CNRS Nantes University UFIP UFIP
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***  TRANSFERASE 15-AUG-16 5LPW  ***

elNémo ID: 20061812334013039

Job options:

ID        	=	 20061812334013039
JOBID     	=	 TRANSFERASE 15-AUG-16 5LPW
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    TRANSFERASE                             15-AUG-16   5LPW              
TITLE     CRYSTAL STRUCTURE OF THE APO-BRI1 KINASE DOMAIN (865-1160)            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN BRASSINOSTEROID INSENSITIVE 1;                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: ATBRI1,BRASSINOSTEROID LRR RECEPTOR KINASE;                 
COMPND   5 EC: 2.7.10.1,2.7.11.1;                                               
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;                           
SOURCE   3 ORGANISM_COMMON: MOUSE-EAR CRESS;                                    
SOURCE   4 ORGANISM_TAXID: 3702;                                                
SOURCE   5 GENE: BRI1, AT4G39400, F23K16.30;                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: RIL;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PMH-HT                                    
KEYWDS    BRASSINOSTEROID RECEPTOR, KINASE DOMAIN, DUAL-SPECIFICIFY KINASE,     
KEYWDS   2 MEMBRANE RECEPTOR KINASE, PLASMA MEMBRANE, TRANSFERASE               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.BOJAR,J.MARTINEZ,M.HOTHORN                                          
REVDAT   1   24-AUG-16 5LPW    0                                                
SPRSDE     24-AUG-16 5LPW      4OA6                                             
JRNL        AUTH   D.BOJAR,J.MARTINEZ,J.SANTIAGO,V.RYBIN,R.BAYLISS,M.HOTHORN    
JRNL        TITL   CRYSTAL STRUCTURES OF THE PHOSPHORYLATED BRI1 KINASE DOMAIN  
JRNL        TITL 2 AND IMPLICATIONS FOR BRASSINOSTEROID SIGNAL INITIATION.      
JRNL        REF    PLANT J.                      V.  78    31 2014              
JRNL        REFN                   ESSN 1365-313X                               
JRNL        PMID   24461462                                                     
JRNL        DOI    10.1111/TPJ.12445                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.43 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.43                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.36                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.370                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 14555                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.206                           
REMARK   3   R VALUE            (WORKING SET) : 0.204                           
REMARK   3   FREE R VALUE                     : 0.248                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.060                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 736                             
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 19.3568 -  4.1458    1.00     2863   150  0.1710 0.2169        
REMARK   3     2  4.1458 -  3.2959    1.00     2822   148  0.2118 0.2401        
REMARK   3     3  3.2959 -  2.8808    1.00     2799   131  0.2387 0.2997        
REMARK   3     4  2.8808 -  2.6181    1.00     2772   153  0.2629 0.3135        
REMARK   3     5  2.6181 -  2.4308    0.93     2563   154  0.2984 0.3620        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.360            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.300           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 71.20                          
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      :  0.003           2215                                  
REMARK   3   ANGLE     :  0.661           3003                                  
REMARK   3   CHIRALITY :  0.023            339                                  
REMARK   3   PLANARITY :  0.003            380                                  
REMARK   3   DIHEDRAL  : 13.626            806                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 5                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (CHAIN A AND RESSEQ 866:969)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  30.6930  35.3646  18.1791              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5482 T22:   0.6499                                     
REMARK   3      T33:   0.6367 T12:   0.0921                                     
REMARK   3      T13:   0.0501 T23:  -0.0331                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.3422 L22:   8.0754                                     
REMARK   3      L33:   5.3715 L12:  -4.1537                                     
REMARK   3      L13:  -3.5648 L23:   4.6157                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2806 S12:  -0.4451 S13:   0.9936                       
REMARK   3      S21:  -0.4804 S22:   0.3464 S23:  -0.1636                       
REMARK   3      S31:  -0.5610 S32:   0.4053 S33:  -0.3988                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN A AND RESSEQ 970:1086)                          
REMARK   3    ORIGIN FOR THE GROUP (A):  42.8141  20.3291  15.5217              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5858 T22:   0.4024                                     
REMARK   3      T33:   0.4376 T12:   0.1105                                     
REMARK   3      T13:  -0.0296 T23:  -0.0659                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.4509 L22:   6.9928                                     
REMARK   3      L33:   4.0066 L12:  -0.0516                                     
REMARK   3      L13:  -0.8425 L23:   0.6476                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2149 S12:  -0.1978 S13:  -0.4993                       
REMARK   3      S21:   0.3216 S22:   0.3487 S23:  -0.2598                       
REMARK   3      S31:  -0.1550 S32:   0.1341 S33:  -0.1502                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (CHAIN A AND RESSEQ 1095:1116)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  53.1144  10.2192  30.3180              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4016 T22:   1.5142                                     
REMARK   3      T33:   1.4554 T12:   0.3000                                     
REMARK   3      T13:  -0.3070 T23:   0.6285                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1425 L22:   5.3940                                     
REMARK   3      L33:   1.6432 L12:   0.8727                                     
REMARK   3      L13:   0.0246 L23:   0.5336                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1232 S12:  -2.8678 S13:  -2.0446                       
REMARK   3      S21:   1.2942 S22:  -0.1702 S23:  -1.8412                       
REMARK   3      S31:   0.4380 S32:   1.3473 S33:   0.8508                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (CHAIN A AND RESSEQ 1117:1124)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  42.0663   2.5668  36.5397              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4821 T22:   1.7236                                     
REMARK   3      T33:   1.6009 T12:   0.0842                                     
REMARK   3      T13:  -0.2057 T23:   0.9421                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5651 L22:   3.5291                                     
REMARK   3      L33:   5.1830 L12:   0.4001                                     
REMARK   3      L13:   0.2807 L23:   0.4493                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2556 S12:  -2.1094 S13:  -2.0516                       
REMARK   3      S21:   0.2448 S22:   0.0677 S23:   0.4834                       
REMARK   3      S31:   1.5165 S32:   1.1161 S33:   0.2513                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: (CHAIN A AND RESSEQ 1125:1160)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  45.5910   6.2644  16.7338              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7952 T22:   0.6347                                     
REMARK   3      T33:   1.2440 T12:   0.1761                                     
REMARK   3      T13:   0.0403 T23:   0.1871                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4505 L22:   4.4340                                     
REMARK   3      L33:   3.7848 L12:   0.8189                                     
REMARK   3      L13:   3.4627 L23:   1.0552                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3692 S12:  -1.0583 S13:  -2.2363                       
REMARK   3      S21:   0.5688 S22:   0.2857 S23:  -0.5213                       
REMARK   3      S31:   0.1845 S32:  -0.0365 S33:   0.0841                       
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 5LPW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-AUG-16.                  
REMARK 100 THE DEPOSITION ID IS D_1200001181.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-AUG-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06DA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000040                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 2M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 14560                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.430                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.360                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY                : 14.01                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06200                            
REMARK 200   FOR THE DATA SET  : 28.5600                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.43                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.58                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 13.55                              
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.990                              
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: 3UIM                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.99                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.93                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 26% PEG 20K/MME 550 MORPHEUS MIX, 0.12   
REMARK 280  M ETH GLYCOL MIX, 0.1 M HEPES PH 7.5, VAPOR DIFFUSION, HANGING      
REMARK 280  DROP, TEMPERATURE 298.0K                                            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 62                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z                                                 
REMARK 290       5555   Y,-X+Y,Z+2/3                                            
REMARK 290       6555   X-Y,X,Z+1/3                                             
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       33.53000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       16.76500            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       33.53000            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       16.76500            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2                             
REMARK 350 SURFACE AREA OF THE COMPLEX: 13290 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     GLU A   865                                                      
REMARK 465     LYS A   972                                                      
REMARK 465     LYS A   973                                                      
REMARK 465     ALA A   974                                                      
REMARK 465     ASP A  1087                                                      
REMARK 465     SER A  1088                                                      
REMARK 465     PRO A  1089                                                      
REMARK 465     ASP A  1090                                                      
REMARK 465     PHE A  1091                                                      
REMARK 465     GLY A  1092                                                      
REMARK 465     ASP A  1093                                                      
REMARK 465     ASN A  1094                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 866    CG   CD   CE   NZ                                   
REMARK 470     PHE A 894    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     HIS A 915    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLN A 919    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 947    CG   CD   CE   NZ                                   
REMARK 470     ASP A 950    CG   OD1  OD2                                       
REMARK 470     LYS A 977    CG   CD   CE   NZ                                   
REMARK 470     ARG A1084    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A1101    CG   CD   CE   NZ                                   
REMARK 470     GLN A1102    CG   CD   OE1  NE2                                  
REMARK 470     HIS A1103    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS A1105    CG   CD   CE   NZ                                   
REMARK 470     LEU A1106    CG   CD1  CD2                                       
REMARK 470     ARG A1107    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE A1108    CG1  CG2  CD1                                       
REMARK 470     SER A1109    OG                                                  
REMARK 470     ASP A1110    CG   OD1  OD2                                       
REMARK 470     VAL A1111    CG1  CG2                                            
REMARK 470     GLU A1119    CG   CD   OE1  OE2                                  
REMARK 470     LEU A1128    CG   CD1  CD2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A  1208     O    HOH A  1210              2.12            
REMARK 500   O    HOH A  1202     O    HOH A  1205              2.12            
REMARK 500   OD2  ASP A   904     OG   SER A   906              2.18            
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    HIS A 915       63.63     60.21                                   
REMARK 500    THR A 930      -88.96   -117.68                                   
REMARK 500    HIS A 969       77.83   -112.23                                   
REMARK 500    ASP A1009       40.13   -154.17                                   
REMARK 500    ASP A1018     -164.75    -76.63                                   
REMARK 500    ASP A1027       79.85     60.56                                   
REMARK 500    LEU A1106     -118.48   -100.72                                   
REMARK 500    ASP A1110      -12.09   -157.49                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  5LPW A  865  1160  UNP    O22476   BRI1_ARATH     865   1160             
SEQADV 5LPW ALA A  872  UNP  O22476    THR   872 ENGINEERED MUTATION            
SEQRES   1 A  296  GLU LYS PRO LEU ARG LYS LEU ALA PHE ALA ASP LEU LEU          
SEQRES   2 A  296  GLN ALA THR ASN GLY PHE HIS ASN ASP SER LEU ILE GLY          
SEQRES   3 A  296  SER GLY GLY PHE GLY ASP VAL TYR LYS ALA ILE LEU LYS          
SEQRES   4 A  296  ASP GLY SER ALA VAL ALA ILE LYS LYS LEU ILE HIS VAL          
SEQRES   5 A  296  SER GLY GLN GLY ASP ARG GLU PHE MET ALA GLU MET GLU          
SEQRES   6 A  296  THR ILE GLY LYS ILE LYS HIS ARG ASN LEU VAL PRO LEU          
SEQRES   7 A  296  LEU GLY TYR CYS LYS VAL GLY ASP GLU ARG LEU LEU VAL          
SEQRES   8 A  296  TYR GLU PHE MET LYS TYR GLY SER LEU GLU ASP VAL LEU          
SEQRES   9 A  296  HIS ASP PRO LYS LYS ALA GLY VAL LYS LEU ASN TRP SER          
SEQRES  10 A  296  THR ARG ARG LYS ILE ALA ILE GLY SER ALA ARG GLY LEU          
SEQRES  11 A  296  ALA PHE LEU HIS HIS ASN CYS SER PRO HIS ILE ILE HIS          
SEQRES  12 A  296  ARG ASP MET LYS SER SER ASN VAL LEU LEU ASP GLU ASN          
SEQRES  13 A  296  LEU GLU ALA ARG VAL SER ASP PHE GLY MET ALA ARG LEU          
SEQRES  14 A  296  MET SER ALA MET ASP TPO HIS LEU SEP VAL SEP THR LEU          
SEQRES  15 A  296  ALA GLY THR PRO GLY TYR VAL PRO PRO GLU TYR TYR GLN          
SEQRES  16 A  296  SEP PHE ARG CYS SER THR LYS GLY ASP VAL TYR SER TYR          
SEQRES  17 A  296  GLY VAL VAL LEU LEU GLU LEU LEU THR GLY LYS ARG PRO          
SEQRES  18 A  296  THR ASP SER PRO ASP PHE GLY ASP ASN ASN LEU VAL GLY          
SEQRES  19 A  296  TRP VAL LYS GLN HIS ALA LYS LEU ARG ILE SER ASP VAL          
SEQRES  20 A  296  PHE ASP PRO GLU LEU MET LYS GLU ASP PRO ALA LEU GLU          
SEQRES  21 A  296  ILE GLU LEU LEU GLN HIS LEU LYS VAL ALA VAL ALA CYS          
SEQRES  22 A  296  LEU ASP ASP ARG ALA TRP ARG ARG PRO THR MET VAL GLN          
SEQRES  23 A  296  VAL MET ALA MET PHE LYS GLU ILE GLN ALA                      
MODRES 5LPW TPO A 1039  THR  MODIFIED RESIDUE                                   
MODRES 5LPW SEP A 1042  SER  MODIFIED RESIDUE                                   
MODRES 5LPW SEP A 1044  SER  MODIFIED RESIDUE                                   
MODRES 5LPW SEP A 1060  SER  MODIFIED RESIDUE                                   
HET    TPO  A1039      11                                                       
HET    SEP  A1042      10                                                       
HET    SEP  A1044      10                                                       
HET    SEP  A1060      10                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     SEP PHOSPHOSERINE                                                    
HETSYN     TPO PHOSPHONOTHREONINE                                               
HETSYN     SEP PHOSPHONOSERINE                                                  
FORMUL   1  TPO    C4 H10 N O6 P                                                
FORMUL   1  SEP    3(C3 H8 N O6 P)                                              
FORMUL   2  HOH   *10(H2 O)                                                     
HELIX    1 AA1 ALA A  872  THR A  880  1                                   9    
HELIX    2 AA2 HIS A  884  LEU A  888  5                                   5    
HELIX    3 AA3 GLY A  918  THR A  930  1                                  13    
HELIX    4 AA4 ILE A  931  ILE A  934  5                                   4    
HELIX    5 AA5 SER A  963  HIS A  969  1                                   7    
HELIX    6 AA6 ASN A  979  ASN A 1000  1                                  22    
HELIX    7 AA7 LYS A 1011  SER A 1013  5                                   3    
HELIX    8 AA8 PRO A 1054  GLN A 1059  5                                   6    
HELIX    9 AA9 SER A 1064  GLY A 1082  1                                  19    
HELIX   10 AB1 LEU A 1096  ALA A 1104  1                                   9    
HELIX   11 AB2 ASP A 1113  ASP A 1120  1                                   8    
HELIX   12 AB3 LEU A 1123  LEU A 1138  1                                  16    
HELIX   13 AB4 THR A 1147  ALA A 1160  1                                  14    
SHEET    1 AA1 5 ARG A 869  LYS A 870  0                                        
SHEET    2 AA1 5 LEU A 942  VAL A 948  1  O  LEU A 943   N  ARG A 869           
SHEET    3 AA1 5 GLU A 951  GLU A 957 -1  O  LEU A 953   N  CYS A 946           
SHEET    4 AA1 5 ALA A 907  LEU A 913 -1  N  LEU A 913   O  ARG A 952           
SHEET    5 AA1 5 GLY A 895  ILE A 901 -1  N  ASP A 896   O  LYS A 912           
SHEET    1 AA2 2 HIS A1004  ILE A1006  0                                        
SHEET    2 AA2 2 ARG A1032  MET A1034 -1  O  MET A1034   N  HIS A1004           
SHEET    1 AA3 2 VAL A1015  LEU A1017  0                                        
SHEET    2 AA3 2 ALA A1023  VAL A1025 -1  O  ARG A1024   N  LEU A1016           
SHEET    1 AA4 2 LEU A1041  SEP A1042  0                                        
SHEET    2 AA4 2 ARG A1062  CYS A1063 -1  O  CYS A1063   N  LEU A1041           
LINK         C   ASP A1038                 N   TPO A1039     1555   1555  1.33  
LINK         C   TPO A1039                 N   HIS A1040     1555   1555  1.33  
LINK         C   LEU A1041                 N   SEP A1042     1555   1555  1.33  
LINK         C   SEP A1042                 N   VAL A1043     1555   1555  1.33  
LINK         C   VAL A1043                 N   SEP A1044     1555   1555  1.33  
LINK         C   SEP A1044                 N   THR A1045     1555   1555  1.33  
LINK         C   GLN A1059                 N   SEP A1060     1555   1555  1.33  
LINK         C   SEP A1060                 N   PHE A1061     1555   1555  1.33  
CISPEP   1 SER A 1002    PRO A 1003          0         3.17                     
CRYST1  116.137  116.137   50.295  90.00  90.00 120.00 P 62          6          
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      0.008611  0.004971  0.000000        0.00000                         
SCALE2      0.000000  0.009943  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.019883        0.00000                         
ATOM      1  N   LYS A 866      18.263  26.343   9.382  1.00134.55           N  
ANISOU    1  N   LYS A 866    14172  17985  18965   2495  -2953  -2542       N  
ATOM      2  CA  LYS A 866      19.006  27.257  10.242  1.00133.10           C  
ANISOU    2  CA  LYS A 866    14423  17653  18498   2400  -2587  -1901       C  
ATOM      3  C   LYS A 866      20.045  28.047   9.450  1.00128.03           C  
ANISOU    3  C   LYS A 866    14395  17142  17107   2683  -2719  -1485       C  
ATOM      4  O   LYS A 866      21.236  27.734   9.501  1.00122.30           O  
ANISOU    4  O   LYS A 866    13997  16353  16119   2494  -2463  -1187       O  
ATOM      5  CB  LYS A 866      19.687  26.487  11.377  1.00129.65           C  
ANISOU    5  CB  LYS A 866    14029  16943  18290   1932  -2010  -1654       C  
ATOM      6  N   PRO A 867      19.596  29.079   8.716  1.00124.81           N  
ANISOU    6  N   PRO A 867    14154  16896  16371   3166  -3081  -1464       N  
ATOM      7  CA  PRO A 867      20.490  29.890   7.883  1.00120.68           C  
ANISOU    7  CA  PRO A 867    14270  16432  15151   3481  -3114  -1047       C  
ATOM      8  C   PRO A 867      21.338  30.860   8.700  1.00115.76           C  
ANISOU    8  C   PRO A 867    14011  15550  14423   3277  -2635   -513       C  
ATOM      9  O   PRO A 867      20.993  31.183   9.836  1.00117.41           O  
ANISOU    9  O   PRO A 867    13997  15602  15013   3047  -2408   -479       O  
ATOM     10  CB  PRO A 867      19.522  30.649   6.973  1.00120.68           C  
ANISOU   10  CB  PRO A 867    14308  16649  14896   4133  -3628  -1216       C  
ATOM     11  CG  PRO A 867      18.295  30.796   7.799  1.00120.98           C  
ANISOU   11  CG  PRO A 867    13778  16643  15547   4070  -3709  -1535       C  
ATOM     12  CD  PRO A 867      18.198  29.540   8.629  1.00122.86           C  
ANISOU   12  CD  PRO A 867    13509  16765  16406   3484  -3444  -1839       C  
ATOM     13  N   LEU A 868      22.441  31.315   8.116  1.00106.36           N  
ANISOU   13  N   LEU A 868    13354  14314  12743   3359  -2456   -152       N  
ATOM     14  CA  LEU A 868      23.329  32.260   8.779  1.00 96.75           C  
ANISOU   14  CA  LEU A 868    12441  12843  11478   3154  -1986    252       C  
ATOM     15  C   LEU A 868      22.684  33.641   8.830  1.00101.56           C  
ANISOU   15  C   LEU A 868    13218  13304  12066   3478  -1996    425       C  
ATOM     16  O   LEU A 868      22.512  34.289   7.799  1.00109.52           O  
ANISOU   16  O   LEU A 868    14615  14326  12670   3971  -2153    582       O  
ATOM     17  CB  LEU A 868      24.675  32.319   8.053  1.00 90.37           C  
ANISOU   17  CB  LEU A 868    12102  11995  10241   3129  -1728    515       C  
ATOM     18  CG  LEU A 868      25.838  33.030   8.744  1.00 80.65           C  
ANISOU   18  CG  LEU A 868    11063  10514   9065   2799  -1193    785       C  
ATOM     19  CD1 LEU A 868      26.221  32.317  10.027  1.00 71.34           C  
ANISOU   19  CD1 LEU A 868     9494   9359   8253   2342  -1043    633       C  
ATOM     20  CD2 LEU A 868      27.025  33.115   7.806  1.00 79.10           C  
ANISOU   20  CD2 LEU A 868    11304  10271   8480   2828   -927    984       C  
ATOM     21  N   ARG A 869      22.323  34.083  10.031  1.00 98.33           N  
ANISOU   21  N   ARG A 869    12550  12747  12062   3248  -1812    406       N  
ATOM     22  CA  ARG A 869      21.612  35.349  10.212  1.00 94.95           C  
ANISOU   22  CA  ARG A 869    12211  12155  11713   3536  -1815    516       C  
ATOM     23  C   ARG A 869      22.531  36.563  10.121  1.00 88.77           C  
ANISOU   23  C   ARG A 869    11949  11052  10728   3554  -1381    913       C  
ATOM     24  O   ARG A 869      23.656  36.543  10.613  1.00 91.30           O  
ANISOU   24  O   ARG A 869    12343  11255  11093   3146   -985   1005       O  
ATOM     25  CB  ARG A 869      20.893  35.365  11.564  1.00 93.36           C  
ANISOU   25  CB  ARG A 869    11532  11907  12034   3270  -1727    311       C  
ATOM     26  CG  ARG A 869      19.803  34.320  11.719  1.00102.20           C  
ANISOU   26  CG  ARG A 869    12098  13238  13494   3245  -2037   -111       C  
ATOM     27  CD  ARG A 869      19.285  34.281  13.150  1.00106.52           C  
ANISOU   27  CD  ARG A 869    12250  13693  14528   2922  -1777   -248       C  
ATOM     28  NE  ARG A 869      18.804  35.586  13.599  1.00110.60           N  
ANISOU   28  NE  ARG A 869    12817  14049  15155   3102  -1693   -159       N  
ATOM     29  CZ  ARG A 869      18.403  35.850  14.839  1.00107.01           C  
ANISOU   29  CZ  ARG A 869    12108  13501  15051   2885  -1428   -243       C  
ATOM     30  NH1 ARG A 869      18.427  34.897  15.763  1.00102.09           N  
ANISOU   30  NH1 ARG A 869    11211  12924  14655   2512  -1193   -369       N  
ATOM     31  NH2 ARG A 869      17.980  37.066  15.159  1.00105.80           N  
ANISOU   31  NH2 ARG A 869    12012  13188  14998   3076  -1362   -188       N  
ATOM     32  N   LYS A 870      22.044  37.624   9.492  1.00 91.39           N  
ANISOU   32  N   LYS A 870    12628  11224  10871   4053  -1438   1118       N  
ATOM     33  CA  LYS A 870      22.764  38.890   9.484  1.00 92.98           C  
ANISOU   33  CA  LYS A 870    13314  11001  11012   4064   -923   1483       C  
ATOM     34  C   LYS A 870      22.218  39.780  10.591  1.00 86.59           C  
ANISOU   34  C   LYS A 870    12281   9964  10654   3960   -766   1414       C  
ATOM     35  O   LYS A 870      21.140  40.354  10.456  1.00 90.63           O  
ANISOU   35  O   LYS A 870    12779  10444  11214   4405  -1016   1407       O  
ATOM     36  CB  LYS A 870      22.641  39.584   8.128  1.00 96.36           C  
ANISOU   36  CB  LYS A 870    14386  11299  10927   4728   -957   1834       C  
ATOM     37  CG  LYS A 870      23.441  40.870   8.010  1.00101.81           C  
ANISOU   37  CG  LYS A 870    15650  11438  11594   4731   -283   2250       C  
ATOM     38  CD  LYS A 870      23.239  41.511   6.645  1.00113.83           C  
ANISOU   38  CD  LYS A 870    17910  12810  12531   5495   -273   2672       C  
ATOM     39  CE  LYS A 870      24.037  42.795   6.507  1.00120.17           C  
ANISOU   39  CE  LYS A 870    19317  12957  13386   5460    544   3104       C  
ATOM     40  NZ  LYS A 870      23.761  43.481   5.212  1.00129.03           N  
ANISOU   40  NZ  LYS A 870    21001  14042  13983   5965    626   3363       N  
ATOM     41  N   LEU A 871      22.962  39.885  11.687  1.00 77.34           N  
ANISOU   41  N   LEU A 871    10915   8670   9799   3413   -379   1318       N  
ATOM     42  CA  LEU A 871      22.489  40.615  12.856  1.00 73.90           C  
ANISOU   42  CA  LEU A 871    10219   8077   9784   3273   -230   1172       C  
ATOM     43  C   LEU A 871      22.891  42.080  12.825  1.00 84.14           C  
ANISOU   43  C   LEU A 871    11909   8868  11191   3346    244   1390       C  
ATOM     44  O   LEU A 871      24.042  42.414  12.539  1.00 88.64           O  
ANISOU   44  O   LEU A 871    12782   9192  11705   3138    681   1531       O  
ATOM     45  CB  LEU A 871      23.010  39.963  14.131  1.00 66.13           C  
ANISOU   45  CB  LEU A 871     8817   7274   9037   2726    -96    896       C  
ATOM     46  CG  LEU A 871      22.504  38.537  14.332  1.00 68.73           C  
ANISOU   46  CG  LEU A 871     8761   7996   9357   2642   -450    695       C  
ATOM     47  CD1 LEU A 871      23.187  37.881  15.517  1.00 66.71           C  
ANISOU   47  CD1 LEU A 871     8242   7892   9215   2200   -257    521       C  
ATOM     48  CD2 LEU A 871      21.000  38.555  14.515  1.00 64.80           C  
ANISOU   48  CD2 LEU A 871     7957   7578   9087   2904   -752    530       C  
ATOM     49  N   ALA A 872      21.930  42.950  13.122  1.00 83.66           N  
ANISOU   49  N   ALA A 872    11820   8620  11347   3635    198   1385       N  
ATOM     50  CA  ALA A 872      22.188  44.380  13.203  1.00 85.34           C  
ANISOU   50  CA  ALA A 872    12382   8279  11765   3709    689   1560       C  
ATOM     51  C   ALA A 872      23.192  44.666  14.308  1.00 78.65           C  
ANISOU   51  C   ALA A 872    11314   7288  11283   3084   1156   1297       C  
ATOM     52  O   ALA A 872      23.162  44.035  15.367  1.00 70.25           O  
ANISOU   52  O   ALA A 872     9762   6562  10368   2744   1009    952       O  
ATOM     53  CB  ALA A 872      20.895  45.145  13.444  1.00 92.44           C  
ANISOU   53  CB  ALA A 872    13203   9050  12869   4141    500   1535       C  
ATOM     54  N   PHE A 873      24.086  45.614  14.057  1.00 77.30           N  
ANISOU   54  N   PHE A 873    11505   6610  11254   2961   1741   1432       N  
ATOM     55  CA  PHE A 873      25.108  45.954  15.031  1.00 79.09           C  
ANISOU   55  CA  PHE A 873    11473   6707  11873   2385   2175   1068       C  
ATOM     56  C   PHE A 873      24.498  46.461  16.335  1.00 85.29           C  
ANISOU   56  C   PHE A 873    11857   7508  13040   2272   2140    699       C  
ATOM     57  O   PHE A 873      25.060  46.249  17.413  1.00 77.36           O  
ANISOU   57  O   PHE A 873    10448   6727  12217   1856   2198    265       O  
ATOM     58  CB  PHE A 873      26.065  46.996  14.455  1.00 81.02           C  
ANISOU   58  CB  PHE A 873    12157   6301  12328   2278   2898   1232       C  
ATOM     59  CG  PHE A 873      27.084  47.473  15.440  1.00 83.07           C  
ANISOU   59  CG  PHE A 873    12070   6399  13095   1696   3349    725       C  
ATOM     60  CD1 PHE A 873      28.159  46.673  15.783  1.00 78.08           C  
ANISOU   60  CD1 PHE A 873    11094   6134  12438   1263   3327    387       C  
ATOM     61  CD2 PHE A 873      26.958  48.714  16.039  1.00 85.75           C  
ANISOU   61  CD2 PHE A 873    12387   6242  13950   1614   3762    521       C  
ATOM     62  CE1 PHE A 873      29.095  47.103  16.698  1.00 79.03           C  
ANISOU   62  CE1 PHE A 873    10826   6185  13017    787   3663   -188       C  
ATOM     63  CE2 PHE A 873      27.886  49.145  16.958  1.00 85.80           C  
ANISOU   63  CE2 PHE A 873    12002   6149  14448   1090   4130    -71       C  
ATOM     64  CZ  PHE A 873      28.961  48.339  17.287  1.00 82.97           C  
ANISOU   64  CZ  PHE A 873    11272   6216  14038    688   4057   -449       C  
ATOM     65  N   ALA A 874      23.346  47.120  16.227  1.00 93.18           N  
ANISOU   65  N   ALA A 874    12978   8302  14124   2699   2026    853       N  
ATOM     66  CA  ALA A 874      22.654  47.683  17.384  1.00 95.74           C  
ANISOU   66  CA  ALA A 874    12957   8604  14814   2653   2023    521       C  
ATOM     67  C   ALA A 874      22.187  46.595  18.349  1.00 84.66           C  
ANISOU   67  C   ALA A 874    11020   7831  13316   2484   1600    208       C  
ATOM     68  O   ALA A 874      22.300  46.748  19.566  1.00 80.12           O  
ANISOU   68  O   ALA A 874    10109   7377  12956   2206   1711   -189       O  
ATOM     69  CB  ALA A 874      21.468  48.536  16.930  1.00 98.63           C  
ANISOU   69  CB  ALA A 874    13570   8637  15267   3227   1950    775       C  
ATOM     70  N   ASP A 875      21.659  45.505  17.799  1.00 81.76           N  
ANISOU   70  N   ASP A 875    10595   7845  12626   2675   1153    372       N  
ATOM     71  CA  ASP A 875      21.255  44.348  18.597  1.00 79.17           C  
ANISOU   71  CA  ASP A 875     9820   8035  12225   2508    854    136       C  
ATOM     72  C   ASP A 875      22.403  43.825  19.455  1.00 70.66           C  
ANISOU   72  C   ASP A 875     8571   7194  11083   2051   1024   -113       C  
ATOM     73  O   ASP A 875      22.259  43.642  20.666  1.00 65.12           O  
ANISOU   73  O   ASP A 875     7564   6723  10456   1892   1052   -409       O  
ATOM     74  CB  ASP A 875      20.745  43.218  17.698  1.00 92.62           C  
ANISOU   74  CB  ASP A 875    11510  10033  13647   2724    426    313       C  
ATOM     75  CG  ASP A 875      19.544  43.622  16.869  1.00107.35           C  
ANISOU   75  CG  ASP A 875    13465  11791  15531   3265    135    458       C  
ATOM     76  OD1 ASP A 875      18.843  44.583  17.252  1.00104.66           O  
ANISOU   76  OD1 ASP A 875    13082  11221  15465   3464    219    391       O  
ATOM     77  OD2 ASP A 875      19.297  42.966  15.835  1.00117.64           O  
ANISOU   77  OD2 ASP A 875    14864  13269  16566   3528   -206    596       O  
ATOM     78  N   LEU A 876      23.542  43.582  18.815  1.00 65.45           N  
ANISOU   78  N   LEU A 876     8117   6497  10254   1893   1138     -5       N  
ATOM     79  CA  LEU A 876      24.708  43.054  19.513  1.00 61.93           C  
ANISOU   79  CA  LEU A 876     7487   6312   9731   1531   1240   -275       C  
ATOM     80  C   LEU A 876      25.169  44.041  20.581  1.00 74.89           C  
ANISOU   80  C   LEU A 876     8957   7822  11674   1320   1550   -690       C  
ATOM     81  O   LEU A 876      25.597  43.649  21.667  1.00 67.42           O  
ANISOU   81  O   LEU A 876     7730   7232  10655   1155   1509  -1041       O  
ATOM     82  CB  LEU A 876      25.831  42.754  18.521  1.00 63.37           C  
ANISOU   82  CB  LEU A 876     7902   6423   9751   1417   1351   -116       C  
ATOM     83  CG  LEU A 876      25.430  41.801  17.387  1.00 61.83           C  
ANISOU   83  CG  LEU A 876     7892   6369   9230   1648   1037    240       C  
ATOM     84  CD1 LEU A 876      26.620  41.422  16.536  1.00 66.26           C  
ANISOU   84  CD1 LEU A 876     8658   6912   9607   1513   1179    348       C  
ATOM     85  CD2 LEU A 876      24.765  40.557  17.940  1.00 60.12           C  
ANISOU   85  CD2 LEU A 876     7376   6590   8877   1669    674    164       C  
ATOM     86  N   LEU A 877      25.043  45.327  20.265  1.00 79.38           N  
ANISOU   86  N   LEU A 877     9717   7875  12568   1378   1859   -660       N  
ATOM     87  CA  LEU A 877      25.410  46.406  21.173  1.00 78.26           C  
ANISOU   87  CA  LEU A 877     9410   7512  12814   1179   2196  -1108       C  
ATOM     88  C   LEU A 877      24.584  46.410  22.462  1.00 80.75           C  
ANISOU   88  C   LEU A 877     9410   8119  13154   1242   2037  -1413       C  
ATOM     89  O   LEU A 877      25.136  46.526  23.557  1.00 78.50           O  
ANISOU   89  O   LEU A 877     8845   8069  12914   1046   2106  -1912       O  
ATOM     90  CB  LEU A 877      25.261  47.753  20.462  1.00 90.54           C  
ANISOU   90  CB  LEU A 877    11305   8351  14744   1289   2610   -926       C  
ATOM     91  CG  LEU A 877      25.667  49.001  21.244  1.00 89.99           C  
ANISOU   91  CG  LEU A 877    11086   7902  15205   1054   3058  -1419       C  
ATOM     92  CD1 LEU A 877      27.151  48.968  21.564  1.00 84.18           C  
ANISOU   92  CD1 LEU A 877    10112   7243  14629    610   3306  -1904       C  
ATOM     93  CD2 LEU A 877      25.308  50.258  20.464  1.00 96.19           C  
ANISOU   93  CD2 LEU A 877    12298   7899  16352   1257   3496  -1112       C  
ATOM     94  N   GLN A 878      23.265  46.291  22.335  1.00 69.60           N  
ANISOU   94  N   GLN A 878     8026   6713  11706   1543   1830  -1158       N  
ATOM     95  CA  GLN A 878      22.405  46.311  23.514  1.00 74.83           C  
ANISOU   95  CA  GLN A 878     8403   7609  12418   1608   1762  -1426       C  
ATOM     96  C   GLN A 878      22.410  44.964  24.241  1.00 66.33           C  
ANISOU   96  C   GLN A 878     7121   7123  10960   1551   1535  -1488       C  
ATOM     97  O   GLN A 878      22.276  44.919  25.464  1.00 72.97           O  
ANISOU   97  O   GLN A 878     7757   8238  11733   1523   1589  -1810       O  
ATOM     98  CB  GLN A 878      20.973  46.718  23.136  1.00 90.30           C  
ANISOU   98  CB  GLN A 878    10404   9342  14563   1955   1664  -1200       C  
ATOM     99  CG  GLN A 878      20.178  45.688  22.346  1.00 97.49           C  
ANISOU   99  CG  GLN A 878    11322  10461  15259   2181   1300   -853       C  
ATOM    100  CD  GLN A 878      19.482  44.672  23.237  1.00101.83           C  
ANISOU  100  CD  GLN A 878    11537  11453  15701   2141   1164   -996       C  
ATOM    101  OE1 GLN A 878      18.933  45.017  24.287  1.00 90.79           O  
ANISOU  101  OE1 GLN A 878     9928  10117  14452   2139   1306  -1264       O  
ATOM    102  NE2 GLN A 878      19.512  43.410  22.823  1.00 64.80           N  
ANISOU  102  NE2 GLN A 878     6818   7039  10765   2109    948   -821       N  
ATOM    103  N   ALA A 879      22.572  43.873  23.494  1.00 63.59           N  
ANISOU  103  N   ALA A 879     6865   6949  10347   1566   1320  -1176       N  
ATOM    104  CA  ALA A 879      22.620  42.540  24.090  1.00 61.00           C  
ANISOU  104  CA  ALA A 879     6405   7087   9684   1530   1174  -1174       C  
ATOM    105  C   ALA A 879      23.803  42.399  25.036  1.00 76.70           C  
ANISOU  105  C   ALA A 879     8310   9382  11451   1377   1249  -1518       C  
ATOM    106  O   ALA A 879      23.740  41.641  26.001  1.00 86.96           O  
ANISOU  106  O   ALA A 879     9518  11059  12462   1438   1220  -1609       O  
ATOM    107  CB  ALA A 879      22.678  41.470  23.010  1.00 58.62           C  
ANISOU  107  CB  ALA A 879     6222   6848   9202   1561    954   -823       C  
ATOM    108  N   THR A 880      24.880  43.128  24.752  1.00 70.11           N  
ANISOU  108  N   THR A 880     7505   8378  10756   1211   1370  -1729       N  
ATOM    109  CA  THR A 880      26.074  43.093  25.592  1.00 72.79           C  
ANISOU  109  CA  THR A 880     7675   9037  10945   1088   1390  -2193       C  
ATOM    110  C   THR A 880      26.150  44.310  26.504  1.00 80.48           C  
ANISOU  110  C   THR A 880     8466   9924  12187   1030   1585  -2734       C  
ATOM    111  O   THR A 880      27.185  44.572  27.120  1.00 81.31           O  
ANISOU  111  O   THR A 880     8367  10243  12284    921   1606  -3267       O  
ATOM    112  CB  THR A 880      27.358  43.037  24.751  1.00 67.96           C  
ANISOU  112  CB  THR A 880     7100   8330  10390    890   1430  -2229       C  
ATOM    113  OG1 THR A 880      27.429  44.200  23.918  1.00 77.80           O  
ANISOU  113  OG1 THR A 880     8475   8997  12087    756   1724  -2192       O  
ATOM    114  CG2 THR A 880      27.379  41.789  23.882  1.00 63.05           C  
ANISOU  114  CG2 THR A 880     6647   7831   9479    953   1228  -1759       C  
ATOM    115  N   ASN A 881      25.045  45.046  26.580  1.00 85.77           N  
ANISOU  115  N   ASN A 881     9173  10296  13120   1123   1708  -2654       N  
ATOM    116  CA  ASN A 881      24.977  46.312  27.306  1.00 89.89           C  
ANISOU  116  CA  ASN A 881     9544  10622  13987   1071   1936  -3148       C  
ATOM    117  C   ASN A 881      26.133  47.246  26.937  1.00 88.62           C  
ANISOU  117  C   ASN A 881     9321  10114  14236    794   2187  -3524       C  
ATOM    118  O   ASN A 881      26.958  47.602  27.781  1.00 88.48           O  
ANISOU  118  O   ASN A 881     9025  10317  14277    666   2231  -4186       O  
ATOM    119  CB  ASN A 881      24.950  46.069  28.819  1.00 90.00           C  
ANISOU  119  CB  ASN A 881     9348  11181  13667   1191   1853  -3602       C  
ATOM    120  CG  ASN A 881      24.600  47.322  29.604  1.00102.49           C  
ANISOU  120  CG  ASN A 881    10771  12581  15588   1185   2070  -4111       C  
ATOM    121  OD1 ASN A 881      25.478  48.002  30.135  1.00104.78           O  
ANISOU  121  OD1 ASN A 881    10848  12923  16041   1045   2154  -4757       O  
ATOM    122  ND2 ASN A 881      23.310  47.640  29.668  1.00109.64           N  
ANISOU  122  ND2 ASN A 881    11736  13272  16651   1337   2162  -3886       N  
ATOM    123  N   GLY A 882      26.181  47.635  25.667  1.00 82.99           N  
ANISOU  123  N   GLY A 882     8866   8855  13810    724   2378  -3129       N  
ATOM    124  CA  GLY A 882      27.220  48.520  25.175  1.00 85.27           C  
ANISOU  124  CA  GLY A 882     9154   8680  14563    437   2764  -3400       C  
ATOM    125  C   GLY A 882      28.597  47.900  25.301  1.00 90.55           C  
ANISOU  125  C   GLY A 882     9588   9729  15090    214   2682  -3768       C  
ATOM    126  O   GLY A 882      29.568  48.596  25.601  1.00 99.77           O  
ANISOU  126  O   GLY A 882    10485  10763  16660    -63   2945  -4402       O  
ATOM    127  N   PHE A 883      28.668  46.590  25.072  1.00 93.27           N  
ANISOU  127  N   PHE A 883     9999  10530  14908    341   2325  -3419       N  
ATOM    128  CA  PHE A 883      29.904  45.818  25.203  1.00 88.96           C  
ANISOU  128  CA  PHE A 883     9236  10420  14146    224   2168  -3718       C  
ATOM    129  C   PHE A 883      30.538  46.032  26.568  1.00 97.42           C  
ANISOU  129  C   PHE A 883     9869  11955  15190    206   2050  -4555       C  
ATOM    130  O   PHE A 883      31.743  46.270  26.679  1.00106.33           O  
ANISOU  130  O   PHE A 883    10679  13166  16556    -10   2134  -5156       O  
ATOM    131  CB  PHE A 883      30.892  46.182  24.097  1.00 75.39           C  
ANISOU  131  CB  PHE A 883     7584   8256  12803    -66   2524  -3702       C  
ATOM    132  CG  PHE A 883      30.397  45.860  22.722  1.00 72.95           C  
ANISOU  132  CG  PHE A 883     7745   7597  12377     35   2591  -2901       C  
ATOM    133  CD1 PHE A 883      30.317  44.548  22.294  1.00 78.16           C  
ANISOU  133  CD1 PHE A 883     8527   8636  12536    194   2234  -2484       C  
ATOM    134  CD2 PHE A 883      30.010  46.867  21.855  1.00 80.66           C  
ANISOU  134  CD2 PHE A 883     9060   7863  13723     22   3014  -2581       C  
ATOM    135  CE1 PHE A 883      29.861  44.243  21.030  1.00 74.49           C  
ANISOU  135  CE1 PHE A 883     8462   7907  11934    323   2246  -1839       C  
ATOM    136  CE2 PHE A 883      29.552  46.569  20.586  1.00 82.05           C  
ANISOU  136  CE2 PHE A 883     9697   7789  13690    219   3021  -1873       C  
ATOM    137  CZ  PHE A 883      29.477  45.252  20.174  1.00 69.93           C  
ANISOU  137  CZ  PHE A 883     8227   6698  11646    363   2611  -1539       C  
ATOM    138  N   HIS A 884      29.709  45.947  27.603  1.00 92.98           N  
ANISOU  138  N   HIS A 884     9277  11715  14337    458   1862  -4634       N  
ATOM    139  CA  HIS A 884      30.160  46.151  28.970  1.00 97.91           C  
ANISOU  139  CA  HIS A 884     9546  12850  14807    557   1708  -5422       C  
ATOM    140  C   HIS A 884      31.081  45.017  29.410  1.00 98.22           C  
ANISOU  140  C   HIS A 884     9439  13589  14291    748   1327  -5617       C  
ATOM    141  O   HIS A 884      31.022  43.909  28.868  1.00 82.84           O  
ANISOU  141  O   HIS A 884     7727  11767  11983    865   1167  -5024       O  
ATOM    142  CB  HIS A 884      28.961  46.263  29.911  1.00 98.49           C  
ANISOU  142  CB  HIS A 884     9708  13088  14625    831   1653  -5357       C  
ATOM    143  CG  HIS A 884      29.272  46.925  31.215  1.00104.40           C  
ANISOU  143  CG  HIS A 884    10124  14190  15353    915   1610  -6234       C  
ATOM    144  ND1 HIS A 884      29.520  46.214  32.370  1.00109.67           N  
ANISOU  144  ND1 HIS A 884    10705  15631  15335   1282   1277  -6550       N  
ATOM    145  CD2 HIS A 884      29.369  48.233  31.550  1.00111.47           C  
ANISOU  145  CD2 HIS A 884    10770  14773  16812    718   1864  -6888       C  
ATOM    146  CE1 HIS A 884      29.758  47.057  33.359  1.00118.05           C  
ANISOU  146  CE1 HIS A 884    11513  16873  16469   1262   1210  -7208       C  
ATOM    147  NE2 HIS A 884      29.673  48.288  32.888  1.00119.74           N  
ANISOU  147  NE2 HIS A 884    11604  16437  17457    880   1547  -7412       N  
ATOM    148  N   ASN A 885      31.926  45.308  30.396  1.00107.64           N  
ANISOU  148  N   ASN A 885    10233  15241  15424    818   1169  -6494       N  
ATOM    149  CA  ASN A 885      32.922  44.361  30.881  1.00110.81           C  
ANISOU  149  CA  ASN A 885    10448  16347  15309   1083    769  -6813       C  
ATOM    150  C   ASN A 885      32.298  43.134  31.543  1.00103.30           C  
ANISOU  150  C   ASN A 885     9837  15918  13496   1598    474  -6290       C  
ATOM    151  O   ASN A 885      32.875  42.047  31.522  1.00101.60           O  
ANISOU  151  O   ASN A 885     9683  16100  12821   1844    207  -6122       O  
ATOM    152  CB  ASN A 885      33.872  45.062  31.859  1.00121.49           C  
ANISOU  152  CB  ASN A 885    11305  18071  16784   1032    542  -7737       C  
ATOM    153  CG  ASN A 885      35.090  44.223  32.198  1.00124.65           C  
ANISOU  153  CG  ASN A 885    11438  19132  16792   1258     77  -8040       C  
ATOM    154  OD1 ASN A 885      35.149  43.589  33.251  1.00129.63           O  
ANISOU  154  OD1 ASN A 885    12103  20431  16719   1757   -347  -8083       O  
ATOM    155  ND2 ASN A 885      36.071  44.215  31.302  1.00124.25           N  
ANISOU  155  ND2 ASN A 885    11131  18877  17203    928    185  -8228       N  
ATOM    156  N   ASP A 886      31.115  43.315  32.122  1.00105.51           N  
ANISOU  156  N   ASP A 886    10344  16148  13595   1762    584  -6031       N  
ATOM    157  CA  ASP A 886      30.416  42.230  32.805  1.00103.87           C  
ANISOU  157  CA  ASP A 886    10488  16334  12644   2221    462  -5528       C  
ATOM    158  C   ASP A 886      29.986  41.117  31.844  1.00 94.90           C  
ANISOU  158  C   ASP A 886     9691  14946  11421   2180    508  -4626       C  
ATOM    159  O   ASP A 886      29.737  39.984  32.264  1.00 89.53           O  
ANISOU  159  O   ASP A 886     9285  14572  10163   2536    428  -4219       O  
ATOM    160  CB  ASP A 886      29.195  42.776  33.549  1.00106.61           C  
ANISOU  160  CB  ASP A 886    10960  16593  12952   2330    676  -5485       C  
ATOM    161  CG  ASP A 886      29.571  43.743  34.658  1.00113.19           C  
ANISOU  161  CG  ASP A 886    11510  17732  13764   2413    573  -6323       C  
ATOM    162  OD1 ASP A 886      30.748  43.745  35.075  1.00119.94           O  
ANISOU  162  OD1 ASP A 886    12110  18984  14478   2463    226  -6809       O  
ATOM    163  OD2 ASP A 886      28.686  44.495  35.120  1.00111.80           O  
