885  1.00 39.82           C  
ANISOU 3489  CD1 LEU C 463     5125   4659   5345     81   -555      2       C  
ATOM   3490  CD2 LEU C 463       1.629  17.949 -42.380  1.00 38.78           C  
ANISOU 3490  CD2 LEU C 463     4948   4487   5299      9   -567    -45       C  
ATOM   3491  N   PHE C 464      -2.354  21.612 -40.672  1.00 37.87           N  
ANISOU 3491  N   PHE C 464     4796   4489   5103     10   -384     90       N  
ATOM   3492  CA  PHE C 464      -3.216  22.638 -41.238  1.00 36.49           C  
ANISOU 3492  CA  PHE C 464     4594   4325   4944     -7   -349     96       C  
ATOM   3493  C   PHE C 464      -3.470  23.757 -40.234  1.00 42.62           C  
ANISOU 3493  C   PHE C 464     5373   5138   5681     38   -323     81       C  
ATOM   3494  O   PHE C 464      -3.346  23.581 -39.019  1.00 46.23           O  
ANISOU 3494  O   PHE C 464     5852   5626   6089     81   -322     86       O  
ATOM   3495  CB  PHE C 464      -4.548  22.036 -41.680  1.00 39.30           C  
ANISOU 3495  CB  PHE C 464     4932   4681   5321    -43   -328    171       C  
ATOM   3496  CG  PHE C 464      -4.419  21.015 -42.770  1.00 35.50           C  
ANISOU 3496  CG  PHE C 464     4442   4161   4884    -87   -358    177       C  
ATOM   3497  CD1 PHE C 464      -5.151  19.837 -42.726  1.00 28.53           C  
ANISOU 3497  CD1 PHE C 464     3560   3262   4019   -112   -363    240       C  
ATOM   3498  CD2 PHE C 464      -3.573  21.235 -43.842  1.00 32.43           C  
ANISOU 3498  CD2 PHE C 464     4045   3755   4522   -102   -382    118       C  
ATOM   3499  CE1 PHE C 464      -5.034  18.892 -43.732  1.00 25.90           C  
ANISOU 3499  CE1 PHE C 464     3220   2888   3732   -149   -398    234       C  
ATOM   3500  CE2 PHE C 464      -3.452  20.297 -44.853  1.00 36.62           C  
ANISOU 3500  CE2 PHE C 464     4567   4258   5088   -134   -412    113       C  
ATOM   3501  CZ  PHE C 464      -4.184  19.124 -44.797  1.00 27.70           C  
ANISOU 3501  CZ  PHE C 464     3440   3106   3978   -156   -423    166       C  
ATOM   3502  N   ARG C 465      -3.856  24.920 -40.764  1.00 38.27           N  
ANISOU 3502  N   ARG C 465     4802   4587   5152     32   -303     61       N  
ATOM   3503  CA  ARG C 465      -4.089  26.106 -39.953  1.00 37.29           C  
ANISOU 3503  CA  ARG C 465     4680   4488   5003     77   -283     32       C  
ATOM   3504  C   ARG C 465      -5.485  26.700 -40.079  1.00 45.41           C  
ANISOU 3504  C   ARG C 465     5684   5537   6034     79   -242     74       C  
ATOM   3505  O   ARG C 465      -5.875  27.484 -39.207  1.00 50.49           O  
ANISOU 3505  O   ARG C 465     6328   6211   6644    127   -223     58       O  
ATOM   3506  CB  ARG C 465      -3.064  27.200 -40.295  1.00 42.81           C  
ANISOU 3506  CB  ARG C 465     5377   5159   5732     79   -305    -47       C  
ATOM   3507  CG  ARG C 465      -1.645  26.873 -39.861  1.00 44.00           C  
ANISOU 3507  CG  ARG C 465     5546   5302   5869     93   -345   -103       C  
ATOM   3508  CD  ARG C 465      -1.547  26.761 -38.347  1.00 44.08           C  
ANISOU 3508  CD  ARG C 465     5581   5353   5816    153   -349   -117       C  
ATOM   3509  NE  ARG C 465      -1.046  25.455 -37.929  1.00 57.24           N  
ANISOU 3509  NE  ARG C 465     7267   7029   7452    159   -371    -95       N  
ATOM   3510  CZ  ARG C 465       0.216  25.208 -37.595  1.00 56.74           C  
ANISOU 3510  CZ  ARG C 465     7217   6961   7379    177   -411   -148       C  
ATOM   3511  NH1 ARG C 465       1.117  26.181 -37.619  1.00 59.91           N  
ANISOU 3511  NH1 ARG C 465     7611   7352   7800    185   -432   -228       N  
ATOM   3512  NH2 ARG C 465       0.577  23.986 -37.229  1.00 47.26           N  
ANISOU 3512  NH2 ARG C 465     6036   5767   6154    186   -431   -119       N  
ATOM   3513  N   ASN C 466      -6.241  26.368 -41.119  1.00 50.32           N  
ANISOU 3513  N   ASN C 466     6282   6147   6691     33   -230    123       N  
ATOM   3514  CA  ASN C 466      -7.599  26.859 -41.273  1.00 54.07           C  
ANISOU 3514  CA  ASN C 466     6729   6647   7169     35   -193    166       C  
ATOM   3515  C   ASN C 466      -8.497  25.702 -41.740  1.00 57.31           C  
ANISOU 3515  C   ASN C 466     7119   7066   7592     -8   -184    241       C  
ATOM   3516  O   ASN C 466      -8.006  24.746 -42.328  1.00 53.76           O  
ANISOU 3516  O   ASN C 466     6676   6586   7164    -46   -212    246       O  
ATOM   3517  CB  ASN C 466      -7.678  28.036 -42.257  1.00 48.01           C  
ANISOU 3517  CB  ASN C 466     5943   5852   6446     25   -191    139       C  
ATOM   3518  CG  ASN C 466      -7.368  27.638 -43.686  1.00 46.19           C  
ANISOU 3518  CG  ASN C 466     5699   5591   6259    -31   -211    148       C  
ATOM   3519  OD1 ASN C 466      -8.178  26.997 -44.352  1.00 48.93           O  
ANISOU 3519  OD1 ASN C 466     6024   5947   6619    -64   -203    197       O  
ATOM   3520  ND2 ASN C 466      -6.201  28.043 -44.173  1.00 41.01           N  
ANISOU 3520  ND2 ASN C 466     5052   4904   5625    -42   -236     98       N  
ATOM   3521  N   PRO C 467      -9.799  25.795 -41.460  1.00 62.83           N  
ANISOU 3521  N   PRO C 467     7791   7804   8277      0   -148    294       N  
ATOM   3522  CA  PRO C 467     -10.693  24.664 -41.789  1.00 59.37           C  
ANISOU 3522  CA  PRO C 467     7329   7375   7856    -45   -140    368       C  
ATOM   3523  C   PRO C 467     -11.008  24.502 -43.267  1.00 51.57           C  
ANISOU 3523  C   PRO C 467     6315   6358   6922    -98   -156    375       C  
ATOM   3524  O   PRO C 467     -11.647  23.505 -43.632  1.00 55.17           O  
ANISOU 3524  O   PRO C 467     6751   6811   7400   -140   -160    425       O  
ATOM   3525  CB  PRO C 467     -11.965  24.994 -40.994  1.00 61.35           C  
ANISOU 3525  CB  PRO C 467     7551   7688   8073    -16    -93    418       C  
ATOM   3526  CG  PRO C 467     -11.943  26.476 -40.857  1.00 63.92           C  
ANISOU 3526  CG  PRO C 467     7876   8025   8387     35    -80    362       C  
ATOM   3527  CD  PRO C 467     -10.497  26.840 -40.700  1.00 64.62           C  
ANISOU 3527  CD  PRO C 467     8006   8075   8473     53   -113    288       C  
ATOM   3528  N   HIS C 468     -10.600  25.431 -44.128  1.00 46.09           N  
ANISOU 3528  N   HIS C 468     5619   5644   6251    -97   -165    329       N  
ATOM   3529  CA  HIS C 468     -10.742  25.243 -45.567  1.00 51.71           C  
ANISOU 3529  CA  HIS C 468     6308   6336   7002   -141   -184    332       C  
ATOM   3530  C   HIS C 468      -9.691  24.297 -46.140  1.00 59.24           C  
ANISOU 3530  C   HIS C 468     7282   7255   7973   -172   -225    303       C  
ATOM   3531  O   HIS C 468      -9.589  24.175 -47.366  1.00 63.60           O  
ANISOU 3531  O   HIS C 468     7817   7797   8551   -202   -245    291       O  
ATOM   3532  CB  HIS C 468     -10.670  26.592 -46.291  1.00 67.20           C  
ANISOU 3532  CB  HIS C 468     8259   8293   8980   -128   -178    304       C  
ATOM   3533  CG  HIS C 468     -11.849  27.483 -46.044  1.00 84.10           C  
ANISOU 3533  CG  HIS C 468    10373  10465  11115   -100   -143    332       C  
ATOM   3534  ND1 HIS C 468     -12.699  27.889 -47.051  1.00 92.16           N  
ANISOU 3534  ND1 HIS C 468    11358  11497  12160   -114   -137    358       N  
ATOM   3535  CD2 HIS C 468     -12.319  28.048 -44.907  1.00 89.55           C  
ANISOU 3535  CD2 HIS C 468    11066  11183  11778    -52   -114    335       C  
ATOM   3536  CE1 HIS C 468     -13.640  28.666 -46.545  1.00 95.37           C  
ANISOU 3536  CE1 HIS C 468    11746  11933  12558    -76   -106    377       C  
ATOM   3537  NE2 HIS C 468     -13.433  28.777 -45.246  1.00 96.72           N  
ANISOU 3537  NE2 HIS C 468    11938  12114  12695    -37    -91    361       N  
ATOM   3538  N   GLN C 469      -8.920  23.627 -45.285  1.00 54.88           N  
ANISOU 3538  N   GLN C 469     6762   6689   7403   -159   -240    290       N  
ATOM   3539  CA  GLN C 469      -7.809  22.784 -45.696  1.00 48.60           C  
ANISOU 3539  CA  GLN C 469     5986   5860   6619   -176   -282    254       C  
ATOM   3540  C   GLN C 469      -8.102  21.322 -45.395  1.00 42.99           C  
ANISOU 3540  C   GLN C 469     5283   5132   5921   -198   -300    295       C  
ATOM   3541  O   GLN C 469      -8.769  20.996 -44.410  1.00 52.10           O  
ANISOU 3541  O   GLN C 469     6438   6301   7057   -190   -279    348       O  
ATOM   3542  CB  GLN C 469      -6.514  23.179 -44.987  1.00 49.25           C  
ANISOU 3542  CB  GLN C 469     6101   5935   6677   -140   -293    200       C  
ATOM   3543  CG  GLN C 469      -5.963  24.530 -45.361  1.00 37.92           C  
ANISOU 3543  CG  GLN C 469     4661   4501   5246   -126   -287    153       C  
ATOM   3544  CD  GLN C 469      -4.683  24.828 -44.615  1.00 40.97           C  
ANISOU 3544  CD  GLN C 469     5074   4879   5614    -95   -304     97       C  
ATOM   3545  OE1 GLN C 469      -4.705  25.180 -43.436  1.00 37.66           O  
ANISOU 3545  OE1 GLN C 469     4672   4474   5163    -57   -292     92       O  
ATOM   3546  NE2 GLN C 469      -3.554  24.654 -45.289  1.00 39.29           N  
ANISOU 3546  NE2 GLN C 469     4862   4650   5417   -110   -333     53       N  
ATOM   3547  N   ALA C 470      -7.565  20.443 -46.239  1.00 39.13           N  
ANISOU 3547  N   ALA C 470     4795   4610   5461   -224   -341    269       N  
ATOM   3548  CA  ALA C 470      -7.698  19.004 -46.053  1.00 40.01           C  
ANISOU 3548  CA  ALA C 470     4917   4687   5597   -247   -370    299       C  
ATOM   3549  C   ALA C 470      -6.671  18.298 -46.926  1.00 35.47           C  
ANISOU 3549  C   ALA C 470     4354   4078   5047   -255   -421    238       C  
ATOM   3550  O   ALA C 470      -6.001  18.914 -47.760  1.00 36.14           O  
ANISOU 3550  O   ALA C 470     4430   4176   5126   -249   -428    182       O  
ATOM   3551  CB  ALA C 470      -9.115  18.519 -46.383  1.00 33.04           C  
ANISOU 3551  CB  ALA C 470     4000   3807   4747   -288   -360    360       C  
ATOM   3552  N   LEU C 471      -6.554  16.989 -46.718  1.00 44.52           N  
ANISOU 3552  N   LEU C 471     5516   5179   6221   -267   -457    253       N  
ATOM   3553  CA  LEU C 471      -5.747  16.126 -47.570  1.00 38.04           C  
ANISOU 3553  CA  LEU C 471     4702   4321   5430   -272   -511    195       C  
ATOM   3554  C   LEU C 471      -6.664  15.394 -48.540  1.00 36.36           C  
ANISOU 3554  C   LEU C 471     4461   4088   5268   -316   -536    206       C  
ATOM   3555  O   LEU C 471      -7.548  14.642 -48.117  1.00 34.13           O  
ANISOU 3555  O   LEU C 471     4174   3775   5018   -345   -539    268       O  
ATOM   3556  CB  LEU C 471      -4.941  15.120 -46.749  1.00 35.35           C  
ANISOU 3556  CB  LEU C 471     4401   3935   5095   -250   -546    194       C  
ATOM   3557  CG  LEU C 471      -4.284  14.031 -47.604  1.00 43.65           C  
ANISOU 3557  CG  LEU C 471     5457   4939   6188   -253   -609    137       C  
ATOM   3558  CD1 LEU C 471      -3.131  14.600 -48.423  1.00 41.59           C  
ANISOU 3558  CD1 LEU C 471     5189   4711   5903   -227   -620     48       C  
ATOM   3559  CD2 LEU C 471      -3.830  12.845 -46.761  1.00 33.36           C  
ANISOU 3559  CD2 LEU C 471     4193   3576   4908   -238   -647    158       C  
ATOM   3560  N   LEU C 472      -6.463  15.629 -49.831  1.00 38.26           N  
ANISOU 3560  N   LEU C 472     4678   4348   5513   -322   -552    149       N  
ATOM   3561  CA  LEU C 472      -7.104  14.859 -50.886  1.00 28.76           C  
ANISOU 3561  CA  LEU C 472     3447   3127   4353   -356   -590    134       C  
ATOM   3562  C   LEU C 472      -6.111  13.820 -51.381  1.00 31.39           C  
ANISOU 3562  C   LEU C 472     3798   3419   4711   -342   -651     64       C  
ATOM   3563  O   LEU C 472      -4.990  14.165 -51.762  1.00 29.75           O  
ANISOU 3563  O   LEU C 472     3597   3237   4471   -309   -658      1       O  
ATOM   3564  CB  LEU C 472      -7.542  15.765 -52.037  1.00 35.67           C  
ANISOU 3564  CB  LEU C 472     4282   4062   5210   -364   -571    114       C  
ATOM   3565  CG  LEU C 472      -8.303  17.039 -51.666  1.00 41.49           C  
ANISOU 3565  CG  LEU C 472     5002   4844   5917   -364   -511    168       C  
ATOM   3566  CD1 LEU C 472      -8.671  17.800 -52.920  1.00 42.72           C  
ANISOU 3566  CD1 LEU C 472     5119   5052   6059   -370   -503    149       C  
ATOM   3567  CD2 LEU C 472      -9.543  16.718 -50.849  1.00 40.36           C  
ANISOU 3567  CD2 LEU C 472     4849   4687   5798   -390   -491    247       C  
ATOM   3568  N   HIS C 473      -6.513  12.553 -51.365  1.00 37.49           N  
ANISOU 3568  N   HIS C 473     4576   4126   5541   -365   -697     74       N  
ATOM   3569  CA  HIS C 473      -5.585  11.472 -51.669  1.00 36.11           C  
ANISOU 3569  CA  HIS C 473     4424   3900   5397   -345   -761      8       C  
ATOM   3570  C   HIS C 473      -6.319  10.369 -52.407  1.00 38.55           C  
ANISOU 3570  C   HIS C 473     4715   4156   5776   -380   -818     -8       C  
ATOM   3571  O   HIS C 473      -7.429   9.999 -52.013  1.00 43.85           O  
ANISOU 3571  O   HIS C 473     5375   4794   6492   -424   -813     63       O  
ATOM   3572  CB  HIS C 473      -4.961  10.919 -50.385  1.00 41.11           C  
ANISOU 3572  CB  HIS C 473     5103   4481   6036   -322   -770     41       C  
ATOM   3573  CG  HIS C 473      -5.968  10.448 -49.381  1.00 46.41           C  
ANISOU 3573  CG  HIS C 473     5783   5109   6744   -357   -755    144       C  
ATOM   3574  ND1 HIS C 473      -6.537   9.193 -49.427  1.00 46.42           N  
ANISOU 3574  ND1 HIS C 473     5785   5030   6823   -392   -803    171       N  
ATOM   3575  CD2 HIS C 473      -6.515  11.069 -48.310  1.00 47.47           C  
ANISOU 3575  CD2 HIS C 473     5920   5273   6845   -362   -697    228       C  
ATOM   3576  CE1 HIS C 473      -7.385   9.059 -48.423  1.00 43.34           C  
ANISOU 3576  CE1 HIS C 473     5396   4625   6446   -422   -772    276       C  
ATOM   3577  NE2 HIS C 473      -7.391  10.184 -47.730  1.00 46.00           N  
ANISOU 3577  NE2 HIS C 473     5734   5034   6712   -401   -706    311       N  
ATOM   3578  N   THR C 474      -5.703   9.832 -53.460  1.00 44.23           N  
ANISOU 3578  N   THR C 474     5428   4871   6508   -360   -872   -103       N  
ATOM   3579  CA  THR C 474      -6.335   8.701 -54.133  1.00 44.26           C  
ANISOU 3579  CA  THR C 474     5417   4815   6585   -389   -938   -132       C  
ATOM   3580  C   THR C 474      -5.298   7.901 -54.906  1.00 39.54           C  
ANISOU 3580  C   THR C 474     4829   4195   6000   -346  -1006   -245       C  
ATOM   3581  O   THR C 474      -4.272   8.426 -55.334  1.00 44.05           O  
ANISOU 3581  O   THR C 474     5399   4829   6510   -300   -996   -308       O  
ATOM   3582  CB  THR C 474      -7.471   9.143 -55.074  1.00 48.54           C  
ANISOU 3582  CB  THR C 474     5908   5409   7127   -426   -927   -130       C  
ATOM   3583  OG1 THR C 474      -8.233   7.996 -55.473  1.00 53.30           O  
ANISOU 3583  OG1 THR C 474     6496   5940   7814   -464   -991   -144       O  
ATOM   3584  CG2 THR C 474      -6.923   9.819 -56.318  1.00 57.62           C  
ANISOU 3584  CG2 THR C 474     7031   6649   8213   -391   -925   -215       C  
ATOM   3585  N   ALA C 475      -5.579   6.610 -55.069  1.00 29.84           N  
ANISOU 3585  N   ALA C 475     3608   2873   4856   -362  -1078   -270       N  
ATOM   3586  CA  ALA C 475      -4.740   5.713 -55.867  1.00 25.57           C  
ANISOU 3586  CA  ALA C 475     3074   2302   4339   -319  -1155   -387       C  
ATOM   3587  C   ALA C 475      -3.299   5.681 -55.362  1.00 36.19           C  
ANISOU 3587  C   ALA C 475     4454   3647   5648   -257  -1157   -421       C  
ATOM   3588  O   ALA C 475      -2.348   5.619 -56.143  1.00 46.14           O  
ANISOU 3588  O   ALA C 475     5706   4951   6874   -204  -1184   -524       O  
ATOM   3589  CB  ALA C 475      -4.785   6.090 -57.349  1.00 20.68           C  
ANISOU 3589  CB  ALA C 475     2409   1772   3676   -303  -1168   -480       C  
ATOM   3590  N   ASN C 476      -3.129   5.734 -54.047  1.00 34.84           N  
ANISOU 3590  N   ASN C 476     4320   3437   5480   -259  -1127   -336       N  
ATOM   3591  CA  ASN C 476      -1.841   5.409 -53.461  1.00 39.28           C  
ANISOU 3591  CA  ASN C 476     4919   3975   6029   -202  -1146   -366       C  
ATOM   3592  C   ASN C 476      -1.845   3.922 -53.100  1.00 44.90           C  
ANISOU 3592  C   ASN C 476     5666   4555   6839   -200  -1225   -366       C  
ATOM   3593  O   ASN C 476      -2.714   3.165 -53.551  1.00 50.49           O  
ANISOU 3593  O   ASN C 476     6363   5196   7624   -241  -1271   -369       O  
ATOM   3594  CB  ASN C 476      -1.557   6.327 -52.266  1.00 38.00           C  
ANISOU 3594  CB  ASN C 476     4777   3853   5808   -196  -1075   -284       C  
ATOM   3595  CG  ASN C 476      -1.479   7.789 -52.662  1.00 38.52           C  
ANISOU 3595  CG  ASN C 476     4810   4036   5789   -196  -1006   -291       C  
ATOM   3596  OD1 ASN C 476      -0.972   8.126 -53.732  1.00 38.75           O  
ANISOU 3596  OD1 ASN C 476     4810   4130   5783   -172  -1012   -374       O  
ATOM   3597  ND2 ASN C 476      -1.978   8.666 -51.797  1.00 35.56           N  
ANISOU 3597  ND2 ASN C 476     4439   3691   5383   -219   -941   -202       N  
ATOM   3598  N   ARG C 477      -0.881   3.486 -52.309  1.00 46.43           N  
ANISOU 3598  N   ARG C 477     5900   4706   7036   -154  -1246   -364       N  
ATOM   3599  CA  ARG C 477      -0.898   2.084 -51.921  1.00 45.92           C  
ANISOU 3599  CA  ARG C 477     5871   4506   7070   -152  -1322   -353       C  
ATOM   3600  C   ARG C 477      -1.987   1.864 -50.879  1.00 51.38           C  
ANISOU 3600  C   ARG C 477     6579   5134   7810   -217  -1297   -208       C  
ATOM   3601  O   ARG C 477      -2.052   2.609 -49.897  1.00 56.09           O  
ANISOU 3601  O   ARG C 477     7185   5778   8349   -223  -1229   -119       O  
ATOM   3602  CB  ARG C 477       0.453   1.635 -51.375  1.00 40.90           C  
ANISOU 3602  CB  ARG C 477     5273   3842   6423    -78  -1356   -390       C  
ATOM   3603  CG  ARG C 477       0.552   0.125 -51.292  1.00 37.82           C  
ANISOU 3603  CG  ARG C 477     4918   3310   6144    -64  -1451   -408       C  
ATOM   3604  CD  ARG C 477       1.922  -0.381 -50.921  1.00 32.53           C  
ANISOU 3604  CD  ARG C 477     4281   2612   5466     20  -1496   -462       C  
ATOM   3605  NE  ARG C 477       1.935  -1.839 -50.968  1.00 40.72           N  
ANISOU 3605  NE  ARG C 477     5349   3504   6618     34  -1593   -485       N  
ATOM   3606  CZ  ARG C 477       2.937  -2.597 -50.541  1.00 41.47           C  
ANISOU 3606  CZ  ARG C 477     5476   3552   6729    104  -1642   -510       C  
ATOM   3607  NH1 ARG C 477       4.020  -2.039 -50.023  1.00 51.73           N  
ANISOU 3607  NH1 ARG C 477     6788   4910   7956    164  -1620   -528       N  
ATOM   3608  NH2 ARG C 477       2.850  -3.917 -50.627  1.00 46.35           N  
ANISOU 3608  NH2 ARG C 477     6103   4082   7423    116  -1706   -512       N  
ATOM   3609  N   PRO C 478      -2.862   0.875 -51.064  1.00 53.63           N  
ANISOU 3609  N   PRO C 478     6862   5315   8200   -266  -1350   -183       N  
ATOM   3610  CA  PRO C 478      -3.951   0.670 -50.102  1.00 50.37           C  
ANISOU 3610  CA  PRO C 478     6455   4850   7834   -335  -1321    -36       C  
ATOM   3611  C   PRO C 478      -3.394   0.402 -48.714  1.00 50.85           C  
ANISOU 3611  C   PRO C 478     6565   4872   7885   -307  -1309     56       C  
ATOM   3612  O   PRO C 478      -2.474  -0.400 -48.542  1.00 54.98           O  
ANISOU 3612  O   PRO C 478     7125   5323   8441   -256  -1371     16       O  
ATOM   3613  CB  PRO C 478      -4.698  -0.549 -50.658  1.00 43.61           C  
ANISOU 3613  CB  PRO C 478     5591   3871   7108   -383  -1403    -50       C  
ATOM   3614  CG  PRO C 478      -4.213  -0.714 -52.065  1.00 40.83           C  
ANISOU 3614  CG  PRO C 478     5215   3559   6741   -336  -1449   -208       C  
ATOM   3615  CD  PRO C 478      -2.826  -0.175 -52.095  1.00 48.81           C  
ANISOU 3615  CD  PRO C 478     6246   4625   7674   -258  -1445   -289       C  
ATOM   3616  N   GLU C 479      -3.954   1.096 -47.721  1.00 53.64           N  
ANISOU 3616  N   GLU C 479     6915   5279   8186   -336  -1231    176       N  
ATOM   3617  CA  GLU C 479      -3.442   0.953 -46.364  1.00 62.49           C  
ANISOU 3617  CA  GLU C 479     8080   6385   9279   -305  -1213    266       C  
ATOM   3618  C   GLU C 479      -3.523  -0.490 -45.886  1.00 64.26           C  
ANISOU 3618  C   GLU C 479     8340   6464   9614   -319  -1284    329       C  
ATOM   3619  O   GLU C 479      -2.686  -0.917 -45.091  1.00 58.19           O  
ANISOU 3619  O   GLU C 479     7614   5659   8836   -268  -1306    355       O  
ATOM   3620  CB  GLU C 479      -4.192   1.883 -45.406  1.00 65.96           C  
ANISOU 3620  CB  GLU C 479     8505   6910   9648   -335  -1119    384       C  
ATOM   3621  CG  GLU C 479      -3.680   1.847 -43.962  1.00 78.91           C  
ANISOU 3621  CG  GLU C 479    10186   8557  11239   -297  -1095    476       C  
ATOM   3622  CD  GLU C 479      -2.359   2.586 -43.770  1.00 91.88           C  
ANISOU 3622  CD  GLU C 479    11849  10277  12786   -216  -1082    396       C  
ATOM   3623  OE1 GLU C 479      -1.782   2.499 -42.664  1.00 94.68           O  
ANISOU 3623  OE1 GLU C 479    12238  10638  13099   -173  -1075    451       O  
ATOM   3624  OE2 GLU C 479      -1.899   3.258 -44.717  1.00 94.06           O  
ANISOU 3624  OE2 GLU C 479    12102  10610  13027   -195  -1079    282       O  
ATOM   3625  N   ASP C 480      -4.492  -1.266 -46.380  1.00 72.80           N  
ANISOU 3625  N   ASP C 480     9401   7456  10804   -387  -1325    351       N  
ATOM   3626  CA  ASP C 480      -4.610  -2.652 -45.930  1.00 75.20           C  
ANISOU 3626  CA  ASP C 480     9728   7643  11201   -400  -1380    413       C  
ATOM   3627  C   ASP C 480      -3.375  -3.470 -46.302  1.00 69.71           C  
ANISOU 3627  C   ASP C 480     9067   6892  10529   -321  -1460    301       C  
ATOM   3628  O   ASP C 480      -2.968  -4.364 -45.549  1.00 70.96           O  
ANISOU 3628  O   ASP C 480     9261   6983  10719   -297  -1490    357       O  
ATOM   3629  CB  ASP C 480      -5.885  -3.292 -46.487  1.00 80.29           C  
ANISOU 3629  CB  ASP C 480    10325   8258  11923   -476  -1390    436       C  
ATOM   3630  CG  ASP C 480      -6.144  -2.931 -47.936  1.00 90.10           C  
ANISOU 3630  CG  ASP C 480    11525   9543  13167   -483  -1408    302       C  
ATOM   3631  OD1 ASP C 480      -5.904  -3.785 -48.815  1.00 88.50           O  
ANISOU 3631  OD1 ASP C 480    11316   9292  13015   -460  -1478    200       O  
ATOM   3632  OD2 ASP C 480      -6.606  -1.800 -48.195  1.00103.22           O  
ANISOU 3632  OD2 ASP C 480    13157  11289  14775   -509  -1353    302       O  
ATOM   3633  N   GLU C 481      -2.749  -3.171 -47.447  1.00 66.79           N  
ANISOU 3633  N   GLU C 481     8683   6558  10138   -278  -1491    145       N  
ATOM   3634  CA  GLU C 481      -1.486  -3.834 -47.771  1.00 67.89           C  
ANISOU 3634  CA  GLU C 481     8850   6664  10283   -193  -1559     35       C  
ATOM   3635  C   GLU C 481      -0.343  -3.303 -46.916  1.00 68.65           C  
ANISOU 3635  C   GLU C 481     8988   6786  10311   -124  -1545     46       C  
ATOM   3636  O   GLU C 481       0.543  -4.067 -46.515  1.00 76.27           O  
ANISOU 3636  O   GLU C 481     9987   7701  11290    -63  -1592     32       O  
ATOM   3637  CB  GLU C 481      -1.125  -3.664 -49.245  1.00 64.46           C  
ANISOU 3637  CB  GLU C 481     8380   6279   9832   -159  -1591   -133       C  
ATOM   3638  CG  GLU C 481      -2.212  -3.922 -50.248  1.00 66.96           C  
ANISOU 3638  CG  GLU C 481     8650   6599  10194   -215  -1601   -164       C  
ATOM   3639  CD  GLU C 481      -1.683  -3.774 -51.656  1.00 70.25           C  
ANISOU 3639  CD  GLU C 481     9035   7078  10577   -163  -1632   -330       C  
ATOM   3640  OE1 GLU C 481      -0.445  -3.818 -51.829  1.00 62.28           O  
ANISOU 3640  OE1 GLU C 481     8043   6092   9531    -82  -1660   -420       O  
ATOM   3641  OE2 GLU C 481      -2.492  -3.582 -52.584  1.00 79.36           O  
ANISOU 3641  OE2 GLU C 481    10146   8272  11735   -199  -1625   -368       O  
ATOM   3642  N   CYS C 482      -0.320  -1.991 -46.667  1.00 55.98           N  
ANISOU 3642  N   CYS C 482     7367   5299   8602   -125  -1464     63       N  
ATOM   3643  CA  CYS C 482       0.700  -1.413 -45.797  1.00 56.36           C  
ANISOU 3643  CA  CYS C 482     7440   5422   8554    -59  -1428     76       C  
ATOM   3644  C   CYS C 482       0.697  -2.101 -44.437  1.00 64.33           C  
ANISOU 3644  C   CYS C 482     8496   6356   9591    -54  -1439    211       C  
ATOM   3645  O   CYS C 482       1.727  -2.608 -43.977  1.00 66.85           O  
ANISOU 3645  O   CYS C 482     8852   6638   9908     17  -1485    193       O  
ATOM   3646  CB  CYS C 482       0.470   0.095 -45.647  1.00 50.68           C  
ANISOU 3646  CB  CYS C 482     6688   4850   7718    -74  -1328     92       C  
ATOM   3647  SG  CYS C 482       0.415   1.034 -47.204  1.00 49.32           S  
ANISOU 3647  SG  CYS C 482     6458   4778   7503    -84  -1305    -44       S  
ATOM   3648  N   VAL C 483      -0.469  -2.135 -43.787  1.00 72.26           N  
ANISOU 3648  N   VAL C 483     9496   7342  10619   -126  -1398    352       N  
ATOM   3649  CA  VAL C 483      -0.633  -2.887 -42.545  1.00 78.33           C  
ANISOU 3649  CA  VAL C 483    10304   8035  11422   -132  -1408    499       C  
ATOM   3650  C   VAL C 483      -0.206  -4.335 -42.742  1.00 70.42           C  
ANISOU 3650  C   VAL C 483     9328   6911  10517   -109  -1497    470       C  
ATOM   3651  O   VAL C 483       0.573  -4.884 -41.953  1.00 64.35           O  
ANISOU 3651  O   VAL C 483     8599   6112   9739    -52  -1524    505       O  
ATOM   3652  CB  VAL C 483      -2.091  -2.799 -42.052  1.00 85.97           C  
ANISOU 3652  CB  VAL C 483    11248   9005  12413   -224  -1351    647       C  
ATOM   3653  CG1 VAL C 483      -2.216  -3.370 -40.651  1.00 85.21           C  
ANISOU 3653  CG1 VAL C 483    11184   8874  12316   -224  -1339    811       C  
ATOM   3654  CG2 VAL C 483      -2.586  -1.358 -42.079  1.00 87.96           C  
ANISOU 3654  CG2 VAL C 483    11456   9410  12554   -245  -1253    644       C  
ATOM   3655  N   GLY C 484      -0.697  -4.966 -43.814  1.00 72.63           N  
ANISOU 3655  N   GLY C 484     9576   7147  10874   -147  -1536    396       N  
ATOM   3656  CA  GLY C 484      -0.466  -6.388 -44.009  1.00 71.44           C  
ANISOU 3656  CA  GLY C 484     9437   6897  10808   -133  -1610    370       C  
ATOM   3657  C   GLY C 484       0.995  -6.764 -44.168  1.00 74.65           C  
ANISOU 3657  C   GLY C 484     9874   7288  11200    -32  -1672    259       C  
ATOM   3658  O   GLY C 484       1.406  -7.854 -43.760  1.00 79.99           O  
ANISOU 3658  O   GLY C 484    10579   7887  11926     -4  -1723    283       O  
ATOM   3659  N   GLU C 485       1.796  -5.885 -44.766  1.00 69.42           N  
ANISOU 3659  N   GLU C 485     9205   6702  10471     24  -1669    138       N  
ATOM   3660  CA  GLU C 485       3.223  -6.123 -44.934  1.00 67.06           C  
ANISOU 3660  CA  GLU C 485     8925   6409  10146    124  -1721     26       C  
ATOM   3661  C   GLU C 485       4.027  -5.630 -43.727  1.00 64.11           C  
ANISOU 3661  C   GLU C 485     8590   6071   9698    182  -1696     92       C  
ATOM   3662  O   GLU C 485       5.257  -5.744 -43.711  1.00 64.96           O  
ANISOU 3662  O   GLU C 485     8712   6195   9775    269  -1734      9       O  
ATOM   3663  CB  GLU C 485       3.700  -5.476 -46.250  1.00 73.35           C  
ANISOU 3663  CB  GLU C 485     9684   7281  10906    157  -1729   -143       C  
ATOM   3664  CG  GLU C 485       5.195  -5.582 -46.560  1.00 86.58           C  
ANISOU 3664  CG  GLU C 485    11365   8989  12542    263  -1774   -273       C  
ATOM   3665  CD  GLU C 485       5.547  -5.192 -47.983  1.00 99.44           C  
ANISOU 3665  CD  GLU C 485    12946  10693  14143    290  -1785   -436       C  
ATOM   3666  OE1 GLU C 485       4.623  -5.038 -48.810  1.00101.96           O  
ANISOU 3666  OE1 GLU C 485    13232  11025  14483    230  -1770   -455       O  
ATOM   3667  OE2 GLU C 485       6.752  -5.014 -48.265  1.00104.13           O  
ANISOU 3667  OE2 GLU C 485    13533  11345  14687    372  -1804   -542       O  
ATOM   3668  N   GLY C 486       3.354  -5.127 -42.696  1.00 62.34           N  
ANISOU 3668  N   GLY C 486     8379   5865   9441    138  -1635    240       N  
ATOM   3669  CA  GLY C 486       4.049  -4.686 -41.505  1.00 63.27           C  
ANISOU 3669  CA  GLY C 486     8532   6025   9482    197  -1614    309       C  
ATOM   3670  C   GLY C 486       4.673  -3.318 -41.609  1.00 73.64           C  
ANISOU 3670  C   GLY C 486     9818   7492  10670    233  -1554    229       C  
ATOM   3671  O   GLY C 486       5.609  -3.017 -40.862  1.00 81.38           O  
ANISOU 3671  O   GLY C 486    10814   8532  11573    302  -1548    227       O  
ATOM   3672  N   LEU C 487       4.188  -2.476 -42.521  1.00 68.47           N  
ANISOU 3672  N   LEU C 487     9116   6912   9988    188  -1507    161       N  
ATOM   3673  CA  LEU C 487       4.690  -1.113 -42.676  1.00 59.21           C  
ANISOU 3673  CA  LEU C 487     7909   5890   8697    209  -1441     90       C  
ATOM   3674  C   LEU C 487       3.792  -0.183 -41.865  1.00 61.02           C  
ANISOU 3674  C   LEU C 487     8128   6199   8859    156  -1350    206       C  
ATOM   3675  O   LEU C 487       2.963   0.557 -42.394  1.00 61.29           O  
ANISOU 3675  O   LEU C 487     8125   6285   8877     97  -1296    203       O  
ATOM   3676  CB  LEU C 487       4.746  -0.726 -44.149  1.00 52.88           C  
ANISOU 3676  CB  LEU C 487     7062   5127   7902    198  -1445    -47       C  
ATOM   3677  CG  LEU C 487       5.767  -1.508 -44.979  1.00 48.77           C  
ANISOU 3677  CG  LEU C 487     6544   4558   7428    265  -1530   -182       C  
ATOM   3678  CD1 LEU C 487       5.427  -1.458 -46.459  1.00 42.68           C  
ANISOU 3678  CD1 LEU C 487     5731   3797   6687    239  -1544   -291       C  
ATOM   3679  CD2 LEU C 487       7.165  -0.965 -44.729  1.00 41.83           C  
ANISOU 3679  CD2 LEU C 487     5660   3772   6463    347  -1524   -256       C  
ATOM   3680  N   ALA C 488       3.964  -0.241 -40.551  1.00 62.49           N  
ANISOU 3680  N   ALA C 488     8345   6395   9001    183  -1334    308       N  
ATOM   3681  CA  ALA C 488       3.280   0.628 -39.607  1.00 56.71           C  
ANISOU 3681  CA  ALA C 488     7606   5751   8188    154  -1251    412       C  
ATOM   3682  C   ALA C 488       4.313   1.492 -38.892  1.00 54.58           C  
ANISOU 3682  C   ALA C 488     7341   5590   7806    224  -1225    373       C  
ATOM   3683  O   ALA C 488       5.519   1.371 -39.119  1.00 51.02           O  
ANISOU 3683  O   ALA C 488     6896   5144   7345    290  -1272    276       O  
ATOM   3684  CB  ALA C 488       2.454  -0.191 -38.611  1.00 57.36           C  
ANISOU 3684  CB  ALA C 488     7718   5764   8311    121  -1251    579       C  
ATOM   3685  N   CYS C 489       3.835   2.374 -38.018  1.00 56.91           N  
ANISOU 3685  N   CYS C 489     7629   5977   8017    212  -1153    446       N  
ATOM   3686  CA  CYS C 489       4.750   3.219 -37.269  1.00 58.34           C  
ANISOU 3686  CA  CYS C 489     7813   6260   8094    276  -1132    409       C  
ATOM   3687  C   CYS C 489       5.547   2.390 -36.266  1.00 52.71           C  
ANISOU 3687  C   CYS C 489     7145   5514   7369    346  -1184    458       C  
ATOM   3688  O   CYS C 489       5.137   1.306 -35.840  1.00 50.70           O  
ANISOU 3688  O   CYS C 489     6922   5171   7172    337  -1216    563       O  
ATOM   3689  CB  CYS C 489       3.996   4.334 -36.544  1.00 66.97           C  
ANISOU 3689  CB  CYS C 489     8888   7456   9101    252  -1048    471       C  
ATOM   3690  SG  CYS C 489       3.347   5.638 -37.622  1.00 85.14           S  
ANISOU 3690  SG  CYS C 489    11135   9822  11391    193   -985    395       S  
ATOM   3691  N   HIS C 490       6.710   2.919 -35.897  1.00 50.68           N  
ANISOU 3691  N   HIS C 490     6887   5329   7039    417  -1195    382       N  
ATOM   3692  CA  HIS C 490       7.552   2.279 -34.898  1.00 49.30           C  
ANISOU 3692  CA  HIS C 490     6751   5144   6837    494  -1243    419       C  
ATOM   3693  C   HIS C 490       6.852   2.274 -33.543  1.00 55.14           C  
ANISOU 3693  C   HIS C 490     7514   5920   7516    493  -1203    570       C  
ATOM   3694  O   HIS C 490       6.061   3.166 -33.229  1.00 52.38           O  
ANISOU 3694  O   HIS C 490     7143   5649   7109    456  -1131    608       O  
ATOM   3695  CB  HIS C 490       8.893   3.008 -34.802  1.00 45.44           C  
ANISOU 3695  CB  HIS C 490     6246   4743   6277    564  -1258    298       C  
ATOM   3696  CG  HIS C 490       9.967   2.227 -34.111  1.00 46.64           C  
ANISOU 3696  CG  HIS C 490     6431   4873   6419    651  -1327    301       C  
ATOM   3697  ND1 HIS C 490      10.150   2.258 -32.746  1.00 50.89           N  
ANISOU 3697  ND1 HIS C 490     6995   5464   6876    701  -1323    383       N  
ATOM   3698  CD2 HIS C 490      10.928   1.409 -34.601  1.00 45.83           C  
ANISOU 3698  CD2 HIS C 490     6336   4705   6372    703  -1403    228       C  
ATOM   3699  CE1 HIS C 490      11.172   1.485 -32.423  1.00 59.85           C  
ANISOU 3699  CE1 HIS C 490     8155   6566   8021    779  -1395    365       C  
ATOM   3700  NE2 HIS C 490      11.661   0.958 -33.531  1.00 58.08           N  
ANISOU 3700  NE2 HIS C 490     7920   6267   7881    782  -1445    271       N  
ATOM   3701  N   GLN C 491       7.152   1.247 -32.738  1.00 63.23           N  
ANISOU 3701  N   GLN C 491     8582   6891   8553    538  -1252    658       N  
ATOM   3702  CA  GLN C 491       6.572   1.137 -31.400  1.00 67.71           C  
ANISOU 3702  CA  GLN C 491     9171   7499   9055    546  -1217    812       C  
ATOM   3703  C   GLN C 491       6.729   2.432 -30.611  1.00 65.23           C  
ANISOU 3703  C   GLN C 491     8839   7340   8606    580  -1158    786       C  
ATOM   3704  O   GLN C 491       5.839   2.816 -29.844  1.00 65.79           O  
ANISOU 3704  O   GLN C 491     8906   7478   8615    558  -1096    887       O  
ATOM   3705  CB  GLN C 491       7.225  -0.027 -30.649  1.00 75.45           C  
ANISOU 3705  CB  GLN C 491    10201   8415  10053    612  -1287    888       C  
ATOM   3706  CG  GLN C 491       7.230   0.124 -29.134  1.00 89.03           C  
ANISOU 3706  CG  GLN C 491    11941  10228  11657    664  -1261   1002       C  
ATOM   3707  CD  GLN C 491       8.092  -0.924 -28.449  1.00100.28           C  
ANISOU 3707  CD  GLN C 491    13413  11600  13089    744  -1337   1056       C  
ATOM   3708  OE1 GLN C 491       7.739  -1.443 -27.391  1.00107.91           O  
ANISOU 3708  OE1 GLN C 491    14408  12574  14020    761  -1331   1211       O  
ATOM   3709  NE2 GLN C 491       9.230  -1.243 -29.066  1.00100.32           N  
ANISOU 3709  NE2 GLN C 491    13422  11554  13139    796  -1410    932       N  
ATOM   3710  N   LEU C 492       7.844   3.133 -30.813  1.00 61.44           N  
ANISOU 3710  N   LEU C 492     8342   6920   8080    632  -1178    647       N  
ATOM   3711  CA  LEU C 492       8.171   4.298 -30.004  1.00 57.72           C  
ANISOU 3711  CA  LEU C 492     7857   6587   7488    674  -1139    609       C  
ATOM   3712  C   LEU C 492       7.507   5.579 -30.491  1.00 55.11           C  
ANISOU 3712  C   LEU C 492     7483   6321   7133    618  -1068    552       C  
ATOM   3713  O   LEU C 492       7.470   6.560 -29.740  1.00 55.33           O  
ANISOU 3713  O   LEU C 492     7500   6458   7065    643  -1027    541       O  
ATOM   3714  CB  LEU C 492       9.688   4.478 -29.966  1.00 51.70           C  
ANISOU 3714  CB  LEU C 492     7091   5858   6695    753  -1196    486       C  
ATOM   3715  CG  LEU C 492      10.410   3.348 -29.228  1.00 53.69           C  
ANISOU 3715  CG  LEU C 492     7385   6069   6945    828  -1266    545       C  
ATOM   3716  CD1 LEU C 492      11.901   3.358 -29.522  1.00 50.03           C  
ANISOU 3716  CD1 LEU C 492     6910   5616   6482    897  -1332    410       C  
ATOM   3717  CD2 LEU C 492      10.152   3.456 -27.733  1.00 58.42           C  
ANISOU 3717  CD2 LEU C 492     8007   6754   7434    873  -1242    658       C  
ATOM   3718  N   CYS C 493       6.987   5.601 -31.717  1.00 49.20           N  
ANISOU 3718  N   CYS C 493     6712   5512   6470    547  -1055    514       N  
ATOM   3719  CA  CYS C 493       6.308   6.789 -32.221  1.00 45.62           C  
ANISOU 3719  CA  CYS C 493     6220   5115   5999    494   -990    470       C  
ATOM   3720  C   CYS C 493       5.042   7.047 -31.412  1.00 58.75           C  
ANISOU 3720  C   CYS C 493     7882   6825   7613    466   -924    592       C  
ATOM   3721  O   CYS C 493       4.125   6.219 -31.403  1.00 69.52           O  
ANISOU 3721  O   CYS C 493     9258   8129   9029    421   -916    706       O  
ATOM   3722  CB  CYS C 493       5.972   6.630 -33.702  1.00 45.16           C  
ANISOU 3722  CB  CYS C 493     6138   4981   6039    428   -995    416       C  
ATOM   3723  SG  CYS C 493       7.400   6.444 -34.791  1.00 57.65           S  
ANISOU 3723  SG  CYS C 493     7707   6527   7670    461  -1062    262       S  
ATOM   3724  N   ALA C 494       4.993   8.194 -30.736  1.00 60.25           N  
ANISOU 3724  N   ALA C 494     8058   7127   7709    492   -879    567       N  
ATOM   3725  CA  ALA C 494       3.844   8.529 -29.906  1.00 58.30           C  
ANISOU 3725  CA  ALA C 494     7806   6945   7401    478   -813    672       C  
ATOM   3726  C   ALA C 494       2.583   8.658 -30.752  1.00 59.68           C  
ANISOU 3726  C   ALA C 494     7952   7084   7640    391   -766    708       C  
ATOM   3727  O   ALA C 494       2.624   9.133 -31.891  1.00 66.75           O  
ANISOU 3727  O   ALA C 494     8823   7949   8590    352   -766    616       O  
ATOM   3728  CB  ALA C 494       4.100   9.830 -29.145  1.00 53.68           C  
ANISOU 3728  CB  ALA C 494     7206   6483   6706    529   -781    608       C  
ATOM   3729  N   ARG C 495       1.460   8.209 -30.187  1.00 55.44           N  
ANISOU 3729  N   ARG C 495     7415   6554   7095    362   -726    846       N  
ATOM   3730  CA  ARG C 495       0.134   8.319 -30.805  1.00 57.55           C  
ANISOU 3730  CA  ARG C 495     7650   6803   7415    282   -677    897       C  
ATOM   3731  C   ARG C 495       0.072   7.671 -32.188  1.00 53.94           C  
ANISOU 3731  C   ARG C 495     7187   6226   7083    219   -716    860       C  
ATOM   3732  O   ARG C 495      -0.871   7.913 -32.949  1.00 57.53           O  
ANISOU 3732  O   ARG C 495     7609   6664   7586    153   -683    865       O  
ATOM   3733  CB  ARG C 495      -0.322   9.779 -30.885  1.00 68.22           C  
ANISOU 3733  CB  ARG C 495     8965   8246   8708    280   -617    832       C  
ATOM   3734  CG  ARG C 495      -0.632  10.408 -29.536  1.00 78.62           C  
ANISOU 3734  CG  ARG C 495    10281   9687   9904    334   -568    881       C  
ATOM   3735  CD  ARG C 495      -1.475  11.661 -29.704  1.00 88.48           C  
ANISOU 3735  CD  ARG C 495    11490  11008  11121    317   -504    844       C  
ATOM   3736  NE  ARG C 495      -2.361  11.886 -28.565  1.00 99.22           N  
ANISOU 3736  NE  ARG C 495    12838  12471  12392    341   -445    941       N  
ATOM   3737  CZ  ARG C 495      -3.508  12.554 -28.635  1.00103.86           C  
ANISOU 3737  CZ  ARG C 495    13386  13111  12965    314   -382    966       C  
ATOM   3738  NH1 ARG C 495      -3.915  13.058 -29.792  1.00101.75           N  
ANISOU 3738  NH1 ARG C 495    13092  12799  12770    258   -372    905       N  
ATOM   3739  NH2 ARG C 495      -4.255  12.713 -27.550  1.00105.58           N  
ANISOU 3739  NH2 ARG C 495    13589  13433  13092    345   -328   1054       N  
ATOM   3740  N   GLY C 496       1.057   6.843 -32.526  1.00 49.66           N  
ANISOU 3740  N   GLY C 496     6673   5604   6593    242   -787    818       N  
ATOM   3741  CA  GLY C 496       1.068   6.174 -33.813  1.00 50.00           C  
ANISOU 3741  CA  GLY C 496     6710   5536   6750    194   -831    772       C  
ATOM   3742  C   GLY C 496       1.223   7.088 -35.008  1.00 50.84           C  
ANISOU 3742  C   GLY C 496     6783   5660   6874    171   -821    641       C  
ATOM   3743  O   GLY C 496       0.708   6.777 -36.086  1.00 54.17           O  
ANISOU 3743  O   GLY C 496     7186   6018   7377    113   -831    623       O  
ATOM   3744  N   HIS C 497       1.924   8.207 -34.851  1.00 47.76           N  
ANISOU 3744  N   HIS C 497     6383   5353   6411    213   -803    551       N  
ATOM   3745  CA  HIS C 497       2.107   9.185 -35.915  1.00 40.99           C  
ANISOU 3745  CA  HIS C 497     5491   4519   5563    192   -789    437       C  
ATOM   3746  C   HIS C 497       3.549   9.149 -36.401  1.00 40.91           C  
ANISOU 3746  C   HIS C 497     5486   4496   5562    236   -843    320       C  
ATOM   3747  O   HIS C 497       4.480   9.276 -35.598  1.00 50.44           O  
ANISOU 3747  O   HIS C 497     6709   5742   6713    298   -864    295       O  
ATOM   3748  CB  HIS C 497       1.751  10.590 -35.425  1.00 45.29           C  
ANISOU 3748  CB  HIS C 497     6014   5165   6029    201   -726    422       C  
ATOM   3749  CG  HIS C 497       0.311  10.754 -35.052  1.00 57.03           C  
ANISOU 3749  CG  HIS C 497     7487   6679   7505    161   -666    525       C  
ATOM   3750  ND1 HIS C 497      -0.709  10.110 -35.718  1.00 60.53           N  
ANISOU 3750  ND1 HIS C 497     7916   7062   8022     94   -660    587       N  
ATOM   3751  CD2 HIS C 497      -0.279  11.485 -34.076  1.00 60.41           C  
ANISOU 3751  CD2 HIS C 497     7908   7192   7854    181   -612    572       C  
ATOM   3752  CE1 HIS C 497      -1.866  10.442 -35.173  1.00 62.95           C  
ANISOU 3752  CE1 HIS C 497     8203   7417   8297     72   -602    673       C  
ATOM   3753  NE2 HIS C 497      -1.633  11.274 -34.174  1.00 61.66           N  
ANISOU 3753  NE2 HIS C 497     8045   7345   8039    126   -571    665       N  
ATOM   3754  N   CYS C 498       3.734   8.987 -37.711  1.00 32.96           N  
ANISOU 3754  N   CYS C 498     4459   3443   4620    206   -867    247       N  
ATOM   3755  CA  CYS C 498       5.079   8.911 -38.265  1.00 31.64           C  
ANISOU 3755  CA  CYS C 498     4288   3272   4463    246   -917    135       C  
ATOM   3756  C   CYS C 498       5.041   9.225 -39.755  1.00 32.84           C  
ANISOU 3756  C   CYS C 498     4402   3414   4660    206   -915     54       C  
ATOM   3757  O   CYS C 498       3.989   9.168 -40.397  1.00 37.05           O  
ANISOU 3757  O   CYS C 498     4922   3922   5234    149   -892     87       O  
ATOM   3758  CB  CYS C 498       5.712   7.536 -38.011  1.00 35.88           C  
ANISOU 3758  CB  CYS C 498     4860   3734   5038    287   -987    152       C  
ATOM   3759  SG  CYS C 498       4.893   6.151 -38.838  1.00 43.74           S  
ANISOU 3759  SG  CYS C 498     5867   4607   6147    237  -1025    200       S  
ATOM   3760  N   TRP C 499       6.215   9.566 -40.292  1.00 30.84           N  
ANISOU 3760  N   TRP C 499     4130   3190   4398    237   -938    -52       N  
ATOM   3761  CA  TRP C 499       6.384   9.922 -41.695  1.00 34.46           C  
ANISOU 3761  CA  TRP C 499     4549   3659   4885    209   -937   -135       C  
ATOM   3762  C   TRP C 499       6.996   8.802 -42.523  1.00 36.83           C  
ANISOU 3762  C   TRP C 499     4850   3901   5241    230  -1001   -193       C  
ATOM   3763  O   TRP C 499       7.224   8.989 -43.723  1.00 39.87           O  
ANISOU 3763  O   TRP C 499     5201   4304   5645    216  -1004   -267       O  
ATOM   3764  CB  TRP C 499       7.258  11.176 -41.822  1.00 33.42           C  
ANISOU 3764  CB  TRP C 499     4384   3609   4706    224   -913   -213       C  
ATOM   3765  CG  TRP C 499       6.607  12.438 -41.353  1.00 35.12           C  
ANISOU 3765  CG  TRP C 499     4589   3877   4878    198   -851   -180       C  
ATOM   3766  CD1 TRP C 499       6.693  12.992 -40.109  1.00 40.89           C  
ANISOU 3766  CD1 TRP C 499     5336   4646   5555    227   -833   -153       C  
ATOM   3767  CD2 TRP C 499       5.785  13.318 -42.129  1.00 31.69           C  
ANISOU 3767  CD2 TRP C 499     4124   3464   4452    145   -802   -176       C  
ATOM   3768  NE1 TRP C 499       5.966  14.157 -40.059  1.00 38.78           N  
ANISOU 3768  NE1 TRP C 499     5051   4419   5265    196   -777   -137       N  
ATOM   3769  CE2 TRP C 499       5.399  14.379 -41.286  1.00 31.74           C  
ANISOU 3769  CE2 TRP C 499     4131   3515   4412    145   -757   -147       C  
ATOM   3770  CE3 TRP C 499       5.333  13.308 -43.452  1.00 22.16           C  
ANISOU 3770  CE3 TRP C 499     2889   2246   3284    102   -795   -196       C  
ATOM   3771  CZ2 TRP C 499       4.585  15.421 -41.723  1.00 19.94           C  
ANISOU 3771  CZ2 TRP C 499     2612   2046   2916    104   -706   -135       C  
ATOM   3772  CZ3 TRP C 499       4.525  14.342 -43.883  1.00 27.04           C  
ANISOU 3772  CZ3 TRP C 499     3482   2896   3895     60   -743   -179       C  
ATOM   3773  CH2 TRP C 499       4.160  15.385 -43.022  1.00 28.82           C  
ANISOU 3773  CH2 TRP C 499     3712   3159   4082     61   -700   -148       C  
ATOM   3774  N   GLY C 500       7.279   7.655 -41.916  1.00 35.85           N  
ANISOU 3774  N   GLY C 500     4765   3714   5143    268  -1053   -162       N  
ATOM   3775  CA  GLY C 500       7.924   6.558 -42.594  1.00 36.06           C  
ANISOU 3775  CA  GLY C 500     4796   3680   5224    300  -1122   -223       C  
ATOM   3776  C   GLY C 500       8.275   5.452 -41.622  1.00 38.90           C  
ANISOU 3776  C   GLY C 500     5203   3972   5603    349  -1176   -172       C  
ATOM   3777  O   GLY C 500       7.964   5.526 -40.430  1.00 42.64           O  
ANISOU 3777  O   GLY C 500     5706   4452   6043    355  -1156    -81       O  
ATOM   3778  N   PRO C 501       8.936   4.406 -42.106  1.00 39.02           N  
ANISOU 3778  N   PRO C 501     5228   3925   5672    390  -1246   -228       N  
ATOM   3779  CA  PRO C 501       9.259   3.275 -41.235  1.00 40.16           C  
ANISOU 3779  CA  PRO C 501     5421   3992   5846    439  -1305   -175       C  
ATOM   3780  C   PRO C 501      10.451   3.571 -40.342  1.00 45.48           C  
ANISOU 3780  C   PRO C 501     6101   4727   6453    512  -1318   -200       C  
ATOM   3781  O   PRO C 501      11.345   4.347 -40.686  1.00 48.26           O  
ANISOU 3781  O   PRO C 501     6415   5163   6760    537  -1307   -295       O  
ATOM   3782  CB  PRO C 501       9.586   2.157 -42.229  1.00 39.59           C  
ANISOU 3782  CB  PRO C 501     5351   3834   5858    462  -1379   -249       C  
ATOM   3783  CG  PRO C 501      10.184   2.888 -43.389  1.00 39.69           C  
ANISOU 3783  CG  PRO C 501     5308   3929   5842    466  -1363   -377       C  
ATOM   3784  CD  PRO C 501       9.451   4.211 -43.473  1.00 41.22           C  
ANISOU 3784  CD  PRO C 501     5472   4206   5983    400  -1277   -346       C  
ATOM   3785  N   GLY C 502      10.449   2.938 -39.173  1.00 47.72           N  
ANISOU 3785  N   GLY C 502     6430   4969   6731    545  -1342   -108       N  
ATOM   3786  CA  GLY C 502      11.598   2.965 -38.302  1.00 44.98           C  
ANISOU 3786  CA  GLY C 502     6094   4667   6329    625  -1372   -130       C  
ATOM   3787  C   GLY C 502      11.552   4.058 -37.258  1.00 52.10           C  
ANISOU 3787  C   GLY C 502     6992   5670   7135    626  -1315    -89       C  
ATOM   3788  O   GLY C 502      10.615   4.856 -37.179  1.00 48.12           O  
ANISOU 3788  O   GLY C 502     6476   5203   6603    567  -1249    -43       O  
ATOM   3789  N   PRO C 503      12.601   4.117 -36.427  1.00 49.95           N  
ANISOU 3789  N   PRO C 503     6727   5446   6808    700  -1345   -113       N  
ATOM   3790  CA  PRO C 503      12.608   5.013 -35.266  1.00 47.69           C  
ANISOU 3790  CA  PRO C 503     6442   5250   6427    715  -1305    -74       C  
ATOM   3791  C   PRO C 503      13.177   6.407 -35.505  1.00 47.47           C  
ANISOU 3791  C   PRO C 503     6363   5328   6344    709  -1268   -176       C  
ATOM   3792  O   PRO C 503      13.404   7.126 -34.527  1.00 49.67           O  
ANISOU 3792  O   PRO C 503     6641   5683   6548    735  -1250   -168       O  
ATOM   3793  CB  PRO C 503      13.498   4.242 -34.282  1.00 46.42           C  
ANISOU 3793  CB  PRO C 503     6314   5082   6240    804  -1369    -51       C  
ATOM   3794  CG  PRO C 503      14.488   3.551 -35.166  1.00 42.60           C  
ANISOU 3794  CG  PRO C 503     5816   4552   5817    845  -1434   -151       C  
ATOM   3795  CD  PRO C 503      13.749   3.195 -36.433  1.00 41.73           C  
ANISOU 3795  CD  PRO C 503     5697   4367   5793    780  -1425   -166       C  
ATOM   3796  N   THR C 504      13.419   6.816 -36.750  1.00 45.07           N  
ANISOU 3796  N   THR C 504     6015   5032   6077    675  -1259   -270       N  
ATOM   3797  CA  THR C 504      13.806   8.191 -37.044  1.00 48.48           C  
ANISOU 3797  CA  THR C 504     6396   5554   6469    654  -1217   -350       C  
ATOM   3798  C   THR C 504      12.703   8.952 -37.770  1.00 45.66           C  
ANISOU 3798  C   THR C 504     6020   5200   6128    570  -1151   -330       C  
ATOM   3799  O   THR C 504      12.960  10.019 -38.334  1.00 55.29           O  
ANISOU 3799  O   THR C 504     7195   6477   7337    542  -1119   -397       O  
ATOM   3800  CB  THR C 504      15.096   8.237 -37.867  1.00 49.57           C  
ANISOU 3800  CB  THR C 504     6488   5723   6625    684  -1253   -473       C  
ATOM   3801  OG1 THR C 504      14.885   7.603 -39.135  1.00 50.66           O  
ANISOU 3801  OG1 THR C 504     6614   5805   6829    660  -1265   -503       O  
ATOM   3802  CG2 THR C 504      16.231   7.541 -37.131  1.00 48.44           C  
ANISOU 3802  CG2 THR C 504     6358   5585   6463    773  -1320   -498       C  
ATOM   3803  N   GLN C 505      11.476   8.429 -37.760  1.00 38.84           N  
ANISOU 3803  N   GLN C 505     5188   4276   5295    530  -1132   -236       N  
ATOM   3804  CA  GLN C 505      10.384   9.004 -38.537  1.00 35.32           C  
ANISOU 3804  CA  GLN C 505     4722   3826   4871    454  -1077   -217       C  
ATOM   3805  C   GLN C 505       9.169   9.367 -37.692  1.00 36.87           C  
ANISOU 3805  C   GLN C 505     4941   4033   5036    423  -1025   -111       C  
ATOM   3806  O   GLN C 505       8.139   9.762 -38.251  1.00 43.28           O  
ANISOU 3806  O   GLN C 505     5738   4838   5868    362   -980    -83       O  
ATOM   3807  CB  GLN C 505       9.975   8.045 -39.659  1.00 37.66           C  
ANISOU 3807  CB  GLN C 505     5019   4043   5247    425  -1103   -221       C  
ATOM   3808  CG  GLN C 505      11.077   7.796 -40.680  1.00 43.80           C  
ANISOU 3808  CG  GLN C 505     5764   4825   6051    454  -1145   -336       C  
ATOM   3809  CD  GLN C 505      11.274   8.978 -41.608  1.00 51.08           C  
ANISOU 3809  CD  GLN C 505     6631   5820   6956    419  -1102   -410       C  
ATOM   3810  OE1 GLN C 505      10.428   9.868 -41.678  1.00 57.17           O  
ANISOU 3810  OE1 GLN C 505     7392   6618   7711    366  -1044   -375       O  
ATOM   3811  NE2 GLN C 505      12.398   8.999 -42.316  1.00 53.28           N  
ANISOU 3811  NE2 GLN C 505     6872   6134   7237    450  -1129   -510       N  
ATOM   3812  N   CYS C 506       9.255   9.252 -36.370  1.00 35.92           N  
ANISOU 3812  N   CYS C 506     4851   3936   4862    467  -1030    -53       N  
ATOM   3813  CA  CYS C 506       8.150   9.662 -35.515  1.00 33.65           C  
ANISOU 3813  CA  CYS C 506     4578   3678   4531    445   -977     43       C  
