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***  Eutla_projet_1  ***

elNémo ID: 23010419095965391

Job options:

ID        	=	 23010419095965391
JOBID     	=	 Eutla_projet_1
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 Eutla_projet_1

HEADER    TRANSFERASE                             09-APR-19   6OID              
TITLE     REDOX REGULATION OF FN3K FROM ARABIDOPSIS THALIANA                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN-RIBULOSAMINE 3-KINASE, CHLOROPLASTIC;              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: FRUCTOSAMINE 3-KINASE-RELATED PROTEIN,ATFN3K-RP;            
COMPND   5 EC: 2.7.1.172;                                                       
COMPND   6 ENGINEERED: 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: AT3G61080, T27I15_170;                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008                                      
KEYWDS    KINASE, FRUCTOSAMINE-3-KINASE, SMALL MOLECULE KINASE, PROTEIN REPAIR, 
KEYWDS   2 PHOSPHOTRANSFERASE, DEGLYCATION, PLANT PROTEIN, TRANSFERASE          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Z.A.WOOD,R.KADIRVELRAJ,S.SHRESTHA                                     
REVDAT   2   23-SEP-20 6OID    1       JRNL                                     
REVDAT   1   20-MAY-20 6OID    0                                                
JRNL        AUTH   S.SHRESTHA,S.KATIYAR,C.E.SANZ-RODRIGUEZ,N.R.KEMPPINEN,       
JRNL        AUTH 2 H.W.KIM,R.KADIRVELRAJ,C.PANAGOS,N.KEYHANINEJAD,M.COLONNA,    
JRNL        AUTH 3 P.CHOPRA,D.P.BYRNE,G.J.BOONS,E.VAN DER KNAAP,P.A.EYERS,      
JRNL        AUTH 4 A.S.EDISON,Z.A.WOOD,N.KANNAN                                 
JRNL        TITL   A REDOX-ACTIVE SWITCH IN FRUCTOSAMINE-3-KINASES EXPANDS THE  
JRNL        TITL 2 REGULATORY REPERTOIRE OF THE PROTEIN KINASE SUPERFAMILY.     
JRNL        REF    SCI.SIGNAL.                   V.  13       2020              
JRNL        REFN                   ESSN 1937-9145                               
JRNL        PMID   32636308                                                     
JRNL        DOI    10.1126/SCISIGNAL.AAX6313                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.37 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.12_2829: ???)                              
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) : 2.37                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 53.50                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 37988                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.177                           
REMARK   3   R VALUE            (WORKING SET) : 0.175                           
REMARK   3   FREE R VALUE                     : 0.204                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.010                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1903                            
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 53.5177 -  5.6984    1.00     2737   146  0.1755 0.2120        
REMARK   3     2  5.6984 -  4.5238    1.00     2631   134  0.1411 0.1555        
REMARK   3     3  4.5238 -  3.9521    1.00     2605   136  0.1323 0.1441        
REMARK   3     4  3.9521 -  3.5909    1.00     2609   143  0.1498 0.1748        
REMARK   3     5  3.5909 -  3.3335    1.00     2579   135  0.1813 0.2273        
REMARK   3     6  3.3335 -  3.1370    1.00     2573   133  0.1927 0.2204        
REMARK   3     7  3.1370 -  2.9799    1.00     2555   138  0.2118 0.2365        
REMARK   3     8  2.9799 -  2.8502    1.00     2553   138  0.2131 0.2710        
REMARK   3     9  2.8502 -  2.7405    1.00     2583   127  0.2280 0.2610        
REMARK   3    10  2.7405 -  2.6459    1.00     2551   136  0.2230 0.2757        
REMARK   3    11  2.6459 -  2.5632    1.00     2558   138  0.2286 0.2572        
REMARK   3    12  2.5632 -  2.4899    1.00     2548   135  0.2393 0.2691        
REMARK   3    13  2.4899 -  2.4244    1.00     2546   134  0.2479 0.3004        
REMARK   3    14  2.4244 -  2.3652    0.97     2457   130  0.2841 0.3296        
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)     : 0.280            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.210           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.009           4850                                  
REMARK   3   ANGLE     :  1.071           6567                                  
REMARK   3   CHIRALITY :  0.068            650                                  
REMARK   3   PLANARITY :  0.006            834                                  
REMARK   3   DIHEDRAL  : 15.996           1741                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 8                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 7 THROUGH 43 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  63.9317   7.0554  35.1953              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8351 T22:   0.4531                                     
REMARK   3      T33:   0.6129 T12:   0.2789                                     
REMARK   3      T13:   0.2529 T23:   0.2477                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3761 L22:   1.5675                                     
REMARK   3      L33:   2.3304 L12:  -0.0719                                     
REMARK   3      L13:   0.2772 L23:  -1.1911                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4057 S12:  -0.4546 S13:  -0.6742                       
REMARK   3      S21:   0.4298 S22:   0.1249 S23:  -0.0578                       
REMARK   3      S31:   0.6753 S32:   0.6338 S33:   0.1822                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 44 THROUGH 106 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  63.3595  20.1511   9.0246              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4097 T22:   0.4611                                     
REMARK   3      T33:   0.3487 T12:  -0.0217                                     
REMARK   3      T13:   0.0134 T23:   0.0335                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1818 L22:   3.0098                                     
REMARK   3      L33:   2.9782 L12:   0.2337                                     
REMARK   3      L13:   0.3545 L23:   0.5394                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1371 S12:   0.1105 S13:  -0.1260                       
REMARK   3      S21:  -0.1320 S22:  -0.1104 S23:  -0.2539                       
REMARK   3      S31:  -0.0023 S32:  -0.0227 S33:  -0.0472                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 107 THROUGH 147 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  46.3738  21.9564   7.9324              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4471 T22:   0.4889                                     
REMARK   3      T33:   0.4529 T12:   0.0154                                     
REMARK   3      T13:  -0.0789 T23:   0.0449                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5838 L22:   3.2915                                     
REMARK   3      L33:   1.9710 L12:   0.2843                                     
REMARK   3      L13:  -0.1292 L23:  -0.0359                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0382 S12:   0.4696 S13:   0.0235                       
REMARK   3      S21:  -0.6829 S22:   0.1268 S23:   0.1613                       
REMARK   3      S31:   0.2151 S32:  -0.1321 S33:   0.0046                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 148 THROUGH 295 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  41.5914  23.1197  19.5088              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3966 T22:   0.3580                                     
REMARK   3      T33:   0.4446 T12:   0.0535                                     
REMARK   3      T13:  -0.0112 T23:   0.0723                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3892 L22:   2.0550                                     
REMARK   3      L33:   2.0557 L12:  -0.2604                                     
REMARK   3      L13:  -0.2250 L23:  -0.5700                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0131 S12:  -0.0743 S13:  -0.0544                       
REMARK   3      S21:   0.1087 S22:   0.1983 S23:   0.3896                       
REMARK   3      S31:   0.1210 S32:  -0.2211 S33:  -0.0034                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 7 THROUGH 43 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  69.7300  12.3302  17.8642              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4808 T22:   0.4392                                     
REMARK   3      T33:   0.5884 T12:   0.0793                                     
REMARK   3      T13:   0.0833 T23:   0.0219                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9463 L22:   1.2177                                     
REMARK   3      L33:   1.7715 L12:   0.5689                                     
REMARK   3      L13:  -1.1143 L23:  -0.3077                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2913 S12:   0.1910 S13:  -0.6194                       
REMARK   3      S21:   0.0273 S22:  -0.0469 S23:  -0.1306                       
REMARK   3      S31:   0.2664 S32:   0.3423 S33:   0.0791                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 44 THROUGH 106 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  58.7016  14.6744  45.1455              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6534 T22:   0.5165                                     
REMARK   3      T33:   0.4103 T12:   0.1881                                     
REMARK   3      T13:   0.0636 T23:   0.1341                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2127 L22:   2.6985                                     
REMARK   3      L33:   2.6185 L12:  -0.3181                                     
REMARK   3      L13:  -0.1885 L23:   0.6953                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4857 S12:  -0.8347 S13:  -0.1388                       
REMARK   3      S21:   0.4800 S22:   0.2499 S23:   0.0479                       
REMARK   3      S31:   0.4049 S32:   0.2247 S33:  -0.0149                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 107 THROUGH 147 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  61.2788  31.4117  47.1904              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6403 T22:   0.7424                                     
REMARK   3      T33:   0.4932 T12:   0.1505                                     
REMARK   3      T13:  -0.0119 T23:  -0.0967                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4413 L22:   1.6750                                     
REMARK   3      L33:   1.9948 L12:  -0.1870                                     
REMARK   3      L13:  -0.7576 L23:   0.3383                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2038 S12:  -1.0533 S13:  -0.0117                       
REMARK   3      S21:   0.3568 S22:   0.2444 S23:  -0.0261                       
REMARK   3      S31:   0.2416 S32:   0.6140 S33:  -0.1262                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 148 THROUGH 295 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  60.7677  37.1309  36.0376              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3804 T22:   0.4581                                     
REMARK   3      T33:   0.4160 T12:   0.0788                                     
REMARK   3      T13:   0.0066 T23:  -0.0832                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6323 L22:   1.8968                                     
REMARK   3      L33:   2.5005 L12:  -0.1357                                     
REMARK   3      L13:  -1.0298 L23:  -0.3515                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0752 S12:  -0.3201 S13:   0.4466                       
REMARK   3      S21:   0.0164 S22:   0.0913 S23:   0.0179                       
REMARK   3      S31:  -0.0580 S32:   0.4223 S33:  -0.1727                       
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 6OID COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-APR-19.                  
REMARK 100 THE DEPOSITION ID IS D_1000239627.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-NOV-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38000                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.350                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 53.504                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 14.50                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 14.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.37                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.43                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 14.60                              
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 3F7W, 3JR1, AND 5IGS                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2 M AMMONIUM SULFATE, 0.1 M MES PH       
REMARK 280  5.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       35.36000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       35.36000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       79.43000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       81.82000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       79.43000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       81.82000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       35.36000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       79.43000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       81.82000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       35.36000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       79.43000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       81.82000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 11070 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 24690 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -226.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -19                                                      
REMARK 465     GLY A   -18                                                      
REMARK 465     SER A   -17                                                      
REMARK 465     SER A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     HIS A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     SER A    -8                                                      
REMARK 465     GLY A    -7                                                      
REMARK 465     LEU A    -6                                                      
REMARK 465     VAL A    -5                                                      
REMARK 465     PRO A    -4                                                      
REMARK 465     ARG A    -3                                                      
REMARK 465     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     MET A     4                                                      
REMARK 465     SER A     5                                                      
REMARK 465     GLU A     6                                                      
REMARK 465     LYS A   296                                                      
REMARK 465     ALA A   297                                                      
REMARK 465     MET B   -19                                                      
REMARK 465     GLY B   -18                                                      
REMARK 465     SER B   -17                                                      
REMARK 465     SER B   -16                                                      
REMARK 465     HIS B   -15                                                      
REMARK 465     HIS B   -14                                                      
REMARK 465     HIS B   -13                                                      
REMARK 465     HIS B   -12                                                      
REMARK 465     HIS B   -11                                                      
REMARK 465     HIS B   -10                                                      
REMARK 465     SER B    -9                                                      
REMARK 465     SER B    -8                                                      
REMARK 465     GLY B    -7                                                      
REMARK 465     LEU B    -6                                                      
REMARK 465     VAL B    -5                                                      
REMARK 465     PRO B    -4                                                      
REMARK 465     ARG B    -3                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     SER B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     ALA B     3                                                      
REMARK 465     MET B     4                                                      
REMARK 465     SER B     5                                                      
REMARK 465     GLU B     6                                                      
REMARK 465     LYS B   296                                                      
REMARK 465     ALA B   297                                                      
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    THR A  15      -72.68    -78.64                                   
REMARK 500    THR A  74      -72.41   -122.96                                   
REMARK 500    ASN A 133     -151.10   -135.78                                   
REMARK 500    ARG A 156      -77.61   -118.42                                   
REMARK 500    ASP A 201       57.81   -155.74                                   
REMARK 500    THR B  15      -80.75    -94.60                                   
REMARK 500    THR B  74      -79.16   -119.89                                   
REMARK 500    ASN B 106       90.22   -164.43                                   
REMARK 500    ASN B 133     -151.61   -136.84                                   
REMARK 500    ARG B 156      -75.25   -114.88                                   
REMARK 500    ASP B 201       58.74   -156.51                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ADP A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 307                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 308                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 309                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 310                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 311                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 312                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 313                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 314                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 315                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 316                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ADP B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 307                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 308                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS B 309                 
DBREF  6OID A    1   297  UNP    Q9LEW8   FN3KR_ARATH     30    326             
DBREF  6OID B    1   297  UNP    Q9LEW8   FN3KR_ARATH     30    326             
SEQADV 6OID MET A  -19  UNP  Q9LEW8              INITIATING METHIONINE          
SEQADV 6OID GLY A  -18  UNP  Q9LEW8              EXPRESSION TAG                 
SEQADV 6OID SER A  -17  UNP  Q9LEW8              EXPRESSION TAG                 
SEQADV 6OID SER A  -16  UNP  Q9LEW8              EXPRESSION TAG                 
SEQADV 6OID HIS A  -15  UNP  Q9LEW8              EXPRESSION TAG                 
SEQADV 6OID HIS A  -14  UNP  Q9LEW8              EXPRESSION TAG                 
SEQADV 6OID HIS A  -13  UNP  Q9LEW8              EXPRESSION TAG                 
SEQADV 6OID HIS A  -12  UNP  Q9LEW8              EXPRESSION TAG                 
SEQADV 6OID HIS A  -11  UNP  Q9LEW8              EXPRESSION TAG                 
SEQADV 6OID HIS A  -10  UNP  Q9LEW8              EXPRESSION TAG                 
SEQADV 6OID SER A   -9  UNP  Q9LEW8              EXPRESSION TAG                 
SEQADV 6OID SER A   -8  UNP  Q9LEW8              EXPRESSION TAG                 
SEQADV 6OID GLY A   -7  UNP  Q9LEW8              EXPRESSION TAG                 
SEQADV 6OID LEU A   -6  UNP  Q9LEW8              EXPRESSION TAG                 
SEQADV 6OID VAL A   -5  UNP  Q9LEW8              EXPRESSION TAG                 
SEQADV 6OID PRO A   -4  UNP  Q9LEW8              EXPRESSION TAG                 
SEQADV 6OID ARG A   -3  UNP  Q9LEW8              EXPRESSION TAG                 
SEQADV 6OID GLY A   -2  UNP  Q9LEW8              EXPRESSION TAG                 
SEQADV 6OID SER A   -1  UNP  Q9LEW8              EXPRESSION TAG                 
SEQADV 6OID HIS A    0  UNP  Q9LEW8              EXPRESSION TAG                 
SEQADV 6OID MET B  -19  UNP  Q9LEW8              INITIATING METHIONINE          
SEQADV 6OID GLY B  -18  UNP  Q9LEW8              EXPRESSION TAG                 
SEQADV 6OID SER B  -17  UNP  Q9LEW8              EXPRESSION TAG                 
SEQADV 6OID SER B  -16  UNP  Q9LEW8              EXPRESSION TAG                 
SEQADV 6OID HIS B  -15  UNP  Q9LEW8              EXPRESSION TAG                 
SEQADV 6OID HIS B  -14  UNP  Q9LEW8              EXPRESSION TAG                 
SEQADV 6OID HIS B  -13  UNP  Q9LEW8              EXPRESSION TAG                 
SEQADV 6OID HIS B  -12  UNP  Q9LEW8              EXPRESSION TAG                 
SEQADV 6OID HIS B  -11  UNP  Q9LEW8              EXPRESSION TAG                 
SEQADV 6OID HIS B  -10  UNP  Q9LEW8              EXPRESSION TAG                 
SEQADV 6OID SER B   -9  UNP  Q9LEW8              EXPRESSION TAG                 
SEQADV 6OID SER B   -8  UNP  Q9LEW8              EXPRESSION TAG                 
SEQADV 6OID GLY B   -7  UNP  Q9LEW8              EXPRESSION TAG                 
SEQADV 6OID LEU B   -6  UNP  Q9LEW8              EXPRESSION TAG                 
SEQADV 6OID VAL B   -5  UNP  Q9LEW8              EXPRESSION TAG                 
SEQADV 6OID PRO B   -4  UNP  Q9LEW8              EXPRESSION TAG                 
SEQADV 6OID ARG B   -3  UNP  Q9LEW8              EXPRESSION TAG                 
SEQADV 6OID GLY B   -2  UNP  Q9LEW8              EXPRESSION TAG                 
SEQADV 6OID SER B   -1  UNP  Q9LEW8              EXPRESSION TAG                 
SEQADV 6OID HIS B    0  UNP  Q9LEW8              EXPRESSION TAG                 
SEQRES   1 A  317  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  317  LEU VAL PRO ARG GLY SER HIS MET ALA ALA MET SER GLU          
SEQRES   3 A  317  ASP PRO ILE ARG GLU TRP ILE LEU THR GLU GLY LYS ALA          
SEQRES   4 A  317  THR GLN ILE THR LYS ILE GLY SER VAL GLY GLY GLY CYS          
SEQRES   5 A  317  ILE ASN LEU ALA SER HIS TYR GLN THR ASP ALA GLY SER          
SEQRES   6 A  317  PHE PHE VAL LYS THR ASN ARG SER ILE GLY PRO ALA MET          
SEQRES   7 A  317  PHE GLU GLY GLU ALA LEU GLY LEU GLU ALA MET TYR GLU          
SEQRES   8 A  317  THR ARG THR ILE ARG VAL PRO ASN PRO HIS LYS ALA GLY          
SEQRES   9 A  317  GLU LEU PRO THR GLY GLY SER TYR ILE ILE MET GLU PHE          
SEQRES  10 A  317  ILE ASP PHE GLY GLY SER ARG GLY ASN GLN ALA GLU LEU          
SEQRES  11 A  317  GLY ARG LYS LEU ALA GLU MET HIS LYS ALA GLY LYS THR          
SEQRES  12 A  317  SER LYS GLY PHE GLY PHE GLU VAL ASP ASN THR ILE GLY          
SEQRES  13 A  317  SER THR PRO GLN ILE ASN THR TRP SER SER ASP TRP ILE          
SEQRES  14 A  317  GLU PHE TYR GLY GLU LYS ARG LEU GLY TYR GLN LEU LYS          
SEQRES  15 A  317  LEU ALA ARG ASP GLN TYR GLY ASP SER ALA ILE TYR GLN          
SEQRES  16 A  317  LYS GLY HIS THR LEU ILE GLN ASN MET ALA PRO LEU PHE          
SEQRES  17 A  317  GLU ASN VAL VAL ILE GLU PRO CYS LEU LEU HIS GLY ASP          
SEQRES  18 A  317  LEU TRP SER GLY ASN ILE ALA TYR ASP LYS ASN ASN GLU          
SEQRES  19 A  317  PRO VAL ILE LEU ASP PRO ALA CYS TYR TYR GLY HIS ASN          
SEQRES  20 A  317  GLU ALA ASP PHE GLY MET SER TRP CYS ALA GLY PHE GLY          
SEQRES  21 A  317  GLU SER PHE TYR ASN ALA TYR PHE LYS VAL MET PRO LYS          
SEQRES  22 A  317  GLN ALA GLY TYR GLU LYS ARG ARG ASP LEU TYR LEU LEU          
SEQRES  23 A  317  TYR HIS TYR LEU ASN HIS TYR ASN LEU PHE GLY SER GLY          
SEQRES  24 A  317  TYR ARG SER SER ALA MET SER ILE ILE ASP ASP TYR LEU          
SEQRES  25 A  317  ARG MET LEU LYS ALA                                          
SEQRES   1 B  317  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B  317  LEU VAL PRO ARG GLY SER HIS MET ALA ALA MET SER GLU          
SEQRES   3 B  317  ASP PRO ILE ARG GLU TRP ILE LEU THR GLU GLY LYS ALA          
SEQRES   4 B  317  THR GLN ILE THR LYS ILE GLY SER VAL GLY GLY GLY CYS          
SEQRES   5 B  317  ILE ASN LEU ALA SER HIS TYR GLN THR ASP ALA GLY SER          
SEQRES   6 B  317  PHE PHE VAL LYS THR ASN ARG SER ILE GLY PRO ALA MET          
SEQRES   7 B  317  PHE GLU GLY GLU ALA LEU GLY LEU GLU ALA MET TYR GLU          
SEQRES   8 B  317  THR ARG THR ILE ARG VAL PRO ASN PRO HIS LYS ALA GLY          
SEQRES   9 B  317  GLU LEU PRO THR GLY GLY SER TYR ILE ILE MET GLU PHE          
SEQRES  10 B  317  ILE ASP PHE GLY GLY SER ARG GLY ASN GLN ALA GLU LEU          
SEQRES  11 B  317  GLY ARG LYS LEU ALA GLU MET HIS LYS ALA GLY LYS THR          
SEQRES  12 B  317  SER LYS GLY PHE GLY PHE GLU VAL ASP ASN THR ILE GLY          
SEQRES  13 B  317  SER THR PRO GLN ILE ASN THR TRP SER SER ASP TRP ILE          
SEQRES  14 B  317  GLU PHE TYR GLY GLU LYS ARG LEU GLY TYR GLN LEU LYS          
SEQRES  15 B  317  LEU ALA ARG ASP GLN TYR GLY ASP SER ALA ILE TYR GLN          
SEQRES  16 B  317  LYS GLY HIS THR LEU ILE GLN ASN MET ALA PRO LEU PHE          
SEQRES  17 B  317  GLU ASN VAL VAL ILE GLU PRO CYS LEU LEU HIS GLY ASP          
SEQRES  18 B  317  LEU TRP SER GLY ASN ILE ALA TYR ASP LYS ASN ASN GLU          
SEQRES  19 B  317  PRO VAL ILE LEU ASP PRO ALA CYS TYR TYR GLY HIS ASN          
SEQRES  20 B  317  GLU ALA ASP PHE GLY MET SER TRP CYS ALA GLY PHE GLY          
SEQRES  21 B  317  GLU SER PHE TYR ASN ALA TYR PHE LYS VAL MET PRO LYS          
SEQRES  22 B  317  GLN ALA GLY TYR GLU LYS ARG ARG ASP LEU TYR LEU LEU          
SEQRES  23 B  317  TYR HIS TYR LEU ASN HIS TYR ASN LEU PHE GLY SER GLY          
SEQRES  24 B  317  TYR ARG SER SER ALA MET SER ILE ILE ASP ASP TYR LEU          
SEQRES  25 B  317  ARG MET LEU LYS ALA                                          
HET    ADP  A 301      27                                                       
HET    SO4  A 302       5                                                       
HET    SO4  A 303       5                                                       
HET    SO4  A 304       5                                                       
HET    SO4  A 305       5                                                       
HET    SO4  A 306       5                                                       
HET    SO4  A 307       5                                                       
HET    SO4  A 308       5                                                       
HET    SO4  A 309       5                                                       
HET    SO4  A 310       5                                                       
HET     CL  A 311       1                                                       
HET    EDO  A 312       4                                                       
HET    EDO  A 313       4                                                       
HET    EDO  A 314       4                                                       
HET    EDO  A 315       4                                                       
HET    DMS  A 316       4                                                       
HET    ADP  B 301      27                                                       
HET    SO4  B 302       5                                                       
HET    SO4  B 303       5                                                       
HET    SO4  B 304       5                                                       
HET    SO4  B 305       5                                                       
HET    SO4  B 306       5                                                       
HET     CL  B 307       1                                                       
HET    EDO  B 308       4                                                       
HET    DMS  B 309       4                                                       
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETNAM     SO4 SULFATE ION                                                      
HETNAM      CL CHLORIDE ION                                                     
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     DMS DIMETHYL SULFOXIDE                                               
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3  ADP    2(C10 H15 N5 O10 P2)                                         
FORMUL   4  SO4    14(O4 S 2-)                                                  
FORMUL  13   CL    2(CL 1-)                                                     
FORMUL  14  EDO    5(C2 H6 O2)                                                  
FORMUL  18  DMS    2(C2 H6 O S)                                                 
FORMUL  28  HOH   *89(H2 O)                                                     
HELIX    1 AA1 ASP A    7  GLU A   16  1                                  10    
HELIX    2 AA2 PRO A   56  THR A   72  1                                  17    
HELIX    3 AA3 ASN A  106  GLY A  121  1                                  16    
HELIX    4 AA4 ASP A  147  ARG A  156  1                                  10    
HELIX    5 AA5 ARG A  156  GLY A  169  1                                  14    
HELIX    6 AA6 ASP A  170  ASN A  183  1                                  14    
HELIX    7 AA7 MET A  184  GLU A  189  5                                   6    
HELIX    8 AA8 TRP A  203  GLY A  205  5                                   3    
HELIX    9 AA9 HIS A  226  GLY A  232  5                                   7    
HELIX   10 AB1 MET A  233  ALA A  237  5                                   5    
HELIX   11 AB2 GLY A  240  MET A  251  1                                  12    
HELIX   12 AB3 ARG A  260  GLY A  277  1                                  18    
HELIX   13 AB4 TYR A  280  LEU A  295  1                                  16    
HELIX   14 AB5 PRO B    8  THR B   15  1                                   8    
HELIX   15 AB6 PRO B   56  THR B   72  1                                  17    
HELIX   16 AB7 ASN B  106  GLY B  121  1                                  16    
HELIX   17 AB8 ASP B  147  ARG B  156  1                                  10    
HELIX   18 AB9 ARG B  156  GLY B  169  1                                  14    
HELIX   19 AC1 ASP B  170  ASN B  183  1                                  14    
HELIX   20 AC2 MET B  184  GLU B  189  5                                   6    
HELIX   21 AC3 TRP B  203  GLY B  205  5                                   3    
HELIX   22 AC4 HIS B  226  GLY B  232  5                                   7    
HELIX   23 AC5 MET B  233  ALA B  237  5                                   5    
HELIX   24 AC6 GLY B  240  MET B  251  1                                  12    
HELIX   25 AC7 GLY B  256  GLY B  277  1                                  22    
HELIX   26 AC8 TYR B  280  LEU B  295  1                                  16    
SHEET    1 AA1 5 ILE A  22  GLY A  29  0                                        
SHEET    2 AA1 5 LEU B  35  THR B  41 -1  O  HIS B  38   N  GLY A  26           
SHEET    3 AA1 5 GLY B  44  ASN B  51 -1  O  THR B  50   N  LEU B  35           
SHEET    4 AA1 5 SER B  91  GLU B  96 -1  O  MET B  95   N  PHE B  47           
SHEET    5 AA1 5 PRO B  80  GLU B  85 -1  N  LYS B  82   O  ILE B  94           
SHEET    1 AA2 5 PRO A  80  GLU A  85  0                                        
SHEET    2 AA2 5 SER A  91  GLU A  96 -1  O  ILE A  94   N  LYS A  82           
SHEET    3 AA2 5 GLY A  44  ASN A  51 -1  N  PHE A  47   O  MET A  95           
SHEET    4 AA2 5 LEU A  35  THR A  41 -1  N  SER A  37   O  VAL A  48           
SHEET    5 AA2 5 ILE B  22  GLY B  29 -1  O  GLY B  26   N  HIS A  38           
SHEET    1 AA3 2 ASN A 133  ILE A 135  0                                        
SHEET    2 AA3 2 THR A 138  GLN A 140 -1  O  GLN A 140   N  ASN A 133           
SHEET    1 AA4 2 CYS A 196  LEU A 198  0                                        
SHEET    2 AA4 2 TYR A 223  GLY A 225 -1  O  TYR A 223   N  LEU A 198           
SHEET    1 AA5 2 ILE A 207  TYR A 209  0                                        
SHEET    2 AA5 2 PRO A 215  ILE A 217 -1  O  VAL A 216   N  ALA A 208           
SHEET    1 AA6 2 ASN B 133  ILE B 135  0                                        
SHEET    2 AA6 2 THR B 138  GLN B 140 -1  O  GLN B 140   N  ASN B 133           
SHEET    1 AA7 2 CYS B 196  LEU B 198  0                                        
SHEET    2 AA7 2 TYR B 223  GLY B 225 -1  O  TYR B 223   N  LEU B 198           
SHEET    1 AA8 2 ILE B 207  TYR B 209  0                                        
SHEET    2 AA8 2 PRO B 215  ILE B 217 -1  O  VAL B 216   N  ALA B 208           
SSBOND   1 CYS A   32    CYS B   32                          1555   1555  2.06  
SSBOND   2 CYS A  236    CYS B  236                          1555   1555  2.06  
SITE     1 AC1 15 ASN A  34  PHE A  47  LYS A  49  PRO A  78                    
SITE     2 AC1 15 GLU A  96  PHE A  97  ILE A  98  PHE A 100                    
SITE     3 AC1 15 ASP A 219  EDO A 315  DMS A 316  HOH A 402                    
SITE     4 AC1 15 HOH A 438  PHE B 276  GLY B 277                               
SITE     1 AC2  4 GLY A 256  TYR A 257  GLU A 258  LYS A 259                    
SITE     1 AC3  4 ARG A  76  ASP A  99  LYS A 211  HOH A 403                    
SITE     1 AC4  3 ALA A 172  ARG A 281  SER B 103                               
SITE     1 AC5  2 ARG A 112  LYS A 113                                          
SITE     1 AC6  2 LYS A 162  ARG A 165                                          
SITE     1 AC7  4 HIS A  38  DMS A 316  HOH A 408  LYS B  24                    
SITE     1 AC8  4 ASN A  79  HIS A  81  GLU A  96  HOH A 401                    
SITE     1 AC9  2 SER A 145  SER A 146                                          
SITE     1 AD1  4 ASN A 106  GLN A 107  ALA A 108  SER A 242                    
SITE     1 AD2  1 HIS A 272                                                     
SITE     1 AD3  7 PHE A 276  GLY A 277  SER A 278  GLY A 279                    
SITE     2 AD3  7 GLY B 205  ILE B 207  ADP B 301                               
SITE     1 AD4  1 HIS A  81                                                     
SITE     1 AD5  3 GLY A 240  GLU A 241  SER A 242                               
SITE     1 AD6  6 GLY A 205  ILE A 207  ADP A 301  PHE B 276                    
SITE     2 AD6  6 GLY B 277  GLY B 279                                          
SITE     1 AD7  6 HIS A  38  PHE A  47  PHE A  97  ADP A 301                    
SITE     2 AD7  6 SO4 A 307  VAL B  28                                          
SITE     1 AD8 14 PHE A 276  GLY A 277  EDO A 312  ASN B  34                    
SITE     2 AD8 14 PHE B  47  LYS B  49  PRO B  78  MET B  95                    
SITE     3 AD8 14 GLU B  96  PHE B  97  ILE B  98  PHE B 100                    
SITE     4 AD8 14 ASP B 219  HOH B 427                                          
SITE     1 AD9  4 GLY B 256  TYR B 257  GLU B 258  LYS B 259                    
SITE     1 AE1  3 ARG B  76  ASP B  99  LYS B 211                               
SITE     1 AE2  2 ARG B 112  LYS B 113                                          
SITE     1 AE3  4 SER A 103  ALA B 172  LYS B 176  ARG B 281                    
SITE     1 AE4  4 LYS A  24  GLY A  26  HIS B  38  GLN B  40                    
SITE     1 AE5  1 HIS B 272                                                     
SITE     1 AE6  3 ASN B 106  GLN B 107  SER B 242                               
SITE     1 AE7  6 ARG B  10  ILE B  22  THR B  23  LYS B  24                    
SITE     2 AE7  6 ILE B  25  SER B  27                                          
CRYST1  158.860  163.640   70.720  90.00  90.00  90.00 C 2 2 21     16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.006295  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006111  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014140        0.00000                         
ATOM      1  N   ASP A   7      69.358  -0.958  45.730  1.00105.86           N  
ANISOU    1  N   ASP A   7    15615  12182  12426   4401   2576   3652       N  
ATOM      2  CA  ASP A   7      68.066  -0.411  45.313  1.00104.46           C  
ANISOU    2  CA  ASP A   7    15492  11887  12311   4187   2629   3520       C  
ATOM      3  C   ASP A   7      67.420   0.404  46.429  1.00103.31           C  
ANISOU    3  C   ASP A   7    15396  11812  12046   4103   2559   3526       C  
ATOM      4  O   ASP A   7      66.581  -0.105  47.166  1.00100.42           O  
ANISOU    4  O   ASP A   7    15142  11331  11680   4081   2654   3553       O  
ATOM      5  CB  ASP A   7      67.131  -1.539  44.863  1.00104.04           C  
ANISOU    5  CB  ASP A   7    15559  11573  12400   4129   2815   3478       C  
ATOM      6  CG  ASP A   7      65.916  -1.034  44.092  1.00109.59           C  
ANISOU    6  CG  ASP A   7    16279  12159  13202   3901   2866   3337       C  
ATOM      7  OD1 ASP A   7      65.719   0.197  43.989  1.00106.91           O  
ANISOU    7  OD1 ASP A   7    15873  11932  12816   3795   2771   3271       O  
ATOM      8  OD2 ASP A   7      65.156  -1.880  43.578  1.00112.76           O  
ANISOU    8  OD2 ASP A   7    16762  12354  13726   3823   2992   3294       O  
ATOM      9  N   PRO A   8      67.807   1.680  46.541  1.00102.65           N  
ANISOU    9  N   PRO A   8    15233  11916  11853   4053   2390   3500       N  
ATOM     10  CA  PRO A   8      67.266   2.520  47.627  1.00 98.33           C  
ANISOU   10  CA  PRO A   8    14752  11441  11168   3980   2310   3499       C  
ATOM     11  C   PRO A   8      65.763   2.768  47.542  1.00 88.43           C  
ANISOU   11  C   PRO A   8    13580  10044   9973   3816   2425   3399       C  
ATOM     12  O   PRO A   8      65.146   3.066  48.572  1.00 91.01           O  
ANISOU   12  O   PRO A   8    13992  10381  10205   3791   2425   3417       O  
ATOM     13  CB  PRO A   8      68.059   3.828  47.493  1.00 97.64           C  
ANISOU   13  CB  PRO A   8    14563  11573  10963   3939   2091   3475       C  
ATOM     14  CG  PRO A   8      69.273   3.475  46.695  1.00 96.21           C  
ANISOU   14  CG  PRO A   8    14244  11477  10835   4051   2046   3524       C  
ATOM     15  CD  PRO A   8      68.821   2.397  45.750  1.00 97.10           C  
ANISOU   15  CD  PRO A   8    14382  11379  11133   4069   2252   3483       C  
ATOM     16  N   ILE A   9      65.152   2.692  46.359  1.00 81.62           N  
ANISOU   16  N   ILE A   9    12691   9058   9263   3702   2519   3296       N  
ATOM     17  CA  ILE A   9      63.710   2.912  46.271  1.00 83.15           C  
ANISOU   17  CA  ILE A   9    12941   9130   9523   3540   2622   3213       C  
ATOM     18  C   ILE A   9      62.958   1.803  47.003  1.00 90.00           C  
ANISOU   18  C   ILE A   9    13908   9854  10434   3572   2772   3287       C  
ATOM     19  O   ILE A   9      62.209   2.065  47.953  1.00 82.85           O  
ANISOU   19  O   ILE A   9    13066   8958   9456   3547   2797   3310       O  
ATOM     20  CB  ILE A   9      63.264   3.033  44.805  1.00 70.41           C  
ANISOU   20  CB  ILE A   9    11271   7414   8069   3398   2673   3091       C  
ATOM     21  CG1 ILE A   9      63.923   4.247  44.148  1.00 67.06           C  
ANISOU   21  CG1 ILE A   9    10752   7139   7590   3355   2520   3020       C  
ATOM     22  CG2 ILE A   9      61.754   3.182  44.725  1.00 70.47           C  
ANISOU   22  CG2 ILE A   9    11317   7303   8157   3228   2776   3020       C  
ATOM     23  CD1 ILE A   9      63.906   4.200  42.610  1.00 63.94           C  
ANISOU   23  CD1 ILE A   9    10291   6655   7348   3263   2558   2919       C  
ATOM     24  N   ARG A  10      63.154   0.545  46.577  1.00 96.12           N  
ANISOU   24  N   ARG A  10    14706  10493  11321   3632   2871   3327       N  
ATOM     25  CA  ARG A  10      62.581  -0.585  47.310  1.00 94.75           C  
ANISOU   25  CA  ARG A  10    14635  10188  11177   3674   2995   3414       C  
ATOM     26  C   ARG A  10      63.051  -0.589  48.756  1.00 90.42           C  
ANISOU   26  C   ARG A  10    14139   9752  10466   3817   2942   3532       C  
ATOM     27  O   ARG A  10      62.256  -0.819  49.673  1.00 88.69           O  
ANISOU   27  O   ARG A  10    13998   9487  10213   3805   3012   3583       O  
ATOM     28  CB  ARG A  10      62.916  -1.910  46.621  1.00103.05           C  
ANISOU   28  CB  ARG A  10    15721  11085  12350   3731   3083   3439       C  
ATOM     29  CG  ARG A  10      62.008  -2.200  45.423  1.00111.66           C  
ANISOU   29  CG  ARG A  10    16814  12000  13612   3552   3168   3333       C  
ATOM     30  CD  ARG A  10      62.227  -3.588  44.799  1.00119.81           C  
ANISOU   30  CD  ARG A  10    17920  12850  14752   3597   3254   3352       C  
ATOM     31  NE  ARG A  10      61.523  -3.697  43.516  1.00118.23           N  
ANISOU   31  NE  ARG A  10    17717  12504  14702   3414   3294   3233       N  
ATOM     32  CZ  ARG A  10      60.550  -4.565  43.249  1.00113.27           C  
ANISOU   32  CZ  ARG A  10    17173  11680  14186   3292   3380   3225       C  
ATOM     33  NH1 ARG A  10      60.155  -5.438  44.176  1.00113.85           N  
ANISOU   33  NH1 ARG A  10    17342  11673  14245   3339   3445   3336       N  
ATOM     34  NH2 ARG A  10      59.976  -4.562  42.049  1.00105.57           N  
ANISOU   34  NH2 ARG A  10    16186  10589  13336   3116   3388   3111       N  
ATOM     35  N   GLU A  11      64.335  -0.321  48.984  1.00 92.66           N  
ANISOU   35  N   GLU A  11    14373  10187  10645   3950   2812   3582       N  
ATOM     36  CA  GLU A  11      64.841  -0.253  50.351  1.00 99.24           C  
ANISOU   36  CA  GLU A  11    15254  11137  11315   4072   2733   3692       C  
ATOM     37  C   GLU A  11      64.044   0.728  51.212  1.00 93.06           C  
ANISOU   37  C   GLU A  11    14524  10417  10418   3985   2697   3662       C  
ATOM     38  O   GLU A  11      63.593   0.377  52.309  1.00 92.57           O  
ANISOU   38  O   GLU A  11    14558  10325  10289   4028   2751   3736       O  
ATOM     39  CB  GLU A  11      66.314   0.139  50.345  1.00110.78           C  
ANISOU   39  CB  GLU A  11    16625  12783  12683   4188   2561   3739       C  
ATOM     40  CG  GLU A  11      66.893   0.327  51.733  1.00120.04           C  
ANISOU   40  CG  GLU A  11    17841  14088  13678   4290   2443   3848       C  
ATOM     41  CD  GLU A  11      68.394   0.498  51.709  1.00128.88           C  
ANISOU   41  CD  GLU A  11    18854  15389  14727   4407   2274   3922       C  
ATOM     42  OE1 GLU A  11      69.062  -0.226  50.936  1.00133.18           O  
ANISOU   42  OE1 GLU A  11    19324  15908  15371   4502   2317   3950       O  
ATOM     43  OE2 GLU A  11      68.904   1.354  52.464  1.00129.32           O  
ANISOU   43  OE2 GLU A  11    18900  15611  14624   4401   2093   3953       O  
ATOM     44  N   TRP A  12      63.871   1.974  50.741  1.00 94.22           N  
ANISOU   44  N   TRP A  12    14616  10652  10533   3869   2606   3555       N  
ATOM     45  CA  TRP A  12      63.184   2.983  51.558  1.00 87.75           C  
ANISOU   45  CA  TRP A  12    13858   9898   9586   3800   2564   3519       C  
ATOM     46  C   TRP A  12      61.722   2.610  51.775  1.00 87.96           C  
ANISOU   46  C   TRP A  12    13946   9782   9693   3725   2746   3506       C  
ATOM     47  O   TRP A  12      61.192   2.765  52.885  1.00 72.35           O  
ANISOU   47  O   TRP A  12    12057   7820   7613   3752   2774   3550       O  
ATOM     48  CB  TRP A  12      63.284   4.380  50.932  1.00 77.82           C  
ANISOU   48  CB  TRP A  12    12538   8751   8279   3685   2428   3401       C  
ATOM     49  CG  TRP A  12      62.706   5.470  51.830  1.00 85.73           C  
ANISOU   49  CG  TRP A  12    13622   9827   9123   3631   2367   3362       C  
ATOM     50  CD1 TRP A  12      63.391   6.244  52.726  1.00 89.03           C  
ANISOU   50  CD1 TRP A  12    14094  10392   9342   3666   2187   3386       C  
ATOM     51  CD2 TRP A  12      61.324   5.871  51.935  1.00 83.78           C  
ANISOU   51  CD2 TRP A  12    13422   9507   8904   3537   2485   3295       C  
ATOM     52  NE1 TRP A  12      62.527   7.106  53.373  1.00 83.42           N  
ANISOU   52  NE1 TRP A  12    13477   9693   8527   3605   2192   3329       N  
ATOM     53  CE2 TRP A  12      61.256   6.894  52.906  1.00 82.74           C  
ANISOU   53  CE2 TRP A  12    13380   9479   8579   3537   2380   3277       C  
ATOM     54  CE3 TRP A  12      60.142   5.462  51.301  1.00 81.09           C  
ANISOU   54  CE3 TRP A  12    13051   9027   8734   3448   2662   3254       C  
ATOM     55  CZ2 TRP A  12      60.056   7.506  53.265  1.00 83.27           C  
ANISOU   55  CZ2 TRP A  12    13507   9514   8617   3479   2464   3220       C  
ATOM     56  CZ3 TRP A  12      58.948   6.082  51.651  1.00 81.80           C  
ANISOU   56  CZ3 TRP A  12    13180   9099   8802   3379   2735   3208       C  
ATOM     57  CH2 TRP A  12      58.917   7.092  52.625  1.00 85.15           C  
ANISOU   57  CH2 TRP A  12    13693   9629   9030   3408   2645   3192       C  
ATOM     58  N   ILE A  13      61.056   2.127  50.720  1.00 78.41           N  
ANISOU   58  N   ILE A  13    12689   8435   8667   3627   2865   3451       N  
ATOM     59  CA  ILE A  13      59.649   1.760  50.811  1.00 81.96           C  
ANISOU   59  CA  ILE A  13    13172   8757   9214   3534   3024   3448       C  
ATOM     60  C   ILE A  13      59.427   0.704  51.898  1.00 91.72           C  
ANISOU   60  C   ILE A  13    14502   9924  10424   3636   3122   3581       C  
ATOM     61  O   ILE A  13      58.356   0.655  52.517  1.00 88.15           O  
ANISOU   61  O   ILE A  13    14093   9427   9972   3598   3222   3611       O  
ATOM     62  CB  ILE A  13      59.154   1.328  49.410  1.00 79.34           C  
ANISOU   62  CB  ILE A  13    12771   8288   9087   3401   3101   3372       C  
ATOM     63  CG1 ILE A  13      59.119   2.559  48.496  1.00 84.94           C  
ANISOU   63  CG1 ILE A  13    13396   9071   9806   3284   3013   3239       C  
ATOM     64  CG2 ILE A  13      57.773   0.705  49.449  1.00 81.54           C  
ANISOU   64  CG2 ILE A  13    13071   8423   9488   3299   3253   3395       C  
ATOM     65  CD1 ILE A  13      58.332   2.391  47.190  1.00 83.89           C  
ANISOU   65  CD1 ILE A  13    13198   8810   9865   3115   3084   3147       C  
ATOM     66  N   LEU A  14      60.432  -0.130  52.175  1.00 97.34           N  
ANISOU   66  N   LEU A  14    15245  10632  11108   3772   3093   3668       N  
ATOM     67  CA  LEU A  14      60.329  -1.122  53.241  1.00100.04           C  
ANISOU   67  CA  LEU A  14    15685  10913  11412   3878   3171   3799       C  
ATOM     68  C   LEU A  14      61.064  -0.708  54.524  1.00104.89           C  
ANISOU   68  C   LEU A  14    16361  11671  11822   4010   3062   3873       C  
ATOM     69  O   LEU A  14      60.752  -1.230  55.596  1.00101.30           O  
ANISOU   69  O   LEU A  14    15998  11185  11305   4079   3126   3971       O  
ATOM     70  CB  LEU A  14      60.812  -2.483  52.722  1.00 92.31           C  
ANISOU   70  CB  LEU A  14    14720   9802  10550   3939   3231   3855       C  
ATOM     71  CG  LEU A  14      60.121  -2.776  51.365  1.00 90.34           C  
ANISOU   71  CG  LEU A  14    14421   9409  10493   3784   3310   3763       C  
ATOM     72  CD1 LEU A  14      60.551  -4.061  50.716  1.00 92.34           C  
ANISOU   72  CD1 LEU A  14    14708   9515  10860   3829   3364   3796       C  
ATOM     73  CD2 LEU A  14      58.611  -2.743  51.390  1.00 93.20           C  
ANISOU   73  CD2 LEU A  14    14792   9682  10939   3630   3420   3745       C  
ATOM     74  N   THR A  15      61.964   0.275  54.463  1.00116.66           N  
ANISOU   74  N   THR A  15    17806  13319  13201   4031   2891   3828       N  
ATOM     75  CA  THR A  15      62.573   0.796  55.686  1.00126.31           C  
ANISOU   75  CA  THR A  15    19094  14677  14220   4122   2762   3889       C  
ATOM     76  C   THR A  15      61.595   1.744  56.366  1.00123.83           C  
ANISOU   76  C   THR A  15    18848  14397  13806   4051   2780   3839       C  
ATOM     77  O   THR A  15      61.009   1.416  57.402  1.00130.67           O  
ANISOU   77  O   THR A  15    19813  15225  14610   4098   2866   3910       O  
ATOM     78  CB  THR A  15      63.877   1.538  55.362  1.00136.21           C  
ANISOU   78  CB  THR A  15    20272  16093  15390   4147   2551   3865       C  
ATOM     79  OG1 THR A  15      64.720   0.715  54.551  1.00142.22           O  
ANISOU   79  OG1 THR A  15    20950  16825  16263   4218   2554   3900       O  
ATOM     80  CG2 THR A  15      64.613   1.947  56.641  1.00137.59           C  
ANISOU   80  CG2 THR A  15    20520  16402  15357   4230   2393   3944       C  
ATOM     81  N   GLU A  16      61.415   2.925  55.784  1.00117.62           N  
ANISOU   81  N   GLU A  16    18012  13679  12999   3943   2702   3718       N  
ATOM     82  CA  GLU A  16      60.575   3.972  56.335  1.00111.08           C  
ANISOU   82  CA  GLU A  16    17248  12893  12066   3883   2703   3656       C  
ATOM     83  C   GLU A  16      59.185   4.009  55.718  1.00 95.96           C  
ANISOU   83  C   GLU A  16    15292  10874  10295   3774   2872   3591       C  
ATOM     84  O   GLU A  16      58.278   4.611  56.301  1.00 84.50           O  
ANISOU   84  O   GLU A  16    13897   9432   8777   3754   2929   3569       O  
ATOM     85  CB  GLU A  16      61.262   5.328  56.166  1.00116.61           C  
ANISOU   85  CB  GLU A  16    17935  13739  12633   3830   2491   3566       C  
ATOM     86  CG  GLU A  16      62.595   5.362  56.893  1.00126.57           C  
ANISOU   86  CG  GLU A  16    19233  15117  13740   3920   2301   3644       C  
ATOM     87  CD  GLU A  16      62.983   6.745  57.369  1.00131.14           C  
ANISOU   87  CD  GLU A  16    19873  15832  14122   3864   2095   3582       C  
ATOM     88  OE1 GLU A  16      63.080   7.659  56.520  1.00128.75           O  
ANISOU   88  OE1 GLU A  16    19505  15583  13830   3756   2000   3473       O  
ATOM     89  OE2 GLU A  16      63.185   6.912  58.594  1.00135.87           O  
ANISOU   89  OE2 GLU A  16    20595  16477  14551   3921   2025   3642       O  
ATOM     90  N   GLY A  17      58.992   3.399  54.553  1.00 93.95           N  
ANISOU   90  N   GLY A  17    14940  10521  10234   3703   2949   3563       N  
ATOM     91  CA  GLY A  17      57.658   3.383  53.995  1.00 94.31           C  
ANISOU   91  CA  GLY A  17    14940  10470  10423   3585   3095   3516       C  
ATOM     92  C   GLY A  17      56.689   2.409  54.637  1.00 98.24           C  
ANISOU   92  C   GLY A  17    15484  10858  10985   3606   3271   3621       C  
ATOM     93  O   GLY A  17      55.499   2.456  54.301  1.00 97.58           O  
ANISOU   93  O   GLY A  17    15356  10710  11011   3505   3385   3599       O  
ATOM     94  N   LYS A  18      57.167   1.527  55.528  1.00 95.64           N  
ANISOU   94  N   LYS A  18    15236  10509  10595   3730   3290   3740       N  
ATOM     95  CA  LYS A  18      56.312   0.629  56.305  1.00 97.15           C  
ANISOU   95  CA  LYS A  18    15487  10607  10819   3760   3445   3854       C  
ATOM     96  C   LYS A  18      55.513  -0.340  55.431  1.00 98.18           C  
ANISOU   96  C   LYS A  18    15556  10579  11171   3647   3573   3871       C  
ATOM     97  O   LYS A  18      54.420  -0.759  55.804  1.00109.17           O  
ANISOU   97  O   LYS A  18    16958  11901  12621   3606   3703   3939       O  
ATOM     98  CB  LYS A  18      55.357   1.417  57.205  1.00 96.08           C  
ANISOU   98  CB  LYS A  18    15400  10528  10578   3768   3504   3859       C  
ATOM     99  CG  LYS A  18      56.020   2.293  58.253  1.00103.48           C  
ANISOU   99  CG  LYS A  18    16440  11600  11280   3876   3383   3853       C  
ATOM    100  CD  LYS A  18      55.105   3.461  58.632  1.00109.18           C  
ANISOU  100  CD  LYS A  18    17187  12382  11916   3850   3413   3790       C  
ATOM    101  CE  LYS A  18      55.203   3.812  60.119  1.00116.38           C  
ANISOU  101  CE  LYS A  18    18250  13361  12609   3977   3394   3848       C  
ATOM    102  NZ  LYS A  18      54.030   4.620  60.580  1.00118.26           N  
ANISOU  102  NZ  LYS A  18    18522  13618  12794   3977   3494   3822       N  
ATOM    103  N   ALA A  19      56.030  -0.727  54.273  1.00 90.38           N  
ANISOU  103  N   ALA A  19    14506   9529  10305   3590   3533   3816       N  
ATOM    104  CA  ALA A  19      55.329  -1.657  53.395  1.00 90.53           C  
ANISOU  104  CA  ALA A  19    14486   9385  10527   3468   3630   3823       C  
ATOM    105  C   ALA A  19      55.976  -3.034  53.472  1.00 89.14           C  
ANISOU  105  C   ALA A  19    14381   9096  10391   3550   3653   3914       C  
ATOM    106  O   ALA A  19      57.092  -3.182  53.983  1.00 91.66           O  
ANISOU  106  O   ALA A  19    14751   9479  10598   3701   3582   3956       O  
ATOM    107  CB  ALA A  19      55.328  -1.154  51.947  1.00 89.15           C  
ANISOU  107  CB  ALA A  19    14207   9194  10471   3331   3578   3687       C  
ATOM    108  N   THR A  20      55.242  -4.065  53.017  1.00 94.47           N  
ANISOU  108  N   THR A  20    15068   9603  11224   3450   3747   3955       N  
ATOM    109  CA  THR A  20      55.833  -5.403  52.906  1.00108.69           C  
ANISOU  109  CA  THR A  20    16950  11271  13076   3516   3766   4026       C  
ATOM    110  C   THR A  20      55.758  -6.039  51.513  1.00110.95           C  
ANISOU  110  C   THR A  20    17216  11403  13537   3393   3770   3958       C  
ATOM    111  O   THR A  20      56.553  -6.946  51.238  1.00111.45           O  
ANISOU  111  O   THR A  20    17346  11378  13623   3475   3759   3984       O  
ATOM    112  CB  THR A  20      55.243  -6.378  53.953  1.00110.43           C  
ANISOU  112  CB  THR A  20    17269  11404  13284   3553   3866   4178       C  
ATOM    113  OG1 THR A  20      53.829  -6.564  53.759  1.00111.47           O  
ANISOU  113  OG1 THR A  20    17370  11446  13536   3381   3953   4202       O  
ATOM    114  CG2 THR A  20      55.515  -5.866  55.376  1.00106.13           C  
ANISOU  114  CG2 THR A  20    16772  11004  12548   3703   3855   4249       C  
ATOM    115  N   GLN A  21      54.862  -5.595  50.624  1.00111.31           N  
ANISOU  115  N   GLN A  21    17178  11414  13701   3204   3779   3871       N  
ATOM    116  CA  GLN A  21      54.903  -6.082  49.246  1.00111.62           C  
ANISOU  116  CA  GLN A  21    17206  11317  13889   3086   3758   3788       C  
ATOM    117  C   GLN A  21      54.582  -4.953  48.273  1.00104.77           C  
ANISOU  117  C   GLN A  21    16215  10519  13074   2948   3705   3646       C  
ATOM    118  O   GLN A  21      53.710  -4.115  48.522  1.00104.75           O  
ANISOU  118  O   GLN A  21    16139  10598  13064   2864   3721   3631       O  
ATOM    119  CB  GLN A  21      53.941  -7.267  48.955  1.00112.79           C  
ANISOU  119  CB  GLN A  21    17418  11258  14179   2942   3824   3851       C  
ATOM    120  CG  GLN A  21      52.423  -6.977  48.969  1.00107.36           C  
ANISOU  120  CG  GLN A  21    16660  10556  13577   2747   3867   3873       C  
ATOM    121  CD  GLN A  21      51.572  -8.142  48.406  1.00 98.91           C  
ANISOU  121  CD  GLN A  21    15647   9273  12660   2569   3890   3924       C  
ATOM    122  OE1 GLN A  21      52.071  -9.251  48.177  1.00 91.92           O  
ANISOU  122  OE1 GLN A  21    14884   8238  11805   2606   3886   3955       O  
ATOM    123  NE2 GLN A  21      50.283  -7.879  48.179  1.00 95.11           N  
ANISOU  123  NE2 GLN A  21    15083   8783  12273   2374   3904   3936       N  
ATOM    124  N   ILE A  22      55.307  -4.948  47.164  1.00 98.70           N  
ANISOU  124  N   ILE A  22    15428   9718  12357   2934   3646   3546       N  
ATOM    125  CA  ILE A  22      55.068  -4.046  46.052  1.00 90.81           C  
ANISOU  125  CA  ILE A  22    14324   8753  11427   2791   3592   3405       C  
ATOM    126  C   ILE A  22      54.290  -4.833  45.009  1.00 92.06           C  
ANISOU  126  C   ILE A  22    14501   8720  11759   2599   3611   3369       C  
ATOM    127  O   ILE A  22      54.822  -5.762  44.396  1.00 91.74           O  
ANISOU  127  O   ILE A  22    14541   8546  11771   2620   3607   3358       O  
ATOM    128  CB  ILE A  22      56.386  -3.501  45.488  1.00 86.23           C  
ANISOU  128  CB  ILE A  22    13712   8268  10786   2895   3507   3322       C  
ATOM    129  CG1 ILE A  22      57.143  -2.714  46.571  1.00 86.05           C  
ANISOU  129  CG1 ILE A  22    13677   8439  10580   3068   3457   3369       C  
ATOM    130  CG2 ILE A  22      56.120  -2.671  44.242  1.00 71.97           C  
ANISOU  130  CG2 ILE A  22    11808   6473   9062   2734   3453   3176       C  
ATOM    131  CD1 ILE A  22      58.499  -2.190  46.148  1.00 76.77           C  
ANISOU  131  CD1 ILE A  22    12461   7378   9332   3180   3356   3318       C  
ATOM    132  N   THR A  23      53.043  -4.452  44.769  1.00 98.00           N  
ANISOU  132  N   THR A  23    15180   9460  12595   2412   3622   3349       N  
ATOM    133  CA  THR A  23      52.197  -5.253  43.898  1.00104.23           C  
ANISOU  133  CA  THR A  23    15992  10069  13542   2211   3621   3337       C  
ATOM    134  C   THR A  23      52.259  -4.822  42.442  1.00107.62           C  
ANISOU  134  C   THR A  23    16361  10467  14061   2070   3545   3181       C  
ATOM    135  O   THR A  23      51.970  -5.641  41.561  1.00115.03           O  
ANISOU  135  O   THR A  23    17357  11238  15111   1937   3519   3152       O  
ATOM    136  CB  THR A  23      50.730  -5.188  44.355  1.00103.73           C  
ANISOU  136  CB  THR A  23    15873  10005  13537   2062   3662   3418       C  
ATOM    137  OG1 THR A  23      50.211  -3.868  44.171  1.00 98.40           O  
ANISOU  137  OG1 THR A  23    15058   9473  12855   1990   3639   3342       O  
ATOM    138  CG2 THR A  23      50.592  -5.551  45.823  1.00109.55           C  
ANISOU  138  CG2 THR A  23    16664  10779  14179   2197   3745   3574       C  
ATOM    139  N   LYS A  24      52.648  -3.577  42.168  1.00100.78           N  
ANISOU  139  N   LYS A  24    15395   9753  13143   2094   3499   3080       N  
ATOM    140  CA  LYS A  24      52.710  -3.079  40.802  1.00 90.74           C  
ANISOU  140  CA  LYS A  24    14063   8464  11951   1960   3426   2930       C  
ATOM    141  C   LYS A  24      53.555  -1.809  40.777  1.00 89.09           C  
ANISOU  141  C   LYS A  24    13777   8433  11638   2062   3379   2850       C  
ATOM    142  O   LYS A  24      53.662  -1.100  41.782  1.00 89.89           O  
ANISOU  142  O   LYS A  24    13852   8681  11623   2172   3391   2901       O  
ATOM    143  CB  LYS A  24      51.300  -2.827  40.261  1.00 85.97           C  
ANISOU  143  CB  LYS A  24    13375   7823  11466   1715   3402   2899       C  
ATOM    144  CG  LYS A  24      51.205  -2.713  38.755  1.00 86.31           C  
ANISOU  144  CG  LYS A  24    13387   7792  11615   1540   3318   2756       C  
ATOM    145  CD  LYS A  24      49.797  -2.339  38.362  1.00 93.10           C  
ANISOU  145  CD  LYS A  24    14145   8653  12575   1308   3280   2742       C  
ATOM    146  CE  LYS A  24      49.718  -1.961  36.905  1.00102.41           C  
ANISOU  146  CE  LYS A  24    15273   9799  13838   1138   3180   2587       C  
ATOM    147  NZ  LYS A  24      48.416  -1.305  36.595  1.00110.18           N  
ANISOU  147  NZ  LYS A  24    16129  10837  14896    936   3131   2571       N  
ATOM    148  N   ILE A  25      54.189  -1.553  39.635  1.00 84.55           N  
ANISOU  148  N   ILE A  25    13182   7844  11100   2026   3318   2729       N  
ATOM    149  CA  ILE A  25      54.925  -0.311  39.388  1.00 76.90           C  
ANISOU  149  CA  ILE A  25    12135   7032  10052   2080   3254   2644       C  
ATOM    150  C   ILE A  25      54.515   0.185  38.010  1.00 76.49           C  
ANISOU  150  C   ILE A  25    12013   6942  10109   1881   3194   2497       C  
ATOM    151  O   ILE A  25      54.858  -0.438  36.996  1.00 80.61           O  
ANISOU  151  O   ILE A  25    12576   7346  10705   1834   3176   2432       O  
ATOM    152  CB  ILE A  25      56.445  -0.498  39.465  1.00 72.54           C  
ANISOU  152  CB  ILE A  25    11627   6529   9406   2288   3235   2663       C  
ATOM    153  CG1 ILE A  25      56.881  -0.882  40.877  1.00 69.92           C  
ANISOU  153  CG1 ILE A  25    11356   6259   8952   2485   3274   2806       C  
ATOM    154  CG2 ILE A  25      57.175   0.754  38.998  1.00 68.65           C  
ANISOU  154  CG2 ILE A  25    11050   6185   8851   2308   3148   2574       C  
ATOM    155  CD1 ILE A  25      58.395  -1.008  40.989  1.00 69.30           C  
ANISOU  155  CD1 ILE A  25    11298   6256   8776   2695   3237   2839       C  
ATOM    156  N   GLY A  26      53.831   1.327  37.963  1.00 65.54           N  
ANISOU  156  N   GLY A  26    10526   5657   8720   1775   3158   2442       N  
ATOM    157  CA  GLY A  26      53.404   1.926  36.712  1.00 64.31           C  
ANISOU  157  CA  GLY A  26    10292   5484   8658   1583   3090   2303       C  
ATOM    158  C   GLY A  26      54.251   3.151  36.396  1.00 68.23           C  
ANISOU  158  C   GLY A  26    10734   6118   9072   1634   3021   2215       C  
ATOM    159  O   GLY A  26      54.378   4.060  37.218  1.00 66.97           O  
ANISOU  159  O   GLY A  26    10550   6100   8797   1721   3008   2248       O  
ATOM    160  N   SER A  27      54.823   3.149  35.192  1.00 66.05           N  
ANISOU  160  N   SER A  27    10450   5794   8851   1578   2971   2106       N  
ATOM    161  CA  SER A  27      55.830   4.115  34.782  1.00 70.09           C  
ANISOU  161  CA  SER A  27    10923   6417   9292   1638   2903   2036       C  
ATOM    162  C   SER A  27      55.444   4.776  33.468  1.00 71.66           C  
ANISOU  162  C   SER A  27    11049   6597   9581   1436   2833   1880       C  
ATOM    163  O   SER A  27      54.991   4.101  32.535  1.00 70.60           O  
ANISOU  163  O   SER A  27    10926   6334   9563   1299   2828   1813       O  
ATOM    164  CB  SER A  27      57.196   3.449  34.617  1.00 72.13           C  
ANISOU  164  CB  SER A  27    11242   6652   9510   1814   2914   2069       C  
ATOM    165  OG  SER A  27      57.698   3.026  35.865  1.00 73.95           O  
ANISOU  165  OG  SER A  27    11525   6936   9635   2014   2955   2210       O  
ATOM    166  N   VAL A  28      55.615   6.104  33.412  1.00 66.59           N  
ANISOU  166  N   VAL A  28    10342   6086   8874   1416   2765   1822       N  
ATOM    167  CA  VAL A  28      55.509   6.879  32.179  1.00 62.11           C  
ANISOU  167  CA  VAL A  28     9706   5524   8368   1249   2686   1671       C  
ATOM    168  C   VAL A  28      56.754   7.750  32.057  1.00 60.18           C  
ANISOU  168  C   VAL A  28     9453   5389   8023   1356   2624   1650       C  
ATOM    169  O   VAL A  28      57.525   7.911  33.007  1.00 64.47           O  
ANISOU  169  O   VAL A  28    10030   6029   8439   1543   2621   1756       O  
ATOM    170  CB  VAL A  28      54.234   7.737  32.122  1.00 59.55           C  
ANISOU  170  CB  VAL A  28     9301   5245   8078   1075   2649   1614       C  
ATOM    171  CG1 VAL A  28      52.985   6.839  32.219  1.00 58.85           C  
ANISOU  171  CG1 VAL A  28     9208   5058   8096    970   2696   1657       C  
ATOM    172  CG2 VAL A  28      54.249   8.770  33.232  1.00 57.28           C  
ANISOU  172  CG2 VAL A  28     9012   5101   7650   1176   2642   1677       C  
ATOM    173  N   GLY A  29      56.942   8.321  30.870  1.00 58.24           N  
ANISOU  173  N   GLY A  29     9159   5138   7831   1231   2557   1516       N  
ATOM    174  CA  GLY A  29      58.095   9.178  30.630  1.00 59.11           C  
ANISOU  174  CA  GLY A  29     9255   5346   7859   1313   2487   1498       C  
ATOM    175  C   GLY A  29      59.334   8.391  30.235  1.00 70.02           C  
ANISOU  175  C   GLY A  29    10666   6690   9247   1471   2514   1532       C  
ATOM    176  O   GLY A  29      59.228   7.328  29.620  1.00 73.75           O  
ANISOU  176  O   GLY A  29    11174   7033   9816   1444   2573   1499       O  
ATOM    177  N   GLY A  30      60.513   8.918  30.562  1.00 69.27           N  
ANISOU  177  N   GLY A  30    10558   6719   9042   1643   2460   1603       N  
ATOM    178  CA  GLY A  30      61.761   8.208  30.366  1.00 69.77           C  
ANISOU  178  CA  GLY A  30    10625   6790   9094   1845   2483   1668       C  
ATOM    179  C   GLY A  30      62.364   8.249  28.977  1.00 74.15           C  
ANISOU  179  C   GLY A  30    11142   7299   9733   1809   2471   1553       C  
ATOM    180  O   GLY A  30      63.465   7.721  28.789  1.00 77.99           O  
ANISOU  180  O   GLY A  30    11613   7817  10204   2002   2493   1609       O  
ATOM    181  N   GLY A  31      61.698   8.834  27.997  1.00 71.19           N  
ANISOU  181  N   GLY A  31    10744   6865   9442   1576   2438   1393       N  
ATOM    182  CA  GLY A  31      62.295   8.925  26.679  1.00 79.69           C  
ANISOU  182  CA  GLY A  31    11785   7906  10586   1539   2425   1273       C  
ATOM    183  C   GLY A  31      63.494   9.866  26.640  1.00 82.32           C  
ANISOU  183  C   GLY A  31    11975   8495  10807   1625   2296   1262       C  
ATOM    184  O   GLY A  31      63.802  10.576  27.596  1.00 88.15           O  
ANISOU  184  O   GLY A  31    12640   9451  11401   1671   2186   1330       O  
ATOM    185  N   CYS A  32      64.214   9.841  25.518  1.00 74.49           N  
ANISOU  185  N   CYS A  32    10914   7536   9854   1620   2281   1158       N  
ATOM    186  CA  CYS A  32      65.279  10.802  25.272  1.00 71.70           C  
ANISOU  186  CA  CYS A  32    10365   7489   9387   1617   2121   1105       C  
ATOM    187  C   CYS A  32      64.823  11.781  24.194  1.00 66.64           C  
ANISOU  187  C   CYS A  32     9667   6865   8787   1341   2031    900       C  
ATOM    188  O   CYS A  32      64.073  11.423  23.287  1.00 72.24           O  
ANISOU  188  O   CYS A  32    10474   7342   9630   1209   2116    794       O  
ATOM    189  CB  CYS A  32      66.593  10.111  24.891  1.00 81.03           C  
ANISOU  189  CB  CYS A  32    11477   8751  10560   1849   2167   1169       C  
ATOM    190  SG  CYS A  32      67.138   8.925  26.190  1.00106.02           S  
ANISOU  190  SG  CYS A  32    14715  11892  13675   2192   2272   1425       S  
ATOM    191  N   ILE A  33      65.233  13.034  24.354  1.00 60.56           N  
ANISOU  191  N   ILE A  33     8755   6359   7895   1241   1848    851       N  
ATOM    192  CA  ILE A  33      64.847  14.095  23.437  1.00 62.10           C  
ANISOU  192  CA  ILE A  33     8894   6593   8108    978   1742    665       C  
ATOM    193  C   ILE A  33      65.708  14.083  22.191  1.00 64.29           C  
ANISOU  193  C   ILE A  33     9057   6966   8405    969   1714    571       C  
ATOM    194  O   ILE A  33      66.701  13.360  22.115  1.00 63.80           O  
ANISOU  194  O   ILE A  33     8935   6981   8325   1179   1765    663       O  
ATOM    195  CB  ILE A  33      64.949  15.480  24.104  1.00 76.52           C  
ANISOU  195  CB  ILE A  33    10660   8628   9784    865   1559    653       C  
ATOM    196  CG1 ILE A  33      66.225  15.576  24.943  1.00 89.58           C  
ANISOU  196  CG1 ILE A  33    12444  10164  11427    854   1609    722       C  
ATOM    197  CG2 ILE A  33      63.721  15.751  24.959  1.00 83.21           C  
ANISOU  197  CG2 ILE A  33    11442   9539  10634    611   1435    466       C  
ATOM    198  CD1 ILE A  33      66.234  16.740  25.909  1.00 96.41           C  
ANISOU  198  CD1 ILE A  33    13276  11248  12106    806   1432    735       C  
ATOM    199  N   ASN A  34      65.323  14.890  21.211  1.00 58.76           N  
ANISOU  199  N   ASN A  34     8332   6243   7749    735   1652    394       N  
ATOM    200  CA  ASN A  34      66.083  14.954  19.970  1.00 63.92           C  
ANISOU  200  CA  ASN A  34     8897   6960   8429    707   1643    294       C  
ATOM    201  C   ASN A  34      67.438  15.638  20.133  1.00 53.74           C  
ANISOU  201  C   ASN A  34     7401   6018   7001    777   1498    349       C  
ATOM    202  O   ASN A  34      67.558  16.676  20.788  1.00 48.09           O  
ANISOU  202  O   ASN A  34     6604   5507   6162    689   1324    365       O  
ATOM    203  CB  ASN A  34      65.268  15.702  18.918  1.00 59.86           C  
ANISOU  203  CB  ASN A  34     8406   6358   7981    419   1586     95       C  
ATOM    204  CG  ASN A  34      64.121  14.879  18.397  1.00 64.79           C  
ANISOU  204  CG  ASN A  34     9216   6638   8764    342   1733     38       C  
ATOM    205  OD1 ASN A  34      64.085  13.647  18.538  1.00 72.27           O  
ANISOU  205  OD1 ASN A  34    10285   7395   9781    506   1891    126       O  
ATOM    206  ND2 ASN A  34      63.166  15.549  17.813  1.00 61.95           N  
ANISOU  206  ND2 ASN A  34     8885   6193   8458     89   1675   -100       N  
ATOM    207  N   LEU A  35      68.441  15.082  19.457  1.00 42.12           N  
ANISOU  207  N   LEU A  35     5850   4608   5547    923   1568    376       N  
ATOM    208  CA  LEU A  35      69.703  15.777  19.237  1.00 47.03           C  
ANISOU  208  CA  LEU A  35     6247   5560   6062    942   1435    408       C  
ATOM    209  C   LEU A  35      69.540  16.705  18.038  1.00 47.44           C  
ANISOU  209  C   LEU A  35     6245   5650   6129    684   1346    216       C  
ATOM    210  O   LEU A  35      69.078  16.284  16.972  1.00 51.87           O  
ANISOU  210  O   LEU A  35     6906   6000   6801    621   1461     90       O  
ATOM    211  CB  LEU A  35      70.827  14.774  18.981  1.00 48.05           C  
ANISOU  211  CB  LEU A  35     6305   5747   6206   1226   1568    530       C  
ATOM    212  CG  LEU A  35      72.284  15.239  19.040  1.00 53.06           C  
ANISOU  212  CG  LEU A  35     6678   6755   6729   1322   1453    646       C  
ATOM    213  CD1 LEU A  35      72.661  15.565  20.453  1.00 48.27           C  
ANISOU  213  CD1 LEU A  35     5992   6348   6000   1393   1314    816       C  
ATOM    214  CD2 LEU A  35      73.218  14.177  18.488  1.00 52.31           C  
ANISOU  214  CD2 LEU A  35     6532   6666   6677   1603   1631    738       C  
ATOM    215  N   ALA A  36      69.893  17.972  18.218  1.00 44.41           N  
ANISOU  215  N   ALA A  36     5721   5523   5628    524   1132    194       N  
ATOM    216  CA  ALA A  36      69.790  18.980  17.170  1.00 43.62           C  
ANISOU  216  CA  ALA A  36     5563   5487   5524    268   1020     23       C  
ATOM    217  C   ALA A  36      71.191  19.453  16.769  1.00 48.93           C  
ANISOU  217  C   ALA A  36     6001   6485   6107    295    917     81       C  
ATOM    218  O   ALA A  36      71.978  19.875  17.627  1.00 48.45           O  
ANISOU  218  O   ALA A  36     5805   6681   5923    351    778    223       O  
ATOM    219  CB  ALA A  36      68.931  20.146  17.662  1.00 37.67           C  
ANISOU  219  CB  ALA A  36     4865   4744   4705     34    849    -60       C  
ATOM    220  N   SER A  37      71.494  19.405  15.467  1.00 41.83           N  
ANISOU  220  N   SER A  37     5053   5577   5263    245    979    -20       N  
ATOM    221  CA  SER A  37      72.852  19.601  14.979  1.00 46.81           C  
ANISOU  221  CA  SER A  37     5454   6499   5831    316    938     59       C  
ATOM    222  C   SER A  37      72.929  20.637  13.859  1.00 48.89           C  
ANISOU  222  C   SER A  37     5637   6865   6074     55    823    -95       C  
ATOM    223  O   SER A  37      72.096  20.671  12.946  1.00 42.13           O  
ANISOU  223  O   SER A  37     4919   5788   5302    -93    883   -276       O  
ATOM    224  CB  SER A  37      73.459  18.287  14.487  1.00 49.46           C  
ANISOU  224  CB  SER A  37     5791   6761   6241    606   1175    138       C  
ATOM    225  OG  SER A  37      73.595  17.375  15.559  1.00 47.51           O  
ANISOU  225  OG  SER A  37     5588   6467   5995    862   1264    308       O  
ATOM    226  N   HIS A  38      73.949  21.485  13.954  1.00 41.73           N  
ANISOU  226  N   HIS A  38     4505   6300   5050     -8    645    -10       N  
ATOM    227  CA  HIS A  38      74.315  22.421  12.903  1.00 45.92           C  
ANISOU  227  CA  HIS A  38     4916   6985   5546   -224    536   -113       C  
ATOM    228  C   HIS A  38      75.495  21.833  12.132  1.00 43.88           C  
ANISOU  228  C   HIS A  38     4478   6893   5302    -35    667    -16       C  
ATOM    229  O   HIS A  38      76.586  21.702  12.690  1.00 38.54           O  
ANISOU  229  O   HIS A  38     3600   6486   4557    126    630    189       O  
ATOM    230  CB  HIS A  38      74.704  23.759  13.515  1.00 40.02           C  
ANISOU  230  CB  HIS A  38     4040   6513   4650   -429    244    -67       C  
ATOM    231  CG  HIS A  38      75.080  24.777  12.491  1.00 52.47           C  
ANISOU  231  CG  HIS A  38     5498   8255   6182   -671    113   -163       C  
ATOM    232  ND1 HIS A  38      75.611  26.004  12.814  1.00 53.60           N  
ANISOU  232  ND1 HIS A  38     5511   8669   6186   -874   -157   -117       N  
ATOM    233  CD2 HIS A  38      74.965  24.758  11.144  1.00 51.57           C  
ANISOU  233  CD2 HIS A  38     5395   8059   6140   -753    210   -305       C  
ATOM    234  CE1 HIS A  38      75.821  26.691  11.709  1.00 49.99           C  
ANISOU  234  CE1 HIS A  38     4977   8296   5721  -1069   -217   -221       C  
ATOM    235  NE2 HIS A  38      75.425  25.962  10.684  1.00 50.02           N  
ANISOU  235  NE2 HIS A  38     5064   8090   5850   -998      5   -339       N  
ATOM    236  N   TYR A  39      75.284  21.469  10.864  1.00 47.15           N  
ANISOU  236  N   TYR A  39     4967   7149   5799    -46    822   -152       N  
ATOM    237  CA  TYR A  39      76.347  20.939  10.005  1.00 44.39           C  
ANISOU  237  CA  TYR A  39     4470   6941   5455    139    970    -77       C  