ANISOU  163  OD2 ASP A 886    11362  17361  13754   2378    781  -6390       O  
ATOM    164  N   SER A 887      29.901  41.449  30.558  1.00 88.12           N  
ANISOU  164  N   SER A 887     8834  13514  11132   1773    667  -4332       N  
ATOM    165  CA  SER A 887      29.501  40.489  29.537  1.00 82.21           C  
ANISOU  165  CA  SER A 887     8359  12521  10356   1716    684  -3580       C  
ATOM    166  C   SER A 887      30.713  39.800  28.928  1.00 85.12           C  
ANISOU  166  C   SER A 887     8658  13047  10635   1675    505  -3613       C  
ATOM    167  O   SER A 887      30.590  38.740  28.309  1.00 75.52           O  
ANISOU  167  O   SER A 887     7657  11795   9242   1727    450  -3080       O  
ATOM    168  CB  SER A 887      28.690  41.178  28.438  1.00 83.37           C  
ANISOU  168  CB  SER A 887     8598  12016  11062   1410    915  -3225       C  
ATOM    169  OG  SER A 887      27.462  41.670  28.940  1.00100.22           O  
ANISOU  169  OG  SER A 887    10789  14005  13285   1488   1063  -3141       O  
ATOM    170  N   LEU A 888      31.877  40.419  29.107  1.00 91.42           N  
ANISOU  170  N   LEU A 888     9112  14009  11615   1569    433  -4303       N  
ATOM    171  CA  LEU A 888      33.132  39.931  28.538  1.00 94.81           C  
ANISOU  171  CA  LEU A 888     9373  14582  12067   1496    296  -4478       C  
ATOM    172  C   LEU A 888      33.576  38.616  29.178  1.00 87.30           C  
ANISOU  172  C   LEU A 888     8507  14236  10427   1970    -42  -4400       C  
ATOM    173  O   LEU A 888      33.658  38.514  30.399  1.00 94.79           O  
ANISOU  173  O   LEU A 888     9410  15695  10910   2377   -240  -4743       O  
ATOM    174  CB  LEU A 888      34.226  40.991  28.706  1.00 94.58           C  
ANISOU  174  CB  LEU A 888     8855  14583  12496   1255    347  -5380       C  
ATOM    175  CG  LEU A 888      35.545  40.781  27.962  1.00 89.43           C  
ANISOU  175  CG  LEU A 888     7930  13945  12106   1048    336  -5674       C  
ATOM    176  CD1 LEU A 888      35.336  40.949  26.470  1.00 82.00           C  
ANISOU  176  CD1 LEU A 888     7234  12319  11603    651    709  -5098       C  
ATOM    177  CD2 LEU A 888      36.604  41.749  28.472  1.00101.20           C  
ANISOU  177  CD2 LEU A 888     8824  15590  14038    874    359  -6757       C  
ATOM    178  N   ILE A 889      33.856  37.611  28.355  1.00 83.91           N  
ANISOU  178  N   ILE A 889     8239  13742   9902   1968    -95  -3944       N  
ATOM    179  CA  ILE A 889      34.312  36.323  28.873  1.00 97.35           C  
ANISOU  179  CA  ILE A 889    10066  15935  10986   2445   -372  -3816       C  
ATOM    180  C   ILE A 889      35.591  35.838  28.183  1.00105.15           C  
ANISOU  180  C   ILE A 889    10835  17047  12070   2389   -529  -4023       C  
ATOM    181  O   ILE A 889      35.861  34.638  28.113  1.00106.78           O  
ANISOU  181  O   ILE A 889    11227  17447  11898   2691   -683  -3698       O  
ATOM    182  CB  ILE A 889      33.219  35.244  28.735  1.00 89.18           C  
ANISOU  182  CB  ILE A 889     9508  14715   9662   2607   -252  -2976       C  
ATOM    183  CG1 ILE A 889      32.819  35.059  27.270  1.00 83.78           C  
ANISOU  183  CG1 ILE A 889     8939  13483   9408   2197    -77  -2484       C  
ATOM    184  CG2 ILE A 889      32.004  35.608  29.574  1.00 90.56           C  
ANISOU  184  CG2 ILE A 889     9863  14839   9706   2724    -74  -2827       C  
ATOM    185  CD1 ILE A 889      31.801  33.953  27.055  1.00 79.80           C  
ANISOU  185  CD1 ILE A 889     8799  12789   8734   2311     33  -1793       C  
ATOM    186  N   GLY A 890      36.384  36.784  27.691  1.00108.07           N  
ANISOU  186  N   GLY A 890    10803  17270  12989   2000   -436  -4587       N  
ATOM    187  CA  GLY A 890      37.614  36.473  26.988  1.00111.61           C  
ANISOU  187  CA  GLY A 890    10974  17787  13644   1874   -497  -4867       C  
ATOM    188  C   GLY A 890      37.957  37.592  26.026  1.00119.99           C  
ANISOU  188  C   GLY A 890    11803  18320  15469   1269   -103  -5129       C  
ATOM    189  O   GLY A 890      37.113  38.012  25.235  1.00123.24           O  
ANISOU  189  O   GLY A 890    12521  18164  16142    972    221  -4606       O  
ATOM    190  N   SER A 891      39.190  38.084  26.092  1.00124.38           N  
ANISOU  190  N   SER A 891    11817  19046  16395   1114   -103  -5956       N  
ATOM    191  CA  SER A 891      39.590  39.221  25.270  1.00127.80           C  
ANISOU  191  CA  SER A 891    12022  18911  17623    524    401  -6267       C  
ATOM    192  C   SER A 891      41.046  39.137  24.824  1.00141.01           C  
ANISOU  192  C   SER A 891    13192  20703  19682    332    471  -6898       C  
ATOM    193  O   SER A 891      41.819  38.329  25.337  1.00142.28           O  
ANISOU  193  O   SER A 891    13069  21486  19506    702     31  -7273       O  
ATOM    194  CB  SER A 891      39.354  40.533  26.027  1.00121.73           C  
ANISOU  194  CB  SER A 891    10993  18028  17233    360    556  -6873       C  
ATOM    195  OG  SER A 891      40.028  40.537  27.275  1.00119.65           O  
ANISOU  195  OG  SER A 891    10237  18458  16766    678    121  -7753       O  
ATOM    196  N   GLY A 892      41.406  39.981  23.861  1.00150.09           N  
ANISOU  196  N   GLY A 892    14251  21232  21544   -219   1066  -7003       N  
ATOM    197  CA  GLY A 892      42.768  40.059  23.364  1.00155.18           C  
ANISOU  197  CA  GLY A 892    14381  21871  22710   -505   1297  -7648       C  
ATOM    198  C   GLY A 892      43.194  38.826  22.593  1.00156.54           C  
ANISOU  198  C   GLY A 892    14725  22204  22549   -349   1159  -7196       C  
ATOM    199  O   GLY A 892      42.392  37.921  22.357  1.00155.81           O  
ANISOU  199  O   GLY A 892    15184  22160  21857    -54    921  -6348       O  
ATOM    200  N   GLY A 893      44.464  38.795  22.197  1.00156.24           N  
ANISOU  200  N   GLY A 893    14307  22163  22893   -597   1273  -7717       N  
ATOM    201  CA  GLY A 893      45.018  37.659  21.483  1.00148.82           C  
ANISOU  201  CA  GLY A 893    13439  21395  21709   -453   1171  -7431       C  
ATOM    202  C   GLY A 893      44.411  37.464  20.108  1.00138.47           C  
ANISOU  202  C   GLY A 893    12680  19537  20396   -644   1679  -6543       C  
ATOM    203  O   GLY A 893      45.044  37.759  19.093  1.00140.24           O  
ANISOU  203  O   GLY A 893    12853  19347  21084  -1034   2252  -6598       O  
ATOM    204  N   PHE A 894      43.179  36.964  20.076  1.00129.35           N  
ANISOU  204  N   PHE A 894    12151  18334  18661   -374   1434  -5682       N  
ATOM    205  CA  PHE A 894      42.483  36.703  18.820  1.00117.04           C  
ANISOU  205  CA  PHE A 894    11233  16295  16944   -476   1728  -4789       C  
ATOM    206  C   PHE A 894      41.192  37.514  18.704  1.00104.41           C  
ANISOU  206  C   PHE A 894    10103  14232  15335   -553   1924  -4263       C  
ATOM    207  O   PHE A 894      40.989  38.237  17.726  1.00100.60           O  
ANISOU  207  O   PHE A 894     9935  13161  15129   -828   2469  -3948       O  
ATOM    208  CB  PHE A 894      42.175  35.209  18.682  1.00109.77           C  
ANISOU  208  CB  PHE A 894    10600  15714  15392    -72   1259  -4263       C  
ATOM    209  N   GLY A 895      40.324  37.393  19.704  1.00 93.51           N  
ANISOU  209  N   GLY A 895     8792  13118  13619   -265   1505  -4160       N  
ATOM    210  CA  GLY A 895      39.049  38.083  19.681  1.00 94.76           C  
ANISOU  210  CA  GLY A 895     9343  12898  13763   -283   1628  -3701       C  
ATOM    211  C   GLY A 895      38.485  38.365  21.062  1.00109.90           C  
ANISOU  211  C   GLY A 895    11097  15118  15541    -76   1312  -3973       C  
ATOM    212  O   GLY A 895      38.830  37.686  22.034  1.00109.89           O  
ANISOU  212  O   GLY A 895    10843  15696  15215    227    880  -4295       O  
ATOM    213  N   ASP A 896      37.623  39.380  21.145  1.00112.01           N  
ANISOU  213  N   ASP A 896    11541  14994  16026   -191   1543  -3838       N  
ATOM    214  CA  ASP A 896      36.889  39.686  22.373  1.00 98.52           C  
ANISOU  214  CA  ASP A 896     9757  13516  14162     10   1296  -4011       C  
ATOM    215  C   ASP A 896      35.547  38.967  22.377  1.00 88.74           C  
ANISOU  215  C   ASP A 896     8953  12310  12455    299   1053  -3281       C  
ATOM    216  O   ASP A 896      34.744  39.130  21.459  1.00 80.36           O  
ANISOU  216  O   ASP A 896     8260  10821  11452    235   1229  -2721       O  
ATOM    217  CB  ASP A 896      36.677  41.192  22.525  1.00105.86           C  
ANISOU  217  CB  ASP A 896    10593  13985  15644   -268   1701  -4332       C  
ATOM    218  CG  ASP A 896      37.954  41.924  22.872  1.00118.38           C  
ANISOU  218  CG  ASP A 896    11609  15600  17770   -555   1924  -5266       C  
ATOM    219  OD1 ASP A 896      39.025  41.534  22.355  1.00131.66           O  
ANISOU  219  OD1 ASP A 896    13070  17361  19595   -694   2012  -5501       O  
ATOM    220  OD2 ASP A 896      37.886  42.881  23.669  1.00111.93           O  
ANISOU  220  OD2 ASP A 896    10523  14732  17273   -648   2018  -5826       O  
ATOM    221  N   VAL A 897      35.302  38.178  23.417  1.00 80.96           N  
ANISOU  221  N   VAL A 897     7922  11828  11011    646    671  -3315       N  
ATOM    222  CA  VAL A 897      34.117  37.337  23.448  1.00 75.63           C  
ANISOU  222  CA  VAL A 897     7604  11172   9958    889    512  -2678       C  
ATOM    223  C   VAL A 897      33.164  37.745  24.563  1.00 79.04           C  
ANISOU  223  C   VAL A 897     8056  11705  10270   1061    467  -2732       C  
ATOM    224  O   VAL A 897      33.570  37.917  25.715  1.00 75.16           O  
ANISOU  224  O   VAL A 897     7338  11610   9609   1240    328  -3225       O  
ATOM    225  CB  VAL A 897      34.497  35.857  23.612  1.00 75.55           C  
ANISOU  225  CB  VAL A 897     7654  11558   9495   1181    230  -2503       C  
ATOM    226  CG1 VAL A 897      33.252  34.982  23.589  1.00 69.00           C  
ANISOU  226  CG1 VAL A 897     7165  10648   8404   1363    174  -1884       C  
ATOM    227  CG2 VAL A 897      35.466  35.447  22.513  1.00 75.21           C  
ANISOU  227  CG2 VAL A 897     7565  11431   9580   1016    282  -2494       C  
ATOM    228  N   TYR A 898      31.893  37.900  24.205  1.00 69.59           N  
ANISOU  228  N   TYR A 898     7116  10177   9150   1039    572  -2263       N  
ATOM    229  CA  TYR A 898      30.869  38.292  25.160  1.00 66.81           C  
ANISOU  229  CA  TYR A 898     6786   9863   8735   1181    591  -2277       C  
ATOM    230  C   TYR A 898      29.768  37.242  25.277  1.00 69.30           C  
ANISOU  230  C   TYR A 898     7335  10222   8774   1390    525  -1759       C  
ATOM    231  O   TYR A 898      29.297  36.695  24.280  1.00 68.11           O  
ANISOU  231  O   TYR A 898     7344   9837   8698   1327    520  -1336       O  
ATOM    232  CB  TYR A 898      30.250  39.630  24.764  1.00 71.55           C  
ANISOU  232  CB  TYR A 898     7402   9983   9799    972    839  -2302       C  
ATOM    233  CG  TYR A 898      31.193  40.813  24.800  1.00 83.82           C  
ANISOU  233  CG  TYR A 898     8715  11381  11751    728   1040  -2869       C  
ATOM    234  CD1 TYR A 898      31.976  41.138  23.699  1.00 80.18           C  
ANISOU  234  CD1 TYR A 898     8274  10588  11604    469   1254  -2861       C  
ATOM    235  CD2 TYR A 898      31.282  41.619  25.928  1.00 89.64           C  
ANISOU  235  CD2 TYR A 898     9200  12273  12585    748   1071  -3447       C  
ATOM    236  CE1 TYR A 898      32.826  42.220  23.725  1.00 90.38           C  
ANISOU  236  CE1 TYR A 898     9320  11651  13369    195   1551  -3410       C  
ATOM    237  CE2 TYR A 898      32.129  42.704  25.962  1.00 97.19           C  
ANISOU  237  CE2 TYR A 898     9876  13039  14014    482   1297  -4057       C  
ATOM    238  CZ  TYR A 898      32.899  43.000  24.859  1.00102.69           C  
ANISOU  238  CZ  TYR A 898    10576  13349  15093    184   1567  -4036       C  
ATOM    239  OH  TYR A 898      33.749  44.081  24.889  1.00119.16           O  
ANISOU  239  OH  TYR A 898    12356  15166  17754   -130   1901  -4679       O  
ATOM    240  N   LYS A 899      29.372  36.966  26.512  1.00 70.33           N  
ANISOU  240  N   LYS A 899     7475  10651   8595   1646    506  -1837       N  
ATOM    241  CA  LYS A 899      28.196  36.158  26.790  1.00 70.94           C  
ANISOU  241  CA  LYS A 899     7744  10686   8525   1803    593  -1409       C  
ATOM    242  C   LYS A 899      26.963  37.059  26.739  1.00 76.98           C  
ANISOU  242  C   LYS A 899     8476  11130   9644   1689    756  -1361       C  
ATOM    243  O   LYS A 899      26.913  38.078  27.427  1.00 86.15           O  
ANISOU  243  O   LYS A 899     9519  12327  10887   1692    828  -1712       O  
ATOM    244  CB  LYS A 899      28.333  35.486  28.155  1.00 71.81           C  
ANISOU  244  CB  LYS A 899     7951  11224   8108   2178    597  -1474       C  
ATOM    245  CG  LYS A 899      27.039  35.028  28.791  1.00 77.79           C  
ANISOU  245  CG  LYS A 899     8882  11899   8776   2323    856  -1155       C  
ATOM    246  CD  LYS A 899      27.293  34.576  30.220  1.00 87.37           C  
ANISOU  246  CD  LYS A 899    10268  13547   9381   2766    919  -1241       C  
ATOM    247  CE  LYS A 899      28.035  35.654  31.005  1.00 99.03           C  
ANISOU  247  CE  LYS A 899    11550  15388  10690   2883    739  -1868       C  
ATOM    248  NZ  LYS A 899      28.539  35.164  32.321  1.00108.34           N  
ANISOU  248  NZ  LYS A 899    12910  17117  11138   3435    676  -2023       N  
ATOM    249  N   ALA A 900      25.979  36.705  25.917  1.00 60.13           N  
ANISOU  249  N   ALA A 900     6409   8696   7741   1612    794   -990       N  
ATOM    250  CA  ALA A 900      24.805  37.565  25.760  1.00 59.85           C  
ANISOU  250  CA  ALA A 900     6306   8368   8067   1560    897   -971       C  
ATOM    251  C   ALA A 900      23.517  36.803  25.476  1.00 68.51           C  
ANISOU  251  C   ALA A 900     7395   9321   9315   1598    951   -673       C  
ATOM    252  O   ALA A 900      23.527  35.613  25.151  1.00 70.15           O  
ANISOU  252  O   ALA A 900     7667   9568   9420   1608    923   -451       O  
ATOM    253  CB  ALA A 900      25.049  38.579  24.652  1.00 56.54           C  
ANISOU  253  CB  ALA A 900     5893   7623   7967   1408    844   -998       C  
ATOM    254  N   ILE A 901      22.404  37.516  25.602  1.00 65.86           N  
ANISOU  254  N   ILE A 901     6941   8800   9282   1616   1046   -728       N  
ATOM    255  CA  ILE A 901      21.102  36.989  25.243  1.00 55.96           C  
ANISOU  255  CA  ILE A 901     5564   7390   8310   1636   1083   -576       C  
ATOM    256  C   ILE A 901      20.473  37.911  24.206  1.00 60.52           C  
ANISOU  256  C   ILE A 901     6058   7694   9242   1664    901   -587       C  
ATOM    257  O   ILE A 901      20.224  39.084  24.479  1.00 64.08           O  
ANISOU  257  O   ILE A 901     6473   8021   9854   1713    961   -741       O  
ATOM    258  CB  ILE A 901      20.184  36.861  26.467  1.00 58.35           C  
ANISOU  258  CB  ILE A 901     5763   7752   8654   1707   1409   -656       C  
ATOM    259  CG1 ILE A 901      20.825  35.958  27.522  1.00 67.33           C  
ANISOU  259  CG1 ILE A 901     7093   9162   9329   1796   1620   -584       C  
ATOM    260  CG2 ILE A 901      18.806  36.327  26.064  1.00 63.76           C  
ANISOU  260  CG2 ILE A 901     6215   8245   9765   1681   1490   -600       C  
ATOM    261  CD1 ILE A 901      20.017  35.833  28.791  1.00 72.59           C  
ANISOU  261  CD1 ILE A 901     7758   9891   9932   1915   2033   -620       C  
ATOM    262  N   LEU A 902      20.238  37.384  23.010  1.00 59.39           N  
ANISOU  262  N   LEU A 902     5912   7462   9194   1682    673   -436       N  
ATOM    263  CA  LEU A 902      19.639  38.167  21.934  1.00 59.55           C  
ANISOU  263  CA  LEU A 902     5916   7268   9441   1836    448   -414       C  
ATOM    264  C   LEU A 902      18.201  38.547  22.279  1.00 68.34           C  
ANISOU  264  C   LEU A 902     6741   8297  10928   1968    486   -573       C  
ATOM    265  O   LEU A 902      17.594  37.954  23.173  1.00 64.71           O  
ANISOU  265  O   LEU A 902     6071   7926  10589   1888    712   -678       O  
ATOM    266  CB  LEU A 902      19.690  37.391  20.618  1.00 56.35           C  
ANISOU  266  CB  LEU A 902     5567   6875   8969   1892    158   -273       C  
ATOM    267  CG  LEU A 902      21.094  37.065  20.110  1.00 57.55           C  
ANISOU  267  CG  LEU A 902     5995   7086   8784   1781    127   -124       C  
ATOM    268  CD1 LEU A 902      21.026  36.292  18.803  1.00 64.51           C  
ANISOU  268  CD1 LEU A 902     6927   7996   9589   1870   -156    -22       C  
ATOM    269  CD2 LEU A 902      21.912  38.338  19.942  1.00 54.48           C  
ANISOU  269  CD2 LEU A 902     5843   6526   8330   1783    229    -98       C  
ATOM    270  N   LYS A 903      17.655  39.529  21.567  1.00 73.89           N  
ANISOU  270  N   LYS A 903     7450   8811  11813   2202    304   -584       N  
ATOM    271  CA  LYS A 903      16.335  40.064  21.900  1.00 82.87           C  
ANISOU  271  CA  LYS A 903     8287   9867  13333   2376    319   -783       C  
ATOM    272  C   LYS A 903      15.211  39.043  21.684  1.00 84.23           C  
ANISOU  272  C   LYS A 903     8056  10152  13796   2401    203   -948       C  
ATOM    273  O   LYS A 903      14.068  39.282  22.070  1.00 98.47           O  
ANISOU  273  O   LYS A 903     9507  11923  15985   2499    266  -1187       O  
ATOM    274  CB  LYS A 903      16.056  41.345  21.097  1.00 75.65           C  
ANISOU  274  CB  LYS A 903     7523   8705  12515   2715    125   -726       C  
ATOM    275  CG  LYS A 903      16.223  41.208  19.593  1.00 82.09           C  
ANISOU  275  CG  LYS A 903     8560   9494  13137   2972   -246   -523       C  
ATOM    276  CD  LYS A 903      16.050  42.550  18.902  1.00 92.83           C  
ANISOU  276  CD  LYS A 903    10203  10554  14513   3378   -333   -381       C  
ATOM    277  CE  LYS A 903      16.200  42.425  17.391  1.00 98.85           C  
ANISOU  277  CE  LYS A 903    11273  11314  14970   3735   -681   -143       C  
ATOM    278  NZ  LYS A 903      15.866  43.702  16.690  1.00 98.21           N  
ANISOU  278  NZ  LYS A 903    11528  10919  14869   4262   -748     48       N  
ATOM    279  N   ASP A 904      15.543  37.906  21.081  1.00 90.33           N  
ANISOU  279  N   ASP A 904     8842  11039  14443   2296     67   -875       N  
ATOM    280  CA  ASP A 904      14.587  36.817  20.916  1.00 95.61           C  
ANISOU  280  CA  ASP A 904     9090  11776  15463   2241     30  -1106       C  
ATOM    281  C   ASP A 904      14.794  35.730  21.970  1.00 99.02           C  
ANISOU  281  C   ASP A 904     9481  12234  15906   1910    502  -1075       C  
ATOM    282  O   ASP A 904      14.110  34.709  21.964  1.00 98.31           O  
ANISOU  282  O   ASP A 904     9071  12120  16164   1782    632  -1254       O  
ATOM    283  CB  ASP A 904      14.703  36.214  19.516  1.00101.45           C  
ANISOU  283  CB  ASP A 904     9842  12598  16105   2374   -415  -1115       C  
ATOM    284  CG  ASP A 904      16.091  35.684  19.226  1.00101.86           C  
ANISOU  284  CG  ASP A 904    10309  12698  15694   2212   -396   -818       C  
ATOM    285  OD1 ASP A 904      16.955  36.481  18.799  1.00107.40           O  
ANISOU  285  OD1 ASP A 904    11402  13359  16047   2323   -493   -586       O  
ATOM    286  OD2 ASP A 904      16.320  34.475  19.430  1.00 99.97           O  
ANISOU  286  OD2 ASP A 904    10000  12504  15480   1976   -236   -828       O  
ATOM    287  N   GLY A 905      15.753  35.948  22.864  1.00 97.34           N  
ANISOU  287  N   GLY A 905     9604  12061  15318   1803    775   -870       N  
ATOM    288  CA  GLY A 905      15.998  35.029  23.960  1.00 83.75           C  
ANISOU  288  CA  GLY A 905     7955  10384  13481   1619   1235   -782       C  
ATOM    289  C   GLY A 905      17.086  34.006  23.702  1.00 74.74           C  
ANISOU  289  C   GLY A 905     7089   9319  11989   1521   1211   -557       C  
ATOM    290  O   GLY A 905      17.356  33.154  24.548  1.00 74.85           O  
ANISOU  290  O   GLY A 905     7235   9355  11850   1446   1586   -429       O  
ATOM    291  N   SER A 906      17.716  34.083  22.536  1.00 73.09           N  
ANISOU  291  N   SER A 906     6999   9140  11630   1566    798   -490       N  
ATOM    292  CA  SER A 906      18.799  33.164  22.205  1.00 66.97           C  
ANISOU  292  CA  SER A 906     6466   8442  10538   1487    751   -307       C  
ATOM    293  C   SER A 906      20.013  33.398  23.095  1.00 71.42           C  
ANISOU  293  C   SER A 906     7341   9157  10637   1491    905   -167       C  
ATOM    294  O   SER A 906      20.489  34.526  23.226  1.00 70.39           O  
ANISOU  294  O   SER A 906     7307   9073  10366   1542    817   -218       O  
ATOM    295  CB  SER A 906      19.206  33.309  20.738  1.00 68.25           C  
ANISOU  295  CB  SER A 906     6704   8614  10612   1561    307   -285       C  
ATOM    296  OG  SER A 906      18.079  33.270  19.884  1.00 78.91           O  
ANISOU  296  OG  SER A 906     7753   9905  12325   1665     56   -493       O  
ATOM    297  N   ALA A 907      20.504  32.326  23.707  1.00 74.59           N  
ANISOU  297  N   ALA A 907     7887   9627  10826   1468   1141    -30       N  
ATOM    298  CA  ALA A 907      21.751  32.373  24.457  1.00 67.79           C  
ANISOU  298  CA  ALA A 907     7296   8989   9471   1556   1190     48       C  
ATOM    299  C   ALA A 907      22.915  32.197  23.500  1.00 74.02           C  
ANISOU  299  C   ALA A 907     8208   9853  10064   1524    882     96       C  
ATOM    300  O   ALA A 907      23.066  31.144  22.884  1.00 79.62           O  
ANISOU  300  O   ALA A 907     8948  10505  10798   1485    838    208       O  
ATOM    301  CB  ALA A 907      21.779  31.305  25.535  1.00 63.77           C  
ANISOU  301  CB  ALA A 907     6953   8527   8749   1660   1579    211       C  
ATOM    302  N   VAL A 908      23.731  33.238  23.368  1.00 70.80           N  
ANISOU  302  N   VAL A 908     7852   9541   9509   1523    718    -21       N  
ATOM    303  CA  VAL A 908      24.800  33.236  22.380  1.00 60.51           C  
ANISOU  303  CA  VAL A 908     6642   8264   8086   1464    497     -4       C  
ATOM    304  C   VAL A 908      26.136  33.696  22.942  1.00 60.68           C  
ANISOU  304  C   VAL A 908     6720   8507   7830   1484    490   -175       C  
ATOM    305  O   VAL A 908      26.211  34.242  24.046  1.00 57.64           O  
ANISOU  305  O   VAL A 908     6296   8269   7336   1562    594   -357       O  
ATOM    306  CB  VAL A 908      24.460  34.147  21.183  1.00 61.67           C  
ANISOU  306  CB  VAL A 908     6775   8201   8455   1419    329     -8       C  
ATOM    307  CG1 VAL A 908      23.197  33.668  20.475  1.00 64.82           C  
ANISOU  307  CG1 VAL A 908     7051   8459   9119   1460    221     53       C  
ATOM    308  CG2 VAL A 908      24.313  35.592  21.648  1.00 60.69           C  
ANISOU  308  CG2 VAL A 908     6621   7991   8449   1426    417   -160       C  
ATOM    309  N   ALA A 909      27.186  33.456  22.160  1.00 59.86           N  
ANISOU  309  N   ALA A 909     6673   8443   7627   1423    364   -176       N  
ATOM    310  CA  ALA A 909      28.502  34.032  22.400  1.00 55.09           C  
ANISOU  310  CA  ALA A 909     6026   8008   6898   1387    345   -443       C  
ATOM    311  C   ALA A 909      28.826  34.972  21.247  1.00 57.97           C  
ANISOU  311  C   ALA A 909     6419   8115   7492   1207    363   -473       C  
ATOM    312  O   ALA A 909      28.672  34.612  20.073  1.00 53.46           O  
ANISOU  312  O   ALA A 909     5970   7386   6957   1176    298   -251       O  
ATOM    313  CB  ALA A 909      29.565  32.946  22.527  1.00 50.08           C  
ANISOU  313  CB  ALA A 909     5417   7634   5976   1493    255   -456       C  
ATOM    314  N   ILE A 910      29.262  36.182  21.576  1.00 58.16           N  
ANISOU  314  N   ILE A 910     6354   8075   7669   1109    489   -757       N  
ATOM    315  CA  ILE A 910      29.528  37.182  20.553  1.00 58.93           C  
ANISOU  315  CA  ILE A 910     6546   7826   8019    954    643   -743       C  
ATOM    316  C   ILE A 910      31.000  37.559  20.530  1.00 70.26           C  
ANISOU  316  C   ILE A 910     7850   9311   9535    776    786  -1094       C  
ATOM    317  O   ILE A 910      31.518  38.137  21.485  1.00 71.47           O  
ANISOU  317  O   ILE A 910     7769   9605   9783    722    847  -1534       O  
ATOM    318  CB  ILE A 910      28.679  38.450  20.770  1.00 58.08           C  
ANISOU  318  CB  ILE A 910     6456   7427   8185    956    790   -780       C  
ATOM    319  CG1 ILE A 910      27.191  38.105  20.716  1.00 56.40           C  
ANISOU  319  CG1 ILE A 910     6298   7168   7963   1138    646   -500       C  
ATOM    320  CG2 ILE A 910      29.023  39.498  19.729  1.00 54.53           C  
ANISOU  320  CG2 ILE A 910     6190   6547   7981    848   1042   -712       C  
ATOM    321  CD1 ILE A 910      26.269  39.274  21.055  1.00 63.30           C  
ANISOU  321  CD1 ILE A 910     7151   7797   9104   1198    761   -559       C  
ATOM    322  N   LYS A 911      31.671  37.227  19.433  1.00 68.41           N  
ANISOU  322  N   LYS A 911     7734   8977   9283    690    846   -960       N  
ATOM    323  CA  LYS A 911      33.076  37.562  19.279  1.00 62.03           C  
ANISOU  323  CA  LYS A 911     6759   8175   8636    485   1048  -1321       C  
ATOM    324  C   LYS A 911      33.234  38.891  18.543  1.00 66.20           C  
ANISOU  324  C   LYS A 911     7425   8186   9541    281   1484  -1328       C  
ATOM    325  O   LYS A 911      32.777  39.042  17.409  1.00 66.14           O  
ANISOU  325  O   LYS A 911     7779   7855   9496    338   1610   -898       O  
ATOM    326  CB  LYS A 911      33.822  36.446  18.542  1.00 59.94           C  
ANISOU  326  CB  LYS A 911     6535   8077   8164    501    952  -1207       C  
ATOM    327  CG  LYS A 911      35.345  36.583  18.598  1.00 63.76           C  
ANISOU  327  CG  LYS A 911     6723   8681   8823    316   1113  -1690       C  
ATOM    328  CD  LYS A 911      36.060  35.252  18.391  1.00 56.18           C  
ANISOU  328  CD  LYS A 911     5694   8056   7595    433    891  -1683       C  
ATOM    329  CE  LYS A 911      36.125  34.850  16.925  1.00 65.01           C  
ANISOU  329  CE  LYS A 911     7110   8936   8653    374   1034  -1309       C  
ATOM    330  NZ  LYS A 911      36.937  33.601  16.717  1.00 63.96           N  
ANISOU  330  NZ  LYS A 911     6875   9104   8323    469    858  -1372       N  
ATOM    331  N   LYS A 912      33.863  39.857  19.204  1.00 66.21           N  
ANISOU  331  N   LYS A 912     7153   8102   9902     81   1730  -1836       N  
ATOM    332  CA  LYS A 912      34.170  41.142  18.583  1.00 81.12           C  
ANISOU  332  CA  LYS A 912     9158   9414  12250   -155   2277  -1899       C  
ATOM    333  C   LYS A 912      35.594  41.090  18.037  1.00 84.90           C  
ANISOU  333  C   LYS A 912     9473   9834  12953   -425   2601  -2199       C  
ATOM    334  O   LYS A 912      36.557  41.011  18.803  1.00 89.42           O  
ANISOU  334  O   LYS A 912     9557  10718  13699   -569   2546  -2842       O  
ATOM    335  CB  LYS A 912      34.007  42.287  19.590  1.00 84.60           C  
ANISOU  335  CB  LYS A 912     9357   9711  13077   -267   2439  -2357       C  
ATOM    336  CG  LYS A 912      34.041  43.688  18.982  1.00 96.52           C  
ANISOU  336  CG  LYS A 912    11073  10488  15110   -469   3070  -2329       C  
ATOM    337  CD  LYS A 912      33.968  44.753  20.070  1.00101.25           C  
ANISOU  337  CD  LYS A 912    11356  10968  16145   -605   3221  -2904       C  
ATOM    338  CE  LYS A 912      33.525  46.107  19.521  1.00104.89           C  
ANISOU  338  CE  LYS A 912    12155  10629  17069   -679   3807  -2693       C  
ATOM    339  NZ  LYS A 912      34.546  46.749  18.647  1.00102.53           N  
ANISOU  339  NZ  LYS A 912    11954   9749  17255  -1003   4526  -2778       N  
ATOM    340  N   LEU A 913      35.730  41.122  16.715  1.00 81.58           N  
ANISOU  340  N   LEU A 913     9445   9045  12508   -455   2932  -1770       N  
ATOM    341  CA  LEU A 913      37.028  40.880  16.089  1.00 88.11           C  
ANISOU  341  CA  LEU A 913    10144   9839  13495   -691   3259  -1991       C  
ATOM    342  C   LEU A 913      38.000  42.043  16.228  1.00103.60           C  
ANISOU  342  C   LEU A 913    11818  11390  16158  -1098   3913  -2562       C  
ATOM    343  O   LEU A 913      37.608  43.215  16.218  1.00 88.77           O  
ANISOU  343  O   LEU A 913    10112   8974  14641  -1197   4341  -2521       O  
ATOM    344  CB  LEU A 913      36.852  40.538  14.612  1.00 87.54           C  
ANISOU  344  CB  LEU A 913    10631   9512  13119   -558   3451  -1349       C  
ATOM    345  CG  LEU A 913      36.437  39.090  14.359  1.00 89.90           C  
ANISOU  345  CG  LEU A 913    11026  10295  12838   -268   2853  -1034       C  
ATOM    346  CD1 LEU A 913      36.375  38.817  12.876  1.00 93.64           C  
ANISOU  346  CD1 LEU A 913    12017  10550  13014   -130   3053   -521       C  
ATOM    347  CD2 LEU A 913      37.407  38.141  15.041  1.00 87.97           C  
ANISOU  347  CD2 LEU A 913    10276  10573  12577   -351   2567  -1518       C  
ATOM    348  N   ILE A 914      39.277  41.693  16.342  1.00115.12           N  
ANISOU  348  N   ILE A 914    12810  13081  17850  -1330   4009  -3129       N  
ATOM    349  CA  ILE A 914      40.332  42.662  16.590  1.00132.38           C  
ANISOU  349  CA  ILE A 914    14537  14959  20804  -1765   4601  -3876       C  
ATOM    350  C   ILE A 914      41.175  42.909  15.337  1.00145.31           C  
ANISOU  350  C   ILE A 914    16372  16075  22762  -2049   5390  -3752       C  
ATOM    351  O   ILE A 914      41.417  41.990  14.552  1.00142.66           O  
ANISOU  351  O   ILE A 914    16249  15927  22029  -1921   5289  -3397       O  
ATOM    352  CB  ILE A 914      41.244  42.189  17.739  1.00129.28           C  
ANISOU  352  CB  ILE A 914    13341  15245  20536  -1808   4150  -4799       C  
ATOM    353  CG1 ILE A 914      40.432  41.399  18.770  1.00115.72           C  
ANISOU  353  CG1 ILE A 914    11601  14186  18183  -1367   3291  -4681       C  
ATOM    354  CG2 ILE A 914      41.952  43.371  18.382  1.00133.85           C  
ANISOU  354  CG2 ILE A 914    13342  15571  21943  -2205   4594  -5728       C  
ATOM    355  CD1 ILE A 914      41.248  40.915  19.946  1.00118.84           C  
ANISOU  355  CD1 ILE A 914    11312  15299  18541  -1248   2790  -5519       C  
ATOM    356  N   HIS A 915      41.606  44.158  15.165  1.00154.83           N  
ANISOU  356  N   HIS A 915    17525  16593  24709  -2434   6228  -4053       N  
ATOM    357  CA  HIS A 915      42.476  44.572  14.060  1.00155.96           C  
ANISOU  357  CA  HIS A 915    17846  16122  25290  -2762   7185  -4002       C  
ATOM    358  C   HIS A 915      41.856  44.332  12.684  1.00157.50           C  
ANISOU  358  C   HIS A 915    18977  15980  24885  -2452   7427  -2932       C  
ATOM    359  O   HIS A 915      42.381  43.554  11.889  1.00158.93           O  
ANISOU  359  O   HIS A 915    19283  16321  24781  -2415   7492  -2740       O  
ATOM    360  CB  HIS A 915      43.829  43.858  14.149  1.00152.07           C  
ANISOU  360  CB  HIS A 915    16665  16069  25045  -3004   7150  -4725       C  
ATOM    361  N   VAL A 916      40.749  45.017  12.406  1.00159.25           N  
ANISOU  361  N   VAL A 916    19843  15756  24908  -2190   7547  -2283       N  
ATOM    362  CA  VAL A 916      40.067  44.910  11.118  1.00156.80           C  
ANISOU  362  CA  VAL A 916    20451  15146  23979  -1785   7729  -1303       C  
ATOM    363  C   VAL A 916      40.961  45.452   9.996  1.00158.89           C  
ANISOU  363  C   VAL A 916    21092  14707  24571  -2024   8866  -1138       C  
ATOM    364  O   VAL A 916      41.917  46.184  10.262  1.00161.55           O  
ANISOU  364  O   VAL A 916    21034  14669  25680  -2443   9462  -1783       O  
ATOM    365  CB  VAL A 916      38.713  45.668  11.136  1.00120.29           C  
ANISOU  365  CB  VAL A 916    16380  10176  19147  -1404   7629   -736       C  
ATOM    366  CG1 VAL A 916      38.935  47.177  11.026  1.00132.87           C  
ANISOU  366  CG1 VAL A 916    18197  10813  21474  -1660   8671   -785       C  
ATOM    367  CG2 VAL A 916      37.788  45.170  10.030  1.00109.77           C  
ANISOU  367  CG2 VAL A 916    15847   8915  16947   -804   7337    170       C  
ATOM    368  N   SER A 917      40.650  45.077   8.755  1.00155.57           N  
ANISOU  368  N   SER A 917    21443  14190  23477  -1633   8994   -352       N  
ATOM    369  CA  SER A 917      41.423  45.479   7.578  1.00159.79           C  
ANISOU  369  CA  SER A 917    22456  14205  24052  -1612   9807   -153       C  
ATOM    370  C   SER A 917      42.873  45.024   7.695  1.00161.82           C  
ANISOU  370  C   SER A 917    22044  14652  24790  -2078   9975   -917       C  
ATOM    371  O   SER A 917      43.805  45.797   7.467  1.00169.45           O  
ANISOU  371  O   SER A 917    22937  15093  26355  -2321  10662  -1316       O  
ATOM    372  CB  SER A 917      41.357  46.995   7.368  1.00168.79           C  
ANISOU  372  CB  SER A 917    23974  14545  25613  -1534  10545    -79       C  
ATOM    373  OG  SER A 917      40.031  47.417   7.101  1.00169.83           O  
ANISOU  373  OG  SER A 917    24777  14531  25219   -988  10347    659       O  
ATOM    374  N   GLY A 918      43.046  43.757   8.053  1.00155.97           N  
ANISOU  374  N   GLY A 918    20808  14677  23777  -2150   9337  -1142       N  
ATOM    375  CA  GLY A 918      44.359  43.162   8.212  1.00153.50           C  
ANISOU  375  CA  GLY A 918    19823  14674  23828  -2493   9296  -1872       C  
ATOM    376  C   GLY A 918      44.217  41.713   8.632  1.00139.56           C  
ANISOU  376  C   GLY A 918    17611  13831  21584  -2365   8483  -1981       C  
ATOM    377  O   GLY A 918      43.703  40.887   7.877  1.00130.06           O  
ANISOU  377  O   GLY A 918    16919  12889  19607  -1961   8119  -1375       O  
ATOM    378  N   GLN A 919      44.667  41.404   9.844  1.00137.35           N  
ANISOU  378  N   GLN A 919    16446  14062  21676  -2563   7952  -2791       N  
ATOM    379  CA  GLN A 919      44.517  40.061  10.385  1.00129.90           C  
ANISOU  379  CA  GLN A 919    15177  13973  20206  -2265   6892  -2903       C  
ATOM    380  C   GLN A 919      43.058  39.797  10.740  1.00120.08           C  
ANISOU  380  C   GLN A 919    14336  12963  18326  -1820   6116  -2329       C  
ATOM    381  O   GLN A 919      42.577  38.672  10.626  1.00107.29           O  
ANISOU  381  O   GLN A 919    12859  11822  16084  -1475   5432  -2015       O  
ATOM    382  CB  GLN A 919      45.408  39.869  11.614  1.00130.45           C  
ANISOU  382  CB  GLN A 919    14249  14530  20787  -2490   6538  -3923       C  
ATOM    383  N   GLY A 920      42.356  40.847  11.154  1.00122.06           N  
ANISOU  383  N   GLY A 920    14749  12833  18797  -1845   6276  -2229       N  
ATOM    384  CA  GLY A 920      40.975  40.728  11.588  1.00115.74           C  
ANISOU  384  CA  GLY A 920    14235  12222  17517  -1462   5603  -1788       C  
ATOM    385  C   GLY A 920      39.984  40.386  10.490  1.00113.71           C  
ANISOU  385  C   GLY A 920    14770  11864  16569  -1032   5470   -919       C  
ATOM    386  O   GLY A 920      39.119  39.534  10.679  1.00108.37           O  
ANISOU  386  O   GLY A 920    14164  11634  15379   -697   4715   -666       O  
ATOM    387  N   ASP A 921      40.103  41.046   9.343  1.00117.21           N  
ANISOU  387  N   ASP A 921    15811  11720  17002  -1014   6225   -489       N  
ATOM    388  CA  ASP A 921      39.159  40.836   8.252  1.00108.05           C  
ANISOU  388  CA  ASP A 921    15439  10485  15132   -511   6092    295       C  
ATOM    389  C   ASP A 921      39.353  39.471   7.596  1.00100.89           C  
ANISOU  389  C   ASP A 921    14578  10085  13671   -320   5667    405       C  
ATOM    390  O   ASP A 921      38.384  38.823   7.195  1.00 91.82           O  
ANISOU  390  O   ASP A 921    13746   9225  11914    114   5070    797       O  
ATOM    391  CB  ASP A 921      39.288  41.942   7.206  1.00109.98           C  
ANISOU  391  CB  ASP A 921    16397   9950  15442   -455   7075    756       C  
ATOM    392  CG  ASP A 921      38.093  42.001   6.279  1.00112.04           C  
ANISOU  392  CG  ASP A 921    17487  10132  14951    198   6847   1537       C  
ATOM    393  OD1 ASP A 921      36.957  41.793   6.759  1.00 98.52           O  
ANISOU  393  OD1 ASP A 921    15721   8732  12979    505   6074   1644       O  
ATOM    394  OD2 ASP A 921      38.288  42.254   5.073  1.00129.07           O  
ANISOU  394  OD2 ASP A 921    20342  11932  16767    438   7445   2016       O  
ATOM    395  N   ARG A 922      40.606  39.043   7.484  1.00101.86           N  
ANISOU  395  N   ARG A 922    14340  10307  14055   -645   5985     -2       N  
ATOM    396  CA  ARG A 922      40.916  37.723   6.946  1.00 98.39           C  
ANISOU  396  CA  ARG A 922    13870  10340  13176   -500   5612     12       C  
ATOM    397  C   ARG A 922      40.359  36.637   7.865  1.00 80.63           C  
ANISOU  397  C   ARG A 922    11190   8723  10723   -348   4616   -176       C  
ATOM    398  O   ARG A 922      39.799  35.644   7.400  1.00 74.99           O  
ANISOU  398  O   ARG A 922    10681   8328   9482    -33   4106     85       O  
ATOM    399  CB  ARG A 922      42.426  37.550   6.765  1.00109.44           C  
ANISOU  399  CB  ARG A 922    14874  11708  15002   -896   6179   -476       C  
ATOM    400  CG  ARG A 922      42.823  36.231   6.124  1.00116.08           C  
ANISOU  400  CG  ARG A 922    15709  12979  15417   -742   5885   -468       C  
ATOM    401  CD  ARG A 922      42.216  36.092   4.736  1.00128.72           C  
ANISOU  401  CD  ARG A 922    18156  14438  16315   -335   6024    207       C  
ATOM    402  NE  ARG A 922      42.376  34.747   4.189  1.00132.66           N  
ANISOU  402  NE  ARG A 922    18644  15399  16363   -137   5596    192       N  
ATOM    403  CZ  ARG A 922      41.477  33.775   4.319  1.00131.93           C  
ANISOU  403  CZ  ARG A 922    18557  15739  15830    189   4733    313       C  
ATOM    404  NH1 ARG A 922      40.348  33.994   4.980  1.00127.58           N  
ANISOU  404  NH1 ARG A 922    18011  15244  15220    354   4210    465       N  
ATOM    405  NH2 ARG A 922      41.706  32.582   3.788  1.00133.85           N  
ANISOU  405  NH2 ARG A 922    18781  16330  15747    333   4440    247       N  
ATOM    406  N   GLU A 923      40.511  36.838   9.171  1.00 73.35           N  
ANISOU  406  N   GLU A 923     9686   7959  10224   -557   4385   -648       N  
ATOM    407  CA  GLU A 923      39.942  35.928  10.157  1.00 77.58           C  
ANISOU  407  CA  GLU A 923     9887   9022  10568   -382   3554   -774       C  
ATOM    408  C   GLU A 923      38.424  35.836  10.005  1.00 77.78           C  
ANISOU  408  C   GLU A 923    10330   9052  10169    -24   3114   -258       C  
ATOM    409  O   GLU A 923      37.853  34.746  10.071  1.00 71.55           O  
ANISOU  409  O   GLU A 923     9524   8621   9040    204   2541   -144       O  
ATOM    410  CB  GLU A 923      40.305  36.375  11.577  1.00 83.18           C  
ANISOU  410  CB  GLU A 923     9994   9872  11739   -595   3448  -1350       C  
ATOM    411  CG  GLU A 923      41.725  36.044  12.006  1.00 89.66           C  
ANISOU  411  CG  GLU A 923    10200  10952  12913   -830   3548  -2024       C  
ATOM    412  CD  GLU A 923      42.081  36.639  13.360  1.00103.88           C  
ANISOU  412  CD  GLU A 923    11409  12909  15151   -988   3444  -2678       C  
ATOM    413  OE1 GLU A 923      41.201  36.669  14.249  1.00105.25           O  
ANISOU  413  OE1 GLU A 923    11579  13260  15151   -799   2993  -2600       O  
ATOM    414  OE2 GLU A 923      43.237  37.084  13.535  1.00108.28           O  
ANISOU  414  OE2 GLU A 923    11479  13421  16240  -1294   3827  -3321       O  
ATOM    415  N   PHE A 924      37.786  36.988   9.799  1.00 76.53           N  
ANISOU  415  N   PHE A 924    10523   8468  10088     28   3417     15       N  
ATOM    416  CA  PHE A 924      36.339  37.071   9.610  1.00 65.72           C  
ANISOU  416  CA  PHE A 924     9518   7079   8374    399   3031    450       C  
ATOM    417  C   PHE A 924      35.874  36.211   8.441  1.00 65.23           C  
ANISOU  417  C   PHE A 924     9857   7183   7744    751   2762    810       C  
ATOM    418  O   PHE A 924      34.969  35.391   8.584  1.00 61.90           O  
ANISOU  418  O   PHE A 924     9368   7080   7073    979   2151    871       O  
ATOM    419  CB  PHE A 924      35.914  38.528   9.385  1.00 82.22           C  
ANISOU  419  CB  PHE A 924    11989   8614  10638    450   3513    702       C  
ATOM    420  CG  PHE A 924      34.426  38.722   9.305  1.00 71.73           C  
ANISOU  420  CG  PHE A 924    10952   7283   9021    865   3089   1066       C  
ATOM    421  CD1 PHE A 924      33.657  38.777  10.460  1.00 68.77           C  
ANISOU  421  CD1 PHE A 924    10221   7078   8831    854   2675    884       C  
ATOM    422  CD2 PHE A 924      33.795  38.853   8.078  1.00 71.65           C  
ANISOU  422  CD2 PHE A 924    11559   7127   8537   1311   3103   1554       C  
ATOM    423  CE1 PHE A 924      32.284  38.955  10.391  1.00 65.33           C  
ANISOU  423  CE1 PHE A 924     9980   6643   8199   1225   2304   1155       C  
ATOM    424  CE2 PHE A 924      32.425  39.032   8.004  1.00 76.46           C  
ANISOU  424  CE2 PHE A 924    12360   7782   8911   1739   2659   1801       C  
ATOM    425  CZ  PHE A 924      31.670  39.083   9.161  1.00 71.04           C  
ANISOU  425  CZ  PHE A 924    11254   7240   8498   1669   2272   1587       C  
ATOM    426  N   MET A 925      36.502  36.406   7.286  1.00 69.21           N  
ANISOU  426  N   MET A 925    10768   7460   8067    789   3261   1004       N  
ATOM    427  CA  MET A 925      36.167  35.645   6.089  1.00 75.72           C  
ANISOU  427  CA  MET A 925    12004   8464   8302   1157   3043   1289       C  
ATOM    428  C   MET A 925      36.526  34.171   6.232  1.00 78.53           C  
ANISOU  428  C   MET A 925    11975   9293   8569   1083   2593   1003       C  
ATOM    429  O   MET A 925      35.865  33.309   5.652  1.00 81.58           O  
ANISOU  429  O   MET A 925    12504   9943   8551   1385   2131   1106       O  
ATOM    430  CB  MET A 925      36.870  36.234   4.867  1.00 75.80           C  
ANISOU  430  CB  MET A 925    12582   8106   8113   1226   3790   1565       C  
ATOM    431  CG  MET A 925      36.218  37.495   4.312  1.00 92.19           C  
ANISOU  431  CG  MET A 925    15304   9707  10016   1554   4170   2043       C  
ATOM    432  SD  MET A 925      34.650  37.180   3.475  1.00200.64           S  
ANISOU  432  SD  MET A 925    29541  23717  22978   2326   3446   2441       S  
ATOM    433  CE  MET A 925      33.477  37.594   4.761  1.00 77.45           C  
ANISOU  433  CE  MET A 925    13520   8150   7758   2313   2909   2315       C  
ATOM    434  N   ALA A 926      37.573  33.888   7.001  1.00 76.33           N  
ANISOU  434  N   ALA A 926    11196   9118   8687    710   2727    602       N  
ATOM    435  CA  ALA A 926      37.995  32.511   7.225  1.00 72.38           C  
ANISOU  435  CA  ALA A 926    10341   9023   8135    677   2341    340       C  
ATOM    436  C   ALA A 926      36.870  31.728   7.882  1.00 61.15           C  
ANISOU  436  C   ALA A 926     8753   7872   6609    863   1655    363       C  
ATOM    437  O   ALA A 926      36.544  30.622   7.461  1.00 62.61           O  
ANISOU  437  O   ALA A 926     8964   8277   6548   1035   1300    379       O  
ATOM    438  CB  ALA A 926      39.255  32.461   8.079  1.00 65.46           C  
ANISOU  438  CB  ALA A 926     8926   8240   7708    335   2545   -131       C  
ATOM    439  N   GLU A 927      36.264  32.318   8.904  1.00 59.10           N  
ANISOU  439  N   GLU A 927     8319   7560   6575    817   1526    337       N  
ATOM    440  CA  GLU A 927      35.168  31.662   9.599  1.00 64.00           C  
ANISOU  440  CA  GLU A 927     8779   8380   7160    964    993    358       C  
ATOM    441  C   GLU A 927      33.913  31.637   8.735  1.00 65.03           C  
ANISOU  441  C   GLU A 927     9244   8468   6997   1276    735    631       C  
ATOM    442  O   GLU A 927      33.214  30.625   8.678  1.00 67.45           O  
ANISOU  442  O   GLU A 927     9453   8966   7208   1412    328    593       O  
ATOM    443  CB  GLU A 927      34.887  32.353  10.931  1.00 56.67           C  
ANISOU  443  CB  GLU A 927     7585   7419   6529    847    975    234       C  
ATOM    444  CG  GLU A 927      36.097  32.430  11.838  1.00 58.73           C  
ANISOU  444  CG  GLU A 927     7463   7797   7053    611   1148   -142       C  
ATOM    445  CD  GLU A 927      35.716  32.508  13.297  1.00 69.04           C  
ANISOU  445  CD  GLU A 927     8467   9262   8501    615    923   -316       C  
ATOM    446  OE1 GLU A 927      34.584  32.100  13.628  1.00 74.12           O  
ANISOU  446  OE1 GLU A 927     9164   9960   9038    779    625   -132       O  
ATOM    447  OE2 GLU A 927      36.542  32.981  14.109  1.00 71.99           O  
ANISOU  447  OE2 GLU A 927     8535   9717   9100    468   1059   -679       O  
ATOM    448  N   MET A 928      33.638  32.747   8.056  1.00 64.26           N  
ANISOU  448  N   MET A 928     9532   8107   6777   1418    986    874       N  
ATOM    449  CA  MET A 928      32.458  32.843   7.205  1.00 68.91           C  
ANISOU  449  CA  MET A 928    10449   8700   7032   1824    696   1099       C  
ATOM    450  C   MET A 928      32.480  31.780   6.108  1.00 68.30           C  
ANISOU  450  C   MET A 928    10522   8859   6569   2037    460   1067       C  
ATOM    451  O   MET A 928      31.448  31.185   5.796  1.00 71.72           O  
ANISOU  451  O   MET A 928    10911   9486   6853   2299    -24   1000       O  
ATOM    452  CB  MET A 928      32.349  34.241   6.582  1.00 68.97           C  
ANISOU  452  CB  MET A 928    10952   8350   6903   2026   1088   1419       C  
ATOM    453  CG  MET A 928      32.000  35.351   7.567  1.00 62.94           C  
ANISOU  453  CG  MET A 928    10068   7323   6521   1901   1250   1437       C  
ATOM    454  SD  MET A 928      30.288  35.310   8.157  1.00 73.06           S  
ANISOU  454  SD  MET A 928    11142   8756   7864   2171    638   1414       S  