ATOM   3814  C   CYS C 506       7.982  11.176 -35.560  1.00 43.96           C  
ANISOU 3814  C   CYS C 506     5850   5060   5792    424   -923     -7       C  
ATOM   3815  O   CYS C 506       8.960  11.919 -35.675  1.00 50.38           O  
ANISOU 3815  O   CYS C 506     6638   5919   6584    447   -934   -102       O  
ATOM   3816  CB  CYS C 506       8.406   9.223 -34.075  1.00 35.80           C  
ANISOU 3816  CB  CYS C 506     4887   3973   4741    507   -996    110       C  
ATOM   3817  SG  CYS C 506       8.860   7.489 -33.851  1.00 53.68           S  
ANISOU 3817  SG  CYS C 506     7195   6146   7055    549  -1071    167       S  
ATOM   3818  N   VAL C 507       6.734  11.643 -35.466  1.00 52.12           N  
ANISOU 3818  N   VAL C 507     6879   6106   6817    380   -866     58       N  
ATOM   3819  CA  VAL C 507       6.531  13.077 -35.286  1.00 59.01           C  
ANISOU 3819  CA  VAL C 507     7727   7050   7644    371   -818     19       C  
ATOM   3820  C   VAL C 507       6.850  13.470 -33.848  1.00 57.95           C  
ANISOU 3820  C   VAL C 507     7610   6985   7423    433   -817     29       C  
ATOM   3821  O   VAL C 507       7.468  14.512 -33.596  1.00 60.38           O  
ANISOU 3821  O   VAL C 507     7900   7349   7695    456   -815    -51       O  
ATOM   3822  CB  VAL C 507       5.105  13.498 -35.707  1.00 54.75           C  
ANISOU 3822  CB  VAL C 507     7173   6506   7123    310   -759     76       C  
ATOM   3823  CG1 VAL C 507       4.717  12.841 -37.026  1.00 48.56           C  
ANISOU 3823  CG1 VAL C 507     6377   5652   6422    255   -769     78       C  
ATOM   3824  CG2 VAL C 507       4.070  13.204 -34.628  1.00 59.29           C  
ANISOU 3824  CG2 VAL C 507     7770   7103   7656    317   -727    190       C  
ATOM   3825  N   ASN C 508       6.476  12.624 -32.888  1.00 58.47           N  
ANISOU 3825  N   ASN C 508     7710   7050   7457    462   -823    127       N  
ATOM   3826  CA  ASN C 508       6.830  12.805 -31.491  1.00 67.07           C  
ANISOU 3826  CA  ASN C 508     8819   8211   8455    531   -830    143       C  
ATOM   3827  C   ASN C 508       7.381  11.497 -30.942  1.00 67.71           C  
ANISOU 3827  C   ASN C 508     8935   8258   8532    577   -883    199       C  
ATOM   3828  O   ASN C 508       7.100  10.410 -31.453  1.00 71.56           O  
ANISOU 3828  O   ASN C 508     9438   8664   9088    548   -903    258       O  
ATOM   3829  CB  ASN C 508       5.639  13.281 -30.645  1.00 75.72           C  
ANISOU 3829  CB  ASN C 508     9916   9366   9487    529   -770    224       C  
ATOM   3830  CG  ASN C 508       5.466  14.789 -30.680  1.00 86.79           C  
ANISOU 3830  CG  ASN C 508    11288  10828  10859    524   -732    145       C  
ATOM   3831  OD1 ASN C 508       6.444  15.536 -30.637  1.00 88.75           O  
ANISOU 3831  OD1 ASN C 508    11523  11106  11091    553   -757     39       O  
ATOM   3832  ND2 ASN C 508       4.220  15.244 -30.749  1.00 89.28           N  
ANISOU 3832  ND2 ASN C 508    11590  11160  11172    487   -673    197       N  
ATOM   3833  N   CYS C 509       8.168  11.626 -29.880  1.00 61.31           N  
ANISOU 3833  N   CYS C 509     8137   7511   7645    651   -911    179       N  
ATOM   3834  CA  CYS C 509       8.956  10.534 -29.325  1.00 61.78           C  
ANISOU 3834  CA  CYS C 509     8229   7550   7694    709   -971    211       C  
ATOM   3835  C   CYS C 509       8.411  10.212 -27.941  1.00 61.48           C  
ANISOU 3835  C   CYS C 509     8221   7570   7569    753   -954    329       C  
ATOM   3836  O   CYS C 509       8.358  11.091 -27.074  1.00 64.03           O  
ANISOU 3836  O   CYS C 509     8536   7992   7800    791   -929    308       O  
ATOM   3837  CB  CYS C 509      10.426  10.946 -29.263  1.00 74.15           C  
ANISOU 3837  CB  CYS C 509     9780   9154   9239    764  -1024     85       C  
ATOM   3838  SG  CYS C 509      11.689   9.662 -29.304  1.00 89.19           S  
ANISOU 3838  SG  CYS C 509    11705  11004  11177    824  -1112     70       S  
ATOM   3839  N   SER C 510       8.000   8.958 -27.736  1.00 60.67           N  
ANISOU 3839  N   SER C 510     8150   7406   7495    749   -968    453       N  
ATOM   3840  CA  SER C 510       7.372   8.587 -26.474  1.00 61.63           C  
ANISOU 3840  CA  SER C 510     8297   7583   7536    782   -944    587       C  
ATOM   3841  C   SER C 510       8.385   8.429 -25.346  1.00 65.56           C  
ANISOU 3841  C   SER C 510     8817   8150   7943    881   -992    578       C  
ATOM   3842  O   SER C 510       8.042   8.650 -24.180  1.00 65.93           O  
ANISOU 3842  O   SER C 510     8871   8294   7883    927   -965    645       O  
ATOM   3843  CB  SER C 510       6.567   7.298 -26.645  1.00 62.28           C  
ANISOU 3843  CB  SER C 510     8403   7570   7690    737   -943    733       C  
ATOM   3844  OG  SER C 510       7.378   6.246 -27.133  1.00 64.94           O  
ANISOU 3844  OG  SER C 510     8764   7805   8107    750  -1016    719       O  
ATOM   3845  N   GLN C 511       9.624   8.052 -25.659  1.00 69.32           N  
ANISOU 3845  N   GLN C 511     9298   8587   8453    920  -1062    497       N  
ATOM   3846  CA  GLN C 511      10.645   7.961 -24.622  1.00 70.70           C  
ANISOU 3846  CA  GLN C 511     9489   8834   8540   1018  -1112    476       C  
ATOM   3847  C   GLN C 511      11.745   8.991 -24.860  1.00 65.88           C  
ANISOU 3847  C   GLN C 511     8844   8277   7912   1046  -1140    302       C  
ATOM   3848  O   GLN C 511      11.540  10.179 -24.588  1.00 71.34           O  
ANISOU 3848  O   GLN C 511     9509   9051   8546   1044  -1102    239       O  
ATOM   3849  CB  GLN C 511      11.212   6.542 -24.541  1.00 75.57           C  
ANISOU 3849  CB  GLN C 511    10142   9368   9201   1055  -1179    545       C  
ATOM   3850  CG  GLN C 511      10.153   5.480 -24.265  1.00 80.33           C  
ANISOU 3850  CG  GLN C 511    10780   9909   9833   1022  -1157    728       C  
ATOM   3851  CD  GLN C 511       9.315   5.771 -23.027  1.00 84.87           C  
ANISOU 3851  CD  GLN C 511    11362  10594  10292   1044  -1101    844       C  
ATOM   3852  OE1 GLN C 511       9.809   6.309 -22.035  1.00 85.32           O  
ANISOU 3852  OE1 GLN C 511    11418  10768  10231   1121  -1108    814       O  
ATOM   3853  NE2 GLN C 511       8.035   5.419 -23.086  1.00 85.78           N  
ANISOU 3853  NE2 GLN C 511    11480  10675  10437    977  -1045    974       N  
ATOM   3854  N   PHE C 512      12.904   8.575 -25.365  1.00 55.95           N  
ANISOU 3854  N   PHE C 512     7581   6974   6705   1073  -1205    221       N  
ATOM   3855  CA  PHE C 512      14.033   9.488 -25.452  1.00 52.36           C  
ANISOU 3855  CA  PHE C 512     7088   6579   6227   1105  -1236     65       C  
ATOM   3856  C   PHE C 512      14.540   9.597 -26.882  1.00 53.51           C  
ANISOU 3856  C   PHE C 512     7199   6653   6478   1052  -1250    -37       C  
ATOM   3857  O   PHE C 512      14.234   8.769 -27.741  1.00 55.46           O  
ANISOU 3857  O   PHE C 512     7458   6803   6812   1011  -1253      3       O  
ATOM   3858  CB  PHE C 512      15.166   9.052 -24.518  1.00 53.36           C  
ANISOU 3858  CB  PHE C 512     7227   6758   6288   1206  -1307     48       C  
ATOM   3859  CG  PHE C 512      14.772   9.038 -23.073  1.00 53.26           C  
ANISOU 3859  CG  PHE C 512     7243   6837   6154   1269  -1297    139       C  
ATOM   3860  CD1 PHE C 512      14.284   7.883 -22.488  1.00 46.83           C  
ANISOU 3860  CD1 PHE C 512     6476   5993   5323   1293  -1302    296       C  
ATOM   3861  CD2 PHE C 512      14.866  10.187 -22.304  1.00 50.39           C  
ANISOU 3861  CD2 PHE C 512     6859   6593   5695   1302  -1281     69       C  
ATOM   3862  CE1 PHE C 512      13.909   7.867 -21.160  1.00 47.41           C  
ANISOU 3862  CE1 PHE C 512     6573   6165   5277   1353  -1287    389       C  
ATOM   3863  CE2 PHE C 512      14.492  10.179 -20.973  1.00 49.94           C  
ANISOU 3863  CE2 PHE C 512     6825   6634   5515   1367  -1270    148       C  
ATOM   3864  CZ  PHE C 512      14.013   9.016 -20.401  1.00 53.20           C  
ANISOU 3864  CZ  PHE C 512     7283   7028   5903   1392  -1271    313       C  
ATOM   3865  N   LEU C 513      15.319  10.647 -27.128  1.00 52.70           N  
ANISOU 3865  N   LEU C 513     7052   6604   6368   1053  -1257   -172       N  
ATOM   3866  CA  LEU C 513      15.893  10.923 -28.438  1.00 54.93           C  
ANISOU 3866  CA  LEU C 513     7291   6843   6736   1006  -1265   -275       C  
ATOM   3867  C   LEU C 513      17.411  10.907 -28.337  1.00 53.22           C  
ANISOU 3867  C   LEU C 513     7045   6663   6512   1068  -1333   -381       C  
ATOM   3868  O   LEU C 513      17.991  11.634 -27.523  1.00 54.79           O  
ANISOU 3868  O   LEU C 513     7226   6947   6643   1111  -1351   -441       O  
ATOM   3869  CB  LEU C 513      15.412  12.270 -28.977  1.00 56.54           C  
ANISOU 3869  CB  LEU C 513     7458   7072   6954    937  -1207   -335       C  
ATOM   3870  CG  LEU C 513      14.164  12.263 -29.860  1.00 61.86           C  
ANISOU 3870  CG  LEU C 513     8136   7682   7686    853  -1147   -273       C  
ATOM   3871  CD1 LEU C 513      13.558  13.654 -29.954  1.00 60.55           C  
ANISOU 3871  CD1 LEU C 513     7944   7557   7505    806  -1089   -310       C  
ATOM   3872  CD2 LEU C 513      14.508  11.733 -31.244  1.00 62.94           C  
ANISOU 3872  CD2 LEU C 513     8253   7743   7917    814  -1163   -312       C  
ATOM   3873  N   ARG C 514      18.048  10.073 -29.154  1.00 48.31           N  
ANISOU 3873  N   ARG C 514     6415   5981   5958   1074  -1374   -408       N  
ATOM   3874  CA  ARG C 514      19.489  10.135 -29.369  1.00 45.85           C  
ANISOU 3874  CA  ARG C 514     6060   5704   5658   1119  -1431   -523       C  
ATOM   3875  C   ARG C 514      19.694  10.550 -30.818  1.00 49.09           C  
ANISOU 3875  C   ARG C 514     6418   6085   6147   1050  -1409   -604       C  
ATOM   3876  O   ARG C 514      19.288   9.830 -31.739  1.00 54.24           O  
ANISOU 3876  O   ARG C 514     7083   6661   6866   1018  -1401   -573       O  
ATOM   3877  CB  ARG C 514      20.175   8.806 -29.059  1.00 47.80           C  
ANISOU 3877  CB  ARG C 514     6335   5918   5909   1199  -1503   -494       C  
ATOM   3878  CG  ARG C 514      21.688   8.868 -29.229  1.00 46.67           C  
ANISOU 3878  CG  ARG C 514     6141   5821   5772   1252  -1563   -616       C  
ATOM   3879  CD  ARG C 514      22.417   7.790 -28.437  1.00 43.64           C  
ANISOU 3879  CD  ARG C 514     5787   5436   5358   1356  -1640   -586       C  
ATOM   3880  NE  ARG C 514      21.724   6.505 -28.469  1.00 55.47           N  
ANISOU 3880  NE  ARG C 514     7349   6834   6893   1366  -1650   -466       N  
ATOM   3881  CZ  ARG C 514      21.358   5.828 -27.386  1.00 55.64           C  
ANISOU 3881  CZ  ARG C 514     7429   6848   6864   1418  -1669   -351       C  
ATOM   3882  NH1 ARG C 514      21.628   6.307 -26.180  1.00 53.01           N  
ANISOU 3882  NH1 ARG C 514     7099   6612   6430   1472  -1681   -346       N  
ATOM   3883  NH2 ARG C 514      20.730   4.666 -27.507  1.00 56.61           N  
ANISOU 3883  NH2 ARG C 514     7605   6867   7037   1416  -1680   -241       N  
ATOM   3884  N   GLY C 515      20.310  11.711 -31.016  1.00 54.85           N  
ANISOU 3884  N   GLY C 515     7091   6879   6872   1028  -1399   -706       N  
ATOM   3885  CA  GLY C 515      20.303  12.336 -32.320  1.00 55.81           C  
ANISOU 3885  CA  GLY C 515     7162   6985   7058    952  -1362   -765       C  
ATOM   3886  C   GLY C 515      18.881  12.590 -32.771  1.00 61.17           C  
ANISOU 3886  C   GLY C 515     7867   7615   7758    878  -1294   -689       C  
ATOM   3887  O   GLY C 515      18.182  13.436 -32.208  1.00 67.58           O  
ANISOU 3887  O   GLY C 515     8689   8455   8533    854  -1254   -664       O  
ATOM   3888  N   GLN C 516      18.442  11.846 -33.786  1.00 61.77           N  
ANISOU 3888  N   GLN C 516     7952   7623   7895    845  -1284   -658       N  
ATOM   3889  CA  GLN C 516      17.063  11.875 -34.259  1.00 68.73           C  
ANISOU 3889  CA  GLN C 516     8859   8452   8802    779  -1227   -580       C  
ATOM   3890  C   GLN C 516      16.417  10.496 -34.225  1.00 66.36           C  
ANISOU 3890  C   GLN C 516     8614   8073   8529    793  -1245   -487       C  
ATOM   3891  O   GLN C 516      15.331  10.314 -34.790  1.00 67.14           O  
ANISOU 3891  O   GLN C 516     8728   8118   8663    737  -1208   -427       O  
ATOM   3892  CB  GLN C 516      16.994  12.465 -35.671  1.00 81.15           C  
ANISOU 3892  CB  GLN C 516    10384  10019  10432    708  -1191   -634       C  
ATOM   3893  CG  GLN C 516      17.831  13.720 -35.825  1.00 93.58           C  
ANISOU 3893  CG  GLN C 516    11897  11662  11997    692  -1182   -729       C  
ATOM   3894  CD  GLN C 516      18.515  13.829 -37.176  1.00100.82           C  
ANISOU 3894  CD  GLN C 516    12754  12587  12966    662  -1182   -802       C  
ATOM   3895  OE1 GLN C 516      19.093  12.862 -37.676  1.00 99.30           O  
ANISOU 3895  OE1 GLN C 516    12555  12377  12797    697  -1221   -827       O  
ATOM   3896  NE2 GLN C 516      18.483  15.025 -37.757  1.00103.18           N  
ANISOU 3896  NE2 GLN C 516    13007  12918  13280    601  -1139   -837       N  
ATOM   3897  N   GLU C 517      17.059   9.520 -33.587  1.00 62.59           N  
ANISOU 3897  N   GLU C 517     8163   7581   8037    867  -1306   -471       N  
ATOM   3898  CA  GLU C 517      16.477   8.199 -33.403  1.00 56.50           C  
ANISOU 3898  CA  GLU C 517     7447   6726   7294    885  -1330   -372       C  
ATOM   3899  C   GLU C 517      15.790   8.134 -32.045  1.00 55.49           C  
ANISOU 3899  C   GLU C 517     7366   6617   7100    907  -1315   -262       C  
ATOM   3900  O   GLU C 517      16.339   8.598 -31.038  1.00 55.66           O  
ANISOU 3900  O   GLU C 517     7386   6715   7048    959  -1328   -280       O  
ATOM   3901  CB  GLU C 517      17.546   7.110 -33.513  1.00 53.10           C  
ANISOU 3901  CB  GLU C 517     7021   6261   6892    957  -1408   -411       C  
ATOM   3902  CG  GLU C 517      17.141   5.781 -32.888  1.00 57.21           C  
ANISOU 3902  CG  GLU C 517     7606   6701   7429    996  -1446   -299       C  
ATOM   3903  CD  GLU C 517      17.970   4.616 -33.392  1.00 68.25           C  
ANISOU 3903  CD  GLU C 517     9010   8034   8889   1052  -1521   -340       C  
ATOM   3904  OE1 GLU C 517      17.772   3.486 -32.896  1.00 69.05           O  
ANISOU 3904  OE1 GLU C 517     9162   8059   9012   1090  -1564   -253       O  
ATOM   3905  OE2 GLU C 517      18.812   4.830 -34.288  1.00 73.09           O  
ANISOU 3905  OE2 GLU C 517     9573   8671   9528   1059  -1538   -458       O  
ATOM   3906  N   CYS C 518      14.582   7.574 -32.029  1.00 53.72           N  
ANISOU 3906  N   CYS C 518     7179   6330   6902    867  -1286   -149       N  
ATOM   3907  CA  CYS C 518      13.871   7.347 -30.781  1.00 54.02           C  
ANISOU 3907  CA  CYS C 518     7260   6386   6879    887  -1270    -28       C  
ATOM   3908  C   CYS C 518      14.376   6.070 -30.124  1.00 51.05           C  
ANISOU 3908  C   CYS C 518     6927   5966   6504    959  -1336     35       C  
ATOM   3909  O   CYS C 518      14.481   5.023 -30.772  1.00 55.72           O  
ANISOU 3909  O   CYS C 518     7534   6460   7177    958  -1377     46       O  
ATOM   3910  CB  CYS C 518      12.362   7.283 -31.025  1.00 66.60           C  
ANISOU 3910  CB  CYS C 518     8869   7936   8502    811  -1210     74       C  
ATOM   3911  SG  CYS C 518      11.671   8.943 -31.202  1.00 85.49           S  
ANISOU 3911  SG  CYS C 518    11221  10408  10854    751  -1128     29       S  
ATOM   3912  N   VAL C 519      14.710   6.172 -28.839  1.00 44.71           N  
ANISOU 3912  N   VAL C 519     6143   5236   5610   1026  -1350     71       N  
ATOM   3913  CA  VAL C 519      15.262   5.079 -28.055  1.00 44.62           C  
ANISOU 3913  CA  VAL C 519     6171   5201   5583   1106  -1415    136       C  
ATOM   3914  C   VAL C 519      14.487   4.979 -26.748  1.00 47.91           C  
ANISOU 3914  C   VAL C 519     6625   5664   5915   1126  -1385    276       C  
ATOM   3915  O   VAL C 519      13.845   5.935 -26.299  1.00 50.72           O  
ANISOU 3915  O   VAL C 519     6968   6101   6203   1101  -1325    287       O  
ATOM   3916  CB  VAL C 519      16.770   5.264 -27.777  1.00 46.76           C  
ANISOU 3916  CB  VAL C 519     6418   5533   5815   1189  -1477     22       C  
ATOM   3917  CG1 VAL C 519      17.559   5.245 -29.079  1.00 43.92           C  
ANISOU 3917  CG1 VAL C 519     6018   5133   5538   1174  -1506   -107       C  
ATOM   3918  CG2 VAL C 519      17.011   6.563 -27.023  1.00 53.76           C  
ANISOU 3918  CG2 VAL C 519     7276   6550   6600   1208  -1449    -38       C  
ATOM   3919  N   GLU C 520      14.565   3.797 -26.133  1.00 53.49           N  
ANISOU 3919  N   GLU C 520     7377   6320   6626   1175  -1431    385       N  
ATOM   3920  CA  GLU C 520      13.811   3.527 -24.914  1.00 62.89           C  
ANISOU 3920  CA  GLU C 520     8604   7552   7739   1195  -1403    540       C  
ATOM   3921  C   GLU C 520      14.469   4.156 -23.692  1.00 63.49           C  
ANISOU 3921  C   GLU C 520     8676   7768   7679   1282  -1415    513       C  
ATOM   3922  O   GLU C 520      13.775   4.688 -22.818  1.00 68.75           O  
ANISOU 3922  O   GLU C 520     9344   8525   8250   1284  -1363    580       O  
ATOM   3923  CB  GLU C 520      13.651   2.017 -24.725  1.00 71.60           C  
ANISOU 3923  CB  GLU C 520     9757   8543   8904   1212  -1449    677       C  
ATOM   3924  CG  GLU C 520      12.223   1.517 -24.893  1.00 83.66           C  
ANISOU 3924  CG  GLU C 520    11303   9994  10489   1127  -1398    821       C  
ATOM   3925  CD  GLU C 520      11.343   1.853 -23.704  1.00 93.24           C  
ANISOU 3925  CD  GLU C 520    12526  11309  11594   1129  -1336    954       C  
ATOM   3926  OE1 GLU C 520      10.121   2.027 -23.893  1.00 91.25           O  
ANISOU 3926  OE1 GLU C 520    12263  11045  11361   1049  -1268   1029       O  
ATOM   3927  OE2 GLU C 520      11.876   1.936 -22.578  1.00 99.38           O  
ANISOU 3927  OE2 GLU C 520    13316  12182  12260   1215  -1354    982       O  
ATOM   3928  N   GLU C 521      15.796   4.102 -23.605  1.00 59.04           N  
ANISOU 3928  N   GLU C 521     8102   7230   7102   1357  -1484    413       N  
ATOM   3929  CA  GLU C 521      16.506   4.746 -22.510  1.00 68.20           C  
ANISOU 3929  CA  GLU C 521     9251   8525   8136   1440  -1504    366       C  
ATOM   3930  C   GLU C 521      17.883   5.184 -22.989  1.00 64.30           C  
ANISOU 3930  C   GLU C 521     8714   8057   7660   1477  -1560    191       C  
ATOM   3931  O   GLU C 521      18.422   4.657 -23.966  1.00 65.06           O  
ANISOU 3931  O   GLU C 521     8800   8064   7855   1465  -1598    134       O  
ATOM   3932  CB  GLU C 521      16.636   3.824 -21.290  1.00 81.79           C  
ANISOU 3932  CB  GLU C 521    11019  10271   9784   1527  -1544    500       C  
ATOM   3933  CG  GLU C 521      16.740   4.578 -19.967  1.00 95.60           C  
ANISOU 3933  CG  GLU C 521    12764  12183  11378   1596  -1532    502       C  
ATOM   3934  CD  GLU C 521      17.356   3.751 -18.853  1.00105.03           C  
ANISOU 3934  CD  GLU C 521    13994  13418  12494   1705  -1595    587       C  
ATOM   3935  OE1 GLU C 521      17.061   2.540 -18.771  1.00105.33           O  
ANISOU 3935  OE1 GLU C 521    14077  13366  12579   1710  -1615    730       O  
ATOM   3936  OE2 GLU C 521      18.132   4.317 -18.053  1.00107.18           O  
ANISOU 3936  OE2 GLU C 521    14249  13814  12660   1786  -1628    511       O  
ATOM   3937  N   CYS C 522      18.441   6.169 -22.292  1.00 60.47           N  
ANISOU 3937  N   CYS C 522     8200   7697   7079   1523  -1565    104       N  
ATOM   3938  CA  CYS C 522      19.800   6.623 -22.538  1.00 59.00           C  
ANISOU 3938  CA  CYS C 522     7967   7553   6896   1565  -1621    -55       C  
ATOM   3939  C   CYS C 522      20.781   5.835 -21.675  1.00 55.20           C  
ANISOU 3939  C   CYS C 522     7506   7106   6363   1678  -1704    -35       C  
ATOM   3940  O   CYS C 522      20.407   5.188 -20.694  1.00 52.48           O  
ANISOU 3940  O   CYS C 522     7209   6780   5951   1730  -1712     97       O  
ATOM   3941  CB  CYS C 522      19.943   8.120 -22.249  1.00 58.99           C  
ANISOU 3941  CB  CYS C 522     7920   7663   6832   1553  -1593   -170       C  
ATOM   3942  SG  CYS C 522      18.713   9.206 -23.017  1.00 69.71           S  
ANISOU 3942  SG  CYS C 522     9257   9000   8229   1433  -1495   -184       S  
ATOM   3943  N   ARG C 523      22.058   5.908 -22.050  1.00 50.98           N  
ANISOU 3943  N   ARG C 523     6929   6585   5856   1718  -1765   -166       N  
ATOM   3944  CA  ARG C 523      23.116   5.193 -21.338  1.00 55.18           C  
ANISOU 3944  CA  ARG C 523     7465   7145   6357   1796  -1815   -169       C  
ATOM   3945  C   ARG C 523      23.533   6.000 -20.107  1.00 60.84           C  
ANISOU 3945  C   ARG C 523     8163   8005   6950   1845  -1812   -213       C  
ATOM   3946  O   ARG C 523      24.639   6.534 -20.005  1.00 63.21           O  
ANISOU 3946  O   ARG C 523     8412   8369   7236   1869  -1837   -345       O  
ATOM   3947  CB  ARG C 523      24.294   4.930 -22.267  1.00 54.47           C  
ANISOU 3947  CB  ARG C 523     7330   7012   6353   1799  -1855   -293       C  
ATOM   3948  CG  ARG C 523      23.879   4.530 -23.671  1.00 53.55           C  
ANISOU 3948  CG  ARG C 523     7214   6775   6358   1738  -1850   -297       C  
ATOM   3949  CD  ARG C 523      25.071   4.169 -24.543  1.00 57.94           C  
ANISOU 3949  CD  ARG C 523     7725   7300   6990   1750  -1888   -415       C  
ATOM   3950  NE  ARG C 523      24.643   3.759 -25.878  1.00 61.90           N  
ANISOU 3950  NE  ARG C 523     8226   7693   7601   1697  -1882   -421       N  
ATOM   3951  CZ  ARG C 523      24.917   4.430 -26.992  1.00 63.82           C  
ANISOU 3951  CZ  ARG C 523     8410   7942   7897   1648  -1870   -537       C  
ATOM   3952  NH1 ARG C 523      25.631   5.547 -26.938  1.00 64.88           N  
ANISOU 3952  NH1 ARG C 523     8479   8179   7993   1640  -1860   -653       N  
ATOM   3953  NH2 ARG C 523      24.480   3.983 -28.161  1.00 59.62           N  
ANISOU 3953  NH2 ARG C 523     7880   7314   7458   1605  -1866   -537       N  
ATOM   3954  N   VAL C 524      22.605   6.089 -19.154  1.00 57.92           N  
ANISOU 3954  N   VAL C 524     7831   7686   6488   1860  -1777    -99       N  
ATOM   3955  CA  VAL C 524      22.909   6.759 -17.896  1.00 55.47           C  
ANISOU 3955  CA  VAL C 524     7509   7515   6054   1913  -1773   -131       C  
ATOM   3956  C   VAL C 524      23.609   5.808 -16.937  1.00 57.67           C  
ANISOU 3956  C   VAL C 524     7808   7820   6282   1991  -1811    -68       C  
ATOM   3957  O   VAL C 524      24.584   6.180 -16.276  1.00 63.59           O  
ANISOU 3957  O   VAL C 524     8527   8659   6975   2043  -1839   -160       O  
ATOM   3958  CB  VAL C 524      21.625   7.343 -17.282  1.00 53.79           C  
ANISOU 3958  CB  VAL C 524     7320   7364   5753   1898  -1716    -48       C  
ATOM   3959  CG1 VAL C 524      21.945   8.092 -16.000  1.00 48.96           C  
ANISOU 3959  CG1 VAL C 524     6690   6900   5012   1956  -1711    -99       C  
ATOM   3960  CG2 VAL C 524      20.932   8.261 -18.277  1.00 55.47           C  
ANISOU 3960  CG2 VAL C 524     7512   7544   6021   1822  -1682   -110       C  
ATOM   3961  N   LEU C 525      23.134   4.570 -16.854  1.00 63.08           N  
ANISOU 3961  N   LEU C 525     8547   8427   6996   1999  -1814     90       N  
ATOM   3962  CA  LEU C 525      23.677   3.574 -15.940  1.00 67.13           C  
ANISOU 3962  CA  LEU C 525     9085   8955   7467   2070  -1849    176       C  
ATOM   3963  C   LEU C 525      24.411   2.445 -16.644  1.00 64.88           C  
ANISOU 3963  C   LEU C 525     8806   8552   7292   2081  -1900    176       C  
ATOM   3964  O   LEU C 525      25.443   1.988 -16.149  1.00 62.39           O  
ANISOU 3964  O   LEU C 525     8482   8266   6957   2146  -1947    148       O  
ATOM   3965  CB  LEU C 525      22.550   2.992 -15.078  1.00 64.44           C  
ANISOU 3965  CB  LEU C 525     8797   8625   7063   2075  -1811    377       C  
ATOM   3966  CG  LEU C 525      21.732   4.055 -14.341  1.00 60.01           C  
ANISOU 3966  CG  LEU C 525     8229   8187   6383   2069  -1754    385       C  
ATOM   3967  CD1 LEU C 525      20.570   3.434 -13.581  1.00 59.30           C  
ANISOU 3967  CD1 LEU C 525     8187   8108   6237   2066  -1709    593       C  
ATOM   3968  CD2 LEU C 525      22.625   4.856 -13.407  1.00 60.41           C  
ANISOU 3968  CD2 LEU C 525     8243   8382   6327   2134  -1773    263       C  
ATOM   3969  N   GLN C 526      23.912   1.987 -17.791  1.00 67.83           N  
ANISOU 3969  N   GLN C 526     9195   8795   7783   2022  -1894    201       N  
ATOM   3970  CA  GLN C 526      24.527   0.900 -18.540  1.00 69.88           C  
ANISOU 3970  CA  GLN C 526     9462   8936   8155   2030  -1940    194       C  
ATOM   3971  C   GLN C 526      24.783   1.362 -19.966  1.00 74.21           C  
ANISOU 3971  C   GLN C 526     9970   9426   8802   1976  -1942     51       C  
ATOM   3972  O   GLN C 526      23.896   1.938 -20.602  1.00 78.48           O  
ANISOU 3972  O   GLN C 526    10508   9940   9370   1908  -1901     50       O  
ATOM   3973  CB  GLN C 526      23.630  -0.343 -18.548  1.00 72.82           C  
ANISOU 3973  CB  GLN C 526     9895   9187   8588   2011  -1935    379       C  
ATOM   3974  CG  GLN C 526      22.966  -0.649 -17.218  1.00 81.38           C  
ANISOU 3974  CG  GLN C 526    11018  10331   9574   2039  -1911    553       C  
ATOM   3975  CD  GLN C 526      21.587  -1.256 -17.389  1.00 85.86           C  
ANISOU 3975  CD  GLN C 526    11630  10800  10192   1977  -1871    727       C  
ATOM   3976  OE1 GLN C 526      20.650  -0.580 -17.815  1.00 90.07           O  
ANISOU 3976  OE1 GLN C 526    12163  11333  10728   1915  -1823    729       O  
ATOM   3977  NE2 GLN C 526      21.456  -2.536 -17.060  1.00 81.82           N  
ANISOU 3977  NE2 GLN C 526    11157  10205   9728   1992  -1892    876       N  
ATOM   3978  N   GLY C 527      25.991   1.108 -20.466  1.00 74.39           N  
ANISOU 3978  N   GLY C 527     9957   9436   8874   2006  -1986    -66       N  
ATOM   3979  CA  GLY C 527      26.302   1.405 -21.850  1.00 71.49           C  
ANISOU 3979  CA  GLY C 527     9547   9015   8601   1958  -1988   -194       C  
ATOM   3980  C   GLY C 527      27.463   2.354 -22.052  1.00 71.93           C  
ANISOU 3980  C   GLY C 527     9529   9167   8635   1969  -1999   -370       C  
ATOM   3981  O   GLY C 527      27.842   3.089 -21.137  1.00 76.13           O  
ANISOU 3981  O   GLY C 527    10040   9812   9075   2000  -1996   -407       O  
ATOM   3982  N   LEU C 528      28.038   2.342 -23.251  1.00 67.58           N  
ANISOU 3982  N   LEU C 528     8935   8572   8171   1944  -2010   -481       N  
ATOM   3983  CA  LEU C 528      29.152   3.224 -23.589  1.00 63.80           C  
ANISOU 3983  CA  LEU C 528     8378   8176   7687   1943  -2015   -645       C  
ATOM   3984  C   LEU C 528      29.012   3.777 -25.007  1.00 69.47           C  
ANISOU 3984  C   LEU C 528     9049   8860   8486   1868  -1987   -734       C  
ATOM   3985  O   LEU C 528      28.684   3.034 -25.935  1.00 77.38           O  
ANISOU 3985  O   LEU C 528    10068   9762   9570   1848  -1992   -711       O  
ATOM   3986  CB  LEU C 528      30.488   2.492 -23.443  1.00 56.69           C  
ANISOU 3986  CB  LEU C 528     7458   7288   6795   2016  -2066   -703       C  
ATOM   3987  CG  LEU C 528      30.831   1.972 -22.034  1.00 59.28           C  
ANISOU 3987  CG  LEU C 528     7822   7662   7039   2097  -2098   -629       C  
ATOM   3988  CD1 LEU C 528      31.546   0.627 -22.094  1.00 58.10           C  
ANISOU 3988  CD1 LEU C 528     7694   7449   6933   2162  -2151   -606       C  
ATOM   3989  CD2 LEU C 528      31.659   2.990 -21.265  1.00 59.62           C  
ANISOU 3989  CD2 LEU C 528     7812   7839   7001   2122  -2100   -727       C  
ATOM   3990  N   PRO C 529      29.251   5.089 -25.182  1.00 70.12           N  
ANISOU 3990  N   PRO C 529     9069   9023   8550   1824  -1958   -834       N  
ATOM   3991  CA  PRO C 529      29.627   6.041 -24.128  1.00 72.42           C  
ANISOU 3991  CA  PRO C 529     9336   9426   8754   1843  -1952   -875       C  
ATOM   3992  C   PRO C 529      28.457   6.392 -23.211  1.00 69.51           C  
ANISOU 3992  C   PRO C 529     9019   9080   8310   1837  -1927   -771       C  
ATOM   3993  O   PRO C 529      27.332   6.532 -23.694  1.00 66.59           O  
ANISOU 3993  O   PRO C 529     8675   8658   7966   1782  -1895   -710       O  
ATOM   3994  CB  PRO C 529      30.086   7.282 -24.912  1.00 68.44           C  
ANISOU 3994  CB  PRO C 529     8748   8968   8286   1777  -1922  -1009       C  
ATOM   3995  CG  PRO C 529      30.204   6.843 -26.346  1.00 66.31           C  
ANISOU 3995  CG  PRO C 529     8454   8628   8114   1740  -1918  -1044       C  
ATOM   3996  CD  PRO C 529      29.219   5.734 -26.505  1.00 66.69           C  
ANISOU 3996  CD  PRO C 529     8579   8574   8188   1750  -1928   -921       C  
ATOM   3997  N   ARG C 530      28.722   6.511 -21.911  1.00 63.11           N  
ANISOU 3997  N   ARG C 530     8224   8350   7406   1894  -1940   -750       N  
ATOM   3998  CA  ARG C 530      27.677   6.895 -20.976  1.00 55.89           C  
ANISOU 3998  CA  ARG C 530     7352   7477   6405   1896  -1912   -659       C  
ATOM   3999  C   ARG C 530      27.148   8.279 -21.327  1.00 55.57           C  
ANISOU 3999  C   ARG C 530     7276   7474   6365   1825  -1870   -729       C  
ATOM   4000  O   ARG C 530      27.831   9.098 -21.947  1.00 57.77           O  
ANISOU 4000  O   ARG C 530     7488   7774   6690   1786  -1865   -858       O  
ATOM   4001  CB  ARG C 530      28.199   6.883 -19.540  1.00 51.06           C  
ANISOU 4001  CB  ARG C 530     6750   6963   5688   1974  -1934   -648       C  
ATOM   4002  CG  ARG C 530      28.870   5.589 -19.138  1.00 58.02           C  
ANISOU 4002  CG  ARG C 530     7659   7817   6567   2047  -1981   -589       C  
ATOM   4003  CD  ARG C 530      27.947   4.651 -18.373  1.00 63.46           C  
ANISOU 4003  CD  ARG C 530     8425   8477   7208   2079  -1976   -407       C  
ATOM   4004  NE  ARG C 530      28.622   3.385 -18.096  1.00 71.03           N  
ANISOU 4004  NE  ARG C 530     9409   9396   8184   2143  -2024   -351       N  
ATOM   4005  CZ  ARG C 530      28.469   2.674 -16.983  1.00 75.09           C  
ANISOU 4005  CZ  ARG C 530     9969   9935   8627   2203  -2038   -227       C  
ATOM   4006  NH1 ARG C 530      27.657   3.100 -16.026  1.00 82.41           N  
ANISOU 4006  NH1 ARG C 530    10920  10936   9455   2208  -2003   -145       N  
ATOM   4007  NH2 ARG C 530      29.133   1.536 -16.826  1.00 76.86           N  
ANISOU 4007  NH2 ARG C 530    10211  10114   8878   2259  -2085   -183       N  
ATOM   4008  N   GLU C 531      25.908   8.536 -20.927  1.00 56.55           N  
ANISOU 4008  N   GLU C 531     7442   7603   6440   1808  -1835   -637       N  
ATOM   4009  CA  GLU C 531      25.209   9.743 -21.330  1.00 54.73           C  
ANISOU 4009  CA  GLU C 531     7188   7392   6216   1740  -1794   -686       C  
ATOM   4010  C   GLU C 531      24.527  10.384 -20.130  1.00 56.93           C  
ANISOU 4010  C   GLU C 531     7490   7759   6380   1766  -1770   -647       C  
ATOM   4011  O   GLU C 531      24.398   9.788 -19.057  1.00 57.34           O  
ANISOU 4011  O   GLU C 531     7585   7853   6349   1831  -1777   -557       O  
ATOM   4012  CB  GLU C 531      24.173   9.443 -22.425  1.00 53.22           C  
ANISOU 4012  CB  GLU C 531     7020   7100   6101   1677  -1770   -617       C  
ATOM   4013  CG  GLU C 531      24.590   8.354 -23.401  1.00 64.72           C  
ANISOU 4013  CG  GLU C 531     8479   8456   7655   1673  -1796   -605       C  
ATOM   4014  CD  GLU C 531      23.789   8.381 -24.683  1.00 70.61           C  
ANISOU 4014  CD  GLU C 531     9224   9109   8497   1579  -1747   -589       C  
ATOM   4015  OE1 GLU C 531      22.773   7.661 -24.761  1.00 70.65           O  
ANISOU 4015  OE1 GLU C 531     9284   9037   8522   1554  -1715   -464       O  
ATOM   4016  OE2 GLU C 531      24.178   9.118 -25.614  1.00 76.34           O  
ANISOU 4016  OE2 GLU C 531     9890   9837   9280   1521  -1729   -697       O  
ATOM   4017  N   TYR C 532      24.112  11.628 -20.327  1.00 51.29           N  
ANISOU 4017  N   TYR C 532     6745   7077   5664   1715  -1739   -720       N  
ATOM   4018  CA  TYR C 532      23.171  12.318 -19.463  1.00 44.31           C  
ANISOU 4018  CA  TYR C 532     5885   6264   4686   1725  -1705   -684       C  
ATOM   4019  C   TYR C 532      21.957  12.693 -20.302  1.00 45.12           C  
ANISOU 4019  C   TYR C 532     6000   6301   4842   1637  -1642   -639       C  
ATOM   4020  O   TYR C 532      21.973  12.600 -21.532  1.00 43.39           O  
ANISOU 4020  O   TYR C 532     5760   5991   4734   1562  -1621   -659       O  
ATOM   4021  CB  TYR C 532      23.801  13.563 -18.823  1.00 50.00           C  
ANISOU 4021  CB  TYR C 532     6557   7075   5365   1735  -1708   -823       C  
ATOM   4022  CG  TYR C 532      24.069  14.692 -19.792  1.00 47.35           C  
ANISOU 4022  CG  TYR C 532     6159   6710   5120   1652  -1696   -952       C  
ATOM   4023  CD1 TYR C 532      23.231  15.799 -19.846  1.00 43.91           C  
ANISOU 4023  CD1 TYR C 532     5718   6291   4677   1607  -1660   -984       C  
ATOM   4024  CD2 TYR C 532      25.159  14.653 -20.654  1.00 46.19           C  
ANISOU 4024  CD2 TYR C 532     5960   6521   5071   1619  -1717  -1037       C  
ATOM   4025  CE1 TYR C 532      23.470  16.835 -20.730  1.00 49.37           C  
ANISOU 4025  CE1 TYR C 532     6354   6947   5459   1526  -1646  -1092       C  
ATOM   4026  CE2 TYR C 532      25.406  15.683 -21.540  1.00 50.83           C  
ANISOU 4026  CE2 TYR C 532     6488   7082   5744   1538  -1698  -1139       C  
ATOM   4027  CZ  TYR C 532      24.559  16.771 -21.575  1.00 58.26           C  
ANISOU 4027  CZ  TYR C 532     7427   8030   6681   1489  -1662  -1163       C  
ATOM   4028  OH  TYR C 532      24.801  17.799 -22.458  1.00 62.60           O  
ANISOU 4028  OH  TYR C 532     7917   8544   7322   1403  -1639  -1254       O  
ATOM   4029  N   VAL C 533      20.888  13.109 -19.636  1.00 49.29           N  
ANISOU 4029  N   VAL C 533     6556   6873   5297   1635  -1589   -576       N  
ATOM   4030  CA  VAL C 533      19.644  13.470 -20.304  1.00 50.19           C  
ANISOU 4030  CA  VAL C 533     6681   6926   5462   1543  -1505   -523       C  
ATOM   4031  C   VAL C 533      19.403  14.959 -20.121  1.00 53.28           C  
ANISOU 4031  C   VAL C 533     7038   7376   5830   1517  -1477   -628       C  
ATOM   4032  O   VAL C 533      19.572  15.497 -19.020  1.00 56.35           O  
ANISOU 4032  O   VAL C 533     7425   7871   6115   1586  -1501   -673       O  
ATOM   4033  CB  VAL C 533      18.449  12.655 -19.771  1.00 46.62           C  
ANISOU 4033  CB  VAL C 533     6289   6468   4957   1553  -1458   -346       C  
ATOM   4034  CG1 VAL C 533      17.181  12.999 -20.547  1.00 43.54           C  
ANISOU 4034  CG1 VAL C 533     5903   6013   4629   1455  -1373   -295       C  
ATOM   4035  CG2 VAL C 533      18.740  11.166 -19.857  1.00 43.77           C  
ANISOU 4035  CG2 VAL C 533     5964   6042   4624   1585  -1496   -241       C  
ATOM   4036  N   ASN C 534      19.017  15.629 -21.205  1.00 55.06           N  
ANISOU 4036  N   ASN C 534     7238   7532   6151   1421  -1431   -670       N  
ATOM   4037  CA  ASN C 534      18.542  17.006 -21.115  1.00 62.86           C  
ANISOU 4037  CA  ASN C 534     8200   8552   7130   1388  -1395   -747       C  
ATOM   4038  C   ASN C 534      17.362  17.164 -22.057  1.00 65.62           C  
ANISOU 4038  C   ASN C 534     8560   8822   7552   1294  -1315   -681       C  
ATOM   4039  O   ASN C 534      17.497  16.933 -23.263  1.00 67.73           O  
ANISOU 4039  O   ASN C 534     8810   9000   7923   1225  -1304   -684       O  
ATOM   4040  CB  ASN C 534      19.642  18.018 -21.452  1.00 66.53           C  
ANISOU 4040  CB  ASN C 534     8603   9027   7646   1370  -1440   -913       C  
ATOM   4041  CG  ASN C 534      19.212  19.452 -21.193  1.00 69.01           C  
ANISOU 4041  CG  ASN C 534     8896   9375   7950   1348  -1417   -998       C  
ATOM   4042  OD1 ASN C 534      19.334  20.317 -22.059  1.00 65.83           O  
ANISOU 4042  OD1 ASN C 534     8453   8919   7638   1273  -1402  -1074       O  
ATOM   4043  ND2 ASN C 534      18.693  19.705 -19.996  1.00 71.84           N  
ANISOU 4043  ND2 ASN C 534     9281   9823   8194   1418  -1413   -984       N  
ATOM   4044  N   ALA C 535      16.211  17.543 -21.500  1.00 63.21           N  
ANISOU 4044  N   ALA C 535     8277   8554   7185   1298  -1262   -624       N  
ATOM   4045  CA  ALA C 535      14.973  17.719 -22.257  1.00 58.70           C  
ANISOU 4045  CA  ALA C 535     7714   7919   6669   1218  -1185   -555       C  
ATOM   4046  C   ALA C 535      14.706  16.516 -23.158  1.00 59.54           C  
ANISOU 4046  C   ALA C 535     7841   7930   6850   1169  -1169   -449       C  
ATOM   4047  O   ALA C 535      14.504  16.643 -24.367  1.00 62.45           O  
ANISOU 4047  O   ALA C 535     8193   8217   7320   1088  -1143   -461       O  
ATOM   4048  CB  ALA C 535      15.004  19.017 -23.064  1.00 46.02           C  
ANISOU 4048  CB  ALA C 535     6065   6278   5141   1150  -1167   -667       C  
ATOM   4049  N   ARG C 536      14.732  15.329 -22.550  1.00 58.60           N  
ANISOU 4049  N   ARG C 536     7761   7822   6683   1222  -1190   -347       N  
ATOM   4050  CA  ARG C 536      14.444  14.063 -23.221  1.00 61.35           C  
ANISOU 4050  CA  ARG C 536     8135   8077   7097   1187  -1185   -238       C  
ATOM   4051  C   ARG C 536      15.442  13.746 -24.329  1.00 58.74           C  
ANISOU 4051  C   ARG C 536     7780   7670   6869   1157  -1228   -313       C  
ATOM   4052  O   ARG C 536      15.136  12.968 -25.239  1.00 57.16           O  
ANISOU 4052  O   ARG C 536     7591   7378   6750   1108  -1217   -257       O  
ATOM   4053  CB  ARG C 536      13.016  14.047 -23.775  1.00 65.58           C  
ANISOU 4053  CB  ARG C 536     8683   8562   7675   1111  -1108   -144       C  
ATOM   4054  CG  ARG C 536      11.961  14.325 -22.725  1.00 74.43           C  
ANISOU 4054  CG  ARG C 536     9821   9765   8695   1140  -1059    -63       C  
ATOM   4055  CD  ARG C 536      11.700  13.097 -21.877  1.00 80.76           C  
ANISOU 4055  CD  ARG C 536    10665  10584   9436   1189  -1067     83       C  
ATOM   4056  NE  ARG C 536      10.502  12.396 -22.324  1.00 85.38           N  
ANISOU 4056  NE  ARG C 536    11267  11101  10071   1125  -1014    220       N  
ATOM   4057  CZ  ARG C 536       9.276  12.685 -21.903  1.00 88.69           C  
ANISOU 4057  CZ  ARG C 536    11687  11568  10442   1108   -946    302       C  
ATOM   4058  NH1 ARG C 536       8.236  12.003 -22.360  1.00 90.09           N  
ANISOU 4058  NH1 ARG C 536    11875  11680  10676   1043   -902    425       N  
ATOM   4059  NH2 ARG C 536       9.092  13.659 -21.022  1.00 88.52           N  
ANISOU 4059  NH2 ARG C 536    11653  11663  10316   1158   -925    255       N  
ATOM   4060  N   HIS C 537      16.636  14.329 -24.275  1.00 56.28           N  
ANISOU 4060  N   HIS C 537     7431   7398   6554   1187  -1278   -442       N  
ATOM   4061  CA  HIS C 537      17.686  14.049 -25.243  1.00 56.35           C  
ANISOU 4061  CA  HIS C 537     7407   7355   6647   1169  -1320   -518       C  
ATOM   4062  C   HIS C 537      18.837  13.326 -24.559  1.00 61.01           C  
ANISOU 4062  C   HIS C 537     8002   7983   7194   1260  -1398   -539       C  
ATOM   4063  O   HIS C 537      19.305  13.758 -23.496  1.00 62.91           O  
ANISOU 4063  O   HIS C 537     8238   8315   7349   1327  -1431   -583       O  
ATOM   4064  CB  HIS C 537      18.187  15.333 -25.909  1.00 59.58           C  
ANISOU 4064  CB  HIS C 537     7757   7775   7106   1118  -1314   -652       C  
ATOM   4065  CG  HIS C 537      17.273  15.857 -26.973  1.00 61.58           C  
ANISOU 4065  CG  HIS C 537     8000   7968   7431   1023  -1247   -636       C  
ATOM   4066  ND1 HIS C 537      16.205  16.682 -26.697  1.00 64.57           N  
ANISOU 4066  ND1 HIS C 537     8388   8365   7783    994  -1191   -611       N  
ATOM   4067  CD2 HIS C 537      17.268  15.672 -28.315  1.00 64.36           C  
ANISOU 4067  CD2 HIS C 537     8331   8247   7877    955  -1229   -644       C  
ATOM   4068  CE1 HIS C 537      15.581  16.984 -27.822  1.00 66.04           C  
ANISOU 4068  CE1 HIS C 537     8559   8488   8045    912  -1142   -600       C  
ATOM   4069  NE2 HIS C 537      16.206  16.384 -28.819  1.00 68.55           N  
ANISOU 4069  NE2 HIS C 537     8858   8752   8434    886  -1164   -619       N  
ATOM   4070  N   CYS C 538      19.265  12.217 -25.164  1.00 59.38           N  
ANISOU 4070  N   CYS C 538     7806   7709   7047   1266  -1430   -509       N  
ATOM   4071  CA  CYS C 538      20.481  11.524 -24.760  1.00 57.45           C  
ANISOU 4071  CA  CYS C 538     7557   7489   6784   1349  -1509   -543       C  
ATOM   4072  C   CYS C 538      21.680  12.310 -25.273  1.00 52.80           C  
ANISOU 4072  C   CYS C 538     6897   6933   6230   1341  -1543   -698       C  
ATOM   4073  O   CYS C 538      21.802  12.545 -26.480  1.00 50.41           O  
ANISOU 4073  O   CYS C 538     6558   6580   6015   1273  -1522   -749       O  
ATOM   4074  CB  CYS C 538      20.513  10.102 -25.320  1.00 53.54           C  
ANISOU 4074  CB  CYS C 538     7094   6899   6351   1358  -1534   -467       C  
ATOM   4075  SG  CYS C 538      19.067   9.059 -25.011  1.00 54.29           S  
ANISOU 4075  SG  CYS C 538     7263   6922   6441   1342  -1494   -275       S  
ATOM   4076  N   LEU C 539      22.562  12.714 -24.369  1.00 52.38           N  
ANISOU 4076  N   LEU C 539     6822   6970   6110   1409  -1595   -772       N  
ATOM   4077  CA  LEU C 539      23.727  13.486 -24.763  1.00 53.25           C  
ANISOU 4077  CA  LEU C 539     6858   7118   6255   1400  -1630   -918       C  
ATOM   4078  C   LEU C 539      24.975  12.916 -24.107  1.00 51.76           C  
ANISOU 4078  C   LEU C 539     6655   6986   6026   1497  -1714   -963       C  
ATOM   4079  O   LEU C 539      24.919  12.424 -22.977  1.00 51.76           O  
ANISOU 4079  O   LEU C 539     6698   7026   5942   1570  -1732   -901       O  
ATOM   4080  CB  LEU C 539      23.554  14.966 -24.393  1.00 50.05           C  
ANISOU 4080  CB  LEU C 539     6421   6772   5823   1366  -1606   -997       C  
ATOM   4081  CG  LEU C 539      22.474  15.651 -25.234  1.00 47.73           C  
ANISOU 4081  CG  LEU C 539     6129   6419   5588   1265  -1525   -971       C  
ATOM   4082  CD1 LEU C 539      22.058  16.985 -24.637  1.00 49.22           C  
ANISOU 4082  CD1 LEU C 539     6306   6659   5737   1249  -1502  -1025       C  
ATOM   4083  CD2 LEU C 539      22.950  15.820 -26.672  1.00 40.94           C  
ANISOU 4083  CD2 LEU C 539     5215   5504   4836   1190  -1512  -1029       C  
ATOM   4084  N   PRO C 540      26.116  12.964 -24.797  1.00 51.31           N  
ANISOU 4084  N   PRO C 540     6538   6922   6038   1478  -1725  -1056       N  
ATOM   4085  CA  PRO C 540      27.288  12.201 -24.343  1.00 52.05           C  
ANISOU 4085  CA  PRO C 540     6622   7038   6117   1549  -1766  -1079       C  
ATOM   4086  C   PRO C 540      28.034  12.910 -23.221  1.00 48.06           C  
ANISOU 4086  C   PRO C 540     6089   6622   5548   1589  -1779  -1150       C  
ATOM   4087  O   PRO C 540      28.261  14.122 -23.274  1.00 57.31           O  
ANISOU 4087  O   PRO C 540     7210   7827   6739   1541  -1757  -1239       O  
ATOM   4088  CB  PRO C 540      28.149  12.102 -25.606  1.00 51.55           C  
ANISOU 4088  CB  PRO C 540     6497   6939   6151   1508  -1765  -1155       C  
ATOM   4089  CG  PRO C 540      27.832  13.363 -26.348  1.00 47.35           C  
ANISOU 4089  CG  PRO C 540     5916   6407   5668   1413  -1718  -1214       C  
ATOM   4090  CD  PRO C 540      26.378  13.673 -26.063  1.00 48.66           C  
ANISOU 4090  CD  PRO C 540     6137   6557   5794   1391  -1696  -1136       C  
ATOM   4091  N   CYS C 541      28.415  12.143 -22.203  1.00 49.71           N  
ANISOU 4091  N   CYS C 541     6333   6867   5687   1676  -1814  -1109       N  
ATOM   4092  CA  CYS C 541      29.353  12.639 -21.209  1.00 59.09           C  
ANISOU 4092  CA  CYS C 541     7489   8140   6824   1723  -1836  -1187       C  
ATOM   4093  C   CYS C 541      30.685  12.973 -21.873  1.00 62.15           C  
ANISOU 4093  C   CYS C 541     7794   8532   7288   1699  -1845  -1305       C  
ATOM   4094  O   CYS C 541      31.026  12.452 -22.939  1.00 64.80           O  
ANISOU 4094  O   CYS C 541     8109   8814   7699   1673  -1845  -1313       O  
ATOM   4095  CB  CYS C 541      29.578  11.603 -20.106  1.00 62.63           C  
ANISOU 4095  CB  CYS C 541     7986   8621   7187   1822  -1874  -1113       C  
ATOM   4096  SG  CYS C 541      28.157  11.289 -19.035  1.00 73.90           S  
ANISOU 4096  SG  CYS C 541     9501  10073   8504   1861  -1856   -965       S  
ATOM   4097  N   HIS C 542      31.439  13.858 -21.234  1.00 65.40           N  
ANISOU 4097  N   HIS C 542     8157   9011   7682   1708  -1852  -1398       N  
ATOM   4098  CA  HIS C 542      32.791  14.126 -21.696  1.00 63.30           C  
ANISOU 4098  CA  HIS C 542     7811   8761   7481   1695  -1863  -1500       C  
ATOM   4099  C   HIS C 542      33.613  12.841 -21.615  1.00 59.13           C  
ANISOU 4099  C   HIS C 542     7294   8232   6942   1771  -1906  -1481       C  
ATOM   4100  O   HIS C 542      33.455  12.063 -20.666  1.00 54.92           O  
ANISOU 4100  O   HIS C 542     6819   7720   6329   1849  -1938  -1414       O  
ATOM   4101  CB  HIS C 542      33.437  15.229 -20.856  1.00 63.91           C  
ANISOU 4101  CB  HIS C 542     7838   8909   7537   1702  -1871  -1593       C  
ATOM   4102  CG  HIS C 542      34.691  15.788 -21.451  1.00 66.01           C  
ANISOU 4102  CG  HIS C 542     8010   9187   7885   1663  -1871  -1696       C  
ATOM   4103  ND1 HIS C 542      35.936  15.250 -21.205  1.00 68.64           N  
ANISOU 4103  ND1 HIS C 542     8309   9558   8214   1722  -1909  -1741       N  
ATOM   4104  CD2 HIS C 542      34.894  16.837 -22.283  1.00 61.54           C  
ANISOU 4104  CD2 HIS C 542     7377   8601   7405   1571  -1835  -1755       C  
ATOM   4105  CE1 HIS C 542      36.851  15.944 -21.859  1.00 68.17           C  
ANISOU 4105  CE1 HIS C 542     8162   9507   8234   1668  -1897  -1824       C  
ATOM   4106  NE2 HIS C 542      36.244  16.912 -22.521  1.00 64.92           N  
ANISOU 4106  NE2 HIS C 542     7729   9060   7879   1574  -1851  -1830       N  
ATOM   4107  N   PRO C 543      34.482  12.573 -22.596  1.00 56.94           N  
ANISOU 4107  N   PRO C 543     6962   7931   6740   1750  -1907  -1532       N  
ATOM   4108  CA  PRO C 543      35.216  11.295 -22.604  1.00 57.22           C  
ANISOU 4108  CA  PRO C 543     7011   7957   6770   1825  -1949  -1515       C  
ATOM   4109  C   PRO C 543      36.171  11.114 -21.435  1.00 59.78           C  
ANISOU 4109  C   PRO C 543     7327   8356   7031   1909  -1995  -1550       C  
ATOM   4110  O   PRO C 543      36.655   9.994 -21.230  1.00 60.90           O  
ANISOU 4110  O   PRO C 543     7495   8491   7154   1982  -2035  -1521       O  
ATOM   4111  CB  PRO C 543      35.979  11.334 -23.935  1.00 54.12           C  
ANISOU 4111  CB  PRO C 543     6547   7543   6473   1777  -1931  -1584       C  
ATOM   4112  CG  PRO C 543      35.249  12.336 -24.772  1.00 51.01           C  
ANISOU 4112  CG  PRO C 543     6128   7121   6133   1673  -1876  -1592       C  
ATOM   4113  CD  PRO C 543      34.736  13.362 -23.812  1.00 51.75           C  
ANISOU 4113  CD  PRO C 543     6233   7252   6177   1658  -1866  -1596       C  
ATOM   4114  N   GLU C 544      36.460  12.160 -20.668  1.00 55.80           N  
ANISOU 4114  N   GLU C 544     6787   7918   6496   1905  -1994  -1614       N  
ATOM   4115  CA  GLU C 544      37.347  12.041 -19.520  1.00 55.63           C  
ANISOU 4115  CA  GLU C 544     6754   7972   6410   1987  -2039  -1652       C  
ATOM   4116  C   GLU C 544      36.620  11.645 -18.243  1.00 59.45           C  
ANISOU 4116  C   GLU C 544     7317   8488   6784   2056  -2059  -1566       C  
ATOM   4117  O   GLU C 544      37.273  11.447 -17.213  1.00 63.75           O  
ANISOU 4117  O   GLU C 544     7861   9099   7262   2133  -2098  -1585       O  
ATOM   4118  CB  GLU C 544      38.108  13.352 -19.303  1.00 60.20           C  
ANISOU 4118  CB  GLU C 544     7250   8609   7016   1952  -2034  -1769       C  
ATOM   4119  CG  GLU C 544      39.247  13.559 -20.286  1.00 66.26           C  
ANISOU 4119  CG  GLU C 544     7928   9374   7875   1912  -2028  -1854       C  
ATOM   4120  CD  GLU C 544      40.233  12.403 -20.285  1.00 74.13           C  
ANISOU 4120  CD  GLU C 544     8919  10384   8862   1990  -2071  -1860       C  
ATOM   4121  OE1 GLU C 544      40.524  11.867 -19.195  1.00 76.42           O  
ANISOU 4121  OE1 GLU C 544     9242  10719   9073   2079  -2116  -1844       O  
ATOM   4122  OE2 GLU C 544      40.710  12.026 -21.376  1.00 75.50           O  
ANISOU 4122  OE2 GLU C 544     9056  10528   9103   1965  -2059  -1880       O  
ATOM   4123  N   CYS C 545      35.294  11.526 -18.280  1.00 61.71           N  
ANISOU 4123  N   CYS C 545     7668   8733   7045   2032  -2031  -1470       N  
ATOM   4124  CA  CYS C 545      34.563  11.017 -17.129  1.00 64.22           C  
ANISOU 4124  CA  CYS C 545     8062   9083   7256   2098  -2043  -1368       C  
ATOM   4125  C   CYS C 545      34.758   9.510 -17.014  1.00 64.65           C  
ANISOU 4125  C   CYS C 545     8168   9105   7293   2166  -2079  -1275       C  
ATOM   4126  O   CYS C 545      34.571   8.772 -17.985  1.00 66.62           O  
ANISOU 4126  O   CYS C 545     8433   9269   7609   2141  -2075  -1231       O  
ATOM   4127  CB  CYS C 545      33.072  11.337 -17.245  1.00 68.15           C  
ANISOU 4127  CB  CYS C 545     8610   9549   7735   2049  -1998  -1287       C  
ATOM   4128  SG  CYS C 545      32.636  13.076 -17.485  1.00 72.70           S  
ANISOU 4128  SG  CYS C 545     9137  10144   8343   1962  -1954  -1383       S  
ATOM   4129  N   GLN C 546      35.136   9.059 -15.830  1.00 60.82           N  
ANISOU 4129  N   GLN C 546     7706   8684   6720   2253  -2115  -1244       N  
ATOM   4130  CA  GLN C 546      35.212   7.631 -15.556  1.00 63.54           C  
ANISOU 4130  CA  GLN C 546     8106   8996   7041   2322  -2149  -1136       C  
ATOM   4131  C   GLN C 546      33.803   7.060 -15.461  1.00 65.12           C  
ANISOU 4131  C   GLN C 546     8387   9144   7214   2309  -2122   -978       C  
ATOM   4132  O   GLN C 546      33.009   7.538 -14.641  1.00 70.36           O  
ANISOU 4132  O   GLN C 546     9078   9862   7795   2314  -2098   -929       O  
ATOM   4133  CB  GLN C 546      35.977   7.390 -14.259  1.00 68.36           C  
ANISOU 4133  CB  GLN C 546     8717   9698   7559   2417  -2193  -1142       C  
ATOM   4134  CG  GLN C 546      36.084   5.935 -13.834  1.00 73.62           C  
ANISOU 4134  CG  GLN C 546     9440  10336   8196   2493  -2232  -1022       C  
ATOM   4135  CD  GLN C 546      36.195   5.786 -12.327  1.00 78.71           C  
ANISOU 4135  CD  GLN C 546    10110  11078   8718   2578  -2256   -972       C  
ATOM   4136  OE1 GLN C 546      36.062   6.760 -11.585  1.00 77.86           O  
ANISOU 4136  OE1 GLN C 546     9983  11059   8541   2582  -2242  -1024       O  
ATOM   4137  NE2 GLN C 546      36.450   4.566 -11.869  1.00 80.83           N  
ANISOU 4137  NE2 GLN C 546    10420  11330   8960   2649  -2295   -872       N  
ATOM   4138  N   PRO C 547      33.441   6.067 -16.276  1.00 64.53           N  
ANISOU 4138  N   PRO C 547     8348   8964   7206   2293  -2123   -896       N  