ATOM    238  C   TYR A  39      76.870  22.048   9.108  1.00 49.83           C  
ANISOU  238  C   TYR A  39     4986   7868   6079    -94    829   -137       C  
ATOM    239  O   TYR A  39      76.115  22.585   8.294  1.00 49.31           O  
ANISOU  239  O   TYR A  39     5045   7649   6042   -332    792   -340       O  
ATOM    240  CB  TYR A  39      75.862  19.797   9.110  1.00 47.21           C  
ANISOU  240  CB  TYR A  39     5045   6969   5925    289   1240   -185       C  
ATOM    241  CG  TYR A  39      75.783  18.426   9.729  1.00 38.81           C  
ANISOU  241  CG  TYR A  39     4114   5713   4921    606   1441    -78       C  
ATOM    242  CD1 TYR A  39      74.953  18.177  10.815  1.00 39.57           C  
ANISOU  242  CD1 TYR A  39     4355   5633   5045    606   1409    -60       C  
ATOM    243  CD2 TYR A  39      76.484  17.370   9.189  1.00 43.52           C  
ANISOU  243  CD2 TYR A  39     4712   6282   5541    906   1671      0       C  
ATOM    244  CE1 TYR A  39      74.859  16.928  11.364  1.00 40.55           C  
ANISOU  244  CE1 TYR A  39     4612   5573   5222    883   1588     38       C  
ATOM    245  CE2 TYR A  39      76.396  16.112   9.723  1.00 46.59           C  
ANISOU  245  CE2 TYR A  39     5246   6475   5980   1195   1853     93       C  
ATOM    246  CZ  TYR A  39      75.583  15.893  10.811  1.00 47.71           C  
ANISOU  246  CZ  TYR A  39     5524   6450   6152   1175   1806    113       C  
ATOM    247  OH  TYR A  39      75.497  14.635  11.347  1.00 55.04           O  
ANISOU  247  OH  TYR A  39     6605   7180   7129   1456   1984    211       O  
ATOM    248  N   GLN A  40      78.146  22.327   9.182  1.00 53.60           N  
ANISOU  248  N   GLN A  40     5180   8710   6476    -21    763     44       N  
ATOM    249  CA  GLN A  40      78.735  23.322   8.344  1.00 53.00           C  
ANISOU  249  CA  GLN A  40     4921   8880   6336   -230    637     16       C  
ATOM    250  C   GLN A  40      79.482  22.588   7.266  1.00 56.09           C  
ANISOU  250  C   GLN A  40     5228   9322   6763    -17    872     55       C  
ATOM    251  O   GLN A  40      80.240  21.729   7.542  1.00 57.35           O  
ANISOU  251  O   GLN A  40     5282   9580   6930    290   1018    234       O  
ATOM    252  CB  GLN A  40      79.686  24.119   9.178  1.00 71.31           C  
ANISOU  252  CB  GLN A  40     6972  11587   8537   -299    398    217       C  
ATOM    253  CG  GLN A  40      79.107  25.354   9.792  1.00 84.84           C  
ANISOU  253  CG  GLN A  40     8747  13318  10169   -623    106    136       C  
ATOM    254  CD  GLN A  40      80.066  26.515   9.798  1.00103.57           C  
ANISOU  254  CD  GLN A  40    10861  16076  12415   -832   -151    250       C  
ATOM    255  OE1 GLN A  40      80.670  26.781  10.806  1.00114.29           O  
ANISOU  255  OE1 GLN A  40    12085  17656  13684   -817   -316    434       O  
ATOM    256  NE2 GLN A  40      80.203  27.206   8.692  1.00106.44           N  
ANISOU  256  NE2 GLN A  40    11243  16435  12765  -1006   -187    144       N  
ATOM    257  N   THR A  41      79.251  22.921   6.019  1.00 54.49           N  
ANISOU  257  N   THR A  41     5083   9044   6577   -170    914   -113       N  
ATOM    258  CA  THR A  41      79.906  22.263   4.891  1.00 61.07           C  
ANISOU  258  CA  THR A  41     5870   9905   7430     27   1150    -95       C  
ATOM    259  C   THR A  41      80.452  23.309   3.919  1.00 66.87           C  
ANISOU  259  C   THR A  41     6420  10889   8096   -205   1039   -130       C  
ATOM    260  O   THR A  41      80.211  24.509   4.063  1.00 68.26           O  
ANISOU  260  O   THR A  41     6545  11172   8220   -531    781   -193       O  
ATOM    261  CB  THR A  41      78.948  21.301   4.149  1.00 62.05           C  
ANISOU  261  CB  THR A  41     6337   9588   7651    119   1384   -290       C  
ATOM    262  OG1 THR A  41      78.102  22.039   3.266  1.00 58.59           O  
ANISOU  262  OG1 THR A  41     6048   8987   7227   -201   1298   -528       O  
ATOM    263  CG2 THR A  41      78.067  20.509   5.122  1.00 49.24           C  
ANISOU  263  CG2 THR A  41     4943   7667   6101    231   1435   -302       C  
ATOM    264  N   ASP A  42      81.204  22.844   2.911  1.00 67.90           N  
ANISOU  264  N   ASP A  42     6464  11114   8222    -26   1241    -85       N  
ATOM    265  CA  ASP A  42      81.678  23.751   1.864  1.00 65.70           C  
ANISOU  265  CA  ASP A  42     6032  11048   7883   -237   1169   -127       C  
ATOM    266  C   ASP A  42      80.561  24.183   0.925  1.00 67.37           C  
ANISOU  266  C   ASP A  42     6515  10956   8127   -512   1143   -421       C  
ATOM    267  O   ASP A  42      80.808  24.989   0.031  1.00 68.76           O  
ANISOU  267  O   ASP A  42     6603  11270   8254   -719   1071   -483       O  
ATOM    268  CB  ASP A  42      82.839  23.136   1.063  1.00 67.05           C  
ANISOU  268  CB  ASP A  42     6021  11426   8028     53   1408     24       C  
ATOM    269  CG  ASP A  42      82.487  21.805   0.411  1.00 80.26           C  
ANISOU  269  CG  ASP A  42     7974  12756   9765    354   1738    -72       C  
ATOM    270  OD1 ASP A  42      81.706  21.031   0.990  1.00 85.16           O  
ANISOU  270  OD1 ASP A  42     8843  13060  10454    465   1807   -136       O  
ATOM    271  OD2 ASP A  42      83.023  21.512  -0.682  1.00 87.05           O  
ANISOU  271  OD2 ASP A  42     8812  13666  10598    487   1933    -72       O  
ATOM    272  N   ALA A  43      79.347  23.664   1.095  1.00 67.15           N  
ANISOU  272  N   ALA A  43     6807  10524   8181   -523   1199   -591       N  
ATOM    273  CA  ALA A  43      78.191  24.088   0.317  1.00 58.04           C  
ANISOU  273  CA  ALA A  43     5909   9077   7066   -799   1149   -858       C  
ATOM    274  C   ALA A  43      77.156  24.813   1.176  1.00 58.91           C  
ANISOU  274  C   ALA A  43     6122   9066   7196  -1058    914   -951       C  
ATOM    275  O   ALA A  43      75.980  24.884   0.800  1.00 67.67           O  
ANISOU  275  O   ALA A  43     7482   9863   8366  -1228    901  -1155       O  
ATOM    276  CB  ALA A  43      77.557  22.882  -0.371  1.00 56.24           C  
ANISOU  276  CB  ALA A  43     5990   8460   6919   -620   1412   -986       C  
ATOM    277  N   GLY A  44      77.562  25.345   2.324  1.00 62.56           N  
ANISOU  277  N   GLY A  44     6720   8904   8145   -807   1847    618       N  
ATOM    278  CA  GLY A  44      76.638  25.992   3.235  1.00 55.92           C  
ANISOU  278  CA  GLY A  44     6057   7882   7309   -839   1635    684       C  
ATOM    279  C   GLY A  44      76.159  25.073   4.343  1.00 56.30           C  
ANISOU  279  C   GLY A  44     6102   7874   7415   -710   1388    563       C  
ATOM    280  O   GLY A  44      76.589  23.924   4.478  1.00 61.69           O  
ANISOU  280  O   GLY A  44     6646   8624   8170   -595   1354    442       O  
ATOM    281  N   SER A  45      75.221  25.594   5.135  1.00 48.27           N  
ANISOU  281  N   SER A  45     5249   6727   6366   -727   1218    602       N  
ATOM    282  CA  SER A  45      74.805  24.926   6.364  1.00 45.86           C  
ANISOU  282  CA  SER A  45     4942   6372   6110   -652    988    519       C  
ATOM    283  C   SER A  45      73.619  23.997   6.143  1.00 41.44           C  
ANISOU  283  C   SER A  45     4539   5824   5384   -505    920    485       C  
ATOM    284  O   SER A  45      72.838  24.162   5.207  1.00 51.37           O  
ANISOU  284  O   SER A  45     5947   7103   6467   -471   1002    529       O  
ATOM    285  CB  SER A  45      74.440  25.955   7.431  1.00 49.17           C  
ANISOU  285  CB  SER A  45     5435   6670   6578   -753    851    546       C  
ATOM    286  OG  SER A  45      75.597  26.631   7.869  1.00 50.95           O  
ANISOU  286  OG  SER A  45     5486   6877   6994   -897    862    538       O  
ATOM    287  N   PHE A  46      73.485  23.013   7.039  1.00 47.60           N  
ANISOU  287  N   PHE A  46     5277   6588   6219   -428    756    415       N  
ATOM    288  CA  PHE A  46      72.282  22.182   7.127  1.00 42.46           C  
ANISOU  288  CA  PHE A  46     4769   5918   5445   -329    660    388       C  
ATOM    289  C   PHE A  46      71.887  21.977   8.585  1.00 44.97           C  
ANISOU  289  C   PHE A  46     5104   6181   5801   -342    458    389       C  
ATOM    290  O   PHE A  46      72.735  21.973   9.481  1.00 45.11           O  
ANISOU  290  O   PHE A  46     4994   6197   5949   -380    368    383       O  
ATOM    291  CB  PHE A  46      72.466  20.810   6.457  1.00 43.47           C  
ANISOU  291  CB  PHE A  46     4847   6086   5584   -206    699    299       C  
ATOM    292  CG  PHE A  46      72.732  20.892   4.996  1.00 47.90           C  
ANISOU  292  CG  PHE A  46     5409   6740   6050   -183    905    271       C  
ATOM    293  CD1 PHE A  46      71.700  21.097   4.101  1.00 55.04           C  
ANISOU  293  CD1 PHE A  46     6489   7682   6741   -165    957    291       C  
ATOM    294  CD2 PHE A  46      74.023  20.785   4.513  1.00 53.17           C  
ANISOU  294  CD2 PHE A  46     5891   7481   6829   -181   1048    226       C  
ATOM    295  CE1 PHE A  46      71.955  21.180   2.737  1.00 52.29           C  
ANISOU  295  CE1 PHE A  46     6157   7452   6258   -148   1145    274       C  
ATOM    296  CE2 PHE A  46      74.290  20.874   3.151  1.00 52.66           C  
ANISOU  296  CE2 PHE A  46     5830   7539   6641   -171   1265    199       C  
ATOM    297  CZ  PHE A  46      73.250  21.067   2.266  1.00 51.46           C  
ANISOU  297  CZ  PHE A  46     5880   7431   6242   -156   1310    228       C  
ATOM    298  N   PHE A  47      70.582  21.824   8.815  1.00 39.25           N  
ANISOU  298  N   PHE A  47     4531   5435   4947   -316    388    398       N  
ATOM    299  CA  PHE A  47      70.045  21.569  10.139  1.00 40.83           C  
ANISOU  299  CA  PHE A  47     4765   5614   5133   -335    226    406       C  
ATOM    300  C   PHE A  47      69.548  20.127  10.200  1.00 43.30           C  
ANISOU  300  C   PHE A  47     5103   5914   5436   -258    157    393       C  
ATOM    301  O   PHE A  47      68.821  19.660   9.317  1.00 43.29           O  
ANISOU  301  O   PHE A  47     5174   5912   5361   -206    214    362       O  
ATOM    302  CB  PHE A  47      68.931  22.563  10.509  1.00 42.35           C  
ANISOU  302  CB  PHE A  47     5086   5795   5209   -379    208    419       C  
ATOM    303  CG  PHE A  47      68.398  22.348  11.886  1.00 48.91           C  
ANISOU  303  CG  PHE A  47     5944   6643   5995   -409     72    414       C  
ATOM    304  CD1 PHE A  47      69.160  22.687  12.995  1.00 53.77           C  
ANISOU  304  CD1 PHE A  47     6492   7274   6665   -476    -22    404       C  
ATOM    305  CD2 PHE A  47      67.157  21.760  12.087  1.00 46.90           C  
ANISOU  305  CD2 PHE A  47     5774   6412   5633   -382     36    417       C  
ATOM    306  CE1 PHE A  47      68.692  22.446  14.289  1.00 49.71           C  
ANISOU  306  CE1 PHE A  47     6013   6810   6064   -508   -145    405       C  
ATOM    307  CE2 PHE A  47      66.688  21.522  13.361  1.00 44.67           C  
ANISOU  307  CE2 PHE A  47     5514   6172   5287   -424    -65    426       C  
ATOM    308  CZ  PHE A  47      67.458  21.858  14.468  1.00 46.79           C  
ANISOU  308  CZ  PHE A  47     5734   6469   5575   -484   -153    425       C  
ATOM    309  N   VAL A  48      69.974  19.418  11.220  1.00 36.63           N  
ANISOU  309  N   VAL A  48     4198   5049   4669   -254     26    419       N  
ATOM    310  CA  VAL A  48      69.741  17.992  11.337  1.00 45.27           C  
ANISOU  310  CA  VAL A  48     5306   6086   5810   -187    -49    429       C  
ATOM    311  C   VAL A  48      69.226  17.693  12.737  1.00 49.58           C  
ANISOU  311  C   VAL A  48     5906   6633   6299   -242   -202    514       C  
ATOM    312  O   VAL A  48      69.747  18.225  13.726  1.00 48.33           O  
ANISOU  312  O   VAL A  48     5703   6524   6135   -294   -288    550       O  
ATOM    313  CB  VAL A  48      71.034  17.213  11.068  1.00 44.92           C  
ANISOU  313  CB  VAL A  48     5113   6001   5955    -99    -58    401       C  
ATOM    314  CG1 VAL A  48      70.836  15.734  11.329  1.00 40.11           C  
ANISOU  314  CG1 VAL A  48     4527   5280   5432    -23   -163    424       C  
ATOM    315  CG2 VAL A  48      71.543  17.489   9.667  1.00 42.00           C  
ANISOU  315  CG2 VAL A  48     4683   5666   5608    -54    125    309       C  
ATOM    316  N   LYS A  49      68.198  16.849  12.818  1.00 48.55           N  
ANISOU  316  N   LYS A  49     5870   6461   6116   -244   -232    542       N  
ATOM    317  CA  LYS A  49      67.734  16.280  14.080  1.00 45.70           C  
ANISOU  317  CA  LYS A  49     5563   6100   5703   -301   -360    650       C  
ATOM    318  C   LYS A  49      67.787  14.765  14.007  1.00 43.61           C  
ANISOU  318  C   LYS A  49     5309   5696   5566   -249   -430    704       C  
ATOM    319  O   LYS A  49      67.449  14.166  12.980  1.00 47.31           O  
ANISOU  319  O   LYS A  49     5796   6082   6098   -201   -362    625       O  
ATOM    320  CB  LYS A  49      66.325  16.748  14.428  1.00 48.22           C  
ANISOU  320  CB  LYS A  49     5980   6497   5844   -387   -323    651       C  
ATOM    321  CG  LYS A  49      66.283  18.203  14.737  1.00 49.01           C  
ANISOU  321  CG  LYS A  49     6078   6700   5843   -428   -282    599       C  
ATOM    322  CD  LYS A  49      64.955  18.629  15.332  1.00 44.91           C  
ANISOU  322  CD  LYS A  49     5631   6272   5161   -496   -258    590       C  
ATOM    323  CE  LYS A  49      63.885  18.790  14.266  1.00 48.02           C  
ANISOU  323  CE  LYS A  49     6056   6660   5530   -465   -158    523       C  
ATOM    324  NZ  LYS A  49      62.592  19.266  14.837  1.00 55.90           N  
ANISOU  324  NZ  LYS A  49     7084   7760   6394   -514   -129    496       N  
ATOM    325  N   THR A  50      68.256  14.151  15.084  1.00 44.38           N  
ANISOU  325  N   THR A  50     5397   5760   5706   -254   -578    837       N  
ATOM    326  CA  THR A  50      68.332  12.701  15.183  1.00 47.44           C  
ANISOU  326  CA  THR A  50     5809   5975   6242   -204   -671    924       C  
ATOM    327  C   THR A  50      67.684  12.256  16.486  1.00 53.71           C  
ANISOU  327  C   THR A  50     6703   6785   6919   -312   -784   1115       C  
ATOM    328  O   THR A  50      67.605  13.012  17.459  1.00 49.72           O  
ANISOU  328  O   THR A  50     6215   6443   6234   -393   -822   1175       O  
ATOM    329  CB  THR A  50      69.799  12.154  15.117  1.00 45.42           C  
ANISOU  329  CB  THR A  50     5425   5623   6212    -61   -764    933       C  
ATOM    330  OG1 THR A  50      70.625  12.842  16.059  1.00 50.82           O  
ANISOU  330  OG1 THR A  50     6028   6435   6847    -77   -869   1002       O  
ATOM    331  CG2 THR A  50      70.375  12.327  13.772  1.00 44.68           C  
ANISOU  331  CG2 THR A  50     5231   5509   6237     41   -626    747       C  
ATOM    332  N   ASN A  51      67.180  11.032  16.480  1.00 53.53           N  
ANISOU  332  N   ASN A  51     6755   6593   6991   -326   -826   1203       N  
ATOM    333  CA  ASN A  51      66.722  10.410  17.719  1.00 61.46           C  
ANISOU  333  CA  ASN A  51     7857   7587   7909   -432   -937   1433       C  
ATOM    334  C   ASN A  51      66.949   8.916  17.561  1.00 69.50           C  
ANISOU  334  C   ASN A  51     8912   8321   9172   -370  -1035   1537       C  
ATOM    335  O   ASN A  51      66.310   8.285  16.711  1.00 68.02           O  
ANISOU  335  O   ASN A  51     8761   7982   9102   -382   -960   1444       O  
ATOM    336  CB  ASN A  51      65.268  10.719  18.013  1.00 57.90           C  
ANISOU  336  CB  ASN A  51     7488   7260   7250   -600   -833   1445       C  
ATOM    337  CG  ASN A  51      64.898  10.331  19.413  1.00 67.37           C  
ANISOU  337  CG  ASN A  51     8777   8526   8294   -728   -920   1687       C  
ATOM    338  OD1 ASN A  51      65.165   9.198  19.833  1.00 73.60           O  
ANISOU  338  OD1 ASN A  51     9624   9140   9201   -727  -1042   1883       O  
ATOM    339  ND2 ASN A  51      64.296  11.265  20.163  1.00 58.03           N  
ANISOU  339  ND2 ASN A  51     7611   7595   6842   -836   -857   1680       N  
ATOM    340  N   ARG A  52      67.849   8.360  18.380  1.00 73.35           N  
ANISOU  340  N   ARG A  52     9393   8731   9745   -301  -1215   1723       N  
ATOM    341  CA  ARG A  52      68.263   6.969  18.236  1.00 85.96           C  
ANISOU  341  CA  ARG A  52    11016  10018  11628   -199  -1333   1824       C  
ATOM    342  C   ARG A  52      67.191   5.989  18.688  1.00 95.17           C  
ANISOU  342  C   ARG A  52    12342  11026  12792   -353  -1353   2017       C  
ATOM    343  O   ARG A  52      67.297   4.800  18.369  1.00 98.59           O  
ANISOU  343  O   ARG A  52    12817  11146  13495   -291  -1422   2064       O  
ATOM    344  CB  ARG A  52      69.558   6.713  19.020  1.00 94.18           C  
ANISOU  344  CB  ARG A  52    11988  11030  12765    -63  -1546   1988       C  
ATOM    345  CG  ARG A  52      70.804   7.402  18.456  1.00105.63           C  
ANISOU  345  CG  ARG A  52    13238  12573  14322    106  -1538   1793       C  
ATOM    346  CD  ARG A  52      72.037   7.206  19.356  1.00118.50           C  
ANISOU  346  CD  ARG A  52    14773  14216  16034    228  -1777   1961       C  
ATOM    347  NE  ARG A  52      73.161   8.066  18.967  1.00126.56           N  
ANISOU  347  NE  ARG A  52    15577  15392  17119    337  -1758   1777       N  
ATOM    348  CZ  ARG A  52      74.359   8.069  19.556  1.00129.69           C  
ANISOU  348  CZ  ARG A  52    15824  15840  17614    456  -1953   1855       C  
ATOM    349  NH1 ARG A  52      74.612   7.254  20.572  1.00131.74           N  
ANISOU  349  NH1 ARG A  52    16142  16009  17905    504  -2203   2129       N  
ATOM    350  NH2 ARG A  52      75.310   8.891  19.128  1.00126.75           N  
ANISOU  350  NH2 ARG A  52    15235  15614  17310    521  -1906   1669       N  
ATOM    351  N   SER A  53      66.157   6.455  19.394  1.00 96.63           N  
ANISOU  351  N   SER A  53    12607  11411  12698   -554  -1285   2115       N  
ATOM    352  CA  SER A  53      65.167   5.547  19.955  1.00101.36           C  
ANISOU  352  CA  SER A  53    13343  11890  13280   -733  -1295   2333       C  
ATOM    353  C   SER A  53      63.967   5.310  19.046  1.00102.61           C  
ANISOU  353  C   SER A  53    13515  11973  13500   -849  -1135   2166       C  
ATOM    354  O   SER A  53      63.408   4.207  19.067  1.00 94.73           O  
ANISOU  354  O   SER A  53    12604  10731  12657   -950  -1160   2288       O  
ATOM    355  CB  SER A  53      64.656   6.091  21.297  1.00104.26           C  
ANISOU  355  CB  SER A  53    13777  12542  13295   -905  -1294   2539       C  
ATOM    356  OG  SER A  53      63.753   7.185  21.132  1.00100.63           O  
ANISOU  356  OG  SER A  53    13273  12358  12602  -1011  -1110   2354       O  
ATOM    357  N   ILE A  54      63.614   6.284  18.197  1.00102.90           N  
ANISOU  357  N   ILE A  54    13465  12190  13443   -829   -988   1891       N  
ATOM    358  CA  ILE A  54      62.318   6.344  17.521  1.00 97.47           C  
ANISOU  358  CA  ILE A  54    12772  11540  12721   -961   -846   1742       C  
ATOM    359  C   ILE A  54      62.463   5.970  16.053  1.00 99.39           C  
ANISOU  359  C   ILE A  54    12973  11603  13189   -844   -813   1480       C  
ATOM    360  O   ILE A  54      63.472   6.294  15.417  1.00103.93           O  
ANISOU  360  O   ILE A  54    13483  12166  13839   -657   -822   1337       O  
ATOM    361  CB  ILE A  54      61.691   7.744  17.621  1.00 83.53           C  
ANISOU  361  CB  ILE A  54    10946  10120  10672  -1015   -717   1626       C  
ATOM    362  CG1 ILE A  54      61.545   8.195  19.068  1.00 82.51           C  
ANISOU  362  CG1 ILE A  54    10857  10207  10288  -1125   -732   1833       C  
ATOM    363  CG2 ILE A  54      60.333   7.747  16.981  1.00 84.28           C  
ANISOU  363  CG2 ILE A  54    11013  10262  10747  -1140   -597   1492       C  
ATOM    364  CD1 ILE A  54      60.791   9.539  19.168  1.00 77.94           C  
ANISOU  364  CD1 ILE A  54    10215   9941   9457  -1175   -593   1687       C  
ATOM    365  N   GLY A  55      61.457   5.263  15.526  1.00 92.14           N  
ANISOU  365  N   GLY A  55    12084  10555  12372   -967   -772   1411       N  
ATOM    366  CA  GLY A  55      61.342   4.992  14.112  1.00 79.37           C  
ANISOU  366  CA  GLY A  55    10431   8824  10901   -892   -730   1126       C  
ATOM    367  C   GLY A  55      60.916   6.227  13.336  1.00 71.24           C  
ANISOU  367  C   GLY A  55     9320   8083   9665   -861   -611    909       C  
ATOM    368  O   GLY A  55      60.446   7.223  13.902  1.00 72.14           O  
ANISOU  368  O   GLY A  55     9404   8457   9551   -927   -552    970       O  
ATOM    369  N   PRO A  56      61.033   6.158  12.006  1.00 68.03           N  
ANISOU  369  N   PRO A  56     8884   7632   9334   -758   -576    649       N  
ATOM    370  CA  PRO A  56      60.999   7.377  11.172  1.00 61.62           C  
ANISOU  370  CA  PRO A  56     8006   7072   8332   -674   -480    470       C  
ATOM    371  C   PRO A  56      59.640   8.041  10.978  1.00 61.79           C  
ANISOU  371  C   PRO A  56     7994   7308   8175   -796   -419    412       C  
ATOM    372  O   PRO A  56      59.600   9.126  10.384  1.00 63.54           O  
ANISOU  372  O   PRO A  56     8174   7731   8238   -719   -355    306       O  
ATOM    373  CB  PRO A  56      61.559   6.887   9.830  1.00 58.91           C  
ANISOU  373  CB  PRO A  56     7658   6607   8120   -534   -467    226       C  
ATOM    374  CG  PRO A  56      61.351   5.411   9.835  1.00 65.54           C  
ANISOU  374  CG  PRO A  56     8556   7136   9212   -594   -549    215       C  
ATOM    375  CD  PRO A  56      61.507   4.980  11.260  1.00 66.48           C  
ANISOU  375  CD  PRO A  56     8719   7134   9405   -674   -630    518       C  
ATOM    376  N   ALA A  57      58.539   7.474  11.476  1.00 60.29           N  
ANISOU  376  N   ALA A  57     7809   7087   8011   -982   -435    489       N  
ATOM    377  CA  ALA A  57      57.211   8.011  11.169  1.00 59.89           C  
ANISOU  377  CA  ALA A  57     7687   7240   7828  -1085   -384    399       C  
ATOM    378  C   ALA A  57      57.057   9.459  11.611  1.00 55.93           C  
ANISOU  378  C   ALA A  57     7135   7018   7100  -1041   -314    441       C  
ATOM    379  O   ALA A  57      56.445  10.269  10.903  1.00 57.67           O  
ANISOU  379  O   ALA A  57     7294   7411   7206   -998   -278    307       O  
ATOM    380  CB  ALA A  57      56.127   7.153  11.825  1.00 56.60           C  
ANISOU  380  CB  ALA A  57     7258   6755   7492  -1317   -397    505       C  
ATOM    381  N   MET A  58      57.578   9.807  12.785  1.00 55.11           N  
ANISOU  381  N   MET A  58     7057   6955   6927  -1048   -307    623       N  
ATOM    382  CA  MET A  58      57.406  11.174  13.271  1.00 54.89           C  
ANISOU  382  CA  MET A  58     6986   7170   6700  -1014   -242    635       C  
ATOM    383  C   MET A  58      58.145  12.184  12.377  1.00 53.44           C  
ANISOU  383  C   MET A  58     6795   7043   6467   -833   -221    507       C  
ATOM    384  O   MET A  58      57.561  13.194  11.960  1.00 59.04           O  
ANISOU  384  O   MET A  58     7458   7911   7063   -791   -173    417       O  
ATOM    385  CB  MET A  58      57.850  11.277  14.738  1.00 54.97           C  
ANISOU  385  CB  MET A  58     7035   7222   6630  -1070   -252    835       C  
ATOM    386  CG  MET A  58      57.886  12.720  15.264  1.00 76.85           C  
ANISOU  386  CG  MET A  58     9775  10215   9210  -1016   -194    810       C  
ATOM    387  SD  MET A  58      58.731  13.022  16.852  1.00 95.91           S  
ANISOU  387  SD  MET A  58    12243  12705  11494  -1044   -231    987       S  
ATOM    388  CE  MET A  58      60.468  13.022  16.399  1.00 86.56           C  
ANISOU  388  CE  MET A  58    11084  11364  10439   -880   -326    980       C  
ATOM    389  N   PHE A  59      59.425  11.925  12.047  1.00 52.32           N  
ANISOU  389  N   PHE A  59     6691   6768   6419   -725   -254    503       N  
ATOM    390  CA  PHE A  59      60.164  12.868  11.197  1.00 50.85           C  
ANISOU  390  CA  PHE A  59     6492   6645   6185   -581   -211    400       C  
ATOM    391  C   PHE A  59      59.601  12.919   9.785  1.00 48.15           C  
ANISOU  391  C   PHE A  59     6140   6338   5815   -534   -182    231       C  
ATOM    392  O   PHE A  59      59.553  13.997   9.184  1.00 54.44           O  
ANISOU  392  O   PHE A  59     6926   7262   6497   -461   -134    177       O  
ATOM    393  CB  PHE A  59      61.659  12.516  11.119  1.00 53.20           C  
ANISOU  393  CB  PHE A  59     6796   6814   6603   -481   -237    419       C  
ATOM    394  CG  PHE A  59      62.440  12.891  12.350  1.00 51.46           C  
ANISOU  394  CG  PHE A  59     6569   6617   6367   -488   -277    565       C  
ATOM    395  CD1 PHE A  59      62.130  14.038  13.057  1.00 46.79           C  
ANISOU  395  CD1 PHE A  59     5969   6190   5620   -529   -248    604       C  
ATOM    396  CD2 PHE A  59      63.502  12.106  12.780  1.00 61.46           C  
ANISOU  396  CD2 PHE A  59     7832   7742   7778   -442   -357    648       C  
ATOM    397  CE1 PHE A  59      62.840  14.385  14.211  1.00 49.35           C  
ANISOU  397  CE1 PHE A  59     6289   6555   5906   -546   -300    712       C  
ATOM    398  CE2 PHE A  59      64.225  12.450  13.916  1.00 52.64           C  
ANISOU  398  CE2 PHE A  59     6701   6671   6628   -449   -424    781       C  
ATOM    399  CZ  PHE A  59      63.885  13.591  14.631  1.00 45.02           C  
ANISOU  399  CZ  PHE A  59     5736   5890   5481   -511   -395    805       C  
ATOM    400  N   GLU A  60      59.115  11.792   9.262  1.00 50.47           N  
ANISOU  400  N   GLU A  60     6444   6525   6207   -584   -223    150       N  
ATOM    401  CA  GLU A  60      58.520  11.807   7.929  1.00 55.14           C  
ANISOU  401  CA  GLU A  60     7027   7181   6743   -549   -218    -29       C  
ATOM    402  C   GLU A  60      57.269  12.680   7.904  1.00 53.37           C  
ANISOU  402  C   GLU A  60     6747   7154   6377   -589   -212    -37       C  
ATOM    403  O   GLU A  60      57.059  13.449   6.957  1.00 56.18           O  
ANISOU  403  O   GLU A  60     7099   7638   6610   -501   -200   -119       O  
ATOM    404  CB  GLU A  60      58.225  10.378   7.474  1.00 57.59           C  
ANISOU  404  CB  GLU A  60     7356   7320   7205   -614   -278   -139       C  
ATOM    405  CG  GLU A  60      59.514   9.627   7.097  1.00 70.43           C  
ANISOU  405  CG  GLU A  60     9027   8758   8976   -509   -277   -201       C  
ATOM    406  CD  GLU A  60      59.349   8.118   6.933  1.00 77.75           C  
ANISOU  406  CD  GLU A  60     9987   9438  10116   -572   -346   -291       C  
ATOM    407  OE1 GLU A  60      58.214   7.602   7.058  1.00 76.38           O  
ANISOU  407  OE1 GLU A  60     9802   9237   9982   -725   -395   -307       O  
ATOM    408  OE2 GLU A  60      60.378   7.442   6.694  1.00 83.45           O  
ANISOU  408  OE2 GLU A  60    10736   9983  10991   -469   -350   -351       O  
ATOM    409  N   GLY A  61      56.466  12.630   8.968  1.00 47.39           N  
ANISOU  409  N   GLY A  61     5943   6436   5627   -710   -216     60       N  
ATOM    410  CA  GLY A  61      55.312  13.519   9.049  1.00 46.85           C  
ANISOU  410  CA  GLY A  61     5792   6563   5445   -725   -200     43       C  
ATOM    411  C   GLY A  61      55.712  14.979   9.159  1.00 47.08           C  
ANISOU  411  C   GLY A  61     5831   6699   5357   -601   -151     81       C  
ATOM    412  O   GLY A  61      55.088  15.851   8.545  1.00 51.57           O  
ANISOU  412  O   GLY A  61     6362   7394   5839   -524   -154     23       O  
ATOM    413  N   GLU A  62      56.778  15.261   9.914  1.00 46.85           N  
ANISOU  413  N   GLU A  62     5854   6608   5338   -579   -119    179       N  
ATOM    414  CA  GLU A  62      57.313  16.619   9.989  1.00 45.38           C  
ANISOU  414  CA  GLU A  62     5687   6481   5074   -477    -76    202       C  
ATOM    415  C   GLU A  62      57.764  17.126   8.617  1.00 48.34           C  
ANISOU  415  C   GLU A  62     6099   6857   5409   -357    -65    138       C  
ATOM    416  O   GLU A  62      57.499  18.279   8.250  1.00 48.90           O  
ANISOU  416  O   GLU A  62     6172   7005   5402   -279    -46    136       O  
ATOM    417  CB  GLU A  62      58.485  16.667  10.990  1.00 43.72           C  
ANISOU  417  CB  GLU A  62     5513   6200   4898   -493    -67    299       C  
ATOM    418  CG  GLU A  62      59.071  18.086  11.140  1.00 53.48           C  
ANISOU  418  CG  GLU A  62     6763   7477   6079   -418    -27    307       C  
ATOM    419  CD  GLU A  62      60.148  18.220  12.225  1.00 63.51           C  
ANISOU  419  CD  GLU A  62     8048   8711   7372   -448    -41    382       C  
ATOM    420  OE1 GLU A  62      60.520  17.208  12.845  1.00 64.73           O  
ANISOU  420  OE1 GLU A  62     8209   8809   7578   -508    -89    452       O  
ATOM    421  OE2 GLU A  62      60.603  19.360  12.477  1.00 62.65           O  
ANISOU  421  OE2 GLU A  62     7945   8624   7236   -415    -17    373       O  
ATOM    422  N   ALA A  63      58.487  16.289   7.860  1.00 44.43           N  
ANISOU  422  N   ALA A  63     5640   6274   4966   -337    -71     91       N  
ATOM    423  CA  ALA A  63      58.987  16.711   6.555  1.00 43.96           C  
ANISOU  423  CA  ALA A  63     5621   6247   4834   -236    -36     34       C  
ATOM    424  C   ALA A  63      57.841  17.023   5.594  1.00 50.93           C  
ANISOU  424  C   ALA A  63     6497   7255   5598   -201    -78    -36       C  
ATOM    425  O   ALA A  63      57.883  18.025   4.867  1.00 47.62           O  
ANISOU  425  O   ALA A  63     6113   6914   5068   -114    -57    -11       O  
ATOM    426  CB  ALA A  63      59.908  15.636   5.965  1.00 43.64           C  
ANISOU  426  CB  ALA A  63     5604   6105   4871   -217    -22    -41       C  
ATOM    427  N   LEU A  64      56.812  16.170   5.562  1.00 49.82           N  
ANISOU  427  N   LEU A  64     6309   7136   5487   -273   -149   -116       N  
ATOM    428  CA  LEU A  64      55.685  16.443   4.672  1.00 54.75           C  
ANISOU  428  CA  LEU A  64     6898   7901   6002   -240   -219   -192       C  
ATOM    429  C   LEU A  64      54.883  17.657   5.132  1.00 51.68           C  
ANISOU  429  C   LEU A  64     6452   7616   5568   -193   -227   -118       C  
ATOM    430  O   LEU A  64      54.338  18.383   4.294  1.00 48.72           O  
ANISOU  430  O   LEU A  64     6075   7352   5085    -97   -277   -128       O  
ATOM    431  CB  LEU A  64      54.777  15.219   4.553  1.00 58.08           C  
ANISOU  431  CB  LEU A  64     7257   8318   6495   -351   -299   -313       C  
ATOM    432  CG  LEU A  64      55.335  14.013   3.791  1.00 58.92           C  
ANISOU  432  CG  LEU A  64     7421   8319   6647   -374   -316   -448       C  
ATOM    433  CD1 LEU A  64      54.412  12.830   3.928  1.00 62.94           C  
ANISOU  433  CD1 LEU A  64     7865   8774   7277   -519   -397   -553       C  
ATOM    434  CD2 LEU A  64      55.566  14.334   2.321  1.00 50.33           C  
ANISOU  434  CD2 LEU A  64     6397   7347   5381   -262   -328   -549       C  
ATOM    435  N   GLY A  65      54.811  17.903   6.446  1.00 47.81           N  
ANISOU  435  N   GLY A  65     5919   7095   5152   -247   -185    -48       N  
ATOM    436  CA  GLY A  65      54.169  19.122   6.920  1.00 44.97           C  
ANISOU  436  CA  GLY A  65     5507   6816   4763   -181   -175     -8       C  
ATOM    437  C   GLY A  65      54.919  20.365   6.480  1.00 49.51           C  
ANISOU  437  C   GLY A  65     6173   7355   5283    -56   -142     63       C  
ATOM    438  O   GLY A  65      54.328  21.319   5.964  1.00 51.26           O  
ANISOU  438  O   GLY A  65     6386   7637   5453     54   -180     78       O  
ATOM    439  N   LEU A  66      56.240  20.361   6.666  1.00 44.71           N  
ANISOU  439  N   LEU A  66     5647   6641   4702    -74    -76    116       N  
ATOM    440  CA  LEU A  66      57.052  21.493   6.236  1.00 45.28           C  
ANISOU  440  CA  LEU A  66     5799   6663   4742      8    -29    193       C  
ATOM    441  C   LEU A  66      56.798  21.699   4.755  1.00 47.45           C  
ANISOU  441  C   LEU A  66     6124   7008   4896     95    -64    197       C  
ATOM    442  O   LEU A  66      56.450  22.808   4.333  1.00 56.45           O  
ANISOU  442  O   LEU A  66     7296   8164   5986    190    -85    265       O  
ATOM    443  CB  LEU A  66      58.533  21.277   6.598  1.00 39.37           C  
ANISOU  443  CB  LEU A  66     5092   5811   4055    -44     43    232       C  
ATOM    444  CG  LEU A  66      58.901  21.309   8.084  1.00 42.38           C  
ANISOU  444  CG  LEU A  66     5440   6140   4523   -118     57    250       C  
ATOM    445  CD1 LEU A  66      60.296  20.766   8.328  1.00 44.56           C  
ANISOU  445  CD1 LEU A  66     5725   6335   4869   -163     89    276       C  
ATOM    446  CD2 LEU A  66      58.748  22.729   8.663  1.00 42.88           C  
ANISOU  446  CD2 LEU A  66     5512   6185   4594    -79     75    274       C  
ATOM    447  N   GLU A  67      56.980  20.643   3.951  1.00 46.70           N  
ANISOU  447  N   GLU A  67     6044   6951   4748     68    -78    124       N  
ATOM    448  CA  GLU A  67      56.819  20.781   2.507  1.00 52.72           C  
ANISOU  448  CA  GLU A  67     6868   7815   5347    143   -111    116       C  
ATOM    449  C   GLU A  67      55.510  21.437   2.079  1.00 55.35           C  
ANISOU  449  C   GLU A  67     7169   8261   5599    229   -227    133       C  
ATOM    450  O   GLU A  67      55.507  22.338   1.226  1.00 53.68           O  
ANISOU  450  O   GLU A  67     7035   8095   5265    327   -245    232       O  
ATOM    451  CB  GLU A  67      57.007  19.428   1.822  1.00 48.41           C  
ANISOU  451  CB  GLU A  67     6328   7303   4762     96   -122    -26       C  
ATOM    452  CG  GLU A  67      56.990  19.521   0.290  1.00 50.04           C  
ANISOU  452  CG  GLU A  67     6614   7648   4752    167   -143    -55       C  
ATOM    453  CD  GLU A  67      58.082  20.470  -0.287  1.00 71.52           C  
ANISOU  453  CD  GLU A  67     9437  10368   7370    220    -21     84       C  
ATOM    454  OE1 GLU A  67      59.240  20.477   0.195  1.00 74.87           O  
ANISOU  454  OE1 GLU A  67     9862  10685   7899    181    102    120       O  
ATOM    455  OE2 GLU A  67      57.785  21.215  -1.245  1.00 76.14           O  
ANISOU  455  OE2 GLU A  67    10097  11066   7768    294    -52    170       O  
ATOM    456  N   ALA A  68      54.391  21.010   2.676  1.00 46.58           N  
ANISOU  456  N   ALA A  68     5936   7199   4564    194   -306     50       N  
ATOM    457  CA  ALA A  68      53.099  21.622   2.371  1.00 47.52           C  
ANISOU  457  CA  ALA A  68     5977   7435   4642    288   -425     51       C  
ATOM    458  C   ALA A  68      53.090  23.112   2.712  1.00 49.97           C  
ANISOU  458  C   ALA A  68     6316   7680   4989    406   -405    181       C  
ATOM    459  O   ALA A  68      52.621  23.933   1.918  1.00 52.78           O  
ANISOU  459  O   ALA A  68     6703   8089   5261    539   -491    258       O  
ATOM    460  CB  ALA A  68      51.985  20.897   3.126  1.00 47.43           C  
ANISOU  460  CB  ALA A  68     5795   7488   4739    203   -478    -65       C  
ATOM    461  N   MET A  69      53.573  23.483   3.908  1.00 46.33           N  
ANISOU  461  N   MET A  69     5850   7097   4657    363   -306    204       N  
ATOM    462  CA  MET A  69      53.599  24.902   4.266  1.00 48.23           C  
ANISOU  462  CA  MET A  69     6125   7242   4958    468   -286    294       C  
ATOM    463  C   MET A  69      54.571  25.667   3.389  1.00 51.78           C  
ANISOU  463  C   MET A  69     6735   7601   5336    517   -249    441       C  
ATOM    464  O   MET A  69      54.296  26.810   2.988  1.00 54.32           O  
ANISOU  464  O   MET A  69     7111   7869   5658    642   -294    549       O  
ATOM    465  CB  MET A  69      53.938  25.103   5.742  1.00 42.44           C  
ANISOU  465  CB  MET A  69     5355   6416   4355    397   -194    253       C  
ATOM    466  CG  MET A  69      52.897  24.515   6.695  1.00 46.60           C  
ANISOU  466  CG  MET A  69     5720   7050   4936    345   -205    133       C  
ATOM    467  SD  MET A  69      53.317  24.855   8.415  1.00 55.14           S  
ANISOU  467  SD  MET A  69     6784   8062   6106    268    -95     90       S  
ATOM    468  CE  MET A  69      54.918  24.049   8.485  1.00 51.14           C  
ANISOU  468  CE  MET A  69     6392   7459   5581    129    -39    152       C  
ATOM    469  N   TYR A  70      55.699  25.039   3.059  1.00 51.60           N  
ANISOU  469  N   TYR A  70     6786   7560   5260    422   -165    453       N  
ATOM    470  CA  TYR A  70      56.690  25.692   2.216  1.00 53.18           C  
ANISOU  470  CA  TYR A  70     7121   7701   5383    438    -96    594       C  
ATOM    471  C   TYR A  70      56.112  26.053   0.849  1.00 55.68           C  
ANISOU  471  C   TYR A  70     7511   8129   5517    549   -187    687       C  
ATOM    472  O   TYR A  70      56.342  27.159   0.341  1.00 60.85           O  
ANISOU  472  O   TYR A  70     8273   8711   6138    616   -178    861       O  
ATOM    473  CB  TYR A  70      57.908  24.788   2.067  1.00 49.18           C  
ANISOU  473  CB  TYR A  70     6636   7197   4852    327     14    553       C  
ATOM    474  CG  TYR A  70      59.101  25.482   1.467  1.00 47.14           C  
ANISOU  474  CG  TYR A  70     6481   6876   4554    307    132    691       C  
ATOM    475  CD1 TYR A  70      59.276  25.536   0.098  1.00 41.68           C  
ANISOU  475  CD1 TYR A  70     5882   6293   3660    343    154    770       C  
ATOM    476  CD2 TYR A  70      60.040  26.121   2.279  1.00 49.18           C  
ANISOU  476  CD2 TYR A  70     6739   6982   4967    241    222    742       C  
ATOM    477  CE1 TYR A  70      60.379  26.188  -0.460  1.00 49.09           C  
ANISOU  477  CE1 TYR A  70     6907   7190   4554    302    290    914       C  
ATOM    478  CE2 TYR A  70      61.132  26.781   1.732  1.00 50.40           C  
ANISOU  478  CE2 TYR A  70     6965   7078   5106    196    341    873       C  
ATOM    479  CZ  TYR A  70      61.297  26.803   0.363  1.00 53.05           C  
ANISOU  479  CZ  TYR A  70     7388   7525   5243    223    386    967       C  
ATOM    480  OH  TYR A  70      62.384  27.431  -0.182  1.00 64.05           O  
ANISOU  480  OH  TYR A  70     8843   8880   6612    157    529   1109       O  
ATOM    481  N   GLU A  71      55.333  25.150   0.251  1.00 50.84           N  
ANISOU  481  N   GLU A  71     6844   7688   4785    563   -289    581       N  
ATOM    482  CA  GLU A  71      54.828  25.378  -1.102  1.00 55.03           C  
ANISOU  482  CA  GLU A  71     7446   8366   5097    661   -397    656       C  
ATOM    483  C   GLU A  71      53.735  26.443  -1.180  1.00 59.06           C  
ANISOU  483  C   GLU A  71     7934   8873   5634    820   -544    761       C  
ATOM    484  O   GLU A  71      53.438  26.906  -2.285  1.00 66.24           O  
ANISOU  484  O   GLU A  71     8931   9876   6360    921   -642    890       O  
ATOM    485  CB  GLU A  71      54.323  24.073  -1.716  1.00 55.12           C  
ANISOU  485  CB  GLU A  71     7399   8566   4978    620   -480    475       C  
ATOM    486  CG  GLU A  71      55.446  23.155  -2.200  1.00 64.86           C  
ANISOU  486  CG  GLU A  71     8703   9827   6116    519   -352    394       C  
ATOM    487  CD  GLU A  71      54.985  21.731  -2.491  1.00 74.55           C  
ANISOU  487  CD  GLU A  71     9857  11168   7299    455   -425    161       C  
ATOM    488  OE1 GLU A  71      53.801  21.413  -2.242  1.00 81.44           O  
ANISOU  488  OE1 GLU A  71    10611  12104   8229    460   -570     66       O  
ATOM    489  OE2 GLU A  71      55.806  20.925  -2.973  1.00 77.12           O  
ANISOU  489  OE2 GLU A  71    10234  11517   7551    397   -334     58       O  
ATOM    490  N   THR A  72      53.093  26.819  -0.065  1.00 53.54           N  
ANISOU  490  N   THR A  72     7114   8082   5147    857   -568    705       N  
ATOM    491  CA  THR A  72      52.123  27.913  -0.155  1.00 56.86           C  
ANISOU  491  CA  THR A  72     7504   8475   5624   1039   -701    798       C  
ATOM    492  C   THR A  72      52.785  29.244  -0.462  1.00 60.67           C  
ANISOU  492  C   THR A  72     8160   8765   6126   1113   -657   1030       C  
ATOM    493  O   THR A  72      52.090  30.179  -0.870  1.00 59.22           O  
ANISOU  493  O   THR A  72     8000   8543   5957   1287   -787   1159       O  
ATOM    494  CB  THR A  72      51.310  28.085   1.131  1.00 52.85           C  
ANISOU  494  CB  THR A  72     6818   7919   5342   1072   -708    662       C  
ATOM    495  OG1 THR A  72      52.180  28.497   2.203  1.00 50.01           O  
ANISOU  495  OG1 THR A  72     6502   7363   5134    993   -551    656       O  
ATOM    496  CG2 THR A  72      50.540  26.811   1.494  1.00 44.53           C  
ANISOU  496  CG2 THR A  72     5578   7049   4293    979   -746    456       C  
ATOM    497  N   ARG A  73      54.094  29.369  -0.222  1.00 56.69           N  
ANISOU  497  N   ARG A  73     7765   8123   5651    986   -484   1087       N  
ATOM    498  CA  ARG A  73      54.818  30.605  -0.500  1.00 57.07           C  
ANISOU  498  CA  ARG A  73     7976   7969   5740   1011   -423   1312       C  
ATOM    499  C   ARG A  73      54.210  31.798   0.255  1.00 55.76           C  
ANISOU  499  C   ARG A  73     7784   7589   5813   1146   -485   1339       C  
ATOM    500  O   ARG A  73      53.961  32.860  -0.307  1.00 59.93           O  
ANISOU  500  O   ARG A  73     8418   7994   6360   1278   -564   1536       O  
ATOM    501  CB  ARG A  73      54.892  30.861  -2.008  1.00 53.89           C  
ANISOU  501  CB  ARG A  73     7726   7670   5081   1068   -479   1531       C  
ATOM    502  CG  ARG A  73      55.705  29.811  -2.780  1.00 67.56           C  
ANISOU  502  CG  ARG A  73     9503   9594   6571    932   -375   1490       C  
ATOM    503  CD  ARG A  73      56.129  30.300  -4.178  1.00 89.81           C  
ANISOU  503  CD  ARG A  73    12511  12491   9121    951   -359   1744       C  
ATOM    504  NE  ARG A  73      57.076  31.422  -4.142  1.00105.15           N  
ANISOU  504  NE  ARG A  73    14589  14203  11162    894   -222   1979       N  
ATOM    505  CZ  ARG A  73      57.067  32.450  -4.996  1.00111.30           C  
ANISOU  505  CZ  ARG A  73    15537  14918  11832    961   -260   2283       C  
ATOM    506  NH1 ARG A  73      56.158  32.511  -5.967  1.00112.07           N  
ANISOU  506  NH1 ARG A  73    15696  15190  11697   1108   -447   2394       N  
ATOM    507  NH2 ARG A  73      57.964  33.424  -4.876  1.00111.96           N  
ANISOU  507  NH2 ARG A  73    15732  14762  12046    875   -121   2485       N  
ATOM    508  N   THR A  74      53.945  31.597   1.544  1.00 53.50           N  
ANISOU  508  N   THR A  74     7357   7263   5708   1117   -449   1132       N  
ATOM    509  CA  THR A  74      53.474  32.663   2.418  1.00 56.34           C  
ANISOU  509  CA  THR A  74     7680   7422   6304   1231   -473   1092       C  
ATOM    510  C   THR A  74      54.280  32.985   3.672  1.00 59.35           C  
ANISOU  510  C   THR A  74     8063   7624   6865   1112   -334    980       C  
ATOM    511  O   THR A  74      54.963  34.009   3.722  1.00 70.66           O  
ANISOU  511  O   THR A  74     9620   8810   8418   1100   -287   1089       O  
ATOM    512  CB  THR A  74      52.059  32.357   2.918  1.00 53.69           C  
ANISOU  512  CB  THR A  74     7139   7233   6027   1358   -580    911       C  
ATOM    513  OG1 THR A  74      52.036  31.063   3.549  1.00 55.27           O  
ANISOU  513  OG1 THR A  74     7207   7621   6170   1205   -514    721       O  
ATOM    514  CG2 THR A  74      51.061  32.373   1.763  1.00 50.82           C  
ANISOU  514  CG2 THR A  74     6750   7018   5541   1527   -768   1015       C  
ATOM    515  N   ILE A  75      54.229  32.106   4.681  1.00 53.82           N  
ANISOU  515  N   ILE A  75     7229   7044   6175   1008   -276    771       N  
ATOM    516  CA  ILE A  75      54.969  32.315   5.925  1.00 47.31           C  
ANISOU  516  CA  ILE A  75     6399   6097   5479    890   -166    652       C  
ATOM    517  C   ILE A  75      56.250  31.516   5.714  1.00 49.76           C  
ANISOU  517  C   ILE A  75     6764   6452   5691    698    -73    703       C  
ATOM    518  O   ILE A  75      56.252  30.466   5.052  1.00 46.14           O  
ANISOU  518  O   ILE A  75     6284   6170   5078    655    -82    722       O  
ATOM    519  CB  ILE A  75      54.201  31.827   7.170  1.00 52.49           C  
ANISOU  519  CB  ILE A  75     6888   6880   6177    886   -155    420       C  
ATOM    520  CG1 ILE A  75      54.917  32.221   8.459  1.00 49.14           C  
ANISOU  520  CG1 ILE A  75     6476   6336   5859    784    -63    295       C  
ATOM    521  CG2 ILE A  75      53.965  30.293   7.142  1.00 48.31           C  
ANISOU  521  CG2 ILE A  75     6256   6601   5499    779   -152    360       C  
ATOM    522  CD1 ILE A  75      53.978  32.223   9.636  1.00 55.35           C  
ANISOU  522  CD1 ILE A  75     7121   7219   6691    834    -49     79       C  
ATOM    523  N   ARG A  76      57.361  32.025   6.250  1.00 52.10           N  
ANISOU  523  N   ARG A  76     7121   6583   6090    585     13    711       N  
ATOM    524  CA  ARG A  76      58.642  31.344   6.065  1.00 49.85           C  
ANISOU  524  CA  ARG A  76     6860   6337   5744    417    103    755       C  
ATOM    525  C   ARG A  76      58.747  30.087   6.934  1.00 45.97           C  
ANISOU  525  C   ARG A  76     6253   6004   5208    321    120    600       C  
ATOM    526  O   ARG A  76      58.471  30.127   8.139  1.00 49.38           O  
ANISOU  526  O   ARG A  76     6620   6436   5707    303    113    460       O  
ATOM    527  CB  ARG A  76      59.790  32.289   6.382  1.00 46.72           C  
ANISOU  527  CB  ARG A  76     6534   5725   5492    316    177    806       C  
ATOM    528  CG  ARG A  76      61.129  31.630   6.198  1.00 44.42           C  
ANISOU  528  CG  ARG A  76     6228   5487   5161    154    271    843       C  
ATOM    529  CD  ARG A  76      62.263  32.627   6.157  1.00 41.60           C  
ANISOU  529  CD  ARG A  76     5933   4928   4944     42    348    937       C  
ATOM    530  NE  ARG A  76      63.439  31.936   5.681  1.00 47.88           N  
ANISOU  530  NE  ARG A  76     6690   5820   5681    -85    447    992       N  
ATOM    531  CZ  ARG A  76      64.685  32.368   5.785  1.00 53.67           C  
ANISOU  531  CZ  ARG A  76     7406   6454   6532   -233    534   1034       C  
ATOM    532  NH1 ARG A  76      64.950  33.531   6.360  1.00 42.64           N  
ANISOU  532  NH1 ARG A  76     6046   4833   5323   -293    527   1027       N  
ATOM    533  NH2 ARG A  76      65.668  31.617   5.308  1.00 47.59           N  
ANISOU  533  NH2 ARG A  76     6568   5810   5705   -322    630   1064       N  
ATOM    534  N   VAL A  77      59.116  28.963   6.317  1.00 43.31           N  
ANISOU  534  N   VAL A  77     5900   5802   4753    264    141    625       N  
ATOM    535  CA  VAL A  77      59.433  27.736   7.049  1.00 44.86           C  
ANISOU  535  CA  VAL A  77     6011   6101   4932    164    155    519       C  
ATOM    536  C   VAL A  77      60.717  27.147   6.474  1.00 39.66           C  
ANISOU  536  C   VAL A  77     5371   5451   4248     77    229    576       C  
ATOM    537  O   VAL A  77      61.057  27.383   5.307  1.00 45.84           O  
ANISOU  537  O   VAL A  77     6221   6235   4961    100    271    681       O  
ATOM    538  CB  VAL A  77      58.271  26.710   6.995  1.00 47.71           C  
ANISOU  538  CB  VAL A  77     6295   6622   5208    202     89    441       C  
ATOM    539  CG1 VAL A  77      56.934  27.375   7.295  1.00 53.83           C  
ANISOU  539  CG1 VAL A  77     7025   7418   6011    313     26    391       C  
ATOM    540  CG2 VAL A  77      58.227  25.990   5.674  1.00 40.05           C  
ANISOU  540  CG2 VAL A  77     5354   5747   4116    224     74    485       C  
ATOM    541  N   PRO A  78      61.448  26.360   7.261  1.00 39.64           N  
ANISOU  541  N   PRO A  78     5303   5465   4292    -16    246    511       N  
ATOM    542  CA  PRO A  78      62.657  25.726   6.722  1.00 43.33           C  
ANISOU  542  CA  PRO A  78     5754   5948   4760    -74    316    541       C  
ATOM    543  C   PRO A  78      62.290  24.788   5.589  1.00 46.84           C  
ANISOU  543  C   PRO A  78     6214   6504   5079    -24    318    531       C  
ATOM    544  O   PRO A  78      61.353  23.999   5.702  1.00 51.36           O  
ANISOU  544  O   PRO A  78     6761   7148   5607      2    246    459       O  
ATOM    545  CB  PRO A  78      63.227  24.936   7.911  1.00 43.09           C  
ANISOU  545  CB  PRO A  78     5641   5922   4810   -150    287    468       C  
ATOM    546  CG  PRO A  78      62.434  25.345   9.122  1.00 41.97           C  
ANISOU  546  CG  PRO A  78     5490   5773   4685   -156    221    410       C  
ATOM    547  CD  PRO A  78      61.153  25.930   8.644  1.00 35.22           C  
ANISOU  547  CD  PRO A  78     4676   4933   3771    -62    199    412       C  
ATOM    548  N   ASN A  79      63.049  24.858   4.508  1.00 46.41           N  
ANISOU  548  N   ASN A  79     6195   6473   4966    -25    408    592       N  
ATOM    549  CA  ASN A  79      62.865  23.930   3.401  1.00 42.77           C  
ANISOU  549  CA  ASN A  79     5751   6133   4367     18    421    547       C  
ATOM    550  C   ASN A  79      63.335  22.537   3.814  1.00 49.38           C  
ANISOU  550  C   ASN A  79     6505   6982   5277    -14    417    424       C  
ATOM    551  O   ASN A  79      64.498  22.380   4.202  1.00 48.91           O  
ANISOU  551  O   ASN A  79     6381   6874   5328    -60    479    422       O  
ATOM    552  CB  ASN A  79      63.635  24.428   2.192  1.00 48.31           C  
ANISOU  552  CB  ASN A  79     6512   6879   4963     17    544    643       C  
ATOM    553  CG  ASN A  79      63.345  23.613   0.951  1.00 51.08           C  
ANISOU  553  CG  ASN A  79     6903   7386   5120     70    557    580       C  
ATOM    554  OD1 ASN A  79      62.316  22.946   0.866  1.00 51.19           O  
ANISOU  554  OD1 ASN A  79     6918   7460   5073    116    444    485       O  
ATOM    555  ND2 ASN A  79      64.243  23.674  -0.020  1.00 45.07           N  
ANISOU  555  ND2 ASN A  79     6167   6702   4254     54    698    619       N  
ATOM    556  N   PRO A  80      62.477  21.521   3.800  1.00 49.52           N  
ANISOU  556  N   PRO A  80     6510   7045   5262      6    333    325       N  
ATOM    557  CA  PRO A  80      62.906  20.182   4.228  1.00 47.59           C  
ANISOU  557  CA  PRO A  80     6201   6761   5119    -22    317    226       C  
ATOM    558  C   PRO A  80      63.607  19.446   3.101  1.00 47.18           C  
ANISOU  558  C   PRO A  80     6151   6757   5017     15    398    140       C  
ATOM    559  O   PRO A  80      63.254  19.586   1.934  1.00 52.94           O  
ANISOU  559  O   PRO A  80     6944   7595   5577     57    426    116       O  
ATOM    560  CB  PRO A  80      61.588  19.484   4.575  1.00 44.39           C  
ANISOU  560  CB  PRO A  80     5790   6373   4705    -35    203    162       C  
ATOM    561  CG  PRO A  80      60.611  20.085   3.553  1.00 47.32           C  
ANISOU  561  CG  PRO A  80     6215   6854   4908     23    174    167       C  
ATOM    562  CD  PRO A  80      61.044  21.561   3.451  1.00 45.75           C  
ANISOU  562  CD  PRO A  80     6063   6640   4679     51    237    302       C  
ATOM    563  N   HIS A  81      64.589  18.623   3.463  1.00 49.50           N  
ANISOU  563  N   HIS A  81     6372   6981   5453     10    428     83       N  
ATOM    564  CA  HIS A  81      65.401  17.917   2.474  1.00 46.87           C  
ANISOU  564  CA  HIS A  81     6016   6689   5103     61    528    -30       C  
ATOM    565  C   HIS A  81      65.226  16.407   2.497  1.00 51.03           C  
ANISOU  565  C   HIS A  81     6522   7138   5728     89    462   -187       C  
ATOM    566  O   HIS A  81      65.070  15.789   1.443  1.00 48.99           O  
ANISOU  566  O   HIS A  81     6298   6941   5375    134    494   -335       O  
ATOM    567  CB  HIS A  81      66.884  18.260   2.676  1.00 46.08           C  
ANISOU  567  CB  HIS A  81     5818   6570   5119     57    642     13       C  
ATOM    568  CG  HIS A  81      67.207  19.691   2.401  1.00 51.69           C  
ANISOU  568  CG  HIS A  81     6553   7341   5746     13    736    153       C  
ATOM    569  ND1 HIS A  81      66.806  20.329   1.246  1.00 57.78           N  
ANISOU  569  ND1 HIS A  81     7424   8229   6302     25    809    197       N  
ATOM    570  CD2 HIS A  81      67.889  20.610   3.123  1.00 51.72           C  
ANISOU  570  CD2 HIS A  81     6501   7292   5858    -52    760    264       C  
ATOM    571  CE1 HIS A  81      67.236  21.578   1.265  1.00 55.25           C  
ANISOU  571  CE1 HIS A  81     7115   7900   5976    -32    883    349       C  
ATOM    572  NE2 HIS A  81      67.893  21.776   2.393  1.00 51.06           N  
ANISOU  572  NE2 HIS A  81     6487   7263   5650    -85    856    376       N  
ATOM    573  N   LYS A  82      65.295  15.781   3.666  1.00 44.44           N  
ANISOU  573  N   LYS A  82     5640   6164   5080     61    369   -160       N  
ATOM    574  CA  LYS A  82      65.214  14.331   3.714  1.00 46.72           C  
ANISOU  574  CA  LYS A  82     5919   6330   5503     84    304   -285       C  
ATOM    575  C   LYS A  82      64.938  13.883   5.144  1.00 46.29           C  
ANISOU  575  C   LYS A  82     5847   6138   5602     21    178   -178       C  
ATOM    576  O   LYS A  82      65.440  14.482   6.100  1.00 48.37           O  
ANISOU  576  O   LYS A  82     6069   6395   5913     -5    163    -44       O  
ATOM    577  CB  LYS A  82      66.494  13.670   3.188  1.00 55.60           C  
ANISOU  577  CB  LYS A  82     6969   7413   6743    180    396   -406       C  
ATOM    578  CG  LYS A  82      66.337  12.162   3.124  1.00 64.12           C  
ANISOU  578  CG  LYS A  82     8056   8327   7981    219    322   -559       C  
ATOM    579  CD  LYS A  82      67.148  11.548   2.029  1.00 67.79           C  
ANISOU  579  CD  LYS A  82     8481   8807   8468    332    438   -774       C  
ATOM    580  CE  LYS A  82      66.887  10.057   1.925  1.00 72.84           C  
ANISOU  580  CE  LYS A  82     9146   9244   9285    372    353   -954       C  
ATOM    581  NZ  LYS A  82      67.738   9.465   0.859  1.00 78.86           N  
ANISOU  581  NZ  LYS A  82     9860  10027  10077    505    481  -1206       N  
ATOM    582  N   ALA A  83      64.099  12.863   5.277  1.00 45.57           N  
ANISOU  582  N   ALA A  83     5794   5948   5571    -20     87   -234       N  
ATOM    583  CA  ALA A  83      63.853  12.193   6.542  1.00 52.14           C  
ANISOU  583  CA  ALA A  83     6624   6639   6548    -90    -22   -123       C  
ATOM    584  C   ALA A  83      63.993  10.700   6.313  1.00 56.52           C  
ANISOU  584  C   ALA A  83     7190   6993   7291    -63    -74   -233       C  
ATOM    585  O   ALA A  83      63.830  10.218   5.192  1.00 57.32           O  
ANISOU  585  O   ALA A  83     7314   7091   7375    -20    -40   -426       O  
ATOM    586  CB  ALA A  83      62.477  12.530   7.100  1.00 46.88           C  
ANISOU  586  CB  ALA A  83     5991   6041   5780   -208    -76    -47       C  
ATOM    587  N   GLY A  84      64.346   9.976   7.362  1.00 58.68           N  
ANISOU  587  N   GLY A  84     7456   7096   7745    -81   -162   -113       N  
ATOM    588  CA  GLY A  84      64.503   8.543   7.222  1.00 53.66           C  
ANISOU  588  CA  GLY A  84     6841   6215   7333    -48   -225   -197       C  
ATOM    589  C   GLY A  84      65.015   7.907   8.488  1.00 58.84           C  
ANISOU  589  C   GLY A  84     7493   6689   8176    -53   -336      0       C  
ATOM    590  O   GLY A  84      64.959   8.498   9.571  1.00 60.55           O  
ANISOU  590  O   GLY A  84     7706   6990   8310   -123   -376    203       O  
ATOM    591  N   GLU A  85      65.490   6.673   8.338  1.00 66.35           N  
ANISOU  591  N   GLU A  85     8452   7382   9377     27   -395    -67       N  
ATOM    592  CA  GLU A  85      65.867   5.823   9.459  1.00 73.32           C  
ANISOU  592  CA  GLU A  85     9355   8035  10468     28   -532    135       C  
ATOM    593  C   GLU A  85      67.384   5.727   9.556  1.00 67.75           C  
ANISOU  593  C   GLU A  85     8544   7272   9927    223   -554    137       C  
ATOM    594  O   GLU A  85      68.076   5.636   8.538  1.00 69.31           O  
ANISOU  594  O   GLU A  85     8667   7471  10198    370   -465    -89       O  
ATOM    595  CB  GLU A  85      65.257   4.420   9.324  1.00 85.20           C  
ANISOU  595  CB  GLU A  85    10948   9233  12191    -26   -610     88       C  
ATOM    596  CG  GLU A  85      65.761   3.669   8.091  1.00101.13           C  
ANISOU  596  CG  GLU A  85    12944  11091  14390    129   -567   -219       C  
ATOM    597  CD  GLU A  85      65.092   2.322   7.853  1.00110.06           C  
ANISOU  597  CD  GLU A  85    14170  11897  15751     61   -645   -316       C  
ATOM    598  OE1 GLU A  85      64.476   1.776   8.796  1.00109.41           O  
ANISOU  598  OE1 GLU A  85    14166  11647  15759    -90   -749    -86       O  
ATOM    599  OE2 GLU A  85      65.217   1.798   6.722  1.00112.70           O  
ANISOU  599  OE2 GLU A  85    14502  12141  16178    154   -596   -627       O  
ATOM    600  N   LEU A  86      67.891   5.722  10.780  1.00 70.11           N  
ANISOU  600  N   LEU A  86     8826   7536  10278    225   -675    385       N  
ATOM    601  CA  LEU A  86      69.320   5.533  11.019  1.00 73.86           C  
ANISOU  601  CA  LEU A  86     9177   7946  10943    413   -739    411       C  
ATOM    602  C   LEU A  86      69.638   4.044  11.029  1.00 80.29           C  
ANISOU  602  C   LEU A  86    10018   8395  12092    531   -855    406       C  
ATOM    603  O   LEU A  86      68.945   3.278  11.712  1.00 79.97           O  
ANISOU  603  O   LEU A  86    10107   8155  12121    424   -971    585       O  
ATOM    604  CB  LEU A  86      69.701   6.152  12.362  1.00 72.96           C  
ANISOU  604  CB  LEU A  86     9035   7962  10726    363   -853    679       C  
ATOM    605  CG  LEU A  86      69.699   7.674  12.403  1.00 67.20           C  
ANISOU  605  CG  LEU A  86     8251   7558   9726    285   -751    661       C  
ATOM    606  CD1 LEU A  86      69.796   8.175  13.825  1.00 61.32           C  
ANISOU  606  CD1 LEU A  86     7519   6928   8852    198   -879    906       C  
ATOM    607  CD2 LEU A  86      70.863   8.180  11.566  1.00 62.98           C  
ANISOU  607  CD2 LEU A  86     7545   7120   9264    432   -647    481       C  
ATOM    608  N   PRO A  87      70.687   3.596  10.319  1.00 90.24           N  
ANISOU  608  N   PRO A  87    11156   9550  13581    751   -825    211       N  
ATOM    609  CA  PRO A  87      70.975   2.150  10.314  1.00101.09           C  
ANISOU  609  CA  PRO A  87    12561  10533  15315    887   -944    186       C  
ATOM    610  C   PRO A  87      71.265   1.615  11.703  1.00115.88           C  
ANISOU  610  C   PRO A  87    14473  12226  17330    897  -1174    538       C  
ATOM    611  O   PRO A  87      70.878   0.483  12.019  1.00120.34           O  
ANISOU  611  O   PRO A  87    15164  12449  18110    882  -1297    644       O  
ATOM    612  CB  PRO A  87      72.180   2.033   9.368  1.00 93.32           C  
ANISOU  612  CB  PRO A  87    11391   9553  14513   1141   -845    -98       C  
ATOM    613  CG  PRO A  87      72.108   3.246   8.504  1.00 85.59           C  
ANISOU  613  CG  PRO A  87    10347   8942  13232   1079   -628   -276       C  
ATOM    614  CD  PRO A  87      71.590   4.329   9.414  1.00 83.88           C  
ANISOU  614  CD  PRO A  87    10180   8961  12728    881   -664    -13       C  
ATOM    615  N   THR A  88      71.912   2.413  12.555  1.00123.22           N  
ANISOU  615  N   THR A  88    15309  13378  18134    907  -1243    730       N  
ATOM    616  CA  THR A  88      72.134   2.009  13.940  1.00131.13           C  
ANISOU  616  CA  THR A  88    16362  14270  19193    897  -1476   1089       C  
ATOM    617  C   THR A  88      70.832   1.824  14.711  1.00125.81           C  
ANISOU  617  C   THR A  88    15905  13557  18339    639  -1521   1333       C  
ATOM    618  O   THR A  88      70.823   1.125  15.729  1.00128.95           O  
ANISOU  618  O   THR A  88    16400  13774  18821    616  -1709   1640       O  
ATOM    619  CB  THR A  88      73.004   3.048  14.652  1.00137.41           C  
ANISOU  619  CB  THR A  88    17008  15370  19831    928  -1535   1203       C  
ATOM    620  OG1 THR A  88      72.183   4.129  15.119  1.00135.58           O  
ANISOU  620  OG1 THR A  88    16858  15433  19223    692  -1463   1290       O  
ATOM    621  CG2 THR A  88      74.057   3.600  13.696  1.00137.83           C  
ANISOU  621  CG2 THR A  88    16826  15572  19972   1101  -1400    915       C  
ATOM    622  N   GLY A  89      69.742   2.438  14.259  1.00116.38           N  
ANISOU  622  N   GLY A  89    14780  12541  16899    446  -1354   1217       N  
ATOM    623  CA  GLY A  89      68.473   2.413  14.984  1.00108.62           C  
ANISOU  623  CA  GLY A  89    13961  11589  15722    187  -1363   1425       C  
ATOM    624  C   GLY A  89      68.096   3.851  15.283  1.00103.35           C  
ANISOU  624  C   GLY A  89    13259  11328  14682     58  -1258   1427       C  
ATOM    625  O   GLY A  89      68.915   4.661  15.718  1.00105.48           O  
ANISOU  625  O   GLY A  89    13428  11802  14846    129  -1293   1468       O  
ATOM    626  N   GLY A  90      66.834   4.174  15.026  1.00 94.61           N  
ANISOU  626  N   GLY A  90    12224  10330  13395   -132  -1135   1366       N  
ATOM    627  CA  GLY A  90      66.324   5.526  15.162  1.00 82.03           C  
ANISOU  627  CA  GLY A  90    10601   9088  11478   -241  -1021   1326       C  
ATOM    628  C   GLY A  90      66.130   6.209  13.819  1.00 74.88           C  
ANISOU  628  C   GLY A  90     9628   8307  10517   -196   -856   1018       C  
ATOM    629  O   GLY A  90      66.187   5.594  12.751  1.00 69.19           O  
ANISOU  629  O   GLY A  90     8897   7426   9965   -114   -814    818       O  
ATOM    630  N   SER A  91      65.955   7.528  13.878  1.00 66.81           N  
ANISOU  630  N   SER A  91     8563   7574   9247   -242   -767    979       N  
ATOM    631  CA  SER A  91      65.547   8.273  12.698  1.00 61.60           C  
ANISOU  631  CA  SER A  91     7868   7052   8484   -231   -618    744       C  
ATOM    632  C   SER A  91      66.200   9.649  12.687  1.00 58.84           C  
ANISOU  632  C   SER A  91     7436   6934   7988   -181   -554    706       C  
ATOM    633  O   SER A  91      66.721  10.131  13.701  1.00 55.95           O  
ANISOU  633  O   SER A  91     7043   6655   7561   -194   -623    846       O  
ATOM    634  CB  SER A  91      64.027   8.427  12.653  1.00 59.75           C  
ANISOU  634  CB  SER A  91     7699   6903   8100   -400   -560    732       C  
ATOM    635  OG  SER A  91      63.559   9.007  13.866  1.00 69.82           O  
ANISOU  635  OG  SER A  91     8999   8334   9195   -523   -580    915       O  
ATOM    636  N   TYR A  92      66.118  10.298  11.526  1.00 55.40           N  
ANISOU  636  N   TYR A  92     6966   6599   7483   -138   -425    517       N  
ATOM    637  CA  TYR A  92      66.703  11.615  11.332  1.00 52.84           C  
ANISOU  637  CA  TYR A  92     6572   6462   7044   -105   -346    477       C  
ATOM    638  C   TYR A  92      65.851  12.447  10.391  1.00 48.85           C  
ANISOU  638  C   TYR A  92     6100   6092   6369   -140   -224    358       C  
ATOM    639  O   TYR A  92      65.067  11.921   9.598  1.00 47.36           O  
ANISOU  639  O   TYR A  92     5958   5865   6171   -151   -196    254       O  
ATOM    640  CB  TYR A  92      68.097  11.525  10.731  1.00 48.04           C  
ANISOU  640  CB  TYR A  92     5850   5819   6586     40   -311    387       C  
ATOM    641  CG  TYR A  92      68.090  11.005   9.309  1.00 55.67           C  
ANISOU  641  CG  TYR A  92     6812   6731   7609    125   -207    184       C  
ATOM    642  CD1 TYR A  92      68.158   9.633   9.047  1.00 56.63           C  
ANISOU  642  CD1 TYR A  92     6951   6640   7927    197   -261    113       C  
ATOM    643  CD2 TYR A  92      68.017  11.879   8.224  1.00 52.92           C  
ANISOU  643  CD2 TYR A  92     6455   6541   7112    134    -58     61       C  
ATOM    644  CE1 TYR A  92      68.160   9.146   7.745  1.00 58.26           C  
ANISOU  644  CE1 TYR A  92     7158   6809   8170    277   -165   -114       C  
ATOM    645  CE2 TYR A  92      68.005  11.397   6.916  1.00 54.82           C  
ANISOU  645  CE2 TYR A  92     6703   6769   7356    208     38   -134       C  
ATOM    646  CZ  TYR A  92      68.083  10.032   6.682  1.00 61.06           C  
ANISOU  646  CZ  TYR A  92     7503   7364   8332    280    -13   -241       C  
ATOM    647  OH  TYR A  92      68.071   9.564   5.379  1.00 66.35           O  
ANISOU  647  OH  TYR A  92     8183   8037   8988    354     83   -475       O  
ATOM    648  N   ILE A  93      66.094  13.752  10.418  1.00 43.95           N  
ANISOU  648  N   ILE A  93     5449   5622   5628   -149   -162    367       N  
ATOM    649  CA  ILE A  93      65.595  14.654   9.391  1.00 44.10           C  
ANISOU  649  CA  ILE A  93     5490   5757   5508   -144    -50    274       C  
ATOM    650  C   ILE A  93      66.662  15.696   9.082  1.00 49.21           C  
ANISOU  650  C   ILE A  93     6070   6479   6148   -104     33    268       C  
ATOM    651  O   ILE A  93      67.382  16.151   9.984  1.00 47.11           O  
ANISOU  651  O   ILE A  93     5748   6224   5927   -128    -12    345       O  
ATOM    652  CB  ILE A  93      64.278  15.324   9.824  1.00 43.08           C  
ANISOU  652  CB  ILE A  93     5421   5721   5226   -234    -60    316       C  
ATOM    653  CG1 ILE A  93      63.735  16.179   8.681  1.00 40.63           C  
ANISOU  653  CG1 ILE A  93     5138   5513   4788   -203     27    237       C  
ATOM    654  CG2 ILE A  93      64.463  16.103  11.125  1.00 36.71           C  
ANISOU  654  CG2 ILE A  93     4601   4970   4376   -292   -102    422       C  
ATOM    655  CD1 ILE A  93      62.348  16.668   8.930  1.00 45.82           C  
ANISOU  655  CD1 ILE A  93     5827   6251   5329   -257      8    249       C  
ATOM    656  N   ILE A  94      66.764  16.062   7.798  1.00 47.64           N  
ANISOU  656  N   ILE A  94     5875   6340   5884    -57    151    177       N  
ATOM    657  CA  ILE A  94      67.652  17.111   7.307  1.00 40.43           C  
ANISOU  657  CA  ILE A  94     4909   5505   4948    -46    262    185       C  
ATOM    658  C   ILE A  94      66.803  18.225   6.699  1.00 45.88           C  
ANISOU  658  C   ILE A  94     5688   6284   5460    -77    323    207       C  
ATOM    659  O   ILE A  94      65.942  17.956   5.853  1.00 46.73           O  
ANISOU  659  O   ILE A  94     5867   6431   5456    -51    337    149       O  
ATOM    660  CB  ILE A  94      68.643  16.570   6.258  1.00 46.23           C  
ANISOU  660  CB  ILE A  94     5566   6248   5749     40    372     79       C  
ATOM    661  CG1 ILE A  94      69.345  15.297   6.763  1.00 43.93           C  
ANISOU  661  CG1 ILE A  94     5189   5837   5668    109    292     39       C  
ATOM    662  CG2 ILE A  94      69.668  17.653   5.878  1.00 38.65           C  
ANISOU  662  CG2 ILE A  94     4524   5375   4786     19    503    113       C  
ATOM    663  CD1 ILE A  94      70.284  14.705   5.725  1.00 48.03           C  
ANISOU  663  CD1 ILE A  94     5614   6365   6271    218    412   -107       C  
ATOM    664  N   MET A  95      67.079  19.474   7.087  1.00 41.36           N  
ANISOU  664  N   MET A  95     5109   5734   4872   -127    349    286       N  
ATOM    665  CA  MET A  95      66.351  20.615   6.544  1.00 47.54           C  
ANISOU  665  CA  MET A  95     5979   6564   5520   -139    396    329       C  
ATOM    666  C   MET A  95      67.272  21.829   6.437  1.00 46.00           C  
ANISOU  666  C   MET A  95     5754   6361   5362   -185    485    397       C  
ATOM    667  O   MET A  95      68.420  21.821   6.883  1.00 48.12           O  
ANISOU  667  O   MET A  95     5916   6607   5760   -221    501    398       O  
ATOM    668  CB  MET A  95      65.111  20.941   7.394  1.00 44.85           C  
ANISOU  668  CB  MET A  95     5695   6215   5130   -164    296    350       C  
ATOM    669  CG  MET A  95      65.427  21.586   8.712  1.00 45.86           C  
ANISOU  669  CG  MET A  95     5792   6306   5327   -227    245    387       C  
ATOM    670  SD  MET A  95      63.996  21.816   9.803  1.00 45.02           S  
ANISOU  670  SD  MET A  95     5730   6227   5149   -252    157    377       S  
ATOM    671  CE  MET A  95      63.657  20.119  10.241  1.00 44.44           C  
ANISOU  671  CE  MET A  95     5633   6159   5094   -270     83    366       C  
ATOM    672  N   GLU A  96      66.733  22.877   5.825  1.00 47.18           N  
ANISOU  672  N   GLU A  96     5994   6522   5409   -187    532    461       N  
ATOM    673  CA  GLU A  96      67.399  24.164   5.726  1.00 43.30           C  
ANISOU  673  CA  GLU A  96     5505   5985   4964   -251    610    548       C  
ATOM    674  C   GLU A  96      67.796  24.720   7.093  1.00 45.22           C  
ANISOU  674  C   GLU A  96     5691   6143   5346   -327    536    541       C  
ATOM    675  O   GLU A  96      67.031  24.661   8.062  1.00 45.72           O  
ANISOU  675  O   GLU A  96     5781   6189   5402   -320    425    503       O  
ATOM    676  CB  GLU A  96      66.476  25.161   5.022  1.00 44.68           C  
ANISOU  676  CB  GLU A  96     5813   6147   5017   -220    625    636       C  
ATOM    677  CG  GLU A  96      67.065  26.583   4.904  1.00 45.54           C  
ANISOU  677  CG  GLU A  96     5953   6157   5194   -297    702    752       C  
ATOM    678  CD  GLU A  96      66.058  27.602   4.344  1.00 56.58           C  
ANISOU  678  CD  GLU A  96     7495   7500   6502   -242    681    860       C  
ATOM    679  OE1 GLU A  96      64.892  27.220   4.082  1.00 52.24           O  
ANISOU  679  OE1 GLU A  96     7001   7017   5833   -141    599    832       O  
ATOM    680  OE2 GLU A  96      66.428  28.791   4.192  1.00 56.23           O  
ANISOU  680  OE2 GLU A  96     7503   7336   6526   -301    735    974       O  
ATOM    681  N   PHE A  97      69.002  25.281   7.161  1.00 40.05           N  
ANISOU  681  N   PHE A  97     4951   5456   4810   -411    602    568       N  
ATOM    682  CA  PHE A  97      69.458  25.985   8.348  1.00 41.78           C  
ANISOU  682  CA  PHE A  97     5119   5601   5155   -501    528    546       C  
ATOM    683  C   PHE A  97      69.114  27.461   8.247  1.00 46.99           C  
ANISOU  683  C   PHE A  97     5878   6144   5831   -552    559    603       C  
ATOM    684  O   PHE A  97      69.447  28.113   7.254  1.00 51.24           O  
ANISOU  684  O   PHE A  97     6451   6646   6371   -586    681    701       O  
ATOM    685  CB  PHE A  97      70.968  25.830   8.550  1.00 41.34           C  
ANISOU  685  CB  PHE A  97     4888   5566   5253   -577    560    528       C  
ATOM    686  CG  PHE A  97      71.441  26.414   9.845  1.00 41.62           C  
ANISOU  686  CG  PHE A  97     4858   5551   5403   -674    447    478       C  
ATOM    687  CD1 PHE A  97      71.777  27.750   9.939  1.00 46.35           C  
ANISOU  687  CD1 PHE A  97     5470   6046   6094   -790    482    494       C  
ATOM    688  CD2 PHE A  97      71.452  25.643  10.994  1.00 46.13           C  
ANISOU  688  CD2 PHE A  97     5378   6173   5978   -651    293    416       C  
ATOM    689  CE1 PHE A  97      72.177  28.298  11.151  1.00 52.82           C  
ANISOU  689  CE1 PHE A  97     6235   6824   7009   -885    363    410       C  
ATOM    690  CE2 PHE A  97      71.841  26.185  12.214  1.00 46.63           C  
ANISOU  690  CE2 PHE A  97     5393   6222   6102   -740    171    356       C  
ATOM    691  CZ  PHE A  97      72.212  27.518  12.280  1.00 48.19           C  
ANISOU  691  CZ  PHE A  97     5591   6327   6393   -857    206    334       C  
ATOM    692  N   ILE A  98      68.466  27.990   9.281  1.00 46.90           N  
ANISOU  692  N   ILE A  98     5917   6070   5835   -557    454    542       N  
ATOM    693  CA  ILE A  98      68.069  29.393   9.334  1.00 52.42           C  
ANISOU  693  CA  ILE A  98     6714   6618   6585   -585    461    564       C  
ATOM    694  C   ILE A  98      68.667  30.035  10.579  1.00 53.27           C  
ANISOU  694  C   ILE A  98     6764   6651   6824   -694    386    457       C  
ATOM    695  O   ILE A  98      68.627  29.457  11.673  1.00 56.67           O  
ANISOU  695  O   ILE A  98     7142   7168   7223   -696    281    353       O  
ATOM    696  CB  ILE A  98      66.535  29.555   9.353  1.00 53.20           C  
ANISOU  696  CB  ILE A  98     6927   6708   6576   -461    408    547       C  
ATOM    697  CG1 ILE A  98      65.893  28.883   8.139  1.00 49.24           C  
ANISOU  697  CG1 ILE A  98     6474   6303   5931   -358    451    631       C  
ATOM    698  CG2 ILE A  98      66.154  31.038   9.446  1.00 44.74           C  
ANISOU  698  CG2 ILE A  98     5953   5448   5599   -462    406    557       C  
ATOM    699  CD1 ILE A  98      64.399  29.144   8.063  1.00 47.64           C  
ANISOU  699  CD1 ILE A  98     6355   6100   5647   -236    389    620       C  
ATOM    700  N   ASP A  99      69.199  31.243  10.420  1.00 49.70           N  
ANISOU  700  N   ASP A  99     6334   6036   6514   -794    434    487       N  
ATOM    701  CA  ASP A  99      69.782  31.977  11.537  1.00 63.03           C  
ANISOU  701  CA  ASP A  99     7972   7635   8340   -916    356    359       C  
ATOM    702  C   ASP A  99      68.701  32.788  12.249  1.00 57.63           C  