ATOM    455  CE  MET A 928      29.411  35.795   6.672  1.00 77.41           C  
ANISOU  455  CE  MET A 928    12298   9240   7876   2830    484   1756       C  
ATOM    456  N   GLU A 929      33.659  31.529   5.542  1.00 64.97           N  
ANISOU  456  N   GLU A 929    10226   8426   6033   1910    811   1045       N  
ATOM    457  CA  GLU A 929      33.788  30.600   4.419  1.00 69.29           C  
ANISOU  457  CA  GLU A 929    10961   9185   6181   2123    656    998       C  
ATOM    458  C   GLU A 929      33.958  29.141   4.836  1.00 70.78           C  
ANISOU  458  C   GLU A 929    10714   9633   6545   1959    326    676       C  
ATOM    459  O   GLU A 929      33.967  28.251   3.989  1.00 75.01           O  
ANISOU  459  O   GLU A 929    11335  10351   6817   2120    141    559       O  
ATOM    460  CB  GLU A 929      34.964  31.000   3.531  1.00 77.10           C  
ANISOU  460  CB  GLU A 929    12326  10016   6951   2089   1261   1130       C  
ATOM    461  CG  GLU A 929      34.669  32.150   2.591  1.00101.05           C  
ANISOU  461  CG  GLU A 929    16013  12796   9585   2448   1593   1526       C  
ATOM    462  CD  GLU A 929      35.525  32.100   1.344  1.00118.27           C  
ANISOU  462  CD  GLU A 929    18674  14929  11332   2589   2069   1664       C  
ATOM    463  OE1 GLU A 929      36.569  32.785   1.312  1.00129.43           O  
ANISOU  463  OE1 GLU A 929    20216  16012  12949   2317   2813   1756       O  
ATOM    464  OE2 GLU A 929      35.155  31.372   0.397  1.00120.73           O  
ANISOU  464  OE2 GLU A 929    19216  15533  11124   2968   1727   1634       O  
ATOM    465  N   THR A 930      34.104  28.895   6.133  1.00 68.43           N  
ANISOU  465  N   THR A 930     9987   9342   6671   1680    275    534       N  
ATOM    466  CA  THR A 930      34.281  27.534   6.629  1.00 63.61           C  
ANISOU  466  CA  THR A 930     9027   8906   6233   1574     37    296       C  
ATOM    467  C   THR A 930      33.136  27.138   7.549  1.00 57.94           C  
ANISOU  467  C   THR A 930     8040   8212   5763   1586   -309    244       C  
ATOM    468  O   THR A 930      32.131  26.587   7.101  1.00 63.34           O  
ANISOU  468  O   THR A 930     8709   8957   6402   1754   -632    163       O  
ATOM    469  CB  THR A 930      35.617  27.367   7.386  1.00 60.63           C  
ANISOU  469  CB  THR A 930     8396   8551   6090   1315    311    154       C  
ATOM    470  OG1 THR A 930      35.682  28.313   8.465  1.00 59.44           O  
ANISOU  470  OG1 THR A 930     8087   8309   6189   1164    450    167       O  
ATOM    471  CG2 THR A 930      36.791  27.583   6.445  1.00 54.47           C  
ANISOU  471  CG2 THR A 930     7804   7740   5152   1261    710    128       C  
ATOM    472  N   ILE A 931      33.295  27.426   8.836  1.00 49.94           N  
ANISOU  472  N   ILE A 931     6794   7157   5023   1416   -218    242       N  
ATOM    473  CA  ILE A 931      32.282  27.092   9.826  1.00 57.12           C  
ANISOU  473  CA  ILE A 931     7475   8059   6168   1416   -427    220       C  
ATOM    474  C   ILE A 931      30.938  27.741   9.488  1.00 65.83           C  
ANISOU  474  C   ILE A 931     8660   9094   7258   1573   -619    291       C  
ATOM    475  O   ILE A 931      29.880  27.192   9.791  1.00 70.74           O  
ANISOU  475  O   ILE A 931     9090   9719   8070   1615   -839    196       O  
ATOM    476  CB  ILE A 931      32.729  27.510  11.253  1.00 66.75           C  
ANISOU  476  CB  ILE A 931     8503   9283   7574   1278   -271    212       C  
ATOM    477  CG1 ILE A 931      31.727  27.013  12.293  1.00 67.48           C  
ANISOU  477  CG1 ILE A 931     8413   9359   7865   1303   -404    219       C  
ATOM    478  CG2 ILE A 931      32.921  29.022  11.362  1.00 62.94           C  
ANISOU  478  CG2 ILE A 931     8115   8692   7105   1210    -58    274       C  
ATOM    479  CD1 ILE A 931      31.457  25.531  12.198  1.00 75.95           C  
ANISOU  479  CD1 ILE A 931     9406  10427   9026   1346   -509    156       C  
ATOM    480  N   GLY A 932      30.984  28.893   8.826  1.00 69.97           N  
ANISOU  480  N   GLY A 932     9469   9536   7581   1685   -503    444       N  
ATOM    481  CA  GLY A 932      29.780  29.628   8.495  1.00 68.88           C  
ANISOU  481  CA  GLY A 932     9440   9343   7389   1927   -697    526       C  
ATOM    482  C   GLY A 932      28.964  28.988   7.390  1.00 74.24           C  
ANISOU  482  C   GLY A 932    10176  10175   7858   2225  -1079    393       C  
ATOM    483  O   GLY A 932      27.803  29.344   7.188  1.00 78.66           O  
ANISOU  483  O   GLY A 932    10702  10762   8422   2475  -1362    346       O  
ATOM    484  N   LYS A 933      29.562  28.043   6.671  1.00 73.74           N  
ANISOU  484  N   LYS A 933    10162  10234   7621   2226  -1113    269       N  
ATOM    485  CA  LYS A 933      28.872  27.402   5.556  1.00 68.74           C  
ANISOU  485  CA  LYS A 933     9564   9791   6761   2528  -1498     43       C  
ATOM    486  C   LYS A 933      28.643  25.906   5.775  1.00 74.22           C  
ANISOU  486  C   LYS A 933     9870  10554   7775   2361  -1681   -312       C  
ATOM    487  O   LYS A 933      28.227  25.199   4.862  1.00 76.00           O  
ANISOU  487  O   LYS A 933    10054  10943   7879   2554  -1982   -614       O  
ATOM    488  CB  LYS A 933      29.648  27.624   4.255  1.00 69.81           C  
ANISOU  488  CB  LYS A 933    10171  10009   6345   2766  -1373    165       C  
ATOM    489  CG  LYS A 933      29.770  29.089   3.861  1.00 84.41           C  
ANISOU  489  CG  LYS A 933    12495  11710   7867   3000  -1115    545       C  
ATOM    490  CD  LYS A 933      30.163  29.251   2.405  1.00 91.81           C  
ANISOU  490  CD  LYS A 933    13972  12746   8163   3390  -1036    668       C  
ATOM    491  CE  LYS A 933      28.998  29.779   1.585  1.00100.95           C  
ANISOU  491  CE  LYS A 933    15405  14053   8897   4010  -1445    696       C  
ATOM    492  NZ  LYS A 933      28.517  31.091   2.105  1.00104.14           N  
ANISOU  492  NZ  LYS A 933    15956  14201   9413   4115  -1300   1012       N  
ATOM    493  N   ILE A 934      28.914  25.425   6.985  1.00 73.82           N  
ANISOU  493  N   ILE A 934     9555  10367   8125   2038  -1479   -292       N  
ATOM    494  CA  ILE A 934      28.659  24.027   7.321  1.00 69.33           C  
ANISOU  494  CA  ILE A 934     8668   9751   7922   1886  -1536   -563       C  
ATOM    495  C   ILE A 934      28.059  23.886   8.717  1.00 75.61           C  
ANISOU  495  C   ILE A 934     9182  10370   9175   1691  -1400   -521       C  
ATOM    496  O   ILE A 934      28.184  24.783   9.552  1.00 72.64           O  
ANISOU  496  O   ILE A 934     8859   9948   8791   1637  -1238   -279       O  
ATOM    497  CB  ILE A 934      29.944  23.174   7.250  1.00 66.13           C  
ANISOU  497  CB  ILE A 934     8337   9339   7451   1761  -1326   -552       C  
ATOM    498  CG1 ILE A 934      30.983  23.684   8.252  1.00 70.73           C  
ANISOU  498  CG1 ILE A 934     8982   9867   8027   1608  -1004   -273       C  
ATOM    499  CG2 ILE A 934      30.508  23.154   5.835  1.00 61.75           C  
ANISOU  499  CG2 ILE A 934     8051   8954   6455   1948  -1409   -635       C  
ATOM    500  CD1 ILE A 934      32.292  22.927   8.214  1.00 74.57           C  
ANISOU  500  CD1 ILE A 934     9495  10383   8453   1542   -827   -299       C  
ATOM    501  N   LYS A 935      27.397  22.757   8.957  1.00 81.74           N  
ANISOU  501  N   LYS A 935     9668  11024  10365   1591  -1418   -781       N  
ATOM    502  CA  LYS A 935      26.841  22.442  10.272  1.00 79.27           C  
ANISOU  502  CA  LYS A 935     9139  10492  10488   1417  -1172   -721       C  
ATOM    503  C   LYS A 935      27.159  20.994  10.645  1.00 79.39           C  
ANISOU  503  C   LYS A 935     9072  10290  10802   1283   -925   -793       C  
ATOM    504  O   LYS A 935      27.067  20.097   9.807  1.00 88.76           O  
ANISOU  504  O   LYS A 935    10159  11446  12121   1280  -1037  -1106       O  
ATOM    505  CB  LYS A 935      25.325  22.678  10.301  1.00 73.94           C  
ANISOU  505  CB  LYS A 935     8149   9773  10172   1434  -1334   -982       C  
ATOM    506  CG  LYS A 935      24.894  24.140  10.173  1.00 80.19           C  
ANISOU  506  CG  LYS A 935     9028  10717  10725   1614  -1530   -862       C  
ATOM    507  CD  LYS A 935      25.382  24.989  11.343  1.00 83.23           C  
ANISOU  507  CD  LYS A 935     9570  11037  11018   1526  -1239   -478       C  
ATOM    508  CE  LYS A 935      24.609  26.306  11.453  1.00 83.65           C  
ANISOU  508  CE  LYS A 935     9607  11128  11047   1665  -1364   -427       C  
ATOM    509  NZ  LYS A 935      24.665  27.131  10.211  1.00 79.63           N  
ANISOU  509  NZ  LYS A 935     9340  10774  10141   1956  -1659   -410       N  
ATOM    510  N   HIS A 936      27.535  20.772  11.902  1.00 67.02           N  
ANISOU  510  N   HIS A 936     7575   8571   9319   1219   -583   -512       N  
ATOM    511  CA  HIS A 936      27.878  19.435  12.382  1.00 58.06           C  
ANISOU  511  CA  HIS A 936     6457   7176   8426   1175   -277   -480       C  
ATOM    512  C   HIS A 936      27.778  19.357  13.906  1.00 68.31           C  
ANISOU  512  C   HIS A 936     7837   8294   9824   1190    110   -164       C  
ATOM    513  O   HIS A 936      28.084  20.321  14.609  1.00 70.23           O  
ANISOU  513  O   HIS A 936     8190   8722   9772   1267    102     59       O  
ATOM    514  CB  HIS A 936      29.289  19.045  11.922  1.00 63.24           C  
ANISOU  514  CB  HIS A 936     7320   7961   8746   1276   -317   -411       C  
ATOM    515  CG  HIS A 936      29.667  17.630  12.243  1.00 55.31           C  
ANISOU  515  CG  HIS A 936     6361   6672   7981   1298    -36   -393       C  
ATOM    516  ND1 HIS A 936      30.032  17.226  13.507  1.00 59.45           N  
ANISOU  516  ND1 HIS A 936     7046   7037   8506   1419    299    -70       N  
ATOM    517  CD2 HIS A 936      29.745  16.528  11.459  1.00 57.80           C  
ANISOU  517  CD2 HIS A 936     6614   6820   8526   1263    -25   -659       C  
ATOM    518  CE1 HIS A 936      30.312  15.933  13.493  1.00 73.27           C  
ANISOU  518  CE1 HIS A 936     8863   8491  10484   1472    533    -86       C  
ATOM    519  NE2 HIS A 936      30.147  15.486  12.259  1.00 56.65           N  
ANISOU  519  NE2 HIS A 936     6601   6361   8561   1346    350   -462       N  
ATOM    520  N   ARG A 937      27.359  18.195  14.403  1.00 75.28           N  
ANISOU  520  N   ARG A 937     8687   8797  11119   1136    485   -163       N  
ATOM    521  CA  ARG A 937      27.158  17.960  15.834  1.00 71.19           C  
ANISOU  521  CA  ARG A 937     8321   8052  10678   1208    949    167       C  
ATOM    522  C   ARG A 937      28.372  18.321  16.704  1.00 67.40           C  
ANISOU  522  C   ARG A 937     8162   7823   9624   1492    957    533       C  
ATOM    523  O   ARG A 937      28.212  18.775  17.838  1.00 70.49           O  
ANISOU  523  O   ARG A 937     8674   8253   9856   1612   1150    768       O  
ATOM    524  CB  ARG A 937      26.772  16.491  16.059  1.00 82.01           C  
ANISOU  524  CB  ARG A 937     9704   8895  12563   1144   1441    149       C  
ATOM    525  CG  ARG A 937      26.590  16.090  17.516  1.00 96.97           C  
ANISOU  525  CG  ARG A 937    11871  10481  14493   1290   2040    563       C  
ATOM    526  CD  ARG A 937      25.939  14.713  17.651  1.00114.30           C  
ANISOU  526  CD  ARG A 937    14051  12020  17358   1155   2658    513       C  
ATOM    527  NE  ARG A 937      26.849  13.607  17.357  1.00121.88           N  
ANISOU  527  NE  ARG A 937    15241  12776  18291   1317   2768    599       N  
ATOM    528  CZ  ARG A 937      26.932  12.992  16.180  1.00126.49           C  
ANISOU  528  CZ  ARG A 937    15596  13269  19194   1143   2567    185       C  
ATOM    529  NH1 ARG A 937      27.788  11.993  16.012  1.00129.89           N  
ANISOU  529  NH1 ARG A 937    16260  13493  19600   1321   2707    286       N  
ATOM    530  NH2 ARG A 937      26.159  13.372  15.171  1.00126.49           N  
ANISOU  530  NH2 ARG A 937    15141  13409  19511    842   2205   -354       N  
ATOM    531  N   ASN A 938      29.577  18.123  16.171  1.00 58.44           N  
ANISOU  531  N   ASN A 938     7131   6886   8188   1619    739    517       N  
ATOM    532  CA  ASN A 938      30.804  18.389  16.917  1.00 59.92           C  
ANISOU  532  CA  ASN A 938     7525   7355   7887   1913    692    731       C  
ATOM    533  C   ASN A 938      31.539  19.645  16.459  1.00 65.27           C  
ANISOU  533  C   ASN A 938     8110   8459   8232   1872    321    593       C  
ATOM    534  O   ASN A 938      32.731  19.810  16.726  1.00 67.59           O  
ANISOU  534  O   ASN A 938     8460   9017   8205   2064    218    601       O  
ATOM    535  CB  ASN A 938      31.749  17.191  16.822  1.00 68.64           C  
ANISOU  535  CB  ASN A 938     8792   8351   8938   2137    789    796       C  
ATOM    536  CG  ASN A 938      31.170  15.947  17.454  1.00 69.55           C  
ANISOU  536  CG  ASN A 938     9092   7966   9368   2240   1280   1009       C  
ATOM    537  OD1 ASN A 938      30.854  14.980  16.765  1.00 74.50           O  
ANISOU  537  OD1 ASN A 938     9660   8237  10412   2094   1433    864       O  
ATOM    538  ND2 ASN A 938      31.035  15.960  18.775  1.00 59.60           N  
ANISOU  538  ND2 ASN A 938     8077   6654   7913   2509   1575   1342       N  
ATOM    539  N   LEU A 939      30.833  20.519  15.755  1.00 62.68           N  
ANISOU  539  N   LEU A 939     7628   8174   8011   1643    147    441       N  
ATOM    540  CA  LEU A 939      31.373  21.827  15.423  1.00 63.51           C  
ANISOU  540  CA  LEU A 939     7700   8574   7858   1596    -73    366       C  
ATOM    541  C   LEU A 939      30.512  22.898  16.075  1.00 67.36           C  
ANISOU  541  C   LEU A 939     8129   9075   8388   1536    -51    417       C  
ATOM    542  O   LEU A 939      29.285  22.846  15.985  1.00 67.38           O  
ANISOU  542  O   LEU A 939     8036   8893   8671   1437    -12    389       O  
ATOM    543  CB  LEU A 939      31.427  22.036  13.909  1.00 53.18           C  
ANISOU  543  CB  LEU A 939     6360   7305   6542   1472   -278    186       C  
ATOM    544  CG  LEU A 939      32.164  20.987  13.072  1.00 59.08           C  
ANISOU  544  CG  LEU A 939     7146   8033   7269   1509   -304     74       C  
ATOM    545  CD1 LEU A 939      32.166  21.400  11.608  1.00 60.70           C  
ANISOU  545  CD1 LEU A 939     7376   8332   7356   1440   -495    -94       C  
ATOM    546  CD2 LEU A 939      33.588  20.749  13.573  1.00 51.08           C  
ANISOU  546  CD2 LEU A 939     6184   7182   6043   1661   -239    116       C  
ATOM    547  N   VAL A 940      31.151  23.849  16.751  1.00 65.57           N  
ANISOU  547  N   VAL A 940     7916   9068   7929   1599    -70    428       N  
ATOM    548  CA  VAL A 940      30.433  24.990  17.303  1.00 60.39           C  
ANISOU  548  CA  VAL A 940     7203   8430   7312   1541    -53    435       C  
ATOM    549  C   VAL A 940      29.722  25.713  16.172  1.00 55.31           C  
ANISOU  549  C   VAL A 940     6508   7698   6809   1391   -202    359       C  
ATOM    550  O   VAL A 940      30.351  26.100  15.194  1.00 62.82           O  
ANISOU  550  O   VAL A 940     7517   8712   7639   1351   -309    297       O  
ATOM    551  CB  VAL A 940      31.370  25.967  18.036  1.00 69.47           C  
ANISOU  551  CB  VAL A 940     8331   9836   8229   1606    -72    343       C  
ATOM    552  CG1 VAL A 940      30.629  27.237  18.411  1.00 64.45           C  
ANISOU  552  CG1 VAL A 940     7634   9174   7682   1517    -50    308       C  
ATOM    553  CG2 VAL A 940      31.962  25.310  19.269  1.00 74.36           C  
ANISOU  553  CG2 VAL A 940     9012  10620   8620   1883      6    389       C  
ATOM    554  N   PRO A 941      28.396  25.864  16.283  1.00 53.38           N  
ANISOU  554  N   PRO A 941     6166   7308   6809   1350   -191    357       N  
ATOM    555  CA  PRO A 941      27.640  26.517  15.211  1.00 61.37           C  
ANISOU  555  CA  PRO A 941     7130   8275   7911   1324   -397    264       C  
ATOM    556  C   PRO A 941      27.839  28.030  15.188  1.00 62.50           C  
ANISOU  556  C   PRO A 941     7356   8474   7918   1338   -424    302       C  
ATOM    557  O   PRO A 941      27.775  28.681  16.231  1.00 55.38           O  
ANISOU  557  O   PRO A 941     6414   7587   7041   1325   -292    327       O  
ATOM    558  CB  PRO A 941      26.186  26.166  15.546  1.00 59.41           C  
ANISOU  558  CB  PRO A 941     6670   7870   8034   1296   -356    178       C  
ATOM    559  CG  PRO A 941      26.184  25.976  17.026  1.00 55.75           C  
ANISOU  559  CG  PRO A 941     6215   7365   7603   1293    -44    311       C  
ATOM    560  CD  PRO A 941      27.520  25.369  17.360  1.00 55.31           C  
ANISOU  560  CD  PRO A 941     6339   7415   7260   1367     38    425       C  
ATOM    561  N   LEU A 942      28.095  28.573  14.003  1.00 66.03           N  
ANISOU  561  N   LEU A 942     7947   8927   8215   1385   -550    304       N  
ATOM    562  CA  LEU A 942      28.098  30.012  13.809  1.00 62.43           C  
ANISOU  562  CA  LEU A 942     7620   8409   7693   1423   -508    372       C  
ATOM    563  C   LEU A 942      26.673  30.452  13.484  1.00 64.86           C  
ANISOU  563  C   LEU A 942     7865   8637   8140   1579   -697    352       C  
ATOM    564  O   LEU A 942      26.166  30.184  12.399  1.00 68.20           O  
ANISOU  564  O   LEU A 942     8334   9090   8488   1746   -936    299       O  
ATOM    565  CB  LEU A 942      29.069  30.417  12.698  1.00 58.74           C  
ANISOU  565  CB  LEU A 942     7413   7929   6977   1447   -446    436       C  
ATOM    566  CG  LEU A 942      29.181  31.917  12.416  1.00 66.24           C  
ANISOU  566  CG  LEU A 942     8574   8707   7887   1489   -271    550       C  
ATOM    567  CD1 LEU A 942      29.534  32.671  13.684  1.00 60.69           C  
ANISOU  567  CD1 LEU A 942     7720   7960   7378   1320    -53    465       C  
ATOM    568  CD2 LEU A 942      30.209  32.189  11.331  1.00 72.48           C  
ANISOU  568  CD2 LEU A 942     9657   9432   8450   1493    -73    637       C  
ATOM    569  N   LEU A 943      26.028  31.113  14.439  1.00 61.77           N  
ANISOU  569  N   LEU A 943     7345   8181   7943   1561   -612    343       N  
ATOM    570  CA  LEU A 943      24.627  31.491  14.289  1.00 66.44           C  
ANISOU  570  CA  LEU A 943     7795   8714   8737   1720   -788    267       C  
ATOM    571  C   LEU A 943      24.446  32.737  13.425  1.00 71.56           C  
ANISOU  571  C   LEU A 943     8686   9269   9232   1963   -886    377       C  
ATOM    572  O   LEU A 943      23.478  32.842  12.674  1.00 79.55           O  
ANISOU  572  O   LEU A 943     9663  10307  10256   2236  -1174    303       O  
ATOM    573  CB  LEU A 943      23.989  31.713  15.662  1.00 69.83           C  
ANISOU  573  CB  LEU A 943     7999   9097   9435   1624   -610    211       C  
ATOM    574  CG  LEU A 943      23.982  30.502  16.600  1.00 78.45           C  
ANISOU  574  CG  LEU A 943     8925  10225  10657   1467   -429    167       C  
ATOM    575  CD1 LEU A 943      23.384  30.877  17.947  1.00 87.56           C  
ANISOU  575  CD1 LEU A 943     9942  11340  11986   1428   -191    148       C  
ATOM    576  CD2 LEU A 943      23.229  29.328  15.980  1.00 69.10           C  
ANISOU  576  CD2 LEU A 943     7542   9009   9704   1464   -561     10       C  
ATOM    577  N   GLY A 944      25.374  33.680  13.527  1.00 66.89           N  
ANISOU  577  N   GLY A 944     8341   8559   8516   1898   -630    527       N  
ATOM    578  CA  GLY A 944      25.265  34.902  12.757  1.00 58.24           C  
ANISOU  578  CA  GLY A 944     7562   7272   7294   2141   -591    698       C  
ATOM    579  C   GLY A 944      26.538  35.714  12.641  1.00 65.74           C  
ANISOU  579  C   GLY A 944     8799   8028   8151   1996   -195    833       C  
ATOM    580  O   GLY A 944      27.616  35.298  13.075  1.00 67.27           O  
ANISOU  580  O   GLY A 944     8905   8298   8355   1712    -10    741       O  
ATOM    581  N   TYR A 945      26.402  36.896  12.052  1.00 65.16           N  
ANISOU  581  N   TYR A 945     9062   7679   8019   2217    -36   1031       N  
ATOM    582  CA  TYR A 945      27.544  37.761  11.808  1.00 65.64           C  
ANISOU  582  CA  TYR A 945     9418   7446   8076   2072    454   1153       C  
ATOM    583  C   TYR A 945      27.127  39.224  11.726  1.00 80.99           C  
ANISOU  583  C   TYR A 945    11639   8982  10150   2269    715   1331       C  
ATOM    584  O   TYR A 945      25.957  39.546  11.498  1.00 75.46           O  
ANISOU  584  O   TYR A 945    11007   8259   9404   2649    443   1432       O  
ATOM    585  CB  TYR A 945      28.256  37.350  10.517  1.00 61.46           C  
ANISOU  585  CB  TYR A 945     9243   6930   7179   2181    538   1331       C  
ATOM    586  CG  TYR A 945      27.414  37.543   9.277  1.00 72.50           C  
ANISOU  586  CG  TYR A 945    11045   8305   8196   2726    304   1591       C  
ATOM    587  CD1 TYR A 945      26.459  36.605   8.910  1.00 76.60           C  
ANISOU  587  CD1 TYR A 945    11388   9173   8544   2991   -270   1465       C  
ATOM    588  CD2 TYR A 945      27.569  38.667   8.476  1.00 80.65           C  
ANISOU  588  CD2 TYR A 945    12638   8960   9044   3016    672   1934       C  
ATOM    589  CE1 TYR A 945      25.681  36.780   7.779  1.00 80.73           C  
ANISOU  589  CE1 TYR A 945    12235   9760   8679   3570   -572   1608       C  
ATOM    590  CE2 TYR A 945      26.796  38.849   7.342  1.00 87.84           C  
ANISOU  590  CE2 TYR A 945    13976   9901   9499   3644    415   2184       C  
ATOM    591  CZ  TYR A 945      25.855  37.902   6.998  1.00 90.89           C  
ANISOU  591  CZ  TYR A 945    14130  10729   9678   3938   -258   1987       C  
ATOM    592  OH  TYR A 945      25.088  38.080   5.870  1.00105.69           O  
ANISOU  592  OH  TYR A 945    16384  12713  11060   4635   -595   2143       O  
ATOM    593  N   CYS A 946      28.099  40.106  11.916  1.00 82.68           N  
ANISOU  593  N   CYS A 946    11984   8854  10575   2016   1261   1325       N  
ATOM    594  CA  CYS A 946      27.872  41.529  11.769  1.00 72.63           C  
ANISOU  594  CA  CYS A 946    11039   7077   9481   2175   1647   1513       C  
ATOM    595  C   CYS A 946      29.039  42.161  11.022  1.00 83.87           C  
ANISOU  595  C   CYS A 946    12871   8075  10920   2047   2311   1685       C  
ATOM    596  O   CYS A 946      30.132  42.314  11.571  1.00 71.84           O  
ANISOU  596  O   CYS A 946    11107   6455   9735   1576   2703   1389       O  
ATOM    597  CB  CYS A 946      27.684  42.190  13.133  1.00 67.55           C  
ANISOU  597  CB  CYS A 946    10022   6337   9307   1921   1753   1199       C  
ATOM    598  SG  CYS A 946      27.178  43.933  13.040  1.00 74.72           S  
ANISOU  598  SG  CYS A 946    11301   6578  10511   2159   2197   1402       S  
ATOM    599  N   LYS A 947      28.802  42.508   9.762  1.00 91.93           N  
ANISOU  599  N   LYS A 947    14506   8857  11568   2499   2447   2135       N  
ATOM    600  CA  LYS A 947      29.803  43.180   8.947  1.00 99.20           C  
ANISOU  600  CA  LYS A 947    15930   9280  12480   2441   3204   2388       C  
ATOM    601  C   LYS A 947      29.371  44.616   8.679  1.00112.43           C  
ANISOU  601  C   LYS A 947    18125  10301  14294   2760   3687   2737       C  
ATOM    602  O   LYS A 947      28.777  44.914   7.643  1.00117.64           O  
ANISOU  602  O   LYS A 947    19411  10812  14477   3392   3663   3222       O  
ATOM    603  CB  LYS A 947      30.024  42.435   7.629  1.00 96.51           C  
ANISOU  603  CB  LYS A 947    16015   9140  11516   2760   3113   2687       C  
ATOM    604  N   VAL A 948      29.667  45.501   9.625  1.00112.91           N  
ANISOU  604  N   VAL A 948    17929   9977  14993   2368   4115   2466       N  
ATOM    605  CA  VAL A 948      29.296  46.905   9.504  1.00121.46           C  
ANISOU  605  CA  VAL A 948    19465  10354  16331   2616   4648   2748       C  
ATOM    606  C   VAL A 948      30.504  47.809   9.743  1.00121.49           C  
ANISOU  606  C   VAL A 948    19478   9696  16985   2064   5635   2550       C  
ATOM    607  O   VAL A 948      31.102  47.790  10.822  1.00114.13           O  
ANISOU  607  O   VAL A 948    17891   8875  16599   1470   5692   1935       O  
ATOM    608  CB  VAL A 948      28.165  47.274  10.490  1.00127.55           C  
ANISOU  608  CB  VAL A 948    19884  11227  17352   2746   4192   2546       C  
ATOM    609  CG1 VAL A 948      28.051  48.778  10.639  1.00136.71           C  
ANISOU  609  CG1 VAL A 948    21375  11587  18983   2822   4865   2680       C  
ATOM    610  CG2 VAL A 948      26.838  46.678  10.033  1.00124.48           C  
ANISOU  610  CG2 VAL A 948    19590  11305  16403   3401   3372   2786       C  
ATOM    611  N   GLY A 949      30.858  48.588   8.722  1.00127.30           N  
ANISOU  611  N   GLY A 949    20952   9764  17653   2289   6421   3038       N  
ATOM    612  CA  GLY A 949      31.978  49.511   8.792  1.00127.19           C  
ANISOU  612  CA  GLY A 949    20867   9208  18251   1755   7391   2775       C  
ATOM    613  C   GLY A 949      33.302  48.852   9.125  1.00128.58           C  
ANISOU  613  C   GLY A 949    20580   9439  18835   1064   7698   2291       C  
ATOM    614  O   GLY A 949      33.748  47.943   8.426  1.00138.75           O  
ANISOU  614  O   GLY A 949    21981  11070  19666   1108   7572   2436       O  
ATOM    615  N   ASP A 950      33.932  49.317  10.198  1.00124.43           N  
ANISOU  615  N   ASP A 950    19417   8733  19128    438   8004   1598       N  
ATOM    616  CA  ASP A 950      35.187  48.738  10.660  1.00125.80           C  
ANISOU  616  CA  ASP A 950    18901   9222  19674   -202   8102    911       C  
ATOM    617  C   ASP A 950      34.941  47.734  11.781  1.00123.17           C  
ANISOU  617  C   ASP A 950    17802   9815  19184   -308   7069    385       C  
ATOM    618  O   ASP A 950      35.880  47.275  12.432  1.00128.65           O  
ANISOU  618  O   ASP A 950    17830  10865  20185   -764   6995   -282       O  
ATOM    619  CB  ASP A 950      36.144  49.834  11.133  1.00132.74           C  
ANISOU  619  CB  ASP A 950    19423   9514  21500   -779   8996    308       C  
ATOM    620  N   GLU A 951      33.674  47.394  12.000  1.00115.75           N  
ANISOU  620  N   GLU A 951    16964   9252  17764    152   6302    681       N  
ATOM    621  CA  GLU A 951      33.303  46.450  13.051  1.00112.37           C  
ANISOU  621  CA  GLU A 951    15915   9626  17155    111   5412    284       C  
ATOM    622  C   GLU A 951      32.998  45.058  12.497  1.00 96.39           C  
ANISOU  622  C   GLU A 951    13975   8228  14420    401   4746    590       C  
ATOM    623  O   GLU A 951      32.161  44.904  11.608  1.00 95.29           O  
ANISOU  623  O   GLU A 951    14354   8064  13789    890   4538   1160       O  
ATOM    624  CB  GLU A 951      32.095  46.979  13.833  1.00116.64           C  
ANISOU  624  CB  GLU A 951    16391  10159  17768    347   5065    284       C  
ATOM    625  CG  GLU A 951      32.361  48.274  14.592  1.00123.73           C  
ANISOU  625  CG  GLU A 951    17089  10512  19412     33   5634   -157       C  
ATOM    626  CD  GLU A 951      33.375  48.100  15.709  1.00124.44           C  
ANISOU  626  CD  GLU A 951    16409  10936  19936   -504   5616  -1032       C  
ATOM    627  OE1 GLU A 951      33.297  47.083  16.431  1.00127.32           O  
ANISOU  627  OE1 GLU A 951    16349  12057  19971   -485   4916  -1291       O  
ATOM    628  OE2 GLU A 951      34.254  48.974  15.862  1.00120.82           O  
ANISOU  628  OE2 GLU A 951    15771   9977  20157   -915   6316  -1486       O  
ATOM    629  N   ARG A 952      33.688  44.051  13.027  1.00 88.21           N  
ANISOU  629  N   ARG A 952    12419   7753  13343    134   4406    166       N  
ATOM    630  CA  ARG A 952      33.457  42.656  12.642  1.00 85.71           C  
ANISOU  630  CA  ARG A 952    12104   8014  12447    353   3794    363       C  
ATOM    631  C   ARG A 952      33.078  41.815  13.855  1.00 83.52           C  
ANISOU  631  C   ARG A 952    11290   8347  12095    325   3121     20       C  
ATOM    632  O   ARG A 952      33.888  41.635  14.770  1.00 75.56           O  
ANISOU  632  O   ARG A 952     9787   7587  11337     24   3106   -515       O  
ATOM    633  CB  ARG A 952      34.697  42.047  11.981  1.00 74.59           C  
ANISOU  633  CB  ARG A 952    10670   6685  10984    134   4068    269       C  
ATOM    634  CG  ARG A 952      35.278  42.848  10.833  1.00 98.34           C  
ANISOU  634  CG  ARG A 952    14205   9061  14098    104   4895    570       C  
ATOM    635  CD  ARG A 952      34.370  42.862   9.618  1.00105.38           C  
ANISOU  635  CD  ARG A 952    15845   9797  14396    663   4826   1291       C  
ATOM    636  NE  ARG A 952      34.963  43.629   8.526  1.00119.45           N  
ANISOU  636  NE  ARG A 952    18231  10949  16205    696   5705   1642       N  
ATOM    637  CZ  ARG A 952      34.381  43.832   7.349  1.00123.44           C  
ANISOU  637  CZ  ARG A 952    19510  11233  16159   1244   5821   2289       C  
ATOM    638  NH1 ARG A 952      33.182  43.323   7.105  1.00120.78           N  
ANISOU  638  NH1 ARG A 952    19344  11291  15254   1785   5045   2566       N  
ATOM    639  NH2 ARG A 952      34.999  44.544   6.416  1.00126.47           N  
ANISOU  639  NH2 ARG A 952    20493  11000  16559   1280   6735   2631       N  
ATOM    640  N   LEU A 953      31.855  41.292  13.864  1.00 65.60           N  
ANISOU  640  N   LEU A 953     9119   6323   9483    669   2586    301       N  
ATOM    641  CA  LEU A 953      31.418  40.444  14.965  1.00 64.93           C  
ANISOU  641  CA  LEU A 953     8610   6750   9312    669   2054     56       C  
ATOM    642  C   LEU A 953      30.855  39.109  14.479  1.00 66.69           C  
ANISOU  642  C   LEU A 953     8893   7342   9106    903   1564    303       C  
ATOM    643  O   LEU A 953      30.249  39.021  13.410  1.00 71.14           O  
ANISOU  643  O   LEU A 953     9813   7799   9419   1185   1470    666       O  
ATOM    644  CB  LEU A 953      30.380  41.175  15.823  1.00 72.77           C  
ANISOU  644  CB  LEU A 953     9508   7649  10494    773   1958     -5       C  
ATOM    645  CG  LEU A 953      30.890  42.442  16.519  1.00 74.03           C  
ANISOU  645  CG  LEU A 953     9515   7475  11140    517   2406   -375       C  
ATOM    646  CD1 LEU A 953      30.493  43.685  15.739  1.00 78.68           C  
ANISOU  646  CD1 LEU A 953    10550   7416  11928    654   2845    -55       C  
ATOM    647  CD2 LEU A 953      30.401  42.522  17.954  1.00 63.59           C  
ANISOU  647  CD2 LEU A 953     7806   6427   9928    494   2162   -741       C  
ATOM    648  N   LEU A 954      31.066  38.073  15.281  1.00 54.83           N  
ANISOU  648  N   LEU A 954     7046   6268   7521    820   1264     74       N  
ATOM    649  CA  LEU A 954      30.605  36.726  14.958  1.00 57.63           C  
ANISOU  649  CA  LEU A 954     7398   6925   7573    981    868    233       C  
ATOM    650  C   LEU A 954      29.805  36.172  16.127  1.00 49.90           C  
ANISOU  650  C   LEU A 954     6145   6201   6612   1036    586    124       C  
ATOM    651  O   LEU A 954      30.176  36.365  17.287  1.00 52.86           O  
ANISOU  651  O   LEU A 954     6280   6711   7092    926    645   -150       O  
ATOM    652  CB  LEU A 954      31.793  35.810  14.626  1.00 54.04           C  
ANISOU  652  CB  LEU A 954     6877   6673   6984    855    890    126       C  
ATOM    653  CG  LEU A 954      32.557  36.183  13.349  1.00 53.80           C  
ANISOU  653  CG  LEU A 954     7149   6395   6896    812   1225    263       C  
ATOM    654  CD1 LEU A 954      33.939  35.530  13.297  1.00 53.66           C  
ANISOU  654  CD1 LEU A 954     6943   6561   6883    614   1347     16       C  
ATOM    655  CD2 LEU A 954      31.745  35.829  12.109  1.00 54.27           C  
ANISOU  655  CD2 LEU A 954     7580   6408   6633   1115   1038    630       C  
ATOM    656  N   VAL A 955      28.700  35.496  15.831  1.00 48.90           N  
ANISOU  656  N   VAL A 955     6046   6142   6390   1223    307    299       N  
ATOM    657  CA  VAL A 955      27.798  35.066  16.893  1.00 47.75           C  
ANISOU  657  CA  VAL A 955     5671   6145   6328   1266    164    224       C  
ATOM    658  C   VAL A 955      27.573  33.554  16.887  1.00 55.95           C  
ANISOU  658  C   VAL A 955     6616   7384   7260   1300    -24    262       C  
ATOM    659  O   VAL A 955      27.158  32.967  15.888  1.00 60.81           O  
ANISOU  659  O   VAL A 955     7304   7979   7822   1393   -197    360       O  
ATOM    660  CB  VAL A 955      26.445  35.799  16.791  1.00 62.32           C  
ANISOU  660  CB  VAL A 955     7530   7811   8339   1435     92    303       C  
ATOM    661  CG1 VAL A 955      25.560  35.464  17.985  1.00 48.63           C  
ANISOU  661  CG1 VAL A 955     5536   6196   6744   1438     60    190       C  
ATOM    662  CG2 VAL A 955      26.679  37.299  16.713  1.00 61.65           C  
ANISOU  662  CG2 VAL A 955     7597   7439   8389   1428    335    302       C  
ATOM    663  N   TYR A 956      27.854  32.935  18.024  1.00 53.40           N  
ANISOU  663  N   TYR A 956     6148   7244   6896   1259     28    165       N  
ATOM    664  CA  TYR A 956      27.846  31.486  18.146  1.00 56.49           C  
ANISOU  664  CA  TYR A 956     6502   7757   7206   1293    -37    222       C  
ATOM    665  C   TYR A 956      26.855  31.070  19.213  1.00 61.13           C  
ANISOU  665  C   TYR A 956     6974   8348   7903   1349     55    239       C  
ATOM    666  O   TYR A 956      26.494  31.873  20.070  1.00 59.11           O  
ANISOU  666  O   TYR A 956     6660   8101   7700   1366    159    167       O  
ATOM    667  CB  TYR A 956      29.237  30.951  18.520  1.00 47.83           C  
ANISOU  667  CB  TYR A 956     5416   6864   5895   1286      3    141       C  
ATOM    668  CG  TYR A 956      30.397  31.536  17.748  1.00 53.48           C  
ANISOU  668  CG  TYR A 956     6182   7578   6560   1184     33     40       C  
ATOM    669  CD1 TYR A 956      30.926  32.780  18.082  1.00 64.36           C  
ANISOU  669  CD1 TYR A 956     7502   8925   8027   1087    175   -152       C  
ATOM    670  CD2 TYR A 956      30.992  30.829  16.712  1.00 55.10           C  
ANISOU  670  CD2 TYR A 956     6477   7788   6673   1167    -20     95       C  
ATOM    671  CE1 TYR A 956      31.999  33.315  17.385  1.00 59.33           C  
ANISOU  671  CE1 TYR A 956     6890   8217   7436    949    321   -274       C  
ATOM    672  CE2 TYR A 956      32.069  31.356  16.007  1.00 44.60           C  
ANISOU  672  CE2 TYR A 956     5196   6428   5322   1059    104      0       C  
ATOM    673  CZ  TYR A 956      32.564  32.597  16.350  1.00 56.72           C  
ANISOU  673  CZ  TYR A 956     6667   7892   6995    937    302   -179       C  
ATOM    674  OH  TYR A 956      33.627  33.122  15.656  1.00 67.14           O  
ANISOU  674  OH  TYR A 956     8014   9113   8383    786    536   -300       O  
ATOM    675  N   GLU A 957      26.429  29.812  19.176  1.00 66.34           N  
ANISOU  675  N   GLU A 957     7606   8972   8627   1368     78    317       N  
ATOM    676  CA  GLU A 957      25.623  29.273  20.262  1.00 66.06           C  
ANISOU  676  CA  GLU A 957     7507   8890   8704   1411    309    363       C  
ATOM    677  C   GLU A 957      26.480  29.190  21.512  1.00 57.42           C  
ANISOU  677  C   GLU A 957     6536   8001   7279   1550    460    393       C  
ATOM    678  O   GLU A 957      27.648  28.805  21.440  1.00 52.91           O  
ANISOU  678  O   GLU A 957     6059   7590   6455   1621    376    387       O  
ATOM    679  CB  GLU A 957      25.063  27.900  19.908  1.00 74.27           C  
ANISOU  679  CB  GLU A 957     8495   9762   9962   1374    396    416       C  
ATOM    680  CG  GLU A 957      24.248  27.281  21.022  1.00 85.96           C  
ANISOU  680  CG  GLU A 957     9949  11104  11609   1398    782    495       C  
ATOM    681  CD  GLU A 957      23.702  25.926  20.651  1.00 97.78           C  
ANISOU  681  CD  GLU A 957    11369  12340  13444   1310    965    498       C  
ATOM    682  OE1 GLU A 957      23.654  25.619  19.441  1.00102.95           O  
ANISOU  682  OE1 GLU A 957    11901  12952  14264   1221    701    349       O  
ATOM    683  OE2 GLU A 957      23.328  25.167  21.569  1.00102.50           O  
ANISOU  683  OE2 GLU A 957    12045  12758  14143   1343   1408    636       O  
ATOM    684  N   PHE A 958      25.908  29.558  22.654  1.00 58.05           N  
ANISOU  684  N   PHE A 958     6607   8112   7337   1632    664    386       N  
ATOM    685  CA  PHE A 958      26.661  29.556  23.900  1.00 60.55           C  
ANISOU  685  CA  PHE A 958     7059   8697   7252   1860    763    366       C  
ATOM    686  C   PHE A 958      27.008  28.134  24.339  1.00 71.57           C  
ANISOU  686  C   PHE A 958     8667  10105   8419   2073    935    592       C  
ATOM    687  O   PHE A 958      26.157  27.247  24.338  1.00 76.61           O  
ANISOU  687  O   PHE A 958     9355  10470   9282   2038   1212    785       O  
ATOM    688  CB  PHE A 958      25.881  30.270  25.005  1.00 56.43           C  
ANISOU  688  CB  PHE A 958     6512   8210   6720   1935    970    300       C  
ATOM    689  CG  PHE A 958      26.623  30.354  26.310  1.00 63.78           C  
ANISOU  689  CG  PHE A 958     7592   9489   7153   2248   1023    216       C  
ATOM    690  CD1 PHE A 958      27.736  31.169  26.437  1.00 69.07           C  
ANISOU  690  CD1 PHE A 958     8169  10455   7619   2295    757   -108       C  
ATOM    691  CD2 PHE A 958      26.209  29.620  27.407  1.00 71.97           C  
ANISOU  691  CD2 PHE A 958     8859  10557   7927   2523   1361    424       C  
ATOM    692  CE1 PHE A 958      28.423  31.249  27.632  1.00 68.99           C  
ANISOU  692  CE1 PHE A 958     8240  10843   7132   2642    724   -297       C  
ATOM    693  CE2 PHE A 958      26.892  29.696  28.607  1.00 77.23           C  
ANISOU  693  CE2 PHE A 958     9708  11611   8025   2922   1361    334       C  
ATOM    694  CZ  PHE A 958      28.001  30.511  28.718  1.00 75.34           C  
ANISOU  694  CZ  PHE A 958     9320  11741   7564   2997    990    -65       C  
ATOM    695  N   MET A 959      28.267  27.927  24.709  1.00 65.96           N  
ANISOU  695  N   MET A 959     8066   9692   7303   2309    791    535       N  
ATOM    696  CA  MET A 959      28.702  26.646  25.242  1.00 65.26           C  
ANISOU  696  CA  MET A 959     8242   9638   6915   2632    946    771       C  
ATOM    697  C   MET A 959      28.792  26.716  26.764  1.00 77.34           C  
ANISOU  697  C   MET A 959     9993  11436   7956   3058   1111    813       C  
ATOM    698  O   MET A 959      29.664  27.391  27.316  1.00 81.70           O  
ANISOU  698  O   MET A 959    10485  12407   8152   3272    850    523       O  
ATOM    699  CB  MET A 959      30.046  26.240  24.636  1.00 69.18           C  
ANISOU  699  CB  MET A 959     8718  10320   7248   2716    652    669       C  
ATOM    700  CG  MET A 959      29.999  26.058  23.128  1.00 66.31           C  
ANISOU  700  CG  MET A 959     8207   9713   7274   2360    526    649       C  
ATOM    701  SD  MET A 959      28.755  24.854  22.608  1.00 72.22           S  
ANISOU  701  SD  MET A 959     9029   9975   8438   2205    833    923       S  
ATOM    702  CE  MET A 959      28.650  25.217  20.859  1.00 97.98           C  
ANISOU  702  CE  MET A 959    12058  13123  12047   1840    534    734       C  
ATOM    703  N   LYS A 960      27.884  26.004  27.426  1.00 79.45           N  
ANISOU  703  N   LYS A 960    10511  11457   8220   3191   1574   1138       N  
ATOM    704  CA  LYS A 960      27.694  26.089  28.874  1.00 76.46           C  
ANISOU  704  CA  LYS A 960    10416  11277   7360   3612   1844   1241       C  
ATOM    705  C   LYS A 960      28.973  25.912  29.695  1.00 91.39           C  
ANISOU  705  C   LYS A 960    12531  13674   8518   4206   1594   1166       C  
ATOM    706  O   LYS A 960      29.294  26.752  30.539  1.00101.60           O  
ANISOU  706  O   LYS A 960    13792  15398   9415   4458   1414    874       O  
ATOM    707  CB  LYS A 960      26.662  25.048  29.320  1.00 77.08           C  
ANISOU  707  CB  LYS A 960    10804  10910   7574   3680   2510   1682       C  
ATOM    708  CG  LYS A 960      26.165  25.228  30.747  1.00 89.04           C  
ANISOU  708  CG  LYS A 960    12636  12541   8654   4057   2930   1829       C  
ATOM    709  CD  LYS A 960      25.087  24.207  31.097  1.00102.01           C  
ANISOU  709  CD  LYS A 960    14569  13630  10561   4043   3731   2267       C  
ATOM    710  CE  LYS A 960      24.571  24.409  32.517  1.00111.97           C  
ANISOU  710  CE  LYS A 960    16200  14995  11350   4436   4236   2443       C  
ATOM    711  NZ  LYS A 960      23.581  23.369  32.915  1.00115.38           N  
ANISOU  711  NZ  LYS A 960    16961  14823  12054   4433   5160   2896       N  
ATOM    712  N   TYR A 961      29.704  24.829  29.451  1.00 86.50           N  
ANISOU  712  N   TYR A 961    12112  13027   7728   4463   1556   1371       N  
ATOM    713  CA  TYR A 961      30.836  24.487  30.308  1.00 80.63           C  
ANISOU  713  CA  TYR A 961    11620  12768   6246   5160   1333   1332       C  
ATOM    714  C   TYR A 961      32.176  24.957  29.751  1.00 81.40           C  
ANISOU  714  C   TYR A 961    11334  13287   6305   5141    707    832       C  
ATOM    715  O   TYR A 961      33.229  24.457  30.144  1.00 91.13           O  
ANISOU  715  O   TYR A 961    12683  14888   7053   5690    452    756       O  
ATOM    716  CB  TYR A 961      30.864  22.980  30.559  1.00 83.19           C  
ANISOU  716  CB  TYR A 961    12458  12807   6345   5592   1723   1880       C  
ATOM    717  CG  TYR A 961      29.669  22.496  31.348  1.00101.38           C  
ANISOU  717  CG  TYR A 961    15199  14707   8612   5712   2460   2362       C  
ATOM    718  CD1 TYR A 961      29.598  22.685  32.722  1.00111.14           C  
ANISOU  718  CD1 TYR A 961    16778  16210   9239   6268   2610   2441       C  
ATOM    719  CD2 TYR A 961      28.606  21.865  30.719  1.00103.48           C  
ANISOU  719  CD2 TYR A 961    15459  14285   9575   5223   2990   2648       C  
ATOM    720  CE1 TYR A 961      28.505  22.252  33.447  1.00116.18           C  
ANISOU  720  CE1 TYR A 961    17767  16384   9993   6301   3304   2837       C  
ATOM    721  CE2 TYR A 961      27.507  21.428  31.436  1.00105.76           C  
ANISOU  721  CE2 TYR A 961    16094  14155   9936   5281   3757   3036       C  
ATOM    722  CZ  TYR A 961      27.462  21.624  32.800  1.00115.97           C  
ANISOU  722  CZ  TYR A 961    17778  15692  10595   5831   3956   3170       C  
ATOM    723  OH  TYR A 961      26.370  21.191  33.518  1.00128.50           O  
ANISOU  723  OH  TYR A 961    19648  16769  12409   5809   4685   3488       O  
ATOM    724  N   GLY A 962      32.129  25.926  28.841  1.00 78.85           N  
ANISOU  724  N   GLY A 962    10559  12896   6505   4539    495    485       N  
ATOM    725  CA  GLY A 962      33.331  26.572  28.345  1.00 79.50           C  
ANISOU  725  CA  GLY A 962    10239  13322   6644   4437     24    -45       C  
ATOM    726  C   GLY A 962      34.275  25.666  27.580  1.00 81.59           C  
ANISOU  726  C   GLY A 962    10478  13579   6943   4515   -145     -6       C  
ATOM    727  O   GLY A 962      33.850  24.707  26.938  1.00 86.51           O  
ANISOU  727  O   GLY A 962    11299  13787   7786   4390     89    405       O  
ATOM    728  N   SER A 963      35.566  25.975  27.652  1.00 80.77           N  
ANISOU  728  N   SER A 963    10085  13937   6665   4716   -544   -504       N  
ATOM    729  CA  SER A 963      36.568  25.226  26.905  1.00 80.94           C  
ANISOU  729  CA  SER A 963    10004  13995   6754   4783   -725   -563       C  
ATOM    730  C   SER A 963      37.087  24.044  27.706  1.00 83.21           C  
ANISOU  730  C   SER A 963    10642  14517   6457   5566   -788   -337       C  
ATOM    731  O   SER A 963      37.019  24.030  28.934  1.00 92.14           O  
ANISOU  731  O   SER A 963    12012  15945   7053   6122   -800   -315       O  
ATOM    732  CB  SER A 963      37.738  26.129  26.509  1.00 78.19           C  
ANISOU  732  CB  SER A 963     9106  13992   6612   4583  -1068  -1268       C  
ATOM    733  OG  SER A 963      38.614  26.341  27.603  1.00 83.74           O  
ANISOU  733  OG  SER A 963     9647  15322   6849   5159  -1415  -1758       O  
ATOM    734  N   LEU A 964      37.608  23.053  26.995  1.00 81.00           N  
ANISOU  734  N   LEU A 964    10418  14073   6285   5629   -799   -170       N  
ATOM    735  CA  LEU A 964      38.227  21.895  27.620  1.00 87.49           C  
ANISOU  735  CA  LEU A 964    11563  14972   6708   6259   -773    -11       C  
ATOM    736  C   LEU A 964      39.417  22.328  28.470  1.00 96.10           C  
ANISOU  736  C   LEU A 964    12387  16640   7486   6658  -1127   -658       C  
ATOM    737  O   LEU A 964      39.653  21.786  29.547  1.00107.09           O  
ANISOU  737  O   LEU A 964    14078  18174   8437   7270  -1066   -597       O  
ATOM    738  CB  LEU A 964      38.667  20.890  26.554  1.00 73.49           C  
ANISOU  738  CB  LEU A 964     9803  12906   5215   6144   -739    159       C  
ATOM    739  CG  LEU A 964      39.374  19.625  27.044  1.00 85.73           C  
ANISOU  739  CG  LEU A 964    11680  14442   6451   6693   -660    289       C  
ATOM    740  CD1 LEU A 964      38.393  18.705  27.745  1.00 88.78           C  
ANISOU  740  CD1 LEU A 964    12692  14397   6644   6988   -138    946       C  
ATOM    741  CD2 LEU A 964      40.059  18.913  25.890  1.00 78.97           C  
ANISOU  741  CD2 LEU A 964    10671  13423   5909   6523   -750    247       C  
ATOM    742  N   GLU A 965      40.153  23.319  27.976  1.00 96.22           N  
ANISOU  742  N   GLU A 965    11820  16963   7775   6323  -1463  -1305       N  
ATOM    743  CA  GLU A 965      41.335  23.834  28.660  1.00103.62           C  
ANISOU  743  CA  GLU A 965    12382  18430   8558   6622  -1791  -2057       C  
ATOM    744  C   GLU A 965      41.000  24.397  30.038  1.00112.87           C  
ANISOU  744  C   GLU A 965    13636  19883   9365   7036  -1814  -2202       C  
ATOM    745  O   GLU A 965      41.712  24.142  31.009  1.00123.89           O  
ANISOU  745  O   GLU A 965    15051  21625  10395   7661  -1964  -2490       O  
ATOM    746  CB  GLU A 965      42.013  24.909  27.807  1.00103.14           C  
ANISOU  746  CB  GLU A 965    11659  18526   9002   6051  -2011  -2729       C  