ATOM   4139  CA  PRO C 547      32.109   5.466 -16.147  1.00 65.48           C  
ANISOU 4139  CA  PRO C 547     8543   9029   7308   2280  -2098   -735       C  
ATOM   4140  C   PRO C 547      31.924   4.835 -14.776  1.00 68.32           C  
ANISOU 4140  C   PRO C 547     8953   9443   7562   2358  -2116   -616       C  
ATOM   4141  O   PRO C 547      32.859   4.292 -14.184  1.00 70.07           O  
ANISOU 4141  O   PRO C 547     9169   9700   7754   2430  -2162   -626       O  
ATOM   4142  CB  PRO C 547      32.086   4.410 -17.258  1.00 59.50           C  
ANISOU 4142  CB  PRO C 547     7806   8146   6657   2260  -2111   -691       C  
ATOM   4143  CG  PRO C 547      33.098   4.884 -18.248  1.00 59.74           C  
ANISOU 4143  CG  PRO C 547     7762   8173   6765   2231  -2120   -849       C  
ATOM   4144  CD  PRO C 547      34.181   5.525 -17.428  1.00 61.68           C  
ANISOU 4144  CD  PRO C 547     7956   8529   6949   2278  -2143   -954       C  
ATOM   4145  N   GLN C 548      30.698   4.915 -14.271  1.00 65.86           N  
ANISOU 4145  N   GLN C 548     8689   9142   7191   2343  -2077   -498       N  
ATOM   4146  CA  GLN C 548      30.375   4.489 -12.917  1.00 64.79           C  
ANISOU 4146  CA  GLN C 548     8597   9078   6943   2408  -2081   -379       C  
ATOM   4147  C   GLN C 548      29.468   3.267 -12.945  1.00 64.47           C  
ANISOU 4147  C   GLN C 548     8625   8946   6924   2404  -2071   -183       C  
ATOM   4148  O   GLN C 548      28.520   3.199 -13.734  1.00 60.31           O  
ANISOU 4148  O   GLN C 548     8120   8334   6460   2337  -2036   -126       O  
ATOM   4149  CB  GLN C 548      29.702   5.623 -12.133  1.00 64.69           C  
ANISOU 4149  CB  GLN C 548     8578   9173   6829   2400  -2038   -398       C  
ATOM   4150  CG  GLN C 548      30.548   6.877 -12.017  1.00 62.03           C  
ANISOU 4150  CG  GLN C 548     8172   8919   6477   2402  -2048   -588       C  
ATOM   4151  CD  GLN C 548      31.787   6.657 -11.171  1.00 58.21           C  
ANISOU 4151  CD  GLN C 548     7664   8511   5941   2486  -2101   -645       C  
ATOM   4152  OE1 GLN C 548      32.898   6.983 -11.586  1.00 62.89           O  
ANISOU 4152  OE1 GLN C 548     8201   9106   6588   2486  -2131   -782       O  
ATOM   4153  NE2 GLN C 548      31.600   6.094  -9.976  1.00 49.00           N  
ANISOU 4153  NE2 GLN C 548     6538   7412   4670   2558  -2110   -536       N  
ATOM   4154  N   ASN C 549      29.770   2.299 -12.083  1.00 71.26           N  
ANISOU 4154  N   ASN C 549     9517   9821   7738   2475  -2105    -79       N  
ATOM   4155  CA  ASN C 549      28.926   1.127 -11.898  1.00 73.46           C  
ANISOU 4155  CA  ASN C 549     9858  10020   8032   2474  -2097    124       C  
ATOM   4156  C   ASN C 549      27.978   1.387 -10.734  1.00 74.58           C  
ANISOU 4156  C   ASN C 549    10029  10258   8050   2487  -2054    244       C  
ATOM   4157  O   ASN C 549      28.421   1.575  -9.595  1.00 75.72           O  
ANISOU 4157  O   ASN C 549    10166  10521   8083   2554  -2069    236       O  
ATOM   4158  CB  ASN C 549      29.770  -0.122 -11.638  1.00 77.20           C  
ANISOU 4158  CB  ASN C 549    10350  10450   8535   2542  -2158    181       C  
ATOM   4159  CG  ASN C 549      30.540  -0.570 -12.864  1.00 83.69           C  
ANISOU 4159  CG  ASN C 549    11150  11161   9487   2528  -2195     85       C  
ATOM   4160  OD1 ASN C 549      30.030  -0.518 -13.984  1.00 86.11           O  
ANISOU 4160  OD1 ASN C 549    11457  11372   9887   2458  -2171     66       O  
ATOM   4161  ND2 ASN C 549      31.777  -1.008 -12.659  1.00 83.26           N  
ANISOU 4161  ND2 ASN C 549    11074  11126   9435   2597  -2252     21       N  
ATOM   4162  N   GLY C 550      26.680   1.410 -11.024  1.00 76.58           N  
ANISOU 4162  N   GLY C 550    10313  10465   8319   2423  -2000    350       N  
ATOM   4163  CA  GLY C 550      25.671   1.629 -10.009  1.00 78.72           C  
ANISOU 4163  CA  GLY C 550    10609  10824   8475   2428  -1951    472       C  
ATOM   4164  C   GLY C 550      25.280   3.070  -9.776  1.00 80.06           C  
ANISOU 4164  C   GLY C 550    10748  11107   8565   2410  -1905    363       C  
ATOM   4165  O   GLY C 550      24.611   3.356  -8.777  1.00 80.06           O  
ANISOU 4165  O   GLY C 550    10761  11210   8449   2432  -1866    437       O  
ATOM   4166  N   SER C 551      25.664   3.985 -10.663  1.00 76.99           N  
ANISOU 4166  N   SER C 551    10316  10701   8235   2372  -1907    190       N  
ATOM   4167  CA  SER C 551      25.386   5.402 -10.468  1.00 71.33           C  
ANISOU 4167  CA  SER C 551     9565  10082   7455   2356  -1871     71       C  
ATOM   4168  C   SER C 551      25.511   6.117 -11.805  1.00 65.98           C  
ANISOU 4168  C   SER C 551     8852   9330   6887   2284  -1868    -65       C  
ATOM   4169  O   SER C 551      25.959   5.543 -12.801  1.00 62.56           O  
ANISOU 4169  O   SER C 551     8415   8788   6567   2257  -1896    -84       O  
ATOM   4170  CB  SER C 551      26.331   6.015  -9.430  1.00 77.23           C  
ANISOU 4170  CB  SER C 551    10278  10964   8104   2430  -1900    -43       C  
ATOM   4171  OG  SER C 551      26.283   7.429  -9.472  1.00 79.66           O  
ANISOU 4171  OG  SER C 551    10541  11338   8386   2408  -1878   -194       O  
ATOM   4172  N   VAL C 552      25.099   7.389 -11.816  1.00 63.30           N  
ANISOU 4172  N   VAL C 552     8484   9053   6515   2253  -1832   -161       N  
ATOM   4173  CA  VAL C 552      25.275   8.200 -13.015  1.00 55.64           C  
ANISOU 4173  CA  VAL C 552     7473   8025   5644   2184  -1830   -298       C  
ATOM   4174  C   VAL C 552      26.747   8.564 -13.177  1.00 54.52           C  
ANISOU 4174  C   VAL C 552     7274   7901   5540   2205  -1880   -464       C  
ATOM   4175  O   VAL C 552      27.534   8.557 -12.225  1.00 52.82           O  
ANISOU 4175  O   VAL C 552     7045   7769   5254   2275  -1911   -502       O  
ATOM   4176  CB  VAL C 552      24.397   9.460 -12.976  1.00 54.22           C  
ANISOU 4176  CB  VAL C 552     7278   7899   5425   2144  -1779   -349       C  
ATOM   4177  CG1 VAL C 552      22.964   9.099 -12.638  1.00 53.08           C  
ANISOU 4177  CG1 VAL C 552     7186   7759   5224   2133  -1725   -179       C  
ATOM   4178  CG2 VAL C 552      24.950  10.462 -11.978  1.00 58.72           C  
ANISOU 4178  CG2 VAL C 552     7810   8596   5905   2193  -1788   -471       C  
ATOM   4179  N   THR C 553      27.122   8.886 -14.412  1.00 54.51           N  
ANISOU 4179  N   THR C 553     7235   7823   5652   2143  -1887   -562       N  
ATOM   4180  CA  THR C 553      28.513   9.158 -14.750  1.00 55.27           C  
ANISOU 4180  CA  THR C 553     7272   7925   5803   2151  -1928   -710       C  
ATOM   4181  C   THR C 553      28.826  10.644 -14.856  1.00 57.93           C  
ANISOU 4181  C   THR C 553     7546   8314   6151   2113  -1915   -869       C  
ATOM   4182  O   THR C 553      29.919  11.065 -14.461  1.00 57.45           O  
ANISOU 4182  O   THR C 553     7437   8309   6081   2145  -1946   -982       O  
ATOM   4183  CB  THR C 553      28.878   8.452 -16.065  1.00 57.38           C  
ANISOU 4183  CB  THR C 553     7532   8077   6195   2112  -1945   -716       C  
ATOM   4184  OG1 THR C 553      28.875   7.031 -15.865  1.00 64.80           O  
ANISOU 4184  OG1 THR C 553     8522   8965   7133   2159  -1970   -587       O  
ATOM   4185  CG2 THR C 553      30.253   8.875 -16.554  1.00 55.01           C  
ANISOU 4185  CG2 THR C 553     7159   7787   5955   2107  -1975   -874       C  
ATOM   4186  N   CYS C 554      27.891  11.452 -15.354  1.00 60.92           N  
ANISOU 4186  N   CYS C 554     7923   8673   6551   2046  -1872   -879       N  
ATOM   4187  CA  CYS C 554      28.108  12.887 -15.463  1.00 62.34           C  
ANISOU 4187  CA  CYS C 554     8046   8889   6753   2003  -1858  -1021       C  
ATOM   4188  C   CYS C 554      26.773  13.608 -15.319  1.00 62.31           C  
ANISOU 4188  C   CYS C 554     8067   8902   6707   1970  -1810   -984       C  
ATOM   4189  O   CYS C 554      25.700  13.003 -15.404  1.00 63.82           O  
ANISOU 4189  O   CYS C 554     8313   9062   6872   1965  -1783   -851       O  
ATOM   4190  CB  CYS C 554      28.785  13.252 -16.789  1.00 63.27           C  
ANISOU 4190  CB  CYS C 554     8104   8934   7001   1929  -1862  -1121       C  
ATOM   4191  SG  CYS C 554      27.718  13.103 -18.240  1.00 63.72           S  
ANISOU 4191  SG  CYS C 554     8181   8881   7149   1837  -1823  -1057       S  
ATOM   4192  N   PHE C 555      26.856  14.920 -15.095  1.00 56.40           N  
ANISOU 4192  N   PHE C 555     7275   8198   5956   1949  -1799  -1102       N  
ATOM   4193  CA  PHE C 555      25.691  15.782 -14.962  1.00 50.28           C  
ANISOU 4193  CA  PHE C 555     6515   7443   5147   1919  -1755  -1095       C  
ATOM   4194  C   PHE C 555      25.541  16.742 -16.134  1.00 53.27           C  
ANISOU 4194  C   PHE C 555     6852   7751   5638   1821  -1734  -1179       C  
ATOM   4195  O   PHE C 555      24.593  17.537 -16.157  1.00 55.08           O  
ANISOU 4195  O   PHE C 555     7089   7986   5854   1789  -1698  -1184       O  
ATOM   4196  CB  PHE C 555      25.761  16.567 -13.645  1.00 41.68           C  
ANISOU 4196  CB  PHE C 555     5414   6464   3959   1981  -1758  -1158       C  
ATOM   4197  CG  PHE C 555      25.997  15.704 -12.433  1.00 47.39           C  
ANISOU 4197  CG  PHE C 555     6170   7268   4567   2080  -1779  -1083       C  
ATOM   4198  CD1 PHE C 555      27.281  15.439 -11.989  1.00 44.49           C  
ANISOU 4198  CD1 PHE C 555     5773   6934   4198   2131  -1828  -1146       C  
ATOM   4199  CD2 PHE C 555      24.931  15.151 -11.747  1.00 57.73           C  
ANISOU 4199  CD2 PHE C 555     7538   8624   5771   2121  -1746   -944       C  
ATOM   4200  CE1 PHE C 555      27.491  14.650 -10.883  1.00 47.46           C  
ANISOU 4200  CE1 PHE C 555     6180   7385   4468   2221  -1847  -1074       C  
ATOM   4201  CE2 PHE C 555      25.143  14.362 -10.642  1.00 57.77           C  
ANISOU 4201  CE2 PHE C 555     7572   8706   5673   2207  -1762   -865       C  
ATOM   4202  CZ  PHE C 555      26.423  14.111 -10.209  1.00 50.02           C  
ANISOU 4202  CZ  PHE C 555     6562   7754   4688   2258  -1814   -931       C  
ATOM   4203  N   GLY C 556      26.447  16.687 -17.103  1.00 49.35           N  
ANISOU 4203  N   GLY C 556     6309   7191   5250   1773  -1751  -1241       N  
ATOM   4204  CA  GLY C 556      26.418  17.566 -18.242  1.00 46.65           C  
ANISOU 4204  CA  GLY C 556     5922   6784   5020   1675  -1728  -1313       C  
ATOM   4205  C   GLY C 556      27.504  17.215 -19.236  1.00 46.89           C  
ANISOU 4205  C   GLY C 556     5903   6759   5153   1638  -1746  -1358       C  
ATOM   4206  O   GLY C 556      28.200  16.204 -19.102  1.00 56.03           O  
ANISOU 4206  O   GLY C 556     7069   7922   6299   1689  -1778  -1329       O  
ATOM   4207  N   PRO C 557      27.677  18.058 -20.258  1.00 48.76           N  
ANISOU 4207  N   PRO C 557     6087   6946   5496   1548  -1722  -1427       N  
ATOM   4208  CA  PRO C 557      28.636  17.732 -21.323  1.00 53.40           C  
ANISOU 4208  CA  PRO C 557     6623   7486   6180   1508  -1728  -1462       C  
ATOM   4209  C   PRO C 557      30.090  18.033 -20.992  1.00 59.17           C  
ANISOU 4209  C   PRO C 557     7288   8259   6936   1530  -1757  -1559       C  
ATOM   4210  O   PRO C 557      30.977  17.444 -21.624  1.00 59.69           O  
ANISOU 4210  O   PRO C 557     7321   8307   7053   1529  -1770  -1574       O  
ATOM   4211  CB  PRO C 557      28.157  18.601 -22.493  1.00 50.40           C  
ANISOU 4211  CB  PRO C 557     6210   7045   5894   1400  -1683  -1485       C  
ATOM   4212  CG  PRO C 557      27.530  19.785 -21.825  1.00 43.23           C  
ANISOU 4212  CG  PRO C 557     5306   6163   4956   1387  -1666  -1521       C  
ATOM   4213  CD  PRO C 557      26.890  19.265 -20.565  1.00 41.98           C  
ANISOU 4213  CD  PRO C 557     5215   6065   4669   1479  -1684  -1461       C  
ATOM   4214  N   GLU C 558      30.372  18.908 -20.033  1.00 60.52           N  
ANISOU 4214  N   GLU C 558     7437   8487   7072   1555  -1769  -1627       N  
ATOM   4215  CA  GLU C 558      31.720  19.433 -19.874  1.00 55.73           C  
ANISOU 4215  CA  GLU C 558     6755   7911   6511   1556  -1793  -1729       C  
ATOM   4216  C   GLU C 558      32.563  18.570 -18.936  1.00 56.45           C  
ANISOU 4216  C   GLU C 558     6856   8065   6529   1657  -1842  -1731       C  
ATOM   4217  O   GLU C 558      32.055  17.757 -18.160  1.00 53.27           O  
ANISOU 4217  O   GLU C 558     6519   7693   6027   1732  -1858  -1658       O  
ATOM   4218  CB  GLU C 558      31.672  20.873 -19.365  1.00 51.67           C  
ANISOU 4218  CB  GLU C 558     6205   7417   6012   1527  -1787  -1810       C  
ATOM   4219  CG  GLU C 558      31.092  21.852 -20.372  1.00 58.19           C  
ANISOU 4219  CG  GLU C 558     7005   8174   6929   1419  -1741  -1821       C  
ATOM   4220  CD  GLU C 558      30.936  23.247 -19.806  1.00 69.77           C  
ANISOU 4220  CD  GLU C 558     8447   9652   8412   1398  -1740  -1895       C  
ATOM   4221  OE1 GLU C 558      31.776  24.115 -20.126  1.00 71.67           O  
ANISOU 4221  OE1 GLU C 558     8615   9878   8739   1345  -1744  -1971       O  
ATOM   4222  OE2 GLU C 558      29.976  23.477 -19.040  1.00 71.10           O  
ANISOU 4222  OE2 GLU C 558     8665   9845   8505   1435  -1736  -1877       O  
ATOM   4223  N   ALA C 559      33.882  18.774 -19.017  1.00 56.36           N  
ANISOU 4223  N   ALA C 559     6774   8075   6567   1658  -1866  -1814       N  
ATOM   4224  CA  ALA C 559      34.848  17.971 -18.277  1.00 53.93           C  
ANISOU 4224  CA  ALA C 559     6463   7823   6204   1749  -1914  -1827       C  
ATOM   4225  C   ALA C 559      34.849  18.253 -16.780  1.00 58.79           C  
ANISOU 4225  C   ALA C 559     7098   8519   6720   1829  -1945  -1853       C  
ATOM   4226  O   ALA C 559      35.507  17.521 -16.034  1.00 59.63           O  
ANISOU 4226  O   ALA C 559     7214   8679   6763   1914  -1986  -1850       O  
ATOM   4227  CB  ALA C 559      36.253  18.197 -18.837  1.00 55.28           C  
ANISOU 4227  CB  ALA C 559     6546   7999   6459   1722  -1928  -1914       C  
ATOM   4228  N   ASP C 560      34.152  19.292 -16.325  1.00 63.52           N  
ANISOU 4228  N   ASP C 560     7701   9131   7302   1807  -1928  -1880       N  
ATOM   4229  CA  ASP C 560      34.024  19.577 -14.903  1.00 63.56           C  
ANISOU 4229  CA  ASP C 560     7727   9219   7205   1887  -1954  -1904       C  
ATOM   4230  C   ASP C 560      32.715  19.062 -14.325  1.00 62.65           C  
ANISOU 4230  C   ASP C 560     7699   9124   6981   1932  -1934  -1798       C  
ATOM   4231  O   ASP C 560      32.400  19.351 -13.167  1.00 62.27           O  
ANISOU 4231  O   ASP C 560     7672   9149   6839   1996  -1945  -1808       O  
ATOM   4232  CB  ASP C 560      34.156  21.079 -14.644  1.00 65.90           C  
ANISOU 4232  CB  ASP C 560     7968   9524   7547   1847  -1953  -2011       C  
ATOM   4233  CG  ASP C 560      33.248  21.911 -15.527  1.00 64.28           C  
ANISOU 4233  CG  ASP C 560     7762   9245   7418   1749  -1905  -2003       C  
ATOM   4234  OD1 ASP C 560      32.429  21.331 -16.269  1.00 60.90           O  
ANISOU 4234  OD1 ASP C 560     7379   8767   6994   1716  -1871  -1914       O  
ATOM   4235  OD2 ASP C 560      33.350  23.154 -15.471  1.00 64.60           O  
ANISOU 4235  OD2 ASP C 560     7756   9276   7515   1705  -1904  -2086       O  
ATOM   4236  N   GLN C 561      31.943  18.310 -15.108  1.00 57.01           N  
ANISOU 4236  N   GLN C 561     7033   8349   6278   1900  -1906  -1696       N  
ATOM   4237  CA  GLN C 561      30.687  17.727 -14.657  1.00 53.10           C  
ANISOU 4237  CA  GLN C 561     6619   7869   5687   1936  -1885  -1579       C  
ATOM   4238  C   GLN C 561      30.766  16.207 -14.562  1.00 48.13           C  
ANISOU 4238  C   GLN C 561     6042   7236   5009   1993  -1904  -1467       C  
ATOM   4239  O   GLN C 561      29.744  15.522 -14.623  1.00 47.91           O  
ANISOU 4239  O   GLN C 561     6078   7187   4939   1998  -1882  -1346       O  
ATOM   4240  CB  GLN C 561      29.537  18.146 -15.572  1.00 48.24           C  
ANISOU 4240  CB  GLN C 561     6023   7184   5122   1852  -1836  -1540       C  
ATOM   4241  CG  GLN C 561      29.649  19.560 -16.109  1.00 50.43           C  
ANISOU 4241  CG  GLN C 561     6238   7429   5493   1770  -1817  -1648       C  
ATOM   4242  CD  GLN C 561      28.341  20.056 -16.686  1.00 55.98           C  
ANISOU 4242  CD  GLN C 561     6971   8085   6216   1706  -1770  -1607       C  
ATOM   4243  OE1 GLN C 561      28.205  20.215 -17.897  1.00 54.85           O  
ANISOU 4243  OE1 GLN C 561     6809   7864   6169   1621  -1746  -1604       O  
ATOM   4244  NE2 GLN C 561      27.370  20.310 -15.816  1.00 61.80           N  
ANISOU 4244  NE2 GLN C 561     7752   8873   6856   1749  -1756  -1576       N  
ATOM   4245  N   CYS C 562      31.972  15.668 -14.424  1.00 52.47           N  
ANISOU 4245  N   CYS C 562     6562   7802   5570   2036  -1945  -1503       N  
ATOM   4246  CA  CYS C 562      32.135  14.240 -14.210  1.00 56.39           C  
ANISOU 4246  CA  CYS C 562     7107   8296   6021   2100  -1970  -1401       C  
ATOM   4247  C   CYS C 562      31.935  13.905 -12.738  1.00 60.94           C  
ANISOU 4247  C   CYS C 562     7726   8966   6461   2196  -1987  -1346       C  
ATOM   4248  O   CYS C 562      32.263  14.695 -11.848  1.00 66.52           O  
ANISOU 4248  O   CYS C 562     8404   9753   7117   2232  -2000  -1428       O  
ATOM   4249  CB  CYS C 562      33.524  13.772 -14.650  1.00 54.74           C  
ANISOU 4249  CB  CYS C 562     6850   8071   5877   2113  -2009  -1464       C  
ATOM   4250  SG  CYS C 562      33.979  14.108 -16.368  1.00 57.57           S  
ANISOU 4250  SG  CYS C 562     7145   8338   6392   2008  -1988  -1532       S  
ATOM   4251  N   VAL C 563      31.378  12.719 -12.486  1.00 58.75           N  
ANISOU 4251  N   VAL C 563     7517   8678   6127   2238  -1987  -1201       N  
ATOM   4252  CA  VAL C 563      31.356  12.202 -11.121  1.00 54.95           C  
ANISOU 4252  CA  VAL C 563     7073   8286   5519   2333  -2006  -1133       C  
ATOM   4253  C   VAL C 563      32.777  11.931 -10.646  1.00 57.42           C  
ANISOU 4253  C   VAL C 563     7348   8645   5825   2398  -2062  -1208       C  
ATOM   4254  O   VAL C 563      33.135  12.225  -9.498  1.00 62.37           O  
ANISOU 4254  O   VAL C 563     7964   9372   6363   2467  -2083  -1246       O  
ATOM   4255  CB  VAL C 563      30.473  10.943 -11.041  1.00 52.23           C  
ANISOU 4255  CB  VAL C 563     6806   7905   5134   2353  -1991   -945       C  
ATOM   4256  CG1 VAL C 563      30.665  10.238  -9.707  1.00 42.36           C  
ANISOU 4256  CG1 VAL C 563     5589   6742   3764   2452  -2016   -865       C  
ATOM   4257  CG2 VAL C 563      29.011  11.313 -11.249  1.00 40.02           C  
ANISOU 4257  CG2 VAL C 563     5296   6341   3571   2302  -1933   -870       C  
ATOM   4258  N   ALA C 564      33.612  11.382 -11.526  1.00 52.51           N  
ANISOU 4258  N   ALA C 564     6701   7956   5296   2379  -2087  -1236       N  
ATOM   4259  CA  ALA C 564      35.023  11.163 -11.242  1.00 52.11           C  
ANISOU 4259  CA  ALA C 564     6604   7942   5252   2432  -2139  -1318       C  
ATOM   4260  C   ALA C 564      35.776  11.129 -12.564  1.00 54.21           C  
ANISOU 4260  C   ALA C 564     6820   8129   5650   2372  -2144  -1391       C  
ATOM   4261  O   ALA C 564      35.210  10.809 -13.613  1.00 56.64           O  
ANISOU 4261  O   ALA C 564     7146   8347   6027   2311  -2117  -1341       O  
ATOM   4262  CB  ALA C 564      35.248   9.871 -10.449  1.00 52.13           C  
ANISOU 4262  CB  ALA C 564     6658   7973   5177   2525  -2175  -1208       C  
ATOM   4263  N   CYS C 565      37.061  11.467 -12.501  1.00 54.96           N  
ANISOU 4263  N   CYS C 565     6846   8261   5774   2391  -2178  -1511       N  
ATOM   4264  CA  CYS C 565      37.885  11.575 -13.696  1.00 61.77           C  
ANISOU 4264  CA  CYS C 565     7646   9069   6756   2336  -2179  -1593       C  
ATOM   4265  C   CYS C 565      38.505  10.229 -14.055  1.00 70.95           C  
ANISOU 4265  C   CYS C 565     8826  10193   7938   2383  -2213  -1544       C  
ATOM   4266  O   CYS C 565      38.829   9.417 -13.185  1.00 75.75           O  
ANISOU 4266  O   CYS C 565     9467  10842   8472   2471  -2252  -1494       O  
ATOM   4267  CB  CYS C 565      38.991  12.612 -13.503  1.00 67.80           C  
ANISOU 4267  CB  CYS C 565     8319   9890   7551   2328  -2196  -1742       C  
ATOM   4268  SG  CYS C 565      38.419  14.305 -13.216  1.00 70.67           S  
ANISOU 4268  SG  CYS C 565     8649  10282   7921   2264  -2162  -1821       S  
ATOM   4269  N   ALA C 566      38.677  10.007 -15.360  1.00 69.60           N  
ANISOU 4269  N   ALA C 566     8630   9945   7869   2325  -2197  -1562       N  
ATOM   4270  CA  ALA C 566      39.238   8.751 -15.843  1.00 62.79           C  
ANISOU 4270  CA  ALA C 566     7782   9037   7039   2366  -2227  -1526       C  
ATOM   4271  C   ALA C 566      40.759   8.728 -15.769  1.00 62.99           C  
ANISOU 4271  C   ALA C 566     7736   9113   7083   2410  -2268  -1634       C  
ATOM   4272  O   ALA C 566      41.351   7.650 -15.637  1.00 63.06           O  
ANISOU 4272  O   ALA C 566     7763   9117   7081   2481  -2309  -1604       O  
ATOM   4273  CB  ALA C 566      38.783   8.491 -17.280  1.00 54.69           C  
ANISOU 4273  CB  ALA C 566     6758   7912   6110   2293  -2194  -1505       C  
ATOM   4274  N   HIS C 567      41.407   9.889 -15.855  1.00 67.57           N  
ANISOU 4274  N   HIS C 567     8234   9742   7697   2369  -2257  -1755       N  
ATOM   4275  CA  HIS C 567      42.863   9.941 -15.823  1.00 69.37           C  
ANISOU 4275  CA  HIS C 567     8386  10023   7949   2403  -2293  -1859       C  
ATOM   4276  C   HIS C 567      43.348  10.967 -14.809  1.00 68.09           C  
ANISOU 4276  C   HIS C 567     8177   9951   7743   2420  -2309  -1943       C  
ATOM   4277  O   HIS C 567      43.546  10.632 -13.637  1.00 69.96           O  
ANISOU 4277  O   HIS C 567     8442  10251   7889   2507  -2350  -1925       O  
ATOM   4278  CB  HIS C 567      43.412  10.238 -17.218  1.00 71.69           C  
ANISOU 4278  CB  HIS C 567     8606  10276   8355   2328  -2264  -1930       C  
ATOM   4279  CG  HIS C 567      43.013   9.222 -18.241  1.00 75.68           C  
ANISOU 4279  CG  HIS C 567     9153  10697   8906   2318  -2252  -1862       C  
ATOM   4280  ND1 HIS C 567      43.361   7.892 -18.142  1.00 74.68           N  
ANISOU 4280  ND1 HIS C 567     9066  10551   8758   2399  -2295  -1814       N  
ATOM   4281  CD2 HIS C 567      42.281   9.335 -19.375  1.00 78.12           C  
ANISOU 4281  CD2 HIS C 567     9468  10934   9282   2238  -2205  -1835       C  
ATOM   4282  CE1 HIS C 567      42.868   7.231 -19.174  1.00 75.65           C  
ANISOU 4282  CE1 HIS C 567     9218  10589   8936   2369  -2276  -1765       C  
ATOM   4283  NE2 HIS C 567      42.208   8.084 -19.937  1.00 77.40           N  
ANISOU 4283  NE2 HIS C 567     9419  10781   9209   2273  -2221  -1777       N  
ATOM   4284  N   TYR C 568      43.541  12.214 -15.227  1.00 62.91           N  
ANISOU 4284  N   TYR C 568     7449   9302   7151   2340  -2281  -2033       N  
ATOM   4285  CA  TYR C 568      44.006  13.227 -14.294  1.00 61.07           C  
ANISOU 4285  CA  TYR C 568     7168   9146   6888   2353  -2300  -2120       C  
ATOM   4286  C   TYR C 568      42.967  14.330 -14.171  1.00 57.69           C  
ANISOU 4286  C   TYR C 568     6754   8705   6463   2287  -2260  -2119       C  
ATOM   4287  O   TYR C 568      42.007  14.400 -14.938  1.00 57.06           O  
ANISOU 4287  O   TYR C 568     6706   8555   6420   2220  -2215  -2061       O  
ATOM   4288  CB  TYR C 568      45.365  13.792 -14.723  1.00 63.63           C  
ANISOU 4288  CB  TYR C 568     7384   9502   7289   2326  -2314  -2241       C  
ATOM   4289  CG  TYR C 568      46.432  12.729 -14.835  1.00 69.50           C  
ANISOU 4289  CG  TYR C 568     8110  10267   8028   2396  -2355  -2252       C  
ATOM   4290  CD1 TYR C 568      46.831  12.001 -13.721  1.00 75.05           C  
ANISOU 4290  CD1 TYR C 568     8847  11030   8638   2508  -2410  -2235       C  
ATOM   4291  CD2 TYR C 568      47.038  12.451 -16.052  1.00 69.08           C  
ANISOU 4291  CD2 TYR C 568     8007  10179   8062   2355  -2338  -2278       C  
ATOM   4292  CE1 TYR C 568      47.805  11.023 -13.817  1.00 78.62           C  
ANISOU 4292  CE1 TYR C 568     9284  11500   9088   2576  -2450  -2245       C  
ATOM   4293  CE2 TYR C 568      48.013  11.477 -16.158  1.00 73.06           C  
ANISOU 4293  CE2 TYR C 568     8494  10705   8562   2424  -2377  -2293       C  
ATOM   4294  CZ  TYR C 568      48.393  10.767 -15.038  1.00 77.49           C  
ANISOU 4294  CZ  TYR C 568     9090  11319   9034   2534  -2434  -2277       C  
ATOM   4295  OH  TYR C 568      49.364   9.797 -15.142  1.00 76.66           O  
ANISOU 4295  OH  TYR C 568     8969  11233   8926   2606  -2475  -2293       O  
ATOM   4296  N   LYS C 569      43.152  15.183 -13.169  1.00 59.43           N  
ANISOU 4296  N   LYS C 569     6949   8992   6641   2311  -2281  -2185       N  
ATOM   4297  CA  LYS C 569      42.289  16.337 -12.960  1.00 65.17           C  
ANISOU 4297  CA  LYS C 569     7678   9711   7371   2255  -2250  -2203       C  
ATOM   4298  C   LYS C 569      43.153  17.586 -12.906  1.00 66.31           C  
ANISOU 4298  C   LYS C 569     7728   9885   7584   2212  -2263  -2333       C  
ATOM   4299  O   LYS C 569      44.063  17.684 -12.077  1.00 68.46           O  
ANISOU 4299  O   LYS C 569     7962  10230   7821   2275  -2312  -2403       O  
ATOM   4300  CB  LYS C 569      41.454  16.197 -11.683  1.00 63.75           C  
ANISOU 4300  CB  LYS C 569     7572   9585   7064   2331  -2261  -2149       C  
ATOM   4301  CG  LYS C 569      40.417  17.305 -11.511  1.00 62.46           C  
ANISOU 4301  CG  LYS C 569     7421   9412   6901   2279  -2226  -2159       C  
ATOM   4302  CD  LYS C 569      39.643  17.175 -10.205  1.00 69.13           C  
ANISOU 4302  CD  LYS C 569     8330  10326   7610   2362  -2235  -2111       C  
ATOM   4303  CE  LYS C 569      38.369  16.363 -10.386  1.00 69.44           C  
ANISOU 4303  CE  LYS C 569     8462  10327   7596   2363  -2198  -1968       C  
ATOM   4304  NZ  LYS C 569      37.697  16.075  -9.089  1.00 66.53           N  
ANISOU 4304  NZ  LYS C 569     8154  10038   7085   2451  -2206  -1904       N  
ATOM   4305  N   ASP C 570      42.887  18.510 -13.812  1.00 62.82           N  
ANISOU 4305  N   ASP C 570     7245   9383   7240   2104  -2222  -2360       N  
ATOM   4306  CA  ASP C 570      43.373  19.878 -13.793  1.00 64.14           C  
ANISOU 4306  CA  ASP C 570     7333   9558   7479   2043  -2227  -2465       C  
ATOM   4307  C   ASP C 570      42.217  20.747 -13.314  1.00 58.97           C  
ANISOU 4307  C   ASP C 570     6718   8891   6799   2021  -2206  -2457       C  
ATOM   4308  O   ASP C 570      41.512  21.339 -14.141  1.00 57.07           O  
ANISOU 4308  O   ASP C 570     6477   8580   6627   1930  -2159  -2436       O  
ATOM   4309  CB  ASP C 570      43.852  20.290 -15.187  1.00 68.63           C  
ANISOU 4309  CB  ASP C 570     7831  10068   8177   1934  -2193  -2489       C  
ATOM   4310  CG  ASP C 570      44.650  21.575 -15.180  1.00 74.77           C  
ANISOU 4310  CG  ASP C 570     8516  10858   9036   1873  -2207  -2598       C  
ATOM   4311  OD1 ASP C 570      45.092  21.994 -14.092  1.00 73.71           O  
ANISOU 4311  OD1 ASP C 570     8361  10785   8860   1929  -2254  -2669       O  
ATOM   4312  OD2 ASP C 570      44.841  22.160 -16.268  1.00 78.27           O  
ANISOU 4312  OD2 ASP C 570     8904  11251   9584   1770  -2173  -2611       O  
ATOM   4313  N   PRO C 571      41.972  20.824 -11.990  1.00 54.68           N  
ANISOU 4313  N   PRO C 571     6207   8416   6153   2107  -2238  -2473       N  
ATOM   4314  CA  PRO C 571      40.761  21.397 -11.386  1.00 61.92           C  
ANISOU 4314  CA  PRO C 571     7177   9337   7014   2114  -2219  -2451       C  
ATOM   4315  C   PRO C 571      40.359  22.718 -12.037  1.00 62.09           C  
ANISOU 4315  C   PRO C 571     7159   9292   7140   2006  -2187  -2498       C  
ATOM   4316  O   PRO C 571      41.194  23.604 -12.159  1.00 69.45           O  
ANISOU 4316  O   PRO C 571     8014  10222   8154   1961  -2208  -2594       O  
ATOM   4317  CB  PRO C 571      41.144  21.626  -9.917  1.00 59.94           C  
ANISOU 4317  CB  PRO C 571     6919   9186   6670   2214  -2272  -2517       C  
ATOM   4318  CG  PRO C 571      42.414  20.883  -9.691  1.00 55.15           C  
ANISOU 4318  CG  PRO C 571     6279   8630   6048   2274  -2318  -2546       C  
ATOM   4319  CD  PRO C 571      42.921  20.337 -10.981  1.00 52.56           C  
ANISOU 4319  CD  PRO C 571     5924   8236   5811   2210  -2297  -2516       C  
ATOM   4320  N   PRO C 572      39.075  22.853 -12.443  1.00 56.09           N  
ANISOU 4320  N   PRO C 572     6454   8479   6377   1962  -2139  -2427       N  
ATOM   4321  CA  PRO C 572      37.958  21.917 -12.207  1.00 54.52           C  
ANISOU 4321  CA  PRO C 572     6351   8288   6078   2012  -2115  -2312       C  
ATOM   4322  C   PRO C 572      37.776  20.776 -13.223  1.00 49.55           C  
ANISOU 4322  C   PRO C 572     5756   7603   5468   1986  -2087  -2212       C  
ATOM   4323  O   PRO C 572      36.764  20.101 -13.136  1.00 48.84           O  
ANISOU 4323  O   PRO C 572     5743   7505   5310   2011  -2064  -2112       O  
ATOM   4324  CB  PRO C 572      36.733  22.827 -12.245  1.00 53.00           C  
ANISOU 4324  CB  PRO C 572     6185   8061   5893   1964  -2077  -2304       C  
ATOM   4325  CG  PRO C 572      37.130  24.017 -13.034  1.00 51.25           C  
ANISOU 4325  CG  PRO C 572     5889   7777   5807   1860  -2068  -2383       C  
ATOM   4326  CD  PRO C 572      38.626  24.135 -13.013  1.00 57.47           C  
ANISOU 4326  CD  PRO C 572     6598   8590   6648   1863  -2110  -2468       C  
ATOM   4327  N   PHE C 573      38.714  20.574 -14.144  1.00 48.88           N  
ANISOU 4327  N   PHE C 573     5616   7484   5473   1940  -2089  -2237       N  
ATOM   4328  CA  PHE C 573      38.453  19.800 -15.353  1.00 54.19           C  
ANISOU 4328  CA  PHE C 573     6308   8088   6194   1892  -2054  -2160       C  
ATOM   4329  C   PHE C 573      39.130  18.437 -15.332  1.00 62.48           C  
ANISOU 4329  C   PHE C 573     7375   9160   7206   1963  -2083  -2120       C  
ATOM   4330  O   PHE C 573      40.316  18.337 -15.021  1.00 60.69           O  
ANISOU 4330  O   PHE C 573     7097   8980   6984   2002  -2123  -2186       O  
ATOM   4331  CB  PHE C 573      38.907  20.572 -16.589  1.00 47.07           C  
ANISOU 4331  CB  PHE C 573     5331   7128   5427   1780  -2026  -2208       C  
ATOM   4332  CG  PHE C 573      38.092  21.795 -16.856  1.00 42.20           C  
ANISOU 4332  CG  PHE C 573     4707   6466   4860   1698  -1991  -2224       C  
ATOM   4333  CD1 PHE C 573      38.580  23.054 -16.544  1.00 47.78           C  
ANISOU 4333  CD1 PHE C 573     5351   7184   5619   1663  -2006  -2321       C  
ATOM   4334  CD2 PHE C 573      36.831  21.687 -17.411  1.00 39.10           C  
ANISOU 4334  CD2 PHE C 573     4372   6017   4465   1657  -1946  -2144       C  
ATOM   4335  CE1 PHE C 573      37.825  24.182 -16.789  1.00 51.75           C  
ANISOU 4335  CE1 PHE C 573     5850   7639   6172   1590  -1977  -2335       C  
ATOM   4336  CE2 PHE C 573      36.069  22.809 -17.659  1.00 41.79           C  
ANISOU 4336  CE2 PHE C 573     4708   6316   4853   1585  -1914  -2159       C  
ATOM   4337  CZ  PHE C 573      36.566  24.060 -17.348  1.00 50.31           C  
ANISOU 4337  CZ  PHE C 573     5727   7403   5985   1552  -1930  -2254       C  
ATOM   4338  N   CYS C 574      38.380  17.394 -15.694  1.00 62.04           N  
ANISOU 4338  N   CYS C 574     7390   9065   7117   1978  -2066  -2012       N  
ATOM   4339  CA  CYS C 574      38.985  16.099 -15.991  1.00 61.88           C  
ANISOU 4339  CA  CYS C 574     7384   9039   7090   2027  -2089  -1971       C  
ATOM   4340  C   CYS C 574      39.789  16.211 -17.281  1.00 64.60           C  
ANISOU 4340  C   CYS C 574     7655   9341   7550   1957  -2073  -2020       C  
ATOM   4341  O   CYS C 574      39.259  16.634 -18.314  1.00 66.30           O  
ANISOU 4341  O   CYS C 574     7858   9495   7838   1868  -2028  -2006       O  
ATOM   4342  CB  CYS C 574      37.911  15.022 -16.127  1.00 59.42           C  
ANISOU 4342  CB  CYS C 574     7164   8684   6728   2050  -2075  -1841       C  
ATOM   4343  SG  CYS C 574      36.993  14.611 -14.629  1.00 59.67           S  
ANISOU 4343  SG  CYS C 574     7286   8776   6612   2142  -2090  -1753       S  
ATOM   4344  N   VAL C 575      41.062  15.832 -17.225  1.00 63.71           N  
ANISOU 4344  N   VAL C 575     7491   9267   7450   1999  -2109  -2076       N  
ATOM   4345  CA  VAL C 575      41.961  15.944 -18.364  1.00 64.78           C  
ANISOU 4345  CA  VAL C 575     7548   9382   7685   1942  -2096  -2129       C  
ATOM   4346  C   VAL C 575      42.684  14.623 -18.592  1.00 73.86           C  
ANISOU 4346  C   VAL C 575     8705  10536   8821   2011  -2126  -2110       C  
ATOM   4347  O   VAL C 575      42.902  13.832 -17.665  1.00 78.04           O  
ANISOU 4347  O   VAL C 575     9277  11105   9270   2108  -2171  -2086       O  
ATOM   4348  CB  VAL C 575      42.982  17.091 -18.185  1.00 53.34           C  
ANISOU 4348  CB  VAL C 575     6001   7980   6286   1907  -2108  -2243       C  
ATOM   4349  CG1 VAL C 575      42.270  18.433 -18.105  1.00 46.28           C  
ANISOU 4349  CG1 VAL C 575     5097   7065   5423   1830  -2078  -2265       C  
ATOM   4350  CG2 VAL C 575      43.838  16.858 -16.951  1.00 49.41           C  
ANISOU 4350  CG2 VAL C 575     5494   7564   5717   2005  -2168  -2293       C  
ATOM   4351  N   ALA C 576      43.060  14.398 -19.856  1.00 75.13           N  
ANISOU 4351  N   ALA C 576     8823  10660   9061   1961  -2100  -2120       N  
ATOM   4352  CA  ALA C 576      43.837  13.217 -20.220  1.00 71.66           C  
ANISOU 4352  CA  ALA C 576     8380  10224   8623   2022  -2127  -2117       C  
ATOM   4353  C   ALA C 576      45.271  13.323 -19.710  1.00 76.21           C  
ANISOU 4353  C   ALA C 576     8884  10879   9194   2071  -2170  -2208       C  
ATOM   4354  O   ALA C 576      45.786  12.388 -19.085  1.00 77.17           O  
ANISOU 4354  O   ALA C 576     9031  11031   9259   2168  -2218  -2201       O  
ATOM   4355  CB  ALA C 576      43.814  13.021 -21.738  1.00 65.96           C  
ANISOU 4355  CB  ALA C 576     7628   9449   7985   1956  -2085  -2110       C  
ATOM   4356  N   ARG C 577      45.935  14.453 -19.970  1.00 81.33           N  
ANISOU 4356  N   ARG C 577     9439  11558   9903   2004  -2155  -2293       N  
ATOM   4357  CA  ARG C 577      47.256  14.721 -19.414  1.00 87.65           C  
ANISOU 4357  CA  ARG C 577    10165  12436  10701   2042  -2196  -2384       C  
ATOM   4358  C   ARG C 577      47.281  16.092 -18.755  1.00 86.77           C  
ANISOU 4358  C   ARG C 577    10013  12356  10601   1996  -2198  -2444       C  
ATOM   4359  O   ARG C 577      46.512  16.992 -19.110  1.00 89.32           O  
ANISOU 4359  O   ARG C 577    10336  12636  10964   1910  -2157  -2431       O  
ATOM   4360  CB  ARG C 577      48.372  14.663 -20.476  1.00 95.25           C  
ANISOU 4360  CB  ARG C 577    11034  13417  11738   2008  -2184  -2442       C  
ATOM   4361  CG  ARG C 577      48.517  13.319 -21.171  1.00104.85           C  
ANISOU 4361  CG  ARG C 577    12279  14609  12950   2060  -2188  -2403       C  
ATOM   4362  CD  ARG C 577      47.880  13.377 -22.578  1.00113.01           C  
ANISOU 4362  CD  ARG C 577    13310  15578  14051   1973  -2126  -2363       C  
ATOM   4363  NE  ARG C 577      47.400  12.037 -22.972  1.00118.33           N  
ANISOU 4363  NE  ARG C 577    14059  16201  14701   2030  -2132  -2295       N  
ATOM   4364  CZ  ARG C 577      46.763  11.774 -24.124  1.00117.59           C  
ANISOU 4364  CZ  ARG C 577    13982  16047  14652   1979  -2089  -2253       C  
ATOM   4365  NH1 ARG C 577      46.365  10.529 -24.369  1.00118.20           N  
ANISOU 4365  NH1 ARG C 577    14129  16074  14708   2038  -2105  -2197       N  
ATOM   4366  NH2 ARG C 577      46.539  12.741 -25.019  1.00118.26           N  
ANISOU 4366  NH2 ARG C 577    14012  16121  14801   1872  -2032  -2266       N  
ATOM   4367  N   CYS C 578      48.191  16.241 -17.802  1.00 82.57           N  
ANISOU 4367  N   CYS C 578     9442  11896  10033   2056  -2250  -2513       N  
ATOM   4368  CA  CYS C 578      48.578  17.572 -17.384  1.00 80.16           C  
ANISOU 4368  CA  CYS C 578     9070  11623   9764   2006  -2258  -2596       C  
ATOM   4369  C   CYS C 578      49.264  18.282 -18.548  1.00 82.76           C  
ANISOU 4369  C   CYS C 578     9300  11941  10205   1901  -2224  -2645       C  
ATOM   4370  O   CYS C 578      50.141  17.706 -19.204  1.00 86.29           O  
ANISOU 4370  O   CYS C 578     9698  12410  10679   1911  -2226  -2663       O  
ATOM   4371  CB  CYS C 578      49.495  17.510 -16.164  1.00 84.36           C  
ANISOU 4371  CB  CYS C 578     9577  12239  10236   2097  -2324  -2665       C  
ATOM   4372  SG  CYS C 578      48.718  16.745 -14.703  1.00 92.99           S  
ANISOU 4372  SG  CYS C 578    10783  13363  11187   2222  -2363  -2603       S  
ATOM   4373  N   PRO C 579      48.870  19.513 -18.847  1.00 83.84           N  
ANISOU 4373  N   PRO C 579     9407  12045  10406   1800  -2193  -2663       N  
ATOM   4374  CA  PRO C 579      49.379  20.195 -20.043  1.00 86.85           C  
ANISOU 4374  CA  PRO C 579     9700  12409  10892   1689  -2155  -2689       C  
ATOM   4375  C   PRO C 579      50.854  20.540 -19.907  1.00 99.77           C  
ANISOU 4375  C   PRO C 579    11231  14113  12563   1688  -2191  -2783       C  
ATOM   4376  O   PRO C 579      51.338  20.876 -18.823  1.00101.10           O  
ANISOU 4376  O   PRO C 579    11383  14330  12701   1737  -2243  -2846       O  
ATOM   4377  CB  PRO C 579      48.502  21.450 -20.132  1.00 77.76           C  
ANISOU 4377  CB  PRO C 579     8556  11201   9788   1594  -2123  -2681       C  
ATOM   4378  CG  PRO C 579      47.958  21.636 -18.738  1.00 79.67           C  
ANISOU 4378  CG  PRO C 579     8858  11459   9953   1665  -2162  -2694       C  
ATOM   4379  CD  PRO C 579      47.881  20.304 -18.101  1.00 82.90           C  
ANISOU 4379  CD  PRO C 579     9336  11901  10260   1786  -2191  -2654       C  
ATOM   4380  N   SER C 580      51.570  20.447 -21.024  1.00105.11           N  
ANISOU 4380  N   SER C 580    11834  14799  13302   1634  -2164  -2791       N  
ATOM   4381  CA  SER C 580      53.027  20.517 -21.002  1.00104.40           C  
ANISOU 4381  CA  SER C 580    11645  14784  13239   1644  -2198  -2871       C  
ATOM   4382  C   SER C 580      53.598  21.273 -22.201  1.00105.08           C  
ANISOU 4382  C   SER C 580    11630  14870  13426   1522  -2157  -2889       C  
ATOM   4383  O   SER C 580      52.861  21.842 -23.004  1.00106.18           O  
ANISOU 4383  O   SER C 580    11777  14950  13618   1427  -2105  -2841       O  
ATOM   4384  CB  SER C 580      53.610  19.103 -20.954  1.00100.50           C  
ANISOU 4384  CB  SER C 580    11167  14335  12685   1755  -2224  -2866       C  
ATOM   4385  OG  SER C 580      53.097  18.381 -19.848  1.00 99.23           O  
ANISOU 4385  OG  SER C 580    11100  14175  12429   1865  -2263  -2841       O  
ATOM   4386  N   TYR C 588      48.177  32.315 -20.904  1.00 88.99           N  
ANISOU 4386  N   TYR C 588     9643  12284  11884    837  -2113  -2983       N  
ATOM   4387  CA  TYR C 588      49.107  33.122 -21.688  1.00 92.78           C  
ANISOU 4387  CA  TYR C 588    10022  12749  12481    719  -2112  -3004       C  
ATOM   4388  C   TYR C 588      50.484  32.894 -21.143  1.00 95.73           C  
ANISOU 4388  C   TYR C 588    10320  13204  12847    761  -2169  -3085       C  
ATOM   4389  O   TYR C 588      51.430  32.640 -21.890  1.00 94.96           O  
ANISOU 4389  O   TYR C 588    10145  13147  12788    716  -2157  -3076       O  
ATOM   4390  CB  TYR C 588      48.720  34.598 -21.652  1.00 94.72           C  
ANISOU 4390  CB  TYR C 588    10258  12908  12824    628  -2123  -3032       C  
ATOM   4391  CG  TYR C 588      47.556  34.829 -22.562  1.00102.03           C  
ANISOU 4391  CG  TYR C 588    11236  13754  13778    561  -2057  -2940       C  
ATOM   4392  CD1 TYR C 588      46.819  33.747 -23.011  1.00103.60           C  
ANISOU 4392  CD1 TYR C 588    11501  13966  13898    607  -2007  -2857       C  
ATOM   4393  CD2 TYR C 588      47.210  36.094 -23.006  1.00102.57           C  
ANISOU 4393  CD2 TYR C 588    11287  13732  13952    451  -2047  -2933       C  
ATOM   4394  CE1 TYR C 588      45.780  33.891 -23.833  1.00104.38           C  
ANISOU 4394  CE1 TYR C 588    11645  13999  14017    550  -1949  -2775       C  
ATOM   4395  CE2 TYR C 588      46.139  36.256 -23.860  1.00103.95           C  
ANISOU 4395  CE2 TYR C 588    11511  13838  14148    394  -1986  -2846       C  
ATOM   4396  CZ  TYR C 588      45.438  35.126 -24.265  1.00108.66           C  
ANISOU 4396  CZ  TYR C 588    12170  14457  14658    446  -1937  -2768       C  
ATOM   4397  OH  TYR C 588      44.368  35.142 -25.096  1.00112.21           O  
ANISOU 4397  OH  TYR C 588    12670  14848  15117    400  -1878  -2682       O  
ATOM   4398  N   MET C 589      50.572  32.983 -19.825  1.00 99.83           N  
ANISOU 4398  N   MET C 589    10860  13755  13314    851  -2230  -3164       N  
ATOM   4399  CA  MET C 589      51.691  32.421 -19.094  1.00104.72           C  
ANISOU 4399  CA  MET C 589    11433  14467  13886    933  -2285  -3234       C  
ATOM   4400  C   MET C 589      51.972  31.040 -19.667  1.00106.71           C  
ANISOU 4400  C   MET C 589    11693  14777  14074    984  -2252  -3173       C  
ATOM   4401  O   MET C 589      51.050  30.224 -19.788  1.00108.72           O  
ANISOU 4401  O   MET C 589    12033  15020  14257   1036  -2214  -3101       O  
ATOM   4402  CB  MET C 589      51.370  32.330 -17.603  1.00108.12           C  
ANISOU 4402  CB  MET C 589    11921  14933  14228   1054  -2340  -3298       C  
ATOM   4403  CG  MET C 589      51.131  33.668 -16.932  1.00114.76           C  
ANISOU 4403  CG  MET C 589    12753  15724  15126   1021  -2382  -3373       C  
ATOM   4404  SD  MET C 589      51.984  33.762 -15.351  1.00123.31           S  
ANISOU 4404  SD  MET C 589    13804  16893  16155   1131  -2478  -3506       S  
ATOM   4405  CE  MET C 589      51.332  32.303 -14.546  1.00122.64           C  
ANISOU 4405  CE  MET C 589    13821  16882  15896   1294  -2472  -3458       C  
ATOM   4406  N   PRO C 590      53.204  30.759 -20.082  1.00106.88           N  
ANISOU 4406  N   PRO C 590    11626  14858  14126    966  -2263  -3199       N  
ATOM   4407  CA  PRO C 590      53.533  29.402 -20.537  1.00103.65           C  
ANISOU 4407  CA  PRO C 590    11224  14508  13652   1030  -2239  -3153       C  
ATOM   4408  C   PRO C 590      53.401  28.432 -19.374  1.00 99.03           C  
ANISOU 4408  C   PRO C 590    10706  13976  12944   1181  -2280  -3174       C  
ATOM   4409  O   PRO C 590      53.976  28.644 -18.305  1.00 95.80           O  
ANISOU 4409  O   PRO C 590    10274  13614  12510   1240  -2343  -3258       O  
ATOM   4410  CB  PRO C 590      54.985  29.525 -21.018  1.00107.29           C  
ANISOU 4410  CB  PRO C 590    11562  15028  14175    980  -2257  -3199       C  
ATOM   4411  CG  PRO C 590      55.238  31.006 -21.147  1.00109.59           C  
ANISOU 4411  CG  PRO C 590    11786  15271  14581    858  -2271  -3239       C  
ATOM   4412  CD  PRO C 590      54.366  31.657 -20.127  1.00109.35           C  
ANISOU 4412  CD  PRO C 590    11827  15189  14534    889  -2302  -3273       C  
ATOM   4413  N   ILE C 591      52.619  27.377 -19.576  1.00 97.88           N  
ANISOU 4413  N   ILE C 591    10644  13823  12724   1244  -2244  -3096       N  
ATOM   4414  CA  ILE C 591      52.204  26.502 -18.486  1.00 98.58           C  
ANISOU 4414  CA  ILE C 591    10815  13946  12694   1380  -2276  -3092       C  
ATOM   4415  C   ILE C 591      52.943  25.174 -18.599  1.00 93.77           C  
ANISOU 4415  C   ILE C 591    10198  13404  12026   1465  -2286  -3081       C  
ATOM   4416  O   ILE C 591      53.080  24.611 -19.693  1.00 89.13           O  
ANISOU 4416  O   ILE C 591     9593  12809  11463   1432  -2243  -3030       O  
ATOM   4417  CB  ILE C 591      50.674  26.322 -18.460  1.00102.93           C  
ANISOU 4417  CB  ILE C 591    11476  14435  13199   1393  -2237  -3011       C  
ATOM   4418  CG1 ILE C 591      50.192  25.343 -19.522  1.00106.11           C  
ANISOU 4418  CG1 ILE C 591    11918  14812  13588   1386  -2179  -2915       C  
ATOM   4419  CG2 ILE C 591      49.971  27.641 -18.680  1.00102.33           C  
ANISOU 4419  CG2 ILE C 591    11398  14283  13198   1291  -2215  -3014       C  
ATOM   4420  CD1 ILE C 591      48.837  24.834 -19.226  1.00107.46           C  
ANISOU 4420  CD1 ILE C 591    12201  14944  13686   1435  -2157  -2840       C  
ATOM   4421  N   TRP C 592      53.460  24.707 -17.465  1.00 94.95           N  
ANISOU 4421  N   TRP C 592    10356  13622  12101   1576  -2346  -3133       N  
ATOM   4422  CA  TRP C 592      54.133  23.418 -17.341  1.00 97.86           C  
ANISOU 4422  CA  TRP C 592    10726  14053  12402   1677  -2368  -3128       C  
ATOM   4423  C   TRP C 592      53.638  22.792 -16.047  1.00 94.59           C  
ANISOU 4423  C   TRP C 592    10400  13669  11871   1805  -2409  -3120       C  
ATOM   4424  O   TRP C 592      53.885  23.330 -14.963  1.00102.28           O  
ANISOU 4424  O   TRP C 592    11362  14682  12819   1845  -2460  -3190       O  
ATOM   4425  CB  TRP C 592      55.653  23.577 -17.319  1.00106.17           C  
ANISOU 4425  CB  TRP C 592    11667  15178  13494   1674  -2410  -3215       C  
ATOM   4426  CG  TRP C 592      56.246  24.054 -18.604  1.00111.58           C  
ANISOU 4426  CG  TRP C 592    12260  15852  14284   1555  -2370  -3216       C  
ATOM   4427  CD1 TRP C 592      56.617  25.330 -18.911  1.00113.94           C  
ANISOU 4427  CD1 TRP C 592    12478  16131  14682   1439  -2369  -3260       C  
ATOM   4428  CD2 TRP C 592      56.556  23.258 -19.753  1.00113.64           C  
ANISOU 4428  CD2 TRP C 592    12497  16122  14558   1541  -2328  -3168       C  
ATOM   4429  NE1 TRP C 592      57.132  25.380 -20.184  1.00114.69           N  
ANISOU 4429  NE1 TRP C 592    12499  16229  14849   1351  -2326  -3236       N  
ATOM   4430  CE2 TRP C 592      57.105  24.121 -20.722  1.00115.25           C  
ANISOU 4430  CE2 TRP C 592    12602  16320  14866   1414  -2299  -3183       C  
ATOM   4431  CE3 TRP C 592      56.418  21.901 -20.058  1.00114.04           C  
ANISOU 4431  CE3 TRP C 592    12601  16186  14545   1625  -2313  -3115       C  
ATOM   4432  CZ2 TRP C 592      57.517  23.670 -21.974  1.00116.66           C  
ANISOU 4432  CZ2 TRP C 592    12730  16516  15078   1372  -2253  -3147       C  
ATOM   4433  CZ3 TRP C 592      56.828  21.455 -21.301  1.00115.48           C  
ANISOU 4433  CZ3 TRP C 592    12735  16377  14765   1585  -2271  -3087       C  
ATOM   4434  CH2 TRP C 592      57.370  22.337 -22.244  1.00116.75           C  
ANISOU 4434  CH2 TRP C 592    12794  16542  15022   1462  -2239  -3104       C  
ATOM   4435  N   LYS C 593      52.941  21.665 -16.152  1.00 85.51           N  
ANISOU 4435  N   LYS C 593     9336  12501  10650   1869  -2387  -3035       N  
ATOM   4436  CA  LYS C 593      52.293  21.061 -15.000  1.00 81.65           C  
ANISOU 4436  CA  LYS C 593     8941  12035  10049   1981  -2417  -3005       C  
ATOM   4437  C   LYS C 593      52.624  19.575 -14.933  1.00 80.40           C  
ANISOU 4437  C   LYS C 593     8821  11910   9817   2084  -2435  -2961       C  
ATOM   4438  O   LYS C 593      52.966  18.943 -15.936  1.00 82.41           O  
ANISOU 4438  O   LYS C 593     9055  12149  10108   2064  -2409  -2933       O  
ATOM   4439  CB  LYS C 593      50.775  21.291 -15.046  1.00 79.88           C  
ANISOU 4439  CB  LYS C 593     8805  11741   9806   1950  -2374  -2928       C  
ATOM   4440  CG  LYS C 593      50.411  22.772 -14.962  1.00 81.20           C  
ANISOU 4440  CG  LYS C 593     8941  11873  10037   1861  -2365  -2976       C  
ATOM   4441  CD  LYS C 593      48.974  23.050 -15.359  1.00 79.24           C  
ANISOU 4441  CD  LYS C 593     8764  11547   9795   1808  -2311  -2898       C  
ATOM   4442  CE  LYS C 593      48.052  22.983 -14.157  1.00 75.40           C  
ANISOU 4442  CE  LYS C 593     8362  11080   9206   1890  -2331  -2879       C  
ATOM   4443  NZ  LYS C 593      47.530  24.328 -13.790  1.00 67.41           N  
ANISOU 4443  NZ  LYS C 593     7340  10041   8231   1836  -2331  -2928       N  
ATOM   4444  N   PHE C 594      52.529  19.029 -13.727  1.00 77.16           N  
ANISOU 4444  N   PHE C 594     8466  11548   9301   2197  -2482  -2958       N  
ATOM   4445  CA  PHE C 594      52.882  17.649 -13.449  1.00 75.68           C  
ANISOU 4445  CA  PHE C 594     8319  11397   9037   2307  -2511  -2919       C  
ATOM   4446  C   PHE C 594      51.822  17.057 -12.504  1.00 83.51           C  
ANISOU 4446  C   PHE C 594     9426  12388   9917   2390  -2521  -2840       C  
ATOM   4447  O   PHE C 594      51.159  17.798 -11.792  1.00 85.24           O  
ANISOU 4447  O   PHE C 594     9670  12612  10105   2384  -2522  -2850       O  
ATOM   4448  CB  PHE C 594      54.275  17.540 -12.816  1.00 67.38           C  
ANISOU 4448  CB  PHE C 594     7197  10437   7969   2374  -2575  -3011       C  
ATOM   4449  CG  PHE C 594      54.333  17.975 -11.379  1.00 63.65           C  
ANISOU 4449  CG  PHE C 594     6734  10029   7422   2444  -2629  -3063       C  
ATOM   4450  CD1 PHE C 594      54.223  17.048 -10.354  1.00 56.72           C  
ANISOU 4450  CD1 PHE C 594     5925   9201   6424   2570  -2670  -3025       C  
ATOM   4451  CD2 PHE C 594      54.500  19.310 -11.052  1.00 69.34           C  
ANISOU 4451  CD2 PHE C 594     7393  10761   8190   2385  -2640  -3150       C  
ATOM   4452  CE1 PHE C 594      54.275  17.444  -9.032  1.00 56.41           C  
ANISOU 4452  CE1 PHE C 594     5892   9231   6309   2638  -2718  -3074       C  
ATOM   4453  CE2 PHE C 594      54.554  19.712  -9.731  1.00 69.13           C  
ANISOU 4453  CE2 PHE C 594     7374  10799   8095   2455  -2692  -3206       C  
ATOM   4454  CZ  PHE C 594      54.442  18.778  -8.720  1.00 64.02           C  
ANISOU 4454  CZ  PHE C 594     6794  10210   7322   2583  -2729  -3169       C  
ATOM   4455  N   PRO C 595      51.682  15.724 -12.512  1.00 83.32           N  
ANISOU 4455  N   PRO C 595     9468  12359   9832   2467  -2529  -2762       N  
ATOM   4456  CA  PRO C 595      50.596  15.115 -11.717  1.00 83.61           C  
ANISOU 4456  CA  PRO C 595     9616  12389   9764   2535  -2532  -2667       C  
ATOM   4457  C   PRO C 595      50.942  14.851 -10.257  1.00 84.01           C  
ANISOU 4457  C   PRO C 595     9687  12529   9703   2651  -2594  -2687       C  
ATOM   4458  O   PRO C 595      51.920  14.157  -9.952  1.00 86.25           O  
ANISOU 4458  O   PRO C 595     9948  12865   9958   2727  -2641  -2713       O  
ATOM   4459  CB  PRO C 595      50.322  13.795 -12.458  1.00 83.93           C  
ANISOU 4459  CB  PRO C 595     9715  12374   9801   2558  -2516  -2570       C  
ATOM   4460  CG  PRO C 595      51.146  13.852 -13.734  1.00 82.84           C  
ANISOU 4460  CG  PRO C 595     9495  12210   9770   2492  -2495  -2620       C  
ATOM   4461  CD  PRO C 595      52.285  14.759 -13.429  1.00 81.49           C  
ANISOU 4461  CD  PRO C 595     9220  12108   9635   2477  -2524  -2741       C  
ATOM   4462  N   ASP C 596      50.124  15.402  -9.352  1.00 86.23           N  
ANISOU 4462  N   ASP C 596    10012  12833   9919   2667  -2593  -2675       N  
ATOM   4463  CA  ASP C 596      50.099  15.050  -7.933  1.00 89.34           C  