ANISOU  702  C   ASP A  99     7411   6840   7647   -855    286    246       C  
ATOM    703  O   ASP A  99      68.187  33.765  11.705  1.00 61.30           O  
ANISOU  703  O   ASP A  99     7991   7124   8177   -821    331    304       O  
ATOM    704  CB  ASP A  99      70.901  32.899  11.050  1.00 77.17           C  
ANISOU  704  CB  ASP A  99     9715   9282  10324  -1079    444    427       C  
ATOM    705  CG  ASP A  99      71.556  33.667  12.181  1.00102.96           C  
ANISOU  705  CG  ASP A  99    12918  12452  13752  -1226    348    269       C  
ATOM    706  OD1 ASP A  99      72.189  33.028  13.047  1.00112.17           O  
ANISOU  706  OD1 ASP A  99    13946  13764  14910  -1271    247    160       O  
ATOM    707  OD2 ASP A  99      71.439  34.911  12.203  1.00114.69           O  
ANISOU  707  OD2 ASP A  99    14495  13707  15375  -1295    360    249       O  
ATOM    708  N   PHE A 100      68.346  32.324  13.444  1.00 50.81           N  
ANISOU  708  N   PHE A 100     6518   6096   6691   -831    178     94       N  
ATOM    709  CA  PHE A 100      67.353  32.955  14.302  1.00 54.81           C  
ANISOU  709  CA  PHE A 100     7108   6553   7163   -771    121    -61       C  
ATOM    710  C   PHE A 100      67.998  34.070  15.116  1.00 60.37           C  
ANISOU  710  C   PHE A 100     7809   7108   8022   -900     68   -221       C  
ATOM    711  O   PHE A 100      69.222  34.133  15.226  1.00 79.46           O  
ANISOU  711  O   PHE A 100    10130   9514  10547  -1049     46   -220       O  
ATOM    712  CB  PHE A 100      66.714  31.923  15.233  1.00 50.92           C  
ANISOU  712  CB  PHE A 100     6586   6288   6474   -712     50   -145       C  
ATOM    713  CG  PHE A 100      65.948  30.850  14.514  1.00 48.16           C  
ANISOU  713  CG  PHE A 100     6243   6062   5995   -598     90    -20       C  
ATOM    714  CD1 PHE A 100      65.236  31.141  13.362  1.00 44.43           C  
ANISOU  714  CD1 PHE A 100     5840   5506   5535   -497    162     84       C  
ATOM    715  CD2 PHE A 100      65.939  29.549  14.990  1.00 53.00           C  
ANISOU  715  CD2 PHE A 100     6797   6865   6478   -597     41     -3       C  
ATOM    716  CE1 PHE A 100      64.531  30.156  12.698  1.00 46.51           C  
ANISOU  716  CE1 PHE A 100     6102   5890   5678   -405    183    171       C  
ATOM    717  CE2 PHE A 100      65.236  28.559  14.331  1.00 50.50           C  
ANISOU  717  CE2 PHE A 100     6485   6633   6067   -512     73     91       C  
ATOM    718  CZ  PHE A 100      64.530  28.863  13.183  1.00 50.91           C  
ANISOU  718  CZ  PHE A 100     6597   6620   6129   -420    142    162       C  
ATOM    719  N   GLY A 101      67.179  34.946  15.689  1.00 67.29           N  
ANISOU  719  N   GLY A 101     8775   7871   8921   -843     43   -379       N  
ATOM    720  CA  GLY A 101      67.704  36.033  16.494  1.00 85.92           C  
ANISOU  720  CA  GLY A 101    11145  10069  11431   -962    -14   -576       C  
ATOM    721  C   GLY A 101      67.237  37.417  16.095  1.00 98.28           C  
ANISOU  721  C   GLY A 101    12834  11309  13199   -921     28   -608       C  
ATOM    722  O   GLY A 101      68.016  38.369  16.113  1.00101.43           O  
ANISOU  722  O   GLY A 101    13244  11477  13816  -1064     19   -656       O  
ATOM    723  N   GLY A 102      65.963  37.535  15.738  1.00103.44           N  
ANISOU  723  N   GLY A 102    13573  11929  13801   -727     65   -581       N  
ATOM    724  CA  GLY A 102      65.419  38.822  15.350  1.00110.37           C  
ANISOU  724  CA  GLY A 102    14572  12480  14883   -645     87   -597       C  
ATOM    725  C   GLY A 102      65.477  39.778  16.525  1.00118.63           C  
ANISOU  725  C   GLY A 102    15645  13379  16052   -696     24   -917       C  
ATOM    726  O   GLY A 102      65.194  39.399  17.662  1.00123.83           O  
ANISOU  726  O   GLY A 102    16254  14251  16544   -682    -25  -1151       O  
ATOM    727  N   SER A 103      65.933  41.002  16.273  1.00122.40           N  
ANISOU  727  N   SER A 103    16201  13492  16813   -778     24   -931       N  
ATOM    728  CA  SER A 103      66.111  41.987  17.342  1.00128.84           C  
ANISOU  728  CA  SER A 103    17048  14123  17783   -851    -43  -1266       C  
ATOM    729  C   SER A 103      64.869  42.462  18.097  1.00134.75           C  
ANISOU  729  C   SER A 103    17854  14840  18506   -644    -58  -1550       C  
ATOM    730  O   SER A 103      64.886  42.544  19.325  1.00138.43           O  
ANISOU  730  O   SER A 103    18289  15425  18883   -684   -112  -1879       O  
ATOM    731  CB  SER A 103      66.875  43.204  16.808  1.00127.42           C  
ANISOU  731  CB  SER A 103    16947  13511  17956  -1002    -34  -1197       C  
ATOM    732  OG  SER A 103      67.291  44.050  17.866  1.00124.48           O  
ANISOU  732  OG  SER A 103    16584  12971  17740  -1128   -114  -1543       O  
ATOM    733  N   ARG A 104      63.799  42.776  17.377  1.00134.08           N  
ANISOU  733  N   ARG A 104    17841  14616  18488   -418    -14  -1433       N  
ATOM    734  CA  ARG A 104      62.581  43.244  18.031  1.00134.45           C  
ANISOU  734  CA  ARG A 104    17910  14635  18539   -195    -15  -1708       C  
ATOM    735  C   ARG A 104      61.510  42.168  18.129  1.00126.68           C  
ANISOU  735  C   ARG A 104    16835  14038  17260    -23     25  -1682       C  
ATOM    736  O   ARG A 104      60.806  42.059  19.133  1.00133.67           O  
ANISOU  736  O   ARG A 104    17669  15114  18007     66     38  -1968       O  
ATOM    737  CB  ARG A 104      62.024  44.470  17.303  1.00140.56           C  
ANISOU  737  CB  ARG A 104    18810  14958  19639    -32    -15  -1644       C  
ATOM    738  CG  ARG A 104      62.829  45.740  17.522  1.00145.70           C  
ANISOU  738  CG  ARG A 104    19563  15169  20628   -183    -56  -1781       C  
ATOM    739  CD  ARG A 104      63.064  46.477  16.213  1.00148.51           C  
ANISOU  739  CD  ARG A 104    20046  15119  21263   -188    -45  -1424       C  
ATOM    740  NE  ARG A 104      64.365  47.139  16.184  1.00153.19           N  
ANISOU  740  NE  ARG A 104    20685  15427  22092   -481    -58  -1401       N  
ATOM    741  CZ  ARG A 104      65.444  46.639  15.591  1.00152.48           C  
ANISOU  741  CZ  ARG A 104    20546  15442  21947   -717    -20  -1133       C  
ATOM    742  NH1 ARG A 104      65.382  45.467  14.974  1.00147.68           N  
ANISOU  742  NH1 ARG A 104    19859  15199  21054   -681     30   -878       N  
ATOM    743  NH2 ARG A 104      66.587  47.311  15.614  1.00155.24           N  
ANISOU  743  NH2 ARG A 104    20913  15528  22542   -993    -27  -1137       N  
ATOM    744  N   GLY A 105      61.393  41.381  17.067  1.00111.28           N  
ANISOU  744  N   GLY A 105    14862  12207  15213     12     51  -1345       N  
ATOM    745  CA  GLY A 105      60.402  40.328  16.990  1.00100.67           C  
ANISOU  745  CA  GLY A 105    13427  11199  13623    152     83  -1287       C  
ATOM    746  C   GLY A 105      59.175  40.960  16.369  1.00 98.57           C  
ANISOU  746  C   GLY A 105    13190  10767  13496    416     88  -1255       C  
ATOM    747  O   GLY A 105      58.983  42.171  16.478  1.00104.06           O  
ANISOU  747  O   GLY A 105    13963  11132  14443    509     67  -1390       O  
ATOM    748  N   ASN A 106      58.326  40.255  15.626  1.00 92.94           N  
ANISOU  748  N   ASN A 106    12419  10233  12662    556     97  -1071       N  
ATOM    749  CA  ASN A 106      57.203  40.935  14.927  1.00 85.98           C  
ANISOU  749  CA  ASN A 106    11554   9176  11937    822     69  -1013       C  
ATOM    750  C   ASN A 106      55.786  40.285  14.883  1.00 82.28           C  
ANISOU  750  C   ASN A 106    10941   8991  11331   1027     79  -1052       C  
ATOM    751  O   ASN A 106      55.454  39.572  13.969  1.00 70.63           O  
ANISOU  751  O   ASN A 106     9431   7662   9745   1065     56   -817       O  
ATOM    752  CB  ASN A 106      57.687  41.186  13.497  1.00 83.96           C  
ANISOU  752  CB  ASN A 106    11416   8705  11781    804     33   -642       C  
ATOM    753  CG  ASN A 106      56.993  42.332  12.814  1.00 88.88           C  
ANISOU  753  CG  ASN A 106    12128   8987  12656   1032    -28   -554       C  
ATOM    754  OD1 ASN A 106      56.000  42.863  13.295  1.00 92.10           O  
ANISOU  754  OD1 ASN A 106    12483   9333  13178   1248    -49   -768       O  
ATOM    755  ND2 ASN A 106      57.516  42.715  11.676  1.00 86.96           N  
ANISOU  755  ND2 ASN A 106    12016   8524  12500    991    -54   -229       N  
ATOM    756  N   GLN A 107      54.956  40.571  15.875  1.00 73.32           N  
ANISOU  756  N   GLN A 107     8047   8305  11508     54    185    460       N  
ATOM    757  CA  GLN A 107      53.612  39.997  16.017  1.00 73.87           C  
ANISOU  757  CA  GLN A 107     8165   8440  11464    170    114    479       C  
ATOM    758  C   GLN A 107      52.577  40.162  14.935  1.00 69.94           C  
ANISOU  758  C   GLN A 107     7743   7904  10926    233    101    673       C  
ATOM    759  O   GLN A 107      51.941  39.231  14.548  1.00 67.59           O  
ANISOU  759  O   GLN A 107     7476   7731  10473    287     50    726       O  
ATOM    760  CB  GLN A 107      53.008  40.467  17.303  1.00 79.54           C  
ANISOU  760  CB  GLN A 107     8861   9089  12270    211     77    323       C  
ATOM    761  CG  GLN A 107      53.640  39.821  18.492  1.00 87.25           C  
ANISOU  761  CG  GLN A 107     9789  10179  13184    184     37    133       C  
ATOM    762  CD  GLN A 107      52.804  38.712  19.019  1.00 90.05           C  
ANISOU  762  CD  GLN A 107    10162  10680  13374    266    -18     97       C  
ATOM    763  OE1 GLN A 107      51.968  38.199  18.330  1.00 95.44           O  
ANISOU  763  OE1 GLN A 107    10876  11409  13978    326    -29    216       O  
ATOM    764  NE2 GLN A 107      53.014  38.354  20.251  1.00 91.53           N  
ANISOU  764  NE2 GLN A 107    10333  10936  13508    262    -57    -64       N  
ATOM    765  N   ALA A 108      52.383  41.361  14.472  1.00 67.69           N  
ANISOU  765  N   ALA A 108     7488   7440  10789    224    134    780       N  
ATOM    766  CA  ALA A 108      51.429  41.595  13.401  1.00 62.38           C  
ANISOU  766  CA  ALA A 108     6890   6729  10083    287     97    988       C  
ATOM    767  C   ALA A 108      51.844  40.852  12.143  1.00 63.52           C  
ANISOU  767  C   ALA A 108     7107   7003  10026    246    115   1131       C  
ATOM    768  O   ALA A 108      50.999  40.308  11.423  1.00 69.81           O  
ANISOU  768  O   ALA A 108     7962   7884  10680    304     39   1243       O  
ATOM    769  CB  ALA A 108      51.310  43.093  13.124  1.00 60.37           C  
ANISOU  769  CB  ALA A 108     6663   6229  10044    280    134   1094       C  
ATOM    770  N   GLU A 109      53.141  40.825  11.852  1.00 56.13           N  
ANISOU  770  N   GLU A 109     6163   6086   9078    144    219   1120       N  
ATOM    771  CA  GLU A 109      53.600  40.065  10.698  1.00 57.59           C  
ANISOU  771  CA  GLU A 109     6419   6402   9059    108    268   1227       C  
ATOM    772  C   GLU A 109      53.336  38.570  10.866  1.00 57.81           C  
ANISOU  772  C   GLU A 109     6443   6626   8895    159    203   1131       C  
ATOM    773  O   GLU A 109      53.069  37.868   9.883  1.00 63.55           O  
ANISOU  773  O   GLU A 109     7264   7457   9427    172    188   1223       O  
ATOM    774  CB  GLU A 109      55.075  40.334  10.457  1.00 59.06           C  
ANISOU  774  CB  GLU A 109     6566   6571   9305     -9    417   1217       C  
ATOM    775  CG  GLU A 109      55.574  39.765   9.170  1.00 70.33           C  
ANISOU  775  CG  GLU A 109     8080   8108  10535    -49    511   1339       C  
ATOM    776  CD  GLU A 109      55.021  40.475   7.953  1.00 82.74           C  
ANISOU  776  CD  GLU A 109     9802   9603  12032    -56    522   1584       C  
ATOM    777  OE1 GLU A 109      54.173  41.381   8.089  1.00 85.93           O  
ANISOU  777  OE1 GLU A 109    10233   9861  12557    -12    439   1671       O  
ATOM    778  OE2 GLU A 109      55.448  40.124   6.837  1.00 89.38           O  
ANISOU  778  OE2 GLU A 109    10742  10530  12689   -100    616   1693       O  
ATOM    779  N   LEU A 110      53.424  38.060  12.095  1.00 48.55           N  
ANISOU  779  N   LEU A 110     5177   5502   7769    183    164    945       N  
ATOM    780  CA  LEU A 110      53.093  36.663  12.319  1.00 47.61           C  
ANISOU  780  CA  LEU A 110     5060   5539   7488    233    100    867       C  
ATOM    781  C   LEU A 110      51.616  36.395  12.020  1.00 47.16           C  
ANISOU  781  C   LEU A 110     5060   5506   7353    307    -12    946       C  
ATOM    782  O   LEU A 110      51.275  35.375  11.410  1.00 48.10           O  
ANISOU  782  O   LEU A 110     5239   5737   7299    322    -55    974       O  
ATOM    783  CB  LEU A 110      53.465  36.261  13.749  1.00 46.63           C  
ANISOU  783  CB  LEU A 110     4838   5451   7428    242     74    677       C  
ATOM    784  CG  LEU A 110      52.948  34.887  14.174  1.00 50.71           C  
ANISOU  784  CG  LEU A 110     5363   6100   7805    298     -1    607       C  
ATOM    785  CD1 LEU A 110      53.561  33.784  13.305  1.00 45.27           C  
ANISOU  785  CD1 LEU A 110     4718   5517   6965    286     37    631       C  
ATOM    786  CD2 LEU A 110      53.203  34.640  15.671  1.00 44.90           C  
ANISOU  786  CD2 LEU A 110     4551   5388   7121    309    -36    444       C  
ATOM    787  N   GLY A 111      50.725  37.291  12.453  1.00 52.40           N  
ANISOU  787  N   GLY A 111     5696   6059   8156    353    -60    971       N  
ATOM    788  CA  GLY A 111      49.304  37.099  12.192  1.00 43.14           C  
ANISOU  788  CA  GLY A 111     4537   4905   6948    427   -170   1049       C  
ATOM    789  C   GLY A 111      48.959  37.226  10.719  1.00 43.51           C  
ANISOU  789  C   GLY A 111     4688   4961   6883    422   -216   1248       C  
ATOM    790  O   GLY A 111      48.192  36.426  10.175  1.00 47.05           O  
ANISOU  790  O   GLY A 111     5175   5511   7191    445   -315   1295       O  
ATOM    791  N   ARG A 112      49.541  38.213  10.051  1.00 49.11           N  
ANISOU  791  N   ARG A 112     5453   5565   7643    381   -148   1369       N  
ATOM    792  CA  ARG A 112      49.340  38.376   8.619  1.00 52.77           C  
ANISOU  792  CA  ARG A 112     6044   6042   7966    366   -181   1575       C  
ATOM    793  C   ARG A 112      49.744  37.070   7.937  1.00 57.37           C  
ANISOU  793  C   ARG A 112     6708   6803   8288    323   -170   1541       C  
ATOM    794  O   ARG A 112      48.918  36.406   7.291  1.00 57.48           O  
ANISOU  794  O   ARG A 112     6788   6911   8142    347   -290   1598       O  
ATOM    795  CB  ARG A 112      50.112  39.613   8.143  1.00 53.52           C  
ANISOU  795  CB  ARG A 112     6188   5986   8162    310    -71   1701       C  
ATOM    796  CG  ARG A 112      49.807  40.004   6.714  1.00 45.97           C  
ANISOU  796  CG  ARG A 112     5382   5019   7067    300   -111   1950       C  
ATOM    797  CD  ARG A 112      50.507  41.272   6.329  1.00 53.30           C  
ANISOU  797  CD  ARG A 112     6357   5774   8119    240      7   2091       C  
ATOM    798  NE  ARG A 112      51.932  41.059   6.105  1.00 70.05           N  
ANISOU  798  NE  ARG A 112     8496   7943  10177    125    194   2040       N  
ATOM    799  CZ  ARG A 112      52.454  40.556   4.987  1.00 77.09           C  
ANISOU  799  CZ  ARG A 112     9515   8954  10823     63    273   2132       C  
ATOM    800  NH1 ARG A 112      51.674  40.200   3.970  1.00 80.73           N  
ANISOU  800  NH1 ARG A 112    10120   9504  11048     96    160   2277       N  
ATOM    801  NH2 ARG A 112      53.766  40.406   4.886  1.00 80.97           N  
ANISOU  801  NH2 ARG A 112     9984   9478  11302    -33    465   2071       N  
ATOM    802  N   LYS A 113      51.016  36.685   8.072  1.00 55.37           N  
ANISOU  802  N   LYS A 113     6444   6591   8002    260    -29   1441       N  
ATOM    803  CA  LYS A 113      51.561  35.583   7.285  1.00 49.91           C  
ANISOU  803  CA  LYS A 113     5843   6041   7081    223     23   1415       C  
ATOM    804  C   LYS A 113      50.810  34.292   7.551  1.00 49.46           C  
ANISOU  804  C   LYS A 113     5782   6098   6913    267    -95   1311       C  
ATOM    805  O   LYS A 113      50.625  33.472   6.642  1.00 48.00           O  
ANISOU  805  O   LYS A 113     5713   6011   6513    253   -128   1333       O  
ATOM    806  CB  LYS A 113      53.041  35.401   7.606  1.00 54.41           C  
ANISOU  806  CB  LYS A 113     6348   6624   7700    168    194   1304       C  
ATOM    807  CG  LYS A 113      53.928  36.527   7.062  1.00 60.55           C  
ANISOU  807  CG  LYS A 113     7144   7307   8556     93    342   1420       C  
ATOM    808  CD  LYS A 113      54.140  36.394   5.582  1.00 60.38           C  
ANISOU  808  CD  LYS A 113     7289   7349   8303     48    421   1563       C  
ATOM    809  CE  LYS A 113      55.432  37.051   5.145  1.00 71.60           C  
ANISOU  809  CE  LYS A 113     8700   8723   9783    -47    637   1621       C  
ATOM    810  NZ  LYS A 113      55.690  36.747   3.705  1.00 78.49           N  
ANISOU  810  NZ  LYS A 113     9751   9687  10383    -91    745   1741       N  
ATOM    811  N   LEU A 114      50.375  34.096   8.796  1.00 40.63           N  
ANISOU  811  N   LEU A 114     4542   4962   5933    312   -154   1193       N  
ATOM    812  CA  LEU A 114      49.655  32.887   9.147  1.00 40.79           C  
ANISOU  812  CA  LEU A 114     4550   5072   5874    342   -253   1102       C  
ATOM    813  C   LEU A 114      48.294  32.859   8.469  1.00 43.41           C  
ANISOU  813  C   LEU A 114     4931   5426   6135    364   -410   1215       C  
ATOM    814  O   LEU A 114      47.877  31.817   7.948  1.00 48.75           O  
ANISOU  814  O   LEU A 114     5675   6195   6652    349   -486   1194       O  
ATOM    815  CB  LEU A 114      49.516  32.779  10.673  1.00 42.53           C  
ANISOU  815  CB  LEU A 114     4639   5269   6252    377   -260    968       C  
ATOM    816  CG  LEU A 114      48.789  31.512  11.140  1.00 44.76           C  
ANISOU  816  CG  LEU A 114     4906   5633   6467    397   -344    885       C  
ATOM    817  CD1 LEU A 114      49.683  30.263  10.983  1.00 43.55           C  
ANISOU  817  CD1 LEU A 114     4805   5555   6187    373   -290    792       C  
ATOM    818  CD2 LEU A 114      48.269  31.641  12.573  1.00 46.68           C  
ANISOU  818  CD2 LEU A 114     5036   5848   6853    434   -361    799       C  
ATOM    819  N   ALA A 115      47.587  33.992   8.473  1.00 42.08           N  
ANISOU  819  N   ALA A 115     4723   5167   6100    402   -468   1331       N  
ATOM    820  CA  ALA A 115      46.289  34.057   7.806  1.00 45.36           C  
ANISOU  820  CA  ALA A 115     5159   5601   6474    433   -640   1457       C  
ATOM    821  C   ALA A 115      46.433  33.826   6.311  1.00 47.35           C  
ANISOU  821  C   ALA A 115     5585   5924   6481    384   -683   1577       C  
ATOM    822  O   ALA A 115      45.621  33.117   5.712  1.00 51.39           O  
ANISOU  822  O   ALA A 115     6147   6524   6856    375   -831   1601       O  
ATOM    823  CB  ALA A 115      45.610  35.395   8.093  1.00 48.33           C  
ANISOU  823  CB  ALA A 115     5450   5843   7069    501   -682   1565       C  
ATOM    824  N   GLU A 116      47.488  34.376   5.701  1.00 45.39           N  
ANISOU  824  N   GLU A 116     5437   5644   6167    342   -549   1645       N  
ATOM    825  CA  GLU A 116      47.769  34.100   4.290  1.00 47.79           C  
ANISOU  825  CA  GLU A 116     5932   6030   6197    286   -549   1744       C  
ATOM    826  C   GLU A 116      48.001  32.616   4.037  1.00 49.53           C  
ANISOU  826  C   GLU A 116     6224   6382   6215    248   -540   1592       C  
ATOM    827  O   GLU A 116      47.634  32.101   2.973  1.00 53.88           O  
ANISOU  827  O   GLU A 116     6924   7021   6524    215   -631   1639       O  
ATOM    828  CB  GLU A 116      48.988  34.896   3.810  1.00 48.11           C  
ANISOU  828  CB  GLU A 116     6048   6013   6218    236   -355   1826       C  
ATOM    829  CG  GLU A 116      48.880  36.442   3.867  1.00 58.82           C  
ANISOU  829  CG  GLU A 116     7373   7208   7766    257   -347   1999       C  
ATOM    830  CD  GLU A 116      47.975  37.053   2.805  1.00 80.06           C  
ANISOU  830  CD  GLU A 116    10186   9883  10351    278   -507   2240       C  
ATOM    831  OE1 GLU A 116      47.886  38.309   2.752  1.00 89.32           O  
ANISOU  831  OE1 GLU A 116    11352  10905  11680    301   -503   2404       O  
ATOM    832  OE2 GLU A 116      47.368  36.295   2.011  1.00 86.00           O  
ANISOU  832  OE2 GLU A 116    11046  10764  10867    270   -646   2268       O  
ATOM    833  N   MET A 117      48.651  31.914   4.976  1.00 44.74           N  
ANISOU  833  N   MET A 117     5524   5782   5694    253   -434   1409       N  
ATOM    834  CA  MET A 117      48.873  30.480   4.784  1.00 43.71           C  
ANISOU  834  CA  MET A 117     5459   5747   5403    229   -423   1263       C  
ATOM    835  C   MET A 117      47.552  29.719   4.843  1.00 47.44           C  
ANISOU  835  C   MET A 117     5919   6264   5841    235   -629   1236       C  
ATOM    836  O   MET A 117      47.319  28.806   4.044  1.00 53.95           O  
ANISOU  836  O   MET A 117     6872   7166   6460    194   -694   1195       O  
ATOM    837  CB  MET A 117      49.844  29.923   5.832  1.00 46.92           C  
ANISOU  837  CB  MET A 117     5758   6137   5934    245   -284   1096       C  
ATOM    838  CG  MET A 117      50.217  28.449   5.584  1.00 49.79           C  
ANISOU  838  CG  MET A 117     6197   6570   6151    233   -249    950       C  
ATOM    839  SD  MET A 117      51.220  27.626   6.864  1.00 55.15           S  
ANISOU  839  SD  MET A 117     6744   7227   6984    273   -135    771       S  
ATOM    840  CE  MET A 117      50.013  27.256   8.162  1.00 45.23           C  
ANISOU  840  CE  MET A 117     5370   5946   5870    303   -300    730       C  
ATOM    841  N   HIS A 118      46.684  30.070   5.797  1.00 51.77           N  
ANISOU  841  N   HIS A 118     6311   6764   6596    279   -723   1246       N  
ATOM    842  CA  HIS A 118      45.341  29.494   5.844  1.00 54.24           C  
ANISOU  842  CA  HIS A 118     6579   7116   6915    278   -916   1243       C  
ATOM    843  C   HIS A 118      44.598  29.731   4.537  1.00 56.18           C  
ANISOU  843  C   HIS A 118     6940   7412   6994    251  -1086   1385       C  
ATOM    844  O   HIS A 118      43.898  28.847   4.042  1.00 56.80           O  
ANISOU  844  O   HIS A 118     7070   7562   6948    207  -1232   1349       O  
ATOM    845  CB  HIS A 118      44.546  30.092   7.003  1.00 43.57           C  
ANISOU  845  CB  HIS A 118     5031   5699   5824    337   -957   1255       C  
ATOM    846  CG  HIS A 118      45.054  29.711   8.348  1.00 47.08           C  
ANISOU  846  CG  HIS A 118     5376   6116   6398    355   -833   1111       C  
ATOM    847  ND1 HIS A 118      44.652  30.349   9.497  1.00 48.49           N  
ANISOU  847  ND1 HIS A 118     5403   6232   6789    408   -808   1095       N  
ATOM    848  CD2 HIS A 118      45.927  28.748   8.734  1.00 47.60           C  
ANISOU  848  CD2 HIS A 118     5476   6206   6402    332   -733    977       C  
ATOM    849  CE1 HIS A 118      45.246  29.790  10.537  1.00 46.32           C  
ANISOU  849  CE1 HIS A 118     5088   5958   6553    407   -709    963       C  
ATOM    850  NE2 HIS A 118      46.026  28.817  10.100  1.00 45.76           N  
ANISOU  850  NE2 HIS A 118     5121   5936   6329    366   -670    899       N  
ATOM    851  N   LYS A 119      44.734  30.926   3.972  1.00 55.98           N  
ANISOU  851  N   LYS A 119     6960   7344   6966    273  -1079   1553       N  
ATOM    852  CA  LYS A 119      43.980  31.271   2.777  1.00 54.14           C  
ANISOU  852  CA  LYS A 119     6836   7156   6577    259  -1266   1721       C  
ATOM    853  C   LYS A 119      44.546  30.574   1.543  1.00 55.65           C  
ANISOU  853  C   LYS A 119     7268   7449   6426    180  -1244   1700       C  
ATOM    854  O   LYS A 119      43.792  30.039   0.726  1.00 59.95           O  
ANISOU  854  O   LYS A 119     7910   8081   6786    137  -1437   1721       O  
ATOM    855  CB  LYS A 119      43.984  32.785   2.615  1.00 51.44           C  
ANISOU  855  CB  LYS A 119     6477   6715   6354    313  -1256   1923       C  
ATOM    856  CG  LYS A 119      43.096  33.311   1.539  1.00 56.46           C  
ANISOU  856  CG  LYS A 119     7196   7376   6879    323  -1478   2134       C  
ATOM    857  CD  LYS A 119      43.198  34.829   1.478  1.00 63.44           C  
ANISOU  857  CD  LYS A 119     8064   8125   7916    386  -1443   2338       C  
ATOM    858  CE  LYS A 119      42.499  35.386   0.244  1.00 69.21           C  
ANISOU  858  CE  LYS A 119     8923   8882   8492    395  -1660   2587       C  
ATOM    859  NZ  LYS A 119      42.544  36.875   0.184  1.00 71.01           N  
ANISOU  859  NZ  LYS A 119     9139   8948   8893    464  -1636   2807       N  
ATOM    860  N   ALA A 120      45.873  30.535   1.406  1.00 55.46           N  
ANISOU  860  N   ALA A 120     7338   7419   6315    156  -1009   1643       N  
ATOM    861  CA  ALA A 120      46.482  29.930   0.227  1.00 56.76           C  
ANISOU  861  CA  ALA A 120     7737   7678   6152     88   -943   1612       C  
ATOM    862  C   ALA A 120      46.457  28.409   0.259  1.00 57.88           C  
ANISOU  862  C   ALA A 120     7924   7885   6183     50   -958   1395       C  
ATOM    863  O   ALA A 120      46.367  27.778  -0.796  1.00 64.52           O  
ANISOU  863  O   ALA A 120     8964   8813   6738     -9  -1015   1362       O  
ATOM    864  CB  ALA A 120      47.931  30.393   0.077  1.00 48.53           C  
ANISOU  864  CB  ALA A 120     6751   6605   5082     76   -658   1620       C  
ATOM    865  N   GLY A 121      46.545  27.801   1.436  1.00 56.66           N  
ANISOU  865  N   GLY A 121     7606   7683   6240     81   -908   1245       N  
ATOM    866  CA  GLY A 121      46.616  26.355   1.503  1.00 59.49           C  
ANISOU  866  CA  GLY A 121     8013   8072   6518     48   -904   1047       C  
ATOM    867  C   GLY A 121      45.291  25.637   1.367  1.00 62.29           C  
ANISOU  867  C   GLY A 121     8364   8463   6841      4  -1157   1016       C  
ATOM    868  O   GLY A 121      44.515  25.590   2.318  1.00 69.41           O  
ANISOU  868  O   GLY A 121     9080   9325   7967     26  -1253   1012       O  
ATOM    869  N   LYS A 122      45.044  25.036   0.204  1.00 65.23           N  
ANISOU  869  N   LYS A 122     8939   8912   6935    -66  -1257    981       N  
ATOM    870  CA  LYS A 122      43.751  24.461  -0.136  1.00 65.65           C  
ANISOU  870  CA  LYS A 122     9000   9010   6934   -130  -1533    966       C  
ATOM    871  C   LYS A 122      43.906  23.015  -0.587  1.00 68.12           C  
ANISOU  871  C   LYS A 122     9473   9342   7069   -205  -1531    754       C  
ATOM    872  O   LYS A 122      44.998  22.557  -0.941  1.00 65.85           O  
ANISOU  872  O   LYS A 122     9334   9050   6637   -202  -1324    639       O  
ATOM    873  CB  LYS A 122      43.031  25.273  -1.231  1.00 71.92           C  
ANISOU  873  CB  LYS A 122     9894   9884   7549   -156  -1744   1155       C  
ATOM    874  CG  LYS A 122      42.728  26.707  -0.821  1.00 83.58           C  
ANISOU  874  CG  LYS A 122    11211  11315   9229    -75  -1773   1374       C  
ATOM    875  CD  LYS A 122      42.105  27.505  -1.954  1.00 90.85           C  
ANISOU  875  CD  LYS A 122    12249  12304   9967    -88  -1983   1584       C  
ATOM    876  CE  LYS A 122      41.752  28.911  -1.490  1.00 95.05           C  
ANISOU  876  CE  LYS A 122    12611  12758  10747      7  -2015   1800       C  
ATOM    877  NZ  LYS A 122      41.165  29.737  -2.577  1.00102.71           N  
ANISOU  877  NZ  LYS A 122    13694  13776  11554      9  -2228   2035       N  
ATOM    878  N   THR A 123      42.782  22.301  -0.571  1.00 66.99           N  
ANISOU  878  N   THR A 123     9288   9210   6957   -275  -1762    698       N  
ATOM    879  CA  THR A 123      42.737  20.905  -0.975  1.00 65.21           C  
ANISOU  879  CA  THR A 123     9208   8977   6591   -362  -1799    490       C  
ATOM    880  C   THR A 123      41.363  20.586  -1.539  1.00 71.40           C  
ANISOU  880  C   THR A 123     9999   9821   7309   -468  -2129    503       C  
ATOM    881  O   THR A 123      40.346  21.132  -1.099  1.00 75.54           O  
ANISOU  881  O   THR A 123    10316  10357   8030   -461  -2308    635       O  
ATOM    882  CB  THR A 123      43.036  19.950   0.188  1.00 68.80           C  
ANISOU  882  CB  THR A 123     9543   9318   7279   -342  -1667    340       C  
ATOM    883  OG1 THR A 123      43.140  18.611  -0.315  1.00 66.76           O  
ANISOU  883  OG1 THR A 123     9462   9028   6877   -420  -1676    133       O  
ATOM    884  CG2 THR A 123      41.928  20.025   1.266  1.00 48.32           C  
ANISOU  884  CG2 THR A 123     6685   6688   4986   -348  -1809    408       C  
ATOM    885  N   SER A 124      41.351  19.687  -2.519  1.00 69.29           N  
ANISOU  885  N   SER A 124     9968   9590   6771   -566  -2207    352       N  
ATOM    886  CA  SER A 124      40.127  19.153  -3.103  1.00 71.82           C  
ANISOU  886  CA  SER A 124    10317   9963   7010   -693  -2532    313       C  
ATOM    887  C   SER A 124      39.641  17.884  -2.416  1.00 70.98           C  
ANISOU  887  C   SER A 124    10115   9754   7101   -772  -2577    133       C  
ATOM    888  O   SER A 124      38.581  17.371  -2.784  1.00 75.84           O  
ANISOU  888  O   SER A 124    10716  10397   7701   -895  -2850     88       O  
ATOM    889  CB  SER A 124      40.344  18.885  -4.592  1.00 77.99           C  
ANISOU  889  CB  SER A 124    11433  10840   7358   -774  -2609    234       C  
ATOM    890  OG  SER A 124      41.647  18.363  -4.814  1.00 84.16           O  
ANISOU  890  OG  SER A 124    12417  11578   7983   -741  -2304     72       O  
ATOM    891  N   LYS A 125      40.390  17.367  -1.435  1.00 69.71           N  
ANISOU  891  N   LYS A 125     9886   9472   7128   -710  -2326     39       N  
ATOM    892  CA  LYS A 125      40.110  16.083  -0.806  1.00 68.66           C  
ANISOU  892  CA  LYS A 125     9706   9217   7162   -781  -2328   -128       C  
ATOM    893  C   LYS A 125      39.329  16.189   0.501  1.00 69.90           C  
ANISOU  893  C   LYS A 125     9554   9322   7684   -772  -2368    -31       C  
ATOM    894  O   LYS A 125      38.980  15.156   1.081  1.00 74.99           O  
ANISOU  894  O   LYS A 125    10145   9862   8486   -844  -2378   -139       O  
ATOM    895  CB  LYS A 125      41.421  15.329  -0.582  1.00 73.23           C  
ANISOU  895  CB  LYS A 125    10424   9687   7711   -717  -2037   -291       C  
ATOM    896  CG  LYS A 125      42.245  15.233  -1.845  1.00 81.56           C  
ANISOU  896  CG  LYS A 125    11778  10796   8413   -717  -1948   -398       C  
ATOM    897  CD  LYS A 125      43.549  14.496  -1.655  1.00 87.66           C  
ANISOU  897  CD  LYS A 125    12663  11459   9184   -637  -1651   -564       C  
ATOM    898  CE  LYS A 125      44.341  14.487  -2.954  1.00 95.03           C  
ANISOU  898  CE  LYS A 125    13888  12462   9757   -636  -1535   -669       C  
ATOM    899  NZ  LYS A 125      45.767  14.133  -2.726  1.00 96.10           N  
ANISOU  899  NZ  LYS A 125    14074  12515   9926   -517  -1199   -778       N  
ATOM    900  N   GLY A 126      39.032  17.396   0.972  1.00 66.38           N  
ANISOU  900  N   GLY A 126     8912   8935   7373   -688  -2380    167       N  
ATOM    901  CA  GLY A 126      38.283  17.561   2.205  1.00 52.94           C  
ANISOU  901  CA  GLY A 126     6921   7193   6000   -673  -2392    251       C  
ATOM    902  C   GLY A 126      39.164  17.821   3.411  1.00 59.36           C  
ANISOU  902  C   GLY A 126     7643   7933   6977   -550  -2119    274       C  
ATOM    903  O   GLY A 126      40.254  18.390   3.281  1.00 60.74           O  
ANISOU  903  O   GLY A 126     7912   8119   7050   -451  -1949    295       O  
ATOM    904  N   PHE A 127      38.704  17.409   4.588  1.00 55.97           N  
ANISOU  904  N   PHE A 127     7033   7436   6799   -563  -2077    273       N  
ATOM    905  CA  PHE A 127      39.438  17.626   5.831  1.00 55.68           C  
ANISOU  905  CA  PHE A 127     6906   7338   6912   -456  -1847    298       C  
ATOM    906  C   PHE A 127      40.311  16.416   6.139  1.00 54.82           C  
ANISOU  906  C   PHE A 127     6933   7117   6777   -463  -1703    152       C  
ATOM    907  O   PHE A 127      39.878  15.271   5.986  1.00 62.77           O  
ANISOU  907  O   PHE A 127     8000   8055   7794   -571  -1779     49       O  
ATOM    908  CB  PHE A 127      38.462  17.910   6.978  1.00 50.95           C  
ANISOU  908  CB  PHE A 127     6046   6735   6578   -459  -1864    389       C  
ATOM    909  CG  PHE A 127      37.513  19.046   6.683  1.00 55.20           C  
ANISOU  909  CG  PHE A 127     6424   7365   7183   -441  -2013    528       C  
ATOM    910  CD1 PHE A 127      37.938  20.368   6.783  1.00 52.47           C  
ANISOU  910  CD1 PHE A 127     6036   7055   6844   -316  -1937    637       C  
ATOM    911  CD2 PHE A 127      36.212  18.796   6.279  1.00 60.21           C  
ANISOU  911  CD2 PHE A 127     6947   8039   7890   -547  -2238    551       C  
ATOM    912  CE1 PHE A 127      37.084  21.418   6.511  1.00 54.79           C  
ANISOU  912  CE1 PHE A 127     6187   7409   7221   -282  -2073    773       C  
ATOM    913  CE2 PHE A 127      35.338  19.848   5.992  1.00 63.43           C  
ANISOU  913  CE2 PHE A 127     7191   8528   8383   -512  -2389    689       C  
ATOM    914  CZ  PHE A 127      35.776  21.161   6.110  1.00 60.31           C  
ANISOU  914  CZ  PHE A 127     6763   8153   7997   -371  -2303    804       C  
ATOM    915  N   GLY A 128      41.553  16.670   6.528  1.00 50.32           N  
ANISOU  915  N   GLY A 128     6412   6522   6186   -348  -1503    143       N  
ATOM    916  CA  GLY A 128      42.489  15.590   6.764  1.00 42.85           C  
ANISOU  916  CA  GLY A 128     5588   5466   5225   -326  -1367     15       C  
ATOM    917  C   GLY A 128      43.842  15.928   6.178  1.00 50.19           C  
ANISOU  917  C   GLY A 128     6650   6416   6003   -230  -1216    -28       C  
ATOM    918  O   GLY A 128      44.185  17.109   6.052  1.00 54.70           O  
ANISOU  918  O   GLY A 128     7174   7070   6539   -165  -1171     70       O  
ATOM    919  N   PHE A 129      44.600  14.905   5.788  1.00 51.92           N  
ANISOU  919  N   PHE A 129     7030   6551   6143   -222  -1130   -174       N  
ATOM    920  CA  PHE A 129      45.949  15.089   5.266  1.00 53.59           C  
ANISOU  920  CA  PHE A 129     7352   6775   6236   -128   -952   -231       C  
ATOM    921  C   PHE A 129      46.365  13.831   4.503  1.00 56.18           C  
ANISOU  921  C   PHE A 129     7886   7011   6450   -154   -908   -422       C  
ATOM    922  O   PHE A 129      45.739  12.774   4.609  1.00 62.29           O  
ANISOU  922  O   PHE A 129     8706   7684   7277   -234  -1001   -507       O  
ATOM    923  CB  PHE A 129      46.945  15.421   6.399  1.00 44.63           C  
ANISOU  923  CB  PHE A 129     6085   5609   5265     -3   -787   -180       C  
ATOM    924  CG  PHE A 129      48.202  16.152   5.923  1.00 47.99           C  
ANISOU  924  CG  PHE A 129     6539   6091   5604     87   -617   -178       C  
ATOM    925  CD1 PHE A 129      48.107  17.384   5.270  1.00 43.53           C  
ANISOU  925  CD1 PHE A 129     5973   5640   4927     74   -632    -76       C  
ATOM    926  CD2 PHE A 129      49.467  15.617   6.141  1.00 50.85           C  
ANISOU  926  CD2 PHE A 129     6918   6387   6018    183   -443   -265       C  
ATOM    927  CE1 PHE A 129      49.254  18.065   4.849  1.00 49.24           C  
ANISOU  927  CE1 PHE A 129     6716   6408   5585    139   -460    -63       C  
ATOM    928  CE2 PHE A 129      50.619  16.295   5.717  1.00 50.53           C  
ANISOU  928  CE2 PHE A 129     6874   6401   5924    255   -275   -261       C  
ATOM    929  CZ  PHE A 129      50.509  17.515   5.067  1.00 45.66           C  
ANISOU  929  CZ  PHE A 129     6262   5897   5189    224   -276   -160       C  
ATOM    930  N   GLU A 130      47.450  13.962   3.738  1.00 60.27           N  
ANISOU  930  N   GLU A 130     8526   7556   6820    -87   -749   -494       N  
ATOM    931  CA  GLU A 130      47.949  12.865   2.912  1.00 65.33           C  
ANISOU  931  CA  GLU A 130     9377   8114   7334    -94   -670   -695       C  
ATOM    932  C   GLU A 130      48.357  11.647   3.740  1.00 66.83           C  
ANISOU  932  C   GLU A 130     9548   8120   7724    -39   -596   -792       C  
ATOM    933  O   GLU A 130      48.182  10.507   3.294  1.00 69.24           O  
ANISOU  933  O   GLU A 130    10009   8306   7992    -90   -621   -955       O  
ATOM    934  CB  GLU A 130      49.152  13.373   2.117  1.00 88.42           C  
ANISOU  934  CB  GLU A 130    12390  11110  10097    -11   -460   -732       C  
ATOM    935  CG  GLU A 130      48.859  14.429   1.063  1.00113.59           C  
ANISOU  935  CG  GLU A 130    15664  14461  13033    -71   -512   -647       C  
ATOM    936  CD  GLU A 130      50.128  14.940   0.361  1.00131.05           C  
ANISOU  936  CD  GLU A 130    17952  16738  15102      6   -263   -667       C  
ATOM    937  OE1 GLU A 130      51.253  14.619   0.813  1.00132.22           O  
ANISOU  937  OE1 GLU A 130    18033  16817  15390    117    -54   -731       O  
ATOM    938  OE2 GLU A 130      49.995  15.651  -0.659  1.00136.67           O  
ANISOU  938  OE2 GLU A 130    18790  17572  15564    -48   -278   -612       O  
ATOM    939  N   VAL A 131      48.898  11.860   4.942  1.00 57.69           N  
ANISOU  939  N   VAL A 131     8214   6929   6778     64   -516   -695       N  
ATOM    940  CA  VAL A 131      49.318  10.786   5.833  1.00 65.70           C  
ANISOU  940  CA  VAL A 131     9201   7772   7990    131   -460   -745       C  
ATOM    941  C   VAL A 131      48.888  11.110   7.259  1.00 62.53           C  
ANISOU  941  C   VAL A 131     8606   7371   7783    139   -531   -579       C  
ATOM    942  O   VAL A 131      48.664  12.267   7.619  1.00 56.25           O  
ANISOU  942  O   VAL A 131     7677   6705   6989    139   -561   -445       O  
ATOM    943  CB  VAL A 131      50.853  10.549   5.794  1.00 70.51           C  
ANISOU  943  CB  VAL A 131     9817   8329   8644    292   -242   -824       C  
ATOM    944  CG1 VAL A 131      51.290  10.072   4.420  1.00 76.37           C  
ANISOU  944  CG1 VAL A 131    10767   9053   9196    289   -135  -1013       C  
ATOM    945  CG2 VAL A 131      51.623  11.820   6.204  1.00 66.99           C  
ANISOU  945  CG2 VAL A 131     9200   8018   8233    378   -149   -694       C  
ATOM    946  N   ASP A 132      48.744  10.063   8.070  1.00 63.88           N  
ANISOU  946  N   ASP A 132     8774   7385   8111    142   -553   -591       N  
ATOM    947  CA  ASP A 132      48.682  10.271   9.507  1.00 58.99           C  
ANISOU  947  CA  ASP A 132     7995   6760   7660    183   -568   -443       C  
ATOM    948  C   ASP A 132      50.034  10.783   9.992  1.00 58.76           C  
ANISOU  948  C   ASP A 132     7872   6769   7686    343   -435   -408       C  
ATOM    949  O   ASP A 132      51.078  10.434   9.441  1.00 63.04           O  
ANISOU  949  O   ASP A 132     8476   7264   8214    438   -315   -512       O  
ATOM    950  CB  ASP A 132      48.306   8.983  10.230  1.00 61.81           C  
ANISOU  950  CB  ASP A 132     8395   6931   8160    151   -609   -448       C  
ATOM    951  CG  ASP A 132      46.885   8.528   9.917  1.00 75.87           C  
ANISOU  951  CG  ASP A 132    10225   8676   9927    -31   -752   -466       C  
ATOM    952  OD1 ASP A 132      46.161   9.248   9.192  1.00 80.66           O  
ANISOU  952  OD1 ASP A 132    10817   9415  10414   -122   -839   -465       O  
ATOM    953  OD2 ASP A 132      46.478   7.461  10.424  1.00 78.61           O  
ANISOU  953  OD2 ASP A 132    10615   8859  10395    -87   -785   -468       O  
ATOM    954  N   ASN A 133      50.005  11.663  10.998  1.00 49.30           N  
ANISOU  954  N   ASN A 133     6518   5662   6552    369   -453   -270       N  
ATOM    955  CA  ASN A 133      51.232  12.180  11.597  1.00 44.49           C  
ANISOU  955  CA  ASN A 133     5799   5093   6014    502   -359   -231       C  
ATOM    956  C   ASN A 133      51.074  12.168  13.114  1.00 47.57           C  
ANISOU  956  C   ASN A 133     6085   5467   6521    524   -414   -110       C  
ATOM    957  O   ASN A 133      50.355  11.328  13.663  1.00 53.69           O  
ANISOU  957  O   ASN A 133     6906   6146   7348    470   -479    -78       O  
ATOM    958  CB  ASN A 133      51.586  13.584  11.067  1.00 43.56           C  
ANISOU  958  CB  ASN A 133     5610   5132   5810    509   -307   -205       C  
ATOM    959  CG  ASN A 133      50.410  14.599  11.121  1.00 48.65           C  
ANISOU  959  CG  ASN A 133     6201   5884   6398    405   -408   -110       C  
ATOM    960  OD1 ASN A 133      49.466  14.462  11.896  1.00 54.29           O  
ANISOU  960  OD1 ASN A 133     6874   6585   7169    347   -499    -43       O  
ATOM    961  ND2 ASN A 133      50.481  15.620  10.265  1.00 48.34           N  
ANISOU  961  ND2 ASN A 133     6163   5949   6256    385   -380    -98       N  
ATOM    962  N   THR A 134      51.738  13.068  13.814  1.00 40.89           N  
ANISOU  962  N   THR A 134     5112   4713   5713    593   -387    -45       N  
ATOM    963  CA  THR A 134      51.715  13.015  15.266  1.00 51.15           C  
ANISOU  963  CA  THR A 134     6337   6004   7091    621   -437     57       C  
ATOM    964  C   THR A 134      51.622  14.430  15.802  1.00 54.04           C  
ANISOU  964  C   THR A 134     6582   6516   7436    606   -447    123       C  
ATOM    965  O   THR A 134      52.095  15.371  15.166  1.00 56.47           O  
ANISOU  965  O   THR A 134     6840   6905   7712    620   -396     94       O  
ATOM    966  CB  THR A 134      52.966  12.312  15.852  1.00 54.62           C  
ANISOU  966  CB  THR A 134     6756   6361   7635    759   -411     54       C  
ATOM    967  OG1 THR A 134      54.160  12.931  15.354  1.00 50.84           O  
ANISOU  967  OG1 THR A 134     6195   5946   7177    846   -329     -2       O  
ATOM    968  CG2 THR A 134      52.994  10.825  15.477  1.00 53.74           C  
ANISOU  968  CG2 THR A 134     6774   6067   7577    784   -402     -5       C  
ATOM    969  N   ILE A 135      50.985  14.575  16.963  1.00 46.96           N  
ANISOU  969  N   ILE A 135     5647   5643   6554    572   -500    210       N  
ATOM    970  CA  ILE A 135      50.923  15.838  17.684  1.00 48.59           C  
ANISOU  970  CA  ILE A 135     5747   5965   6749    568   -505    258       C  
ATOM    971  C   ILE A 135      51.670  15.612  18.991  1.00 59.12           C  
ANISOU  971  C   ILE A 135     7048   7294   8120    642   -531    304       C  
ATOM    972  O   ILE A 135      51.177  14.915  19.895  1.00 58.18           O  
ANISOU  972  O   ILE A 135     6977   7132   7996    622   -567    371       O  
ATOM    973  CB  ILE A 135      49.478  16.331  17.901  1.00 48.45           C  
ANISOU  973  CB  ILE A 135     5710   5995   6703    465   -532    306       C  
ATOM    974  CG1 ILE A 135      49.464  17.560  18.795  1.00 49.89           C  
ANISOU  974  CG1 ILE A 135     5796   6274   6886    476   -522    339       C  
ATOM    975  CG2 ILE A 135      48.564  15.238  18.456  1.00 41.23           C  
ANISOU  975  CG2 ILE A 135     4857   5006   5803    402   -564    356       C  
ATOM    976  CD1 ILE A 135      50.316  18.641  18.273  1.00 52.62           C  
ANISOU  976  CD1 ILE A 135     6080   6674   7239    518   -490    299       C  
ATOM    977  N   GLY A 136      52.877  16.165  19.078  1.00 57.77           N  
ANISOU  977  N   GLY A 136     6798   7168   7985    721   -516    274       N  
ATOM    978  CA  GLY A 136      53.800  15.668  20.086  1.00 53.88           C  
ANISOU  978  CA  GLY A 136     6282   6653   7538    810   -567    309       C  
ATOM    979  C   GLY A 136      54.185  14.262  19.661  1.00 60.26           C  
ANISOU  979  C   GLY A 136     7165   7325   8405    874   -562    297       C  
ATOM    980  O   GLY A 136      54.485  14.009  18.486  1.00 66.68           O  
ANISOU  980  O   GLY A 136     7998   8093   9245    893   -494    216       O  
ATOM    981  N   SER A 137      54.107  13.315  20.581  1.00 62.22           N  
ANISOU  981  N   SER A 137     7476   7497   8669    904   -626    376       N  
ATOM    982  CA  SER A 137      54.325  11.924  20.209  1.00 66.68           C  
ANISOU  982  CA  SER A 137     8131   7897   9308    961   -621    370       C  
ATOM    983  C   SER A 137      53.031  11.153  19.933  1.00 61.28           C  
ANISOU  983  C   SER A 137     7576   7115   8591    849   -612    387       C  
ATOM    984  O   SER A 137      53.097   9.987  19.536  1.00 60.29           O  
ANISOU  984  O   SER A 137     7544   6830   8533    877   -603    365       O  
ATOM    985  CB  SER A 137      55.154  11.215  21.295  1.00 67.74           C  
ANISOU  985  CB  SER A 137     8260   7971   9507   1076   -706    461       C  
ATOM    986  OG  SER A 137      54.334  10.757  22.358  1.00 75.21           O  
ANISOU  986  OG  SER A 137     9300   8889  10389   1016   -765    586       O  
ATOM    987  N   THR A 138      51.857  11.768  20.146  1.00 55.57           N  
ANISOU  987  N   THR A 138     6852   6477   7787    724   -613    420       N  
ATOM    988  CA  THR A 138      50.575  11.082  19.968  1.00 54.68           C  
ANISOU  988  CA  THR A 138     6827   6284   7665    602   -614    444       C  
ATOM    989  C   THR A 138      50.216  10.998  18.485  1.00 58.27           C  
ANISOU  989  C   THR A 138     7317   6706   8116    547   -585    327       C  
ATOM    990  O   THR A 138      50.328  12.002  17.778  1.00 56.96           O  
ANISOU  990  O   THR A 138     7089   6653   7902    543   -560    266       O  
ATOM    991  CB  THR A 138      49.471  11.830  20.699  1.00 53.83           C  
ANISOU  991  CB  THR A 138     6673   6289   7493    498   -614    515       C  
ATOM    992  OG1 THR A 138      49.905  12.135  22.026  1.00 58.55           O  
ANISOU  992  OG1 THR A 138     7246   6950   8051    551   -635    601       O  
ATOM    993  CG2 THR A 138      48.178  11.011  20.749  1.00 49.27           C  
ANISOU  993  CG2 THR A 138     6161   5623   6935    367   -613    564       C  
ATOM    994  N   PRO A 139      49.754   9.845  17.986  1.00 58.60           N  
ANISOU  994  N   PRO A 139     7471   6596   8199    493   -593    293       N  
ATOM    995  CA  PRO A 139      49.269   9.787  16.603  1.00 52.42           C  
ANISOU  995  CA  PRO A 139     6740   5799   7380    417   -588    174       C  
ATOM    996  C   PRO A 139      48.148  10.791  16.364  1.00 55.91           C  
ANISOU  996  C   PRO A 139     7107   6383   7752    298   -619    195       C  
ATOM    997  O   PRO A 139      47.316  11.058  17.239  1.00 55.51           O  
ANISOU  997  O   PRO A 139     6997   6381   7715    231   -638    292       O  
ATOM    998  CB  PRO A 139      48.759   8.348  16.464  1.00 48.99           C  
ANISOU  998  CB  PRO A 139     6435   5163   7014    350   -612    154       C  
ATOM    999  CG  PRO A 139      49.462   7.591  17.501  1.00 50.83           C  
ANISOU  999  CG  PRO A 139     6696   5280   7335    452   -607    242       C  
ATOM   1000  CD  PRO A 139      49.600   8.540  18.656  1.00 58.47           C  
ANISOU 1000  CD  PRO A 139     7551   6404   8260    487   -616    365       C  
ATOM   1001  N   GLN A 140      48.146  11.357  15.163  1.00 51.59           N  
ANISOU 1001  N   GLN A 140     6566   5903   7131    280   -616    106       N  
ATOM   1002  CA  GLN A 140      47.116  12.288  14.726  1.00 48.66           C  
ANISOU 1002  CA  GLN A 140     6130   5655   6705    183   -664    125       C  
ATOM   1003  C   GLN A 140      46.509  11.689  13.462  1.00 51.87           C  
ANISOU 1003  C   GLN A 140     6641   6008   7060     85   -722     28       C  
ATOM   1004  O   GLN A 140      47.165  11.642  12.417  1.00 53.48           O  
ANISOU 1004  O   GLN A 140     6931   6207   7182    124   -692    -74       O  
ATOM   1005  CB  GLN A 140      47.697  13.693  14.496  1.00 46.89           C  
ANISOU 1005  CB  GLN A 140     5820   5572   6424    251   -625    134       C  
ATOM   1006  CG  GLN A 140      46.651  14.752  14.059  1.00 52.10           C  
ANISOU 1006  CG  GLN A 140     6406   6346   7044    171   -681    173       C  
ATOM   1007  CD  GLN A 140      47.123  16.191  14.247  1.00 53.01           C  
ANISOU 1007  CD  GLN A 140     6422   6573   7147    236   -638    215       C  
ATOM   1008  OE1 GLN A 140      46.787  16.830  15.244  1.00 48.77           O  
ANISOU 1008  OE1 GLN A 140     5785   6082   6662    242   -631    282       O  
ATOM   1009  NE2 GLN A 140      47.865  16.720  13.267  1.00 45.30           N  
ANISOU 1009  NE2 GLN A 140     5480   5633   6098    275   -599    172       N  
ATOM   1010  N   ILE A 141      45.258  11.234  13.570  1.00 52.10           N  
ANISOU 1010  N   ILE A 141     6661   6002   7134    -48   -803     55       N  
ATOM   1011  CA  ILE A 141      44.578  10.506  12.499  1.00 54.33           C  
ANISOU 1011  CA  ILE A 141     7044   6218   7382   -166   -889    -44       C  
ATOM   1012  C   ILE A 141      44.021  11.501  11.485  1.00 57.44           C  
ANISOU 1012  C   ILE A 141     7400   6758   7666   -216   -969    -58       C  
ATOM   1013  O   ILE A 141      43.303  12.438  11.853  1.00 52.73           O  
ANISOU 1013  O   ILE A 141     6659   6275   7100   -241  -1007     41       O  
ATOM   1014  CB  ILE A 141      43.455   9.630  13.077  1.00 56.24           C  
ANISOU 1014  CB  ILE A 141     7266   6360   7744   -304   -949      0       C  
ATOM   1015  CG1 ILE A 141      43.971   8.769  14.229  1.00 58.03           C  
ANISOU 1015  CG1 ILE A 141     7529   6448   8074   -249   -869     61       C  
ATOM   1016  CG2 ILE A 141      42.855   8.759  12.001  1.00 55.60           C  
ANISOU 1016  CG2 ILE A 141     7299   6185   7641   -436  -1049   -124       C  
ATOM   1017  CD1 ILE A 141      45.199   7.973  13.874  1.00 60.32           C  
ANISOU 1017  CD1 ILE A 141     7964   6600   8355   -137   -811    -36       C  
ATOM   1018  N   ASN A 142      44.343  11.297  10.201  1.00 52.99           N  
ANISOU 1018  N   ASN A 142     6975   6189   6970   -227   -993   -179       N  
ATOM   1019  CA  ASN A 142      44.094  12.306   9.179  1.00 46.36           C  
ANISOU 1019  CA  ASN A 142     6133   5493   5988   -247  -1058   -177       C  
ATOM   1020  C   ASN A 142      43.274  11.760   8.011  1.00 59.63           C  
ANISOU 1020  C   ASN A 142     7928   7163   7566   -385  -1207   -276       C  
ATOM   1021  O   ASN A 142      43.334  12.289   6.893  1.00 56.68           O  
ANISOU 1021  O   ASN A 142     7637   6884   7016   -395  -1255   -312       O  
ATOM   1022  CB  ASN A 142      45.411  12.914   8.698  1.00 49.82           C  
ANISOU 1022  CB  ASN A 142     6630   5985   6314   -119   -929   -209       C  
ATOM   1023  CG  ASN A 142      46.038  13.819   9.750  1.00 55.36           C  
ANISOU 1023  CG  ASN A 142     7185   6742   7108     -7   -830    -98       C  
ATOM   1024  OD1 ASN A 142      45.330  14.393  10.589  1.00 53.21           O  
ANISOU 1024  OD1 ASN A 142     6771   6517   6929    -29   -873     10       O  
ATOM   1025  ND2 ASN A 142      47.361  13.953   9.712  1.00 57.13           N  
ANISOU 1025  ND2 ASN A 142     7437   6960   7312    108   -695   -135       N  
ATOM   1026  N   THR A 143      42.469  10.733   8.275  1.00 54.35           N  
ANISOU 1026  N   THR A 143     7265   6381   7002   -503  -1289   -312       N  
ATOM   1027  CA  THR A 143      41.635  10.123   7.253  1.00 54.88           C  
ANISOU 1027  CA  THR A 143     7433   6425   6994   -657  -1453   -420       C  
ATOM   1028  C   THR A 143      40.699  11.163   6.648  1.00 60.67           C  
ANISOU 1028  C   THR A 143     8066   7333   7653   -720  -1618   -341       C  
ATOM   1029  O   THR A 143      39.985  11.870   7.367  1.00 62.02           O  
ANISOU 1029  O   THR A 143     8030   7579   7957   -725  -1653   -198       O  
ATOM   1030  CB  THR A 143      40.822   8.983   7.887  1.00 61.04           C  
ANISOU 1030  CB  THR A 143     8181   7052   7959   -788  -1510   -435       C  
ATOM   1031  OG1 THR A 143      41.714   7.972   8.366  1.00 70.63           O  
ANISOU 1031  OG1 THR A 143     9512   8083   9241   -720  -1370   -501       O  
ATOM   1032  CG2 THR A 143      39.849   8.367   6.891  1.00 50.09           C  
ANISOU 1032  CG2 THR A 143     6872   5640   6521   -974  -1708   -551       C  
ATOM   1033  N   TRP A 144      40.693  11.234   5.318  1.00 58.32           N  
ANISOU 1033  N   TRP A 144     7921   7096   7141   -766  -1720   -434       N  
ATOM   1034  CA  TRP A 144      39.951  12.280   4.629  1.00 57.11           C  
ANISOU 1034  CA  TRP A 144     7699   7112   6890   -803  -1888   -342       C  
ATOM   1035  C   TRP A 144      38.466  12.198   4.943  1.00 61.38           C  
ANISOU 1035  C   TRP A 144     8048   7672   7602   -939  -2084   -274       C  
ATOM   1036  O   TRP A 144      37.850  11.135   4.832  1.00 65.35           O  
ANISOU 1036  O   TRP A 144     8584   8078   8166  -1083  -2187   -374       O  
ATOM   1037  CB  TRP A 144      40.161  12.192   3.119  1.00 54.14           C  
ANISOU 1037  CB  TRP A 144     7557   6792   6221   -849  -1979   -462       C  
ATOM   1038  CG  TRP A 144      41.534  12.496   2.668  1.00 59.97           C  
ANISOU 1038  CG  TRP A 144     8457   7549   6779   -719  -1779   -508       C  
ATOM   1039  CD1 TRP A 144      42.438  11.621   2.140  1.00 62.92           C  
ANISOU 1039  CD1 TRP A 144     9052   7829   7026   -698  -1651   -692       C  
ATOM   1040  CD2 TRP A 144      42.182  13.778   2.695  1.00 62.93           C  
ANISOU 1040  CD2 TRP A 144     8776   8036   7098   -592  -1668   -372       C  
ATOM   1041  NE1 TRP A 144      43.607  12.282   1.821  1.00 67.11           N  
ANISOU 1041  NE1 TRP A 144     9653   8422   7423   -567  -1460   -675       N  
ATOM   1042  CE2 TRP A 144      43.479  13.603   2.160  1.00 64.16           C  
ANISOU 1042  CE2 TRP A 144     9114   8171   7091   -508  -1471   -477       C  
ATOM   1043  CE3 TRP A 144      41.785  15.058   3.099  1.00 59.54           C  
ANISOU 1043  CE3 TRP A 144     8158   7711   6752   -542  -1711   -178       C  
ATOM   1044  CZ2 TRP A 144      44.381  14.659   2.022  1.00 60.25           C  
ANISOU 1044  CZ2 TRP A 144     8611   7762   6519   -395  -1318   -385       C  
ATOM   1045  CZ3 TRP A 144      42.680  16.104   2.961  1.00 53.33           C  
ANISOU 1045  CZ3 TRP A 144     7384   6994   5887   -428  -1568    -92       C  
ATOM   1046  CH2 TRP A 144      43.966  15.898   2.429  1.00 56.44           C  
ANISOU 1046  CH2 TRP A 144     7954   7371   6122   -363  -1375   -191       C  
ATOM   1047  N   SER A 145      37.886  13.350   5.269  1.00 65.21           N  
ANISOU 1047  N   SER A 145     8328   8278   8170   -896  -2137   -108       N  
ATOM   1048  CA  SER A 145      36.466  13.490   5.537  1.00 68.22           C  
ANISOU 1048  CA  SER A 145     8482   8704   8733  -1001  -2313    -24       C  
ATOM   1049  C   SER A 145      35.939  14.763   4.882  1.00 68.83           C  
ANISOU 1049  C   SER A 145     8465   8941   8745   -962  -2470    101       C  
ATOM   1050  O   SER A 145      36.684  15.723   4.656  1.00 69.89           O  
ANISOU 1050  O   SER A 145     8658   9139   8759   -831  -2383    169       O  
ATOM   1051  CB  SER A 145      36.204  13.534   7.033  1.00 68.51           C  
ANISOU 1051  CB  SER A 145     8306   8693   9033   -967  -2167     70       C  
ATOM   1052  OG  SER A 145      34.837  13.799   7.265  1.00 83.67           O  
ANISOU 1052  OG  SER A 145     9980  10672  11140  -1055  -2311    158       O  
ATOM   1053  N   SER A 146      34.642  14.763   4.574  1.00 69.80           N  
ANISOU 1053  N   SER A 146     8434   9120   8966  -1079  -2708    140       N  
ATOM   1054  CA  SER A 146      34.010  15.890   3.892  1.00 69.53           C  
ANISOU 1054  CA  SER A 146     8301   9229   8889  -1046  -2903    271       C  
ATOM   1055  C   SER A 146      33.177  16.770   4.816  1.00 71.06           C  
ANISOU 1055  C   SER A 146     8166   9463   9369   -981  -2890    433       C  
ATOM   1056  O   SER A 146      32.745  17.846   4.388  1.00 74.96           O  
ANISOU 1056  O   SER A 146     8560  10056   9867   -913  -3020    564       O  
ATOM   1057  CB  SER A 146      33.116  15.400   2.748  1.00 67.86           C  
ANISOU 1057  CB  SER A 146     8136   9073   8574  -1210  -3225    208       C  
ATOM   1058  OG  SER A 146      31.891  14.914   3.254  1.00 72.30           O  
ANISOU 1058  OG  SER A 146     8445   9615   9410  -1339  -3351    217       O  
ATOM   1059  N   ASP A 147      32.919  16.333   6.048  1.00 70.01           N  
ANISOU 1059  N   ASP A 147     7871   9254   9474   -999  -2736    430       N  
ATOM   1060  CA  ASP A 147      32.184  17.107   7.042  1.00 69.57           C  
ANISOU 1060  CA  ASP A 147     7513   9230   9689   -933  -2669    560       C  
ATOM   1061  C   ASP A 147      33.125  17.412   8.199  1.00 59.77           C  
ANISOU 1061  C   ASP A 147     6298   7933   8481   -801  -2364    575       C  
ATOM   1062  O   ASP A 147      33.749  16.498   8.749  1.00 59.03           O  
ANISOU 1062  O   ASP A 147     6323   7744   8361   -834  -2215    489       O  
ATOM   1063  CB  ASP A 147      30.949  16.334   7.537  1.00 77.32           C  
ANISOU 1063  CB  ASP A 147     8267  10188  10924  -1089  -2744    549       C  
ATOM   1064  CG  ASP A 147      30.146  17.096   8.599  1.00 90.60           C  
ANISOU 1064  CG  ASP A 147     9624  11906  12894  -1020  -2641    672       C  
ATOM   1065  OD1 ASP A 147      30.100  18.342   8.556  1.00 97.95           O  
ANISOU 1065  OD1 ASP A 147    10457  12904  13854   -874  -2644    777       O  
ATOM   1066  OD2 ASP A 147      29.568  16.444   9.496  1.00 98.22           O  
ANISOU 1066  OD2 ASP A 147    10437  12822  14060  -1111  -2539    662       O  
ATOM   1067  N   TRP A 148      33.237  18.697   8.557  1.00 57.97           N  
ANISOU 1067  N   TRP A 148     6634   7231   8159   -544  -1493    906       N  
ATOM   1068  CA  TRP A 148      34.189  19.091   9.597  1.00 54.53           C  
ANISOU 1068  CA  TRP A 148     6286   6723   7708   -406  -1299    902       C  
ATOM   1069  C   TRP A 148      33.721  18.656  10.980  1.00 52.78           C  
ANISOU 1069  C   TRP A 148     5992   6424   7639   -423  -1175    980       C  
ATOM   1070  O   TRP A 148      34.520  18.146  11.774  1.00 53.53           O  
ANISOU 1070  O   TRP A 148     6211   6414   7716   -385  -1071    927       O  
ATOM   1071  CB  TRP A 148      34.421  20.602   9.564  1.00 51.16           C  
ANISOU 1071  CB  TRP A 148     5813   6387   7238   -256  -1221    979       C  
ATOM   1072  CG  TRP A 148      35.193  21.101  10.738  1.00 54.52           C  
ANISOU 1072  CG  TRP A 148     6296   6748   7670   -131  -1033    983       C  
ATOM   1073  CD1 TRP A 148      34.720  21.874  11.759  1.00 54.74           C  
ANISOU 1073  CD1 TRP A 148     6216   6787   7796    -49   -901   1089       C  
ATOM   1074  CD2 TRP A 148      36.575  20.847  11.035  1.00 49.39           C  
ANISOU 1074  CD2 TRP A 148     5825   6021   6920    -72   -959    870       C  
ATOM   1075  NE1 TRP A 148      35.719  22.119  12.670  1.00 48.46           N  
ANISOU 1075  NE1 TRP A 148     5531   5926   6955     46   -762   1038       N  
ATOM   1076  CE2 TRP A 148      36.867  21.499  12.248  1.00 46.39           C  
ANISOU 1076  CE2 TRP A 148     5434   5614   6577     31   -801    912       C  
ATOM   1077  CE3 TRP A 148      37.594  20.132  10.390  1.00 46.85           C  
ANISOU 1077  CE3 TRP A 148     5666   5656   6479    -92  -1011    735       C  
ATOM   1078  CZ2 TRP A 148      38.144  21.470  12.825  1.00 47.64           C  
ANISOU 1078  CZ2 TRP A 148     5727   5714   6659    105   -712    830       C  
ATOM   1079  CZ3 TRP A 148      38.843  20.091  10.967  1.00 44.34           C  
ANISOU 1079  CZ3 TRP A 148     5470   5277   6101     -7   -908    666       C  
ATOM   1080  CH2 TRP A 148      39.112  20.758  12.175  1.00 42.24           C  
ANISOU 1080  CH2 TRP A 148     5178   4995   5875     84   -769    716       C  
ATOM   1081  N   ILE A 149      32.432  18.852  11.282  1.00 55.87           N  
ANISOU 1081  N   ILE A 149     6176   6877   8174   -472  -1181   1117       N  
ATOM   1082  CA  ILE A 149      31.879  18.476  12.583  1.00 59.96           C  
ANISOU 1082  CA  ILE A 149     6606   7342   8834   -488  -1049   1213       C  
ATOM   1083  C   ILE A 149      32.153  17.010  12.860  1.00 58.06           C  
ANISOU 1083  C   ILE A 149     6480   6958   8622   -608  -1068   1140       C  
ATOM   1084  O   ILE A 149      32.426  16.610  13.998  1.00 60.66           O  
ANISOU 1084  O   ILE A 149     6855   7204   8988   -574   -928   1172       O  
ATOM   1085  CB  ILE A 149      30.363  18.772  12.617  1.00 65.99           C  
ANISOU 1085  CB  ILE A 149     7107   8208   9759   -547  -1079   1371       C  
ATOM   1086  CG1 ILE A 149      30.087  20.271  12.468  1.00 64.22           C  
ANISOU 1086  CG1 ILE A 149     6771   8107   9525   -397  -1033   1460       C  
ATOM   1087  CG2 ILE A 149      29.720  18.240  13.898  1.00 56.74           C  
ANISOU 1087  CG2 ILE A 149     5835   6988   8735   -583   -938   1480       C  
ATOM   1088  CD1 ILE A 149      28.611  20.621  12.473  1.00 60.50           C  
ANISOU 1088  CD1 ILE A 149     6022   7747   9218   -429  -1057   1627       C  
ATOM   1089  N   GLU A 150      32.099  16.198  11.808  1.00 61.87           N  
ANISOU 1089  N   GLU A 150     7020   7406   9082   -744  -1245   1040       N  
ATOM   1090  CA  GLU A 150      32.340  14.765  11.895  1.00 63.60           C  
ANISOU 1090  CA  GLU A 150     7363   7463   9341   -867  -1283    955       C  
ATOM   1091  C   GLU A 150      33.825  14.474  12.065  1.00 63.93           C  
ANISOU 1091  C   GLU A 150     7641   7400   9248   -758  -1209    829       C  
ATOM   1092  O   GLU A 150      34.222  13.716  12.956  1.00 67.65           O  
ANISOU 1092  O   GLU A 150     8196   7742   9765   -751  -1111    836       O  
ATOM   1093  CB  GLU A 150      31.759  14.122  10.641  1.00 72.69           C  
ANISOU 1093  CB  GLU A 150     8499   8619  10501  -1044  -1506    871       C  
ATOM   1094  CG  GLU A 150      31.370  12.684  10.728  1.00 90.37           C  
ANISOU 1094  CG  GLU A 150    10773  10696  12867  -1233  -1574    829       C  
ATOM   1095  CD  GLU A 150      30.281  12.358   9.709  1.00105.58           C  
ANISOU 1095  CD  GLU A 150    12574  12683  14857  -1431  -1797    810       C  
ATOM   1096  OE1 GLU A 150      29.219  13.028   9.740  1.00109.71           O  
ANISOU 1096  OE1 GLU A 150    12855  13356  15474  -1459  -1827    956       O  
ATOM   1097  OE2 GLU A 150      30.489  11.459   8.866  1.00111.28           O  
ANISOU 1097  OE2 GLU A 150    13438  13310  15535  -1553  -1945    644       O  
ATOM   1098  N   PHE A 151      34.664  15.106  11.245  1.00 60.66           N  
ANISOU 1098  N   PHE A 151     7326   7051   8671   -663  -1247    730       N  
ATOM   1099  CA  PHE A 151      36.104  14.899  11.349  1.00 56.56           C  
ANISOU 1099  CA  PHE A 151     7005   6455   8029   -552  -1175    617       C  
ATOM   1100  C   PHE A 151      36.616  15.305  12.730  1.00 56.52           C  
ANISOU 1100  C   PHE A 151     7001   6432   8041   -423   -992    697       C  
ATOM   1101  O   PHE A 151      37.360  14.556  13.379  1.00 57.81           O  
ANISOU 1101  O   PHE A 151     7284   6481   8200   -389   -923    663       O  
ATOM   1102  CB  PHE A 151      36.835  15.686  10.255  1.00 49.18           C  
ANISOU 1102  CB  PHE A 151     6140   5623   6924   -470  -1228    529       C  
ATOM   1103  CG  PHE A 151      38.320  15.513  10.296  1.00 51.85           C  
ANISOU 1103  CG  PHE A 151     6655   5900   7143   -356  -1153    421       C  
ATOM   1104  CD1 PHE A 151      39.111  16.326  11.108  1.00 54.98           C  
ANISOU 1104  CD1 PHE A 151     7057   6327   7507   -214  -1014    465       C  
ATOM   1105  CD2 PHE A 151      38.933  14.502   9.563  1.00 49.06           C  
ANISOU 1105  CD2 PHE A 151     6464   5457   6721   -390  -1219    270       C  
ATOM   1106  CE1 PHE A 151      40.493  16.156  11.171  1.00 51.47           C  
ANISOU 1106  CE1 PHE A 151     6750   5841   6966   -113   -951    375       C  
ATOM   1107  CE2 PHE A 151      40.311  14.326   9.614  1.00 51.50           C  
ANISOU 1107  CE2 PHE A 151     6917   5718   6934   -271  -1140    181       C  
ATOM   1108  CZ  PHE A 151      41.093  15.153  10.419  1.00 47.99           C  
ANISOU 1108  CZ  PHE A 151     6451   5319   6462   -135  -1009    240       C  
ATOM   1109  N   TYR A 152      36.233  16.494  13.196  1.00 56.19           N  
ANISOU 1109  N   TYR A 152     6833   6503   8013   -344   -915    802       N  
ATOM   1110  CA  TYR A 152      36.771  16.977  14.460  1.00 53.24           C  
ANISOU 1110  CA  TYR A 152     6477   6125   7625   -218   -751    852       C  
ATOM   1111  C   TYR A 152      36.246  16.154  15.630  1.00 55.60           C  
ANISOU 1111  C   TYR A 152     6743   6347   8035   -265   -666    945       C  
ATOM   1112  O   TYR A 152      36.987  15.878  16.582  1.00 55.23           O  
ANISOU 1112  O   TYR A 152     6789   6245   7949   -189   -565    946       O  
ATOM   1113  CB  TYR A 152      36.444  18.461  14.644  1.00 55.93           C  
ANISOU 1113  CB  TYR A 152     6704   6587   7959   -123   -687    926       C  
ATOM   1114  CG  TYR A 152      37.203  19.075  15.796  1.00 55.05           C  
ANISOU 1114  CG  TYR A 152     6645   6474   7796     11   -537    933       C  
ATOM   1115  CD1 TYR A 152      38.573  19.357  15.691  1.00 43.29           C  
ANISOU 1115  CD1 TYR A 152     5290   4973   6186     96   -521    832       C  
ATOM   1116  CD2 TYR A 152      36.560  19.375  16.988  1.00 53.36           C  
ANISOU 1116  CD2 TYR A 152     6346   6282   7648     50   -411   1037       C  
ATOM   1117  CE1 TYR A 152      39.280  19.915  16.765  1.00 44.54           C  
ANISOU 1117  CE1 TYR A 152     5492   5137   6294    204   -404    828       C  
ATOM   1118  CE2 TYR A 152      37.256  19.930  18.052  1.00 50.35           C  
ANISOU 1118  CE2 TYR A 152     6027   5907   7198    168   -285   1025       C  
ATOM   1119  CZ  TYR A 152      38.602  20.196  17.938  1.00 46.91           C  
ANISOU 1119  CZ  TYR A 152     5721   5456   6646    237   -293    918       C  
ATOM   1120  OH  TYR A 152      39.253  20.746  19.012  1.00 53.54           O  
ANISOU 1120  OH  TYR A 152     6614   6310   7418    339   -187    902       O  
ATOM   1121  N   GLY A 153      34.970  15.751  15.570  1.00 56.58           N  
ANISOU 1121  N   GLY A 153     6728   6474   8295   -393   -710   1035       N  
ATOM   1122  CA  GLY A 153      34.382  14.969  16.654  1.00 47.55           C  
ANISOU 1122  CA  GLY A 153     5536   5262   7270   -450   -618   1148       C  
ATOM   1123  C   GLY A 153      34.972  13.578  16.783  1.00 53.14           C  
ANISOU 1123  C   GLY A 153     6399   5800   7991   -512   -639   1093       C  
ATOM   1124  O   GLY A 153      35.154  13.076  17.892  1.00 60.57           O  
ANISOU 1124  O   GLY A 153     7381   6675   8956   -480   -523   1170       O  
ATOM   1125  N   GLU A 154      35.289  12.940  15.661  1.00 51.42           N  
ANISOU 1125  N   GLU A 154     6278   5506   7751   -591   -783    961       N  
ATOM   1126  CA  GLU A 154      35.771  11.564  15.691  1.00 61.17           C  
ANISOU 1126  CA  GLU A 154     7665   6553   9022   -653   -808    900       C  
ATOM   1127  C   GLU A 154      37.291  11.513  15.740  1.00 61.15           C  
ANISOU 1127  C   GLU A 154     7849   6507   8878   -502   -766    792       C  
ATOM   1128  O   GLU A 154      37.865  10.994  16.699  1.00 64.85           O  
ANISOU 1128  O   GLU A 154     8398   6892   9350   -433   -667    840       O  
ATOM   1129  CB  GLU A 154      35.262  10.801  14.460  1.00 69.89           C  
ANISOU 1129  CB  GLU A 154     8786   7584  10185   -826   -986    796       C  
ATOM   1130  CG  GLU A 154      33.747  10.684  14.402  1.00 87.59           C  
ANISOU 1130  CG  GLU A 154    10827   9860  12592  -1002  -1049    907       C  
ATOM   1131  CD  GLU A 154      33.253  10.226  13.044  1.00104.48           C  
ANISOU 1131  CD  GLU A 154    12967  11979  14750  -1168  -1257    784       C  
ATOM   1132  OE1 GLU A 154      34.101   9.889  12.183  1.00110.49           O  
ANISOU 1132  OE1 GLU A 154    13910  12679  15392  -1143  -1338    607       O  
ATOM   1133  OE2 GLU A 154      32.020  10.238  12.827  1.00108.85           O  
ANISOU 1133  OE2 GLU A 154    13335  12593  15430  -1317  -1341    864       O  
ATOM   1134  N   LYS A 155      37.951  12.090  14.735  1.00 62.67           N  
ANISOU 1134  N   LYS A 155     8099   6770   8943   -443   -836    663       N  
ATOM   1135  CA  LYS A 155      39.394  11.958  14.572  1.00 56.77           C  
ANISOU 1135  CA  LYS A 155     7514   5984   8072   -315   -810    550       C  
ATOM   1136  C   LYS A 155      40.209  12.935  15.416  1.00 54.05           C  
ANISOU 1136  C   LYS A 155     7159   5741   7635   -151   -692    595       C  
ATOM   1137  O   LYS A 155      41.441  12.864  15.379  1.00 58.31           O  
ANISOU 1137  O   LYS A 155     7809   6263   8083    -42   -666    517       O  
ATOM   1138  CB  LYS A 155      39.732  12.086  13.086  1.00 56.13           C  
ANISOU 1138  CB  LYS A 155     7497   5937   7891   -332   -928    396       C  
ATOM   1139  CG  LYS A 155      39.084  10.948  12.277  1.00 64.53           C  
ANISOU 1139  CG  LYS A 155     8612   6876   9029   -496  -1057    315       C  
ATOM   1140  CD  LYS A 155      38.956  11.221  10.799  1.00 73.26           C  
ANISOU 1140  CD  LYS A 155     9739   8064  10034   -548  -1195    189       C  
ATOM   1141  CE  LYS A 155      37.784  10.402  10.217  1.00 82.08           C  
ANISOU 1141  CE  LYS A 155    10821   9107  11257   -756  -1342    158       C  
ATOM   1142  NZ  LYS A 155      37.482  10.685   8.771  1.00 77.37           N  
ANISOU 1142  NZ  LYS A 155    10231   8618  10547   -824  -1503     45       N  
ATOM   1143  N   ARG A 156      39.575  13.845  16.163  1.00 51.18           N  
ANISOU 1143  N   ARG A 156     6666   5483   7296   -130   -620    709       N  
ATOM   1144  CA  ARG A 156      40.320  14.698  17.086  1.00 50.95           C  
ANISOU 1144  CA  ARG A 156     6643   5533   7183     12   -511    739       C  
ATOM   1145  C   ARG A 156      39.869  14.468  18.528  1.00 50.33           C  
ANISOU 1145  C   ARG A 156     6525   5442   7158     28   -398    873       C  
ATOM   1146  O   ARG A 156      40.537  13.749  19.273  1.00 53.91           O  
ANISOU 1146  O   ARG A 156     7072   5824   7590     79   -350    892       O  
ATOM   1147  CB  ARG A 156      40.190  16.173  16.691  1.00 49.77           C  
ANISOU 1147  CB  ARG A 156     6406   5524   6981     59   -510    731       C  
ATOM   1148  CG  ARG A 156      40.906  16.528  15.392  1.00 48.47           C  
ANISOU 1148  CG  ARG A 156     6297   5392   6727     76   -594    613       C  
ATOM   1149  CD  ARG A 156      42.418  16.484  15.547  1.00 49.48           C  
ANISOU 1149  CD  ARG A 156     6540   5506   6755    185   -557    532       C  
ATOM   1150  NE  ARG A 156      43.157  16.782  14.313  1.00 49.99           N  
ANISOU 1150  NE  ARG A 156     6655   5609   6729    207   -616    429       N  
ATOM   1151  CZ  ARG A 156      43.486  15.863  13.406  1.00 49.58           C  
ANISOU 1151  CZ  ARG A 156     6697   5492   6649    176   -684    335       C  
ATOM   1152  NH1 ARG A 156      43.138  14.595  13.603  1.00 44.12           N  
ANISOU 1152  NH1 ARG A 156     6060   4673   6030    113   -709    328       N  
ATOM   1153  NH2 ARG A 156      44.179  16.197  12.317  1.00 43.78           N  
ANISOU 1153  NH2 ARG A 156     6008   4812   5814    209   -717    248       N  
ATOM   1154  N   LEU A 157      38.721  15.025  18.919  1.00 51.22           N  
ANISOU 1154  N   LEU A 157     6497   5625   7338    -11   -351    977       N  
ATOM   1155  CA  LEU A 157      38.216  14.837  20.281  1.00 54.93           C  
ANISOU 1155  CA  LEU A 157     6924   6101   7845      7   -225   1113       C  
ATOM   1156  C   LEU A 157      37.991  13.360  20.618  1.00 61.04           C  
ANISOU 1156  C   LEU A 157     7747   6732   8712    -81   -224   1181       C  
ATOM   1157  O   LEU A 157      38.415  12.884  21.678  1.00 64.78           O  
ANISOU 1157  O   LEU A 157     8291   7171   9151    -19   -136   1251       O  
ATOM   1158  CB  LEU A 157      36.902  15.592  20.456  1.00 46.21           C  
ANISOU 1158  CB  LEU A 157     5644   5093   6821    -27   -174   1213       C  
ATOM   1159  CG  LEU A 157      36.962  17.089  20.254  1.00 48.99           C  
ANISOU 1159  CG  LEU A 157     5940   5566   7109     67   -153   1172       C  
ATOM   1160  CD1 LEU A 157      35.551  17.644  20.511  1.00 44.93           C  
ANISOU 1160  CD1 LEU A 157     5240   5130   6701     41    -89   1293       C  
ATOM   1161  CD2 LEU A 157      38.001  17.693  21.217  1.00 42.62           C  
ANISOU 1161  CD2 LEU A 157     5232   4796   6164    210    -59   1131       C  
ATOM   1162  N   GLY A 158      37.301  12.625  19.739  1.00 57.61           N  
ANISOU 1162  N   GLY A 158     7280   6212   8397   -230   -325   1168       N  
ATOM   1163  CA  GLY A 158      36.924  11.250  20.061  1.00 55.92           C  
ANISOU 1163  CA  GLY A 158     7100   5840   8306   -339   -321   1244       C  
ATOM   1164  C   GLY A 158      38.120  10.330  20.223  1.00 57.52           C  
ANISOU 1164  C   GLY A 158     7492   5905   8460   -272   -324   1187       C  
ATOM   1165  O   GLY A 158      38.152   9.480  21.118  1.00 59.88           O  
ANISOU 1165  O   GLY A 158     7841   6105   8808   -271   -249   1298       O  
ATOM   1166  N   TYR A 159      39.111  10.471  19.346  1.00 58.19           N  
ANISOU 1166  N   TYR A 159     7678   5981   8451   -210   -405   1025       N  
ATOM   1167  CA  TYR A 159      40.343   9.706  19.486  1.00 56.10           C  