ATOM    747  CG  GLU A 965      43.261  25.513  28.432  1.00110.65           C  
ANISOU  747  CG  GLU A 965    12136  19977   9929   6273  -2303  -3623       C  
ATOM    748  CD  GLU A 965      43.900  26.568  27.548  1.00115.84           C  
ANISOU  748  CD  GLU A 965    12153  20670  11191   5620  -2383  -4292       C  
ATOM    749  OE1 GLU A 965      43.468  27.738  27.607  1.00113.15           O  
ANISOU  749  OE1 GLU A 965    11543  20334  11115   5251  -2346  -4570       O  
ATOM    750  OE2 GLU A 965      44.832  26.226  26.789  1.00124.63           O  
ANISOU  750  OE2 GLU A 965    13035  21770  12549   5462  -2441  -4541       O  
ATOM    751  N   ASP A 966      39.917  25.165  30.115  1.00111.38           N  
ANISOU  751  N   ASP A 966    13488  19561   9269   6721  -1676  -2015       N  
ATOM    752  CA  ASP A 966      39.472  25.742  31.379  1.00115.05           C  
ANISOU  752  CA  ASP A 966    14034  20256   9425   7064  -1678  -2110       C  
ATOM    753  C   ASP A 966      39.099  24.654  32.374  1.00124.84           C  
ANISOU  753  C   ASP A 966    15897  21385  10152   7748  -1423  -1542       C  
ATOM    754  O   ASP A 966      39.248  24.824  33.583  1.00141.32           O  
ANISOU  754  O   ASP A 966    18046  23785  11863   8309  -1515  -1719       O  
ATOM    755  CB  ASP A 966      38.276  26.670  31.162  1.00110.55           C  
ANISOU  755  CB  ASP A 966    13469  19496   9039   6543  -1516  -1956       C  
ATOM    756  CG  ASP A 966      38.635  27.908  30.370  1.00111.95           C  
ANISOU  756  CG  ASP A 966    13048  19793   9697   5918  -1728  -2602       C  
ATOM    757  OD1 ASP A 966      39.813  28.321  30.421  1.00116.99           O  
ANISOU  757  OD1 ASP A 966    13177  20755  10520   5963  -2012  -3302       O  
ATOM    758  OD2 ASP A 966      37.739  28.470  29.699  1.00104.58           O  
ANISOU  758  OD2 ASP A 966    12142  18494   9098   5329  -1488  -2411       O  
ATOM    759  N   VAL A 967      38.615  23.534  31.852  1.00118.05           N  
ANISOU  759  N   VAL A 967    15491  20056   9306   7706  -1076   -875       N  
ATOM    760  CA  VAL A 967      38.145  22.443  32.691  1.00116.39           C  
ANISOU  760  CA  VAL A 967    15921  19601   8701   8275   -690   -280       C  
ATOM    761  C   VAL A 967      39.298  21.556  33.160  1.00119.73           C  
ANISOU  761  C   VAL A 967    16459  20266   8768   8956   -839   -448       C  
ATOM    762  O   VAL A 967      39.389  21.227  34.343  1.00132.50           O  
ANISOU  762  O   VAL A 967    18392  22053   9899   9669   -773   -381       O  
ATOM    763  CB  VAL A 967      37.100  21.592  31.951  1.00103.94           C  
ANISOU  763  CB  VAL A 967    14759  17354   7379   7919   -173    464       C  
ATOM    764  CG1 VAL A 967      36.630  20.448  32.830  1.00108.57           C  
ANISOU  764  CG1 VAL A 967    16003  17611   7639   8475    334   1045       C  
ATOM    765  CG2 VAL A 967      35.922  22.462  31.534  1.00 91.43           C  
ANISOU  765  CG2 VAL A 967    13084  15563   6094   7312    -10    608       C  
ATOM    766  N   LEU A 968      40.180  21.177  32.239  1.00112.85           N  
ANISOU  766  N   LEU A 968    15347  19420   8112   8767  -1042   -673       N  
ATOM    767  CA  LEU A 968      41.347  20.373  32.594  1.00118.56           C  
ANISOU  767  CA  LEU A 968    16140  20408   8499   9387  -1222   -901       C  
ATOM    768  C   LEU A 968      42.305  21.149  33.495  1.00127.72           C  
ANISOU  768  C   LEU A 968    16899  22239   9388   9863  -1673  -1691       C  
ATOM    769  O   LEU A 968      43.059  20.561  34.273  1.00136.88           O  
ANISOU  769  O   LEU A 968    18230  23696  10084  10626  -1795  -1856       O  
ATOM    770  CB  LEU A 968      42.079  19.896  31.340  1.00116.53           C  
ANISOU  770  CB  LEU A 968    15653  20037   8586   9009  -1361  -1017       C  
ATOM    771  CG  LEU A 968      41.578  18.587  30.732  1.00115.85           C  
ANISOU  771  CG  LEU A 968    16057  19363   8596   8935   -951   -289       C  
ATOM    772  CD1 LEU A 968      42.436  18.187  29.543  1.00115.30           C  
ANISOU  772  CD1 LEU A 968    15693  19257   8860   8627  -1167   -492       C  
ATOM    773  CD2 LEU A 968      41.567  17.484  31.781  1.00122.63           C  
ANISOU  773  CD2 LEU A 968    17540  20138   8916   9738   -658    107       C  
ATOM    774  N   HIS A 969      42.272  22.472  33.379  1.00126.23           N  
ANISOU  774  N   HIS A 969    16168  22286   9508   9429  -1909  -2206       N  
ATOM    775  CA  HIS A 969      43.049  23.344  34.250  1.00136.74           C  
ANISOU  775  CA  HIS A 969    17043  24221  10692   9813  -2301  -3010       C  
ATOM    776  C   HIS A 969      42.085  24.122  35.141  1.00143.35           C  
ANISOU  776  C   HIS A 969    17966  25107  11394   9889  -2216  -2881       C  
ATOM    777  O   HIS A 969      41.806  25.299  34.906  1.00139.17           O  
ANISOU  777  O   HIS A 969    16993  24647  11237   9351  -2330  -3227       O  
ATOM    778  CB  HIS A 969      43.933  24.283  33.429  1.00136.05           C  
ANISOU  778  CB  HIS A 969    16187  24363  11143   9242  -2616  -3834       C  
ATOM    779  CG  HIS A 969      44.879  23.565  32.507  1.00137.18           C  
ANISOU  779  CG  HIS A 969    16230  24450  11440   9113  -2702  -3974       C  
ATOM    780  ND1 HIS A 969      44.447  22.749  31.491  1.00130.31           N  
ANISOU  780  ND1 HIS A 969    15684  23090  10738   8731  -2453  -3325       N  
ATOM    781  CD2 HIS A 969      46.233  23.546  32.465  1.00141.78           C  
ANISOU  781  CD2 HIS A 969    16404  25414  12052   9325  -3017  -4718       C  
ATOM    782  CE1 HIS A 969      45.497  22.252  30.850  1.00129.69           C  
ANISOU  782  CE1 HIS A 969    15406  23091  10777   8709  -2623  -3625       C  
ATOM    783  NE2 HIS A 969      46.588  22.722  31.423  1.00139.07           N  
ANISOU  783  NE2 HIS A 969    16161  24801  11878   9054  -2959  -4467       N  
ATOM    784  N   ASP A 970      41.590  23.433  36.166  1.00128.67           N  
ANISOU  784  N   ASP A 970    20601  19703   8583   2602   -595   -451       N  
ATOM    785  CA  ASP A 970      40.463  23.877  36.985  1.00139.17           C  
ANISOU  785  CA  ASP A 970    22120  21223   9534   2591    -89   -586       C  
ATOM    786  C   ASP A 970      40.580  25.304  37.512  1.00146.39           C  
ANISOU  786  C   ASP A 970    23130  22250  10241   2466   -124  -1336       C  
ATOM    787  O   ASP A 970      41.672  25.759  37.855  1.00150.07           O  
ANISOU  787  O   ASP A 970    23612  22861  10549   2362   -605  -1657       O  
ATOM    788  CB  ASP A 970      40.282  22.922  38.168  1.00151.34           C  
ANISOU  788  CB  ASP A 970    23864  23165  10474   2629      1    -53       C  
ATOM    789  CG  ASP A 970      40.926  21.569  37.931  1.00154.31           C  
ANISOU  789  CG  ASP A 970    24153  23482  10995   2712   -298    626       C  
ATOM    790  OD1 ASP A 970      40.343  20.547  38.349  1.00158.65           O  
ANISOU  790  OD1 ASP A 970    24784  24096  11402   2766    -15   1236       O  
ATOM    791  OD2 ASP A 970      42.022  21.526  37.332  1.00151.69           O  
ANISOU  791  OD2 ASP A 970    23654  23016  10966   2716   -802    547       O  
ATOM    792  N   PRO A 971      39.443  26.014  37.572  1.00145.23           N  
ANISOU  792  N   PRO A 971    23021  22013  10147   2471    400  -1627       N  
ATOM    793  CA  PRO A 971      39.372  27.348  38.173  1.00143.25           C  
ANISOU  793  CA  PRO A 971    22879  21835   9713   2358    474  -2338       C  
ATOM    794  C   PRO A 971      39.428  27.281  39.694  1.00147.12           C  
ANISOU  794  C   PRO A 971    23662  22870   9366   2296    489  -2381       C  
ATOM    795  O   PRO A 971      39.272  26.186  40.236  1.00147.70           O  
ANISOU  795  O   PRO A 971    23844  23231   9044   2362    549  -1791       O  
ATOM    796  CB  PRO A 971      38.017  27.875  37.696  1.00141.61           C  
ANISOU  796  CB  PRO A 971    22575  21338   9893   2435   1076  -2497       C  
ATOM    797  CG  PRO A 971      37.197  26.647  37.505  1.00142.23           C  
ANISOU  797  CG  PRO A 971    22599  21444   9997   2566   1413  -1807       C  
ATOM    798  CD  PRO A 971      38.149  25.600  36.999  1.00140.74           C  
ANISOU  798  CD  PRO A 971    22350  21218   9906   2585    958  -1314       C  
ATOM    799  N   GLY A 975      35.529  23.456  39.253  1.00126.33           N  
ANISOU  799  N   GLY A 975    20818  20116   7066   2681   2287    -58       N  
ATOM    800  CA  GLY A 975      34.788  23.388  38.007  1.00124.66           C  
ANISOU  800  CA  GLY A 975    20316  19447   7602   2752   2562     20       C  
ATOM    801  C   GLY A 975      33.986  22.107  37.875  1.00132.37           C  
ANISOU  801  C   GLY A 975    21183  20338   8773   2776   2958    739       C  
ATOM    802  O   GLY A 975      33.208  21.757  38.763  1.00141.37           O  
ANISOU  802  O   GLY A 975    22404  21727   9584   2746   3401    973       O  
ATOM    803  N   VAL A 976      34.178  21.408  36.760  1.00129.56           N  
ANISOU  803  N   VAL A 976    20636  19616   8974   2807   2817   1076       N  
ATOM    804  CA  VAL A 976      33.478  20.153  36.494  1.00132.05           C  
ANISOU  804  CA  VAL A 976    20802  19755   9617   2793   3170   1746       C  
ATOM    805  C   VAL A 976      34.466  19.002  36.302  1.00132.08           C  
ANISOU  805  C   VAL A 976    20841  19655   9689   2789   2743   2280       C  
ATOM    806  O   VAL A 976      35.221  18.981  35.331  1.00130.57           O  
ANISOU  806  O   VAL A 976    20549  19208   9854   2818   2349   2199       O  
ATOM    807  CB  VAL A 976      32.579  20.264  35.241  1.00125.87           C  
ANISOU  807  CB  VAL A 976    19688  18564   9572   2810   3495   1684       C  
ATOM    808  CG1 VAL A 976      31.932  18.924  34.925  1.00127.49           C  
ANISOU  808  CG1 VAL A 976    19694  18544  10202   2742   3828   2357       C  
ATOM    809  CG2 VAL A 976      31.523  21.342  35.435  1.00126.27           C  
ANISOU  809  CG2 VAL A 976    19638  18675   9665   2841   3934   1200       C  
ATOM    810  N   LYS A 977      34.457  18.045  37.227  1.00132.95           N  
ANISOU  810  N   LYS A 977    21085  19947   9482   2755   2829   2826       N  
ATOM    811  CA  LYS A 977      35.365  16.902  37.156  1.00127.71           C  
ANISOU  811  CA  LYS A 977    20438  19153   8933   2769   2435   3368       C  
ATOM    812  C   LYS A 977      35.026  15.986  35.981  1.00125.43           C  
ANISOU  812  C   LYS A 977    19858  18337   9462   2743   2585   3741       C  
ATOM    813  O   LYS A 977      33.902  15.496  35.868  1.00127.38           O  
ANISOU  813  O   LYS A 977    19950  18408  10041   2663   3127   4017       O  
ATOM    814  CB  LYS A 977      35.332  16.110  38.466  1.00130.41           C  
ANISOU  814  CB  LYS A 977    21008  19789   8754   2734   2531   3895       C  
ATOM    815  N   LEU A 978      36.005  15.758  35.110  1.00120.85           N  
ANISOU  815  N   LEU A 978    19178  17502   9237   2790   2107   3724       N  
ATOM    816  CA  LEU A 978      35.803  14.920  33.932  1.00113.06           C  
ANISOU  816  CA  LEU A 978    17919  15997   9041   2749   2196   4009       C  
ATOM    817  C   LEU A 978      36.292  13.489  34.139  1.00114.40           C  
ANISOU  817  C   LEU A 978    18050  15930   9486   2738   2043   4646       C  
ATOM    818  O   LEU A 978      37.496  13.234  34.156  1.00110.81           O  
ANISOU  818  O   LEU A 978    17634  15475   8995   2825   1508   4696       O  
ATOM    819  CB  LEU A 978      36.513  15.523  32.718  1.00100.49           C  
ANISOU  819  CB  LEU A 978    16167  14189   7824   2755   1787   3525       C  
ATOM    820  CG  LEU A 978      35.943  16.814  32.134  1.00 96.24           C  
ANISOU  820  CG  LEU A 978    15504  13655   7409   2681   1907   2855       C  
ATOM    821  CD1 LEU A 978      36.720  17.219  30.890  1.00 86.54           C  
ANISOU  821  CD1 LEU A 978    14041  12141   6701   2598   1458   2424       C  
ATOM    822  CD2 LEU A 978      34.468  16.648  31.815  1.00100.28           C  
ANISOU  822  CD2 LEU A 978    15781  13980   8339   2572   2488   2940       C  
ATOM    823  N   ASN A 979      35.354  12.559  34.287  1.00120.11           N  
ANISOU  823  N   ASN A 979    18664  16422  10552   2625   2514   5114       N  
ATOM    824  CA  ASN A 979      35.695  11.143  34.359  1.00132.10           C  
ANISOU  824  CA  ASN A 979    20109  17588  12495   2593   2422   5702       C  
ATOM    825  C   ASN A 979      36.128  10.643  32.985  1.00124.98           C  
ANISOU  825  C   ASN A 979    18919  16141  12428   2575   2209   5643       C  
ATOM    826  O   ASN A 979      35.971  11.350  31.988  1.00121.89           O  
ANISOU  826  O   ASN A 979    18395  15654  12266   2561   2213   5218       O  
ATOM    827  CB  ASN A 979      34.515  10.323  34.885  1.00146.08           C  
ANISOU  827  CB  ASN A 979    21823  19227  14455   2441   3015   6171       C  
ATOM    828  CG  ASN A 979      33.279  10.456  34.018  1.00151.43           C  
ANISOU  828  CG  ASN A 979    22187  19625  15727   2283   3525   6004       C  
ATOM    829  OD1 ASN A 979      33.047   9.646  33.121  1.00153.21           O  
ANISOU  829  OD1 ASN A 979    22117  19319  16775   2158   3605   6147       O  
ATOM    830  ND2 ASN A 979      32.477  11.481  34.282  1.00154.56           N  
ANISOU  830  ND2 ASN A 979    22615  20365  15747   2280   3860   5661       N  
ATOM    831  N   TRP A 980      36.671   9.431  32.929  1.00120.59           N  
ANISOU  831  N   TRP A 980    18272  15213  12332   2575   2025   6051       N  
ATOM    832  CA  TRP A 980      37.227   8.919  31.682  1.00113.60           C  
ANISOU  832  CA  TRP A 980    17111  13808  12244   2566   1784   5930       C  
ATOM    833  C   TRP A 980      36.177   8.708  30.594  1.00107.86           C  
ANISOU  833  C   TRP A 980    16082  12641  12257   2363   2194   5800       C  
ATOM    834  O   TRP A 980      36.418   9.024  29.429  1.00104.07           O  
ANISOU  834  O   TRP A 980    15367  11966  12211   2287   1983   5277       O  
ATOM    835  CB  TRP A 980      37.972   7.605  31.921  1.00119.43           C  
ANISOU  835  CB  TRP A 980    17801  14203  13375   2613   1541   6368       C  
ATOM    836  CG  TRP A 980      38.346   6.932  30.636  1.00119.06           C  
ANISOU  836  CG  TRP A 980    17427  13553  14256   2566   1412   6201       C  
ATOM    837  CD1 TRP A 980      37.916   5.716  30.192  1.00121.80           C  
ANISOU  837  CD1 TRP A 980    17547  13315  15418   2415   1642   6408       C  
ATOM    838  CD2 TRP A 980      39.197   7.458  29.609  1.00118.61           C  
ANISOU  838  CD2 TRP A 980    17225  13422  14420   2652   1048   5721       C  
ATOM    839  NE1 TRP A 980      38.460   5.444  28.959  1.00119.48           N  
ANISOU  839  NE1 TRP A 980    16980  12599  15818   2398   1434   6042       N  
ATOM    840  CE2 TRP A 980      39.249   6.498  28.579  1.00119.45           C  
ANISOU  840  CE2 TRP A 980    17020  12904  15463   2547   1083   5641       C  
ATOM    841  CE3 TRP A 980      39.926   8.644  29.464  1.00114.00           C  
ANISOU  841  CE3 TRP A 980    16730  13240  13344   2785    700   5300       C  
ATOM    842  CZ2 TRP A 980      40.002   6.687  27.421  1.00121.49           C  
ANISOU  842  CZ2 TRP A 980    17059  12958  16145   2576    808   5156       C  
ATOM    843  CZ3 TRP A 980      40.671   8.830  28.314  1.00107.50           C  
ANISOU  843  CZ3 TRP A 980    15640  12223  12983   2739    403   4752       C  
ATOM    844  CH2 TRP A 980      40.703   7.857  27.308  1.00114.11           C  
ANISOU  844  CH2 TRP A 980    16179  12476  14701   2642    469   4689       C  
ATOM    845  N   SER A 981      35.021   8.172  30.976  1.00114.12           N  
ANISOU  845  N   SER A 981    16799  13319  13241   2190   2705   6098       N  
ATOM    846  CA  SER A 981      33.960   7.866  30.019  1.00113.05           C  
ANISOU  846  CA  SER A 981    16317  12756  13881   1951   3086   5987       C  
ATOM    847  C   SER A 981      33.508   9.109  29.265  1.00108.02           C  
ANISOU  847  C   SER A 981    15520  12358  13165   1870   3040   5261       C  
ATOM    848  O   SER A 981      33.099   9.027  28.108  1.00105.43           O  
ANISOU  848  O   SER A 981    14842  11728  13487   1679   3011   4860       O  
ATOM    849  CB  SER A 981      32.764   7.225  30.726  1.00122.50           C  
ANISOU  849  CB  SER A 981    17431  13897  15217   1769   3638   6369       C  
ATOM    850  OG  SER A 981      32.163   8.132  31.631  1.00125.52           O  
ANISOU  850  OG  SER A 981    18012  14837  14843   1826   3926   6348       O  
ATOM    851  N   THR A 982      33.584  10.261  29.924  1.00112.25           N  
ANISOU  851  N   THR A 982    16312  13437  12902   2015   3010   5069       N  
ATOM    852  CA  THR A 982      33.241  11.523  29.282  1.00113.40           C  
ANISOU  852  CA  THR A 982    16331  13789  12965   1976   2933   4393       C  
ATOM    853  C   THR A 982      34.421  12.057  28.471  1.00104.21           C  
ANISOU  853  C   THR A 982    15166  12616  11813   2039   2350   3920       C  
ATOM    854  O   THR A 982      34.234  12.611  27.389  1.00101.95           O  
ANISOU  854  O   THR A 982    14650  12231  11854   1933   2224   3423       O  
ATOM    855  CB  THR A 982      32.798  12.586  30.308  1.00120.69           C  
ANISOU  855  CB  THR A 982    17514  15243  13097   2101   3186   4315       C  
ATOM    856  OG1 THR A 982      33.850  12.811  31.254  1.00131.26           O  
ANISOU  856  OG1 THR A 982    19262  16934  13677   2313   2901   4462       O  
ATOM    857  CG2 THR A 982      31.546  12.124  31.045  1.00121.76           C  
ANISOU  857  CG2 THR A 982    17606  15415  13243   2020   3850   4745       C  
ATOM    858  N   ARG A 983      35.632  11.884  28.995  1.00103.46           N  
ANISOU  858  N   ARG A 983    15312  12636  11363   2212   1998   4099       N  
ATOM    859  CA  ARG A 983      36.836  12.299  28.280  1.00 98.57           C  
ANISOU  859  CA  ARG A 983    14651  11996  10806   2262   1476   3690       C  
ATOM    860  C   ARG A 983      36.964  11.577  26.944  1.00 98.28           C  
ANISOU  860  C   ARG A 983    14277  11474  11590   2112   1375   3516       C  
ATOM    861  O   ARG A 983      37.382  12.175  25.951  1.00 96.79           O  
ANISOU  861  O   ARG A 983    13954  11261  11561   2052   1130   3016       O  
ATOM    862  CB  ARG A 983      38.091  12.049  29.120  1.00 98.86           C  
ANISOU  862  CB  ARG A 983    14929  12217  10416   2478   1109   3974       C  
ATOM    863  CG  ARG A 983      38.252  12.978  30.312  1.00102.17           C  
ANISOU  863  CG  ARG A 983    15699  13201   9919   2626   1053   3950       C  
ATOM    864  CD  ARG A 983      39.629  12.821  30.943  1.00105.35           C  
ANISOU  864  CD  ARG A 983    16271  13810   9948   2830    547   4120       C  
ATOM    865  NE  ARG A 983      39.790  13.655  32.130  1.00109.65           N  
ANISOU  865  NE  ARG A 983    17167  14932   9561   2959    457   4065       N  
ATOM    866  CZ  ARG A 983      40.926  13.779  32.810  1.00112.22           C  
ANISOU  866  CZ  ARG A 983    17599  15551   9487   3070    -39   4048       C  
ATOM    867  NH1 ARG A 983      42.011  13.123  32.418  1.00113.05           N  
ANISOU  867  NH1 ARG A 983    17525  15435   9995   3156   -462   4188       N  
ATOM    868  NH2 ARG A 983      40.979  14.561  33.879  1.00115.60           N  
ANISOU  868  NH2 ARG A 983    18264  16478   9180   3067   -113   3839       N  
ATOM    869  N   ARG A 984      36.602  10.296  26.919  1.00 95.26           N  
ANISOU  869  N   ARG A 984    13771  10701  11724   2043   1586   3923       N  
ATOM    870  CA  ARG A 984      36.698   9.517  25.689  1.00 94.06           C  
ANISOU  870  CA  ARG A 984    13308  10068  12364   1892   1512   3712       C  
ATOM    871  C   ARG A 984      35.622   9.948  24.698  1.00 84.79           C  
ANISOU  871  C   ARG A 984    11875   8844  11496   1661   1684   3274       C  
ATOM    872  O   ARG A 984      35.805   9.844  23.486  1.00 81.02           O  
ANISOU  872  O   ARG A 984    11180   8164  11441   1541   1515   2861       O  
ATOM    873  CB  ARG A 984      36.594   8.012  25.973  1.00103.23           C  
ANISOU  873  CB  ARG A 984    14403  10757  14065   1874   1699   4252       C  
ATOM    874  CG  ARG A 984      35.206   7.515  26.334  1.00117.08           C  
ANISOU  874  CG  ARG A 984    16068  12357  16059   1696   2211   4582       C  
ATOM    875  CD  ARG A 984      35.081   6.012  26.117  1.00129.19           C  
ANISOU  875  CD  ARG A 984    17422  13250  18413   1586   2375   4926       C  
ATOM    876  NE  ARG A 984      35.335   5.646  24.726  1.00134.18           N  
ANISOU  876  NE  ARG A 984    17753  13507  19721   1441   2172   4378       N  
ATOM    877  CZ  ARG A 984      36.237   4.747  24.341  1.00143.10           C  
ANISOU  877  CZ  ARG A 984    18817  14207  21349   1515   1977   4400       C  
ATOM    878  NH1 ARG A 984      36.969   4.109  25.244  1.00152.60           N  
ANISOU  878  NH1 ARG A 984    20200  15321  22460   1729   1897   4940       N  
ATOM    879  NH2 ARG A 984      36.401   4.481  23.051  1.00137.72           N  
ANISOU  879  NH2 ARG A 984    17873  13240  21214   1369   1840   3822       N  
ATOM    880  N   LYS A 985      34.503  10.447  25.212  1.00 85.92           N  
ANISOU  880  N   LYS A 985    12033   9202  11408   1614   2015   3358       N  
ATOM    881  CA  LYS A 985      33.455  10.969  24.346  1.00 89.57           C  
ANISOU  881  CA  LYS A 985    12225   9673  12136   1437   2132   2963       C  
ATOM    882  C   LYS A 985      33.907  12.296  23.744  1.00 81.71           C  
ANISOU  882  C   LYS A 985    11289   8962  10797   1505   1823   2457       C  
ATOM    883  O   LYS A 985      33.670  12.573  22.567  1.00 82.75           O  
ANISOU  883  O   LYS A 985    11204   9017  11219   1382   1683   2063       O  
ATOM    884  CB  LYS A 985      32.143  11.142  25.112  1.00 96.42           C  
ANISOU  884  CB  LYS A 985    13042  10686  12907   1394   2602   3201       C  
ATOM    885  CG  LYS A 985      30.977  11.527  24.222  1.00105.29           C  
ANISOU  885  CG  LYS A 985    13798  11779  14428   1221   2709   2844       C  
ATOM    886  CD  LYS A 985      30.878  10.581  23.035  1.00112.44           C  
ANISOU  886  CD  LYS A 985    14382  12272  16067    995   2567   2658       C  
ATOM    887  CE  LYS A 985      29.923  11.103  21.976  1.00114.70           C  
ANISOU  887  CE  LYS A 985    14316  12611  16655    848   2501   2221       C  
ATOM    888  NZ  LYS A 985      29.881  10.192  20.801  1.00115.81           N  
ANISOU  888  NZ  LYS A 985    14171  12401  17430    618   2320   1963       N  
ATOM    889  N   ILE A 986      34.568  13.107  24.563  1.00 73.12           N  
ANISOU  889  N   ILE A 986    10502   8198   9082   1693   1709   2479       N  
ATOM    890  CA  ILE A 986      35.152  14.359  24.101  1.00 68.57           C  
ANISOU  890  CA  ILE A 986    10008   7836   8209   1751   1420   2036       C  
ATOM    891  C   ILE A 986      36.163  14.082  22.997  1.00 68.85           C  
ANISOU  891  C   ILE A 986     9936   7678   8548   1690   1076   1785       C  
ATOM    892  O   ILE A 986      36.171  14.758  21.967  1.00 62.24           O  
ANISOU  892  O   ILE A 986     8993   6854   7803   1612    934   1404       O  
ATOM    893  CB  ILE A 986      35.823  15.122  25.259  1.00 69.95           C  
ANISOU  893  CB  ILE A 986    10521   8357   7701   1940   1329   2085       C  
ATOM    894  CG1 ILE A 986      34.760  15.593  26.257  1.00 73.72           C  
ANISOU  894  CG1 ILE A 986    11113   9079   7819   2002   1719   2215       C  
ATOM    895  CG2 ILE A 986      36.638  16.293  24.736  1.00 66.78           C  
ANISOU  895  CG2 ILE A 986    10180   8082   7111   1965    999   1631       C  
ATOM    896  CD1 ILE A 986      35.325  16.229  27.503  1.00 79.02           C  
ANISOU  896  CD1 ILE A 986    12143  10125   7754   2179   1662   2247       C  
ATOM    897  N   ALA A 987      36.995  13.066  23.214  1.00 75.33           N  
ANISOU  897  N   ALA A 987    10778   8314   9532   1738    966   2023       N  
ATOM    898  CA  ALA A 987      38.000  12.656  22.238  1.00 67.53           C  
ANISOU  898  CA  ALA A 987     9660   7120   8878   1700    700   1788       C  
ATOM    899  C   ALA A 987      37.359  12.171  20.942  1.00 65.11           C  
ANISOU  899  C   ALA A 987     9080   6553   9107   1493    776   1525       C  
ATOM    900  O   ALA A 987      37.764  12.571  19.853  1.00 66.87           O  
ANISOU  900  O   ALA A 987     9215   6792   9399   1417    604   1130       O  
ATOM    901  CB  ALA A 987      38.888  11.573  22.820  1.00 73.49           C  
ANISOU  901  CB  ALA A 987    10453   7683   9786   1830    603   2141       C  
ATOM    902  N   ILE A 988      36.363  11.302  21.064  1.00 73.42           N  
ANISOU  902  N   ILE A 988     9995   7376  10524   1388   1037   1741       N  
ATOM    903  CA  ILE A 988      35.640  10.807  19.896  1.00 78.59           C  
ANISOU  903  CA  ILE A 988    10366   7803  11690   1166   1086   1456       C  
ATOM    904  C   ILE A 988      34.904  11.951  19.202  1.00 70.25           C  
ANISOU  904  C   ILE A 988     9237   7022  10432   1092   1036   1122       C  
ATOM    905  O   ILE A 988      34.947  12.080  17.977  1.00 69.95           O  
ANISOU  905  O   ILE A 988     9068   6978  10533    975    869    739       O  
ATOM    906  CB  ILE A 988      34.638   9.694  20.277  1.00 77.96           C  
ANISOU  906  CB  ILE A 988    10120   7409  12093   1038   1396   1764       C  
ATOM    907  CG1 ILE A 988      35.392   8.421  20.664  1.00 90.25           C  
ANISOU  907  CG1 ILE A 988    11708   8570  14012   1098   1417   2073       C  
ATOM    908  CG2 ILE A 988      33.695   9.402  19.127  1.00 74.10           C  
ANISOU  908  CG2 ILE A 988     9307   6772  12076    784   1417   1400       C  
ATOM    909  CD1 ILE A 988      34.493   7.255  21.026  1.00 99.20           C  
ANISOU  909  CD1 ILE A 988    12682   9302  15708    949   1747   2417       C  
ATOM    910  N   GLY A 989      34.241  12.787  19.992  1.00 60.27           N  
ANISOU  910  N   GLY A 989     8067   6008   8826   1178   1185   1276       N  
ATOM    911  CA  GLY A 989      33.499  13.909  19.450  1.00 66.47           C  
ANISOU  911  CA  GLY A 989     8772   7016   9468   1159   1147   1020       C  
ATOM    912  C   GLY A 989      34.388  14.859  18.669  1.00 68.21           C  
ANISOU  912  C   GLY A 989     9113   7385   9416   1201    847    703       C  
ATOM    913  O   GLY A 989      34.122  15.155  17.504  1.00 72.01           O  
ANISOU  913  O   GLY A 989     9457   7894  10008   1100    702    427       O  
ATOM    914  N   SER A 990      35.449  15.334  19.311  1.00 58.75           N  
ANISOU  914  N   SER A 990     8167   6298   7857   1341    751    755       N  
ATOM    915  CA  SER A 990      36.391  16.238  18.663  1.00 59.44           C  
ANISOU  915  CA  SER A 990     8359   6498   7729   1358    507    482       C  
ATOM    916  C   SER A 990      36.994  15.605  17.407  1.00 60.53           C  
ANISOU  916  C   SER A 990     8363   6495   8142   1225    359    252       C  
ATOM    917  O   SER A 990      37.139  16.270  16.378  1.00 57.99           O  
ANISOU  917  O   SER A 990     8024   6264   7746   1156    233      2       O  
ATOM    918  CB  SER A 990      37.494  16.636  19.640  1.00 60.06           C  
ANISOU  918  CB  SER A 990     8671   6691   7460   1499    411    564       C  
ATOM    919  OG  SER A 990      38.080  15.481  20.214  1.00 75.02           O  
ANISOU  919  OG  SER A 990    10569   8453   9483   1546    408    802       O  
ATOM    920  N   ALA A 991      37.328  14.318  17.493  1.00 56.06           N  
ANISOU  920  N   ALA A 991     7709   5699   7893   1195    398    345       N  
ATOM    921  CA  ALA A 991      37.862  13.577  16.350  1.00 54.26           C  
ANISOU  921  CA  ALA A 991     7340   5306   7971   1077    312     74       C  
ATOM    922  C   ALA A 991      36.891  13.574  15.177  1.00 57.37           C  
ANISOU  922  C   ALA A 991     7563   5723   8510    899    300   -189       C  
ATOM    923  O   ALA A 991      37.288  13.804  14.035  1.00 68.55           O  
ANISOU  923  O   ALA A 991     8959   7226   9862    812    178   -501       O  
ATOM    924  CB  ALA A 991      38.203  12.143  16.750  1.00 52.78           C  
ANISOU  924  CB  ALA A 991     7068   4787   8200   1096    392    240       C  
ATOM    925  N   ARG A 992      35.621  13.310  15.466  1.00 53.59           N  
ANISOU  925  N   ARG A 992     6952   5197   8214    842    428    -57       N  
ATOM    926  CA  ARG A 992      34.575  13.310  14.447  1.00 54.94           C  
ANISOU  926  CA  ARG A 992     6911   5424   8542    679    366   -294       C  
ATOM    927  C   ARG A 992      34.440  14.678  13.771  1.00 56.95           C  
ANISOU  927  C   ARG A 992     7242   5991   8403    718    195   -428       C  
ATOM    928  O   ARG A 992      34.210  14.764  12.565  1.00 58.13           O  
ANISOU  928  O   ARG A 992     7302   6253   8532    602     30   -696       O  
ATOM    929  CB  ARG A 992      33.241  12.892  15.071  1.00 58.88           C  
ANISOU  929  CB  ARG A 992     7208   5827   9339    625    557    -86       C  
ATOM    930  CG  ARG A 992      32.125  12.611  14.078  1.00 65.40           C  
ANISOU  930  CG  ARG A 992     7722   6667  10461    428    464   -344       C  
ATOM    931  CD  ARG A 992      31.103  11.658  14.683  1.00 75.61           C  
ANISOU  931  CD  ARG A 992     8750   7711  12266    304    705   -166       C  
ATOM    932  NE  ARG A 992      30.822  11.982  16.078  1.00 84.32           N  
ANISOU  932  NE  ARG A 992     9955   8840  13243    457    990    268       N  
ATOM    933  CZ  ARG A 992      30.668  11.080  17.043  1.00 93.74           C  
ANISOU  933  CZ  ARG A 992    11127   9775  14716    429   1285    602       C  
ATOM    934  NH1 ARG A 992      30.765   9.787  16.772  1.00100.97           N  
ANISOU  934  NH1 ARG A 992    11903  10314  16147    255   1332    558       N  
ATOM    935  NH2 ARG A 992      30.416  11.474  18.283  1.00 99.36           N  
ANISOU  935  NH2 ARG A 992    11969  10595  15188    576   1551    982       N  
ATOM    936  N   GLY A 993      34.593  15.743  14.552  1.00 56.21           N  
ANISOU  936  N   GLY A 993     7331   6032   7993    884    233   -238       N  
ATOM    937  CA  GLY A 993      34.520  17.097  14.022  1.00 51.75           C  
ANISOU  937  CA  GLY A 993     6860   5682   7119    943     98   -311       C  
ATOM    938  C   GLY A 993      35.589  17.354  12.972  1.00 59.13           C  
ANISOU  938  C   GLY A 993     7908   6689   7867    875    -61   -526       C  
ATOM    939  O   GLY A 993      35.292  17.863  11.890  1.00 55.81           O  
ANISOU  939  O   GLY A 993     7466   6420   7320    815   -205   -651       O  
ATOM    940  N   LEU A 994      36.832  16.992  13.284  1.00 56.31           N  
ANISOU  940  N   LEU A 994     7661   6245   7492    889    -30   -551       N  
ATOM    941  CA  LEU A 994      37.934  17.171  12.344  1.00 54.69           C  
ANISOU  941  CA  LEU A 994     7525   6103   7150    817   -109   -763       C  
ATOM    942  C   LEU A 994      37.800  16.254  11.133  1.00 56.57           C  
ANISOU  942  C   LEU A 994     7622   6336   7536    655   -146  -1044       C  
ATOM    943  O   LEU A 994      38.143  16.643  10.013  1.00 55.54           O  
ANISOU  943  O   LEU A 994     7543   6375   7186    569   -214  -1232       O  
ATOM    944  CB  LEU A 994      39.273  16.920  13.029  1.00 46.19           C  
ANISOU  944  CB  LEU A 994     6518   4928   6103    885    -71   -736       C  
ATOM    945  CG  LEU A 994      39.644  17.853  14.174  1.00 54.66           C  
ANISOU  945  CG  LEU A 994     7749   6049   6970   1020    -82   -550       C  
ATOM    946  CD1 LEU A 994      41.018  17.472  14.714  1.00 59.91           C  
ANISOU  946  CD1 LEU A 994     8420   6650   7694   1075   -118   -558       C  
ATOM    947  CD2 LEU A 994      39.619  19.307  13.706  1.00 53.99           C  
ANISOU  947  CD2 LEU A 994     7788   6101   6623   1004   -134   -590       C  
ATOM    948  N   ALA A 995      37.310  15.039  11.367  1.00 52.57           N  
ANISOU  948  N   ALA A 995     6948   5631   7394    605    -85  -1078       N  
ATOM    949  CA  ALA A 995      37.094  14.077  10.292  1.00 55.34           C  
ANISOU  949  CA  ALA A 995     7147   5935   7945    434   -120  -1420       C  
ATOM    950  C   ALA A 995      36.136  14.650   9.259  1.00 56.28           C  
ANISOU  950  C   ALA A 995     7219   6329   7835    337   -295  -1553       C  
ATOM    951  O   ALA A 995      36.367  14.545   8.052  1.00 62.16           O  
ANISOU  951  O   ALA A 995     7977   7240   8402    218   -386  -1864       O  
ATOM    952  CB  ALA A 995      36.554  12.772  10.846  1.00 56.85           C  
ANISOU  952  CB  ALA A 995     7150   5801   8648    384    -14  -1391       C  
ATOM    953  N   PHE A 996      35.061  15.257   9.752  1.00 50.14           N  
ANISOU  953  N   PHE A 996     6381   5620   7050    404   -341  -1313       N  
ATOM    954  CA  PHE A 996      34.086  15.916   8.903  1.00 55.38           C  
ANISOU  954  CA  PHE A 996     6967   6547   7525    369   -552  -1358       C  
ATOM    955  C   PHE A 996      34.771  17.003   8.069  1.00 59.62           C  
ANISOU  955  C   PHE A 996     7740   7338   7576    404   -659  -1360       C  
ATOM    956  O   PHE A 996      34.560  17.095   6.858  1.00 64.10           O  
ANISOU  956  O   PHE A 996     8306   8149   7900    307   -842  -1542       O  
ATOM    957  CB  PHE A 996      32.961  16.501   9.760  1.00 60.60           C  
ANISOU  957  CB  PHE A 996     7510   7202   8314    494   -528  -1064       C  
ATOM    958  CG  PHE A 996      31.832  17.105   8.968  1.00 64.72           C  
ANISOU  958  CG  PHE A 996     7869   7967   8753    495   -776  -1078       C  
ATOM    959  CD1 PHE A 996      30.841  16.304   8.423  1.00 70.28           C  
ANISOU  959  CD1 PHE A 996     8257   8711   9733    339   -923  -1285       C  
ATOM    960  CD2 PHE A 996      31.749  18.476   8.789  1.00 68.88           C  
ANISOU  960  CD2 PHE A 996     8536   8660   8975    657   -883   -877       C  
ATOM    961  CE1 PHE A 996      29.796  16.854   7.702  1.00 67.27           C  
ANISOU  961  CE1 PHE A 996     7684   8588   9286    358  -1214  -1290       C  
ATOM    962  CE2 PHE A 996      30.706  19.035   8.069  1.00 75.51           C  
ANISOU  962  CE2 PHE A 996     9208   9715   9765    700  -1148   -836       C  
ATOM    963  CZ  PHE A 996      29.728  18.222   7.525  1.00 70.61           C  
ANISOU  963  CZ  PHE A 996     8254   9190   9385    558  -1335  -1040       C  
ATOM    964  N   LEU A 997      35.608  17.805   8.722  1.00 52.78           N  
ANISOU  964  N   LEU A 997     7076   6415   6562    528   -541  -1156       N  
ATOM    965  CA  LEU A 997      36.363  18.859   8.044  1.00 51.57           C  
ANISOU  965  CA  LEU A 997     7143   6430   6022    538   -579  -1113       C  
ATOM    966  C   LEU A 997      37.287  18.314   6.957  1.00 49.12           C  
ANISOU  966  C   LEU A 997     6888   6234   5542    384   -547  -1411       C  
ATOM    967  O   LEU A 997      37.378  18.888   5.874  1.00 56.48           O  
ANISOU  967  O   LEU A 997     7937   7416   6107    323   -631  -1436       O  
ATOM    968  CB  LEU A 997      37.192  19.664   9.050  1.00 49.18           C  
ANISOU  968  CB  LEU A 997     7002   5990   5694    658   -444   -915       C  
ATOM    969  CG  LEU A 997      36.479  20.451  10.151  1.00 48.29           C  
ANISOU  969  CG  LEU A 997     6902   5786   5659    828   -424   -663       C  
ATOM    970  CD1 LEU A 997      37.484  21.252  10.965  1.00 44.90           C  
ANISOU  970  CD1 LEU A 997     6656   5255   5148    901   -327   -578       C  
ATOM    971  CD2 LEU A 997      35.406  21.363   9.575  1.00 53.70           C  
ANISOU  971  CD2 LEU A 997     7562   6597   6243    898   -575   -526       C  
ATOM    972  N   HIS A 998      37.960  17.200   7.244  1.00 54.60           N  
ANISOU  972  N   HIS A 998     7499   6745   6503    333   -408  -1622       N  
ATOM    973  CA  HIS A 998      38.983  16.663   6.341  1.00 58.41           C  
ANISOU  973  CA  HIS A 998     8012   7296   6887    216   -305  -1946       C  
ATOM    974  C   HIS A 998      38.434  15.823   5.189  1.00 68.14           C  
ANISOU  974  C   HIS A 998     9151   8678   8060     58   -398  -2329       C  
ATOM    975  O   HIS A 998      39.016  15.793   4.104  1.00 74.28           O  
ANISOU  975  O   HIS A 998    10019   9676   8529    -47   -346  -2590       O  
ATOM    976  CB  HIS A 998      39.991  15.810   7.122  1.00 55.38           C  
ANISOU  976  CB  HIS A 998     7544   6618   6879    265   -126  -2026       C  
ATOM    977  CG  HIS A 998      40.756  16.565   8.162  1.00 63.55           C  
ANISOU  977  CG  HIS A 998     8663   7560   7921    397    -68  -1741       C  
ATOM    978  ND1 HIS A 998      41.579  15.942   9.077  1.00 61.71           N  
ANISOU  978  ND1 HIS A 998     8350   7094   8003    491     14  -1711       N  
ATOM    979  CD2 HIS A 998      40.826  17.891   8.431  1.00 63.49           C  
ANISOU  979  CD2 HIS A 998     8806   7656   7660    450   -106  -1492       C  
ATOM    980  CE1 HIS A 998      42.122  16.852   9.864  1.00 66.75           C  
ANISOU  980  CE1 HIS A 998     9080   7744   8536    581     -2  -1488       C  
ATOM    981  NE2 HIS A 998      41.683  18.042   9.497  1.00 65.14           N  
ANISOU  981  NE2 HIS A 998     9020   7718   8014    549    -55  -1374       N  
ATOM    982  N   HIS A 999      37.330  15.122   5.421  1.00 71.50           N  
ANISOU  982  N   HIS A 999     9388   8996   8783     23   -518  -2393       N  
ATOM    983  CA  HIS A 999      36.900  14.108   4.467  1.00 72.79           C  
ANISOU  983  CA  HIS A 999     9419   9226   9011   -154   -606  -2853       C  
ATOM    984  C   HIS A 999      35.530  14.381   3.878  1.00 73.20           C  
ANISOU  984  C   HIS A 999     9368   9544   8900   -222   -916  -2867       C  
ATOM    985  O   HIS A 999      35.299  14.141   2.694  1.00 78.28           O  
ANISOU  985  O   HIS A 999    10015  10478   9248   -364  -1080  -3219       O  
ATOM    986  CB  HIS A 999      36.923  12.732   5.134  1.00 75.56           C  
ANISOU  986  CB  HIS A 999     9568   9142  10001   -191   -466  -3030       C  
ATOM    987  CG  HIS A 999      38.276  12.344   5.643  1.00 89.00           C  
ANISOU  987  CG  HIS A 999    11324  10584  11909    -98   -212  -3033       C  
ATOM    988  ND1 HIS A 999      38.705  12.644   6.918  1.00 87.38           N  
ANISOU  988  ND1 HIS A 999    11155  10171  11874     76   -116  -2619       N  
ATOM    989  CD2 HIS A 999      39.310  11.712   5.038  1.00 96.58           C  
ANISOU  989  CD2 HIS A 999    12288  11485  12925   -141    -48  -3413       C  
ATOM    990  CE1 HIS A 999      39.939  12.200   7.081  1.00 81.48           C  
ANISOU  990  CE1 HIS A 999    10408   9249  11300    140     52  -2718       C  
ATOM    991  NE2 HIS A 999      40.329  11.629   5.957  1.00 93.05           N  
ANISOU  991  NE2 HIS A 999    11840  10781  12736     19    118  -3196       N  
ATOM    992  N   ASN A1000      34.625  14.887   4.703  1.00 70.44           N  
ANISOU  992  N   ASN A1000     8914   9121   8729   -112  -1001  -2500       N  
ATOM    993  CA  ASN A1000      33.262  15.121   4.263  1.00 72.80           C  
ANISOU  993  CA  ASN A1000     9028   9643   8990   -148  -1308  -2490       C  
ATOM    994  C   ASN A1000      33.102  16.456   3.536  1.00 82.56           C  
ANISOU  994  C   ASN A1000    10443  11268   9658    -47  -1526  -2247       C  
ATOM    995  O   ASN A1000      32.207  16.611   2.705  1.00 89.45           O  
ANISOU  995  O   ASN A1000    11205  12448  10334    -92  -1857  -2325       O  
ATOM    996  CB  ASN A1000      32.312  15.048   5.457  1.00 76.26           C  
ANISOU  996  CB  ASN A1000     9226   9828   9924    -67  -1254  -2214       C  
ATOM    997  CG  ASN A1000      32.249  13.659   6.065  1.00 75.74           C  
ANISOU  997  CG  ASN A1000     8956   9374  10447   -194  -1064  -2403       C  
ATOM    998  OD1 ASN A1000      33.034  13.318   6.949  1.00 82.42           O  
ANISOU  998  OD1 ASN A1000     9902   9920  11493   -124   -793  -2265       O  
ATOM    999  ND2 ASN A1000      31.310  12.851   5.594  1.00 82.02           N  
ANISOU  999  ND2 ASN A1000     9453  10163  11547   -385  -1225  -2708       N  
ATOM   1000  N   CYS A1001      33.972  17.415   3.842  1.00 76.81           N  
ANISOU 1000  N   CYS A1001     9980  10515   8690     87  -1361  -1944       N  
ATOM   1001  CA  CYS A1001      33.920  18.722   3.188  1.00 72.81           C  
ANISOU 1001  CA  CYS A1001     9673  10293   7699    185  -1519  -1649       C  
ATOM   1002  C   CYS A1001      34.777  18.782   1.925  1.00 75.78           C  
ANISOU 1002  C   CYS A1001    10295  10979   7521     60  -1507  -1831       C  
ATOM   1003  O   CYS A1001      35.952  18.422   1.939  1.00 79.68           O  
ANISOU 1003  O   CYS A1001    10909  11373   7993    -15  -1222  -2007       O  
ATOM   1004  CB  CYS A1001      34.363  19.825   4.150  1.00 65.13           C  
ANISOU 1004  CB  CYS A1001     8854   9101   6792    370  -1338  -1235       C  
ATOM   1005  SG  CYS A1001      33.314  20.025   5.602  1.00 69.24           S  
ANISOU 1005  SG  CYS A1001     9143   9342   7823    551  -1310   -991       S  
ATOM   1006  N   SER A1002      34.173  19.242   0.836  1.00 79.60           N  
ANISOU 1006  N   SER A1002    10836  11860   7546     48  -1814  -1776       N  
ATOM   1007  CA  SER A1002      34.901  19.521  -0.393  1.00 84.32           C  
ANISOU 1007  CA  SER A1002    11720  12825   7492    -51  -1789  -1842       C  
ATOM   1008  C   SER A1002      34.571  20.939  -0.854  1.00 96.29           C  
ANISOU 1008  C   SER A1002    13431  14554   8600     98  -1982  -1298       C  
ATOM   1009  O   SER A1002      33.438  21.213  -1.252  1.00110.94           O  
ANISOU 1009  O   SER A1002    15169  16634  10347    181  -2383  -1156       O  
ATOM   1010  CB  SER A1002      34.558  18.506  -1.481  1.00 85.11           C  
ANISOU 1010  CB  SER A1002    11749  13280   7310   -243  -1992  -2375       C  
ATOM   1011  OG  SER A1002      35.398  18.680  -2.607  1.00 86.66           O  
ANISOU 1011  OG  SER A1002    12248  13844   6834   -349  -1871  -2488       O  
ATOM   1012  N   PRO A1003      35.556  21.852  -0.805  1.00 85.64           N  
ANISOU 1012  N   PRO A1003    12354  13111   7073    134  -1706   -977       N  
ATOM   1013  CA  PRO A1003      36.962  21.666  -0.419  1.00 77.77           C  
ANISOU 1013  CA  PRO A1003    11465  11893   6191     38  -1258  -1115       C  
ATOM   1014  C   PRO A1003      37.165  21.269   1.039  1.00 69.54           C  
ANISOU 1014  C   PRO A1003    10228  10380   5814    105  -1084  -1189       C  
ATOM   1015  O   PRO A1003      36.344  21.602   1.892  1.00 65.33           O  
ANISOU 1015  O   PRO A1003     9561   9644   5618    258  -1220   -974       O  
ATOM   1016  CB  PRO A1003      37.583  23.047  -0.672  1.00 80.58           C  
ANISOU 1016  CB  PRO A1003    12105  12248   6264     84  -1113   -621       C  
ATOM   1017  CG  PRO A1003      36.643  23.733  -1.605  1.00 90.08           C  
ANISOU 1017  CG  PRO A1003    13423  13794   7010    168  -1475   -286       C  
ATOM   1018  CD  PRO A1003      35.289  23.238  -1.223  1.00 87.63           C  
ANISOU 1018  CD  PRO A1003    12809  13476   7009    278  -1853   -406       C  
ATOM   1019  N   HIS A1004      38.250  20.547   1.303  1.00 72.13           N  
ANISOU 1019  N   HIS A1004    10535  10561   6310      4   -782  -1490       N  
ATOM   1020  CA  HIS A1004      38.620  20.166   2.660  1.00 67.42           C  
ANISOU 1020  CA  HIS A1004     9789   9557   6268     75   -623  -1520       C  
ATOM   1021  C   HIS A1004      38.913  21.405   3.481  1.00 63.24           C  
ANISOU 1021  C   HIS A1004     9370   8820   5839    201   -550  -1110       C  
ATOM   1022  O   HIS A1004      39.319  22.438   2.939  1.00 64.87           O  
ANISOU 1022  O   HIS A1004     9775   9126   5748    182   -495   -863       O  
ATOM   1023  CB  HIS A1004      39.848  19.249   2.667  1.00 69.89           C  
ANISOU 1023  CB  HIS A1004    10054   9772   6731    -28   -336  -1881       C  
ATOM   1024  CG  HIS A1004      39.664  17.978   1.902  1.00 75.69           C  
ANISOU 1024  CG  HIS A1004    10680  10637   7441   -154   -358  -2369       C  
ATOM   1025  ND1 HIS A1004      38.424  17.454   1.616  1.00 85.06           N  
ANISOU 1025  ND1 HIS A1004    11746  11926   8648   -183   -639  -2511       N  
ATOM   1026  CD2 HIS A1004      40.570  17.127   1.363  1.00 79.81           C  
ANISOU 1026  CD2 HIS A1004    11173  11187   7965   -262   -126  -2794       C  
ATOM   1027  CE1 HIS A1004      38.573  16.329   0.930  1.00 89.83           C  
ANISOU 1027  CE1 HIS A1004    12272  12603   9257   -324   -592  -3026       C  
ATOM   1028  NE2 HIS A1004      39.862  16.113   0.766  1.00 89.84           N  
ANISOU 1028  NE2 HIS A1004    12336  12555   9243   -360   -269  -3208       N  
ATOM   1029  N   ILE A1005      38.714  21.300   4.788  1.00 56.36           N  
ANISOU 1029  N   ILE A1005     8379   7654   5383    317   -534  -1044       N  
ATOM   1030  CA  ILE A1005      39.023  22.403   5.681  1.00 52.34           C  
ANISOU 1030  CA  ILE A1005     7966   6931   4990    428   -462   -757       C  
ATOM   1031  C   ILE A1005      40.142  22.020   6.630  1.00 59.24           C  
ANISOU 1031  C   ILE A1005     8792   7591   6126    416   -272   -886       C  
ATOM   1032  O   ILE A1005      40.042  21.029   7.358  1.00 53.38           O  
ANISOU 1032  O   ILE A1005     7901   6729   5652    454   -264  -1028       O  
ATOM   1033  CB  ILE A1005      37.797  22.841   6.497  1.00 52.44           C  
ANISOU 1033  CB  ILE A1005     7903   6823   5199    608   -610   -550       C  
ATOM   1034  CG1 ILE A1005      36.664  23.259   5.560  1.00 57.06           C  
ANISOU 1034  CG1 ILE A1005     8480   7626   5576    654   -854   -397       C  
ATOM   1035  CG2 ILE A1005      38.166  23.976   7.436  1.00 47.07           C  
ANISOU 1035  CG2 ILE A1005     7340   5908   4637    717   -515   -344       C  
ATOM   1036  CD1 ILE A1005      35.417  23.713   6.278  1.00 56.76           C  
ANISOU 1036  CD1 ILE A1005     8305   7475   5786    851   -981   -207       C  
ATOM   1037  N   ILE A1006      41.216  22.803   6.606  1.00 61.25           N  
ANISOU 1037  N   ILE A1006     9156   7794   6321    359   -129   -816       N  
ATOM   1038  CA  ILE A1006      42.280  22.664   7.589  1.00 50.78           C  