ANISOU 4463  CA  ASP C 596    10450  13311  10185   2781  -2641  -2663       C  
ATOM   4464  C   ASP C 596      49.841  13.552  -7.791  1.00 88.96           C  
ANISOU 4464  C   ASP C 596    10485  13255  10060   2863  -2651  -2543       C  
ATOM   4465  O   ASP C 596      49.307  12.917  -8.707  1.00 86.95           O  
ANISOU 4465  O   ASP C 596    10273  12919   9844   2823  -2614  -2459       O  
ATOM   4466  CB  ASP C 596      49.018  15.910  -7.231  1.00 97.37           C  
ANISOU 4466  CB  ASP C 596    11504  14338  11153   2768  -2621  -2656       C  
ATOM   4467  CG  ASP C 596      48.654  15.454  -5.808  1.00112.00           C  
ANISOU 4467  CG  ASP C 596    13422  16276  12857   2885  -2654  -2611       C  
ATOM   4468  OD1 ASP C 596      47.963  16.251  -5.129  1.00111.89           O  
ANISOU 4468  OD1 ASP C 596    13423  16291  12799   2886  -2645  -2631       O  
ATOM   4469  OD2 ASP C 596      49.010  14.350  -5.338  1.00125.53           O  
ANISOU 4469  OD2 ASP C 596    15172  18029  14494   2977  -2688  -2555       O  
ATOM   4470  N   GLU C 597      50.228  12.986  -6.646  1.00 88.75           N  
ANISOU 4470  N   GLU C 597    10483  13312   9927   2976  -2704  -2533       N  
ATOM   4471  CA  GLU C 597      50.016  11.569  -6.388  1.00 89.15           C  
ANISOU 4471  CA  GLU C 597    10614  13358   9902   3058  -2722  -2412       C  
ATOM   4472  C   GLU C 597      48.539  11.209  -6.284  1.00 88.56           C  
ANISOU 4472  C   GLU C 597    10640  13237   9772   3048  -2679  -2276       C  
ATOM   4473  O   GLU C 597      48.192  10.031  -6.424  1.00 97.12           O  
ANISOU 4473  O   GLU C 597    11794  14281  10827   3084  -2681  -2157       O  
ATOM   4474  CB  GLU C 597      50.740  11.155  -5.105  1.00 94.27           C  
ANISOU 4474  CB  GLU C 597    11261  14114  10443   3181  -2788  -2431       C  
ATOM   4475  CG  GLU C 597      52.107  11.798  -4.924  1.00103.49           C  
ANISOU 4475  CG  GLU C 597    12322  15349  11649   3194  -2833  -2583       C  
ATOM   4476  CD  GLU C 597      53.184  11.145  -5.762  1.00110.26           C  
ANISOU 4476  CD  GLU C 597    13131  16183  12581   3195  -2853  -2613       C  
ATOM   4477  OE1 GLU C 597      52.881  10.167  -6.493  1.00111.98           O  
ANISOU 4477  OE1 GLU C 597    13399  16328  12821   3190  -2834  -2519       O  
ATOM   4478  OE2 GLU C 597      54.360  11.598  -5.703  1.00112.95           O  
ANISOU 4478  OE2 GLU C 597    13379  16578  12958   3203  -2889  -2732       O  
ATOM   4479  N   GLU C 598      47.665  12.181  -6.035  1.00 81.71           N  
ANISOU 4479  N   GLU C 598     9782  12372   8891   3001  -2644  -2288       N  
ATOM   4480  CA  GLU C 598      46.231  11.921  -6.025  1.00 82.43           C  
ANISOU 4480  CA  GLU C 598     9963  12421   8938   2981  -2598  -2162       C  
ATOM   4481  C   GLU C 598      45.579  12.165  -7.381  1.00 74.92           C  
ANISOU 4481  C   GLU C 598     9013  11357   8095   2866  -2540  -2138       C  
ATOM   4482  O   GLU C 598      44.359  12.012  -7.504  1.00 72.59           O  
ANISOU 4482  O   GLU C 598     8787  11019   7776   2838  -2499  -2038       O  
ATOM   4483  CB  GLU C 598      45.533  12.769  -4.953  1.00 90.91           C  
ANISOU 4483  CB  GLU C 598    11052  13566   9924   3003  -2591  -2178       C  
ATOM   4484  CG  GLU C 598      44.647  11.950  -4.017  1.00100.01           C  
ANISOU 4484  CG  GLU C 598    12297  14760  10941   3081  -2588  -2038       C  
ATOM   4485  CD  GLU C 598      43.936  12.793  -2.973  1.00106.10           C  
ANISOU 4485  CD  GLU C 598    13081  15611  11620   3108  -2576  -2057       C  
ATOM   4486  OE1 GLU C 598      42.811  12.421  -2.577  1.00108.71           O  
ANISOU 4486  OE1 GLU C 598    13487  15950  11869   3125  -2544  -1935       O  
ATOM   4487  OE2 GLU C 598      44.498  13.823  -2.547  1.00106.51           O  
ANISOU 4487  OE2 GLU C 598    13066  15720  11683   3113  -2599  -2194       O  
ATOM   4488  N   GLY C 599      46.361  12.534  -8.396  1.00 70.44           N  
ANISOU 4488  N   GLY C 599     8371  10749   7645   2800  -2535  -2225       N  
ATOM   4489  CA  GLY C 599      45.867  12.706  -9.744  1.00 68.63           C  
ANISOU 4489  CA  GLY C 599     8137  10419   7520   2695  -2482  -2205       C  
ATOM   4490  C   GLY C 599      45.718  14.143 -10.198  1.00 76.64           C  
ANISOU 4490  C   GLY C 599     9089  11415   8615   2595  -2447  -2294       C  
ATOM   4491  O   GLY C 599      45.389  14.371 -11.369  1.00 79.68           O  
ANISOU 4491  O   GLY C 599     9461  11722   9093   2503  -2403  -2284       O  
ATOM   4492  N   ALA C 600      45.954  15.113  -9.321  1.00 77.34           N  
ANISOU 4492  N   ALA C 600     9139  11571   8674   2611  -2469  -2380       N  
ATOM   4493  CA  ALA C 600      45.748  16.517  -9.646  1.00 72.15           C  
ANISOU 4493  CA  ALA C 600     8428  10892   8095   2519  -2441  -2460       C  
ATOM   4494  C   ALA C 600      46.989  17.116 -10.300  1.00 74.01           C  
ANISOU 4494  C   ALA C 600     8556  11124   8439   2464  -2454  -2571       C  
ATOM   4495  O   ALA C 600      48.120  16.711 -10.023  1.00 81.86           O  
ANISOU 4495  O   ALA C 600     9507  12172   9423   2520  -2500  -2621       O  
ATOM   4496  CB  ALA C 600      45.381  17.312  -8.392  1.00 66.86           C  
ANISOU 4496  CB  ALA C 600     7766  10291   7346   2563  -2460  -2503       C  
ATOM   4497  N   CYS C 601      46.764  18.090 -11.178  1.00 69.04           N  
ANISOU 4497  N   CYS C 601     7882  10434   7914   2351  -2414  -2605       N  
ATOM   4498  CA  CYS C 601      47.849  18.748 -11.896  1.00 71.34           C  
ANISOU 4498  CA  CYS C 601     8070  10720   8318   2281  -2418  -2698       C  
ATOM   4499  C   CYS C 601      48.306  19.978 -11.118  1.00 76.44           C  
ANISOU 4499  C   CYS C 601     8654  11413   8977   2274  -2451  -2810       C  
ATOM   4500  O   CYS C 601      47.501  20.869 -10.828  1.00 75.63           O  
ANISOU 4500  O   CYS C 601     8569  11291   8878   2239  -2435  -2820       O  
ATOM   4501  CB  CYS C 601      47.411  19.141 -13.307  1.00 76.77           C  
ANISOU 4501  CB  CYS C 601     8740  11318   9113   2159  -2356  -2668       C  
ATOM   4502  SG  CYS C 601      46.983  17.758 -14.403  1.00 85.76           S  
ANISOU 4502  SG  CYS C 601     9936  12394  10255   2159  -2318  -2554       S  
ATOM   4503  N   GLN C 602      49.590  20.021 -10.783  1.00 79.67           N  
ANISOU 4503  N   GLN C 602     8990  11884   9397   2309  -2501  -2897       N  
ATOM   4504  CA  GLN C 602      50.225  21.163 -10.147  1.00 77.32           C  
ANISOU 4504  CA  GLN C 602     8619  11630   9130   2297  -2541  -3015       C  
ATOM   4505  C   GLN C 602      51.148  21.870 -11.131  1.00 73.81           C  
ANISOU 4505  C   GLN C 602     8071  11157   8819   2192  -2532  -3082       C  
ATOM   4506  O   GLN C 602      51.642  21.258 -12.084  1.00 78.03           O  
ANISOU 4506  O   GLN C 602     8578  11671   9397   2164  -2511  -3053       O  
ATOM   4507  CB  GLN C 602      51.038  20.729  -8.918  1.00 80.21           C  
ANISOU 4507  CB  GLN C 602     8975  12099   9402   2419  -2611  -3069       C  
ATOM   4508  CG  GLN C 602      50.389  19.646  -8.079  1.00 82.75           C  
ANISOU 4508  CG  GLN C 602     9396  12460   9585   2534  -2621  -2981       C  
ATOM   4509  CD  GLN C 602      49.140  20.125  -7.371  1.00 82.73           C  
ANISOU 4509  CD  GLN C 602     9460  12457   9516   2548  -2604  -2950       C  
ATOM   4510  OE1 GLN C 602      48.979  21.317  -7.112  1.00 81.76           O  
ANISOU 4510  OE1 GLN C 602     9302  12331   9431   2505  -2608  -3025       O  
ATOM   4511  NE2 GLN C 602      48.247  19.196  -7.054  1.00 86.31           N  
ANISOU 4511  NE2 GLN C 602    10011  12914   9871   2608  -2586  -2837       N  
ATOM   4512  N   PRO C 603      51.402  23.161 -10.938  1.00 72.57           N  
ANISOU 4512  N   PRO C 603     7850  10995   8726   2132  -2548  -3172       N  
ATOM   4513  CA  PRO C 603      52.365  23.858 -11.794  1.00 77.37           C  
ANISOU 4513  CA  PRO C 603     8353  11584   9458   2032  -2546  -3235       C  
ATOM   4514  C   PRO C 603      53.796  23.487 -11.430  1.00 83.03           C  
ANISOU 4514  C   PRO C 603     8998  12384  10166   2089  -2602  -3310       C  
ATOM   4515  O   PRO C 603      54.095  23.048 -10.318  1.00 80.68           O  
ANISOU 4515  O   PRO C 603     8720  12161   9775   2201  -2655  -3341       O  
ATOM   4516  CB  PRO C 603      52.097  25.344 -11.513  1.00 78.27           C  
ANISOU 4516  CB  PRO C 603     8435  11666   9637   1961  -2555  -3306       C  
ATOM   4517  CG  PRO C 603      50.848  25.386 -10.671  1.00 78.28           C  
ANISOU 4517  CG  PRO C 603     8530  11664   9550   2019  -2551  -3270       C  
ATOM   4518  CD  PRO C 603      50.773  24.073  -9.970  1.00 75.77           C  
ANISOU 4518  CD  PRO C 603     8278  11411   9100   2149  -2569  -3217       C  
ATOM   4519  N   CYS C 604      54.692  23.668 -12.411  1.00 89.35           N  
ANISOU 4519  N   CYS C 604     9711  13174  11063   2009  -2590  -3337       N  
ATOM   4520  CA  CYS C 604      56.091  23.389 -12.130  1.00 94.18           C  
ANISOU 4520  CA  CYS C 604    10244  13867  11675   2055  -2643  -3413       C  
ATOM   4521  C   CYS C 604      56.764  24.609 -11.507  1.00 99.40           C  
ANISOU 4521  C   CYS C 604    10824  14556  12387   2022  -2695  -3531       C  
ATOM   4522  O   CYS C 604      56.418  25.750 -11.830  1.00100.08           O  
ANISOU 4522  O   CYS C 604    10885  14583  12558   1919  -2677  -3552       O  
ATOM   4523  CB  CYS C 604      56.826  22.998 -13.408  1.00 92.05           C  
ANISOU 4523  CB  CYS C 604     9910  13587  11477   1993  -2610  -3393       C  
ATOM   4524  SG  CYS C 604      56.308  21.416 -14.107  1.00 92.24           S  
ANISOU 4524  SG  CYS C 604    10016  13589  11440   2050  -2565  -3274       S  
ATOM   4525  N   PRO C 605      57.721  24.396 -10.602  1.00103.11           N  
ANISOU 4525  N   PRO C 605    11253  15115  12809   2108  -2763  -3609       N  
ATOM   4526  CA  PRO C 605      58.360  25.530  -9.925  1.00106.94           C  
ANISOU 4526  CA  PRO C 605    11662  15629  13340   2085  -2820  -3729       C  
ATOM   4527  C   PRO C 605      59.757  25.835 -10.442  1.00116.87           C  
ANISOU 4527  C   PRO C 605    12796  16921  14688   2024  -2845  -3801       C  
ATOM   4528  O   PRO C 605      60.731  25.723  -9.691  1.00123.99           O  
ANISOU 4528  O   PRO C 605    13646  17906  15559   2093  -2911  -3884       O  
ATOM   4529  CB  PRO C 605      58.406  25.073  -8.460  1.00102.68           C  
ANISOU 4529  CB  PRO C 605    11166  15176  12674   2232  -2883  -3768       C  
ATOM   4530  CG  PRO C 605      58.115  23.549  -8.491  1.00101.54           C  
ANISOU 4530  CG  PRO C 605    11102  15054  12424   2330  -2863  -3668       C  
ATOM   4531  CD  PRO C 605      58.050  23.130  -9.933  1.00101.02           C  
ANISOU 4531  CD  PRO C 605    11029  14925  12429   2247  -2797  -3590       C  
ATOM   4532  N   ILE C 606      59.875  26.237 -11.708  1.00118.96           N  
ANISOU 4532  N   ILE C 606    13011  17128  15061   1897  -2795  -3770       N  
ATOM   4533  CA  ILE C 606      61.193  26.509 -12.275  1.00120.44           C  
ANISOU 4533  CA  ILE C 606    13076  17352  15334   1833  -2813  -3829       C  
ATOM   4534  C   ILE C 606      61.234  27.836 -13.029  1.00121.15           C  
ANISOU 4534  C   ILE C 606    13097  17374  15562   1673  -2791  -3848       C  
ATOM   4535  O   ILE C 606      62.321  28.371 -13.284  1.00119.02           O  
ANISOU 4535  O   ILE C 606    12716  17134  15372   1609  -2819  -3913       O  
ATOM   4536  CB  ILE C 606      61.657  25.341 -13.171  1.00118.84           C  
ANISOU 4536  CB  ILE C 606    12862  17179  15115   1854  -2777  -3767       C  
ATOM   4537  CG1 ILE C 606      60.512  24.790 -14.032  1.00115.42           C  
ANISOU 4537  CG1 ILE C 606    12517  16671  14667   1830  -2698  -3646       C  
ATOM   4538  CG2 ILE C 606      62.287  24.229 -12.332  1.00118.69           C  
ANISOU 4538  CG2 ILE C 606    12857  17253  14988   2003  -2829  -3793       C  
ATOM   4539  CD1 ILE C 606      60.150  25.633 -15.238  1.00113.02           C  
ANISOU 4539  CD1 ILE C 606    12179  16288  14476   1677  -2637  -3606       C  
ATOM   4540  N   ASN C 607      60.062  28.377 -13.374  1.00121.50           N  
ANISOU 4540  N   ASN C 607    13203  17326  15634   1609  -2743  -3791       N  
ATOM   4541  CA  ASN C 607      59.959  29.628 -14.130  1.00117.55           C  
ANISOU 4541  CA  ASN C 607    12651  16748  15265   1456  -2719  -3795       C  
ATOM   4542  C   ASN C 607      60.861  29.540 -15.368  1.00114.71           C  
ANISOU 4542  C   ASN C 607    12194  16402  14987   1362  -2687  -3770       C  
ATOM   4543  O   ASN C 607      60.728  28.620 -16.169  1.00111.41           O  
ANISOU 4543  O   ASN C 607    11800  15992  14539   1375  -2634  -3692       O  
ATOM   4544  CB  ASN C 607      60.327  30.829 -13.231  1.00116.46           C  
ANISOU 4544  CB  ASN C 607    12463  16609  15178   1434  -2789  -3909       C  
ATOM   4545  CG  ASN C 607      60.264  32.170 -13.957  1.00117.22           C  
ANISOU 4545  CG  ASN C 607    12504  16618  15417   1275  -2772  -3915       C  
ATOM   4546  OD1 ASN C 607      60.149  32.237 -15.182  1.00119.48           O  
ANISOU 4546  OD1 ASN C 607    12770  16858  15770   1172  -2710  -3839       O  
ATOM   4547  ND2 ASN C 607      60.348  33.254 -13.189  1.00114.35           N  
ANISOU 4547  ND2 ASN C 607    12115  16232  15100   1255  -2831  -4008       N  
TER    4548      ASN C 607                                                      
ATOM   4549  N   ASP A   1      28.769  21.991  -4.276  1.00 91.39           N  
ANISOU 4549  N   ASP A   1    11528  11672  11522   -262   -890    908       N  
ATOM   4550  CA  ASP A   1      29.023  23.403  -4.016  1.00 89.01           C  
ANISOU 4550  CA  ASP A   1    11250  11432  11139   -191   -695    851       C  
ATOM   4551  C   ASP A   1      29.911  23.581  -2.790  1.00 81.73           C  
ANISOU 4551  C   ASP A   1    10421  10500  10133   -198   -656    807       C  
ATOM   4552  O   ASP A   1      29.547  23.185  -1.681  1.00 86.76           O  
ANISOU 4552  O   ASP A   1    11068  11157  10739   -259   -650    908       O  
ATOM   4553  CB  ASP A   1      27.706  24.159  -3.837  1.00 92.78           C  
ANISOU 4553  CB  ASP A   1    11649  12001  11603   -178   -539    975       C  
ATOM   4554  CG  ASP A   1      26.995  24.405  -5.154  1.00 94.31           C  
ANISOU 4554  CG  ASP A   1    11758  12211  11863   -148   -542    991       C  
ATOM   4555  OD1 ASP A   1      27.003  25.561  -5.628  1.00 92.80           O  
ANISOU 4555  OD1 ASP A   1    11563  12048  11648    -75   -424    938       O  
ATOM   4556  OD2 ASP A   1      26.440  23.441  -5.719  1.00 94.50           O  
ANISOU 4556  OD2 ASP A   1    11728  12214  11965   -203   -673   1059       O  
ATOM   4557  N   ILE A   2      31.079  24.183  -3.001  1.00 65.09           N  
ANISOU 4557  N   ILE A   2     8377   8372   7984   -144   -633    661       N  
ATOM   4558  CA  ILE A   2      32.093  24.348  -1.966  1.00 54.82           C  
ANISOU 4558  CA  ILE A   2     7168   7054   6606   -150   -616    600       C  
ATOM   4559  C   ILE A   2      32.104  25.803  -1.522  1.00 58.77           C  
ANISOU 4559  C   ILE A   2     7706   7608   7017   -100   -423    575       C  
ATOM   4560  O   ILE A   2      32.137  26.716  -2.357  1.00 60.05           O  
ANISOU 4560  O   ILE A   2     7853   7786   7178    -44   -353    517       O  
ATOM   4561  CB  ILE A   2      33.481  23.917  -2.468  1.00 49.93           C  
ANISOU 4561  CB  ILE A   2     6592   6379   6002   -130   -746    452       C  
ATOM   4562  CG1 ILE A   2      33.424  22.487  -3.010  1.00 52.77           C  
ANISOU 4562  CG1 ILE A   2     6920   6673   6459   -160   -950    459       C  
ATOM   4563  CG2 ILE A   2      34.509  24.035  -1.354  1.00 49.40           C  
ANISOU 4563  CG2 ILE A   2     6616   6295   5859   -145   -739    402       C  
ATOM   4564  CD1 ILE A   2      34.781  21.883  -3.290  1.00 48.92           C  
ANISOU 4564  CD1 ILE A   2     6470   6131   5985   -131  -1094    313       C  
ATOM   4565  N   GLN A   3      32.083  26.016  -0.212  1.00 53.81           N  
ANISOU 4565  N   GLN A   3     7131   7004   6311   -124   -348    617       N  
ATOM   4566  CA  GLN A   3      32.117  27.351   0.363  1.00 56.45           C  
ANISOU 4566  CA  GLN A   3     7518   7376   6553    -74   -177    584       C  
ATOM   4567  C   GLN A   3      33.521  27.693   0.843  1.00 56.73           C  
ANISOU 4567  C   GLN A   3     7661   7374   6519    -75   -192    469       C  
ATOM   4568  O   GLN A   3      34.284  26.823   1.271  1.00 61.34           O  
ANISOU 4568  O   GLN A   3     8281   7921   7104   -125   -310    450       O  
ATOM   4569  CB  GLN A   3      31.129  27.480   1.528  1.00 63.55           C  
ANISOU 4569  CB  GLN A   3     8404   8348   7393    -91    -67    697       C  
ATOM   4570  CG  GLN A   3      29.662  27.466   1.121  1.00 70.61           C  
ANISOU 4570  CG  GLN A   3     9182   9309   8339    -76    -11    813       C  
ATOM   4571  CD  GLN A   3      29.186  26.093   0.686  1.00 82.91           C  
ANISOU 4571  CD  GLN A   3    10662  10853   9988   -154   -163    910       C  
ATOM   4572  OE1 GLN A   3      29.378  25.103   1.393  1.00 86.43           O  
ANISOU 4572  OE1 GLN A   3    11129  11284  10426   -239   -264    967       O  
ATOM   4573  NE2 GLN A   3      28.567  26.025  -0.487  1.00 85.49           N  
ANISOU 4573  NE2 GLN A   3    10904  11175  10401   -132   -194    933       N  
ATOM   4574  N   MET A   4      33.851  28.980   0.758  1.00 52.91           N  
ANISOU 4574  N   MET A   4     7230   6895   5980    -21    -82    395       N  
ATOM   4575  CA  MET A   4      35.097  29.535   1.268  1.00 54.81           C  
ANISOU 4575  CA  MET A   4     7575   7109   6141    -26    -75    295       C  
ATOM   4576  C   MET A   4      34.739  30.545   2.351  1.00 56.15           C  
ANISOU 4576  C   MET A   4     7818   7303   6213      0     75    309       C  
ATOM   4577  O   MET A   4      34.127  31.582   2.063  1.00 71.15           O  
ANISOU 4577  O   MET A   4     9715   9214   8105     64    184    307       O  
ATOM   4578  CB  MET A   4      35.895  30.208   0.150  1.00 57.44           C  
ANISOU 4578  CB  MET A   4     7914   7425   6486      2    -94    193       C  
ATOM   4579  CG  MET A   4      36.257  29.287  -1.008  1.00 57.12           C  
ANISOU 4579  CG  MET A   4     7796   7379   6528     -9   -232    158       C  
ATOM   4580  SD  MET A   4      37.395  27.982  -0.522  1.00 59.72           S  
ANISOU 4580  SD  MET A   4     8148   7678   6866    -55   -396    108       S  
ATOM   4581  CE  MET A   4      38.962  28.782  -0.855  1.00 61.57           C  
ANISOU 4581  CE  MET A   4     8433   7930   7033    -49   -402    -32       C  
ATOM   4582  N   THR A   5      35.102  30.243   3.594  1.00 47.69           N  
ANISOU 4582  N   THR A   5     6814   6239   5067    -45     72    321       N  
ATOM   4583  CA  THR A   5      34.806  31.126   4.718  1.00 51.75           C  
ANISOU 4583  CA  THR A   5     7404   6785   5473    -20    209    322       C  
ATOM   4584  C   THR A   5      36.086  31.869   5.102  1.00 52.58           C  
ANISOU 4584  C   THR A   5     7635   6844   5500    -28    206    213       C  
ATOM   4585  O   THR A   5      37.095  31.248   5.443  1.00 46.58           O  
ANISOU 4585  O   THR A   5     6914   6060   4724    -90    104    185       O  
ATOM   4586  CB  THR A   5      34.220  30.358   5.909  1.00 59.30           C  
ANISOU 4586  CB  THR A   5     8348   7804   6379    -75    221    422       C  
ATOM   4587  OG1 THR A   5      35.280  29.854   6.741  1.00 69.53           O  
ANISOU 4587  OG1 THR A   5     9727   9073   7619   -148    136    396       O  
ATOM   4588  CG2 THR A   5      33.368  29.183   5.423  1.00 66.62           C  
ANISOU 4588  CG2 THR A   5     9152   8758   7402   -114    141    536       C  
ATOM   4589  N   GLN A   6      36.047  33.196   5.016  1.00 53.59           N  
ANISOU 4589  N   GLN A   6     7825   6953   5585     33    307    155       N  
ATOM   4590  CA  GLN A   6      37.214  34.057   5.195  1.00 50.84           C  
ANISOU 4590  CA  GLN A   6     7595   6552   5169     22    299     56       C  
ATOM   4591  C   GLN A   6      37.187  34.694   6.582  1.00 53.18           C  
ANISOU 4591  C   GLN A   6     8007   6857   5342     30    391     36       C  
ATOM   4592  O   GLN A   6      36.122  35.048   7.101  1.00 54.66           O  
ANISOU 4592  O   GLN A   6     8186   7086   5495     89    503     70       O  
ATOM   4593  CB  GLN A   6      37.245  35.145   4.115  1.00 50.58           C  
ANISOU 4593  CB  GLN A   6     7569   6479   5171     72    325      7       C  
ATOM   4594  CG  GLN A   6      38.626  35.676   3.738  1.00 50.43           C  
ANISOU 4594  CG  GLN A   6     7621   6417   5121     25    256    -78       C  
ATOM   4595  CD  GLN A   6      38.612  36.300   2.354  1.00 51.60           C  
ANISOU 4595  CD  GLN A   6     7727   6549   5331     46    241    -94       C  
ATOM   4596  OE1 GLN A   6      37.742  35.986   1.541  1.00 45.30           O  
ANISOU 4596  OE1 GLN A   6     6825   5772   4615     82    247    -44       O  
ATOM   4597  NE2 GLN A   6      39.563  37.188   2.080  1.00 59.91           N  
ANISOU 4597  NE2 GLN A   6     8856   7567   6339     12    214   -155       N  
ATOM   4598  N   SER A   7      38.362  34.832   7.177  1.00 58.59           N  
ANISOU 4598  N   SER A   7     8796   7511   5955    -27    341    -24       N  
ATOM   4599  CA  SER A   7      38.496  35.456   8.484  1.00 63.85           C  
ANISOU 4599  CA  SER A   7     9588   8179   6493    -28    413    -57       C  
ATOM   4600  C   SER A   7      39.884  36.071   8.618  1.00 68.25           C  
ANISOU 4600  C   SER A   7    10263   8675   6993    -78    353   -143       C  
ATOM   4601  O   SER A   7      40.875  35.487   8.160  1.00 70.67           O  
ANISOU 4601  O   SER A   7    10541   8971   7339   -141    237   -157       O  
ATOM   4602  CB  SER A   7      38.241  34.438   9.601  1.00 60.94           C  
ANISOU 4602  CB  SER A   7     9204   7878   6072    -83    405     14       C  
ATOM   4603  OG  SER A   7      39.371  33.611   9.811  1.00 62.96           O  
ANISOU 4603  OG  SER A   7     9478   8114   6329   -175    273     11       O  
ATOM   4604  N   PRO A   8      39.958  37.269   9.223  1.00 63.95           N  
ANISOU 4604  N   PRO A   8     9851   8092   6357    -46    427   -206       N  
ATOM   4605  CA  PRO A   8      38.807  38.021   9.737  1.00 63.14           C  
ANISOU 4605  CA  PRO A   8     9781   8002   6206     51    564   -211       C  
ATOM   4606  C   PRO A   8      38.122  38.834   8.642  1.00 63.40           C  
ANISOU 4606  C   PRO A   8     9773   7992   6322    142    606   -222       C  
ATOM   4607  O   PRO A   8      38.676  38.954   7.552  1.00 60.80           O  
ANISOU 4607  O   PRO A   8     9415   7618   6066    114    529   -231       O  
ATOM   4608  CB  PRO A   8      39.442  38.935  10.780  1.00 65.02           C  
ANISOU 4608  CB  PRO A   8    10195   8196   6313     40    588   -293       C  
ATOM   4609  CG  PRO A   8      40.787  39.242  10.194  1.00 63.55           C  
ANISOU 4609  CG  PRO A   8    10064   7937   6145    -36    475   -338       C  
ATOM   4610  CD  PRO A   8      41.223  37.991   9.449  1.00 61.75           C  
ANISOU 4610  CD  PRO A   8     9700   7752   6012   -102    372   -282       C  
ATOM   4611  N   SER A   9      36.938  39.382   8.921  1.00 62.83           N  
ANISOU 4611  N   SER A   9     9693   7943   6235    250    723   -220       N  
ATOM   4612  CA  SER A   9      36.262  40.203   7.925  1.00 60.77           C  
ANISOU 4612  CA  SER A   9     9400   7632   6056    343    756   -228       C  
ATOM   4613  C   SER A   9      36.874  41.593   7.805  1.00 60.41           C  
ANISOU 4613  C   SER A   9     9510   7466   5979    366    737   -319       C  
ATOM   4614  O   SER A   9      36.633  42.276   6.804  1.00 60.18           O  
ANISOU 4614  O   SER A   9     9467   7372   6025    410    721   -321       O  
ATOM   4615  CB  SER A   9      34.769  40.314   8.247  1.00 66.62           C  
ANISOU 4615  CB  SER A   9    10068   8446   6800    463    882   -197       C  
ATOM   4616  OG  SER A   9      34.554  40.961   9.487  1.00 72.91           O  
ANISOU 4616  OG  SER A   9    10973   9258   7471    525    974   -264       O  
ATOM   4617  N   SER A  10      37.656  42.021   8.795  1.00 56.29           N  
ANISOU 4617  N   SER A  10     9138   6908   5344    328    729   -387       N  
ATOM   4618  CA  SER A  10      38.390  43.275   8.716  1.00 59.48           C  
ANISOU 4618  CA  SER A  10     9702   7187   5712    321    683   -466       C  
ATOM   4619  C   SER A  10      39.474  43.276   9.784  1.00 57.54           C  
ANISOU 4619  C   SER A  10     9589   6929   5346    231    643   -516       C  
ATOM   4620  O   SER A  10      39.297  42.713  10.868  1.00 54.29           O  
ANISOU 4620  O   SER A  10     9184   6593   4852    227    695   -514       O  
ATOM   4621  CB  SER A  10      37.472  44.491   8.888  1.00 68.13           C  
ANISOU 4621  CB  SER A  10    10877   8211   6797    467    764   -526       C  
ATOM   4622  OG  SER A  10      36.518  44.274   9.912  1.00 78.33           O  
ANISOU 4622  OG  SER A  10    12148   9591   8021    562    886   -539       O  
ATOM   4623  N   LEU A  11      40.599  43.912   9.461  1.00 59.04           N  
ANISOU 4623  N   LEU A  11     9880   7031   5522    148    546   -552       N  
ATOM   4624  CA  LEU A  11      41.719  44.028  10.382  1.00 64.20           C  
ANISOU 4624  CA  LEU A  11    10666   7663   6065     52    492   -598       C  
ATOM   4625  C   LEU A  11      42.402  45.373  10.175  1.00 68.55           C  
ANISOU 4625  C   LEU A  11    11379   8080   6587     23    424   -659       C  
ATOM   4626  O   LEU A  11      42.305  45.987   9.110  1.00 72.60           O  
ANISOU 4626  O   LEU A  11    11876   8529   7179     35    387   -644       O  
ATOM   4627  CB  LEU A  11      42.724  42.876  10.202  1.00 59.14           C  
ANISOU 4627  CB  LEU A  11     9933   7097   5439    -77    400   -548       C  
ATOM   4628  CG  LEU A  11      43.389  42.675   8.835  1.00 58.30           C  
ANISOU 4628  CG  LEU A  11     9727   6996   5428   -146    304   -513       C  
ATOM   4629  CD1 LEU A  11      44.647  43.524   8.684  1.00 57.07           C  
ANISOU 4629  CD1 LEU A  11     9685   6775   5224   -248    208   -551       C  
ATOM   4630  CD2 LEU A  11      43.703  41.202   8.609  1.00 59.78           C  
ANISOU 4630  CD2 LEU A  11     9763   7287   5665   -199    256   -460       C  
ATOM   4631  N   SER A  12      43.108  45.820  11.212  1.00 67.55           N  
ANISOU 4631  N   SER A  12    11413   7909   6343    -27    399   -720       N  
ATOM   4632  CA  SER A  12      43.834  47.086  11.187  1.00 64.98           C  
ANISOU 4632  CA  SER A  12    11266   7448   5975    -74    318   -775       C  
ATOM   4633  C   SER A  12      45.263  46.828  11.647  1.00 65.13           C  
ANISOU 4633  C   SER A  12    11343   7486   5917   -234    219   -774       C  
ATOM   4634  O   SER A  12      45.492  46.494  12.814  1.00 73.27           O  
ANISOU 4634  O   SER A  12    12439   8552   6848   -254    241   -804       O  
ATOM   4635  CB  SER A  12      43.152  48.130  12.073  1.00 69.74           C  
ANISOU 4635  CB  SER A  12    12041   7955   6502     47    384   -872       C  
ATOM   4636  OG  SER A  12      43.842  49.367  12.027  1.00 79.43           O  
ANISOU 4636  OG  SER A  12    13454   9031   7697     -2    286   -923       O  
ATOM   4637  N   ALA A  13      46.218  46.981  10.733  1.00 57.16           N  
ANISOU 4637  N   ALA A  13    10303   6465   4950   -350    108   -736       N  
ATOM   4638  CA  ALA A  13      47.625  46.763  11.029  1.00 57.79           C  
ANISOU 4638  CA  ALA A  13    10414   6576   4966   -504      5   -729       C  
ATOM   4639  C   ALA A  13      48.434  47.971  10.577  1.00 59.35           C  
ANISOU 4639  C   ALA A  13    10738   6671   5143   -601   -104   -738       C  
ATOM   4640  O   ALA A  13      48.019  48.730   9.697  1.00 60.13           O  
ANISOU 4640  O   ALA A  13    10846   6695   5305   -570   -117   -725       O  
ATOM   4641  CB  ALA A  13      48.153  45.491  10.356  1.00 57.18           C  
ANISOU 4641  CB  ALA A  13    10134   6638   4954   -569    -34   -664       C  
ATOM   4642  N   SER A  14      49.601  48.139  11.189  1.00 61.84           N  
ANISOU 4642  N   SER A  14    11148   6981   5369   -730   -191   -751       N  
ATOM   4643  CA  SER A  14      50.441  49.296  10.927  1.00 66.69           C  
ANISOU 4643  CA  SER A  14    11898   7497   5945   -846   -308   -752       C  
ATOM   4644  C   SER A  14      51.380  49.038   9.750  1.00 69.76           C  
ANISOU 4644  C   SER A  14    12139   7984   6381   -980   -401   -675       C  
ATOM   4645  O   SER A  14      51.553  47.908   9.288  1.00 62.50           O  
ANISOU 4645  O   SER A  14    11026   7210   5511   -984   -384   -639       O  
ATOM   4646  CB  SER A  14      51.241  49.670  12.175  1.00 65.41           C  
ANISOU 4646  CB  SER A  14    11916   7284   5655   -929   -363   -800       C  
ATOM   4647  OG  SER A  14      50.403  50.229  13.171  1.00 70.40           O  
ANISOU 4647  OG  SER A  14    12714   7807   6226   -808   -290   -885       O  
ATOM   4648  N   VAL A  15      51.992  50.122   9.265  1.00 75.12           N  
ANISOU 4648  N   VAL A  15    12917   8585   7041  -1091   -507   -653       N  
ATOM   4649  CA  VAL A  15      52.911  50.026   8.138  1.00 69.43           C  
ANISOU 4649  CA  VAL A  15    12061   7975   6346  -1232   -598   -577       C  
ATOM   4650  C   VAL A  15      54.131  49.208   8.534  1.00 67.21           C  
ANISOU 4650  C   VAL A  15    11694   7837   6006  -1345   -651   -567       C  
ATOM   4651  O   VAL A  15      54.686  49.367   9.629  1.00 66.77           O  
ANISOU 4651  O   VAL A  15    11767   7739   5862  -1398   -686   -600       O  
ATOM   4652  CB  VAL A  15      53.312  51.430   7.655  1.00 63.39           C  
ANISOU 4652  CB  VAL A  15    11437   7091   5557  -1347   -713   -543       C  
ATOM   4653  CG1 VAL A  15      54.296  51.340   6.498  1.00 62.48           C  
ANISOU 4653  CG1 VAL A  15    11170   7122   5448  -1510   -805   -457       C  
ATOM   4654  CG2 VAL A  15      52.080  52.220   7.249  1.00 63.24           C  
ANISOU 4654  CG2 VAL A  15    11501   6919   5607  -1221   -673   -556       C  
ATOM   4655  N   GLY A  16      54.555  48.321   7.635  1.00 62.62           N  
ANISOU 4655  N   GLY A  16    10892   7428   5474  -1377   -660   -525       N  
ATOM   4656  CA  GLY A  16      55.672  47.443   7.889  1.00 62.64           C  
ANISOU 4656  CA  GLY A  16    10781   7580   5439  -1460   -712   -520       C  
ATOM   4657  C   GLY A  16      55.337  46.180   8.649  1.00 63.74           C  
ANISOU 4657  C   GLY A  16    10851   7768   5599  -1355   -643   -556       C  
ATOM   4658  O   GLY A  16      56.225  45.341   8.838  1.00 65.68           O  
ANISOU 4658  O   GLY A  16    10991   8135   5828  -1408   -693   -554       O  
ATOM   4659  N   ASP A  17      54.093  46.007   9.082  1.00 60.92           N  
ANISOU 4659  N   ASP A  17    10543   7327   5276  -1212   -538   -584       N  
ATOM   4660  CA  ASP A  17      53.716  44.858   9.890  1.00 58.11           C  
ANISOU 4660  CA  ASP A  17    10137   7012   4929  -1129   -480   -604       C  
ATOM   4661  C   ASP A  17      53.335  43.671   9.008  1.00 56.78           C  
ANISOU 4661  C   ASP A  17     9748   6957   4867  -1056   -450   -581       C  
ATOM   4662  O   ASP A  17      53.000  43.815   7.829  1.00 55.82           O  
ANISOU 4662  O   ASP A  17     9531   6863   4814  -1034   -439   -560       O  
ATOM   4663  CB  ASP A  17      52.558  45.215  10.824  1.00 65.94           C  
ANISOU 4663  CB  ASP A  17    11276   7885   5893  -1018   -379   -641       C  
ATOM   4664  CG  ASP A  17      52.456  44.274  12.010  1.00 76.31           C  
ANISOU 4664  CG  ASP A  17    12595   9235   7163   -988   -346   -654       C  
ATOM   4665  OD1 ASP A  17      51.512  44.430  12.813  1.00 83.47           O  
ANISOU 4665  OD1 ASP A  17    13598  10082   8035   -898   -255   -684       O  
ATOM   4666  OD2 ASP A  17      53.319  43.379  12.139  1.00 75.25           O  
ANISOU 4666  OD2 ASP A  17    12366   9196   7028  -1053   -414   -635       O  
ATOM   4667  N   ARG A  18      53.394  42.484   9.606  1.00 57.95           N  
ANISOU 4667  N   ARG A  18     9825   7167   5028  -1024   -448   -584       N  
ATOM   4668  CA  ARG A  18      53.104  41.234   8.916  1.00 57.59           C  
ANISOU 4668  CA  ARG A  18     9584   7216   5081   -957   -442   -569       C  
ATOM   4669  C   ARG A  18      51.637  40.877   9.124  1.00 56.50           C  
ANISOU 4669  C   ARG A  18     9447   7026   4994   -831   -334   -558       C  
ATOM   4670  O   ARG A  18      51.193  40.697  10.263  1.00 60.10           O  
ANISOU 4670  O   ARG A  18     9994   7440   5403   -802   -289   -562       O  
ATOM   4671  CB  ARG A  18      54.025  40.130   9.435  1.00 62.37           C  
ANISOU 4671  CB  ARG A  18    10114   7905   5678   -997   -524   -573       C  
ATOM   4672  CG  ARG A  18      53.703  38.732   8.951  1.00 71.61           C  
ANISOU 4672  CG  ARG A  18    11109   9147   6950   -918   -535   -566       C  
ATOM   4673  CD  ARG A  18      54.804  37.768   9.366  1.00 83.53           C  
ANISOU 4673  CD  ARG A  18    12548  10734   8456   -962   -645   -577       C  
ATOM   4674  NE  ARG A  18      55.925  37.786   8.431  1.00 93.05           N  
ANISOU 4674  NE  ARG A  18    13630  12054   9670  -1015   -727   -601       N  
ATOM   4675  CZ  ARG A  18      56.188  36.813   7.565  1.00 92.88           C  
ANISOU 4675  CZ  ARG A  18    13428  12134   9730   -965   -779   -624       C  
ATOM   4676  NH1 ARG A  18      55.416  35.735   7.524  1.00 86.58           N  
ANISOU 4676  NH1 ARG A  18    12563  11313   9019   -868   -771   -621       N  
ATOM   4677  NH2 ARG A  18      57.226  36.910   6.745  1.00 93.73           N  
ANISOU 4677  NH2 ARG A  18    13419  12369   9826  -1013   -845   -653       N  
ATOM   4678  N   VAL A  19      50.890  40.772   8.026  1.00 49.83           N  
ANISOU 4678  N   VAL A  19     8495   6199   4238   -764   -294   -541       N  
ATOM   4679  CA  VAL A  19      49.441  40.603   8.061  1.00 48.58           C  
ANISOU 4679  CA  VAL A  19     8328   5997   4132   -649   -190   -523       C  
ATOM   4680  C   VAL A  19      49.084  39.237   7.491  1.00 54.56           C  
ANISOU 4680  C   VAL A  19     8908   6834   4987   -598   -203   -497       C  
ATOM   4681  O   VAL A  19      49.535  38.878   6.396  1.00 55.53           O  
ANISOU 4681  O   VAL A  19     8903   7028   5168   -614   -260   -499       O  
ATOM   4682  CB  VAL A  19      48.726  41.723   7.282  1.00 50.38           C  
ANISOU 4682  CB  VAL A  19     8597   6159   4388   -607   -137   -520       C  
ATOM   4683  CG1 VAL A  19      47.226  41.514   7.313  1.00 55.73           C  
ANISOU 4683  CG1 VAL A  19     9247   6808   5121   -483    -31   -499       C  
ATOM   4684  CG2 VAL A  19      49.098  43.084   7.851  1.00 46.69           C  
ANISOU 4684  CG2 VAL A  19     8321   5592   3828   -658   -147   -550       C  
ATOM   4685  N   THR A  20      48.259  38.489   8.227  1.00 57.92           N  
ANISOU 4685  N   THR A  20     9329   7252   5426   -540   -154   -471       N  
ATOM   4686  CA  THR A  20      47.825  37.153   7.836  1.00 51.76           C  
ANISOU 4686  CA  THR A  20     8401   6526   4739   -497   -178   -438       C  
ATOM   4687  C   THR A  20      46.312  37.152   7.648  1.00 55.38           C  
ANISOU 4687  C   THR A  20     8832   6962   5249   -405    -75   -397       C  
ATOM   4688  O   THR A  20      45.566  37.533   8.560  1.00 62.27           O  
ANISOU 4688  O   THR A  20     9795   7800   6066   -372     12   -385       O  
ATOM   4689  CB  THR A  20      48.237  36.117   8.884  1.00 55.30           C  
ANISOU 4689  CB  THR A  20     8856   6994   5162   -531   -238   -423       C  
ATOM   4690  OG1 THR A  20      49.607  35.751   8.682  1.00 54.65           O  
ANISOU 4690  OG1 THR A  20     8731   6958   5077   -595   -357   -457       O  
ATOM   4691  CG2 THR A  20      47.373  34.868   8.786  1.00 66.56           C  
ANISOU 4691  CG2 THR A  20    10175   8441   6673   -479   -244   -370       C  
ATOM   4692  N   ILE A  21      45.866  36.728   6.467  1.00 55.32           N  
ANISOU 4692  N   ILE A  21     8693   6986   5340   -364    -85   -379       N  
ATOM   4693  CA  ILE A  21      44.455  36.558   6.138  1.00 58.19           C  
ANISOU 4693  CA  ILE A  21     8997   7343   5768   -283     -5   -331       C  
ATOM   4694  C   ILE A  21      44.206  35.071   5.920  1.00 61.83           C  
ANISOU 4694  C   ILE A  21     9332   7849   6311   -274    -68   -291       C  
ATOM   4695  O   ILE A  21      44.973  34.406   5.212  1.00 60.85           O  
ANISOU 4695  O   ILE A  21     9122   7762   6236   -297   -170   -317       O  
ATOM   4696  CB  ILE A  21      44.070  37.375   4.892  1.00 57.96           C  
ANISOU 4696  CB  ILE A  21     8932   7302   5790   -248     25   -335       C  
ATOM   4697  CG1 ILE A  21      44.277  38.870   5.141  1.00 60.41           C  
ANISOU 4697  CG1 ILE A  21     9384   7543   6026   -259     68   -369       C  
ATOM   4698  CG2 ILE A  21      42.636  37.087   4.479  1.00 55.09           C  
ANISOU 4698  CG2 ILE A  21     8486   6941   5503   -165     95   -279       C  
ATOM   4699  CD1 ILE A  21      44.150  39.722   3.893  1.00 57.72           C  
ANISOU 4699  CD1 ILE A  21     9018   7185   5727   -252     66   -367       C  
ATOM   4700  N   THR A  22      43.139  34.550   6.525  1.00 65.48           N  
ANISOU 4700  N   THR A  22     9781   8314   6786   -239    -15   -229       N  
ATOM   4701  CA  THR A  22      42.864  33.119   6.519  1.00 64.96           C  
ANISOU 4701  CA  THR A  22     9617   8274   6790   -247    -89   -176       C  
ATOM   4702  C   THR A  22      41.550  32.840   5.799  1.00 62.02           C  
ANISOU 4702  C   THR A  22     9146   7915   6503   -188    -41   -116       C  
ATOM   4703  O   THR A  22      40.608  33.630   5.885  1.00 69.78           O  
ANISOU 4703  O   THR A  22    10151   8895   7466   -139     76    -93       O  
ATOM   4704  CB  THR A  22      42.836  32.578   7.961  1.00 68.69           C  
ANISOU 4704  CB  THR A  22    10154   8750   7194   -290    -95   -133       C  
ATOM   4705  OG1 THR A  22      44.179  32.343   8.402  1.00 76.76           O  
ANISOU 4705  OG1 THR A  22    11226   9764   8176   -353   -195   -179       O  
ATOM   4706  CG2 THR A  22      42.043  31.286   8.069  1.00 68.69           C  
ANISOU 4706  CG2 THR A  22    10066   8770   7262   -296   -141    -44       C  
ATOM   4707  N   CYS A  23      41.505  31.727   5.066  1.00 56.44           N  
ANISOU 4707  N   CYS A  23     8330   7222   5893   -189   -140    -95       N  
ATOM   4708  CA  CYS A  23      40.331  31.352   4.284  1.00 64.61           C  
ANISOU 4708  CA  CYS A  23     9263   8270   7016   -146   -118    -35       C  
ATOM   4709  C   CYS A  23      40.242  29.833   4.257  1.00 64.48           C  
ANISOU 4709  C   CYS A  23     9172   8252   7075   -173   -243     11       C  
ATOM   4710  O   CYS A  23      41.173  29.169   3.792  1.00 62.71           O  
ANISOU 4710  O   CYS A  23     8917   8018   6891   -186   -370    -46       O  
ATOM   4711  CB  CYS A  23      40.428  31.937   2.872  1.00 69.73           C  
ANISOU 4711  CB  CYS A  23     9856   8924   7713   -110   -114    -84       C  
ATOM   4712  SG  CYS A  23      39.295  31.285   1.631  1.00 80.37           S  
ANISOU 4712  SG  CYS A  23    11065  10289   9181    -69   -136    -27       S  
ATOM   4713  N   ARG A  24      39.138  29.287   4.766  1.00 63.59           N  
ANISOU 4713  N   ARG A  24     9030   8151   6978   -181   -216    114       N  
ATOM   4714  CA  ARG A  24      38.983  27.847   4.936  1.00 66.22           C  
ANISOU 4714  CA  ARG A  24     9313   8469   7376   -225   -348    179       C  
ATOM   4715  C   ARG A  24      37.916  27.307   3.991  1.00 66.04           C  
ANISOU 4715  C   ARG A  24     9183   8454   7457   -202   -369    242       C  
ATOM   4716  O   ARG A  24      36.811  27.860   3.906  1.00 71.62           O  
ANISOU 4716  O   ARG A  24     9856   9198   8157   -173   -249    301       O  
ATOM   4717  CB  ARG A  24      38.631  27.500   6.386  1.00 74.85           C  
ANISOU 4717  CB  ARG A  24    10461   9582   8398   -287   -327    269       C  
ATOM   4718  CG  ARG A  24      37.975  26.134   6.558  1.00 87.48           C  
ANISOU 4718  CG  ARG A  24    12000  11174  10065   -342   -439    384       C  
ATOM   4719  CD  ARG A  24      38.288  25.504   7.912  1.00 95.84           C  
ANISOU 4719  CD  ARG A  24    13125  12232  11059   -430   -502    448       C  
ATOM   4720  NE  ARG A  24      39.538  24.746   7.895  1.00 99.87           N  
ANISOU 4720  NE  ARG A  24    13666  12670  11611   -453   -678    387       N  
ATOM   4721  CZ  ARG A  24      40.046  24.117   8.952  1.00104.55           C  
ANISOU 4721  CZ  ARG A  24    14320  13241  12162   -529   -772    430       C  
ATOM   4722  NH1 ARG A  24      39.415  24.154  10.120  1.00105.28           N  
ANISOU 4722  NH1 ARG A  24    14450  13390  12160   -599   -702    538       N  
ATOM   4723  NH2 ARG A  24      41.185  23.448   8.844  1.00106.84           N  
ANISOU 4723  NH2 ARG A  24    14628  13463  12504   -533   -939    366       N  
ATOM   4724  N   ALA A  25      38.258  26.227   3.290  1.00 58.29           N  
ANISOU 4724  N   ALA A  25     8146   7434   6568   -209   -527    223       N  
ATOM   4725  CA  ALA A  25      37.344  25.556   2.382  1.00 54.30           C  
ANISOU 4725  CA  ALA A  25     7546   6923   6164   -198   -580    278       C  
ATOM   4726  C   ALA A  25      36.506  24.527   3.129  1.00 53.68           C  
ANISOU 4726  C   ALA A  25     7449   6835   6111   -266   -643    416       C  
ATOM   4727  O   ALA A  25      36.941  23.942   4.126  1.00 64.15           O  
ANISOU 4727  O   ALA A  25     8832   8138   7406   -325   -717    448       O  
ATOM   4728  CB  ALA A  25      38.115  24.873   1.251  1.00 48.67           C  
ANISOU 4728  CB  ALA A  25     6786   6173   5532   -168   -730    179       C  
ATOM   4729  N   SER A  26      35.287  24.313   2.636  1.00 48.06           N  
ANISOU 4729  N   SER A  26     6658   6148   5455   -268   -621    509       N  
ATOM   4730  CA  SER A  26      34.373  23.360   3.251  1.00 53.62           C  
ANISOU 4730  CA  SER A  26     7331   6859   6184   -347   -681    660       C  
ATOM   4731  C   SER A  26      34.697  21.914   2.899  1.00 64.51           C  
ANISOU 4731  C   SER A  26     8699   8146   7665   -391   -913    670       C  
ATOM   4732  O   SER A  26      34.202  21.005   3.574  1.00 68.34           O  
ANISOU 4732  O   SER A  26     9183   8617   8166   -480  -1004    797       O  
ATOM   4733  CB  SER A  26      32.931  23.680   2.849  1.00 51.32           C  
ANISOU 4733  CB  SER A  26     6948   6637   5913   -337   -575    761       C  
ATOM   4734  OG  SER A  26      32.757  23.580   1.447  1.00 54.76           O  
ANISOU 4734  OG  SER A  26     7319   7043   6444   -289   -627    716       O  
ATOM   4735  N   GLN A  27      35.498  21.680   1.862  1.00 65.65           N  
ANISOU 4735  N   GLN A  27     8835   8233   7876   -331  -1015    541       N  
ATOM   4736  CA  GLN A  27      35.940  20.341   1.504  1.00 61.62           C  
ANISOU 4736  CA  GLN A  27     8324   7625   7463   -347  -1246    516       C  
ATOM   4737  C   GLN A  27      37.377  20.426   1.012  1.00 64.31           C  
ANISOU 4737  C   GLN A  27     8692   7936   7807   -272  -1312    335       C  
ATOM   4738  O   GLN A  27      38.001  21.491   1.026  1.00 74.39           O  
ANISOU 4738  O   GLN A  27     9990   9269   9006   -231  -1182    250       O  
ATOM   4739  CB  GLN A  27      35.057  19.717   0.418  1.00 59.95           C  
ANISOU 4739  CB  GLN A  27     8036   7388   7356   -344  -1330    557       C  
ATOM   4740  CG  GLN A  27      33.585  19.593   0.745  1.00 68.79           C  
ANISOU 4740  CG  GLN A  27     9104   8552   8480   -420  -1275    742       C  
ATOM   4741  CD  GLN A  27      32.752  19.386  -0.509  1.00 77.37           C  
ANISOU 4741  CD  GLN A  27    10108   9637   9653   -398  -1308    759       C  
ATOM   4742  OE1 GLN A  27      31.538  19.592  -0.507  1.00 87.20           O  
ANISOU 4742  OE1 GLN A  27    11288  10945  10897   -436  -1223    889       O  
ATOM   4743  NE2 GLN A  27      33.415  18.989  -1.596  1.00 73.40           N  
ANISOU 4743  NE2 GLN A  27     9600   9072   9217   -335  -1430    623       N  
ATOM   4744  N   ASP A  28      37.893  19.288   0.564  1.00 57.73           N  
ANISOU 4744  N   ASP A  28     7855   7017   7064   -255  -1521    275       N  
ATOM   4745  CA  ASP A  28      39.140  19.276  -0.186  1.00 55.69           C  
ANISOU 4745  CA  ASP A  28     7588   6753   6820   -166  -1591     90       C  
ATOM   4746  C   ASP A  28      38.977  20.079  -1.468  1.00 55.79           C  
ANISOU 4746  C   ASP A  28     7531   6843   6824   -101  -1481      9       C  
ATOM   4747  O   ASP A  28      38.127  19.761  -2.306  1.00 65.69           O  
ANISOU 4747  O   ASP A  28     8731   8088   8141    -95  -1511     43       O  
ATOM   4748  CB  ASP A  28      39.543  17.839  -0.509  1.00 60.39           C  
ANISOU 4748  CB  ASP A  28     8183   7237   7523   -144  -1846     38       C  
ATOM   4749  CG  ASP A  28      40.862  17.755  -1.253  1.00 66.13           C  
ANISOU 4749  CG  ASP A  28     8888   7979   8261    -39  -1923   -165       C  
ATOM   4750  OD1 ASP A  28      40.925  17.037  -2.273  1.00 68.80           O  
ANISOU 4750  OD1 ASP A  28     9182   8281   8679     26  -2057   -256       O  
ATOM   4751  OD2 ASP A  28      41.838  18.397  -0.811  1.00 67.64           O  
ANISOU 4751  OD2 ASP A  28     9101   8223   8376    -21  -1853   -235       O  
ATOM   4752  N   VAL A  29      39.777  21.134  -1.613  1.00 52.54           N  
ANISOU 4752  N   VAL A  29     7124   6509   6331    -62  -1361    -87       N  
ATOM   4753  CA  VAL A  29      39.866  21.875  -2.862  1.00 59.55           C  
ANISOU 4753  CA  VAL A  29     7950   7475   7203     -7  -1282   -176       C  
ATOM   4754  C   VAL A  29      41.257  21.783  -3.471  1.00 61.78           C  
ANISOU 4754  C   VAL A  29     8206   7799   7469     57  -1357   -350       C  
ATOM   4755  O   VAL A  29      41.551  22.476  -4.447  1.00 57.20           O  
ANISOU 4755  O   VAL A  29     7575   7308   6852     91  -1289   -431       O  
ATOM   4756  CB  VAL A  29      39.442  23.347  -2.681  1.00 58.87           C  
ANISOU 4756  CB  VAL A  29     7878   7458   7030    -25  -1066   -123       C  
ATOM   4757  CG1 VAL A  29      38.047  23.428  -2.083  1.00 62.81           C  
ANISOU 4757  CG1 VAL A  29     8385   7939   7542    -72   -986     39       C  
ATOM   4758  CG2 VAL A  29      40.443  24.091  -1.819  1.00 52.85           C  
ANISOU 4758  CG2 VAL A  29     7185   6721   6174    -37   -998   -168       C  
ATOM   4759  N   ASN A  30      42.119  20.937  -2.908  1.00 62.25           N  
ANISOU 4759  N   ASN A  30     8295   7805   7553     70  -1501   -405       N  
ATOM   4760  CA  ASN A  30      43.474  20.685  -3.411  1.00 59.15           C  
ANISOU 4760  CA  ASN A  30     7865   7459   7152    142  -1593   -577       C  
ATOM   4761  C   ASN A  30      44.226  22.015  -3.377  1.00 56.43           C  
ANISOU 4761  C   ASN A  30     7520   7229   6692    131  -1437   -623       C  
ATOM   4762  O   ASN A  30      44.259  22.663  -2.319  1.00 48.02           O  
ANISOU 4762  O   ASN A  30     6528   6153   5565     73  -1344   -547       O  
ATOM   4763  CB  ASN A  30      43.381  20.006  -4.773  1.00 54.00           C  
ANISOU 4763  CB  ASN A  30     7131   6821   6565    216  -1699   -678       C  
ATOM   4764  CG  ASN A  30      44.650  19.271  -5.145  1.00 61.48           C  
ANISOU 4764  CG  ASN A  30     8037   7789   7532    307  -1852   -855       C  
ATOM   4765  OD1 ASN A  30      45.506  19.806  -5.849  1.00 59.74           O  
ANISOU 4765  OD1 ASN A  30     7751   7701   7246    353  -1803   -981       O  
ATOM   4766  ND2 ASN A  30      44.778  18.034  -4.677  1.00 69.06           N  
ANISOU 4766  ND2 ASN A  30     9033   8624   8582    332  -2045   -864       N  
ATOM   4767  N   THR A  31      44.833  22.456  -4.476  1.00 57.20           N  
ANISOU 4767  N   THR A  31     7542   7440   6751    176  -1411   -740       N  
ATOM   4768  CA  THR A  31      45.516  23.740  -4.529  1.00 58.40           C  
ANISOU 4768  CA  THR A  31     7693   7704   6794    148  -1276   -770       C  
ATOM   4769  C   THR A  31      44.805  24.745  -5.423  1.00 56.91           C  
ANISOU 4769  C   THR A  31     7474   7581   6570    126  -1141   -731       C  
ATOM   4770  O   THR A  31      45.312  25.857  -5.609  1.00 55.75           O  
ANISOU 4770  O   THR A  31     7327   7522   6335     94  -1040   -748       O  
ATOM   4771  CB  THR A  31      46.961  23.555  -5.008  1.00 55.62           C  
ANISOU 4771  CB  THR A  31     7269   7459   6404    199  -1353   -930       C  
ATOM   4772  OG1 THR A  31      46.966  23.169  -6.388  1.00 55.96           O  
ANISOU 4772  OG1 THR A  31     7210   7582   6470    264  -1405  -1031       O  
ATOM   4773  CG2 THR A  31      47.660  22.483  -4.186  1.00 49.39           C  
ANISOU 4773  CG2 THR A  31     6505   6595   5666    235  -1508   -974       C  
ATOM   4774  N   ALA A  32      43.648  24.387  -5.978  1.00 52.33           N  
ANISOU 4774  N   ALA A  32     6869   6956   6057    136  -1148   -671       N  
ATOM   4775  CA  ALA A  32      42.880  25.293  -6.822  1.00 53.40           C  
ANISOU 4775  CA  ALA A  32     6975   7144   6170    117  -1032   -623       C  
ATOM   4776  C   ALA A  32      42.338  26.458  -6.007  1.00 52.66           C  
ANISOU 4776  C   ALA A  32     6960   7020   6027     62   -878   -507       C  
ATOM   4777  O   ALA A  32      41.133  26.533  -5.744  1.00 59.51           O  
ANISOU 4777  O   ALA A  32     7850   7827   6935     50   -823   -394       O  
ATOM   4778  CB  ALA A  32      41.731  24.547  -7.507  1.00 52.93           C  
ANISOU 4778  CB  ALA A  32     6874   7036   6202    138  -1089   -577       C  
ATOM   4779  N   VAL A  33      43.221  27.365  -5.596  1.00 46.59           N  
ANISOU 4779  N   VAL A  33     6234   6297   5170     33   -814   -539       N  
ATOM   4780  CA  VAL A  33      42.843  28.541  -4.824  1.00 44.49           C  
ANISOU 4780  CA  VAL A  33     6057   6000   4849    -10   -678   -453       C  
ATOM   4781  C   VAL A  33      43.577  29.748  -5.388  1.00 44.51           C  
ANISOU 4781  C   VAL A  33     6059   6089   4765    -42   -615   -497       C  
ATOM   4782  O   VAL A  33      44.769  29.672  -5.707  1.00 43.45           O  
ANISOU 4782  O   VAL A  33     5886   6040   4584    -51   -671   -592       O  
ATOM   4783  CB  VAL A  33      43.150  28.357  -3.322  1.00 41.95           C  
ANISOU 4783  CB  VAL A  33     5826   5611   4502    -33   -681   -424       C  
ATOM   4784  CG1 VAL A  33      43.171  29.700  -2.608  1.00 38.47           C  
ANISOU 4784  CG1 VAL A  33     5481   5160   3977    -72   -552   -383       C  
ATOM   4785  CG2 VAL A  33      42.114  27.450  -2.686  1.00 41.70           C  
ANISOU 4785  CG2 VAL A  33     5807   5494   4542    -26   -712   -333       C  
ATOM   4786  N   ALA A  34      42.855  30.859  -5.522  1.00 43.30           N  
ANISOU 4786  N   ALA A  34     5944   5917   4590    -62   -505   -425       N  
ATOM   4787  CA  ALA A  34      43.436  32.117  -5.958  1.00 40.23           C  
ANISOU 4787  CA  ALA A  34     5578   5587   4122   -109   -450   -441       C  
ATOM   4788  C   ALA A  34      43.101  33.205  -4.950  1.00 42.45           C  
ANISOU 4788  C   ALA A  34     5984   5784   4362   -131   -350   -375       C  