ANISOU 1167  CA  TYR A 159     7577   5603   8134   -115   -399    969       C  
ATOM   1168  C   TYR A 159      41.032   9.995  20.816  1.00 54.48           C  
ANISOU 1168  C   TYR A 159     7397   5467   7835     34   -283   1064       C  
ATOM   1169  O   TYR A 159      41.511   9.072  21.495  1.00 55.92           O  
ANISOU 1169  O   TYR A 159     7672   5540   8035     80   -241   1132       O  
ATOM   1170  CB  TYR A 159      41.262  10.021  18.320  1.00 57.18           C  
ANISOU 1170  CB  TYR A 159     7790   5764   8174    -58   -485    787       C  
ATOM   1171  CG  TYR A 159      42.564   9.291  18.357  1.00 60.73           C  
ANISOU 1171  CG  TYR A 159     8389   6111   8575     56   -476    722       C  
ATOM   1172  CD1 TYR A 159      42.676   8.005  17.842  1.00 62.50           C  
ANISOU 1172  CD1 TYR A 159     8731   6133   8884      4   -524    662       C  
ATOM   1173  CD2 TYR A 159      43.693   9.892  18.877  1.00 54.12           C  
ANISOU 1173  CD2 TYR A 159     7574   5376   7615    217   -422    715       C  
ATOM   1174  CE1 TYR A 159      43.875   7.341  17.850  1.00 63.70           C  
ANISOU 1174  CE1 TYR A 159     9015   6187   9001    130   -506    605       C  
ATOM   1175  CE2 TYR A 159      44.899   9.231  18.897  1.00 58.55           C  
ANISOU 1175  CE2 TYR A 159     8250   5858   8140    332   -416    666       C  
ATOM   1176  CZ  TYR A 159      44.988   7.962  18.374  1.00 65.50           C  
ANISOU 1176  CZ  TYR A 159     9243   6538   9108    299   -452    615       C  
ATOM   1177  OH  TYR A 159      46.196   7.307  18.387  1.00 72.82           O  
ANISOU 1177  OH  TYR A 159    10279   7382  10009    435   -435    571       O  
ATOM   1178  N   GLN A 160      41.098  11.270  21.202  1.00 52.41           N  
ANISOU 1178  N   GLN A 160     7059   5383   7471    111   -236   1069       N  
ATOM   1179  CA  GLN A 160      41.747  11.631  22.461  1.00 51.01           C  
ANISOU 1179  CA  GLN A 160     6908   5290   7182    245   -142   1137       C  
ATOM   1180  C   GLN A 160      40.982  11.079  23.668  1.00 56.89           C  
ANISOU 1180  C   GLN A 160     7626   6011   7978    218    -37   1322       C  
ATOM   1181  O   GLN A 160      41.594  10.682  24.669  1.00 50.53           O  
ANISOU 1181  O   GLN A 160     6894   5202   7102    311     22   1400       O  
ATOM   1182  CB  GLN A 160      41.897  13.148  22.554  1.00 44.62           C  
ANISOU 1182  CB  GLN A 160     6031   4657   6266    315   -119   1083       C  
ATOM   1183  CG  GLN A 160      42.943  13.737  21.630  1.00 43.32           C  
ANISOU 1183  CG  GLN A 160     5905   4531   6025    372   -195    929       C  
ATOM   1184  CD  GLN A 160      44.340  13.519  22.156  1.00 54.43           C  
ANISOU 1184  CD  GLN A 160     7406   5945   7332    496   -189    899       C  
ATOM   1185  OE1 GLN A 160      44.527  13.313  23.357  1.00 51.51           O  
ANISOU 1185  OE1 GLN A 160     7060   5600   6911    559   -126    991       O  
ATOM   1186  NE2 GLN A 160      45.332  13.541  21.264  1.00 48.49           N  
ANISOU 1186  NE2 GLN A 160     6698   5181   6543    536   -254    780       N  
ATOM   1187  N   LEU A 161      39.644  11.069  23.599  1.00 61.83           N  
ANISOU 1187  N   LEU A 161     8137   6635   8721     94    -11   1404       N  
ATOM   1188  CA  LEU A 161      38.827  10.543  24.693  1.00 59.53           C  
ANISOU 1188  CA  LEU A 161     7802   6327   8490     56    104   1596       C  
ATOM   1189  C   LEU A 161      39.027   9.040  24.875  1.00 63.48           C  
ANISOU 1189  C   LEU A 161     8404   6630   9084      8     98   1676       C  
ATOM   1190  O   LEU A 161      39.122   8.555  26.009  1.00 65.83           O  
ANISOU 1190  O   LEU A 161     8746   6917   9351     62    198   1827       O  
ATOM   1191  CB  LEU A 161      37.348  10.849  24.442  1.00 53.57           C  
ANISOU 1191  CB  LEU A 161     6875   5615   7866    -75    127   1666       C  
ATOM   1192  CG  LEU A 161      36.933  12.316  24.557  1.00 53.79           C  
ANISOU 1192  CG  LEU A 161     6786   5831   7821    -10    178   1641       C  
ATOM   1193  CD1 LEU A 161      35.486  12.471  24.173  1.00 57.43           C  
ANISOU 1193  CD1 LEU A 161     7063   6321   8436   -139    183   1718       C  
ATOM   1194  CD2 LEU A 161      37.158  12.829  25.970  1.00 54.05           C  
ANISOU 1194  CD2 LEU A 161     6843   5981   7714    126    327   1724       C  
ATOM   1195  N   LYS A 162      39.037   8.282  23.774  1.00 61.68           N  
ANISOU 1195  N   LYS A 162     8222   6241   8973    -94    -16   1581       N  
ATOM   1196  CA  LYS A 162      39.267   6.843  23.863  1.00 62.73           C  
ANISOU 1196  CA  LYS A 162     8470   6150   9213   -137    -25   1638       C  
ATOM   1197  C   LYS A 162      40.628   6.554  24.478  1.00 65.26           C  
ANISOU 1197  C   LYS A 162     8932   6453   9411     43      2   1643       C  
ATOM   1198  O   LYS A 162      40.755   5.736  25.397  1.00 64.32           O  
ANISOU 1198  O   LYS A 162     8877   6246   9316     79     76   1800       O  
ATOM   1199  CB  LYS A 162      39.175   6.227  22.464  1.00 65.37           C  
ANISOU 1199  CB  LYS A 162     8850   6324   9664   -261   -164   1483       C  
ATOM   1200  CG  LYS A 162      39.627   4.790  22.370  1.00 74.45           C  
ANISOU 1200  CG  LYS A 162    10154   7214  10920   -281   -186   1488       C  
ATOM   1201  CD  LYS A 162      39.065   4.096  21.150  1.00 84.11           C  
ANISOU 1201  CD  LYS A 162    11400   8265  12294   -462   -309   1363       C  
ATOM   1202  CE  LYS A 162      39.323   2.598  21.226  1.00 93.71           C  
ANISOU 1202  CE  LYS A 162    12768   9185  13652   -499   -308   1394       C  
ATOM   1203  NZ  LYS A 162      38.603   1.863  20.155  1.00100.25           N  
ANISOU 1203  NZ  LYS A 162    13617   9828  14645   -709   -427   1278       N  
ATOM   1204  N   LEU A 163      41.647   7.273  24.020  1.00 68.50           N  
ANISOU 1204  N   LEU A 163     9379   6962   9687    162    -54   1488       N  
ATOM   1205  CA  LEU A 163      42.994   7.102  24.539  1.00 63.17           C  
ANISOU 1205  CA  LEU A 163     8809   6299   8894    336    -43   1484       C  
ATOM   1206  C   LEU A 163      42.986   7.406  26.027  1.00 63.92           C  
ANISOU 1206  C   LEU A 163     8883   6524   8878    424     64   1652       C  
ATOM   1207  O   LEU A 163      43.619   6.688  26.806  1.00 71.99           O  
ANISOU 1207  O   LEU A 163     9992   7494   9868    521     97   1761       O  
ATOM   1208  CB  LEU A 163      43.953   7.918  23.681  1.00 62.08           C  
ANISOU 1208  CB  LEU A 163     8679   6258   8650    417   -121   1290       C  
ATOM   1209  CG  LEU A 163      45.429   8.044  23.954  1.00 69.09           C  
ANISOU 1209  CG  LEU A 163     9634   7206   9413    593   -133   1243       C  
ATOM   1210  CD1 LEU A 163      46.071   6.671  24.065  1.00 71.34           C  
ANISOU 1210  CD1 LEU A 163    10039   7299   9768    657   -136   1294       C  
ATOM   1211  CD2 LEU A 163      46.002   8.820  22.786  1.00 64.68           C  
ANISOU 1211  CD2 LEU A 163     9054   6719   8803    608   -206   1051       C  
ATOM   1212  N   ALA A 164      42.278   8.460  26.449  1.00 62.47           N  
ANISOU 1212  N   ALA A 164     8591   6515   8630    403    122   1677       N  
ATOM   1213  CA  ALA A 164      42.255   8.792  27.873  1.00 61.13           C  
ANISOU 1213  CA  ALA A 164     8415   6484   8329    493    231   1819       C  
ATOM   1214  C   ALA A 164      41.537   7.718  28.685  1.00 70.69           C  
ANISOU 1214  C   ALA A 164     9641   7589   9628    438    327   2042       C  
ATOM   1215  O   ALA A 164      41.899   7.457  29.837  1.00 70.82           O  
ANISOU 1215  O   ALA A 164     9716   7660   9534    539    399   2182       O  
ATOM   1216  CB  ALA A 164      41.591  10.146  28.096  1.00 59.94           C  
ANISOU 1216  CB  ALA A 164     8152   6522   8100    486    286   1784       C  
ATOM   1217  N   ARG A 165      40.496   7.111  28.115  1.00 75.36           N  
ANISOU 1217  N   ARG A 165    10177   8039  10417    272    326   2086       N  
ATOM   1218  CA  ARG A 165      39.800   6.041  28.815  1.00 72.32           C  
ANISOU 1218  CA  ARG A 165     9800   7530  10148    197    419   2307       C  
ATOM   1219  C   ARG A 165      40.713   4.841  29.013  1.00 72.97           C  
ANISOU 1219  C   ARG A 165    10038   7430  10259    267    393   2370       C  
ATOM   1220  O   ARG A 165      40.701   4.209  30.072  1.00 74.24           O  
ANISOU 1220  O   ARG A 165    10246   7564  10397    313    488   2579       O  
ATOM   1221  CB  ARG A 165      38.550   5.641  28.041  1.00 72.26           C  
ANISOU 1221  CB  ARG A 165     9689   7398  10367    -17    399   2320       C  
ATOM   1222  CG  ARG A 165      37.498   4.927  28.873  1.00 78.98           C  
ANISOU 1222  CG  ARG A 165    10479   8189  11339   -121    528   2570       C  
ATOM   1223  CD  ARG A 165      36.509   4.249  27.952  1.00 81.27           C  
ANISOU 1223  CD  ARG A 165    10692   8299  11887   -349    464   2561       C  
ATOM   1224  NE  ARG A 165      37.243   3.565  26.894  1.00 85.34           N  
ANISOU 1224  NE  ARG A 165    11338   8610  12476   -373    315   2389       N  
ATOM   1225  CZ  ARG A 165      36.675   2.921  25.884  1.00 86.29           C  
ANISOU 1225  CZ  ARG A 165    11443   8549  12796   -560    214   2310       C  
ATOM   1226  NH1 ARG A 165      35.351   2.865  25.796  1.00 91.72           N  
ANISOU 1226  NH1 ARG A 165    11969   9237  13644   -751    234   2402       N  
ATOM   1227  NH2 ARG A 165      37.436   2.337  24.965  1.00 81.02           N  
ANISOU 1227  NH2 ARG A 165    10917   7705  12163   -553     92   2136       N  
ATOM   1228  N   ASP A 166      41.554   4.550  28.024  1.00 75.62           N  
ANISOU 1228  N   ASP A 166    10453   7647  10630    294    272   2198       N  
ATOM   1229  CA  ASP A 166      42.396   3.360  28.067  1.00 77.15           C  
ANISOU 1229  CA  ASP A 166    10793   7638  10884    367    247   2244       C  
ATOM   1230  C   ASP A 166      43.598   3.532  28.994  1.00 76.35           C  
ANISOU 1230  C   ASP A 166    10760   7663  10586    583    266   2304       C  
ATOM   1231  O   ASP A 166      43.998   2.584  29.671  1.00 83.89           O  
ANISOU 1231  O   ASP A 166    11807   8505  11562    660    304   2468       O  
ATOM   1232  CB  ASP A 166      42.863   3.010  26.654  1.00 76.34           C  
ANISOU 1232  CB  ASP A 166    10751   7373  10880    333    124   2025       C  
ATOM   1233  CG  ASP A 166      41.714   2.644  25.724  1.00 82.68           C  
ANISOU 1233  CG  ASP A 166    11506   8029  11880    109     81   1967       C  
ATOM   1234  OD1 ASP A 166      40.571   2.439  26.196  1.00 82.67           O  
ANISOU 1234  OD1 ASP A 166    11423   8006  11982    -28    150   2122       O  
ATOM   1235  OD2 ASP A 166      41.963   2.563  24.504  1.00 87.63           O  
ANISOU 1235  OD2 ASP A 166    12173   8569  12554     69    -24   1764       O  
ATOM   1236  N   GLN A 167      44.190   4.718  29.037  1.00 74.10           N  
ANISOU 1236  N   GLN A 167    10429   7608  10117    680    233   2179       N  
ATOM   1237  CA  GLN A 167      45.379   4.934  29.854  1.00 66.53           C  
ANISOU 1237  CA  GLN A 167     9521   6786   8971    872    223   2214       C  
ATOM   1238  C   GLN A 167      45.053   5.077  31.333  1.00 67.59           C  
ANISOU 1238  C   GLN A 167     9650   7069   8964    925    329   2421       C  
ATOM   1239  O   GLN A 167      45.854   4.676  32.180  1.00 72.75           O  
ANISOU 1239  O   GLN A 167    10374   7761   9506   1067    332   2541       O  
ATOM   1240  CB  GLN A 167      46.090   6.207  29.415  1.00 69.36           C  
ANISOU 1240  CB  GLN A 167     9826   7338   9190    935    150   2007       C  
ATOM   1241  CG  GLN A 167      46.640   6.181  28.032  1.00 85.94           C  
ANISOU 1241  CG  GLN A 167    11937   9340  11375    920     53   1805       C  
ATOM   1242  CD  GLN A 167      47.629   7.294  27.814  1.00 98.82           C  
ANISOU 1242  CD  GLN A 167    13527  11162  12858   1015     -9   1649       C  
ATOM   1243  OE1 GLN A 167      48.578   7.150  27.059  1.00113.06           O  
ANISOU 1243  OE1 GLN A 167    15356  12923  14678   1080    -77   1531       O  
ATOM   1244  NE2 GLN A 167      47.401   8.426  28.467  1.00 94.14           N  
ANISOU 1244  NE2 GLN A 167    12868  10775  12127   1019     20   1644       N  
ATOM   1245  N   TYR A 168      43.902   5.648  31.662  1.00 67.66           N  
ANISOU 1245  N   TYR A 168     9573   7173   8964    825    418   2470       N  
ATOM   1246  CA  TYR A 168      43.604   6.047  33.025  1.00 63.39           C  
ANISOU 1246  CA  TYR A 168     9021   6821   8243    889    528   2627       C  
ATOM   1247  C   TYR A 168      42.328   5.445  33.580  1.00 65.26           C  
ANISOU 1247  C   TYR A 168     9223   6991   8582    779    669   2848       C  
ATOM   1248  O   TYR A 168      41.960   5.771  34.718  1.00 67.79           O  
ANISOU 1248  O   TYR A 168     9532   7478   8747    829    786   2988       O  
ATOM   1249  CB  TYR A 168      43.485   7.573  33.119  1.00 58.54           C  
ANISOU 1249  CB  TYR A 168     8329   6444   7470    909    534   2473       C  
ATOM   1250  CG  TYR A 168      44.673   8.366  32.618  1.00 63.58           C  
ANISOU 1250  CG  TYR A 168     8979   7173   8004    998    406   2256       C  
ATOM   1251  CD1 TYR A 168      45.791   8.559  33.422  1.00 62.75           C  
ANISOU 1251  CD1 TYR A 168     8935   7207   7698   1149    363   2264       C  
ATOM   1252  CD2 TYR A 168      44.653   8.978  31.367  1.00 59.64           C  
ANISOU 1252  CD2 TYR A 168     8421   6640   7601    926    329   2052       C  
ATOM   1253  CE1 TYR A 168      46.869   9.308  32.981  1.00 61.39           C  
ANISOU 1253  CE1 TYR A 168     8754   7124   7446   1215    249   2073       C  
ATOM   1254  CE2 TYR A 168      45.721   9.735  30.920  1.00 53.16           C  
ANISOU 1254  CE2 TYR A 168     7601   5906   6692    999    228   1870       C  
ATOM   1255  CZ  TYR A 168      46.827   9.893  31.727  1.00 60.43           C  
ANISOU 1255  CZ  TYR A 168     8572   6954   7435   1138    190   1881       C  
ATOM   1256  OH  TYR A 168      47.889  10.644  31.287  1.00 62.88           O  
ANISOU 1256  OH  TYR A 168     8865   7352   7675   1195     90   1709       O  
ATOM   1257  N   GLY A 169      41.631   4.600  32.820  1.00 60.87           N  
ANISOU 1257  N   GLY A 169     8645   6204   8279    626    665   2881       N  
ATOM   1258  CA  GLY A 169      40.300   4.192  33.234  1.00 65.09           C  
ANISOU 1258  CA  GLY A 169     9105   6691   8935    489    797   3076       C  
ATOM   1259  C   GLY A 169      39.363   5.353  33.476  1.00 69.53           C  
ANISOU 1259  C   GLY A 169     9528   7468   9423    449    885   3047       C  
ATOM   1260  O   GLY A 169      38.478   5.257  34.333  1.00 76.69           O  
ANISOU 1260  O   GLY A 169    10377   8442  10320    415   1039   3246       O  
ATOM   1261  N   ASP A 170      39.553   6.466  32.759  1.00 67.54           N  
ANISOU 1261  N   ASP A 170     9220   7327   9116    463    803   2813       N  
ATOM   1262  CA  ASP A 170      38.751   7.677  32.951  1.00 70.77           C  
ANISOU 1262  CA  ASP A 170     9504   7933   9453    453    883   2766       C  
ATOM   1263  C   ASP A 170      37.482   7.572  32.109  1.00 72.01           C  
ANISOU 1263  C   ASP A 170     9512   7998   9851    263    890   2772       C  
ATOM   1264  O   ASP A 170      37.319   8.223  31.077  1.00 66.72           O  
ANISOU 1264  O   ASP A 170     8769   7336   9246    209    796   2593       O  
ATOM   1265  CB  ASP A 170      39.553   8.921  32.591  1.00 63.88           C  
ANISOU 1265  CB  ASP A 170     8643   7204   8424    555    792   2528       C  
ATOM   1266  CG  ASP A 170      38.891  10.204  33.076  1.00 68.22           C  
ANISOU 1266  CG  ASP A 170     9100   7961   8859    592    896   2493       C  
ATOM   1267  OD1 ASP A 170      37.662  10.202  33.349  1.00 67.72           O  
ANISOU 1267  OD1 ASP A 170     8925   7924   8883    516   1024   2621       O  
ATOM   1268  OD2 ASP A 170      39.606  11.224  33.171  1.00 66.49           O  
ANISOU 1268  OD2 ASP A 170     8917   7874   8474    697    852   2335       O  
ATOM   1269  N   SER A 171      36.546   6.753  32.587  1.00 73.46           N  
ANISOU 1269  N   SER A 171     9640   8105  10165    160   1004   2995       N  
ATOM   1270  CA  SER A 171      35.301   6.607  31.859  1.00 72.22           C  
ANISOU 1270  CA  SER A 171     9321   7872  10247    -34   1006   3019       C  
ATOM   1271  C   SER A 171      34.393   7.818  32.027  1.00 74.52           C  
ANISOU 1271  C   SER A 171     9445   8377  10494    -23   1101   3002       C  
ATOM   1272  O   SER A 171      33.517   8.035  31.185  1.00 80.04           O  
ANISOU 1272  O   SER A 171     9991   9055  11366   -157   1056   2956       O  
ATOM   1273  CB  SER A 171      34.588   5.333  32.304  1.00 77.62           C  
ANISOU 1273  CB  SER A 171     9986   8396  11110   -166   1099   3271       C  
ATOM   1274  OG  SER A 171      34.404   5.353  33.701  1.00 81.31           O  
ANISOU 1274  OG  SER A 171    10463   8999  11430    -68   1289   3487       O  
ATOM   1275  N   ALA A 172      34.593   8.627  33.069  1.00 69.05           N  
ANISOU 1275  N   ALA A 172     8777   7888   9570    139   1225   3029       N  
ATOM   1276  CA  ALA A 172      33.778   9.830  33.223  1.00 66.46           C  
ANISOU 1276  CA  ALA A 172     8304   7749   9199    173   1325   2995       C  
ATOM   1277  C   ALA A 172      34.058  10.836  32.110  1.00 71.95           C  
ANISOU 1277  C   ALA A 172     8965   8470   9905    185   1178   2743       C  
ATOM   1278  O   ALA A 172      33.123  11.327  31.464  1.00 75.95           O  
ANISOU 1278  O   ALA A 172     9303   9004  10551    103   1175   2718       O  
ATOM   1279  CB  ALA A 172      34.010  10.472  34.590  1.00 62.66           C  
ANISOU 1279  CB  ALA A 172     7890   7470   8448    353   1487   3050       C  
ATOM   1280  N   ILE A 173      35.338  11.154  31.863  1.00 70.88           N  
ANISOU 1280  N   ILE A 173     8975   8329   9625    285   1056   2568       N  
ATOM   1281  CA  ILE A 173      35.639  12.104  30.793  1.00 63.53           C  
ANISOU 1281  CA  ILE A 173     8015   7419   8704    293    925   2346       C  
ATOM   1282  C   ILE A 173      35.191  11.533  29.457  1.00 62.11           C  
ANISOU 1282  C   ILE A 173     7758   7087   8753    124    791   2306       C  
ATOM   1283  O   ILE A 173      34.691  12.268  28.600  1.00 60.68           O  
ANISOU 1283  O   ILE A 173     7464   6944   8646     79    733   2211       O  
ATOM   1284  CB  ILE A 173      37.137  12.489  30.781  1.00 61.45           C  
ANISOU 1284  CB  ILE A 173     7911   7178   8257    420    824   2180       C  
ATOM   1285  CG1 ILE A 173      37.332  13.860  30.138  1.00 58.57           C  
ANISOU 1285  CG1 ILE A 173     7507   6902   7845    469    765   1986       C  
ATOM   1286  CG2 ILE A 173      37.965  11.514  29.973  1.00 62.11           C  
ANISOU 1286  CG2 ILE A 173     8091   7089   8419    369    673   2123       C  
ATOM   1287  CD1 ILE A 173      38.663  14.510  30.465  1.00 49.83           C  
ANISOU 1287  CD1 ILE A 173     6529   5869   6537    603    712   1844       C  
ATOM   1288  N   TYR A 174      35.274  10.212  29.291  1.00 61.45           N  
ANISOU 1288  N   TYR A 174     7732   6829   8788     24    745   2387       N  
ATOM   1289  CA  TYR A 174      34.852   9.595  28.038  1.00 66.91           C  
ANISOU 1289  CA  TYR A 174     8369   7365   9688   -148    608   2332       C  
ATOM   1290  C   TYR A 174      33.352   9.739  27.811  1.00 71.92           C  
ANISOU 1290  C   TYR A 174     8789   8040  10499   -290    654   2432       C  
ATOM   1291  O   TYR A 174      32.911   9.943  26.672  1.00 68.32           O  
ANISOU 1291  O   TYR A 174     8240   7561  10159   -395    528   2331       O  
ATOM   1292  CB  TYR A 174      35.250   8.124  28.026  1.00 62.54           C  
ANISOU 1292  CB  TYR A 174     7939   6594   9230   -220    565   2400       C  
ATOM   1293  CG  TYR A 174      34.852   7.373  26.772  1.00 70.07           C  
ANISOU 1293  CG  TYR A 174     8867   7364  10393   -406    419   2324       C  
ATOM   1294  CD1 TYR A 174      33.592   6.783  26.656  1.00 69.62           C  
ANISOU 1294  CD1 TYR A 174     8669   7234  10551   -599    441   2455       C  
ATOM   1295  CD2 TYR A 174      35.747   7.227  25.712  1.00 73.65           C  
ANISOU 1295  CD2 TYR A 174     9436   7720  10826   -393    260   2121       C  
ATOM   1296  CE1 TYR A 174      33.232   6.091  25.517  1.00 71.12           C  
ANISOU 1296  CE1 TYR A 174     8843   7256  10923   -782    291   2368       C  
ATOM   1297  CE2 TYR A 174      35.397   6.533  24.570  1.00 75.61           C  
ANISOU 1297  CE2 TYR A 174     9682   7805  11241   -560    124   2033       C  
ATOM   1298  CZ  TYR A 174      34.138   5.961  24.479  1.00 79.90           C  
ANISOU 1298  CZ  TYR A 174    10093   8273  11991   -759    131   2150       C  
ATOM   1299  OH  TYR A 174      33.783   5.260  23.346  1.00 84.16           O  
ANISOU 1299  OH  TYR A 174    10637   8649  12690   -940    -21   2046       O  
ATOM   1300  N   GLN A 175      32.550   9.609  28.871  1.00 71.38           N  
ANISOU 1300  N   GLN A 175     8630   8040  10452   -293    833   2638       N  
ATOM   1301  CA  GLN A 175      31.102   9.667  28.691  1.00 72.61           C  
ANISOU 1301  CA  GLN A 175     8554   8237  10796   -431    887   2756       C  
ATOM   1302  C   GLN A 175      30.632  11.101  28.502  1.00 70.60           C  
ANISOU 1302  C   GLN A 175     8161   8176  10488   -344    919   2681       C  
ATOM   1303  O   GLN A 175      29.850  11.384  27.591  1.00 68.53           O  
ANISOU 1303  O   GLN A 175     7735   7929  10374   -449    832   2648       O  
ATOM   1304  CB  GLN A 175      30.373   9.020  29.870  1.00 73.67           C  
ANISOU 1304  CB  GLN A 175     8624   8384  10984   -467   1087   3020       C  
ATOM   1305  CG  GLN A 175      30.539   7.519  29.974  1.00 83.82           C  
ANISOU 1305  CG  GLN A 175    10005   9448  12395   -594   1061   3138       C  
ATOM   1306  CD  GLN A 175      29.825   6.955  31.192  1.00 98.16           C  
ANISOU 1306  CD  GLN A 175    11755  11291  14251   -621   1279   3424       C  
ATOM   1307  OE1 GLN A 175      28.783   7.470  31.609  1.00102.53           O  
ANISOU 1307  OE1 GLN A 175    12113  11997  14847   -633   1424   3546       O  
ATOM   1308  NE2 GLN A 175      30.397   5.912  31.786  1.00101.16           N  
ANISOU 1308  NE2 GLN A 175    12295  11528  14612   -615   1315   3544       N  
ATOM   1309  N   LYS A 176      31.068  12.009  29.380  1.00 67.78           N  
ANISOU 1309  N   LYS A 176     7868   7964   9921   -151   1044   2658       N  
ATOM   1310  CA  LYS A 176      30.757  13.421  29.191  1.00 69.44           C  
ANISOU 1310  CA  LYS A 176     7980   8328  10077    -48   1073   2564       C  
ATOM   1311  C   LYS A 176      31.308  13.923  27.859  1.00 65.36           C  
ANISOU 1311  C   LYS A 176     7495   7767   9571    -64    867   2355       C  
ATOM   1312  O   LYS A 176      30.691  14.764  27.193  1.00 58.73           O  
ANISOU 1312  O   LYS A 176     6514   6999   8803    -68    831   2311       O  
ATOM   1313  CB  LYS A 176      31.328  14.252  30.337  1.00 75.39           C  
ANISOU 1313  CB  LYS A 176     8845   9214  10586    158   1220   2535       C  
ATOM   1314  CG  LYS A 176      30.635  14.093  31.665  1.00 78.55           C  
ANISOU 1314  CG  LYS A 176     9192   9715  10938    209   1456   2733       C  
ATOM   1315  CD  LYS A 176      30.955  15.298  32.521  1.00 79.77           C  
ANISOU 1315  CD  LYS A 176     9418  10027  10864    412   1584   2650       C  
ATOM   1316  CE  LYS A 176      30.611  15.086  33.967  1.00 85.52           C  
ANISOU 1316  CE  LYS A 176    10168  10866  11461    496   1815   2819       C  
ATOM   1317  NZ  LYS A 176      31.311  16.111  34.797  1.00 88.16           N  
ANISOU 1317  NZ  LYS A 176    10650  11327  11520    692   1889   2685       N  
ATOM   1318  N   GLY A 177      32.488  13.437  27.471  1.00 61.07           N  
ANISOU 1318  N   GLY A 177     7137   7114   8952    -60    737   2235       N  
ATOM   1319  CA  GLY A 177      33.058  13.835  26.200  1.00 59.26           C  
ANISOU 1319  CA  GLY A 177     6947   6846   8722    -75    554   2047       C  
ATOM   1320  C   GLY A 177      32.177  13.459  25.025  1.00 65.29           C  
ANISOU 1320  C   GLY A 177     7571   7552   9685   -251    425   2051       C  
ATOM   1321  O   GLY A 177      31.930  14.277  24.132  1.00 64.72           O  
ANISOU 1321  O   GLY A 177     7415   7543   9635   -252    337   1964       O  
ATOM   1322  N   HIS A 178      31.690  12.216  24.999  1.00 68.84           N  
ANISOU 1322  N   HIS A 178     7994   7879  10284   -409    403   2154       N  
ATOM   1323  CA AHIS A 178      30.870  11.797  23.869  0.50 74.43           C  
ANISOU 1323  CA AHIS A 178     8574   8529  11178   -597    256   2141       C  
ATOM   1324  CA BHIS A 178      30.872  11.801  23.867  0.50 74.43           C  
ANISOU 1324  CA BHIS A 178     8574   8528  11177   -597    256   2141       C  
ATOM   1325  C   HIS A 178      29.480  12.409  23.908  1.00 77.62           C  
ANISOU 1325  C   HIS A 178     8715   9069  11709   -644    319   2265       C  
ATOM   1326  O   HIS A 178      28.821  12.470  22.867  1.00 78.15           O  
ANISOU 1326  O   HIS A 178     8650   9148  11897   -765    177   2232       O  
ATOM   1327  CB AHIS A 178      30.787  10.274  23.796  0.50 76.00           C  
ANISOU 1327  CB AHIS A 178     8832   8530  11515   -767    204   2198       C  
ATOM   1328  CB BHIS A 178      30.799  10.278  23.783  0.50 76.01           C  
ANISOU 1328  CB BHIS A 178     8834   8530  11514   -766    202   2196       C  
ATOM   1329  CG AHIS A 178      31.930   9.661  23.051  0.50 79.43           C  
ANISOU 1329  CG AHIS A 178     9480   8810  11888   -770     58   2025       C  
ATOM   1330  CG BHIS A 178      31.963   9.676  23.060  0.50 79.48           C  
ANISOU 1330  CG BHIS A 178     9491   8818  11889   -764     59   2022       C  
ATOM   1331  ND1AHIS A 178      32.061   9.760  21.682  0.50 79.74           N  
ANISOU 1331  ND1AHIS A 178     9534   8822  11940   -839   -131   1853       N  
ATOM   1332  ND1BHIS A 178      32.106   9.752  21.692  0.50 79.71           N  
ANISOU 1332  ND1BHIS A 178     9538   8816  11932   -835   -130   1850       N  
ATOM   1333  CD2AHIS A 178      33.014   8.974  23.483  0.50 80.30           C  
ANISOU 1333  CD2AHIS A 178     9796   8799  11915   -695     80   1999       C  
ATOM   1334  CD2BHIS A 178      33.058   9.024  23.517  0.50 80.36           C  
ANISOU 1334  CD2BHIS A 178     9807   8814  11912   -683     85   1997       C  
ATOM   1335  CE1AHIS A 178      33.167   9.145  21.301  0.50 78.42           C  
ANISOU 1335  CE1AHIS A 178     9575   8519  11704   -807   -206   1722       C  
ATOM   1336  CE1BHIS A 178      33.229   9.155  21.334  0.50 78.49           C  
ANISOU 1336  CE1BHIS A 178     9591   8527  11703   -797   -202   1720       C  
ATOM   1337  NE2AHIS A 178      33.765   8.661  22.375  0.50 79.11           N  
ANISOU 1337  NE2AHIS A 178     9773   8542  11741   -717    -83   1810       N  
ATOM   1338  NE2BHIS A 178      33.827   8.707  22.422  0.50 79.01           N  
ANISOU 1338  NE2BHIS A 178     9767   8537  11716   -703    -77   1809       N  
ATOM   1339  N   THR A 179      29.029  12.873  25.078  1.00 76.17           N  
ANISOU 1339  N   THR A 179     8450   8998  11491   -541    529   2406       N  
ATOM   1340  CA  THR A 179      27.799  13.655  25.137  1.00 73.33           C  
ANISOU 1340  CA  THR A 179     7838   8790  11235   -534    611   2512       C  
ATOM   1341  C   THR A 179      27.990  14.990  24.424  1.00 70.57           C  
ANISOU 1341  C   THR A 179     7465   8543  10807   -414    539   2374       C  
ATOM   1342  O   THR A 179      27.137  15.415  23.639  1.00 72.35           O  
ANISOU 1342  O   THR A 179     7498   8836  11157   -473    458   2395       O  
ATOM   1343  CB  THR A 179      27.364  13.861  26.596  1.00 68.69           C  
ANISOU 1343  CB  THR A 179     7195   8303  10603   -426    875   2681       C  
ATOM   1344  OG1 THR A 179      27.146  12.591  27.220  1.00 78.88           O  
ANISOU 1344  OG1 THR A 179     8500   9494  11976   -548    943   2837       O  
ATOM   1345  CG2 THR A 179      26.086  14.661  26.686  1.00 70.04           C  
ANISOU 1345  CG2 THR A 179     7095   8630  10888   -399    982   2796       C  
ATOM   1346  N   LEU A 180      29.115  15.662  24.690  1.00 65.54           N  
ANISOU 1346  N   LEU A 180     7018   7917   9969   -247    565   2243       N  
ATOM   1347  CA  LEU A 180      29.430  16.916  24.012  1.00 61.70           C  
ANISOU 1347  CA  LEU A 180     6536   7500   9409   -137    499   2112       C  
ATOM   1348  C   LEU A 180      29.533  16.718  22.504  1.00 62.81           C  
ANISOU 1348  C   LEU A 180     6669   7587   9610   -256    263   2009       C  
ATOM   1349  O   LEU A 180      28.958  17.486  21.729  1.00 70.08           O  
ANISOU 1349  O   LEU A 180     7451   8586  10590   -251    193   2004       O  
ATOM   1350  CB  LEU A 180      30.724  17.503  24.577  1.00 59.30           C  
ANISOU 1350  CB  LEU A 180     6448   7194   8889     29    553   1985       C  
ATOM   1351  CG  LEU A 180      31.231  18.769  23.890  1.00 60.36           C  
ANISOU 1351  CG  LEU A 180     6617   7371   8947    135    485   1844       C  
ATOM   1352  CD1 LEU A 180      30.138  19.820  23.874  1.00 62.86           C  
ANISOU 1352  CD1 LEU A 180     6735   7796   9353    202    569   1920       C  
ATOM   1353  CD2 LEU A 180      32.433  19.305  24.624  1.00 60.91           C  
ANISOU 1353  CD2 LEU A 180     6880   7443   8822    280    553   1735       C  
ATOM   1354  N   ILE A 181      30.279  15.697  22.070  1.00 64.12           N  
ANISOU 1354  N   ILE A 181     6989   7621   9753   -353    142   1926       N  
ATOM   1355  CA  ILE A 181      30.457  15.428  20.644  1.00 61.67           C  
ANISOU 1355  CA  ILE A 181     6704   7259   9470   -462    -77   1809       C  
ATOM   1356  C   ILE A 181      29.118  15.227  19.951  1.00 70.40           C  
ANISOU 1356  C   ILE A 181     7580   8407  10760   -621   -174   1897       C  
ATOM   1357  O   ILE A 181      28.917  15.676  18.815  1.00 75.65           O  
ANISOU 1357  O   ILE A 181     8186   9125  11433   -654   -328   1831       O  
ATOM   1358  CB  ILE A 181      31.360  14.203  20.453  1.00 59.95           C  
ANISOU 1358  CB  ILE A 181     6685   6875   9217   -538   -159   1720       C  
ATOM   1359  CG1 ILE A 181      32.783  14.510  20.917  1.00 57.90           C  
ANISOU 1359  CG1 ILE A 181     6634   6596   8770   -374   -102   1618       C  
ATOM   1360  CG2 ILE A 181      31.294  13.701  19.012  1.00 56.11           C  
ANISOU 1360  CG2 ILE A 181     6211   6327   8781   -683   -377   1609       C  
ATOM   1361  CD1 ILE A 181      33.707  13.317  20.834  1.00 57.47           C  
ANISOU 1361  CD1 ILE A 181     6768   6381   8686   -416   -160   1548       C  
ATOM   1362  N   GLN A 182      28.177  14.553  20.619  1.00 64.48           N  
ANISOU 1362  N   GLN A 182     6691   7647  10163   -724    -88   2057       N  
ATOM   1363  CA  GLN A 182      26.894  14.278  19.987  1.00 70.50           C  
ANISOU 1363  CA  GLN A 182     7214   8452  11120   -897   -191   2148       C  
ATOM   1364  C   GLN A 182      26.004  15.513  19.937  1.00 69.29           C  
ANISOU 1364  C   GLN A 182     6831   8483  11015   -800   -138   2238       C  
ATOM   1365  O   GLN A 182      25.160  15.607  19.046  1.00 69.02           O  
ANISOU 1365  O   GLN A 182     6611   8517  11098   -907   -284   2268       O  
ATOM   1366  CB  GLN A 182      26.191  13.124  20.696  1.00 76.02           C  
ANISOU 1366  CB  GLN A 182     7827   9070  11986  -1055   -115   2302       C  
ATOM   1367  CG  GLN A 182      26.823  11.775  20.382  1.00 82.32           C  
ANISOU 1367  CG  GLN A 182     8817   9659  12800  -1201   -228   2213       C  
ATOM   1368  CD  GLN A 182      26.361  10.696  21.333  1.00 94.74           C  
ANISOU 1368  CD  GLN A 182    10355  11128  14515  -1317   -103   2381       C  
ATOM   1369  OE1 GLN A 182      25.210  10.702  21.771  1.00101.22           O  
ANISOU 1369  OE1 GLN A 182    10936  12030  15494  -1392    -14   2562       O  
ATOM   1370  NE2 GLN A 182      27.262   9.770  21.678  1.00 96.26           N  
ANISOU 1370  NE2 GLN A 182    10779  11141  14656  -1323    -86   2336       N  
ATOM   1371  N   ASN A 183      26.191  16.468  20.857  1.00 71.09           N  
ANISOU 1371  N   ASN A 183     7071   8789  11151   -595     61   2276       N  
ATOM   1372  CA  ASN A 183      25.437  17.719  20.904  1.00 73.27           C  
ANISOU 1372  CA  ASN A 183     7154   9219  11468   -463    142   2353       C  
ATOM   1373  C   ASN A 183      26.230  18.919  20.373  1.00 77.81           C  
ANISOU 1373  C   ASN A 183     7849   9823  11893   -297     98   2216       C  
ATOM   1374  O   ASN A 183      25.951  20.061  20.755  1.00 80.90           O  
ANISOU 1374  O   ASN A 183     8163  10302  12272   -129    226   2256       O  
ATOM   1375  CB  ASN A 183      24.968  18.010  22.330  1.00 73.07           C  
ANISOU 1375  CB  ASN A 183     7050   9258  11456   -343    417   2492       C  
ATOM   1376  CG  ASN A 183      24.124  16.884  22.922  1.00 82.56           C  
ANISOU 1376  CG  ASN A 183     8112  10441  12816   -503    491   2662       C  
ATOM   1377  OD1 ASN A 183      23.655  15.996  22.207  1.00 83.36           O  
ANISOU 1377  OD1 ASN A 183     8121  10491  13061   -716    329   2690       O  
ATOM   1378  ND2 ASN A 183      23.894  16.946  24.234  1.00 83.38           N  
ANISOU 1378  ND2 ASN A 183     8196  10590  12894   -403    742   2780       N  
ATOM   1379  N   MET A 184      27.196  18.686  19.479  1.00 75.47           N  
ANISOU 1379  N   MET A 184     7736   9448  11489   -341    -75   2058       N  
ATOM   1380  CA  MET A 184      28.191  19.701  19.129  1.00 72.29           C  
ANISOU 1380  CA  MET A 184     7488   9050  10928   -190    -91   1927       C  
ATOM   1381  C   MET A 184      27.681  20.731  18.117  1.00 69.29           C  
ANISOU 1381  C   MET A 184     6972   8769  10587   -144   -193   1945       C  
ATOM   1382  O   MET A 184      28.059  21.904  18.207  1.00 70.47           O  
ANISOU 1382  O   MET A 184     7165   8945  10664     21   -120   1913       O  
ATOM   1383  CB  MET A 184      29.431  19.008  18.562  1.00 68.55           C  
ANISOU 1383  CB  MET A 184     7252   8466  10329   -250   -220   1766       C  
ATOM   1384  CG  MET A 184      30.738  19.609  18.958  1.00 71.44           C  
ANISOU 1384  CG  MET A 184     7825   8797  10521   -100   -146   1649       C  
ATOM   1385  SD  MET A 184      32.117  18.571  18.416  1.00 71.20           S  
ANISOU 1385  SD  MET A 184     8042   8639  10372   -171   -273   1487       S  
ATOM   1386  CE  MET A 184      31.985  18.543  16.640  1.00 75.84           C  
ANISOU 1386  CE  MET A 184     8603   9247  10964   -276   -508   1411       C  
ATOM   1387  N   ALA A 185      26.807  20.325  17.193  1.00 66.22           N  
ANISOU 1387  N   ALA A 185     6415   8430  10314   -288   -359   2003       N  
ATOM   1388  CA  ALA A 185      26.432  21.156  16.046  1.00 65.56           C  
ANISOU 1388  CA  ALA A 185     6224   8442  10242   -261   -502   2017       C  
ATOM   1389  C   ALA A 185      26.003  22.587  16.368  1.00 71.00           C  
ANISOU 1389  C   ALA A 185     6794   9217  10967    -60   -368   2108       C  
ATOM   1390  O   ALA A 185      26.366  23.490  15.595  1.00 67.80           O  
ANISOU 1390  O   ALA A 185     6433   8838  10492     29   -441   2069       O  
ATOM   1391  CB  ALA A 185      25.313  20.464  15.259  1.00 59.14           C  
ANISOU 1391  CB  ALA A 185     5200   7698   9575   -452   -685   2100       C  
ATOM   1392  N   PRO A 186      25.223  22.872  17.418  1.00 66.06           N  
ANISOU 1392  N   PRO A 186     6015   8634  10449     21   -173   2233       N  
ATOM   1393  CA  PRO A 186      24.856  24.281  17.678  1.00 64.73           C  
ANISOU 1393  CA  PRO A 186     5752   8527  10315    232    -40   2301       C  
ATOM   1394  C   PRO A 186      26.036  25.227  17.829  1.00 65.82           C  
ANISOU 1394  C   PRO A 186     6125   8587  10295    391     31   2168       C  
ATOM   1395  O   PRO A 186      25.885  26.432  17.573  1.00 62.56           O  
ANISOU 1395  O   PRO A 186     5666   8199   9904    541     66   2199       O  
ATOM   1396  CB  PRO A 186      24.039  24.198  18.976  1.00 68.41           C  
ANISOU 1396  CB  PRO A 186     6074   9032  10886    290    192   2423       C  
ATOM   1397  CG  PRO A 186      23.459  22.810  18.962  1.00 63.65           C  
ANISOU 1397  CG  PRO A 186     5360   8439  10384     68    113   2493       C  
ATOM   1398  CD  PRO A 186      24.506  21.943  18.309  1.00 60.59           C  
ANISOU 1398  CD  PRO A 186     5204   7945   9872    -76    -69   2337       C  
ATOM   1399  N   LEU A 187      27.211  24.728  18.230  1.00 60.26           N  
ANISOU 1399  N   LEU A 187     5665   7785   9444    362     50   2027       N  
ATOM   1400  CA  LEU A 187      28.378  25.595  18.358  1.00 55.44           C  
ANISOU 1400  CA  LEU A 187     5266   7105   8693    491    102   1898       C  
ATOM   1401  C   LEU A 187      28.839  26.115  17.004  1.00 59.99           C  
ANISOU 1401  C   LEU A 187     5889   7682   9221    483    -72   1851       C  
ATOM   1402  O   LEU A 187      29.566  27.118  16.939  1.00 59.24           O  
ANISOU 1402  O   LEU A 187     5911   7543   9056    601    -30   1786       O  
ATOM   1403  CB  LEU A 187      29.526  24.839  19.046  1.00 53.24           C  
ANISOU 1403  CB  LEU A 187     5213   6740   8274    451    140   1772       C  
ATOM   1404  CG  LEU A 187      29.233  24.328  20.462  1.00 57.59           C  
ANISOU 1404  CG  LEU A 187     5757   7292   8834    470    323   1820       C  
ATOM   1405  CD1 LEU A 187      30.443  23.647  21.122  1.00 55.16           C  
ANISOU 1405  CD1 LEU A 187     5677   6906   8374    449    347   1705       C  
ATOM   1406  CD2 LEU A 187      28.718  25.459  21.320  1.00 59.48           C  
ANISOU 1406  CD2 LEU A 187     5927   7571   9103    650    524   1867       C  
ATOM   1407  N   PHE A 188      28.420  25.460  15.927  1.00 55.92           N  
ANISOU 1407  N   PHE A 188     5287   7218   8740    343   -267   1886       N  
ATOM   1408  CA  PHE A 188      28.848  25.810  14.589  1.00 56.04           C  
ANISOU 1408  CA  PHE A 188     5357   7255   8682    323   -442   1846       C  
ATOM   1409  C   PHE A 188      27.856  26.698  13.831  1.00 62.33           C  
ANISOU 1409  C   PHE A 188     5949   8154   9580    386   -508   1989       C  
ATOM   1410  O   PHE A 188      28.222  27.252  12.783  1.00 68.01           O  
ANISOU 1410  O   PHE A 188     6716   8895  10227    409   -625   1979       O  
ATOM   1411  CB  PHE A 188      29.164  24.522  13.830  1.00 51.53           C  
ANISOU 1411  CB  PHE A 188     4861   6674   8046    135   -625   1764       C  
ATOM   1412  CG  PHE A 188      30.423  23.874  14.322  1.00 56.83           C  
ANISOU 1412  CG  PHE A 188     5767   7234   8593    114   -575   1616       C  
ATOM   1413  CD1 PHE A 188      31.660  24.246  13.803  1.00 55.23           C  
ANISOU 1413  CD1 PHE A 188     5751   6990   8243    161   -608   1499       C  
ATOM   1414  CD2 PHE A 188      30.384  22.952  15.356  1.00 59.30           C  
ANISOU 1414  CD2 PHE A 188     6103   7490   8939     60   -482   1610       C  
ATOM   1415  CE1 PHE A 188      32.838  23.676  14.292  1.00 53.90           C  
ANISOU 1415  CE1 PHE A 188     5778   6731   7971    154   -559   1373       C  
ATOM   1416  CE2 PHE A 188      31.552  22.372  15.838  1.00 53.71           C  
ANISOU 1416  CE2 PHE A 188     5603   6686   8119     57   -440   1490       C  
ATOM   1417  CZ  PHE A 188      32.781  22.743  15.304  1.00 55.09           C  
ANISOU 1417  CZ  PHE A 188     5950   6827   8154    108   -481   1369       C  
ATOM   1418  N   GLU A 189      26.636  26.876  14.346  1.00 56.68           N  
ANISOU 1418  N   GLU A 189     5004   7505   9026    426   -428   2133       N  
ATOM   1419  CA  GLU A 189      25.710  27.908  13.862  1.00 65.41           C  
ANISOU 1419  CA  GLU A 189     5906   8701  10247    541   -444   2286       C  
ATOM   1420  C   GLU A 189      25.532  27.844  12.347  1.00 63.51           C  
ANISOU 1420  C   GLU A 189     5610   8552   9969    454   -699   2323       C  
ATOM   1421  O   GLU A 189      25.333  28.871  11.684  1.00 59.48           O  
ANISOU 1421  O   GLU A 189     5040   8086   9474    570   -739   2412       O  
ATOM   1422  CB  GLU A 189      26.175  29.301  14.302  1.00 68.91           C  
ANISOU 1422  CB  GLU A 189     6441   9066  10676    757   -274   2273       C  
ATOM   1423  CG  GLU A 189      26.563  29.357  15.780  1.00 80.95           C  
ANISOU 1423  CG  GLU A 189     8075  10500  12184    838    -37   2193       C  
ATOM   1424  CD  GLU A 189      26.687  30.768  16.332  1.00 81.85           C  
ANISOU 1424  CD  GLU A 189     8231  10541  12326   1055    145   2194       C  
ATOM   1425  OE1 GLU A 189      27.096  30.924  17.509  1.00 79.69           O  
ANISOU 1425  OE1 GLU A 189     8076  10194  12011   1129    330   2106       O  
ATOM   1426  OE2 GLU A 189      26.386  31.722  15.590  1.00 80.56           O  
ANISOU 1426  OE2 GLU A 189     7994  10390  12226   1153     99   2281       O  
ATOM   1427  N   ASN A 190      25.634  26.629  11.802  1.00 63.63           N  
ANISOU 1427  N   ASN A 190     5662   8589   9926    252   -871   2252       N  
ATOM   1428  CA  ASN A 190      25.405  26.284  10.400  1.00 69.44           C  
ANISOU 1428  CA  ASN A 190     6355   9426  10605    130  -1134   2261       C  
ATOM   1429  C   ASN A 190      26.390  26.925   9.434  1.00 72.31           C  
ANISOU 1429  C   ASN A 190     6906   9777  10791    193  -1213   2194       C  
ATOM   1430  O   ASN A 190      26.135  26.919   8.223  1.00 76.32           O  
ANISOU 1430  O   ASN A 190     7368  10394  11235    135  -1419   2230       O  
ATOM   1431  CB  ASN A 190      23.985  26.618   9.954  1.00 76.11           C  
ANISOU 1431  CB  ASN A 190     6888  10427  11605    135  -1234   2455       C  
ATOM   1432  CG  ASN A 190      23.005  25.560  10.346  1.00 88.31           C  
ANISOU 1432  CG  ASN A 190     8236  12020  13296    -31  -1275   2507       C  
ATOM   1433  OD1 ASN A 190      23.267  24.373  10.147  1.00 87.82           O  
ANISOU 1433  OD1 ASN A 190     8267  11918  13182   -225  -1387   2392       O  
ATOM   1434  ND2 ASN A 190      21.857  25.969  10.885  1.00 93.38           N  
ANISOU 1434  ND2 ASN A 190     8602  12745  14135     43  -1182   2683       N  
ATOM   1435  N   VAL A 191      27.512  27.468   9.918  1.00 62.90           N  
ANISOU 1435  N   VAL A 191     5921   8467   9513    303  -1060   2100       N  
ATOM   1436  CA  VAL A 191      28.441  28.109   9.005  1.00 64.77           C  
ANISOU 1436  CA  VAL A 191     6319   8695   9596    357  -1120   2056       C  
ATOM   1437  C   VAL A 191      29.121  27.059   8.143  1.00 68.36           C  
ANISOU 1437  C   VAL A 191     6926   9163   9883    200  -1286   1916       C  
ATOM   1438  O   VAL A 191      29.321  25.911   8.553  1.00 68.37           O  
ANISOU 1438  O   VAL A 191     6994   9111   9874     77  -1293   1805       O  
ATOM   1439  CB  VAL A 191      29.472  28.976   9.749  1.00 58.14           C  
ANISOU 1439  CB  VAL A 191     5646   7722   8724    499   -919   1991       C  
ATOM   1440  CG1 VAL A 191      28.756  29.979  10.656  1.00 55.64           C  
ANISOU 1440  CG1 VAL A 191     5192   7376   8572    660   -743   2107       C  
ATOM   1441  CG2 VAL A 191      30.468  28.104  10.527  1.00 50.63           C  
ANISOU 1441  CG2 VAL A 191     4881   6665   7692    430   -839   1817       C  
ATOM   1442  N   VAL A 192      29.467  27.457   6.943  1.00 68.32           N  
ANISOU 1442  N   VAL A 192     6984   9229   9746    211  -1413   1926       N  
ATOM   1443  CA  VAL A 192      30.200  26.617   6.009  1.00 67.17           C  
ANISOU 1443  CA  VAL A 192     7005   9104   9412     91  -1557   1786       C  
ATOM   1444  C   VAL A 192      31.686  26.792   6.300  1.00 65.54           C  
ANISOU 1444  C   VAL A 192     7031   8778   9091    153  -1421   1657       C  
ATOM   1445  O   VAL A 192      32.156  27.905   6.557  1.00 63.46           O  
ANISOU 1445  O   VAL A 192     6802   8469   8842    289  -1292   1709       O  
ATOM   1446  CB  VAL A 192      29.840  26.994   4.556  1.00 69.45           C  
ANISOU 1446  CB  VAL A 192     7246   9550   9591     82  -1755   1870       C  
ATOM   1447  CG1 VAL A 192      30.858  26.444   3.559  1.00 60.99           C  
ANISOU 1447  CG1 VAL A 192     6393   8497   8282     13  -1854   1721       C  
ATOM   1448  CG2 VAL A 192      28.419  26.527   4.224  1.00 67.26           C  
ANISOU 1448  CG2 VAL A 192     6738   9405   9414    -23  -1933   1966       C  
ATOM   1449  N   ILE A 193      32.425  25.687   6.279  1.00 58.26           N  
ANISOU 1449  N   ILE A 193     6265   7801   8071     52  -1448   1490       N  
ATOM   1450  CA  ILE A 193      33.803  25.644   6.745  1.00 55.76           C  
ANISOU 1450  CA  ILE A 193     6144   7372   7672     99  -1315   1365       C  
ATOM   1451  C   ILE A 193      34.675  25.188   5.586  1.00 54.31           C  
ANISOU 1451  C   ILE A 193     6123   7227   7287     51  -1418   1253       C  
ATOM   1452  O   ILE A 193      34.451  24.113   5.017  1.00 54.43           O  
ANISOU 1452  O   ILE A 193     6171   7271   7240    -70  -1556   1166       O  
ATOM   1453  CB  ILE A 193      33.955  24.737   7.977  1.00 60.03           C  
ANISOU 1453  CB  ILE A 193     6719   7798   8293     54  -1216   1279       C  
ATOM   1454  CG1 ILE A 193      33.254  25.410   9.163  1.00 59.48           C  
ANISOU 1454  CG1 ILE A 193     6509   7699   8391    137  -1073   1391       C  
ATOM   1455  CG2 ILE A 193      35.433  24.496   8.301  1.00 55.21           C  
ANISOU 1455  CG2 ILE A 193     6309   7092   7576     88  -1120   1140       C  
ATOM   1456  CD1 ILE A 193      33.164  24.595  10.386  1.00 61.09           C  
ANISOU 1456  CD1 ILE A 193     6716   7820   8675     97   -976   1350       C  
ATOM   1457  N   GLU A 194      35.622  26.044   5.189  1.00 55.37           N  
ANISOU 1457  N   GLU A 194     6352   7363   7321    146  -1351   1259       N  
ATOM   1458  CA  GLU A 194      36.526  25.696   4.102  1.00 65.64           C  
ANISOU 1458  CA  GLU A 194     7808   8712   8420    121  -1416   1163       C  
ATOM   1459  C   GLU A 194      37.810  25.077   4.648  1.00 63.67           C  
ANISOU 1459  C   GLU A 194     7717   8352   8121    127  -1306   1007       C  
ATOM   1460  O   GLU A 194      38.377  25.574   5.627  1.00 61.68           O  
ANISOU 1460  O   GLU A 194     7477   8011   7948    198  -1156   1010       O  
ATOM   1461  CB  GLU A 194      36.870  26.923   3.266  1.00 74.05           C  
ANISOU 1461  CB  GLU A 194     8883   9854   9398    214  -1403   1275       C  
ATOM   1462  CG  GLU A 194      35.739  27.326   2.346  1.00101.57           C  
ANISOU 1462  CG  GLU A 194    12242  13482  12866    204  -1559   1419       C  
ATOM   1463  CD  GLU A 194      35.519  26.312   1.230  1.00119.41           C  
ANISOU 1463  CD  GLU A 194    14559  15858  14954     90  -1752   1328       C  
ATOM   1464  OE1 GLU A 194      36.521  25.751   0.726  1.00125.95           O  
ANISOU 1464  OE1 GLU A 194    15560  16681  15613     69  -1743   1188       O  
ATOM   1465  OE2 GLU A 194      34.344  26.056   0.879  1.00122.81           O  
ANISOU 1465  OE2 GLU A 194    14859  16382  15420     20  -1912   1390       O  
ATOM   1466  N   PRO A 195      38.298  24.009   4.031  1.00 62.51           N  
ANISOU 1466  N   PRO A 195     7696   8212   7844     58  -1378    865       N  
ATOM   1467  CA  PRO A 195      39.566  23.427   4.490  1.00 56.90           C  
ANISOU 1467  CA  PRO A 195     7128   7404   7089     84  -1272    729       C  
ATOM   1468  C   PRO A 195      40.715  24.412   4.319  1.00 54.24           C  
ANISOU 1468  C   PRO A 195     6848   7081   6681    187  -1154    755       C  
ATOM   1469  O   PRO A 195      40.898  25.002   3.259  1.00 58.84           O  
ANISOU 1469  O   PRO A 195     7451   7764   7143    213  -1189    806       O  
ATOM   1470  CB  PRO A 195      39.732  22.187   3.605  1.00 55.29           C  
ANISOU 1470  CB  PRO A 195     7044   7215   6749      2  -1386    582       C  
ATOM   1471  CG  PRO A 195      38.322  21.909   3.043  1.00 60.88           C  
ANISOU 1471  CG  PRO A 195     7651   8002   7480   -105  -1565    629       C  
ATOM   1472  CD  PRO A 195      37.686  23.249   2.922  1.00 57.13           C  
ANISOU 1472  CD  PRO A 195     7031   7622   7054    -44  -1565    816       C  
ATOM   1473  N   CYS A 196      41.493  24.585   5.379  1.00 51.74           N  
ANISOU 1473  N   CYS A 196     6552   6669   6440    240  -1018    726       N  
ATOM   1474  CA  CYS A 196      42.678  25.432   5.355  1.00 47.67           C  
ANISOU 1474  CA  CYS A 196     6081   6149   5881    318   -904    737       C  
ATOM   1475  C   CYS A 196      43.876  24.617   5.824  1.00 45.31           C  
ANISOU 1475  C   CYS A 196     5884   5786   5546    332   -834    601       C  
ATOM   1476  O   CYS A 196      43.757  23.769   6.712  1.00 45.92           O  
ANISOU 1476  O   CYS A 196     5971   5783   5693    309   -826    538       O  
ATOM   1477  CB  CYS A 196      42.502  26.691   6.251  1.00 46.49           C  
ANISOU 1477  CB  CYS A 196     5843   5949   5873    376   -808    843       C  
ATOM   1478  SG  CYS A 196      41.220  27.924   5.715  1.00 58.91           S  
ANISOU 1478  SG  CYS A 196     7286   7584   7512    403   -860   1034       S  
ATOM   1479  N   LEU A 197      45.020  24.846   5.204  1.00 46.87           N  
ANISOU 1479  N   LEU A 197     6149   6024   5636    374   -780    570       N  
ATOM   1480  CA  LEU A 197      46.257  24.249   5.683  1.00 45.23           C  
ANISOU 1480  CA  LEU A 197     6010   5765   5409    409   -699    464       C  
ATOM   1481  C   LEU A 197      46.590  24.815   7.062  1.00 46.32           C  
ANISOU 1481  C   LEU A 197     6093   5826   5681    439   -609    489       C  
ATOM   1482  O   LEU A 197      46.846  26.014   7.192  1.00 53.22           O  
ANISOU 1482  O   LEU A 197     6919   6706   6598    466   -550    565       O  
ATOM   1483  CB  LEU A 197      47.391  24.504   4.689  1.00 45.56           C  
ANISOU 1483  CB  LEU A 197     6108   5886   5316    452   -647    447       C  
ATOM   1484  CG  LEU A 197      48.674  23.789   5.168  1.00 47.01           C  
ANISOU 1484  CG  LEU A 197     6345   6027   5489    498   -566    339       C  
ATOM   1485  CD1 LEU A 197      48.427  22.298   5.330  1.00 45.73           C  
ANISOU 1485  CD1 LEU A 197     6260   5801   5314    480   -623    219       C  
ATOM   1486  CD2 LEU A 197      49.816  24.044   4.254  1.00 43.03           C  
ANISOU 1486  CD2 LEU A 197     5876   5609   4866    546   -494    330       C  
ATOM   1487  N   LEU A 198      46.580  23.957   8.086  1.00 44.65           N  
ANISOU 1487  N   LEU A 198     5897   5538   5531    434   -601    425       N  
ATOM   1488  CA  LEU A 198      46.885  24.325   9.466  1.00 43.01           C  
ANISOU 1488  CA  LEU A 198     5653   5268   5420    464   -527    432       C  
ATOM   1489  C   LEU A 198      48.291  23.881   9.865  1.00 46.69           C  
ANISOU 1489  C   LEU A 198     6167   5721   5853    509   -471    352       C  
ATOM   1490  O   LEU A 198      48.750  22.807   9.475  1.00 41.58           O  
ANISOU 1490  O   LEU A 198     5587   5069   5143    521   -489    277       O  
ATOM   1491  CB  LEU A 198      45.869  23.693  10.433  1.00 47.57           C  
ANISOU 1491  CB  LEU A 198     6207   5785   6084    434   -550    442       C  
ATOM   1492  CG  LEU A 198      44.371  23.900  10.167  1.00 44.81           C  
ANISOU 1492  CG  LEU A 198     5784   5451   5790    385   -612    524       C  
ATOM   1493  CD1 LEU A 198      43.525  23.307  11.272  1.00 43.69           C  
ANISOU 1493  CD1 LEU A 198     5605   5252   5743    360   -603    543       C  
ATOM   1494  CD2 LEU A 198      44.071  25.369  10.021  1.00 35.66           C  
ANISOU 1494  CD2 LEU A 198     4553   4325   4672    416   -579    619       C  
ATOM   1495  N   HIS A 199      48.956  24.701  10.680  1.00 49.41           N  
ANISOU 1495  N   HIS A 199     6473   6054   6245    538   -405    365       N  
ATOM   1496  CA  HIS A 199      50.203  24.282  11.308  1.00 41.31           C  
ANISOU 1496  CA  HIS A 199     5467   5024   5207    579   -365    301       C  
ATOM   1497  C   HIS A 199      49.954  23.157  12.316  1.00 40.11           C  
ANISOU 1497  C   HIS A 199     5347   4812   5079    592   -383    266       C  
ATOM   1498  O   HIS A 199      50.684  22.152  12.342  1.00 44.19           O  
ANISOU 1498  O   HIS A 199     5910   5318   5562    630   -383    210       O  
ATOM   1499  CB  HIS A 199      50.881  25.493  11.980  1.00 33.82           C  
ANISOU 1499  CB  HIS A 199     4463   4079   4309    586   -312    319       C  
ATOM   1500  CG  HIS A 199      52.153  25.153  12.701  1.00 41.85           C  
ANISOU 1500  CG  HIS A 199     5474   5109   5318    622   -288    262       C  
ATOM   1501  ND1 HIS A 199      52.176  24.506  13.922  1.00 43.72           N  
ANISOU 1501  ND1 HIS A 199     5726   5316   5569    647   -299    231       N  
ATOM   1502  CD2 HIS A 199      53.449  25.365  12.366  1.00 42.89           C  
ANISOU 1502  CD2 HIS A 199     5575   5294   5429    641   -256    242       C  
ATOM   1503  CE1 HIS A 199      53.429  24.326  14.300  1.00 41.56           C  
ANISOU 1503  CE1 HIS A 199     5432   5078   5281    683   -288    194       C  
ATOM   1504  NE2 HIS A 199      54.222  24.847  13.376  1.00 40.80           N  
ANISOU 1504  NE2 HIS A 199     5298   5032   5171    677   -260    198       N  
ATOM   1505  N   GLY A 200      48.950  23.313  13.178  1.00 40.26           N  
ANISOU 1505  N   GLY A 200     5343   4793   5162    569   -387    307       N  
ATOM   1506  CA  GLY A 200      48.497  22.229  14.039  1.00 41.62           C  
ANISOU 1506  CA  GLY A 200     5546   4910   5359    569   -398    302       C  
ATOM   1507  C   GLY A 200      49.105  22.165  15.436  1.00 47.37           C  
ANISOU 1507  C   GLY A 200     6277   5628   6093    615   -359    293       C  
ATOM   1508  O   GLY A 200      48.616  21.389  16.275  1.00 44.70           O  
ANISOU 1508  O   GLY A 200     5961   5248   5775    618   -357    316       O  
ATOM   1509  N   ASP A 201      50.155  22.936  15.722  1.00 43.43           N  
ANISOU 1509  N   ASP A 201     5756   5173   5575    646   -333    265       N  
ATOM   1510  CA  ASP A 201      50.766  22.906  17.053  1.00 44.93           C  
ANISOU 1510  CA  ASP A 201     5947   5373   5752    686   -316    250       C  
ATOM   1511  C   ASP A 201      51.489  24.223  17.310  1.00 46.24           C  
ANISOU 1511  C   ASP A 201     6068   5580   5921    681   -297    223       C  
ATOM   1512  O   ASP A 201      52.692  24.243  17.597  1.00 48.03           O  
ANISOU 1512  O   ASP A 201     6276   5849   6122    706   -306    185       O  
ATOM   1513  CB  ASP A 201      51.748  21.729  17.186  1.00 45.75           C  
ANISOU 1513  CB  ASP A 201     6085   5480   5820    742   -334    223       C  
ATOM   1514  CG  ASP A 201      52.247  21.523  18.633  1.00 55.54           C  
ANISOU 1514  CG  ASP A 201     7329   6742   7033    789   -333    228       C  
ATOM   1515  OD1 ASP A 201      51.538  21.895  19.601  1.00 59.05           O  
ANISOU 1515  OD1 ASP A 201     7777   7182   7475    776   -315    254       O  
ATOM   1516  OD2 ASP A 201      53.348  20.974  18.805  1.00 56.86           O  
ANISOU 1516  OD2 ASP A 201     7494   6938   7173    846   -350    210       O  
ATOM   1517  N   LEU A 202      50.771  25.329  17.236  1.00 42.93           N  
ANISOU 1517  N   LEU A 202     5625   5142   5544    647   -272    244       N  
ATOM   1518  CA  LEU A 202      51.403  26.643  17.142  1.00 46.07           C  
ANISOU 1518  CA  LEU A 202     5987   5548   5968    625   -253    221       C  
ATOM   1519  C   LEU A 202      51.496  27.256  18.535  1.00 46.37           C  
ANISOU 1519  C   LEU A 202     6035   5579   6006    632   -238    177       C  
ATOM   1520  O   LEU A 202      50.527  27.828  19.035  1.00 49.03           O  
ANISOU 1520  O   LEU A 202     6383   5875   6371    634   -202    189       O  
ATOM   1521  CB  LEU A 202      50.601  27.529  16.201  1.00 43.67           C  
ANISOU 1521  CB  LEU A 202     5662   5214   5718    595   -233    275       C  
ATOM   1522  CG  LEU A 202      51.265  28.796  15.716  1.00 49.84           C  
ANISOU 1522  CG  LEU A 202     6410   5985   6540    565   -210    277       C  
ATOM   1523  CD1 LEU A 202      52.577  28.442  15.020  1.00 47.72           C  
ANISOU 1523  CD1 LEU A 202     6119   5778   6233    559   -221    259       C  
ATOM   1524  CD2 LEU A 202      50.301  29.418  14.753  1.00 53.28           C  
ANISOU 1524  CD2 LEU A 202     6832   6393   7019    554   -197    358       C  
ATOM   1525  N   TRP A 203      52.671  27.148  19.157  1.00 48.06           N  
ANISOU 1525  N   TRP A 203     6240   5840   6180    640   -266    122       N  
ATOM   1526  CA  TRP A 203      52.941  27.786  20.445  1.00 43.65           C  
ANISOU 1526  CA  TRP A 203     5696   5290   5597    637   -271     59       C  
ATOM   1527  C   TRP A 203      54.345  28.403  20.384  1.00 48.03           C  
ANISOU 1527  C   TRP A 203     6199   5885   6167    597   -308      3       C  
ATOM   1528  O   TRP A 203      55.013  28.364  19.342  1.00 51.78           O  
ANISOU 1528  O   TRP A 203     6621   6378   6674    579   -310     28       O  
ATOM   1529  CB  TRP A 203      52.745  26.785  21.593  1.00 41.93           C  
ANISOU 1529  CB  TRP A 203     5524   5111   5296    691   -286     63       C  
ATOM   1530  CG  TRP A 203      53.783  25.723  21.648  1.00 49.08           C  
ANISOU 1530  CG  TRP A 203     6414   6080   6155    728   -338     69       C  
ATOM   1531  CD1 TRP A 203      53.900  24.662  20.808  1.00 52.07           C  
ANISOU 1531  CD1 TRP A 203     6788   6452   6544    756   -344    114       C  
ATOM   1532  CD2 TRP A 203      54.844  25.597  22.606  1.00 45.74           C  
ANISOU 1532  CD2 TRP A 203     5978   5737   5667    751   -395     28       C  
ATOM   1533  NE1 TRP A 203      54.981  23.894  21.157  1.00 45.82           N  
ANISOU 1533  NE1 TRP A 203     5979   5720   5711    807   -388    110       N  
ATOM   1534  CE2 TRP A 203      55.584  24.441  22.255  1.00 48.13           C  
ANISOU 1534  CE2 TRP A 203     6256   6076   5957    804   -426     66       C  
ATOM   1535  CE3 TRP A 203      55.255  26.356  23.712  1.00 45.77           C  
ANISOU 1535  CE3 TRP A 203     5988   5786   5617    732   -429    -44       C  
ATOM   1536  CZ2 TRP A 203      56.710  24.015  22.978  1.00 48.21           C  
ANISOU 1536  CZ2 TRP A 203     6232   6174   5912    849   -490     56       C  
ATOM   1537  CZ3 TRP A 203      56.385  25.932  24.440  1.00 48.36           C  
ANISOU 1537  CZ3 TRP A 203     6285   6214   5875    761   -508    -64       C  
ATOM   1538  CH2 TRP A 203      57.099  24.776  24.060  1.00 48.64           C  
ANISOU 1538  CH2 TRP A 203     6279   6291   5909    822   -538     -4       C  
ATOM   1539  N   SER A 204      54.783  29.010  21.496  1.00 45.94           N  
ANISOU 1539  N   SER A 204     5945   5637   5875    578   -335    -74       N  
ATOM   1540  CA  SER A 204      56.009  29.823  21.500  1.00 48.30           C  
ANISOU 1540  CA  SER A 204     6182   5959   6211    511   -377   -135       C  
ATOM   1541  C   SER A 204      57.242  29.038  21.076  1.00 52.05           C  
ANISOU 1541  C   SER A 204     6575   6530   6673    525   -423   -111       C  
ATOM   1542  O   SER A 204      58.128  29.585  20.417  1.00 53.10           O  
ANISOU 1542  O   SER A 204     6627   6678   6872    469   -426   -112       O  
ATOM   1543  CB  SER A 204      56.258  30.414  22.888  1.00 48.59           C  
ANISOU 1543  CB  SER A 204     6255   6012   6195    487   -421   -240       C  
ATOM   1544  OG  SER A 204      55.456  31.563  23.072  1.00 66.58           O  
ANISOU 1544  OG  SER A 204     8591   8182   8524    456   -367   -285       O  
ATOM   1545  N   GLY A 205      57.356  27.780  21.510  1.00 52.89           N  
ANISOU 1545  N   GLY A 205     6696   6700   6701    604   -453    -85       N  
ATOM   1546  CA  GLY A 205      58.515  26.986  21.158  1.00 52.22           C  
ANISOU 1546  CA  GLY A 205     6532   6701   6610    642   -488    -60       C  
ATOM   1547  C   GLY A 205      58.640  26.650  19.678  1.00 54.77           C  
ANISOU 1547  C   GLY A 205     6819   7008   6982    656   -433     -5       C  
ATOM   1548  O   GLY A 205      59.707  26.197  19.266  1.00 51.99           O  
ANISOU 1548  O   GLY A 205     6387   6727   6638    687   -442      9       O  
ATOM   1549  N   ASN A 206      57.595  26.877  18.878  1.00 51.73           N  
ANISOU 1549  N   ASN A 206     6489   6543   6622    638   -376     26       N  
ATOM   1550  CA  ASN A 206      57.575  26.558  17.454  1.00 49.38           C  
ANISOU 1550  CA  ASN A 206     6181   6240   6342    651   -328     73       C  
ATOM   1551  C   ASN A 206      57.586  27.801  16.576  1.00 45.91           C  
ANISOU 1551  C   ASN A 206     5704   5773   5965    574   -285     94       C  
ATOM   1552  O   ASN A 206      57.344  27.695  15.369  1.00 47.12           O  
ANISOU 1552  O   ASN A 206     5866   5924   6115    580   -243    141       O  
ATOM   1553  CB  ASN A 206      56.339  25.715  17.111  1.00 46.59           C  
ANISOU 1553  CB  ASN A 206     5917   5829   5957    689   -313    104       C  
ATOM   1554  CG  ASN A 206      56.453  24.287  17.577  1.00 53.89           C  
ANISOU 1554  CG  ASN A 206     6878   6764   6834    769   -338    106       C  
ATOM   1555  OD1 ASN A 206      57.551  23.772  17.734  1.00 58.36           O  
ANISOU 1555  OD1 ASN A 206     7398   7389   7386    819   -356     96       O  
ATOM   1556  ND2 ASN A 206      55.316  23.636  17.812  1.00 49.55           N  
ANISOU 1556  ND2 ASN A 206     6404   6152   6270    781   -338    129       N  
ATOM   1557  N   ILE A 207      57.808  28.975  17.158  1.00 48.17           N  
ANISOU 1557  N   ILE A 207     5962   6033   6307    502   -296     62       N  
ATOM   1558  CA  ILE A 207      57.797  30.245  16.446  1.00 48.45           C  
ANISOU 1558  CA  ILE A 207     5970   6014   6423    425   -252     92       C  
ATOM   1559  C   ILE A 207      59.157  30.900  16.639  1.00 50.01           C  
ANISOU 1559  C   ILE A 207     6065   6255   6681    354   -270     64       C  
ATOM   1560  O   ILE A 207      59.714  30.864  17.738  1.00 49.05           O  
ANISOU 1560  O   ILE A 207     5919   6169   6549    340   -335     -8       O  
ATOM   1561  CB  ILE A 207      56.677  31.169  16.966  1.00 50.04           C  
ANISOU 1561  CB  ILE A 207     6241   6105   6667    396   -240     76       C  
ATOM   1562  CG1 ILE A 207      55.305  30.518  16.804  1.00 48.32           C  
ANISOU 1562  CG1 ILE A 207     6097   5858   6404    459   -225    116       C  
ATOM   1563  CG2 ILE A 207      56.726  32.530  16.273  1.00 48.08           C  
ANISOU 1563  CG2 ILE A 207     5968   5779   6522    321   -193    118       C  
ATOM   1564  CD1 ILE A 207      54.203  31.207  17.596  1.00 48.86           C  
ANISOU 1564  CD1 ILE A 207     6223   5838   6503    460   -208     94       C  
ATOM   1565  N   ALA A 208      59.688  31.508  15.582  1.00 50.13           N  
ANISOU 1565  N   ALA A 208     6015   6275   6758    304   -215    127       N  
ATOM   1566  CA  ALA A 208      60.992  32.154  15.655  1.00 46.84           C  
ANISOU 1566  CA  ALA A 208     5477   5900   6420    219   -224    117       C  
ATOM   1567  C   ALA A 208      61.011  33.305  14.665  1.00 46.16           C  
ANISOU 1567  C   ALA A 208     5364   5745   6428    137   -149    198       C  
ATOM   1568  O   ALA A 208      60.077  33.480  13.878  1.00 52.59           O  
ANISOU 1568  O   ALA A 208     6251   6503   7228    164    -96    267       O  
ATOM   1569  CB  ALA A 208      62.120  31.147  15.391  1.00 44.23           C  
ANISOU 1569  CB  ALA A 208     5044   5713   6049    278   -227    132       C  
ATOM   1570  N   TYR A 209      62.073  34.118  14.717  1.00 53.01           N  
ANISOU 1570  N   TYR A 209     6122   6618   7400     30   -149    200       N  
ATOM   1571  CA  TYR A 209      62.201  35.267  13.817  1.00 56.90           C  
ANISOU 1571  CA  TYR A 209     6583   7034   8001    -62    -70    294       C  
ATOM   1572  C   TYR A 209      63.591  35.283  13.200  1.00 57.27           C  
ANISOU 1572  C   TYR A 209     6468   7193   8100   -114    -27    359       C  
ATOM   1573  O   TYR A 209      64.576  35.004  13.881  1.00 62.65           O  
ANISOU 1573  O   TYR A 209     7041   7961   8803   -143    -89    297       O  
ATOM   1574  CB  TYR A 209      61.907  36.604  14.553  1.00 55.02           C  
ANISOU 1574  CB  TYR A 209     6388   6627   7888   -173    -98    237       C  
ATOM   1575  CG  TYR A 209      60.460  36.715  14.973  1.00 55.74           C  
ANISOU 1575  CG  TYR A 209     6631   6607   7942   -108   -105    200       C  
ATOM   1576  CD1 TYR A 209      60.010  36.107  16.144  1.00 56.37           C  
ANISOU 1576  CD1 TYR A 209     6777   6704   7937    -50   -178     82       C  
ATOM   1577  CD2 TYR A 209      59.534  37.391  14.182  1.00 53.27           C  
ANISOU 1577  CD2 TYR A 209     6385   6183   7674    -94    -33    299       C  
ATOM   1578  CE1 TYR A 209      58.678  36.167  16.522  1.00 49.51           C  
ANISOU 1578  CE1 TYR A 209     6029   5747   7035     16   -168     60       C  
ATOM   1579  CE2 TYR A 209      58.195  37.456  14.545  1.00 53.64           C  
ANISOU 1579  CE2 TYR A 209     6545   6141   7694    -23    -35    278       C  
ATOM   1580  CZ  TYR A 209      57.776  36.851  15.709  1.00 54.37           C  
ANISOU 1580  CZ  TYR A 209     6693   6254   7710     29    -96    157       C  
ATOM   1581  OH  TYR A 209      56.462  36.931  16.062  1.00 54.43           O  
ANISOU 1581  OH  TYR A 209     6797   6184   7701    100    -82    146       O  
ATOM   1582  N   ASP A 210      63.668  35.593  11.910  1.00 55.38           N  
ANISOU 1582  N   ASP A 210     6204   6967   7873   -120     80    492       N  
ATOM   1583  CA  ASP A 210      64.927  35.531  11.185  1.00 60.30           C  
ANISOU 1583  CA  ASP A 210     6668   7713   8529   -151    152    574       C  
ATOM   1584  C   ASP A 210      65.610  36.905  11.215  1.00 71.46           C  
ANISOU 1584  C   ASP A 210     7983   9040  10128   -326    175    623       C  
ATOM   1585  O   ASP A 210      65.238  37.788  11.993  1.00 71.70           O  
ANISOU 1585  O   ASP A 210     8068   8917  10257   -420    114    555       O  
ATOM   1586  CB  ASP A 210      64.699  34.987   9.766  1.00 50.37           C  
ANISOU 1586  CB  ASP A 210     5442   6541   7153    -50    264    690       C  
ATOM   1587  CG  ASP A 210      63.957  35.961   8.843  1.00 58.87           C  
ANISOU 1587  CG  ASP A 210     6595   7517   8255    -91    340    816       C  
ATOM   1588  OD1 ASP A 210      63.673  37.118   9.232  1.00 60.08           O  
ANISOU 1588  OD1 ASP A 210     6770   7515   8542   -197    322    828       O  
ATOM   1589  OD2 ASP A 210      63.673  35.566   7.687  1.00 61.25           O  
ANISOU 1589  OD2 ASP A 210     6940   7895   8437    -10    418    908       O  
ATOM   1590  N   LYS A 211      66.625  37.091  10.360  1.00 73.33           N  
ANISOU 1590  N   LYS A 211     8074   9372  10417   -373    272    740       N  
ATOM   1591  CA  LYS A 211      67.442  38.308  10.371  1.00 78.17           C  
ANISOU 1591  CA  LYS A 211     8562   9914  11226   -557    297    798       C  
ATOM   1592  C   LYS A 211      66.660  39.555   9.950  1.00 75.45           C  
ANISOU 1592  C   LYS A 211     8325   9366  10976   -638    350    884       C  
ATOM   1593  O   LYS A 211      66.969  40.656  10.423  1.00 76.11           O  
ANISOU 1593  O   LYS A 211     8372   9305  11240   -799    323    867       O  
ATOM   1594  CB  LYS A 211      68.661  38.122   9.460  1.00 85.90           C  
ANISOU 1594  CB  LYS A 211     9349  11060  12229   -572    413    929       C  
ATOM   1595  CG  LYS A 211      68.315  37.960   7.966  1.00 90.73           C  
ANISOU 1595  CG  LYS A 211    10015  11731  12727   -478    570   1092       C  
ATOM   1596  CD  LYS A 211      69.551  37.771   7.080  1.00 93.37           C  
ANISOU 1596  CD  LYS A 211    10157  12244  13074   -482    708   1222       C  
ATOM   1597  CE  LYS A 211      69.171  37.527   5.611  1.00 94.22           C  
ANISOU 1597  CE  LYS A 211    10343  12432  13023   -371    862   1368       C  
ATOM   1598  NZ  LYS A 211      68.370  36.272   5.411  1.00 93.59           N  
ANISOU 1598  NZ  LYS A 211    10417  12423  12719   -177    833   1279       N  
ATOM   1599  N   ASN A 212      65.665  39.418   9.060  1.00 71.92           N  
ANISOU 1599  N   ASN A 212     8008   8901  10418   -530    420    978       N  
ATOM   1600  CA  ASN A 212      64.781  40.528   8.693  1.00 70.76           C  
ANISOU 1600  CA  ASN A 212     7974   8561  10352   -573    461   1069       C  
ATOM   1601  C   ASN A 212      63.599  40.708   9.662  1.00 69.61           C  
ANISOU 1601  C   ASN A 212     7984   8258  10208   -536    362    937       C  
ATOM   1602  O   ASN A 212      62.664  41.447   9.328  1.00 69.61           O  
ANISOU 1602  O   ASN A 212     8090   8110  10249   -524    396   1013       O  
ATOM   1603  CB  ASN A 212      64.232  40.348   7.270  1.00 72.64           C  
ANISOU 1603  CB  ASN A 212     8271   8867  10460   -471    571   1245       C  
ATOM   1604  CG  ASN A 212      65.309  39.999   6.245  1.00 85.71           C  
ANISOU 1604  CG  ASN A 212     9792  10710  12064   -469    690   1372       C  
ATOM   1605  OD1 ASN A 212      66.302  40.708   6.095  1.00 88.68           O  
ANISOU 1605  OD1 ASN A 212    10031  11076  12588   -601    754   1456       O  
ATOM   1606  ND2 ASN A 212      65.113  38.888   5.538  1.00 89.45           N  
ANISOU 1606  ND2 ASN A 212    10304  11356  12329   -321    723   1382       N  
ATOM   1607  N   ASN A 213      63.623  40.071  10.839  1.00 68.97           N  
ANISOU 1607  N   ASN A 213     7913   8211  10083   -512    250    754       N  
ATOM   1608  CA  ASN A 213      62.490  40.097  11.777  1.00 67.99           C  
ANISOU 1608  CA  ASN A 213     7933   7968   9930   -457    172    630       C  
ATOM   1609  C   ASN A 213      61.191  39.630  11.131  1.00 63.11           C  
ANISOU 1609  C   ASN A 213     7435   7358   9187   -313    204    700       C  
ATOM   1610  O   ASN A 213      60.117  40.155  11.412  1.00 69.34           O  
ANISOU 1610  O   ASN A 213     8333   8005  10009   -284    196    688       O  
ATOM   1611  CB  ASN A 213      62.310  41.481  12.413  1.00 77.13           C  
ANISOU 1611  CB  ASN A 213     9142   8895  11270   -578    157    580       C  
ATOM   1612  CG  ASN A 213      63.416  41.824  13.373  1.00 91.35           C  
ANISOU 1612  CG  ASN A 213    10848  10686  13175   -724     78    450       C  
ATOM   1613  OD1 ASN A 213      63.347  41.484  14.553  1.00 97.77           O  
ANISOU 1613  OD1 ASN A 213    11699  11513  13937   -712    -26    278       O  
ATOM   1614  ND2 ASN A 213      64.455  42.480  12.872  1.00 92.68           N  
ANISOU 1614  ND2 ASN A 213    10887  10842  13485   -865    124    539       N  
ATOM   1615  N   GLU A 214      61.302  38.646  10.235  1.00 51.95           N  
ANISOU 1615  N   GLU A 214     5995   6114   7631   -223    242    772       N  
ATOM   1616  CA  GLU A 214      60.147  37.958   9.674  1.00 55.14           C  
ANISOU 1616  CA  GLU A 214     6500   6558   7892    -94    243    811       C  
ATOM   1617  C   GLU A 214      59.885  36.646  10.417  1.00 52.86           C  
ANISOU 1617  C   GLU A 214     6245   6359   7479     -3    163    676       C  
ATOM   1618  O   GLU A 214      60.829  35.993  10.879  1.00 48.87           O  
ANISOU 1618  O   GLU A 214     5664   5953   6952     -7    133    600       O  
ATOM   1619  CB  GLU A 214      60.361  37.670   8.180  1.00 58.55           C  
ANISOU 1619  CB  GLU A 214     6907   7113   8225    -51    331    964       C  
ATOM   1620  CG  GLU A 214      60.266  38.915   7.288  1.00 65.11           C  
ANISOU 1620  CG  GLU A 214     7737   7854   9148   -112    417   1142       C  
ATOM   1621  CD  GLU A 214      58.868  39.526   7.235  1.00 75.29           C  
ANISOU 1621  CD  GLU A 214     9138   9004  10463    -69    397   1195       C  
ATOM   1622  OE1 GLU A 214      57.923  38.789   6.904  1.00 77.64           O  
ANISOU 1622  OE1 GLU A 214     9507   9371  10624     36    360   1196       O  
ATOM   1623  OE2 GLU A 214      58.716  40.746   7.493  1.00 80.26           O  
ANISOU 1623  OE2 GLU A 214     9781   9452  11260   -139    420   1241       O  
ATOM   1624  N   PRO A 215      58.625  36.240  10.575  1.00 53.13           N  
ANISOU 1624  N   PRO A 215     6383   6361   7443     80    126    653       N  
ATOM   1625  CA  PRO A 215      58.338  35.003  11.315  1.00 50.20           C  
ANISOU 1625  CA  PRO A 215     6047   6058   6969    157     57    538       C  
ATOM   1626  C   PRO A 215      58.729  33.736  10.561  1.00 48.72           C  
ANISOU 1626  C   PRO A 215     5841   6022   6647    232     69    552       C  
ATOM   1627  O   PRO A 215      58.701  33.668   9.329  1.00 53.75           O  
ANISOU 1627  O   PRO A 215     6481   6718   7222    256    126    649       O  
ATOM   1628  CB  PRO A 215      56.824  35.063  11.528  1.00 50.17           C  
ANISOU 1628  CB  PRO A 215     6143   5970   6951    211     33    541       C  
ATOM   1629  CG  PRO A 215      56.324  35.961  10.420  1.00 45.69           C  
ANISOU 1629  CG  PRO A 215     5588   5348   6423    200     91    687       C  
ATOM   1630  CD  PRO A 215      57.404  36.977  10.215  1.00 47.11           C  
ANISOU 1630  CD  PRO A 215     5699   5485   6717    101    145    735       C  
ATOM   1631  N   VAL A 216      59.092  32.722  11.339  1.00 43.18           N  
ANISOU 1631  N   VAL A 216     5130   5381   5895    277     17    451       N  