ANISOU 1038  CA  ILE A1006     7760   6282   5253    365    -15   -907       C  
ATOM   1039  C   ILE A1006      42.055  23.709   8.675  1.00 54.15           C  
ANISOU 1039  C   ILE A1006     8266   6520   5788    481    -73   -708       C  
ATOM   1040  O   ILE A1006      41.988  24.904   8.393  1.00 69.53           O  
ANISOU 1040  O   ILE A1006    10356   8423   7640    468    -65   -521       O  
ATOM   1041  CB  ILE A1006      43.673  22.839   6.963  1.00 47.08           C  
ANISOU 1041  CB  ILE A1006     7292   5866   4732    207    189  -1016       C  
ATOM   1042  CG1 ILE A1006      43.782  22.022   5.679  1.00 50.67           C  
ANISOU 1042  CG1 ILE A1006     7721   6557   4975     90    288  -1232       C  
ATOM   1043  CG2 ILE A1006      44.755  22.439   7.956  1.00 48.52           C  
ANISOU 1043  CG2 ILE A1006     7313   5890   5234    230    243  -1159       C  
ATOM   1044  CD1 ILE A1006      44.984  22.374   4.839  1.00 57.13           C  
ANISOU 1044  CD1 ILE A1006     8564   7490   5652    -79    555  -1298       C  
ATOM   1045  N   HIS A1007      41.926  23.253   9.915  1.00 49.68           N  
ANISOU 1045  N   HIS A1007     7622   5836   5419    597   -120   -747       N  
ATOM   1046  CA  HIS A1007      41.625  24.136  11.036  1.00 51.09           C  
ANISOU 1046  CA  HIS A1007     7884   5872   5658    719   -162   -633       C  
ATOM   1047  C   HIS A1007      42.820  25.024  11.388  1.00 59.43           C  
ANISOU 1047  C   HIS A1007     8997   6818   6766    640   -115   -682       C  
ATOM   1048  O   HIS A1007      42.659  26.229  11.610  1.00 53.70           O  
ANISOU 1048  O   HIS A1007     8396   5960   6047    660   -115   -594       O  
ATOM   1049  CB  HIS A1007      41.196  23.303  12.247  1.00 51.20           C  
ANISOU 1049  CB  HIS A1007     7818   5849   5785    853   -197   -654       C  
ATOM   1050  CG  HIS A1007      40.676  24.113  13.391  1.00 50.73           C  
ANISOU 1050  CG  HIS A1007     7857   5702   5716    994   -208   -576       C  
ATOM   1051  ND1 HIS A1007      41.506  24.772  14.273  1.00 54.39           N  
ANISOU 1051  ND1 HIS A1007     8401   6092   6173   1002   -223   -657       N  
ATOM   1052  CD2 HIS A1007      39.412  24.362  13.805  1.00 54.76           C  
ANISOU 1052  CD2 HIS A1007     8377   6198   6231   1131   -193   -471       C  
ATOM   1053  CE1 HIS A1007      40.774  25.396  15.178  1.00 60.82           C  
ANISOU 1053  CE1 HIS A1007     9309   6854   6947   1140   -206   -629       C  
ATOM   1054  NE2 HIS A1007      39.499  25.164  14.918  1.00 53.18           N  
ANISOU 1054  NE2 HIS A1007     8291   5915   5999   1229   -164   -505       N  
ATOM   1055  N   ARG A1008      44.003  24.404  11.440  1.00 51.60           N  
ANISOU 1055  N   ARG A1008     7881   5856   5870    552    -77   -842       N  
ATOM   1056  CA  ARG A1008      45.292  25.066  11.688  1.00 42.26           C  
ANISOU 1056  CA  ARG A1008     6658   4595   4803    437    -42   -938       C  
ATOM   1057  C   ARG A1008      45.490  25.599  13.113  1.00 49.11           C  
ANISOU 1057  C   ARG A1008     7557   5358   5744    521   -173   -998       C  
ATOM   1058  O   ARG A1008      46.506  26.232  13.393  1.00 60.04           O  
ANISOU 1058  O   ARG A1008     8887   6670   7254    409   -188  -1117       O  
ATOM   1059  CB  ARG A1008      45.515  26.215  10.693  1.00 49.37           C  
ANISOU 1059  CB  ARG A1008     7668   5441   5650    276     91   -832       C  
ATOM   1060  CG  ARG A1008      45.779  25.766   9.261  1.00 60.10           C  
ANISOU 1060  CG  ARG A1008     8998   6969   6869    142    253   -821       C  
ATOM   1061  CD  ARG A1008      45.851  26.958   8.303  1.00 69.20           C  
ANISOU 1061  CD  ARG A1008    10312   8079   7901     -1    394   -607       C  
ATOM   1062  NE  ARG A1008      47.130  27.667   8.347  1.00 74.32           N  
ANISOU 1062  NE  ARG A1008    10885   8597   8755   -194    552   -659       N  
ATOM   1063  CZ  ARG A1008      47.264  28.982   8.188  1.00 78.18           C  
ANISOU 1063  CZ  ARG A1008    11505   8876   9325   -303    638   -471       C  
ATOM   1064  NH1 ARG A1008      46.197  29.744   7.993  1.00 80.71           N  
ANISOU 1064  NH1 ARG A1008    12047   9086   9534   -196    566   -200       N  
ATOM   1065  NH2 ARG A1008      48.467  29.540   8.234  1.00 83.30           N  
ANISOU 1065  NH2 ARG A1008    12032   9393  10226   -517    796   -550       N  
ATOM   1066  N   ASP A1009      44.541  25.353  14.013  1.00 51.75           N  
ANISOU 1066  N   ASP A1009     7968   5702   5994    701   -257   -942       N  
ATOM   1067  CA  ASP A1009      44.701  25.818  15.394  1.00 59.04           C  
ANISOU 1067  CA  ASP A1009     8955   6589   6889    788   -370  -1034       C  
ATOM   1068  C   ASP A1009      43.907  24.955  16.364  1.00 55.80           C  
ANISOU 1068  C   ASP A1009     8570   6277   6353    980   -416   -953       C  
ATOM   1069  O   ASP A1009      43.298  25.452  17.311  1.00 60.89           O  
ANISOU 1069  O   ASP A1009     9349   6920   6869   1096   -424   -963       O  
ATOM   1070  CB  ASP A1009      44.286  27.289  15.536  1.00 57.43           C  
ANISOU 1070  CB  ASP A1009     8921   6214   6687    778   -333  -1055       C  
ATOM   1071  CG  ASP A1009      45.074  28.017  16.620  1.00 73.68           C  
ANISOU 1071  CG  ASP A1009    11009   8210   8775    743   -449  -1291       C  
ATOM   1072  OD1 ASP A1009      46.224  27.611  16.885  1.00 78.49           O  
ANISOU 1072  OD1 ASP A1009    11467   8905   9451    657   -567  -1422       O  
ATOM   1073  OD2 ASP A1009      44.553  28.994  17.203  1.00 82.39           O  
ANISOU 1073  OD2 ASP A1009    12268   9179   9859    805   -434  -1378       O  
ATOM   1074  N   MET A1010      43.926  23.652  16.115  1.00 54.56           N  
ANISOU 1074  N   MET A1010     8285   6190   6255   1007   -411   -878       N  
ATOM   1075  CA  MET A1010      43.336  22.691  17.028  1.00 60.26           C  
ANISOU 1075  CA  MET A1010     9010   6971   6915   1161   -427   -748       C  
ATOM   1076  C   MET A1010      44.083  22.708  18.359  1.00 61.61           C  
ANISOU 1076  C   MET A1010     9222   7227   6960   1248   -586   -786       C  
ATOM   1077  O   MET A1010      45.309  22.619  18.390  1.00 60.63           O  
ANISOU 1077  O   MET A1010     8978   7124   6934   1195   -727   -895       O  
ATOM   1078  CB  MET A1010      43.360  21.291  16.414  1.00 57.03           C  
ANISOU 1078  CB  MET A1010     8438   6540   6691   1148   -387   -684       C  
ATOM   1079  CG  MET A1010      42.701  20.226  17.275  1.00 63.08           C  
ANISOU 1079  CG  MET A1010     9199   7301   7468   1283   -363   -488       C  
ATOM   1080  SD  MET A1010      40.965  20.574  17.637  1.00 73.63           S  
ANISOU 1080  SD  MET A1010    10641   8658   8678   1354   -209   -345       S  
ATOM   1081  CE  MET A1010      40.517  19.081  18.520  1.00 80.29           C  
ANISOU 1081  CE  MET A1010    11430   9461   9617   1454   -128    -81       C  
ATOM   1082  N   LYS A1011      43.333  22.843  19.449  1.00 58.54           N  
ANISOU 1082  N   LYS A1011     8987   6915   6339   1384   -565   -705       N  
ATOM   1083  CA  LYS A1011      43.896  22.834  20.797  1.00 58.51           C  
ANISOU 1083  CA  LYS A1011     9072   7067   6094   1485   -733   -727       C  
ATOM   1084  C   LYS A1011      42.780  22.743  21.832  1.00 60.30           C  
ANISOU 1084  C   LYS A1011     9480   7406   6026   1638   -597   -581       C  
ATOM   1085  O   LYS A1011      41.604  22.895  21.500  1.00 61.62           O  
ANISOU 1085  O   LYS A1011     9670   7502   6240   1656   -373   -513       O  
ATOM   1086  CB  LYS A1011      44.751  24.080  21.049  1.00 55.23           C  
ANISOU 1086  CB  LYS A1011     8702   6663   5622   1393   -889  -1031       C  
ATOM   1087  CG  LYS A1011      44.034  25.411  20.851  1.00 59.18           C  
ANISOU 1087  CG  LYS A1011     9347   7034   6102   1349   -742  -1190       C  
ATOM   1088  CD  LYS A1011      44.995  26.564  21.084  1.00 65.05           C  
ANISOU 1088  CD  LYS A1011    10110   7720   6887   1221   -896  -1512       C  
ATOM   1089  CE  LYS A1011      44.392  27.902  20.687  1.00 64.43           C  
ANISOU 1089  CE  LYS A1011    10152   7404   6923   1167   -735  -1647       C  
ATOM   1090  NZ  LYS A1011      45.288  29.028  21.078  1.00 65.41           N  
ANISOU 1090  NZ  LYS A1011    10302   7422   7128   1026   -873  -1997       N  
ATOM   1091  N   SER A1012      43.149  22.503  23.086  1.00 59.70           N  
ANISOU 1091  N   SER A1012     9518   7531   5634   1752   -731   -529       N  
ATOM   1092  CA  SER A1012      42.161  22.289  24.137  1.00 68.49           C  
ANISOU 1092  CA  SER A1012    10817   8799   6407   1897   -553   -352       C  
ATOM   1093  C   SER A1012      41.280  23.517  24.380  1.00 68.81           C  
ANISOU 1093  C   SER A1012    11010   8843   6292   1916   -355   -585       C  
ATOM   1094  O   SER A1012      40.119  23.380  24.767  1.00 69.80           O  
ANISOU 1094  O   SER A1012    11201   9014   6308   2008    -73   -447       O  
ATOM   1095  CB  SER A1012      42.853  21.872  25.436  1.00 69.55           C  
ANISOU 1095  CB  SER A1012    11082   9208   6137   2019   -774   -245       C  
ATOM   1096  OG  SER A1012      43.935  22.734  25.734  1.00 72.99           O  
ANISOU 1096  OG  SER A1012    11539   9749   6444   1966  -1083   -590       O  
ATOM   1097  N   SER A1013      41.821  24.710  24.148  1.00 68.23           N  
ANISOU 1097  N   SER A1013    10967   8689   6269   1829   -476   -937       N  
ATOM   1098  CA  SER A1013      41.048  25.933  24.356  1.00 74.63           C  
ANISOU 1098  CA  SER A1013    11911   9426   7019   1866   -291  -1186       C  
ATOM   1099  C   SER A1013      40.043  26.145  23.221  1.00 76.04           C  
ANISOU 1099  C   SER A1013    11963   9363   7568   1850    -69  -1078       C  
ATOM   1100  O   SER A1013      39.120  26.944  23.345  1.00 80.13           O  
ANISOU 1100  O   SER A1013    12539   9796   8109   1938    135  -1186       O  
ATOM   1101  CB  SER A1013      41.970  27.149  24.485  1.00 77.82           C  
ANISOU 1101  CB  SER A1013    12383   9753   7434   1761   -492  -1601       C  
ATOM   1102  OG  SER A1013      42.446  27.583  23.223  1.00 82.05           O  
ANISOU 1102  OG  SER A1013    12762  10014   8397   1596   -545  -1638       O  
ATOM   1103  N   ASN A1014      40.226  25.424  22.118  1.00 71.78           N  
ANISOU 1103  N   ASN A1014    11237   8724   7312   1752   -123   -884       N  
ATOM   1104  CA  ASN A1014      39.298  25.493  20.995  1.00 62.07           C  
ANISOU 1104  CA  ASN A1014     9877   7333   6374   1733     19   -766       C  
ATOM   1105  C   ASN A1014      38.429  24.249  20.918  1.00 62.69           C  
ANISOU 1105  C   ASN A1014     9823   7477   6518   1776    157   -489       C  
ATOM   1106  O   ASN A1014      37.875  23.921  19.868  1.00 57.54           O  
ANISOU 1106  O   ASN A1014     9008   6736   6118   1719    187   -389       O  
ATOM   1107  CB  ASN A1014      40.048  25.695  19.678  1.00 57.47           C  
ANISOU 1107  CB  ASN A1014     9194   6607   6037   1567   -119   -798       C  
ATOM   1108  CG  ASN A1014      40.590  27.101  19.536  1.00 64.34           C  
ANISOU 1108  CG  ASN A1014    10162   7318   6967   1500   -175  -1025       C  
ATOM   1109  OD1 ASN A1014      40.206  27.999  20.285  1.00 70.54           O  
ANISOU 1109  OD1 ASN A1014    11081   8050   7672   1594   -103  -1189       O  
ATOM   1110  ND2 ASN A1014      41.481  27.302  18.572  1.00 62.54           N  
ANISOU 1110  ND2 ASN A1014     9864   6991   6905   1330   -268  -1048       N  
ATOM   1111  N   VAL A1015      38.325  23.551  22.040  1.00 59.57           N  
ANISOU 1111  N   VAL A1015     9503   7243   5889   1864    233   -362       N  
ATOM   1112  CA  VAL A1015      37.332  22.503  22.180  1.00 61.80           C  
ANISOU 1112  CA  VAL A1015     9671   7550   6261   1901    443    -87       C  
ATOM   1113  C   VAL A1015      36.348  22.948  23.242  1.00 65.90           C  
ANISOU 1113  C   VAL A1015    10294   8196   6549   2044    725    -84       C  
ATOM   1114  O   VAL A1015      36.689  23.040  24.421  1.00 74.25           O  
ANISOU 1114  O   VAL A1015    11560   9443   7206   2128    750   -105       O  
ATOM   1115  CB  VAL A1015      37.949  21.146  22.563  1.00 61.74           C  
ANISOU 1115  CB  VAL A1015     9647   7584   6226   1884    369    157       C  
ATOM   1116  CG1 VAL A1015      36.855  20.137  22.867  1.00 54.22           C  
ANISOU 1116  CG1 VAL A1015     8594   6616   5393   1905    644    460       C  
ATOM   1117  CG2 VAL A1015      38.835  20.639  21.444  1.00 57.65           C  
ANISOU 1117  CG2 VAL A1015     8981   6921   6001   1757    154    110       C  
ATOM   1118  N   LEU A1016      35.129  23.251  22.818  1.00 64.13           N  
ANISOU 1118  N   LEU A1016     9911   7893   6563   2079    932    -75       N  
ATOM   1119  CA  LEU A1016      34.112  23.723  23.747  1.00 74.08           C  
ANISOU 1119  CA  LEU A1016    11214   9260   7673   2228   1263   -107       C  
ATOM   1120  C   LEU A1016      33.189  22.574  24.144  1.00 70.91           C  
ANISOU 1120  C   LEU A1016    10660   8931   7353   2223   1557    213       C  
ATOM   1121  O   LEU A1016      33.123  21.557  23.445  1.00 67.94           O  
ANISOU 1121  O   LEU A1016    10091   8445   7279   2097   1486    412       O  
ATOM   1122  CB  LEU A1016      33.320  24.879  23.133  1.00 64.06           C  
ANISOU 1122  CB  LEU A1016     9824   7840   6677   2309   1329   -300       C  
ATOM   1123  CG  LEU A1016      34.172  26.007  22.541  1.00 67.86           C  
ANISOU 1123  CG  LEU A1016    10427   8161   7197   2281   1062   -553       C  
ATOM   1124  CD1 LEU A1016      33.302  27.201  22.151  1.00 66.40           C  
ANISOU 1124  CD1 LEU A1016    10152   7794   7284   2417   1169   -691       C  
ATOM   1125  CD2 LEU A1016      35.281  26.434  23.500  1.00 60.57           C  
ANISOU 1125  CD2 LEU A1016     9798   7340   5878   2278    957   -778       C  
ATOM   1126  N   LEU A1017      32.493  22.736  25.268  1.00 64.33           N  
ANISOU 1126  N   LEU A1017     9912   8270   6259   2346   1913    242       N  
ATOM   1127  CA  LEU A1017      31.626  21.686  25.797  1.00 71.74           C  
ANISOU 1127  CA  LEU A1017    10720   9284   7253   2326   2269    583       C  
ATOM   1128  C   LEU A1017      30.231  22.216  26.097  1.00 77.89           C  
ANISOU 1128  C   LEU A1017    11309  10108   8178   2435   2698    513       C  
ATOM   1129  O   LEU A1017      30.069  23.108  26.928  1.00 86.14           O  
ANISOU 1129  O   LEU A1017    12535  11306   8889   2591   2905    290       O  
ATOM   1130  CB  LEU A1017      32.236  21.085  27.066  1.00 79.59           C  
ANISOU 1130  CB  LEU A1017    12026  10515   7700   2364   2350    807       C  
ATOM   1131  CG  LEU A1017      33.706  20.661  26.985  1.00 76.39           C  
ANISOU 1131  CG  LEU A1017    11804  10104   7117   2313   1909    858       C  
ATOM   1132  CD1 LEU A1017      34.237  20.289  28.359  1.00 73.77           C  
ANISOU 1132  CD1 LEU A1017    11797  10071   6160   2407   1950   1068       C  
ATOM   1133  CD2 LEU A1017      33.879  19.511  26.006  1.00 78.78           C  
ANISOU 1133  CD2 LEU A1017    11866  10145   7921   2163   1755   1095       C  
ATOM   1134  N   ASP A1018      29.222  21.657  25.434  1.00 80.15           N  
ANISOU 1134  N   ASP A1018    11204  10264   8987   2353   2836    668       N  
ATOM   1135  CA  ASP A1018      27.844  22.099  25.638  1.00 84.04           C  
ANISOU 1135  CA  ASP A1018    11412  10789   9732   2459   3240    611       C  
ATOM   1136  C   ASP A1018      27.258  21.565  26.946  1.00 91.05           C  
ANISOU 1136  C   ASP A1018    12357  11892  10345   2489   3792    841       C  
ATOM   1137  O   ASP A1018      27.993  21.087  27.812  1.00 86.38           O  
ANISOU 1137  O   ASP A1018    12117  11463   9241   2475   3826   1019       O  
ATOM   1138  CB  ASP A1018      26.963  21.688  24.449  1.00 85.76           C  
ANISOU 1138  CB  ASP A1018    11137  10821  10626   2345   3145    677       C  
ATOM   1139  CG  ASP A1018      26.993  20.193  24.171  1.00 88.38           C  
ANISOU 1139  CG  ASP A1018    11321  11060  11200   2106   3122    985       C  
ATOM   1140  OD1 ASP A1018      26.988  19.388  25.126  1.00 90.22           O  
ANISOU 1140  OD1 ASP A1018    11669  11370  11241   2056   3441   1268       O  
ATOM   1141  OD2 ASP A1018      27.011  19.819  22.980  1.00 90.79           O  
ANISOU 1141  OD2 ASP A1018    11402  11205  11892   1966   2788    943       O  
ATOM   1142  N   GLU A1019      25.934  21.641  27.078  1.00 96.28           N  
ANISOU 1142  N   GLU A1019    12658  12572  11350   2535   4223    860       N  
ATOM   1143  CA  GLU A1019      25.247  21.199  28.292  1.00 98.21           C  
ANISOU 1143  CA  GLU A1019    12918  13036  11360   2557   4848   1083       C  
ATOM   1144  C   GLU A1019      25.406  19.698  28.521  1.00 93.27           C  
ANISOU 1144  C   GLU A1019    12303  12376  10759   2337   4946   1583       C  
ATOM   1145  O   GLU A1019      25.326  19.223  29.653  1.00 95.98           O  
ANISOU 1145  O   GLU A1019    12859  12930  10680   2342   5369   1872       O  
ATOM   1146  CB  GLU A1019      23.756  21.550  28.236  1.00101.25           C  
ANISOU 1146  CB  GLU A1019    12804  13412  12256   2634   5297    994       C  
ATOM   1147  CG  GLU A1019      23.417  22.748  27.371  1.00116.06           C  
ANISOU 1147  CG  GLU A1019    14442  15135  14520   2807   5036    600       C  
ATOM   1148  CD  GLU A1019      23.195  22.371  25.919  1.00124.29           C  
ANISOU 1148  CD  GLU A1019    15081  15932  16211   2660   4579    658       C  
ATOM   1149  OE1 GLU A1019      22.223  21.638  25.639  1.00126.45           O  
ANISOU 1149  OE1 GLU A1019    14875  16161  17010   2527   4770    836       O  
ATOM   1150  OE2 GLU A1019      23.997  22.801  25.060  1.00123.84           O  
ANISOU 1150  OE2 GLU A1019    15184  15745  16126   2662   4037    514       O  
ATOM   1151  N   ASN A1020      25.622  18.955  27.442  1.00 86.04           N  
ANISOU 1151  N   ASN A1020    11167  11186  10339   2147   4568   1686       N  
ATOM   1152  CA  ASN A1020      25.785  17.510  27.532  1.00 96.76           C  
ANISOU 1152  CA  ASN A1020    12499  12401  11863   1933   4633   2128       C  
ATOM   1153  C   ASN A1020      27.253  17.099  27.600  1.00 99.34           C  
ANISOU 1153  C   ASN A1020    13251  12699  11794   1929   4212   2243       C  
ATOM   1154  O   ASN A1020      27.580  15.914  27.513  1.00103.15           O  
ANISOU 1154  O   ASN A1020    13725  12985  12481   1777   4161   2583       O  
ATOM   1155  CB  ASN A1020      25.108  16.831  26.342  1.00 98.15           C  
ANISOU 1155  CB  ASN A1020    12152  12274  12868   1712   4498   2123       C  
ATOM   1156  CG  ASN A1020      23.619  17.098  26.290  1.00102.81           C  
ANISOU 1156  CG  ASN A1020    12230  12893  13940   1702   4897   2050       C  
ATOM   1157  OD1 ASN A1020      22.951  17.172  27.323  1.00101.74           O  
ANISOU 1157  OD1 ASN A1020    12080  12939  13639   1767   5477   2208       O  
ATOM   1158  ND2 ASN A1020      23.088  17.247  25.081  1.00104.92           N  
ANISOU 1158  ND2 ASN A1020    12060  13011  14794   1627   4587   1806       N  
ATOM   1159  N   LEU A1021      28.125  18.091  27.762  1.00 98.51           N  
ANISOU 1159  N   LEU A1021    13485  12762  11183   2097   3917   1946       N  
ATOM   1160  CA  LEU A1021      29.570  17.880  27.807  1.00 91.96           C  
ANISOU 1160  CA  LEU A1021    13006  11937   9997   2113   3476   1983       C  
ATOM   1161  C   LEU A1021      30.084  17.151  26.574  1.00 88.57           C  
ANISOU 1161  C   LEU A1021    12380  11181  10090   1949   3071   1989       C  
ATOM   1162  O   LEU A1021      31.030  16.371  26.660  1.00 92.84           O  
ANISOU 1162  O   LEU A1021    13083  11637  10554   1917   2852   2203       O  
ATOM   1163  CB  LEU A1021      29.966  17.108  29.069  1.00 94.74           C  
ANISOU 1163  CB  LEU A1021    13683  12474   9839   2153   3680   2434       C  
ATOM   1164  CG  LEU A1021      29.960  17.908  30.372  1.00104.20           C  
ANISOU 1164  CG  LEU A1021    15243  14099  10251   2341   3935   2351       C  
ATOM   1165  CD1 LEU A1021      30.335  17.025  31.553  1.00107.21           C  
ANISOU 1165  CD1 LEU A1021    15953  14693  10089   2375   4104   2885       C  
ATOM   1166  CD2 LEU A1021      30.902  19.097  30.265  1.00104.07           C  
ANISOU 1166  CD2 LEU A1021    15464  14207   9873   2462   3499   1850       C  
ATOM   1167  N   GLU A1022      29.457  17.398  25.429  1.00 88.64           N  
ANISOU 1167  N   GLU A1022    12035  11020  10623   1861   2969   1747       N  
ATOM   1168  CA  GLU A1022      29.966  16.862  24.178  1.00 86.26           C  
ANISOU 1168  CA  GLU A1022    11577  10467  10730   1711   2575   1648       C  
ATOM   1169  C   GLU A1022      30.843  17.904  23.499  1.00 81.99           C  
ANISOU 1169  C   GLU A1022    11189   9974   9989   1787   2159   1284       C  
ATOM   1170  O   GLU A1022      30.516  19.092  23.485  1.00 80.70           O  
ANISOU 1170  O   GLU A1022    11045   9925   9694   1906   2173   1045       O  
ATOM   1171  CB  GLU A1022      28.831  16.428  23.250  1.00 99.59           C  
ANISOU 1171  CB  GLU A1022    12797  11977  13067   1543   2647   1595       C  
ATOM   1172  CG  GLU A1022      29.289  15.431  22.193  1.00115.05           C  
ANISOU 1172  CG  GLU A1022    14611  13666  15438   1346   2350   1555       C  
ATOM   1173  CD  GLU A1022      28.171  14.977  21.282  1.00124.41           C  
ANISOU 1173  CD  GLU A1022    15323  14704  17241   1154   2371   1444       C  
ATOM   1174  OE1 GLU A1022      27.130  15.665  21.226  1.00130.64           O  
ANISOU 1174  OE1 GLU A1022    15868  15622  18148   1204   2502   1346       O  
ATOM   1175  OE2 GLU A1022      28.336  13.929  20.620  1.00121.98           O  
ANISOU 1175  OE2 GLU A1022    14868  14148  17329    959   2242   1426       O  
ATOM   1176  N   ALA A1023      31.963  17.447  22.949  1.00 79.19           N  
ANISOU 1176  N   ALA A1023    10927   9502   9657   1720   1821   1253       N  
ATOM   1177  CA  ALA A1023      32.961  18.332  22.368  1.00 68.90           C  
ANISOU 1177  CA  ALA A1023     9777   8237   8164   1761   1463    957       C  
ATOM   1178  C   ALA A1023      32.459  18.996  21.097  1.00 67.97           C  
ANISOU 1178  C   ALA A1023     9445   8056   8324   1706   1314    699       C  
ATOM   1179  O   ALA A1023      31.841  18.357  20.250  1.00 69.80           O  
ANISOU 1179  O   ALA A1023     9398   8170   8952   1574   1293    701       O  
ATOM   1180  CB  ALA A1023      34.247  17.565  22.086  1.00 65.67           C  
ANISOU 1180  CB  ALA A1023     9456   7720   7777   1701   1194   1001       C  
ATOM   1181  N   ARG A1024      32.719  20.293  20.975  1.00 63.58           N  
ANISOU 1181  N   ARG A1024     9023   7575   7558   1808   1198    480       N  
ATOM   1182  CA  ARG A1024      32.398  21.014  19.755  1.00 66.94           C  
ANISOU 1182  CA  ARG A1024     9302   7943   8189   1783   1013    300       C  
ATOM   1183  C   ARG A1024      33.589  21.900  19.387  1.00 58.21           C  
ANISOU 1183  C   ARG A1024     8428   6825   6864   1791    761    119       C  
ATOM   1184  O   ARG A1024      33.955  22.809  20.137  1.00 60.10           O  
ANISOU 1184  O   ARG A1024     8879   7109   6849   1902    799     17       O  
ATOM   1185  CB  ARG A1024      31.101  21.823  19.927  1.00 60.27           C  
ANISOU 1185  CB  ARG A1024     8293   7133   7473   1918   1210    273       C  
ATOM   1186  CG  ARG A1024      29.974  21.005  20.587  1.00 65.79           C  
ANISOU 1186  CG  ARG A1024     8758   7868   8372   1908   1555    460       C  
ATOM   1187  CD  ARG A1024      28.578  21.572  20.365  1.00 69.31           C  
ANISOU 1187  CD  ARG A1024     8876   8327   9132   2006   1703    421       C  
ATOM   1188  NE  ARG A1024      28.127  21.405  18.987  1.00 67.66           N  
ANISOU 1188  NE  ARG A1024     8366   8061   9282   1903   1412    370       N  
ATOM   1189  CZ  ARG A1024      26.923  21.758  18.550  1.00 71.07           C  
ANISOU 1189  CZ  ARG A1024     8430   8511  10062   1972   1424    350       C  
ATOM   1190  NH1 ARG A1024      26.042  22.290  19.387  1.00 78.21           N  
ANISOU 1190  NH1 ARG A1024     9200   9457  11061   2149   1768    368       N  
ATOM   1191  NH2 ARG A1024      26.600  21.576  17.276  1.00 71.05           N  
ANISOU 1191  NH2 ARG A1024     8181   8510  10305   1872   1087    298       N  
ATOM   1192  N   VAL A1025      34.212  21.603  18.249  1.00 51.41           N  
ANISOU 1192  N   VAL A1025     7519   5904   6110   1656    527     56       N  
ATOM   1193  CA  VAL A1025      35.420  22.308  17.822  1.00 55.73           C  
ANISOU 1193  CA  VAL A1025     8244   6431   6500   1619    330    -89       C  
ATOM   1194  C   VAL A1025      35.095  23.750  17.434  1.00 61.40           C  
ANISOU 1194  C   VAL A1025     9017   7104   7206   1699    294   -176       C  
ATOM   1195  O   VAL A1025      34.095  24.011  16.766  1.00 60.26           O  
ANISOU 1195  O   VAL A1025     8712   6948   7237   1736    287   -127       O  
ATOM   1196  CB  VAL A1025      36.111  21.588  16.634  1.00 51.71           C  
ANISOU 1196  CB  VAL A1025     7652   5889   6105   1451    158   -143       C  
ATOM   1197  CG1 VAL A1025      37.360  22.340  16.199  1.00 52.05           C  
ANISOU 1197  CG1 VAL A1025     7844   5918   6013   1395     19   -275       C  
ATOM   1198  CG2 VAL A1025      36.467  20.164  17.016  1.00 53.82           C  
ANISOU 1198  CG2 VAL A1025     7854   6118   6477   1397    199    -63       C  
ATOM   1199  N   SER A1026      35.950  24.677  17.858  1.00 62.21           N  
ANISOU 1199  N   SER A1026     9329   7164   7144   1726    252   -302       N  
ATOM   1200  CA  SER A1026      35.709  26.102  17.665  1.00 61.15           C  
ANISOU 1200  CA  SER A1026     9275   6903   7054   1812    251   -383       C  
ATOM   1201  C   SER A1026      36.905  26.835  17.057  1.00 59.73           C  
ANISOU 1201  C   SER A1026     9231   6614   6849   1690     99   -478       C  
ATOM   1202  O   SER A1026      37.963  26.244  16.823  1.00 62.71           O  
ANISOU 1202  O   SER A1026     9620   7048   7161   1544      0   -511       O  
ATOM   1203  CB  SER A1026      35.346  26.754  19.000  1.00 70.65           C  
ANISOU 1203  CB  SER A1026    10598   8101   8143   1978    436   -507       C  
ATOM   1204  OG  SER A1026      35.122  28.145  18.848  1.00 90.13           O  
ANISOU 1204  OG  SER A1026    13137  10373  10734   2076    454   -619       O  
ATOM   1205  N   ASP A1027      36.706  28.129  16.811  1.00 59.10           N  
ANISOU 1205  N   ASP A1027     9230   6351   6876   1755    107   -510       N  
ATOM   1206  CA  ASP A1027      37.733  29.067  16.342  1.00 60.52           C  
ANISOU 1206  CA  ASP A1027     9543   6356   7097   1634     25   -582       C  
ATOM   1207  C   ASP A1027      38.339  28.687  14.992  1.00 55.21           C  
ANISOU 1207  C   ASP A1027     8821   5735   6421   1451    -83   -446       C  
ATOM   1208  O   ASP A1027      39.446  28.147  14.920  1.00 54.96           O  
ANISOU 1208  O   ASP A1027     8786   5783   6315   1291   -128   -531       O  
ATOM   1209  CB  ASP A1027      38.849  29.213  17.381  1.00 63.79           C  
ANISOU 1209  CB  ASP A1027    10080   6771   7385   1561      4   -834       C  
ATOM   1210  CG  ASP A1027      39.632  30.512  17.218  1.00 84.35           C  
ANISOU 1210  CG  ASP A1027    12806   9109  10135   1460    -24   -975       C  
ATOM   1211  OD1 ASP A1027      39.633  31.084  16.105  1.00 74.64           O  
ANISOU 1211  OD1 ASP A1027    11575   7713   9071   1394    -28   -805       O  
ATOM   1212  OD2 ASP A1027      40.247  30.966  18.208  1.00 94.08           O  
ANISOU 1212  OD2 ASP A1027    14136  10299  11313   1437    -45  -1253       O  
ATOM   1213  N   PHE A1028      37.616  29.005  13.925  1.00 57.31           N  
ANISOU 1213  N   PHE A1028     9042   5974   6758   1488   -125   -242       N  
ATOM   1214  CA  PHE A1028      38.097  28.782  12.570  1.00 42.33           C  
ANISOU 1214  CA  PHE A1028     7140   4166   4776   1324   -205   -112       C  
ATOM   1215  C   PHE A1028      38.730  30.050  11.999  1.00 47.97           C  
ANISOU 1215  C   PHE A1028     8012   4656   5557   1244   -181     -9       C  
ATOM   1216  O   PHE A1028      38.779  30.233  10.781  1.00 48.07           O  
ANISOU 1216  O   PHE A1028     8061   4721   5481   1165   -222    202       O  
ATOM   1217  CB  PHE A1028      36.951  28.307  11.672  1.00 48.62           C  
ANISOU 1217  CB  PHE A1028     7801   5130   5540   1395   -310     63       C  
ATOM   1218  CG  PHE A1028      36.512  26.889  11.941  1.00 46.05           C  
ANISOU 1218  CG  PHE A1028     7295   5005   5196   1381   -321    -38       C  
ATOM   1219  CD1 PHE A1028      35.909  26.547  13.142  1.00 46.40           C  
ANISOU 1219  CD1 PHE A1028     7259   5028   5344   1507   -221   -105       C  
ATOM   1220  CD2 PHE A1028      36.697  25.901  10.986  1.00 47.80           C  
ANISOU 1220  CD2 PHE A1028     7436   5421   5304   1233   -400    -71       C  
ATOM   1221  CE1 PHE A1028      35.508  25.240  13.391  1.00 55.05           C  
ANISOU 1221  CE1 PHE A1028     8188   6254   6476   1474   -197   -145       C  
ATOM   1222  CE2 PHE A1028      36.298  24.595  11.227  1.00 49.19           C  
ANISOU 1222  CE2 PHE A1028     7438   5703   5550   1203   -397   -177       C  
ATOM   1223  CZ  PHE A1028      35.704  24.263  12.432  1.00 43.20           C  
ANISOU 1223  CZ  PHE A1028     6593   4881   4941   1319   -294   -184       C  
ATOM   1224  N   GLY A1029      39.213  30.923  12.884  1.00 45.26           N  
ANISOU 1224  N   GLY A1029     7769   4065   5362   1252   -109   -161       N  
ATOM   1225  CA  GLY A1029      39.833  32.170  12.472  1.00 53.59           C  
ANISOU 1225  CA  GLY A1029     8960   4820   6581   1151    -56    -81       C  
ATOM   1226  C   GLY A1029      41.065  32.027  11.589  1.00 62.52           C  
ANISOU 1226  C   GLY A1029    10106   6016   7635    875    -13    -28       C  
ATOM   1227  O   GLY A1029      41.367  32.925  10.799  1.00 67.79           O  
ANISOU 1227  O   GLY A1029    10877   6486   8394    777     56    190       O  
ATOM   1228  N   MET A1030      41.779  30.910  11.718  1.00 59.09           N  
ANISOU 1228  N   MET A1030     9556   5837   7059    758    -27   -207       N  
ATOM   1229  CA AMET A1030      42.961  30.674  10.891  0.59 64.84           C  
ANISOU 1229  CA AMET A1030    10245   6654   7737    510     59   -202       C  
ATOM   1230  CA BMET A1030      42.969  30.657  10.911  0.41 62.34           C  
ANISOU 1230  CA BMET A1030     9925   6340   7420    510     58   -208       C  
ATOM   1231  C   MET A1030      42.740  29.528   9.908  1.00 64.23           C  
ANISOU 1231  C   MET A1030    10094   6906   7405    486     48   -128       C  
ATOM   1232  O   MET A1030      43.669  29.109   9.212  1.00 60.38           O  
ANISOU 1232  O   MET A1030     9549   6550   6842    302    154   -177       O  
ATOM   1233  CB AMET A1030      44.189  30.380  11.759  0.59 57.28           C  
ANISOU 1233  CB AMET A1030     9169   5695   6900    383     58   -514       C  
ATOM   1234  CB BMET A1030      44.163  30.312  11.805  0.41 55.28           C  
ANISOU 1234  CB BMET A1030     8910   5454   6639    392     51   -523       C  
ATOM   1235  CG AMET A1030      44.652  31.540  12.634  0.59 54.62           C  
ANISOU 1235  CG AMET A1030     8890   5049   6813    331     55   -678       C  
ATOM   1236  CG BMET A1030      44.412  31.297  12.939  0.41 55.98           C  
ANISOU 1236  CG BMET A1030     9056   5274   6938    403     12   -717       C  
ATOM   1237  SD AMET A1030      44.954  33.075  11.735  0.59 69.62           S  
ANISOU 1237  SD AMET A1030    10924   6568   8959    153    226   -444       S  
ATOM   1238  SD BMET A1030      45.924  30.930  13.854  0.41 64.09           S  
ANISOU 1238  SD BMET A1030     9902   6374   8077    242    -78  -1080       S  
ATOM   1239  CE AMET A1030      46.212  32.569  10.567  0.59 76.31           C  
ANISOU 1239  CE AMET A1030    11637   7610   9749   -142    400   -365       C  
ATOM   1240  CE BMET A1030      46.920  32.357  13.433  0.41101.46           C  
ANISOU 1240  CE BMET A1030    14639  10753  13158    -48     54  -1114       C  
ATOM   1241  N   ALA A1031      41.509  29.030   9.841  1.00 57.33           N  
ANISOU 1241  N   ALA A1031     9198   6160   6424    663    -66    -47       N  
ATOM   1242  CA  ALA A1031      41.202  27.903   8.961  1.00 51.02           C  
ANISOU 1242  CA  ALA A1031     8316   5660   5409    630   -109    -52       C  
ATOM   1243  C   ALA A1031      41.337  28.278   7.488  1.00 53.60           C  
ANISOU 1243  C   ALA A1031     8754   6118   5495    509    -65    159       C  
ATOM   1244  O   ALA A1031      41.155  29.439   7.111  1.00 59.95           O  
ANISOU 1244  O   ALA A1031     9706   6768   6305    529    -52    437       O  
ATOM   1245  CB  ALA A1031      39.810  27.374   9.245  1.00 54.65           C  
ANISOU 1245  CB  ALA A1031     8688   6204   5873    819   -251    -24       C  
ATOM   1246  N   ARG A1032      41.663  27.286   6.662  1.00 55.10           N  
ANISOU 1246  N   ARG A1032     8884   6585   5469    390    -27     29       N  
ATOM   1247  CA  ARG A1032      41.835  27.496   5.230  1.00 54.03           C  
ANISOU 1247  CA  ARG A1032     8874   6667   4988    263     39    193       C  
ATOM   1248  C   ARG A1032      41.192  26.369   4.437  1.00 62.97           C  
ANISOU 1248  C   ARG A1032     9941   8143   5842    263    -86     44       C  
ATOM   1249  O   ARG A1032      41.019  25.261   4.941  1.00 66.27           O  
ANISOU 1249  O   ARG A1032    10185   8588   6406    294   -136   -243       O  
ATOM   1250  CB  ARG A1032      43.316  27.596   4.866  1.00 57.65           C  
ANISOU 1250  CB  ARG A1032     9340   7126   5437     34    325    104       C  
ATOM   1251  CG  ARG A1032      44.046  28.784   5.460  1.00 64.51           C  
ANISOU 1251  CG  ARG A1032    10259   7655   6598    -34    453    231       C  
ATOM   1252  CD  ARG A1032      43.667  30.095   4.781  1.00 69.48           C  
ANISOU 1252  CD  ARG A1032    11118   8155   7126    -36    478    675       C  
ATOM   1253  NE  ARG A1032      44.412  31.217   5.349  1.00 76.71           N  
ANISOU 1253  NE  ARG A1032    12064   8678   8405   -138    624    748       N  
ATOM   1254  CZ  ARG A1032      44.024  31.907   6.419  1.00 83.45           C  
ANISOU 1254  CZ  ARG A1032    12922   9188   9597     -4    508    722       C  
ATOM   1255  NH1 ARG A1032      42.893  31.597   7.042  1.00 80.59           N  
ANISOU 1255  NH1 ARG A1032    12530   8845   9244    249    282    664       N  
ATOM   1256  NH2 ARG A1032      44.767  32.911   6.869  1.00 85.89           N  
ANISOU 1256  NH2 ARG A1032    13251   9132  10252   -136    641    723       N  
ATOM   1257  N   LEU A1033      40.852  26.658   3.187  1.00 67.00           N  
ANISOU 1257  N   LEU A1033    10597   8911   5948    220   -141    243       N  
ATOM   1258  CA  LEU A1033      40.257  25.668   2.306  1.00 64.85           C  
ANISOU 1258  CA  LEU A1033    10279   9009   5351    191   -291     54       C  
ATOM   1259  C   LEU A1033      41.322  25.014   1.434  1.00 75.37           C  
ANISOU 1259  C   LEU A1033    11650  10589   6399    -23    -34   -213       C  
ATOM   1260  O   LEU A1033      42.251  25.677   0.973  1.00 78.87           O  
ANISOU 1260  O   LEU A1033    12234  11042   6690   -150    225    -55       O  
ATOM   1261  CB  LEU A1033      39.177  26.309   1.431  1.00 64.22           C  
ANISOU 1261  CB  LEU A1033    10327   9144   4928    291   -567    404       C  
ATOM   1262  CG  LEU A1033      37.943  26.850   2.160  1.00 68.00           C  
ANISOU 1262  CG  LEU A1033    10703   9419   5714    537   -835    629       C  
ATOM   1263  CD1 LEU A1033      37.030  27.584   1.198  1.00 74.45           C  
ANISOU 1263  CD1 LEU A1033    11632  10446   6209    657  -1121   1034       C  
ATOM   1264  CD2 LEU A1033      37.183  25.735   2.861  1.00 61.44           C  
ANISOU 1264  CD2 LEU A1033     9593   8587   5164    598   -975    292       C  
ATOM   1265  N   MET A1034      41.186  23.709   1.223  1.00 76.45           N  
ANISOU 1265  N   MET A1034    11642  10896   6509    -68    -74   -635       N  
ATOM   1266  CA  MET A1034      42.088  22.969   0.348  1.00 77.54           C  
ANISOU 1266  CA  MET A1034    11793  11280   6388   -246    181   -978       C  
ATOM   1267  C   MET A1034      41.301  22.033  -0.556  1.00 84.70           C  
ANISOU 1267  C   MET A1034    12686  12540   6955   -285    -17  -1288       C  
ATOM   1268  O   MET A1034      40.387  21.344  -0.102  1.00 87.55           O  
ANISOU 1268  O   MET A1034    12874  12821   7570   -206   -273  -1454       O  
ATOM   1269  CB  MET A1034      43.110  22.169   1.161  1.00 73.74           C  
ANISOU 1269  CB  MET A1034    11094  10543   6381   -274    417  -1319       C  
ATOM   1270  CG  MET A1034      44.103  21.388   0.302  1.00 76.47           C  
ANISOU 1270  CG  MET A1034    11401  11098   6555   -430    733  -1719       C  
ATOM   1271  SD  MET A1034      45.205  20.322   1.254  1.00 79.28           S  
ANISOU 1271  SD  MET A1034    11435  11129   7559   -399    944  -2112       S  
ATOM   1272  CE  MET A1034      44.092  18.996   1.713  1.00 68.75           C  
ANISOU 1272  CE  MET A1034     9948   9669   6506   -288    652  -2394       C  
ATOM   1273  N   SER A1035      41.652  22.012  -1.838  1.00 91.42           N  
ANISOU 1273  N   SER A1035    13717  13795   7226   -425    111  -1380       N  
ATOM   1274  CA  SER A1035      41.032  21.088  -2.778  1.00 93.52           C  
ANISOU 1274  CA  SER A1035    13982  14445   7107   -496    -70  -1780       C  
ATOM   1275  C   SER A1035      41.375  19.648  -2.419  1.00 93.83           C  
ANISOU 1275  C   SER A1035    13770  14310   7570   -547     59  -2403       C  
ATOM   1276  O   SER A1035      42.434  19.376  -1.853  1.00 96.97           O  
ANISOU 1276  O   SER A1035    14054  14434   8356   -558    387  -2537       O  
ATOM   1277  CB  SER A1035      41.477  21.393  -4.208  1.00100.14           C  
ANISOU 1277  CB  SER A1035    15105  15792   7152   -640    100  -1766       C  
ATOM   1278  OG  SER A1035      40.952  20.439  -5.117  1.00107.32           O  
ANISOU 1278  OG  SER A1035    16019  17105   7652   -727    -76  -2258       O  
ATOM   1279  N   ALA A1036      40.478  18.727  -2.752  1.00 95.64           N  
ANISOU 1279  N   ALA A1036    13891  14677   7770   -576   -213  -2780       N  
ATOM   1280  CA  ALA A1036      40.707  17.311  -2.489  1.00 96.32           C  
ANISOU 1280  CA  ALA A1036    13744  14546   8307   -631    -99  -3377       C  
ATOM   1281  C   ALA A1036      41.755  16.746  -3.443  1.00 97.55           C  
ANISOU 1281  C   ALA A1036    13978  14933   8154   -773    276  -3863       C  
ATOM   1282  O   ALA A1036      42.226  15.620  -3.272  1.00 96.15           O  
ANISOU 1282  O   ALA A1036    13603  14463   8464   -776    455  -4279       O  
ATOM   1283  CB  ALA A1036      39.406  16.534  -2.605  1.00100.86           C  
ANISOU 1283  CB  ALA A1036    14162  15170   8991   -658   -493  -3657       C  
ATOM   1284  N   MET A1037      42.114  17.539  -4.447  1.00100.27           N  
ANISOU 1284  N   MET A1037    14592  15661   7845   -827    395  -3627       N  
ATOM   1285  CA  MET A1037      43.125  17.152  -5.421  1.00101.75           C  
ANISOU 1285  CA  MET A1037    14850  15989   7822   -896    777  -3886       C  
ATOM   1286  C   MET A1037      44.521  17.567  -4.962  1.00100.56           C  
ANISOU 1286  C   MET A1037    14639  15664   7904   -910   1264  -3778       C  
ATOM   1287  O   MET A1037      45.490  17.448  -5.715  1.00108.60           O  
ANISOU 1287  O   MET A1037    15688  16820   8755   -968   1644  -3923       O  
ATOM   1288  CB  MET A1037      42.809  17.772  -6.785  1.00107.32           C  
ANISOU 1288  CB  MET A1037    15881  17206   7691   -940    681  -3675       C  
ATOM   1289  CG  MET A1037      41.469  17.340  -7.366  1.00110.03           C  
ANISOU 1289  CG  MET A1037    16263  17758   7783   -940    173  -3825       C  
ATOM   1290  SD  MET A1037      40.844  18.477  -8.620  1.00159.04           S  
ANISOU 1290  SD  MET A1037    22874  24524  13030   -916   -102  -3317       S  
ATOM   1291  CE  MET A1037      42.242  18.557  -9.736  1.00117.58           C  
ANISOU 1291  CE  MET A1037    17856  19525   7293   -985    490  -3403       C  
ATOM   1292  N   ASP A1038      44.618  18.055  -3.727  1.00 92.09           N  
ANISOU 1292  N   ASP A1038    13463  14284   7243   -857   1246  -3527       N  
ATOM   1293  CA  ASP A1038      45.898  18.473  -3.158  1.00 92.08           C  
ANISOU 1293  CA  ASP A1038    13345  14027   7614   -851   1624  -3370       C  
ATOM   1294  C   ASP A1038      46.198  17.746  -1.853  1.00 85.56           C  
ANISOU 1294  C   ASP A1038    12192  12681   7636   -713   1584  -3515       C  
ATOM   1295  O   ASP A1038      45.289  17.445  -1.077  1.00 89.20           O  
ANISOU 1295  O   ASP A1038    12579  12908   8404   -601   1234  -3434       O  
ATOM   1296  CB  ASP A1038      45.915  19.984  -2.919  1.00 96.31           C  
ANISOU 1296  CB  ASP A1038    14058  14542   7993   -848   1587  -2686       C  
ATOM   1297  CG  ASP A1038      45.856  20.779  -4.204  1.00107.61           C  
ANISOU 1297  CG  ASP A1038    15824  16456   8606   -980   1704  -2433       C  
ATOM   1298  OD1 ASP A1038      46.366  20.289  -5.233  1.00111.81           O  
ANISOU 1298  OD1 ASP A1038    16422  17338   8724  -1101   2008  -2788       O  
ATOM   1299  OD2 ASP A1038      45.301  21.897  -4.183  1.00114.93           O  
ANISOU 1299  OD2 ASP A1038    16951  17396   9322   -942   1499  -1859       O  
HETATM 1300  N   TPO A1039      47.475  17.468  -1.612  1.00 84.62           N  
ANISOU 1300  N   TPO A1039    11865  12396   7892   -714   1948  -3704       N  
HETATM 1301  CA  TPO A1039      47.888  16.832  -0.368  1.00 83.55           C  
ANISOU 1301  CA  TPO A1039    11422  11792   8532   -559   1895  -3773       C  
HETATM 1302  CB  TPO A1039      49.106  15.941  -0.587  1.00 86.20           C  
ANISOU 1302  CB  TPO A1039    11485  12038   9231   -551   2287  -4252       C  
HETATM 1303  CG2 TPO A1039      48.647  14.494  -0.750  1.00 84.41           C  
ANISOU 1303  CG2 TPO A1039    11138  11642   9292   -478   2173  -4667       C  
HETATM 1304  OG1 TPO A1039      49.822  16.338  -1.758  1.00 92.83           O  
ANISOU 1304  OG1 TPO A1039    12418  13250   9605   -713   2688  -4370       O  
HETATM 1305  P   TPO A1039      51.355  16.554  -1.313  1.00109.01           P  
ANISOU 1305  P   TPO A1039    14146  15131  12141   -703   3067  -4389       P  
HETATM 1306  O1P TPO A1039      52.131  17.424  -2.426  1.00114.16           O  
ANISOU 1306  O1P TPO A1039    14919  16178  12280   -920   3530  -4291       O  
HETATM 1307  O2P TPO A1039      52.065  15.118  -1.161  1.00129.66           O  
ANISOU 1307  O2P TPO A1039    16382  17451  15431   -547   3156  -4807       O  
HETATM 1308  O3P TPO A1039      51.404  17.253  -0.010  1.00104.09           O  
ANISOU 1308  O3P TPO A1039    13434  14199  11918   -609   2776  -3916       O  
HETATM 1309  C   TPO A1039      48.178  17.886   0.689  1.00 86.22           C  
ANISOU 1309  C   TPO A1039    11736  11915   9109   -498   1789  -3262       C  
HETATM 1310  O   TPO A1039      48.032  17.636   1.885  1.00 88.40           O  
ANISOU 1310  O   TPO A1039    11867  11861   9861   -349   1569  -3145       O  
ATOM   1311  N   HIS A1040      48.588  19.069   0.244  1.00 88.24           N  
ANISOU 1311  N   HIS A1040    12147  12358   9024   -623   1956  -2962       N  
ATOM   1312  CA  HIS A1040      48.893  20.157   1.164  1.00 85.23           C  
ANISOU 1312  CA  HIS A1040    11750  11757   8876   -601   1873  -2536       C  
ATOM   1313  C   HIS A1040      48.445  21.502   0.609  1.00 78.47           C  
ANISOU 1313  C   HIS A1040    11207  11075   7532   -708   1856  -2089       C  
ATOM   1314  O   HIS A1040      48.043  21.610  -0.551  1.00 81.14           O  
ANISOU 1314  O   HIS A1040    11773  11757   7300   -802   1932  -2072       O  
ATOM   1315  CB  HIS A1040      50.392  20.199   1.475  1.00 87.32           C  
ANISOU 1315  CB  HIS A1040    11723  11895   9562   -651   2183  -2658       C  
ATOM   1316  CG  HIS A1040      51.232  20.696   0.339  1.00 88.74           C  
ANISOU 1316  CG  HIS A1040    11943  12348   9425   -864   2645  -2688       C  
ATOM   1317  ND1 HIS A1040      51.733  19.862  -0.638  1.00 96.59           N  
ANISOU 1317  ND1 HIS A1040    12855  13579  10265   -927   3004  -3120       N  
ATOM   1318  CD2 HIS A1040      51.659  21.941   0.026  1.00 90.71           C  
ANISOU 1318  CD2 HIS A1040    12310  12660   9494  -1039   2846  -2336       C  
ATOM   1319  CE1 HIS A1040      52.433  20.573  -1.504  1.00102.26           C  
ANISOU 1319  CE1 HIS A1040    13643  14540  10670  -1131   3427  -3017       C  
ATOM   1320  NE2 HIS A1040      52.404  21.838  -1.124  1.00 99.79           N  
ANISOU 1320  NE2 HIS A1040    13451  14110  10356  -1211   3338  -2516       N  
ATOM   1321  N   LEU A1041      48.518  22.523   1.455  1.00 70.88           N  
ANISOU 1321  N   LEU A1041    10263   9868   6802   -685   1742  -1730       N  
ATOM   1322  CA  LEU A1041      48.193  23.886   1.063  1.00 71.65           C  
ANISOU 1322  CA  LEU A1041    10632  10006   6586   -768   1743  -1264       C  
ATOM   1323  C   LEU A1041      49.308  24.833   1.493  1.00 71.04           C  
ANISOU 1323  C   LEU A1041    10448   9704   6841   -900   1973  -1101       C  
ATOM   1324  O   LEU A1041      49.684  24.867   2.664  1.00 74.25           O  
ANISOU 1324  O   LEU A1041    10650   9823   7740   -831   1842  -1172       O  
ATOM   1325  CB  LEU A1041      46.866  24.321   1.681  1.00 73.52           C  
ANISOU 1325  CB  LEU A1041    11016  10104   6816   -596   1324   -987       C  
ATOM   1326  CG  LEU A1041      46.509  25.797   1.519  1.00 74.50           C  
ANISOU 1326  CG  LEU A1041    11385  10137   6784   -622   1285   -479       C  
ATOM   1327  CD1 LEU A1041      46.203  26.118   0.068  1.00 74.16           C  
ANISOU 1327  CD1 LEU A1041    11609  10458   6111   -718   1387   -252       C  
ATOM   1328  CD2 LEU A1041      45.338  26.144   2.402  1.00 74.23           C  
ANISOU 1328  CD2 LEU A1041    11397   9891   6919   -412    908   -296       C  
HETATM 1329  N   SEP A1042      49.836  25.598   0.545  1.00 69.06           N  
ANISOU 1329  N   SEP A1042    10332   9596   6313  -1103   2312   -882       N  
HETATM 1330  CA  SEP A1042      50.925  26.526   0.838  1.00 77.48           C  