ATOM   4789  O   ALA A  34      42.065  33.156  -4.287  1.00 45.80           O  
ANISOU 4789  O   ALA A  34     6450   6127   4824    -98   -294   -305       O  
ATOM   4790  CB  ALA A  34      42.938  32.515  -7.353  1.00 33.96           C  
ANISOU 4790  CB  ALA A  34     4708   4852   3342   -111   -436   -426       C  
ATOM   4791  N   TRP A  35      44.000  34.177  -4.828  1.00 43.49           N  
ANISOU 4791  N   TRP A  35     6172   5943   4408   -188   -333   -401       N  
ATOM   4792  CA  TRP A  35      43.801  35.358  -4.004  1.00 39.19           C  
ANISOU 4792  CA  TRP A  35     5757   5317   3815   -210   -251   -356       C  
ATOM   4793  C   TRP A  35      43.809  36.583  -4.901  1.00 43.80           C  
ANISOU 4793  C   TRP A  35     6354   5921   4367   -253   -225   -334       C  
ATOM   4794  O   TRP A  35      44.749  36.775  -5.692  1.00 53.68           O  
ANISOU 4794  O   TRP A  35     7552   7274   5569   -314   -276   -373       O  
ATOM   4795  CB  TRP A  35      44.885  35.495  -2.936  1.00 35.81           C  
ANISOU 4795  CB  TRP A  35     5414   4882   3312   -255   -271   -397       C  
ATOM   4796  CG  TRP A  35      44.809  34.478  -1.855  1.00 42.55           C  
ANISOU 4796  CG  TRP A  35     6285   5694   4188   -225   -294   -399       C  
ATOM   4797  CD1 TRP A  35      45.396  33.249  -1.847  1.00 43.08           C  
ANISOU 4797  CD1 TRP A  35     6279   5805   4286   -214   -389   -447       C  
ATOM   4798  CD2 TRP A  35      44.111  34.600  -0.609  1.00 44.85           C  
ANISOU 4798  CD2 TRP A  35     6675   5896   4470   -203   -227   -350       C  
ATOM   4799  NE1 TRP A  35      45.106  32.595  -0.676  1.00 42.63           N  
ANISOU 4799  NE1 TRP A  35     6274   5682   4243   -199   -396   -418       N  
ATOM   4800  CE2 TRP A  35      44.319  33.402   0.101  1.00 42.78           C  
ANISOU 4800  CE2 TRP A  35     6394   5630   4230   -196   -291   -356       C  
ATOM   4801  CE3 TRP A  35      43.330  35.604  -0.027  1.00 47.49           C  
ANISOU 4801  CE3 TRP A  35     7111   6157   4776   -185   -124   -304       C  
ATOM   4802  CZ2 TRP A  35      43.774  33.179   1.365  1.00 44.04           C  
ANISOU 4802  CZ2 TRP A  35     6628   5731   4374   -189   -250   -307       C  
ATOM   4803  CZ3 TRP A  35      42.789  35.381   1.229  1.00 46.45           C  
ANISOU 4803  CZ3 TRP A  35     7047   5976   4626   -162    -75   -272       C  
ATOM   4804  CH2 TRP A  35      43.015  34.178   1.910  1.00 45.39           C  
ANISOU 4804  CH2 TRP A  35     6888   5854   4505   -172   -136   -268       C  
ATOM   4805  N   TYR A  36      42.767  37.401  -4.759  1.00 43.06           N  
ANISOU 4805  N   TYR A  36     6326   5737   4297   -220   -149   -269       N  
ATOM   4806  CA  TYR A  36      42.580  38.647  -5.483  1.00 50.11           C  
ANISOU 4806  CA  TYR A  36     7254   6612   5173   -253   -130   -231       C  
ATOM   4807  C   TYR A  36      42.614  39.837  -4.535  1.00 45.97           C  
ANISOU 4807  C   TYR A  36     6890   5977   4599   -262    -84   -218       C  
ATOM   4808  O   TYR A  36      42.256  39.727  -3.354  1.00 48.06           O  
ANISOU 4808  O   TYR A  36     7230   6170   4860   -212    -33   -222       O  
ATOM   4809  CB  TYR A  36      41.248  38.663  -6.238  1.00 46.50           C  
ANISOU 4809  CB  TYR A  36     6738   6130   4800   -192    -95   -168       C  
ATOM   4810  CG  TYR A  36      41.071  37.525  -7.202  1.00 41.63           C  
ANISOU 4810  CG  TYR A  36     5975   5606   4235   -178   -145   -179       C  
ATOM   4811  CD1 TYR A  36      40.589  36.297  -6.776  1.00 39.58           C  
ANISOU 4811  CD1 TYR A  36     5664   5341   4034   -121   -152   -184       C  
ATOM   4812  CD2 TYR A  36      41.389  37.680  -8.541  1.00 39.35           C  
ANISOU 4812  CD2 TYR A  36     5605   5414   3933   -229   -194   -184       C  
ATOM   4813  CE1 TYR A  36      40.426  35.256  -7.659  1.00 38.83           C  
ANISOU 4813  CE1 TYR A  36     5449   5317   3990   -107   -213   -201       C  
ATOM   4814  CE2 TYR A  36      41.229  36.645  -9.432  1.00 34.45           C  
ANISOU 4814  CE2 TYR A  36     4858   4880   3353   -211   -243   -208       C  
ATOM   4815  CZ  TYR A  36      40.748  35.435  -8.986  1.00 39.12           C  
ANISOU 4815  CZ  TYR A  36     5409   5446   4009   -146   -256   -220       C  
ATOM   4816  OH  TYR A  36      40.586  34.395  -9.869  1.00 46.86           O  
ANISOU 4816  OH  TYR A  36     6275   6497   5033   -125   -321   -251       O  
ATOM   4817  N   GLN A  37      43.030  40.979  -5.086  1.00 43.12           N  
ANISOU 4817  N   GLN A  37     6582   5606   4195   -332   -108   -201       N  
ATOM   4818  CA  GLN A  37      43.030  42.263  -4.399  1.00 47.83           C  
ANISOU 4818  CA  GLN A  37     7342   6082   4751   -344    -86   -188       C  
ATOM   4819  C   GLN A  37      42.077  43.195  -5.127  1.00 43.42           C  
ANISOU 4819  C   GLN A  37     6805   5449   4244   -313    -70   -126       C  
ATOM   4820  O   GLN A  37      42.068  43.235  -6.365  1.00 45.62           O  
ANISOU 4820  O   GLN A  37     6994   5798   4542   -358   -113    -90       O  
ATOM   4821  CB  GLN A  37      44.433  42.859  -4.365  1.00 48.74           C  
ANISOU 4821  CB  GLN A  37     7515   6233   4770   -472   -156   -212       C  
ATOM   4822  CG  GLN A  37      44.664  43.955  -3.352  1.00 51.87           C  
ANISOU 4822  CG  GLN A  37     8098   6498   5111   -492   -149   -219       C  
ATOM   4823  CD  GLN A  37      45.756  44.891  -3.810  1.00 51.56           C  
ANISOU 4823  CD  GLN A  37     8112   6482   4997   -636   -235   -202       C  
ATOM   4824  OE1 GLN A  37      46.740  45.111  -3.105  1.00 55.72           O  
ANISOU 4824  OE1 GLN A  37     8714   7009   5446   -711   -271   -232       O  
ATOM   4825  NE2 GLN A  37      45.585  45.447  -5.006  1.00 48.05           N  
ANISOU 4825  NE2 GLN A  37     7624   6064   4570   -687   -274   -145       N  
ATOM   4826  N   GLN A  38      41.263  43.925  -4.366  1.00 38.09           N  
ANISOU 4826  N   GLN A  38     6245   4638   3588   -229    -13   -117       N  
ATOM   4827  CA  GLN A  38      40.341  44.882  -4.958  1.00 55.18           C  
ANISOU 4827  CA  GLN A  38     8443   6715   5810   -183     -6    -63       C  
ATOM   4828  C   GLN A  38      40.379  46.168  -4.155  1.00 58.28           C  
ANISOU 4828  C   GLN A  38     9024   6955   6166   -165     -6    -82       C  
ATOM   4829  O   GLN A  38      40.136  46.152  -2.947  1.00 53.15           O  
ANISOU 4829  O   GLN A  38     8456   6246   5494    -89     57   -129       O  
ATOM   4830  CB  GLN A  38      38.914  44.331  -5.028  1.00 52.86           C  
ANISOU 4830  CB  GLN A  38     8060   6416   5609    -52     69    -32       C  
ATOM   4831  CG  GLN A  38      37.929  45.330  -5.591  1.00 50.25           C  
ANISOU 4831  CG  GLN A  38     7760   5990   5343     10     73     22       C  
ATOM   4832  CD  GLN A  38      36.501  44.835  -5.542  1.00 49.68           C  
ANISOU 4832  CD  GLN A  38     7596   5921   5358    143    152     55       C  
ATOM   4833  OE1 GLN A  38      35.789  44.871  -6.545  1.00 54.51           O  
ANISOU 4833  OE1 GLN A  38     8122   6548   6041    161    136    117       O  
ATOM   4834  NE2 GLN A  38      36.079  44.358  -4.373  1.00 44.06           N  
ANISOU 4834  NE2 GLN A  38     6898   5206   4635    227    236     21       N  
ATOM   4835  N   LYS A  39      40.698  47.248  -4.813  1.00 62.25           N  
ANISOU 4835  N   LYS A  39     9598   7397   6657   -240    -82    -45       N  
ATOM   4836  CA  LYS A  39      40.607  48.592  -4.284  1.00 66.76           C  
ANISOU 4836  CA  LYS A  39    10356   7797   7214   -219   -109    -55       C  
ATOM   4837  C   LYS A  39      39.272  49.219  -4.678  1.00 67.94           C  
ANISOU 4837  C   LYS A  39    10514   7841   7458    -95    -86    -16       C  
ATOM   4838  O   LYS A  39      38.703  48.867  -5.716  1.00 73.50           O  
ANISOU 4838  O   LYS A  39    11087   8610   8229    -88    -89     46       O  
ATOM   4839  CB  LYS A  39      41.779  49.444  -4.788  1.00 65.83           C  
ANISOU 4839  CB  LYS A  39    10318   7666   7028   -392   -231    -24       C  
ATOM   4840  CG  LYS A  39      43.048  49.172  -3.992  1.00 65.82           C  
ANISOU 4840  CG  LYS A  39    10365   7717   6924   -490   -252    -77       C  
ATOM   4841  CD  LYS A  39      44.321  49.461  -4.762  1.00 68.87           C  
ANISOU 4841  CD  LYS A  39    10729   8198   7239   -685   -361    -34       C  
ATOM   4842  CE  LYS A  39      45.499  48.772  -4.087  1.00 67.72           C  
ANISOU 4842  CE  LYS A  39    10562   8162   7008   -761   -365    -88       C  
ATOM   4843  NZ  LYS A  39      46.818  49.369  -4.435  1.00 69.89           N  
ANISOU 4843  NZ  LYS A  39    10869   8495   7191   -953   -474    -55       N  
ATOM   4844  N   PRO A  40      38.749  50.124  -3.849  1.00 69.99           N  
ANISOU 4844  N   PRO A  40    10925   7941   7726     11    -65    -56       N  
ATOM   4845  CA  PRO A  40      37.357  50.572  -4.005  1.00 69.89           C  
ANISOU 4845  CA  PRO A  40    10905   7840   7810    172    -22    -38       C  
ATOM   4846  C   PRO A  40      37.033  51.076  -5.404  1.00 69.10           C  
ANISOU 4846  C   PRO A  40    10755   7719   7783    127   -107     56       C  
ATOM   4847  O   PRO A  40      37.794  51.836  -6.006  1.00 68.42           O  
ANISOU 4847  O   PRO A  40    10745   7585   7668     -8   -224     99       O  
ATOM   4848  CB  PRO A  40      37.239  51.690  -2.967  1.00 71.30           C  
ANISOU 4848  CB  PRO A  40    11288   7840   7962    261    -26   -112       C  
ATOM   4849  CG  PRO A  40      38.220  51.311  -1.915  1.00 71.57           C  
ANISOU 4849  CG  PRO A  40    11392   7914   7889    195     -5   -182       C  
ATOM   4850  CD  PRO A  40      39.376  50.685  -2.639  1.00 71.03           C  
ANISOU 4850  CD  PRO A  40    11234   7978   7776      5    -72   -133       C  
ATOM   4851  N   GLY A  41      35.883  50.642  -5.919  1.00 70.57           N  
ANISOU 4851  N   GLY A  41    10808   7947   8060    231    -52     98       N  
ATOM   4852  CA  GLY A  41      35.444  51.041  -7.243  1.00 72.98           C  
ANISOU 4852  CA  GLY A  41    11052   8239   8437    198   -127    193       C  
ATOM   4853  C   GLY A  41      36.353  50.601  -8.365  1.00 78.71           C  
ANISOU 4853  C   GLY A  41    11685   9100   9120      8   -204    255       C  
ATOM   4854  O   GLY A  41      36.333  51.204  -9.441  1.00 85.07           O  
ANISOU 4854  O   GLY A  41    12486   9883   9952    -69   -298    337       O  
ATOM   4855  N   LYS A  42      37.154  49.561  -8.146  1.00 76.75           N  
ANISOU 4855  N   LYS A  42    11360   8998   8803    -66   -170    216       N  
ATOM   4856  CA  LYS A  42      38.101  49.076  -9.136  1.00 71.73           C  
ANISOU 4856  CA  LYS A  42    10626   8516   8113   -233   -236    251       C  
ATOM   4857  C   LYS A  42      37.884  47.588  -9.366  1.00 65.62           C  
ANISOU 4857  C   LYS A  42     9672   7904   7356   -204   -170    233       C  
ATOM   4858  O   LYS A  42      37.332  46.879  -8.521  1.00 63.23           O  
ANISOU 4858  O   LYS A  42     9342   7602   7081    -90    -80    188       O  
ATOM   4859  CB  LYS A  42      39.552  49.330  -8.697  1.00 74.94           C  
ANISOU 4859  CB  LYS A  42    11121   8945   8407   -371   -290    213       C  
ATOM   4860  CG  LYS A  42      39.994  50.778  -8.804  1.00 78.99           C  
ANISOU 4860  CG  LYS A  42    11800   9321   8891   -461   -397    254       C  
ATOM   4861  CD  LYS A  42      40.147  51.196 -10.254  1.00 83.40           C  
ANISOU 4861  CD  LYS A  42    12299   9940   9450   -594   -498    359       C  
ATOM   4862  CE  LYS A  42      40.439  52.679 -10.376  1.00 88.71           C  
ANISOU 4862  CE  LYS A  42    13146  10451  10109   -683   -623    418       C  
ATOM   4863  NZ  LYS A  42      39.388  53.495  -9.710  1.00 93.97           N  
ANISOU 4863  NZ  LYS A  42    13953  10887  10866   -514   -610    397       N  
ATOM   4864  N   ALA A  43      38.326  47.123 -10.529  1.00 62.77           N  
ANISOU 4864  N   ALA A  43     9190   7686   6972   -313   -223    269       N  
ATOM   4865  CA  ALA A  43      38.268  45.701 -10.816  1.00 58.85           C  
ANISOU 4865  CA  ALA A  43     8535   7340   6487   -296   -185    241       C  
ATOM   4866  C   ALA A  43      39.235  44.949  -9.905  1.00 60.52           C  
ANISOU 4866  C   ALA A  43     8753   7613   6629   -317   -161    153       C  
ATOM   4867  O   ALA A  43      40.322  45.454  -9.602  1.00 63.64           O  
ANISOU 4867  O   ALA A  43     9230   8010   6941   -412   -204    128       O  
ATOM   4868  CB  ALA A  43      38.612  45.431 -12.279  1.00 60.97           C  
ANISOU 4868  CB  ALA A  43     8681   7755   6730   -406   -254    283       C  
ATOM   4869  N   PRO A  44      38.866  43.758  -9.438  1.00 58.84           N  
ANISOU 4869  N   PRO A  44     8460   7447   6450   -237   -104    114       N  
ATOM   4870  CA  PRO A  44      39.813  42.942  -8.674  1.00 51.06           C  
ANISOU 4870  CA  PRO A  44     7469   6526   5404   -263   -100     36       C  
ATOM   4871  C   PRO A  44      41.041  42.612  -9.506  1.00 47.96           C  
ANISOU 4871  C   PRO A  44     6998   6286   4939   -386   -175      9       C  
ATOM   4872  O   PRO A  44      41.013  42.614 -10.739  1.00 46.04           O  
ANISOU 4872  O   PRO A  44     6665   6131   4697   -438   -218     42       O  
ATOM   4873  CB  PRO A  44      39.009  41.679  -8.338  1.00 55.03           C  
ANISOU 4873  CB  PRO A  44     7878   7055   5974   -165    -48     25       C  
ATOM   4874  CG  PRO A  44      37.578  42.104  -8.427  1.00 58.42           C  
ANISOU 4874  CG  PRO A  44     8309   7398   6488    -68      3     90       C  
ATOM   4875  CD  PRO A  44      37.532  43.138  -9.513  1.00 60.75           C  
ANISOU 4875  CD  PRO A  44     8619   7675   6788   -123    -49    146       C  
ATOM   4876  N   LYS A  45      42.140  42.333  -8.812  1.00 48.38           N  
ANISOU 4876  N   LYS A  45     7081   6381   4922   -432   -190    -55       N  
ATOM   4877  CA  LYS A  45      43.400  42.023  -9.467  1.00 50.80           C  
ANISOU 4877  CA  LYS A  45     7306   6849   5149   -541   -256    -93       C  
ATOM   4878  C   LYS A  45      43.984  40.742  -8.898  1.00 49.51           C  
ANISOU 4878  C   LYS A  45     7075   6760   4976   -506   -259   -178       C  
ATOM   4879  O   LYS A  45      43.992  40.534  -7.682  1.00 53.09           O  
ANISOU 4879  O   LYS A  45     7606   7131   5434   -459   -226   -205       O  
ATOM   4880  CB  LYS A  45      44.402  43.173  -9.321  1.00 54.12           C  
ANISOU 4880  CB  LYS A  45     7827   7260   5477   -664   -302    -77       C  
ATOM   4881  CG  LYS A  45      44.109  44.346 -10.241  1.00 62.01           C  
ANISOU 4881  CG  LYS A  45     8863   8227   6471   -738   -341     11       C  
ATOM   4882  CD  LYS A  45      45.169  45.425 -10.120  1.00 66.82           C  
ANISOU 4882  CD  LYS A  45     9570   8833   6984   -882   -407     37       C  
ATOM   4883  CE  LYS A  45      45.204  46.301 -11.361  1.00 66.80           C  
ANISOU 4883  CE  LYS A  45     9550   8878   6954  -1001   -476    129       C  
ATOM   4884  NZ  LYS A  45      46.342  47.261 -11.327  1.00 71.13           N  
ANISOU 4884  NZ  LYS A  45    10178   9451   7399  -1170   -556    165       N  
ATOM   4885  N   LEU A  46      44.471  39.888  -9.793  1.00 44.29           N  
ANISOU 4885  N   LEU A  46     6271   6258   4299   -527   -304   -222       N  
ATOM   4886  CA  LEU A  46      45.035  38.607  -9.396  1.00 44.18           C  
ANISOU 4886  CA  LEU A  46     6185   6315   4288   -485   -329   -309       C  
ATOM   4887  C   LEU A  46      46.349  38.801  -8.649  1.00 47.89           C  
ANISOU 4887  C   LEU A  46     6702   6824   4673   -550   -357   -357       C  
ATOM   4888  O   LEU A  46      47.264  39.470  -9.141  1.00 51.47           O  
ANISOU 4888  O   LEU A  46     7140   7377   5039   -657   -393   -355       O  
ATOM   4889  CB  LEU A  46      45.258  37.734 -10.629  1.00 45.88           C  
ANISOU 4889  CB  LEU A  46     6238   6693   4502   -483   -379   -359       C  
ATOM   4890  CG  LEU A  46      45.622  36.263 -10.391  1.00 41.54           C  
ANISOU 4890  CG  LEU A  46     5603   6198   3982   -410   -423   -455       C  
ATOM   4891  CD1 LEU A  46      44.597  35.582  -9.494  1.00 38.53           C  
ANISOU 4891  CD1 LEU A  46     5273   5667   3701   -314   -393   -431       C  
ATOM   4892  CD2 LEU A  46      45.765  35.534 -11.714  1.00 42.86           C  
ANISOU 4892  CD2 LEU A  46     5620   6521   4143   -400   -475   -514       C  
ATOM   4893  N   LEU A  47      46.436  38.224  -7.450  1.00 47.74           N  
ANISOU 4893  N   LEU A  47     6736   6731   4674   -497   -345   -391       N  
ATOM   4894  CA  LEU A  47      47.674  38.197  -6.683  1.00 46.61           C  
ANISOU 4894  CA  LEU A  47     6625   6627   4458   -549   -381   -442       C  
ATOM   4895  C   LEU A  47      48.311  36.820  -6.635  1.00 55.01           C  
ANISOU 4895  C   LEU A  47     7577   7787   5536   -502   -438   -530       C  
ATOM   4896  O   LEU A  47      49.512  36.691  -6.907  1.00 61.57           O  
ANISOU 4896  O   LEU A  47     8337   8758   6300   -555   -493   -587       O  
ATOM   4897  CB  LEU A  47      47.452  38.692  -5.251  1.00 45.66           C  
ANISOU 4897  CB  LEU A  47     6667   6350   4333   -537   -336   -416       C  
ATOM   4898  CG  LEU A  47      46.779  40.047  -5.011  1.00 50.73           C  
ANISOU 4898  CG  LEU A  47     7450   6860   4967   -554   -284   -347       C  
ATOM   4899  CD1 LEU A  47      46.390  40.159  -3.541  1.00 55.21           C  
ANISOU 4899  CD1 LEU A  47     8153   7288   5537   -503   -233   -346       C  
ATOM   4900  CD2 LEU A  47      47.694  41.191  -5.429  1.00 42.14           C  
ANISOU 4900  CD2 LEU A  47     6405   5815   3792   -683   -328   -326       C  
ATOM   4901  N   ILE A  48      47.552  35.777  -6.296  1.00 56.24           N  
ANISOU 4901  N   ILE A  48     7713   7876   5779   -405   -436   -540       N  
ATOM   4902  CA  ILE A  48      48.155  34.452  -6.156  1.00 56.68           C  
ANISOU 4902  CA  ILE A  48     7683   7994   5860   -355   -512   -625       C  
ATOM   4903  C   ILE A  48      47.268  33.404  -6.812  1.00 57.64           C  
ANISOU 4903  C   ILE A  48     7717   8108   6075   -269   -537   -636       C  
ATOM   4904  O   ILE A  48      46.055  33.387  -6.598  1.00 58.42           O  
ANISOU 4904  O   ILE A  48     7861   8097   6240   -231   -489   -566       O  
ATOM   4905  CB  ILE A  48      48.431  34.106  -4.679  1.00 53.98           C  
ANISOU 4905  CB  ILE A  48     7434   7557   5520   -342   -521   -628       C  
ATOM   4906  CG1 ILE A  48      49.713  34.800  -4.221  1.00 60.31           C  
ANISOU 4906  CG1 ILE A  48     8277   8416   6221   -428   -540   -652       C  
ATOM   4907  CG2 ILE A  48      48.557  32.603  -4.487  1.00 48.81           C  
ANISOU 4907  CG2 ILE A  48     6707   6908   4932   -267   -605   -687       C  
ATOM   4908  CD1 ILE A  48      49.656  35.357  -2.830  1.00 63.37           C  
ANISOU 4908  CD1 ILE A  48     8822   8677   6579   -457   -500   -608       C  
ATOM   4909  N   TYR A  49      47.874  32.540  -7.621  1.00 57.17           N  
ANISOU 4909  N   TYR A  49     7531   8174   6018   -239   -615   -728       N  
ATOM   4910  CA  TYR A  49      47.187  31.430  -8.258  1.00 59.13           C  
ANISOU 4910  CA  TYR A  49     7698   8416   6352   -158   -665   -758       C  
ATOM   4911  C   TYR A  49      47.784  30.120  -7.765  1.00 58.10           C  
ANISOU 4911  C   TYR A  49     7531   8280   6264    -92   -769   -846       C  
ATOM   4912  O   TYR A  49      48.943  30.064  -7.346  1.00 63.46           O  
ANISOU 4912  O   TYR A  49     8199   9023   6891   -106   -809   -910       O  
ATOM   4913  CB  TYR A  49      47.294  31.514  -9.787  1.00 61.46           C  
ANISOU 4913  CB  TYR A  49     7874   8862   6615   -166   -681   -803       C  
ATOM   4914  CG  TYR A  49      48.704  31.329 -10.305  1.00 63.49           C  
ANISOU 4914  CG  TYR A  49     8026   9308   6788   -180   -739   -919       C  
ATOM   4915  CD1 TYR A  49      49.169  30.074 -10.677  1.00 58.43           C  
ANISOU 4915  CD1 TYR A  49     7283   8740   6177    -93   -837  -1043       C  
ATOM   4916  CD2 TYR A  49      49.574  32.406 -10.408  1.00 65.41           C  
ANISOU 4916  CD2 TYR A  49     8271   9660   6920   -280   -704   -904       C  
ATOM   4917  CE1 TYR A  49      50.457  29.898 -11.145  1.00 61.94           C  
ANISOU 4917  CE1 TYR A  49     7617   9378   6541    -91   -885  -1159       C  
ATOM   4918  CE2 TYR A  49      50.865  32.241 -10.875  1.00 65.74           C  
ANISOU 4918  CE2 TYR A  49     8200   9902   6877   -298   -753  -1004       C  
ATOM   4919  CZ  TYR A  49      51.301  30.986 -11.242  1.00 65.41           C  
ANISOU 4919  CZ  TYR A  49     8044   9945   6863   -196   -838  -1136       C  
ATOM   4920  OH  TYR A  49      52.584  30.812 -11.708  1.00 66.02           O  
ANISOU 4920  OH  TYR A  49     7994  10240   6852   -199   -882  -1245       O  
ATOM   4921  N   SER A  50      46.977  29.060  -7.832  1.00 61.68           N  
ANISOU 4921  N   SER A  50     7967   8654   6816    -22   -824   -845       N  
ATOM   4922  CA  SER A  50      47.397  27.721  -7.413  1.00 63.23           C  
ANISOU 4922  CA  SER A  50     8137   8815   7072     47   -947   -921       C  
ATOM   4923  C   SER A  50      47.979  27.738  -6.000  1.00 63.48           C  
ANISOU 4923  C   SER A  50     8258   8776   7086     22   -956   -900       C  
ATOM   4924  O   SER A  50      49.033  27.156  -5.731  1.00 67.05           O  
ANISOU 4924  O   SER A  50     8675   9272   7528     51  -1046   -989       O  
ATOM   4925  CB  SER A  50      48.388  27.117  -8.411  1.00 64.54           C  
ANISOU 4925  CB  SER A  50     8174   9135   7214    101  -1039  -1072       C  
ATOM   4926  OG  SER A  50      47.745  26.793  -9.633  1.00 64.61           O  
ANISOU 4926  OG  SER A  50     8107   9189   7253    137  -1056  -1099       O  
ATOM   4927  N   ALA A  51      47.293  28.453  -5.104  1.00 61.22           N  
ANISOU 4927  N   ALA A  51     8083   8388   6789    -28   -861   -785       N  
ATOM   4928  CA  ALA A  51      47.507  28.421  -3.658  1.00 58.71           C  
ANISOU 4928  CA  ALA A  51     7868   7981   6458    -55   -860   -741       C  
ATOM   4929  C   ALA A  51      48.744  29.184  -3.193  1.00 57.83           C  
ANISOU 4929  C   ALA A  51     7788   7936   6248   -111   -844   -779       C  
ATOM   4930  O   ALA A  51      48.643  30.016  -2.285  1.00 56.43           O  
ANISOU 4930  O   ALA A  51     7721   7702   6019   -167   -767   -713       O  
ATOM   4931  CB  ALA A  51      47.570  26.976  -3.153  1.00 54.86           C  
ANISOU 4931  CB  ALA A  51     7368   7423   6052     -3   -994   -767       C  
ATOM   4932  N   ASP A  52      49.915  28.916  -3.777  1.00 57.92           N  
ANISOU 4932  N   ASP A  52     7704   8075   6229    -96   -918   -887       N  
ATOM   4933  CA  ASP A  52      51.148  29.507  -3.268  1.00 58.44           C  
ANISOU 4933  CA  ASP A  52     7788   8211   6204   -155   -921   -917       C  
ATOM   4934  C   ASP A  52      52.043  30.104  -4.349  1.00 52.27           C  
ANISOU 4934  C   ASP A  52     6901   7616   5343   -187   -913   -985       C  
ATOM   4935  O   ASP A  52      53.181  30.485  -4.047  1.00 55.59           O  
ANISOU 4935  O   ASP A  52     7310   8124   5688   -238   -933  -1018       O  
ATOM   4936  CB  ASP A  52      51.942  28.475  -2.455  1.00 66.65           C  
ANISOU 4936  CB  ASP A  52     8821   9227   7275   -116  -1040   -973       C  
ATOM   4937  CG  ASP A  52      52.250  27.220  -3.241  1.00 77.89           C  
ANISOU 4937  CG  ASP A  52    10117  10708   8771    -13  -1165  -1084       C  
ATOM   4938  OD1 ASP A  52      51.651  27.026  -4.318  1.00 80.83           O  
ANISOU 4938  OD1 ASP A  52    10420  11115   9177     29  -1156  -1108       O  
ATOM   4939  OD2 ASP A  52      53.088  26.422  -2.771  1.00 84.92           O  
ANISOU 4939  OD2 ASP A  52    10980  11602   9684     30  -1279  -1151       O  
ATOM   4940  N   PHE A  53      51.570  30.210  -5.588  1.00 48.02           N  
ANISOU 4940  N   PHE A  53     6283   7151   4812   -170   -888   -999       N  
ATOM   4941  CA  PHE A  53      52.352  30.815  -6.658  1.00 53.10           C  
ANISOU 4941  CA  PHE A  53     6820   7990   5365   -217   -876  -1050       C  
ATOM   4942  C   PHE A  53      52.019  32.297  -6.774  1.00 59.68           C  
ANISOU 4942  C   PHE A  53     7734   8811   6130   -327   -773   -947       C  
ATOM   4943  O   PHE A  53      50.847  32.674  -6.848  1.00 61.87           O  
ANISOU 4943  O   PHE A  53     8081   8975   6450   -325   -709   -865       O  
ATOM   4944  CB  PHE A  53      52.090  30.114  -7.990  1.00 54.15           C  
ANISOU 4944  CB  PHE A  53     6820   8227   5530   -144   -914  -1128       C  
ATOM   4945  CG  PHE A  53      52.738  28.765  -8.104  1.00 65.25           C  
ANISOU 4945  CG  PHE A  53     8124   9688   6980    -33  -1035  -1263       C  
ATOM   4946  CD1 PHE A  53      52.225  27.673  -7.421  1.00 71.11           C  
ANISOU 4946  CD1 PHE A  53     8917  10266   7835     50  -1110  -1268       C  
ATOM   4947  CD2 PHE A  53      53.858  28.587  -8.897  1.00 67.25           C  
ANISOU 4947  CD2 PHE A  53     8229  10162   7162    -12  -1080  -1385       C  
ATOM   4948  CE1 PHE A  53      52.820  26.430  -7.525  1.00 69.67           C  
ANISOU 4948  CE1 PHE A  53     8653  10114   7704    158  -1241  -1395       C  
ATOM   4949  CE2 PHE A  53      54.458  27.347  -9.006  1.00 71.19           C  
ANISOU 4949  CE2 PHE A  53     8634  10708   7707    110  -1199  -1525       C  
ATOM   4950  CZ  PHE A  53      53.938  26.267  -8.319  1.00 72.03           C  
ANISOU 4950  CZ  PHE A  53     8806  10625   7938    198  -1286  -1532       C  
ATOM   4951  N   LEU A  54      53.051  33.132  -6.796  1.00 62.25           N  
ANISOU 4951  N   LEU A  54     8049   9254   6351   -423   -767   -948       N  
ATOM   4952  CA  LEU A  54      52.861  34.565  -6.957  1.00 64.30           C  
ANISOU 4952  CA  LEU A  54     8389   9500   6543   -537   -696   -852       C  
ATOM   4953  C   LEU A  54      52.661  34.901  -8.429  1.00 68.06           C  
ANISOU 4953  C   LEU A  54     8760  10115   6986   -567   -680   -850       C  
ATOM   4954  O   LEU A  54      53.473  34.524  -9.280  1.00 73.78           O  
ANISOU 4954  O   LEU A  54     9334  11044   7655   -569   -724   -931       O  
ATOM   4955  CB  LEU A  54      54.054  35.334  -6.393  1.00 61.52           C  
ANISOU 4955  CB  LEU A  54     8072   9214   6089   -647   -712   -842       C  
ATOM   4956  CG  LEU A  54      53.906  36.863  -6.448  1.00 63.63           C  
ANISOU 4956  CG  LEU A  54     8449   9439   6289   -775   -660   -739       C  
ATOM   4957  CD1 LEU A  54      52.988  37.347  -5.338  1.00 65.83           C  
ANISOU 4957  CD1 LEU A  54     8917   9479   6615   -759   -606   -667       C  
ATOM   4958  CD2 LEU A  54      55.258  37.553  -6.374  1.00 60.99           C  
ANISOU 4958  CD2 LEU A  54     8092   9243   5837   -906   -700   -736       C  
ATOM   4959  N   TYR A  55      51.572  35.602  -8.724  1.00 64.84           N  
ANISOU 4959  N   TYR A  55     8427   9601   6606   -587   -619   -759       N  
ATOM   4960  CA  TYR A  55      51.287  36.027 -10.086  1.00 62.26           C  
ANISOU 4960  CA  TYR A  55     8019   9389   6247   -630   -607   -735       C  
ATOM   4961  C   TYR A  55      52.282  37.101 -10.514  1.00 60.30           C  
ANISOU 4961  C   TYR A  55     7749   9291   5871   -778   -616   -702       C  
ATOM   4962  O   TYR A  55      52.752  37.901  -9.701  1.00 63.97           O  
ANISOU 4962  O   TYR A  55     8321   9693   6292   -860   -612   -653       O  
ATOM   4963  CB  TYR A  55      49.848  36.539 -10.177  1.00 57.68           C  
ANISOU 4963  CB  TYR A  55     7534   8641   5740   -611   -547   -637       C  
ATOM   4964  CG  TYR A  55      49.391  36.976 -11.551  1.00 54.20           C  
ANISOU 4964  CG  TYR A  55     7024   8293   5279   -654   -539   -597       C  
ATOM   4965  CD1 TYR A  55      49.368  36.084 -12.615  1.00 53.26           C  
ANISOU 4965  CD1 TYR A  55     6756   8316   5164   -603   -573   -670       C  
ATOM   4966  CD2 TYR A  55      48.938  38.270 -11.771  1.00 50.27           C  
ANISOU 4966  CD2 TYR A  55     6615   7727   4759   -741   -506   -486       C  
ATOM   4967  CE1 TYR A  55      48.934  36.478 -13.869  1.00 54.97           C  
ANISOU 4967  CE1 TYR A  55     6910   8623   5354   -650   -567   -629       C  
ATOM   4968  CE2 TYR A  55      48.501  38.674 -13.018  1.00 47.22           C  
ANISOU 4968  CE2 TYR A  55     6168   7420   4355   -788   -508   -437       C  
ATOM   4969  CZ  TYR A  55      48.501  37.775 -14.063  1.00 53.63           C  
ANISOU 4969  CZ  TYR A  55     6827   8388   5162   -747   -535   -506       C  
ATOM   4970  OH  TYR A  55      48.066  38.175 -15.305  1.00 57.84           O  
ANISOU 4970  OH  TYR A  55     7301   9008   5668   -801   -540   -455       O  
ATOM   4971  N   SER A  56      52.611  37.104 -11.804  1.00 61.05           N  
ANISOU 4971  N   SER A  56     7703   9593   5900   -821   -634   -726       N  
ATOM   4972  CA  SER A  56      53.658  37.983 -12.311  1.00 68.89           C  
ANISOU 4972  CA  SER A  56     8641  10777   6757   -975   -653   -695       C  
ATOM   4973  C   SER A  56      53.268  39.450 -12.163  1.00 69.14           C  
ANISOU 4973  C   SER A  56     8823  10681   6765  -1103   -631   -552       C  
ATOM   4974  O   SER A  56      52.123  39.836 -12.413  1.00 68.67           O  
ANISOU 4974  O   SER A  56     8841  10479   6772  -1081   -599   -481       O  
ATOM   4975  CB  SER A  56      53.953  37.666 -13.777  1.00 74.99           C  
ANISOU 4975  CB  SER A  56     9226  11809   7455   -994   -671   -746       C  
ATOM   4976  OG  SER A  56      52.799  37.828 -14.583  1.00 79.63           O  
ANISOU 4976  OG  SER A  56     9829  12335   8091   -979   -645   -690       O  
ATOM   4977  N   GLY A  57      54.237  40.271 -11.754  1.00 65.53           N  
ANISOU 4977  N   GLY A  57     8409  10273   6216  -1236   -659   -510       N  
ATOM   4978  CA  GLY A  57      54.034  41.693 -11.578  1.00 63.35           C  
ANISOU 4978  CA  GLY A  57     8286   9874   5911  -1367   -663   -381       C  
ATOM   4979  C   GLY A  57      53.634  42.121 -10.182  1.00 66.19           C  
ANISOU 4979  C   GLY A  57     8849   9966   6333  -1332   -644   -351       C  
ATOM   4980  O   GLY A  57      53.621  43.326  -9.903  1.00 70.55           O  
ANISOU 4980  O   GLY A  57     9544  10407   6856  -1439   -662   -260       O  
ATOM   4981  N   VAL A  58      53.319  41.179  -9.298  1.00 60.91           N  
ANISOU 4981  N   VAL A  58     8204   9194   5746  -1190   -615   -426       N  
ATOM   4982  CA  VAL A  58      52.838  41.484  -7.952  1.00 57.01           C  
ANISOU 4982  CA  VAL A  58     7896   8461   5305  -1143   -586   -405       C  
ATOM   4983  C   VAL A  58      54.030  41.544  -7.003  1.00 57.45           C  
ANISOU 4983  C   VAL A  58     7988   8549   5291  -1209   -627   -434       C  
ATOM   4984  O   VAL A  58      54.940  40.709  -7.106  1.00 60.40           O  
ANISOU 4984  O   VAL A  58     8223   9094   5631  -1198   -661   -510       O  
ATOM   4985  CB  VAL A  58      51.796  40.446  -7.501  1.00 54.60           C  
ANISOU 4985  CB  VAL A  58     7594   8034   5117   -972   -536   -451       C  
ATOM   4986  CG1 VAL A  58      51.389  40.663  -6.052  1.00 51.27           C  
ANISOU 4986  CG1 VAL A  58     7346   7404   4730   -926   -502   -438       C  
ATOM   4987  CG2 VAL A  58      50.576  40.499  -8.413  1.00 52.01           C  
ANISOU 4987  CG2 VAL A  58     7239   7665   4857   -919   -499   -408       C  
ATOM   4988  N   PRO A  59      54.082  42.517  -6.087  1.00 54.71           N  
ANISOU 4988  N   PRO A  59     7822   8047   4920  -1274   -632   -381       N  
ATOM   4989  CA  PRO A  59      55.224  42.611  -5.168  1.00 56.48           C  
ANISOU 4989  CA  PRO A  59     8088   8299   5072  -1348   -678   -403       C  
ATOM   4990  C   PRO A  59      55.439  41.324  -4.385  1.00 63.22           C  
ANISOU 4990  C   PRO A  59     8887   9164   5969  -1232   -673   -493       C  
ATOM   4991  O   PRO A  59      54.495  40.612  -4.038  1.00 65.32           O  
ANISOU 4991  O   PRO A  59     9174   9317   6326  -1097   -626   -520       O  
ATOM   4992  CB  PRO A  59      54.835  43.767  -4.241  1.00 55.48           C  
ANISOU 4992  CB  PRO A  59     8195   7945   4939  -1392   -672   -342       C  
ATOM   4993  CG  PRO A  59      53.935  44.615  -5.070  1.00 55.57           C  
ANISOU 4993  CG  PRO A  59     8254   7881   4979  -1410   -656   -269       C  
ATOM   4994  CD  PRO A  59      53.169  43.666  -5.952  1.00 58.31           C  
ANISOU 4994  CD  PRO A  59     8450   8303   5402  -1293   -608   -300       C  
ATOM   4995  N   SER A  60      56.711  41.036  -4.099  1.00 63.87           N  
ANISOU 4995  N   SER A  60     8898   9387   5985  -1292   -732   -532       N  
ATOM   4996  CA  SER A  60      57.079  39.796  -3.426  1.00 65.09           C  
ANISOU 4996  CA  SER A  60     8988   9567   6177  -1191   -752   -616       C  
ATOM   4997  C   SER A  60      56.704  39.783  -1.949  1.00 63.69           C  
ANISOU 4997  C   SER A  60     8988   9181   6032  -1150   -734   -608       C  
ATOM   4998  O   SER A  60      56.830  38.733  -1.309  1.00 58.41           O  
ANISOU 4998  O   SER A  60     8287   8501   5407  -1063   -753   -664       O  
ATOM   4999  CB  SER A  60      58.581  39.540  -3.578  1.00 67.68           C  
ANISOU 4999  CB  SER A  60     9175  10118   6422  -1266   -826   -660       C  
ATOM   5000  OG  SER A  60      59.340  40.539  -2.923  1.00 74.42           O  
ANISOU 5000  OG  SER A  60    10138  10950   7188  -1413   -862   -602       O  
ATOM   5001  N   ARG A  61      56.248  40.904  -1.391  1.00 64.54           N  
ANISOU 5001  N   ARG A  61     9282   9124   6114  -1208   -704   -543       N  
ATOM   5002  CA  ARG A  61      55.765  40.874  -0.016  1.00 63.55           C  
ANISOU 5002  CA  ARG A  61     9322   8813   6011  -1156   -674   -544       C  
ATOM   5003  C   ARG A  61      54.441  40.136   0.120  1.00 64.39           C  
ANISOU 5003  C   ARG A  61     9434   8813   6219  -1007   -603   -555       C  
ATOM   5004  O   ARG A  61      53.959  39.966   1.245  1.00 64.49           O  
ANISOU 5004  O   ARG A  61     9562   8696   6247   -955   -571   -555       O  
ATOM   5005  CB  ARG A  61      55.628  42.296   0.534  1.00 60.74           C  
ANISOU 5005  CB  ARG A  61     9170   8311   5597  -1245   -665   -487       C  
ATOM   5006  CG  ARG A  61      54.600  43.161  -0.176  1.00 61.61           C  
ANISOU 5006  CG  ARG A  61     9340   8328   5740  -1232   -618   -437       C  
ATOM   5007  CD  ARG A  61      54.433  44.491   0.547  1.00 62.68           C  
ANISOU 5007  CD  ARG A  61     9699   8288   5829  -1295   -622   -399       C  
ATOM   5008  NE  ARG A  61      53.429  45.347  -0.078  1.00 60.93           N  
ANISOU 5008  NE  ARG A  61     9544   7958   5648  -1270   -589   -353       N  
ATOM   5009  CZ  ARG A  61      53.653  46.105  -1.146  1.00 63.74           C  
ANISOU 5009  CZ  ARG A  61     9869   8368   5982  -1372   -637   -294       C  
ATOM   5010  NH1 ARG A  61      54.851  46.118  -1.715  1.00 62.91           N  
ANISOU 5010  NH1 ARG A  61     9656   8441   5804  -1510   -712   -276       N  
ATOM   5011  NH2 ARG A  61      52.679  46.852  -1.646  1.00 68.00           N  
ANISOU 5011  NH2 ARG A  61    10478   8791   6569  -1338   -615   -251       N  
ATOM   5012  N   PHE A  62      53.848  39.698  -0.989  1.00 56.94           N  
ANISOU 5012  N   PHE A  62     8365   7932   5337   -945   -582   -560       N  
ATOM   5013  CA  PHE A  62      52.637  38.890  -0.977  1.00 55.50           C  
ANISOU 5013  CA  PHE A  62     8162   7671   5253   -813   -529   -565       C  
ATOM   5014  C   PHE A  62      53.013  37.428  -1.166  1.00 62.45           C  
ANISOU 5014  C   PHE A  62     8891   8654   6183   -742   -582   -631       C  
ATOM   5015  O   PHE A  62      53.589  37.058  -2.195  1.00 67.84           O  
ANISOU 5015  O   PHE A  62     9422   9494   6859   -750   -626   -672       O  
ATOM   5016  CB  PHE A  62      51.669  39.328  -2.075  1.00 52.59           C  
ANISOU 5016  CB  PHE A  62     7761   7291   4929   -788   -481   -525       C  
ATOM   5017  CG  PHE A  62      51.072  40.681  -1.852  1.00 52.08           C  
ANISOU 5017  CG  PHE A  62     7854   7091   4842   -825   -435   -463       C  
ATOM   5018  CD1 PHE A  62      49.967  40.835  -1.032  1.00 53.90           C  
ANISOU 5018  CD1 PHE A  62     8203   7161   5115   -741   -364   -443       C  
ATOM   5019  CD2 PHE A  62      51.605  41.799  -2.471  1.00 55.27           C  
ANISOU 5019  CD2 PHE A  62     8287   7531   5182   -942   -469   -425       C  
ATOM   5020  CE1 PHE A  62      49.409  42.081  -0.827  1.00 57.98           C  
ANISOU 5020  CE1 PHE A  62     8865   7548   5616   -754   -327   -402       C  
ATOM   5021  CE2 PHE A  62      51.051  43.049  -2.270  1.00 56.54           C  
ANISOU 5021  CE2 PHE A  62     8604   7545   5332   -969   -446   -372       C  
ATOM   5022  CZ  PHE A  62      49.951  43.190  -1.447  1.00 58.32           C  
ANISOU 5022  CZ  PHE A  62     8950   7604   5607   -864   -374   -368       C  
ATOM   5023  N   SER A  63      52.685  36.602  -0.180  1.00 61.34           N  
ANISOU 5023  N   SER A  63     8792   8427   6087   -674   -585   -641       N  
ATOM   5024  CA  SER A  63      52.851  35.166  -0.292  1.00 59.60           C  
ANISOU 5024  CA  SER A  63     8450   8261   5933   -594   -649   -697       C  
ATOM   5025  C   SER A  63      51.518  34.482  -0.033  1.00 60.56           C  
ANISOU 5025  C   SER A  63     8596   8267   6146   -501   -609   -664       C  
ATOM   5026  O   SER A  63      50.594  35.061   0.548  1.00 55.57           O  
ANISOU 5026  O   SER A  63     8082   7519   5514   -497   -529   -604       O  
ATOM   5027  CB  SER A  63      53.907  34.635   0.688  1.00 63.32           C  
ANISOU 5027  CB  SER A  63     8934   8751   6374   -615   -727   -733       C  
ATOM   5028  OG  SER A  63      53.613  35.021   2.019  1.00 68.87           O  
ANISOU 5028  OG  SER A  63     9801   9321   7045   -643   -691   -685       O  
ATOM   5029  N   GLY A  64      51.429  33.251  -0.496  1.00 60.45           N  
ANISOU 5029  N   GLY A  64     8466   8293   6209   -426   -672   -707       N  
ATOM   5030  CA  GLY A  64      50.307  32.389  -0.165  1.00 56.05           C  
ANISOU 5030  CA  GLY A  64     7922   7635   5741   -351   -665   -672       C  
ATOM   5031  C   GLY A  64      50.826  31.047   0.290  1.00 63.00           C  
ANISOU 5031  C   GLY A  64     8752   8516   6670   -308   -780   -717       C  
ATOM   5032  O   GLY A  64      51.836  30.558  -0.210  1.00 64.94           O  
ANISOU 5032  O   GLY A  64     8896   8864   6914   -293   -868   -800       O  
ATOM   5033  N   SER A  65      50.143  30.467   1.269  1.00 65.10           N  
ANISOU 5033  N   SER A  65     9089   8671   6975   -290   -785   -661       N  
ATOM   5034  CA  SER A  65      50.489  29.148   1.768  1.00 63.96           C  
ANISOU 5034  CA  SER A  65     8914   8498   6889   -255   -910   -685       C  
ATOM   5035  C   SER A  65      49.216  28.340   1.955  1.00 63.36           C  
ANISOU 5035  C   SER A  65     8849   8327   6899   -215   -915   -615       C  
ATOM   5036  O   SER A  65      48.107  28.881   1.993  1.00 63.88           O  
ANISOU 5036  O   SER A  65     8960   8351   6962   -222   -806   -541       O  
ATOM   5037  CB  SER A  65      51.260  29.214   3.091  1.00 65.53           C  
ANISOU 5037  CB  SER A  65     9206   8666   7027   -311   -944   -671       C  
ATOM   5038  OG  SER A  65      50.395  29.529   4.167  1.00 69.19           O  
ANISOU 5038  OG  SER A  65     9794   9034   7460   -346   -865   -578       O  
ATOM   5039  N   ARG A  66      49.392  27.030   2.080  1.00 55.58           N  
ANISOU 5039  N   ARG A  66     7819   7308   5991   -175  -1051   -636       N  
ATOM   5040  CA  ARG A  66      48.278  26.113   2.235  1.00 51.10           C  
ANISOU 5040  CA  ARG A  66     7254   6652   5510   -151  -1090   -564       C  
ATOM   5041  C   ARG A  66      48.623  25.063   3.284  1.00 58.34           C  
ANISOU 5041  C   ARG A  66     8212   7495   6459   -166  -1223   -538       C  
ATOM   5042  O   ARG A  66      49.770  24.623   3.402  1.00 62.27           O  
ANISOU 5042  O   ARG A  66     8684   8015   6961   -148  -1337   -615       O  
ATOM   5043  CB  ARG A  66      47.904  25.433   0.900  1.00 46.06           C  
ANISOU 5043  CB  ARG A  66     6503   6035   4963    -79  -1151   -616       C  
ATOM   5044  CG  ARG A  66      47.189  24.106   1.074  1.00 36.78           C  
ANISOU 5044  CG  ARG A  66     5320   4762   3893    -54  -1271   -567       C  
ATOM   5045  CD  ARG A  66      46.772  23.468  -0.235  1.00 51.98           C  
ANISOU 5045  CD  ARG A  66     7147   6700   5905     15  -1336   -621       C  
ATOM   5046  NE  ARG A  66      45.822  22.384   0.032  1.00 60.39           N  
ANISOU 5046  NE  ARG A  66     8227   7654   7063     12  -1432   -536       N  
ATOM   5047  CZ  ARG A  66      46.102  21.096  -0.142  1.00 58.32           C  
ANISOU 5047  CZ  ARG A  66     7937   7329   6895     60  -1622   -586       C  
ATOM   5048  NH1 ARG A  66      47.300  20.747  -0.579  1.00 57.28           N  
ANISOU 5048  NH1 ARG A  66     7751   7242   6772    130  -1725   -731       N  
ATOM   5049  NH2 ARG A  66      45.185  20.173   0.123  1.00 56.85           N  
ANISOU 5049  NH2 ARG A  66     7773   7035   6790     37  -1714   -491       N  
ATOM   5050  N   SER A  67      47.608  24.686   4.061  1.00 60.06           N  
ANISOU 5050  N   SER A  67     8491   7633   6696   -202  -1211   -421       N  
ATOM   5051  CA  SER A  67      47.701  23.673   5.114  1.00 59.86           C  
ANISOU 5051  CA  SER A  67     8514   7529   6699   -237  -1339   -361       C  
ATOM   5052  C   SER A  67      46.361  22.933   5.128  1.00 59.24           C  
ANISOU 5052  C   SER A  67     8430   7385   6693   -249  -1360   -251       C  
ATOM   5053  O   SER A  67      45.416  23.347   5.804  1.00 64.41           O  
ANISOU 5053  O   SER A  67     9139   8038   7297   -304  -1247   -141       O  
ATOM   5054  CB  SER A  67      48.015  24.304   6.463  1.00 55.91           C  
ANISOU 5054  CB  SER A  67     8125   7029   6089   -316  -1274   -307       C  
ATOM   5055  OG  SER A  67      48.152  23.320   7.477  1.00 59.05           O  
ANISOU 5055  OG  SER A  67     8571   7358   6509   -361  -1407   -242       O  
ATOM   5056  N   GLY A  68      46.286  21.856   4.357  1.00 49.83           N  
ANISOU 5056  N   GLY A  68     7168   6150   5617   -195  -1508   -286       N  
ATOM   5057  CA  GLY A  68      45.051  21.092   4.274  1.00 56.27           C  
ANISOU 5057  CA  GLY A  68     7971   6900   6507   -215  -1552   -180       C  
ATOM   5058  C   GLY A  68      43.966  21.897   3.586  1.00 59.22           C  
ANISOU 5058  C   GLY A  68     8309   7328   6864   -206  -1383   -142       C  
ATOM   5059  O   GLY A  68      44.094  22.291   2.421  1.00 60.57           O  
ANISOU 5059  O   GLY A  68     8412   7548   7052   -143  -1345   -233       O  
ATOM   5060  N   THR A  69      42.876  22.148   4.307  1.00 57.62           N  
ANISOU 5060  N   THR A  69     8145   7125   6624   -270  -1282     -5       N  
ATOM   5061  CA  THR A  69      41.791  22.988   3.820  1.00 62.24           C  
ANISOU 5061  CA  THR A  69     8699   7764   7188   -259  -1114     41       C  
ATOM   5062  C   THR A  69      41.956  24.450   4.219  1.00 69.54           C  
ANISOU 5062  C   THR A  69     9677   8752   7995   -261   -926     19       C  
ATOM   5063  O   THR A  69      41.043  25.248   3.986  1.00 75.39           O  
ANISOU 5063  O   THR A  69    10404   9530   8711   -247   -781     61       O  
ATOM   5064  CB  THR A  69      40.444  22.466   4.329  1.00 61.63           C  
ANISOU 5064  CB  THR A  69     8615   7669   7133   -318  -1105    201       C  
ATOM   5065  OG1 THR A  69      40.527  22.216   5.738  1.00 67.27           O  
ANISOU 5065  OG1 THR A  69     9405   8372   7783   -399  -1122    286       O  
ATOM   5066  CG2 THR A  69      40.058  21.182   3.613  1.00 54.89           C  
ANISOU 5066  CG2 THR A  69     7701   6747   6408   -313  -1282    225       C  
ATOM   5067  N   ASP A  70      43.090  24.818   4.811  1.00 70.24           N  
ANISOU 5067  N   ASP A  70     9828   8848   8014   -275   -935    -46       N  
ATOM   5068  CA  ASP A  70      43.329  26.176   5.289  1.00 65.12           C  
ANISOU 5068  CA  ASP A  70     9250   8242   7251   -287   -781    -68       C  
ATOM   5069  C   ASP A  70      44.265  26.888   4.323  1.00 65.56           C  
ANISOU 5069  C   ASP A  70     9276   8338   7296   -246   -768   -190       C  
ATOM   5070  O   ASP A  70      45.350  26.386   4.026  1.00 67.93           O  
ANISOU 5070  O   ASP A  70     9545   8644   7621   -233   -888   -273       O  
ATOM   5071  CB  ASP A  70      43.924  26.161   6.696  1.00 67.92           C  
ANISOU 5071  CB  ASP A  70     9703   8584   7520   -351   -799    -43       C  
ATOM   5072  CG  ASP A  70      42.893  25.852   7.758  1.00 79.23           C  
ANISOU 5072  CG  ASP A  70    11175  10013   8917   -406   -756     88       C  
ATOM   5073  OD1 ASP A  70      42.953  24.752   8.346  1.00 84.13           O  
ANISOU 5073  OD1 ASP A  70    11801  10596   9570   -456   -887    152       O  
ATOM   5074  OD2 ASP A  70      42.018  26.710   8.001  1.00 86.01           O  
ANISOU 5074  OD2 ASP A  70    12055  10912   9713   -398   -595    129       O  
ATOM   5075  N   PHE A  71      43.854  28.055   3.841  1.00 59.69           N  
ANISOU 5075  N   PHE A  71     8538   7627   6513   -226   -630   -199       N  
ATOM   5076  CA  PHE A  71      44.653  28.821   2.895  1.00 59.68           C  
ANISOU 5076  CA  PHE A  71     8509   7675   6493   -207   -614   -295       C  
ATOM   5077  C   PHE A  71      44.952  30.188   3.487  1.00 64.28           C  
ANISOU 5077  C   PHE A  71     9195   8264   6966   -239   -500   -303       C  
ATOM   5078  O   PHE A  71      44.048  30.863   3.990  1.00 64.88           O  
ANISOU 5078  O   PHE A  71     9331   8317   7005   -236   -384   -245       O  
ATOM   5079  CB  PHE A  71      43.936  28.933   1.550  1.00 54.30           C  
ANISOU 5079  CB  PHE A  71     7736   7019   5875   -160   -586   -298       C  
ATOM   5080  CG  PHE A  71      43.749  27.610   0.872  1.00 51.25           C  
ANISOU 5080  CG  PHE A  71     7255   6623   5593   -127   -714   -308       C  
ATOM   5081  CD1 PHE A  71      42.683  26.792   1.204  1.00 58.57           C  
ANISOU 5081  CD1 PHE A  71     8173   7500   6583   -129   -739   -214       C  
ATOM   5082  CD2 PHE A  71      44.661  27.167  -0.069  1.00 49.08           C  
ANISOU 5082  CD2 PHE A  71     6903   6396   5348    -95   -816   -414       C  
ATOM   5083  CE1 PHE A  71      42.518  25.568   0.598  1.00 58.17           C  
ANISOU 5083  CE1 PHE A  71     8049   7422   6631   -104   -876   -223       C  
ATOM   5084  CE2 PHE A  71      44.500  25.945  -0.679  1.00 53.28           C  
ANISOU 5084  CE2 PHE A  71     7360   6909   5976    -54   -945   -439       C  
ATOM   5085  CZ  PHE A  71      43.429  25.142  -0.346  1.00 58.21           C  
ANISOU 5085  CZ  PHE A  71     7989   7458   6669    -60   -982   -342       C  
ATOM   5086  N   THR A  72      46.222  30.588   3.438  1.00 64.57           N  
ANISOU 5086  N   THR A  72     9250   8335   6950   -269   -540   -378       N  
ATOM   5087  CA  THR A  72      46.686  31.780   4.139  1.00 63.61           C  
ANISOU 5087  CA  THR A  72     9242   8206   6722   -315   -466   -388       C  
ATOM   5088  C   THR A  72      47.370  32.724   3.164  1.00 62.91           C  
ANISOU 5088  C   THR A  72     9130   8170   6603   -331   -452   -447       C  
ATOM   5089  O   THR A  72      48.378  32.365   2.550  1.00 67.69           O  
ANISOU 5089  O   THR A  72     9657   8845   7218   -342   -541   -510       O  
ATOM   5090  CB  THR A  72      47.643  31.409   5.276  1.00 67.00           C  
ANISOU 5090  CB  THR A  72     9736   8625   7096   -366   -539   -402       C  
ATOM   5091  OG1 THR A  72      46.960  30.584   6.229  1.00 70.47           O  
ANISOU 5091  OG1 THR A  72    10205   9020   7552   -368   -552   -331       O  
ATOM   5092  CG2 THR A  72      48.146  32.662   5.970  1.00 68.83           C  
ANISOU 5092  CG2 THR A  72    10094   8845   7214   -420   -471   -416       C  
ATOM   5093  N   LEU A  73      46.826  33.927   3.029  1.00 57.32           N  
ANISOU 5093  N   LEU A  73     8487   7435   5857   -333   -348   -424       N  
ATOM   5094  CA  LEU A  73      47.509  35.016   2.348  1.00 47.89           C  
ANISOU 5094  CA  LEU A  73     7306   6276   4613   -377   -339   -460       C  
ATOM   5095  C   LEU A  73      48.311  35.802   3.374  1.00 47.39           C  
ANISOU 5095  C   LEU A  73     7377   6183   4448   -445   -334   -475       C  
ATOM   5096  O   LEU A  73      47.792  36.147   4.439  1.00 47.74           O  
ANISOU 5096  O   LEU A  73     7536   6153   4450   -438   -271   -447       O  
ATOM   5097  CB  LEU A  73      46.503  35.930   1.648  1.00 44.51           C  
ANISOU 5097  CB  LEU A  73     6891   5815   4205   -346   -249   -424       C  
ATOM   5098  CG  LEU A  73      47.082  37.219   1.039  1.00 45.36           C  
ANISOU 5098  CG  LEU A  73     7040   5937   4256   -405   -243   -439       C  
ATOM   5099  CD1 LEU A  73      47.918  36.900  -0.184  1.00 42.89           C  
ANISOU 5099  CD1 LEU A  73     6597   5746   3956   -441   -320   -477       C  
ATOM   5100  CD2 LEU A  73      45.979  38.201   0.700  1.00 43.11           C  
ANISOU 5100  CD2 LEU A  73     6808   5582   3991   -367   -157   -394       C  
ATOM   5101  N   THR A  74      49.576  36.067   3.069  1.00 50.98           N  
ANISOU 5101  N   THR A  74     7811   6705   4855   -512   -402   -519       N  
ATOM   5102  CA  THR A  74      50.428  36.850   3.950  1.00 54.53           C  
ANISOU 5102  CA  THR A  74     8383   7131   5205   -592   -413   -530       C  
ATOM   5103  C   THR A  74      50.982  38.056   3.208  1.00 54.37           C  
ANISOU 5103  C   THR A  74     8384   7140   5133   -664   -416   -536       C  
ATOM   5104  O   THR A  74      51.426  37.944   2.061  1.00 56.55           O  
ANISOU 5104  O   THR A  74     8536   7519   5429   -682   -457   -553       O  
ATOM   5105  CB  THR A  74      51.582  36.011   4.512  1.00 55.45           C  
ANISOU 5105  CB  THR A  74     8464   7304   5301   -628   -514   -565       C  
ATOM   5106  OG1 THR A  74      51.056  34.978   5.353  1.00 59.23           O  
ANISOU 5106  OG1 THR A  74     8951   7735   5819   -580   -524   -543       O  
ATOM   5107  CG2 THR A  74      52.529  36.880   5.330  1.00 61.13           C  
ANISOU 5107  CG2 THR A  74     9305   8008   5914   -725   -535   -573       C  
ATOM   5108  N   ILE A  75      50.928  39.212   3.862  1.00 53.70           N  
ANISOU 5108  N   ILE A  75     8459   6967   4979   -707   -376   -521       N  
ATOM   5109  CA  ILE A  75      51.619  40.416   3.417  1.00 57.12           C  
ANISOU 5109  CA  ILE A  75     8948   7408   5349   -804   -405   -517       C  
ATOM   5110  C   ILE A  75      52.726  40.672   4.431  1.00 63.72           C  
ANISOU 5110  C   ILE A  75     9879   8240   6092   -895   -463   -535       C  
ATOM   5111  O   ILE A  75      52.450  41.000   5.591  1.00 66.36           O  
ANISOU 5111  O   ILE A  75    10362   8470   6380   -887   -429   -537       O  
ATOM   5112  CB  ILE A  75      50.669  41.616   3.300  1.00 49.47           C  
ANISOU 5112  CB  ILE A  75     8100   6319   4380   -780   -336   -487       C  
ATOM   5113  CG1 ILE A  75      49.328  41.172   2.714  1.00 46.96           C  