ATOM   1632  CA  VAL A 216      59.403  31.381  10.864  1.00 43.52           C  
ANISOU 1632  CA  VAL A 216     5175   5539   5822    365     22    434       C  
ATOM   1633  C   VAL A 216      58.687  30.415  11.793  1.00 47.25           C  
ANISOU 1633  C   VAL A 216     5722   5988   6243    427    -52    347       C  
ATOM   1634  O   VAL A 216      58.786  30.562  13.013  1.00 49.10           O  
ANISOU 1634  O   VAL A 216     5947   6188   6522    405   -104    280       O  
ATOM   1635  CB  VAL A 216      60.920  31.092  10.898  1.00 43.17           C  
ANISOU 1635  CB  VAL A 216     5010   5599   5795    363     47    419       C  
ATOM   1636  CG1 VAL A 216      61.218  29.737  10.264  1.00 36.87           C  
ANISOU 1636  CG1 VAL A 216     4226   4903   4880    476     74    405       C  
ATOM   1637  CG2 VAL A 216      61.734  32.217  10.260  1.00 37.59           C  
ANISOU 1637  CG2 VAL A 216     4202   4902   5177    272    121    508       C  
ATOM   1638  N   ILE A 217      57.985  29.418  11.241  1.00 42.44           N  
ANISOU 1638  N   ILE A 217     5188   5400   5538    498    -59    348       N  
ATOM   1639  CA  ILE A 217      57.326  28.454  12.116  1.00 43.47           C  
ANISOU 1639  CA  ILE A 217     5383   5501   5634    547   -120    282       C  
ATOM   1640  C   ILE A 217      57.877  27.061  11.832  1.00 46.83           C  
ANISOU 1640  C   ILE A 217     5820   5992   5982    631   -119    245       C  
ATOM   1641  O   ILE A 217      58.284  26.766  10.702  1.00 47.21           O  
ANISOU 1641  O   ILE A 217     5865   6100   5974    661    -69    268       O  
ATOM   1642  CB  ILE A 217      55.784  28.510  12.003  1.00 43.41           C  
ANISOU 1642  CB  ILE A 217     5456   5423   5615    544   -144    308       C  
ATOM   1643  CG1 ILE A 217      55.296  28.200  10.597  1.00 49.36           C  
ANISOU 1643  CG1 ILE A 217     6249   6211   6294    562   -129    360       C  
ATOM   1644  CG2 ILE A 217      55.266  29.912  12.409  1.00 38.05           C  
ANISOU 1644  CG2 ILE A 217     4764   4662   5029    484   -134    341       C  
ATOM   1645  CD1 ILE A 217      53.759  28.359  10.470  1.00 42.43           C  
ANISOU 1645  CD1 ILE A 217     5422   5278   5421    550   -166    400       C  
ATOM   1646  N   LEU A 218      57.902  26.211  12.883  1.00 46.07           N  
ANISOU 1646  N   LEU A 218     5743   5881   5879    675   -168    191       N  
ATOM   1647  CA  LEU A 218      58.665  24.956  12.925  1.00 47.96           C  
ANISOU 1647  CA  LEU A 218     5979   6167   6078    765   -168    156       C  
ATOM   1648  C   LEU A 218      57.835  23.825  13.531  1.00 48.09           C  
ANISOU 1648  C   LEU A 218     6089   6117   6064    813   -214    128       C  
ATOM   1649  O   LEU A 218      56.833  24.059  14.219  1.00 45.67           O  
ANISOU 1649  O   LEU A 218     5827   5751   5776    774   -249    134       O  
ATOM   1650  CB  LEU A 218      59.940  25.112  13.778  1.00 50.51           C  
ANISOU 1650  CB  LEU A 218     6192   6555   6444    776   -184    141       C  
ATOM   1651  CG  LEU A 218      60.733  26.412  13.637  1.00 52.80           C  
ANISOU 1651  CG  LEU A 218     6370   6890   6802    691   -159    167       C  
ATOM   1652  CD1 LEU A 218      61.611  26.683  14.861  1.00 51.83           C  
ANISOU 1652  CD1 LEU A 218     6154   6810   6728    667   -221    134       C  
ATOM   1653  CD2 LEU A 218      61.555  26.384  12.367  1.00 48.12           C  
ANISOU 1653  CD2 LEU A 218     5713   6375   6195    715    -74    207       C  
ATOM   1654  N   ASP A 219      58.317  22.591  13.352  1.00 44.94           N  
ANISOU 1654  N   ASP A 219     5717   5727   5633    903   -207    102       N  
ATOM   1655  CA  ASP A 219      57.743  21.405  13.984  1.00 52.98           C  
ANISOU 1655  CA  ASP A 219     6819   6671   6640    952   -245     86       C  
ATOM   1656  C   ASP A 219      56.224  21.294  13.808  1.00 50.10           C  
ANISOU 1656  C   ASP A 219     6544   6222   6270    894   -270     94       C  
ATOM   1657  O   ASP A 219      55.484  21.264  14.792  1.00 47.56           O  
ANISOU 1657  O   ASP A 219     6245   5854   5972    870   -302    114       O  
ATOM   1658  CB  ASP A 219      58.084  21.347  15.468  1.00 58.86           C  
ANISOU 1658  CB  ASP A 219     7528   7426   7409    973   -289     97       C  
ATOM   1659  CG  ASP A 219      59.551  21.256  15.727  1.00 76.32           C  
ANISOU 1659  CG  ASP A 219     9639   9728   9632   1037   -286     95       C  
ATOM   1660  OD1 ASP A 219      60.200  20.368  15.137  1.00 89.64           O  
ANISOU 1660  OD1 ASP A 219    11324  11425  11308   1130   -251     85       O  
ATOM   1661  OD2 ASP A 219      60.054  22.083  16.520  1.00 79.50           O  
ANISOU 1661  OD2 ASP A 219     9960  10191  10056    995   -320     99       O  
ATOM   1662  N   PRO A 220      55.728  21.237  12.578  1.00 51.04           N  
ANISOU 1662  N   PRO A 220     6709   6334   6352    871   -257     84       N  
ATOM   1663  CA  PRO A 220      54.278  21.223  12.402  1.00 49.70           C  
ANISOU 1663  CA  PRO A 220     6596   6102   6186    806   -295    101       C  
ATOM   1664  C   PRO A 220      53.679  19.876  12.785  1.00 50.07           C  
ANISOU 1664  C   PRO A 220     6725   6057   6245    825   -330     79       C  
ATOM   1665  O   PRO A 220      54.369  18.867  12.940  1.00 55.02           O  
ANISOU 1665  O   PRO A 220     7385   6653   6865    900   -319     45       O  
ATOM   1666  CB  PRO A 220      54.099  21.504  10.910  1.00 47.86           C  
ANISOU 1666  CB  PRO A 220     6384   5910   5891    782   -284     95       C  
ATOM   1667  CG  PRO A 220      55.321  20.912  10.300  1.00 56.17           C  
ANISOU 1667  CG  PRO A 220     7445   7008   6891    863   -234     46       C  
ATOM   1668  CD  PRO A 220      56.431  21.217  11.283  1.00 53.35           C  
ANISOU 1668  CD  PRO A 220     6997   6687   6587    903   -207     61       C  
ATOM   1669  N   ALA A 221      52.356  19.906  12.959  1.00 52.67           N  
ANISOU 1669  N   ALA A 221     7074   6335   6603    756   -367    110       N  
ATOM   1670  CA  ALA A 221      51.470  18.743  13.001  1.00 45.11           C  
ANISOU 1670  CA  ALA A 221     6190   5282   5670    731   -406    100       C  
ATOM   1671  C   ALA A 221      50.310  19.003  12.032  1.00 46.64           C  
ANISOU 1671  C   ALA A 221     6390   5477   5852    646   -452    106       C  
ATOM   1672  O   ALA A 221      49.157  19.105  12.440  1.00 42.84           O  
ANISOU 1672  O   ALA A 221     5886   4967   5427    583   -481    158       O  
ATOM   1673  CB  ALA A 221      50.957  18.514  14.423  1.00 38.78           C  
ANISOU 1673  CB  ALA A 221     5377   4430   4928    725   -405    157       C  
ATOM   1674  N   CYS A 222      50.642  19.155  10.746  1.00 44.46           N  
ANISOU 1674  N   CYS A 222     6138   5254   5498    650   -457     63       N  
ATOM   1675  CA  CYS A 222      49.757  19.753   9.744  1.00 47.71           C  
ANISOU 1675  CA  CYS A 222     6538   5716   5874    581   -504     86       C  
ATOM   1676  C   CYS A 222      48.545  18.903   9.421  1.00 50.97           C  
ANISOU 1676  C   CYS A 222     6996   6067   6304    504   -588     67       C  
ATOM   1677  O   CYS A 222      48.569  17.673   9.520  1.00 47.58           O  
ANISOU 1677  O   CYS A 222     6644   5545   5888    505   -608      2       O  
ATOM   1678  CB  CYS A 222      50.477  19.978   8.416  1.00 51.16           C  
ANISOU 1678  CB  CYS A 222     7007   6236   6195    612   -485     45       C  
ATOM   1679  SG  CYS A 222      51.729  21.247   8.422  1.00 56.08           S  
ANISOU 1679  SG  CYS A 222     7549   6954   6803    665   -392     93       S  
ATOM   1680  N   TYR A 223      47.493  19.589   8.982  1.00 45.69           N  
ANISOU 1680  N   TYR A 223     6272   5446   5642    436   -642    128       N  
ATOM   1681  CA  TYR A 223      46.367  18.980   8.288  1.00 48.70           C  
ANISOU 1681  CA  TYR A 223     6677   5811   6016    347   -746    108       C  
ATOM   1682  C   TYR A 223      45.482  20.095   7.765  1.00 43.33           C  
ANISOU 1682  C   TYR A 223     5907   5225   5332    306   -791    202       C  
ATOM   1683  O   TYR A 223      45.711  21.276   8.040  1.00 49.08           O  
ANISOU 1683  O   TYR A 223     6566   6002   6079    348   -731    281       O  
ATOM   1684  CB  TYR A 223      45.576  18.015   9.178  1.00 46.39           C  
ANISOU 1684  CB  TYR A 223     6385   5404   5838    289   -775    115       C  
ATOM   1685  CG  TYR A 223      44.861  18.637  10.336  1.00 48.92           C  
ANISOU 1685  CG  TYR A 223     6596   5721   6270    275   -738    228       C  
ATOM   1686  CD1 TYR A 223      45.549  19.012  11.485  1.00 47.42           C  
ANISOU 1686  CD1 TYR A 223     6388   5519   6111    350   -644    259       C  
ATOM   1687  CD2 TYR A 223      43.482  18.822  10.302  1.00 48.03           C  
ANISOU 1687  CD2 TYR A 223     6396   5624   6228    191   -799    302       C  
ATOM   1688  CE1 TYR A 223      44.873  19.558  12.585  1.00 49.80           C  
ANISOU 1688  CE1 TYR A 223     6606   5819   6495    346   -601    349       C  
ATOM   1689  CE2 TYR A 223      42.800  19.369  11.385  1.00 40.94           C  
ANISOU 1689  CE2 TYR A 223     5398   4726   5432    193   -746    405       C  
ATOM   1690  CZ  TYR A 223      43.494  19.734  12.527  1.00 48.12           C  
ANISOU 1690  CZ  TYR A 223     6311   5619   6355    273   -641    423       C  
ATOM   1691  OH  TYR A 223      42.807  20.265  13.608  1.00 48.09           O  
ANISOU 1691  OH  TYR A 223     6223   5618   6430    283   -579    511       O  
ATOM   1692  N   TYR A 224      44.472  19.704   6.995  1.00 43.22           N  
ANISOU 1692  N   TYR A 224     5893   5231   5296    222   -904    194       N  
ATOM   1693  CA  TYR A 224      43.500  20.630   6.434  1.00 43.48           C  
ANISOU 1693  CA  TYR A 224     5832   5361   5329    184   -969    296       C  
ATOM   1694  C   TYR A 224      42.270  20.656   7.336  1.00 48.88           C  
ANISOU 1694  C   TYR A 224     6401   6005   6168    127   -992    384       C  
ATOM   1695  O   TYR A 224      41.588  19.636   7.498  1.00 52.22           O  
ANISOU 1695  O   TYR A 224     6829   6365   6648     43  -1059    350       O  
ATOM   1696  CB  TYR A 224      43.132  20.222   5.007  1.00 42.52           C  
ANISOU 1696  CB  TYR A 224     5767   5313   5074    126  -1095    239       C  
ATOM   1697  CG  TYR A 224      44.289  20.372   4.055  1.00 45.07           C  
ANISOU 1697  CG  TYR A 224     6193   5704   5227    195  -1052    173       C  
ATOM   1698  CD1 TYR A 224      44.550  21.598   3.424  1.00 47.45           C  
ANISOU 1698  CD1 TYR A 224     6455   6122   5453    245  -1020    270       C  
ATOM   1699  CD2 TYR A 224      45.125  19.310   3.781  1.00 50.56           C  
ANISOU 1699  CD2 TYR A 224     7021   6345   5844    219  -1030     26       C  
ATOM   1700  CE1 TYR A 224      45.630  21.756   2.561  1.00 44.65           C  
ANISOU 1700  CE1 TYR A 224     6184   5840   4943    308   -961    228       C  
ATOM   1701  CE2 TYR A 224      46.217  19.461   2.918  1.00 58.49           C  
ANISOU 1701  CE2 TYR A 224     8108   7424   6690    296   -967    -29       C  
ATOM   1702  CZ  TYR A 224      46.461  20.680   2.317  1.00 52.65           C  
ANISOU 1702  CZ  TYR A 224     7320   6813   5873    335   -931     76       C  
ATOM   1703  OH  TYR A 224      47.537  20.811   1.472  1.00 49.43           O  
ANISOU 1703  OH  TYR A 224     6984   6485   5310    408   -855     37       O  
ATOM   1704  N   GLY A 225      41.979  21.818   7.903  1.00 45.56           N  
ANISOU 1704  N   GLY A 225     5877   5614   5820    173   -930    498       N  
ATOM   1705  CA  GLY A 225      40.917  21.896   8.876  1.00 47.43           C  
ANISOU 1705  CA  GLY A 225     6003   5817   6202    145   -915    583       C  
ATOM   1706  C   GLY A 225      40.329  23.285   8.972  1.00 49.85           C  
ANISOU 1706  C   GLY A 225     6191   6183   6567    194   -881    710       C  
ATOM   1707  O   GLY A 225      40.594  24.157   8.142  1.00 51.26           O  
ANISOU 1707  O   GLY A 225     6370   6428   6678    232   -894    748       O  
ATOM   1708  N   HIS A 226      39.512  23.471  10.001  1.00 43.20           N  
ANISOU 1708  N   HIS A 226     5251   5311   5854    199   -829    784       N  
ATOM   1709  CA  HIS A 226      38.957  24.781  10.294  1.00 41.03           C  
ANISOU 1709  CA  HIS A 226     4869   5066   5656    267   -769    897       C  
ATOM   1710  C   HIS A 226      40.071  25.726  10.711  1.00 45.31           C  
ANISOU 1710  C   HIS A 226     5476   5572   6168    358   -658    870       C  
ATOM   1711  O   HIS A 226      40.851  25.408  11.619  1.00 46.18           O  
ANISOU 1711  O   HIS A 226     5656   5623   6268    379   -582    797       O  
ATOM   1712  CB  HIS A 226      37.924  24.675  11.414  1.00 43.46           C  
ANISOU 1712  CB  HIS A 226     5067   5346   6100    264   -711    967       C  
ATOM   1713  CG  HIS A 226      37.067  25.892  11.562  1.00 41.95           C  
ANISOU 1713  CG  HIS A 226     4745   5190   6003    335   -664   1090       C  
ATOM   1714  ND1 HIS A 226      36.234  26.083  12.643  1.00 45.61           N  
ANISOU 1714  ND1 HIS A 226     5108   5637   6585    370   -569   1157       N  
ATOM   1715  CD2 HIS A 226      36.884  26.962  10.747  1.00 41.12           C  
ANISOU 1715  CD2 HIS A 226     4593   5135   5896    387   -694   1168       C  
ATOM   1716  CE1 HIS A 226      35.588  27.231  12.499  1.00 43.64           C  
ANISOU 1716  CE1 HIS A 226     4754   5417   6408    449   -538   1261       C  
ATOM   1717  NE2 HIS A 226      35.973  27.786  11.362  1.00 45.03           N  
ANISOU 1717  NE2 HIS A 226     4962   5628   6518    460   -616   1274       N  
ATOM   1718  N   ASN A 227      40.148  26.894  10.057  1.00 45.18           N  
ANISOU 1718  N   ASN A 227     5435   5590   6141    408   -652    937       N  
ATOM   1719  CA  ASN A 227      41.249  27.807  10.367  1.00 43.54           C  
ANISOU 1719  CA  ASN A 227     5289   5338   5917    472   -555    909       C  
ATOM   1720  C   ASN A 227      41.279  28.166  11.857  1.00 44.94           C  
ANISOU 1720  C   ASN A 227     5458   5439   6179    520   -439    886       C  
ATOM   1721  O   ASN A 227      42.361  28.304  12.436  1.00 46.10           O  
ANISOU 1721  O   ASN A 227     5679   5543   6295    540   -378    807       O  
ATOM   1722  CB  ASN A 227      41.168  29.063   9.495  1.00 40.43           C  
ANISOU 1722  CB  ASN A 227     4861   4973   5528    515   -558   1011       C  
ATOM   1723  CG  ASN A 227      39.979  29.957   9.849  1.00 47.21           C  
ANISOU 1723  CG  ASN A 227     5603   5815   6519    570   -527   1131       C  
ATOM   1724  OD1 ASN A 227      38.870  29.487  10.052  1.00 53.30           O  
ANISOU 1724  OD1 ASN A 227     6284   6618   7350    551   -568   1175       O  
ATOM   1725  ND2 ASN A 227      40.221  31.248   9.928  1.00 46.67           N  
ANISOU 1725  ND2 ASN A 227     5533   5691   6509    640   -450   1186       N  
ATOM   1726  N   GLU A 228      40.114  28.257  12.511  1.00 43.99           N  
ANISOU 1726  N   GLU A 228     5245   5311   6158    537   -411    951       N  
ATOM   1727  CA  GLU A 228      40.110  28.613  13.926  1.00 38.31           C  
ANISOU 1727  CA  GLU A 228     4530   4531   5493    593   -292    924       C  
ATOM   1728  C   GLU A 228      40.812  27.570  14.797  1.00 42.96           C  
ANISOU 1728  C   GLU A 228     5201   5099   6021    564   -271    826       C  
ATOM   1729  O   GLU A 228      41.205  27.891  15.921  1.00 45.11           O  
ANISOU 1729  O   GLU A 228     5513   5334   6293    610   -182    778       O  
ATOM   1730  CB  GLU A 228      38.669  28.805  14.427  1.00 46.95           C  
ANISOU 1730  CB  GLU A 228     5500   5638   6701    624   -251   1021       C  
ATOM   1731  CG  GLU A 228      37.829  29.930  13.775  1.00 45.87           C  
ANISOU 1731  CG  GLU A 228     5259   5517   6651    683   -254   1141       C  
ATOM   1732  CD  GLU A 228      36.356  29.921  14.267  1.00 51.66           C  
ANISOU 1732  CD  GLU A 228     5842   6282   7505    716   -215   1245       C  
ATOM   1733  OE1 GLU A 228      36.031  29.138  15.180  1.00 50.29           O  
ANISOU 1733  OE1 GLU A 228     5654   6112   7344    691   -168   1223       O  
ATOM   1734  OE2 GLU A 228      35.516  30.686  13.738  1.00 59.54           O  
ANISOU 1734  OE2 GLU A 228     6728   7305   8588    770   -228   1362       O  
ATOM   1735  N   ALA A 229      40.974  26.330  14.327  1.00 43.40           N  
ANISOU 1735  N   ALA A 229     5289   5176   6024    495   -353    794       N  
ATOM   1736  CA  ALA A 229      41.627  25.342  15.183  1.00 47.04           C  
ANISOU 1736  CA  ALA A 229     5828   5606   6440    484   -329    721       C  
ATOM   1737  C   ALA A 229      43.118  25.613  15.353  1.00 49.36           C  
ANISOU 1737  C   ALA A 229     6213   5884   6656    519   -304    631       C  
ATOM   1738  O   ALA A 229      43.724  25.055  16.269  1.00 44.89           O  
ANISOU 1738  O   ALA A 229     5701   5299   6054    534   -271    581       O  
ATOM   1739  CB  ALA A 229      41.414  23.919  14.650  1.00 35.39           C  
ANISOU 1739  CB  ALA A 229     4373   4128   4947    404   -417    706       C  
ATOM   1740  N   ASP A 230      43.707  26.487  14.566  1.00 46.19           N  
ANISOU 1740  N   ASP A 230     5820   5497   6234    532   -314    623       N  
ATOM   1741  CA  ASP A 230      45.097  26.787  14.732  1.00 42.84           C  
ANISOU 1741  CA  ASP A 230     5457   5066   5756    553   -288    549       C  
ATOM   1742  C   ASP A 230      45.397  27.642  15.941  1.00 46.43           C  
ANISOU 1742  C   ASP A 230     5919   5485   6237    596   -210    517       C  
ATOM   1743  O   ASP A 230      46.516  27.846  16.246  1.00 46.13           O  
ANISOU 1743  O   ASP A 230     5919   5446   6161    603   -198    452       O  
ATOM   1744  CB  ASP A 230      45.690  27.398  13.482  1.00 44.39           C  
ANISOU 1744  CB  ASP A 230     5656   5289   5920    544   -314    560       C  
ATOM   1745  CG  ASP A 230      46.868  26.623  12.948  1.00 55.35           C  
ANISOU 1745  CG  ASP A 230     7102   6709   7221    534   -342    493       C  
ATOM   1746  OD1 ASP A 230      47.320  25.700  13.598  1.00 47.00           O  
ANISOU 1746  OD1 ASP A 230     6082   5639   6137    542   -343    435       O  
ATOM   1747  OD2 ASP A 230      47.343  26.938  11.872  1.00 47.19           O  
ANISOU 1747  OD2 ASP A 230     6074   5712   6143    527   -356    506       O  
ATOM   1748  N   PHE A 231      44.395  28.141  16.623  1.00 41.84           N  
ANISOU 1748  N   PHE A 231     5298   4881   5718    624   -156    559       N  
ATOM   1749  CA  PHE A 231      44.591  28.906  17.848  1.00 42.89           C  
ANISOU 1749  CA  PHE A 231     5457   4979   5860    670    -77    509       C  
ATOM   1750  C   PHE A 231      44.467  28.044  19.105  1.00 45.64           C  
ANISOU 1750  C   PHE A 231     5836   5345   6159    686    -46    483       C  
ATOM   1751  O   PHE A 231      44.519  28.574  20.218  1.00 46.30           O  
ANISOU 1751  O   PHE A 231     5950   5417   6225    728     21    437       O  
ATOM   1752  CB  PHE A 231      43.589  30.065  17.929  1.00 47.89           C  
ANISOU 1752  CB  PHE A 231     6039   5570   6587    715    -12    564       C  
ATOM   1753  CG  PHE A 231      43.620  31.011  16.749  1.00 52.29           C  
ANISOU 1753  CG  PHE A 231     6566   6100   7200    711    -34    618       C  
ATOM   1754  CD1 PHE A 231      44.805  31.357  16.142  1.00 53.35           C  
ANISOU 1754  CD1 PHE A 231     6740   6227   7303    678    -65    579       C  
ATOM   1755  CD2 PHE A 231      42.442  31.578  16.267  1.00 59.11           C  
ANISOU 1755  CD2 PHE A 231     7351   6954   8153    747    -20    724       C  
ATOM   1756  CE1 PHE A 231      44.829  32.245  15.061  1.00 49.07           C  
ANISOU 1756  CE1 PHE A 231     6174   5662   6809    675    -74    650       C  
ATOM   1757  CE2 PHE A 231      42.464  32.463  15.199  1.00 59.02           C  
ANISOU 1757  CE2 PHE A 231     7316   6920   8188    753    -40    794       C  
ATOM   1758  CZ  PHE A 231      43.671  32.793  14.594  1.00 52.68           C  
ANISOU 1758  CZ  PHE A 231     6568   6105   7344    715    -65    760       C  
ATOM   1759  N   GLY A 232      44.327  26.727  18.953  1.00 48.31           N  
ANISOU 1759  N   GLY A 232     6177   5709   6470    654    -91    510       N  
ATOM   1760  CA  GLY A 232      44.143  25.838  20.089  1.00 40.48           C  
ANISOU 1760  CA  GLY A 232     5213   4729   5438    669    -57    516       C  
ATOM   1761  C   GLY A 232      45.323  25.721  21.040  1.00 42.17           C  
ANISOU 1761  C   GLY A 232     5503   4961   5558    699    -52    438       C  
ATOM   1762  O   GLY A 232      45.156  25.136  22.109  1.00 45.82           O  
ANISOU 1762  O   GLY A 232     5995   5443   5973    725    -15    455       O  
ATOM   1763  N   MET A 233      46.506  26.225  20.690  1.00 46.81           N  
ANISOU 1763  N   MET A 233     6115   5554   6117    696    -91    365       N  
ATOM   1764  CA  MET A 233      47.628  26.237  21.623  1.00 46.45           C  
ANISOU 1764  CA  MET A 233     6120   5541   5989    720   -101    291       C  
ATOM   1765  C   MET A 233      47.912  27.636  22.168  1.00 48.27           C  
ANISOU 1765  C   MET A 233     6363   5758   6217    731    -66    216       C  
ATOM   1766  O   MET A 233      48.975  27.860  22.755  1.00 43.36           O  
ANISOU 1766  O   MET A 233     5772   5168   5535    731    -97    138       O  
ATOM   1767  CB  MET A 233      48.895  25.667  20.967  1.00 50.64           C  
ANISOU 1767  CB  MET A 233     6657   6094   6491    706   -173    259       C  
ATOM   1768  CG  MET A 233      48.987  24.134  20.893  1.00 53.04           C  
ANISOU 1768  CG  MET A 233     6985   6401   6768    718   -206    300       C  
ATOM   1769  SD  MET A 233      49.017  23.372  22.539  1.00 54.04           S  
ANISOU 1769  SD  MET A 233     7163   6560   6812    770   -184    323       S  
ATOM   1770  CE  MET A 233      50.616  23.917  23.152  1.00 46.39           C  
ANISOU 1770  CE  MET A 233     6201   5663   5763    797   -232    233       C  
ATOM   1771  N   SER A 234      46.970  28.570  22.022  1.00 47.73           N  
ANISOU 1771  N   SER A 234     6271   5642   6221    741     -6    236       N  
ATOM   1772  CA  SER A 234      47.236  29.972  22.341  1.00 53.26           C  
ANISOU 1772  CA  SER A 234     6993   6295   6948    747     28    158       C  
ATOM   1773  C   SER A 234      47.527  30.193  23.820  1.00 53.21           C  
ANISOU 1773  C   SER A 234     7056   6314   6845    779     57     65       C  
ATOM   1774  O   SER A 234      48.167  31.190  24.175  1.00 52.45           O  
ANISOU 1774  O   SER A 234     6997   6184   6747    764     53    -37       O  
ATOM   1775  CB  SER A 234      46.048  30.854  21.933  1.00 54.62           C  
ANISOU 1775  CB  SER A 234     7127   6400   7227    775     99    213       C  
ATOM   1776  OG  SER A 234      44.901  30.576  22.737  1.00 52.54           O  
ANISOU 1776  OG  SER A 234     6857   6154   6953    831    177    254       O  
ATOM   1777  N   TRP A 235      47.078  29.286  24.689  1.00 43.14           N  
ANISOU 1777  N   TRP A 235     5805   5099   5487    819     85     99       N  
ATOM   1778  CA  TRP A 235      47.345  29.435  26.113  1.00 44.18           C  
ANISOU 1778  CA  TRP A 235     6013   5280   5495    857    110     18       C  
ATOM   1779  C   TRP A 235      48.832  29.354  26.460  1.00 51.29           C  
ANISOU 1779  C   TRP A 235     6946   6233   6309    824      9    -72       C  
ATOM   1780  O   TRP A 235      49.195  29.656  27.598  1.00 57.84           O  
ANISOU 1780  O   TRP A 235     7843   7110   7025    844      6   -161       O  
ATOM   1781  CB  TRP A 235      46.571  28.368  26.892  1.00 43.85           C  
ANISOU 1781  CB  TRP A 235     5984   5301   5377    905    165    106       C  
ATOM   1782  CG  TRP A 235      46.886  26.967  26.478  1.00 55.69           C  
ANISOU 1782  CG  TRP A 235     7458   6832   6869    881     99    195       C  
ATOM   1783  CD1 TRP A 235      46.248  26.236  25.514  1.00 64.08           C  
ANISOU 1783  CD1 TRP A 235     8460   7859   8029    852     93    297       C  
ATOM   1784  CD2 TRP A 235      47.906  26.111  27.021  1.00 53.87           C  
ANISOU 1784  CD2 TRP A 235     7269   6669   6532    890     27    188       C  
ATOM   1785  NE1 TRP A 235      46.814  24.983  25.418  1.00 62.16           N  
ANISOU 1785  NE1 TRP A 235     8230   7637   7751    841     30    341       N  
ATOM   1786  CE2 TRP A 235      47.828  24.881  26.337  1.00 57.98           C  
ANISOU 1786  CE2 TRP A 235     7758   7171   7102    873     -7    286       C  
ATOM   1787  CE3 TRP A 235      48.873  26.267  28.017  1.00 54.56           C  
ANISOU 1787  CE3 TRP A 235     7414   6832   6486    912    -20    108       C  
ATOM   1788  CZ2 TRP A 235      48.686  23.817  26.614  1.00 64.19           C  
ANISOU 1788  CZ2 TRP A 235     8571   7996   7822    892    -71    315       C  
ATOM   1789  CZ3 TRP A 235      49.726  25.211  28.290  1.00 57.96           C  
ANISOU 1789  CZ3 TRP A 235     7855   7323   6843    930    -95    148       C  
ATOM   1790  CH2 TRP A 235      49.629  24.005  27.590  1.00 63.41           C  
ANISOU 1790  CH2 TRP A 235     8515   7979   7599    927   -113    254       C  
ATOM   1791  N   CYS A 236      49.695  28.938  25.521  1.00 47.51           N  
ANISOU 1791  N   CYS A 236     6417   5760   5874    778    -74    -49       N  
ATOM   1792  CA  CYS A 236      51.142  28.956  25.694  1.00 46.72           C  
ANISOU 1792  CA  CYS A 236     6313   5714   5724    744   -170   -123       C  
ATOM   1793  C   CYS A 236      51.815  29.644  24.519  1.00 48.38           C  
ANISOU 1793  C   CYS A 236     6462   5873   6046    679   -203   -141       C  
ATOM   1794  O   CYS A 236      52.927  29.275  24.130  1.00 48.87           O  
ANISOU 1794  O   CYS A 236     6479   5984   6106    652   -274   -145       O  
ATOM   1795  CB  CYS A 236      51.707  27.539  25.854  1.00 44.20           C  
ANISOU 1795  CB  CYS A 236     5984   5477   5332    775   -229    -59       C  
ATOM   1796  SG  CYS A 236      53.378  27.549  26.613  1.00 63.90           S  
ANISOU 1796  SG  CYS A 236     8471   8080   7728    763   -346   -146       S  
ATOM   1797  N   ALA A 237      51.156  30.627  23.922  1.00 46.62           N  
ANISOU 1797  N   ALA A 237     6233   5555   5926    660   -145   -138       N  
ATOM   1798  CA  ALA A 237      51.669  31.229  22.706  1.00 45.29           C  
ANISOU 1798  CA  ALA A 237     6009   5337   5863    602   -162   -120       C  
ATOM   1799  C   ALA A 237      52.024  32.697  22.846  1.00 54.14           C  
ANISOU 1799  C   ALA A 237     7145   6373   7054    549   -150   -207       C  
ATOM   1800  O   ALA A 237      52.825  33.190  22.048  1.00 54.14           O  
ANISOU 1800  O   ALA A 237     7095   6348   7128    485   -176   -202       O  
ATOM   1801  CB  ALA A 237      50.657  31.080  21.558  1.00 40.75           C  
ANISOU 1801  CB  ALA A 237     5401   4717   5365    618   -117     -8       C  
ATOM   1802  N   GLY A 238      51.474  33.404  23.827  1.00 59.83           N  
ANISOU 1802  N   GLY A 238     7936   7042   7756    574   -104   -288       N  
ATOM   1803  CA  GLY A 238      51.714  34.832  23.897  1.00 69.54           C  
ANISOU 1803  CA  GLY A 238     9195   8154   9074    524    -85   -377       C  
ATOM   1804  C   GLY A 238      51.282  35.604  22.661  1.00 69.70           C  
ANISOU 1804  C   GLY A 238     9177   8059   9249    508    -33   -288       C  
ATOM   1805  O   GLY A 238      52.056  36.406  22.131  1.00 67.81           O  
ANISOU 1805  O   GLY A 238     8913   7752   9101    429    -54   -305       O  
ATOM   1806  N   PHE A 239      50.078  35.349  22.157  1.00 66.79           N  
ANISOU 1806  N   PHE A 239     8791   7674   8911    579     30   -178       N  
ATOM   1807  CA  PHE A 239      49.565  36.110  21.023  1.00 63.86           C  
ANISOU 1807  CA  PHE A 239     8384   7205   8675    580     74    -78       C  
ATOM   1808  C   PHE A 239      49.101  37.475  21.517  1.00 65.80           C  
ANISOU 1808  C   PHE A 239     8691   7295   9016    604    149   -144       C  
ATOM   1809  O   PHE A 239      48.158  37.553  22.312  1.00 70.28           O  
ANISOU 1809  O   PHE A 239     9301   7842   9559    688    218   -176       O  
ATOM   1810  CB  PHE A 239      48.397  35.380  20.355  1.00 58.89           C  
ANISOU 1810  CB  PHE A 239     7705   6622   8047    644     98     60       C  
ATOM   1811  CG  PHE A 239      48.781  34.123  19.613  1.00 54.54           C  
ANISOU 1811  CG  PHE A 239     7106   6190   7428    618     29    127       C  
ATOM   1812  CD1 PHE A 239      49.999  34.018  18.956  1.00 50.25           C  
ANISOU 1812  CD1 PHE A 239     6537   5682   6875    552    -26    121       C  
ATOM   1813  CD2 PHE A 239      47.897  33.041  19.559  1.00 58.50           C  
ANISOU 1813  CD2 PHE A 239     7584   6760   7881    661     26    195       C  
ATOM   1814  CE1 PHE A 239      50.351  32.834  18.266  1.00 50.67           C  
ANISOU 1814  CE1 PHE A 239     6555   5836   6860    545    -77    170       C  
ATOM   1815  CE2 PHE A 239      48.226  31.868  18.868  1.00 54.77           C  
ANISOU 1815  CE2 PHE A 239     7084   6373   7352    638    -37    240       C  
ATOM   1816  CZ  PHE A 239      49.454  31.763  18.221  1.00 52.58           C  
ANISOU 1816  CZ  PHE A 239     6795   6128   7054    588    -84    222       C  
ATOM   1817  N   GLY A 240      49.707  38.551  21.002  1.00 67.90           N  
ANISOU 1817  N   GLY A 240     8960   7441   9397    538    150   -155       N  
ATOM   1818  CA  GLY A 240      49.297  39.892  21.364  1.00 75.58           C  
ANISOU 1818  CA  GLY A 240    10000   8231  10485    561    225   -216       C  
ATOM   1819  C   GLY A 240      48.037  40.332  20.631  1.00 79.69           C  
ANISOU 1819  C   GLY A 240    10492   8671  11115    658    308    -71       C  
ATOM   1820  O   GLY A 240      47.473  39.620  19.800  1.00 78.03           O  
ANISOU 1820  O   GLY A 240    10206   8556  10888    693    295     75       O  
ATOM   1821  N   GLU A 241      47.560  41.528  20.985  1.00 76.22           N  
ANISOU 1821  N   GLU A 241    10117   8051  10791    706    392   -119       N  
ATOM   1822  CA  GLU A 241      46.400  42.063  20.278  1.00 71.62           C  
ANISOU 1822  CA  GLU A 241     9497   7383  10333    810    470     31       C  
ATOM   1823  C   GLU A 241      46.752  42.412  18.838  1.00 64.04           C  
ANISOU 1823  C   GLU A 241     8474   6388   9470    756    437    196       C  
ATOM   1824  O   GLU A 241      45.901  42.322  17.950  1.00 61.16           O  
ANISOU 1824  O   GLU A 241     8037   6052   9147    826    451    369       O  
ATOM   1825  CB  GLU A 241      45.839  43.289  20.992  1.00 82.71           C  
ANISOU 1825  CB  GLU A 241    10992   8584  11851    892    580    -59       C  
ATOM   1826  CG  GLU A 241      44.484  43.710  20.452  1.00 95.15           C  
ANISOU 1826  CG  GLU A 241    12512  10096  13546   1036    670    101       C  
ATOM   1827  CD  GLU A 241      44.087  45.101  20.885  1.00111.12           C  
ANISOU 1827  CD  GLU A 241    14625  11872  15724   1119    784     34       C  
ATOM   1828  OE1 GLU A 241      44.784  46.064  20.493  1.00117.72           O  
ANISOU 1828  OE1 GLU A 241    15513  12531  16685   1046    779     22       O  
ATOM   1829  OE2 GLU A 241      43.089  45.232  21.627  1.00115.99           O  
ANISOU 1829  OE2 GLU A 241    15261  12466  16343   1257    888     -6       O  
ATOM   1830  N   SER A 242      47.999  42.802  18.588  1.00 56.43           N  
ANISOU 1830  N   SER A 242     7528   5376   8537    630    392    152       N  
ATOM   1831  CA  SER A 242      48.421  43.043  17.224  1.00 61.95           C  
ANISOU 1831  CA  SER A 242     8166   6069   9303    575    370    317       C  
ATOM   1832  C   SER A 242      48.444  41.757  16.400  1.00 62.19           C  
ANISOU 1832  C   SER A 242     8110   6320   9200    569    301    426       C  
ATOM   1833  O   SER A 242      48.402  41.823  15.166  1.00 67.58           O  
ANISOU 1833  O   SER A 242     8741   7031   9905    565    293    591       O  
ATOM   1834  CB  SER A 242      49.789  43.724  17.218  1.00 67.51           C  
ANISOU 1834  CB  SER A 242     8895   6679  10077    431    348    245       C  
ATOM   1835  OG  SER A 242      50.735  42.900  17.860  1.00 84.43           O  
ANISOU 1835  OG  SER A 242    11028   8960  12091    349    270    109       O  
ATOM   1836  N   PHE A 243      48.562  40.598  17.043  1.00 58.33           N  
ANISOU 1836  N   PHE A 243     7615   5982   8566    567    252    335       N  
ATOM   1837  CA  PHE A 243      48.472  39.345  16.306  1.00 53.70           C  
ANISOU 1837  CA  PHE A 243     6963   5578   7863    572    192    423       C  
ATOM   1838  C   PHE A 243      47.079  39.177  15.708  1.00 50.07           C  
ANISOU 1838  C   PHE A 243     6458   5144   7421    669    210    564       C  
ATOM   1839  O   PHE A 243      46.920  39.025  14.493  1.00 51.19           O  
ANISOU 1839  O   PHE A 243     6551   5345   7555    667    180    705       O  
ATOM   1840  CB  PHE A 243      48.826  38.166  17.221  1.00 50.02           C  
ANISOU 1840  CB  PHE A 243     6509   5239   7259    559    144    302       C  
ATOM   1841  CG  PHE A 243      48.572  36.823  16.598  1.00 46.90           C  
ANISOU 1841  CG  PHE A 243     6063   5000   6756    575     90    376       C  
ATOM   1842  CD1 PHE A 243      49.507  36.256  15.733  1.00 48.53           C  
ANISOU 1842  CD1 PHE A 243     6237   5297   6905    516     39    409       C  
ATOM   1843  CD2 PHE A 243      47.411  36.124  16.872  1.00 44.93           C  
ANISOU 1843  CD2 PHE A 243     5799   4802   6469    645     96    408       C  
ATOM   1844  CE1 PHE A 243      49.275  35.033  15.139  1.00 43.20           C  
ANISOU 1844  CE1 PHE A 243     5535   4746   6133    532     -8    458       C  
ATOM   1845  CE2 PHE A 243      47.169  34.894  16.280  1.00 49.61           C  
ANISOU 1845  CE2 PHE A 243     6354   5517   6978    643     40    466       C  
ATOM   1846  CZ  PHE A 243      48.111  34.342  15.415  1.00 49.94           C  
ANISOU 1846  CZ  PHE A 243     6384   5635   6958    588    -15    481       C  
ATOM   1847  N   TYR A 244      46.054  39.240  16.550  1.00 50.88           N  
ANISOU 1847  N   TYR A 244     6573   5213   7547    755    259    530       N  
ATOM   1848  CA  TYR A 244      44.691  39.027  16.083  1.00 54.47           C  
ANISOU 1848  CA  TYR A 244     6960   5709   8029    845    271    665       C  
ATOM   1849  C   TYR A 244      44.215  40.149  15.159  1.00 57.01           C  
ANISOU 1849  C   TYR A 244     7254   5924   8485    893    305    815       C  
ATOM   1850  O   TYR A 244      43.419  39.900  14.248  1.00 55.40           O  
ANISOU 1850  O   TYR A 244     6973   5796   8282    935    269    968       O  
ATOM   1851  CB  TYR A 244      43.763  38.883  17.282  1.00 49.44           C  
ANISOU 1851  CB  TYR A 244     6330   5062   7393    930    337    596       C  
ATOM   1852  CG  TYR A 244      43.921  37.582  18.038  1.00 52.03           C  
ANISOU 1852  CG  TYR A 244     6665   5522   7580    900    301    509       C  
ATOM   1853  CD1 TYR A 244      43.453  36.377  17.503  1.00 49.71           C  
ANISOU 1853  CD1 TYR A 244     6302   5368   7219    886    236    593       C  
ATOM   1854  CD2 TYR A 244      44.546  37.549  19.286  1.00 56.34           C  
ANISOU 1854  CD2 TYR A 244     7294   6052   8060    883    325    346       C  
ATOM   1855  CE1 TYR A 244      43.599  35.173  18.187  1.00 51.79           C  
ANISOU 1855  CE1 TYR A 244     6578   5730   7370    860    208    528       C  
ATOM   1856  CE2 TYR A 244      44.689  36.343  19.993  1.00 59.23           C  
ANISOU 1856  CE2 TYR A 244     7669   6541   8295    866    293    290       C  
ATOM   1857  CZ  TYR A 244      44.220  35.161  19.437  1.00 61.62           C  
ANISOU 1857  CZ  TYR A 244     7903   6961   8551    856    241    387       C  
ATOM   1858  OH  TYR A 244      44.352  33.969  20.130  1.00 55.90           O  
ANISOU 1858  OH  TYR A 244     7192   6333   7714    841    216    346       O  
ATOM   1859  N   ASN A 245      44.694  41.380  15.352  1.00 61.71           N  
ANISOU 1859  N   ASN A 245     7910   6341   9195    886    365    780       N  
ATOM   1860  CA  ASN A 245      44.270  42.471  14.479  1.00 63.88           C  
ANISOU 1860  CA  ASN A 245     8166   6495   9609    939    404    941       C  
ATOM   1861  C   ASN A 245      44.781  42.271  13.061  1.00 61.58           C  
ANISOU 1861  C   ASN A 245     7833   6296   9270    875    336   1091       C  
ATOM   1862  O   ASN A 245      44.079  42.585  12.090  1.00 64.21           O  
ANISOU 1862  O   ASN A 245     8111   6641   9643    937    326   1277       O  
ATOM   1863  CB  ASN A 245      44.746  43.814  15.034  1.00 71.80           C  
ANISOU 1863  CB  ASN A 245     9260   7261  10759    931    487    859       C  
ATOM   1864  CG  ASN A 245      43.919  44.282  16.217  1.00 84.28           C  
ANISOU 1864  CG  ASN A 245    10888   8727  12409   1041    580    750       C  
ATOM   1865  OD1 ASN A 245      42.739  43.943  16.342  1.00 86.41           O  
ANISOU 1865  OD1 ASN A 245    11093   9063  12674   1156    606    815       O  
ATOM   1866  ND2 ASN A 245      44.533  45.065  17.092  1.00 95.76           N  
ANISOU 1866  ND2 ASN A 245    12450  10011  13925   1004    631    581       N  
ATOM   1867  N   ALA A 246      46.002  41.753  12.923  1.00 57.24           N  
ANISOU 1867  N   ALA A 246     7303   5820   8626    759    290   1017       N  
ATOM   1868  CA  ALA A 246      46.566  41.513  11.607  1.00 47.91           C  
ANISOU 1868  CA  ALA A 246     6088   4739   7376    703    242   1146       C  
ATOM   1869  C   ALA A 246      45.947  40.280  10.964  1.00 54.48           C  
ANISOU 1869  C   ALA A 246     6863   5775   8062    729    160   1206       C  
ATOM   1870  O   ALA A 246      45.724  40.260   9.747  1.00 56.96           O  
ANISOU 1870  O   ALA A 246     7143   6168   8332    741    124   1362       O  
ATOM   1871  CB  ALA A 246      48.082  41.354  11.724  1.00 38.46           C  
ANISOU 1871  CB  ALA A 246     4917   3560   6136    581    234   1043       C  
ATOM   1872  N   TYR A 247      45.668  39.251  11.775  1.00 50.29           N  
ANISOU 1872  N   TYR A 247     6328   5326   7453    735    129   1084       N  
ATOM   1873  CA  TYR A 247      45.040  38.031  11.276  1.00 45.06           C  
ANISOU 1873  CA  TYR A 247     5617   4832   6671    745     48   1122       C  
ATOM   1874  C   TYR A 247      43.681  38.329  10.642  1.00 48.58           C  
ANISOU 1874  C   TYR A 247     5994   5296   7168    827     28   1284       C  
ATOM   1875  O   TYR A 247      43.424  37.959   9.489  1.00 51.74           O  
ANISOU 1875  O   TYR A 247     6357   5812   7489    820    -46   1397       O  
ATOM   1876  CB  TYR A 247      44.900  36.999  12.409  1.00 36.54           C  
ANISOU 1876  CB  TYR A 247     4548   3801   5533    740     36    977       C  
ATOM   1877  CG  TYR A 247      44.400  35.687  11.873  1.00 47.57           C  
ANISOU 1877  CG  TYR A 247     5906   5349   6820    726    -50   1004       C  
ATOM   1878  CD1 TYR A 247      43.032  35.450  11.707  1.00 47.61           C  
ANISOU 1878  CD1 TYR A 247     5839   5397   6854    776    -80   1093       C  
ATOM   1879  CD2 TYR A 247      45.299  34.694  11.471  1.00 44.69           C  
ANISOU 1879  CD2 TYR A 247     5571   5079   6330    662   -104    944       C  
ATOM   1880  CE1 TYR A 247      42.565  34.246  11.165  1.00 48.48           C  
ANISOU 1880  CE1 TYR A 247     5913   5634   6871    743   -174   1111       C  
ATOM   1881  CE2 TYR A 247      44.842  33.484  10.935  1.00 42.37           C  
ANISOU 1881  CE2 TYR A 247     5259   4900   5940    644   -186    954       C  
ATOM   1882  CZ  TYR A 247      43.474  33.269  10.778  1.00 47.64           C  
ANISOU 1882  CZ  TYR A 247     5861   5602   6639    675   -227   1033       C  
ATOM   1883  OH  TYR A 247      43.010  32.087  10.227  1.00 48.62           O  
ANISOU 1883  OH  TYR A 247     5966   5828   6678    638   -320   1035       O  
ATOM   1884  N   PHE A 248      42.793  38.991  11.383  1.00 41.38           N  
ANISOU 1884  N   PHE A 248     5060   4281   6383    912     92   1295       N  
ATOM   1885  CA  PHE A 248      41.438  39.206  10.882  1.00 45.93           C  
ANISOU 1885  CA  PHE A 248     5542   4889   7019   1002     70   1453       C  
ATOM   1886  C   PHE A 248      41.352  40.268   9.799  1.00 56.16           C  
ANISOU 1886  C   PHE A 248     6823   6132   8383   1045     73   1637       C  
ATOM   1887  O   PHE A 248      40.269  40.453   9.232  1.00 63.22           O  
ANISOU 1887  O   PHE A 248     7629   7074   9318   1123     36   1793       O  
ATOM   1888  CB  PHE A 248      40.502  39.444  12.055  1.00 44.09           C  
ANISOU 1888  CB  PHE A 248     5277   4583   6892   1092    151   1407       C  
ATOM   1889  CG  PHE A 248      40.248  38.180  12.837  1.00 47.16           C  
ANISOU 1889  CG  PHE A 248     5647   5078   7193   1057    126   1295       C  
ATOM   1890  CD1 PHE A 248      39.735  37.055  12.188  1.00 54.01           C  
ANISOU 1890  CD1 PHE A 248     6442   6108   7972   1015     17   1352       C  
ATOM   1891  CD2 PHE A 248      40.613  38.063  14.167  1.00 49.68           C  
ANISOU 1891  CD2 PHE A 248     6033   5339   7504   1054    201   1132       C  
ATOM   1892  CE1 PHE A 248      39.522  35.850  12.875  1.00 50.69           C  
ANISOU 1892  CE1 PHE A 248     6009   5768   7485    972     -4   1263       C  
ATOM   1893  CE2 PHE A 248      40.390  36.864  14.861  1.00 52.42           C  
ANISOU 1893  CE2 PHE A 248     6366   5786   7767   1024    181   1055       C  
ATOM   1894  CZ  PHE A 248      39.845  35.757  14.209  1.00 47.17           C  
ANISOU 1894  CZ  PHE A 248     5623   5261   7038    981     83   1126       C  
ATOM   1895  N   LYS A 249      42.452  40.965   9.496  1.00 54.48           N  
ANISOU 1895  N   LYS A 249     6685   5827   8187    994    113   1637       N  
ATOM   1896  CA  LYS A 249      42.497  41.780   8.281  1.00 50.90           C  
ANISOU 1896  CA  LYS A 249     6222   5355   7762   1016    106   1836       C  
ATOM   1897  C   LYS A 249      42.524  40.904   7.023  1.00 54.01           C  
ANISOU 1897  C   LYS A 249     6584   5965   7973    973     -8   1927       C  
ATOM   1898  O   LYS A 249      41.932  41.263   6.005  1.00 59.25           O  
ANISOU 1898  O   LYS A 249     7202   6687   8624   1027    -54   2119       O  
ATOM   1899  CB  LYS A 249      43.726  42.686   8.292  1.00 50.89           C  
ANISOU 1899  CB  LYS A 249     6304   5202   7832    952    186   1815       C  
ATOM   1900  CG  LYS A 249      43.608  43.995   9.041  1.00 54.95           C  
ANISOU 1900  CG  LYS A 249     6860   5463   8556   1007    295   1803       C  
ATOM   1901  CD  LYS A 249      44.966  44.730   9.062  1.00 58.67           C  
ANISOU 1901  CD  LYS A 249     7408   5793   9090    901    355   1758       C  
ATOM   1902  CE  LYS A 249      44.809  46.184   9.470  1.00 77.99           C  
ANISOU 1902  CE  LYS A 249     9907   7962  11762    953    458   1791       C  
ATOM   1903  NZ  LYS A 249      45.959  46.746  10.240  1.00 86.42           N  
ANISOU 1903  NZ  LYS A 249    11058   8859  12917    840    514   1624       N  
ATOM   1904  N   VAL A 250      43.202  39.752   7.071  1.00 55.96           N  
ANISOU 1904  N   VAL A 250     6860   6333   8069    884    -57   1789       N  
ATOM   1905  CA  VAL A 250      43.298  38.857   5.915  1.00 56.33           C  
ANISOU 1905  CA  VAL A 250     6900   6576   7928    843   -159   1838       C  
ATOM   1906  C   VAL A 250      42.107  37.903   5.830  1.00 54.41           C  
ANISOU 1906  C   VAL A 250     6585   6463   7624    864   -267   1839       C  
ATOM   1907  O   VAL A 250      41.631  37.604   4.733  1.00 52.81           O  
ANISOU 1907  O   VAL A 250     6352   6402   7314    867   -367   1950       O  
ATOM   1908  CB  VAL A 250      44.634  38.066   5.959  1.00 53.31           C  
ANISOU 1908  CB  VAL A 250     6584   6249   7422    748   -150   1688       C  
ATOM   1909  CG1 VAL A 250      44.733  37.042   4.802  1.00 38.37           C  
ANISOU 1909  CG1 VAL A 250     4703   4554   5322    715   -246   1707       C  
ATOM   1910  CG2 VAL A 250      45.814  38.994   5.902  1.00 48.22           C  
ANISOU 1910  CG2 VAL A 250     5984   5498   6840    710    -54   1708       C  
ATOM   1911  N   MET A 251      41.591  37.447   6.971  1.00 53.03           N  
ANISOU 1911  N   MET A 251     6382   6249   7519    874   -252   1725       N  
ATOM   1912  CA  MET A 251      40.558  36.419   7.062  1.00 60.07           C  
ANISOU 1912  CA  MET A 251     7200   7253   8371    868   -344   1707       C  
ATOM   1913  C   MET A 251      39.296  36.943   7.733  1.00 59.61           C  
ANISOU 1913  C   MET A 251     7040   7136   8474    959   -309   1780       C  
ATOM   1914  O   MET A 251      39.381  37.524   8.823  1.00 60.53           O  
ANISOU 1914  O   MET A 251     7177   7112   8708   1005   -193   1714       O  
ATOM   1915  CB  MET A 251      41.042  35.182   7.862  1.00 58.54           C  
ANISOU 1915  CB  MET A 251     7052   7083   8107    794   -349   1515       C  
ATOM   1916  CG  MET A 251      42.123  34.348   7.188  1.00 71.03           C  
ANISOU 1916  CG  MET A 251     8717   8750   9523    715   -396   1433       C  
ATOM   1917  SD  MET A 251      41.460  33.321   5.854  1.00 68.53           S  
ANISOU 1917  SD  MET A 251     8374   8617   9047    671   -559   1483       S  
ATOM   1918  CE  MET A 251      40.281  32.291   6.737  1.00 66.91           C  
ANISOU 1918  CE  MET A 251     8090   8425   8909    646   -614   1421       C  
ATOM   1919  N   PRO A 252      38.129  36.824   7.095  1.00 55.82           N  
ANISOU 1919  N   PRO A 252     6446   6760   8003    995   -402   1916       N  
ATOM   1920  CA  PRO A 252      36.885  37.269   7.748  1.00 58.65           C  
ANISOU 1920  CA  PRO A 252     6682   7077   8525   1093   -360   1994       C  
ATOM   1921  C   PRO A 252      36.497  36.331   8.884  1.00 58.62           C  
ANISOU 1921  C   PRO A 252     6646   7084   8542   1059   -333   1861       C  
ATOM   1922  O   PRO A 252      36.454  35.110   8.719  1.00 59.73           O  
ANISOU 1922  O   PRO A 252     6780   7334   8580    962   -428   1794       O  
ATOM   1923  CB  PRO A 252      35.846  37.239   6.614  1.00 57.38           C  
ANISOU 1923  CB  PRO A 252     6394   7063   8344   1119   -498   2181       C  
ATOM   1924  CG  PRO A 252      36.343  36.157   5.701  1.00 59.92           C  
ANISOU 1924  CG  PRO A 252     6772   7534   8461    996   -636   2121       C  
ATOM   1925  CD  PRO A 252      37.884  36.152   5.807  1.00 51.43           C  
ANISOU 1925  CD  PRO A 252     5863   6381   7297    940   -559   1988       C  
ATOM   1926  N   LYS A 253      36.174  36.929  10.027  1.00 56.21           N  
ANISOU 1926  N   LYS A 253     6325   6660   8372   1145   -197   1831       N  
ATOM   1927  CA  LYS A 253      35.767  36.204  11.221  1.00 48.17           C  
ANISOU 1927  CA  LYS A 253     5278   5646   7380   1134   -139   1726       C  
ATOM   1928  C   LYS A 253      34.345  35.671  11.052  1.00 54.38           C  
ANISOU 1928  C   LYS A 253     5883   6555   8226   1148   -207   1842       C  
ATOM   1929  O   LYS A 253      33.449  36.418  10.632  1.00 57.84           O  
ANISOU 1929  O   LYS A 253     6199   7006   8772   1245   -212   2002       O  
ATOM   1930  CB  LYS A 253      35.839  37.137  12.431  1.00 54.44           C  
ANISOU 1930  CB  LYS A 253     6119   6281   8285   1236     35   1661       C  
ATOM   1931  CG  LYS A 253      35.395  36.515  13.750  1.00 55.89           C  
ANISOU 1931  CG  LYS A 253     6279   6473   8483   1246    121   1566       C  
ATOM   1932  CD  LYS A 253      35.517  37.477  14.949  1.00 48.02           C  
ANISOU 1932  CD  LYS A 253     5354   5324   7566   1352    295   1478       C  
ATOM   1933  CE  LYS A 253      36.948  37.871  15.242  1.00 50.53           C  
ANISOU 1933  CE  LYS A 253     5849   5532   7817   1301    322   1329       C  
ATOM   1934  NZ  LYS A 253      36.994  38.821  16.378  1.00 48.53           N  
ANISOU 1934  NZ  LYS A 253     5671   5129   7637   1397    476   1230       N  
ATOM   1935  N   GLN A 254      34.134  34.380  11.347  1.00 56.28           N  
ANISOU 1935  N   GLN A 254     6095   6882   8406   1047   -263   1773       N  
ATOM   1936  CA  GLN A 254      32.829  33.750  11.179  1.00 51.64           C  
ANISOU 1936  CA  GLN A 254     5325   6416   7881   1026   -341   1876       C  
ATOM   1937  C   GLN A 254      32.078  33.658  12.496  1.00 54.30           C  
ANISOU 1937  C   GLN A 254     5577   6724   8331   1084   -201   1867       C  
ATOM   1938  O   GLN A 254      32.679  33.486  13.556  1.00 49.19           O  
ANISOU 1938  O   GLN A 254     5041   5999   7652   1085    -86   1737       O  
ATOM   1939  CB  GLN A 254      32.922  32.350  10.584  1.00 47.26           C  
ANISOU 1939  CB  GLN A 254     4780   5970   7209    866   -499   1822       C  
ATOM   1940  CG  GLN A 254      33.468  32.299   9.172  1.00 55.90           C  
ANISOU 1940  CG  GLN A 254     5940   7131   8171    808   -649   1839       C  
ATOM   1941  CD  GLN A 254      33.601  30.871   8.653  1.00 60.11           C  
ANISOU 1941  CD  GLN A 254     6507   7750   8583    654   -794   1751       C  
ATOM   1942  OE1 GLN A 254      34.584  30.169   8.932  1.00 64.03           O  
ANISOU 1942  OE1 GLN A 254     7147   8197   8983    590   -772   1603       O  
ATOM   1943  NE2 GLN A 254      32.601  30.438   7.880  1.00 55.95           N  
ANISOU 1943  NE2 GLN A 254     5846   7349   8065    595   -949   1841       N  
ATOM   1944  N   ALA A 255      30.744  33.705  12.392  1.00 52.66           N  
ANISOU 1944  N   ALA A 255     5162   6600   8246   1129   -220   2014       N  
ATOM   1945  CA  ALA A 255      29.854  33.659  13.549  1.00 53.21           C  
ANISOU 1945  CA  ALA A 255     5114   6667   8435   1199    -76   2041       C  
ATOM   1946  C   ALA A 255      30.117  32.444  14.429  1.00 56.78           C  
ANISOU 1946  C   ALA A 255     5624   7129   8820   1087    -42   1922       C  
ATOM   1947  O   ALA A 255      30.250  31.310  13.946  1.00 51.74           O  
ANISOU 1947  O   ALA A 255     4994   6557   8108    935   -181   1891       O  
ATOM   1948  CB  ALA A 255      28.382  33.659  13.093  1.00 47.37           C  
ANISOU 1948  CB  ALA A 255     4109   6055   7835   1230   -141   2232       C  
ATOM   1949  N   GLY A 256      30.126  32.690  15.737  1.00 58.41           N  
ANISOU 1949  N   GLY A 256     5871   7268   9054   1172    147   1862       N  
ATOM   1950  CA  GLY A 256      30.449  31.688  16.729  1.00 54.95           C  
ANISOU 1950  CA  GLY A 256     5508   6827   8542   1095    208   1761       C  
ATOM   1951  C   GLY A 256      31.924  31.534  17.011  1.00 54.88           C  
ANISOU 1951  C   GLY A 256     5736   6735   8382   1051    209   1589       C  
ATOM   1952  O   GLY A 256      32.309  30.572  17.683  1.00 55.26           O  
ANISOU 1952  O   GLY A 256     5856   6789   8353    975    226   1513       O  
ATOM   1953  N   TYR A 257      32.762  32.450  16.514  1.00 49.07           N  
ANISOU 1953  N   TYR A 257     5113   5923   7610   1095    191   1538       N  
ATOM   1954  CA  TYR A 257      34.201  32.340  16.723  1.00 47.24           C  
ANISOU 1954  CA  TYR A 257     5080   5622   7246   1047    183   1384       C  
ATOM   1955  C   TYR A 257      34.560  32.358  18.209  1.00 51.17           C  
ANISOU 1955  C   TYR A 257     5675   6068   7700   1096    333   1272       C  
ATOM   1956  O   TYR A 257      35.357  31.527  18.675  1.00 47.64           O  
ANISOU 1956  O   TYR A 257     5333   5626   7140   1022    314   1173       O  
ATOM   1957  CB  TYR A 257      34.933  33.458  15.977  1.00 48.67           C  
ANISOU 1957  CB  TYR A 257     5340   5726   7425   1089    159   1372       C  
ATOM   1958  CG  TYR A 257      36.301  33.720  16.551  1.00 50.54           C  
ANISOU 1958  CG  TYR A 257     5758   5874   7571   1076    206   1214       C  
ATOM   1959  CD1 TYR A 257      37.365  32.872  16.270  1.00 52.62           C  
ANISOU 1959  CD1 TYR A 257     6119   6165   7710    967    116   1127       C  
ATOM   1960  CD2 TYR A 257      36.529  34.792  17.391  1.00 48.85           C  
ANISOU 1960  CD2 TYR A 257     5614   5549   7397   1173    338   1147       C  
ATOM   1961  CE1 TYR A 257      38.603  33.098  16.794  1.00 48.51           C  
ANISOU 1961  CE1 TYR A 257     5736   5580   7115    954    150    994       C  
ATOM   1962  CE2 TYR A 257      37.787  35.021  17.935  1.00 44.44           C  
ANISOU 1962  CE2 TYR A 257     5211   4919   6757   1144    363    996       C  
ATOM   1963  CZ  TYR A 257      38.816  34.172  17.625  1.00 48.44           C  
ANISOU 1963  CZ  TYR A 257     5788   5471   7147   1034    265    929       C  
ATOM   1964  OH  TYR A 257      40.068  34.385  18.147  1.00 52.64           O  
ANISOU 1964  OH  TYR A 257     6447   5948   7605   1004    278    792       O  
ATOM   1965  N   GLU A 258      34.003  33.314  18.968  1.00 50.06           N  
ANISOU 1965  N   GLU A 258     5507   5878   7637   1230    485   1283       N  
ATOM   1966  CA  GLU A 258      34.304  33.389  20.400  1.00 54.49           C  
ANISOU 1966  CA  GLU A 258     6171   6402   8131   1285    630   1168       C  
ATOM   1967  C   GLU A 258      33.788  32.169  21.134  1.00 55.63           C  
ANISOU 1967  C   GLU A 258     6261   6642   8235   1236    664   1200       C  
ATOM   1968  O   GLU A 258      34.453  31.645  22.037  1.00 52.86           O  
ANISOU 1968  O   GLU A 258     6028   6293   7762   1210    702   1102       O  
ATOM   1969  CB  GLU A 258      33.708  34.648  21.019  1.00 57.17           C  
ANISOU 1969  CB  GLU A 258     6494   6667   8561   1449    795   1168       C  
ATOM   1970  CG  GLU A 258      34.572  35.876  20.840  1.00 75.48           C  
ANISOU 1970  CG  GLU A 258     8946   8844  10888   1495    806   1071       C  
ATOM   1971  CD  GLU A 258      35.895  35.784  21.593  1.00 87.48           C  
ANISOU 1971  CD  GLU A 258    10659  10317  12261   1439    806    883       C  
ATOM   1972  OE1 GLU A 258      36.017  34.945  22.531  1.00 77.62           O  
ANISOU 1972  OE1 GLU A 258     9452   9140  10901   1410    841    824       O  
ATOM   1973  OE2 GLU A 258      36.809  36.577  21.250  1.00 95.66           O  
ANISOU 1973  OE2 GLU A 258    11799  11248  13300   1422    770    805       O  
ATOM   1974  N   LYS A 259      32.610  31.701  20.737  1.00 50.65           N  
ANISOU 1974  N   LYS A 259     5444   6092   7709   1218    644   1349       N  
ATOM   1975  CA  LYS A 259      31.971  30.568  21.382  1.00 52.64           C  
ANISOU 1975  CA  LYS A 259     5616   6427   7958   1162    685   1410       C  
ATOM   1976  C   LYS A 259      32.772  29.274  21.211  1.00 52.69           C  
ANISOU 1976  C   LYS A 259     5716   6446   7859   1011    561   1357       C  
ATOM   1977  O   LYS A 259      32.746  28.412  22.090  1.00 56.65           O  
ANISOU 1977  O   LYS A 259     6243   6975   8306    977    622   1357       O  
ATOM   1978  CB  LYS A 259      30.552  30.438  20.809  1.00 53.04           C  
ANISOU 1978  CB  LYS A 259     5424   6560   8171   1158    664   1588       C  
ATOM   1979  CG  LYS A 259      29.817  29.151  21.110  1.00 64.02           C  
ANISOU 1979  CG  LYS A 259     6693   8034   9596   1052    659   1682       C  
ATOM   1980  CD  LYS A 259      28.521  29.106  20.306  1.00 71.36           C  
ANISOU 1980  CD  LYS A 259     7369   9050  10696   1025    591   1851       C  
ATOM   1981  CE  LYS A 259      27.546  30.172  20.798  1.00 74.54           C  
ANISOU 1981  CE  LYS A 259     7627   9476  11218   1205    766   1942       C  
ATOM   1982  NZ  LYS A 259      26.291  30.174  20.000  1.00 86.07           N  
ANISOU 1982  NZ  LYS A 259     8816  11035  12853   1190    689   2121       N  
ATOM   1983  N   ARG A 260      33.499  29.131  20.107  1.00 52.46           N  
ANISOU 1983  N   ARG A 260     5743   6393   7795    930    399   1317       N  
ATOM   1984  CA  ARG A 260      34.203  27.901  19.785  1.00 48.12           C  
ANISOU 1984  CA  ARG A 260     5273   5847   7162    798    279   1269       C  
ATOM   1985  C   ARG A 260      35.646  27.871  20.267  1.00 43.92           C  
ANISOU 1985  C   ARG A 260     4936   5262   6489    804    284   1124       C  
ATOM   1986  O   ARG A 260      36.322  26.862  20.059  1.00 46.41           O  
ANISOU 1986  O   ARG A 260     5326   5573   6736    716    198   1081       O  
ATOM   1987  CB  ARG A 260      34.182  27.658  18.274  1.00 50.58           C  
ANISOU 1987  CB  ARG A 260     5539   6180   7500    708    100   1300       C  
ATOM   1988  CG  ARG A 260      32.835  27.233  17.696  1.00 48.33           C  
ANISOU 1988  CG  ARG A 260     5057   5968   7338    648     35   1438       C  
ATOM   1989  CD  ARG A 260      32.944  26.894  16.208  1.00 49.98           C  
ANISOU 1989  CD  ARG A 260     5254   6207   7529    549   -162   1442       C  
ATOM   1990  NE  ARG A 260      33.276  28.060  15.365  1.00 52.07           N  
ANISOU 1990  NE  ARG A 260     5539   6469   7778    623   -200   1446       N  
ATOM   1991  CZ  ARG A 260      32.374  28.890  14.833  1.00 55.97           C  
ANISOU 1991  CZ  ARG A 260     5886   7010   8369    685   -216   1567       C  
ATOM   1992  NH1 ARG A 260      31.082  28.697  15.062  1.00 54.59           N  
ANISOU 1992  NH1 ARG A 260     5520   6901   8319    683   -198   1687       N  
ATOM   1993  NH2 ARG A 260      32.760  29.917  14.082  1.00 47.73           N  
ANISOU 1993  NH2 ARG A 260     4879   5949   7307    752   -245   1581       N  
ATOM   1994  N   ARG A 261      36.158  28.951  20.857  1.00 48.91           N  
ANISOU 1994  N   ARG A 261     5651   5850   7084    903    375   1045       N  
ATOM   1995  CA  ARG A 261      37.584  28.991  21.175  1.00 44.56           C  
ANISOU 1995  CA  ARG A 261     5264   5259   6409    893    352    909       C  
ATOM   1996  C   ARG A 261      37.983  27.856  22.111  1.00 49.54           C  
ANISOU 1996  C   ARG A 261     5966   5919   6940    858    369    880       C  
ATOM   1997  O   ARG A 261      38.986  27.169  21.877  1.00 53.52           O  
ANISOU 1997  O   ARG A 261     6554   6415   7367    799    280    821       O  
ATOM   1998  CB  ARG A 261      37.956  30.349  21.768  1.00 42.83           C  
ANISOU 1998  CB  ARG A 261     5116   4981   6178    993    447    822       C  
ATOM   1999  CG  ARG A 261      38.118  31.438  20.735  1.00 54.71           C  
ANISOU 1999  CG  ARG A 261     6604   6425   7758   1011    403    829       C  
ATOM   2000  CD  ARG A 261      38.175  32.794  21.381  1.00 60.82           C  
ANISOU 2000  CD  ARG A 261     7433   7115   8562   1114    517    760       C  
ATOM   2001  NE  ARG A 261      39.498  33.061  21.926  1.00 76.28           N  
ANISOU 2001  NE  ARG A 261     9538   9028  10416   1091    507    608       N  
ATOM   2002  CZ  ARG A 261      39.755  34.054  22.768  1.00 77.62           C  
ANISOU 2002  CZ  ARG A 261     9794   9123  10575   1159    598    500       C  
ATOM   2003  NH1 ARG A 261      38.763  34.848  23.149  1.00 73.94           N  
ANISOU 2003  NH1 ARG A 261     9289   8612  10194   1270    723    529       N  
ATOM   2004  NH2 ARG A 261      40.987  34.244  23.233  1.00 76.18           N  
ANISOU 2004  NH2 ARG A 261     9733   8913  10299   1118    564    360       N  
ATOM   2005  N   ASP A 262      37.202  27.632  23.173  1.00 46.98           N  
ANISOU 2005  N   ASP A 262     5605   5631   6616    903    491    932       N  
ATOM   2006  CA  ASP A 262      37.518  26.562  24.125  1.00 46.70           C  
ANISOU 2006  CA  ASP A 262     5637   5626   6481    879    520    932       C  
ATOM   2007  C   ASP A 262      37.418  25.178  23.502  1.00 48.63           C  
ANISOU 2007  C   ASP A 262     5847   5869   6762    764    416   1003       C  
ATOM   2008  O   ASP A 262      38.176  24.275  23.869  1.00 52.57           O  
ANISOU 2008  O   ASP A 262     6439   6359   7176    731    380    976       O  
ATOM   2009  CB  ASP A 262      36.606  26.671  25.346  1.00 52.22           C  
ANISOU 2009  CB  ASP A 262     6297   6375   7171    957    691    993       C  
ATOM   2010  CG  ASP A 262      37.096  27.716  26.338  1.00 66.39           C  
ANISOU 2010  CG  ASP A 262     8202   8166   8855   1068    793    874       C  
ATOM   2011  OD1 ASP A 262      38.226  28.245  26.156  1.00 67.01           O  
ANISOU 2011  OD1 ASP A 262     8389   8202   8869   1066    718    746       O  
ATOM   2012  OD2 ASP A 262      36.346  28.029  27.284  1.00 70.28           O  
ANISOU 2012  OD2 ASP A 262     8673   8701   9331   1155    949    904       O  
ATOM   2013  N   LEU A 263      36.518  24.995  22.540  1.00 49.12           N  
ANISOU 2013  N   LEU A 263     5779   5935   6950    702    357   1089       N  
ATOM   2014  CA  LEU A 263      36.411  23.702  21.882  1.00 48.35           C  
ANISOU 2014  CA  LEU A 263     5660   5820   6891    580    246   1133       C  
ATOM   2015  C   LEU A 263      37.719  23.302  21.203  1.00 45.88           C  
ANISOU 2015  C   LEU A 263     5475   5462   6495    541    124   1025       C  
ATOM   2016  O   LEU A 263      38.062  22.114  21.167  1.00 46.07           O  
ANISOU 2016  O   LEU A 263     5554   5450   6501    475     70   1024       O  
ATOM   2017  CB  LEU A 263      35.280  23.754  20.867  1.00 51.66           C  
ANISOU 2017  CB  LEU A 263     5917   6263   7448    518    179   1222       C  
ATOM   2018  CG  LEU A 263      34.852  22.433  20.245  1.00 59.83           C  
ANISOU 2018  CG  LEU A 263     6905   7278   8548    374     69   1273       C  
ATOM   2019  CD1 LEU A 263      34.113  21.571  21.252  1.00 62.94           C  
ANISOU 2019  CD1 LEU A 263     7242   7676   8998    336    167   1379       C  
ATOM   2020  CD2 LEU A 263      33.999  22.722  19.009  1.00 59.92           C  
ANISOU 2020  CD2 LEU A 263     6775   7329   8661    316    -43   1325       C  
ATOM   2021  N   TYR A 264      38.463  24.271  20.665  1.00 43.94           N  
ANISOU 2021  N   TYR A 264     5276   5211   6208    585     89    941       N  
ATOM   2022  CA  TYR A 264      39.734  23.971  20.009  1.00 45.96           C  
ANISOU 2022  CA  TYR A 264     5637   5439   6387    559     -9    846       C  
ATOM   2023  C   TYR A 264      40.895  23.930  20.988  1.00 42.19           C  
ANISOU 2023  C   TYR A 264     5276   4956   5798    613     33    766       C  
ATOM   2024  O   TYR A 264      41.859  23.204  20.746  1.00 45.39           O  
ANISOU 2024  O   TYR A 264     5758   5341   6147    590    -33    715       O  
ATOM   2025  CB  TYR A 264      40.029  24.981  18.875  1.00 42.36           C  
ANISOU 2025  CB  TYR A 264     5167   4987   5942    568    -68    811       C  
ATOM   2026  CG  TYR A 264      39.022  24.870  17.740  1.00 47.74           C  
ANISOU 2026  CG  TYR A 264     5741   5690   6707    508   -148    889       C  
ATOM   2027  CD1 TYR A 264      38.751  23.642  17.151  1.00 43.91           C  
ANISOU 2027  CD1 TYR A 264     5249   5200   6234    412   -241    903       C  
ATOM   2028  CD2 TYR A 264      38.271  25.980  17.323  1.00 43.62           C  
ANISOU 2028  CD2 TYR A 264     5122   5193   6257    550   -131    953       C  
ATOM   2029  CE1 TYR A 264      37.794  23.525  16.125  1.00 42.55           C  
ANISOU 2029  CE1 TYR A 264     4975   5063   6130    343   -335    966       C  
ATOM   2030  CE2 TYR A 264      37.313  25.871  16.312  1.00 42.57           C  
ANISOU 2030  CE2 TYR A 264     4877   5103   6194    497   -219   1036       C  
ATOM   2031  CZ  TYR A 264      37.080  24.636  15.718  1.00 47.76           C  
ANISOU 2031  CZ  TYR A 264     5528   5771   6849    387   -328   1037       C  
ATOM   2032  OH  TYR A 264      36.142  24.499  14.708  1.00 51.83           O  
ANISOU 2032  OH  TYR A 264     5932   6339   7422    321   -438   1108       O  
ATOM   2033  N   LEU A 265      40.826  24.671  22.095  1.00 36.86           N  
ANISOU 2033  N   LEU A 265     4617   4303   5087    688    137    753       N  
ATOM   2034  CA  LEU A 265      41.780  24.437  23.176  1.00 45.52           C  
ANISOU 2034  CA  LEU A 265     5817   5415   6064    730    165    692       C  
ATOM   2035  C   LEU A 265      41.657  23.014  23.708  1.00 49.18           C  
ANISOU 2035  C   LEU A 265     6304   5877   6504    701    167    763       C  
ATOM   2036  O   LEU A 265      42.663  22.382  24.055  1.00 46.95           O  
ANISOU 2036  O   LEU A 265     6105   5594   6138    712    128    727       O  
ATOM   2037  CB  LEU A 265      41.560  25.434  24.319  1.00 39.96           C  
ANISOU 2037  CB  LEU A 265     5133   4741   5310    813    281    660       C  
ATOM   2038  CG  LEU A 265      41.872  26.898  24.028  1.00 48.09           C  
ANISOU 2038  CG  LEU A 265     6171   5742   6358    850    289    572       C  
ATOM   2039  CD1 LEU A 265      41.315  27.792  25.124  1.00 50.15           C  
ANISOU 2039  CD1 LEU A 265     6448   6015   6593    935    421    545       C  
ATOM   2040  CD2 LEU A 265      43.346  27.113  23.882  1.00 52.30           C  
ANISOU 2040  CD2 LEU A 265     6784   6267   6819    834    208    463       C  
ATOM   2041  N   LEU A 266      40.426  22.491  23.742  1.00 43.53           N  
ANISOU 2041  N   LEU A 266     5505   5158   5875    663    211    874       N  
ATOM   2042  CA  LEU A 266      40.132  21.230  24.416  1.00 42.14           C  
ANISOU 2042  CA  LEU A 266     5345   4970   5696    633    242    967       C  
ATOM   2043  C   LEU A 266      40.913  20.074  23.820  1.00 43.59           C  
ANISOU 2043  C   LEU A 266     5597   5088   5879    578    134    946       C  
ATOM   2044  O   LEU A 266      41.403  19.207  24.553  1.00 54.51           O  
ANISOU 2044  O   LEU A 266     7054   6454   7203    597    147    978       O  
ATOM   2045  CB  LEU A 266      38.628  20.955  24.342  1.00 40.04           C  
ANISOU 2045  CB  LEU A 266     4948   4707   5557    578    297   1094       C  
ATOM   2046  CG  LEU A 266      38.119  19.613  24.849  1.00 46.38           C  
ANISOU 2046  CG  LEU A 266     5741   5478   6403    515    329   1215       C  
ATOM   2047  CD1 LEU A 266      38.464  19.444  26.348  1.00 37.65           C  
ANISOU 2047  CD1 LEU A 266     4720   4420   5167    599    445   1254       C  
ATOM   2048  CD2 LEU A 266      36.601  19.512  24.611  1.00 44.62           C  
ANISOU 2048  CD2 LEU A 266     5353   5268   6332    444    372   1337       C  
ATOM   2049  N   TYR A 267      41.047  20.042  22.493  1.00 42.64           N  
ANISOU 2049  N   TYR A 267     5457   4928   5816    521     29    895       N  
ATOM   2050  CA  TYR A 267      41.838  18.989  21.855  1.00 44.16           C  
ANISOU 2050  CA  TYR A 267     5726   5051   6002    484    -64    853       C  
ATOM   2051  C   TYR A 267      43.248  18.928  22.425  1.00 42.15           C  
ANISOU 2051  C   TYR A 267     5572   4811   5632    566    -68    789       C  
ATOM   2052  O   TYR A 267      43.769  17.847  22.701  1.00 43.41           O  
ANISOU 2052  O   TYR A 267     5801   4919   5775    575    -86    809       O  
ATOM   2053  CB  TYR A 267      41.908  19.227  20.353  1.00 41.91           C  
ANISOU 2053  CB  TYR A 267     5418   4751   5753    433   -164    785       C  
ATOM   2054  CG  TYR A 267      42.836  18.294  19.601  1.00 47.43           C  
ANISOU 2054  CG  TYR A 267     6208   5386   6428    417   -249    713       C  
ATOM   2055  CD1 TYR A 267      42.551  16.925  19.496  1.00 45.77           C  
ANISOU 2055  CD1 TYR A 267     6036   5079   6277    353   -281    744       C  
ATOM   2056  CD2 TYR A 267      43.986  18.782  18.965  1.00 43.47           C  
ANISOU 2056  CD2 TYR A 267     5752   4912   5854    464   -288    615       C  
ATOM   2057  CE1 TYR A 267      43.398  16.063  18.784  1.00 49.06           C  
ANISOU 2057  CE1 TYR A 267     6547   5421   6674    353   -347    665       C  
ATOM   2058  CE2 TYR A 267      44.846  17.925  18.240  1.00 44.22           C  
ANISOU 2058  CE2 TYR A 267     5924   4953   5923    467   -348    546       C  
ATOM   2059  CZ  TYR A 267      44.545  16.569  18.159  1.00 51.68           C  
ANISOU 2059  CZ  TYR A 267     6919   5796   6921    419   -376    565       C  
ATOM   2060  OH  TYR A 267      45.367  15.714  17.435  1.00 50.88           O  
ANISOU 2060  OH  TYR A 267     6906   5626   6799    434   -424    485       O  
ATOM   2061  N   HIS A 268      43.884  20.088  22.598  1.00 41.71           N  
ANISOU 2061  N   HIS A 268     5521   4820   5505    626    -55    715       N  
ATOM   2062  CA  HIS A 268      45.237  20.130  23.117  1.00 42.92           C  
ANISOU 2062  CA  HIS A 268     5747   5006   5556    693    -75    651       C  
ATOM   2063  C   HIS A 268      45.293  19.866  24.614  1.00 46.53           C  
ANISOU 2063  C   HIS A 268     6247   5506   5927    751    -10    704       C  
ATOM   2064  O   HIS A 268      46.245  19.235  25.084  1.00 49.88           O  
ANISOU 2064  O   HIS A 268     6732   5939   6280    797    -42    702       O  
ATOM   2065  CB  HIS A 268      45.869  21.475  22.764  1.00 40.14           C  
ANISOU 2065  CB  HIS A 268     5378   4700   5173    714    -90    553       C  
ATOM   2066  CG  HIS A 268      46.083  21.638  21.299  1.00 43.28           C  
ANISOU 2066  CG  HIS A 268     5750   5069   5624    671   -156    511       C  
ATOM   2067  ND1 HIS A 268      47.068  20.951  20.620  1.00 37.85           N  
ANISOU 2067  ND1 HIS A 268     5100   4363   4917    675   -218    468       N  
ATOM   2068  CD2 HIS A 268      45.407  22.356  20.366  1.00 42.51           C  
ANISOU 2068  CD2 HIS A 268     5595   4966   5590    632   -164    515       C  
ATOM   2069  CE1 HIS A 268      47.013  21.265  19.338  1.00 37.07           C  
ANISOU 2069  CE1 HIS A 268     4977   4256   4853    636   -257    439       C  
ATOM   2070  NE2 HIS A 268      46.010  22.112  19.156  1.00 42.73           N  
ANISOU 2070  NE2 HIS A 268     5635   4982   5619    607   -233    473       N  
ATOM   2071  N   TYR A 269      44.274  20.278  25.370  1.00 41.29           N  
ANISOU 2071  N   TYR A 269     5551   4876   5261    758     83    762       N  
ATOM   2072  CA  TYR A 269      44.231  19.892  26.777  1.00 43.99           C  
ANISOU 2072  CA  TYR A 269     5942   5268   5504    813    155    831       C  
ATOM   2073  C   TYR A 269      44.120  18.379  26.932  1.00 51.24           C  
ANISOU 2073  C   TYR A 269     6891   6123   6456    790    149    946       C  
ATOM   2074  O   TYR A 269      44.772  17.788  27.803  1.00 54.60           O  
ANISOU 2074  O   TYR A 269     7386   6575   6783    848    150    988       O  
ATOM   2075  CB  TYR A 269      43.072  20.597  27.477  1.00 45.73           C  
ANISOU 2075  CB  TYR A 269     6117   5539   5721    830    278    876       C  
ATOM   2076  CG  TYR A 269      43.364  22.057  27.744  1.00 60.21           C  
ANISOU 2076  CG  TYR A 269     7962   7427   7487    882    302    755       C  
ATOM   2077  CD1 TYR A 269      44.667  22.495  27.979  1.00 66.88           C  
ANISOU 2077  CD1 TYR A 269     8876   8308   8228    916    231    641       C  
ATOM   2078  CD2 TYR A 269      42.345  23.008  27.736  1.00 59.74           C  
ANISOU 2078  CD2 TYR A 269     7839   7375   7484    895    391    755       C  
ATOM   2079  CE1 TYR A 269      44.943  23.849  28.221  1.00 66.83           C  
ANISOU 2079  CE1 TYR A 269     8887   8331   8175    946    247    520       C  
ATOM   2080  CE2 TYR A 269      42.615  24.361  27.963  1.00 54.65           C  
ANISOU 2080  CE2 TYR A 269     7220   6751   6795    943    417    636       C  
ATOM   2081  CZ  TYR A 269      43.908  24.772  28.203  1.00 60.70           C  
ANISOU 2081  CZ  TYR A 269     8067   7538   7459    960    342    515       C  
ATOM   2082  OH  TYR A 269      44.166  26.105  28.442  1.00 62.86           O  
ANISOU 2082  OH  TYR A 269     8372   7811   7702    992    363    391       O  
ATOM   2083  N   LEU A 270      43.308  17.727  26.096  1.00 46.49           N  
ANISOU 2083  N   LEU A 270     6238   5432   5995    704    134   1002       N  
ATOM   2084  CA  LEU A 270      43.246  16.272  26.154  1.00 45.57           C  
ANISOU 2084  CA  LEU A 270     6161   5220   5933    669    122   1099       C  
ATOM   2085  C   LEU A 270      44.584  15.653  25.762  1.00 46.91           C  
ANISOU 2085  C   LEU A 270     6413   5340   6070    712     29   1035       C  
ATOM   2086  O   LEU A 270      45.045  14.699  26.393  1.00 49.83           O  
ANISOU 2086  O   LEU A 270     6851   5673   6410    755     34   1110       O  
ATOM   2087  CB  LEU A 270      42.116  15.747  25.259  1.00 47.93           C  
ANISOU 2087  CB  LEU A 270     6387   5427   6397    548    106   1147       C  
ATOM   2088  CG  LEU A 270      40.674  16.024  25.703  1.00 52.93           C  
ANISOU 2088  CG  LEU A 270     6914   6098   7098    500    207   1257       C  
ATOM   2089  CD1 LEU A 270      39.679  15.580  24.629  1.00 53.64           C  
ANISOU 2089  CD1 LEU A 270     6914   6110   7358    367    151   1283       C  
ATOM   2090  CD2 LEU A 270      40.341  15.375  27.057  1.00 50.08           C  
ANISOU 2090  CD2 LEU A 270     6579   5754   6695    530    322   1408       C  
ATOM   2091  N   ASN A 271      45.215  16.157  24.706  1.00 46.42           N  
ANISOU 2091  N   ASN A 271     6342   5277   6018    706    -49    909       N  
ATOM   2092  CA  ASN A 271      46.510  15.601  24.321  1.00 43.10           C  
ANISOU 2092  CA  ASN A 271     5985   4823   5569    760   -121    849       C  
ATOM   2093  C   ASN A 271      47.539  15.772  25.435  1.00 44.79           C  
ANISOU 2093  C   ASN A 271     6238   5130   5652    866   -116    857       C  
ATOM   2094  O   ASN A 271      48.342  14.865  25.690  1.00 53.11           O  
ANISOU 2094  O   ASN A 271     7346   6148   6686    929   -145    893       O  
ATOM   2095  CB  ASN A 271      47.022  16.251  23.035  1.00 43.33           C  
ANISOU 2095  CB  ASN A 271     5987   4861   5614    742   -185    720       C  
ATOM   2096  CG  ASN A 271      48.180  15.482  22.426  1.00 48.44           C  
ANISOU 2096  CG  ASN A 271     6689   5455   6260    791   -244    666       C  