ANISOU 1330  CA  SEP A1042    11267  10432   7738  -1285   2576   -733       C  
HETATM 1331  CB  SEP A1042      51.828  26.681  -0.385  1.00 89.31           C  
ANISOU 1331  CB  SEP A1042    12779  12198   8956  -1535   3116   -707       C  
HETATM 1332  OG  SEP A1042      52.267  25.409  -0.826  1.00 99.85           O  
ANISOU 1332  OG  SEP A1042    13920  13801  10218  -1514   3309  -1193       O  
HETATM 1333  C   SEP A1042      50.393  27.883   1.292  1.00 82.25           C  
ANISOU 1333  C   SEP A1042    12082  10734   8436  -1281   2391   -274       C  
HETATM 1334  O   SEP A1042      49.609  28.516   0.587  1.00 87.95           O  
ANISOU 1334  O   SEP A1042    13127  11546   8743  -1270   2347    115       O  
HETATM 1335  P   SEP A1042      53.223  25.543  -2.109  1.00103.59           P  
ANISOU 1335  P   SEP A1042    14400  14599  10360  -1773   3946  -1210       P  
HETATM 1336  O1P SEP A1042      52.553  26.549  -3.173  1.00123.81           O  
ANISOU 1336  O1P SEP A1042    17456  17393  12195  -1888   4032   -643       O  
HETATM 1337  O2P SEP A1042      53.399  24.090  -2.780  1.00108.39           O  
ANISOU 1337  O2P SEP A1042    14887  15552  10745  -1709   4139  -1796       O  
HETATM 1338  O3P SEP A1042      54.657  26.112  -1.644  1.00121.93           O  
ANISOU 1338  O3P SEP A1042    16336  16662  13328  -1975   4303  -1217       O  
ATOM   1339  N   VAL A1043      50.825  28.324   2.471  1.00 83.78           N  
ANISOU 1339  N   VAL A1043    12085  10568   9181  -1276   2267   -335       N  
ATOM   1340  CA  VAL A1043      50.304  29.549   3.070  1.00 85.11           C  
ANISOU 1340  CA  VAL A1043    12426  10385   9527  -1246   2077    -11       C  
ATOM   1341  C   VAL A1043      51.301  30.708   3.062  1.00 95.16           C  
ANISOU 1341  C   VAL A1043    13632  11373  11151  -1521   2369    160       C  
ATOM   1342  O   VAL A1043      52.386  30.614   2.484  1.00 93.18           O  
ANISOU 1342  O   VAL A1043    13202  11235  10967  -1754   2758     82       O  
ATOM   1343  CB  VAL A1043      49.861  29.308   4.522  1.00 81.24           C  
ANISOU 1343  CB  VAL A1043    11822   9679   9366  -1031   1679   -227       C  
ATOM   1344  CG1 VAL A1043      48.681  28.349   4.565  1.00 77.73           C  
ANISOU 1344  CG1 VAL A1043    11467   9438   8629   -776   1399   -301       C  
ATOM   1345  CG2 VAL A1043      51.023  28.779   5.347  1.00 79.01           C  
ANISOU 1345  CG2 VAL A1043    11164   9339   9518  -1090   1698   -613       C  
HETATM 1346  N   SEP A1044      50.918  31.800   3.719  1.00 97.33           N  
ANISOU 1346  N   SEP A1044    14031  11254  11696  -1498   2202    366       N  
HETATM 1347  CA  SEP A1044      51.724  33.015   3.750  1.00104.75           C  
ANISOU 1347  CA  SEP A1044    14930  11828  13044  -1773   2452    541       C  
HETATM 1348  CB  SEP A1044      50.840  34.247   3.531  1.00109.99           C  
ANISOU 1348  CB  SEP A1044    15951  12166  13673  -1720   2394   1038       C  
HETATM 1349  OG  SEP A1044      50.027  34.510   4.666  1.00108.79           O  
ANISOU 1349  OG  SEP A1044    15847  11746  13744  -1479   2001    908       O  
HETATM 1350  C   SEP A1044      52.486  33.157   5.064  1.00 99.95           C  
ANISOU 1350  C   SEP A1044    13997  10944  13037  -1838   2297    139       C  
HETATM 1351  O   SEP A1044      53.576  33.725   5.101  1.00 95.06           O  
ANISOU 1351  O   SEP A1044    13154  10128  12836  -2130   2539     77       O  
HETATM 1352  P   SEP A1044      48.531  33.949   4.450  1.00166.97           P  
ANISOU 1352  P   SEP A1044    23438  19372  20632  -1127   1694   1052       P  
HETATM 1353  O1P SEP A1044      48.170  33.959   2.882  1.00 98.35           O  
ANISOU 1353  O1P SEP A1044    15001  10990  11376  -1160   1874   1520       O  
HETATM 1354  O2P SEP A1044      48.428  32.444   5.016  1.00131.68           O  
ANISOU 1354  O2P SEP A1044    18753  15259  16020   -967   1481    584       O  
HETATM 1355  O3P SEP A1044      47.487  34.882   5.243  1.00 92.91           O  
ANISOU 1355  O3P SEP A1044    14221   9576  11506   -898   1426   1190       O  
ATOM   1356  N   THR A1045      51.906  32.643   6.144  1.00 96.59           N  
ANISOU 1356  N   THR A1045    13537  10522  12639  -1576   1889   -131       N  
ATOM   1357  CA  THR A1045      52.521  32.765   7.460  1.00100.88           C  
ANISOU 1357  CA  THR A1045    13820  10869  13642  -1602   1667   -511       C  
ATOM   1358  C   THR A1045      52.412  31.481   8.273  1.00 94.35           C  
ANISOU 1358  C   THR A1045    12822  10310  12718  -1357   1361   -849       C  
ATOM   1359  O   THR A1045      51.611  30.600   7.966  1.00 87.61           O  
ANISOU 1359  O   THR A1045    12092   9703  11493  -1142   1285   -789       O  
ATOM   1360  CB  THR A1045      51.890  33.915   8.269  1.00106.82           C  
ANISOU 1360  CB  THR A1045    14774  11202  14609  -1546   1466   -456       C  
ATOM   1361  OG1 THR A1045      50.469  33.902   8.086  1.00107.95           O  
ANISOU 1361  OG1 THR A1045    15245  11378  14391  -1264   1326   -195       O  
ATOM   1362  CG2 THR A1045      52.438  35.257   7.810  1.00112.00           C  
ANISOU 1362  CG2 THR A1045    15471  11452  15632  -1858   1757   -233       C  
ATOM   1363  N   LEU A1046      53.237  31.384   9.311  1.00 94.67           N  
ANISOU 1363  N   LEU A1046    12566  10291  13113  -1399   1175  -1192       N  
ATOM   1364  CA  LEU A1046      53.177  30.269  10.243  1.00 87.94           C  
ANISOU 1364  CA  LEU A1046    11565   9647  12202  -1154    851  -1452       C  
ATOM   1365  C   LEU A1046      52.077  30.502  11.270  1.00 85.77           C  
ANISOU 1365  C   LEU A1046    11550   9274  11765   -916    530  -1452       C  
ATOM   1366  O   LEU A1046      52.135  31.453  12.048  1.00 86.96           O  
ANISOU 1366  O   LEU A1046    11748   9183  12109   -978    399  -1568       O  
ATOM   1367  CB  LEU A1046      54.525  30.079  10.942  1.00 95.93           C  
ANISOU 1367  CB  LEU A1046    12141  10680  13629  -1272    735  -1786       C  
ATOM   1368  CG  LEU A1046      54.549  29.143  12.153  1.00100.47           C  
ANISOU 1368  CG  LEU A1046    12574  11420  14180  -1013    324  -2011       C  
ATOM   1369  CD1 LEU A1046      54.106  27.734  11.774  1.00 97.09           C  
ANISOU 1369  CD1 LEU A1046    12156  11233  13503   -773    347  -1937       C  
ATOM   1370  CD2 LEU A1046      55.934  29.126  12.785  1.00104.58           C  
ANISOU 1370  CD2 LEU A1046    12633  11966  15135  -1142    162  -2316       C  
ATOM   1371  N   ALA A1047      51.074  29.632  11.267  1.00 88.91           N  
ANISOU 1371  N   ALA A1047    12100   9853  11828   -658    430  -1354       N  
ATOM   1372  CA  ALA A1047      49.953  29.761  12.190  1.00 87.27           C  
ANISOU 1372  CA  ALA A1047    12117   9590  11453   -423    194  -1337       C  
ATOM   1373  C   ALA A1047      49.873  28.573  13.141  1.00 82.93           C  
ANISOU 1373  C   ALA A1047    11457   9250  10801   -205    -50  -1485       C  
ATOM   1374  O   ALA A1047      50.191  27.442  12.769  1.00 87.57           O  
ANISOU 1374  O   ALA A1047    11879  10022  11372   -161    -17  -1500       O  
ATOM   1375  CB  ALA A1047      48.650  29.906  11.425  1.00 82.56           C  
ANISOU 1375  CB  ALA A1047    11795   8986  10587   -306    288  -1035       C  
ATOM   1376  N   GLY A1048      49.442  28.841  14.370  1.00 74.76           N  
ANISOU 1376  N   GLY A1048    10529   8174   9701    -65   -275  -1589       N  
ATOM   1377  CA  GLY A1048      49.282  27.800  15.366  1.00 60.36           C  
ANISOU 1377  CA  GLY A1048     8657   6547   7729    151   -497  -1651       C  
ATOM   1378  C   GLY A1048      49.567  28.300  16.767  1.00 65.20           C  
ANISOU 1378  C   GLY A1048     9294   7161   8319    192   -755  -1879       C  
ATOM   1379  O   GLY A1048      49.795  29.490  16.981  1.00 69.24           O  
ANISOU 1379  O   GLY A1048     9865   7483   8962     51   -761  -2042       O  
ATOM   1380  N   THR A1049      49.556  27.382  17.724  1.00 66.13           N  
ANISOU 1380  N   THR A1049     9377   7488   8263    384   -971  -1892       N  
ATOM   1381  CA  THR A1049      49.850  27.711  19.111  1.00 65.29           C  
ANISOU 1381  CA  THR A1049     9310   7481   8016    445  -1258  -2110       C  
ATOM   1382  C   THR A1049      51.031  26.862  19.586  1.00 70.09           C  
ANISOU 1382  C   THR A1049     9619   8293   8719    475  -1534  -2182       C  
ATOM   1383  O   THR A1049      51.083  25.663  19.303  1.00 74.48           O  
ANISOU 1383  O   THR A1049    10051   8943   9307    602  -1516  -1982       O  
ATOM   1384  CB  THR A1049      48.622  27.471  20.011  1.00 61.92           C  
ANISOU 1384  CB  THR A1049     9167   7163   7196    688  -1274  -2006       C  
ATOM   1385  OG1 THR A1049      47.487  28.145  19.455  1.00 64.04           O  
ANISOU 1385  OG1 THR A1049     9641   7238   7452    697  -1014  -1910       O  
ATOM   1386  CG2 THR A1049      48.868  27.981  21.422  1.00 57.71           C  
ANISOU 1386  CG2 THR A1049     8739   6768   6421    737  -1538  -2278       C  
ATOM   1387  N   PRO A1050      51.997  27.484  20.282  1.00 74.22           N  
ANISOU 1387  N   PRO A1050     9996   8863   9340    358  -1804  -2483       N  
ATOM   1388  CA  PRO A1050      53.148  26.744  20.812  1.00 77.82           C  
ANISOU 1388  CA  PRO A1050    10123   9537   9910    412  -2140  -2552       C  
ATOM   1389  C   PRO A1050      52.722  25.566  21.683  1.00 84.56           C  
ANISOU 1389  C   PRO A1050    11083  10636  10410    731  -2338  -2304       C  
ATOM   1390  O   PRO A1050      51.894  25.725  22.580  1.00 88.25           O  
ANISOU 1390  O   PRO A1050    11871  11216  10443    866  -2402  -2273       O  
ATOM   1391  CB  PRO A1050      53.906  27.800  21.633  1.00 86.56           C  
ANISOU 1391  CB  PRO A1050    11146  10677  11065    242  -2445  -2959       C  
ATOM   1392  CG  PRO A1050      52.977  28.978  21.745  1.00 85.39           C  
ANISOU 1392  CG  PRO A1050    11364  10325  10757    160  -2261  -3096       C  
ATOM   1393  CD  PRO A1050      52.119  28.930  20.526  1.00 84.16           C  
ANISOU 1393  CD  PRO A1050    11347   9940  10690    153  -1818  -2795       C  
ATOM   1394  N   GLY A1051      53.286  24.395  21.401  1.00 81.05           N  
ANISOU 1394  N   GLY A1051    10368  10250  10178    851  -2396  -2119       N  
ATOM   1395  CA  GLY A1051      52.903  23.171  22.078  1.00 72.03           C  
ANISOU 1395  CA  GLY A1051     9309   9258   8802   1150  -2534  -1800       C  
ATOM   1396  C   GLY A1051      51.993  22.324  21.209  1.00 74.18           C  
ANISOU 1396  C   GLY A1051     9681   9358   9147   1225  -2164  -1519       C  
ATOM   1397  O   GLY A1051      51.719  21.168  21.527  1.00 83.18           O  
ANISOU 1397  O   GLY A1051    10834  10525  10247   1442  -2203  -1228       O  
ATOM   1398  N   TYR A1052      51.529  22.903  20.104  1.00 67.91           N  
ANISOU 1398  N   TYR A1052     8952   8379   8472   1038  -1820  -1600       N  
ATOM   1399  CA  TYR A1052      50.596  22.225  19.205  1.00 66.07           C  
ANISOU 1399  CA  TYR A1052     8815   8014   8274   1073  -1500  -1400       C  
ATOM   1400  C   TYR A1052      51.092  22.207  17.767  1.00 64.08           C  
ANISOU 1400  C   TYR A1052     8352   7634   8361    895  -1245  -1512       C  
ATOM   1401  O   TYR A1052      50.581  21.460  16.933  1.00 58.74           O  
ANISOU 1401  O   TYR A1052     7682   6881   7757    918  -1025  -1413       O  
ATOM   1402  CB  TYR A1052      49.223  22.899  19.240  1.00 54.79           C  
ANISOU 1402  CB  TYR A1052     7734   6542   6542   1061  -1320  -1336       C  
ATOM   1403  CG  TYR A1052      48.487  22.788  20.554  1.00 58.91           C  
ANISOU 1403  CG  TYR A1052     8496   7204   6683   1247  -1444  -1205       C  
ATOM   1404  CD1 TYR A1052      48.605  23.773  21.525  1.00 60.56           C  
ANISOU 1404  CD1 TYR A1052     8852   7527   6629   1236  -1616  -1397       C  
ATOM   1405  CD2 TYR A1052      47.656  21.707  20.815  1.00 54.26           C  
ANISOU 1405  CD2 TYR A1052     7990   6627   5998   1417  -1356   -908       C  
ATOM   1406  CE1 TYR A1052      47.920  23.676  22.727  1.00 62.70           C  
ANISOU 1406  CE1 TYR A1052     9369   7977   6478   1408  -1681  -1298       C  
ATOM   1407  CE2 TYR A1052      46.969  21.603  22.009  1.00 56.08           C  
ANISOU 1407  CE2 TYR A1052     8448   7008   5851   1575  -1402   -752       C  
ATOM   1408  CZ  TYR A1052      47.104  22.588  22.962  1.00 63.33           C  
ANISOU 1408  CZ  TYR A1052     9531   8092   6438   1578  -1556   -948       C  
ATOM   1409  OH  TYR A1052      46.419  22.481  24.152  1.00 71.40           O  
ANISOU 1409  OH  TYR A1052    10802   9313   7015   1737  -1558   -813       O  
ATOM   1410  N   VAL A1053      52.069  23.056  17.470  1.00 60.79           N  
ANISOU 1410  N   VAL A1053     7752   7204   8141    697  -1258  -1736       N  
ATOM   1411  CA  VAL A1053      52.542  23.200  16.102  1.00 58.93           C  
ANISOU 1411  CA  VAL A1053     7348   6880   8163    498   -953  -1829       C  
ATOM   1412  C   VAL A1053      53.223  21.926  15.621  1.00 68.11           C  
ANISOU 1412  C   VAL A1053     8195   8054   9629    595   -890  -1842       C  
ATOM   1413  O   VAL A1053      54.119  21.407  16.286  1.00 74.01           O  
ANISOU 1413  O   VAL A1053     8659   8858  10602    715  -1137  -1887       O  
ATOM   1414  CB  VAL A1053      53.520  24.381  15.960  1.00 64.28           C  
ANISOU 1414  CB  VAL A1053     7857   7515   9051    239   -946  -2046       C  
ATOM   1415  CG1 VAL A1053      53.974  24.517  14.514  1.00 63.03           C  
ANISOU 1415  CG1 VAL A1053     7551   7292   9104     24   -558  -2086       C  
ATOM   1416  CG2 VAL A1053      52.866  25.667  16.438  1.00 69.62           C  
ANISOU 1416  CG2 VAL A1053     8842   8105   9505    149   -995  -2074       C  
ATOM   1417  N   PRO A1054      52.779  21.409  14.467  1.00 66.47           N  
ANISOU 1417  N   PRO A1054     8031   7795   9431    557   -574  -1820       N  
ATOM   1418  CA  PRO A1054      53.447  20.292  13.796  1.00 66.44           C  
ANISOU 1418  CA  PRO A1054     7725   7764   9754    617   -424  -1924       C  
ATOM   1419  C   PRO A1054      54.875  20.674  13.438  1.00 68.63           C  
ANISOU 1419  C   PRO A1054     7613   8076  10386    468   -339  -2143       C  
ATOM   1420  O   PRO A1054      55.083  21.767  12.919  1.00 62.43           O  
ANISOU 1420  O   PRO A1054     6869   7307   9544    216   -166  -2209       O  
ATOM   1421  CB  PRO A1054      52.602  20.079  12.536  1.00 66.51           C  
ANISOU 1421  CB  PRO A1054     7931   7758   9583    524    -88  -1932       C  
ATOM   1422  CG  PRO A1054      51.285  20.691  12.846  1.00 65.12           C  
ANISOU 1422  CG  PRO A1054     8140   7583   9018    526   -166  -1739       C  
ATOM   1423  CD  PRO A1054      51.576  21.848  13.744  1.00 67.35           C  
ANISOU 1423  CD  PRO A1054     8476   7879   9234    472   -364  -1718       C  
ATOM   1424  N   PRO A1055      55.842  19.787  13.708  1.00 68.79           N  
ANISOU 1424  N   PRO A1055     7236   8085  10814    624   -447  -2234       N  
ATOM   1425  CA  PRO A1055      57.258  20.102  13.492  1.00 71.03           C  
ANISOU 1425  CA  PRO A1055     7056   8413  11521    501   -393  -2455       C  
ATOM   1426  C   PRO A1055      57.555  20.530  12.060  1.00 77.81           C  
ANISOU 1426  C   PRO A1055     7853   9287  12422    228    124  -2619       C  
ATOM   1427  O   PRO A1055      58.440  21.359  11.848  1.00 87.58           O  
ANISOU 1427  O   PRO A1055     8844  10561  13874     -1    237  -2747       O  
ATOM   1428  CB  PRO A1055      57.970  18.785  13.830  1.00 67.42           C  
ANISOU 1428  CB  PRO A1055     6206   7903  11508    793   -542  -2486       C  
ATOM   1429  CG  PRO A1055      56.913  17.733  13.714  1.00 72.65           C  
ANISOU 1429  CG  PRO A1055     7152   8442  12008    991   -481  -2329       C  
ATOM   1430  CD  PRO A1055      55.648  18.398  14.152  1.00 67.62           C  
ANISOU 1430  CD  PRO A1055     7024   7847  10822    930   -592  -2119       C  
ATOM   1431  N   GLU A1056      56.817  19.989  11.095  1.00 79.42           N  
ANISOU 1431  N   GLU A1056     8284   9481  12412    234    435  -2616       N  
ATOM   1432  CA  GLU A1056      57.074  20.304   9.696  1.00 77.86           C  
ANISOU 1432  CA  GLU A1056     8071   9364  12150     -8    937  -2757       C  
ATOM   1433  C   GLU A1056      56.524  21.681   9.324  1.00 75.69           C  
ANISOU 1433  C   GLU A1056     8151   9126  11482   -274   1049  -2590       C  
ATOM   1434  O   GLU A1056      56.886  22.230   8.283  1.00 79.98           O  
ANISOU 1434  O   GLU A1056     8684   9746  11961   -516   1450  -2629       O  
ATOM   1435  CB  GLU A1056      56.484  19.226   8.774  1.00 62.54           C  
ANISOU 1435  CB  GLU A1056     6254   7435  10073     87   1196  -2867       C  
ATOM   1436  CG  GLU A1056      54.967  19.235   8.668  1.00 64.22           C  
ANISOU 1436  CG  GLU A1056     6962   7651   9789    114   1099  -2679       C  
ATOM   1437  CD  GLU A1056      54.301  18.348   9.702  1.00 65.65           C  
ANISOU 1437  CD  GLU A1056     7207   7684  10053    389    739  -2553       C  
ATOM   1438  OE1 GLU A1056      55.001  17.856  10.614  1.00 64.65           O  
ANISOU 1438  OE1 GLU A1056     6795   7462  10305    573    506  -2546       O  
ATOM   1439  OE2 GLU A1056      53.075  18.140   9.598  1.00 61.44           O  
ANISOU 1439  OE2 GLU A1056     6995   7137   9213    422    689  -2438       O  
ATOM   1440  N   TYR A1057      55.659  22.236  10.173  1.00 68.39           N  
ANISOU 1440  N   TYR A1057     7539   8137  10309   -217    722  -2388       N  
ATOM   1441  CA  TYR A1057      55.140  23.590   9.960  1.00 70.01           C  
ANISOU 1441  CA  TYR A1057     8060   8304  10237   -426    788  -2219       C  
ATOM   1442  C   TYR A1057      56.217  24.642  10.185  1.00 78.47           C  
ANISOU 1442  C   TYR A1057     8881   9305  11628   -667    822  -2300       C  
ATOM   1443  O   TYR A1057      56.083  25.778   9.733  1.00 87.11           O  
ANISOU 1443  O   TYR A1057    10159  10317  12622   -899   1005  -2178       O  
ATOM   1444  CB  TYR A1057      53.949  23.884  10.879  1.00 65.39           C  
ANISOU 1444  CB  TYR A1057     7830   7649   9367   -276    454  -2037       C  
ATOM   1445  CG  TYR A1057      52.625  23.350  10.382  1.00 62.20           C  
ANISOU 1445  CG  TYR A1057     7745   7289   8599   -154    502  -1896       C  
ATOM   1446  CD1 TYR A1057      52.572  22.256   9.530  1.00 61.60           C  
ANISOU 1446  CD1 TYR A1057     7596   7303   8505   -103    695  -1999       C  
ATOM   1447  CD2 TYR A1057      51.427  23.951  10.754  1.00 54.42           C  
ANISOU 1447  CD2 TYR A1057     7103   6249   7325    -96    358  -1700       C  
ATOM   1448  CE1 TYR A1057      51.367  21.764   9.072  1.00 55.45           C  
ANISOU 1448  CE1 TYR A1057     7070   6570   7427    -23    702  -1920       C  
ATOM   1449  CE2 TYR A1057      50.211  23.467  10.298  1.00 49.43           C  
ANISOU 1449  CE2 TYR A1057     6696   5670   6415      4    378  -1585       C  
ATOM   1450  CZ  TYR A1057      50.188  22.371   9.458  1.00 57.50           C  
ANISOU 1450  CZ  TYR A1057     7633   6793   7422     27    531  -1699       C  
ATOM   1451  OH  TYR A1057      48.992  21.876   8.993  1.00 56.57           O  
ANISOU 1451  OH  TYR A1057     7702   6734   7060     96    517  -1635       O  
ATOM   1452  N   TYR A1058      57.276  24.267  10.897  1.00 81.42           N  
ANISOU 1452  N   TYR A1058     8820   9692  12424   -610    626  -2495       N  
ATOM   1453  CA  TYR A1058      58.402  25.169  11.125  1.00 81.08           C  
ANISOU 1453  CA  TYR A1058     8437   9590  12778   -861    632  -2636       C  
ATOM   1454  C   TYR A1058      59.361  25.182   9.940  1.00 83.18           C  
ANISOU 1454  C   TYR A1058     8377   9908  13320  -1093   1150  -2741       C  
ATOM   1455  O   TYR A1058      60.166  26.102   9.792  1.00 89.02           O  
ANISOU 1455  O   TYR A1058     8885  10571  14367  -1392   1314  -2803       O  
ATOM   1456  CB  TYR A1058      59.170  24.774  12.388  1.00 79.53           C  
ANISOU 1456  CB  TYR A1058     7860   9435  12922   -701    154  -2810       C  
ATOM   1457  CG  TYR A1058      58.423  24.984  13.686  1.00 80.81           C  
ANISOU 1457  CG  TYR A1058     8320   9587  12797   -528   -344  -2737       C  
ATOM   1458  CD1 TYR A1058      58.262  26.257  14.222  1.00 80.16           C  
ANISOU 1458  CD1 TYR A1058     8414   9396  12647   -717   -488  -2782       C  
ATOM   1459  CD2 TYR A1058      57.905  23.909  14.391  1.00 76.47           C  
ANISOU 1459  CD2 TYR A1058     7870   9122  12063   -181   -638  -2633       C  
ATOM   1460  CE1 TYR A1058      57.591  26.451  15.414  1.00 78.30           C  
ANISOU 1460  CE1 TYR A1058     8456   9183  12112   -554   -898  -2770       C  
ATOM   1461  CE2 TYR A1058      57.236  24.092  15.583  1.00 85.60           C  
ANISOU 1461  CE2 TYR A1058     9307  10312  12906    -28  -1037  -2554       C  
ATOM   1462  CZ  TYR A1058      57.079  25.365  16.091  1.00 89.13           C  
ANISOU 1462  CZ  TYR A1058     9933  10698  13236   -211  -1160  -2645       C  
ATOM   1463  OH  TYR A1058      56.408  25.550  17.279  1.00 95.92           O  
ANISOU 1463  OH  TYR A1058    11082  11621  13741    -54  -1513  -2617       O  
ATOM   1464  N   GLN A1059      59.274  24.154   9.101  1.00 76.19           N  
ANISOU 1464  N   GLN A1059     7466   9144  12338   -969   1434  -2784       N  
ATOM   1465  CA  GLN A1059      60.247  23.951   8.036  1.00 84.13           C  
ANISOU 1465  CA  GLN A1059     8117  10247  13599  -1138   1956  -2947       C  
ATOM   1466  C   GLN A1059      59.808  24.550   6.702  1.00 91.14           C  
ANISOU 1466  C   GLN A1059     9361  11211  14057  -1385   2476  -2776       C  
ATOM   1467  O   GLN A1059      60.641  24.835   5.841  1.00104.66           O  
ANISOU 1467  O   GLN A1059    10836  13000  15929  -1629   2973  -2842       O  
ATOM   1468  CB  GLN A1059      60.526  22.459   7.872  1.00 93.09           C  
ANISOU 1468  CB  GLN A1059     8982  11465  14922   -853   2002  -3165       C  
ATOM   1469  CG  GLN A1059      60.947  21.780   9.163  1.00106.92           C  
ANISOU 1469  CG  GLN A1059    10396  13145  17083   -564   1469  -3251       C  
ATOM   1470  CD  GLN A1059      60.715  20.282   9.135  1.00118.69           C  
ANISOU 1470  CD  GLN A1059    11827  14615  18654   -216   1424  -3341       C  
ATOM   1471  OE1 GLN A1059      60.057  19.761   8.234  1.00111.23           O  
ANISOU 1471  OE1 GLN A1059    11155  13705  17404   -196   1733  -3375       O  
ATOM   1472  NE2 GLN A1059      61.252  19.581  10.127  1.00130.79           N  
ANISOU 1472  NE2 GLN A1059    13003  16082  20610     59   1017  -3379       N  
HETATM 1473  N   SEP A1060      58.503  24.736   6.531  1.00 88.87           N  
ANISOU 1473  N   SEP A1060     9626  10921  13219  -1315   2366  -2537       N  
HETATM 1474  CA  SEP A1060      57.968  25.328   5.307  1.00 96.86           C  
ANISOU 1474  CA  SEP A1060    11021  12032  13748  -1509   2765  -2306       C  
HETATM 1475  CB  SEP A1060      57.919  24.296   4.176  1.00112.33           C  
ANISOU 1475  CB  SEP A1060    13000  14255  15428  -1446   3131  -2475       C  
HETATM 1476  OG  SEP A1060      57.032  24.708   3.148  1.00122.85           O  
ANISOU 1476  OG  SEP A1060    14816  15741  16122  -1543   3334  -2222       O  
HETATM 1477  C   SEP A1060      56.584  25.928   5.527  1.00 86.97           C  
ANISOU 1477  C   SEP A1060    10303  10690  12051  -1435   2478  -1992       C  
HETATM 1478  O   SEP A1060      55.854  25.512   6.426  1.00 77.33           O  
ANISOU 1478  O   SEP A1060     9192   9400  10789  -1189   2048  -2005       O  
HETATM 1479  P   SEP A1060      57.810  25.438   1.938  1.00200.08           P  
ANISOU 1479  P   SEP A1060    24573  25677  25772  -1887   3974  -2103       P  
HETATM 1480  O1P SEP A1060      57.656  24.564   0.596  1.00121.53           O  
ANISOU 1480  O1P SEP A1060    14765  16114  15297  -1871   4387  -2290       O  
HETATM 1481  O2P SEP A1060      59.371  25.594   2.300  1.00159.67           O  
ANISOU 1481  O2P SEP A1060    18837  20449  21381  -2057   4217  -2325       O  
HETATM 1482  O3P SEP A1060      57.168  26.894   1.690  1.00132.76           O  
ANISOU 1482  O3P SEP A1060    16487  17028  16928  -2077   3973  -1579       O  
ATOM   1483  N   PHE A1061      56.229  26.904   4.694  1.00 93.88           N  
ANISOU 1483  N   PHE A1061    11494  11563  12611  -1639   2740  -1685       N  
ATOM   1484  CA  PHE A1061      54.931  27.564   4.779  1.00 92.43           C  
ANISOU 1484  CA  PHE A1061    11784  11280  12053  -1558   2501  -1358       C  
ATOM   1485  C   PHE A1061      53.836  26.709   4.161  1.00 93.47           C  
ANISOU 1485  C   PHE A1061    12198  11656  11659  -1359   2432  -1332       C  
ATOM   1486  O   PHE A1061      53.132  27.144   3.249  1.00 96.43           O  
ANISOU 1486  O   PHE A1061    12917  12149  11572  -1411   2554  -1050       O  
ATOM   1487  CB  PHE A1061      54.972  28.927   4.089  1.00 94.14           C  
ANISOU 1487  CB  PHE A1061    12225  11369  12175  -1827   2791   -983       C  
ATOM   1488  CG  PHE A1061      55.883  29.911   4.749  1.00101.23           C  
ANISOU 1488  CG  PHE A1061    12875  11949  13640  -2056   2821  -1008       C  
ATOM   1489  CD1 PHE A1061      55.504  30.547   5.919  1.00 99.41           C  
ANISOU 1489  CD1 PHE A1061    12705  11415  13651  -1979   2418  -1022       C  
ATOM   1490  CD2 PHE A1061      57.117  30.209   4.197  1.00109.38           C  
ANISOU 1490  CD2 PHE A1061    13596  12988  14976  -2364   3272  -1052       C  
ATOM   1491  CE1 PHE A1061      56.341  31.460   6.529  1.00 96.16           C  
ANISOU 1491  CE1 PHE A1061    12058  10703  13775  -2214   2417  -1118       C  
ATOM   1492  CE2 PHE A1061      57.959  31.121   4.803  1.00109.16           C  
ANISOU 1492  CE2 PHE A1061    13295  12647  15534  -2612   3285  -1110       C  
ATOM   1493  CZ  PHE A1061      57.570  31.747   5.971  1.00 99.78           C  
ANISOU 1493  CZ  PHE A1061    12180  11149  14583  -2541   2833  -1161       C  
ATOM   1494  N   ARG A1062      53.698  25.490   4.663  1.00 88.31           N  
ANISOU 1494  N   ARG A1062    11386  11067  11100  -1135   2218  -1617       N  
ATOM   1495  CA  ARG A1062      52.704  24.566   4.153  1.00 77.94           C  
ANISOU 1495  CA  ARG A1062    10274   9946   9394   -970   2136  -1672       C  
ATOM   1496  C   ARG A1062      51.918  23.961   5.302  1.00 73.31           C  
ANISOU 1496  C   ARG A1062     9695   9222   8939   -707   1692  -1720       C  
ATOM   1497  O   ARG A1062      52.486  23.597   6.331  1.00 82.35           O  
ANISOU 1497  O   ARG A1062    10577  10227  10486   -608   1520  -1865       O  
ATOM   1498  CB  ARG A1062      53.371  23.471   3.315  1.00 79.42           C  
ANISOU 1498  CB  ARG A1062    10250  10356   9571   -992   2462  -2018       C  
ATOM   1499  CG  ARG A1062      53.954  23.971   2.001  1.00 90.38           C  
ANISOU 1499  CG  ARG A1062    11702  11973  10663  -1249   2971  -1959       C  
ATOM   1500  CD  ARG A1062      54.737  22.889   1.275  1.00107.97           C  
ANISOU 1500  CD  ARG A1062    13669  14411  12942  -1261   3346  -2386       C  
ATOM   1501  NE  ARG A1062      55.968  22.537   1.977  1.00120.26           N  
ANISOU 1501  NE  ARG A1062    14716  15798  15178  -1235   3418  -2641       N  
ATOM   1502  CZ  ARG A1062      56.880  21.692   1.508  1.00124.40           C  
ANISOU 1502  CZ  ARG A1062    14897  16430  15939  -1229   3775  -3029       C  
ATOM   1503  NH1 ARG A1062      56.703  21.110   0.329  1.00124.88           N  
ANISOU 1503  NH1 ARG A1062    15105  16777  15566  -1266   4122  -3249       N  
ATOM   1504  NH2 ARG A1062      57.972  21.432   2.216  1.00124.81           N  
ANISOU 1504  NH2 ARG A1062    14443  16316  16664  -1176   3776  -3220       N  
ATOM   1505  N   CYS A1063      50.605  23.872   5.126  1.00 61.85           N  
ANISOU 1505  N   CYS A1063     8534   7828   7140   -597   1506  -1573       N  
ATOM   1506  CA  CYS A1063      49.740  23.244   6.113  1.00 51.08           C  
ANISOU 1506  CA  CYS A1063     7184   6354   5869   -367   1155  -1593       C  
ATOM   1507  C   CYS A1063      48.985  22.091   5.461  1.00 54.18           C  
ANISOU 1507  C   CYS A1063     7623   6905   6059   -287   1144  -1753       C  
ATOM   1508  O   CYS A1063      48.935  21.990   4.232  1.00 58.44           O  
ANISOU 1508  O   CYS A1063     8261   7672   6271   -403   1351  -1822       O  
ATOM   1509  CB  CYS A1063      48.765  24.261   6.705  1.00 56.84           C  
ANISOU 1509  CB  CYS A1063     8159   6953   6486   -303    923  -1293       C  
ATOM   1510  SG  CYS A1063      47.620  24.960   5.501  1.00 75.23           S  
ANISOU 1510  SG  CYS A1063    10829   9437   8317   -351    955   -997       S  
ATOM   1511  N   SER A1064      48.400  21.224   6.281  1.00 51.18           N  
ANISOU 1511  N   SER A1064     7177   6407   5860   -104    910  -1819       N  
ATOM   1512  CA  SER A1064      47.704  20.046   5.769  1.00 52.39           C  
ANISOU 1512  CA  SER A1064     7326   6637   5942    -50    889  -2018       C  
ATOM   1513  C   SER A1064      46.769  19.437   6.812  1.00 51.60           C  
ANISOU 1513  C   SER A1064     7214   6361   6030    129    617  -1936       C  
ATOM   1514  O   SER A1064      46.803  19.800   7.989  1.00 56.35           O  
ANISOU 1514  O   SER A1064     7801   6812   6796    233    465  -1757       O  
ATOM   1515  CB  SER A1064      48.716  18.994   5.309  1.00 55.91           C  
ANISOU 1515  CB  SER A1064     7526   7092   6626    -70   1126  -2390       C  
ATOM   1516  OG  SER A1064      49.455  18.511   6.414  1.00 49.65           O  
ANISOU 1516  OG  SER A1064     6479   6069   6316     70   1041  -2422       O  
ATOM   1517  N   THR A1065      45.939  18.498   6.376  1.00 54.34           N  
ANISOU 1517  N   THR A1065     7563   6738   6345    147    573  -2087       N  
ATOM   1518  CA  THR A1065      45.058  17.794   7.294  1.00 52.76           C  
ANISOU 1518  CA  THR A1065     7318   6352   6375    284    383  -2007       C  
ATOM   1519  C   THR A1065      45.890  16.963   8.276  1.00 59.71           C  
ANISOU 1519  C   THR A1065     7994   6991   7703    416    387  -2049       C  
ATOM   1520  O   THR A1065      45.514  16.824   9.442  1.00 58.48           O  
ANISOU 1520  O   THR A1065     7837   6684   7699    550    237  -1831       O  
ATOM   1521  CB  THR A1065      44.054  16.903   6.540  1.00 54.30           C  
ANISOU 1521  CB  THR A1065     7507   6602   6521    231    345  -2210       C  
ATOM   1522  OG1 THR A1065      44.758  15.928   5.755  1.00 63.73           O  
ANISOU 1522  OG1 THR A1065     8573   7795   7847    166    531  -2611       O  
ATOM   1523  CG2 THR A1065      43.184  17.751   5.623  1.00 47.47           C  
ANISOU 1523  CG2 THR A1065     6831   6018   5189    136    258  -2118       C  
ATOM   1524  N   LYS A1066      47.028  16.438   7.816  1.00 52.48           N  
ANISOU 1524  N   LYS A1066     6900   6054   6986    392    566  -2311       N  
ATOM   1525  CA  LYS A1066      47.933  15.715   8.706  1.00 58.60           C  
ANISOU 1525  CA  LYS A1066     7443   6603   8217    550    538  -2320       C  
ATOM   1526  C   LYS A1066      48.484  16.641   9.795  1.00 55.34           C  
ANISOU 1526  C   LYS A1066     7032   6198   7796    617    380  -2056       C  
ATOM   1527  O   LYS A1066      48.782  16.193  10.906  1.00 58.06           O  
ANISOU 1527  O   LYS A1066     7270   6393   8396    787    216  -1915       O  
ATOM   1528  CB  LYS A1066      49.079  15.072   7.918  1.00 64.68           C  
ANISOU 1528  CB  LYS A1066     7976   7359   9242    525    786  -2682       C  
ATOM   1529  CG  LYS A1066      48.657  13.895   7.040  1.00 71.39           C  
ANISOU 1529  CG  LYS A1066     8784   8129  10212    495    931  -3036       C  
ATOM   1530  CD  LYS A1066      47.881  12.844   7.842  1.00 74.96           C  
ANISOU 1530  CD  LYS A1066     9203   8261  11016    635    763  -2923       C  
ATOM   1531  CE  LYS A1066      47.580  11.596   7.011  1.00 78.25           C  
ANISOU 1531  CE  LYS A1066     9532   8514  11685    592    912  -3345       C  
ATOM   1532  NZ  LYS A1066      48.787  10.753   6.717  1.00 71.35           N  
ANISOU 1532  NZ  LYS A1066     8381   7448  11282    691   1133  -3684       N  
ATOM   1533  N   GLY A1067      48.608  17.929   9.482  1.00 60.82           N  
ANISOU 1533  N   GLY A1067     7855   7061   8193    479    418  -1988       N  
ATOM   1534  CA  GLY A1067      48.995  18.913  10.479  1.00 49.61           C  
ANISOU 1534  CA  GLY A1067     6461   5634   6754    506    257  -1802       C  
ATOM   1535  C   GLY A1067      47.951  19.019  11.577  1.00 52.30           C  
ANISOU 1535  C   GLY A1067     6980   5914   6978    640     35  -1554       C  
ATOM   1536  O   GLY A1067      48.290  19.094  12.764  1.00 54.04           O  
ANISOU 1536  O   GLY A1067     7165   6090   7280    760   -149  -1445       O  
ATOM   1537  N   ASP A1068      46.678  19.019  11.181  1.00 52.06           N  
ANISOU 1537  N   ASP A1068     7126   5912   6741    621     54  -1477       N  
ATOM   1538  CA  ASP A1068      45.566  19.022  12.132  1.00 55.69           C  
ANISOU 1538  CA  ASP A1068     7717   6321   7120    744    -83  -1259       C  
ATOM   1539  C   ASP A1068      45.572  17.784  13.023  1.00 58.42           C  
ANISOU 1539  C   ASP A1068     7952   6523   7721    901   -153  -1180       C  
ATOM   1540  O   ASP A1068      45.255  17.860  14.216  1.00 53.44           O  
ANISOU 1540  O   ASP A1068     7399   5871   7033   1027   -267   -972       O  
ATOM   1541  CB  ASP A1068      44.228  19.102  11.397  1.00 57.90           C  
ANISOU 1541  CB  ASP A1068     8114   6662   7224    689    -47  -1224       C  
ATOM   1542  CG  ASP A1068      43.853  20.522  11.011  1.00 58.65           C  
ANISOU 1542  CG  ASP A1068     8382   6856   7044    622    -52  -1126       C  
ATOM   1543  OD1 ASP A1068      44.526  21.471  11.481  1.00 58.68           O  
ANISOU 1543  OD1 ASP A1068     8440   6837   7020    611    -69  -1085       O  
ATOM   1544  OD2 ASP A1068      42.875  20.681  10.246  1.00 56.14           O  
ANISOU 1544  OD2 ASP A1068     8135   6625   6572    584    -57  -1088       O  
ATOM   1545  N   VAL A1069      45.916  16.642  12.435  1.00 54.87           N  
ANISOU 1545  N   VAL A1069     7333   5966   7548    897    -63  -1343       N  
ATOM   1546  CA  VAL A1069      45.930  15.386  13.171  1.00 60.82           C  
ANISOU 1546  CA  VAL A1069     7974   6507   8628   1050   -107  -1233       C  
ATOM   1547  C   VAL A1069      46.960  15.431  14.293  1.00 59.97           C  
ANISOU 1547  C   VAL A1069     7786   6385   8613   1209   -274  -1082       C  
ATOM   1548  O   VAL A1069      46.692  14.984  15.413  1.00 58.58           O  
ANISOU 1548  O   VAL A1069     7659   6135   8464   1365   -391   -802       O  
ATOM   1549  CB  VAL A1069      46.222  14.193  12.245  1.00 55.77           C  
ANISOU 1549  CB  VAL A1069     7147   5698   8345   1017     39  -1504       C  
ATOM   1550  CG1 VAL A1069      46.426  12.937  13.060  1.00 60.99           C  
ANISOU 1550  CG1 VAL A1069     7676   6062   9438   1201     -8  -1346       C  
ATOM   1551  CG2 VAL A1069      45.088  14.006  11.243  1.00 46.97           C  
ANISOU 1551  CG2 VAL A1069     6108   4620   7120    860    138  -1673       C  
ATOM   1552  N   TYR A1070      48.135  15.975  13.986  1.00 54.15           N  
ANISOU 1552  N   TYR A1070     6918   5743   7914   1162   -287  -1258       N  
ATOM   1553  CA  TYR A1070      49.170  16.163  14.991  1.00 54.52           C  
ANISOU 1553  CA  TYR A1070     6845   5830   8040   1289   -506  -1165       C  
ATOM   1554  C   TYR A1070      48.631  16.967  16.164  1.00 60.03           C  
ANISOU 1554  C   TYR A1070     7779   6658   8371   1341   -692   -938       C  
ATOM   1555  O   TYR A1070      48.722  16.537  17.314  1.00 66.26           O  
ANISOU 1555  O   TYR A1070     8587   7449   9142   1522   -886   -707       O  
ATOM   1556  CB  TYR A1070      50.394  16.861  14.393  1.00 56.49           C  
ANISOU 1556  CB  TYR A1070     6895   6183   8385   1164   -460  -1421       C  
ATOM   1557  CG  TYR A1070      51.512  17.071  15.388  1.00 61.50           C  
ANISOU 1557  CG  TYR A1070     7337   6881   9150   1275   -736  -1378       C  
ATOM   1558  CD1 TYR A1070      51.577  18.227  16.156  1.00 64.73           C  
ANISOU 1558  CD1 TYR A1070     7876   7446   9273   1219   -930  -1340       C  
ATOM   1559  CD2 TYR A1070      52.500  16.110  15.568  1.00 68.17           C  
ANISOU 1559  CD2 TYR A1070     7849   7623  10430   1446   -826  -1400       C  
ATOM   1560  CE1 TYR A1070      52.594  18.423  17.069  1.00 72.46           C  
ANISOU 1560  CE1 TYR A1070     8663   8522  10348   1302  -1237  -1349       C  
ATOM   1561  CE2 TYR A1070      53.524  16.301  16.481  1.00 69.30           C  
ANISOU 1561  CE2 TYR A1070     7777   7863  10693   1561  -1145  -1356       C  
ATOM   1562  CZ  TYR A1070      53.564  17.460  17.227  1.00 70.08           C  
ANISOU 1562  CZ  TYR A1070     8014   8162  10453   1475  -1365  -1342       C  
ATOM   1563  OH  TYR A1070      54.571  17.663  18.136  1.00 76.65           O  
ANISOU 1563  OH  TYR A1070     8620   9128  11377   1569  -1734  -1347       O  
ATOM   1564  N   SER A1071      48.072  18.135  15.861  1.00 58.13           N  
ANISOU 1564  N   SER A1071     7728   6529   7831   1194   -623  -1002       N  
ATOM   1565  CA  SER A1071      47.510  19.006  16.885  1.00 57.32           C  
ANISOU 1565  CA  SER A1071     7853   6533   7391   1236   -746   -872       C  
ATOM   1566  C   SER A1071      46.437  18.294  17.705  1.00 55.47           C  
ANISOU 1566  C   SER A1071     7764   6269   7045   1387   -741   -597       C  
ATOM   1567  O   SER A1071      46.384  18.432  18.930  1.00 54.44           O  
ANISOU 1567  O   SER A1071     7752   6241   6690   1513   -886   -440       O  
ATOM   1568  CB  SER A1071      46.939  20.269  16.245  1.00 57.83           C  
ANISOU 1568  CB  SER A1071     8080   6636   7256   1075   -623   -973       C  
ATOM   1569  OG  SER A1071      47.963  20.997  15.595  1.00 54.65           O  
ANISOU 1569  OG  SER A1071     7561   6248   6957    916   -598  -1172       O  
ATOM   1570  N   TYR A1072      45.590  17.530  17.024  1.00 56.60           N  
ANISOU 1570  N   TYR A1072     7890   6285   7333   1357   -563   -553       N  
ATOM   1571  CA  TYR A1072      44.608  16.691  17.702  1.00 57.72           C  
ANISOU 1571  CA  TYR A1072     8103   6343   7483   1465   -505   -280       C  
ATOM   1572  C   TYR A1072      45.273  15.762  18.712  1.00 63.14           C  
ANISOU 1572  C   TYR A1072     8731   6968   8291   1651   -647    -39       C  
ATOM   1573  O   TYR A1072      44.777  15.589  19.827  1.00 63.15           O  
ANISOU 1573  O   TYR A1072     8882   7028   8085   1772   -671    255       O  
ATOM   1574  CB  TYR A1072      43.809  15.856  16.702  1.00 49.62           C  
ANISOU 1574  CB  TYR A1072     6985   5147   6722   1369   -323   -340       C  
ATOM   1575  CG  TYR A1072      42.861  14.893  17.383  1.00 59.30           C  
ANISOU 1575  CG  TYR A1072     8231   6228   8072   1444   -231    -52       C  
ATOM   1576  CD1 TYR A1072      41.644  15.334  17.886  1.00 59.49           C  
ANISOU 1576  CD1 TYR A1072     8385   6340   7876   1441   -130    105       C  
ATOM   1577  CD2 TYR A1072      43.189  13.551  17.542  1.00 56.91           C  
ANISOU 1577  CD2 TYR A1072     7798   5670   8155   1520   -213     78       C  
ATOM   1578  CE1 TYR A1072      40.775  14.468  18.518  1.00 62.47           C  
ANISOU 1578  CE1 TYR A1072     8758   6587   8391   1481     11    391       C  
ATOM   1579  CE2 TYR A1072      42.326  12.676  18.175  1.00 59.48           C  
ANISOU 1579  CE2 TYR A1072     8144   5819   8637   1563    -92    391       C  
ATOM   1580  CZ  TYR A1072      41.119  13.140  18.659  1.00 69.91           C  
ANISOU 1580  CZ  TYR A1072     9591   7262   9711   1528     33    550       C  
ATOM   1581  OH  TYR A1072      40.248  12.279  19.289  1.00 72.60           O  
ANISOU 1581  OH  TYR A1072     9926   7428  10229   1542    209    880       O  
ATOM   1582  N   GLY A1073      46.392  15.163  18.309  1.00 66.10           N  
ANISOU 1582  N   GLY A1073     8883   7234   8998   1687   -728   -147       N  
ATOM   1583  CA  GLY A1073      47.133  14.255  19.168  1.00 67.32           C  
ANISOU 1583  CA  GLY A1073     8935   7304   9341   1899   -906    103       C  
ATOM   1584  C   GLY A1073      47.464  14.868  20.515  1.00 67.61           C  
ANISOU 1584  C   GLY A1073     9120   7605   8965   2028  -1169    294       C  
ATOM   1585  O   GLY A1073      47.285  14.232  21.553  1.00 66.35           O  
ANISOU 1585  O   GLY A1073     9061   7450   8701   2206  -1261    674       O  
ATOM   1586  N   VAL A1074      47.933  16.113  20.491  1.00 60.26           N  
ANISOU 1586  N   VAL A1074     8216   6895   7787   1925  -1284     28       N  
ATOM   1587  CA  VAL A1074      48.273  16.842  21.707  1.00 64.73           C  
ANISOU 1587  CA  VAL A1074     8923   7739   7932   2008  -1555     81       C  
ATOM   1588  C   VAL A1074      47.075  16.951  22.645  1.00 71.96           C  
ANISOU 1588  C   VAL A1074    10165   8773   8402   2075  -1452    336       C  
ATOM   1589  O   VAL A1074      47.200  16.742  23.853  1.00 73.50           O  
ANISOU 1589  O   VAL A1074    10494   9155   8277   2242  -1641    588       O  
ATOM   1590  CB  VAL A1074      48.785  18.261  21.386  1.00 67.21           C  
ANISOU 1590  CB  VAL A1074     9219   8191   8126   1825  -1625   -311       C  
ATOM   1591  CG1 VAL A1074      49.206  18.974  22.664  1.00 67.37           C  
ANISOU 1591  CG1 VAL A1074     9366   8494   7739   1895  -1942   -344       C  
ATOM   1592  CG2 VAL A1074      49.934  18.195  20.397  1.00 58.62           C  
ANISOU 1592  CG2 VAL A1074     7790   6999   7483   1726  -1642   -559       C  
ATOM   1593  N   VAL A1075      45.918  17.278  22.077  1.00 69.08           N  
ANISOU 1593  N   VAL A1075     9914   8327   8008   1951  -1149    273       N  
ATOM   1594  CA  VAL A1075      44.686  17.379  22.849  1.00 69.86           C  
ANISOU 1594  CA  VAL A1075    10261   8518   7763   2003   -968    486       C  
ATOM   1595  C   VAL A1075      44.350  16.036  23.482  1.00 70.29           C  
ANISOU 1595  C   VAL A1075    10337   8476   7894   2149   -903    944       C  
ATOM   1596  O   VAL A1075      43.988  15.963  24.656  1.00 80.63           O  
ANISOU 1596  O   VAL A1075    11858   9973   8806   2273   -897   1225       O  
ATOM   1597  CB  VAL A1075      43.507  17.837  21.976  1.00 65.76           C  
ANISOU 1597  CB  VAL A1075     9762   7891   7331   1857   -672    348       C  
ATOM   1598  CG1 VAL A1075      42.244  17.952  22.813  1.00 65.40           C  
ANISOU 1598  CG1 VAL A1075     9914   7948   6988   1921   -452    550       C  
ATOM   1599  CG2 VAL A1075      43.832  19.163  21.306  1.00 69.10           C  
ANISOU 1599  CG2 VAL A1075    10184   8359   7713   1722   -722    -26       C  
ATOM   1600  N   LEU A1076      44.483  14.975  22.693  1.00 64.92           N  
ANISOU 1600  N   LEU A1076     9446   7492   7731   2130   -832   1015       N  
ATOM   1601  CA  LEU A1076      44.275  13.620  23.189  1.00 77.89           C  
ANISOU 1601  CA  LEU A1076    11073   8931   9591   2260   -764   1462       C  
ATOM   1602  C   LEU A1076      45.242  13.284  24.328  1.00 84.84           C  
ANISOU 1602  C   LEU A1076    12008   9964  10262   2493  -1083   1773       C  
ATOM   1603  O   LEU A1076      44.907  12.514  25.227  1.00 93.80           O  
ANISOU 1603  O   LEU A1076    13277  11075  11290   2635  -1039   2263       O  
ATOM   1604  CB  LEU A1076      44.424  12.608  22.055  1.00 77.07           C  
ANISOU 1604  CB  LEU A1076    10705   8430  10149   2193   -660   1365       C  
ATOM   1605  CG  LEU A1076      44.092  11.165  22.433  1.00 83.39           C  
ANISOU 1605  CG  LEU A1076    11470   8895  11322   2295   -537   1808       C  
ATOM   1606  CD1 LEU A1076      42.717  11.101  23.077  1.00 80.26           C  
ANISOU 1606  CD1 LEU A1076    11265   8535  10696   2242   -255   2119       C  
ATOM   1607  CD2 LEU A1076      44.162  10.257  21.216  1.00 85.34           C  
ANISOU 1607  CD2 LEU A1076    11455   8724  12247   2198   -408   1578       C  
ATOM   1608  N   LEU A1077      46.439  13.865  24.289  1.00 77.26           N  
ANISOU 1608  N   LEU A1077    10933   9171   9250   2527  -1412   1511       N  
ATOM   1609  CA  LEU A1077      47.393  13.692  25.381  1.00 84.79           C  
ANISOU 1609  CA  LEU A1077    11911  10347   9958   2750  -1804   1758       C  
ATOM   1610  C   LEU A1077      46.933  14.445  26.618  1.00 90.92           C  
ANISOU 1610  C   LEU A1077    13036  11542   9968   2796  -1869   1867       C  
ATOM   1611  O   LEU A1077      47.102  13.971  27.740  1.00101.11           O  
ANISOU 1611  O   LEU A1077    14483  13021  10914   2999  -2054   2290       O  
ATOM   1612  CB  LEU A1077      48.792  14.166  24.982  1.00 81.26           C  
ANISOU 1612  CB  LEU A1077    11181   9981   9714   2743  -2144   1391       C  
ATOM   1613  CG  LEU A1077      49.703  13.171  24.266  1.00 81.95           C  
ANISOU 1613  CG  LEU A1077    10891   9745  10501   2840  -2216   1405       C  
ATOM   1614  CD1 LEU A1077      51.157  13.597  24.412  1.00 79.44           C  
ANISOU 1614  CD1 LEU A1077    10294   9622  10267   2909  -2636   1182       C  
ATOM   1615  CD2 LEU A1077      49.495  11.768  24.808  1.00 93.09           C  
ANISOU 1615  CD2 LEU A1077    12327  10905  12138   3076  -2204   1979       C  
ATOM   1616  N   GLU A1078      46.360  15.626  26.410  1.00 77.64           N  
ANISOU 1616  N   GLU A1078    11484  10006   8010   2620  -1712   1484       N  
ATOM   1617  CA  GLU A1078      45.867  16.423  27.522  1.00 87.28           C  
ANISOU 1617  CA  GLU A1078    13035  11606   8523   2655  -1713   1478       C  
ATOM   1618  C   GLU A1078      44.758  15.674  28.248  1.00 94.23           C  
ANISOU 1618  C   GLU A1078    14145  12498   9161   2750  -1396   1984       C  
ATOM   1619  O   GLU A1078      44.669  15.716  29.471  1.00103.54           O  
ANISOU 1619  O   GLU A1078    15594  14019   9728   2886  -1470   2228       O  
ATOM   1620  CB  GLU A1078      45.368  17.786  27.039  1.00 83.54           C  
ANISOU 1620  CB  GLU A1078    12623  11173   7944   2462  -1543    971       C  
ATOM   1621  CG  GLU A1078      46.450  18.656  26.418  1.00 88.40           C  
ANISOU 1621  CG  GLU A1078    13041  11782   8764   2336  -1816    495       C  