ANISOU 5113  CG1 ILE A  75     7703   5982   4157   -664   -264   -465       C  
ATOM   5114  CG2 ILE A  75      51.291  42.700   2.435  1.00 43.62           C  
ANISOU 5114  CG2 ILE A  75     7374   5601   3599   -885   -387   -466       C  
ATOM   5115  CD1 ILE A  75      48.290  42.273   2.651  1.00 44.71           C  
ANISOU 5115  CD1 ILE A  75     7527   5577   3885   -616   -195   -440       C  
ATOM   5116  N   SER A  76      53.981  40.514   4.002  1.00 67.50           N  
ANISOU 5116  N   SER A  76    10267   8844   6537   -981   -549   -551       N  
ATOM   5117  CA  SER A  76      55.098  40.488   4.940  1.00 71.39           C  
ANISOU 5117  CA  SER A  76    10813   9357   6953  -1063   -618   -566       C  
ATOM   5118  C   SER A  76      55.555  41.874   5.379  1.00 74.85           C  
ANISOU 5118  C   SER A  76    11420   9723   7297  -1177   -637   -546       C  
ATOM   5119  O   SER A  76      56.214  41.990   6.418  1.00 76.47           O  
ANISOU 5119  O   SER A  76    11723   9899   7433  -1237   -678   -554       O  
ATOM   5120  CB  SER A  76      56.282  39.736   4.328  1.00 72.78           C  
ANISOU 5120  CB  SER A  76    10810   9711   7131  -1102   -707   -595       C  
ATOM   5121  OG  SER A  76      57.097  40.606   3.562  1.00 76.15           O  
ANISOU 5121  OG  SER A  76    11204  10232   7497  -1218   -749   -578       O  
ATOM   5122  N   SER A  77      55.235  42.924   4.615  1.00 72.06           N  
ANISOU 5122  N   SER A  77    11109   9331   6938  -1213   -621   -515       N  
ATOM   5123  CA  SER A  77      55.628  44.287   4.981  1.00 68.40           C  
ANISOU 5123  CA  SER A  77    10821   8777   6392  -1324   -659   -492       C  
ATOM   5124  C   SER A  77      54.524  45.223   4.480  1.00 63.75           C  
ANISOU 5124  C   SER A  77    10321   8060   5839  -1277   -604   -467       C  
ATOM   5125  O   SER A  77      54.599  45.793   3.390  1.00 68.14           O  
ANISOU 5125  O   SER A  77    10828   8655   6406  -1335   -634   -427       O  
ATOM   5126  CB  SER A  77      56.994  44.667   4.409  1.00 66.09           C  
ANISOU 5126  CB  SER A  77    10458   8618   6034  -1485   -762   -465       C  
ATOM   5127  OG  SER A  77      57.267  46.042   4.619  1.00 60.68           O  
ANISOU 5127  OG  SER A  77     9947   7830   5278  -1602   -811   -428       O  
ATOM   5128  N   LEU A  78      53.490  45.375   5.305  1.00 56.50           N  
ANISOU 5128  N   LEU A  78     9533   6997   4937  -1169   -526   -491       N  
ATOM   5129  CA  LEU A  78      52.306  46.135   4.922  1.00 55.66           C  
ANISOU 5129  CA  LEU A  78     9500   6768   4879  -1087   -466   -479       C  
ATOM   5130  C   LEU A  78      52.679  47.554   4.516  1.00 58.71           C  
ANISOU 5130  C   LEU A  78    10011   7072   5224  -1197   -541   -446       C  
ATOM   5131  O   LEU A  78      53.320  48.282   5.279  1.00 65.09           O  
ANISOU 5131  O   LEU A  78    10977   7804   5951  -1284   -601   -457       O  
ATOM   5132  CB  LEU A  78      51.307  46.158   6.077  1.00 54.69           C  
ANISOU 5132  CB  LEU A  78     9507   6520   4752   -963   -376   -520       C  
ATOM   5133  CG  LEU A  78      49.898  46.660   5.752  1.00 53.88           C  
ANISOU 5133  CG  LEU A  78     9442   6314   4716   -834   -294   -518       C  
ATOM   5134  CD1 LEU A  78      49.181  45.675   4.845  1.00 54.82           C  
ANISOU 5134  CD1 LEU A  78     9362   6530   4936   -752   -240   -489       C  
ATOM   5135  CD2 LEU A  78      49.100  46.906   7.024  1.00 54.28           C  
ANISOU 5135  CD2 LEU A  78     9641   6254   4729   -728   -214   -570       C  
ATOM   5136  N   GLN A  79      52.286  47.938   3.309  1.00 61.19           N  
ANISOU 5136  N   GLN A  79    10258   7399   5592  -1202   -549   -399       N  
ATOM   5137  CA  GLN A  79      52.486  49.281   2.797  1.00 62.80           C  
ANISOU 5137  CA  GLN A  79    10577   7514   5772  -1305   -630   -351       C  
ATOM   5138  C   GLN A  79      51.149  50.000   2.666  1.00 63.54           C  
ANISOU 5138  C   GLN A  79    10774   7436   5933  -1181   -579   -352       C  
ATOM   5139  O   GLN A  79      50.099  49.361   2.541  1.00 67.30           O  
ANISOU 5139  O   GLN A  79    11166   7919   6484  -1032   -480   -370       O  
ATOM   5140  CB  GLN A  79      53.197  49.244   1.436  1.00 60.72           C  
ANISOU 5140  CB  GLN A  79    10151   7416   5504  -1434   -699   -283       C  
ATOM   5141  CG  GLN A  79      54.520  48.490   1.450  1.00 64.79           C  
ANISOU 5141  CG  GLN A  79    10531   8130   5957  -1542   -748   -288       C  
ATOM   5142  CD  GLN A  79      55.548  49.114   2.379  1.00 70.00           C  
ANISOU 5142  CD  GLN A  79    11336   8744   6518  -1672   -832   -289       C  
ATOM   5143  OE1 GLN A  79      56.335  48.410   3.013  1.00 72.23           O  
ANISOU 5143  OE1 GLN A  79    11566   9120   6758  -1697   -845   -322       O  
ATOM   5144  NE2 GLN A  79      55.551  50.440   2.457  1.00 67.38           N  
ANISOU 5144  NE2 GLN A  79    11189   8259   6152  -1758   -903   -250       N  
ATOM   5145  N   PRO A  80      51.148  51.336   2.718  1.00 63.98           N  
ANISOU 5145  N   PRO A  80    11015   7330   5965  -1235   -654   -334       N  
ATOM   5146  CA  PRO A  80      49.878  52.076   2.601  1.00 65.01           C  
ANISOU 5146  CA  PRO A  80    11247   7287   6166  -1102   -617   -343       C  
ATOM   5147  C   PRO A  80      49.067  51.726   1.364  1.00 60.30           C  
ANISOU 5147  C   PRO A  80    10487   6759   5667  -1039   -574   -291       C  
ATOM   5148  O   PRO A  80      47.833  51.671   1.437  1.00 57.85           O  
ANISOU 5148  O   PRO A  80    10178   6372   5429   -872   -488   -317       O  
ATOM   5149  CB  PRO A  80      50.342  53.538   2.581  1.00 63.69           C  
ANISOU 5149  CB  PRO A  80    11283   6959   5957  -1221   -753   -312       C  
ATOM   5150  CG  PRO A  80      51.592  53.530   3.386  1.00 63.09           C  
ANISOU 5150  CG  PRO A  80    11277   6921   5773  -1359   -819   -329       C  
ATOM   5151  CD  PRO A  80      52.270  52.221   3.079  1.00 61.53           C  
ANISOU 5151  CD  PRO A  80    10849   6968   5562  -1408   -780   -314       C  
ATOM   5152  N   GLU A  81      49.725  51.476   0.230  1.00 59.06           N  
ANISOU 5152  N   GLU A  81    10179   6755   5506  -1168   -631   -220       N  
ATOM   5153  CA  GLU A  81      49.012  51.117  -0.990  1.00 56.21           C  
ANISOU 5153  CA  GLU A  81     9658   6471   5226  -1120   -598   -171       C  
ATOM   5154  C   GLU A  81      48.291  49.780  -0.882  1.00 57.83           C  
ANISOU 5154  C   GLU A  81     9708   6772   5491   -971   -475   -215       C  
ATOM   5155  O   GLU A  81      47.520  49.440  -1.785  1.00 60.72           O  
ANISOU 5155  O   GLU A  81     9954   7185   5934   -907   -437   -182       O  
ATOM   5156  CB  GLU A  81      49.979  51.077  -2.175  1.00 60.78           C  
ANISOU 5156  CB  GLU A  81    10102   7226   5764  -1300   -684    -95       C  
ATOM   5157  CG  GLU A  81      51.188  50.185  -1.950  1.00 71.59           C  
ANISOU 5157  CG  GLU A  81    11352   8789   7059  -1389   -694   -123       C  
ATOM   5158  CD  GLU A  81      52.476  50.974  -1.827  1.00 84.94           C  
ANISOU 5158  CD  GLU A  81    13125  10503   8647  -1590   -814    -81       C  
ATOM   5159  OE1 GLU A  81      53.234  51.030  -2.818  1.00 90.68           O  
ANISOU 5159  OE1 GLU A  81    13731  11397   9328  -1738   -881    -17       O  
ATOM   5160  OE2 GLU A  81      52.725  51.548  -0.746  1.00 86.89           O  
ANISOU 5160  OE2 GLU A  81    13556  10608   8852  -1606   -845   -112       O  
ATOM   5161  N   ASP A  82      48.521  49.018   0.183  1.00 57.81           N  
ANISOU 5161  N   ASP A  82     9708   6799   5456   -923   -422   -280       N  
ATOM   5162  CA  ASP A  82      47.885  47.721   0.356  1.00 55.63           C  
ANISOU 5162  CA  ASP A  82     9295   6607   5234   -799   -323   -311       C  
ATOM   5163  C   ASP A  82      46.509  47.814   1.000  1.00 59.50           C  
ANISOU 5163  C   ASP A  82     9855   6974   5779   -627   -224   -339       C  
ATOM   5164  O   ASP A  82      45.893  46.774   1.257  1.00 65.20           O  
ANISOU 5164  O   ASP A  82    10475   7756   6541   -529   -143   -356       O  
ATOM   5165  CB  ASP A  82      48.788  46.801   1.180  1.00 59.17           C  
ANISOU 5165  CB  ASP A  82     9707   7152   5624   -837   -327   -356       C  
ATOM   5166  CG  ASP A  82      50.130  46.568   0.519  1.00 60.51           C  
ANISOU 5166  CG  ASP A  82     9771   7478   5742   -988   -417   -336       C  
ATOM   5167  OD1 ASP A  82      50.190  46.603  -0.729  1.00 55.94           O  
ANISOU 5167  OD1 ASP A  82     9077   6991   5188  -1036   -447   -292       O  
ATOM   5168  OD2 ASP A  82      51.124  46.358   1.245  1.00 59.58           O  
ANISOU 5168  OD2 ASP A  82     9681   7402   5553  -1060   -457   -364       O  
ATOM   5169  N   PHE A  83      46.019  49.021   1.279  1.00 58.55           N  
ANISOU 5169  N   PHE A  83     9902   6686   5658   -588   -233   -346       N  
ATOM   5170  CA  PHE A  83      44.622  49.189   1.657  1.00 56.80           C  
ANISOU 5170  CA  PHE A  83     9718   6368   5497   -411   -138   -371       C  
ATOM   5171  C   PHE A  83      43.734  48.652   0.547  1.00 58.50           C  
ANISOU 5171  C   PHE A  83     9761   6654   5814   -347    -99   -316       C  
ATOM   5172  O   PHE A  83      43.786  49.136  -0.588  1.00 62.08           O  
ANISOU 5172  O   PHE A  83    10178   7105   6303   -408   -164   -257       O  
ATOM   5173  CB  PHE A  83      44.311  50.663   1.925  1.00 58.06           C  
ANISOU 5173  CB  PHE A  83    10081   6330   5648   -377   -180   -392       C  
ATOM   5174  CG  PHE A  83      42.840  50.993   1.881  1.00 62.43           C  
ANISOU 5174  CG  PHE A  83    10641   6795   6284   -195   -103   -404       C  
ATOM   5175  CD1 PHE A  83      42.040  50.814   2.999  1.00 66.87           C  
ANISOU 5175  CD1 PHE A  83    11248   7329   6830    -42      7   -476       C  
ATOM   5176  CD2 PHE A  83      42.259  51.485   0.721  1.00 64.16           C  
ANISOU 5176  CD2 PHE A  83    10813   6974   6590   -178   -141   -340       C  
ATOM   5177  CE1 PHE A  83      40.688  51.115   2.958  1.00 68.34           C  
ANISOU 5177  CE1 PHE A  83    11422   7456   7088    132     82   -489       C  
ATOM   5178  CE2 PHE A  83      40.911  51.783   0.673  1.00 69.13           C  
ANISOU 5178  CE2 PHE A  83    11438   7528   7300     -5    -74   -349       C  
ATOM   5179  CZ  PHE A  83      40.124  51.600   1.793  1.00 69.85           C  
ANISOU 5179  CZ  PHE A  83    11564   7600   7377    155     40   -426       C  
ATOM   5180  N   ALA A  84      42.921  47.652   0.872  1.00 53.18           N  
ANISOU 5180  N   ALA A  84     8981   6046   5181   -235      1   -328       N  
ATOM   5181  CA  ALA A  84      42.066  46.998  -0.111  1.00 52.12           C  
ANISOU 5181  CA  ALA A  84     8676   5987   5141   -177     37   -276       C  
ATOM   5182  C   ALA A  84      41.198  45.977   0.611  1.00 55.47           C  
ANISOU 5182  C   ALA A  84     9022   6462   5590    -60    143   -293       C  
ATOM   5183  O   ALA A  84      41.333  45.756   1.820  1.00 57.12           O  
ANISOU 5183  O   ALA A  84     9303   6664   5738    -36    186   -341       O  
ATOM   5184  CB  ALA A  84      42.876  46.309  -1.214  1.00 50.01           C  
ANISOU 5184  CB  ALA A  84     8262   5860   4880   -296    -31   -238       C  
ATOM   5185  N   THR A  85      40.296  45.366  -0.151  1.00 55.68           N  
ANISOU 5185  N   THR A  85     8902   6548   5704      1    179   -245       N  
ATOM   5186  CA  THR A  85      39.601  44.160   0.269  1.00 52.96           C  
ANISOU 5186  CA  THR A  85     8445   6287   5391     71    253   -235       C  
ATOM   5187  C   THR A  85      40.207  42.985  -0.486  1.00 42.75           C  
ANISOU 5187  C   THR A  85     7004   5116   4121    -12    195   -213       C  
ATOM   5188  O   THR A  85      40.386  43.051  -1.709  1.00 42.75           O  
ANISOU 5188  O   THR A  85     6930   5154   4161    -60    138   -182       O  
ATOM   5189  CB  THR A  85      38.101  44.250  -0.004  1.00 52.61           C  
ANISOU 5189  CB  THR A  85     8335   6224   5429    200    328   -195       C  
ATOM   5190  OG1 THR A  85      37.581  45.454   0.571  1.00 58.83           O  
ANISOU 5190  OG1 THR A  85     9259   6894   6199    291    370   -229       O  
ATOM   5191  CG2 THR A  85      37.376  43.062   0.609  1.00 47.67           C  
ANISOU 5191  CG2 THR A  85     7606   5685   4820    258    403   -176       C  
ATOM   5192  N   TYR A  86      40.539  41.927   0.245  1.00 40.05           N  
ANISOU 5192  N   TYR A  86     6628   4838   3753    -26    201   -232       N  
ATOM   5193  CA  TYR A  86      41.193  40.757  -0.319  1.00 47.18           C  
ANISOU 5193  CA  TYR A  86     7405   5846   4677    -89    134   -231       C  
ATOM   5194  C   TYR A  86      40.221  39.586  -0.325  1.00 45.02           C  
ANISOU 5194  C   TYR A  86     7011   5620   4475    -24    168   -191       C  
ATOM   5195  O   TYR A  86      39.517  39.345   0.662  1.00 46.43           O  
ANISOU 5195  O   TYR A  86     7216   5780   4644     34    236   -177       O  
ATOM   5196  CB  TYR A  86      42.460  40.408   0.468  1.00 44.63           C  
ANISOU 5196  CB  TYR A  86     7134   5550   4275   -167     83   -280       C  
ATOM   5197  CG  TYR A  86      43.525  41.484   0.392  1.00 51.97           C  
ANISOU 5197  CG  TYR A  86     8168   6448   5131   -255     32   -310       C  
ATOM   5198  CD1 TYR A  86      44.650  41.322  -0.406  1.00 54.89           C  
ANISOU 5198  CD1 TYR A  86     8470   6905   5479   -353    -56   -323       C  
ATOM   5199  CD2 TYR A  86      43.397  42.670   1.107  1.00 58.38           C  
ANISOU 5199  CD2 TYR A  86     9142   7148   5890   -242     65   -324       C  
ATOM   5200  CE1 TYR A  86      45.622  42.304  -0.482  1.00 57.60           C  
ANISOU 5200  CE1 TYR A  86     8902   7234   5751   -452   -109   -334       C  
ATOM   5201  CE2 TYR A  86      44.361  43.659   1.034  1.00 58.32           C  
ANISOU 5201  CE2 TYR A  86     9239   7103   5819   -336      1   -341       C  
ATOM   5202  CZ  TYR A  86      45.471  43.472   0.238  1.00 59.17           C  
ANISOU 5202  CZ  TYR A  86     9272   7306   5905   -449    -86   -338       C  
ATOM   5203  OH  TYR A  86      46.430  44.457   0.168  1.00 56.92           O  
ANISOU 5203  OH  TYR A  86     9082   6994   5549   -561   -155   -340       O  
ATOM   5204  N   TYR A  87      40.174  38.870  -1.445  1.00 45.47           N  
ANISOU 5204  N   TYR A  87     6936   5745   4596    -39    116   -171       N  
ATOM   5205  CA  TYR A  87      39.226  37.780  -1.634  1.00 51.11           C  
ANISOU 5205  CA  TYR A  87     7535   6497   5388     11    127   -125       C  
ATOM   5206  C   TYR A  87      39.961  36.493  -1.978  1.00 53.42           C  
ANISOU 5206  C   TYR A  87     7735   6862   5700    -35     32   -153       C  
ATOM   5207  O   TYR A  87      40.899  36.500  -2.778  1.00 59.98           O  
ANISOU 5207  O   TYR A  87     8531   7744   6515    -88    -38   -197       O  
ATOM   5208  CB  TYR A  87      38.223  38.102  -2.751  1.00 53.00           C  
ANISOU 5208  CB  TYR A  87     7697   6736   5704     55    147    -72       C  
ATOM   5209  CG  TYR A  87      37.270  39.240  -2.453  1.00 53.79           C  
ANISOU 5209  CG  TYR A  87     7867   6761   5809    129    236    -42       C  
ATOM   5210  CD1 TYR A  87      37.522  40.522  -2.921  1.00 56.96           C  
ANISOU 5210  CD1 TYR A  87     8347   7104   6191    116    227    -52       C  
ATOM   5211  CD2 TYR A  87      36.107  39.027  -1.723  1.00 55.49           C  
ANISOU 5211  CD2 TYR A  87     8066   6970   6050    212    320     -1       C  
ATOM   5212  CE1 TYR A  87      36.650  41.563  -2.661  1.00 62.25           C  
ANISOU 5212  CE1 TYR A  87     9086   7691   6876    200    293    -34       C  
ATOM   5213  CE2 TYR A  87      35.228  40.063  -1.457  1.00 57.61           C  
ANISOU 5213  CE2 TYR A  87     8387   7179   6323    300    401     13       C  
ATOM   5214  CZ  TYR A  87      35.505  41.329  -1.929  1.00 60.67           C  
ANISOU 5214  CZ  TYR A  87     8861   7490   6701    301    384     -9       C  
ATOM   5215  OH  TYR A  87      34.635  42.363  -1.667  1.00 67.03           O  
ANISOU 5215  OH  TYR A  87     9725   8222   7520    404    450     -6       O  
ATOM   5216  N   CYS A  88      39.532  35.389  -1.374  1.00 54.25           N  
ANISOU 5216  N   CYS A  88     7799   6975   5836    -14     24   -127       N  
ATOM   5217  CA  CYS A  88      39.982  34.067  -1.780  1.00 56.74           C  
ANISOU 5217  CA  CYS A  88     8022   7340   6195    -37    -80   -149       C  
ATOM   5218  C   CYS A  88      38.945  33.433  -2.699  1.00 51.27           C  
ANISOU 5218  C   CYS A  88     7217   6666   5596     -1    -95    -97       C  
ATOM   5219  O   CYS A  88      37.772  33.815  -2.708  1.00 51.99           O  
ANISOU 5219  O   CYS A  88     7298   6737   5721     41    -19    -28       O  
ATOM   5220  CB  CYS A  88      40.240  33.168  -0.565  1.00 61.75           C  
ANISOU 5220  CB  CYS A  88     8690   7960   6811    -52   -112   -145       C  
ATOM   5221  SG  CYS A  88      38.822  32.924   0.527  1.00 76.19           S  
ANISOU 5221  SG  CYS A  88    10536   9761   8650    -16    -23    -46       S  
ATOM   5222  N   GLN A  89      39.394  32.460  -3.486  1.00 48.49           N  
ANISOU 5222  N   GLN A  89     6779   6358   5287    -14   -201   -135       N  
ATOM   5223  CA  GLN A  89      38.528  31.830  -4.468  1.00 51.30           C  
ANISOU 5223  CA  GLN A  89     7032   6733   5728     11   -235    -97       C  
ATOM   5224  C   GLN A  89      38.951  30.385  -4.663  1.00 53.70           C  
ANISOU 5224  C   GLN A  89     7274   7052   6079      6   -366   -139       C  
ATOM   5225  O   GLN A  89      40.149  30.085  -4.715  1.00 58.97           O  
ANISOU 5225  O   GLN A  89     7942   7750   6712    -10   -439   -229       O  
ATOM   5226  CB  GLN A  89      38.566  32.563  -5.816  1.00 48.27           C  
ANISOU 5226  CB  GLN A  89     6602   6395   5344      7   -229   -116       C  
ATOM   5227  CG  GLN A  89      37.713  31.905  -6.893  1.00 44.27           C  
ANISOU 5227  CG  GLN A  89     5990   5912   4920     27   -274    -81       C  
ATOM   5228  CD  GLN A  89      37.980  32.460  -8.278  1.00 52.23           C  
ANISOU 5228  CD  GLN A  89     6945   6986   5913      9   -291   -112       C  
ATOM   5229  OE1 GLN A  89      39.127  32.533  -8.720  1.00 58.62           O  
ANISOU 5229  OE1 GLN A  89     7744   7863   6665    -24   -339   -197       O  
ATOM   5230  NE2 GLN A  89      36.918  32.849  -8.974  1.00 50.72           N  
ANISOU 5230  NE2 GLN A  89     6715   6790   5769     25   -256    -39       N  
ATOM   5231  N   GLN A  90      37.961  29.500  -4.764  1.00 45.91           N  
ANISOU 5231  N   GLN A  90     6232   6041   5171     21   -402    -72       N  
ATOM   5232  CA  GLN A  90      38.178  28.122  -5.172  1.00 40.89           C  
ANISOU 5232  CA  GLN A  90     5536   5402   4598     24   -545   -109       C  
ATOM   5233  C   GLN A  90      37.711  27.948  -6.610  1.00 44.81           C  
ANISOU 5233  C   GLN A  90     5943   5937   5147     42   -584   -119       C  
ATOM   5234  O   GLN A  90      36.685  28.509  -7.017  1.00 52.61           O  
ANISOU 5234  O   GLN A  90     6905   6928   6157     48   -509    -41       O  
ATOM   5235  CB  GLN A  90      37.443  27.137  -4.256  1.00 38.86           C  
ANISOU 5235  CB  GLN A  90     5288   5084   4391      8   -589    -19       C  
ATOM   5236  CG  GLN A  90      35.938  27.189  -4.360  1.00 46.16           C  
ANISOU 5236  CG  GLN A  90     6171   6003   5366      9   -527    106       C  
ATOM   5237  CD  GLN A  90      35.351  26.105  -5.249  1.00 56.18           C  
ANISOU 5237  CD  GLN A  90     7359   7259   6729      8   -647    129       C  
ATOM   5238  OE1 GLN A  90      36.076  25.338  -5.888  1.00 57.64           O  
ANISOU 5238  OE1 GLN A  90     7521   7437   6942     18   -778     36       O  
ATOM   5239  NE2 GLN A  90      34.023  26.060  -5.317  1.00 60.90           N  
ANISOU 5239  NE2 GLN A  90     7908   7857   7372     -1   -606    250       N  
ATOM   5240  N   HIS A  91      38.491  27.201  -7.387  1.00 40.56           N  
ANISOU 5240  N   HIS A  91     5356   5433   4623     55   -703   -224       N  
ATOM   5241  CA  HIS A  91      38.073  26.748  -8.706  1.00 41.65           C  
ANISOU 5241  CA  HIS A  91     5409   5606   4810     73   -769   -246       C  
ATOM   5242  C   HIS A  91      38.305  25.249  -8.846  1.00 44.67           C  
ANISOU 5242  C   HIS A  91     5762   5951   5259     97   -936   -306       C  
ATOM   5243  O   HIS A  91      38.572  24.748  -9.937  1.00 44.33           O  
ANISOU 5243  O   HIS A  91     5656   5954   5232    126  -1024   -395       O  
ATOM   5244  CB  HIS A  91      38.774  27.538  -9.814  1.00 39.85           C  
ANISOU 5244  CB  HIS A  91     5140   5484   4516     72   -741   -330       C  
ATOM   5245  CG  HIS A  91      40.271  27.452  -9.786  1.00 54.84           C  
ANISOU 5245  CG  HIS A  91     7038   7449   6348     77   -790   -461       C  
ATOM   5246  ND1 HIS A  91      40.967  26.396 -10.336  1.00 61.19           N  
ANISOU 5246  ND1 HIS A  91     7784   8294   7170    117   -921   -582       N  
ATOM   5247  CD2 HIS A  91      41.207  28.306  -9.306  1.00 59.85           C  
ANISOU 5247  CD2 HIS A  91     7719   8124   6898     49   -730   -493       C  
ATOM   5248  CE1 HIS A  91      42.264  26.595 -10.182  1.00 65.05           C  
ANISOU 5248  CE1 HIS A  91     8271   8858   7587    119   -933   -681       C  
ATOM   5249  NE2 HIS A  91      42.436  27.747  -9.558  1.00 65.57           N  
ANISOU 5249  NE2 HIS A  91     8401   8925   7590     69   -819   -623       N  
ATOM   5250  N   TYR A  92      38.203  24.526  -7.729  1.00 50.01           N  
ANISOU 5250  N   TYR A  92     6488   6542   5970     85   -988   -258       N  
ATOM   5251  CA  TYR A  92      38.284  23.070  -7.776  1.00 56.93           C  
ANISOU 5251  CA  TYR A  92     7351   7353   6925    102  -1166   -294       C  
ATOM   5252  C   TYR A  92      37.027  22.474  -8.395  1.00 58.21           C  
ANISOU 5252  C   TYR A  92     7469   7476   7171     89  -1221   -209       C  
ATOM   5253  O   TYR A  92      37.101  21.499  -9.154  1.00 62.75           O  
ANISOU 5253  O   TYR A  92     8011   8027   7804    118  -1369   -279       O  
ATOM   5254  CB  TYR A  92      38.515  22.513  -6.371  1.00 60.66           C  
ANISOU 5254  CB  TYR A  92     7896   7744   7408     75  -1215   -246       C  
ATOM   5255  CG  TYR A  92      38.707  21.017  -6.320  1.00 60.80           C  
ANISOU 5255  CG  TYR A  92     7918   7674   7511     90  -1422   -282       C  
ATOM   5256  CD1 TYR A  92      39.906  20.439  -6.716  1.00 61.03           C  
ANISOU 5256  CD1 TYR A  92     7933   7712   7545    153  -1548   -445       C  
ATOM   5257  CD2 TYR A  92      37.695  20.184  -5.866  1.00 58.28           C  
ANISOU 5257  CD2 TYR A  92     7614   7264   7268     40  -1501   -152       C  
ATOM   5258  CE1 TYR A  92      40.088  19.073  -6.668  1.00 60.84           C  
ANISOU 5258  CE1 TYR A  92     7920   7589   7606    180  -1754   -487       C  
ATOM   5259  CE2 TYR A  92      37.867  18.817  -5.815  1.00 62.25           C  
ANISOU 5259  CE2 TYR A  92     8133   7665   7854     47  -1713   -179       C  
ATOM   5260  CZ  TYR A  92      39.066  18.267  -6.216  1.00 65.99           C  
ANISOU 5260  CZ  TYR A  92     8604   8130   8339    123  -1842   -351       C  
ATOM   5261  OH  TYR A  92      39.242  16.904  -6.166  1.00 69.64           O  
ANISOU 5261  OH  TYR A  92     9091   8474   8894    143  -2069   -387       O  
ATOM   5262  N   THR A  93      35.868  23.046  -8.090  1.00 55.21           N  
ANISOU 5262  N   THR A  93     7088   7093   6798     51  -1107    -64       N  
ATOM   5263  CA  THR A  93      34.610  22.636  -8.689  1.00 53.85           C  
ANISOU 5263  CA  THR A  93     6861   6900   6697     30  -1141     33       C  
ATOM   5264  C   THR A  93      33.969  23.817  -9.405  1.00 56.56           C  
ANISOU 5264  C   THR A  93     7160   7318   7012     36   -997     77       C  
ATOM   5265  O   THR A  93      34.310  24.981  -9.167  1.00 60.37           O  
ANISOU 5265  O   THR A  93     7669   7846   7424     46   -863     65       O  
ATOM   5266  CB  THR A  93      33.627  22.082  -7.645  1.00 51.31           C  
ANISOU 5266  CB  THR A  93     6557   6515   6422    -28  -1155    193       C  
ATOM   5267  OG1 THR A  93      33.508  23.006  -6.556  1.00 55.00           O  
ANISOU 5267  OG1 THR A  93     7064   7010   6822    -43   -996    262       O  
ATOM   5268  CG2 THR A  93      34.098  20.740  -7.118  1.00 47.33           C  
ANISOU 5268  CG2 THR A  93     6095   5920   5969    -46  -1341    169       C  
ATOM   5269  N   THR A  94      33.039  23.495 -10.297  1.00 55.38           N  
ANISOU 5269  N   THR A  94     6949   7170   6922     26  -1042    130       N  
ATOM   5270  CA  THR A  94      32.171  24.487 -10.915  1.00 50.64           C  
ANISOU 5270  CA  THR A  94     6301   6624   6316     25   -924    206       C  
ATOM   5271  C   THR A  94      30.819  24.403 -10.208  1.00 57.05           C  
ANISOU 5271  C   THR A  94     7091   7410   7176     -8   -874    380       C  
ATOM   5272  O   THR A  94      30.219  23.328 -10.167  1.00 72.33           O  
ANISOU 5272  O   THR A  94     9002   9299   9180    -46   -989    445       O  
ATOM   5273  CB  THR A  94      32.010  24.245 -12.430  1.00 51.91           C  
ANISOU 5273  CB  THR A  94     6397   6823   6502     33  -1003    155       C  
ATOM   5274  OG1 THR A  94      33.288  23.954 -13.009  1.00 46.50           O  
ANISOU 5274  OG1 THR A  94     5721   6174   5773     65  -1082    -17       O  
ATOM   5275  CG2 THR A  94      31.421  25.461 -13.114  1.00 35.77           C  
ANISOU 5275  CG2 THR A  94     4314   4843   4434     35   -880    211       C  
ATOM   5276  N   PRO A  95      30.318  25.538  -9.687  1.00 57.66           N  
ANISOU 5276  N   PRO A  95     7172   7520   7217      5   -710    455       N  
ATOM   5277  CA  PRO A  95      30.820  26.917  -9.842  1.00 55.41           C  
ANISOU 5277  CA  PRO A  95     6917   7275   6861     42   -583    400       C  
ATOM   5278  C   PRO A  95      32.009  27.347  -8.983  1.00 51.70           C  
ANISOU 5278  C   PRO A  95     6535   6797   6312     53   -539    311       C  
ATOM   5279  O   PRO A  95      32.127  26.873  -7.847  1.00 47.24           O  
ANISOU 5279  O   PRO A  95     6013   6198   5738     37   -546    336       O  
ATOM   5280  CB  PRO A  95      29.591  27.755  -9.463  1.00 49.26           C  
ANISOU 5280  CB  PRO A  95     6109   6515   6095     60   -449    530       C  
ATOM   5281  CG  PRO A  95      28.871  26.907  -8.472  1.00 52.37           C  
ANISOU 5281  CG  PRO A  95     6487   6892   6521     27   -469    634       C  
ATOM   5282  CD  PRO A  95      29.039  25.496  -8.954  1.00 54.43           C  
ANISOU 5282  CD  PRO A  95     6726   7115   6841    -18   -648    614       C  
ATOM   5283  N   PRO A  96      32.845  28.235  -9.510  1.00 49.35           N  
ANISOU 5283  N   PRO A  96     6262   6534   5954     68   -499    222       N  
ATOM   5284  CA  PRO A  96      33.840  28.892  -8.665  1.00 41.79           C  
ANISOU 5284  CA  PRO A  96     5389   5572   4916     71   -438    160       C  
ATOM   5285  C   PRO A  96      33.139  29.738  -7.612  1.00 46.22           C  
ANISOU 5285  C   PRO A  96     5997   6109   5456     88   -302    247       C  
ATOM   5286  O   PRO A  96      32.084  30.328  -7.875  1.00 58.76           O  
ANISOU 5286  O   PRO A  96     7548   7704   7074    112   -229    330       O  
ATOM   5287  CB  PRO A  96      34.630  29.764  -9.653  1.00 37.92           C  
ANISOU 5287  CB  PRO A  96     4898   5137   4372     69   -424     77       C  
ATOM   5288  CG  PRO A  96      33.678  29.975 -10.785  1.00 41.41           C  
ANISOU 5288  CG  PRO A  96     5266   5604   4862     72   -423    137       C  
ATOM   5289  CD  PRO A  96      32.929  28.689 -10.900  1.00 51.23           C  
ANISOU 5289  CD  PRO A  96     6452   6825   6188     70   -514    183       C  
ATOM   5290  N   THR A  97      33.705  29.759  -6.393  1.00 42.28           N  
ANISOU 5290  N   THR A  97     5575   5586   4904     81   -273    226       N  
ATOM   5291  CA  THR A  97      33.101  30.509  -5.300  1.00 44.74           C  
ANISOU 5291  CA  THR A  97     5936   5885   5180    104   -146    291       C  
ATOM   5292  C   THR A  97      34.148  31.363  -4.609  1.00 43.07           C  
ANISOU 5292  C   THR A  97     5831   5658   4877    104    -93    213       C  
ATOM   5293  O   THR A  97      35.253  30.897  -4.323  1.00 45.40           O  
ANISOU 5293  O   THR A  97     6164   5948   5138     72   -164    140       O  
ATOM   5294  CB  THR A  97      32.419  29.591  -4.280  1.00 44.37           C  
ANISOU 5294  CB  THR A  97     5873   5834   5152     83   -155    379       C  
ATOM   5295  OG1 THR A  97      33.384  28.715  -3.700  1.00 52.12           O  
ANISOU 5295  OG1 THR A  97     6899   6790   6113     42   -252    327       O  
ATOM   5296  CG2 THR A  97      31.322  28.780  -4.934  1.00 43.50           C  
ANISOU 5296  CG2 THR A  97     5658   5738   5131     71   -213    471       C  
ATOM   5297  N   PHE A  98      33.774  32.613  -4.347  1.00 38.41           N  
ANISOU 5297  N   PHE A  98     5288   5055   4250    142     22    230       N  
ATOM   5298  CA  PHE A  98      34.595  33.597  -3.663  1.00 37.48           C  
ANISOU 5298  CA  PHE A  98     5284   4910   4046    143     77    167       C  
ATOM   5299  C   PHE A  98      34.376  33.534  -2.158  1.00 39.65           C  
ANISOU 5299  C   PHE A  98     5623   5174   4269    154    144    191       C  
ATOM   5300  O   PHE A  98      33.321  33.112  -1.679  1.00 43.31           O  
ANISOU 5300  O   PHE A  98     6038   5661   4759    175    187    273       O  
ATOM   5301  CB  PHE A  98      34.254  35.009  -4.146  1.00 38.66           C  
ANISOU 5301  CB  PHE A  98     5467   5035   4188    185    151    171       C  
ATOM   5302  CG  PHE A  98      34.825  35.359  -5.486  1.00 40.22           C  
ANISOU 5302  CG  PHE A  98     5637   5249   4397    151     88    135       C  
ATOM   5303  CD1 PHE A  98      36.171  35.656  -5.619  1.00 35.24           C  
ANISOU 5303  CD1 PHE A  98     5062   4628   3700     96     41     54       C  
ATOM   5304  CD2 PHE A  98      34.014  35.414  -6.609  1.00 40.15           C  
ANISOU 5304  CD2 PHE A  98     5541   5259   4456    168     76    188       C  
ATOM   5305  CE1 PHE A  98      36.704  35.989  -6.848  1.00 35.72           C  
ANISOU 5305  CE1 PHE A  98     5086   4729   3755     55    -14     27       C  
ATOM   5306  CE2 PHE A  98      34.540  35.748  -7.847  1.00 40.45           C  
ANISOU 5306  CE2 PHE A  98     5552   5328   4490    127     18    159       C  
ATOM   5307  CZ  PHE A  98      35.889  36.037  -7.964  1.00 41.22           C  
ANISOU 5307  CZ  PHE A  98     5701   5448   4514     69    -25     79       C  
ATOM   5308  N   GLY A  99      35.385  33.984  -1.411  1.00 49.34           N  
ANISOU 5308  N   GLY A  99     6957   6377   5414    131    153    123       N  
ATOM   5309  CA  GLY A  99      35.197  34.250  -0.002  1.00 49.87           C  
ANISOU 5309  CA  GLY A  99     7104   6436   5411    146    233    135       C  
ATOM   5310  C   GLY A  99      34.492  35.575   0.224  1.00 51.45           C  
ANISOU 5310  C   GLY A  99     7355   6612   5582    222    354    138       C  
ATOM   5311  O   GLY A  99      34.288  36.371  -0.694  1.00 52.37           O  
ANISOU 5311  O   GLY A  99     7461   6702   5734    254    364    131       O  
ATOM   5312  N   GLN A 100      34.110  35.813   1.479  1.00 51.40           N  
ANISOU 5312  N   GLN A 100     7407   6615   5508    252    441    147       N  
ATOM   5313  CA  GLN A 100      33.402  37.041   1.815  1.00 54.16           C  
ANISOU 5313  CA  GLN A 100     7809   6942   5827    345    555    134       C  
ATOM   5314  C   GLN A 100      34.303  38.268   1.816  1.00 51.62           C  
ANISOU 5314  C   GLN A 100     7627   6537   5451    348    552     44       C  
ATOM   5315  O   GLN A 100      33.787  39.390   1.847  1.00 51.58           O  
ANISOU 5315  O   GLN A 100     7674   6485   5438    431    619     24       O  
ATOM   5316  CB  GLN A 100      32.720  36.915   3.180  1.00 61.25           C  
ANISOU 5316  CB  GLN A 100     8722   7898   6653    382    654    160       C  
ATOM   5317  CG  GLN A 100      31.661  35.829   3.259  1.00 66.30           C  
ANISOU 5317  CG  GLN A 100     9220   8631   7338    374    666    269       C  
ATOM   5318  CD  GLN A 100      32.211  34.509   3.760  1.00 68.51           C  
ANISOU 5318  CD  GLN A 100     9485   8942   7602    267    579    305       C  
ATOM   5319  OE1 GLN A 100      33.422  34.286   3.763  1.00 66.46           O  
ANISOU 5319  OE1 GLN A 100     9296   8633   7323    203    491    246       O  
ATOM   5320  NE2 GLN A 100      31.320  33.626   4.196  1.00 70.67           N  
ANISOU 5320  NE2 GLN A 100     9666   9301   7885    243    594    407       N  
ATOM   5321  N   GLY A 101      35.616  38.088   1.792  1.00 48.65           N  
ANISOU 5321  N   GLY A 101     7309   6139   5037    262    468     -7       N  
ATOM   5322  CA  GLY A 101      36.529  39.218   1.717  1.00 48.17           C  
ANISOU 5322  CA  GLY A 101     7374   6005   4924    241    447    -79       C  
ATOM   5323  C   GLY A 101      37.011  39.676   3.078  1.00 49.20           C  
ANISOU 5323  C   GLY A 101     7644   6104   4944    237    486   -134       C  
ATOM   5324  O   GLY A 101      36.358  39.488   4.104  1.00 50.20           O  
ANISOU 5324  O   GLY A 101     7783   6261   5027    284    565   -122       O  
ATOM   5325  N   THR A 102      38.191  40.293   3.081  1.00 51.25           N  
ANISOU 5325  N   THR A 102     8011   6312   5151    172    427   -194       N  
ATOM   5326  CA  THR A 102      38.776  40.880   4.280  1.00 53.69           C  
ANISOU 5326  CA  THR A 102     8473   6577   5351    158    448   -254       C  
ATOM   5327  C   THR A 102      39.206  42.302   3.961  1.00 53.74           C  
ANISOU 5327  C   THR A 102     8605   6481   5333    156    426   -301       C  
ATOM   5328  O   THR A 102      40.026  42.518   3.062  1.00 50.62           O  
ANISOU 5328  O   THR A 102     8200   6076   4957     77    339   -301       O  
ATOM   5329  CB  THR A 102      39.971  40.064   4.781  1.00 54.97           C  
ANISOU 5329  CB  THR A 102     8648   6778   5461     53    372   -272       C  
ATOM   5330  OG1 THR A 102      39.521  38.783   5.237  1.00 57.57           O  
ANISOU 5330  OG1 THR A 102     8883   7182   5809     53    382   -222       O  
ATOM   5331  CG2 THR A 102      40.675  40.791   5.921  1.00 56.23           C  
ANISOU 5331  CG2 THR A 102     8975   6885   5504     24    380   -334       C  
ATOM   5332  N   LYS A 103      38.646  43.266   4.687  1.00 58.15           N  
ANISOU 5332  N   LYS A 103     9279   6970   5846    242    497   -342       N  
ATOM   5333  CA  LYS A 103      39.034  44.661   4.531  1.00 61.10           C  
ANISOU 5333  CA  LYS A 103     9799   7221   6194    243    460   -390       C  
ATOM   5334  C   LYS A 103      40.281  44.925   5.363  1.00 59.81           C  
ANISOU 5334  C   LYS A 103     9776   7024   5923    146    406   -447       C  
ATOM   5335  O   LYS A 103      40.296  44.657   6.569  1.00 60.05           O  
ANISOU 5335  O   LYS A 103     9866   7078   5873    161    455   -482       O  
ATOM   5336  CB  LYS A 103      37.901  45.592   4.957  1.00 65.71           C  
ANISOU 5336  CB  LYS A 103    10453   7733   6780    393    547   -425       C  
ATOM   5337  CG  LYS A 103      36.673  45.552   4.063  1.00 74.91           C  
ANISOU 5337  CG  LYS A 103    11488   8917   8056    492    590   -368       C  
ATOM   5338  CD  LYS A 103      35.650  44.549   4.572  1.00 80.76           C  
ANISOU 5338  CD  LYS A 103    12097   9781   8808    564    693   -330       C  
ATOM   5339  CE  LYS A 103      34.670  44.154   3.481  1.00 83.55           C  
ANISOU 5339  CE  LYS A 103    12284  10182   9281    611    705   -248       C  
ATOM   5340  NZ  LYS A 103      34.313  42.710   3.554  1.00 83.19           N  
ANISOU 5340  NZ  LYS A 103    12083  10269   9257    576    729   -179       N  
ATOM   5341  N   VAL A 104      41.327  45.443   4.724  1.00 57.88           N  
ANISOU 5341  N   VAL A 104     9582   6737   5672     39    303   -448       N  
ATOM   5342  CA  VAL A 104      42.567  45.797   5.405  1.00 57.59           C  
ANISOU 5342  CA  VAL A 104     9677   6666   5537    -67    236   -493       C  
ATOM   5343  C   VAL A 104      42.666  47.315   5.452  1.00 62.07           C  
ANISOU 5343  C   VAL A 104    10425   7085   6075    -59    198   -533       C  
ATOM   5344  O   VAL A 104      42.701  47.976   4.407  1.00 65.23           O  
ANISOU 5344  O   VAL A 104    10821   7432   6530    -87    137   -499       O  
ATOM   5345  CB  VAL A 104      43.795  45.186   4.713  1.00 55.80           C  
ANISOU 5345  CB  VAL A 104     9363   6525   5313   -210    136   -463       C  
ATOM   5346  CG1 VAL A 104      45.070  45.789   5.275  1.00 56.65           C  
ANISOU 5346  CG1 VAL A 104     9610   6591   5324   -326     56   -500       C  
ATOM   5347  CG2 VAL A 104      43.800  43.675   4.885  1.00 55.88           C  
ANISOU 5347  CG2 VAL A 104     9227   6659   5345   -212    154   -441       C  
ATOM   5348  N   GLU A 105      42.705  47.866   6.660  1.00 63.18           N  
ANISOU 5348  N   GLU A 105    10728   7152   6126    -23    225   -604       N  
ATOM   5349  CA  GLU A 105      42.923  49.288   6.880  1.00 63.57           C  
ANISOU 5349  CA  GLU A 105    10978   7040   6136    -22    169   -656       C  
ATOM   5350  C   GLU A 105      44.259  49.497   7.580  1.00 60.98           C  
ANISOU 5350  C   GLU A 105    10778   6690   5700   -162     85   -688       C  
ATOM   5351  O   GLU A 105      44.608  48.759   8.507  1.00 60.05           O  
ANISOU 5351  O   GLU A 105    10655   6649   5511   -187    118   -710       O  
ATOM   5352  CB  GLU A 105      41.800  49.899   7.723  1.00 67.76           C  
ANISOU 5352  CB  GLU A 105    11609   7490   6644    155    265   -733       C  
ATOM   5353  CG  GLU A 105      42.062  51.347   8.116  1.00 72.23           C  
ANISOU 5353  CG  GLU A 105    12410   7873   7161    168    194   -808       C  
ATOM   5354  CD  GLU A 105      41.236  51.797   9.300  1.00 76.69           C  
ANISOU 5354  CD  GLU A 105    13092   8386   7660    334    290   -917       C  
ATOM   5355  OE1 GLU A 105      40.420  52.737   9.151  1.00 80.31           O  
ANISOU 5355  OE1 GLU A 105    13627   8725   8163    473    298   -965       O  
ATOM   5356  OE2 GLU A 105      41.390  51.213  10.401  1.00 81.37           O  
ANISOU 5356  OE2 GLU A 105    13700   9064   8154    331    354   -957       O  
ATOM   5357  N   ILE A 106      44.998  50.506   7.137  1.00 59.86           N  
ANISOU 5357  N   ILE A 106    10752   6445   5546   -261    -32   -681       N  
ATOM   5358  CA  ILE A 106      46.310  50.814   7.691  1.00 59.65           C  
ANISOU 5358  CA  ILE A 106    10848   6395   5421   -412   -130   -698       C  
ATOM   5359  C   ILE A 106      46.123  51.718   8.902  1.00 61.23           C  
ANISOU 5359  C   ILE A 106    11276   6451   5535   -345   -122   -795       C  
ATOM   5360  O   ILE A 106      45.400  52.720   8.837  1.00 60.24           O  
ANISOU 5360  O   ILE A 106    11268   6182   5439   -241   -123   -837       O  
ATOM   5361  CB  ILE A 106      47.216  51.477   6.637  1.00 59.55           C  
ANISOU 5361  CB  ILE A 106    10847   6352   5426   -570   -269   -633       C  
ATOM   5362  CG1 ILE A 106      47.842  50.441   5.689  1.00 58.57           C  
ANISOU 5362  CG1 ILE A 106    10502   6413   5339   -672   -290   -556       C  
ATOM   5363  CG2 ILE A 106      48.308  52.301   7.302  1.00 60.97           C  
ANISOU 5363  CG2 ILE A 106    11221   6442   5505   -702   -382   -660       C  
ATOM   5364  CD1 ILE A 106      46.860  49.603   4.879  1.00 58.13           C  
ANISOU 5364  CD1 ILE A 106    10251   6448   5387   -566   -203   -521       C  
ATOM   5365  N   LYS A 107      46.766  51.363  10.011  1.00 64.34           N  
ANISOU 5365  N   LYS A 107    11738   6885   5825   -399   -119   -837       N  
ATOM   5366  CA  LYS A 107      46.745  52.175  11.220  1.00 67.60           C  
ANISOU 5366  CA  LYS A 107    12376   7176   6134   -355   -120   -938       C  
ATOM   5367  C   LYS A 107      48.043  52.966  11.317  1.00 69.10           C  
ANISOU 5367  C   LYS A 107    12724   7274   6257   -531   -276   -934       C  
ATOM   5368  O   LYS A 107      49.133  52.388  11.294  1.00 71.20           O  
ANISOU 5368  O   LYS A 107    12924   7641   6487   -686   -337   -882       O  
ATOM   5369  CB  LYS A 107      46.555  51.315  12.469  1.00 68.82           C  
ANISOU 5369  CB  LYS A 107    12515   7434   6200   -305    -17   -984       C  
ATOM   5370  CG  LYS A 107      46.618  52.116  13.766  1.00 74.14           C  
ANISOU 5370  CG  LYS A 107    13424   8001   6746   -269    -20  -1096       C  
ATOM   5371  CD  LYS A 107      47.045  51.275  14.961  1.00 76.51           C  
ANISOU 5371  CD  LYS A 107    13725   8415   6930   -319     21  -1115       C  
ATOM   5372  CE  LYS A 107      46.531  49.853  14.846  1.00 80.02           C  
ANISOU 5372  CE  LYS A 107    13941   9040   7421   -283    124  -1048       C  
ATOM   5373  NZ  LYS A 107      45.050  49.796  14.979  1.00 84.90           N  
ANISOU 5373  NZ  LYS A 107    14504   9687   8067    -91    268  -1083       N  
ATOM   5374  N   ARG A 108      47.922  54.284  11.438  1.00 69.25           N  
ANISOU 5374  N   ARG A 108    12951   7101   6259   -505   -349   -988       N  
ATOM   5375  CA  ARG A 108      49.057  55.190  11.370  1.00 69.55           C  
ANISOU 5375  CA  ARG A 108    13149   7028   6248   -680   -518   -969       C  
ATOM   5376  C   ARG A 108      49.012  56.164  12.543  1.00 71.05           C  
ANISOU 5376  C   ARG A 108    13611   7044   6340   -629   -554  -1089       C  
ATOM   5377  O   ARG A 108      48.138  56.095  13.414  1.00 71.18           O  
ANISOU 5377  O   ARG A 108    13679   7048   6317   -455   -438  -1192       O  
ATOM   5378  CB  ARG A 108      49.061  55.949  10.040  1.00 69.11           C  
ANISOU 5378  CB  ARG A 108    13082   6887   6289   -739   -622   -890       C  
ATOM   5379  CG  ARG A 108      47.783  56.733   9.801  1.00 70.97           C  
ANISOU 5379  CG  ARG A 108    13395   6968   6602   -548   -588   -942       C  
ATOM   5380  CD  ARG A 108      48.052  58.000   9.018  1.00 72.53           C  
ANISOU 5380  CD  ARG A 108    13730   6982   6844   -635   -757   -896       C  
ATOM   5381  NE  ARG A 108      48.797  58.975   9.807  1.00 74.26           N  
ANISOU 5381  NE  ARG A 108    14210   7035   6969   -726   -891   -952       N  
ATOM   5382  CZ  ARG A 108      49.344  60.077   9.307  1.00 75.37           C  
ANISOU 5382  CZ  ARG A 108    14502   7013   7122   -860  -1076   -900       C  
ATOM   5383  NH1 ARG A 108      49.236  60.345   8.012  1.00 75.56           N  
ANISOU 5383  NH1 ARG A 108    14438   7031   7242   -922  -1144   -789       N  
ATOM   5384  NH2 ARG A 108      50.003  60.909  10.100  1.00 76.50           N  
ANISOU 5384  NH2 ARG A 108    14888   7002   7175   -943  -1202   -955       N  
ATOM   5385  N   THR A 109      49.980  57.078  12.556  1.00 73.16           N  
ANISOU 5385  N   THR A 109    14051   7186   6560   -787   -721  -1076       N  
ATOM   5386  CA  THR A 109      50.030  58.112  13.578  1.00 75.81           C  
ANISOU 5386  CA  THR A 109    14669   7331   6804   -754   -788  -1191       C  
ATOM   5387  C   THR A 109      48.787  58.990  13.512  1.00 77.13           C  
ANISOU 5387  C   THR A 109    14952   7323   7032   -538   -758  -1284       C  
ATOM   5388  O   THR A 109      48.177  59.166  12.453  1.00 78.28           O  
ANISOU 5388  O   THR A 109    15005   7441   7299   -480   -757  -1228       O  
ATOM   5389  CB  THR A 109      51.283  58.971  13.406  1.00 77.80           C  
ANISOU 5389  CB  THR A 109    15077   7471   7014   -983   -997  -1136       C  
ATOM   5390  OG1 THR A 109      51.503  59.228  12.012  1.00 76.97           O  
ANISOU 5390  OG1 THR A 109    14871   7365   7010  -1090  -1087  -1009       O  
ATOM   5391  CG2 THR A 109      52.499  58.267  13.982  1.00 79.36           C  
ANISOU 5391  CG2 THR A 109    15229   7815   7111  -1164  -1026  -1096       C  
ATOM   5392  N   VAL A 110      48.415  59.543  14.668  1.00 78.82           N  
ANISOU 5392  N   VAL A 110    15369   7423   7156   -413   -736  -1433       N  
ATOM   5393  CA  VAL A 110      47.286  60.460  14.726  1.00 80.32           C  
ANISOU 5393  CA  VAL A 110    15689   7437   7393   -191   -719  -1546       C  
ATOM   5394  C   VAL A 110      47.575  61.681  13.863  1.00 79.92           C  
ANISOU 5394  C   VAL A 110    15787   7156   7422   -271   -920  -1500       C  
ATOM   5395  O   VAL A 110      48.715  62.158  13.785  1.00 77.82           O  
ANISOU 5395  O   VAL A 110    15642   6813   7115   -489  -1092  -1440       O  
ATOM   5396  CB  VAL A 110      47.000  60.854  16.185  1.00 81.95           C  
ANISOU 5396  CB  VAL A 110    16100   7574   7465    -57   -673  -1727       C  
ATOM   5397  CG1 VAL A 110      45.783  61.759  16.271  1.00 84.04           C  
ANISOU 5397  CG1 VAL A 110    16482   7672   7776    203   -645  -1864       C  
ATOM   5398  CG2 VAL A 110      46.801  59.610  17.040  1.00 81.31           C  
ANISOU 5398  CG2 VAL A 110    15866   7736   7292    -15   -487  -1749       C  
ATOM   5399  N   ALA A 111      46.540  62.182  13.192  1.00 80.66           N  
ANISOU 5399  N   ALA A 111    15868   7146   7634   -104   -908  -1516       N  
ATOM   5400  CA  ALA A 111      46.662  63.356  12.339  1.00 83.06           C  
ANISOU 5400  CA  ALA A 111    16313   7219   8026   -163  -1105  -1467       C  
ATOM   5401  C   ALA A 111      45.467  64.264  12.572  1.00 85.24           C  
ANISOU 5401  C   ALA A 111    16737   7293   8357    108  -1099  -1611       C  
ATOM   5402  O   ALA A 111      44.321  63.808  12.529  1.00 85.15           O  
ANISOU 5402  O   ALA A 111    16578   7377   8399    326   -931  -1659       O  
ATOM   5403  CB  ALA A 111      46.752  62.963  10.860  1.00 82.09           C  
ANISOU 5403  CB  ALA A 111    15972   7197   8023   -282  -1129  -1284       C  
ATOM   5404  N   ALA A 112      45.735  65.543  12.818  1.00 87.51           N  
ANISOU 5404  N   ALA A 112    17313   7305   8633     96  -1291  -1681       N  
ATOM   5405  CA  ALA A 112      44.651  66.480  13.071  1.00 89.90           C  
ANISOU 5405  CA  ALA A 112    17776   7394   8989    367  -1308  -1836       C  
ATOM   5406  C   ALA A 112      43.999  66.905  11.756  1.00 89.11           C  
ANISOU 5406  C   ALA A 112    17600   7196   9064    417  -1379  -1737       C  
ATOM   5407  O   ALA A 112      44.698  67.185  10.778  1.00 86.11           O  
ANISOU 5407  O   ALA A 112    17216   6760   8742    192  -1541  -1572       O  
ATOM   5408  CB  ALA A 112      45.163  67.709  13.818  1.00 92.03           C  
ANISOU 5408  CB  ALA A 112    18307   7447   9213    342  -1490  -1911       C  
ATOM   5409  N   PRO A 113      42.670  66.952  11.703  1.00 90.72           N  
ANISOU 5409  N   PRO A 113    17734   7389   9347    702  -1261  -1829       N  
ATOM   5410  CA  PRO A 113      41.999  67.394  10.477  1.00 91.62           C  
ANISOU 5410  CA  PRO A 113    17782   7399   9630    761  -1336  -1737       C  
ATOM   5411  C   PRO A 113      42.124  68.894  10.275  1.00 94.76           C  
ANISOU 5411  C   PRO A 113    18478   7438  10089    761  -1602  -1773       C  
ATOM   5412  O   PRO A 113      42.226  69.670  11.228  1.00 95.83           O  
ANISOU 5412  O   PRO A 113    18821   7427  10163    843  -1674  -1913       O  
ATOM   5413  CB  PRO A 113      40.537  66.995  10.708  1.00 91.49           C  
ANISOU 5413  CB  PRO A 113    17613   7488   9662   1084  -1124  -1849       C  
ATOM   5414  CG  PRO A 113      40.388  66.971  12.194  1.00 92.01           C  
ANISOU 5414  CG  PRO A 113    17796   7582   9583   1238  -1014  -2055       C  
ATOM   5415  CD  PRO A 113      41.715  66.513  12.735  1.00 90.79           C  
ANISOU 5415  CD  PRO A 113    17690   7519   9289    974  -1043  -2005       C  
ATOM   5416  N   SER A 114      42.115  69.298   9.008  1.00 94.70           N  
ANISOU 5416  N   SER A 114    18434   7335  10212    658  -1745  -1614       N  
ATOM   5417  CA  SER A 114      41.971  70.703   8.654  1.00 97.03           C  
ANISOU 5417  CA  SER A 114    18985   7280  10601    693  -2000  -1632       C  
ATOM   5418  C   SER A 114      40.497  70.978   8.386  1.00 99.41           C  
ANISOU 5418  C   SER A 114    19230   7507  11036   1021  -1931  -1722       C  
ATOM   5419  O   SER A 114      39.894  70.349   7.508  1.00 98.14           O  
ANISOU 5419  O   SER A 114    18815   7507  10967   1052  -1822  -1610       O  
ATOM   5420  CB  SER A 114      42.826  71.057   7.438  1.00 96.39           C  
ANISOU 5420  CB  SER A 114    18911   7134  10580    376  -2217  -1397       C  
ATOM   5421  OG  SER A 114      44.104  70.450   7.517  1.00 93.63           O  
ANISOU 5421  OG  SER A 114    18500   6963  10111     76  -2216  -1287       O  
ATOM   5422  N   VAL A 115      39.915  71.896   9.152  1.00102.74           N  
ANISOU 5422  N   VAL A 115    19760   7802  11475   1250  -1966  -1878       N  
ATOM   5423  CA  VAL A 115      38.487  72.180   9.071  1.00103.79           C  
ANISOU 5423  CA  VAL A 115    19820   7892  11722   1587  -1887  -1988       C  
ATOM   5424  C   VAL A 115      38.253  73.339   8.114  1.00104.10           C  
ANISOU 5424  C   VAL A 115    19950   7678  11924   1579  -2136  -1895       C  
ATOM   5425  O   VAL A 115      38.969  74.348   8.144  1.00105.71           O  
ANISOU 5425  O   VAL A 115    20337   7701  12128   1431  -2369  -1851       O  
ATOM   5426  CB  VAL A 115      37.910  72.487  10.465  1.00107.03           C  
ANISOU 5426  CB  VAL A 115    20269   8341  12057   1856  -1769  -2222       C  
ATOM   5427  CG1 VAL A 115      36.386  72.464  10.421  1.00107.64           C  
ANISOU 5427  CG1 VAL A 115    20207   8461  12231   2208  -1624  -2337       C  
ATOM   5428  CG2 VAL A 115      38.435  71.495  11.492  1.00106.93           C  
ANISOU 5428  CG2 VAL A 115    20205   8563  11861   1790  -1576  -2286       C  
ATOM   5429  N   PHE A 116      37.244  73.190   7.257  1.00103.76           N  
ANISOU 5429  N   PHE A 116    19776   7629  12019   1733  -2092  -1855       N  
ATOM   5430  CA  PHE A 116      36.807  74.249   6.359  1.00106.93           C  
ANISOU 5430  CA  PHE A 116    20236   7806  12587   1768  -2310  -1776       C  
ATOM   5431  C   PHE A 116      35.288  74.255   6.310  1.00107.36           C  
ANISOU 5431  C   PHE A 116    20156   7882  12756   2130  -2180  -1890       C  
ATOM   5432  O   PHE A 116      34.659  73.196   6.362  1.00106.02           O  
ANISOU 5432  O   PHE A 116    19798   7916  12567   2264  -1939  -1926       O  
ATOM   5433  CB  PHE A 116      37.369  74.062   4.941  1.00107.09           C  
ANISOU 5433  CB  PHE A 116    20217   7795  12676   1476  -2450  -1520       C  
ATOM   5434  CG  PHE A 116      38.804  74.484   4.790  1.00109.49           C  
ANISOU 5434  CG  PHE A 116    20667   8030  12903   1114  -2658  -1382       C  
ATOM   5435  CD1 PHE A 116      39.135  75.822   4.625  1.00113.42           C  
ANISOU 5435  CD1 PHE A 116    21343   8301  13450   1031  -2933  -1334       C  
ATOM   5436  CD2 PHE A 116      39.819  73.541   4.793  1.00107.55           C  
ANISOU 5436  CD2 PHE A 116    20374   7956  12535    853  -2583  -1294       C  
ATOM   5437  CE1 PHE A 116      40.456  76.213   4.477  1.00113.19           C  
ANISOU 5437  CE1 PHE A 116    21434   8229  13342    691  -3126  -1195       C  
ATOM   5438  CE2 PHE A 116      41.142  73.924   4.645  1.00108.01           C  