ATOM   2097  OD1 ASN A 271      48.149  14.251  22.347  1.00 49.81           O  
ANISOU 2097  OD1 ASN A 271     6921   5517   6489    792   -252    709       O  
ATOM   2098  ND2 ASN A 271      49.200  16.194  21.999  1.00 41.61           N  
ANISOU 2098  ND2 ASN A 271     5805   4663   5343    834   -276    574       N  
ATOM   2099  N   HIS A 272      47.528  16.930  26.106  1.00 44.26           N  
ANISOU 2099  N   HIS A 272     6144   5179   5493    890    -85    821       N  
ATOM   2100  CA  HIS A 272      48.482  17.194  27.181  1.00 49.60           C  
ANISOU 2100  CA  HIS A 272     6855   5963   6027    977    -99    811       C  
ATOM   2101  C   HIS A 272      48.197  16.303  28.384  1.00 49.44           C  
ANISOU 2101  C   HIS A 272     6889   5952   5942   1023    -48    954       C  
ATOM   2102  O   HIS A 272      49.125  15.767  28.999  1.00 54.81           O  
ANISOU 2102  O   HIS A 272     7614   6671   6540   1103    -90    992       O  
ATOM   2103  CB  HIS A 272      48.446  18.680  27.550  1.00 46.36           C  
ANISOU 2103  CB  HIS A 272     6418   5654   5542    976    -79    717       C  
ATOM   2104  CG  HIS A 272      49.397  19.510  26.752  1.00 50.75           C  
ANISOU 2104  CG  HIS A 272     6939   6232   6111    966   -152    587       C  
ATOM   2105  ND1 HIS A 272      49.321  19.611  25.380  1.00 53.90           N  
ANISOU 2105  ND1 HIS A 272     7297   6562   6621    912   -177    543       N  
ATOM   2106  CD2 HIS A 272      50.462  20.260  27.126  1.00 55.60           C  
ANISOU 2106  CD2 HIS A 272     7550   6935   6641    996   -205    498       C  
ATOM   2107  CE1 HIS A 272      50.293  20.391  24.942  1.00 52.32           C  
ANISOU 2107  CE1 HIS A 272     7069   6405   6407    914   -228    446       C  
ATOM   2108  NE2 HIS A 272      51.008  20.789  25.979  1.00 54.85           N  
ANISOU 2108  NE2 HIS A 272     7404   6815   6620    958   -249    415       N  
ATOM   2109  N   TYR A 273      46.914  16.105  28.695  1.00 46.45           N  
ANISOU 2109  N   TYR A 273     6499   5542   5608    976     44   1050       N  
ATOM   2110  CA  TYR A 273      46.484  15.085  29.648  1.00 50.16           C  
ANISOU 2110  CA  TYR A 273     7016   5992   6051   1000    110   1218       C  
ATOM   2111  C   TYR A 273      47.067  13.709  29.301  1.00 53.96           C  
ANISOU 2111  C   TYR A 273     7547   6348   6608   1018     55   1287       C  
ATOM   2112  O   TYR A 273      47.667  13.042  30.152  1.00 56.61           O  
ANISOU 2112  O   TYR A 273     7944   6707   6860   1102     50   1384       O  
ATOM   2113  CB  TYR A 273      44.951  15.075  29.676  1.00 50.09           C  
ANISOU 2113  CB  TYR A 273     6952   5947   6133    919    216   1305       C  
ATOM   2114  CG  TYR A 273      44.249  14.049  30.552  1.00 54.47           C  
ANISOU 2114  CG  TYR A 273     7533   6468   6696    914    310   1502       C  
ATOM   2115  CD1 TYR A 273      44.878  13.442  31.645  1.00 59.17           C  
ANISOU 2115  CD1 TYR A 273     8212   7112   7158   1006    323   1608       C  
ATOM   2116  CD2 TYR A 273      42.943  13.694  30.280  1.00 49.02           C  
ANISOU 2116  CD2 TYR A 273     6774   5702   6150    814    384   1596       C  
ATOM   2117  CE1 TYR A 273      44.201  12.494  32.427  1.00 61.46           C  
ANISOU 2117  CE1 TYR A 273     8528   7365   7461    999    421   1812       C  
ATOM   2118  CE2 TYR A 273      42.265  12.773  31.046  1.00 54.09           C  
ANISOU 2118  CE2 TYR A 273     7427   6306   6819    793    480   1790       C  
ATOM   2119  CZ  TYR A 273      42.885  12.174  32.115  1.00 58.40           C  
ANISOU 2119  CZ  TYR A 273     8067   6891   7232    886    506   1902       C  
ATOM   2120  OH  TYR A 273      42.167  11.253  32.841  1.00 59.59           O  
ANISOU 2120  OH  TYR A 273     8226   6996   7417    860    613   2116       O  
ATOM   2121  N   ASN A 274      46.910  13.273  28.046  1.00 53.22           N  
ANISOU 2121  N   ASN A 274     7436   6119   6668    947     11   1237       N  
ATOM   2122  CA  ASN A 274      47.390  11.951  27.647  1.00 52.79           C  
ANISOU 2122  CA  ASN A 274     7442   5916   6700    965    -30   1284       C  
ATOM   2123  C   ASN A 274      48.911  11.850  27.653  1.00 54.66           C  
ANISOU 2123  C   ASN A 274     7711   6194   6862   1084   -106   1227       C  
ATOM   2124  O   ASN A 274      49.443  10.775  27.938  1.00 55.01           O  
ANISOU 2124  O   ASN A 274     7817   6158   6926   1155   -118   1316       O  
ATOM   2125  CB  ASN A 274      46.853  11.591  26.259  1.00 53.19           C  
ANISOU 2125  CB  ASN A 274     7476   5822   6913    858    -64   1212       C  
ATOM   2126  CG  ASN A 274      45.442  11.002  26.310  1.00 56.31           C  
ANISOU 2126  CG  ASN A 274     7849   6115   7430    740     -4   1324       C  
ATOM   2127  OD1 ASN A 274      45.137  10.190  27.178  1.00 53.61           O  
ANISOU 2127  OD1 ASN A 274     7545   5721   7104    749     56   1480       O  
ATOM   2128  ND2 ASN A 274      44.576  11.435  25.402  1.00 53.45           N  
ANISOU 2128  ND2 ASN A 274     7417   5736   7157    627    -20   1257       N  
ATOM   2129  N   LEU A 275      49.621  12.947  27.369  1.00 53.60           N  
ANISOU 2129  N   LEU A 275     7529   6182   6653   1108   -155   1092       N  
ATOM   2130  CA  LEU A 275      51.080  12.958  27.305  1.00 52.58           C  
ANISOU 2130  CA  LEU A 275     7399   6113   6467   1209   -229   1034       C  
ATOM   2131  C   LEU A 275      51.758  13.255  28.641  1.00 56.45           C  
ANISOU 2131  C   LEU A 275     7895   6761   6794   1301   -249   1088       C  
ATOM   2132  O   LEU A 275      52.768  12.620  28.963  1.00 59.07           O  
ANISOU 2132  O   LEU A 275     8243   7109   7093   1405   -300   1137       O  
ATOM   2133  CB  LEU A 275      51.565  13.980  26.277  1.00 49.55           C  
ANISOU 2133  CB  LEU A 275     6950   5781   6096   1175   -274    870       C  
ATOM   2134  CG  LEU A 275      51.503  13.637  24.793  1.00 49.47           C  
ANISOU 2134  CG  LEU A 275     6939   5650   6207   1128   -289    791       C  
ATOM   2135  CD1 LEU A 275      52.033  14.818  24.022  1.00 45.59           C  
ANISOU 2135  CD1 LEU A 275     6380   5250   5694   1105   -320    659       C  
ATOM   2136  CD2 LEU A 275      52.345  12.391  24.491  1.00 51.03           C  
ANISOU 2136  CD2 LEU A 275     7188   5747   6455   1218   -314    816       C  
ATOM   2137  N   PHE A 276      51.261  14.222  29.417  1.00 57.75           N  
ANISOU 2137  N   PHE A 276     8046   7046   6849   1272   -215   1072       N  
ATOM   2138  CA  PHE A 276      52.000  14.707  30.575  1.00 48.44           C  
ANISOU 2138  CA  PHE A 276     6875   6038   5492   1348   -257   1075       C  
ATOM   2139  C   PHE A 276      51.296  14.488  31.903  1.00 58.71           C  
ANISOU 2139  C   PHE A 276     8236   7404   6668   1375   -185   1207       C  
ATOM   2140  O   PHE A 276      51.839  14.909  32.929  1.00 73.46           O  
ANISOU 2140  O   PHE A 276    10125   9430   8359   1436   -222   1204       O  
ATOM   2141  CB  PHE A 276      52.343  16.199  30.422  1.00 42.26           C  
ANISOU 2141  CB  PHE A 276     6038   5367   4652   1306   -295    905       C  
ATOM   2142  CG  PHE A 276      53.077  16.515  29.151  1.00 42.36           C  
ANISOU 2142  CG  PHE A 276     5985   5338   4773   1279   -354    788       C  
ATOM   2143  CD1 PHE A 276      54.338  15.997  28.920  1.00 44.47           C  
ANISOU 2143  CD1 PHE A 276     6222   5626   5049   1353   -434    789       C  
ATOM   2144  CD2 PHE A 276      52.480  17.290  28.165  1.00 43.14           C  
ANISOU 2144  CD2 PHE A 276     6047   5380   4964   1187   -322    694       C  
ATOM   2145  CE1 PHE A 276      55.002  16.245  27.720  1.00 49.57           C  
ANISOU 2145  CE1 PHE A 276     6804   6240   5791   1334   -467    692       C  
ATOM   2146  CE2 PHE A 276      53.134  17.553  26.974  1.00 47.03           C  
ANISOU 2146  CE2 PHE A 276     6485   5843   5542   1165   -365    603       C  
ATOM   2147  CZ  PHE A 276      54.399  17.027  26.745  1.00 50.15           C  
ANISOU 2147  CZ  PHE A 276     6853   6262   5941   1237   -431    599       C  
ATOM   2148  N   GLY A 277      50.119  13.875  31.930  1.00 54.66           N  
ANISOU 2148  N   GLY A 277     7750   6787   6234   1328    -84   1322       N  
ATOM   2149  CA  GLY A 277      49.510  13.433  33.173  1.00 54.24           C  
ANISOU 2149  CA  GLY A 277     7753   6786   6070   1364      1   1487       C  
ATOM   2150  C   GLY A 277      48.232  14.188  33.547  1.00 57.52           C  
ANISOU 2150  C   GLY A 277     8153   7249   6454   1301    122   1484       C  
ATOM   2151  O   GLY A 277      47.874  15.221  32.976  1.00 55.69           O  
ANISOU 2151  O   GLY A 277     7868   7028   6265   1241    131   1342       O  
ATOM   2152  N   SER A 278      47.565  13.644  34.574  1.00 59.33           N  
ANISOU 2152  N   SER A 278     8428   7511   6603   1328    224   1657       N  
ATOM   2153  CA  SER A 278      46.232  14.065  34.983  1.00 68.04           C  
ANISOU 2153  CA  SER A 278     9508   8645   7698   1279    371   1706       C  
ATOM   2154  C   SER A 278      46.184  15.465  35.582  1.00 68.11           C  
ANISOU 2154  C   SER A 278     9522   8821   7535   1311    400   1565       C  
ATOM   2155  O   SER A 278      45.084  15.971  35.832  1.00 63.37           O  
ANISOU 2155  O   SER A 278     8891   8249   6937   1284    531   1579       O  
ATOM   2156  CB  SER A 278      45.652  13.071  35.990  1.00 70.80           C  
ANISOU 2156  CB  SER A 278     9907   9000   7992   1310    482   1947       C  
ATOM   2157  OG  SER A 278      46.531  12.910  37.079  1.00 77.20           O  
ANISOU 2157  OG  SER A 278    10805   9951   8578   1427    440   2005       O  
ATOM   2158  N   GLY A 279      47.320  16.120  35.806  1.00 63.42           N  
ANISOU 2158  N   GLY A 279     8960   8333   6805   1365    286   1426       N  
ATOM   2159  CA  GLY A 279      47.241  17.524  36.168  1.00 58.14           C  
ANISOU 2159  CA  GLY A 279     8297   7778   6015   1372    306   1257       C  
ATOM   2160  C   GLY A 279      46.493  18.346  35.133  1.00 60.09           C  
ANISOU 2160  C   GLY A 279     8463   7930   6440   1289    350   1145       C  
ATOM   2161  O   GLY A 279      45.907  19.377  35.459  1.00 63.13           O  
ANISOU 2161  O   GLY A 279     8849   8370   6769   1295    432   1057       O  
ATOM   2162  N   TYR A 280      46.476  17.886  33.879  1.00 63.63           N  
ANISOU 2162  N   TYR A 280     8845   8234   7099   1220    298   1151       N  
ATOM   2163  CA  TYR A 280      45.759  18.568  32.809  1.00 57.68           C  
ANISOU 2163  CA  TYR A 280     8009   7394   6514   1143    324   1069       C  
ATOM   2164  C   TYR A 280      44.301  18.132  32.695  1.00 59.50           C  
ANISOU 2164  C   TYR A 280     8180   7561   6865   1092    452   1204       C  
ATOM   2165  O   TYR A 280      43.545  18.723  31.913  1.00 55.47           O  
ANISOU 2165  O   TYR A 280     7590   7000   6487   1036    482   1157       O  
ATOM   2166  CB  TYR A 280      46.473  18.337  31.471  1.00 54.69           C  
ANISOU 2166  CB  TYR A 280     7589   6911   6278   1093    201    999       C  
ATOM   2167  CG  TYR A 280      47.711  19.188  31.264  1.00 53.62           C  
ANISOU 2167  CG  TYR A 280     7461   6833   6079   1114     91    837       C  
ATOM   2168  CD1 TYR A 280      47.602  20.519  30.867  1.00 48.41           C  
ANISOU 2168  CD1 TYR A 280     6769   6184   5443   1083     96    697       C  
ATOM   2169  CD2 TYR A 280      48.985  18.660  31.447  1.00 53.11           C  
ANISOU 2169  CD2 TYR A 280     7426   6806   5947   1163    -14    834       C  
ATOM   2170  CE1 TYR A 280      48.719  21.303  30.679  1.00 49.30           C  
ANISOU 2170  CE1 TYR A 280     6880   6337   5515   1084      0    557       C  
ATOM   2171  CE2 TYR A 280      50.120  19.435  31.252  1.00 50.62           C  
ANISOU 2171  CE2 TYR A 280     7094   6551   5589   1168   -115    695       C  
ATOM   2172  CZ  TYR A 280      49.979  20.761  30.874  1.00 60.39           C  
ANISOU 2172  CZ  TYR A 280     8301   7792   6853   1120   -107    555       C  
ATOM   2173  OH  TYR A 280      51.095  21.552  30.665  1.00 65.57           O  
ANISOU 2173  OH  TYR A 280     8932   8495   7486   1107   -204    424       O  
ATOM   2174  N   ARG A 281      43.875  17.130  33.460  1.00 59.23           N  
ANISOU 2174  N   ARG A 281     8175   7532   6795   1109    528   1382       N  
ATOM   2175  CA  ARG A 281      42.508  16.649  33.305  1.00 58.65           C  
ANISOU 2175  CA  ARG A 281     8026   7395   6865   1041    645   1522       C  
ATOM   2176  C   ARG A 281      41.482  17.700  33.715  1.00 58.82           C  
ANISOU 2176  C   ARG A 281     7991   7501   6856   1060    783   1497       C  
ATOM   2177  O   ARG A 281      40.397  17.760  33.126  1.00 58.45           O  
ANISOU 2177  O   ARG A 281     7834   7399   6976    991    843   1544       O  
ATOM   2178  CB  ARG A 281      42.303  15.368  34.108  1.00 56.15           C  
ANISOU 2178  CB  ARG A 281     7754   7062   6518   1053    709   1735       C  
ATOM   2179  CG  ARG A 281      40.900  14.796  34.013  1.00 59.59           C  
ANISOU 2179  CG  ARG A 281     8098   7429   7113    966    833   1898       C  
ATOM   2180  CD  ARG A 281      40.680  13.754  35.080  1.00 59.04           C  
ANISOU 2180  CD  ARG A 281     8083   7375   6975    993    932   2121       C  
ATOM   2181  NE  ARG A 281      39.434  13.010  34.890  1.00 65.98           N  
ANISOU 2181  NE  ARG A 281     8865   8158   8046    882   1034   2296       N  
ATOM   2182  CZ  ARG A 281      38.288  13.302  35.492  1.00 68.18           C  
ANISOU 2182  CZ  ARG A 281     9063   8522   8321    875   1207   2404       C  
ATOM   2183  NH1 ARG A 281      38.224  14.326  36.328  1.00 70.07           N  
ANISOU 2183  NH1 ARG A 281     9326   8937   8360    984   1304   2343       N  
ATOM   2184  NH2 ARG A 281      37.209  12.570  35.261  1.00 66.80           N  
ANISOU 2184  NH2 ARG A 281     8780   8256   8343    758   1285   2568       N  
ATOM   2185  N   SER A 282      41.807  18.546  34.700  1.00 56.31           N  
ANISOU 2185  N   SER A 282     7747   7319   6331   1155    830   1416       N  
ATOM   2186  CA  SER A 282      40.832  19.519  35.198  1.00 60.88           C  
ANISOU 2186  CA  SER A 282     8289   7974   6870   1197    984   1389       C  
ATOM   2187  C   SER A 282      40.504  20.595  34.162  1.00 58.11           C  
ANISOU 2187  C   SER A 282     7852   7560   6668   1162    957   1250       C  
ATOM   2188  O   SER A 282      39.339  20.979  34.017  1.00 64.17           O  
ANISOU 2188  O   SER A 282     8520   8323   7540   1155   1076   1297       O  
ATOM   2189  CB  SER A 282      41.334  20.150  36.504  1.00 65.22           C  
ANISOU 2189  CB  SER A 282     8963   8676   7142   1309   1031   1310       C  
ATOM   2190  OG  SER A 282      42.703  20.477  36.451  1.00 79.65           O  
ANISOU 2190  OG  SER A 282    10873  10523   8866   1326    867   1159       O  
ATOM   2191  N   SER A 283      41.514  21.101  33.447  1.00 50.21           N  
ANISOU 2191  N   SER A 283     6881   6516   5681   1144    808   1092       N  
ATOM   2192  CA  SER A 283      41.271  22.029  32.344  1.00 49.98           C  
ANISOU 2192  CA  SER A 283     6773   6415   5804   1105    771    985       C  
ATOM   2193  C   SER A 283      40.345  21.423  31.289  1.00 49.17           C  
ANISOU 2193  C   SER A 283     6541   6221   5921   1014    767   1099       C  
ATOM   2194  O   SER A 283      39.428  22.088  30.797  1.00 52.33           O  
ANISOU 2194  O   SER A 283     6841   6602   6440   1004    824   1099       O  
ATOM   2195  CB  SER A 283      42.599  22.445  31.718  1.00 57.07           C  
ANISOU 2195  CB  SER A 283     7719   7280   6684   1088    609    833       C  
ATOM   2196  OG  SER A 283      43.383  23.157  32.651  1.00 64.35           O  
ANISOU 2196  OG  SER A 283     8742   8288   7418   1155    600    711       O  
ATOM   2197  N   ALA A 284      40.563  20.160  30.929  1.00 49.65           N  
ANISOU 2197  N   ALA A 284     6603   6219   6041    949    696   1194       N  
ATOM   2198  CA  ALA A 284      39.703  19.523  29.935  1.00 51.06           C  
ANISOU 2198  CA  ALA A 284     6670   6307   6423    845    674   1285       C  
ATOM   2199  C   ALA A 284      38.282  19.345  30.457  1.00 55.85           C  
ANISOU 2199  C   ALA A 284     7174   6948   7097    832    829   1437       C  
ATOM   2200  O   ALA A 284      37.312  19.601  29.738  1.00 56.75           O  
ANISOU 2200  O   ALA A 284     7156   7038   7369    776    844   1470       O  
ATOM   2201  CB  ALA A 284      40.282  18.165  29.522  1.00 48.12           C  
ANISOU 2201  CB  ALA A 284     6344   5843   6097    782    571   1340       C  
ATOM   2202  N   MET A 285      38.133  18.886  31.681  1.00 60.81           N  
ANISOU 2202  N   MET A 285     7853   7643   7610    882    945   1544       N  
ATOM   2203  CA  MET A 285      36.817  18.642  32.222  1.00 61.19           C  
ANISOU 2203  CA  MET A 285     7796   7733   7722    870   1110   1709       C  
ATOM   2204  C   MET A 285      36.042  19.914  32.428  1.00 59.52           C  
ANISOU 2204  C   MET A 285     7506   7601   7506    945   1233   1658       C  
ATOM   2205  O   MET A 285      34.877  19.965  32.188  1.00 56.27           O  
ANISOU 2205  O   MET A 285     6944   7197   7241    910   1317   1756       O  
ATOM   2206  CB  MET A 285      36.900  17.815  33.492  1.00 69.62           C  
ANISOU 2206  CB  MET A 285     8946   8858   8649    911   1214   1851       C  
ATOM   2207  CG  MET A 285      35.566  17.380  34.043  1.00 80.86           C  
ANISOU 2207  CG  MET A 285    10253  10320  10150    883   1395   2054       C  
ATOM   2208  SD  MET A 285      34.795  16.076  33.112  1.00 87.72           S  
ANISOU 2208  SD  MET A 285    10989  11040  11303    695   1336   2216       S  
ATOM   2209  CE  MET A 285      36.051  14.837  33.196  1.00 84.53           C  
ANISOU 2209  CE  MET A 285    10756  10527  10833    674   1207   2238       C  
ATOM   2210  N   SER A 286      36.709  20.943  32.873  1.00 57.70           N  
ANISOU 2210  N   SER A 286     7377   7429   7117   1050   1240   1502       N  
ATOM   2211  CA  SER A 286      36.048  22.229  33.046  1.00 59.44           C  
ANISOU 2211  CA  SER A 286     7545   7700   7340   1136   1358   1431       C  
ATOM   2212  C   SER A 286      35.439  22.713  31.728  1.00 63.02           C  
ANISOU 2212  C   SER A 286     7850   8077   8017   1077   1293   1416       C  
ATOM   2213  O   SER A 286      34.274  23.127  31.682  1.00 59.12           O  
ANISOU 2213  O   SER A 286     7216   7612   7636   1103   1412   1491       O  
ATOM   2214  CB  SER A 286      37.047  23.237  33.621  1.00 63.44           C  
ANISOU 2214  CB  SER A 286     8209   8247   7650   1236   1338   1234       C  
ATOM   2215  OG  SER A 286      36.548  24.549  33.534  1.00 72.06           O  
ANISOU 2215  OG  SER A 286     9263   9338   8779   1312   1421   1134       O  
ATOM   2216  N   ILE A 287      36.199  22.622  30.630  1.00 62.68           N  
ANISOU 2216  N   ILE A 287     7829   7948   8040   1002   1106   1332       N  
ATOM   2217  CA  ILE A 287      35.675  23.032  29.329  1.00 56.55           C  
ANISOU 2217  CA  ILE A 287     6922   7112   7451    944   1028   1326       C  
ATOM   2218  C   ILE A 287      34.497  22.157  28.916  1.00 54.89           C  
ANISOU 2218  C   ILE A 287     6546   6893   7416    845   1047   1501       C  
ATOM   2219  O   ILE A 287      33.493  22.655  28.397  1.00 59.61           O  
ANISOU 2219  O   ILE A 287     6987   7505   8157    841   1079   1554       O  
ATOM   2220  CB  ILE A 287      36.786  23.011  28.264  1.00 50.66           C  
ANISOU 2220  CB  ILE A 287     6246   6289   6713    884    834   1209       C  
ATOM   2221  CG1 ILE A 287      37.771  24.160  28.472  1.00 45.78           C  
ANISOU 2221  CG1 ILE A 287     5742   5674   5977    967    815   1038       C  
ATOM   2222  CG2 ILE A 287      36.187  23.061  26.868  1.00 47.41           C  
ANISOU 2222  CG2 ILE A 287     5703   5828   6483    801    737   1240       C  
ATOM   2223  CD1 ILE A 287      38.972  24.152  27.473  1.00 42.66           C  
ANISOU 2223  CD1 ILE A 287     5410   5217   5582    912    639    931       C  
ATOM   2224  N   ILE A 288      34.604  20.841  29.116  1.00 55.39           N  
ANISOU 2224  N   ILE A 288     6636   6929   7483    759   1018   1598       N  
ATOM   2225  CA  ILE A 288      33.508  19.954  28.731  1.00 63.12           C  
ANISOU 2225  CA  ILE A 288     7458   7884   8643    639   1025   1760       C  
ATOM   2226  C   ILE A 288      32.265  20.253  29.559  1.00 66.10           C  
ANISOU 2226  C   ILE A 288     7697   8357   9060    694   1231   1896       C  
ATOM   2227  O   ILE A 288      31.139  20.208  29.050  1.00 67.46           O  
ANISOU 2227  O   ILE A 288     7676   8543   9415    628   1246   2001       O  
ATOM   2228  CB  ILE A 288      33.930  18.476  28.857  1.00 63.81           C  
ANISOU 2228  CB  ILE A 288     7622   7893   8731    540    965   1835       C  
ATOM   2229  CG1 ILE A 288      35.003  18.117  27.823  1.00 58.89           C  
ANISOU 2229  CG1 ILE A 288     7101   7168   8107    482    763   1707       C  
ATOM   2230  CG2 ILE A 288      32.725  17.555  28.674  1.00 62.94           C  
ANISOU 2230  CG2 ILE A 288     7350   7753   8812    405    997   2014       C  
ATOM   2231  CD1 ILE A 288      35.545  16.676  27.968  1.00 50.16           C  
ANISOU 2231  CD1 ILE A 288     6095   5963   7001    410    708   1765       C  
ATOM   2232  N   ASP A 289      32.448  20.554  30.852  1.00 69.61           N  
ANISOU 2232  N   ASP A 289     8235   8883   9331    817   1391   1899       N  
ATOM   2233  CA  ASP A 289      31.311  20.864  31.718  1.00 72.01           C  
ANISOU 2233  CA  ASP A 289     8421   9292   9649    892   1616   2024       C  
ATOM   2234  C   ASP A 289      30.609  22.145  31.281  1.00 71.28           C  
ANISOU 2234  C   ASP A 289     8200   9233   9650    975   1668   1970       C  
ATOM   2235  O   ASP A 289      29.374  22.210  31.264  1.00 69.70           O  
ANISOU 2235  O   ASP A 289     7798   9086   9597    973   1780   2107       O  
ATOM   2236  CB  ASP A 289      31.763  20.989  33.175  1.00 73.77           C  
ANISOU 2236  CB  ASP A 289     8801   9603   9624   1020   1770   2010       C  
ATOM   2237  CG  ASP A 289      31.995  19.646  33.845  1.00 76.45           C  
ANISOU 2237  CG  ASP A 289     9210   9940   9898    955   1791   2155       C  
ATOM   2238  OD1 ASP A 289      31.453  18.628  33.364  1.00 78.56           O  
ANISOU 2238  OD1 ASP A 289     9364  10141  10343    813   1751   2303       O  
ATOM   2239  OD2 ASP A 289      32.736  19.616  34.856  1.00 76.58           O  
ANISOU 2239  OD2 ASP A 289     9398  10018   9683   1045   1842   2121       O  
ATOM   2240  N   ASP A 290      31.378  23.183  30.952  1.00 70.12           N  
ANISOU 2240  N   ASP A 290     8161   9053   9427   1055   1593   1783       N  
ATOM   2241  CA  ASP A 290      30.771  24.447  30.541  1.00 74.92           C  
ANISOU 2241  CA  ASP A 290     8667   9671  10130   1149   1645   1736       C  
ATOM   2242  C   ASP A 290      29.939  24.282  29.277  1.00 63.70           C  
ANISOU 2242  C   ASP A 290     7034   8223   8948   1045   1536   1833       C  
ATOM   2243  O   ASP A 290      28.852  24.849  29.163  1.00 63.68           O  
ANISOU 2243  O   ASP A 290     6849   8270   9078   1103   1635   1917       O  
ATOM   2244  CB  ASP A 290      31.845  25.509  30.330  1.00 80.97           C  
ANISOU 2244  CB  ASP A 290     9597  10379  10788   1225   1564   1523       C  
ATOM   2245  CG  ASP A 290      32.547  25.880  31.602  1.00 89.46           C  
ANISOU 2245  CG  ASP A 290    10865  11496  11629   1337   1671   1410       C  
ATOM   2246  OD1 ASP A 290      32.088  25.444  32.678  1.00 97.36           O  
ANISOU 2246  OD1 ASP A 290    11868  12585  12538   1383   1834   1502       O  
ATOM   2247  OD2 ASP A 290      33.553  26.614  31.526  1.00 93.50           O  
ANISOU 2247  OD2 ASP A 290    11523  11958  12044   1373   1591   1232       O  
ATOM   2248  N   TYR A 291      30.442  23.531  28.305  1.00 61.34           N  
ANISOU 2248  N   TYR A 291     6755   7851   8701    898   1329   1818       N  
ATOM   2249  CA  TYR A 291      29.684  23.347  27.075  1.00 61.77           C  
ANISOU 2249  CA  TYR A 291     6622   7891   8959    790   1202   1896       C  
ATOM   2250  C   TYR A 291      28.415  22.526  27.307  1.00 71.60           C  
ANISOU 2250  C   TYR A 291     7657   9192  10354    703   1283   2098       C  
ATOM   2251  O   TYR A 291      27.383  22.786  26.676  1.00 73.17           O  
ANISOU 2251  O   TYR A 291     7639   9434  10729    676   1266   2191       O  
ATOM   2252  CB  TYR A 291      30.562  22.697  26.013  1.00 50.52           C  
ANISOU 2252  CB  TYR A 291     5291   6375   7528    657    970   1813       C  
ATOM   2253  CG  TYR A 291      31.434  23.668  25.259  1.00 50.10           C  
ANISOU 2253  CG  TYR A 291     5341   6280   7416    715    861   1656       C  
ATOM   2254  CD1 TYR A 291      30.917  24.845  24.724  1.00 49.29           C  
ANISOU 2254  CD1 TYR A 291     5135   6198   7394    796    872   1653       C  
ATOM   2255  CD2 TYR A 291      32.779  23.390  25.059  1.00 47.63           C  
ANISOU 2255  CD2 TYR A 291     5219   5903   6977    688    749   1526       C  
ATOM   2256  CE1 TYR A 291      31.743  25.738  24.012  1.00 52.11           C  
ANISOU 2256  CE1 TYR A 291     5590   6504   7704    841    777   1526       C  
ATOM   2257  CE2 TYR A 291      33.602  24.258  24.373  1.00 49.19           C  
ANISOU 2257  CE2 TYR A 291     5499   6063   7127    730    660   1397       C  
ATOM   2258  CZ  TYR A 291      33.088  25.428  23.842  1.00 53.81           C  
ANISOU 2258  CZ  TYR A 291     5992   6661   7792    800    673   1399       C  
ATOM   2259  OH  TYR A 291      33.950  26.266  23.161  1.00 50.73           O  
ANISOU 2259  OH  TYR A 291     5692   6223   7359    832    589   1284       O  
ATOM   2260  N   LEU A 292      28.472  21.519  28.186  1.00 70.39           N  
ANISOU 2260  N   LEU A 292     7558   9043  10146    652   1367   2180       N  
ATOM   2261  CA  LEU A 292      27.275  20.730  28.465  1.00 67.40           C  
ANISOU 2261  CA  LEU A 292     6974   8713   9921    558   1461   2387       C  
ATOM   2262  C   LEU A 292      26.193  21.591  29.107  1.00 68.59           C  
ANISOU 2262  C   LEU A 292     6951   8986  10124    698   1684   2484       C  
ATOM   2263  O   LEU A 292      25.019  21.503  28.738  1.00 68.58           O  
ANISOU 2263  O   LEU A 292     6694   9041  10323    639   1705   2629       O  
ATOM   2264  CB  LEU A 292      27.634  19.535  29.342  1.00 69.82           C  
ANISOU 2264  CB  LEU A 292     7394   8988  10145    491   1522   2466       C  
ATOM   2265  CG  LEU A 292      28.456  18.461  28.619  1.00 71.86           C  
ANISOU 2265  CG  LEU A 292     7777   9111  10416    334   1308   2410       C  
ATOM   2266  CD1 LEU A 292      28.760  17.318  29.551  1.00 72.58           C  
ANISOU 2266  CD1 LEU A 292     7976   9163  10439    289   1386   2513       C  
ATOM   2267  CD2 LEU A 292      27.697  17.927  27.405  1.00 75.45           C  
ANISOU 2267  CD2 LEU A 292     8049   9517  11100    149   1145   2466       C  
ATOM   2268  N   ARG A 293      26.584  22.462  30.036  1.00 68.73           N  
ANISOU 2268  N   ARG A 293     7102   9048   9964    887   1846   2396       N  
ATOM   2269  CA  ARG A 293      25.683  23.474  30.580  1.00 70.91           C  
ANISOU 2269  CA  ARG A 293     7247   9424  10273   1057   2062   2442       C  
ATOM   2270  C   ARG A 293      25.146  24.381  29.473  1.00 73.32           C  
ANISOU 2270  C   ARG A 293     7386   9720  10750   1089   1968   2424       C  
ATOM   2271  O   ARG A 293      23.937  24.422  29.216  1.00 78.24           O  
ANISOU 2271  O   ARG A 293     7744  10417  11569   1079   2025   2580       O  
ATOM   2272  CB  ARG A 293      26.450  24.278  31.636  1.00 79.81           C  
ANISOU 2272  CB  ARG A 293     8605  10568  11150   1244   2204   2290       C  
ATOM   2273  CG  ARG A 293      25.704  25.391  32.340  1.00 92.28           C  
ANISOU 2273  CG  ARG A 293    10114  12231  12717   1452   2449   2291       C  
ATOM   2274  CD  ARG A 293      26.417  25.775  33.641  1.00 99.36           C  
ANISOU 2274  CD  ARG A 293    11258  13163  13331   1596   2603   2162       C  
ATOM   2275  NE  ARG A 293      26.125  27.150  34.050  1.00108.00           N  
ANISOU 2275  NE  ARG A 293    12373  14276  14385   1809   2771   2053       N  
ATOM   2276  CZ  ARG A 293      25.143  27.514  34.872  1.00112.57           C  
ANISOU 2276  CZ  ARG A 293    12844  14961  14966   1957   3043   2141       C  
ATOM   2277  NH1 ARG A 293      24.327  26.604  35.393  1.00116.51           N  
ANISOU 2277  NH1 ARG A 293    13190  15572  15507   1906   3185   2357       N  
ATOM   2278  NH2 ARG A 293      24.975  28.797  35.168  1.00109.87           N  
ANISOU 2278  NH2 ARG A 293    12546  14606  14591   2158   3182   2013       N  
ATOM   2279  N   MET A 294      26.052  25.086  28.779  1.00 70.24           N  
ANISOU 2279  N   MET A 294     7145   9244  10297   1122   1815   2247       N  
ATOM   2280  CA  MET A 294      25.678  26.026  27.721  1.00 70.61           C  
ANISOU 2280  CA  MET A 294     7069   9275  10484   1168   1720   2229       C  
ATOM   2281  C   MET A 294      24.721  25.400  26.716  1.00 74.61           C  
ANISOU 2281  C   MET A 294     7315   9820  11213   1015   1585   2388       C  
ATOM   2282  O   MET A 294      23.798  26.064  26.230  1.00 83.19           O  
ANISOU 2282  O   MET A 294     8189  10962  12458   1079   1600   2476       O  
ATOM   2283  CB  MET A 294      26.940  26.543  27.020  1.00 70.16           C  
ANISOU 2283  CB  MET A 294     7224   9111  10324   1168   1543   2037       C  
ATOM   2284  CG  MET A 294      26.683  27.288  25.712  1.00 73.33           C  
ANISOU 2284  CG  MET A 294     7514   9486  10863   1173   1395   2039       C  
ATOM   2285  SD  MET A 294      28.168  27.683  24.751  1.00 79.76           S  
ANISOU 2285  SD  MET A 294     8557  10183  11566   1133   1178   1848       S  
ATOM   2286  CE  MET A 294      29.167  28.543  25.965  1.00 75.90           C  
ANISOU 2286  CE  MET A 294     8322   9639  10879   1291   1337   1668       C  
ATOM   2287  N   LEU A 295      24.926  24.130  26.385  1.00 73.27           N  
ANISOU 2287  N   LEU A 295     7159   9619  11061    813   1443   2424       N  
ATOM   2288  CA  LEU A 295      23.989  23.400  25.533  1.00 69.04           C  
ANISOU 2288  CA  LEU A 295     6381   9118  10731    640   1311   2567       C  
ATOM   2289  C   LEU A 295      22.845  22.870  26.401  1.00 69.17           C  
ANISOU 2289  C   LEU A 295     6186   9231  10864    618   1506   2768       C  
ATOM   2290  O   LEU A 295      21.991  22.120  25.938  1.00 75.66           O  
ANISOU 2290  O   LEU A 295     6791  10089  11869    454   1427   2909       O  
ATOM   2291  CB  LEU A 295      24.702  22.256  24.798  1.00 60.11           C  
ANISOU 2291  CB  LEU A 295     5371   7892   9577    430   1080   2504       C  
ATOM   2292  CG  LEU A 295      25.938  22.688  23.991  1.00 64.86           C  
ANISOU 2292  CG  LEU A 295     6192   8407  10046    450    905   2309       C  
ATOM   2293  CD1 LEU A 295      26.756  21.487  23.517  1.00 61.57           C  
ANISOU 2293  CD1 LEU A 295     5928   7889   9576    276    730   2235       C  
ATOM   2294  CD2 LEU A 295      25.589  23.605  22.816  1.00 58.91           C  
ANISOU 2294  CD2 LEU A 295     5320   7685   9379    486    774   2299       C  
TER    2295      LEU A 295                                                      
ATOM   2296  N   ASP B   7      76.297   6.041   7.118  1.00 74.75           N  
ANISOU 2296  N   ASP B   7     8702   8975  10725    875   2289  -1053       N  
ATOM   2297  CA  ASP B   7      75.920   7.366   7.604  1.00 77.92           C  
ANISOU 2297  CA  ASP B   7     9112   9537  10956    809   2019   -911       C  
ATOM   2298  C   ASP B   7      75.020   8.067   6.571  1.00 74.10           C  
ANISOU 2298  C   ASP B   7     8684   9205  10263    605   1921  -1075       C  
ATOM   2299  O   ASP B   7      75.494   8.770   5.673  1.00 75.28           O  
ANISOU 2299  O   ASP B   7     8795   9549  10258    525   1872  -1108       O  
ATOM   2300  CB  ASP B   7      77.162   8.196   7.932  1.00 87.61           C  
ANISOU 2300  CB  ASP B   7    10233  10925  12130    886   1910   -708       C  
ATOM   2301  CG  ASP B   7      76.846   9.399   8.804  1.00 95.64           C  
ANISOU 2301  CG  ASP B   7    11269  12043  13028    853   1661   -531       C  
ATOM   2302  OD1 ASP B   7      75.645   9.649   9.056  1.00 82.93           O  
ANISOU 2302  OD1 ASP B   7     9751  10389  11368    772   1573   -569       O  
ATOM   2303  OD2 ASP B   7      77.802  10.075   9.251  1.00109.44           O  
ANISOU 2303  OD2 ASP B   7    12935  13912  14736    904   1564   -358       O  
ATOM   2304  N   PRO B   8      73.712   7.830   6.671  1.00 67.30           N  
ANISOU 2304  N   PRO B   8     7909   8261   9401    519   1902  -1174       N  
ATOM   2305  CA  PRO B   8      72.796   8.411   5.677  1.00 70.16           C  
ANISOU 2305  CA  PRO B   8     8309   8779   9569    330   1811  -1321       C  
ATOM   2306  C   PRO B   8      72.743   9.938   5.712  1.00 65.77           C  
ANISOU 2306  C   PRO B   8     7738   8429   8822    276   1571  -1175       C  
ATOM   2307  O   PRO B   8      72.479  10.557   4.670  1.00 61.25           O  
ANISOU 2307  O   PRO B   8     7165   8039   8068    143   1506  -1260       O  
ATOM   2308  CB  PRO B   8      71.446   7.770   6.042  1.00 70.59           C  
ANISOU 2308  CB  PRO B   8     8441   8682   9700    276   1842  -1421       C  
ATOM   2309  CG  PRO B   8      71.539   7.551   7.543  1.00 65.10           C  
ANISOU 2309  CG  PRO B   8     7756   7810   9169    434   1825  -1227       C  
ATOM   2310  CD  PRO B   8      72.999   7.220   7.812  1.00 65.93           C  
ANISOU 2310  CD  PRO B   8     7791   7878   9382    592   1923  -1113       C  
ATOM   2311  N   ILE B   9      72.998  10.567   6.869  1.00 58.96           N  
ANISOU 2311  N   ILE B   9     6867   7545   7991    370   1444   -956       N  
ATOM   2312  CA  ILE B   9      73.055  12.027   6.926  1.00 55.95           C  
ANISOU 2312  CA  ILE B   9     6479   7338   7443    320   1241   -819       C  
ATOM   2313  C   ILE B   9      74.238  12.538   6.104  1.00 59.13           C  
ANISOU 2313  C   ILE B   9     6812   7912   7744    301   1248   -804       C  
ATOM   2314  O   ILE B   9      74.079  13.360   5.190  1.00 59.48           O  
ANISOU 2314  O   ILE B   9     6859   8128   7612    186   1169   -840       O  
ATOM   2315  CB  ILE B   9      73.112  12.507   8.387  1.00 53.63           C  
ANISOU 2315  CB  ILE B   9     6197   6971   7207    412   1129   -609       C  
ATOM   2316  CG1 ILE B   9      71.823  12.132   9.114  1.00 48.96           C  
ANISOU 2316  CG1 ILE B   9     5681   6230   6691    409   1115   -629       C  
ATOM   2317  CG2 ILE B   9      73.298  14.010   8.432  1.00 46.40           C  
ANISOU 2317  CG2 ILE B   9     5280   6218   6130    355    948   -478       C  
ATOM   2318  CD1 ILE B   9      71.951  12.098  10.616  1.00 48.23           C  
ANISOU 2318  CD1 ILE B   9     5606   6017   6703    522   1076   -454       C  
ATOM   2319  N   ARG B  10      75.442  12.043   6.418  1.00 60.77           N  
ANISOU 2319  N   ARG B  10     6948   8077   8064    419   1348   -741       N  
ATOM   2320  CA  ARG B  10      76.626  12.354   5.618  1.00 65.01           C  
ANISOU 2320  CA  ARG B  10     7405   8766   8530    409   1389   -741       C  
ATOM   2321  C   ARG B  10      76.413  11.990   4.156  1.00 65.13           C  
ANISOU 2321  C   ARG B  10     7434   8857   8455    295   1501   -962       C  
ATOM   2322  O   ARG B  10      76.704  12.791   3.262  1.00 64.31           O  
ANISOU 2322  O   ARG B  10     7312   8941   8180    198   1446   -977       O  
ATOM   2323  CB  ARG B  10      77.838  11.605   6.185  1.00 70.15           C  
ANISOU 2323  CB  ARG B  10     7964   9335   9353    570   1513   -656       C  
ATOM   2324  CG  ARG B  10      79.203  12.163   5.808  1.00 85.72           C  
ANISOU 2324  CG  ARG B  10     9828  11475  11268    586   1510   -574       C  
ATOM   2325  CD  ARG B  10      80.328  11.458   6.588  1.00 94.34           C  
ANISOU 2325  CD  ARG B  10    10810  12493  12543    765   1607   -446       C  
ATOM   2326  NE  ARG B  10      81.437  12.363   6.912  1.00 98.33           N  
ANISOU 2326  NE  ARG B  10    11210  13168  12984    779   1498   -270       N  
ATOM   2327  CZ  ARG B  10      81.583  13.001   8.078  1.00 97.53           C  
ANISOU 2327  CZ  ARG B  10    11092  13094  12871    808   1339    -77       C  
ATOM   2328  NH1 ARG B  10      80.686  12.849   9.056  1.00 89.69           N  
ANISOU 2328  NH1 ARG B  10    10183  11968  11926    836   1270    -27       N  
ATOM   2329  NH2 ARG B  10      82.630  13.804   8.268  1.00 97.71           N  
ANISOU 2329  NH2 ARG B  10    11014  13285  12826    797   1252     58       N  
ATOM   2330  N   GLU B  11      75.852  10.806   3.900  1.00 70.63           N  
ANISOU 2330  N   GLU B  11     8170   9411   9256    293   1660  -1137       N  
ATOM   2331  CA  GLU B  11      75.594  10.363   2.532  1.00 70.59           C  
ANISOU 2331  CA  GLU B  11     8185   9476   9159    165   1780  -1373       C  
ATOM   2332  C   GLU B  11      74.776  11.384   1.744  1.00 62.36           C  
ANISOU 2332  C   GLU B  11     7181   8638   7877     -4   1616  -1407       C  
ATOM   2333  O   GLU B  11      75.137  11.733   0.615  1.00 69.51           O  
ANISOU 2333  O   GLU B  11     8066   9720   8624   -102   1634  -1487       O  
ATOM   2334  CB  GLU B  11      74.903   8.998   2.559  1.00 91.45           C  
ANISOU 2334  CB  GLU B  11    10883  11913  11952    167   1959  -1555       C  
ATOM   2335  CG  GLU B  11      74.494   8.457   1.193  1.00109.94           C  
ANISOU 2335  CG  GLU B  11    13259  14321  14193      7   2090  -1829       C  
ATOM   2336  CD  GLU B  11      74.046   6.998   1.250  1.00126.46           C  
ANISOU 2336  CD  GLU B  11    15403  16180  16465     15   2314  -2019       C  
ATOM   2337  OE1 GLU B  11      73.012   6.663   0.627  1.00131.05           O  
ANISOU 2337  OE1 GLU B  11    16042  16782  16967   -145   2338  -2217       O  
ATOM   2338  OE2 GLU B  11      74.716   6.191   1.936  1.00132.21           O  
ANISOU 2338  OE2 GLU B  11    16111  16706  17417    180   2467  -1963       O  
ATOM   2339  N   TRP B  12      73.655  11.862   2.312  1.00 58.84           N  
ANISOU 2339  N   TRP B  12     6786   8172   7400    -37   1462  -1342       N  
ATOM   2340  CA  TRP B  12      72.810  12.816   1.593  1.00 53.36           C  
ANISOU 2340  CA  TRP B  12     6117   7667   6492   -181   1307  -1353       C  
ATOM   2341  C   TRP B  12      73.545  14.135   1.363  1.00 58.94           C  
ANISOU 2341  C   TRP B  12     6791   8551   7054   -191   1179  -1191       C  
ATOM   2342  O   TRP B  12      73.553  14.672   0.247  1.00 63.02           O  
ANISOU 2342  O   TRP B  12     7300   9260   7383   -304   1147  -1239       O  
ATOM   2343  CB  TRP B  12      71.491  13.066   2.353  1.00 48.80           C  
ANISOU 2343  CB  TRP B  12     5587   7016   5937   -191   1179  -1296       C  
ATOM   2344  CG  TRP B  12      70.561  13.983   1.562  1.00 56.28           C  
ANISOU 2344  CG  TRP B  12     6545   8163   6676   -327   1030  -1300       C  
ATOM   2345  CD1 TRP B  12      69.602  13.595   0.672  1.00 59.30           C  
ANISOU 2345  CD1 TRP B  12     6936   8636   6960   -462   1046  -1473       C  
ATOM   2346  CD2 TRP B  12      70.536  15.424   1.566  1.00 54.19           C  
ANISOU 2346  CD2 TRP B  12     6280   8037   6275   -340    852  -1117       C  
ATOM   2347  NE1 TRP B  12      68.986  14.691   0.120  1.00 57.26           N  
ANISOU 2347  NE1 TRP B  12     6669   8577   6512   -546    881  -1393       N  
ATOM   2348  CE2 TRP B  12      69.550  15.826   0.638  1.00 55.18           C  
ANISOU 2348  CE2 TRP B  12     6405   8333   6228   -469    769  -1174       C  
ATOM   2349  CE3 TRP B  12      71.271  16.408   2.238  1.00 54.60           C  
ANISOU 2349  CE3 TRP B  12     6327   8087   6330   -264    763   -914       C  
ATOM   2350  CZ2 TRP B  12      69.267  17.167   0.379  1.00 50.95           C  
ANISOU 2350  CZ2 TRP B  12     5870   7948   5541   -502    607  -1018       C  
ATOM   2351  CZ3 TRP B  12      70.987  17.736   1.986  1.00 48.37           C  
ANISOU 2351  CZ3 TRP B  12     5551   7434   5393   -313    613   -780       C  
ATOM   2352  CH2 TRP B  12      69.990  18.106   1.064  1.00 53.06           C  
ANISOU 2352  CH2 TRP B  12     6149   8181   5833   -421    540   -824       C  
ATOM   2353  N   ILE B  13      74.200  14.649   2.409  1.00 56.39           N  
ANISOU 2353  N   ILE B  13     6448   8167   6812    -81   1112   -998       N  
ATOM   2354  CA  ILE B  13      74.885  15.938   2.345  1.00 59.19           C  
ANISOU 2354  CA  ILE B  13     6778   8666   7045    -98    992   -837       C  
ATOM   2355  C   ILE B  13      75.993  15.954   1.299  1.00 58.53           C  
ANISOU 2355  C   ILE B  13     6636   8726   6878   -136   1087   -894       C  
ATOM   2356  O   ILE B  13      76.208  16.978   0.640  1.00 56.40           O  
ANISOU 2356  O   ILE B  13     6363   8628   6439   -219   1004   -834       O  
ATOM   2357  CB  ILE B  13      75.426  16.292   3.748  1.00 56.97           C  
ANISOU 2357  CB  ILE B  13     6482   8283   6881     17    926   -646       C  
ATOM   2358  CG1 ILE B  13      74.248  16.571   4.691  1.00 52.21           C  
ANISOU 2358  CG1 ILE B  13     5950   7572   6315     29    813   -578       C  
ATOM   2359  CG2 ILE B  13      76.401  17.478   3.678  1.00 45.21           C  
ANISOU 2359  CG2 ILE B  13     4956   6935   5288     -8    841   -501       C  
ATOM   2360  CD1 ILE B  13      74.633  17.203   5.997  1.00 55.67           C  
ANISOU 2360  CD1 ILE B  13     6393   7949   6811    101    718   -388       C  
ATOM   2361  N   LEU B  14      76.644  14.812   1.050  1.00 63.03           N  
ANISOU 2361  N   LEU B  14     7163   9227   7560    -84   1274  -1019       N  
ATOM   2362  CA  LEU B  14      77.750  14.780   0.093  1.00 66.12           C  
ANISOU 2362  CA  LEU B  14     7491   9746   7885   -111   1386  -1077       C  
ATOM   2363  C   LEU B  14      77.321  14.398  -1.312  1.00 73.79           C  
ANISOU 2363  C   LEU B  14     8492  10828   8715   -247   1478  -1291       C  
ATOM   2364  O   LEU B  14      78.106  14.575  -2.250  1.00 78.73           O  
ANISOU 2364  O   LEU B  14     9080  11598   9236   -302   1551  -1340       O  
ATOM   2365  CB  LEU B  14      78.841  13.810   0.554  1.00 64.92           C  
ANISOU 2365  CB  LEU B  14     7262   9470   7935     32   1557  -1080       C  
ATOM   2366  CG  LEU B  14      79.362  14.043   1.969  1.00 66.02           C  
ANISOU 2366  CG  LEU B  14     7354   9518   8213    169   1476   -868       C  
ATOM   2367  CD1 LEU B  14      80.333  12.958   2.344  1.00 63.72           C  
ANISOU 2367  CD1 LEU B  14     6976   9109   8125    320   1656   -870       C  
ATOM   2368  CD2 LEU B  14      80.026  15.426   2.059  1.00 61.00           C  
ANISOU 2368  CD2 LEU B  14     6680   9049   7448    126   1325   -695       C  
ATOM   2369  N   THR B  15      76.142  13.804  -1.477  1.00 79.11           N  
ANISOU 2369  N   THR B  15     9229  11443   9387   -309   1490  -1431       N  
ATOM   2370  CA  THR B  15      75.582  13.642  -2.812  1.00 72.89           C  
ANISOU 2370  CA  THR B  15     8472  10807   8417   -473   1533  -1622       C  
ATOM   2371  C   THR B  15      74.629  14.786  -3.151  1.00 64.40           C  
ANISOU 2371  C   THR B  15     7430   9904   7136   -582   1320  -1532       C  
ATOM   2372  O   THR B  15      74.984  15.723  -3.871  1.00 64.82           O  
ANISOU 2372  O   THR B  15     7469  10152   7007   -651   1249  -1460       O  
ATOM   2373  CB  THR B  15      74.865  12.296  -2.936  1.00 73.28           C  
ANISOU 2373  CB  THR B  15     8561  10717   8566   -505   1684  -1850       C  
ATOM   2374  OG1 THR B  15      73.763  12.257  -2.022  1.00 72.88           O  
ANISOU 2374  OG1 THR B  15     8549  10542   8599   -477   1575  -1794       O  
ATOM   2375  CG2 THR B  15      75.821  11.151  -2.613  1.00 66.08           C  
ANISOU 2375  CG2 THR B  15     7618   9613   7876   -380   1916  -1925       C  
ATOM   2376  N   GLU B  16      73.410  14.704  -2.671  1.00 71.06           N  
ANISOU 2376  N   GLU B  16     8312  10679   8010   -596   1229  -1533       N  
ATOM   2377  CA  GLU B  16      72.366  15.691  -2.955  1.00 71.54           C  
ANISOU 2377  CA  GLU B  16     8394  10890   7900   -684   1038  -1446       C  
ATOM   2378  C   GLU B  16      72.494  17.094  -2.410  1.00 69.57           C  
ANISOU 2378  C   GLU B  16     8146  10681   7606   -632    864  -1190       C  
ATOM   2379  O   GLU B  16      72.013  18.013  -3.011  1.00 68.02           O  
ANISOU 2379  O   GLU B  16     7956  10653   7233   -709    742  -1113       O  
ATOM   2380  CB  GLU B  16      71.014  15.161  -2.554  1.00 77.87           C  
ANISOU 2380  CB  GLU B  16     9223  11601   8764   -709   1002  -1521       C  
ATOM   2381  CG  GLU B  16      70.533  13.965  -3.333  1.00 89.74           C  
ANISOU 2381  CG  GLU B  16    10734  13118  10245   -824   1144  -1792       C  
ATOM   2382  CD  GLU B  16      70.462  14.248  -4.795  1.00112.19           C  
ANISOU 2382  CD  GLU B  16    13564  16232  12829   -989   1133  -1893       C  
ATOM   2383  OE1 GLU B  16      70.045  15.352  -5.153  1.00119.39           O  
ANISOU 2383  OE1 GLU B  16    14464  17330  13569  -1036    961  -1751       O  
ATOM   2384  OE2 GLU B  16      70.830  13.365  -5.583  1.00119.79           O  
ANISOU 2384  OE2 GLU B  16    14532  17222  13762  -1071   1305  -2111       O  
ATOM   2385  N   GLY B  17      73.105  17.256  -1.261  1.00 65.03           N  
ANISOU 2385  N   GLY B  17     7567   9951   7190   -504    854  -1057       N  
ATOM   2386  CA  GLY B  17      73.322  18.579  -0.706  1.00 63.19           C  
ANISOU 2386  CA  GLY B  17     7344   9743   6921   -468    710   -830       C  
ATOM   2387  C   GLY B  17      74.398  19.363  -1.411  1.00 73.37           C  
ANISOU 2387  C   GLY B  17     8606  11190   8082   -509    713   -760       C  
ATOM   2388  O   GLY B  17      74.598  20.539  -1.084  1.00 71.09           O  
ANISOU 2388  O   GLY B  17     8333  10933   7746   -503    604   -580       O  
ATOM   2389  N   LYS B  18      75.082  18.705  -2.367  1.00 75.68           N  
ANISOU 2389  N   LYS B  18     8861  11570   8322   -557    852   -908       N  
ATOM   2390  CA  LYS B  18      76.110  19.281  -3.241  1.00 77.81           C  
ANISOU 2390  CA  LYS B  18     9099  12009   8456   -614    888   -878       C  
ATOM   2391  C   LYS B  18      77.370  19.704  -2.488  1.00 75.11           C  
ANISOU 2391  C   LYS B  18     8710  11611   8216   -528    899   -738       C  
ATOM   2392  O   LYS B  18      78.089  20.604  -2.921  1.00 68.02           O  
ANISOU 2392  O   LYS B  18     7795  10841   7207   -575    872   -641       O  
ATOM   2393  CB  LYS B  18      75.549  20.465  -4.035  1.00 76.38           C  
ANISOU 2393  CB  LYS B  18     8953  12017   8053   -720    755   -780       C  
ATOM   2394  CG  LYS B  18      74.420  20.089  -4.975  1.00 79.11           C  
ANISOU 2394  CG  LYS B  18     9320  12483   8256   -826    739   -914       C  
ATOM   2395  CD  LYS B  18      73.499  21.285  -5.168  1.00 89.83           C  
ANISOU 2395  CD  LYS B  18    10710  13951   9472   -870    561   -748       C  
ATOM   2396  CE  LYS B  18      72.936  21.372  -6.571  1.00 99.02           C  
ANISOU 2396  CE  LYS B  18    11869  15362  10391  -1009    539   -820       C  
ATOM   2397  NZ  LYS B  18      72.405  22.736  -6.835  1.00100.72           N  
ANISOU 2397  NZ  LYS B  18    12105  15700  10463  -1032    381   -603       N  
ATOM   2398  N   ALA B  19      77.683  19.033  -1.386  1.00 72.09           N  
ANISOU 2398  N   ALA B  19     8301  11050   8039   -408    944   -726       N  
ATOM   2399  CA  ALA B  19      78.878  19.336  -0.621  1.00 62.82           C  
ANISOU 2399  CA  ALA B  19     7065   9843   6961   -329    950   -595       C  
ATOM   2400  C   ALA B  19      79.931  18.269  -0.880  1.00 65.91           C  
ANISOU 2400  C   ALA B  19     7369  10215   7458   -266   1138   -703       C  
ATOM   2401  O   ALA B  19      79.622  17.147  -1.279  1.00 69.34           O  
ANISOU 2401  O   ALA B  19     7810  10586   7950   -254   1270   -877       O  
ATOM   2402  CB  ALA B  19      78.562  19.406   0.875  1.00 55.12           C  
ANISOU 2402  CB  ALA B  19     6110   8701   6133   -233    860   -475       C  
ATOM   2403  N   THR B  20      81.186  18.612  -0.607  1.00 62.14           N  
ANISOU 2403  N   THR B  20     6807   9785   7018   -226   1159   -599       N  
ATOM   2404  CA  THR B  20      82.270  17.641  -0.674  1.00 65.33           C  
ANISOU 2404  CA  THR B  20     7107  10162   7555   -135   1337   -663       C  
ATOM   2405  C   THR B  20      82.950  17.434   0.665  1.00 65.31           C  
ANISOU 2405  C   THR B  20     7025  10055   7735      3   1318   -521       C  
ATOM   2406  O   THR B  20      83.641  16.423   0.838  1.00 61.98           O  
ANISOU 2406  O   THR B  20     6518   9562   7471    117   1466   -560       O  
ATOM   2407  CB  THR B  20      83.341  18.039  -1.717  1.00 69.15           C  
ANISOU 2407  CB  THR B  20     7520  10829   7923   -206   1420   -682       C  
ATOM   2408  OG1 THR B  20      83.940  19.289  -1.352  1.00 71.52           O  
ANISOU 2408  OG1 THR B  20     7791  11230   8154   -246   1291   -498       O  
ATOM   2409  CG2 THR B  20      82.745  18.165  -3.113  1.00 69.42           C  
ANISOU 2409  CG2 THR B  20     7626  10990   7758   -347   1453   -826       C  
ATOM   2410  N   GLN B  21      82.790  18.356   1.611  1.00 67.30           N  
ANISOU 2410  N   GLN B  21     7302  10299   7969     -5   1146   -354       N  
ATOM   2411  CA  GLN B  21      83.360  18.141   2.929  1.00 64.95           C  
ANISOU 2411  CA  GLN B  21     6933   9921   7825    113   1115   -219       C  
ATOM   2412  C   GLN B  21      82.501  18.777   4.014  1.00 61.00           C  
ANISOU 2412  C   GLN B  21     6524   9337   7318    102    945   -109       C  
ATOM   2413  O   GLN B  21      81.898  19.837   3.818  1.00 59.50           O  
ANISOU 2413  O   GLN B  21     6421   9198   6990     -6    827    -74       O  
ATOM   2414  CB  GLN B  21      84.810  18.635   2.945  1.00 70.88           C  
ANISOU 2414  CB  GLN B  21     7551  10816   8566    112   1126   -112       C  
ATOM   2415  CG  GLN B  21      84.985  20.115   2.741  1.00 87.90           C  
ANISOU 2415  CG  GLN B  21     9737  13111  10550    -30    996    -18       C  
ATOM   2416  CD  GLN B  21      86.433  20.523   2.888  1.00102.00           C  
ANISOU 2416  CD  GLN B  21    11377  15034  12343    -35   1009     87       C  
ATOM   2417  OE1 GLN B  21      87.328  19.667   2.921  1.00103.69           O  
ANISOU 2417  OE1 GLN B  21    11456  15261  12680     70   1131     77       O  
ATOM   2418  NE2 GLN B  21      86.677  21.833   2.981  1.00105.94           N  
ANISOU 2418  NE2 GLN B  21    11900  15634  12719   -159    893    190       N  
ATOM   2419  N   ILE B  22      82.431  18.086   5.145  1.00 58.68           N  
ANISOU 2419  N   ILE B  22     6210   8908   7177    222    946    -53       N  
ATOM   2420  CA  ILE B  22      81.774  18.561   6.356  1.00 51.08           C  
ANISOU 2420  CA  ILE B  22     5319   7860   6229    228    804     58       C  
ATOM   2421  C   ILE B  22      82.865  19.112   7.270  1.00 52.51           C  
ANISOU 2421  C   ILE B  22     5407   8121   6422    245    731    227       C  
ATOM   2422  O   ILE B  22      83.766  18.373   7.670  1.00 50.48           O  
ANISOU 2422  O   ILE B  22     5027   7869   6283    355    803    276       O  
ATOM   2423  CB  ILE B  22      80.982  17.428   7.026  1.00 50.48           C  
ANISOU 2423  CB  ILE B  22     5285   7594   6303    338    857     14       C  
ATOM   2424  CG1 ILE B  22      79.925  16.900   6.042  1.00 49.44           C  
ANISOU 2424  CG1 ILE B  22     5236   7406   6145    292    932   -171       C  
ATOM   2425  CG2 ILE B  22      80.360  17.906   8.351  1.00 48.10           C  
ANISOU 2425  CG2 ILE B  22     5054   7208   6013    346    720    135       C  
ATOM   2426  CD1 ILE B  22      79.149  15.710   6.530  1.00 55.46           C  
ANISOU 2426  CD1 ILE B  22     6039   7976   7057    381   1013   -243       C  
ATOM   2427  N   THR B  23      82.836  20.427   7.536  1.00 49.94           N  
ANISOU 2427  N   THR B  23     5132   7870   5972    131    596    315       N  
ATOM   2428  CA  THR B  23      83.889  21.104   8.287  1.00 53.03           C  
ANISOU 2428  CA  THR B  23     5439   8368   6343    101    522    457       C  
ATOM   2429  C   THR B  23      83.572  21.312   9.770  1.00 59.33           C  
ANISOU 2429  C   THR B  23     6280   9090   7174    122    411    568       C  
ATOM   2430  O   THR B  23      84.496  21.540  10.556  1.00 63.67           O  
ANISOU 2430  O   THR B  23     6734   9728   7730    120    361    683       O  
ATOM   2431  CB  THR B  23      84.236  22.446   7.629  1.00 50.51           C  
ANISOU 2431  CB  THR B  23     5143   8184   5864    -57    467    480       C  
ATOM   2432  OG1 THR B  23      83.095  23.311   7.657  1.00 54.56           O  
ANISOU 2432  OG1 THR B  23     5816   8625   6288   -142    379    477       O  
ATOM   2433  CG2 THR B  23      84.681  22.229   6.201  1.00 51.24           C  
ANISOU 2433  CG2 THR B  23     5182   8374   5912    -80    580    382       C  
ATOM   2434  N   LYS B  24      82.309  21.244  10.180  1.00 58.61           N  
ANISOU 2434  N   LYS B  24     6321   8851   7096    133    373    537       N  
ATOM   2435  CA  LYS B  24      81.990  21.392  11.592  1.00 56.69           C  
ANISOU 2435  CA  LYS B  24     6125   8535   6881    151    283    634       C  
ATOM   2436  C   LYS B  24      80.620  20.789  11.876  1.00 56.28           C  
ANISOU 2436  C   LYS B  24     6186   8301   6895    212    299    571       C  
ATOM   2437  O   LYS B  24      79.710  20.853  11.043  1.00 61.33           O  
ANISOU 2437  O   LYS B  24     6908   8893   7504    178    323    468       O  
ATOM   2438  CB  LYS B  24      82.015  22.865  12.023  1.00 49.03           C  
ANISOU 2438  CB  LYS B  24     5227   7624   5780      4    165    707       C  
ATOM   2439  CG  LYS B  24      82.070  23.037  13.519  1.00 57.43           C  
ANISOU 2439  CG  LYS B  24     6307   8661   6854      4     80    813       C  
ATOM   2440  CD  LYS B  24      81.988  24.485  13.887  1.00 64.02           C  
ANISOU 2440  CD  LYS B  24     7236   9527   7563   -155    -12    855       C  
ATOM   2441  CE  LYS B  24      81.835  24.653  15.367  1.00 63.69           C  
ANISOU 2441  CE  LYS B  24     7240   9445   7516   -170    -87    934       C  
ATOM   2442  NZ  LYS B  24      81.441  26.061  15.656  1.00 66.75           N  
ANISOU 2442  NZ  LYS B  24     7762   9806   7792   -326   -149    943       N  
ATOM   2443  N   ILE B  25      80.487  20.229  13.080  1.00 53.40           N  
ANISOU 2443  N   ILE B  25     5822   7851   6615    295    280    643       N  
ATOM   2444  CA  ILE B  25      79.228  19.693  13.600  1.00 52.89           C  
ANISOU 2444  CA  ILE B  25     5865   7612   6620    348    290    605       C  
ATOM   2445  C   ILE B  25      79.081  20.182  15.035  1.00 47.88           C  
ANISOU 2445  C   ILE B  25     5283   6950   5960    328    190    722       C  
ATOM   2446  O   ILE B  25      79.933  19.881  15.878  1.00 52.08           O  
ANISOU 2446  O   ILE B  25     5728   7539   6521    378    170    832       O  
ATOM   2447  CB  ILE B  25      79.181  18.162  13.559  1.00 50.18           C  
ANISOU 2447  CB  ILE B  25     5468   7163   6435    494    416    558       C  
ATOM   2448  CG1 ILE B  25      79.266  17.645  12.129  1.00 49.61           C  
ANISOU 2448  CG1 ILE B  25     5358   7111   6381    498    533    416       C  
ATOM   2449  CG2 ILE B  25      77.889  17.664  14.178  1.00 45.44           C  
ANISOU 2449  CG2 ILE B  25     4978   6383   5902    533    425    526       C  
ATOM   2450  CD1 ILE B  25      79.198  16.127  12.031  1.00 47.14           C  
ANISOU 2450  CD1 ILE B  25     5008   6669   6235    631    685    349       C  
ATOM   2451  N   GLY B  26      78.060  20.999  15.290  1.00 46.27           N  
ANISOU 2451  N   GLY B  26     5214   6676   5691    247    128    705       N  
ATOM   2452  CA  GLY B  26      77.715  21.452  16.635  1.00 44.34           C  
ANISOU 2452  CA  GLY B  26     5047   6380   5419    218     52    789       C  
ATOM   2453  C   GLY B  26      76.355  20.904  17.044  1.00 51.43           C  
ANISOU 2453  C   GLY B  26     6047   7101   6392    275     82    742       C  
ATOM   2454  O   GLY B  26      75.377  21.065  16.308  1.00 47.08           O  
ANISOU 2454  O   GLY B  26     5563   6485   5840    251    103    649       O  
ATOM   2455  N   SER B  27      76.305  20.262  18.228  1.00 48.05           N  
ANISOU 2455  N   SER B  27     5622   6607   6025    346     82    815       N  
ATOM   2456  CA  SER B  27      75.136  19.492  18.678  1.00 53.04           C  
ANISOU 2456  CA  SER B  27     6332   7068   6753    417    133    778       C  
ATOM   2457  C   SER B  27      74.664  19.925  20.059  1.00 50.64           C  
ANISOU 2457  C   SER B  27     6123   6709   6409    385     74    857       C  
ATOM   2458  O   SER B  27      75.469  20.028  20.996  1.00 44.83           O  
ANISOU 2458  O   SER B  27     5350   6054   5628    379     23    969       O  
ATOM   2459  CB  SER B  27      75.444  17.993  18.726  1.00 50.05           C  
ANISOU 2459  CB  SER B  27     5871   6629   6517    560    232    785       C  
ATOM   2460  OG  SER B  27      75.651  17.507  17.420  1.00 54.00           O  
ANISOU 2460  OG  SER B  27     6309   7147   7063    584    314    679       O  
ATOM   2461  N   VAL B  28      73.345  20.102  20.195  1.00 47.78           N  
ANISOU 2461  N   VAL B  28     5873   6215   6064    365     87    797       N  
ATOM   2462  CA  VAL B  28      72.692  20.373  21.470  1.00 49.34           C  
ANISOU 2462  CA  VAL B  28     6174   6331   6242    344     61    850       C  
ATOM   2463  C   VAL B  28      71.541  19.380  21.651  1.00 56.29           C  
ANISOU 2463  C   VAL B  28     7098   7044   7244    426    141    799       C  
ATOM   2464  O   VAL B  28      71.185  18.628  20.740  1.00 52.54           O  
ANISOU 2464  O   VAL B  28     6585   6520   6857    478    210    709       O  
ATOM   2465  CB  VAL B  28      72.171  21.821  21.559  1.00 44.66           C  
ANISOU 2465  CB  VAL B  28     5688   5737   5544    221      5    834       C  
ATOM   2466  CG1 VAL B  28      73.305  22.803  21.362  1.00 39.23           C  
ANISOU 2466  CG1 VAL B  28     4962   5202   4740    123    -60    876       C  
ATOM   2467  CG2 VAL B  28      71.081  22.045  20.509  1.00 44.09           C  
ANISOU 2467  CG2 VAL B  28     5652   5592   5506    214     38    731       C  
ATOM   2468  N   GLY B  29      70.979  19.357  22.863  1.00 53.44           N  
ANISOU 2468  N   GLY B  29     6821   6601   6884    428    138    852       N  
ATOM   2469  CA  GLY B  29      69.836  18.488  23.115  1.00 45.41           C  
ANISOU 2469  CA  GLY B  29     5852   5422   5979    492    218    806       C  
ATOM   2470  C   GLY B  29      70.256  17.071  23.459  1.00 48.26           C  
ANISOU 2470  C   GLY B  29     6151   5733   6452    612    291    857       C  
ATOM   2471  O   GLY B  29      71.346  16.833  23.965  1.00 54.11           O  
ANISOU 2471  O   GLY B  29     6827   6561   7170    653    264    969       O  
ATOM   2472  N   GLY B  30      69.380  16.117  23.167  1.00 50.54           N  
ANISOU 2472  N   GLY B  30     6454   5880   6868    668    389    777       N  
ATOM   2473  CA  GLY B  30      69.717  14.725  23.399  1.00 51.53           C  
ANISOU 2473  CA  GLY B  30     6530   5925   7122    787    486    818       C  
ATOM   2474  C   GLY B  30      69.566  14.216  24.827  1.00 57.33           C  
ANISOU 2474  C   GLY B  30     7316   6582   7885    844    507    945       C  
ATOM   2475  O   GLY B  30      69.801  13.026  25.064  1.00 68.07           O  
ANISOU 2475  O   GLY B  30     8642   7857   9365    954    600    996       O  
ATOM   2476  N   GLY B  31      69.205  15.058  25.794  1.00 58.73           N  
ANISOU 2476  N   GLY B  31     7578   6782   7955    773    434   1002       N  
ATOM   2477  CA  GLY B  31      69.044  14.568  27.151  1.00 64.62           C  
ANISOU 2477  CA  GLY B  31     8377   7465   8709    817    456   1123       C  
ATOM   2478  C   GLY B  31      67.869  13.614  27.269  1.00 70.11           C  
ANISOU 2478  C   GLY B  31     9132   7962   9547    866    580   1063       C  
ATOM   2479  O   GLY B  31      66.990  13.555  26.411  1.00 70.54           O  
ANISOU 2479  O   GLY B  31     9199   7935   9668    835    630    916       O  
ATOM   2480  N   CYS B  32      67.818  12.879  28.378  1.00 71.80           N  
ANISOU 2480  N   CYS B  32     9380   8103   9798    933    628   1184       N  
ATOM   2481  CA  CYS B  32      66.714  11.956  28.605  1.00 73.59           C  
ANISOU 2481  CA  CYS B  32     9669   8132  10161    971    756   1138       C  
ATOM   2482  C   CYS B  32      65.775  12.478  29.682  1.00 66.81           C  
ANISOU 2482  C   CYS B  32     8927   7226   9231    903    743   1161       C  
ATOM   2483  O   CYS B  32      66.204  13.091  30.661  1.00 67.90           O  
ANISOU 2483  O   CYS B  32     9102   7464   9232    869    663   1276       O  
ATOM   2484  CB  CYS B  32      67.225  10.555  28.940  1.00 89.46           C  
ANISOU 2484  CB  CYS B  32    11637  10050  12303   1111    862   1248       C  
ATOM   2485  SG  CYS B  32      68.290   9.884  27.599  1.00110.14           S  
ANISOU 2485  SG  CYS B  32    14118  12700  15030   1198    914   1200       S  
ATOM   2486  N   ILE B  33      64.485  12.220  29.474  1.00 65.23           N  
ANISOU 2486  N   ILE B  33     8780   6880   9123    875    828   1044       N  
ATOM   2487  CA  ILE B  33      63.428  12.731  30.331  1.00 59.15           C  
ANISOU 2487  CA  ILE B  33     8117   6051   8308    809    837   1037       C  
ATOM   2488  C   ILE B  33      63.306  11.855  31.577  1.00 58.49           C  
ANISOU 2488  C   ILE B  33     8092   5873   8260    870    916   1168       C  
ATOM   2489  O   ILE B  33      63.664  10.680  31.577  1.00 56.52           O  
ANISOU 2489  O   ILE B  33     7804   5545   8125    969    999   1230       O  
ATOM   2490  CB  ILE B  33      62.114  12.749  29.527  1.00 52.64           C  
ANISOU 2490  CB  ILE B  33     7298   5125   7577    759    899    864       C  
ATOM   2491  CG1 ILE B  33      62.220  13.757  28.395  1.00 68.28           C  
ANISOU 2491  CG1 ILE B  33     9229   7221   9495    696    808    764       C  
ATOM   2492  CG2 ILE B  33      60.922  13.029  30.390  1.00 61.42           C  
ANISOU 2492  CG2 ILE B  33     8505   6146   8685    711    944    855       C  
ATOM   2493  CD1 ILE B  33      61.082  13.671  27.378  1.00 78.59           C  
ANISOU 2493  CD1 ILE B  33    10504   8467  10889    656    854    602       C  
ATOM   2494  N   ASN B  34      62.772  12.432  32.651  1.00 60.09           N  
ANISOU 2494  N   ASN B  34     8392   6073   8366    810    902   1214       N  
ATOM   2495  CA  ASN B  34      62.622  11.677  33.885  1.00 57.79           C  
ANISOU 2495  CA  ASN B  34     8166   5706   8085    857    974   1348       C  
ATOM   2496  C   ASN B  34      61.632  10.546  33.676  1.00 58.05           C  
ANISOU 2496  C   ASN B  34     8213   5534   8309    902   1130   1283       C  
ATOM   2497  O   ASN B  34      60.679  10.673  32.901  1.00 60.73           O  
ANISOU 2497  O   ASN B  34     8544   5799   8730    852   1172   1119       O  
ATOM   2498  CB  ASN B  34      62.152  12.572  35.026  1.00 59.94           C  
ANISOU 2498  CB  ASN B  34     8550   6017   8207    765    942   1383       C  
ATOM   2499  CG  ASN B  34      63.260  13.432  35.588  1.00 63.29           C  
ANISOU 2499  CG  ASN B  34     8976   6641   8432    717    808   1486       C  
ATOM   2500  OD1 ASN B  34      64.440  13.162  35.380  1.00 64.98           O  
ANISOU 2500  OD1 ASN B  34     9101   6968   8620    774    743   1579       O  
ATOM   2501  ND2 ASN B  34      62.882  14.466  36.317  1.00 62.65           N  
ANISOU 2501  ND2 ASN B  34     8992   6603   8207    607    776   1466       N  
ATOM   2502  N   LEU B  35      61.908   9.406  34.302  1.00 49.76           N  
ANISOU 2502  N   LEU B  35     7172   4399   7336    997   1218   1415       N  
ATOM   2503  CA  LEU B  35      60.918   8.352  34.429  1.00 52.65           C  
ANISOU 2503  CA  LEU B  35     7581   4556   7869   1023   1382   1377       C  
ATOM   2504  C   LEU B  35      60.070   8.641  35.659  1.00 59.77           C  
ANISOU 2504  C   LEU B  35     8597   5418   8697    966   1415   1429       C  
ATOM   2505  O   LEU B  35      60.613   8.831  36.755  1.00 57.31           O  
ANISOU 2505  O   LEU B  35     8333   5193   8249    979   1366   1595       O  
ATOM   2506  CB  LEU B  35      61.608   6.990  34.548  1.00 55.08           C  
ANISOU 2506  CB  LEU B  35     7855   4768   8304   1159   1482   1507       C  
ATOM   2507  CG  LEU B  35      60.810   5.695  34.410  1.00 57.04           C  
ANISOU 2507  CG  LEU B  35     8131   4775   8764   1197   1678   1456       C  
ATOM   2508  CD1 LEU B  35      60.332   5.549  33.000  1.00 60.45           C  
ANISOU 2508  CD1 LEU B  35     8505   5146   9318   1147   1723   1226       C  
ATOM   2509  CD2 LEU B  35      61.691   4.522  34.764  1.00 53.42           C  
ANISOU 2509  CD2 LEU B  35     7651   4240   8405   1348   1767   1640       C  
ATOM   2510  N   ALA B  36      58.748   8.648  35.480  1.00 57.01           N  
ANISOU 2510  N   ALA B  36     8284   4947   8431    899   1501   1288       N  
ATOM   2511  CA  ALA B  36      57.792   8.897  36.552  1.00 55.05           C  
ANISOU 2511  CA  ALA B  36     8140   4641   8135    840   1559   1311       C  
ATOM   2512  C   ALA B  36      57.009   7.621  36.857  1.00 58.45           C  
ANISOU 2512  C   ALA B  36     8605   4867   8735    874   1738   1321       C  
ATOM   2513  O   ALA B  36      56.403   7.032  35.957  1.00 62.21           O  
ANISOU 2513  O   ALA B  36     9033   5230   9376    864   1823   1180       O  
ATOM   2514  CB  ALA B  36      56.825  10.019  36.154  1.00 54.51           C  
ANISOU 2514  CB  ALA B  36     8079   4602   8032    735   1524   1149       C  
ATOM   2515  N   SER B  37      56.996   7.205  38.123  1.00 56.85           N  
ANISOU 2515  N   SER B  37     8492   4622   8488    902   1799   1482       N  
ATOM   2516  CA  SER B  37      56.474   5.893  38.487  1.00 57.66           C  
ANISOU 2516  CA  SER B  37     8633   4526   8751    950   1977   1532       C  
ATOM   2517  C   SER B  37      55.539   5.951  39.688  1.00 60.26           C  
ANISOU 2517  C   SER B  37     9075   4791   9032    894   2064   1582       C  
ATOM   2518  O   SER B  37      55.815   6.629  40.682  1.00 61.67           O  
ANISOU 2518  O   SER B  37     9322   5089   9022    869   1993   1694       O  
ATOM   2519  CB  SER B  37      57.606   4.904  38.802  1.00 60.45           C  
ANISOU 2519  CB  SER B  37     8972   4858   9139   1086   2004   1735       C  
ATOM   2520  OG  SER B  37      58.426   4.686  37.670  1.00 57.84           O  
ANISOU 2520  OG  SER B  37     8535   4558   8884   1146   1960   1682       O  
ATOM   2521  N   HIS B  38      54.456   5.188  39.591  1.00 57.18           N  
ANISOU 2521  N   HIS B  38     8684   4249   8791    859   2208   1479       N  
ATOM   2522  CA  HIS B  38      53.525   4.924  40.681  1.00 62.59           C  
ANISOU 2522  CA  HIS B  38     9443   4886   9452    807   2307   1506       C  
ATOM   2523  C   HIS B  38      53.858   3.566  41.307  1.00 68.54           C  
ANISOU 2523  C   HIS B  38    10207   5575  10261    885   2400   1645       C  
ATOM   2524  O   HIS B  38      53.776   2.532  40.638  1.00 67.92           O  
ANISOU 2524  O   HIS B  38    10061   5403  10342    912   2482   1573       O  
ATOM   2525  CB  HIS B  38      52.095   4.953  40.134  1.00 65.10           C  
ANISOU 2525  CB  HIS B  38     9718   5133   9885    706   2387   1287       C  
ATOM   2526  CG  HIS B  38      51.033   4.700  41.158  1.00 73.78           C  
ANISOU 2526  CG  HIS B  38    10879   6178  10977    648   2502   1294       C  
ATOM   2527  ND1 HIS B  38      49.697   4.597  40.827  1.00 76.48           N  
ANISOU 2527  ND1 HIS B  38    11174   6460  11426    561   2591   1125       N  
ATOM   2528  CD2 HIS B  38      51.101   4.517  42.499  1.00 78.04           C  
ANISOU 2528  CD2 HIS B  38    11519   6721  11413    663   2546   1454       C  
ATOM   2529  CE1 HIS B  38      48.990   4.379  41.922  1.00 77.52           C  
ANISOU 2529  CE1 HIS B  38    11376   6553  11526    529   2691   1176       C  
ATOM   2530  NE2 HIS B  38      49.816   4.324  42.950  1.00 75.86           N  
ANISOU 2530  NE2 HIS B  38    11260   6377  11185    588   2667   1372       N  
ATOM   2531  N   TYR B  39      54.230   3.578  42.583  1.00 72.58           N  
ANISOU 2531  N   TYR B  39    10804   6138  10633    915   2391   1844       N  
ATOM   2532  CA  TYR B  39      54.573   2.352  43.293  1.00 73.66           C  
ANISOU 2532  CA  TYR B  39    10954   6225  10807    999   2473   2006       C  
ATOM   2533  C   TYR B  39      53.376   1.810  44.066  1.00 78.14           C  
ANISOU 2533  C   TYR B  39    11580   6694  11414    935   2618   1972       C  
ATOM   2534  O   TYR B  39      52.836   2.483  44.944  1.00 77.26           O  
ANISOU 2534  O   TYR B  39    11555   6625  11174    865   2618   1996       O  
ATOM   2535  CB  TYR B  39      55.748   2.594  44.243  1.00 77.47           C  
ANISOU 2535  CB  TYR B  39    11482   6847  11105   1074   2371   2269       C  
ATOM   2536  CG  TYR B  39      57.104   2.402  43.602  1.00 80.63           C  
ANISOU 2536  CG  TYR B  39    11793   7316  11526   1190   2279   2367       C  
ATOM   2537  CD1 TYR B  39      57.499   3.180  42.522  1.00 76.65           C  
ANISOU 2537  CD1 TYR B  39    11229   6860  11032   1180   2183   2256       C  
ATOM   2538  CD2 TYR B  39      57.989   1.444  44.078  1.00 84.78           C  
ANISOU 2538  CD2 TYR B  39    12287   7861  12066   1316   2293   2575       C  
ATOM   2539  CE1 TYR B  39      58.737   3.008  41.933  1.00 76.97           C  
ANISOU 2539  CE1 TYR B  39    11183   6968  11095   1288   2107   2345       C  
ATOM   2540  CE2 TYR B  39      59.230   1.265  43.495  1.00 84.39           C  
ANISOU 2540  CE2 TYR B  39    12140   7881  12044   1429   2216   2667       C  
ATOM   2541  CZ  TYR B  39      59.598   2.050  42.424  1.00 81.32           C  
ANISOU 2541  CZ  TYR B  39    11694   7540  11663   1413   2126   2549       C  
ATOM   2542  OH  TYR B  39      60.832   1.876  41.840  1.00 81.86           O  
ANISOU 2542  OH  TYR B  39    11660   7683  11762   1527   2057   2639       O  
ATOM   2543  N   GLN B  40      52.869   0.641  43.741  1.00 86.18           N  
ANISOU 2543  N   GLN B  40    12559   7580  12607    944   2754   1902       N  
ATOM   2544  CA  GLN B  40      51.725   0.150  44.500  1.00 88.71           C  
ANISOU 2544  CA  GLN B  40    12934   7811  12960    880   2895   1876       C  
ATOM   2545  C   GLN B  40      52.174  -0.903  45.492  1.00 96.55           C  
ANISOU 2545  C   GLN B  40    13976   8763  13945    969   2971   2090       C  
ATOM   2546  O   GLN B  40      52.774  -1.890  45.137  1.00102.92           O  
ANISOU 2546  O   GLN B  40    14736   9508  14864   1058   3018   2147       O  
ATOM   2547  CB  GLN B  40      50.627  -0.354  43.606  1.00 92.94           C  
ANISOU 2547  CB  GLN B  40    13403   8234  13678    798   3009   1647       C  
ATOM   2548  CG  GLN B  40      49.986   0.742  42.803  1.00103.58           C  
ANISOU 2548  CG  GLN B  40    14702   9633  15018    702   2938   1451       C  
ATOM   2549  CD  GLN B  40      48.932   0.228  41.851  1.00112.70           C  
ANISOU 2549  CD  GLN B  40    15774  10702  16345    614   3037   1234       C  
ATOM   2550  OE1 GLN B  40      48.957  -0.921  41.437  1.00124.77           O  
ANISOU 2550  OE1 GLN B  40    17267  12134  18007    629   3138   1204       O  
ATOM   2551  NE2 GLN B  40      47.993   1.091  41.500  1.00108.95           N  
ANISOU 2551  NE2 GLN B  40    15264  10263  15867    517   3015   1084       N  
ATOM   2552  N   THR B  41      51.876  -0.648  46.744  1.00 95.10           N  
ANISOU 2552  N   THR B  41    13890   8620  13624    942   2986   2210       N  
ATOM   2553  CA  THR B  41      52.244  -1.443  47.909  1.00 98.07           C  
ANISOU 2553  CA  THR B  41    14329   8990  13944   1015   3040   2441       C  
ATOM   2554  C   THR B  41      51.060  -1.613  48.855  1.00 96.47           C  
ANISOU 2554  C   THR B  41    14211   8723  13719    930   3169   2423       C  
ATOM   2555  O   THR B  41      50.102  -0.842  48.810  1.00101.98           O  
ANISOU 2555  O   THR B  41    14931   9424  14393    819   3187   2265       O  
ATOM   2556  CB  THR B  41      53.417  -0.808  48.679  1.00 94.43           C  
ANISOU 2556  CB  THR B  41    13908   8710  13260   1072   2883   2673       C  
ATOM   2557  OG1 THR B  41      52.923   0.224  49.542  1.00 87.31           O  
ANISOU 2557  OG1 THR B  41    13107   7902  12164    967   2846   2678       O  
ATOM   2558  CG2 THR B  41      54.429  -0.213  47.712  1.00 88.93           C  
ANISOU 2558  CG2 THR B  41    13131   8106  12553   1121   2735   2652       C  
ATOM   2559  N   ASP B  42      51.132  -2.628  49.710  1.00 98.90           N  
ANISOU 2559  N   ASP B  42    14564   8973  14041    989   3265   2590       N  
ATOM   2560  CA  ASP B  42      50.067  -2.899  50.665  1.00100.29           C  
ANISOU 2560  CA  ASP B  42    14824   9085  14198    918   3400   2594       C  
ATOM   2561  C   ASP B  42      49.891  -1.781  51.683  1.00 96.48           C  
ANISOU 2561  C   ASP B  42    14442   8737  13479    841   3329   2655       C  