ATOM   1622  CD  GLU A1078      45.943  20.035  26.038  1.00 84.09           C  
ANISOU 1622  CD  GLU A1078    12593  11233   8123   2163  -1646     62       C  
ATOM   1623  OE1 GLU A1078      45.802  20.887  26.940  1.00 85.27           O  
ANISOU 1623  OE1 GLU A1078    12970  11637   7793   2185  -1713   -126       O  
ATOM   1624  OE2 GLU A1078      45.686  20.267  24.838  1.00 73.88           O  
ANISOU 1624  OE2 GLU A1078    11159   9681   7231   2015  -1448    -92       O  
ATOM   1625  N   LEU A1079      43.924  14.979  27.484  1.00 85.99           N  
ANISOU 1625  N   LEU A1079    12986  11093   8595   2662  -1035   2133       N  
ATOM   1626  CA  LEU A1079      42.844  14.194  28.064  1.00 88.42           C  
ANISOU 1626  CA  LEU A1079    13445  11339   8814   2707   -679   2625       C  
ATOM   1627  C   LEU A1079      43.393  12.980  28.814  1.00 96.64           C  
ANISOU 1627  C   LEU A1079    14524  12324   9869   2915   -845   3229       C  
ATOM   1628  O   LEU A1079      42.863  12.587  29.856  1.00100.91           O  
ANISOU 1628  O   LEU A1079    15316  13030   9995   3018   -683   3711       O  
ATOM   1629  CB  LEU A1079      41.857  13.758  26.976  1.00 83.76           C  
ANISOU 1629  CB  LEU A1079    12657  10352   8817   2527   -300   2568       C  
ATOM   1630  CG  LEU A1079      40.982  14.867  26.374  1.00 74.54           C  
ANISOU 1630  CG  LEU A1079    11478   9248   7595   2359    -78   2127       C  
ATOM   1631  CD1 LEU A1079      40.249  14.379  25.133  1.00 68.07           C  
ANISOU 1631  CD1 LEU A1079    10402   8061   7399   2186    152   2024       C  
ATOM   1632  CD2 LEU A1079      39.990  15.383  27.403  1.00 66.62           C  
ANISOU 1632  CD2 LEU A1079    10726   8535   6050   2402    209   2252       C  
ATOM   1633  N   LEU A1080      44.466  12.398  28.290  1.00 96.55           N  
ANISOU 1633  N   LEU A1080    14262  12081  10341   2989  -1153   3221       N  
ATOM   1634  CA  LEU A1080      45.068  11.216  28.899  1.00100.88           C  
ANISOU 1634  CA  LEU A1080    14797  12500  11032   3224  -1350   3808       C  
ATOM   1635  C   LEU A1080      45.975  11.571  30.075  1.00107.17           C  
ANISOU 1635  C   LEU A1080    15768  13786  11167   3445  -1826   3971       C  
ATOM   1636  O   LEU A1080      45.891  10.960  31.140  1.00117.42           O  
ANISOU 1636  O   LEU A1080    17249  15216  12150   3546  -1863   4503       O  
ATOM   1637  CB  LEU A1080      45.859  10.425  27.854  1.00 99.14           C  
ANISOU 1637  CB  LEU A1080    14196  11809  11662   3247  -1474   3699       C  
ATOM   1638  CG  LEU A1080      45.043   9.691  26.787  1.00 94.95           C  
ANISOU 1638  CG  LEU A1080    13493  10750  11832   3068  -1053   3635       C  
ATOM   1639  CD1 LEU A1080      45.940   9.213  25.658  1.00 89.91           C  
ANISOU 1639  CD1 LEU A1080    12486   9747  11926   3070  -1182   3311       C  
ATOM   1640  CD2 LEU A1080      44.287   8.522  27.399  1.00 99.60           C  
ANISOU 1640  CD2 LEU A1080    14204  11052  12589   3139   -777   4308       C  
ATOM   1641  N   THR A1081      46.840  12.562  29.877  1.00102.41           N  
ANISOU 1641  N   THR A1081    15052  13439  10420   3404  -2183   3431       N  
ATOM   1642  CA  THR A1081      47.823  12.938  30.889  1.00104.53           C  
ANISOU 1642  CA  THR A1081    15409  14180  10128   3587  -2723   3471       C  
ATOM   1643  C   THR A1081      47.253  13.890  31.939  1.00107.54           C  
ANISOU 1643  C   THR A1081    16158  15078   9624   3491  -2655   3327       C  
ATOM   1644  O   THR A1081      47.585  13.794  33.121  1.00110.06           O  
ANISOU 1644  O   THR A1081    16610  15751   9457   3515  -2889   3548       O  
ATOM   1645  CB  THR A1081      49.059  13.599  30.247  1.00104.17           C  
ANISOU 1645  CB  THR A1081    15012  14165  10401   3525  -3128   2899       C  
ATOM   1646  OG1 THR A1081      48.664  14.796  29.566  1.00104.86           O  
ANISOU 1646  OG1 THR A1081    15105  14272  10466   3245  -2906   2266       O  
ATOM   1647  CG2 THR A1081      49.712  12.654  29.252  1.00101.11           C  
ANISOU 1647  CG2 THR A1081    14206  13286  10924   3582  -3151   2962       C  
ATOM   1648  N   GLY A1082      46.396  14.809  31.503  1.00105.89           N  
ANISOU 1648  N   GLY A1082    16076  14882   9277   3330  -2309   2911       N  
ATOM   1649  CA  GLY A1082      45.855  15.823  32.389  1.00108.86           C  
ANISOU 1649  CA  GLY A1082    16777  15703   8881   3262  -2208   2658       C  
ATOM   1650  C   GLY A1082      46.783  17.019  32.496  1.00113.69           C  
ANISOU 1650  C   GLY A1082    17333  16603   9262   3189  -2642   2023       C  
ATOM   1651  O   GLY A1082      46.531  17.949  33.265  1.00115.49           O  
ANISOU 1651  O   GLY A1082    17772  17171   8937   3087  -2607   1691       O  
ATOM   1652  N   LYS A1083      47.860  16.993  31.715  1.00112.94           N  
ANISOU 1652  N   LYS A1083    16892  16320   9701   3186  -3002   1813       N  
ATOM   1653  CA  LYS A1083      48.868  18.048  31.743  1.00111.79           C  
ANISOU 1653  CA  LYS A1083    16610  16392   9473   3089  -3438   1224       C  
ATOM   1654  C   LYS A1083      48.718  19.027  30.581  1.00108.55           C  
ANISOU 1654  C   LYS A1083    16026  15679   9541   2812  -3193    643       C  
ATOM   1655  O   LYS A1083      48.158  18.689  29.537  1.00103.45           O  
ANISOU 1655  O   LYS A1083    15251  14632   9423   2722  -2810    715       O  
ATOM   1656  CB  LYS A1083      50.275  17.441  31.718  1.00110.86           C  
ANISOU 1656  CB  LYS A1083    16134  16284   9702   3219  -3989   1353       C  
ATOM   1657  CG  LYS A1083      50.868  17.129  33.088  1.00118.89           C  
ANISOU 1657  CG  LYS A1083    17199  17710  10265   3275  -4345   1632       C  
ATOM   1658  CD  LYS A1083      50.205  15.924  33.736  1.00123.44           C  
ANISOU 1658  CD  LYS A1083    17980  18249  10672   3416  -4114   2389       C  
ATOM   1659  CE  LYS A1083      50.869  15.575  35.059  1.00128.60           C  
ANISOU 1659  CE  LYS A1083    18686  19305  10870   3473  -4535   2714       C  
ATOM   1660  NZ  LYS A1083      50.260  14.368  35.683  1.00132.91           N  
ANISOU 1660  NZ  LYS A1083    19443  19761  11297   3585  -4325   3490       N  
ATOM   1661  N   ARG A1084      49.225  20.242  30.776  1.00110.16           N  
ANISOU 1661  N   ARG A1084    16231  16074   9552   2674  -3430     73       N  
ATOM   1662  CA  ARG A1084      49.314  21.229  29.704  1.00101.67           C  
ANISOU 1662  CA  ARG A1084    14970  14701   8958   2413  -3268   -442       C  
ATOM   1663  C   ARG A1084      50.409  20.821  28.724  1.00108.81           C  
ANISOU 1663  C   ARG A1084    15415  15354  10573   2350  -3456   -471       C  
ATOM   1664  O   ARG A1084      51.395  20.202  29.120  1.00117.92           O  
ANISOU 1664  O   ARG A1084    16361  16660  11782   2491  -3879   -308       O  
ATOM   1665  CB  ARG A1084      49.598  22.621  30.272  1.00 97.13           C  
ANISOU 1665  CB  ARG A1084    14521  14354   8030   2274  -3470  -1040       C  
ATOM   1666  N   PRO A1085      50.238  21.159  27.437  1.00108.39           N  
ANISOU 1666  N   PRO A1085    15193  14934  11057   2153  -3136   -667       N  
ATOM   1667  CA  PRO A1085      51.226  20.817  26.404  1.00106.86           C  
ANISOU 1667  CA  PRO A1085    14568  14508  11526   2072  -3210   -737       C  
ATOM   1668  C   PRO A1085      52.592  21.456  26.645  1.00114.52           C  
ANISOU 1668  C   PRO A1085    15251  15641  12621   1976  -3658  -1108       C  
ATOM   1669  O   PRO A1085      53.604  20.967  26.138  1.00119.67           O  
ANISOU 1669  O   PRO A1085    15496  16205  13769   1985  -3818  -1104       O  
ATOM   1670  CB  PRO A1085      50.596  21.368  25.122  1.00 96.98           C  
ANISOU 1670  CB  PRO A1085    13313  12930  10605   1852  -2757   -922       C  
ATOM   1671  CG  PRO A1085      49.144  21.411  25.411  1.00 96.60           C  
ANISOU 1671  CG  PRO A1085    13630  12879  10195   1909  -2433   -749       C  
ATOM   1672  CD  PRO A1085      49.037  21.780  26.857  1.00103.66           C  
ANISOU 1672  CD  PRO A1085    14796  14129  10459   2025  -2661   -779       C  
ATOM   1673  N   THR A1086      52.614  22.537  27.417  1.00113.27           N  
ANISOU 1673  N   THR A1086    15275  15709  12051   1879  -3848  -1463       N  
ATOM   1674  CA  THR A1086      53.847  23.270  27.675  1.00112.00           C  
ANISOU 1674  CA  THR A1086    14831  15694  12028   1733  -4283  -1895       C  
ATOM   1675  C   THR A1086      54.308  23.113  29.123  1.00112.76           C  
ANISOU 1675  C   THR A1086    15017  16274  11552   1917  -4850  -1880       C  
ATOM   1676  O   THR A1086      55.080  22.210  29.449  1.00111.70           O  
ANISOU 1676  O   THR A1086    14634  16305  11503   2118  -5230  -1600       O  
ATOM   1677  CB  THR A1086      53.673  24.764  27.357  1.00105.82           C  
ANISOU 1677  CB  THR A1086    14140  14751  11318   1425  -4105  -2422       C  
ATOM   1678  OG1 THR A1086      52.691  25.327  28.235  1.00110.90           O  
ANISOU 1678  OG1 THR A1086    15249  15556  11333   1479  -4021  -2530       O  
ATOM   1679  CG2 THR A1086      53.214  24.946  25.922  1.00 90.75           C  
ANISOU 1679  CG2 THR A1086    12170  12408   9902   1260  -3578  -2377       C  
ATOM   1680  N   ASN A1095      58.603  20.023  26.025  1.00139.77           N  
ANISOU 1680  N   ASN A1095    17060  19149  16896    789  -3287    201       N  
ATOM   1681  CA  ASN A1095      57.154  19.985  25.863  1.00135.47           C  
ANISOU 1681  CA  ASN A1095    17143  18362  15967    766  -3024     82       C  
ATOM   1682  C   ASN A1095      56.560  18.649  26.300  1.00129.91           C  
ANISOU 1682  C   ASN A1095    16338  17504  15518   1100  -2991    872       C  
ATOM   1683  O   ASN A1095      57.289  17.682  26.525  1.00135.70           O  
ANISOU 1683  O   ASN A1095    16546  18181  16832   1373  -3105   1478       O  
ATOM   1684  CB  ASN A1095      56.772  20.277  24.410  1.00134.19           C  
ANISOU 1684  CB  ASN A1095    17442  17392  16153    646  -2480   -612       C  
ATOM   1685  CG  ASN A1095      57.592  19.472  23.416  1.00140.94           C  
ANISOU 1685  CG  ASN A1095    17973  17534  18044    834  -2137   -531       C  
ATOM   1686  OD1 ASN A1095      58.275  18.517  23.784  1.00149.71           O  
ANISOU 1686  OD1 ASN A1095    18515  18682  19685   1110  -2265    112       O  
ATOM   1687  ND2 ASN A1095      57.525  19.857  22.147  1.00137.16           N  
ANISOU 1687  ND2 ASN A1095    17880  16379  17854    683  -1696  -1188       N  
ATOM   1688  N   LEU A1096      55.236  18.606  26.419  1.00116.19           N  
ANISOU 1688  N   LEU A1096    15100  15687  13361   1076  -2834    854       N  
ATOM   1689  CA  LEU A1096      54.534  17.395  26.830  1.00115.05           C  
ANISOU 1689  CA  LEU A1096    14933  15384  13396   1356  -2764   1559       C  
ATOM   1690  C   LEU A1096      54.818  16.231  25.889  1.00113.17           C  
ANISOU 1690  C   LEU A1096    14490  14338  14170   1635  -2402   1821       C  
ATOM   1691  O   LEU A1096      55.187  15.145  26.330  1.00115.70           O  
ANISOU 1691  O   LEU A1096    14408  14654  14897   1924  -2516   2545       O  
ATOM   1692  CB  LEU A1096      53.026  17.646  26.896  1.00106.44           C  
ANISOU 1692  CB  LEU A1096    14436  14231  11774   1245  -2568   1352       C  
ATOM   1693  CG  LEU A1096      52.148  16.420  27.158  1.00102.88           C  
ANISOU 1693  CG  LEU A1096    14036  13507  11545   1501  -2402   1990       C  
ATOM   1694  CD1 LEU A1096      52.415  15.846  28.540  1.00110.14           C  
ANISOU 1694  CD1 LEU A1096    14624  15065  12159   1650  -2806   2784       C  
ATOM   1695  CD2 LEU A1096      50.679  16.765  26.993  1.00 97.85           C  
ANISOU 1695  CD2 LEU A1096    13973  12694  10510   1363  -2147   1645       C  
ATOM   1696  N   VAL A1097      54.647  16.474  24.594  1.00105.40           N  
ANISOU 1696  N   VAL A1097    13820  12655  13574   1541  -1970   1225       N  
ATOM   1697  CA  VAL A1097      54.861  15.459  23.566  1.00104.01           C  
ANISOU 1697  CA  VAL A1097    13554  11629  14338   1768  -1563   1374       C  
ATOM   1698  C   VAL A1097      56.265  14.859  23.644  1.00106.22           C  
ANISOU 1698  C   VAL A1097    13149  11932  15279   1976  -1689   1779       C  
ATOM   1699  O   VAL A1097      56.454  13.662  23.416  1.00100.36           O  
ANISOU 1699  O   VAL A1097    12154  10746  15233   2278  -1523   2301       O  
ATOM   1700  CB  VAL A1097      54.634  16.049  22.154  1.00100.49           C  
ANISOU 1700  CB  VAL A1097    13598  10468  14116   1567  -1125    562       C  
ATOM   1701  CG1 VAL A1097      54.879  15.002  21.079  1.00102.23           C  
ANISOU 1701  CG1 VAL A1097    13772   9779  15291   1787   -685    709       C  
ATOM   1702  CG2 VAL A1097      53.226  16.614  22.039  1.00 93.05           C  
ANISOU 1702  CG2 VAL A1097    13315   9450  12589   1381  -1027    160       C  
ATOM   1703  N   GLY A1098      57.238  15.698  23.988  1.00114.75           N  
ANISOU 1703  N   GLY A1098    13921  13531  16147   1814  -1994   1537       N  
ATOM   1704  CA  GLY A1098      58.630  15.290  24.050  1.00126.02           C  
ANISOU 1704  CA  GLY A1098    14660  15009  18214   1977  -2143   1831       C  
ATOM   1705  C   GLY A1098      58.922  14.164  25.024  1.00141.44           C  
ANISOU 1705  C   GLY A1098    16110  17241  20391   2319  -2482   2766       C  
ATOM   1706  O   GLY A1098      59.248  13.051  24.611  1.00143.53           O  
ANISOU 1706  O   GLY A1098    16092  16981  21463   2618  -2268   3182       O  
ATOM   1707  N   TRP A1099      58.802  14.445  26.319  1.00151.07           N  
ANISOU 1707  N   TRP A1099    17251  19266  20885   2273  -3010   3100       N  
ATOM   1708  CA  TRP A1099      59.177  13.466  27.334  1.00161.22           C  
ANISOU 1708  CA  TRP A1099    18076  20870  22311   2572  -3414   3984       C  
ATOM   1709  C   TRP A1099      58.140  12.355  27.475  1.00154.01           C  
ANISOU 1709  C   TRP A1099    17422  19633  21460   2806  -3211   4533       C  
ATOM   1710  O   TRP A1099      58.396  11.346  28.130  1.00166.19           O  
ANISOU 1710  O   TRP A1099    18631  21261  23253   3095  -3449   5293       O  
ATOM   1711  CB  TRP A1099      59.414  14.148  28.687  1.00173.80           C  
ANISOU 1711  CB  TRP A1099    19560  23413  23065   2423  -4063   4159       C  
ATOM   1712  CG  TRP A1099      58.204  14.789  29.295  1.00172.38           C  
ANISOU 1712  CG  TRP A1099    19988  23638  21870   2194  -4114   3992       C  
ATOM   1713  CD1 TRP A1099      57.700  16.024  29.008  1.00168.35           C  
ANISOU 1713  CD1 TRP A1099    19937  23273  20755   1848  -3988   3239       C  
ATOM   1714  CD2 TRP A1099      57.362  14.239  30.314  1.00172.67           C  
ANISOU 1714  CD2 TRP A1099    20238  23983  21384   2294  -4294   4588       C  
ATOM   1715  NE1 TRP A1099      56.589  16.272  29.777  1.00165.47           N  
ANISOU 1715  NE1 TRP A1099    20033  23283  19557   1737  -4067   3322       N  
ATOM   1716  CE2 TRP A1099      56.361  15.191  30.588  1.00166.79           C  
ANISOU 1716  CE2 TRP A1099    20062  23555  19753   1997  -4238   4141       C  
ATOM   1717  CE3 TRP A1099      57.354  13.031  31.019  1.00177.52           C  
ANISOU 1717  CE3 TRP A1099    20634  24617  22197   2601  -4482   5450       C  
ATOM   1718  CZ2 TRP A1099      55.362  14.974  31.534  1.00164.89           C  
ANISOU 1718  CZ2 TRP A1099    20161  23645  18845   1991  -4328   4518       C  
ATOM   1719  CZ3 TRP A1099      56.362  12.817  31.957  1.00176.45           C  
ANISOU 1719  CZ3 TRP A1099    20869  24809  21364   2583  -4582   5828       C  
ATOM   1720  CH2 TRP A1099      55.380  13.784  32.206  1.00170.36           C  
ANISOU 1720  CH2 TRP A1099    20647  24346  19735   2277  -4488   5359       C  
ATOM   1721  N   VAL A1100      56.974  12.537  26.864  1.00134.97           N  
ANISOU 1721  N   VAL A1100    15607  16838  18836   2679  -2789   4150       N  
ATOM   1722  CA  VAL A1100      56.015  11.445  26.754  1.00128.12           C  
ANISOU 1722  CA  VAL A1100    14975  15514  18189   2894  -2505   4596       C  
ATOM   1723  C   VAL A1100      56.591  10.403  25.804  1.00128.03           C  
ANISOU 1723  C   VAL A1100    14679  14722  19244   3176  -2161   4802       C  
ATOM   1724  O   VAL A1100      56.539   9.203  26.071  1.00135.40           O  
ANISOU 1724  O   VAL A1100    15421  15451  20573   3481  -2160   5496       O  
ATOM   1725  CB  VAL A1100      54.634  11.924  26.253  1.00119.24           C  
ANISOU 1725  CB  VAL A1100    14539  14118  16650   2681  -2144   4087       C  
ATOM   1726  CG1 VAL A1100      53.867  10.782  25.597  1.00110.80           C  
ANISOU 1726  CG1 VAL A1100    13674  12283  16143   2896  -1712   4370       C  
ATOM   1727  CG2 VAL A1100      53.829  12.516  27.401  1.00122.62           C  
ANISOU 1727  CG2 VAL A1100    15240  15269  16080   2503  -2442   4149       C  
ATOM   1728  N   LYS A1101      57.163  10.877  24.702  1.00121.59           N  
ANISOU 1728  N   LYS A1101    13852  13464  18882   3066  -1859   4194       N  
ATOM   1729  CA  LYS A1101      57.819  10.001  23.740  1.00120.38           C  
ANISOU 1729  CA  LYS A1101    13434  12553  19752   3305  -1492   4309       C  
ATOM   1730  C   LYS A1101      59.080   9.386  24.344  1.00129.90           C  
ANISOU 1730  C   LYS A1101    13877  14025  21452   3573  -1846   4898       C  
ATOM   1731  O   LYS A1101      59.543   8.336  23.899  1.00138.00           O  
ANISOU 1731  O   LYS A1101    14603  14513  23317   3871  -1632   5274       O  
ATOM   1732  CB  LYS A1101      58.159  10.767  22.460  1.00109.48           C  
ANISOU 1732  CB  LYS A1101    12269  10664  18665   3078  -1080   3470       C  
ATOM   1733  N   GLN A1102      59.625  10.048  25.362  1.00134.75           N  
ANISOU 1733  N   GLN A1102    14191  15457  21550   3466  -2405   4974       N  
ATOM   1734  CA  GLN A1102      60.817   9.564  26.053  1.00141.52           C  
ANISOU 1734  CA  GLN A1102    14318  16641  22811   3701  -2852   5529       C  
ATOM   1735  C   GLN A1102      60.450   8.613  27.188  1.00148.21           C  
ANISOU 1735  C   GLN A1102    15075  17805  23432   3960  -3233   6414       C  
ATOM   1736  O   GLN A1102      61.172   7.653  27.461  1.00156.70           O  
ANISOU 1736  O   GLN A1102    15638  18780  25120   4287  -3422   7031       O  
ATOM   1737  CB  GLN A1102      61.637  10.737  26.594  1.00141.49           C  
ANISOU 1737  CB  GLN A1102    14037  17343  22378   3449  -3312   5185       C  
ATOM   1738  N   HIS A1103      59.330   8.886  27.851  1.00145.98           N  
ANISOU 1738  N   HIS A1103    15300  17890  22276   3809  -3337   6470       N  
ATOM   1739  CA  HIS A1103      58.817   7.988  28.880  1.00146.39           C  
ANISOU 1739  CA  HIS A1103    15391  18184  22049   4017  -3612   7273       C  
ATOM   1740  C   HIS A1103      58.154   6.780  28.227  1.00150.07           C  
ANISOU 1740  C   HIS A1103    16097  17900  23020   4204  -3075   7460       C  
ATOM   1741  O   HIS A1103      57.911   5.763  28.878  1.00153.73           O  
ANISOU 1741  O   HIS A1103    16642  18415  23355   4288  -3107   7847       O  
ATOM   1742  CB  HIS A1103      57.829   8.712  29.799  1.00136.59           C  
ANISOU 1742  CB  HIS A1103    14644  17570  19683   3750  -3828   7192       C  
ATOM   1743  N   ALA A1104      57.860   6.904  26.935  1.00148.01           N  
ANISOU 1743  N   ALA A1104    16060  16954  23221   4161  -2527   6975       N  
ATOM   1744  CA  ALA A1104      57.365   5.781  26.149  1.00149.78           C  
ANISOU 1744  CA  ALA A1104    16586  16498  23825   4180  -1951   6840       C  
ATOM   1745  C   ALA A1104      58.480   4.759  25.969  1.00162.63           C  
ANISOU 1745  C   ALA A1104    17748  17908  26136   4362  -1908   7052       C  
ATOM   1746  O   ALA A1104      58.224   3.572  25.757  1.00168.61           O  
ANISOU 1746  O   ALA A1104    18640  18347  27077   4404  -1630   7161       O  
ATOM   1747  CB  ALA A1104      56.846   6.253  24.800  1.00140.70           C  
ANISOU 1747  CB  ALA A1104    15856  14717  22885   4011  -1411   6157       C  
ATOM   1748  N   LYS A1105      59.718   5.236  26.051  1.00164.16           N  
ANISOU 1748  N   LYS A1105    17375  18296  26704   4455  -2202   7091       N  
ATOM   1749  CA  LYS A1105      60.884   4.366  26.004  1.00165.41           C  
ANISOU 1749  CA  LYS A1105    17019  18315  27514   4637  -2233   7321       C  
ATOM   1750  C   LYS A1105      61.079   3.675  27.350  1.00171.50           C  
ANISOU 1750  C   LYS A1105    17594  19599  27971   4778  -2746   7954       C  
ATOM   1751  O   LYS A1105      61.721   2.629  27.436  1.00175.38           O  
ANISOU 1751  O   LYS A1105    17814  19926  28898   4943  -2743   8232       O  
ATOM   1752  CB  LYS A1105      62.135   5.160  25.625  1.00165.35           C  
ANISOU 1752  CB  LYS A1105    16445  18333  28047   4663  -2367   7082       C  
ATOM   1753  N   LEU A1106      60.517   4.268  28.400  1.00171.25           N  
ANISOU 1753  N   LEU A1106    17744  20177  27145   4693  -3180   8154       N  
ATOM   1754  CA  LEU A1106      60.604   3.704  29.744  1.00176.81           C  
ANISOU 1754  CA  LEU A1106    18388  21371  27420   4777  -3665   8698       C  
ATOM   1755  C   LEU A1106      59.316   2.975  30.121  1.00174.95           C  
ANISOU 1755  C   LEU A1106    18719  21047  26706   4731  -3446   8876       C  
ATOM   1756  O   LEU A1106      58.934   2.001  29.473  1.00177.00           O  
ANISOU 1756  O   LEU A1106    19155  20768  27330   4780  -2985   8828       O  
ATOM   1757  CB  LEU A1106      60.909   4.802  30.766  1.00177.38           C  
ANISOU 1757  CB  LEU A1106    18320  22230  26845   4662  -4313   8777       C  
ATOM   1758  N   ARG A1107      58.651   3.449  31.171  1.00170.59           N  
ANISOU 1758  N   ARG A1107    18457  21040  25317   4608  -3771   9045       N  
ATOM   1759  CA  ARG A1107      57.389   2.859  31.609  1.00163.93           C  
ANISOU 1759  CA  ARG A1107    18141  20146  23998   4539  -3565   9190       C  
ATOM   1760  C   ARG A1107      56.210   3.774  31.279  1.00157.54           C  
ANISOU 1760  C   ARG A1107    17797  19364  22699   4311  -3309   8812       C  
ATOM   1761  O   ARG A1107      56.146   4.913  31.743  1.00154.92           O  
ANISOU 1761  O   ARG A1107    17521  19548  21793   4162  -3612   8710       O  
ATOM   1762  CB  ARG A1107      57.424   2.564  33.109  1.00160.91           C  
ANISOU 1762  CB  ARG A1107    17818  20298  23024   4560  -4061   9671       C  
ATOM   1763  N   ILE A1108      55.279   3.265  30.477  1.00152.49           N  
ANISOU 1763  N   ILE A1108    17501  18179  22261   4263  -2768   8575       N  
ATOM   1764  CA  ILE A1108      54.119   4.040  30.044  1.00141.90           C  
ANISOU 1764  CA  ILE A1108    16611  16754  20551   4058  -2484   8177       C  
ATOM   1765  C   ILE A1108      53.125   4.265  31.179  1.00142.86           C  
ANISOU 1765  C   ILE A1108    17098  17353  19832   3919  -2648   8379       C  
ATOM   1766  O   ILE A1108      52.394   5.252  31.188  1.00139.59           O  
ANISOU 1766  O   ILE A1108    16975  17143  18918   3738  -2612   8118       O  
ATOM   1767  CB  ILE A1108      53.389   3.354  28.874  1.00135.37           C  
ANISOU 1767  CB  ILE A1108    16065  15204  20166   4012  -1889   7810       C  
ATOM   1768  N   SER A1109      53.100   3.344  32.136  1.00156.52           N  
ANISOU 1768  N   SER A1109    18831  19242  21398   3997  -2812   8829       N  
ATOM   1769  CA  SER A1109      52.228   3.474  33.298  1.00162.06           C  
ANISOU 1769  CA  SER A1109    19888  20375  21311   3859  -2951   9037       C  
ATOM   1770  C   SER A1109      52.800   4.487  34.284  1.00163.70           C  
ANISOU 1770  C   SER A1109    20012  21316  20872   3770  -3490   9136       C  
ATOM   1771  O   SER A1109      53.108   4.151  35.431  1.00169.87           O  
ANISOU 1771  O   SER A1109    20788  22459  21294   3799  -3850   9515       O  
ATOM   1772  CB  SER A1109      52.033   2.119  33.983  1.00167.65           C  
ANISOU 1772  CB  SER A1109    20666  20963  22073   3968  -2941   9474       C  
ATOM   1773  N   ASP A1110      52.942   5.727  33.829  1.00151.70           N  
ANISOU 1773  N   ASP A1110    18457  20004  19179   3643  -3555   8758       N  
ATOM   1774  CA  ASP A1110      53.503   6.787  34.653  1.00152.76           C  
ANISOU 1774  CA  ASP A1110    18519  20857  18667   3500  -4066   8723       C  
ATOM   1775  C   ASP A1110      53.062   8.154  34.146  1.00148.31           C  
ANISOU 1775  C   ASP A1110    18145  20503  17703   3273  -3986   8211       C  
ATOM   1776  O   ASP A1110      53.233   9.162  34.829  1.00154.03           O  
ANISOU 1776  O   ASP A1110    18951  21855  17719   3064  -4333   8038       O  
ATOM   1777  CB  ASP A1110      55.032   6.699  34.674  1.00156.49           C  
ANISOU 1777  CB  ASP A1110    18424  21442  19591   3664  -4485   8883       C  
ATOM   1778  N   VAL A1111      52.484   8.176  32.948  1.00137.69           N  
ANISOU 1778  N   VAL A1111    16915  18606  16795   3297  -3522   7920       N  
ATOM   1779  CA  VAL A1111      52.124   9.425  32.287  1.00127.97           C  
ANISOU 1779  CA  VAL A1111    15890  17445  15287   3077  -3392   7299       C  
ATOM   1780  C   VAL A1111      50.639   9.760  32.403  1.00128.97           C  
ANISOU 1780  C   VAL A1111    16575  17570  14856   2875  -3063   7035       C  
ATOM   1781  O   VAL A1111      50.249  10.925  32.296  1.00126.53           O  
ANISOU 1781  O   VAL A1111    16544  17498  14033   2589  -3016   6377       O  
ATOM   1782  CB  VAL A1111      52.499   9.388  30.794  1.00120.15           C  
ANISOU 1782  CB  VAL A1111    14766  15730  15155   3141  -3019   6820       C  
ATOM   1783  N   PHE A1112      49.814   8.740  32.619  1.00129.73           N  
ANISOU 1783  N   PHE A1112    16844  17358  15087   2988  -2805   7427       N  
ATOM   1784  CA  PHE A1112      48.365   8.924  32.662  1.00124.26           C  
ANISOU 1784  CA  PHE A1112    16625  16578  14010   2825  -2452   7220       C  
ATOM   1785  C   PHE A1112      47.919   9.815  33.818  1.00126.87           C  
ANISOU 1785  C   PHE A1112    17230  17657  13316   2564  -2670   7117       C  
ATOM   1786  O   PHE A1112      48.618   9.945  34.824  1.00129.05           O  
ANISOU 1786  O   PHE A1112    17389  18455  13189   2519  -3079   7310       O  
ATOM   1787  CB  PHE A1112      47.658   7.569  32.749  1.00124.76           C  
ANISOU 1787  CB  PHE A1112    16788  16151  14464   2918  -2133   7495       C  
ATOM   1788  CG  PHE A1112      47.764   6.748  31.496  1.00119.14           C  
ANISOU 1788  CG  PHE A1112    15952  14637  14678   3073  -1798   7363       C  
ATOM   1789  CD1 PHE A1112      47.142   7.161  30.328  1.00110.57           C  
ANISOU 1789  CD1 PHE A1112    15082  13044  13885   3003  -1444   6859       C  
ATOM   1790  CD2 PHE A1112      48.473   5.559  31.488  1.00120.19           C  
ANISOU 1790  CD2 PHE A1112    15797  14516  15353   3262  -1833   7676       C  
ATOM   1791  CE1 PHE A1112      47.236   6.408  29.173  1.00108.17           C  
ANISOU 1791  CE1 PHE A1112    14726  12011  14363   3073  -1141   6612       C  
ATOM   1792  CE2 PHE A1112      48.569   4.799  30.335  1.00115.40           C  
ANISOU 1792  CE2 PHE A1112    15116  13221  15509   3348  -1508   7455       C  
ATOM   1793  CZ  PHE A1112      47.949   5.224  29.176  1.00110.85           C  
ANISOU 1793  CZ  PHE A1112    14776  12168  15175   3233  -1166   6897       C  
ATOM   1794  N   ASP A1113      46.749  10.427  33.658  1.00127.46           N  
ANISOU 1794  N   ASP A1113    17696  17724  13008   2379  -2371   6735       N  
ATOM   1795  CA  ASP A1113      46.167  11.286  34.685  1.00131.90           C  
ANISOU 1795  CA  ASP A1113    18577  18907  12634   2100  -2470   6519       C  
ATOM   1796  C   ASP A1113      45.882  10.481  35.951  1.00143.19           C  
ANISOU 1796  C   ASP A1113    20107  20483  13816   2090  -2516   6975       C  
ATOM   1797  O   ASP A1113      45.160   9.485  35.907  1.00150.61           O  
ANISOU 1797  O   ASP A1113    21121  21003  15099   2182  -2208   7253       O  
ATOM   1798  CB  ASP A1113      44.884  11.941  34.162  1.00124.47           C  
ANISOU 1798  CB  ASP A1113    18017  17761  11516   1915  -2057   5931       C  
ATOM   1799  CG  ASP A1113      44.418  13.107  35.022  1.00122.71           C  
ANISOU 1799  CG  ASP A1113    18102  18190  10331   1616  -2159   5566       C  
ATOM   1800  OD1 ASP A1113      44.553  13.045  36.262  1.00130.17           O  
ANISOU 1800  OD1 ASP A1113    19116  19505  10839   1508  -2356   5766       O  
ATOM   1801  OD2 ASP A1113      43.905  14.092  34.449  1.00110.82           O  
ANISOU 1801  OD2 ASP A1113    16816  16606   8683   1424  -1990   4827       O  
ATOM   1802  N   PRO A1114      46.464  10.910  37.082  1.00142.29           N  
ANISOU 1802  N   PRO A1114    20021  20930  13111   1971  -2902   7025       N  
ATOM   1803  CA  PRO A1114      46.268  10.261  38.383  1.00145.24           C  
ANISOU 1803  CA  PRO A1114    20565  21472  13146   1957  -2987   7443       C  
ATOM   1804  C   PRO A1114      44.797  10.076  38.749  1.00144.40           C  
ANISOU 1804  C   PRO A1114    20859  21239  12769   1815  -2552   7411       C  
ATOM   1805  O   PRO A1114      44.443   9.070  39.362  1.00151.10           O  
ANISOU 1805  O   PRO A1114    21797  21938  13677   1885  -2454   7856       O  
ATOM   1806  CB  PRO A1114      46.950  11.227  39.356  1.00147.30           C  
ANISOU 1806  CB  PRO A1114    20915  22327  12724   1785  -3409   7241       C  
ATOM   1807  CG  PRO A1114      48.012  11.874  38.542  1.00143.96           C  
ANISOU 1807  CG  PRO A1114    20138  21996  12563   1824  -3676   6967       C  
ATOM   1808  CD  PRO A1114      47.436  12.016  37.161  1.00138.97           C  
ANISOU 1808  CD  PRO A1114    19475  20968  12360   1852  -3297   6671       C  
ATOM   1809  N   GLU A1115      43.953  11.030  38.372  1.00138.70           N  
ANISOU 1809  N   GLU A1115    20368  20566  11767   1613  -2294   6875       N  
ATOM   1810  CA  GLU A1115      42.536  10.968  38.715  1.00139.71           C  
ANISOU 1810  CA  GLU A1115    20841  20596  11648   1457  -1874   6798       C  
ATOM   1811  C   GLU A1115      41.786   9.932  37.881  1.00140.25           C  
ANISOU 1811  C   GLU A1115    20825  20054  12411   1613  -1474   7025       C  
ATOM   1812  O   GLU A1115      40.673   9.536  38.229  1.00145.75           O  
ANISOU 1812  O   GLU A1115    21732  20610  13036   1524  -1132   7115       O  
ATOM   1813  CB  GLU A1115      41.888  12.345  38.551  1.00130.92           C  
ANISOU 1813  CB  GLU A1115    19982  19695  10068   1195  -1731   6096       C  
ATOM   1814  CG  GLU A1115      42.388  13.386  39.543  1.00134.66           C  
ANISOU 1814  CG  GLU A1115    20642  20673   9850   1008  -2037   5782       C  
ATOM   1815  CD  GLU A1115      42.028  13.050  40.979  1.00145.68           C  
ANISOU 1815  CD  GLU A1115    22332  22261  10758    933  -2022   6096       C  
ATOM   1816  OE1 GLU A1115      42.745  13.504  41.897  1.00148.43           O  
ANISOU 1816  OE1 GLU A1115    22780  22947  10671    895  -2356   6076       O  
ATOM   1817  OE2 GLU A1115      41.024  12.337  41.193  1.00152.40           O  
ANISOU 1817  OE2 GLU A1115    23332  22905  11667    913  -1667   6358       O  
ATOM   1818  N   LEU A1116      42.395   9.493  36.784  1.00133.79           N  
ANISOU 1818  N   LEU A1116    19704  18831  12300   1837  -1502   7087       N  
ATOM   1819  CA  LEU A1116      41.788   8.476  35.931  1.00129.01           C  
ANISOU 1819  CA  LEU A1116    19026  17537  12453   1986  -1138   7221       C  
ATOM   1820  C   LEU A1116      41.982   7.081  36.513  1.00136.75           C  
ANISOU 1820  C   LEU A1116    19903  18337  13719   2123  -1171   7783       C  
ATOM   1821  O   LEU A1116      41.086   6.239  36.446  1.00138.33           O  
ANISOU 1821  O   LEU A1116    20188  18159  14213   2123   -845   7910       O  
ATOM   1822  CB  LEU A1116      42.368   8.535  34.517  1.00121.92           C  
ANISOU 1822  CB  LEU A1116    17906  16181  12237   2155  -1121   6993       C  
ATOM   1823  CG  LEU A1116      42.016   9.752  33.660  1.00115.43           C  
ANISOU 1823  CG  LEU A1116    17251  15336  11272   2068   -994   6402       C  
ATOM   1824  CD1 LEU A1116      42.608   9.601  32.269  1.00109.49           C  
ANISOU 1824  CD1 LEU A1116    16329  13980  11290   2250   -935   6207       C  
ATOM   1825  CD2 LEU A1116      40.510   9.954  33.587  1.00115.40           C  
ANISOU 1825  CD2 LEU A1116    17568  15145  11134   1928   -581   6134       C  
ATOM   1826  N   MET A1117      43.159   6.844  37.082  1.00133.54           N  
ANISOU 1826  N   MET A1117    15159  20351  15231    258  -2402   8042       N  
ATOM   1827  CA  MET A1117      43.481   5.552  37.676  1.00140.31           C  
ANISOU 1827  CA  MET A1117    15958  21140  16215    636  -2268   8725       C  
ATOM   1828  C   MET A1117      42.745   5.334  38.995  1.00138.89           C  
ANISOU 1828  C   MET A1117    15627  21245  15901    585  -2090   9160       C  
ATOM   1829  O   MET A1117      42.582   4.200  39.442  1.00141.46           O  
ANISOU 1829  O   MET A1117    15997  21265  16486    781  -1922   9610       O  
ATOM   1830  CB  MET A1117      44.989   5.427  37.895  1.00147.42           C  
ANISOU 1830  CB  MET A1117    16672  22589  16752    997  -2297   8790       C  
ATOM   1831  CG  MET A1117      45.800   5.307  36.614  1.00147.93           C  
ANISOU 1831  CG  MET A1117    16870  22339  16997   1140  -2418   8505       C  
ATOM   1832  SD  MET A1117      45.471   3.776  35.721  1.00156.99           S  
ANISOU 1832  SD  MET A1117    18362  22372  18917   1391  -2333   8749       S  
ATOM   1833  CE  MET A1117      46.701   3.878  34.425  1.00140.57           C  
ANISOU 1833  CE  MET A1117    16352  20212  16845   1577  -2427   8273       C  
ATOM   1834  N   LYS A1118      42.308   6.425  39.618  1.00137.18           N  
ANISOU 1834  N   LYS A1118    15254  21588  15283    310  -2100   8941       N  
ATOM   1835  CA  LYS A1118      41.557   6.342  40.865  1.00141.55           C  
ANISOU 1835  CA  LYS A1118    15657  22451  15676    223  -1898   9247       C  
ATOM   1836  C   LYS A1118      40.177   5.745  40.626  1.00148.37           C  
ANISOU 1836  C   LYS A1118    16661  22629  17083     29  -1796   9514       C  
ATOM   1837  O   LYS A1118      39.653   5.017  41.471  1.00151.48           O  
ANISOU 1837  O   LYS A1118    16998  22998  17557     57  -1579   9971       O  
ATOM   1838  CB  LYS A1118      41.426   7.721  41.516  1.00136.70           C  
ANISOU 1838  CB  LYS A1118    14858  22582  14499    -20  -1935   8876       C  
ATOM   1839  CG  LYS A1118      42.737   8.300  42.017  1.00137.55           C  
ANISOU 1839  CG  LYS A1118    14790  23400  14073    116  -1983   8600       C  
ATOM   1840  CD  LYS A1118      42.529   9.658  42.669  1.00138.60           C  
ANISOU 1840  CD  LYS A1118    14789  24170  13704   -151  -2002   8182       C  
ATOM   1841  CE  LYS A1118      43.848  10.240  43.157  1.00142.61           C  
ANISOU 1841  CE  LYS A1118    15128  25314  13744    -64  -2047   7881       C  
ATOM   1842  NZ  LYS A1118      43.673  11.571  43.803  1.00143.64           N  
ANISOU 1842  NZ  LYS A1118    15168  25987  13423   -331  -2055   7429       N  
ATOM   1843  N   GLU A1119      39.595   6.063  39.473  1.00149.42           N  
ANISOU 1843  N   GLU A1119    16985  22141  17648   -202  -1907   8997       N  
ATOM   1844  CA  GLU A1119      38.280   5.550  39.102  1.00153.46           C  
ANISOU 1844  CA  GLU A1119    17620  21931  18758   -433  -1820   9037       C  
ATOM   1845  C   GLU A1119      38.296   4.028  38.999  1.00157.24           C  
ANISOU 1845  C   GLU A1119    18255  21792  19696   -231  -1707   9611       C  
ATOM   1846  O   GLU A1119      37.475   3.344  39.612  1.00156.96           O  
ANISOU 1846  O   GLU A1119    18185  21577  19877   -323  -1513  10064       O  
ATOM   1847  CB  GLU A1119      37.821   6.165  37.778  1.00147.12           C  
ANISOU 1847  CB  GLU A1119    17012  20585  18301   -676  -2020   8359       C  
ATOM   1848  N   ASP A1120      39.245   3.511  38.226  1.00154.54           N  
ANISOU 1848  N   ASP A1120    18092  21128  19496     40  -1819   9582       N  
ATOM   1849  CA  ASP A1120      39.397   2.075  38.029  1.00149.05           C  
ANISOU 1849  CA  ASP A1120    17596  19793  19245    286  -1736  10074       C  
ATOM   1850  C   ASP A1120      40.735   1.793  37.357  1.00145.27           C  
ANISOU 1850  C   ASP A1120    17225  19257  18715    664  -1852   9933       C  
ATOM   1851  O   ASP A1120      41.006   2.304  36.270  1.00147.36           O  
ANISOU 1851  O   ASP A1120    17613  19316  19062    594  -2017   9398       O  
ATOM   1852  CB  ASP A1120      38.245   1.517  37.185  1.00145.05           C  
ANISOU 1852  CB  ASP A1120    17333  18339  19442      4  -1728   9946       C  
ATOM   1853  CG  ASP A1120      38.068   0.018  37.347  1.00150.13           C  
ANISOU 1853  CG  ASP A1120    18164  18363  20515    152  -1553  10390       C  
ATOM   1854  OD1 ASP A1120      39.027  -0.662  37.764  1.00151.54           O  
ANISOU 1854  OD1 ASP A1120    18370  18688  20522    546  -1479  10630       O  
ATOM   1855  OD2 ASP A1120      36.961  -0.482  37.054  1.00153.65           O  
ANISOU 1855  OD2 ASP A1120    18735  18178  21468   -137  -1492  10415       O  
ATOM   1856  N   PRO A1121      41.587   0.988  38.007  1.00140.81           N  
ANISOU 1856  N   PRO A1121    16613  18886  18002   1053  -1734  10251       N  
ATOM   1857  CA  PRO A1121      42.864   0.608  37.393  1.00141.52           C  
ANISOU 1857  CA  PRO A1121    16773  18917  18081   1456  -1821  10164       C  
ATOM   1858  C   PRO A1121      42.705  -0.465  36.315  1.00140.15           C  
ANISOU 1858  C   PRO A1121    16966  17727  18557   1572  -1822  10158       C  
ATOM   1859  O   PRO A1121      43.701  -0.906  35.739  1.00141.09           O  
ANISOU 1859  O   PRO A1121    17169  17704  18733   1938  -1871  10107       O  
ATOM   1860  CB  PRO A1121      43.674   0.075  38.577  1.00147.26           C  
ANISOU 1860  CB  PRO A1121    17317  20175  18459   1811  -1703  10540       C  
ATOM   1861  CG  PRO A1121      42.650  -0.411  39.537  1.00150.03           C  
ANISOU 1861  CG  PRO A1121    17681  20420  18905   1629  -1515  10921       C  
ATOM   1862  CD  PRO A1121      41.479   0.518  39.399  1.00143.89           C  
ANISOU 1862  CD  PRO A1121    16851  19664  18156   1141  -1534  10696       C  
ATOM   1863  N   ALA A1122      41.468  -0.871  36.045  1.00138.95           N  
ANISOU 1863  N   ALA A1122    17018  16890  18885   1257  -1764  10182       N  
ATOM   1864  CA  ALA A1122      41.200  -1.896  35.042  1.00141.55           C  
ANISOU 1864  CA  ALA A1122    17727  16221  19836   1300  -1760  10101       C  
ATOM   1865  C   ALA A1122      41.177  -1.318  33.628  1.00144.22           C  
ANISOU 1865  C   ALA A1122    18237  16169  20391   1138  -1969   9587       C  
ATOM   1866  O   ALA A1122      41.503  -2.009  32.663  1.00152.65           O  
ANISOU 1866  O   ALA A1122    19597  16588  21815   1314  -2003   9425       O  
ATOM   1867  CB  ALA A1122      39.885  -2.598  35.345  1.00141.74           C  
ANISOU 1867  CB  ALA A1122    17885  15696  20273    988  -1616  10295       C  
ATOM   1868  N   LEU A1123      40.794  -0.051  33.507  1.00134.37           N  
ANISOU 1868  N   LEU A1123    16838  15331  18887    793  -2089   9192       N  
ATOM   1869  CA  LEU A1123      40.678   0.580  32.197  1.00131.20           C  
ANISOU 1869  CA  LEU A1123    16630  14609  18610    566  -2265   8482       C  
ATOM   1870  C   LEU A1123      42.021   1.075  31.663  1.00130.91           C  
ANISOU 1870  C   LEU A1123    16558  14978  18202    822  -2347   8145       C  
ATOM   1871  O   LEU A1123      42.067   1.795  30.668  1.00129.61           O  
ANISOU 1871  O   LEU A1123    16527  14718  17999    623  -2488   7554       O  
ATOM   1872  CB  LEU A1123      39.669   1.738  32.246  1.00128.34           C  
ANISOU 1872  CB  LEU A1123    16154  14475  18134     90  -2357   8107       C  
ATOM   1873  CG  LEU A1123      39.693   2.741  33.406  1.00128.54           C  
ANISOU 1873  CG  LEU A1123    15815  15432  17593      8  -2315   8193       C  
ATOM   1874  CD1 LEU A1123      40.823   3.751  33.274  1.00131.58           C  
ANISOU 1874  CD1 LEU A1123    16078  16495  17421    111  -2423   7834       C  
ATOM   1875  CD2 LEU A1123      38.357   3.455  33.521  1.00123.03           C  
ANISOU 1875  CD2 LEU A1123    15046  14700  16999   -429  -2351   7957       C  
ATOM   1876  N   GLU A1124      43.113   0.681  32.312  1.00138.93           N  
ANISOU 1876  N   GLU A1124    17390  16455  18944   1258  -2261   8529       N  
ATOM   1877  CA  GLU A1124      44.437   1.110  31.874  1.00142.40           C  
ANISOU 1877  CA  GLU A1124    17727  17352  19028   1509  -2319   8239       C  
ATOM   1878  C   GLU A1124      44.811   0.466  30.540  1.00146.06           C  
ANISOU 1878  C   GLU A1124    18521  17104  19872   1675  -2338   7932       C  
ATOM   1879  O   GLU A1124      45.689   0.957  29.829  1.00144.40           O  
ANISOU 1879  O   GLU A1124    18293  17142  19431   1749  -2390   7517       O  
ATOM   1880  CB  GLU A1124      45.498   0.784  32.932  1.00143.93           C  
ANISOU 1880  CB  GLU A1124    17599  18235  18852   1964  -2241   8752       C  
ATOM   1881  CG  GLU A1124      45.940  -0.672  32.974  1.00153.99           C  
ANISOU 1881  CG  GLU A1124    19005  19021  20484   2471  -2137   9245       C  
ATOM   1882  CD  GLU A1124      47.134  -0.900  33.892  1.00160.44           C  
ANISOU 1882  CD  GLU A1124    19484  20578  20899   2967  -2108   9687       C  
ATOM   1883  OE1 GLU A1124      46.941  -1.454  34.995  1.00163.22           O  
ANISOU 1883  OE1 GLU A1124    19773  21056  21186   3048  -1986  10046       O  
ATOM   1884  OE2 GLU A1124      48.265  -0.529  33.510  1.00158.45           O  
ANISOU 1884  OE2 GLU A1124    19050  20783  20369   3189  -2160   9412       O  
ATOM   1885  N   ILE A1125      44.135  -0.627  30.200  1.00143.76           N  
ANISOU 1885  N   ILE A1125    17424  16524  20676   1523   -538   9048       N  
ATOM   1886  CA  ILE A1125      44.412  -1.335  28.955  1.00141.10           C  
ANISOU 1886  CA  ILE A1125    16816  15535  21262   1499   -578   8744       C  
ATOM   1887  C   ILE A1125      43.909  -0.546  27.746  1.00133.41           C  
ANISOU 1887  C   ILE A1125    15703  14623  20365   1623   -280   8278       C  
ATOM   1888  O   ILE A1125      44.582  -0.485  26.716  1.00129.84           O  
ANISOU 1888  O   ILE A1125    15127  13779  20427   1751   -361   7780       O  
ATOM   1889  CB  ILE A1125      43.790  -2.755  28.961  1.00141.09           C  
ANISOU 1889  CB  ILE A1125    16657  15156  21796   1173   -562   9127       C  
ATOM   1890  CG1 ILE A1125      44.014  -3.449  27.614  1.00138.05           C  
ANISOU 1890  CG1 ILE A1125    16000  14121  22331   1171   -598   8708       C  
ATOM   1891  CG2 ILE A1125      42.308  -2.706  29.316  1.00143.53           C  
ANISOU 1891  CG2 ILE A1125    16933  15925  21676    934   -171   9515       C  
ATOM   1892  CD1 ILE A1125      45.474  -3.646  27.259  1.00137.34           C  
ANISOU 1892  CD1 ILE A1125    15877  13606  22699   1379   -954   8315       C  
ATOM   1893  N   GLU A1126      42.738   0.072  27.870  1.00128.53           N  
ANISOU 1893  N   GLU A1126    15112  14554  19169   1560     71   8267       N  
ATOM   1894  CA  GLU A1126      42.217   0.882  26.779  1.00121.32           C  
ANISOU 1894  CA  GLU A1126    14123  13793  18180   1625    325   7544       C  
ATOM   1895  C   GLU A1126      42.901   2.247  26.769  1.00113.15           C  
ANISOU 1895  C   GLU A1126    13303  13094  16595   1907    203   7072       C  
ATOM   1896  O   GLU A1126      43.010   2.882  25.719  1.00108.50           O  
ANISOU 1896  O   GLU A1126    12693  12434  16098   1986    253   6426       O  
ATOM   1897  CB  GLU A1126      40.693   1.036  26.879  1.00127.52           C  
ANISOU 1897  CB  GLU A1126    14824  15039  18589   1458    712   7596       C  
ATOM   1898  CG  GLU A1126      40.196   1.807  28.094  1.00135.82           C  
ANISOU 1898  CG  GLU A1126    16057  16862  18685   1527    826   7858       C  
ATOM   1899  CD  GLU A1126      38.715   2.146  28.006  1.00136.95           C  
ANISOU 1899  CD  GLU A1126    16058  17507  18471   1419   1228   7715       C  
ATOM   1900  OE1 GLU A1126      38.037   2.142  29.056  1.00140.86           O  
ANISOU 1900  OE1 GLU A1126    16568  18543  18408   1327   1409   8155       O  
ATOM   1901  OE2 GLU A1126      38.230   2.424  26.888  1.00130.90           O  
ANISOU 1901  OE2 GLU A1126    15157  16606  17973   1425   1361   7151       O  
ATOM   1902  N   LEU A1127      43.366   2.687  27.935  1.00109.20           N  
ANISOU 1902  N   LEU A1127    13034  12942  15517   2039     14   7409       N  
ATOM   1903  CA  LEU A1127      44.113   3.936  28.034  1.00104.45           C  
ANISOU 1903  CA  LEU A1127    12657  12615  14413   2300   -181   7028       C  
ATOM   1904  C   LEU A1127      45.386   3.856  27.206  1.00111.43           C  
ANISOU 1904  C   LEU A1127    13458  12978  15903   2383   -433   6675       C  
ATOM   1905  O   LEU A1127      45.701   4.773  26.447  1.00111.67           O  
ANISOU 1905  O   LEU A1127    13540  13073  15819   2482   -449   6087       O  
ATOM   1906  CB  LEU A1127      44.457   4.259  29.488  1.00105.35           C  
ANISOU 1906  CB  LEU A1127    13040  13121  13866   2421   -390   7512       C  
ATOM   1907  CG  LEU A1127      43.330   4.754  30.389  1.00111.24           C  
ANISOU 1907  CG  LEU A1127    13923  14576  13769   2418   -143   7719       C  
ATOM   1908  CD1 LEU A1127      43.879   5.113  31.759  1.00112.18           C  
ANISOU 1908  CD1 LEU A1127    14354  15007  13261   2492   -399   7906       C  
ATOM   1909  CD2 LEU A1127      42.630   5.943  29.759  1.00110.54           C  
ANISOU 1909  CD2 LEU A1127    13865  14881  13254   2550     49   7048       C  
ATOM   1910  N   LEU A1128      46.109   2.749  27.358  1.00119.70           N  
ANISOU 1910  N   LEU A1128    14371  13514  17597   2332   -641   7035       N  
ATOM   1911  CA  LEU A1128      47.327   2.510  26.594  1.00121.66           C  
ANISOU 1911  CA  LEU A1128    14461  13259  18504   2417   -863   6705       C  
ATOM   1912  C   LEU A1128      47.027   2.491  25.101  1.00117.37           C  
ANISOU 1912  C   LEU A1128    13719  12475  18401   2333   -611   6081       C  
ATOM   1913  O   LEU A1128      47.753   3.085  24.306  1.00115.15           O  