ANISOU 5438  CE2 PHE A 116    20544   7978  12518    517  -2771  -1160       C  
ATOM   5439  CZ  PHE A 116      41.460  75.263   4.487  1.00111.47           C  
ANISOU 5439  CZ  PHE A 116    21152   8201  13001    434  -3041  -1105       C  
ATOM   5440  N   ILE A 117      34.702  75.446   6.209  1.00110.53           N  
ANISOU 5440  N   ILE A 117    20646   8078  13273   2286  -2343  -1943       N  
ATOM   5441  CA  ILE A 117      33.257  75.599   6.098  1.00112.00           C  
ANISOU 5441  CA  ILE A 117    20702   8270  13583   2627  -2251  -2044       C  
ATOM   5442  C   ILE A 117      32.960  76.484   4.894  1.00112.16           C  
ANISOU 5442  C   ILE A 117    20758   8074  13784   2589  -2494  -1900       C  
ATOM   5443  O   ILE A 117      33.610  77.516   4.696  1.00114.47           O  
ANISOU 5443  O   ILE A 117    21240   8155  14100   2429  -2755  -1837       O  
ATOM   5444  CB  ILE A 117      32.633  76.180   7.386  1.00117.11           C  
ANISOU 5444  CB  ILE A 117    21403   8909  14185   2923  -2176  -2301       C  
ATOM   5445  CG1 ILE A 117      31.105  76.194   7.293  1.00119.44           C  
ANISOU 5445  CG1 ILE A 117    21522   9263  14596   3278  -2047  -2406       C  
ATOM   5446  CG2 ILE A 117      33.163  77.578   7.684  1.00120.69           C  
ANISOU 5446  CG2 ILE A 117    22108   9097  14652   2865  -2447  -2341       C  
ATOM   5447  CD1 ILE A 117      30.421  76.538   8.603  1.00122.05           C  
ANISOU 5447  CD1 ILE A 117    21855   9657  14861   3576  -1918  -2666       C  
ATOM   5448  N   PHE A 118      32.005  76.063   4.070  1.00109.58           N  
ANISOU 5448  N   PHE A 118    20244   7810  13580   2720  -2414  -1836       N  
ATOM   5449  CA  PHE A 118      31.560  76.839   2.925  1.00108.43           C  
ANISOU 5449  CA  PHE A 118    20102   7483  13613   2712  -2624  -1702       C  
ATOM   5450  C   PHE A 118      30.069  77.139   3.053  1.00108.97           C  
ANISOU 5450  C   PHE A 118    20048   7552  13804   3095  -2537  -1842       C  
ATOM   5451  O   PHE A 118      29.274  76.221   3.326  1.00107.30           O  
ANISOU 5451  O   PHE A 118    19636   7558  13577   3297  -2277  -1920       O  
ATOM   5452  CB  PHE A 118      31.833  76.098   1.579  1.00104.69           C  
ANISOU 5452  CB  PHE A 118    19507   7078  13192   2473  -2646  -1447       C  
ATOM   5453  CG  PHE A 118      33.171  75.403   1.505  1.00101.86           C  
ANISOU 5453  CG  PHE A 118    19194   6814  12695   2127  -2641  -1324       C  
ATOM   5454  CD1 PHE A 118      34.231  75.987   0.838  1.00102.13           C  
ANISOU 5454  CD1 PHE A 118    19361   6722  12722   1789  -2892  -1140       C  
ATOM   5455  CD2 PHE A 118      33.354  74.147   2.057  1.00 99.54           C  
ANISOU 5455  CD2 PHE A 118    18795   6750  12276   2132  -2387  -1381       C  
ATOM   5456  CE1 PHE A 118      35.448  75.346   0.748  1.00100.02           C  
ANISOU 5456  CE1 PHE A 118    19114   6562  12327   1469  -2884  -1025       C  
ATOM   5457  CE2 PHE A 118      34.571  73.505   1.968  1.00 97.48           C  
ANISOU 5457  CE2 PHE A 118    18535   6613  11891   1806  -2376  -1262       C  
ATOM   5458  CZ  PHE A 118      35.618  74.104   1.313  1.00 97.00           C  
ANISOU 5458  CZ  PHE A 118    18631   6396  11829   1486  -2633  -1094       C  
ATOM   5459  N   PRO A 119      29.674  78.399   2.880  1.00111.02           N  
ANISOU 5459  N   PRO A 119    20420   7583  14181   3197  -2749  -1874       N  
ATOM   5460  CA  PRO A 119      28.264  78.759   2.922  1.00113.53           C  
ANISOU 5460  CA  PRO A 119    20617   7892  14626   3552  -2688  -1998       C  
ATOM   5461  C   PRO A 119      27.584  78.436   1.604  1.00111.80           C  
ANISOU 5461  C   PRO A 119    20220   7696  14562   3550  -2706  -1816       C  
ATOM   5462  O   PRO A 119      28.262  78.202   0.598  1.00109.01           O  
ANISOU 5462  O   PRO A 119    19878   7312  14228   3257  -2824  -1589       O  
ATOM   5463  CB  PRO A 119      28.296  80.283   3.176  1.00117.56           C  
ANISOU 5463  CB  PRO A 119    21348   8120  15198   3613  -2950  -2082       C  
ATOM   5464  CG  PRO A 119      29.764  80.694   3.103  1.00117.04           C  
ANISOU 5464  CG  PRO A 119    21510   7917  15044   3253  -3165  -1963       C  
ATOM   5465  CD  PRO A 119      30.519  79.549   2.503  1.00112.31           C  
ANISOU 5465  CD  PRO A 119    20814   7487  14372   2968  -3073  -1772       C  
ATOM   5466  N   PRO A 120      26.252  78.402   1.577  1.00112.76           N  
ANISOU 5466  N   PRO A 120    20167   7887  14791   3866  -2589  -1905       N  
ATOM   5467  CA  PRO A 120      25.552  78.124   0.318  1.00111.77           C  
ANISOU 5467  CA  PRO A 120    19865   7784  14819   3872  -2613  -1728       C  
ATOM   5468  C   PRO A 120      25.815  79.207  -0.716  1.00114.27           C  
ANISOU 5468  C   PRO A 120    20321   7831  15267   3701  -2943  -1562       C  
ATOM   5469  O   PRO A 120      25.982  80.385  -0.391  1.00117.11           O  
ANISOU 5469  O   PRO A 120    20875   7972  15651   3728  -3142  -1641       O  
ATOM   5470  CB  PRO A 120      24.077  78.094   0.733  1.00113.14           C  
ANISOU 5470  CB  PRO A 120    19847   8070  15070   4271  -2438  -1895       C  
ATOM   5471  CG  PRO A 120      24.026  78.796   2.052  1.00116.13           C  
ANISOU 5471  CG  PRO A 120    20358   8397  15370   4460  -2418  -2151       C  
ATOM   5472  CD  PRO A 120      25.326  78.499   2.718  1.00114.98           C  
ANISOU 5472  CD  PRO A 120    20375   8271  15042   4223  -2405  -2165       C  
ATOM   5473  N   SER A 121      25.844  78.792  -1.979  1.00113.45           N  
ANISOU 5473  N   SER A 121    20112   7752  15240   3518  -3003  -1324       N  
ATOM   5474  CA  SER A 121      26.104  79.695  -3.091  1.00115.21           C  
ANISOU 5474  CA  SER A 121    20438   7762  15577   3316  -3308  -1131       C  
ATOM   5475  C   SER A 121      24.815  80.371  -3.543  1.00117.63           C  
ANISOU 5475  C   SER A 121    20656   7970  16070   3579  -3380  -1156       C  
ATOM   5476  O   SER A 121      23.748  79.748  -3.556  1.00116.51           O  
ANISOU 5476  O   SER A 121    20291   7989  15989   3825  -3182  -1208       O  
ATOM   5477  CB  SER A 121      26.738  78.939  -4.260  1.00112.67           C  
ANISOU 5477  CB  SER A 121    20035   7534  15241   2983  -3340   -857       C  
ATOM   5478  OG  SER A 121      25.787  78.121  -4.921  1.00112.37           O  
ANISOU 5478  OG  SER A 121    19748   7656  15292   3111  -3191   -782       O  
ATOM   5479  N   ASP A 122      24.926  81.657  -3.906  1.00120.95           N  
ANISOU 5479  N   ASP A 122    21249   8130  16577   3522  -3671  -1116       N  
ATOM   5480  CA  ASP A 122      23.785  82.446  -4.378  1.00123.69           C  
ANISOU 5480  CA  ASP A 122    21542   8347  17105   3749  -3785  -1132       C  
ATOM   5481  C   ASP A 122      22.910  81.665  -5.352  1.00122.64           C  
ANISOU 5481  C   ASP A 122    21145   8372  17081   3804  -3671   -988       C  
ATOM   5482  O   ASP A 122      21.679  81.580  -5.192  1.00122.10           O  
ANISOU 5482  O   ASP A 122    20909   8375  17110   4127  -3542  -1097       O  
ATOM   5483  CB  ASP A 122      24.294  83.732  -5.041  1.00125.80           C  
ANISOU 5483  CB  ASP A 122    22025   8331  17442   3546  -4150  -1006       C  
ATOM   5484  CG  ASP A 122      24.545  84.848  -4.044  1.00128.81           C  
ANISOU 5484  CG  ASP A 122    22648   8505  17791   3657  -4290  -1206       C  
ATOM   5485  OD1 ASP A 122      23.568  85.514  -3.644  1.00130.74           O  
ANISOU 5485  OD1 ASP A 122    22889   8651  18134   3980  -4306  -1376       O  
ATOM   5486  OD2 ASP A 122      25.717  85.068  -3.671  1.00127.91           O  
ANISOU 5486  OD2 ASP A 122    22723   8327  17550   3421  -4391  -1189       O  
ATOM   5487  N   GLU A 123      23.557  81.083  -6.366  1.00123.09           N  
ANISOU 5487  N   GLU A 123    21155   8498  17115   3481  -3721   -739       N  
ATOM   5488  CA  GLU A 123      22.888  80.265  -7.371  1.00125.07           C  
ANISOU 5488  CA  GLU A 123    21163   8908  17450   3478  -3628   -572       C  
ATOM   5489  C   GLU A 123      21.912  79.278  -6.745  1.00126.12           C  
ANISOU 5489  C   GLU A 123    21064   9276  17578   3794  -3308   -722       C  
ATOM   5490  O   GLU A 123      20.765  79.156  -7.183  1.00129.71           O  
ANISOU 5490  O   GLU A 123    21328   9794  18162   4000  -3250   -704       O  
ATOM   5491  CB  GLU A 123      23.931  79.504  -8.191  1.00122.95           C  
ANISOU 5491  CB  GLU A 123    20881   8746  17090   3085  -3652   -333       C  
ATOM   5492  CG  GLU A 123      25.190  80.280  -8.524  1.00124.90           C  
ANISOU 5492  CG  GLU A 123    21357   8828  17271   2730  -3918   -207       C  
ATOM   5493  CD  GLU A 123      25.740  79.912  -9.886  1.00125.01           C  
ANISOU 5493  CD  GLU A 123    21303   8916  17278   2369  -4027     91       C  
ATOM   5494  OE1 GLU A 123      24.967  79.373 -10.719  1.00123.06           O  
ANISOU 5494  OE1 GLU A 123    20854   8781  17123   2420  -3963    208       O  
ATOM   5495  OE2 GLU A 123      26.954  80.133 -10.144  1.00125.48           O  
ANISOU 5495  OE2 GLU A 123    21498   8945  17234   2025  -4173    216       O  
ATOM   5496  N   GLN A 124      22.354  78.568  -5.705  1.00125.61           N  
ANISOU 5496  N   GLN A 124    21009   9357  17361   3831  -3098   -867       N  
ATOM   5497  CA  GLN A 124      21.484  77.577  -5.080  1.00125.03           C  
ANISOU 5497  CA  GLN A 124    20708   9537  17260   4108  -2787  -1001       C  
ATOM   5498  C   GLN A 124      20.416  78.243  -4.225  1.00129.56           C  
ANISOU 5498  C   GLN A 124    21247  10083  17896   4490  -2723  -1240       C  
ATOM   5499  O   GLN A 124      19.264  77.788  -4.195  1.00131.13           O  
ANISOU 5499  O   GLN A 124    21211  10451  18161   4747  -2549  -1292       O  
ATOM   5500  CB  GLN A 124      22.296  76.597  -4.235  1.00121.41           C  
ANISOU 5500  CB  GLN A 124    20269   9253  16607   4017  -2584  -1077       C  
ATOM   5501  CG  GLN A 124      21.416  75.588  -3.515  1.00118.30           C  
ANISOU 5501  CG  GLN A 124    19642   9141  16167   4296  -2262  -1219       C  
ATOM   5502  CD  GLN A 124      22.116  74.883  -2.369  1.00114.89           C  
ANISOU 5502  CD  GLN A 124    19261   8858  15534   4269  -2066  -1358       C  
ATOM   5503  OE1 GLN A 124      21.659  73.841  -1.901  1.00112.81           O  
ANISOU 5503  OE1 GLN A 124    18810   8856  15198   4405  -1802  -1423       O  
ATOM   5504  NE2 GLN A 124      23.232  75.451  -1.914  1.00115.47           N  
ANISOU 5504  NE2 GLN A 124    19587   8774  15514   4082  -2199  -1397       N  
ATOM   5505  N   LEU A 125      20.777  79.324  -3.525  1.00133.69           N  
ANISOU 5505  N   LEU A 125    21998  10405  18395   4528  -2865  -1386       N  
ATOM   5506  CA  LEU A 125      19.824  79.956  -2.624  1.00138.49           C  
ANISOU 5506  CA  LEU A 125    22583  10994  19043   4890  -2800  -1631       C  
ATOM   5507  C   LEU A 125      18.611  80.496  -3.363  1.00141.60           C  
ANISOU 5507  C   LEU A 125    22845  11320  19636   5089  -2886  -1588       C  
ATOM   5508  O   LEU A 125      17.516  80.525  -2.794  1.00145.55           O  
ANISOU 5508  O   LEU A 125    23195  11930  20178   5420  -2734  -1757       O  
ATOM   5509  CB  LEU A 125      20.494  81.070  -1.825  1.00142.17           C  
ANISOU 5509  CB  LEU A 125    23336  11233  19451   4873  -2970  -1780       C  
ATOM   5510  CG  LEU A 125      21.632  80.648  -0.899  1.00141.04           C  
ANISOU 5510  CG  LEU A 125    23330  11154  19104   4714  -2882  -1859       C  
ATOM   5511  CD1 LEU A 125      22.829  81.566  -1.052  1.00142.31           C  
ANISOU 5511  CD1 LEU A 125    23787  11050  19234   4434  -3173  -1784       C  
ATOM   5512  CD2 LEU A 125      21.151  80.623   0.538  1.00142.70           C  
ANISOU 5512  CD2 LEU A 125    23512  11490  19218   5010  -2675  -2147       C  
ATOM   5513  N   LYS A 126      18.762  80.917  -4.623  1.00141.08           N  
ANISOU 5513  N   LYS A 126    22822  11093  19690   4891  -3122  -1361       N  
ATOM   5514  CA  LYS A 126      17.547  81.350  -5.310  1.00143.50           C  
ANISOU 5514  CA  LYS A 126    22984  11356  20184   5090  -3187  -1319       C  
ATOM   5515  C   LYS A 126      16.624  80.182  -5.656  1.00141.25           C  
ANISOU 5515  C   LYS A 126    22372  11359  19936   5218  -2941  -1256       C  
ATOM   5516  O   LYS A 126      15.448  80.413  -5.954  1.00142.59           O  
ANISOU 5516  O   LYS A 126    22378  11553  20245   5453  -2926  -1271       O  
ATOM   5517  CB  LYS A 126      17.868  82.158  -6.572  1.00144.19           C  
ANISOU 5517  CB  LYS A 126    23195  11200  20389   4852  -3512  -1092       C  
ATOM   5518  CG  LYS A 126      18.755  81.487  -7.597  1.00139.85           C  
ANISOU 5518  CG  LYS A 126    22639  10704  19794   4465  -3573   -820       C  
ATOM   5519  CD  LYS A 126      18.704  82.253  -8.916  1.00141.00           C  
ANISOU 5519  CD  LYS A 126    22836  10663  20076   4287  -3864   -596       C  
ATOM   5520  CE  LYS A 126      18.978  83.740  -8.717  1.00144.13           C  
ANISOU 5520  CE  LYS A 126    23495  10750  20517   4286  -4149   -668       C  
ATOM   5521  NZ  LYS A 126      20.431  84.047  -8.615  1.00143.37           N  
ANISOU 5521  NZ  LYS A 126    23642  10542  20290   3951  -4307   -604       N  
ATOM   5522  N   SER A 127      17.112  78.942  -5.599  1.00139.04           N  
ANISOU 5522  N   SER A 127    21994  11302  19534   5077  -2750  -1190       N  
ATOM   5523  CA  SER A 127      16.296  77.773  -5.907  1.00139.14           C  
ANISOU 5523  CA  SER A 127    21700  11600  19568   5182  -2521  -1124       C  
ATOM   5524  C   SER A 127      15.549  77.227  -4.693  1.00141.74           C  
ANISOU 5524  C   SER A 127    21859  12178  19817   5493  -2221  -1358       C  
ATOM   5525  O   SER A 127      14.968  76.140  -4.777  1.00142.38           O  
ANISOU 5525  O   SER A 127    21685  12534  19881   5568  -2003  -1316       O  
ATOM   5526  CB  SER A 127      17.159  76.668  -6.524  1.00134.23           C  
ANISOU 5526  CB  SER A 127    21046  11100  18855   4873  -2474   -925       C  
ATOM   5527  OG  SER A 127      18.341  76.455  -5.775  1.00132.18           O  
ANISOU 5527  OG  SER A 127    20969  10832  18421   4708  -2437   -999       O  
ATOM   5528  N   GLY A 128      15.554  77.946  -3.570  1.00143.23           N  
ANISOU 5528  N   GLY A 128    22179  12292  19949   5664  -2207  -1596       N  
ATOM   5529  CA  GLY A 128      14.747  77.589  -2.421  1.00143.08           C  
ANISOU 5529  CA  GLY A 128    21994  12512  19857   5967  -1940  -1822       C  
ATOM   5530  C   GLY A 128      15.398  76.659  -1.421  1.00140.60           C  
ANISOU 5530  C   GLY A 128    21680  12412  19328   5907  -1710  -1923       C  
ATOM   5531  O   GLY A 128      14.820  76.428  -0.351  1.00141.93           O  
ANISOU 5531  O   GLY A 128    21732  12784  19409   6138  -1493  -2122       O  
ATOM   5532  N   THR A 129      16.570  76.112  -1.728  1.00135.68           N  
ANISOU 5532  N   THR A 129    21178  11761  18612   5600  -1751  -1789       N  
ATOM   5533  CA  THR A 129      17.291  75.240  -0.816  1.00132.11           C  
ANISOU 5533  CA  THR A 129    20749  11493  17955   5518  -1552  -1872       C  
ATOM   5534  C   THR A 129      18.654  75.848  -0.510  1.00130.43           C  
ANISOU 5534  C   THR A 129    20859  11047  17652   5283  -1731  -1892       C  
ATOM   5535  O   THR A 129      19.245  76.542  -1.342  1.00131.06           O  
ANISOU 5535  O   THR A 129    21111  10871  17815   5079  -1997  -1751       O  
ATOM   5536  CB  THR A 129      17.456  73.826  -1.404  1.00128.38           C  
ANISOU 5536  CB  THR A 129    20098  11247  17433   5366  -1402  -1693       C  
ATOM   5537  OG1 THR A 129      16.180  73.340  -1.840  1.00128.47           O  
ANISOU 5537  OG1 THR A 129    19808  11456  17547   5563  -1274  -1643       O  
ATOM   5538  CG2 THR A 129      18.019  72.862  -0.366  1.00126.25           C  
ANISOU 5538  CG2 THR A 129    19817  11204  16949   5326  -1165  -1796       C  
ATOM   5539  N   ALA A 130      19.133  75.601   0.705  1.00128.78           N  
ANISOU 5539  N   ALA A 130    20724  10941  17266   5305  -1586  -2064       N  
ATOM   5540  CA  ALA A 130      20.443  76.049   1.153  1.00127.87           C  
ANISOU 5540  CA  ALA A 130    20896  10649  17039   5084  -1722  -2096       C  
ATOM   5541  C   ALA A 130      21.164  74.874   1.794  1.00123.86           C  
ANISOU 5541  C   ALA A 130    20361  10366  16335   4953  -1509  -2111       C  
ATOM   5542  O   ALA A 130      20.623  74.229   2.699  1.00123.90           O  
ANISOU 5542  O   ALA A 130    20210  10630  16238   5138  -1251  -2254       O  
ATOM   5543  CB  ALA A 130      20.329  77.207   2.151  1.00131.50           C  
ANISOU 5543  CB  ALA A 130    21523  10963  17480   5261  -1800  -2324       C  
ATOM   5544  N   SER A 131      22.378  74.594   1.323  1.00120.87           N  
ANISOU 5544  N   SER A 131    20125   9899  15899   4628  -1618  -1959       N  
ATOM   5545  CA  SER A 131      23.209  73.531   1.879  1.00116.74           C  
ANISOU 5545  CA  SER A 131    19609   9557  15192   4471  -1447  -1962       C  
ATOM   5546  C   SER A 131      24.522  74.132   2.367  1.00116.24           C  
ANISOU 5546  C   SER A 131    19833   9310  15024   4246  -1607  -1995       C  
ATOM   5547  O   SER A 131      25.358  74.544   1.555  1.00113.68           O  
ANISOU 5547  O   SER A 131    19659   8789  14746   3980  -1836  -1831       O  
ATOM   5548  CB  SER A 131      23.459  72.434   0.843  1.00113.82           C  
ANISOU 5548  CB  SER A 131    19111   9297  14837   4279  -1401  -1737       C  
ATOM   5549  OG  SER A 131      23.656  72.982  -0.455  1.00115.38           O  
ANISOU 5549  OG  SER A 131    19373   9284  15182   4109  -1654  -1536       O  
ATOM   5550  N   VAL A 132      24.699  74.199   3.697  1.00116.96           N  
ANISOU 5550  N   VAL A 132    19992   9476  14970   4343  -1490  -2200       N  
ATOM   5551  CA  VAL A 132      25.993  74.548   4.275  1.00116.33           C  
ANISOU 5551  CA  VAL A 132    20161   9276  14763   4119  -1601  -2230       C  
ATOM   5552  C   VAL A 132      26.856  73.299   4.239  1.00112.21           C  
ANISOU 5552  C   VAL A 132    19601   8926  14106   3883  -1469  -2127       C  
ATOM   5553  O   VAL A 132      26.326  72.174   4.309  1.00110.15           O  
ANISOU 5553  O   VAL A 132    19126   8923  13802   3977  -1228  -2124       O  
ATOM   5554  CB  VAL A 132      25.829  75.093   5.708  1.00118.93           C  
ANISOU 5554  CB  VAL A 132    20574   9626  14988   4312  -1531  -2485       C  
ATOM   5555  CG1 VAL A 132      25.370  74.031   6.643  1.00118.23           C  
ANISOU 5555  CG1 VAL A 132    20299   9866  14758   4461  -1211  -2608       C  
ATOM   5556  CG2 VAL A 132      27.135  75.649   6.238  1.00119.51           C  
ANISOU 5556  CG2 VAL A 132    20919   9537  14952   4085  -1691  -2507       C  
ATOM   5557  N   VAL A 133      28.172  73.467   4.058  1.00110.90           N  
ANISOU 5557  N   VAL A 133    19631   8629  13878   3569  -1632  -2026       N  
ATOM   5558  CA  VAL A 133      29.042  72.299   3.969  1.00108.89           C  
ANISOU 5558  CA  VAL A 133    19338   8536  13500   3327  -1519  -1921       C  
ATOM   5559  C   VAL A 133      30.236  72.489   4.888  1.00109.40           C  
ANISOU 5559  C   VAL A 133    19608   8555  13402   3148  -1566  -1995       C  
ATOM   5560  O   VAL A 133      30.799  73.584   4.972  1.00108.43           O  
ANISOU 5560  O   VAL A 133    19688   8212  13297   3050  -1791  -2001       O  
ATOM   5561  CB  VAL A 133      29.490  72.019   2.516  1.00107.16           C  
ANISOU 5561  CB  VAL A 133    19009   8337  13368   3020  -1635  -1634       C  
ATOM   5562  CG1 VAL A 133      30.040  73.273   1.911  1.00107.51           C  
ANISOU 5562  CG1 VAL A 133    19332   8013  13505   2896  -1974  -1564       C  
ATOM   5563  CG2 VAL A 133      30.522  70.892   2.462  1.00103.59           C  
ANISOU 5563  CG2 VAL A 133    18429   8151  12779   2695  -1514  -1500       C  
ATOM   5564  N   CYS A 134      30.607  71.417   5.582  1.00109.40           N  
ANISOU 5564  N   CYS A 134    19503   8820  13245   3078  -1346  -2026       N  
ATOM   5565  CA  CYS A 134      31.766  71.350   6.455  1.00109.82           C  
ANISOU 5565  CA  CYS A 134    19727   8869  13129   2898  -1359  -2084       C  
ATOM   5566  C   CYS A 134      32.668  70.228   5.980  1.00102.66           C  
ANISOU 5566  C   CYS A 134    18645   8211  12152   2558  -1279  -1879       C  
ATOM   5567  O   CYS A 134      32.185  69.207   5.484  1.00101.32           O  
ANISOU 5567  O   CYS A 134    18185   8304  12009   2547  -1104  -1772       O  
ATOM   5568  CB  CYS A 134      31.341  71.071   7.870  1.00113.07           C  
ANISOU 5568  CB  CYS A 134    20113   9444  13405   3120  -1148  -2308       C  
ATOM   5569  SG  CYS A 134      32.491  71.436   9.143  1.00116.30           S  
ANISOU 5569  SG  CYS A 134    20732   9822  13633   2971  -1198  -2418       S  
ATOM   5570  N   LEU A 135      33.972  70.410   6.152  1.00 98.91           N  
ANISOU 5570  N   LEU A 135    18344   7653  11584   2286  -1409  -1830       N  
ATOM   5571  CA  LEU A 135      34.953  69.479   5.623  1.00 94.52           C  
ANISOU 5571  CA  LEU A 135    17642   7304  10966   1953  -1373  -1636       C  
ATOM   5572  C   LEU A 135      36.098  69.329   6.612  1.00 94.75           C  
ANISOU 5572  C   LEU A 135    17816   7361  10824   1789  -1372  -1699       C  
ATOM   5573  O   LEU A 135      36.713  70.322   7.014  1.00 96.19           O  
ANISOU 5573  O   LEU A 135    18286   7287  10973   1738  -1568  -1768       O  
ATOM   5574  CB  LEU A 135      35.479  69.964   4.267  1.00 93.70           C  
ANISOU 5574  CB  LEU A 135    17572   7061  10969   1710  -1603  -1421       C  
ATOM   5575  CG  LEU A 135      36.776  69.332   3.722  1.00 90.61           C  
ANISOU 5575  CG  LEU A 135    17106   6821  10500   1332  -1640  -1231       C  
ATOM   5576  CD1 LEU A 135      36.609  67.838   3.526  1.00 87.85           C  
ANISOU 5576  CD1 LEU A 135    16431   6835  10112   1293  -1390  -1158       C  
ATOM   5577  CD2 LEU A 135      37.163  69.999   2.421  1.00 91.23           C  
ANISOU 5577  CD2 LEU A 135    17238   6746  10679   1122  -1881  -1036       C  
ATOM   5578  N   LEU A 136      36.352  68.092   7.022  1.00 93.36           N  
ANISOU 5578  N   LEU A 136    17444   7488  10539   1712  -1161  -1677       N  
ATOM   5579  CA  LEU A 136      37.584  67.722   7.702  1.00 92.06           C  
ANISOU 5579  CA  LEU A 136    17358   7399  10220   1490  -1162  -1675       C  
ATOM   5580  C   LEU A 136      38.529  67.110   6.683  1.00 89.10           C  
ANISOU 5580  C   LEU A 136    16844   7153   9855   1164  -1217  -1447       C  
ATOM   5581  O   LEU A 136      38.124  66.258   5.887  1.00 87.94           O  
ANISOU 5581  O   LEU A 136    16438   7205   9771   1145  -1105  -1329       O  
ATOM   5582  CB  LEU A 136      37.339  66.720   8.832  1.00 91.46           C  
ANISOU 5582  CB  LEU A 136    17159   7578  10013   1598   -909  -1790       C  
ATOM   5583  CG  LEU A 136      36.107  66.865   9.740  1.00 92.58           C  
ANISOU 5583  CG  LEU A 136    17301   7738  10137   1951   -755  -1998       C  
ATOM   5584  CD1 LEU A 136      36.249  65.918  10.923  1.00 91.79           C  
ANISOU 5584  CD1 LEU A 136    17122   7885   9868   1963   -548  -2084       C  
ATOM   5585  CD2 LEU A 136      35.918  68.294  10.213  1.00 94.97           C  
ANISOU 5585  CD2 LEU A 136    17909   7718  10456   2122   -924  -2171       C  
ATOM   5586  N   ASN A 137      39.784  67.546   6.702  1.00 90.32           N  
ANISOU 5586  N   ASN A 137    17170   7205   9944    909  -1392  -1388       N  
ATOM   5587  CA  ASN A 137      40.741  67.139   5.682  1.00 89.18           C  
ANISOU 5587  CA  ASN A 137    16910   7170   9804    596  -1473  -1175       C  
ATOM   5588  C   ASN A 137      41.936  66.446   6.323  1.00 88.80           C  
ANISOU 5588  C   ASN A 137    16847   7287   9604    387  -1427  -1161       C  
ATOM   5589  O   ASN A 137      42.576  67.005   7.223  1.00 90.51           O  
ANISOU 5589  O   ASN A 137    17291   7373   9727    342  -1517  -1254       O  
ATOM   5590  CB  ASN A 137      41.197  68.339   4.851  1.00 90.94           C  
ANISOU 5590  CB  ASN A 137    17321   7131  10100    439  -1757  -1068       C  
ATOM   5591  CG  ASN A 137      41.236  68.033   3.366  1.00 89.60           C  
ANISOU 5591  CG  ASN A 137    16955   7069  10020    276  -1800   -855       C  
ATOM   5592  OD1 ASN A 137      40.214  67.699   2.764  1.00 90.46           O  
ANISOU 5592  OD1 ASN A 137    16892   7247  10233    432  -1702   -831       O  
ATOM   5593  ND2 ASN A 137      42.416  68.145   2.767  1.00 90.31           N  
ANISOU 5593  ND2 ASN A 137    17065   7185  10064    -41  -1948   -699       N  
ATOM   5594  N   ASN A 138      42.210  65.222   5.862  1.00 87.99           N  
ANISOU 5594  N   ASN A 138    16479   7469   9483    269  -1293  -1051       N  
ATOM   5595  CA  ASN A 138      43.465  64.508   6.102  1.00 87.75           C  
ANISOU 5595  CA  ASN A 138    16392   7613   9335     27  -1281   -987       C  
ATOM   5596  C   ASN A 138      43.698  64.248   7.591  1.00 87.66           C  
ANISOU 5596  C   ASN A 138    16483   7633   9192     98  -1186  -1142       C  
ATOM   5597  O   ASN A 138      44.706  64.654   8.174  1.00 87.06           O  
ANISOU 5597  O   ASN A 138    16581   7480   9019    -54  -1301  -1161       O  
ATOM   5598  CB  ASN A 138      44.639  65.266   5.474  1.00 89.52           C  
ANISOU 5598  CB  ASN A 138    16745   7724   9544   -261  -1521   -857       C  
ATOM   5599  CG  ASN A 138      44.546  65.328   3.961  1.00 88.51           C  
ANISOU 5599  CG  ASN A 138    16478   7631   9520   -375  -1600   -681       C  
ATOM   5600  OD1 ASN A 138      43.594  64.821   3.366  1.00 87.41           O  
ANISOU 5600  OD1 ASN A 138    16154   7587   9472   -234  -1482   -659       O  
ATOM   5601  ND2 ASN A 138      45.529  65.960   3.331  1.00 90.67           N  
ANISOU 5601  ND2 ASN A 138    16840   7835   9776   -639  -1806   -549       N  
ATOM   5602  N   PHE A 139      42.755  63.530   8.193  1.00 85.71           N  
ANISOU 5602  N   PHE A 139    16112   7515   8936    321   -976  -1243       N  
ATOM   5603  CA  PHE A 139      42.830  63.177   9.601  1.00 84.24           C  
ANISOU 5603  CA  PHE A 139    15994   7394   8620    402   -861  -1386       C  
ATOM   5604  C   PHE A 139      42.888  61.667   9.788  1.00 81.61           C  
ANISOU 5604  C   PHE A 139    15406   7365   8239    368   -670  -1339       C  
ATOM   5605  O   PHE A 139      42.354  60.896   8.985  1.00 76.64           O  
ANISOU 5605  O   PHE A 139    14540   6886   7692    395   -575  -1249       O  
ATOM   5606  CB  PHE A 139      41.639  63.744  10.385  1.00 86.09           C  
ANISOU 5606  CB  PHE A 139    16339   7512   8858    711   -785  -1570       C  
ATOM   5607  CG  PHE A 139      40.303  63.195   9.960  1.00 85.61           C  
ANISOU 5607  CG  PHE A 139    16056   7576   8894    925   -616  -1568       C  
ATOM   5608  CD1 PHE A 139      39.695  62.179  10.679  1.00 85.30           C  
ANISOU 5608  CD1 PHE A 139    15852   7765   8792   1051   -394  -1627       C  
ATOM   5609  CD2 PHE A 139      39.647  63.708   8.854  1.00 86.74           C  
ANISOU 5609  CD2 PHE A 139    16157   7611   9189    991   -689  -1499       C  
ATOM   5610  CE1 PHE A 139      38.465  61.677  10.295  1.00 85.32           C  
ANISOU 5610  CE1 PHE A 139    15646   7889   8881   1235   -246  -1615       C  
ATOM   5611  CE2 PHE A 139      38.416  63.210   8.465  1.00 86.35           C  
ANISOU 5611  CE2 PHE A 139    15900   7680   9229   1183   -541  -1492       C  
ATOM   5612  CZ  PHE A 139      37.825  62.193   9.187  1.00 86.06           C  
ANISOU 5612  CZ  PHE A 139    15696   7875   9128   1304   -318  -1550       C  
ATOM   5613  N   TYR A 140      43.562  61.262  10.857  1.00 80.70           N  
ANISOU 5613  N   TYR A 140    15348   7327   7986    300   -630  -1400       N  
ATOM   5614  CA  TYR A 140      43.517  59.901  11.361  1.00 77.42           C  
ANISOU 5614  CA  TYR A 140    14736   7170   7509    304   -451  -1390       C  
ATOM   5615  C   TYR A 140      43.520  60.015  12.884  1.00 78.31           C  
ANISOU 5615  C   TYR A 140    15007   7271   7478    392   -390  -1547       C  
ATOM   5616  O   TYR A 140      44.235  60.855  13.433  1.00 78.86           O  
ANISOU 5616  O   TYR A 140    15313   7179   7471    316   -522  -1610       O  
ATOM   5617  CB  TYR A 140      44.702  59.068  10.847  1.00 74.06           C  
ANISOU 5617  CB  TYR A 140    14174   6899   7066     46   -496  -1248       C  
ATOM   5618  CG  TYR A 140      44.571  57.596  11.166  1.00 72.41           C  
ANISOU 5618  CG  TYR A 140    13742   6947   6825     57   -328  -1221       C  
ATOM   5619  CD1 TYR A 140      43.914  56.734  10.297  1.00 70.62           C  
ANISOU 5619  CD1 TYR A 140    13268   6865   6699    105   -232  -1135       C  
ATOM   5620  CD2 TYR A 140      45.079  57.072  12.349  1.00 71.85           C  
ANISOU 5620  CD2 TYR A 140    13714   6962   6623     16   -278  -1278       C  
ATOM   5621  CE1 TYR A 140      43.775  55.393  10.592  1.00 69.00           C  
ANISOU 5621  CE1 TYR A 140    12871   6874   6470    111    -99  -1108       C  
ATOM   5622  CE2 TYR A 140      44.941  55.732  12.654  1.00 69.00           C  
ANISOU 5622  CE2 TYR A 140    13159   6821   6238     21   -143  -1246       C  
ATOM   5623  CZ  TYR A 140      44.290  54.897  11.770  1.00 68.10           C  
ANISOU 5623  CZ  TYR A 140    12806   6837   6230     69    -58  -1160       C  
ATOM   5624  OH  TYR A 140      44.148  53.562  12.065  1.00 67.33           O  
ANISOU 5624  OH  TYR A 140    12527   6941   6115     68     57  -1123       O  
ATOM   5625  N   PRO A 141      42.739  59.171  13.581  1.00 81.26           N  
ANISOU 5625  N   PRO A 141    15252   7820   7804    539   -196  -1605       N  
ATOM   5626  CA  PRO A 141      41.934  58.059  13.064  1.00 81.71           C  
ANISOU 5626  CA  PRO A 141    15029   8083   7936    610    -40  -1526       C  
ATOM   5627  C   PRO A 141      40.565  58.370  12.488  1.00 85.29           C  
ANISOU 5627  C   PRO A 141    15399   8502   8505    830     30  -1548       C  
ATOM   5628  O   PRO A 141      40.136  59.521  12.381  1.00 86.96           O  
ANISOU 5628  O   PRO A 141    15767   8513   8760    953    -47  -1628       O  
ATOM   5629  CB  PRO A 141      41.782  57.155  14.295  1.00 80.84           C  
ANISOU 5629  CB  PRO A 141    14864   8159   7694    653    113  -1587       C  
ATOM   5630  CG  PRO A 141      41.795  58.097  15.428  1.00 83.97           C  
ANISOU 5630  CG  PRO A 141    15512   8420   7972    745     87  -1753       C  
ATOM   5631  CD  PRO A 141      42.777  59.173  15.053  1.00 85.02           C  
ANISOU 5631  CD  PRO A 141    15860   8323   8122    604   -128  -1745       C  
ATOM   5632  N   ARG A 142      39.893  57.277  12.133  1.00 87.05           N  
ANISOU 5632  N   ARG A 142    15370   8928   8779    875    170  -1472       N  
ATOM   5633  CA  ARG A 142      38.593  57.354  11.475  1.00 92.29           C  
ANISOU 5633  CA  ARG A 142    15903   9602   9562   1062    245  -1463       C  
ATOM   5634  C   ARG A 142      37.614  58.262  12.213  1.00 92.91           C  
ANISOU 5634  C   ARG A 142    16110   9578   9613   1318    297  -1629       C  
ATOM   5635  O   ARG A 142      37.061  59.202  11.636  1.00 89.10           O  
ANISOU 5635  O   ARG A 142    15696   8928   9231   1439    225  -1658       O  
ATOM   5636  CB  ARG A 142      38.008  55.945  11.371  1.00100.93           C  
ANISOU 5636  CB  ARG A 142    16725  10951  10673   1076    405  -1380       C  
ATOM   5637  CG  ARG A 142      36.529  55.887  11.025  1.00107.91           C  
ANISOU 5637  CG  ARG A 142    17460  11893  11648   1292    521  -1386       C  
ATOM   5638  CD  ARG A 142      36.287  55.979   9.541  1.00112.30           C  
ANISOU 5638  CD  ARG A 142    17905  12398  12365   1261    447  -1267       C  
ATOM   5639  NE  ARG A 142      36.711  54.727   8.916  1.00113.55           N  
ANISOU 5639  NE  ARG A 142    17865  12727  12553   1094    467  -1126       N  
ATOM   5640  CZ  ARG A 142      35.971  53.623   8.858  1.00115.76           C  
ANISOU 5640  CZ  ARG A 142    17926  13200  12856   1139    597  -1068       C  
ATOM   5641  NH1 ARG A 142      34.755  53.590   9.393  1.00114.27           N  
ANISOU 5641  NH1 ARG A 142    17672  13086  12661   1338    731  -1127       N  
ATOM   5642  NH2 ARG A 142      36.480  52.551   8.267  1.00117.66           N  
ANISOU 5642  NH2 ARG A 142    18015  13564  13126    981    584   -952       N  
ATOM   5643  N   GLU A 143      37.400  58.006  13.489  1.00 96.40           N  
ANISOU 5643  N   GLU A 143    16589  10121   9916   1404    415  -1742       N  
ATOM   5644  CA  GLU A 143      36.193  58.464  14.165  1.00 99.23           C  
ANISOU 5644  CA  GLU A 143    16969  10491  10245   1679    531  -1890       C  
ATOM   5645  C   GLU A 143      36.340  59.909  14.627  1.00 99.28           C  
ANISOU 5645  C   GLU A 143    17265  10240  10216   1785    411  -2054       C  
ATOM   5646  O   GLU A 143      37.228  60.234  15.416  1.00 97.48           O  
ANISOU 5646  O   GLU A 143    17234   9937   9868   1689    339  -2126       O  
ATOM   5647  CB  GLU A 143      35.854  57.545  15.344  1.00101.72           C  
ANISOU 5647  CB  GLU A 143    17186  11053  10411   1723    715  -1938       C  
ATOM   5648  CG  GLU A 143      35.989  56.030  15.063  1.00101.66           C  
ANISOU 5648  CG  GLU A 143    16930  11283  10414   1569    800  -1773       C  
ATOM   5649  CD  GLU A 143      37.423  55.537  14.950  1.00104.37           C  
ANISOU 5649  CD  GLU A 143    17315  11615  10725   1298    690  -1677       C  
ATOM   5650  OE1 GLU A 143      37.653  54.375  14.511  1.00105.30           O  
ANISOU 5650  OE1 GLU A 143    17243  11886  10880   1165    719  -1539       O  
ATOM   5651  OE2 GLU A 143      38.352  56.310  15.298  1.00107.64           O  
ANISOU 5651  OE2 GLU A 143    17953  11866  11078   1214    564  -1741       O  
ATOM   5652  N   ALA A 144      35.456  60.774  14.140  1.00 99.12           N  
ANISOU 5652  N   ALA A 144    17276  10080  10307   1986    378  -2115       N  
ATOM   5653  CA  ALA A 144      35.306  62.135  14.638  1.00100.91           C  
ANISOU 5653  CA  ALA A 144    17766  10065  10511   2153    279  -2298       C  
ATOM   5654  C   ALA A 144      33.818  62.390  14.858  1.00101.67           C  
ANISOU 5654  C   ALA A 144    17770  10220  10639   2477    414  -2420       C  
ATOM   5655  O   ALA A 144      32.961  61.628  14.393  1.00 98.95           O  
ANISOU 5655  O   ALA A 144    17165  10067  10363   2544    550  -2333       O  
ATOM   5656  CB  ALA A 144      35.880  63.172  13.659  1.00102.09           C  
ANISOU 5656  CB  ALA A 144    18086   9916  10787   2056     36  -2241       C  
ATOM   5657  N   LYS A 145      33.495  63.453  15.588  1.00107.26           N  
ANISOU 5657  N   LYS A 145    18689  10770  11294   2686    376  -2629       N  
ATOM   5658  CA  LYS A 145      32.089  63.808  15.778  1.00111.12           C  
ANISOU 5658  CA  LYS A 145    19097  11307  11818   3017    492  -2763       C  
ATOM   5659  C   LYS A 145      31.898  65.266  15.390  1.00112.42           C  
ANISOU 5659  C   LYS A 145    19484  11134  12096   3174    299  -2873       C  
ATOM   5660  O   LYS A 145      32.452  66.157  16.043  1.00113.62           O  
ANISOU 5660  O   LYS A 145    19826  11137  12209   3140    169  -2967       O  
ATOM   5661  CB  LYS A 145      31.625  63.569  17.216  1.00114.92           C  
ANISOU 5661  CB  LYS A 145    19562  11996  12107   3174    677  -2937       C  
ATOM   5662  CG  LYS A 145      30.328  64.294  17.508  1.00120.04           C  
ANISOU 5662  CG  LYS A 145    20126  12671  12813   3487    741  -3082       C  
ATOM   5663  CD  LYS A 145      29.905  64.230  18.959  1.00123.25           C  
ANISOU 5663  CD  LYS A 145    20471  13303  13054   3597    895  -3233       C  
ATOM   5664  CE  LYS A 145      28.616  65.020  19.139  1.00127.07           C  
ANISOU 5664  CE  LYS A 145    20868  13803  13610   3910    944  -3380       C  
ATOM   5665  NZ  LYS A 145      28.313  65.358  20.556  1.00128.89           N  
ANISOU 5665  NZ  LYS A 145    21105  14175  13693   4024   1037  -3565       N  
ATOM   5666  N   VAL A 146      31.129  65.515  14.330  1.00113.30           N  
ANISOU 5666  N   VAL A 146    19481  11176  12389   3283    261  -2800       N  
ATOM   5667  CA  VAL A 146      30.787  66.872  13.932  1.00118.46           C  
ANISOU 5667  CA  VAL A 146    20293  11537  13180   3438     75  -2881       C  
ATOM   5668  C   VAL A 146      29.375  67.145  14.422  1.00122.97           C  
ANISOU 5668  C   VAL A 146    20707  12241  13777   3766    217  -3023       C  
ATOM   5669  O   VAL A 146      28.526  66.241  14.458  1.00124.96           O  
ANISOU 5669  O   VAL A 146    20718  12760  14001   3881    432  -3005       O  
ATOM   5670  CB  VAL A 146      30.897  67.074  12.407  1.00115.85           C  
ANISOU 5670  CB  VAL A 146    19949  11027  13042   3329    -88  -2699       C  
ATOM   5671  CG1 VAL A 146      32.170  66.538  11.873  1.00111.91           C  
ANISOU 5671  CG1 VAL A 146    19456  10538  12528   2959   -177  -2501       C  
ATOM   5672  CG2 VAL A 146      29.695  66.567  11.641  1.00115.43           C  
ANISOU 5672  CG2 VAL A 146    19602  11138  13117   3473     37  -2610       C  
ATOM   5673  N   GLN A 147      29.144  68.369  14.865  1.00127.14           N  
ANISOU 5673  N   GLN A 147    21364  12600  14345   3908     99  -3166       N  
ATOM   5674  CA  GLN A 147      27.803  68.845  15.137  1.00130.04           C  
ANISOU 5674  CA  GLN A 147    21598  13040  14771   4224    186  -3301       C  
ATOM   5675  C   GLN A 147      27.685  70.288  14.683  1.00130.94           C  
ANISOU 5675  C   GLN A 147    21882  12824  15045   4320    -57  -3353       C  
ATOM   5676  O   GLN A 147      28.669  71.042  14.642  1.00130.87           O  
ANISOU 5676  O   GLN A 147    22120  12560  15046   4158   -275  -3341       O  
ATOM   5677  CB  GLN A 147      27.410  68.714  16.617  1.00133.33           C  
ANISOU 5677  CB  GLN A 147    21950  13696  15014   4355    370  -3481       C  
ATOM   5678  CG  GLN A 147      28.521  68.945  17.611  1.00134.55           C  
ANISOU 5678  CG  GLN A 147    22312  13796  15015   4187    305  -3551       C  
ATOM   5679  CD  GLN A 147      28.137  68.476  18.997  1.00136.38           C  
ANISOU 5679  CD  GLN A 147    22435  14328  15056   4277    523  -3689       C  
ATOM   5680  OE1 GLN A 147      27.065  67.901  19.192  1.00136.41           O  
ANISOU 5680  OE1 GLN A 147    22196  14600  15034   4446    730  -3718       O  
ATOM   5681  NE2 GLN A 147      29.010  68.712  19.969  1.00137.55           N  
ANISOU 5681  NE2 GLN A 147    22754  14444  15066   4154    476  -3767       N  
ATOM   5682  N   TRP A 148      26.463  70.639  14.306  1.00130.72           N  
ANISOU 5682  N   TRP A 148    21711  12811  15146   4576    -22  -3398       N  
ATOM   5683  CA  TRP A 148      26.116  71.968  13.846  1.00132.81           C  
ANISOU 5683  CA  TRP A 148    22097  12787  15576   4708   -237  -3451       C  
ATOM   5684  C   TRP A 148      25.380  72.707  14.944  1.00135.34           C  
ANISOU 5684  C   TRP A 148    22419  13157  15848   4971   -179  -3686       C  
ATOM   5685  O   TRP A 148      24.494  72.151  15.602  1.00135.97           O  
ANISOU 5685  O   TRP A 148    22284  13531  15845   5148     59  -3780       O  
ATOM   5686  CB  TRP A 148      25.241  71.909  12.597  1.00131.13           C  
ANISOU 5686  CB  TRP A 148    21724  12542  15557   4815   -259  -3333       C  
ATOM   5687  CG  TRP A 148      25.926  71.287  11.457  1.00126.68           C  
ANISOU 5687  CG  TRP A 148    21169  11910  15052   4568   -334  -3107       C  
ATOM   5688  CD1 TRP A 148      25.954  69.957  11.143  1.00123.07           C  
ANISOU 5688  CD1 TRP A 148    20536  11685  14539   4470   -158  -2983       C  
ATOM   5689  CD2 TRP A 148      26.689  71.956  10.450  1.00125.44           C  
ANISOU 5689  CD2 TRP A 148    21204  11439  15019   4376   -611  -2970       C  
ATOM   5690  NE1 TRP A 148      26.700  69.757  10.006  1.00120.43           N  
ANISOU 5690  NE1 TRP A 148    20278  11194  14285   4237   -304  -2789       N  
ATOM   5691  CE2 TRP A 148      27.158  70.970   9.560  1.00121.48           C  
ANISOU 5691  CE2 TRP A 148    20630  11000  14528   4168   -581  -2772       C  
ATOM   5692  CE3 TRP A 148      27.028  73.294  10.217  1.00126.08           C  
ANISOU 5692  CE3 TRP A 148    21509  11197  15197   4351   -884  -2990       C  
ATOM   5693  CZ2 TRP A 148      27.945  71.283   8.455  1.00119.46           C  
ANISOU 5693  CZ2 TRP A 148    20510  10507  14371   3932   -812  -2596       C  
ATOM   5694  CZ3 TRP A 148      27.803  73.598   9.123  1.00124.51           C  
ANISOU 5694  CZ3 TRP A 148    21442  10769  15097   4109  -1115  -2804       C  
ATOM   5695  CH2 TRP A 148      28.253  72.602   8.255  1.00121.28           C  
ANISOU 5695  CH2 TRP A 148    20949  10441  14692   3900  -1075  -2609       C  
ATOM   5696  N   LYS A 149      25.772  73.956  15.144  1.00136.57           N  
ANISOU 5696  N   LYS A 149    22816  13028  16048   4984   -400  -3777       N  
ATOM   5697  CA  LYS A 149      24.992  74.890  15.932  1.00140.53           C  
ANISOU 5697  CA  LYS A 149    23340  13503  16553   5261   -399  -3999       C  
ATOM   5698  C   LYS A 149      24.792  76.148  15.105  1.00143.71           C  
ANISOU 5698  C   LYS A 149    23883  13561  17159   5340   -669  -3988       C  
ATOM   5699  O   LYS A 149      25.746  76.900  14.855  1.00148.33           O  
ANISOU 5699  O   LYS A 149    24724  13856  17779   5166   -919  -3938       O  
ATOM   5700  CB  LYS A 149      25.666  75.179  17.272  1.00142.19           C  
ANISOU 5700  CB  LYS A 149    23718  13728  16581   5216   -389  -4158       C  
ATOM   5701  CG  LYS A 149      25.941  73.904  18.079  1.00139.94           C  
ANISOU 5701  CG  LYS A 149    23300  13782  16089   5105   -137  -4149       C  
ATOM   5702  CD  LYS A 149      26.998  74.131  19.129  1.00140.70           C  
ANISOU 5702  CD  LYS A 149    23608  13832  16020   4954   -189  -4232       C  
ATOM   5703  CE  LYS A 149      28.219  74.751  18.483  1.00139.91           C  
ANISOU 5703  CE  LYS A 149    23772  13395  15993   4706   -476  -4109       C  
ATOM   5704  NZ  LYS A 149      29.486  74.377  19.155  1.00139.20           N  
ANISOU 5704  NZ  LYS A 149    23821  13331  15739   4443   -491  -4077       N  
ATOM   5705  N   VAL A 150      23.566  76.314  14.614  1.00142.87           N  
ANISOU 5705  N   VAL A 150    23597  13498  17188   5583   -621  -4010       N  
ATOM   5706  CA  VAL A 150      23.040  77.603  14.178  1.00144.10           C  
ANISOU 5706  CA  VAL A 150    23853  13379  17518   5757   -834  -4072       C  
ATOM   5707  C   VAL A 150      22.733  78.423  15.439  1.00146.11           C  
ANISOU 5707  C   VAL A 150    24202  13627  17684   5972   -818  -4337       C  
ATOM   5708  O   VAL A 150      21.829  78.086  16.203  1.00145.99           O  
ANISOU 5708  O   VAL A 150    23996  13883  17589   6194   -589  -4485       O  
ATOM   5709  CB  VAL A 150      21.789  77.433  13.297  1.00143.49           C  
ANISOU 5709  CB  VAL A 150    23529  13382  17607   5952   -768  -4011       C  
ATOM   5710  CG1 VAL A 150      21.552  78.670  12.446  1.00145.30           C  
ANISOU 5710  CG1 VAL A 150    23893  13268  18047   6025  -1052  -3984       C  
ATOM   5711  CG2 VAL A 150      21.851  76.147  12.440  1.00139.59           C  
ANISOU 5711  CG2 VAL A 150    22840  13069  17127   5789   -641  -3791       C  
ATOM   5712  N   ASP A 151      23.505  79.489  15.654  1.00146.65           N  
ANISOU 5712  N   ASP A 151    24566  13393  17762   5897  -1066  -4392       N  
ATOM   5713  CA  ASP A 151      23.373  80.477  16.739  1.00150.35           C  
ANISOU 5713  CA  ASP A 151    25187  13772  18166   6080  -1122  -4637       C  
ATOM   5714  C   ASP A 151      23.524  79.865  18.134  1.00150.94           C  
ANISOU 5714  C   ASP A 151    25214  14130  18006   6097   -886  -4789       C  
ATOM   5715  O   ASP A 151      22.961  80.330  19.127  1.00154.56           O  
ANISOU 5715  O   ASP A 151    25672  14664  18391   6327   -809  -5016       O  
ATOM   5716  CB  ASP A 151      22.082  81.289  16.571  1.00152.64           C  
ANISOU 5716  CB  ASP A 151    25394  14002  18601   6420  -1153  -4770       C  
ATOM   5717  CG  ASP A 151      20.815  80.583  17.013  1.00151.82           C  
ANISOU 5717  CG  ASP A 151    24970  14265  18450   6676   -844  -4874       C  
ATOM   5718  OD1 ASP A 151      20.780  79.784  17.969  1.00148.34           O  
ANISOU 5718  OD1 ASP A 151    24410  14132  17822   6680   -598  -4955       O  
ATOM   5719  OD2 ASP A 151      19.794  80.865  16.374  1.00153.51           O  
ANISOU 5719  OD2 ASP A 151    25043  14463  18821   6878   -857  -4871       O  
ATOM   5720  N   ASN A 152      24.398  78.864  18.196  1.00147.19           N  
ANISOU 5720  N   ASN A 152    24724  13791  17411   5828   -794  -4655       N  
ATOM   5721  CA  ASN A 152      24.646  78.055  19.391  1.00146.39           C  
ANISOU 5721  CA  ASN A 152    24555  13983  17082   5783   -563  -4745       C  
ATOM   5722  C   ASN A 152      23.399  77.260  19.758  1.00147.50           C  
ANISOU 5722  C   ASN A 152    24374  14499  17170   6004   -259  -4819       C  
ATOM   5723  O   ASN A 152      23.044  77.141  20.933  1.00151.80           O  
ANISOU 5723  O   ASN A 152    24857  15262  17558   6131    -87  -4996       O  
ATOM   5724  CB  ASN A 152      25.121  78.891  20.597  1.00148.98           C  
ANISOU 5724  CB  ASN A 152    25110  14208  17287   5821   -643  -4948       C  
ATOM   5725  CG  ASN A 152      26.037  80.047  20.204  1.00148.92           C  
ANISOU 5725  CG  ASN A 152    25423  13788  17373   5689   -985  -4911       C  
ATOM   5726  OD1 ASN A 152      25.592  81.008  19.577  1.00148.73           O  
ANISOU 5726  OD1 ASN A 152    25471  13520  17518   5824  -1172  -4928       O  
ATOM   5727  ND2 ASN A 152      27.280  80.013  20.665  1.00147.87           N  
ANISOU 5727  ND2 ASN A 152    25481  13581  17121   5437  -1071  -4872       N  
ATOM   5728  N   ALA A 153      22.732  76.717  18.740  1.00146.04           N  
ANISOU 5728  N   ALA A 153    23980  14395  17114   6042   -196  -4676       N  
ATOM   5729  CA  ALA A 153      21.542  75.892  18.896  1.00146.86           C  
ANISOU 5729  CA  ALA A 153    23756  14860  17186   6225     80  -4700       C  
ATOM   5730  C   ALA A 153      21.806  74.562  18.210  1.00144.35           C  
ANISOU 5730  C   ALA A 153    23273  14720  16854   6017    201  -4473       C  
ATOM   5731  O   ALA A 153      22.060  74.525  17.001  1.00143.46           O  
ANISOU 5731  O   ALA A 153    23185  14432  16892   5901     63  -4293       O  
ATOM   5732  CB  ALA A 153      20.311  76.575  18.301  1.00149.02           C  
ANISOU 5732  CB  ALA A 153    23912  15065  17645   6509     37  -4753       C  
ATOM   5733  N   LEU A 154      21.760  73.483  18.982  1.00144.59           N  
ANISOU 5733  N   LEU A 154    23142  15096  16699   5964    449  -4479       N  
ATOM   5734  CA  LEU A 154      22.063  72.160  18.464  1.00140.49           C  
ANISOU 5734  CA  LEU A 154    22475  14763  16142   5762    571  -4274       C  
ATOM   5735  C   LEU A 154      21.027  71.732  17.429  1.00139.82           C  
ANISOU 5735  C   LEU A 154    22135  14780  16210   5882    643  -4154       C  
ATOM   5736  O   LEU A 154      19.862  72.134  17.477  1.00142.81           O  
ANISOU 5736  O   LEU A 154    22363  15240  16659   6145    704  -4253       O  
ATOM   5737  CB  LEU A 154      22.117  71.161  19.619  1.00140.50           C  
ANISOU 5737  CB  LEU A 154    22350  15126  15908   5701    820  -4319       C  
ATOM   5738  CG  LEU A 154      22.350  69.685  19.310  1.00138.68           C  
ANISOU 5738  CG  LEU A 154    21945  15144  15604   5507    980  -4126       C  
ATOM   5739  CD1 LEU A 154      23.707  69.467  18.655  1.00134.80           C  
ANISOU 5739  CD1 LEU A 154    21653  14429  15135   5210    814  -3965       C  
ATOM   5740  CD2 LEU A 154      22.221  68.856  20.576  1.00139.49           C  
ANISOU 5740  CD2 LEU A 154    21915  15611  15473   5483   1219  -4195       C  
ATOM   5741  N   GLN A 155      21.472  70.916  16.478  1.00136.28           N  
ANISOU 5741  N   GLN A 155    21641  14328  15813   5686    631  -3939       N  
ATOM   5742  CA  GLN A 155      20.633  70.418  15.402  1.00134.76           C  
ANISOU 5742  CA  GLN A 155    21217  14220  15764   5759    686  -3796       C  
ATOM   5743  C   GLN A 155      20.582  68.896  15.444  1.00132.30           C  
ANISOU 5743  C   GLN A 155    20681  14251  15335   5638    916  -3662       C  
ATOM   5744  O   GLN A 155      21.480  68.235  15.973  1.00130.48           O  
ANISOU 5744  O   GLN A 155    20524  14104  14947   5432    972  -3630       O  
ATOM   5745  CB  GLN A 155      21.152  70.889  14.038  1.00133.32           C  
ANISOU 5745  CB  GLN A 155    21185  13696  15777   5640    434  -3642       C  
ATOM   5746  CG  GLN A 155      21.648  72.328  14.020  1.00135.24           C  
ANISOU 5746  CG  GLN A 155    21719  13561  16105   5653    162  -3735       C  
ATOM   5747  CD  GLN A 155      20.538  73.337  14.244  1.00137.54           C  
ANISOU 5747  CD  GLN A 155    21964  13802  16494   5964    133  -3901       C  
ATOM   5748  OE1 GLN A 155      19.613  73.447  13.441  1.00137.82           O  
ANISOU 5748  OE1 GLN A 155    21842  13835  16689   6112    125  -3846       O  
ATOM   5749  NE2 GLN A 155      20.629  74.083  15.337  1.00138.20           N  
ANISOU 5749  NE2 GLN A 155    22185  13843  16482   6066    114  -4108       N  
ATOM   5750  N   SER A 156      19.516  68.342  14.867  1.00132.36           N  
ANISOU 5750  N   SER A 156    20410  14456  15425   5761   1043  -3577       N  
ATOM   5751  CA  SER A 156      19.286  66.903  14.881  1.00130.03           C  
ANISOU 5751  CA  SER A 156    19870  14505  15030   5670   1266  -3444       C  
ATOM   5752  C   SER A 156      18.696  66.458  13.553  1.00128.23           C  
ANISOU 5752  C   SER A 156    19461  14286  14976   5692   1258  -3260       C  
ATOM   5753  O   SER A 156      17.679  67.001  13.111  1.00130.81           O  
ANISOU 5753  O   SER A 156    19664  14591  15447   5902   1233  -3287       O  
ATOM   5754  CB  SER A 156      18.340  66.504  16.022  1.00132.01           C  
ANISOU 5754  CB  SER A 156    19889  15137  15130   5822   1511  -3560       C  
ATOM   5755  OG  SER A 156      18.784  67.016  17.266  1.00133.54           O  
ANISOU 5755  OG  SER A 156    20248  15321  15171   5828   1514  -3745       O  
ATOM   5756  N   GLY A 157      19.333  65.472  12.924  1.00124.93           N  
ANISOU 5756  N   GLY A 157    19026  13902  14542   5477   1277  -3075       N  
ATOM   5757  CA  GLY A 157      18.777  64.816  11.756  1.00122.05           C  
ANISOU 5757  CA  GLY A 157    18458  13606  14310   5480   1308  -2888       C  
ATOM   5758  C   GLY A 157      18.431  65.723  10.593  1.00121.76           C  
ANISOU 5758  C   GLY A 157    18473  13281  14511   5579   1104  -2844       C  
ATOM   5759  O   GLY A 157      17.557  65.397   9.785  1.00123.13           O  
ANISOU 5759  O   GLY A 157    18425  13549  14809   5671   1145  -2731       O  
ATOM   5760  N   ASN A 158      19.093  66.875  10.507  1.00121.29           N  
ANISOU 5760  N   ASN A 158    18697  12871  14517   5554    875  -2923       N  
ATOM   5761  CA  ASN A 158      19.028  67.727   9.327  1.00120.78           C  
ANISOU 5761  CA  ASN A 158    18730  12489  14672   5579    639  -2848       C  
ATOM   5762  C   ASN A 158      20.363  67.762   8.594  1.00117.41           C  
ANISOU 5762  C   ASN A 158    18550  11787  14273   5302    443  -2720       C  