ATOM   2562  O   ASP B  42      48.936  -1.823  52.462  1.00101.16           O  
ANISOU 2562  O   ASP B  42    15108   9288  14041    766   3440   2635       O  
ATOM   2563  CB  ASP B  42      50.336  -4.215  51.397  1.00104.67           C  
ANISOU 2563  CB  ASP B  42    15409   9557  14803   1010   3507   2791       C  
ATOM   2564  CG  ASP B  42      51.692  -4.237  52.080  1.00113.82           C  
ANISOU 2564  CG  ASP B  42    16585  10855  15808   1124   3380   3073       C  
ATOM   2565  OD1 ASP B  42      52.658  -3.682  51.520  1.00117.60           O  
ANISOU 2565  OD1 ASP B  42    17005  11444  16235   1173   3230   3098       O  
ATOM   2566  OD2 ASP B  42      51.791  -4.784  53.196  1.00121.39           O  
ANISOU 2566  OD2 ASP B  42    17611  11825  16687   1161   3425   3277       O  
ATOM   2567  N   ALA B  43      50.769  -0.780  51.681  1.00 92.85           N  
ANISOU 2567  N   ALA B  43    13990   8439  12849    847   3159   2721       N  
ATOM   2568  CA  ALA B  43      50.681   0.360  52.583  1.00 86.26           C  
ANISOU 2568  CA  ALA B  43    13257   7745  11771    757   3093   2765       C  
ATOM   2569  C   ALA B  43      50.371   1.657  51.845  1.00 85.06           C  
ANISOU 2569  C   ALA B  43    13088   7636  11594    672   3025   2562       C  
ATOM   2570  O   ALA B  43      50.733   2.737  52.321  1.00 91.27           O  
ANISOU 2570  O   ALA B  43    13945   8566  12168    615   2930   2605       O  
ATOM   2571  CB  ALA B  43      51.971   0.503  53.390  1.00 86.14           C  
ANISOU 2571  CB  ALA B  43    13281   7915  11534    814   2954   3032       C  
ATOM   2572  N   GLY B  44      49.746   1.571  50.675  1.00 85.16           N  
ANISOU 2572  N   GLY B  44    13142   9360   9853   1400   3487   3423       N  
ATOM   2573  CA  GLY B  44      49.430   2.738  49.877  1.00 74.88           C  
ANISOU 2573  CA  GLY B  44    11699   8135   8616   1314   3393   3225       C  
ATOM   2574  C   GLY B  44      50.463   2.995  48.798  1.00 76.94           C  
ANISOU 2574  C   GLY B  44    11955   8318   8962   1368   3158   3099       C  
ATOM   2575  O   GLY B  44      51.407   2.226  48.584  1.00 77.91           O  
ANISOU 2575  O   GLY B  44    12164   8319   9118   1461   3079   3145       O  
ATOM   2576  N   SER B  45      50.264   4.116  48.110  1.00 72.85           N  
ANISOU 2576  N   SER B  45    11330   7874   8477   1309   3055   2939       N  
ATOM   2577  CA  SER B  45      51.064   4.483  46.953  1.00 71.42           C  
ANISOU 2577  CA  SER B  45    11127   7614   8395   1312   2846   2804       C  
ATOM   2578  C   SER B  45      52.246   5.372  47.345  1.00 71.55           C  
ANISOU 2578  C   SER B  45    11154   7864   8168   1557   2628   2781       C  
ATOM   2579  O   SER B  45      52.238   6.035  48.381  1.00 71.84           O  
ANISOU 2579  O   SER B  45    11188   8149   7957   1700   2620   2820       O  
ATOM   2580  CB  SER B  45      50.196   5.199  45.925  1.00 76.00           C  
ANISOU 2580  CB  SER B  45    11585   8129   9163   1100   2833   2641       C  
ATOM   2581  OG  SER B  45      49.266   4.311  45.334  1.00 78.30           O  
ANISOU 2581  OG  SER B  45    11859   8177   9715    860   3001   2634       O  
ATOM   2582  N   PHE B  46      53.278   5.366  46.493  1.00 71.30           N  
ANISOU 2582  N   PHE B  46    11126   7758   8207   1601   2452   2703       N  
ATOM   2583  CA  PHE B  46      54.380   6.321  46.548  1.00 61.00           C  
ANISOU 2583  CA  PHE B  46     9794   6646   6737   1781   2225   2638       C  
ATOM   2584  C   PHE B  46      54.699   6.797  45.140  1.00 64.63           C  
ANISOU 2584  C   PHE B  46    10170   7006   7381   1655   2066   2446       C  
ATOM   2585  O   PHE B  46      54.558   6.045  44.172  1.00 67.26           O  
ANISOU 2585  O   PHE B  46    10545   7095   7917   1521   2139   2442       O  
ATOM   2586  CB  PHE B  46      55.652   5.729  47.155  1.00 68.17           C  
ANISOU 2586  CB  PHE B  46    10759   7627   7516   2003   2143   2724       C  
ATOM   2587  CG  PHE B  46      55.522   5.351  48.594  1.00 70.29           C  
ANISOU 2587  CG  PHE B  46    11094   8040   7573   2145   2237   2879       C  
ATOM   2588  CD1 PHE B  46      55.621   6.314  49.584  1.00 71.93           C  
ANISOU 2588  CD1 PHE B  46    11280   8545   7506   2295   2154   2868       C  
ATOM   2589  CD2 PHE B  46      55.328   4.034  48.962  1.00 72.16           C  
ANISOU 2589  CD2 PHE B  46    11425   8119   7874   2133   2400   3029       C  
ATOM   2590  CE1 PHE B  46      55.517   5.972  50.920  1.00 74.19           C  
ANISOU 2590  CE1 PHE B  46    11633   8983   7571   2428   2235   3003       C  
ATOM   2591  CE2 PHE B  46      55.221   3.681  50.304  1.00 75.88           C  
ANISOU 2591  CE2 PHE B  46    11971   8723   8136   2264   2485   3189       C  
ATOM   2592  CZ  PHE B  46      55.319   4.653  51.281  1.00 71.95           C  
ANISOU 2592  CZ  PHE B  46    11449   8537   7353   2411   2402   3174       C  
ATOM   2593  N   PHE B  47      55.159   8.042  45.028  1.00 59.25           N  
ANISOU 2593  N   PHE B  47     9366   6520   6629   1689   1838   2265       N  
ATOM   2594  CA  PHE B  47      55.541   8.603  43.738  1.00 55.62           C  
ANISOU 2594  CA  PHE B  47     8818   5999   6318   1569   1671   2079       C  
ATOM   2595  C   PHE B  47      57.059   8.739  43.668  1.00 58.55           C  
ANISOU 2595  C   PHE B  47     9188   6452   6605   1733   1522   2075       C  
ATOM   2596  O   PHE B  47      57.688   9.275  44.590  1.00 58.88           O  
ANISOU 2596  O   PHE B  47     9202   6711   6461   1906   1417   2082       O  
ATOM   2597  CB  PHE B  47      54.867   9.958  43.489  1.00 48.20           C  
ANISOU 2597  CB  PHE B  47     7731   5174   5410   1450   1529   1874       C  
ATOM   2598  CG  PHE B  47      55.151  10.507  42.133  1.00 51.31           C  
ANISOU 2598  CG  PHE B  47     8059   5491   5947   1313   1375   1716       C  
ATOM   2599  CD1 PHE B  47      54.551   9.947  41.014  1.00 50.32           C  
ANISOU 2599  CD1 PHE B  47     7951   5165   6005   1128   1440   1685       C  
ATOM   2600  CD2 PHE B  47      56.049  11.557  41.958  1.00 51.52           C  
ANISOU 2600  CD2 PHE B  47     8011   5645   5919   1363   1169   1600       C  
ATOM   2601  CE1 PHE B  47      54.827  10.429  39.743  1.00 54.10           C  
ANISOU 2601  CE1 PHE B  47     8388   5589   6578   1009   1301   1552       C  
ATOM   2602  CE2 PHE B  47      56.325  12.051  40.680  1.00 47.22           C  
ANISOU 2602  CE2 PHE B  47     7423   5027   5493   1228   1047   1481       C  
ATOM   2603  CZ  PHE B  47      55.716  11.482  39.576  1.00 51.47           C  
ANISOU 2603  CZ  PHE B  47     7993   5382   6179   1060   1114   1464       C  
ATOM   2604  N   VAL B  48      57.638   8.241  42.578  1.00 60.45           N  
ANISOU 2604  N   VAL B  48     9452   6534   6984   1677   1514   2048       N  
ATOM   2605  CA  VAL B  48      59.082   8.128  42.404  1.00 51.57           C  
ANISOU 2605  CA  VAL B  48     8317   5459   5819   1828   1417   2054       C  
ATOM   2606  C   VAL B  48      59.454   8.654  41.026  1.00 56.63           C  
ANISOU 2606  C   VAL B  48     8877   6049   6591   1673   1310   1878       C  
ATOM   2607  O   VAL B  48      58.802   8.324  40.029  1.00 61.89           O  
ANISOU 2607  O   VAL B  48     9574   6538   7403   1491   1380   1825       O  
ATOM   2608  CB  VAL B  48      59.557   6.664  42.569  1.00 58.83           C  
ANISOU 2608  CB  VAL B  48     9378   6214   6762   1970   1572   2246       C  
ATOM   2609  CG1 VAL B  48      61.017   6.509  42.173  1.00 58.36           C  
ANISOU 2609  CG1 VAL B  48     9279   6189   6707   2114   1477   2222       C  
ATOM   2610  CG2 VAL B  48      59.378   6.219  44.003  1.00 54.92           C  
ANISOU 2610  CG2 VAL B  48     8941   5821   6105   2125   1643   2406       C  
ATOM   2611  N   LYS B  49      60.515   9.455  40.961  1.00 57.85           N  
ANISOU 2611  N   LYS B  49     8927   6364   6689   1741   1144   1788       N  
ATOM   2612  CA  LYS B  49      61.099   9.846  39.688  1.00 57.68           C  
ANISOU 2612  CA  LYS B  49     8840   6304   6769   1618   1069   1656       C  
ATOM   2613  C   LYS B  49      62.585   9.535  39.597  1.00 68.88           C  
ANISOU 2613  C   LYS B  49    10213   7789   8170   1772   1034   1667       C  
ATOM   2614  O   LYS B  49      63.354   9.852  40.513  1.00 68.75           O  
ANISOU 2614  O   LYS B  49    10126   7957   8040   1946    937   1690       O  
ATOM   2615  CB  LYS B  49      60.972  11.350  39.447  1.00 49.60           C  
ANISOU 2615  CB  LYS B  49     7702   5404   5740   1494    896   1503       C  
ATOM   2616  CG  LYS B  49      59.513  11.779  39.322  1.00 51.12           C  
ANISOU 2616  CG  LYS B  49     7910   5532   5981   1336    907   1460       C  
ATOM   2617  CD  LYS B  49      59.358  13.202  38.800  1.00 45.53           C  
ANISOU 2617  CD  LYS B  49     7110   4882   5308   1203    738   1313       C  
ATOM   2618  CE  LYS B  49      59.613  14.244  39.880  1.00 55.46           C  
ANISOU 2618  CE  LYS B  49     8282   6324   6466   1305    607   1255       C  
ATOM   2619  NZ  LYS B  49      59.417  15.631  39.377  1.00 52.18           N  
ANISOU 2619  NZ  LYS B  49     7792   5921   6114   1175    449   1117       N  
ATOM   2620  N   THR B  50      62.976   8.865  38.510  1.00 67.82           N  
ANISOU 2620  N   THR B  50    10111   7511   8146   1718   1117   1642       N  
ATOM   2621  CA  THR B  50      64.354   8.436  38.317  1.00 63.10           C  
ANISOU 2621  CA  THR B  50     9457   6958   7559   1869   1115   1644       C  
ATOM   2622  C   THR B  50      64.883   9.035  37.028  1.00 61.97           C  
ANISOU 2622  C   THR B  50     9228   6832   7487   1706   1073   1491       C  
ATOM   2623  O   THR B  50      64.127   9.307  36.089  1.00 54.07           O  
ANISOU 2623  O   THR B  50     8273   5732   6540   1492   1094   1417       O  
ATOM   2624  CB  THR B  50      64.525   6.890  38.252  1.00 59.46           C  
ANISOU 2624  CB  THR B  50     9125   6302   7166   2005   1288   1762       C  
ATOM   2625  OG1 THR B  50      63.644   6.334  37.268  1.00 64.24           O  
ANISOU 2625  OG1 THR B  50     9842   6677   7888   1815   1416   1720       O  
ATOM   2626  CG2 THR B  50      64.234   6.256  39.592  1.00 60.62           C  
ANISOU 2626  CG2 THR B  50     9366   6443   7225   2199   1336   1954       C  
ATOM   2627  N   ASN B  51      66.197   9.231  37.000  1.00 57.23           N  
ANISOU 2627  N   ASN B  51     8496   6370   6878   1814   1015   1448       N  
ATOM   2628  CA  ASN B  51      66.888   9.615  35.779  1.00 54.20           C  
ANISOU 2628  CA  ASN B  51     8029   6007   6557   1681   1021   1324       C  
ATOM   2629  C   ASN B  51      68.301   9.047  35.839  1.00 58.27           C  
ANISOU 2629  C   ASN B  51     8434   6608   7099   1881   1050   1322       C  
ATOM   2630  O   ASN B  51      69.070   9.395  36.737  1.00 58.43           O  
ANISOU 2630  O   ASN B  51     8320   6811   7069   2036    936   1335       O  
ATOM   2631  CB  ASN B  51      66.880  11.135  35.623  1.00 51.72           C  
ANISOU 2631  CB  ASN B  51     7605   5827   6218   1510    871   1227       C  
ATOM   2632  CG  ASN B  51      67.359  11.569  34.268  1.00 56.47           C  
ANISOU 2632  CG  ASN B  51     8160   6425   6870   1329    901   1126       C  
ATOM   2633  OD1 ASN B  51      68.442  11.180  33.839  1.00 69.62           O  
ANISOU 2633  OD1 ASN B  51     9740   8142   8569   1394    968   1091       O  
ATOM   2634  ND2 ASN B  51      66.554  12.350  33.573  1.00 46.15           N  
ANISOU 2634  ND2 ASN B  51     6909   5062   5564   1109    860   1085       N  
ATOM   2635  N   ARG B  52      68.629   8.126  34.927  1.00 63.11           N  
ANISOU 2635  N   ARG B  52     9098   7091   7791   1894   1200   1296       N  
ATOM   2636  CA  ARG B  52      69.936   7.469  34.962  1.00 74.35           C  
ANISOU 2636  CA  ARG B  52    10410   8577   9261   2112   1245   1289       C  
ATOM   2637  C   ARG B  52      71.066   8.348  34.429  1.00 76.72           C  
ANISOU 2637  C   ARG B  52    10488   9083   9579   2043   1189   1159       C  
ATOM   2638  O   ARG B  52      72.237   8.035  34.664  1.00 75.98           O  
ANISOU 2638  O   ARG B  52    10238   9108   9524   2235   1185   1142       O  
ATOM   2639  CB  ARG B  52      69.895   6.157  34.171  1.00 85.97           C  
ANISOU 2639  CB  ARG B  52    12014   9825  10826   2161   1439   1283       C  
ATOM   2640  CG  ARG B  52      69.881   6.352  32.652  1.00102.90           C  
ANISOU 2640  CG  ARG B  52    14171  11924  13003   1932   1534   1130       C  
ATOM   2641  CD  ARG B  52      69.770   5.032  31.878  1.00117.76           C  
ANISOU 2641  CD  ARG B  52    16197  13575  14972   1976   1723   1090       C  
ATOM   2642  NE  ARG B  52      69.645   5.247  30.433  1.00126.54           N  
ANISOU 2642  NE  ARG B  52    17342  14665  16072   1747   1806    936       N  
ATOM   2643  CZ  ARG B  52      68.492   5.446  29.792  1.00129.56           C  
ANISOU 2643  CZ  ARG B  52    17867  14943  16417   1513   1806    898       C  
ATOM   2644  NH1 ARG B  52      67.345   5.462  30.464  1.00128.45           N  
ANISOU 2644  NH1 ARG B  52    17830  14703  16273   1466   1742    993       N  
ATOM   2645  NH2 ARG B  52      68.484   5.633  28.475  1.00130.08           N  
ANISOU 2645  NH2 ARG B  52    17964  15018  16440   1330   1870    762       N  
ATOM   2646  N   SER B  53      70.751   9.438  33.725  1.00 71.69           N  
ANISOU 2646  N   SER B  53     9827   8487   8923   1776   1146   1075       N  
ATOM   2647  CA  SER B  53      71.779  10.258  33.100  1.00 76.41           C  
ANISOU 2647  CA  SER B  53    10230   9251   9550   1669   1129    964       C  
ATOM   2648  C   SER B  53      72.252  11.409  33.982  1.00 76.17           C  
ANISOU 2648  C   SER B  53    10018   9423   9501   1666    940    940       C  
ATOM   2649  O   SER B  53      73.347  11.925  33.755  1.00 84.22           O  
ANISOU 2649  O   SER B  53    10827  10603  10570   1637    920    854       O  
ATOM   2650  CB  SER B  53      71.286  10.793  31.754  1.00 82.79           C  
ANISOU 2650  CB  SER B  53    11124   9986  10347   1380   1199    899       C  
ATOM   2651  OG  SER B  53      70.340  11.838  31.912  1.00 91.12           O  
ANISOU 2651  OG  SER B  53    12244  11021  11356   1201   1072    919       O  
ATOM   2652  N   ILE B  54      71.447  11.850  34.947  1.00 71.67           N  
ANISOU 2652  N   ILE B  54     9515   8851   8865   1679    808    995       N  
ATOM   2653  CA  ILE B  54      71.690  13.072  35.711  1.00 75.37           C  
ANISOU 2653  CA  ILE B  54     9842   9485   9309   1635    621    940       C  
ATOM   2654  C   ILE B  54      72.116  12.710  37.130  1.00 77.48           C  
ANISOU 2654  C   ILE B  54    10033   9894   9512   1913    508    985       C  
ATOM   2655  O   ILE B  54      71.552  11.800  37.747  1.00 77.63           O  
ANISOU 2655  O   ILE B  54    10199   9833   9466   2086    547   1105       O  
ATOM   2656  CB  ILE B  54      70.431  13.963  35.723  1.00 79.31           C  
ANISOU 2656  CB  ILE B  54    10473   9890   9773   1443    549    943       C  
ATOM   2657  CG1 ILE B  54      70.017  14.305  34.287  1.00 88.53           C  
ANISOU 2657  CG1 ILE B  54    11726  10929  10984   1186    642    915       C  
ATOM   2658  CG2 ILE B  54      70.643  15.220  36.545  1.00 79.65           C  
ANISOU 2658  CG2 ILE B  54    10384  10076   9802   1404    358    864       C  
ATOM   2659  CD1 ILE B  54      68.849  15.284  34.186  1.00 91.85           C  
ANISOU 2659  CD1 ILE B  54    12252  11258  11388   1003    552    914       C  
ATOM   2660  N   GLY B  55      73.087  13.451  37.660  1.00 74.57           N  
ANISOU 2660  N   GLY B  55     9438   9739   9155   1946    363    890       N  
ATOM   2661  CA  GLY B  55      73.516  13.309  39.032  1.00 65.34           C  
ANISOU 2661  CA  GLY B  55     8180   8749   7896   2198    211    909       C  
ATOM   2662  C   GLY B  55      72.513  13.852  40.028  1.00 68.06           C  
ANISOU 2662  C   GLY B  55     8644   9102   8113   2196     93    933       C  
ATOM   2663  O   GLY B  55      71.567  14.556  39.670  1.00 67.89           O  
ANISOU 2663  O   GLY B  55     8729   8963   8103   1984    103    907       O  
ATOM   2664  N   PRO B  56      72.726  13.555  41.316  1.00 71.30           N  
ANISOU 2664  N   PRO B  56     9033   9669   8391   2448    -25    980       N  
ATOM   2665  CA  PRO B  56      71.653  13.740  42.314  1.00 64.59           C  
ANISOU 2665  CA  PRO B  56     8340   8817   7382   2495    -81   1039       C  
ATOM   2666  C   PRO B  56      71.358  15.185  42.695  1.00 68.97           C  
ANISOU 2666  C   PRO B  56     8826   9462   7916   2330   -239    876       C  
ATOM   2667  O   PRO B  56      70.404  15.408  43.450  1.00 75.28           O  
ANISOU 2667  O   PRO B  56     9753  10259   8592   2355   -268    901       O  
ATOM   2668  CB  PRO B  56      72.169  12.959  43.530  1.00 65.50           C  
ANISOU 2668  CB  PRO B  56     8444   9103   7341   2832   -160   1142       C  
ATOM   2669  CG  PRO B  56      73.665  12.924  43.357  1.00 65.35           C  
ANISOU 2669  CG  PRO B  56     8169   9253   7407   2931   -248   1053       C  
ATOM   2670  CD  PRO B  56      73.895  12.847  41.875  1.00 69.25           C  
ANISOU 2670  CD  PRO B  56     8624   9583   8105   2730    -88   1008       C  
ATOM   2671  N   ALA B  57      72.122  16.169  42.218  1.00 67.12           N  
ANISOU 2671  N   ALA B  57     8397   9298   7806   2163   -330    708       N  
ATOM   2672  CA  ALA B  57      71.926  17.539  42.690  1.00 66.22           C  
ANISOU 2672  CA  ALA B  57     8216   9256   7687   2027   -494    540       C  
ATOM   2673  C   ALA B  57      70.519  18.055  42.382  1.00 64.88           C  
ANISOU 2673  C   ALA B  57     8237   8887   7529   1854   -434    557       C  
ATOM   2674  O   ALA B  57      69.904  18.729  43.215  1.00 67.38           O  
ANISOU 2674  O   ALA B  57     8590   9252   7758   1866   -538    482       O  
ATOM   2675  CB  ALA B  57      72.986  18.457  42.084  1.00 61.02           C  
ANISOU 2675  CB  ALA B  57     7324   8659   7200   1841   -569    374       C  
ATOM   2676  N   MET B  58      69.987  17.735  41.196  1.00 60.03           N  
ANISOU 2676  N   MET B  58     7737   8059   7014   1704   -271    644       N  
ATOM   2677  CA  MET B  58      68.686  18.262  40.774  1.00 58.94           C  
ANISOU 2677  CA  MET B  58     7751   7737   6908   1534   -231    652       C  
ATOM   2678  C   MET B  58      67.546  17.760  41.661  1.00 51.81           C  
ANISOU 2678  C   MET B  58     7004   6819   5863   1673   -195    739       C  
ATOM   2679  O   MET B  58      66.688  18.539  42.090  1.00 62.98           O  
ANISOU 2679  O   MET B  58     8463   8214   7254   1620   -259    671       O  
ATOM   2680  CB  MET B  58      68.429  17.892  39.312  1.00 67.54           C  
ANISOU 2680  CB  MET B  58     8925   8632   8106   1367    -76    728       C  
ATOM   2681  CG  MET B  58      67.014  18.149  38.849  1.00 81.98           C  
ANISOU 2681  CG  MET B  58    10919  10277   9954   1234    -31    764       C  
ATOM   2682  SD  MET B  58      66.647  17.331  37.281  1.00 97.73           S  
ANISOU 2682  SD  MET B  58    13039  12078  12015   1100    153    864       S  
ATOM   2683  CE  MET B  58      66.393  15.644  37.813  1.00 97.70           C  
ANISOU 2683  CE  MET B  58    13138  12055  11928   1323    295    998       C  
ATOM   2684  N   PHE B  59      67.491  16.455  41.909  1.00 52.19           N  
ANISOU 2684  N   PHE B  59     7140   6861   5830   1845    -77    893       N  
ATOM   2685  CA  PHE B  59      66.435  15.912  42.756  1.00 53.13           C  
ANISOU 2685  CA  PHE B  59     7408   6964   5816   1964    -11    999       C  
ATOM   2686  C   PHE B  59      66.586  16.373  44.201  1.00 59.60           C  
ANISOU 2686  C   PHE B  59     8178   8009   6459   2130   -153    935       C  
ATOM   2687  O   PHE B  59      65.587  16.509  44.916  1.00 60.85           O  
ANISOU 2687  O   PHE B  59     8430   8179   6510   2163   -131    950       O  
ATOM   2688  CB  PHE B  59      66.413  14.385  42.651  1.00 54.09           C  
ANISOU 2688  CB  PHE B  59     7644   6994   5912   2100    159   1191       C  
ATOM   2689  CG  PHE B  59      65.742  13.856  41.386  1.00 53.23           C  
ANISOU 2689  CG  PHE B  59     7643   6639   5942   1930    321   1246       C  
ATOM   2690  CD1 PHE B  59      64.604  14.467  40.874  1.00 51.37           C  
ANISOU 2690  CD1 PHE B  59     7465   6282   5770   1732    336   1196       C  
ATOM   2691  CD2 PHE B  59      66.263  12.755  40.714  1.00 52.09           C  
ANISOU 2691  CD2 PHE B  59     7535   6394   5865   1981    446   1332       C  
ATOM   2692  CE1 PHE B  59      63.980  13.978  39.736  1.00 53.31           C  
ANISOU 2692  CE1 PHE B  59     7803   6327   6124   1582    460   1233       C  
ATOM   2693  CE2 PHE B  59      65.644  12.266  39.561  1.00 48.52           C  
ANISOU 2693  CE2 PHE B  59     7184   5727   5524   1823    585   1353       C  
ATOM   2694  CZ  PHE B  59      64.503  12.886  39.073  1.00 53.00           C  
ANISOU 2694  CZ  PHE B  59     7807   6195   6136   1619    584   1303       C  
ATOM   2695  N   GLU B  60      67.819  16.606  44.654  1.00 63.04           N  
ANISOU 2695  N   GLU B  60     8458   8640   6854   2238   -298    853       N  
ATOM   2696  CA  GLU B  60      68.021  17.113  46.007  1.00 57.79           C  
ANISOU 2696  CA  GLU B  60     7737   8215   6004   2390   -461    759       C  
ATOM   2697  C   GLU B  60      67.479  18.525  46.165  1.00 62.03           C  
ANISOU 2697  C   GLU B  60     8237   8751   6580   2230   -573    554       C  
ATOM   2698  O   GLU B  60      66.880  18.852  47.199  1.00 66.51           O  
ANISOU 2698  O   GLU B  60     8857   9430   6982   2321   -622    501       O  
ATOM   2699  CB  GLU B  60      69.501  17.054  46.380  1.00 55.75           C  
ANISOU 2699  CB  GLU B  60     7293   8175   5714   2533   -612    695       C  
ATOM   2700  CG  GLU B  60      69.976  15.649  46.701  1.00 66.66           C  
ANISOU 2700  CG  GLU B  60     8727   9609   6991   2790   -540    902       C  
ATOM   2701  CD  GLU B  60      71.486  15.557  46.814  1.00 84.41           C  
ANISOU 2701  CD  GLU B  60    10756  12053   9263   2921   -684    834       C  
ATOM   2702  OE1 GLU B  60      72.166  16.601  46.679  1.00 90.12           O  
ANISOU 2702  OE1 GLU B  60    11276  12882  10083   2791   -837    617       O  
ATOM   2703  OE2 GLU B  60      71.989  14.442  47.060  1.00 92.46           O  
ANISOU 2703  OE2 GLU B  60    11799  13117  10217   3157   -647    997       O  
ATOM   2704  N   GLY B  61      67.675  19.374  45.153  1.00 58.68           N  
ANISOU 2704  N   GLY B  61     7730   8196   6368   1996   -606    440       N  
ATOM   2705  CA  GLY B  61      67.117  20.714  45.214  1.00 56.02           C  
ANISOU 2705  CA  GLY B  61     7377   7806   6103   1844   -705    259       C  
ATOM   2706  C   GLY B  61      65.602  20.715  45.162  1.00 56.39           C  
ANISOU 2706  C   GLY B  61     7586   7703   6136   1802   -594    319       C  
ATOM   2707  O   GLY B  61      64.946  21.525  45.828  1.00 61.25           O  
ANISOU 2707  O   GLY B  61     8215   8351   6706   1807   -666    187       O  
ATOM   2708  N   GLU B  62      65.028  19.826  44.350  1.00 51.11           N  
ANISOU 2708  N   GLU B  62     7029   6871   5521   1757   -419    498       N  
ATOM   2709  CA  GLU B  62      63.582  19.656  44.334  1.00 51.88           C  
ANISOU 2709  CA  GLU B  62     7257   6846   5608   1727   -304    563       C  
ATOM   2710  C   GLU B  62      63.064  19.221  45.704  1.00 59.67           C  
ANISOU 2710  C   GLU B  62     8307   7993   6372   1929   -266    603       C  
ATOM   2711  O   GLU B  62      62.059  19.752  46.195  1.00 54.29           O  
ANISOU 2711  O   GLU B  62     7660   7314   5654   1924   -259    530       O  
ATOM   2712  CB  GLU B  62      63.196  18.638  43.251  1.00 49.19           C  
ANISOU 2712  CB  GLU B  62     7011   6320   5358   1648   -131    736       C  
ATOM   2713  CG  GLU B  62      61.680  18.411  43.122  1.00 64.45           C  
ANISOU 2713  CG  GLU B  62     9054   8123   7313   1592    -12    795       C  
ATOM   2714  CD  GLU B  62      61.288  17.497  41.952  1.00 72.05           C  
ANISOU 2714  CD  GLU B  62    10099   8894   8383   1483    134    924       C  
ATOM   2715  OE1 GLU B  62      62.185  17.007  41.235  1.00 73.92           O  
ANISOU 2715  OE1 GLU B  62    10324   9096   8667   1460    159    970       O  
ATOM   2716  OE2 GLU B  62      60.076  17.251  41.759  1.00 74.37           O  
ANISOU 2716  OE2 GLU B  62    10460   9081   8716   1421    227    964       O  
ATOM   2717  N   ALA B  63      63.741  18.255  46.339  1.00 52.33           N  
ANISOU 2717  N   ALA B  63     7395   7202   5285   2118   -235    724       N  
ATOM   2718  CA  ALA B  63      63.288  17.769  47.637  1.00 55.21           C  
ANISOU 2718  CA  ALA B  63     7844   7728   5406   2316   -183    800       C  
ATOM   2719  C   ALA B  63      63.306  18.881  48.671  1.00 61.89           C  
ANISOU 2719  C   ALA B  63     8623   8775   6119   2378   -346    586       C  
ATOM   2720  O   ALA B  63      62.356  19.030  49.449  1.00 67.56           O  
ANISOU 2720  O   ALA B  63     9410   9557   6703   2435   -285    566       O  
ATOM   2721  CB  ALA B  63      64.154  16.590  48.111  1.00 47.07           C  
ANISOU 2721  CB  ALA B  63     6847   6808   4229   2528   -151    981       C  
ATOM   2722  N   LEU B  64      64.382  19.669  48.703  1.00 60.02           N  
ANISOU 2722  N   LEU B  64     8243   8642   5921   2362   -548    408       N  
ATOM   2723  CA  LEU B  64      64.461  20.760  49.669  1.00 58.10           C  
ANISOU 2723  CA  LEU B  64     7930   8580   5566   2410   -720    165       C  
ATOM   2724  C   LEU B  64      63.466  21.872  49.343  1.00 58.82           C  
ANISOU 2724  C   LEU B  64     8026   8514   5810   2243   -725      0       C  
ATOM   2725  O   LEU B  64      62.933  22.510  50.256  1.00 60.25           O  
ANISOU 2725  O   LEU B  64     8218   8809   5865   2313   -773   -157       O  
ATOM   2726  CB  LEU B  64      65.895  21.285  49.723  1.00 56.91           C  
ANISOU 2726  CB  LEU B  64     7606   8565   5454   2411   -935      7       C  
ATOM   2727  CG  LEU B  64      66.870  20.287  50.357  1.00 63.62           C  
ANISOU 2727  CG  LEU B  64     8430   9636   6105   2641   -974    135       C  
ATOM   2728  CD1 LEU B  64      68.302  20.723  50.172  1.00 64.18           C  
ANISOU 2728  CD1 LEU B  64     8291   9819   6276   2614  -1170    -14       C  
ATOM   2729  CD2 LEU B  64      66.553  20.132  51.837  1.00 58.60           C  
ANISOU 2729  CD2 LEU B  64     7875   9260   5128   2873  -1012    126       C  
ATOM   2730  N   GLY B  65      63.185  22.099  48.057  1.00 56.38           N  
ANISOU 2730  N   GLY B  65     7714   7946   5761   2039   -676     33       N  
ATOM   2731  CA  GLY B  65      62.143  23.052  47.689  1.00 54.72           C  
ANISOU 2731  CA  GLY B  65     7522   7566   5702   1905   -677    -85       C  
ATOM   2732  C   GLY B  65      60.760  22.599  48.123  1.00 49.94           C  
ANISOU 2732  C   GLY B  65     7021   6956   5000   1976   -512     -1       C  
ATOM   2733  O   GLY B  65      60.023  23.353  48.763  1.00 59.21           O  
ANISOU 2733  O   GLY B  65     8190   8171   6135   2012   -539   -161       O  
ATOM   2734  N   LEU B  66      60.401  21.347  47.813  1.00 53.33           N  
ANISOU 2734  N   LEU B  66     7536   7333   5393   1998   -329    238       N  
ATOM   2735  CA  LEU B  66      59.114  20.819  48.266  1.00 58.99           C  
ANISOU 2735  CA  LEU B  66     8337   8053   6022   2051   -148    330       C  
ATOM   2736  C   LEU B  66      59.012  20.870  49.783  1.00 62.55           C  
ANISOU 2736  C   LEU B  66     8809   8766   6190   2248   -145    266       C  
ATOM   2737  O   LEU B  66      57.945  21.156  50.333  1.00 62.54           O  
ANISOU 2737  O   LEU B  66     8825   8804   6132   2277    -60    201       O  
ATOM   2738  CB  LEU B  66      58.907  19.385  47.774  1.00 57.54           C  
ANISOU 2738  CB  LEU B  66     8245   7770   5845   2042     46    596       C  
ATOM   2739  CG  LEU B  66      58.652  19.097  46.292  1.00 49.55           C  
ANISOU 2739  CG  LEU B  66     7244   6505   5078   1852    100    675       C  
ATOM   2740  CD1 LEU B  66      58.876  17.641  46.013  1.00 49.22           C  
ANISOU 2740  CD1 LEU B  66     7290   6403   5008   1884    258    904       C  
ATOM   2741  CD2 LEU B  66      57.235  19.483  45.897  1.00 54.12           C  
ANISOU 2741  CD2 LEU B  66     7818   6954   5789   1738    164    628       C  
ATOM   2742  N   GLU B  67      60.116  20.595  50.477  1.00 67.63           N  
ANISOU 2742  N   GLU B  67     9446   9608   6644   2392   -238    279       N  
ATOM   2743  CA  GLU B  67      60.086  20.592  51.934  1.00 65.14           C  
ANISOU 2743  CA  GLU B  67     9167   9573   6011   2595   -247    229       C  
ATOM   2744  C   GLU B  67      59.804  21.989  52.490  1.00 64.76           C  
ANISOU 2744  C   GLU B  67     9045   9609   5950   2590   -387    -90       C  
ATOM   2745  O   GLU B  67      58.955  22.155  53.376  1.00 67.68           O  
ANISOU 2745  O   GLU B  67     9458  10109   6148   2682   -299   -156       O  
ATOM   2746  CB  GLU B  67      61.400  20.046  52.473  1.00 58.33           C  
ANISOU 2746  CB  GLU B  67     8297   8907   4957   2758   -358    302       C  
ATOM   2747  CG  GLU B  67      61.457  19.948  53.996  1.00 70.68           C  
ANISOU 2747  CG  GLU B  67     9918  10793   6142   2990   -384    276       C  
ATOM   2748  CD  GLU B  67      60.373  19.050  54.576  1.00 79.55           C  
ANISOU 2748  CD  GLU B  67    11198  11948   7081   3076   -119    499       C  
ATOM   2749  OE1 GLU B  67      60.092  17.983  53.998  1.00 84.07           O  
ANISOU 2749  OE1 GLU B  67    11852  12345   7746   3035     64    765       O  
ATOM   2750  OE2 GLU B  67      59.800  19.402  55.625  1.00 90.26           O  
ANISOU 2750  OE2 GLU B  67    12595  13504   8196   3180    -82    402       O  
ATOM   2751  N   ALA B  68      60.485  23.011  51.965  1.00 59.22           N  
ANISOU 2751  N   ALA B  68     8233   8825   5443   2476   -590   -296       N  
ATOM   2752  CA  ALA B  68      60.264  24.370  52.452  1.00 55.02           C  
ANISOU 2752  CA  ALA B  68     7637   8331   4936   2464   -731   -616       C  
ATOM   2753  C   ALA B  68      58.860  24.923  52.172  1.00 58.82           C  
ANISOU 2753  C   ALA B  68     8136   8644   5570   2389   -624   -689       C  
ATOM   2754  O   ALA B  68      58.308  25.676  52.985  1.00 65.72           O  
ANISOU 2754  O   ALA B  68     8998   9617   6354   2467   -648   -910       O  
ATOM   2755  CB  ALA B  68      61.257  25.318  51.783  1.00 53.68           C  
ANISOU 2755  CB  ALA B  68     7351   8044   5001   2318   -948   -792       C  
ATOM   2756  N   MET B  69      58.248  24.527  51.042  1.00 61.80           N  
ANISOU 2756  N   MET B  69     8536   8778   6168   2250   -505   -514       N  
ATOM   2757  CA  MET B  69      56.886  24.977  50.729  1.00 59.08           C  
ANISOU 2757  CA  MET B  69     8187   8283   5978   2191   -413   -569       C  
ATOM   2758  C   MET B  69      55.914  24.156  51.571  1.00 58.23           C  
ANISOU 2758  C   MET B  69     8139   8334   5653   2315   -187   -458       C  
ATOM   2759  O   MET B  69      54.883  24.672  52.005  1.00 56.74           O  
ANISOU 2759  O   MET B  69     7923   8170   5465   2355   -120   -594       O  
ATOM   2760  CB  MET B  69      56.558  24.789  49.247  1.00 53.15           C  
ANISOU 2760  CB  MET B  69     7435   7248   5510   2007   -379   -422       C  
ATOM   2761  CG  MET B  69      57.358  25.671  48.271  1.00 58.69           C  
ANISOU 2761  CG  MET B  69     8089   7762   6448   1855   -570   -509       C  
ATOM   2762  SD  MET B  69      56.875  25.441  46.531  1.00 57.34           S  
ANISOU 2762  SD  MET B  69     7943   7289   6557   1653   -524   -329       S  
ATOM   2763  CE  MET B  69      57.214  23.704  46.315  1.00 53.86           C  
ANISOU 2763  CE  MET B  69     7570   6917   5979   1671   -344    -41       C  
ATOM   2764  N   TYR B  70      56.210  22.866  51.792  1.00 58.17           N  
ANISOU 2764  N   TYR B  70     8211   8422   5469   2377    -52   -203       N  
ATOM   2765  CA  TYR B  70      55.329  22.029  52.607  1.00 60.94           C  
ANISOU 2765  CA  TYR B  70     8633   8912   5609   2480    187    -64       C  
ATOM   2766  C   TYR B  70      55.207  22.586  54.014  1.00 69.20           C  
ANISOU 2766  C   TYR B  70     9684  10239   6370   2654    171   -255       C  
ATOM   2767  O   TYR B  70      54.120  22.572  54.608  1.00 68.63           O  
ANISOU 2767  O   TYR B  70     9617  10254   6207   2703    348   -282       O  
ATOM   2768  CB  TYR B  70      55.836  20.580  52.645  1.00 65.41           C  
ANISOU 2768  CB  TYR B  70     9304   9512   6036   2529    313    249       C  
ATOM   2769  CG  TYR B  70      54.877  19.555  53.268  1.00 62.78           C  
ANISOU 2769  CG  TYR B  70     9063   9251   5541   2587    601    458       C  
ATOM   2770  CD1 TYR B  70      53.924  18.896  52.487  1.00 60.98           C  
ANISOU 2770  CD1 TYR B  70     8838   8815   5518   2442    792    610       C  
ATOM   2771  CD2 TYR B  70      54.960  19.214  54.627  1.00 62.12           C  
ANISOU 2771  CD2 TYR B  70     9065   9447   5092   2779    683    512       C  
ATOM   2772  CE1 TYR B  70      53.052  17.955  53.040  1.00 58.74           C  
ANISOU 2772  CE1 TYR B  70     8626   8580   5114   2466   1071    801       C  
ATOM   2773  CE2 TYR B  70      54.093  18.263  55.194  1.00 63.47           C  
ANISOU 2773  CE2 TYR B  70     9329   9674   5113   2816    973    730       C  
ATOM   2774  CZ  TYR B  70      53.142  17.642  54.388  1.00 67.99           C  
ANISOU 2774  CZ  TYR B  70     9889  10015   5930   2648   1172    872       C  
ATOM   2775  OH  TYR B  70      52.280  16.704  54.915  1.00 71.32           O  
ANISOU 2775  OH  TYR B  70    10390  10471   6239   2654   1472   1085       O  
ATOM   2776  N   GLU B  71      56.317  23.078  54.567  1.00 66.49           N  
ANISOU 2776  N   GLU B  71     9328  10057   5880   2746    -37   -403       N  
ATOM   2777  CA  GLU B  71      56.304  23.537  55.947  1.00 69.25           C  
ANISOU 2777  CA  GLU B  71     9695  10706   5912   2924    -68   -594       C  
ATOM   2778  C   GLU B  71      55.562  24.856  56.143  1.00 69.11           C  
ANISOU 2778  C   GLU B  71     9596  10657   6007   2907   -124   -933       C  
ATOM   2779  O   GLU B  71      55.146  25.143  57.268  1.00 77.21           O  
ANISOU 2779  O   GLU B  71    10643  11920   6772   3051    -67  -1087       O  
ATOM   2780  CB  GLU B  71      57.730  23.638  56.465  1.00 73.13           C  
ANISOU 2780  CB  GLU B  71    10182  11389   6215   3026   -297   -667       C  
ATOM   2781  CG  GLU B  71      58.321  22.295  56.847  1.00 82.40           C  
ANISOU 2781  CG  GLU B  71    11460  12712   7135   3153   -216   -352       C  
ATOM   2782  CD  GLU B  71      59.825  22.357  57.013  1.00 94.49           C  
ANISOU 2782  CD  GLU B  71    12943  14378   8580   3227   -472   -406       C  
ATOM   2783  OE1 GLU B  71      60.403  23.427  56.719  1.00101.40           O  
ANISOU 2783  OE1 GLU B  71    13695  15203   9629   3139   -696   -683       O  
ATOM   2784  OE2 GLU B  71      60.425  21.352  57.456  1.00 93.15           O  
ANISOU 2784  OE2 GLU B  71    12852  14364   8179   3374   -450   -175       O  
ATOM   2785  N   THR B  72      55.353  25.660  55.098  1.00 63.44           N  
ANISOU 2785  N   THR B  72     8793   9653   5659   2748   -224  -1050       N  
ATOM   2786  CA  THR B  72      54.546  26.853  55.330  1.00 67.03           C  
ANISOU 2786  CA  THR B  72     9180  10061   6228   2761   -258  -1356       C  
ATOM   2787  C   THR B  72      53.115  26.488  55.684  1.00 67.48           C  
ANISOU 2787  C   THR B  72     9238  10174   6227   2814      8  -1300       C  
ATOM   2788  O   THR B  72      52.397  27.320  56.242  1.00 66.95           O  
ANISOU 2788  O   THR B  72     9120  10166   6153   2891     27  -1561       O  
ATOM   2789  CB  THR B  72      54.541  27.791  54.119  1.00 63.42           C  
ANISOU 2789  CB  THR B  72     8647   9264   6185   2592   -416  -1463       C  
ATOM   2790  OG1 THR B  72      53.870  27.165  53.011  1.00 56.29           O  
ANISOU 2790  OG1 THR B  72     7743   8145   5500   2464   -287  -1216       O  
ATOM   2791  CG2 THR B  72      55.967  28.185  53.731  1.00 57.25           C  
ANISOU 2791  CG2 THR B  72     7849   8421   5485   2510   -657  -1519       C  
ATOM   2792  N   ARG B  73      52.692  25.265  55.368  1.00 71.71           N  
ANISOU 2792  N   ARG B  73     9821  10688   6737   2770    221   -979       N  
ATOM   2793  CA  ARG B  73      51.339  24.790  55.654  1.00 76.41           C  
ANISOU 2793  CA  ARG B  73    10400  11334   7299   2790    501   -897       C  
ATOM   2794  C   ARG B  73      50.276  25.685  55.007  1.00 70.11           C  
ANISOU 2794  C   ARG B  73     9471  10334   6835   2716    489  -1083       C  
ATOM   2795  O   ARG B  73      49.285  26.059  55.634  1.00 67.70           O  
ANISOU 2795  O   ARG B  73     9101  10138   6484   2800    623  -1239       O  
ATOM   2796  CB  ARG B  73      51.112  24.658  57.162  1.00 80.84           C  
ANISOU 2796  CB  ARG B  73    11016  12245   7454   2979    646   -968       C  
ATOM   2797  CG  ARG B  73      52.033  23.630  57.828  1.00 87.38           C  
ANISOU 2797  CG  ARG B  73    11988  13283   7929   3075    678   -729       C  
ATOM   2798  CD  ARG B  73      51.467  23.181  59.162  1.00 98.70           C  
ANISOU 2798  CD  ARG B  73    13501  15038   8964   3234    918   -685       C  
ATOM   2799  NE  ARG B  73      50.244  22.412  58.954  1.00108.50           N  
ANISOU 2799  NE  ARG B  73    14725  16206  10295   3151   1238   -477       N  
ATOM   2800  CZ  ARG B  73      49.159  22.492  59.720  1.00114.84           C  
ANISOU 2800  CZ  ARG B  73    15495  17182  10959   3212   1483   -552       C  
ATOM   2801  NH1 ARG B  73      49.130  23.320  60.759  1.00111.36           N  
ANISOU 2801  NH1 ARG B  73    15049  17001  10260   3373   1445   -839       N  
ATOM   2802  NH2 ARG B  73      48.096  21.750  59.434  1.00119.29           N  
ANISOU 2802  NH2 ARG B  73    16019  17659  11647   3106   1771   -355       N  
ATOM   2803  N   THR B  74      50.485  26.037  53.736  1.00 65.96           N  
ANISOU 2803  N   THR B  74     8904   9517   6641   2569    328  -1062       N  
ATOM   2804  CA  THR B  74      49.494  26.816  53.012  1.00 60.20           C  
ANISOU 2804  CA  THR B  74     8061   8578   6236   2508    295  -1194       C  
ATOM   2805  C   THR B  74      48.967  26.101  51.783  1.00 61.19           C  
ANISOU 2805  C   THR B  74     8159   8493   6598   2347    365   -955       C  
ATOM   2806  O   THR B  74      47.874  25.535  51.833  1.00 70.19           O  
ANISOU 2806  O   THR B  74     9236   9669   7763   2335    575   -874       O  
ATOM   2807  CB  THR B  74      50.039  28.190  52.595  1.00 62.11           C  
ANISOU 2807  CB  THR B  74     8275   8639   6686   2489     12  -1441       C  
ATOM   2808  OG1 THR B  74      51.197  28.033  51.778  1.00 56.61           O  
ANISOU 2808  OG1 THR B  74     7639   7803   6068   2365   -148  -1306       O  
ATOM   2809  CG2 THR B  74      50.405  29.044  53.841  1.00 57.59           C  
ANISOU 2809  CG2 THR B  74     7709   8264   5910   2648    -67  -1751       C  
ATOM   2810  N   ILE B  75      49.725  26.110  50.678  1.00 59.76           N  
ANISOU 2810  N   ILE B  75     8016   8102   6586   2216    199   -852       N  
ATOM   2811  CA  ILE B  75      49.240  25.544  49.425  1.00 57.60           C  
ANISOU 2811  CA  ILE B  75     7722   7627   6538   2062    234   -662       C  
ATOM   2812  C   ILE B  75      49.724  24.103  49.519  1.00 60.06           C  
ANISOU 2812  C   ILE B  75     8130   8024   6668   2026    392   -392       C  
ATOM   2813  O   ILE B  75      50.816  23.824  50.035  1.00 56.52           O  
ANISOU 2813  O   ILE B  75     7769   7691   6016   2084    355   -345       O  
ATOM   2814  CB  ILE B  75      49.785  26.243  48.161  1.00 59.60           C  
ANISOU 2814  CB  ILE B  75     7983   7621   7039   1939     -3   -674       C  
ATOM   2815  CG1 ILE B  75      49.048  25.759  46.912  1.00 53.51           C  
ANISOU 2815  CG1 ILE B  75     7179   6670   6481   1801     29   -518       C  
ATOM   2816  CG2 ILE B  75      51.262  25.927  47.941  1.00 47.13           C  
ANISOU 2816  CG2 ILE B  75     6503   6040   5364   1887    -98   -569       C  
ATOM   2817  CD1 ILE B  75      49.182  26.699  45.708  1.00 52.72           C  
ANISOU 2817  CD1 ILE B  75     7075   6321   6636   1708   -198   -561       C  
ATOM   2818  N   ARG B  76      48.910  23.177  49.014  1.00 52.33           N  
ANISOU 2818  N   ARG B  76     7128   6979   5776   1932    563   -220       N  
ATOM   2819  CA  ARG B  76      49.265  21.771  49.083  1.00 55.72           C  
ANISOU 2819  CA  ARG B  76     7657   7447   6067   1896    732     38       C  
ATOM   2820  C   ARG B  76      50.402  21.436  48.113  1.00 59.86           C  
ANISOU 2820  C   ARG B  76     8265   7823   6656   1803    595    162       C  
ATOM   2821  O   ARG B  76      50.376  21.826  46.940  1.00 62.22           O  
ANISOU 2821  O   ARG B  76     8533   7931   7179   1682    462    140       O  
ATOM   2822  CB  ARG B  76      48.057  20.900  48.785  1.00 57.71           C  
ANISOU 2822  CB  ARG B  76     7852   7646   6428   1799    953    162       C  
ATOM   2823  CG  ARG B  76      48.416  19.418  48.856  1.00 60.76           C  
ANISOU 2823  CG  ARG B  76     8360   8031   6697   1756   1138    434       C  
ATOM   2824  CD  ARG B  76      47.203  18.538  48.886  1.00 59.24           C  
ANISOU 2824  CD  ARG B  76     8111   7819   6578   1666   1399    543       C  
ATOM   2825  NE  ARG B  76      47.577  17.162  49.191  1.00 64.14           N  
ANISOU 2825  NE  ARG B  76     8872   8437   7063   1653   1594    803       N  
ATOM   2826  CZ  ARG B  76      46.795  16.117  48.945  1.00 67.63           C  
ANISOU 2826  CZ  ARG B  76     9304   8783   7609   1523   1815    952       C  
ATOM   2827  NH1 ARG B  76      45.601  16.297  48.388  1.00 67.88           N  
ANISOU 2827  NH1 ARG B  76     9171   8743   7876   1395   1857    854       N  
ATOM   2828  NH2 ARG B  76      47.203  14.897  49.252  1.00 62.21           N  
ANISOU 2828  NH2 ARG B  76     8766   8065   6807   1524   1988   1195       N  
ATOM   2829  N   VAL B  77      51.422  20.750  48.625  1.00 56.41           N  
ANISOU 2829  N   VAL B  77     7932   7489   6010   1874    626    289       N  
ATOM   2830  CA  VAL B  77      52.507  20.206  47.810  1.00 51.04           C  
ANISOU 2830  CA  VAL B  77     7324   6697   5372   1806    547    425       C  
ATOM   2831  C   VAL B  77      52.755  18.773  48.257  1.00 51.33           C  
ANISOU 2831  C   VAL B  77     7467   6792   5243   1857    742    666       C  
ATOM   2832  O   VAL B  77      52.442  18.400  49.398  1.00 56.63           O  
ANISOU 2832  O   VAL B  77     8176   7636   5704   1977    889    718       O  
ATOM   2833  CB  VAL B  77      53.809  21.046  47.922  1.00 52.94           C  
ANISOU 2833  CB  VAL B  77     7562   6992   5560   1859    319    300       C  
ATOM   2834  CG1 VAL B  77      53.553  22.509  47.790  1.00 54.99           C  
ANISOU 2834  CG1 VAL B  77     7736   7202   5956   1838    145     54       C  
ATOM   2835  CG2 VAL B  77      54.520  20.766  49.218  1.00 57.52           C  
ANISOU 2835  CG2 VAL B  77     8193   7816   5846   2039    337    314       C  
ATOM   2836  N   PRO B  78      53.309  17.942  47.378  1.00 52.44           N  
ANISOU 2836  N   PRO B  78     7668   6786   5471   1774    756    821       N  
ATOM   2837  CA  PRO B  78      53.654  16.572  47.776  1.00 49.81           C  
ANISOU 2837  CA  PRO B  78     7452   6472   5003   1840    928   1056       C  
ATOM   2838  C   PRO B  78      54.701  16.560  48.884  1.00 53.33           C  
ANISOU 2838  C   PRO B  78     7953   7133   5176   2043    868   1083       C  
ATOM   2839  O   PRO B  78      55.719  17.251  48.815  1.00 55.27           O  
ANISOU 2839  O   PRO B  78     8158   7440   5401   2086    661    966       O  
ATOM   2840  CB  PRO B  78      54.197  15.948  46.482  1.00 48.85           C  
ANISOU 2840  CB  PRO B  78     7366   6141   5055   1718    901   1149       C  
ATOM   2841  CG  PRO B  78      53.849  16.876  45.395  1.00 51.73           C  
ANISOU 2841  CG  PRO B  78     7639   6381   5635   1567    757    991       C  
ATOM   2842  CD  PRO B  78      53.621  18.220  45.964  1.00 49.21           C  
ANISOU 2842  CD  PRO B  78     7232   6181   5285   1622    623    788       C  
ATOM   2843  N   ASN B  79      54.450  15.752  49.899  1.00 54.91           N  
ANISOU 2843  N   ASN B  79     8245   7452   5167   2162   1049   1244       N  
ATOM   2844  CA  ASN B  79      55.401  15.577  50.985  1.00 58.71           C  
ANISOU 2844  CA  ASN B  79     8797   8154   5354   2375    996   1305       C  
ATOM   2845  C   ASN B  79      56.606  14.795  50.484  1.00 63.01           C  
ANISOU 2845  C   ASN B  79     9400   8614   5925   2419    932   1454       C  
ATOM   2846  O   ASN B  79      56.445  13.643  50.065  1.00 64.17           O  
ANISOU 2846  O   ASN B  79     9638   8591   6152   2378   1098   1665       O  
ATOM   2847  CB  ASN B  79      54.734  14.837  52.122  1.00 60.99           C  
ANISOU 2847  CB  ASN B  79     9193   8574   5407   2483   1232   1479       C  
ATOM   2848  CG  ASN B  79      55.605  14.742  53.346  1.00 69.48           C  
ANISOU 2848  CG  ASN B  79    10350   9918   6131   2725   1164   1537       C  
ATOM   2849  OD1 ASN B  79      56.530  15.538  53.539  1.00 71.61           O  
ANISOU 2849  OD1 ASN B  79    10555  10329   6322   2812    919   1362       O  
ATOM   2850  ND2 ASN B  79      55.311  13.761  54.191  1.00 66.51           N  
ANISOU 2850  ND2 ASN B  79    10118   9616   5537   2833   1378   1786       N  
ATOM   2851  N   PRO B  80      57.811  15.363  50.497  1.00 61.05           N  
ANISOU 2851  N   PRO B  80     9094   8472   5631   2499    704   1340       N  
ATOM   2852  CA  PRO B  80      58.972  14.627  49.993  1.00 56.09           C  
ANISOU 2852  CA  PRO B  80     8492   7775   5046   2550    650   1466       C  
ATOM   2853  C   PRO B  80      59.533  13.695  51.055  1.00 58.48           C  
ANISOU 2853  C   PRO B  80     8909   8232   5077   2791    704   1676       C  
ATOM   2854  O   PRO B  80      59.512  13.993  52.250  1.00 61.38           O  
ANISOU 2854  O   PRO B  80     9302   8847   5174   2946    670   1651       O  
ATOM   2855  CB  PRO B  80      59.968  15.740  49.643  1.00 51.92           C  
ANISOU 2855  CB  PRO B  80     7821   7321   4586   2525    386   1235       C  
ATOM   2856  CG  PRO B  80      59.674  16.810  50.675  1.00 57.43           C  
ANISOU 2856  CG  PRO B  80     8470   8238   5113   2594    284   1038       C  
ATOM   2857  CD  PRO B  80      58.156  16.758  50.853  1.00 57.41           C  
ANISOU 2857  CD  PRO B  80     8518   8173   5124   2521    482   1064       C  
ATOM   2858  N   HIS B  81      60.047  12.553  50.597  1.00 60.04           N  
ANISOU 2858  N   HIS B  81     9186   8282   5346   2833    784   1883       N  
ATOM   2859  CA  HIS B  81      60.565  11.517  51.485  1.00 62.30           C  
ANISOU 2859  CA  HIS B  81     9605   8660   5407   3073    846   2131       C  
ATOM   2860  C   HIS B  81      62.063  11.294  51.347  1.00 64.55           C  
ANISOU 2860  C   HIS B  81     9834   9012   5680   3232    664   2143       C  
ATOM   2861  O   HIS B  81      62.762  11.229  52.356  1.00 66.42           O  
ANISOU 2861  O   HIS B  81    10089   9490   5659   3467    551   2196       O  
ATOM   2862  CB  HIS B  81      59.802  10.213  51.245  1.00 66.83           C  
ANISOU 2862  CB  HIS B  81    10340   8984   6070   3022   1129   2396       C  
ATOM   2863  CG  HIS B  81      58.352  10.300  51.611  1.00 71.47           C  
ANISOU 2863  CG  HIS B  81    10972   9550   6633   2898   1331   2414       C  
ATOM   2864  ND1 HIS B  81      57.346   9.830  50.793  1.00 70.24           N  
ANISOU 2864  ND1 HIS B  81    10836   9127   6723   2679   1524   2455       N  
ATOM   2865  CD2 HIS B  81      57.740  10.814  52.703  1.00 71.81           C  
ANISOU 2865  CD2 HIS B  81    11028   9820   6437   2962   1371   2378       C  
ATOM   2866  CE1 HIS B  81      56.177  10.044  51.371  1.00 70.97           C  
ANISOU 2866  CE1 HIS B  81    10935   9284   6746   2611   1677   2450       C  
ATOM   2867  NE2 HIS B  81      56.387  10.647  52.526  1.00 72.48           N  
ANISOU 2867  NE2 HIS B  81    11126   9773   6641   2783   1598   2403       N  
ATOM   2868  N   LYS B  82      62.590  11.166  50.130  1.00 62.87           N  
ANISOU 2868  N   LYS B  82     9546   8612   5730   3118    630   2092       N  
ATOM   2869  CA  LYS B  82      64.016  10.891  49.987  1.00 68.83           C  
ANISOU 2869  CA  LYS B  82    10224   9437   6491   3275    480   2103       C  
ATOM   2870  C   LYS B  82      64.471  11.197  48.561  1.00 69.55           C  
ANISOU 2870  C   LYS B  82    10188   9362   6876   3084    434   1955       C  
ATOM   2871  O   LYS B  82      63.772  10.878  47.593  1.00 67.40           O  
ANISOU 2871  O   LYS B  82     9969   8839   6802   2894    585   1977       O  
ATOM   2872  CB  LYS B  82      64.322   9.429  50.341  1.00 69.01           C  
ANISOU 2872  CB  LYS B  82    10392   9371   6459   3465    610   2381       C  
ATOM   2873  CG  LYS B  82      65.791   9.047  50.326  1.00 71.92           C  
ANISOU 2873  CG  LYS B  82    10658   9826   6842   3645    461   2379       C  
ATOM   2874  CD  LYS B  82      66.072   7.850  51.222  1.00 68.69           C  
ANISOU 2874  CD  LYS B  82    10346   9421   6331   3811    537   2560       C  
ATOM   2875  CE  LYS B  82      67.550   7.493  51.208  1.00 76.21           C  
ANISOU 2875  CE  LYS B  82    11182  10471   7301   4008    376   2552       C  
ATOM   2876  NZ  LYS B  82      67.880   6.250  51.992  1.00 80.54           N  
ANISOU 2876  NZ  LYS B  82    11837  10992   7771   4186    443   2747       N  
ATOM   2877  N   ALA B  83      65.654  11.805  48.446  1.00 68.46           N  
ANISOU 2877  N   ALA B  83     9878   9380   6755   3133    226   1802       N  
ATOM   2878  CA  ALA B  83      66.332  11.986  47.174  1.00 66.77           C  
ANISOU 2878  CA  ALA B  83     9538   9046   6785   2990    191   1690       C  
ATOM   2879  C   ALA B  83      67.751  11.468  47.319  1.00 71.56           C  
ANISOU 2879  C   ALA B  83    10046   9774   7369   3207     90   1731       C  
ATOM   2880  O   ALA B  83      68.323  11.498  48.406  1.00 76.64           O  
ANISOU 2880  O   ALA B  83    10653  10660   7808   3431    -49   1752       O  
ATOM   2881  CB  ALA B  83      66.360  13.456  46.724  1.00 57.25           C  
ANISOU 2881  CB  ALA B  83     8177   7897   5678   2776     45   1427       C  
ATOM   2882  N   GLY B  84      68.327  11.004  46.222  1.00 71.73           N  
ANISOU 2882  N   GLY B  84    10016   9645   7594   3151    153   1731       N  
ATOM   2883  CA  GLY B  84      69.678  10.498  46.304  1.00 75.97           C  
ANISOU 2883  CA  GLY B  84    10432  10295   8137   3366     66   1757       C  
ATOM   2884  C   GLY B  84      70.168   9.919  45.001  1.00 75.67           C  
ANISOU 2884  C   GLY B  84    10354  10064   8333   3291    184   1750       C  
ATOM   2885  O   GLY B  84      69.588  10.140  43.937  1.00 75.19           O  
ANISOU 2885  O   GLY B  84    10329   9815   8424   3037    295   1682       O  
ATOM   2886  N   GLU B  85      71.233   9.139  45.118  1.00 77.74           N  
ANISOU 2886  N   GLU B  85    10547  10383   8609   3533    157   1823       N  
ATOM   2887  CA  GLU B  85      71.999   8.650  43.988  1.00 77.60           C  
ANISOU 2887  CA  GLU B  85    10436  10250   8800   3512    242   1777       C  
ATOM   2888  C   GLU B  85      71.607   7.206  43.710  1.00 71.08           C  
ANISOU 2888  C   GLU B  85     9825   9146   8037   3627    454   1979       C  
ATOM   2889  O   GLU B  85      71.317   6.450  44.638  1.00 69.38           O  
ANISOU 2889  O   GLU B  85     9767   8902   7691   3842    479   2184       O  
ATOM   2890  CB  GLU B  85      73.492   8.767  44.310  1.00 86.63           C  
ANISOU 2890  CB  GLU B  85    11323  11650   9943   3719     66   1696       C  
ATOM   2891  CG  GLU B  85      74.441   8.723  43.126  1.00 97.70           C  
ANISOU 2891  CG  GLU B  85    12535  13023  11562   3644    122   1563       C  
ATOM   2892  CD  GLU B  85      75.848   9.206  43.478  1.00104.11           C  
ANISOU 2892  CD  GLU B  85    13029  14142  12388   3778    -81   1425       C  
ATOM   2893  OE1 GLU B  85      76.189   9.276  44.678  1.00106.95           O  
ANISOU 2893  OE1 GLU B  85    13334  14724  12580   4003   -271   1463       O  
ATOM   2894  OE2 GLU B  85      76.613   9.529  42.547  1.00106.52           O  
ANISOU 2894  OE2 GLU B  85    13130  14478  12864   3651    -48   1272       O  
ATOM   2895  N   LEU B  86      71.517   6.848  42.428  1.00 71.01           N  
ANISOU 2895  N   LEU B  86     9842   8918   8221   3466    614   1920       N  
ATOM   2896  CA  LEU B  86      71.277   5.439  42.126  1.00 74.07           C  
ANISOU 2896  CA  LEU B  86    10418   9026   8698   3583    809   2079       C  
ATOM   2897  C   LEU B  86      72.604   4.684  42.061  1.00 84.38           C  
ANISOU 2897  C   LEU B  86    11604  10373  10082   3868    790   2098       C  
ATOM   2898  O   LEU B  86      73.565   5.175  41.461  1.00 83.04           O  
ANISOU 2898  O   LEU B  86    11203  10350  10001   3834    726   1923       O  
ATOM   2899  CB  LEU B  86      70.545   5.262  40.800  1.00 66.27           C  
ANISOU 2899  CB  LEU B  86     9531   7779   7871   3304    991   1995       C  
ATOM   2900  CG  LEU B  86      69.081   5.660  40.762  1.00 63.66           C  
ANISOU 2900  CG  LEU B  86     9350   7334   7503   3051   1050   2006       C  
ATOM   2901  CD1 LEU B  86      68.520   5.570  39.343  1.00 66.64           C  
ANISOU 2901  CD1 LEU B  86     9786   7501   8034   2782   1187   1889       C  
ATOM   2902  CD2 LEU B  86      68.290   4.819  41.734  1.00 56.46           C  
ANISOU 2902  CD2 LEU B  86     8647   6297   6507   3184   1138   2233       C  
ATOM   2903  N   PRO B  87      72.703   3.500  42.675  1.00 97.05           N  
ANISOU 2903  N   PRO B  87    13349  11858  11667   4132    846   2299       N  
ATOM   2904  CA  PRO B  87      73.978   2.770  42.602  1.00102.73           C  
ANISOU 2904  CA  PRO B  87    13934  12620  12479   4379    816   2286       C  
ATOM   2905  C   PRO B  87      74.332   2.396  41.178  1.00105.18           C  
ANISOU 2905  C   PRO B  87    14204  12740  13022   4345    983   2172       C  
ATOM   2906  O   PRO B  87      75.503   2.470  40.792  1.00104.08           O  
ANISOU 2906  O   PRO B  87    13827  12746  12973   4457    930   2044       O  
ATOM   2907  CB  PRO B  87      73.728   1.544  43.486  1.00102.48           C  
ANISOU 2907  CB  PRO B  87    14096  12457  12387   4487    865   2470       C  
ATOM   2908  CG  PRO B  87      72.260   1.317  43.387  1.00103.97           C  
ANISOU 2908  CG  PRO B  87    14530  12407  12569   4240   1035   2542       C  
ATOM   2909  CD  PRO B  87      71.626   2.677  43.257  1.00100.42           C  
ANISOU 2909  CD  PRO B  87    14029  12092  12035   4046    970   2451       C  
ATOM   2910  N   THR B  88      73.328   2.038  40.372  1.00107.85           N  
ANISOU 2910  N   THR B  88    14742  12786  13450   4111   1178   2161       N  
ATOM   2911  CA  THR B  88      73.544   1.749  38.960  1.00110.25           C  
ANISOU 2911  CA  THR B  88    15016  12936  13939   3970   1336   1988       C  
ATOM   2912  C   THR B  88      74.040   2.967  38.182  1.00104.66           C  
ANISOU 2912  C   THR B  88    14065  12464  13237   3737   1265   1751       C  
ATOM   2913  O   THR B  88      74.653   2.801  37.122  1.00103.84           O  
ANISOU 2913  O   THR B  88    13861  12334  13259   3691   1368   1599       O  
ATOM   2914  CB  THR B  88      72.245   1.219  38.337  1.00115.30           C  
ANISOU 2914  CB  THR B  88    15922  13244  14645   3742   1527   2013       C  
ATOM   2915  OG1 THR B  88      71.397   2.318  37.972  1.00119.47           O  
ANISOU 2915  OG1 THR B  88    16441  13852  15102   3399   1487   1906       O  
ATOM   2916  CG2 THR B  88      71.499   0.338  39.325  1.00114.90           C  
ANISOU 2916  CG2 THR B  88    16084  13035  14539   3808   1562   2224       C  
ATOM   2917  N   GLY B  89      73.796   4.177  38.681  1.00 97.24           N  
ANISOU 2917  N   GLY B  89    13034  11744  12168   3588   1104   1716       N  
ATOM   2918  CA  GLY B  89      74.137   5.429  37.997  1.00 88.67           C  
ANISOU 2918  CA  GLY B  89    11747  10849  11094   3333   1038   1515       C  
ATOM   2919  C   GLY B  89      72.869   6.240  37.811  1.00 82.51           C  
ANISOU 2919  C   GLY B  89    11101  10003  10246   3021   1032   1497       C  
ATOM   2920  O   GLY B  89      71.832   5.731  37.391  1.00 85.54           O  
ANISOU 2920  O   GLY B  89    11702  10147  10654   2904   1165   1547       O  
ATOM   2921  N   GLY B  90      72.954   7.522  38.132  1.00 74.27           N  
ANISOU 2921  N   GLY B  90     9917   9173   9131   2889    871   1413       N  
ATOM   2922  CA  GLY B  90      71.800   8.394  38.114  1.00 70.06           C  
ANISOU 2922  CA  GLY B  90     9487   8599   8535   2634    834   1395       C  
ATOM   2923  C   GLY B  90      71.287   8.734  39.503  1.00 68.53           C  
ANISOU 2923  C   GLY B  90     9338   8510   8192   2737    696   1488       C  
ATOM   2924  O   GLY B  90      71.970   8.565  40.521  1.00 65.44           O  
ANISOU 2924  O   GLY B  90     8861   8286   7717   2986    582   1544       O  
ATOM   2925  N   SER B  91      70.045   9.222  39.536  1.00 67.05           N  
ANISOU 2925  N   SER B  91     9284   8234   7959   2548    705   1497       N  
ATOM   2926  CA  SER B  91      69.451   9.802  40.736  1.00 61.36           C  
ANISOU 2926  CA  SER B  91     8592   7631   7090   2590    584   1539       C  
ATOM   2927  C   SER B  91      67.956   9.507  40.787  1.00 57.51           C  
ANISOU 2927  C   SER B  91     8317   6953   6581   2480    699   1631       C  
ATOM   2928  O   SER B  91      67.336   9.161  39.778  1.00 57.64           O  
ANISOU 2928  O   SER B  91     8430   6764   6706   2311    831   1618       O  
ATOM   2929  CB  SER B  91      69.681  11.302  40.751  1.00 60.26           C  
ANISOU 2929  CB  SER B  91     8288   7668   6940   2429    415   1367       C  
ATOM   2930  OG  SER B  91      69.222  11.840  39.520  1.00 68.55           O  
ANISOU 2930  OG  SER B  91     9357   8584   8104   2148    477   1276       O  
ATOM   2931  N   TYR B  92      67.372   9.694  41.971  1.00 58.40           N  
ANISOU 2931  N   TYR B  92     8488   7155   6545   2569    644   1706       N  
ATOM   2932  CA  TYR B  92      65.959   9.411  42.200  1.00 58.32           C  
ANISOU 2932  CA  TYR B  92     8652   6998   6508   2481    762   1798       C  
ATOM   2933  C   TYR B  92      65.393  10.402  43.208  1.00 62.38           C  
ANISOU 2933  C   TYR B  92     9139   7688   6874   2472    646   1754       C  
ATOM   2934  O   TYR B  92      66.132  11.080  43.929  1.00 65.61           O  
ANISOU 2934  O   TYR B  92     9426   8329   7173   2584    477   1682       O  
ATOM   2935  CB  TYR B  92      65.730   7.972  42.714  1.00 62.31           C  
ANISOU 2935  CB  TYR B  92     9332   7360   6985   2665    922   2021       C  
ATOM   2936  CG  TYR B  92      66.256   7.732  44.123  1.00 65.86           C  
ANISOU 2936  CG  TYR B  92     9789   7999   7235   2955    842   2157       C  
ATOM   2937  CD1 TYR B  92      67.585   7.353  44.340  1.00 65.16           C  
ANISOU 2937  CD1 TYR B  92     9611   8023   7125   3194    754   2186       C  
ATOM   2938  CD2 TYR B  92      65.426   7.890  45.239  1.00 63.09           C  
ANISOU 2938  CD2 TYR B  92     9531   7734   6706   3000    853   2252       C  
ATOM   2939  CE1 TYR B  92      68.080   7.155  45.630  1.00 64.63           C  
ANISOU 2939  CE1 TYR B  92     9549   8153   6853   3476    651   2311       C  
ATOM   2940  CE2 TYR B  92      65.905   7.703  46.526  1.00 62.48           C  
ANISOU 2940  CE2 TYR B  92     9476   7858   6407   3270    772   2376       C  
ATOM   2941  CZ  TYR B  92      67.230   7.329  46.714  1.00 69.59           C  
ANISOU 2941  CZ  TYR B  92    10283   8872   7288   3490    660   2392       C  
ATOM   2942  OH  TYR B  92      67.696   7.138  47.990  1.00 74.12           O  
ANISOU 2942  OH  TYR B  92    10847   9662   7653   3695    561   2456       O  
ATOM   2943  N   ILE B  93      64.063  10.470  43.262  1.00 60.88           N  
ANISOU 2943  N   ILE B  93     9052   7392   6686   2341    739   1779       N  
ATOM   2944  CA  ILE B  93      63.361  11.129  44.359  1.00 60.68           C  
ANISOU 2944  CA  ILE B  93     9035   7514   6504   2372    686   1767       C  
ATOM   2945  C   ILE B  93      62.099  10.332  44.679  1.00 61.27           C  
ANISOU 2945  C   ILE B  93     9270   7444   6564   2345    885   1920       C  
ATOM   2946  O   ILE B  93      61.444   9.799  43.774  1.00 57.20           O  
ANISOU 2946  O   ILE B  93     8819   6704   6211   2187   1019   1942       O  
ATOM   2947  CB  ILE B  93      63.029  12.599  44.023  1.00 50.31           C  
ANISOU 2947  CB  ILE B  93     7607   6266   5243   2186    547   1553       C  
ATOM   2948  CG1 ILE B  93      62.386  13.306  45.228  1.00 55.02           C  
ANISOU 2948  CG1 ILE B  93     8201   7031   5672   2247    489   1509       C  
ATOM   2949  CG2 ILE B  93      62.102  12.681  42.840  1.00 45.57           C  
ANISOU 2949  CG2 ILE B  93     7042   5452   4820   1944    631   1510       C  
ATOM   2950  CD1 ILE B  93      62.256  14.817  45.038  1.00 50.21           C  
ANISOU 2950  CD1 ILE B  93     7472   6489   5117   2108    324   1283       C  
ATOM   2951  N   ILE B  94      61.767  10.244  45.969  1.00 59.18           N  
ANISOU 2951  N   ILE B  94     9066   7320   6099   2494    910   2020       N  
ATOM   2952  CA  ILE B  94      60.546   9.600  46.451  1.00 61.18           C  
ANISOU 2952  CA  ILE B  94     9455   7474   6317   2463   1113   2168       C  
ATOM   2953  C   ILE B  94      59.696  10.654  47.143  1.00 61.83           C  
ANISOU 2953  C   ILE B  94     9482   7723   6289   2410   1068   2050       C  
ATOM   2954  O   ILE B  94      60.187  11.391  48.005  1.00 64.04           O  
ANISOU 2954  O   ILE B  94     9701   8248   6382   2543    919   1971       O  
ATOM   2955  CB  ILE B  94      60.819   8.451  47.444  1.00 60.90           C  
ANISOU 2955  CB  ILE B  94     9570   7452   6117   2699   1230   2432       C  
ATOM   2956  CG1 ILE B  94      61.882   7.482  46.939  1.00 60.90           C  
ANISOU 2956  CG1 ILE B  94     9582   7329   6227   2791   1230   2497       C  
ATOM   2957  CG2 ILE B  94      59.515   7.688  47.750  1.00 53.95           C  
ANISOU 2957  CG2 ILE B  94     8807   6421   5271   2590   1476   2563       C  
ATOM   2958  CD1 ILE B  94      62.173   6.385  47.959  1.00 64.59           C  
ANISOU 2958  CD1 ILE B  94    10128   7822   6589   2958   1303   2659       C  
ATOM   2959  N   MET B  95      58.416  10.691  46.813  1.00 60.83           N  
ANISOU 2959  N   MET B  95     9368   7470   6273   2228   1198   2027       N  
ATOM   2960  CA  MET B  95      57.542  11.652  47.464  1.00 59.12           C  
ANISOU 2960  CA  MET B  95     9090   7403   5969   2191   1175   1907       C  
ATOM   2961  C   MET B  95      56.151  11.046  47.602  1.00 63.61           C  
ANISOU 2961  C   MET B  95     9721   7855   6592   2083   1415   2010       C  
ATOM   2962  O   MET B  95      55.858   9.966  47.077  1.00 68.88           O  
ANISOU 2962  O   MET B  95    10473   8304   7392   2003   1579   2151       O  
ATOM   2963  CB  MET B  95      57.513  12.983  46.688  1.00 55.65           C  
ANISOU 2963  CB  MET B  95     8504   6973   5667   2046    985   1651       C  
ATOM   2964  CG  MET B  95      56.735  12.928  45.374  1.00 57.62           C  
ANISOU 2964  CG  MET B  95     8729   6992   6172   1812   1036   1600       C  
ATOM   2965  SD  MET B  95      56.774  14.442  44.356  1.00 59.19           S  
ANISOU 2965  SD  MET B  95     8789   7171   6528   1653    809   1349       S  
ATOM   2966  CE  MET B  95      58.472  14.443  43.792  1.00 51.49           C  
ANISOU 2966  CE  MET B  95     7794   6211   5559   1702    671   1339       C  
ATOM   2967  N   GLU B  96      55.300  11.776  48.319  1.00 63.25           N  
ANISOU 2967  N   GLU B  96     9621   7958   6454   2076   1436   1919       N  
ATOM   2968  CA  GLU B  96      53.886  11.452  48.451  1.00 55.91           C  
ANISOU 2968  CA  GLU B  96     8693   6956   5594   1951   1653   1964       C  
ATOM   2969  C   GLU B  96      53.198  11.333  47.094  1.00 53.52           C  
ANISOU 2969  C   GLU B  96     8326   6413   5596   1712   1674   1888       C  
ATOM   2970  O   GLU B  96      53.369  12.183  46.218  1.00 53.17           O  
ANISOU 2970  O   GLU B  96     8184   6338   5680   1624   1487   1707       O  
ATOM   2971  CB  GLU B  96      53.198  12.547  49.272  1.00 51.72           C  
ANISOU 2971  CB  GLU B  96     8067   6645   4941   1986   1623   1802       C  
ATOM   2972  CG  GLU B  96      51.704  12.382  49.406  1.00 58.33           C  
ANISOU 2972  CG  GLU B  96     8854   7442   5866   1856   1839   1807       C  
ATOM   2973  CD  GLU B  96      51.017  13.573  50.068  1.00 68.54           C  
ANISOU 2973  CD  GLU B  96    10025   8940   7077   1892   1795   1600       C  
ATOM   2974  OE1 GLU B  96      51.701  14.578  50.393  1.00 68.79           O  
ANISOU 2974  OE1 GLU B  96    10018   9126   6992   2008   1583   1436       O  
ATOM   2975  OE2 GLU B  96      49.775  13.497  50.252  1.00 68.57           O  
ANISOU 2975  OE2 GLU B  96     9959   8943   7150   1801   1979   1587       O  
ATOM   2976  N   PHE B  97      52.360  10.305  46.946  1.00 57.06           N  
ANISOU 2976  N   PHE B  97     8830   6696   6156   1598   1904   2024       N  
ATOM   2977  CA  PHE B  97      51.508  10.155  45.770  1.00 59.85           C  
ANISOU 2977  CA  PHE B  97     9108   6847   6783   1364   1934   1936       C  
ATOM   2978  C   PHE B  97      50.183  10.879  45.991  1.00 64.28           C  
ANISOU 2978  C   PHE B  97     9522   7496   7405   1266   1974   1802       C  
ATOM   2979  O   PHE B  97      49.497  10.639  46.994  1.00 63.90           O  
ANISOU 2979  O   PHE B  97     9479   7546   7255   1302   2166   1885       O  
ATOM   2980  CB  PHE B  97      51.236   8.680  45.453  1.00 58.72           C  
ANISOU 2980  CB  PHE B  97     9080   6464   6766   1268   2155   2117       C  
ATOM   2981  CG  PHE B  97      50.459   8.483  44.180  1.00 65.03           C  
ANISOU 2981  CG  PHE B  97     9803   7065   7841   1025   2158   2001       C  
ATOM   2982  CD1 PHE B  97      49.065   8.537  44.181  1.00 63.54           C  
ANISOU 2982  CD1 PHE B  97     9498   6864   7783    863   2273   1938       C  
ATOM   2983  CD2 PHE B  97      51.120   8.296  42.969  1.00 66.64           C  
ANISOU 2983  CD2 PHE B  97    10036   7120   8163    962   2033   1935       C  
ATOM   2984  CE1 PHE B  97      48.344   8.406  42.994  1.00 63.30           C  
ANISOU 2984  CE1 PHE B  97     9378   6677   7997    645   2239   1810       C  
ATOM   2985  CE2 PHE B  97      50.408   8.150  41.770  1.00 60.67           C  
ANISOU 2985  CE2 PHE B  97     9215   6208   7629    744   2012   1811       C  
ATOM   2986  CZ  PHE B  97      49.021   8.206  41.780  1.00 57.68           C  
ANISOU 2986  CZ  PHE B  97     8718   5820   7378    587   2102   1747       C  
ATOM   2987  N   ILE B  98      49.814  11.743  45.038  1.00 61.15           N  
ANISOU 2987  N   ILE B  98     8995   7066   7175   1149   1801   1601       N  
ATOM   2988  CA  ILE B  98      48.578  12.516  45.098  1.00 61.84           C  
ANISOU 2988  CA  ILE B  98     8917   7224   7356   1071   1801   1448       C  
ATOM   2989  C   ILE B  98      47.738  12.195  43.871  1.00 64.78           C  
ANISOU 2989  C   ILE B  98     9207   7412   7994    853   1800   1384       C  
ATOM   2990  O   ILE B  98      48.252  12.093  42.752  1.00 67.10           O  
ANISOU 2990  O   ILE B  98     9539   7571   8385    777   1666   1354       O  
ATOM   2991  CB  ILE B  98      48.834  14.035  45.189  1.00 62.66           C  
ANISOU 2991  CB  ILE B  98     8928   7472   7408   1164   1561   1250       C  
ATOM   2992  CG1 ILE B  98      49.689  14.362  46.409  1.00 63.32           C  
ANISOU 2992  CG1 ILE B  98     9083   7754   7220   1374   1541   1281       C  
ATOM   2993  CG2 ILE B  98      47.516  14.804  45.278  1.00 61.18           C  
ANISOU 2993  CG2 ILE B  98     8564   7348   7335   1111   1567   1090       C  
ATOM   2994  CD1 ILE B  98      49.847  15.844  46.650  1.00 61.28           C  
ANISOU 2994  CD1 ILE B  98     8732   7631   6921   1459   1330   1065       C  
ATOM   2995  N   ASP B  99      46.441  12.043  44.096  1.00 68.86           N  
ANISOU 2995  N   ASP B  99     9601   7941   8620    753   1950   1353       N  
ATOM   2996  CA  ASP B  99      45.474  11.724  43.058  1.00 76.41           C  
ANISOU 2996  CA  ASP B  99    10446   8754   9831    542   1953   1273       C  
ATOM   2997  C   ASP B  99      44.991  13.024  42.435  1.00 72.18           C  
ANISOU 2997  C   ASP B  99     9746   8283   9397    532   1710   1059       C  
ATOM   2998  O   ASP B  99      44.209  13.753  43.051  1.00 73.78           O  
ANISOU 2998  O   ASP B  99     9803   8626   9605    585   1727    959       O  
ATOM   2999  CB  ASP B  99      44.309  10.952  43.664  1.00 90.49           C  
ANISOU 2999  CB  ASP B  99    12149  10535  11698    437   2239   1339       C  
ATOM   3000  CG  ASP B  99      43.318  10.506  42.634  1.00110.10           C  
ANISOU 3000  CG  ASP B  99    14503  12875  14456    206   2247   1247       C  
ATOM   3001  OD1 ASP B  99      43.564  10.791  41.441  1.00114.31           O  
ANISOU 3001  OD1 ASP B  99    15030  13320  15084    143   2021   1140       O  
ATOM   3002  OD2 ASP B  99      42.296   9.887  43.013  1.00118.10           O  
ANISOU 3002  OD2 ASP B  99    15416  13874  15583     82   2478   1278       O  
ATOM   3003  N   PHE B 100      45.455  13.320  41.221  1.00 72.03           N  
ANISOU 3003  N   PHE B 100     9754   8160   9453    473   1491    992       N  
ATOM   3004  CA  PHE B 100      45.091  14.558  40.543  1.00 67.63           C  
ANISOU 3004  CA  PHE B 100     9075   7637   8985    474   1241    821       C  
ATOM   3005  C   PHE B 100      43.850  14.382  39.698  1.00 70.84           C  
ANISOU 3005  C   PHE B 100     9325   7980   9612    309   1215    725       C  
ATOM   3006  O   PHE B 100      43.427  13.269  39.389  1.00 77.81           O  
ANISOU 3006  O   PHE B 100    10209   8763  10592    161   1361    773       O  
ATOM   3007  CB  PHE B 100      46.214  15.055  39.633  1.00 57.51           C  
ANISOU 3007  CB  PHE B 100     7906   6289   7656    491   1015    809       C  
ATOM   3008  CG  PHE B 100      47.498  15.291  40.340  1.00 57.55           C  
ANISOU 3008  CG  PHE B 100     8034   6362   7469    642   1003    877       C  
ATOM   3009  CD1 PHE B 100      47.516  15.894  41.583  1.00 59.42           C  
ANISOU 3009  CD1 PHE B 100     8237   6755   7585    794   1039    851       C  
ATOM   3010  CD2 PHE B 100      48.693  14.916  39.764  1.00 58.29           C  
ANISOU 3010  CD2 PHE B 100     8265   6379   7501    636    953    950       C  
ATOM   3011  CE1 PHE B 100      48.698  16.112  42.234  1.00 55.04           C  
ANISOU 3011  CE1 PHE B 100     7781   6281   6850    931   1005    895       C  
ATOM   3012  CE2 PHE B 100      49.888  15.134  40.413  1.00 58.69           C  
ANISOU 3012  CE2 PHE B 100     8400   6510   7389    777    928   1000       C  
ATOM   3013  CZ  PHE B 100      49.887  15.735  41.650  1.00 58.71           C  
ANISOU 3013  CZ  PHE B 100     8364   6670   7271    922    943    971       C  
ATOM   3014  N   GLY B 101      43.245  15.511  39.355  1.00 76.18           N  
ANISOU 3014  N   GLY B 101     9857   8712  10377    341   1020    579       N  
ATOM   3015  CA  GLY B 101      42.143  15.529  38.421  1.00 83.21           C  
ANISOU 3015  CA  GLY B 101    10585   9561  11469    210    921    470       C  
ATOM   3016  C   GLY B 101      40.862  16.096  38.985  1.00 91.17           C  
ANISOU 3016  C   GLY B 101    11349  10690  12602    251    953    348       C  
ATOM   3017  O   GLY B 101      39.783  15.671  38.567  1.00100.06           O  
ANISOU 3017  O   GLY B 101    12304  11807  13907    121    985    279       O  
ATOM   3018  N   GLY B 102      40.941  17.038  39.922  1.00 89.52           N  
ANISOU 3018  N   GLY B 102    11105  10599  12311    428    947    301       N  
ATOM   3019  CA  GLY B 102      39.712  17.622  40.412  1.00 95.46           C  
ANISOU 3019  CA  GLY B 102    11611  11469  13192    483    978    162       C  
ATOM   3020  C   GLY B 102      39.012  18.303  39.262  1.00104.62           C  
ANISOU 3020  C   GLY B 102    12626  12581  14544    453    705     35       C  
ATOM   3021  O   GLY B 102      39.565  19.228  38.670  1.00109.08           O  
ANISOU 3021  O   GLY B 102    13276  13087  15082    534    449     11       O  
ATOM   3022  N   SER B 103      37.848  17.817  38.903  1.00110.82           N  
ANISOU 3022  N   SER B 103    13202  13386  15520    331    751    -34       N  
ATOM   3023  CA  SER B 103      37.140  18.335  37.763  1.00119.96           C  
ANISOU 3023  CA  SER B 103    14214  14513  16851    302    478   -147       C  
ATOM   3024  C   SER B 103      36.773  19.813  37.743  1.00131.31           C  
ANISOU 3024  C   SER B 103    15537  15994  18360    498    244   -272       C  
ATOM   3025  O   SER B 103      36.650  20.412  36.694  1.00135.78           O  
ANISOU 3025  O   SER B 103    16094  16497  19000    514    -43   -309       O  
ATOM   3026  CB  SER B 103      35.908  17.461  37.508  1.00124.20           C  
ANISOU 3026  CB  SER B 103    14512  15087  17593    125    591   -218       C  