ANISOU 1913  O   LEU A1128    13406  12127  18219   2410   -659   5544       O  
ATOM   1914  CB  LEU A1128      47.982   1.194  27.021  1.00129.35           C  
ANISOU 1914  CB  LEU A1128    15328  13776  20045   2312  -1106   6983       C  
ATOM   1915  N   GLN A1129      45.945   1.814  24.728  1.00116.50           N  
ANISOU 1915  N   GLN A1129    13484  12246  18534   2150   -349   6165       N  
ATOM   1916  CA  GLN A1129      45.525   1.759  23.334  1.00111.00           C  
ANISOU 1916  CA  GLN A1129    12632  11319  18223   2057   -117   5596       C  
ATOM   1917  C   GLN A1129      45.105   3.137  22.838  1.00108.63           C  
ANISOU 1917  C   GLN A1129    12509  11470  17296   2101     37   5057       C  
ATOM   1918  O   GLN A1129      45.371   3.494  21.693  1.00109.15           O  
ANISOU 1918  O   GLN A1129    12538  11378  17555   2086     94   4474       O  
ATOM   1919  CB  GLN A1129      44.387   0.755  23.156  1.00112.32           C  
ANISOU 1919  CB  GLN A1129    12644  11275  18755   1843     91   5856       C  
ATOM   1920  CG  GLN A1129      44.832  -0.690  23.323  1.00119.25           C  
ANISOU 1920  CG  GLN A1129    13342  11554  20415   1776   -112   6277       C  
ATOM   1921  CD  GLN A1129      43.702  -1.675  23.129  1.00127.32           C  
ANISOU 1921  CD  GLN A1129    14222  12342  21813   1531     56   6551       C  
ATOM   1922  OE1 GLN A1129      42.567  -1.429  23.541  1.00121.98           O  
ANISOU 1922  OE1 GLN A1129    13595  12077  20675   1390    289   6771       O  
ATOM   1923  NE2 GLN A1129      44.005  -2.803  22.497  1.00137.67           N  
ANISOU 1923  NE2 GLN A1129    15340  13027  23939   1467    -73   6475       N  
ATOM   1924  N   HIS A1130      44.454   3.907  23.706  1.00104.89           N  
ANISOU 1924  N   HIS A1130    12239  11555  16061   2155     84   5245       N  
ATOM   1925  CA  HIS A1130      44.129   5.296  23.396  1.00102.65           C  
ANISOU 1925  CA  HIS A1130    12165  11700  15138   2242    128   4753       C  
ATOM   1926  C   HIS A1130      45.404   6.127  23.325  1.00 95.65           C  
ANISOU 1926  C   HIS A1130    11428  10833  14080   2385   -153   4482       C  
ATOM   1927  O   HIS A1130      45.505   7.065  22.535  1.00 82.07           O  
ANISOU 1927  O   HIS A1130     9830   9201  12152   2390   -168   3939       O  
ATOM   1928  CB  HIS A1130      43.168   5.882  24.436  1.00109.02           C  
ANISOU 1928  CB  HIS A1130    13132  13112  15178   2311    219   5008       C  
ATOM   1929  CG  HIS A1130      41.733   5.516  24.209  1.00112.97           C  
ANISOU 1929  CG  HIS A1130    13483  13726  15716   2162    544   5032       C  
ATOM   1930  ND1 HIS A1130      41.229   4.265  24.494  1.00124.00           N  
ANISOU 1930  ND1 HIS A1130    14660  14915  17541   1971    692   5533       N  
ATOM   1931  CD2 HIS A1130      40.696   6.236  23.719  1.00103.92           C  
ANISOU 1931  CD2 HIS A1130    12364  12863  14258   2166    717   4616       C  
ATOM   1932  CE1 HIS A1130      39.943   4.231  24.192  1.00120.66           C  
ANISOU 1932  CE1 HIS A1130    14112  14667  17068   1852    970   5430       C  
ATOM   1933  NE2 HIS A1130      39.595   5.414  23.719  1.00108.80           N  
ANISOU 1933  NE2 HIS A1130    12747  13463  15128   1983    989   4862       N  
ATOM   1934  N   LEU A1131      46.379   5.772  24.155  1.00 96.53           N  
ANISOU 1934  N   LEU A1131    11537  10850  14290   2478   -404   4877       N  
ATOM   1935  CA  LEU A1131      47.683   6.417  24.113  1.00 99.86           C  
ANISOU 1935  CA  LEU A1131    12037  11245  14661   2594   -693   4665       C  
ATOM   1936  C   LEU A1131      48.402   6.051  22.821  1.00100.89           C  
ANISOU 1936  C   LEU A1131    11932  10927  15476   2501   -650   4211       C  
ATOM   1937  O   LEU A1131      49.169   6.847  22.277  1.00100.27           O  
ANISOU 1937  O   LEU A1131    11907  10895  15296   2510   -759   3797       O  
ATOM   1938  CB  LEU A1131      48.526   6.020  25.326  1.00102.94           C  
ANISOU 1938  CB  LEU A1131    12456  11598  15057   2719  -1000   5216       C  
ATOM   1939  CG  LEU A1131      49.937   6.608  25.389  1.00 97.77           C  
ANISOU 1939  CG  LEU A1131    11841  10898  14410   2840  -1340   5050       C  
ATOM   1940  CD1 LEU A1131      49.873   8.123  25.369  1.00 84.75           C  
ANISOU 1940  CD1 LEU A1131    10491   9697  12013   2908  -1425   4695       C  
ATOM   1941  CD2 LEU A1131      50.676   6.106  26.624  1.00 92.91           C  
ANISOU 1941  CD2 LEU A1131    11268  10210  13824   2945  -1666   5586       C  
ATOM   1942  N   LYS A1132      48.140   4.843  22.330  1.00103.02           N  
ANISOU 1942  N   LYS A1132    11940  10773  16429   2399   -493   4287       N  
ATOM   1943  CA  LYS A1132      48.722   4.390  21.072  1.00103.98           C  
ANISOU 1943  CA  LYS A1132    11822  10474  17212   2324   -414   3826       C  
ATOM   1944  C   LYS A1132      48.155   5.196  19.907  1.00100.06           C  
ANISOU 1944  C   LYS A1132    11436  10111  16469   2196   -195   3222       C  
ATOM   1945  O   LYS A1132      48.818   5.393  18.889  1.00 99.25           O  
ANISOU 1945  O   LYS A1132    11252   9857  16603   2129   -160   2733       O  
ATOM   1946  CB  LYS A1132      48.478   2.892  20.869  1.00101.58           C  
ANISOU 1946  CB  LYS A1132    11247   9666  17683   2266   -341   4053       C  
ATOM   1947  CG  LYS A1132      49.307   2.008  21.796  1.00107.63           C  
ANISOU 1947  CG  LYS A1132    11883  10160  18853   2383   -640   4564       C  
ATOM   1948  CD  LYS A1132      48.920   0.537  21.695  1.00114.40           C  
ANISOU 1948  CD  LYS A1132    12527  10503  20434   2310   -628   4851       C  
ATOM   1949  CE  LYS A1132      49.718  -0.300  22.686  1.00122.33           C  
ANISOU 1949  CE  LYS A1132    13494  11337  21648   2347   -969   5251       C  
ATOM   1950  NZ  LYS A1132      49.441  -1.758  22.566  1.00128.70           N  
ANISOU 1950  NZ  LYS A1132    14140  11706  23054   2206  -1011   5392       N  
ATOM   1951  N   VAL A1133      46.925   5.669  20.063  1.00 90.51           N  
ANISOU 1951  N   VAL A1133    10414   9199  14775   2155    -57   3251       N  
ATOM   1952  CA  VAL A1133      46.324   6.529  19.058  1.00 80.39           C  
ANISOU 1952  CA  VAL A1133     9293   8049  13201   2048     76   2701       C  
ATOM   1953  C   VAL A1133      46.995   7.895  19.087  1.00 75.94           C  
ANISOU 1953  C   VAL A1133     8989   7803  12060   2096   -135   2424       C  
ATOM   1954  O   VAL A1133      47.370   8.437  18.046  1.00 68.66           O  
ANISOU 1954  O   VAL A1133     8132   6814  11141   1970   -127   1925       O  
ATOM   1955  CB  VAL A1133      44.815   6.692  19.276  1.00 81.73           C  
ANISOU 1955  CB  VAL A1133     9563   8463  13028   2022    241   2790       C  
ATOM   1956  CG1 VAL A1133      44.214   7.537  18.164  1.00 69.52           C  
ANISOU 1956  CG1 VAL A1133     8189   6978  11248   1916    317   2194       C  
ATOM   1957  CG2 VAL A1133      44.142   5.328  19.347  1.00 76.57           C  
ANISOU 1957  CG2 VAL A1133     8650   7507  12938   1936    423   3139       C  
ATOM   1958  N   ALA A1134      47.159   8.435  20.292  1.00 77.51           N  
ANISOU 1958  N   ALA A1134     9353   8343  11755   2260   -343   2764       N  
ATOM   1959  CA  ALA A1134      47.775   9.744  20.473  1.00 76.21           C  
ANISOU 1959  CA  ALA A1134     9460   8475  11020   2321   -610   2559       C  
ATOM   1960  C   ALA A1134      49.199   9.790  19.923  1.00 78.15           C  
ANISOU 1960  C   ALA A1134     9581   8508  11603   2247   -742   2340       C  
ATOM   1961  O   ALA A1134      49.579  10.761  19.273  1.00 70.87           O  
ANISOU 1961  O   ALA A1134     8830   7688  10410   2138   -843   1934       O  
ATOM   1962  CB  ALA A1134      47.767  10.135  21.947  1.00 72.35           C  
ANISOU 1962  CB  ALA A1134     9148   8346   9994   2535   -827   3003       C  
ATOM   1963  N   VAL A1135      49.986   8.744  20.170  1.00 80.37           N  
ANISOU 1963  N   VAL A1135     9558   8496  12483   2294   -755   2600       N  
ATOM   1964  CA  VAL A1135      51.383   8.755  19.734  1.00 84.57           C  
ANISOU 1964  CA  VAL A1135     9902   8865  13365   2252   -877   2386       C  
ATOM   1965  C   VAL A1135      51.506   8.642  18.212  1.00 80.09           C  
ANISOU 1965  C   VAL A1135     9193   8088  13151   2033   -630   1820       C  
ATOM   1966  O   VAL A1135      52.421   9.214  17.620  1.00 77.45           O  
ANISOU 1966  O   VAL A1135     8829   7802  12797   1913   -691   1481       O  
ATOM   1967  CB  VAL A1135      52.216   7.630  20.405  1.00104.11           C  
ANISOU 1967  CB  VAL A1135    12062  11051  16445   2395  -1003   2780       C  
ATOM   1968  CG1 VAL A1135      52.293   7.845  21.911  1.00103.38           C  
ANISOU 1968  CG1 VAL A1135    12155  11180  15945   2587  -1299   3331       C  
ATOM   1969  CG2 VAL A1135      51.652   6.259  20.085  1.00112.23           C  
ANISOU 1969  CG2 VAL A1135    12839  11690  18113   2376   -778   2898       C  
ATOM   1970  N   ALA A1136      50.585   7.923  17.576  1.00 76.02           N  
ANISOU 1970  N   ALA A1136     8598   7354  12932   1959   -356   1720       N  
ATOM   1971  CA  ALA A1136      50.588   7.815  16.120  1.00 75.16           C  
ANISOU 1971  CA  ALA A1136     8408   7051  13101   1751   -121   1172       C  
ATOM   1972  C   ALA A1136      50.294   9.171  15.477  1.00 76.93           C  
ANISOU 1972  C   ALA A1136     8993   7554  12682   1568   -154    774       C  
ATOM   1973  O   ALA A1136      50.921   9.546  14.484  1.00 70.68           O  
ANISOU 1973  O   ALA A1136     8195   6742  11919   1365    -95    339       O  
ATOM   1974  CB  ALA A1136      49.581   6.784  15.661  1.00 70.75           C  
ANISOU 1974  CB  ALA A1136     7728   6186  12968   1723    124   1181       C  
ATOM   1975  N   CYS A1137      49.338   9.897  16.048  1.00 64.67           N  
ANISOU 1975  N   CYS A1137     7757   6267  10547   1633   -261    918       N  
ATOM   1976  CA  CYS A1137      49.009  11.239  15.580  1.00 65.43           C  
ANISOU 1976  CA  CYS A1137     8242   6608  10012   1498   -392    573       C  
ATOM   1977  C   CYS A1137      50.204  12.182  15.705  1.00 70.86           C  
ANISOU 1977  C   CYS A1137     9042   7483  10398   1432   -662    485       C  
ATOM   1978  O   CYS A1137      50.342  13.125  14.929  1.00 69.04           O  
ANISOU 1978  O   CYS A1137     9063   7339   9831   1209   -753    112       O  
ATOM   1979  CB  CYS A1137      47.825  11.808  16.364  1.00 61.10           C  
ANISOU 1979  CB  CYS A1137     7964   6331   8920   1658   -502    758       C  
ATOM   1980  SG  CYS A1137      46.254  10.947  16.124  1.00 72.36           S  
ANISOU 1980  SG  CYS A1137     9283   7608  10603   1674   -200    805       S  
ATOM   1981  N   LEU A1138      51.069  11.907  16.680  1.00 73.16           N  
ANISOU 1981  N   LEU A1138     9155   7817  10826   1606   -815    846       N  
ATOM   1982  CA  LEU A1138      52.161  12.808  17.036  1.00 73.81           C  
ANISOU 1982  CA  LEU A1138     9338   8096  10611   1580  -1129    847       C  
ATOM   1983  C   LEU A1138      53.495  12.433  16.392  1.00 80.20           C  
ANISOU 1983  C   LEU A1138     9797   8754  11920   1422  -1051    648       C  
ATOM   1984  O   LEU A1138      54.550  12.927  16.800  1.00 77.55           O  
ANISOU 1984  O   LEU A1138     9421   8546  11498   1417  -1302    718       O  
ATOM   1985  CB  LEU A1138      52.319  12.849  18.557  1.00 72.04           C  
ANISOU 1985  CB  LEU A1138     9162   8037  10174   1875  -1402   1355       C  
ATOM   1986  CG  LEU A1138      51.196  13.577  19.297  1.00 77.50           C  
ANISOU 1986  CG  LEU A1138    10237   9013  10196   2035  -1544   1493       C  
ATOM   1987  CD1 LEU A1138      51.258  13.296  20.787  1.00 81.14           C  
ANISOU 1987  CD1 LEU A1138    10696   9613  10520   2325  -1717   2029       C  
ATOM   1988  CD2 LEU A1138      51.265  15.072  19.026  1.00 65.56           C  
ANISOU 1988  CD2 LEU A1138     9130   7727   8053   1927  -1848   1182       C  
ATOM   1989  N   ASP A1139      53.446  11.565  15.386  1.00 80.57           N  
ANISOU 1989  N   ASP A1139     9577   8542  12492   1299   -710    378       N  
ATOM   1990  CA  ASP A1139      54.650  11.182  14.659  1.00 87.09           C  
ANISOU 1990  CA  ASP A1139    10033   9260  13798   1154   -580     99       C  
ATOM   1991  C   ASP A1139      55.232  12.381  13.917  1.00 84.87           C  
ANISOU 1991  C   ASP A1139     9952   9215  13078    819   -662   -262       C  
ATOM   1992  O   ASP A1139      54.494  13.157  13.309  1.00 91.12           O  
ANISOU 1992  O   ASP A1139    11133  10095  13391    616   -665   -489       O  
ATOM   1993  CB  ASP A1139      54.348  10.050  13.675  1.00 88.42           C  
ANISOU 1993  CB  ASP A1139     9926   9112  14558   1103   -199   -173       C  
ATOM   1994  CG  ASP A1139      55.590   9.272  13.285  1.00 95.81           C  
ANISOU 1994  CG  ASP A1139    10352   9897  16153   1111    -72   -365       C  
ATOM   1995  OD1 ASP A1139      56.412   9.805  12.508  1.00 96.34           O  
ANISOU 1995  OD1 ASP A1139    10340  10123  16141    858      5   -743       O  
ATOM   1996  OD2 ASP A1139      55.742   8.127  13.758  1.00100.03           O  
ANISOU 1996  OD2 ASP A1139    10559  10158  17290   1364    -63   -142       O  
ATOM   1997  N   ASP A1140      56.553  12.532  13.970  1.00 77.55           N  
ANISOU 1997  N   ASP A1140     8758   8382  12326    746   -756   -308       N  
ATOM   1998  CA  ASP A1140      57.219  13.646  13.301  1.00 79.90           C  
ANISOU 1998  CA  ASP A1140     9210   8920  12230    375   -845   -606       C  
ATOM   1999  C   ASP A1140      57.015  13.597  11.787  1.00 72.79           C  
ANISOU 1999  C   ASP A1140     8329   7975  11352     19   -485  -1113       C  
ATOM   2000  O   ASP A1140      57.019  14.629  11.115  1.00 71.11           O  
ANISOU 2000  O   ASP A1140     8452   7936  10632   -343   -562  -1348       O  
ATOM   2001  CB  ASP A1140      58.714  13.653  13.629  1.00 92.49           C  
ANISOU 2001  CB  ASP A1140    10407  10619  14117    360   -972   -560       C  
ATOM   2002  CG  ASP A1140      58.991  14.011  15.077  1.00107.34           C  
ANISOU 2002  CG  ASP A1140    12385  12581  15819    642  -1420    -83       C  
ATOM   2003  OD1 ASP A1140      58.198  13.608  15.954  1.00117.54           O  
ANISOU 2003  OD1 ASP A1140    13815  13768  17078    963  -1510    266       O  
ATOM   2004  OD2 ASP A1140      60.001  14.698  15.340  1.00111.51           O  
ANISOU 2004  OD2 ASP A1140    12855  13287  16226    524  -1685    -52       O  
ATOM   2005  N   ARG A1141      56.839  12.392  11.258  1.00 73.85           N  
ANISOU 2005  N   ARG A1141     8130   7859  12069    115   -126  -1276       N  
ATOM   2006  CA  ARG A1141      56.599  12.196   9.835  1.00 68.86           C  
ANISOU 2006  CA  ARG A1141     7512   7157  11494   -183    232  -1766       C  
ATOM   2007  C   ARG A1141      55.107  12.291   9.534  1.00 78.66           C  
ANISOU 2007  C   ARG A1141     9189   8257  12443   -186    256  -1789       C  
ATOM   2008  O   ARG A1141      54.309  11.504  10.047  1.00 71.16           O  
ANISOU 2008  O   ARG A1141     8179   7088  11770    115    289  -1554       O  
ATOM   2009  CB  ARG A1141      57.151  10.841   9.386  1.00 82.41           C  
ANISOU 2009  CB  ARG A1141     8655   8655  14002    -50    575  -1980       C  
ATOM   2010  CG  ARG A1141      58.594  10.611   9.789  1.00 86.52           C  
ANISOU 2010  CG  ARG A1141     8666   9285  14922     33    527  -1957       C  
ATOM   2011  CD  ARG A1141      58.928   9.134   9.823  1.00 97.99           C  
ANISOU 2011  CD  ARG A1141     9570  10428  17232    353    713  -2017       C  
ATOM   2012  NE  ARG A1141      58.153   8.428  10.841  1.00100.82           N  
ANISOU 2012  NE  ARG A1141     9987  10495  17822    733    527  -1544       N  
ATOM   2013  CZ  ARG A1141      58.331   7.150  11.166  1.00 97.92           C  
ANISOU 2013  CZ  ARG A1141     9224   9796  18186   1053    549  -1443       C  
ATOM   2014  NH1 ARG A1141      59.266   6.430  10.557  1.00105.49           N  
ANISOU 2014  NH1 ARG A1141     9671  10663  19748   1092    740  -1830       N  
ATOM   2015  NH2 ARG A1141      57.578   6.594  12.107  1.00 89.21           N  
ANISOU 2015  NH2 ARG A1141     8232   8456  17206   1326    365   -962       N  
ATOM   2016  N   ALA A1142      54.736  13.257   8.701  1.00 76.88           N  
ANISOU 2016  N   ALA A1142     9397   8149  11664   -546    215  -2066       N  
ATOM   2017  CA  ALA A1142      53.333  13.514   8.399  1.00 70.66           C  
ANISOU 2017  CA  ALA A1142     9050   7238  10559   -562    167  -2121       C  
ATOM   2018  C   ALA A1142      52.692  12.351   7.647  1.00 72.15           C  
ANISOU 2018  C   ALA A1142     9059   7115  11241   -506    526  -2336       C  
ATOM   2019  O   ALA A1142      51.491  12.107   7.776  1.00 72.95           O  
ANISOU 2019  O   ALA A1142     9336   7047  11335   -356    505  -2243       O  
ATOM   2020  CB  ALA A1142      53.194  14.800   7.595  1.00 58.76           C  
ANISOU 2020  CB  ALA A1142     8058   5884   8384   -988    -11  -2396       C  
ATOM   2021  N   TRP A1143      53.492  11.640   6.859  1.00 63.80           N  
ANISOU 2021  N   TRP A1143     7637   5989  10617   -623    846  -2644       N  
ATOM   2022  CA  TRP A1143      52.970  10.544   6.052  1.00 69.70           C  
ANISOU 2022  CA  TRP A1143     8227   6421  11837   -580   1163  -2907       C  
ATOM   2023  C   TRP A1143      52.579   9.356   6.927  1.00 68.75           C  
ANISOU 2023  C   TRP A1143     7780   6024  12320   -145   1176  -2556       C  
ATOM   2024  O   TRP A1143      51.708   8.572   6.567  1.00 65.74           O  
ANISOU 2024  O   TRP A1143     7394   5343  12243    -58   1309  -2619       O  
ATOM   2025  CB  TRP A1143      53.992  10.111   4.998  1.00 72.44           C  
ANISOU 2025  CB  TRP A1143     8252   6802  12470   -795   1500  -3374       C  
ATOM   2026  CG  TRP A1143      55.250   9.513   5.559  1.00 84.13           C  
ANISOU 2026  CG  TRP A1143     9154   8348  14464   -588   1561  -3288       C  
ATOM   2027  CD1 TRP A1143      56.392  10.178   5.906  1.00 82.25           C  
ANISOU 2027  CD1 TRP A1143     8762   8432  14055   -707   1455  -3235       C  
ATOM   2028  CD2 TRP A1143      55.498   8.125   5.826  1.00 90.70           C  
ANISOU 2028  CD2 TRP A1143     9479   8888  16096   -226   1697  -3257       C  
ATOM   2029  NE1 TRP A1143      57.331   9.292   6.377  1.00 88.12           N  
ANISOU 2029  NE1 TRP A1143     8916   9112  15453   -425   1522  -3187       N  
ATOM   2030  CE2 TRP A1143      56.809   8.026   6.337  1.00 93.96           C  
ANISOU 2030  CE2 TRP A1143     9443   9465  16795   -121   1656  -3203       C  
ATOM   2031  CE3 TRP A1143      54.740   6.959   5.685  1.00 97.73           C  
ANISOU 2031  CE3 TRP A1143    10258   9369  17507     13   1807  -3266       C  
ATOM   2032  CZ2 TRP A1143      57.377   6.806   6.707  1.00101.57           C  
ANISOU 2032  CZ2 TRP A1143     9861  10182  18548    236   1702  -3176       C  
ATOM   2033  CZ3 TRP A1143      55.306   5.747   6.054  1.00 99.57           C  
ANISOU 2033  CZ3 TRP A1143     9970   9350  18511    348   1847  -3218       C  
ATOM   2034  CH2 TRP A1143      56.611   5.681   6.559  1.00104.28           C  
ANISOU 2034  CH2 TRP A1143    10137  10104  19379    467   1786  -3182       C  
ATOM   2035  N   ARG A1144      53.225   9.252   8.084  1.00 74.24           N  
ANISOU 2035  N   ARG A1144     8227   6810  13170    102   1003  -2167       N  
ATOM   2036  CA  ARG A1144      53.052   8.123   8.988  1.00 69.18           C  
ANISOU 2036  CA  ARG A1144     7271   5916  13100    480    973  -1784       C  
ATOM   2037  C   ARG A1144      51.846   8.330   9.898  1.00 66.57           C  
ANISOU 2037  C   ARG A1144     7233   5586  12475    642    780  -1347       C  
ATOM   2038  O   ARG A1144      51.334   7.383  10.492  1.00 67.85           O  
ANISOU 2038  O   ARG A1144     7227   5514  13039    879    787  -1029       O  
ATOM   2039  CB  ARG A1144      54.328   7.921   9.817  1.00 76.73           C  
ANISOU 2039  CB  ARG A1144     7846   6960  14346    660    839  -1566       C  
ATOM   2040  CG  ARG A1144      54.427   6.603  10.574  1.00 92.26           C  
ANISOU 2040  CG  ARG A1144     9431   8602  17021   1017    798  -1241       C  
ATOM   2041  CD  ARG A1144      54.602   5.416   9.635  1.00100.34           C  
ANISOU 2041  CD  ARG A1144    10103   9280  18740   1054   1068  -1626       C  
ATOM   2042  NE  ARG A1144      54.981   4.201  10.353  1.00 98.74           N  
ANISOU 2042  NE  ARG A1144     9504   8750  19264   1389    949  -1346       N  
ATOM   2043  CZ  ARG A1144      56.230   3.759  10.463  1.00101.11           C  
ANISOU 2043  CZ  ARG A1144     9359   9008  20048   1531    904  -1466       C  
ATOM   2044  NH1 ARG A1144      57.219   4.428   9.896  1.00 85.96           N  
ANISOU 2044  NH1 ARG A1144     7303   7400  17958   1348   1017  -1859       N  
ATOM   2045  NH2 ARG A1144      56.489   2.643  11.134  1.00117.38           N  
ANISOU 2045  NH2 ARG A1144    11107  10715  22779   1843    726  -1194       N  
ATOM   2046  N   ARG A1145      51.392   9.574  10.002  1.00 64.95           N  
ANISOU 2046  N   ARG A1145     7462   5652  11564    504    596  -1342       N  
ATOM   2047  CA  ARG A1145      50.226   9.894  10.824  1.00 68.37           C  
ANISOU 2047  CA  ARG A1145     8166   6157  11655    662    425  -1004       C  
ATOM   2048  C   ARG A1145      48.943   9.308  10.249  1.00 67.71           C  
ANISOU 2048  C   ARG A1145     8152   5820  11754    646    599  -1116       C  
ATOM   2049  O   ARG A1145      48.760   9.274   9.032  1.00 72.80           O  
ANISOU 2049  O   ARG A1145     8888   6319  12455    420    758  -1552       O  
ATOM   2050  CB  ARG A1145      50.059  11.407  10.968  1.00 63.74           C  
ANISOU 2050  CB  ARG A1145     8035   5897  10287    535    147  -1062       C  
ATOM   2051  CG  ARG A1145      51.215  12.111  11.636  1.00 64.49           C  
ANISOU 2051  CG  ARG A1145     8116   6250  10138    546    -95   -910       C  
ATOM   2052  CD  ARG A1145      50.910  13.580  11.858  1.00 59.42           C  
ANISOU 2052  CD  ARG A1145     7962   5883   8730    454   -437   -942       C  
ATOM   2053  NE  ARG A1145      52.106  14.299  12.281  1.00 70.01           N  
ANISOU 2053  NE  ARG A1145     9305   7440   9856    389   -684   -862       N  
ATOM   2054  CZ  ARG A1145      52.587  15.371  11.664  1.00 71.28           C  
ANISOU 2054  CZ  ARG A1145     9738   7746   9598     65   -856  -1126       C  
ATOM   2055  NH1 ARG A1145      51.956  15.867  10.608  1.00 72.63           N  
ANISOU 2055  NH1 ARG A1145    10242   7863   9490   -218   -827  -1483       N  
ATOM   2056  NH2 ARG A1145      53.690  15.954  12.109  1.00 71.04           N  
ANISOU 2056  NH2 ARG A1145     9664   7901   9426      3  -1090  -1016       N  
ATOM   2057  N   PRO A1146      48.042   8.852  11.128  1.00 65.45           N  
ANISOU 2057  N   PRO A1146     7827   5494  11546    866    564   -716       N  
ATOM   2058  CA  PRO A1146      46.722   8.400  10.684  1.00 62.86           C  
ANISOU 2058  CA  PRO A1146     7566   4964  11355    842    692   -785       C  
ATOM   2059  C   PRO A1146      45.847   9.565  10.246  1.00 57.51           C  
ANISOU 2059  C   PRO A1146     7324   4465  10062    702    564  -1050       C  
ATOM   2060  O   PRO A1146      46.075  10.701  10.669  1.00 64.15           O  
ANISOU 2060  O   PRO A1146     8426   5618  10331    701    328  -1036       O  
ATOM   2061  CB  PRO A1146      46.143   7.727  11.929  1.00 65.04           C  
ANISOU 2061  CB  PRO A1146     7664   5245  11800   1089    668   -219       C  
ATOM   2062  CG  PRO A1146      46.840   8.382  13.067  1.00 67.77           C  
ANISOU 2062  CG  PRO A1146     8064   5925  11762   1234    449     97       C  
ATOM   2063  CD  PRO A1146      48.228   8.687  12.580  1.00 66.25           C  
ANISOU 2063  CD  PRO A1146     7808   5742  11624   1128    409   -168       C  
ATOM   2064  N   THR A1147      44.870   9.289   9.391  1.00 59.39           N  
ANISOU 2064  N   THR A1147     7650   4479  10437    591    673  -1306       N  
ATOM   2065  CA  THR A1147      43.851  10.279   9.075  1.00 61.49           C  
ANISOU 2065  CA  THR A1147     8305   4866  10191    507    506  -1526       C  
ATOM   2066  C   THR A1147      42.800  10.213  10.174  1.00 57.90           C  
ANISOU 2066  C   THR A1147     7785   4577   9636    751    453  -1144       C  
ATOM   2067  O   THR A1147      42.698   9.203  10.875  1.00 61.61           O  
ANISOU 2067  O   THR A1147     7924   4969  10516    902    601   -750       O  
ATOM   2068  CB  THR A1147      43.209  10.033   7.700  1.00 63.87           C  
ANISOU 2068  CB  THR A1147     8741   4849  10676    285    609  -1969       C  
ATOM   2069  OG1 THR A1147      42.406   8.849   7.755  1.00 75.34           O  
ANISOU 2069  OG1 THR A1147     9913   6026  12686    389    791  -1803       O  
ATOM   2070  CG2 THR A1147      44.282   9.864   6.640  1.00 61.66           C  
ANISOU 2070  CG2 THR A1147     8453   4424  10552     47    746  -2328       C  
ATOM   2071  N   MET A1148      42.033  11.285  10.339  1.00 63.34           N  
ANISOU 2071  N   MET A1148     8786   5503   9776    785    231  -1262       N  
ATOM   2072  CA  MET A1148      41.050  11.342  11.416  1.00 59.63           C  
ANISOU 2072  CA  MET A1148     8240   5284   9133   1027    197   -948       C  
ATOM   2073  C   MET A1148      39.988  10.254  11.265  1.00 64.29           C  
ANISOU 2073  C   MET A1148     8555   5645  10227   1032    434   -834       C  
ATOM   2074  O   MET A1148      39.417   9.803  12.258  1.00 67.72           O  
ANISOU 2074  O   MET A1148     8763   6249  10720   1196    528   -429       O  
ATOM   2075  CB  MET A1148      40.389  12.723  11.483  1.00 57.76           C  
ANISOU 2075  CB  MET A1148     8384   5318   8242   1082   -115  -1205       C  
ATOM   2076  CG  MET A1148      41.324  13.851  11.914  1.00 50.31           C  
ANISOU 2076  CG  MET A1148     7719   4641   6754   1116   -414  -1226       C  
ATOM   2077  SD  MET A1148      42.322  13.463  13.369  1.00 63.47           S  
ANISOU 2077  SD  MET A1148     9127   6556   8433   1339   -366   -657       S  
ATOM   2078  CE  MET A1148      41.070  13.171  14.606  1.00 54.39           C  
ANISOU 2078  CE  MET A1148     7796   5704   7164   1640   -271   -292       C  
ATOM   2079  N   VAL A1149      39.733   9.829  10.028  1.00 56.28           N  
ANISOU 2079  N   VAL A1149     7569   4253   9563    831    522  -1179       N  
ATOM   2080  CA  VAL A1149      38.866   8.675   9.773  1.00 63.98           C  
ANISOU 2080  CA  VAL A1149     8268   4928  11112    803    726  -1077       C  
ATOM   2081  C   VAL A1149      39.471   7.389  10.354  1.00 76.47           C  
ANISOU 2081  C   VAL A1149     9466   6346  13244    869    921   -631       C  
ATOM   2082  O   VAL A1149      38.768   6.571  10.952  1.00 81.36           O  
ANISOU 2082  O   VAL A1149     9818   6923  14169    931   1037   -256       O  
ATOM   2083  CB  VAL A1149      38.607   8.478   8.260  1.00 61.01           C  
ANISOU 2083  CB  VAL A1149     8042   4141  10996    573    745  -1574       C  
ATOM   2084  CG1 VAL A1149      37.904   7.161   8.004  1.00 66.06           C  
ANISOU 2084  CG1 VAL A1149     8377   4413  12309    543    933  -1444       C  
ATOM   2085  CG2 VAL A1149      37.780   9.615   7.713  1.00 65.69           C  
ANISOU 2085  CG2 VAL A1149     9011   4829  11119    506    505  -1972       C  
ATOM   2086  N   GLN A1150      40.779   7.215  10.182  1.00 74.82           N  
ANISOU 2086  N   GLN A1150     9220   6040  13167    844    936   -671       N  
ATOM   2087  CA  GLN A1150      41.465   6.069  10.770  1.00 70.37           C  
ANISOU 2087  CA  GLN A1150     8311   5304  13125    938   1043   -272       C  
ATOM   2088  C   GLN A1150      41.458   6.172  12.291  1.00 77.96           C  
ANISOU 2088  C   GLN A1150     9179   6614  13828   1129    979    291       C  
ATOM   2089  O   GLN A1150      41.363   5.162  12.989  1.00 66.47           O  
ANISOU 2089  O   GLN A1150     7457   5037  12762   1195   1049    750       O  
ATOM   2090  CB  GLN A1150      42.899   5.967  10.257  1.00 67.62           C  
ANISOU 2090  CB  GLN A1150     7917   4822  12954    894   1054   -499       C  
ATOM   2091  CG  GLN A1150      43.041   5.391   8.857  1.00 66.18           C  
ANISOU 2091  CG  GLN A1150     7708   4234  13204    729   1187   -972       C  
ATOM   2092  CD  GLN A1150      44.461   5.511   8.337  1.00 64.44           C  
ANISOU 2092  CD  GLN A1150     7444   4007  13034    671   1223  -1266       C  
ATOM   2093  OE1 GLN A1150      45.100   6.558   8.482  1.00 67.04           O  
ANISOU 2093  OE1 GLN A1150     7956   4663  12851    623   1117  -1353       O  
ATOM   2094  NE2 GLN A1150      44.971   4.433   7.742  1.00 65.46           N  
ANISOU 2094  NE2 GLN A1150     7312   3901  13659    650   1331  -1388       N  
ATOM   2095  N   VAL A1151      41.565   7.398  12.798  1.00 61.56           N  
ANISOU 2095  N   VAL A1151     7351   4959  11078   1206    818    253       N  
ATOM   2096  CA  VAL A1151      41.473   7.639  14.232  1.00 62.93           C  
ANISOU 2096  CA  VAL A1151     7496   5519  10895   1397    745    734       C  
ATOM   2097  C   VAL A1151      40.103   7.195  14.752  1.00 66.84           C  
ANISOU 2097  C   VAL A1151     7848   6118  11430   1428    877   1015       C  
ATOM   2098  O   VAL A1151      40.016   6.463  15.737  1.00 71.37           O  
ANISOU 2098  O   VAL A1151     8211   6756  12151   1494    952   1546       O  
ATOM   2099  CB  VAL A1151      41.716   9.124  14.573  1.00 61.43           C  
ANISOU 2099  CB  VAL A1151     7640   5748   9951   1485    508    557       C  
ATOM   2100  CG1 VAL A1151      41.394   9.402  16.029  1.00 62.28           C  
ANISOU 2100  CG1 VAL A1151     7745   6286   9634   1701    444    999       C  
ATOM   2101  CG2 VAL A1151      43.157   9.505  14.259  1.00 62.23           C  
ANISOU 2101  CG2 VAL A1151     7831   5793  10021   1430    376    389       C  
ATOM   2102  N   MET A1152      39.040   7.635  14.082  1.00 64.00           N  
ANISOU 2102  N   MET A1152     7599   5774  10943   1359    894    663       N  
ATOM   2103  CA  MET A1152      37.679   7.240  14.443  1.00 74.07           C  
ANISOU 2103  CA  MET A1152     8692   7157  12294   1361   1034    862       C  
ATOM   2104  C   MET A1152      37.522   5.720  14.421  1.00 84.18           C  
ANISOU 2104  C   MET A1152     9637   8050  14299   1242   1219   1224       C  
ATOM   2105  O   MET A1152      36.963   5.126  15.344  1.00 88.35           O  
ANISOU 2105  O   MET A1152     9945   8733  14893   1254   1336   1721       O  
ATOM   2106  CB  MET A1152      36.656   7.881  13.497  1.00 72.57           C  
ANISOU 2106  CB  MET A1152     8660   6935  11980   1291    979    342       C  
ATOM   2107  CG  MET A1152      36.490   9.395  13.650  1.00 63.90           C  
ANISOU 2107  CG  MET A1152     7891   6235  10153   1428    741     15       C  
ATOM   2108  SD  MET A1152      35.806   9.842  15.248  1.00 75.37           S  
ANISOU 2108  SD  MET A1152     9234   8339  11065   1687    770    391       S  
ATOM   2109  CE  MET A1152      34.096   9.340  15.047  1.00 81.04           C  
ANISOU 2109  CE  MET A1152     9657   9071  12065   1625    966    355       C  
ATOM   2110  N   ALA A1153      38.028   5.100  13.361  1.00 78.07           N  
ANISOU 2110  N   ALA A1153     8837   6774  14052   1117   1232    968       N  
ATOM   2111  CA  ALA A1153      37.969   3.652  13.221  1.00 81.43           C  
ANISOU 2111  CA  ALA A1153     8977   6748  15217   1019   1339   1245       C  
ATOM   2112  C   ALA A1153      38.708   2.964  14.364  1.00 85.05           C  
ANISOU 2112  C   ALA A1153     9260   7234  15820   1106   1320   1844       C  
ATOM   2113  O   ALA A1153      38.245   1.955  14.897  1.00 83.60           O  
ANISOU 2113  O   ALA A1153     8848   6909  16008   1040   1383   2320       O  
ATOM   2114  CB  ALA A1153      38.546   3.226  11.884  1.00 84.64           C  
ANISOU 2114  CB  ALA A1153     9418   6647  16094    920   1330    785       C  
ATOM   2115  N   MET A1154      39.852   3.525  14.742  1.00 86.78           N  
ANISOU 2115  N   MET A1154     9602   7628  15743   1234   1201   1833       N  
ATOM   2116  CA  MET A1154      40.648   2.987  15.840  1.00 88.90           C  
ANISOU 2116  CA  MET A1154     9748   7922  16108   1335   1120   2374       C  
ATOM   2117  C   MET A1154      39.919   3.120  17.176  1.00 87.77           C  
ANISOU 2117  C   MET A1154     9588   8228  15532   1380   1158   2917       C  
ATOM   2118  O   MET A1154      40.019   2.240  18.031  1.00 83.80           O  
ANISOU 2118  O   MET A1154     8931   7645  15265   1363   1142   3491       O  
ATOM   2119  CB  MET A1154      42.015   3.680  15.897  1.00 74.23           C  
ANISOU 2119  CB  MET A1154     8025   6175  14004   1457    962   2189       C  
ATOM   2120  CG  MET A1154      43.006   3.160  14.860  1.00 74.08           C  
ANISOU 2120  CG  MET A1154     7902   5699  14545   1419    948   1818       C  
ATOM   2121  SD  MET A1154      44.279   4.349  14.389  1.00115.92           S  
ANISOU 2121  SD  MET A1154    13395  11207  19443   1453    837   1337       S  
ATOM   2122  CE  MET A1154      45.078   4.648  15.961  1.00 72.74           C  
ANISOU 2122  CE  MET A1154     7933   6069  13636   1649    625   1882       C  
ATOM   2123  N   PHE A1155      39.181   4.213  17.348  1.00 82.74           N  
ANISOU 2123  N   PHE A1155     9116   8065  14257   1433   1193   2726       N  
ATOM   2124  CA  PHE A1155      38.411   4.421  18.572  1.00 89.17           C  
ANISOU 2124  CA  PHE A1155     9900   9383  14596   1488   1270   3159       C  
ATOM   2125  C   PHE A1155      37.285   3.404  18.694  1.00 90.88           C  
ANISOU 2125  C   PHE A1155     9843   9491  15195   1304   1471   3505       C  
ATOM   2126  O   PHE A1155      36.973   2.938  19.790  1.00 85.89           O  
ANISOU 2126  O   PHE A1155     9093   9096  14445   1265   1549   4087       O  
ATOM   2127  CB  PHE A1155      37.837   5.836  18.620  1.00 75.67           C  
ANISOU 2127  CB  PHE A1155     8410   8181  12161   1621   1239   2773       C  
ATOM   2128  CG  PHE A1155      38.837   6.881  19.011  1.00 85.07           C  
ANISOU 2128  CG  PHE A1155     9877   9626  12818   1808   1011   2640       C  
ATOM   2129  CD1 PHE A1155      40.026   6.523  19.628  1.00 85.56           C  
ANISOU 2129  CD1 PHE A1155     9941   9594  12974   1866    886   2986       C  
ATOM   2130  CD2 PHE A1155      38.590   8.222  18.765  1.00 70.55           C  
ANISOU 2130  CD2 PHE A1155     8304   8095  10409   1924    876   2170       C  
ATOM   2131  CE1 PHE A1155      40.953   7.485  19.989  1.00 87.62           C  
ANISOU 2131  CE1 PHE A1155    10446  10077  12768   2023    651   2871       C  
ATOM   2132  CE2 PHE A1155      39.511   9.188  19.125  1.00 68.95           C  
ANISOU 2132  CE2 PHE A1155     8370   8101   9729   2074    624   2062       C  
ATOM   2133  CZ  PHE A1155      40.695   8.820  19.737  1.00 82.13           C  
ANISOU 2133  CZ  PHE A1155    10020   9688  11497   2118    522   2417       C  
ATOM   2134  N   LYS A1156      36.680   3.075  17.558  1.00 88.70           N  
ANISOU 2134  N   LYS A1156     9481   8859  15362   1167   1541   3150       N  
ATOM   2135  CA  LYS A1156      35.574   2.133  17.509  1.00 94.45           C  
ANISOU 2135  CA  LYS A1156     9942   9432  16514    963   1703   3419       C  
ATOM   2136  C   LYS A1156      36.045   0.708  17.803  1.00101.10           C  
ANISOU 2136  C   LYS A1156    10602   9811  18001    830   1660   3955       C  
ATOM   2137  O   LYS A1156      35.342  -0.064  18.456  1.00107.39           O  
ANISOU 2137  O   LYS A1156    11197  10652  18955    660   1761   4491       O  
ATOM   2138  CB  LYS A1156      34.886   2.199  16.142  1.00 97.66           C  
ANISOU 2138  CB  LYS A1156    10344   9524  17238    865   1727   2850       C  
ATOM   2139  CG  LYS A1156      33.678   1.284  16.009  1.00111.53           C  
ANISOU 2139  CG  LYS A1156    11814  11105  19456    643   1866   3082       C  
ATOM   2140  CD  LYS A1156      33.093   1.308  14.604  1.00115.99           C  
ANISOU 2140  CD  LYS A1156    12407  11288  20375    554   1836   2503       C  
ATOM   2141  CE  LYS A1156      31.932   0.325  14.483  1.00122.35           C  
ANISOU 2141  CE  LYS A1156    12907  11875  21707    317   1940   2764       C  
ATOM   2142  NZ  LYS A1156      31.391   0.247  13.098  1.00121.70           N  
ANISOU 2142  NZ  LYS A1156    12866  11351  22024    228   1869   2217       N  
ATOM   2143  N   GLU A1157      37.241   0.368  17.332  1.00103.43           N  
ANISOU 2143  N   GLU A1157    10961   9669  18667    901   1493   3808       N  
ATOM   2144  CA  GLU A1157      37.783  -0.978  17.514  1.00110.60           C  
ANISOU 2144  CA  GLU A1157    11711  10060  20253    819   1376   4234       C  
ATOM   2145  C   GLU A1157      38.093  -1.319  18.970  1.00110.09           C  
ANISOU 2145  C   GLU A1157    11627  10226  19978    826   1303   4965       C  
ATOM   2146  O   GLU A1157      38.189  -2.492  19.324  1.00122.78           O  
ANISOU 2146  O   GLU A1157    13098  11452  22099    698   1196   5459       O  
ATOM   2147  CB  GLU A1157      39.054  -1.162  16.681  1.00112.28           C  
ANISOU 2147  CB  GLU A1157    11969   9812  20879    942   1214   3824       C  
ATOM   2148  CG  GLU A1157      38.824  -1.758  15.302  1.00116.75           C  
ANISOU 2148  CG  GLU A1157    12458   9827  22073    849   1232   3362       C  
ATOM   2149  CD  GLU A1157      40.118  -2.182  14.632  1.00123.31           C  
ANISOU 2149  CD  GLU A1157    13266  10208  23380    970   1090   3037       C  
ATOM   2150  OE1 GLU A1157      41.193  -1.714  15.064  1.00127.82           O  
ANISOU 2150  OE1 GLU A1157    13900  10963  23703   1130    997   3034       O  
ATOM   2151  OE2 GLU A1157      40.062  -2.987  13.678  1.00125.98           O  
ANISOU 2151  OE2 GLU A1157    13510  10266  24090    862   1044   2673       O  
ATOM   2152  N   ILE A1158      38.248  -0.302  19.811  1.00101.62           N  
ANISOU 2152  N   ILE A1158    10716   9750  18145    969   1326   5035       N  
ATOM   2153  CA  ILE A1158      38.695  -0.522  21.183  1.00113.45           C  
ANISOU 2153  CA  ILE A1158    12260  11477  19371    998   1222   5686       C  
ATOM   2154  C   ILE A1158      37.586  -1.032  22.106  1.00141.45           C  
ANISOU 2154  C   ILE A1158    15679  15317  22747    773   1394   6313       C  
ATOM   2155  O   ILE A1158      37.789  -1.992  22.853  1.00153.59           O  
ANISOU 2155  O   ILE A1158    17166  16660  24533    634   1280   6956       O  
ATOM   2156  CB  ILE A1158      39.300   0.763  21.776  1.00105.01           C  
ANISOU 2156  CB  ILE A1158    11435  10939  17527   1242   1154   5527       C  
ATOM   2157  CG1 ILE A1158      40.590   1.119  21.036  1.00 96.03           C  
ANISOU 2157  CG1 ILE A1158    10395   9496  16594   1413    953   5047       C  
ATOM   2158  CG2 ILE A1158      39.584   0.592  23.259  1.00 99.36           C  
ANISOU 2158  CG2 ILE A1158    10797  10524  16430   1261   1061   6212       C  
ATOM   2159  CD1 ILE A1158      41.262   2.377  21.534  1.00 95.41           C  
ANISOU 2159  CD1 ILE A1158    10563   9874  15816   1630    832   4877       C  
ATOM   2160  N   GLN A1159      36.415  -0.405  22.050  1.00153.91           N  
ANISOU 2160  N   GLN A1159    17199  17364  23915    723   1655   6128       N  
ATOM   2161  CA  GLN A1159      35.322  -0.780  22.946  1.00166.25           C  
ANISOU 2161  CA  GLN A1159    18600  19326  25242    498   1875   6684       C  
ATOM   2162  C   GLN A1159      34.419  -1.874  22.370  1.00171.27           C  
ANISOU 2162  C   GLN A1159    18959  19549  26564    179   1972   6851       C  
ATOM   2163  O   GLN A1159      33.892  -2.704  23.113  1.00175.36           O  
ANISOU 2163  O   GLN A1159    19333  20124  27174    -99   2046   7512       O  
ATOM   2164  CB  GLN A1159      34.489   0.453  23.303  1.00164.58           C  
ANISOU 2164  CB  GLN A1159    18416  19895  24221    628   2107   6404       C  
ATOM   2165  CG  GLN A1159      35.178   1.413  24.268  1.00163.62           C  
ANISOU 2165  CG  GLN A1159    18559  20290  23318    894   2017   6448       C  
ATOM   2166  CD  GLN A1159      35.279   0.865  25.685  1.00170.69           C  
ANISOU 2166  CD  GLN A1159    19474  21468  23911    769   2036   7249       C  
ATOM   2167  OE1 GLN A1159      36.001  -0.098  25.946  1.00171.66           O  
ANISOU 2167  OE1 GLN A1159    19624  21131  24468    647   1835   7724       O  
ATOM   2168  NE2 GLN A1159      34.553   1.485  26.609  1.00173.93           N  
ANISOU 2168  NE2 GLN A1159    19881  22641  23562    804   2261   7387       N  
ATOM   2169  N   ALA A1160      34.240  -1.874  21.053  1.00168.47           N  
ANISOU 2169  N   ALA A1160    18553  18780  26680    197   1952   6268       N  
ATOM   2170  CA  ALA A1160      33.414  -2.883  20.400  1.00167.98           C  
ANISOU 2170  CA  ALA A1160    18249  18267  27310    -86   1995   6361       C  
ATOM   2171  C   ALA A1160      33.896  -3.156  18.979  1.00161.75           C  
ANISOU 2171  C   ALA A1160    17505  16782  27169    -10   1824   5780       C  
ATOM   2172  O   ALA A1160      34.610  -4.129  18.732  1.00161.83           O  
ANISOU 2172  O   ALA A1160    17507  16176  27805    -46   1604   5938       O  
ATOM   2173  CB  ALA A1160      31.955  -2.451  20.391  1.00168.01           C  
ANISOU 2173  CB  ALA A1160    18051  18758  27028   -216   2287   6256       C  
TER    2174      ALA A1160                                                      
HETATM 2175  O   HOH A1201      19.659  42.431  20.677  1.00 66.24           O  
HETATM 2176  O   HOH A1202      47.488  22.188  13.594  1.00 52.92           O  
HETATM 2177  O   HOH A1203      41.273  28.334  13.297  1.00 52.37           O  
HETATM 2178  O   HOH A1204      46.885  22.355  11.168  1.00 54.78           O  
HETATM 2179  O   HOH A1205      45.378  22.174  13.803  1.00 50.03           O  
HETATM 2180  O   HOH A1206      42.140  13.416   8.467  1.00 60.84           O  
HETATM 2181  O   HOH A1207      30.566  29.761  24.384  1.00 64.22           O  
HETATM 2182  O   HOH A1208      32.850  29.887  19.645  1.00 68.84           O  
HETATM 2183  O   HOH A1209      45.477  29.249  24.135  1.00 74.09           O  
HETATM 2184  O   HOH A1210      33.873  31.430  20.677  1.00 68.43           O  
CONECT 1294 1300                                                                
CONECT 1300 1294 1301                                                           
CONECT 1301 1300 1302 1309                                                      
CONECT 1302 1301 1303 1304                                                      
CONECT 1303 1302                                                                
CONECT 1304 1302 1305                                                           
CONECT 1305 1304 1306 1307 1308                                                 
CONECT 1306 1305                                                                
CONECT 1307 1305                                                                
CONECT 1308 1305                                                                
CONECT 1309 1301 1310 1311                                                      
CONECT 1310 1309                                                                
CONECT 1311 1309                                                                
CONECT 1323 1329                                                                
CONECT 1329 1323 1330                                                           
CONECT 1330 1329 1331 1333                                                      
CONECT 1331 1330 1332                                                           
CONECT 1332 1331 1335                                                           
CONECT 1333 1330 1334 1339                                                      
CONECT 1334 1333                                                                
CONECT 1335 1332 1336 1337 1338                                                 
CONECT 1336 1335                                                                
CONECT 1337 1335                                                                
CONECT 1338 1335                                                                
CONECT 1339 1333                                                                
CONECT 1341 1346                                                                
CONECT 1346 1341 1347                                                           
CONECT 1347 1346 1348 1350                                                      
CONECT 1348 1347 1349                                                           
CONECT 1349 1348 1352                                                           
CONECT 1350 1347 1351 1356                                                      
CONECT 1351 1350                                                                
CONECT 1352 1349 1353 1354 1355                                                 
CONECT 1353 1352                                                                
CONECT 1354 1352                                                                
CONECT 1355 1352                                                                
CONECT 1356 1350                                                                
CONECT 1466 1473                                                                
CONECT 1473 1466 1474                                                           
CONECT 1474 1473 1475 1477                                                      
CONECT 1475 1474 1476                                                           
CONECT 1476 1475 1479                                                           
CONECT 1477 1474 1478 1483                                                      
CONECT 1478 1477                                                                
CONECT 1479 1476 1480 1481 1482                                                 
CONECT 1480 1479                                                                
CONECT 1481 1479                                                                
CONECT 1482 1479                                                                
CONECT 1483 1477                                                                
MASTER      362    0    4   13   11    0    0    6 2178    1   49   23          
END                                                                             



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