ATOM   5763  O   ASN A 158      20.637  68.706   7.848  1.00116.42           O  
ANISOU 5763  O   ASN A 158    18596  11344  14295   5269    199  -2683       O  
ATOM   5764  CB  ASN A 158      18.593  69.142   9.709  1.00125.75           C  
ANISOU 5764  CB  ASN A 158    19476  12924  15381   5778    505  -3028       C  
ATOM   5765  CG  ASN A 158      19.475  69.755  10.780  1.00126.95           C  
ANISOU 5765  CG  ASN A 158    19886  12955  15393   5714    442  -3191       C  
ATOM   5766  OD1 ASN A 158      20.467  69.159  11.201  1.00124.56           O  
ANISOU 5766  OD1 ASN A 158    19687  12699  14943   5506    483  -3162       O  
ATOM   5767  ND2 ASN A 158      19.121  70.958  11.223  1.00128.08           N  
ANISOU 5767  ND2 ASN A 158    20137  12940  15586   5893    335  -3361       N  
ATOM   5768  N   SER A 159      21.196  66.745   8.793  1.00114.14           N  
ANISOU 5768  N   SER A 159    18124  11519  13723   5053    538  -2625       N  
ATOM   5769  CA  SER A 159      22.583  66.795   8.365  1.00110.54           C  
ANISOU 5769  CA  SER A 159    17871  10868  13262   4720    363  -2506       C  
ATOM   5770  C   SER A 159      23.061  65.390   8.039  1.00106.38           C  
ANISOU 5770  C   SER A 159    17141  10601  12676   4414    483  -2294       C  
ATOM   5771  O   SER A 159      22.629  64.415   8.662  1.00107.16           O  
ANISOU 5771  O   SER A 159    17034  11019  12665   4438    708  -2297       O  
ATOM   5772  CB  SER A 159      23.466  67.414   9.455  1.00111.57           C  
ANISOU 5772  CB  SER A 159    18305  10844  13243   4715    302  -2695       C  
ATOM   5773  OG  SER A 159      24.708  67.831   8.926  1.00109.76           O  
ANISOU 5773  OG  SER A 159    18307  10351  13046   4441     75  -2596       O  
ATOM   5774  N   GLN A 160      23.963  65.296   7.062  1.00104.15           N  
ANISOU 5774  N   GLN A 160    16922  10185  12465   4124    324  -2110       N  
ATOM   5775  CA  GLN A 160      24.513  64.016   6.640  1.00100.50           C  
ANISOU 5775  CA  GLN A 160    16288   9938  11961   3830    406  -1912       C  
ATOM   5776  C   GLN A 160      26.024  64.137   6.501  1.00 98.16           C  
ANISOU 5776  C   GLN A 160    16203   9483  11610   3530    251  -1850       C  
ATOM   5777  O   GLN A 160      26.561  65.225   6.264  1.00 99.32           O  
ANISOU 5777  O   GLN A 160    16597   9331  11807   3508     41  -1888       O  
ATOM   5778  CB  GLN A 160      23.886  63.550   5.319  1.00100.01           C  
ANISOU 5778  CB  GLN A 160    15993   9946  12058   3780    393  -1713       C  
ATOM   5779  CG  GLN A 160      22.486  62.954   5.435  1.00101.33           C  
ANISOU 5779  CG  GLN A 160    15872  10374  12253   3995    590  -1717       C  
ATOM   5780  CD  GLN A 160      21.805  62.829   4.083  1.00102.75           C  
ANISOU 5780  CD  GLN A 160    15874  10553  12615   3985    529  -1543       C  
ATOM   5781  OE1 GLN A 160      20.716  62.264   3.970  1.00104.07           O  
ANISOU 5781  OE1 GLN A 160    15787  10935  12822   4114    669  -1503       O  
ATOM   5782  NE2 GLN A 160      22.434  63.392   3.054  1.00103.75           N  
ANISOU 5782  NE2 GLN A 160    16135  10438  12848   3828    313  -1437       N  
ATOM   5783  N   GLU A 161      26.706  62.997   6.652  1.00 93.82           N  
ANISOU 5783  N   GLU A 161    15549   9140  10958   3295    350  -1750       N  
ATOM   5784  CA  GLU A 161      28.153  62.917   6.513  1.00 90.77           C  
ANISOU 5784  CA  GLU A 161    15314   8664  10511   2996    227  -1675       C  
ATOM   5785  C   GLU A 161      28.525  61.844   5.503  1.00 85.60           C  
ANISOU 5785  C   GLU A 161    14460   8164   9900   2745    241  -1456       C  
ATOM   5786  O   GLU A 161      27.884  60.792   5.419  1.00 84.54           O  
ANISOU 5786  O   GLU A 161    14076   8278   9766   2765    403  -1388       O  
ATOM   5787  CB  GLU A 161      28.840  62.593   7.833  1.00 92.39           C  
ANISOU 5787  CB  GLU A 161    15622   8958  10525   2945    317  -1792       C  
ATOM   5788  CG  GLU A 161      28.834  63.692   8.838  1.00 97.03           C  
ANISOU 5788  CG  GLU A 161    16461   9363  11044   3132    266  -2012       C  
ATOM   5789  CD  GLU A 161      29.663  63.319  10.050  1.00 98.35           C  
ANISOU 5789  CD  GLU A 161    16734   9619  11015   3032    337  -2101       C  
ATOM   5790  OE1 GLU A 161      29.265  63.677  11.181  1.00 99.93           O  
ANISOU 5790  OE1 GLU A 161    17020   9840  11108   3235    422  -2296       O  
ATOM   5791  OE2 GLU A 161      30.705  62.655   9.889  1.00 96.84           O  
ANISOU 5791  OE2 GLU A 161    16534   9489  10772   2755    310  -1980       O  
ATOM   5792  N   SER A 162      29.585  62.128   4.752  1.00 83.24           N  
ANISOU 5792  N   SER A 162    14279   7720   9630   2506     63  -1350       N  
ATOM   5793  CA  SER A 162      30.188  61.208   3.803  1.00 82.44           C  
ANISOU 5793  CA  SER A 162    14027   7748   9550   2245     49  -1160       C  
ATOM   5794  C   SER A 162      31.685  61.175   4.066  1.00 84.34           C  
ANISOU 5794  C   SER A 162    14421   7942   9681   1992    -42  -1143       C  
ATOM   5795  O   SER A 162      32.308  62.228   4.218  1.00 90.54           O  
ANISOU 5795  O   SER A 162    15450   8496  10453   1955   -203  -1198       O  
ATOM   5796  CB  SER A 162      29.910  61.642   2.364  1.00 82.13           C  
ANISOU 5796  CB  SER A 162    13942   7595   9668   2201    -93  -1021       C  
ATOM   5797  OG  SER A 162      30.840  61.054   1.478  1.00 79.66           O  
ANISOU 5797  OG  SER A 162    13565   7352   9350   1915   -160   -860       O  
ATOM   5798  N   VAL A 163      32.259  59.975   4.115  1.00 82.34           N  
ANISOU 5798  N   VAL A 163    14028   7905   9354   1818     50  -1066       N  
ATOM   5799  CA  VAL A 163      33.666  59.784   4.452  1.00 80.07           C  
ANISOU 5799  CA  VAL A 163    13852   7616   8954   1586    -14  -1053       C  
ATOM   5800  C   VAL A 163      34.363  59.118   3.276  1.00 76.32           C  
ANISOU 5800  C   VAL A 163    13244   7235   8518   1342    -76   -877       C  
ATOM   5801  O   VAL A 163      33.918  58.067   2.801  1.00 76.02           O  
ANISOU 5801  O   VAL A 163    12976   7391   8516   1331     30   -794       O  
ATOM   5802  CB  VAL A 163      33.833  58.934   5.723  1.00 79.10           C  
ANISOU 5802  CB  VAL A 163    13694   7671   8690   1603    147  -1138       C  
ATOM   5803  CG1 VAL A 163      35.274  58.982   6.205  1.00 78.85           C  
ANISOU 5803  CG1 VAL A 163    13820   7596   8543   1392     59  -1149       C  
ATOM   5804  CG2 VAL A 163      32.874  59.398   6.805  1.00 81.60           C  
ANISOU 5804  CG2 VAL A 163    14074   7965   8965   1875    252  -1308       C  
ATOM   5805  N   THR A 164      35.459  59.718   2.818  1.00 73.76           N  
ANISOU 5805  N   THR A 164    13063   6782   8180   1144   -250   -822       N  
ATOM   5806  CA  THR A 164      36.254  59.105   1.768  1.00 72.03           C  
ANISOU 5806  CA  THR A 164    12722   6675   7972    902   -309   -669       C  
ATOM   5807  C   THR A 164      36.896  57.817   2.274  1.00 72.40           C  
ANISOU 5807  C   THR A 164    12645   6946   7918    793   -193   -664       C  
ATOM   5808  O   THR A 164      37.049  57.594   3.477  1.00 72.43           O  
ANISOU 5808  O   THR A 164    12713   6982   7824    846   -111   -768       O  
ATOM   5809  CB  THR A 164      37.344  60.060   1.278  1.00 72.02           C  
ANISOU 5809  CB  THR A 164    12903   6506   7957    703   -520   -612       C  
ATOM   5810  OG1 THR A 164      38.287  60.296   2.332  1.00 72.43           O  
ANISOU 5810  OG1 THR A 164    13129   6506   7885    628   -551   -698       O  
ATOM   5811  CG2 THR A 164      36.737  61.384   0.845  1.00 75.14           C  
ANISOU 5811  CG2 THR A 164    13446   6649   8454    808   -661   -617       C  
ATOM   5812  N   GLU A 165      37.265  56.959   1.333  1.00 72.68           N  
ANISOU 5812  N   GLU A 165    12501   7137   7976    642   -193   -543       N  
ATOM   5813  CA  GLU A 165      38.016  55.761   1.666  1.00 75.45           C  
ANISOU 5813  CA  GLU A 165    12740   7683   8243    519   -120   -529       C  
ATOM   5814  C   GLU A 165      39.488  56.115   1.842  1.00 76.17           C  
ANISOU 5814  C   GLU A 165    12970   7731   8241    311   -242   -522       C  
ATOM   5815  O   GLU A 165      39.984  57.085   1.262  1.00 79.60           O  
ANISOU 5815  O   GLU A 165    13525   8027   8691    207   -395   -477       O  
ATOM   5816  CB  GLU A 165      37.830  54.694   0.585  1.00 76.80           C  
ANISOU 5816  CB  GLU A 165    12669   8037   8476    453    -80   -417       C  
ATOM   5817  CG  GLU A 165      36.370  54.453   0.204  1.00 79.06           C  
ANISOU 5817  CG  GLU A 165    12817   8356   8868    635     12   -398       C  
ATOM   5818  CD  GLU A 165      35.897  53.049   0.527  1.00 79.54           C  
ANISOU 5818  CD  GLU A 165    12683   8620   8920    682    161   -393       C  
ATOM   5819  OE1 GLU A 165      34.663  52.830   0.628  1.00 78.30           O  
ANISOU 5819  OE1 GLU A 165    12429   8500   8822    850    261   -400       O  
ATOM   5820  OE2 GLU A 165      36.753  52.145   0.705  1.00 79.02           O  
ANISOU 5820  OE2 GLU A 165    12559   8678   8787    552    173   -380       O  
ATOM   5821  N   GLN A 166      40.178  55.326   2.667  1.00 74.93           N  
ANISOU 5821  N   GLN A 166    12793   7692   7986    247   -181   -562       N  
ATOM   5822  CA  GLN A 166      41.509  55.684   3.147  1.00 76.61           C  
ANISOU 5822  CA  GLN A 166    13153   7861   8096     78   -282   -579       C  
ATOM   5823  C   GLN A 166      42.458  55.998   1.998  1.00 75.07           C  
ANISOU 5823  C   GLN A 166    12940   7672   7911   -137   -430   -466       C  
ATOM   5824  O   GLN A 166      42.527  55.259   1.012  1.00 75.92           O  
ANISOU 5824  O   GLN A 166    12856   7931   8060   -209   -416   -378       O  
ATOM   5825  CB  GLN A 166      42.074  54.548   4.000  1.00 77.92           C  
ANISOU 5825  CB  GLN A 166    13243   8193   8171     32   -191   -613       C  
ATOM   5826  CG  GLN A 166      43.376  54.890   4.696  1.00 80.78           C  
ANISOU 5826  CG  GLN A 166    13759   8513   8419   -121   -282   -643       C  
ATOM   5827  CD  GLN A 166      43.758  53.863   5.738  1.00 82.68           C  
ANISOU 5827  CD  GLN A 166    13952   8891   8572   -130   -190   -691       C  
ATOM   5828  OE1 GLN A 166      43.443  52.682   5.602  1.00 90.39           O  
ANISOU 5828  OE1 GLN A 166    14738  10031   9574   -100    -93   -661       O  
ATOM   5829  NE2 GLN A 166      44.434  54.308   6.791  1.00 85.48           N  
ANISOU 5829  NE2 GLN A 166    14485   9171   8821   -176   -231   -762       N  
ATOM   5830  N   ASP A 167      43.187  57.106   2.135  1.00 76.42           N  
ANISOU 5830  N   ASP A 167    13314   7683   8040   -244   -576   -468       N  
ATOM   5831  CA  ASP A 167      44.137  57.519   1.110  1.00 78.06           C  
ANISOU 5831  CA  ASP A 167    13519   7901   8240   -469   -729   -352       C  
ATOM   5832  C   ASP A 167      45.242  56.481   0.958  1.00 76.43           C  
ANISOU 5832  C   ASP A 167    13159   7923   7959   -640   -710   -308       C  
ATOM   5833  O   ASP A 167      45.731  55.917   1.940  1.00 75.23           O  
ANISOU 5833  O   ASP A 167    13018   7835   7729   -643   -652   -374       O  
ATOM   5834  CB  ASP A 167      44.732  58.883   1.461  1.00 81.52           C  
ANISOU 5834  CB  ASP A 167    14220   8119   8637   -559   -898   -365       C  
ATOM   5835  CG  ASP A 167      45.693  59.390   0.404  1.00 82.30           C  
ANISOU 5835  CG  ASP A 167    14318   8231   8720   -810  -1067   -228       C  
ATOM   5836  OD1 ASP A 167      46.913  59.174   0.557  1.00 81.64           O  
ANISOU 5836  OD1 ASP A 167    14227   8251   8540  -1000  -1119   -197       O  
ATOM   5837  OD2 ASP A 167      45.229  60.004  -0.581  1.00 84.21           O  
ANISOU 5837  OD2 ASP A 167    14561   8392   9042   -821  -1151   -146       O  
ATOM   5838  N   SER A 168      45.641  56.236  -0.288  1.00 77.12           N  
ANISOU 5838  N   SER A 168    13098   8136   8067   -779   -764   -197       N  
ATOM   5839  CA  SER A 168      46.532  55.125  -0.589  1.00 77.59           C  
ANISOU 5839  CA  SER A 168    12971   8438   8072   -904   -732   -164       C  
ATOM   5840  C   SER A 168      47.994  55.405  -0.264  1.00 76.77           C  
ANISOU 5840  C   SER A 168    12943   8370   7857  -1110   -838   -147       C  
ATOM   5841  O   SER A 168      48.791  54.460  -0.247  1.00 73.15           O  
ANISOU 5841  O   SER A 168    12344   8106   7345  -1190   -807   -146       O  
ATOM   5842  CB  SER A 168      46.401  54.733  -2.064  1.00 76.93           C  
ANISOU 5842  CB  SER A 168    12691   8498   8040   -967   -744    -65       C  
ATOM   5843  OG  SER A 168      46.970  55.719  -2.908  1.00 82.34           O  
ANISOU 5843  OG  SER A 168    13440   9138   8707  -1144   -898     35       O  
ATOM   5844  N   LYS A 169      48.378  56.655   0.003  1.00 81.09           N  
ANISOU 5844  N   LYS A 169    13706   8735   8371  -1197   -972   -134       N  
ATOM   5845  CA  LYS A 169      49.784  56.947   0.247  1.00 87.62           C  
ANISOU 5845  CA  LYS A 169    14597   9605   9090  -1413  -1085   -101       C  
ATOM   5846  C   LYS A 169      50.082  57.538   1.618  1.00 83.00           C  
ANISOU 5846  C   LYS A 169    14246   8851   8441  -1396  -1122   -189       C  
ATOM   5847  O   LYS A 169      51.172  57.301   2.144  1.00 83.65           O  
ANISOU 5847  O   LYS A 169    14337   9019   8429  -1528  -1158   -194       O  
ATOM   5848  CB  LYS A 169      50.337  57.878  -0.841  1.00 98.01           C  
ANISOU 5848  CB  LYS A 169    15942  10902  10397  -1620  -1253     31       C  
ATOM   5849  CG  LYS A 169      51.860  57.789  -1.006  1.00107.29           C  
ANISOU 5849  CG  LYS A 169    17061  12247  11459  -1873  -1347     99       C  
ATOM   5850  CD  LYS A 169      52.383  56.344  -0.869  1.00113.87           C  
ANISOU 5850  CD  LYS A 169    17669  13346  12252  -1860  -1226     58       C  
ATOM   5851  CE  LYS A 169      51.854  55.396  -1.954  1.00114.66           C  
ANISOU 5851  CE  LYS A 169    17520  13633  12414  -1791  -1130     85       C  
ATOM   5852  NZ  LYS A 169      51.719  54.002  -1.432  1.00111.14           N  
ANISOU 5852  NZ  LYS A 169    16926  13325  11979  -1655   -985     -6       N  
ATOM   5853  N   ASP A 170      49.162  58.294   2.222  1.00 80.48           N  
ANISOU 5853  N   ASP A 170    14114   8301   8164  -1233  -1117   -266       N  
ATOM   5854  CA  ASP A 170      49.385  58.783   3.576  1.00 79.65           C  
ANISOU 5854  CA  ASP A 170    14229   8046   7988  -1197  -1139   -370       C  
ATOM   5855  C   ASP A 170      48.435  58.197   4.609  1.00 75.45           C  
ANISOU 5855  C   ASP A 170    13699   7503   7464   -955   -968   -502       C  
ATOM   5856  O   ASP A 170      48.619  58.457   5.804  1.00 76.91           O  
ANISOU 5856  O   ASP A 170    14050   7599   7575   -918   -967   -599       O  
ATOM   5857  CB  ASP A 170      49.325  60.323   3.624  1.00 82.53           C  
ANISOU 5857  CB  ASP A 170    14860   8132   8363  -1229  -1309   -368       C  
ATOM   5858  CG  ASP A 170      47.942  60.890   3.313  1.00 84.83           C  
ANISOU 5858  CG  ASP A 170    15209   8253   8771  -1019  -1286   -403       C  
ATOM   5859  OD1 ASP A 170      46.941  60.147   3.318  1.00 83.94           O  
ANISOU 5859  OD1 ASP A 170    14955   8221   8717   -825  -1121   -451       O  
ATOM   5860  OD2 ASP A 170      47.858  62.114   3.077  1.00 88.00           O  
ANISOU 5860  OD2 ASP A 170    15801   8429   9204  -1051  -1445   -380       O  
ATOM   5861  N   SER A 171      47.419  57.441   4.186  1.00 71.29           N  
ANISOU 5861  N   SER A 171    12996   7071   7020   -799   -831   -504       N  
ATOM   5862  CA  SER A 171      46.565  56.654   5.075  1.00 69.77           C  
ANISOU 5862  CA  SER A 171    12750   6931   6827   -598   -658   -604       C  
ATOM   5863  C   SER A 171      45.683  57.517   5.976  1.00 71.47           C  
ANISOU 5863  C   SER A 171    13168   6943   7043   -409   -635   -723       C  
ATOM   5864  O   SER A 171      45.433  57.157   7.128  1.00 73.87           O  
ANISOU 5864  O   SER A 171    13516   7270   7283   -302   -533   -824       O  
ATOM   5865  CB  SER A 171      47.393  55.685   5.929  1.00 68.31           C  
ANISOU 5865  CB  SER A 171    12510   6900   6546   -670   -604   -633       C  
ATOM   5866  OG  SER A 171      48.365  55.010   5.149  1.00 67.40           O  
ANISOU 5866  OG  SER A 171    12227   6961   6420   -848   -649   -538       O  
ATOM   5867  N   THR A 172      45.189  58.647   5.479  1.00 73.44           N  
ANISOU 5867  N   THR A 172    13544   7001   7361   -359   -730   -716       N  
ATOM   5868  CA  THR A 172      44.248  59.464   6.234  1.00 75.88           C  
ANISOU 5868  CA  THR A 172    14030   7118   7684   -147   -708   -842       C  
ATOM   5869  C   THR A 172      42.869  59.413   5.584  1.00 74.78           C  
ANISOU 5869  C   THR A 172    13772   6973   7668     50   -624   -835       C  
ATOM   5870  O   THR A 172      42.656  58.761   4.557  1.00 73.66           O  
ANISOU 5870  O   THR A 172    13424   6966   7600     11   -588   -730       O  
ATOM   5871  CB  THR A 172      44.730  60.913   6.350  1.00 79.22           C  
ANISOU 5871  CB  THR A 172    14729   7282   8089   -219   -906   -864       C  
ATOM   5872  OG1 THR A 172      44.712  61.534   5.059  1.00 83.92           O  
ANISOU 5872  OG1 THR A 172    15311   7795   8780   -308  -1040   -743       O  
ATOM   5873  CG2 THR A 172      46.135  60.973   6.927  1.00 79.23           C  
ANISOU 5873  CG2 THR A 172    14839   7298   7968   -435  -1002   -854       C  
ATOM   5874  N   TYR A 173      41.927  60.118   6.205  1.00 75.13           N  
ANISOU 5874  N   TYR A 173    13949   6863   7734    268   -595   -955       N  
ATOM   5875  CA  TYR A 173      40.556  60.222   5.736  1.00 74.58           C  
ANISOU 5875  CA  TYR A 173    13790   6768   7779    481   -521   -967       C  
ATOM   5876  C   TYR A 173      40.187  61.685   5.534  1.00 76.69           C  
ANISOU 5876  C   TYR A 173    14272   6754   8114    568   -674  -1009       C  
ATOM   5877  O   TYR A 173      40.841  62.592   6.056  1.00 78.82           O  
ANISOU 5877  O   TYR A 173    14782   6842   8326    507   -810  -1067       O  
ATOM   5878  CB  TYR A 173      39.572  59.593   6.730  1.00 74.91           C  
ANISOU 5878  CB  TYR A 173    13754   6921   7786    707   -319  -1084       C  
ATOM   5879  CG  TYR A 173      39.781  58.118   6.953  1.00 73.57           C  
ANISOU 5879  CG  TYR A 173    13373   7016   7563    639   -175  -1038       C  
ATOM   5880  CD1 TYR A 173      39.066  57.183   6.221  1.00 74.07           C  
ANISOU 5880  CD1 TYR A 173    13189   7244   7709    682    -70   -955       C  
ATOM   5881  CD2 TYR A 173      40.690  57.659   7.897  1.00 73.75           C  
ANISOU 5881  CD2 TYR A 173    13451   7115   7457    530   -156  -1077       C  
ATOM   5882  CE1 TYR A 173      39.249  55.833   6.418  1.00 72.76           C  
ANISOU 5882  CE1 TYR A 173    12842   7300   7502    621     41   -913       C  
ATOM   5883  CE2 TYR A 173      40.882  56.307   8.102  1.00 73.22           C  
ANISOU 5883  CE2 TYR A 173    13197   7272   7349    471    -43  -1032       C  
ATOM   5884  CZ  TYR A 173      40.156  55.400   7.358  1.00 72.16           C  
ANISOU 5884  CZ  TYR A 173    12826   7288   7304    518     52   -952       C  
ATOM   5885  OH  TYR A 173      40.334  54.052   7.546  1.00 69.57           O  
ANISOU 5885  OH  TYR A 173    12324   7166   6944    459    145   -907       O  
ATOM   5886  N   SER A 174      39.121  61.900   4.769  1.00 77.96           N  
ANISOU 5886  N   SER A 174    14345   6874   8401    712   -660   -978       N  
ATOM   5887  CA  SER A 174      38.489  63.203   4.637  1.00 79.30           C  
ANISOU 5887  CA  SER A 174    14697   6778   8654    858   -784  -1036       C  
ATOM   5888  C   SER A 174      36.984  63.029   4.778  1.00 81.08           C  
ANISOU 5888  C   SER A 174    14805   7046   8958   1154   -633  -1115       C  
ATOM   5889  O   SER A 174      36.419  62.025   4.337  1.00 82.88           O  
ANISOU 5889  O   SER A 174    14783   7482   9224   1185   -490  -1047       O  
ATOM   5890  CB  SER A 174      38.833  63.872   3.297  1.00 78.26           C  
ANISOU 5890  CB  SER A 174    14594   6522   8618    693   -983   -881       C  
ATOM   5891  OG  SER A 174      40.225  64.116   3.193  1.00 77.00           O  
ANISOU 5891  OG  SER A 174    14545   6331   8379    415  -1131   -806       O  
ATOM   5892  N   LEU A 175      36.339  64.012   5.405  1.00 83.98           N  
ANISOU 5892  N   LEU A 175    15351   7215   9344   1375   -669  -1263       N  
ATOM   5893  CA  LEU A 175      34.936  63.894   5.777  1.00 84.87           C  
ANISOU 5893  CA  LEU A 175    15362   7383   9503   1679   -513  -1370       C  
ATOM   5894  C   LEU A 175      34.174  65.151   5.380  1.00 86.68           C  
ANISOU 5894  C   LEU A 175    15726   7349   9859   1864   -651  -1421       C  
ATOM   5895  O   LEU A 175      34.694  66.266   5.479  1.00 87.75           O  
ANISOU 5895  O   LEU A 175    16121   7221   9998   1826   -849  -1465       O  
ATOM   5896  CB  LEU A 175      34.807  63.630   7.285  1.00 85.89           C  
ANISOU 5896  CB  LEU A 175    15544   7599   9490   1818   -362  -1548       C  
ATOM   5897  CG  LEU A 175      33.458  63.314   7.961  1.00 87.09           C  
ANISOU 5897  CG  LEU A 175    15567   7885   9636   2118   -158  -1674       C  
ATOM   5898  CD1 LEU A 175      33.763  62.736   9.329  1.00 86.50           C  
ANISOU 5898  CD1 LEU A 175    15516   7965   9385   2127    -15  -1787       C  
ATOM   5899  CD2 LEU A 175      32.539  64.530   8.112  1.00 89.70           C  
ANISOU 5899  CD2 LEU A 175    16040   7999  10044   2399   -224  -1818       C  
ATOM   5900  N   SER A 176      32.934  64.955   4.938  1.00 86.73           N  
ANISOU 5900  N   SER A 176    15555   7426   9973   2064   -556  -1411       N  
ATOM   5901  CA  SER A 176      32.037  66.034   4.550  1.00 89.07           C  
ANISOU 5901  CA  SER A 176    15940   7498  10404   2277   -668  -1462       C  
ATOM   5902  C   SER A 176      30.743  65.918   5.340  1.00 90.26           C  
ANISOU 5902  C   SER A 176    15996   7746  10554   2615   -482  -1625       C  
ATOM   5903  O   SER A 176      30.166  64.832   5.434  1.00 89.60           O  
ANISOU 5903  O   SER A 176    15660   7938  10447   2662   -275  -1593       O  
ATOM   5904  CB  SER A 176      31.744  65.992   3.046  1.00 88.82           C  
ANISOU 5904  CB  SER A 176    15768   7457  10522   2185   -757  -1268       C  
ATOM   5905  OG  SER A 176      30.369  66.223   2.785  1.00 90.61           O  
ANISOU 5905  OG  SER A 176    15888   7668  10872   2458   -706  -1307       O  
ATOM   5906  N   SER A 177      30.294  67.028   5.914  1.00 92.99           N  
ANISOU 5906  N   SER A 177    16541   7871  10921   2850   -562  -1801       N  
ATOM   5907  CA  SER A 177      29.007  67.091   6.595  1.00 93.60           C  
ANISOU 5907  CA  SER A 177    16531   8027  11004   3199   -405  -1969       C  
ATOM   5908  C   SER A 177      28.233  68.268   6.028  1.00 97.22           C  
ANISOU 5908  C   SER A 177    17090   8220  11629   3413   -569  -2014       C  
ATOM   5909  O   SER A 177      28.684  69.411   6.130  1.00 97.61           O  
ANISOU 5909  O   SER A 177    17423   7962  11703   3423   -784  -2091       O  
ATOM   5910  CB  SER A 177      29.181  67.240   8.105  1.00 93.15           C  
ANISOU 5910  CB  SER A 177    16620   7993  10778   3323   -313  -2191       C  
ATOM   5911  OG  SER A 177      27.931  67.159   8.765  1.00 93.26           O  
ANISOU 5911  OG  SER A 177    16509   8149  10778   3649   -132  -2345       O  
ATOM   5912  N   THR A 178      27.073  67.998   5.434  1.00 98.66           N  
ANISOU 5912  N   THR A 178    17044   8514  11930   3580   -482  -1964       N  
ATOM   5913  CA  THR A 178      26.339  69.035   4.715  1.00100.94           C  
ANISOU 5913  CA  THR A 178    17399   8556  12398   3761   -653  -1971       C  
ATOM   5914  C   THR A 178      24.951  69.199   5.328  1.00103.21           C  
ANISOU 5914  C   THR A 178    17575   8928  12712   4157   -506  -2152       C  
ATOM   5915  O   THR A 178      24.154  68.259   5.383  1.00100.73           O  
ANISOU 5915  O   THR A 178    16976   8915  12383   4241   -284  -2120       O  
ATOM   5916  CB  THR A 178      26.294  68.737   3.209  1.00 99.55           C  
ANISOU 5916  CB  THR A 178    17070   8392  12362   3575   -741  -1718       C  
ATOM   5917  OG1 THR A 178      25.875  69.908   2.495  1.00101.49           O  
ANISOU 5917  OG1 THR A 178    17449   8336  12776   3690   -971  -1708       O  
ATOM   5918  CG2 THR A 178      25.401  67.552   2.855  1.00 98.41           C  
ANISOU 5918  CG2 THR A 178    16571   8578  12241   3622   -516  -1622       C  
ATOM   5919  N   LEU A 179      24.682  70.383   5.840  1.00106.99           N  
ANISOU 5919  N   LEU A 179    18280   9149  13222   4401   -630  -2349       N  
ATOM   5920  CA  LEU A 179      23.393  70.639   6.443  1.00109.95           C  
ANISOU 5920  CA  LEU A 179    18492   9661  13624   4729   -495  -2507       C  
ATOM   5921  C   LEU A 179      22.474  71.257   5.391  1.00111.23           C  
ANISOU 5921  C   LEU A 179    18567   9690  14006   4866   -624  -2429       C  
ATOM   5922  O   LEU A 179      22.899  72.051   4.539  1.00110.08           O  
ANISOU 5922  O   LEU A 179    18580   9261  13985   4739   -883  -2325       O  
ATOM   5923  CB  LEU A 179      23.545  71.517   7.696  1.00113.06           C  
ANISOU 5923  CB  LEU A 179    19044   9990  13924   4828   -520  -2727       C  
ATOM   5924  CG  LEU A 179      22.227  71.741   8.495  1.00115.16           C  
ANISOU 5924  CG  LEU A 179    19131  10438  14187   5167   -354  -2914       C  
ATOM   5925  CD1 LEU A 179      22.246  71.425  10.041  1.00116.46           C  
ANISOU 5925  CD1 LEU A 179    19275  10837  14138   5246   -147  -3106       C  
ATOM   5926  CD2 LEU A 179      21.702  73.136   8.210  1.00117.90           C  
ANISOU 5926  CD2 LEU A 179    19577  10523  14698   5331   -562  -2985       C  
ATOM   5927  N   THR A 180      21.215  70.821   5.414  1.00113.20           N  
ANISOU 5927  N   THR A 180    18544  10167  14299   5106   -441  -2459       N  
ATOM   5928  CA  THR A 180      20.226  71.181   4.402  1.00115.82           C  
ANISOU 5928  CA  THR A 180    18738  10433  14835   5244   -524  -2369       C  
ATOM   5929  C   THR A 180      19.068  71.872   5.106  1.00119.88           C  
ANISOU 5929  C   THR A 180    19149  11011  15387   5564   -457  -2561       C  
ATOM   5930  O   THR A 180      18.435  71.284   5.990  1.00119.20           O  
ANISOU 5930  O   THR A 180    18879  11222  15189   5722   -210  -2677       O  
ATOM   5931  CB  THR A 180      19.738  69.943   3.626  1.00114.96           C  
ANISOU 5931  CB  THR A 180    18367  10554  14758   5224   -372  -2196       C  
ATOM   5932  OG1 THR A 180      20.822  69.364   2.890  1.00110.99           O  
ANISOU 5932  OG1 THR A 180    17884  10055  14232   4821   -442  -1974       O  
ATOM   5933  CG2 THR A 180      18.608  70.295   2.646  1.00116.71           C  
ANISOU 5933  CG2 THR A 180    18418  10738  15188   5383   -445  -2108       C  
ATOM   5934  N   LEU A 181      18.821  73.128   4.748  1.00123.61           N  
ANISOU 5934  N   LEU A 181    19747  11211  16008   5649   -680  -2596       N  
ATOM   5935  CA  LEU A 181      17.609  73.818   5.155  1.00126.79           C  
ANISOU 5935  CA  LEU A 181    20035  11652  16487   5964   -642  -2752       C  
ATOM   5936  C   LEU A 181      16.992  74.427   3.909  1.00127.33           C  
ANISOU 5936  C   LEU A 181    20059  11532  16787   6015   -832  -2621       C  
ATOM   5937  O   LEU A 181      17.614  74.476   2.848  1.00125.35           O  
ANISOU 5937  O   LEU A 181    19911  11093  16623   5794  -1017  -2427       O  
ATOM   5938  CB  LEU A 181      17.880  74.893   6.218  1.00130.45           C  
ANISOU 5938  CB  LEU A 181    20717  11964  16884   6060   -725  -2976       C  
ATOM   5939  CG  LEU A 181      18.328  74.457   7.616  1.00130.58           C  
ANISOU 5939  CG  LEU A 181    20771  12174  16669   6054   -537  -3141       C  
ATOM   5940  CD1 LEU A 181      18.706  75.670   8.454  1.00133.36           C  
ANISOU 5940  CD1 LEU A 181    21379  12308  16983   6119   -683  -3334       C  
ATOM   5941  CD2 LEU A 181      17.251  73.639   8.319  1.00130.83           C  
ANISOU 5941  CD2 LEU A 181    20495  12601  16612   6267   -228  -3234       C  
ATOM   5942  N   SER A 182      15.754  74.876   4.029  1.00130.52           N  
ANISOU 5942  N   SER A 182    20303  12000  17289   6300   -786  -2720       N  
ATOM   5943  CA  SER A 182      15.154  75.606   2.927  1.00132.81           C  
ANISOU 5943  CA  SER A 182    20573  12087  17802   6362   -987  -2613       C  
ATOM   5944  C   SER A 182      15.334  77.104   3.140  1.00137.66           C  
ANISOU 5944  C   SER A 182    21446  12371  18487   6432  -1233  -2736       C  
ATOM   5945  O   SER A 182      15.586  77.571   4.252  1.00140.00           O  
ANISOU 5945  O   SER A 182    21877  12648  18670   6516  -1205  -2940       O  
ATOM   5946  CB  SER A 182      13.673  75.256   2.776  1.00133.88           C  
ANISOU 5946  CB  SER A 182    20376  12466  18025   6623   -820  -2622       C  
ATOM   5947  OG  SER A 182      13.518  74.096   1.973  1.00129.29           O  
ANISOU 5947  OG  SER A 182    19583  12077  17464   6508   -713  -2416       O  
ATOM   5948  N   LYS A 183      15.223  77.847   2.037  1.00138.58           N  
ANISOU 5948  N   LYS A 183    21635  12228  18793   6384  -1484  -2599       N  
ATOM   5949  CA  LYS A 183      15.363  79.299   1.975  1.00140.46           C  
ANISOU 5949  CA  LYS A 183    22116  12123  19129   6427  -1761  -2668       C  
ATOM   5950  C   LYS A 183      14.872  79.992   3.241  1.00142.48           C  
ANISOU 5950  C   LYS A 183    22413  12398  19323   6710  -1693  -2956       C  
ATOM   5951  O   LYS A 183      15.609  80.762   3.869  1.00141.78           O  
ANISOU 5951  O   LYS A 183    22589  12116  19165   6663  -1827  -3074       O  
ATOM   5952  CB  LYS A 183      14.597  79.826   0.757  1.00142.10           C  
ANISOU 5952  CB  LYS A 183    22243  12184  19563   6484  -1936  -2522       C  
ATOM   5953  CG  LYS A 183      14.673  81.324   0.530  1.00145.30           C  
ANISOU 5953  CG  LYS A 183    22889  12228  20090   6521  -2246  -2562       C  
ATOM   5954  CD  LYS A 183      15.797  81.676  -0.430  1.00143.24           C  
ANISOU 5954  CD  LYS A 183    22854  11702  19868   6168  -2524  -2344       C  
ATOM   5955  CE  LYS A 183      15.452  82.900  -1.266  1.00145.86           C  
ANISOU 5955  CE  LYS A 183    23297  11732  20390   6197  -2828  -2272       C  
ATOM   5956  NZ  LYS A 183      15.499  84.155  -0.469  1.00150.27           N  
ANISOU 5956  NZ  LYS A 183    24082  12066  20948   6352  -2982  -2484       N  
ATOM   5957  N   ALA A 184      13.631  79.692   3.630  1.00143.86           N  
ANISOU 5957  N   ALA A 184    22322  12823  19514   6999  -1482  -3067       N  
ATOM   5958  CA  ALA A 184      13.026  80.332   4.794  1.00148.74           C  
ANISOU 5958  CA  ALA A 184    22948  13490  20078   7290  -1405  -3342       C  
ATOM   5959  C   ALA A 184      13.814  80.038   6.065  1.00149.52           C  
ANISOU 5959  C   ALA A 184    23166  13699  19946   7228  -1272  -3500       C  
ATOM   5960  O   ALA A 184      14.282  80.957   6.748  1.00152.23           O  
ANISOU 5960  O   ALA A 184    23753  13845  20241   7261  -1404  -3657       O  
ATOM   5961  CB  ALA A 184      11.574  79.875   4.939  1.00149.24           C  
ANISOU 5961  CB  ALA A 184    22663  13858  20182   7576  -1174  -3404       C  
ATOM   5962  N   ASP A 185      13.971  78.752   6.401  1.00147.16           N  
ANISOU 5962  N   ASP A 185    22699  13715  19500   7134  -1017  -3455       N  
ATOM   5963  CA  ASP A 185      14.671  78.390   7.632  1.00147.07           C  
ANISOU 5963  CA  ASP A 185    22779  13838  19262   7072   -874  -3597       C  
ATOM   5964  C   ASP A 185      16.100  78.916   7.644  1.00146.15           C  
ANISOU 5964  C   ASP A 185    23008  13424  19097   6812  -1098  -3564       C  
ATOM   5965  O   ASP A 185      16.664  79.157   8.716  1.00149.22           O  
ANISOU 5965  O   ASP A 185    23554  13810  19334   6805  -1072  -3726       O  
ATOM   5966  CB  ASP A 185      14.670  76.875   7.819  1.00144.01           C  
ANISOU 5966  CB  ASP A 185    22159  13821  18736   6975   -589  -3513       C  
ATOM   5967  CG  ASP A 185      13.288  76.275   7.687  1.00144.18           C  
ANISOU 5967  CG  ASP A 185    21823  14151  18809   7192   -377  -3504       C  
ATOM   5968  OD1 ASP A 185      12.496  76.787   6.867  1.00146.91           O  
ANISOU 5968  OD1 ASP A 185    22083  14387  19348   7322   -488  -3447       O  
ATOM   5969  OD2 ASP A 185      12.992  75.289   8.398  1.00140.61           O  
ANISOU 5969  OD2 ASP A 185    21167  14055  18202   7223   -105  -3545       O  
ATOM   5970  N   TYR A 186      16.699  79.102   6.468  1.00143.02           N  
ANISOU 5970  N   TYR A 186    22729  12788  18822   6588  -1321  -3351       N  
ATOM   5971  CA  TYR A 186      18.061  79.614   6.395  1.00141.09           C  
ANISOU 5971  CA  TYR A 186    22802  12270  18536   6316  -1548  -3295       C  
ATOM   5972  C   TYR A 186      18.110  81.117   6.640  1.00144.75           C  
ANISOU 5972  C   TYR A 186    23510  12416  19072   6420  -1803  -3426       C  
ATOM   5973  O   TYR A 186      19.058  81.615   7.259  1.00145.29           O  
ANISOU 5973  O   TYR A 186    23829  12335  19040   6300  -1917  -3500       O  
ATOM   5974  CB  TYR A 186      18.676  79.275   5.037  1.00137.36           C  
ANISOU 5974  CB  TYR A 186    22356  11677  18158   6026  -1696  -3012       C  
ATOM   5975  CG  TYR A 186      20.087  79.779   4.865  1.00136.03           C  
ANISOU 5975  CG  TYR A 186    22493  11245  17946   5719  -1937  -2926       C  
ATOM   5976  CD1 TYR A 186      21.144  79.175   5.531  1.00133.86           C  
ANISOU 5976  CD1 TYR A 186    22315  11061  17484   5520  -1848  -2940       C  
ATOM   5977  CD2 TYR A 186      20.363  80.858   4.037  1.00136.75           C  
ANISOU 5977  CD2 TYR A 186    22769  11008  18181   5617  -2256  -2822       C  
ATOM   5978  CE1 TYR A 186      22.437  79.632   5.378  1.00132.70           C  
ANISOU 5978  CE1 TYR A 186    22434  10691  17295   5231  -2068  -2854       C  
ATOM   5979  CE2 TYR A 186      21.654  81.322   3.879  1.00135.39           C  
ANISOU 5979  CE2 TYR A 186    22863  10616  17961   5320  -2479  -2731       C  
ATOM   5980  CZ  TYR A 186      22.686  80.705   4.552  1.00133.09           C  
ANISOU 5980  CZ  TYR A 186    22657  10428  17484   5129  -2381  -2747       C  
ATOM   5981  OH  TYR A 186      23.975  81.157   4.397  1.00131.23           O  
ANISOU 5981  OH  TYR A 186    22672   9992  17199   4826  -2602  -2649       O  
ATOM   5982  N   GLU A 187      17.103  81.857   6.168  1.00146.51           N  
ANISOU 5982  N   GLU A 187    23666  12531  19469   6642  -1903  -3453       N  
ATOM   5983  CA  GLU A 187      17.110  83.301   6.375  1.00150.13           C  
ANISOU 5983  CA  GLU A 187    24360  12678  20003   6753  -2158  -3579       C  
ATOM   5984  C   GLU A 187      16.944  83.689   7.838  1.00152.79           C  
ANISOU 5984  C   GLU A 187    24762  13088  20203   6973  -2050  -3871       C  
ATOM   5985  O   GLU A 187      17.310  84.808   8.212  1.00155.99           O  
ANISOU 5985  O   GLU A 187    25421  13230  20617   7004  -2266  -3984       O  
ATOM   5986  CB  GLU A 187      16.008  83.968   5.548  1.00152.03           C  
ANISOU 5986  CB  GLU A 187    24502  12800  20463   6957  -2281  -3546       C  
ATOM   5987  CG  GLU A 187      16.166  83.836   4.040  1.00149.50           C  
ANISOU 5987  CG  GLU A 187    24154  12353  20297   6740  -2446  -3257       C  
ATOM   5988  CD  GLU A 187      17.354  84.603   3.478  1.00148.64           C  
ANISOU 5988  CD  GLU A 187    24356  11907  20216   6440  -2773  -3120       C  
ATOM   5989  OE1 GLU A 187      17.513  84.605   2.240  1.00146.37           O  
ANISOU 5989  OE1 GLU A 187    24062  11503  20048   6249  -2932  -2882       O  
ATOM   5990  OE2 GLU A 187      18.123  85.208   4.255  1.00149.24           O  
ANISOU 5990  OE2 GLU A 187    24674  11840  20190   6386  -2878  -3242       O  
ATOM   5991  N   LYS A 188      16.417  82.794   8.674  1.00144.17           N  
ANISOU 5991  N   LYS A 188    23449  12353  18978   7115  -1730  -3989       N  
ATOM   5992  CA  LYS A 188      16.027  83.194  10.019  1.00146.13           C  
ANISOU 5992  CA  LYS A 188    23717  12698  19107   7364  -1616  -4272       C  
ATOM   5993  C   LYS A 188      17.200  83.436  10.960  1.00149.49           C  
ANISOU 5993  C   LYS A 188    24408  13033  19359   7208  -1672  -4372       C  
ATOM   5994  O   LYS A 188      16.984  84.011  12.028  1.00151.62           O  
ANISOU 5994  O   LYS A 188    24754  13311  19544   7403  -1642  -4610       O  
ATOM   5995  CB  LYS A 188      15.086  82.156  10.631  1.00142.55           C  
ANISOU 5995  CB  LYS A 188    22932  12678  18554   7546  -1255  -4356       C  
ATOM   5996  CG  LYS A 188      13.675  82.234  10.084  1.00143.22           C  
ANISOU 5996  CG  LYS A 188    22759  12861  18798   7810  -1196  -4354       C  
ATOM   5997  CD  LYS A 188      13.085  80.859   9.851  1.00139.14           C  
ANISOU 5997  CD  LYS A 188    21900  12724  18242   7796   -911  -4237       C  
ATOM   5998  CE  LYS A 188      11.823  80.952   9.012  1.00140.19           C  
ANISOU 5998  CE  LYS A 188    21795  12904  18568   7995   -907  -4170       C  
ATOM   5999  NZ  LYS A 188      10.939  82.055   9.477  1.00147.21           N  
ANISOU 5999  NZ  LYS A 188    22700  13705  19529   8324   -972  -4388       N  
ATOM   6000  N   HIS A 189      18.426  83.038  10.622  1.00150.93           N  
ANISOU 6000  N   HIS A 189    24731  13132  19482   6869  -1753  -4202       N  
ATOM   6001  CA  HIS A 189      19.494  83.326  11.567  1.00155.07           C  
ANISOU 6001  CA  HIS A 189    25503  13573  19843   6736  -1811  -4304       C  
ATOM   6002  C   HIS A 189      20.842  83.522  10.892  1.00148.06           C  
ANISOU 6002  C   HIS A 189    24856  12429  18971   6373  -2058  -4104       C  
ATOM   6003  O   HIS A 189      21.044  83.194   9.721  1.00142.55           O  
ANISOU 6003  O   HIS A 189    24112  11673  18379   6189  -2141  -3872       O  
ATOM   6004  CB  HIS A 189      19.583  82.259  12.644  1.00159.98           C  
ANISOU 6004  CB  HIS A 189    25988  14550  20248   6736  -1496  -4401       C  
ATOM   6005  CG  HIS A 189      19.721  82.840  14.019  1.00169.85           C  
ANISOU 6005  CG  HIS A 189    27382  15801  21353   6869  -1472  -4657       C  
ATOM   6006  ND1 HIS A 189      20.829  83.559  14.422  1.00172.38           N  
ANISOU 6006  ND1 HIS A 189    28015  15872  21611   6707  -1682  -4692       N  
ATOM   6007  CD2 HIS A 189      18.843  82.902  15.047  1.00175.36           C  
ANISOU 6007  CD2 HIS A 189    27956  16706  21966   7159  -1282  -4892       C  
ATOM   6008  CE1 HIS A 189      20.652  83.986  15.660  1.00176.13           C  
ANISOU 6008  CE1 HIS A 189    28555  16403  21963   6888  -1614  -4939       C  
ATOM   6009  NE2 HIS A 189      19.459  83.590  16.066  1.00177.91           N  
ANISOU 6009  NE2 HIS A 189    28518  16909  22169   7162  -1368  -5066       N  
ATOM   6010  N   LYS A 190      21.778  84.021  11.701  1.00147.41           N  
ANISOU 6010  N   LYS A 190    25023  12219  18765   6266  -2163  -4198       N  
ATOM   6011  CA  LYS A 190      22.934  84.784  11.247  1.00144.57           C  
ANISOU 6011  CA  LYS A 190    24958  11534  18439   5996  -2481  -4074       C  
ATOM   6012  C   LYS A 190      24.213  83.951  11.187  1.00138.18           C  
ANISOU 6012  C   LYS A 190    24207  10797  17499   5634  -2449  -3910       C  
ATOM   6013  O   LYS A 190      24.868  83.889  10.142  1.00130.42           O  
ANISOU 6013  O   LYS A 190    23281   9683  16588   5367  -2612  -3677       O  
ATOM   6014  CB  LYS A 190      23.131  85.995  12.168  1.00145.11           C  
ANISOU 6014  CB  LYS A 190    25278  11390  18466   6119  -2651  -4286       C  
ATOM   6015  CG  LYS A 190      22.127  87.125  11.957  1.00146.83           C  
ANISOU 6015  CG  LYS A 190    25525  11415  18850   6414  -2807  -4406       C  
ATOM   6016  CD  LYS A 190      22.536  88.387  12.714  1.00145.98           C  
ANISOU 6016  CD  LYS A 190    25715  11040  18710   6479  -3036  -4579       C  
ATOM   6017  CE  LYS A 190      21.472  89.476  12.612  1.00150.57           C  
ANISOU 6017  CE  LYS A 190    26316  11447  19446   6806  -3175  -4728       C  
ATOM   6018  NZ  LYS A 190      21.790  90.682  13.434  1.00154.20           N  
ANISOU 6018  NZ  LYS A 190    27061  11660  19867   6904  -3386  -4924       N  
ATOM   6019  N   VAL A 191      24.593  83.325  12.298  1.00141.19           N  
ANISOU 6019  N   VAL A 191    24574  11388  17685   5617  -2246  -4027       N  
ATOM   6020  CA  VAL A 191      25.887  82.661  12.421  1.00143.73           C  
ANISOU 6020  CA  VAL A 191    24985  11759  17868   5283  -2235  -3901       C  
ATOM   6021  C   VAL A 191      25.687  81.153  12.336  1.00139.05           C  
ANISOU 6021  C   VAL A 191    24127  11507  17198   5236  -1933  -3821       C  
ATOM   6022  O   VAL A 191      24.834  80.589  13.032  1.00140.00           O  
ANISOU 6022  O   VAL A 191    24049  11895  17248   5462  -1670  -3964       O  
ATOM   6023  CB  VAL A 191      26.607  83.061  13.723  1.00148.40           C  
ANISOU 6023  CB  VAL A 191    25778  12320  18289   5258  -2254  -4070       C  
ATOM   6024  CG1 VAL A 191      25.689  82.913  14.927  1.00150.51           C  
ANISOU 6024  CG1 VAL A 191    25917  12813  18457   5574  -2008  -4333       C  
ATOM   6025  CG2 VAL A 191      27.879  82.243  13.904  1.00146.08           C  
ANISOU 6025  CG2 VAL A 191    25539  12121  17843   4924  -2207  -3942       C  
ATOM   6026  N   TYR A 192      26.477  80.504  11.483  1.00135.19           N  
ANISOU 6026  N   TYR A 192    23634  11016  16717   4939  -1976  -3589       N  
ATOM   6027  CA  TYR A 192      26.396  79.065  11.247  1.00133.95           C  
ANISOU 6027  CA  TYR A 192    23245  11152  16497   4861  -1726  -3483       C  
ATOM   6028  C   TYR A 192      27.720  78.426  11.661  1.00129.96           C  
ANISOU 6028  C   TYR A 192    22844  10712  15822   4560  -1699  -3413       C  
ATOM   6029  O   TYR A 192      28.775  78.777  11.113  1.00129.04           O  
ANISOU 6029  O   TYR A 192    22910  10397  15724   4283  -1920  -3264       O  
ATOM   6030  CB  TYR A 192      26.063  78.789   9.778  1.00129.71           C  
ANISOU 6030  CB  TYR A 192    22584  10569  16130   4792  -1791  -3268       C  
ATOM   6031  CG  TYR A 192      24.604  79.028   9.446  1.00127.33           C  
ANISOU 6031  CG  TYR A 192    22095  10310  15976   5108  -1728  -3333       C  
ATOM   6032  CD1 TYR A 192      24.142  80.296   9.112  1.00131.47           C  
ANISOU 6032  CD1 TYR A 192    22729  10572  16651   5247  -1953  -3380       C  
ATOM   6033  CD2 TYR A 192      23.688  77.987   9.480  1.00121.35           C  
ANISOU 6033  CD2 TYR A 192    21046   9860  15202   5264  -1448  -3346       C  
ATOM   6034  CE1 TYR A 192      22.806  80.517   8.817  1.00134.00           C  
ANISOU 6034  CE1 TYR A 192    22871  10936  17107   5538  -1897  -3440       C  
ATOM   6035  CE2 TYR A 192      22.354  78.196   9.181  1.00124.33           C  
ANISOU 6035  CE2 TYR A 192    21236  10292  15711   5547  -1389  -3398       C  
ATOM   6036  CZ  TYR A 192      21.918  79.462   8.856  1.00131.97           C  
ANISOU 6036  CZ  TYR A 192    22316  10996  16832   5686  -1612  -3448       C  
ATOM   6037  OH  TYR A 192      20.590  79.672   8.564  1.00135.65           O  
ANISOU 6037  OH  TYR A 192    22591  11519  17429   5968  -1555  -3500       O  
ATOM   6038  N   ALA A 193      27.667  77.494  12.624  1.00128.86           N  
ANISOU 6038  N   ALA A 193    22585  10861  15514   4604  -1433  -3511       N  
ATOM   6039  CA  ALA A 193      28.858  76.872  13.199  1.00130.82           C  
ANISOU 6039  CA  ALA A 193    22922  11195  15587   4346  -1387  -3471       C  
ATOM   6040  C   ALA A 193      28.899  75.366  12.918  1.00133.37           C  
ANISOU 6040  C   ALA A 193    23032  11800  15841   4238  -1158  -3350       C  
ATOM   6041  O   ALA A 193      27.946  74.647  13.262  1.00135.41           O  
ANISOU 6041  O   ALA A 193    23063  12322  16065   4436   -909  -3424       O  
ATOM   6042  CB  ALA A 193      28.892  77.154  14.707  1.00131.14           C  
ANISOU 6042  CB  ALA A 193    23041  11318  15469   4468  -1298  -3699       C  
ATOM   6043  N   CYS A 194      30.006  74.890  12.305  1.00134.06           N  
ANISOU 6043  N   CYS A 194    23191  11840  15904   3919  -1243  -3161       N  
ATOM   6044  CA  CYS A 194      30.293  73.459  12.141  1.00134.45           C  
ANISOU 6044  CA  CYS A 194    23082  12139  15864   3776  -1047  -3049       C  
ATOM   6045  C   CYS A 194      31.539  73.048  12.906  1.00133.26           C  
ANISOU 6045  C   CYS A 194    23051  12048  15533   3532  -1034  -3043       C  
ATOM   6046  O   CYS A 194      32.659  73.498  12.580  1.00132.02           O  
ANISOU 6046  O   CYS A 194    23085  11699  15377   3276  -1247  -2939       O  
ATOM   6047  CB  CYS A 194      30.524  73.063  10.697  1.00138.92           C  
ANISOU 6047  CB  CYS A 194    23597  12636  16552   3599  -1136  -2821       C  
ATOM   6048  SG  CYS A 194      31.138  71.392  10.632  1.00144.45           S  
ANISOU 6048  SG  CYS A 194    24159  13609  17118   3388   -929  -2700       S  
ATOM   6049  N   GLU A 195      31.350  72.167  13.894  1.00136.09           N  
ANISOU 6049  N   GLU A 195    23286  12687  15734   3597   -786  -3140       N  
ATOM   6050  CA  GLU A 195      32.361  71.959  14.922  1.00138.06           C  
ANISOU 6050  CA  GLU A 195    23653  12999  15803   3428   -767  -3186       C  
ATOM   6051  C   GLU A 195      32.504  70.510  15.291  1.00139.49           C  
ANISOU 6051  C   GLU A 195    23665  13490  15844   3342   -526  -3142       C  
ATOM   6052  O   GLU A 195      31.526  69.792  15.488  1.00140.38           O  
ANISOU 6052  O   GLU A 195    23561  13842  15934   3523   -302  -3188       O  
ATOM   6053  CB  GLU A 195      32.113  72.750  16.227  1.00142.10           C  
ANISOU 6053  CB  GLU A 195    24263  13497  16229   3604   -757  -3408       C  
ATOM   6054  CG  GLU A 195      31.781  74.235  16.046  1.00154.20           C  
ANISOU 6054  CG  GLU A 195    25957  14738  17894   3749   -978  -3494       C  
ATOM   6055  CD  GLU A 195      32.579  74.857  14.916  1.00155.36           C  
ANISOU 6055  CD  GLU A 195    26268  14596  18167   3526  -1261  -3316       C  
ATOM   6056  OE1 GLU A 195      33.648  74.330  14.518  1.00150.04           O  
ANISOU 6056  OE1 GLU A 195    25639  13923  17447   3229  -1316  -3153       O  
ATOM   6057  OE2 GLU A 195      32.148  75.926  14.369  1.00157.99           O  
ANISOU 6057  OE2 GLU A 195    26685  14694  18651   3637  -1447  -3329       O  
ATOM   6058  N   VAL A 196      33.743  70.107  15.458  1.00137.88           N  
ANISOU 6058  N   VAL A 196    23560  13289  15538   3061   -578  -3055       N  
ATOM   6059  CA  VAL A 196      34.028  68.679  15.484  1.00133.04           C  
ANISOU 6059  CA  VAL A 196    22794  12933  14820   2926   -392  -2962       C  
ATOM   6060  C   VAL A 196      35.071  68.388  16.553  1.00133.12           C  
ANISOU 6060  C   VAL A 196    22900  13030  14651   2741   -377  -2991       C  
ATOM   6061  O   VAL A 196      35.932  69.228  16.861  1.00135.27           O  
ANISOU 6061  O   VAL A 196    23380  13113  14903   2616   -564  -3009       O  
ATOM   6062  CB  VAL A 196      34.481  68.179  14.093  1.00127.51           C  
ANISOU 6062  CB  VAL A 196    22061  12166  14219   2729   -473  -2756       C  
ATOM   6063  CG1 VAL A 196      35.744  68.890  13.677  1.00123.33           C  
ANISOU 6063  CG1 VAL A 196    21752  11393  13716   2460   -737  -2658       C  
ATOM   6064  CG2 VAL A 196      34.653  66.673  14.061  1.00126.51           C  
ANISOU 6064  CG2 VAL A 196    21756  12313  13998   2614   -275  -2664       C  
ATOM   6065  N   THR A 197      34.930  67.220  17.174  1.00131.24           N  
ANISOU 6065  N   THR A 197    22502  13084  14281   2735   -152  -2998       N  
ATOM   6066  CA  THR A 197      35.940  66.651  18.049  1.00128.73           C  
ANISOU 6066  CA  THR A 197    22231  12887  13795   2528   -119  -2984       C  
ATOM   6067  C   THR A 197      36.655  65.526  17.317  1.00123.25           C  
ANISOU 6067  C   THR A 197    21456  12285  13088   2284    -95  -2800       C  
ATOM   6068  O   THR A 197      36.030  64.723  16.606  1.00121.65           O  
ANISOU 6068  O   THR A 197    21079  12206  12938   2340     28  -2726       O  
ATOM   6069  CB  THR A 197      35.334  66.115  19.351  1.00130.13           C  
ANISOU 6069  CB  THR A 197    22287  13338  13819   2669    105  -3114       C  
ATOM   6070  OG1 THR A 197      34.923  64.754  19.176  1.00129.49           O  
ANISOU 6070  OG1 THR A 197    21980  13528  13691   2658    311  -3027       O  
ATOM   6071  CG2 THR A 197      34.139  66.951  19.774  1.00133.33           C  
ANISOU 6071  CG2 THR A 197    22670  13726  14266   2983    152  -3292       C  
ATOM   6072  N   HIS A 198      37.972  65.488  17.500  1.00121.45           N  
ANISOU 6072  N   HIS A 198    21352  12002  12791   2016   -217  -2728       N  
ATOM   6073  CA  HIS A 198      38.820  64.451  16.945  1.00117.86           C  
ANISOU 6073  CA  HIS A 198    20830  11645  12306   1762   -209  -2566       C  
ATOM   6074  C   HIS A 198      39.976  64.193  17.899  1.00118.82           C  
ANISOU 6074  C   HIS A 198    21026  11838  12282   1552   -240  -2556       C  
ATOM   6075  O   HIS A 198      40.422  65.089  18.622  1.00119.60           O  
ANISOU 6075  O   HIS A 198    21289  11812  12340   1536   -354  -2634       O  
ATOM   6076  CB  HIS A 198      39.358  64.824  15.562  1.00114.09           C  
ANISOU 6076  CB  HIS A 198    20379  10989  11981   1591   -400  -2405       C  
ATOM   6077  CG  HIS A 198      40.221  63.764  14.955  1.00108.59           C  
ANISOU 6077  CG  HIS A 198    19496  10469  11294   1311   -388  -2196       C  
ATOM   6078  ND1 HIS A 198      41.583  63.906  14.808  1.00106.28           N  
ANISOU 6078  ND1 HIS A 198    19317  10100  10965   1033   -552  -2104       N  
ATOM   6079  CD2 HIS A 198      39.917  62.531  14.486  1.00102.99           C  
ANISOU 6079  CD2 HIS A 198    18492  10015  10624   1273   -235  -2069       C  
ATOM   6080  CE1 HIS A 198      42.080  62.811  14.260  1.00102.24           C  
ANISOU 6080  CE1 HIS A 198    18582   9794  10469    849   -496  -1937       C  
ATOM   6081  NE2 HIS A 198      41.090  61.962  14.055  1.00 99.58           N  
ANISOU 6081  NE2 HIS A 198    18004   9651  10181    990   -309  -1915       N  
ATOM   6082  N   GLN A 199      40.467  62.953  17.866  1.00117.13           N  
ANISOU 6082  N   GLN A 199    20687  11823  11995   1388   -145  -2453       N  
ATOM   6083  CA  GLN A 199      41.545  62.475  18.724  1.00116.35           C  
ANISOU 6083  CA  GLN A 199    20614  11831  11763   1182   -157  -2421       C  
ATOM   6084  C   GLN A 199      42.853  63.244  18.540  1.00116.65           C  
ANISOU 6084  C   GLN A 199    20833  11674  11816    950   -394  -2356       C  
ATOM   6085  O   GLN A 199      43.777  63.056  19.339  1.00118.07           O  
ANISOU 6085  O   GLN A 199    21056  11916  11892    792   -427  -2339       O  
ATOM   6086  CB  GLN A 199      41.742  60.981  18.440  1.00115.38           C  
ANISOU 6086  CB  GLN A 199    20252  11965  11622   1048    -30  -2277       C  
ATOM   6087  CG  GLN A 199      42.609  60.205  19.413  1.00115.94           C  
ANISOU 6087  CG  GLN A 199    20331  12188  11534    883