ATOM   3027  OG  SER B 103      36.232  16.135  37.134  1.00130.12           O  
ANISOU 3027  OG  SER B 103    15384  15735  18320    -80    731   -121       O  
ATOM   3028  N   ARG B 104      36.568  20.419  38.884  1.00136.25           N  
ANISOU 3028  N   ARG B 104    16079  16723  18966    655    360   -340       N  
ATOM   3029  CA  ARG B 104      36.136  21.807  38.835  1.00137.25           C  
ANISOU 3029  CA  ARG B 104    16085  16864  19199    847    137   -479       C  
ATOM   3030  C   ARG B 104      37.340  22.722  38.660  1.00125.85           C  
ANISOU 3030  C   ARG B 104    14891  15308  17619    959    -57   -427       C  
ATOM   3031  O   ARG B 104      37.346  23.592  37.780  1.00133.05           O  
ANISOU 3031  O   ARG B 104    15823  16118  18611   1020   -346   -450       O  
ATOM   3032  CB  ARG B 104      35.319  22.166  40.089  1.00142.28           C  
ANISOU 3032  CB  ARG B 104    16504  17662  19892    980    336   -617       C  
ATOM   3033  CG  ARG B 104      34.142  21.204  40.381  1.00142.99           C  
ANISOU 3033  CG  ARG B 104    16331  17878  20121    845    585   -660       C  
ATOM   3034  CD  ARG B 104      33.168  21.745  41.444  1.00145.28           C  
ANISOU 3034  CD  ARG B 104    16354  18344  20502    993    749   -829       C  
ATOM   3035  NE  ARG B 104      32.213  20.744  41.928  1.00148.42           N  
ANISOU 3035  NE  ARG B 104    16525  18872  20994    843   1063   -841       N  
ATOM   3036  CZ  ARG B 104      32.256  20.171  43.130  1.00148.68           C  
ANISOU 3036  CZ  ARG B 104    16583  19025  20883    821   1425   -785       C  
ATOM   3037  NH1 ARG B 104      33.188  20.526  44.006  1.00148.64           N  
ANISOU 3037  NH1 ARG B 104    16807  19049  20621    960   1498   -732       N  
ATOM   3038  NH2 ARG B 104      31.349  19.263  43.469  1.00148.21           N  
ANISOU 3038  NH2 ARG B 104    16314  19065  20936    659   1713   -783       N  
ATOM   3039  N   GLY B 105      38.375  22.538  39.470  1.00107.08           N  
ANISOU 3039  N   GLY B 105    12704  12945  15038    984     94   -350       N  
ATOM   3040  CA  GLY B 105      39.455  23.500  39.457  1.00 97.06           C  
ANISOU 3040  CA  GLY B 105    11625  11587  13667   1092    -76   -337       C  
ATOM   3041  C   GLY B 105      39.046  24.781  40.150  1.00 86.59           C  
ANISOU 3041  C   GLY B 105    10189  10293  12419   1301   -152   -509       C  
ATOM   3042  O   GLY B 105      37.865  24.980  40.425  1.00 78.99           O  
ANISOU 3042  O   GLY B 105     8989   9415  11609   1370   -110   -639       O  
ATOM   3043  N   ASN B 106      40.003  25.666  40.419  1.00 82.82           N  
ANISOU 3043  N   ASN B 106     9870   9744  11855   1400   -263   -529       N  
ATOM   3044  CA  ASN B 106      39.723  26.848  41.237  1.00 81.50           C  
ANISOU 3044  CA  ASN B 106     9621   9599  11747   1603   -307   -717       C  
ATOM   3045  C   ASN B 106      40.870  27.853  41.050  1.00 78.03           C  
ANISOU 3045  C   ASN B 106     9382   9002  11265   1655   -509   -715       C  
ATOM   3046  O   ASN B 106      41.855  27.812  41.783  1.00 67.59           O  
ANISOU 3046  O   ASN B 106     8192   7725   9762   1666   -427   -710       O  
ATOM   3047  CB  ASN B 106      39.537  26.472  42.692  1.00 76.91           C  
ANISOU 3047  CB  ASN B 106     8971   9223  11028   1675    -22   -800       C  
ATOM   3048  CG  ASN B 106      38.540  27.371  43.391  1.00 84.75           C  
ANISOU 3048  CG  ASN B 106     9757  10292  12154   1866     -7  -1032       C  
ATOM   3049  OD1 ASN B 106      38.289  28.507  42.949  1.00 72.35           O  
ANISOU 3049  OD1 ASN B 106     8144   8584  10762   1984   -241  -1144       O  
ATOM   3050  ND2 ASN B 106      37.961  26.874  44.487  1.00 90.93           N  
ANISOU 3050  ND2 ASN B 106    10413  11286  12849   1905    277  -1102       N  
ATOM   3051  N   GLN B 107      40.724  28.743  40.059  1.00 75.41           N  
ANISOU 3051  N   GLN B 107     9812   7983  10857    169    583   -313       N  
ATOM   3052  CA  GLN B 107      41.776  29.720  39.769  1.00 69.70           C  
ANISOU 3052  CA  GLN B 107     9143   7322  10019    234    472   -383       C  
ATOM   3053  C   GLN B 107      41.947  30.733  40.904  1.00 62.72           C  
ANISOU 3053  C   GLN B 107     8225   6568   9038    329    525   -422       C  
ATOM   3054  O   GLN B 107      43.069  31.157  41.203  1.00 57.56           O  
ANISOU 3054  O   GLN B 107     7636   5991   8242    397    497   -457       O  
ATOM   3055  CB  GLN B 107      41.478  30.439  38.460  1.00 69.35           C  
ANISOU 3055  CB  GLN B 107     9054   7229  10067    176    316   -457       C  
ATOM   3056  CG  GLN B 107      42.736  30.910  37.766  1.00 84.11           C  
ANISOU 3056  CG  GLN B 107    11016   9111  11832    203    208   -496       C  
ATOM   3057  CD  GLN B 107      42.470  31.559  36.412  1.00 94.99           C  
ANISOU 3057  CD  GLN B 107    12362  10451  13280    148     61   -537       C  
ATOM   3058  OE1 GLN B 107      41.583  32.436  36.250  1.00 90.63           O  
ANISOU 3058  OE1 GLN B 107    11707   9900  12829    147     16   -556       O  
ATOM   3059  NE2 GLN B 107      43.245  31.129  35.422  1.00 97.24           N  
ANISOU 3059  NE2 GLN B 107    12732  10710  13505    113    -14   -544       N  
ATOM   3060  N   ALA B 108      40.843  31.163  41.521  1.00 54.81           N  
ANISOU 3060  N   ALA B 108     7110   5601   8115    330    600   -439       N  
ATOM   3061  CA  ALA B 108      40.944  32.075  42.652  1.00 56.51           C  
ANISOU 3061  CA  ALA B 108     7289   5945   8237    417    667   -502       C  
ATOM   3062  C   ALA B 108      41.570  31.387  43.858  1.00 55.12           C  
ANISOU 3062  C   ALA B 108     7181   5890   7870    487    789   -428       C  
ATOM   3063  O   ALA B 108      42.400  31.978  44.552  1.00 57.88           O  
ANISOU 3063  O   ALA B 108     7561   6370   8061    565    789   -492       O  
ATOM   3064  CB  ALA B 108      39.564  32.645  42.999  1.00 47.78           C  
ANISOU 3064  CB  ALA B 108     6037   4849   7271    408    731   -543       C  
ATOM   3065  N   GLU B 109      41.209  30.131  44.111  1.00 54.02           N  
ANISOU 3065  N   GLU B 109     7068   5713   7746    459    894   -290       N  
ATOM   3066  CA  GLU B 109      41.830  29.406  45.216  1.00 59.71           C  
ANISOU 3066  CA  GLU B 109     7862   6547   8280    541   1009   -178       C  
ATOM   3067  C   GLU B 109      43.338  29.268  45.033  1.00 58.66           C  
ANISOU 3067  C   GLU B 109     7840   6452   7995    607    919   -175       C  
ATOM   3068  O   GLU B 109      44.098  29.356  46.005  1.00 59.40           O  
ANISOU 3068  O   GLU B 109     7966   6718   7884    709    955   -159       O  
ATOM   3069  CB  GLU B 109      41.191  28.029  45.350  1.00 62.13           C  
ANISOU 3069  CB  GLU B 109     8184   6751   8670    489   1141     -8       C  
ATOM   3070  CG  GLU B 109      41.665  27.205  46.518  1.00 64.97           C  
ANISOU 3070  CG  GLU B 109     8617   7216   8852    582   1282    157       C  
ATOM   3071  CD  GLU B 109      41.237  27.757  47.849  1.00 70.58           C  
ANISOU 3071  CD  GLU B 109     9262   8136   9418    650   1405    153       C  
ATOM   3072  OE1 GLU B 109      40.642  28.849  47.888  1.00 74.69           O  
ANISOU 3072  OE1 GLU B 109     9681   8714   9986    632   1380     -1       O  
ATOM   3073  OE2 GLU B 109      41.486  27.089  48.874  1.00 75.84           O  
ANISOU 3073  OE2 GLU B 109     9979   8917   9921    729   1534    310       O  
ATOM   3074  N   LEU B 110      43.787  29.073  43.795  1.00 50.97           N  
ANISOU 3074  N   LEU B 110     6915   5343   7110    553    799   -200       N  
ATOM   3075  CA  LEU B 110      45.216  29.010  43.515  1.00 53.22           C  
ANISOU 3075  CA  LEU B 110     7287   5666   7270    611    713   -215       C  
ATOM   3076  C   LEU B 110      45.897  30.329  43.858  1.00 52.95           C  
ANISOU 3076  C   LEU B 110     7220   5778   7119    661    641   -358       C  
ATOM   3077  O   LEU B 110      46.963  30.338  44.481  1.00 54.64           O  
ANISOU 3077  O   LEU B 110     7468   6135   7155    748    634   -362       O  
ATOM   3078  CB  LEU B 110      45.442  28.676  42.038  1.00 46.88           C  
ANISOU 3078  CB  LEU B 110     6526   4697   6589    531    606   -239       C  
ATOM   3079  CG  LEU B 110      46.866  28.805  41.502  1.00 51.02           C  
ANISOU 3079  CG  LEU B 110     7119   5252   7014    572    506   -285       C  
ATOM   3080  CD1 LEU B 110      47.826  27.778  42.159  1.00 43.67           C  
ANISOU 3080  CD1 LEU B 110     6263   4378   5951    678    570   -169       C  
ATOM   3081  CD2 LEU B 110      46.837  28.616  40.023  1.00 47.32           C  
ANISOU 3081  CD2 LEU B 110     6675   4639   6665    479    412   -326       C  
ATOM   3082  N   GLY B 111      45.289  31.453  43.462  1.00 47.70           N  
ANISOU 3082  N   GLY B 111     6482   5076   6565    608    587   -481       N  
ATOM   3083  CA  GLY B 111      45.888  32.747  43.740  1.00 45.89           C  
ANISOU 3083  CA  GLY B 111     6220   4945   6269    640    531   -632       C  
ATOM   3084  C   GLY B 111      45.918  33.057  45.224  1.00 50.35           C  
ANISOU 3084  C   GLY B 111     6748   5709   6675    721    627   -677       C  
ATOM   3085  O   GLY B 111      46.909  33.579  45.732  1.00 54.25           O  
ANISOU 3085  O   GLY B 111     7246   6344   7021    772    594   -773       O  
ATOM   3086  N   ARG B 112      44.821  32.758  45.930  1.00 46.95           N  
ANISOU 3086  N   ARG B 112     6269   5306   6266    729    749   -620       N  
ATOM   3087  CA  ARG B 112      44.782  32.902  47.383  1.00 51.27           C  
ANISOU 3087  CA  ARG B 112     6784   6068   6629    810    860   -644       C  
ATOM   3088  C   ARG B 112      45.831  32.025  48.071  1.00 52.28           C  
ANISOU 3088  C   ARG B 112     6988   6354   6521    899    881   -531       C  
ATOM   3089  O   ARG B 112      46.586  32.497  48.927  1.00 52.97           O  
ANISOU 3089  O   ARG B 112     7064   6657   6407    973    872   -623       O  
ATOM   3090  CB  ARG B 112      43.391  32.552  47.916  1.00 48.87           C  
ANISOU 3090  CB  ARG B 112     6415   5756   6397    794   1007   -569       C  
ATOM   3091  CG  ARG B 112      43.258  32.842  49.402  1.00 52.14           C  
ANISOU 3091  CG  ARG B 112     6787   6414   6609    876   1132   -614       C  
ATOM   3092  CD  ARG B 112      41.887  32.525  49.952  1.00 61.51           C  
ANISOU 3092  CD  ARG B 112     7900   7608   7865    857   1296   -540       C  
ATOM   3093  NE  ARG B 112      41.670  31.085  50.094  1.00 69.48           N  
ANISOU 3093  NE  ARG B 112     8966   8580   8853    850   1396   -294       N  
ATOM   3094  CZ  ARG B 112      42.157  30.347  51.091  1.00 77.01           C  
ANISOU 3094  CZ  ARG B 112     9981   9707   9573    935   1490   -149       C  
ATOM   3095  NH1 ARG B 112      42.912  30.896  52.038  1.00 84.94           N  
ANISOU 3095  NH1 ARG B 112    10990  10969  10315   1035   1483   -241       N  
ATOM   3096  NH2 ARG B 112      41.901  29.051  51.140  1.00 77.12           N  
ANISOU 3096  NH2 ARG B 112    10049   9638   9614    923   1592     88       N  
ATOM   3097  N   LYS B 113      45.858  30.729  47.751  1.00 51.94           N  
ANISOU 3097  N   LYS B 113     7016   6215   6505    900    914   -333       N  
ATOM   3098  CA  LYS B 113      46.802  29.842  48.432  1.00 53.40           C  
ANISOU 3098  CA  LYS B 113     7270   6538   6481   1008    943   -193       C  
ATOM   3099  C   LYS B 113      48.245  30.181  48.089  1.00 56.67           C  
ANISOU 3099  C   LYS B 113     7711   7025   6796   1051    804   -284       C  
ATOM   3100  O   LYS B 113      49.124  30.063  48.950  1.00 49.25           O  
ANISOU 3100  O   LYS B 113     6777   6307   5628   1160    800   -264       O  
ATOM   3101  CB  LYS B 113      46.508  28.378  48.106  1.00 50.95           C  
ANISOU 3101  CB  LYS B 113     7033   6062   6265    999   1021     36       C  
ATOM   3102  CG  LYS B 113      45.278  27.825  48.797  1.00 51.04           C  
ANISOU 3102  CG  LYS B 113     7018   6059   6317    980   1195    171       C  
ATOM   3103  CD  LYS B 113      45.575  27.530  50.233  1.00 59.37           C  
ANISOU 3103  CD  LYS B 113     8086   7366   7104   1110   1303    291       C  
ATOM   3104  CE  LYS B 113      44.626  26.467  50.771  1.00 72.11           C  
ANISOU 3104  CE  LYS B 113     9716   8916   8765   1099   1498    522       C  
ATOM   3105  NZ  LYS B 113      45.022  26.047  52.148  1.00 79.58           N  
ANISOU 3105  NZ  LYS B 113    10695  10121   9422   1244   1606    689       N  
ATOM   3106  N   LEU B 114      48.509  30.618  46.857  1.00 52.75           N  
ANISOU 3106  N   LEU B 114     7220   6365   6457    968    690   -383       N  
ATOM   3107  CA  LEU B 114      49.873  30.990  46.497  1.00 50.56           C  
ANISOU 3107  CA  LEU B 114     6955   6157   6101    993    571   -476       C  
ATOM   3108  C   LEU B 114      50.325  32.206  47.296  1.00 53.68           C  
ANISOU 3108  C   LEU B 114     7275   6762   6360   1018    538   -671       C  
ATOM   3109  O   LEU B 114      51.440  32.229  47.827  1.00 53.59           O  
ANISOU 3109  O   LEU B 114     7252   6947   6164   1094    492   -709       O  
ATOM   3110  CB  LEU B 114      49.961  31.281  44.996  1.00 46.47           C  
ANISOU 3110  CB  LEU B 114     6455   5425   5775    889    474   -537       C  
ATOM   3111  CG  LEU B 114      51.379  31.634  44.546  1.00 53.47           C  
ANISOU 3111  CG  LEU B 114     7347   6375   6594    902    367   -625       C  
ATOM   3112  CD1 LEU B 114      52.268  30.367  44.496  1.00 51.11           C  
ANISOU 3112  CD1 LEU B 114     7110   6101   6208    991    371   -481       C  
ATOM   3113  CD2 LEU B 114      51.411  32.402  43.224  1.00 48.69           C  
ANISOU 3113  CD2 LEU B 114     6739   5608   6153    790    280   -725       C  
ATOM   3114  N   ALA B 115      49.450  33.209  47.412  1.00 52.22           N  
ANISOU 3114  N   ALA B 115     7030   6541   6272    956    564   -806       N  
ATOM   3115  CA  ALA B 115      49.745  34.416  48.178  1.00 52.02           C  
ANISOU 3115  CA  ALA B 115     6929   6684   6152    966    550  -1025       C  
ATOM   3116  C   ALA B 115      49.958  34.106  49.649  1.00 49.22           C  
ANISOU 3116  C   ALA B 115     6552   6625   5522   1076    621  -1009       C  
ATOM   3117  O   ALA B 115      50.816  34.713  50.299  1.00 59.60           O  
ANISOU 3117  O   ALA B 115     7820   8155   6671   1111    574  -1169       O  
ATOM   3118  CB  ALA B 115      48.606  35.425  48.014  1.00 51.85           C  
ANISOU 3118  CB  ALA B 115     6849   6533   6318    896    588  -1149       C  
ATOM   3119  N   GLU B 116      49.173  33.183  50.203  1.00 50.10           N  
ANISOU 3119  N   GLU B 116     6692   6764   5580   1126    739   -821       N  
ATOM   3120  CA  GLU B 116      49.433  32.729  51.570  1.00 53.30           C  
ANISOU 3120  CA  GLU B 116     7091   7468   5693   1246    810   -750       C  
ATOM   3121  C   GLU B 116      50.825  32.119  51.704  1.00 53.08           C  
ANISOU 3121  C   GLU B 116     7096   7594   5479   1342    723   -670       C  
ATOM   3122  O   GLU B 116      51.482  32.290  52.735  1.00 58.96           O  
ANISOU 3122  O   GLU B 116     7799   8646   5955   1434    708   -729       O  
ATOM   3123  CB  GLU B 116      48.376  31.716  52.018  1.00 54.58           C  
ANISOU 3123  CB  GLU B 116     7288   7596   5853   1275    967   -513       C  
ATOM   3124  CG  GLU B 116      46.942  32.246  52.105  1.00 63.67           C  
ANISOU 3124  CG  GLU B 116     8381   8653   7158   1200   1074   -584       C  
ATOM   3125  CD  GLU B 116      46.734  33.176  53.288  1.00 89.04           C  
ANISOU 3125  CD  GLU B 116    11513  12128  10188   1240   1135   -776       C  
ATOM   3126  OE1 GLU B 116      47.711  33.442  54.027  1.00 98.48           O  
ANISOU 3126  OE1 GLU B 116    12698  13591  11131   1316   1083   -870       O  
ATOM   3127  OE2 GLU B 116      45.588  33.639  53.489  1.00100.51           O  
ANISOU 3127  OE2 GLU B 116    12905  13535  11750   1198   1237   -847       O  
ATOM   3128  N   MET B 117      51.289  31.382  50.689  1.00 52.15           N  
ANISOU 3128  N   MET B 117     7043   7283   5490   1330    666   -540       N  
ATOM   3129  CA  MET B 117      52.639  30.818  50.771  1.00 55.74           C  
ANISOU 3129  CA  MET B 117     7513   7877   5789   1433    584   -469       C  
ATOM   3130  C   MET B 117      53.704  31.909  50.699  1.00 51.28           C  
ANISOU 3130  C   MET B 117     6868   7455   5161   1405    453   -728       C  
ATOM   3131  O   MET B 117      54.662  31.895  51.473  1.00 56.07           O  
ANISOU 3131  O   MET B 117     7425   8347   5531   1505    400   -761       O  
ATOM   3132  CB  MET B 117      52.870  29.778  49.671  1.00 50.35           C  
ANISOU 3132  CB  MET B 117     6915   6941   5276   1427    569   -293       C  
ATOM   3133  CG  MET B 117      54.259  29.113  49.757  1.00 50.99           C  
ANISOU 3133  CG  MET B 117     7003   7158   5212   1557    496   -206       C  
ATOM   3134  SD  MET B 117      54.683  27.987  48.410  1.00 58.28           S  
ANISOU 3134  SD  MET B 117     8016   7787   6341   1554    477    -55       S  
ATOM   3135  CE  MET B 117      55.019  29.096  47.038  1.00 48.61           C  
ANISOU 3135  CE  MET B 117     6756   6414   5302   1389    359   -308       C  
ATOM   3136  N   HIS B 118      53.553  32.870  49.794  1.00 56.44           N  
ANISOU 3136  N   HIS B 118     7498   7921   6024   1269    402   -909       N  
ATOM   3137  CA  HIS B 118      54.495  33.983  49.775  1.00 55.61           C  
ANISOU 3137  CA  HIS B 118     7310   7931   5886   1222    301  -1164       C  
ATOM   3138  C   HIS B 118      54.537  34.678  51.119  1.00 53.81           C  
ANISOU 3138  C   HIS B 118     6999   8004   5441   1263    319  -1339       C  
ATOM   3139  O   HIS B 118      55.615  35.008  51.621  1.00 60.53           O  
ANISOU 3139  O   HIS B 118     7776   9103   6120   1299    239  -1476       O  
ATOM   3140  CB  HIS B 118      54.110  34.985  48.696  1.00 48.27           C  
ANISOU 3140  CB  HIS B 118     6376   6737   5228   1071    274  -1308       C  
ATOM   3141  CG  HIS B 118      54.270  34.467  47.311  1.00 46.55           C  
ANISOU 3141  CG  HIS B 118     6225   6270   5189   1020    233  -1184       C  
ATOM   3142  ND1 HIS B 118      53.768  35.127  46.209  1.00 51.66           N  
ANISOU 3142  ND1 HIS B 118     6888   6665   6074    899    215  -1238       N  
ATOM   3143  CD2 HIS B 118      54.864  33.348  46.845  1.00 47.59           C  
ANISOU 3143  CD2 HIS B 118     6414   6376   5293   1079    211  -1012       C  
ATOM   3144  CE1 HIS B 118      54.043  34.429  45.122  1.00 48.49           C  
ANISOU 3144  CE1 HIS B 118     6549   6114   5760    879    180  -1112       C  
ATOM   3145  NE2 HIS B 118      54.710  33.348  45.482  1.00 47.29           N  
ANISOU 3145  NE2 HIS B 118     6422   6084   5461    985    183   -986       N  
ATOM   3146  N   LYS B 119      53.368  34.880  51.727  1.00 52.47           N  
ANISOU 3146  N   LYS B 119     6830   7836   5269   1260    427  -1347       N  
ATOM   3147  CA  LYS B 119      53.280  35.651  52.960  1.00 55.27           C  
ANISOU 3147  CA  LYS B 119     7104   8467   5430   1286    460  -1554       C  
ATOM   3148  C   LYS B 119      53.818  34.870  54.151  1.00 57.93           C  
ANISOU 3148  C   LYS B 119     7429   9172   5411   1439    467  -1438       C  
ATOM   3149  O   LYS B 119      54.497  35.437  55.006  1.00 58.31           O  
ANISOU 3149  O   LYS B 119     7391   9529   5237   1472    414  -1637       O  
ATOM   3150  CB  LYS B 119      51.835  36.077  53.199  1.00 59.82           C  
ANISOU 3150  CB  LYS B 119     7678   8930   6122   1242    587  -1594       C  
ATOM   3151  CG  LYS B 119      51.654  37.006  54.385  1.00 68.04           C  
ANISOU 3151  CG  LYS B 119     8632  10226   6995   1255    635  -1855       C  
ATOM   3152  CD  LYS B 119      50.187  37.370  54.568  1.00 65.38           C  
ANISOU 3152  CD  LYS B 119     8285   9763   6794   1223    774  -1884       C  
ATOM   3153  CE  LYS B 119      49.944  38.082  55.886  1.00 69.86           C  
ANISOU 3153  CE  LYS B 119     8771  10622   7149   1259    852  -2121       C  
ATOM   3154  NZ  LYS B 119      48.500  38.451  56.011  1.00 77.97           N  
ANISOU 3154  NZ  LYS B 119     9775  11514   8335   1233    997  -2155       N  
ATOM   3155  N   ALA B 120      53.510  33.577  54.238  1.00 63.21           N  
ANISOU 3155  N   ALA B 120     8179   9816   6021   1535    535  -1116       N  
ATOM   3156  CA  ALA B 120      53.948  32.779  55.375  1.00 63.89           C  
ANISOU 3156  CA  ALA B 120     8264  10242   5769   1701    555   -952       C  
ATOM   3157  C   ALA B 120      55.416  32.390  55.286  1.00 67.09           C  
ANISOU 3157  C   ALA B 120     8640  10809   6041   1791    415   -917       C  
ATOM   3158  O   ALA B 120      56.060  32.220  56.323  1.00 71.73           O  
ANISOU 3158  O   ALA B 120     9174  11771   6310   1920    377   -906       O  
ATOM   3159  CB  ALA B 120      53.086  31.522  55.511  1.00 59.36           C  
ANISOU 3159  CB  ALA B 120     7790   9556   5208   1771    696   -600       C  
ATOM   3160  N   GLY B 121      55.955  32.217  54.079  1.00 68.02           N  
ANISOU 3160  N   GLY B 121     8785  10674   6384   1735    339   -892       N  
ATOM   3161  CA  GLY B 121      57.335  31.780  53.913  1.00 64.46           C  
ANISOU 3161  CA  GLY B 121     8297  10358   5835   1826    218   -848       C  
ATOM   3162  C   GLY B 121      58.350  32.895  54.088  1.00 65.59           C  
ANISOU 3162  C   GLY B 121     8304  10723   5894   1771     87  -1174       C  
ATOM   3163  O   GLY B 121      58.515  33.738  53.199  1.00 65.08           O  
ANISOU 3163  O   GLY B 121     8213  10459   6056   1619     42  -1375       O  
ATOM   3164  N   LYS B 122      59.051  32.889  55.225  1.00 66.58           N  
ANISOU 3164  N   LYS B 122     8339  11267   5692   1892     27  -1223       N  
ATOM   3165  CA  LYS B 122      59.906  33.988  55.654  1.00 70.79           C  
ANISOU 3165  CA  LYS B 122     8720  12071   6104   1833    -87  -1571       C  
ATOM   3166  C   LYS B 122      61.306  33.469  55.967  1.00 74.93           C  
ANISOU 3166  C   LYS B 122     9148  12910   6413   1974   -221  -1518       C  
ATOM   3167  O   LYS B 122      61.505  32.277  56.215  1.00 73.73           O  
ANISOU 3167  O   LYS B 122     9045  12842   6127   2157   -212  -1202       O  
ATOM   3168  CB  LYS B 122      59.317  34.651  56.901  1.00 76.66           C  
ANISOU 3168  CB  LYS B 122     9415  13094   6619   1835    -37  -1753       C  
ATOM   3169  CG  LYS B 122      57.906  35.163  56.706  1.00 79.17           C  
ANISOU 3169  CG  LYS B 122     9808  13133   7140   1718    103  -1808       C  
ATOM   3170  CD  LYS B 122      57.284  35.610  58.031  1.00 87.71           C  
ANISOU 3170  CD  LYS B 122    10847  14518   7961   1754    179  -1948       C  
ATOM   3171  CE  LYS B 122      55.859  36.109  57.822  1.00 88.92           C  
ANISOU 3171  CE  LYS B 122    11060  14390   8337   1649    326  -2001       C  
ATOM   3172  NZ  LYS B 122      55.194  36.452  59.098  1.00 97.85           N  
ANISOU 3172  NZ  LYS B 122    12152  15813   9214   1694    424  -2122       N  
ATOM   3173  N   THR B 123      62.280  34.380  55.972  1.00 78.62           N  
ANISOU 3173  N   THR B 123     9466  13550   6857   1891   -343  -1831       N  
ATOM   3174  CA  THR B 123      63.663  34.027  56.280  1.00 78.39           C  
ANISOU 3174  CA  THR B 123     9304  13854   6627   2013   -486  -1829       C  
ATOM   3175  C   THR B 123      64.358  35.249  56.869  1.00 82.69           C  
ANISOU 3175  C   THR B 123     9663  14708   7048   1907   -592  -2249       C  
ATOM   3176  O   THR B 123      64.051  36.397  56.519  1.00 78.17           O  
ANISOU 3176  O   THR B 123     9069  13953   6679   1702   -563  -2544       O  
ATOM   3177  CB  THR B 123      64.437  33.494  55.039  1.00 72.10           C  
ANISOU 3177  CB  THR B 123     8518  12814   6062   2012   -530  -1702       C  
ATOM   3178  OG1 THR B 123      65.725  32.983  55.425  1.00 71.15           O  
ANISOU 3178  OG1 THR B 123     8262  13037   5733   2172   -660  -1653       O  
ATOM   3179  CG2 THR B 123      64.638  34.583  53.995  1.00 66.85           C  
ANISOU 3179  CG2 THR B 123     7813  11884   5703   1774   -545  -1978       C  
ATOM   3180  N   SER B 124      65.286  34.985  57.786  1.00 84.81           N  
ANISOU 3180  N   SER B 124     9792  15448   6985   2053   -713  -2272       N  
ATOM   3181  CA  SER B 124      66.139  36.019  58.358  1.00 91.72           C  
ANISOU 3181  CA  SER B 124    10459  16668   7721   1962   -838  -2679       C  
ATOM   3182  C   SER B 124      67.426  36.209  57.565  1.00 90.64           C  
ANISOU 3182  C   SER B 124    10182  16514   7742   1894   -956  -2798       C  
ATOM   3183  O   SER B 124      68.205  37.122  57.870  1.00 89.24           O  
ANISOU 3183  O   SER B 124     9817  16576   7516   1780  -1058  -3162       O  
ATOM   3184  CB  SER B 124      66.477  35.670  59.809  1.00 97.95           C  
ANISOU 3184  CB  SER B 124    11146  18034   8035   2155   -923  -2662       C  
ATOM   3185  OG  SER B 124      66.732  34.278  59.934  1.00102.62           O  
ANISOU 3185  OG  SER B 124    11795  18726   8469   2409   -939  -2228       O  
ATOM   3186  N   LYS B 125      67.654  35.389  56.543  1.00 83.87           N  
ANISOU 3186  N   LYS B 125     9406  15377   7084   1950   -935  -2520       N  
ATOM   3187  CA  LYS B 125      68.921  35.380  55.837  1.00 81.46           C  
ANISOU 3187  CA  LYS B 125     8961  15095   6893   1925  -1037  -2586       C  
ATOM   3188  C   LYS B 125      68.913  36.248  54.590  1.00 83.70           C  
ANISOU 3188  C   LYS B 125     9264  14970   7567   1670   -983  -2773       C  
ATOM   3189  O   LYS B 125      69.965  36.419  53.971  1.00 84.25           O  
ANISOU 3189  O   LYS B 125     9205  15055   7752   1609  -1051  -2873       O  
ATOM   3190  CB  LYS B 125      69.290  33.943  55.476  1.00 81.16           C  
ANISOU 3190  CB  LYS B 125     8985  15022   6830   2155  -1043  -2184       C  
ATOM   3191  CG  LYS B 125      69.218  32.989  56.653  1.00 88.09           C  
ANISOU 3191  CG  LYS B 125     9872  16256   7343   2429  -1075  -1926       C  
ATOM   3192  CD  LYS B 125      69.597  31.587  56.247  1.00 94.50           C  
ANISOU 3192  CD  LYS B 125    10748  16981   8179   2657  -1067  -1529       C  
ATOM   3193  CE  LYS B 125      69.489  30.628  57.417  1.00104.81           C  
ANISOU 3193  CE  LYS B 125    12075  18617   9132   2939  -1084  -1229       C  
ATOM   3194  NZ  LYS B 125      69.497  29.214  56.941  1.00109.67           N  
ANISOU 3194  NZ  LYS B 125    12818  19004   9847   3146  -1017   -801       N  
ATOM   3195  N   GLY B 126      67.767  36.825  54.224  1.00 82.89           N  
ANISOU 3195  N   GLY B 126     9309  14521   7666   1522   -860  -2820       N  
ATOM   3196  CA  GLY B 126      67.708  37.689  53.061  1.00 72.60           C  
ANISOU 3196  CA  GLY B 126     8030  12834   6722   1291   -806  -2972       C  
ATOM   3197  C   GLY B 126      67.203  37.009  51.807  1.00 71.75           C  
ANISOU 3197  C   GLY B 126     8101  12304   6858   1295   -717  -2680       C  
ATOM   3198  O   GLY B 126      66.378  36.098  51.878  1.00 75.71           O  
ANISOU 3198  O   GLY B 126     8753  12701   7311   1426   -651  -2398       O  
ATOM   3199  N   PHE B 127      67.714  37.422  50.651  1.00 65.93           N  
ANISOU 3199  N   PHE B 127     7341  11333   6377   1149   -709  -2747       N  
ATOM   3200  CA  PHE B 127      67.303  36.853  49.378  1.00 62.83           C  
ANISOU 3200  CA  PHE B 127     7105  10560   6206   1136   -631  -2508       C  
ATOM   3201  C   PHE B 127      68.269  35.756  48.955  1.00 63.64           C  
ANISOU 3201  C   PHE B 127     7168  10755   6258   1284   -679  -2317       C  
ATOM   3202  O   PHE B 127      69.485  35.937  49.013  1.00 66.67           O  
ANISOU 3202  O   PHE B 127     7373  11367   6590   1281   -763  -2453       O  
ATOM   3203  CB  PHE B 127      67.228  37.956  48.330  1.00 58.89           C  
ANISOU 3203  CB  PHE B 127     6617   9751   6006    897   -581  -2672       C  
ATOM   3204  CG  PHE B 127      66.385  39.120  48.761  1.00 64.38           C  
ANISOU 3204  CG  PHE B 127     7330  10351   6782    759   -534  -2884       C  
ATOM   3205  CD1 PHE B 127      64.994  39.035  48.732  1.00 61.96           C  
ANISOU 3205  CD1 PHE B 127     7186   9815   6540    773   -447  -2756       C  
ATOM   3206  CD2 PHE B 127      66.974  40.286  49.225  1.00 59.83           C  
ANISOU 3206  CD2 PHE B 127     6596   9913   6223    619   -572  -3223       C  
ATOM   3207  CE1 PHE B 127      64.211  40.090  49.128  1.00 62.18           C  
ANISOU 3207  CE1 PHE B 127     7222   9750   6653    665   -396  -2951       C  
ATOM   3208  CE2 PHE B 127      66.191  41.354  49.630  1.00 63.11           C  
ANISOU 3208  CE2 PHE B 127     7029  10218   6731    500   -516  -3433       C  
ATOM   3209  CZ  PHE B 127      64.808  41.255  49.582  1.00 67.44           C  
ANISOU 3209  CZ  PHE B 127     7742  10537   7346    532   -427  -3292       C  
ATOM   3210  N   GLY B 128      67.720  34.622  48.533  1.00 58.75           N  
ANISOU 3210  N   GLY B 128     6705   9953   5664   1412   -620  -2015       N  
ATOM   3211  CA  GLY B 128      68.511  33.461  48.192  1.00 56.93           C  
ANISOU 3211  CA  GLY B 128     6457   9780   5394   1582   -646  -1815       C  
ATOM   3212  C   GLY B 128      67.864  32.183  48.685  1.00 63.81           C  
ANISOU 3212  C   GLY B 128     7459  10640   6145   1795   -602  -1507       C  
ATOM   3213  O   GLY B 128      66.637  32.119  48.846  1.00 61.04           O  
ANISOU 3213  O   GLY B 128     7254  10115   5824   1769   -522  -1416       O  
ATOM   3214  N   PHE B 129      68.682  31.166  48.942  1.00 58.02           N  
ANISOU 3214  N   PHE B 129     6668  10089   5288   2007   -649  -1341       N  
ATOM   3215  CA  PHE B 129      68.192  29.867  49.383  1.00 67.20           C  
ANISOU 3215  CA  PHE B 129     7952  11223   6358   2224   -597  -1020       C  
ATOM   3216  C   PHE B 129      69.350  29.125  50.033  1.00 70.13           C  
ANISOU 3216  C   PHE B 129     8184  11934   6529   2468   -690   -912       C  
ATOM   3217  O   PHE B 129      70.520  29.497  49.870  1.00 66.71           O  
ANISOU 3217  O   PHE B 129     7568  11699   6079   2458   -786  -1077       O  
ATOM   3218  CB  PHE B 129      67.597  29.051  48.215  1.00 56.55           C  
ANISOU 3218  CB  PHE B 129     6783   9448   5254   2208   -484   -830       C  
ATOM   3219  CG  PHE B 129      66.633  27.969  48.654  1.00 56.81           C  
ANISOU 3219  CG  PHE B 129     6978   9352   5254   2347   -390   -536       C  
ATOM   3220  CD1 PHE B 129      65.498  28.284  49.386  1.00 66.29           C  
ANISOU 3220  CD1 PHE B 129     8255  10554   6378   2298   -337   -518       C  
ATOM   3221  CD2 PHE B 129      66.861  26.641  48.345  1.00 63.16           C  
ANISOU 3221  CD2 PHE B 129     7854  10027   6118   2524   -341   -282       C  
ATOM   3222  CE1 PHE B 129      64.611  27.283  49.809  1.00 66.96           C  
ANISOU 3222  CE1 PHE B 129     8480  10523   6441   2414   -234   -239       C  
ATOM   3223  CE2 PHE B 129      65.974  25.638  48.766  1.00 68.26           C  
ANISOU 3223  CE2 PHE B 129     8647  10531   6757   2639   -238     -5       C  
ATOM   3224  CZ  PHE B 129      64.848  25.964  49.502  1.00 57.80           C  
ANISOU 3224  CZ  PHE B 129     7393   9220   5350   2579   -184     21       C  
ATOM   3225  N   GLU B 130      69.007  28.070  50.781  1.00 68.68           N  
ANISOU 3225  N   GLU B 130     8079  11816   6198   2690   -657   -622       N  
ATOM   3226  CA  GLU B 130      70.030  27.306  51.493  1.00 71.93           C  
ANISOU 3226  CA  GLU B 130     8365  12563   6403   2959   -747   -471       C  
ATOM   3227  C   GLU B 130      70.982  26.582  50.540  1.00 75.57           C  
ANISOU 3227  C   GLU B 130     8781  12897   7034   3055   -752   -393       C  
ATOM   3228  O   GLU B 130      72.174  26.448  50.842  1.00 75.64           O  
ANISOU 3228  O   GLU B 130     8600  13216   6923   3201   -865   -419       O  
ATOM   3229  CB  GLU B 130      69.379  26.310  52.454  1.00 86.41           C  
ANISOU 3229  CB  GLU B 130    10316  14454   8060   3178   -687   -136       C  
ATOM   3230  CG  GLU B 130      68.648  26.995  53.602  1.00113.79           C  
ANISOU 3230  CG  GLU B 130    13784  18164  11286   3126   -695   -219       C  
ATOM   3231  CD  GLU B 130      67.931  26.033  54.532  1.00134.74           C  
ANISOU 3231  CD  GLU B 130    16563  20869  13763   3326   -611    129       C  
ATOM   3232  OE1 GLU B 130      67.834  24.832  54.191  1.00142.70           O  
ANISOU 3232  OE1 GLU B 130    17687  21639  14892   3478   -525    443       O  
ATOM   3233  OE2 GLU B 130      67.461  26.490  55.602  1.00138.24           O  
ANISOU 3233  OE2 GLU B 130    16988  21585  13952   3325   -620     83       O  
ATOM   3234  N   VAL B 131      70.493  26.127  49.386  1.00 72.78           N  
ANISOU 3234  N   VAL B 131     8586  12113   6955   2978   -635   -314       N  
ATOM   3235  CA  VAL B 131      71.337  25.470  48.396  1.00 69.47           C  
ANISOU 3235  CA  VAL B 131     8134  11553   6710   3053   -620   -271       C  
ATOM   3236  C   VAL B 131      71.019  26.049  47.026  1.00 72.17           C  
ANISOU 3236  C   VAL B 131     8549  11562   7310   2791   -552   -451       C  
ATOM   3237  O   VAL B 131      69.921  26.567  46.786  1.00 58.18           O  
ANISOU 3237  O   VAL B 131     6910   9577   5619   2603   -490   -506       O  
ATOM   3238  CB  VAL B 131      71.154  23.930  48.369  1.00 68.17           C  
ANISOU 3238  CB  VAL B 131     8102  11192   6609   3297   -528     76       C  
ATOM   3239  CG1 VAL B 131      71.604  23.309  49.685  1.00 68.83           C  
ANISOU 3239  CG1 VAL B 131     8103  11620   6430   3589   -598    295       C  
ATOM   3240  CG2 VAL B 131      69.696  23.553  48.052  1.00 69.06           C  
ANISOU 3240  CG2 VAL B 131     8461  10912   6869   3195   -382    208       C  
ATOM   3241  N   ASP B 132      72.005  25.980  46.132  1.00 66.57           N  
ANISOU 3241  N   ASP B 132     7741  10832   6721   2786   -565   -542       N  
ATOM   3242  CA  ASP B 132      71.749  26.211  44.718  1.00 65.68           C  
ANISOU 3242  CA  ASP B 132     7720  10388   6847   2588   -481   -644       C  
ATOM   3243  C   ASP B 132      70.875  25.094  44.189  1.00 65.92           C  
ANISOU 3243  C   ASP B 132     7969  10056   7023   2652   -358   -426       C  
ATOM   3244  O   ASP B 132      70.973  23.947  44.638  1.00 58.42           O  
ANISOU 3244  O   ASP B 132     7056   9098   6041   2888   -329   -197       O  
ATOM   3245  CB  ASP B 132      73.052  26.259  43.921  1.00 65.13           C  
ANISOU 3245  CB  ASP B 132     7489  10400   6855   2594   -505   -769       C  
ATOM   3246  CG  ASP B 132      73.894  27.484  44.248  1.00 76.44           C  
ANISOU 3246  CG  ASP B 132     8698  12149   8197   2468   -612  -1028       C  
ATOM   3247  OD1 ASP B 132      73.409  28.369  44.994  1.00 72.44           O  
ANISOU 3247  OD1 ASP B 132     8176  11762   7584   2355   -663  -1137       O  
ATOM   3248  OD2 ASP B 132      75.056  27.544  43.782  1.00 81.48           O  
ANISOU 3248  OD2 ASP B 132     9165  12920   8876   2485   -640  -1132       O  
ATOM   3249  N   ASN B 133      69.988  25.441  43.258  1.00 56.12           N  
ANISOU 3249  N   ASN B 133     6867   8514   5941   2439   -284   -495       N  
ATOM   3250  CA  ASN B 133      69.170  24.427  42.605  1.00 62.00           C  
ANISOU 3250  CA  ASN B 133     7805   8908   6846   2463   -169   -337       C  
ATOM   3251  C   ASN B 133      69.120  24.727  41.113  1.00 59.41           C  
ANISOU 3251  C   ASN B 133     7527   8353   6695   2273   -120   -481       C  
ATOM   3252  O   ASN B 133      70.055  25.329  40.577  1.00 55.02           O  
ANISOU 3252  O   ASN B 133     6843   7918   6143   2206   -159   -643       O  
ATOM   3253  CB  ASN B 133      67.769  24.333  43.236  1.00 58.07           C  
ANISOU 3253  CB  ASN B 133     7453   8282   6327   2425   -121   -213       C  
ATOM   3254  CG  ASN B 133      67.090  25.694  43.431  1.00 61.66           C  
ANISOU 3254  CG  ASN B 133     7896   8793   6739   2206   -161   -383       C  
ATOM   3255  OD1 ASN B 133      67.444  26.693  42.792  1.00 58.72           O  
ANISOU 3255  OD1 ASN B 133     7454   8447   6412   2038   -201   -589       O  
ATOM   3256  ND2 ASN B 133      66.072  25.720  44.301  1.00 56.27           N  
ANISOU 3256  ND2 ASN B 133     7286   8110   5983   2209   -135   -290       N  
ATOM   3257  N   THR B 134      68.050  24.342  40.426  1.00 59.86           N  
ANISOU 3257  N   THR B 134     7758   8098   6889   2178    -36   -430       N  
ATOM   3258  CA  THR B 134      68.020  24.508  38.978  1.00 60.48           C  
ANISOU 3258  CA  THR B 134     7887   7985   7108   2020      7   -552       C  
ATOM   3259  C   THR B 134      66.657  25.007  38.510  1.00 64.46           C  
ANISOU 3259  C   THR B 134     8524   8279   7689   1815     33   -581       C  
ATOM   3260  O   THR B 134      65.617  24.728  39.119  1.00 59.87           O  
ANISOU 3260  O   THR B 134     8034   7602   7111   1825     59   -468       O  
ATOM   3261  CB  THR B 134      68.359  23.202  38.251  1.00 60.83           C  
ANISOU 3261  CB  THR B 134     7992   7849   7271   2148     91   -479       C  
ATOM   3262  OG1 THR B 134      67.515  22.161  38.747  1.00 62.31           O  
ANISOU 3262  OG1 THR B 134     8310   7853   7513   2255    156   -289       O  
ATOM   3263  CG2 THR B 134      69.855  22.802  38.441  1.00 52.62           C  
ANISOU 3263  CG2 THR B 134     6794   7017   6183   2346     67   -481       C  
ATOM   3264  N   ILE B 135      66.678  25.755  37.417  1.00 59.70           N  
ANISOU 3264  N   ILE B 135     7922   7615   7146   1632     30   -724       N  
ATOM   3265  CA  ILE B 135      65.466  26.207  36.753  1.00 51.78           C  
ANISOU 3265  CA  ILE B 135     7035   6415   6225   1447     48   -752       C  
ATOM   3266  C   ILE B 135      65.467  25.514  35.394  1.00 58.95           C  
ANISOU 3266  C   ILE B 135     8025   7138   7236   1408    109   -777       C  
ATOM   3267  O   ILE B 135      66.229  25.874  34.482  1.00 57.49           O  
ANISOU 3267  O   ILE B 135     7790   7001   7053   1344    111   -885       O  
ATOM   3268  CB  ILE B 135      65.415  27.737  36.646  1.00 55.71           C  
ANISOU 3268  CB  ILE B 135     7469   7002   6696   1269     -8   -882       C  
ATOM   3269  CG1 ILE B 135      64.181  28.203  35.864  1.00 49.34           C  
ANISOU 3269  CG1 ILE B 135     6773   5994   5980   1097      4   -894       C  
ATOM   3270  CG2 ILE B 135      66.733  28.296  36.127  1.00 52.73           C  
ANISOU 3270  CG2 ILE B 135     6965   6776   6294   1234    -27  -1006       C  
ATOM   3271  CD1 ILE B 135      62.877  27.738  36.486  1.00 44.05           C  
ANISOU 3271  CD1 ILE B 135     6196   5200   5341   1121     25   -784       C  
ATOM   3272  N   GLY B 136      64.643  24.481  35.261  1.00 59.03           N  
ANISOU 3272  N   GLY B 136     8155   6941   7332   1447    167   -686       N  
ATOM   3273  CA  GLY B 136      64.868  23.551  34.167  1.00 57.80           C  
ANISOU 3273  CA  GLY B 136     8062   6634   7266   1463    234   -721       C  
ATOM   3274  C   GLY B 136      66.152  22.798  34.445  1.00 62.04           C  
ANISOU 3274  C   GLY B 136     8519   7267   7787   1666    263   -695       C  
ATOM   3275  O   GLY B 136      66.339  22.248  35.536  1.00 66.63           O  
ANISOU 3275  O   GLY B 136     9075   7899   8342   1840    266   -563       O  
ATOM   3276  N   SER B 137      67.058  22.777  33.467  1.00 61.99           N  
ANISOU 3276  N   SER B 137     8464   7301   7788   1655    287   -811       N  
ATOM   3277  CA  SER B 137      68.402  22.244  33.680  1.00 64.42           C  
ANISOU 3277  CA  SER B 137     8659   7740   8079   1846    307   -808       C  
ATOM   3278  C   SER B 137      69.413  23.323  34.029  1.00 60.53           C  
ANISOU 3278  C   SER B 137     7991   7536   7472   1827    233   -883       C  
ATOM   3279  O   SER B 137      70.575  23.002  34.292  1.00 56.61           O  
ANISOU 3279  O   SER B 137     7365   7194   6949   1985    233   -887       O  
ATOM   3280  CB  SER B 137      68.927  21.536  32.420  1.00 60.17           C  
ANISOU 3280  CB  SER B 137     8145   7097   7621   1860    394   -912       C  
ATOM   3281  OG  SER B 137      67.949  20.747  31.806  1.00 63.78           O  
ANISOU 3281  OG  SER B 137     8759   7287   8187   1808    458   -912       O  
ATOM   3282  N   THR B 138      69.032  24.569  33.970  1.00 54.97           N  
ANISOU 3282  N   THR B 138     7272   6899   6717   1638    178   -951       N  
ATOM   3283  CA  THR B 138      70.047  25.581  34.184  1.00 53.57           C  
ANISOU 3283  CA  THR B 138     6922   6970   6461   1596    124  -1049       C  
ATOM   3284  C   THR B 138      70.294  25.744  35.677  1.00 63.93           C  
ANISOU 3284  C   THR B 138     8133   8476   7680   1720     47   -987       C  
ATOM   3285  O   THR B 138      69.339  25.795  36.458  1.00 64.56           O  
ANISOU 3285  O   THR B 138     8291   8505   7736   1719     21   -902       O  
ATOM   3286  CB  THR B 138      69.612  26.913  33.593  1.00 52.60           C  
ANISOU 3286  CB  THR B 138     6815   6834   6337   1350    103  -1144       C  
ATOM   3287  OG1 THR B 138      69.067  26.700  32.288  1.00 60.30           O  
ANISOU 3287  OG1 THR B 138     7916   7623   7371   1240    163  -1166       O  
ATOM   3288  CG2 THR B 138      70.797  27.875  33.503  1.00 49.69           C  
ANISOU 3288  CG2 THR B 138     6267   6684   5927   1280     82  -1267       C  
ATOM   3289  N   PRO B 139      71.552  25.824  36.098  1.00 64.30           N  
ANISOU 3289  N   PRO B 139     7998   8768   7665   1827     10  -1034       N  
ATOM   3290  CA  PRO B 139      71.828  26.138  37.504  1.00 54.03           C  
ANISOU 3290  CA  PRO B 139     6580   7708   6242   1925    -83  -1005       C  
ATOM   3291  C   PRO B 139      71.170  27.457  37.889  1.00 59.02           C  
ANISOU 3291  C   PRO B 139     7214   8377   6833   1725   -136  -1094       C  
ATOM   3292  O   PRO B 139      71.077  28.388  37.083  1.00 59.60           O  
ANISOU 3292  O   PRO B 139     7293   8386   6966   1517   -119  -1213       O  
ATOM   3293  CB  PRO B 139      73.356  26.236  37.551  1.00 52.72           C  
ANISOU 3293  CB  PRO B 139     6190   7808   6034   2012   -117  -1098       C  
ATOM   3294  CG  PRO B 139      73.833  25.432  36.358  1.00 57.02           C  
ANISOU 3294  CG  PRO B 139     6762   8214   6687   2061    -19  -1105       C  
ATOM   3295  CD  PRO B 139      72.787  25.678  35.304  1.00 58.50           C  
ANISOU 3295  CD  PRO B 139     7140   8129   6960   1858     49  -1130       C  
ATOM   3296  N   GLN B 140      70.688  27.519  39.126  1.00 51.47           N  
ANISOU 3296  N   GLN B 140     6260   7520   5777   1797   -191  -1028       N  
ATOM   3297  CA  GLN B 140      70.098  28.729  39.690  1.00 50.56           C  
ANISOU 3297  CA  GLN B 140     6132   7461   5617   1639   -240  -1126       C  
ATOM   3298  C   GLN B 140      70.906  29.068  40.935  1.00 54.02           C  
ANISOU 3298  C   GLN B 140     6385   8244   5895   1736   -335  -1190       C  
ATOM   3299  O   GLN B 140      70.898  28.303  41.905  1.00 63.23           O  
ANISOU 3299  O   GLN B 140     7546   9535   6944   1937   -364  -1054       O  
ATOM   3300  CB  GLN B 140      68.607  28.528  39.998  1.00 48.36           C  
ANISOU 3300  CB  GLN B 140     6031   6985   5357   1616   -206  -1010       C  
ATOM   3301  CG  GLN B 140      67.943  29.753  40.585  1.00 62.45           C  
ANISOU 3301  CG  GLN B 140     7803   8815   7109   1468   -244  -1117       C  
ATOM   3302  CD  GLN B 140      66.421  29.717  40.510  1.00 57.56           C  
ANISOU 3302  CD  GLN B 140     7354   7958   6559   1397   -194  -1031       C  
ATOM   3303  OE1 GLN B 140      65.813  30.329  39.626  1.00 54.04           O  
ANISOU 3303  OE1 GLN B 140     6977   7324   6233   1228   -168  -1085       O  
ATOM   3304  NE2 GLN B 140      65.801  29.009  41.449  1.00 53.79           N  
ANISOU 3304  NE2 GLN B 140     6933   7500   6003   1530   -180   -888       N  
ATOM   3305  N   ILE B 141      71.646  30.179  40.883  1.00 58.21           N  
ANISOU 3305  N   ILE B 141     6759   8937   6423   1596   -382  -1394       N  
ATOM   3306  CA  ILE B 141      72.560  30.565  41.963  1.00 61.37           C  
ANISOU 3306  CA  ILE B 141     6946   9696   6673   1665   -484  -1505       C  
ATOM   3307  C   ILE B 141      71.778  31.258  43.075  1.00 66.45           C  
ANISOU 3307  C   ILE B 141     7609  10429   7210   1615   -532  -1561       C  
ATOM   3308  O   ILE B 141      71.060  32.235  42.827  1.00 69.81           O  
ANISOU 3308  O   ILE B 141     8100  10701   7724   1414   -502  -1669       O  
ATOM   3309  CB  ILE B 141      73.676  31.485  41.439  1.00 65.91           C  
ANISOU 3309  CB  ILE B 141     7331  10399   7311   1510   -502  -1724       C  
ATOM   3310  CG1 ILE B 141      74.358  30.912  40.190  1.00 70.53           C  
ANISOU 3310  CG1 ILE B 141     7909  10876   8014   1527   -429  -1686       C  
ATOM   3311  CG2 ILE B 141      74.713  31.687  42.506  1.00 60.60           C  
ANISOU 3311  CG2 ILE B 141     6417  10123   6485   1603   -617  -1840       C  
ATOM   3312  CD1 ILE B 141      74.850  29.497  40.338  1.00 66.59           C  
ANISOU 3312  CD1 ILE B 141     7395  10445   7461   1805   -430  -1518       C  
ATOM   3313  N   ASN B 142      71.948  30.778  44.315  1.00 67.22           N  
ANISOU 3313  N   ASN B 142     7640  10792   7110   1808   -603  -1490       N  
ATOM   3314  CA  ASN B 142      71.094  31.170  45.433  1.00 60.83           C  
ANISOU 3314  CA  ASN B 142     6873  10074   6166   1804   -630  -1503       C  
ATOM   3315  C   ASN B 142      71.870  31.705  46.638  1.00 68.55           C  
ANISOU 3315  C   ASN B 142     7638  11475   6931   1852   -751  -1666       C  
ATOM   3316  O   ASN B 142      71.349  31.689  47.766  1.00 63.42           O  
ANISOU 3316  O   ASN B 142     7006  10993   6097   1933   -784  -1633       O  
ATOM   3317  CB  ASN B 142      70.224  29.986  45.863  1.00 64.35           C  
ANISOU 3317  CB  ASN B 142     7487  10415   6547   1993   -579  -1218       C  
ATOM   3318  CG  ASN B 142      69.132  29.674  44.868  1.00 60.71           C  
ANISOU 3318  CG  ASN B 142     7240   9543   6284   1898   -465  -1107       C  
ATOM   3319  OD1 ASN B 142      68.662  30.558  44.147  1.00 59.24           O  
ANISOU 3319  OD1 ASN B 142     7100   9170   6239   1684   -433  -1239       O  
ATOM   3320  ND2 ASN B 142      68.718  28.412  44.823  1.00 60.65           N  
ANISOU 3320  ND2 ASN B 142     7359   9392   6293   2059   -403   -860       N  
ATOM   3321  N   THR B 143      73.085  32.203  46.430  1.00 71.65           N  
ANISOU 3321  N   THR B 143     7823  12061   7339   1794   -816  -1855       N  
ATOM   3322  CA  THR B 143      73.870  32.734  47.536  1.00 71.90           C  
ANISOU 3322  CA  THR B 143     7629  12519   7172   1823   -944  -2045       C  
ATOM   3323  C   THR B 143      73.168  33.932  48.182  1.00 70.37           C  
ANISOU 3323  C   THR B 143     7443  12352   6943   1638   -952  -2267       C  
ATOM   3324  O   THR B 143      72.684  34.842  47.495  1.00 68.03           O  
ANISOU 3324  O   THR B 143     7216  11783   6849   1405   -880  -2401       O  
ATOM   3325  CB  THR B 143      75.270  33.093  47.041  1.00 78.24           C  
ANISOU 3325  CB  THR B 143     8197  13485   8045   1758   -996  -2224       C  
ATOM   3326  OG1 THR B 143      75.176  34.148  46.085  1.00 83.78           O  
ANISOU 3326  OG1 THR B 143     8917  13937   8980   1472   -921  -2410       O  
ATOM   3327  CG2 THR B 143      75.893  31.879  46.351  1.00 72.83           C  
ANISOU 3327  CG2 THR B 143     7513  12745   7412   1952   -969  -2006       C  
ATOM   3328  N   TRP B 144      73.098  33.905  49.514  1.00 65.40           N  
ANISOU 3328  N   TRP B 144     6745  12054   6051   1757  -1036  -2297       N  
ATOM   3329  CA  TRP B 144      72.334  34.884  50.278  1.00 67.98           C  
ANISOU 3329  CA  TRP B 144     7092  12427   6311   1623  -1034  -2495       C  
ATOM   3330  C   TRP B 144      72.825  36.301  50.015  1.00 73.41           C  
ANISOU 3330  C   TRP B 144     7632  13114   7145   1352  -1051  -2865       C  
ATOM   3331  O   TRP B 144      74.026  36.552  49.910  1.00 70.76           O  
ANISOU 3331  O   TRP B 144     7083  12987   6814   1314  -1128  -3025       O  
ATOM   3332  CB  TRP B 144      72.427  34.560  51.770  1.00 66.80           C  
ANISOU 3332  CB  TRP B 144     6854  12718   5808   1814  -1134  -2480       C  
ATOM   3333  CG  TRP B 144      71.754  33.254  52.133  1.00 74.79           C  
ANISOU 3333  CG  TRP B 144     8036  13695   6684   2065  -1088  -2099       C  
ATOM   3334  CD1 TRP B 144      72.368  32.087  52.486  1.00 72.42           C  
ANISOU 3334  CD1 TRP B 144     7690  13607   6218   2337  -1146  -1847       C  
ATOM   3335  CD2 TRP B 144      70.337  32.992  52.192  1.00 71.29           C  
ANISOU 3335  CD2 TRP B 144     7827  12983   6278   2064   -966  -1924       C  
ATOM   3336  NE1 TRP B 144      71.426  31.111  52.743  1.00 76.55           N  
ANISOU 3336  NE1 TRP B 144     8416  13984   6684   2497  -1058  -1519       N  
ATOM   3337  CE2 TRP B 144      70.175  31.641  52.568  1.00 70.05           C  
ANISOU 3337  CE2 TRP B 144     7760  12875   5981   2327   -947  -1567       C  
ATOM   3338  CE3 TRP B 144      69.195  33.764  51.943  1.00 66.96           C  
ANISOU 3338  CE3 TRP B 144     7410  12148   5882   1871   -867  -2030       C  
ATOM   3339  CZ2 TRP B 144      68.923  31.050  52.717  1.00 66.39           C  
ANISOU 3339  CZ2 TRP B 144     7509  12191   5526   2381   -827  -1326       C  
ATOM   3340  CZ3 TRP B 144      67.946  33.176  52.088  1.00 62.80           C  
ANISOU 3340  CZ3 TRP B 144     7084  11423   5355   1936   -759  -1795       C  
ATOM   3341  CH2 TRP B 144      67.819  31.832  52.478  1.00 63.34           C  
ANISOU 3341  CH2 TRP B 144     7234  11552   5282   2179   -737  -1452       C  
ATOM   3342  N   SER B 145      71.874  37.216  49.827  1.00 78.58           N  
ANISOU 3342  N   SER B 145     8402  13501   7953   1159   -967  -2990       N  
ATOM   3343  CA  SER B 145      72.159  38.634  49.650  1.00 84.25           C  
ANISOU 3343  CA  SER B 145     9008  14164   8840    894   -959  -3336       C  
ATOM   3344  C   SER B 145      71.073  39.441  50.354  1.00 82.32           C  
ANISOU 3344  C   SER B 145     8846  13853   8580    806   -915  -3488       C  
ATOM   3345  O   SER B 145      69.941  38.977  50.514  1.00 77.90           O  
ANISOU 3345  O   SER B 145     8472  13148   7979    899   -851  -3290       O  
ATOM   3346  CB  SER B 145      72.256  39.011  48.165  1.00 85.34           C  
ANISOU 3346  CB  SER B 145     9210  13913   9303    717   -863  -3308       C  
ATOM   3347  OG  SER B 145      72.447  40.406  48.008  1.00 91.01           O  
ANISOU 3347  OG  SER B 145     9836  14536  10207    458   -835  -3617       O  
ATOM   3348  N   SER B 146      71.416  40.677  50.738  1.00 76.84           N  
ANISOU 3348  N   SER B 146     8006  13249   7943    614   -938  -3855       N  
ATOM   3349  CA  SER B 146      70.527  41.531  51.520  1.00 77.66           C  
ANISOU 3349  CA  SER B 146     8149  13333   8025    531   -900  -4065       C  
ATOM   3350  C   SER B 146      69.794  42.592  50.701  1.00 76.89           C  
ANISOU 3350  C   SER B 146     8164  12773   8278    309   -772  -4162       C  
ATOM   3351  O   SER B 146      68.867  43.219  51.225  1.00 79.89           O  
ANISOU 3351  O   SER B 146     8611  13065   8680    261   -716  -4290       O  
ATOM   3352  CB  SER B 146      71.321  42.241  52.625  1.00 86.80           C  
ANISOU 3352  CB  SER B 146     9066  14907   9005    469  -1007  -4449       C  
ATOM   3353  OG  SER B 146      72.065  43.335  52.097  1.00 88.78           O  
ANISOU 3353  OG  SER B 146     9175  15044   9513    217   -996  -4746       O  
ATOM   3354  N   ASP B 147      70.184  42.820  49.449  1.00 75.53           N  
ANISOU 3354  N   ASP B 147     8009  12315   8375    181   -721  -4100       N  
ATOM   3355  CA  ASP B 147      69.513  43.770  48.572  1.00 75.67           C  
ANISOU 3355  CA  ASP B 147     8140  11886   8724     -9   -601  -4136       C  
ATOM   3356  C   ASP B 147      68.908  43.031  47.379  1.00 76.51           C  
ANISOU 3356  C   ASP B 147     8446  11673   8951     54   -532  -3770       C  
ATOM   3357  O   ASP B 147      69.610  42.276  46.693  1.00 71.06           O  
ANISOU 3357  O   ASP B 147     7739  11017   8243    111   -555  -3601       O  
ATOM   3358  CB  ASP B 147      70.487  44.848  48.101  1.00 82.61           C  
ANISOU 3358  CB  ASP B 147     8862  12698   9830   -247   -585  -4399       C  
ATOM   3359  CG  ASP B 147      69.834  45.861  47.182  1.00 98.25           C  
ANISOU 3359  CG  ASP B 147    10960  14207  12162   -435   -454  -4408       C  
ATOM   3360  OD1 ASP B 147      68.621  46.126  47.339  1.00105.50           O  
ANISOU 3360  OD1 ASP B 147    12026  14920  13141   -411   -392  -4365       O  
ATOM   3361  OD2 ASP B 147      70.536  46.399  46.304  1.00105.52           O  
ANISOU 3361  OD2 ASP B 147    11820  14969  13301   -601   -408  -4449       O  
ATOM   3362  N   TRP B 148      67.608  43.257  47.123  1.00 70.49           N  
ANISOU 3362  N   TRP B 148     7576  11088   8121   -264    -54  -3004       N  
ATOM   3363  CA  TRP B 148      66.934  42.524  46.052  1.00 61.23           C  
ANISOU 3363  CA  TRP B 148     6502   9705   7058    -91    -17  -2714       C  
ATOM   3364  C   TRP B 148      67.427  42.969  44.682  1.00 64.46           C  
ANISOU 3364  C   TRP B 148     6872   9928   7691   -171     32  -2635       C  
ATOM   3365  O   TRP B 148      67.682  42.129  43.816  1.00 69.80           O  
ANISOU 3365  O   TRP B 148     7537  10620   8365    -46     -4  -2420       O  
ATOM   3366  CB  TRP B 148      65.412  42.676  46.153  1.00 60.76           C  
ANISOU 3366  CB  TRP B 148     6621   9376   7089    -20     92  -2667       C  
ATOM   3367  CG  TRP B 148      64.694  42.088  44.959  1.00 56.99           C  
ANISOU 3367  CG  TRP B 148     6236   8670   6749    116    127  -2395       C  
ATOM   3368  CD1 TRP B 148      63.994  42.765  43.995  1.00 55.31           C  
ANISOU 3368  CD1 TRP B 148     6102   8129   6783     82    232  -2329       C  
ATOM   3369  CD2 TRP B 148      64.664  40.702  44.581  1.00 53.69           C  
ANISOU 3369  CD2 TRP B 148     5836   8346   6220    302     52  -2159       C  
ATOM   3370  NE1 TRP B 148      63.507  41.881  43.059  1.00 52.59           N  
ANISOU 3370  NE1 TRP B 148     5820   7693   6469    226    212  -2077       N  
ATOM   3371  CE2 TRP B 148      63.916  40.611  43.388  1.00 55.93           C  
ANISOU 3371  CE2 TRP B 148     6212   8357   6683    354    109  -1980       C  
ATOM   3372  CE3 TRP B 148      65.196  39.525  45.144  1.00 53.04           C  
ANISOU 3372  CE3 TRP B 148     5703   8548   5903    434    -53  -2079       C  
ATOM   3373  CZ2 TRP B 148      63.679  39.389  42.747  1.00 54.17           C  
ANISOU 3373  CZ2 TRP B 148     6042   8130   6411    511     64  -1754       C  
ATOM   3374  CZ3 TRP B 148      64.975  38.321  44.508  1.00 49.91           C  
ANISOU 3374  CZ3 TRP B 148     5364   8121   5477    603    -81  -1841       C  
ATOM   3375  CH2 TRP B 148      64.217  38.259  43.315  1.00 53.75           C  
ANISOU 3375  CH2 TRP B 148     5952   8325   6146    630    -22  -1694       C  
ATOM   3376  N   ILE B 149      67.561  44.283  44.462  1.00 71.13           N  
ANISOU 3376  N   ILE B 149     7709  10586   8732   -375    127  -2804       N  
ATOM   3377  CA  ILE B 149      68.090  44.783  43.191  1.00 70.39           C  
ANISOU 3377  CA  ILE B 149     7575  10323   8849   -464    188  -2726       C  
ATOM   3378  C   ILE B 149      69.483  44.224  42.927  1.00 73.46           C  
ANISOU 3378  C   ILE B 149     7778  11000   9133   -473     86  -2687       C  
ATOM   3379  O   ILE B 149      69.842  43.931  41.779  1.00 76.37           O  
ANISOU 3379  O   ILE B 149     8127  11304   9587   -424    107  -2508       O  
ATOM   3380  CB  ILE B 149      68.071  46.323  43.182  1.00 72.77           C  
ANISOU 3380  CB  ILE B 149     7894  10382   9372   -696    320  -2933       C  
ATOM   3381  CG1 ILE B 149      66.629  46.810  43.257  1.00 74.85           C  
ANISOU 3381  CG1 ILE B 149     8342  10333   9765   -640    440  -2919       C  
ATOM   3382  CG2 ILE B 149      68.757  46.875  41.941  1.00 65.77           C  
ANISOU 3382  CG2 ILE B 149     6951   9348   8691   -804    391  -2853       C  
ATOM   3383  CD1 ILE B 149      66.492  48.306  43.263  1.00 79.31           C  
ANISOU 3383  CD1 ILE B 149     8953  10616  10566   -837    594  -3108       C  
ATOM   3384  N   GLU B 150      70.277  44.038  43.979  1.00 70.92           N  
ANISOU 3384  N   GLU B 150     7314  11018   8616   -522    -25  -2846       N  
ATOM   3385  CA  GLU B 150      71.593  43.439  43.810  1.00 74.28           C  
ANISOU 3385  CA  GLU B 150     7537  11754   8932   -504   -129  -2795       C  
ATOM   3386  C   GLU B 150      71.464  41.966  43.460  1.00 70.01           C  
ANISOU 3386  C   GLU B 150     7033  11313   8253   -225   -193  -2523       C  
ATOM   3387  O   GLU B 150      72.145  41.466  42.557  1.00 72.37           O  
ANISOU 3387  O   GLU B 150     7258  11658   8583   -155   -198  -2368       O  
ATOM   3388  CB  GLU B 150      72.404  43.586  45.096  1.00 89.79           C  
ANISOU 3388  CB  GLU B 150     9331  14087  10700   -615   -250  -3026       C  
ATOM   3389  CG  GLU B 150      73.910  43.482  44.929  1.00105.20           C  
ANISOU 3389  CG  GLU B 150    11019  16345  12609   -694   -337  -3050       C  
ATOM   3390  CD  GLU B 150      74.664  44.075  46.117  1.00118.85           C  
ANISOU 3390  CD  GLU B 150    12571  18385  14203   -899   -440  -3347       C  
ATOM   3391  OE1 GLU B 150      74.404  45.248  46.478  1.00117.41           O  
ANISOU 3391  OE1 GLU B 150    12439  18039  14132  -1135   -368  -3600       O  
ATOM   3392  OE2 GLU B 150      75.529  43.363  46.678  1.00125.75           O  
ANISOU 3392  OE2 GLU B 150    13254  19670  14857   -821   -592  -3326       O  
ATOM   3393  N   PHE B 151      70.610  41.249  44.189  1.00 66.30           N  
ANISOU 3393  N   PHE B 151     6682  10879   7632    -65   -231  -2467       N  
ATOM   3394  CA  PHE B 151      70.459  39.820  43.954  1.00 61.46           C  
ANISOU 3394  CA  PHE B 151     6117  10344   6891    192   -281  -2219       C  
ATOM   3395  C   PHE B 151      69.933  39.540  42.549  1.00 61.06           C  
ANISOU 3395  C   PHE B 151     6194   9995   7009    272   -195  -2017       C  
ATOM   3396  O   PHE B 151      70.483  38.706  41.822  1.00 65.35           O  
ANISOU 3396  O   PHE B 151     6703  10601   7525    398   -214  -1852       O  
ATOM   3397  CB  PHE B 151      69.538  39.207  45.012  1.00 56.99           C  
ANISOU 3397  CB  PHE B 151     5666   9833   6153    323   -312  -2199       C  
ATOM   3398  CG  PHE B 151      69.369  37.721  44.864  1.00 61.80           C  
ANISOU 3398  CG  PHE B 151     6336  10505   6638    578   -351  -1950       C  
ATOM   3399  CD1 PHE B 151      70.261  36.846  45.488  1.00 58.83           C  
ANISOU 3399  CD1 PHE B 151     5834  10473   6046    709   -458  -1891       C  
ATOM   3400  CD2 PHE B 151      68.341  37.192  44.082  1.00 53.09           C  
ANISOU 3400  CD2 PHE B 151     5412   9119   5639    686   -281  -1773       C  
ATOM   3401  CE1 PHE B 151      70.122  35.464  45.354  1.00 53.64           C  
ANISOU 3401  CE1 PHE B 151     5247   9844   5290    952   -474  -1655       C  
ATOM   3402  CE2 PHE B 151      68.206  35.809  43.933  1.00 57.09           C  
ANISOU 3402  CE2 PHE B 151     5986   9661   6045    903   -306  -1559       C  
ATOM   3403  CZ  PHE B 151      69.097  34.942  44.572  1.00 50.48           C  
ANISOU 3403  CZ  PHE B 151     5041   9135   5005   1040   -392  -1498       C  
ATOM   3404  N   TYR B 152      68.860  40.230  42.152  1.00 57.50           N  
ANISOU 3404  N   TYR B 152     5892   9227   6729    207    -98  -2027       N  
ATOM   3405  CA  TYR B 152      68.214  39.918  40.884  1.00 54.46           C  
ANISOU 3405  CA  TYR B 152     5638   8583   6473    291    -35  -1830       C  
ATOM   3406  C   TYR B 152      69.085  40.324  39.702  1.00 55.24           C  
ANISOU 3406  C   TYR B 152     5659   8632   6698    212     11  -1786       C  
ATOM   3407  O   TYR B 152      69.148  39.611  38.696  1.00 60.59           O  
ANISOU 3407  O   TYR B 152     6384   9257   7379    328     20  -1607       O  
ATOM   3408  CB  TYR B 152      66.845  40.597  40.821  1.00 53.86           C  
ANISOU 3408  CB  TYR B 152     5713   8210   6541    250     50  -1844       C  
ATOM   3409  CG  TYR B 152      66.010  40.112  39.670  1.00 53.15           C  
ANISOU 3409  CG  TYR B 152     5757   7899   6539    357     85  -1632       C  
ATOM   3410  CD1 TYR B 152      65.384  38.855  39.717  1.00 49.76           C  
ANISOU 3410  CD1 TYR B 152     5417   7492   5996    531     37  -1483       C  
ATOM   3411  CD2 TYR B 152      65.856  40.891  38.520  1.00 49.92           C  
ANISOU 3411  CD2 TYR B 152     5385   7262   6321    280    165  -1577       C  
ATOM   3412  CE1 TYR B 152      64.611  38.400  38.654  1.00 47.71           C  
ANISOU 3412  CE1 TYR B 152     5277   7043   5809    607     57  -1310       C  
ATOM   3413  CE2 TYR B 152      65.081  40.443  37.457  1.00 54.32           C  
ANISOU 3413  CE2 TYR B 152     6061   7648   6932    375    179  -1387       C  
ATOM   3414  CZ  TYR B 152      64.472  39.198  37.528  1.00 50.57           C  
ANISOU 3414  CZ  TYR B 152     5667   7211   6339    529    119  -1267       C  
ATOM   3415  OH  TYR B 152      63.720  38.766  36.471  1.00 55.68           O  
ANISOU 3415  OH  TYR B 152     6423   7700   7032    598    123  -1102       O  
ATOM   3416  N   GLY B 153      69.775  41.459  39.807  1.00 58.87           N  
ANISOU 3416  N   GLY B 153     6003   9105   7259     10     49  -1954       N  
ATOM   3417  CA  GLY B 153      70.632  41.890  38.715  1.00 57.28           C  
ANISOU 3417  CA  GLY B 153     5718   8860   7184    -78    110  -1907       C  
ATOM   3418  C   GLY B 153      71.820  40.971  38.509  1.00 62.82           C  
ANISOU 3418  C   GLY B 153     6271   9844   7755     20     43  -1827       C  
ATOM   3419  O   GLY B 153      72.218  40.705  37.370  1.00 66.62           O  
ANISOU 3419  O   GLY B 153     6750  10274   8287     70     94  -1684       O  
ATOM   3420  N   GLU B 154      72.389  40.452  39.598  1.00 65.43           N  
ANISOU 3420  N   GLU B 154     6474  10482   7905     65    -67  -1907       N  
ATOM   3421  CA  GLU B 154      73.602  39.644  39.491  1.00 62.94           C  
ANISOU 3421  CA  GLU B 154     5982  10459   7472    167   -128  -1832       C  
ATOM   3422  C   GLU B 154      73.302  38.151  39.391  1.00 66.45           C  
ANISOU 3422  C   GLU B 154     6525  10954   7768    447   -171  -1632       C  
ATOM   3423  O   GLU B 154      73.738  37.493  38.445  1.00 67.48           O  
ANISOU 3423  O   GLU B 154     6655  11079   7906    567   -134  -1479       O  
ATOM   3424  CB  GLU B 154      74.534  39.945  40.660  1.00 67.07           C  
ANISOU 3424  CB  GLU B 154     6280  11321   7884     59   -230  -2019       C  
ATOM   3425  CG  GLU B 154      75.019  41.379  40.648  1.00 79.63           C  
ANISOU 3425  CG  GLU B 154     7755  12863   9638   -241   -177  -2227       C  
ATOM   3426  CD  GLU B 154      75.732  41.761  41.934  1.00101.81           C  
ANISOU 3426  CD  GLU B 154    10365  15995  12322   -382   -291  -2457       C  
ATOM   3427  OE1 GLU B 154      75.953  40.865  42.782  1.00106.00           O  
ANISOU 3427  OE1 GLU B 154    10828  16823  12625   -224   -418  -2425       O  
ATOM   3428  OE2 GLU B 154      76.046  42.960  42.110  1.00110.86           O  
ANISOU 3428  OE2 GLU B 154    11432  17095  13595   -653   -252  -2671       O  
ATOM   3429  N   LYS B 155      72.581  37.594  40.357  1.00 66.76           N  
ANISOU 3429  N   LYS B 155     6653  11039   7672    551   -236  -1631       N  
ATOM   3430  CA  LYS B 155      72.372  36.150  40.344  1.00 63.93           C  
ANISOU 3430  CA  LYS B 155     6382  10729   7179    809   -267  -1442       C  
ATOM   3431  C   LYS B 155      71.197  35.707  39.472  1.00 67.23           C  
ANISOU 3431  C   LYS B 155     7042  10824   7679    892   -196  -1302       C  
ATOM   3432  O   LYS B 155      71.020  34.500  39.276  1.00 65.50           O  
ANISOU 3432  O   LYS B 155     6914  10597   7376   1088   -202  -1148       O  
ATOM   3433  CB  LYS B 155      72.203  35.658  41.780  1.00 63.38           C  
ANISOU 3433  CB  LYS B 155     6292  10877   6914    895   -362  -1479       C  
ATOM   3434  CG  LYS B 155      73.468  35.951  42.593  1.00 75.26           C  
ANISOU 3434  CG  LYS B 155     7536  12757   8303    832   -457  -1602       C  
ATOM   3435  CD  LYS B 155      73.221  36.898  43.730  1.00 91.25           C  
ANISOU 3435  CD  LYS B 155     9520  14871  10278    650   -505  -1830       C  
ATOM   3436  CE  LYS B 155      74.489  37.660  44.127  1.00103.58           C  
ANISOU 3436  CE  LYS B 155    10813  16726  11815    472   -576  -2011       C  
ATOM   3437  NZ  LYS B 155      74.214  38.694  45.176  1.00103.74           N  
ANISOU 3437  NZ  LYS B 155    10817  16800  11799    260   -609  -2275       N  
ATOM   3438  N   ARG B 156      70.428  36.635  38.897  1.00 59.76           N  
ANISOU 3438  N   ARG B 156     6196   9613   6898    749   -127  -1347       N  
ATOM   3439  CA  ARG B 156      69.358  36.237  37.995  1.00 55.78           C  
ANISOU 3439  CA  ARG B 156     5893   8835   6464    820    -76  -1211       C  
ATOM   3440  C   ARG B 156      69.625  36.721  36.571  1.00 56.63           C  
ANISOU 3440  C   ARG B 156     6017   8791   6708    753      2  -1154       C  
ATOM   3441  O   ARG B 156      69.957  35.911  35.700  1.00 53.92           O  
ANISOU 3441  O   ARG B 156     5714   8446   6326    871     21  -1028       O  
ATOM   3442  CB  ARG B 156      67.999  36.738  38.506  1.00 49.31           C  
ANISOU 3442  CB  ARG B 156     5196   7834   5706    759    -63  -1263       C  
ATOM   3443  CG  ARG B 156      67.547  36.014  39.769  1.00 55.52           C  
ANISOU 3443  CG  ARG B 156     6011   8745   6340    861   -121  -1270       C  
ATOM   3444  CD  ARG B 156      67.156  34.563  39.484  1.00 58.72           C  
ANISOU 3444  CD  ARG B 156     6536   9116   6658   1056   -135  -1088       C  
ATOM   3445  NE  ARG B 156      66.789  33.845  40.701  1.00 55.54           N  
ANISOU 3445  NE  ARG B 156     6158   8835   6108   1160   -176  -1071       N  
ATOM   3446  CZ  ARG B 156      67.655  33.190  41.468  1.00 56.92           C  
ANISOU 3446  CZ  ARG B 156     6237   9274   6117   1270   -233  -1053       C  
ATOM   3447  NH1 ARG B 156      68.933  33.145  41.127  1.00 53.01           N  
ANISOU 3447  NH1 ARG B 156     5600   8950   5593   1291   -257  -1055       N  
ATOM   3448  NH2 ARG B 156      67.243  32.574  42.576  1.00 53.35           N  
ANISOU 3448  NH2 ARG B 156     5821   8925   5524   1367   -260  -1020       N  
ATOM   3449  N   LEU B 157      69.442  38.013  36.297  1.00 57.57           N  
ANISOU 3449  N   LEU B 157     6123   8769   6983    574     60  -1238       N  
ATOM   3450  CA  LEU B 157      69.689  38.506  34.945  1.00 56.45           C  
ANISOU 3450  CA  LEU B 157     6002   8486   6961    515    145  -1163       C  
ATOM   3451  C   LEU B 157      71.153  38.334  34.550  1.00 59.22           C  
ANISOU 3451  C   LEU B 157     6188   9036   7275    518    163  -1154       C  
ATOM   3452  O   LEU B 157      71.453  37.869  33.443  1.00 57.61           O  
ANISOU 3452  O   LEU B 157     6028   8800   7063    596    213  -1028       O  
ATOM   3453  CB  LEU B 157      69.273  39.965  34.818  1.00 52.42           C  
ANISOU 3453  CB  LEU B 157     5502   7781   6636    328    218  -1245       C  
ATOM   3454  CG  LEU B 157      67.813  40.323  35.076  1.00 49.09           C  
ANISOU 3454  CG  LEU B 157     5225   7141   6286    324    226  -1243       C  
ATOM   3455  CD1 LEU B 157      67.582  41.832  34.846  1.00 48.38           C  
ANISOU 3455  CD1 LEU B 157     5135   6845   6400    152    325  -1311       C  
ATOM   3456  CD2 LEU B 157      66.854  39.465  34.254  1.00 45.13           C  
ANISOU 3456  CD2 LEU B 157     4887   6513   5749    467    208  -1065       C  
ATOM   3457  N   GLY B 158      72.078  38.717  35.447  1.00 57.53           N  
ANISOU 3457  N   GLY B 158     5778   9043   7036    428    126  -1293       N  
ATOM   3458  CA  GLY B 158      73.496  38.728  35.097  1.00 56.94           C  
ANISOU 3458  CA  GLY B 158     5506   9172   6956    402    150  -1294       C  
ATOM   3459  C   GLY B 158      74.038  37.348  34.767  1.00 61.43           C  
ANISOU 3459  C   GLY B 158     6062   9895   7382    631    128  -1154       C  
ATOM   3460  O   GLY B 158      74.739  37.173  33.770  1.00 63.54           O  
ANISOU 3460  O   GLY B 158     6288  10182   7673    669    203  -1066       O  
ATOM   3461  N   TYR B 159      73.675  36.339  35.566  1.00 58.89           N  
ANISOU 3461  N   TYR B 159     5794   9665   6916    797     42  -1122       N  
ATOM   3462  CA  TYR B 159      74.090  34.969  35.277  1.00 60.35           C  
ANISOU 3462  CA  TYR B 159     5998   9952   6978   1035     38   -980       C  
ATOM   3463  C   TYR B 159      73.578  34.509  33.918  1.00 60.49           C  
ANISOU 3463  C   TYR B 159     6216   9735   7034   1115    124   -849       C  
ATOM   3464  O   TYR B 159      74.327  33.925  33.129  1.00 58.61           O  
ANISOU 3464  O   TYR B 159     5949   9555   6763   1226    186   -762       O  
ATOM   3465  CB  TYR B 159      73.596  34.036  36.380  1.00 61.34           C  
ANISOU 3465  CB  TYR B 159     6184  10161   6961   1188    -53   -956       C  
ATOM   3466  CG  TYR B 159      73.966  32.572  36.236  1.00 62.62           C  
ANISOU 3466  CG  TYR B 159     6384  10406   7004   1449    -49   -806       C  
ATOM   3467  CD1 TYR B 159      75.171  32.082  36.723  1.00 63.80           C  
ANISOU 3467  CD1 TYR B 159     6327  10858   7057   1570    -84   -778       C  
ATOM   3468  CD2 TYR B 159      73.094  31.676  35.640  1.00 64.75           C  
ANISOU 3468  CD2 TYR B 159     6891  10449   7261   1575     -8   -693       C  
ATOM   3469  CE1 TYR B 159      75.496  30.741  36.604  1.00 67.22           C  
ANISOU 3469  CE1 TYR B 159     6803  11343   7395   1831    -62   -629       C  
ATOM   3470  CE2 TYR B 159      73.404  30.344  35.518  1.00 64.52           C  
ANISOU 3470  CE2 TYR B 159     6919  10458   7139   1808     15   -567       C  
ATOM   3471  CZ  TYR B 159      74.605  29.879  35.998  1.00 69.33           C  
ANISOU 3471  CZ  TYR B 159     7333  11346   7662   1946     -4   -529       C  
ATOM   3472  OH  TYR B 159      74.895  28.542  35.872  1.00 70.14           O  
ANISOU 3472  OH  TYR B 159     7504  11461   7687   2200     37   -392       O  
ATOM   3473  N   GLN B 160      72.302  34.773  33.617  1.00 59.19           N  
ANISOU 3473  N   GLN B 160     6249   9313   6928   1060    131   -838       N  
ATOM   3474  CA  GLN B 160      71.741  34.316  32.346  1.00 53.87           C  
ANISOU 3474  CA  GLN B 160     5766   8437   6265   1125    192   -722       C  
ATOM   3475  C   GLN B 160      72.385  35.025  31.155  1.00 53.81           C  
ANISOU 3475  C   GLN B 160     5711   8395   6338   1036    292   -695       C  
ATOM   3476  O   GLN B 160      72.643  34.397  30.119  1.00 52.86           O  
ANISOU 3476  O   GLN B 160     5670   8246   6169   1139    356   -601       O  
ATOM   3477  CB  GLN B 160      70.223  34.516  32.345  1.00 54.45           C  
ANISOU 3477  CB  GLN B 160     6025   8277   6387   1075    163   -714       C  
ATOM   3478  CG  GLN B 160      69.463  33.558  33.255  1.00 46.29           C  
ANISOU 3478  CG  GLN B 160     5082   7240   5264   1190     91   -699       C  
ATOM   3479  CD  GLN B 160      69.310  32.180  32.647  1.00 52.42           C  
ANISOU 3479  CD  GLN B 160     6007   7961   5951   1362    105   -588       C  
ATOM   3480  OE1 GLN B 160      69.376  32.019  31.436  1.00 59.64           O  
ANISOU 3480  OE1 GLN B 160     7007   8782   6871   1377    159   -530       O  
ATOM   3481  NE2 GLN B 160      69.130  31.174  33.489  1.00 50.19           N  
ANISOU 3481  NE2 GLN B 160     5761   7731   5578   1492     64   -559       N  
ATOM   3482  N   LEU B 161      72.669  36.325  31.287  1.00 53.19           N  
ANISOU 3482  N   LEU B 161     5511   8317   6382    844    320   -778       N  
ATOM   3483  CA  LEU B 161      73.294  37.069  30.194  1.00 56.23           C  
ANISOU 3483  CA  LEU B 161     5846   8663   6856    746    433   -739       C  
ATOM   3484  C   LEU B 161      74.688  36.544  29.901  1.00 64.12           C  
ANISOU 3484  C   LEU B 161     6682   9886   7794    831    484   -708       C  
ATOM   3485  O   LEU B 161      75.053  36.321  28.739  1.00 64.10           O  
ANISOU 3485  O   LEU B 161     6727   9854   7774    885    583   -611       O  
ATOM   3486  CB  LEU B 161      73.386  38.550  30.543  1.00 51.71           C  
ANISOU 3486  CB  LEU B 161     5166   8038   6444    515    463   -846       C  
ATOM   3487  CG  LEU B 161      72.091  39.356  30.591  1.00 52.91           C  
ANISOU 3487  CG  LEU B 161     5466   7934   6702    418    460   -861       C  
ATOM   3488  CD1 LEU B 161      72.433  40.771  31.033  1.00 54.43           C  
ANISOU 3488  CD1 LEU B 161     5533   8089   7059    194    511   -988       C  
ATOM   3489  CD2 LEU B 161      71.384  39.342  29.224  1.00 41.18           C  
ANISOU 3489  CD2 LEU B 161     4168   6246   5232    463    522   -705       C  
ATOM   3490  N   LYS B 162      75.484  36.348  30.953  1.00 67.06           N  
ANISOU 3490  N   LYS B 162     6854  10502   8124    848    420   -788       N  
ATOM   3491  CA  LYS B 162      76.828  35.819  30.778  1.00 64.70           C  
ANISOU 3491  CA  LYS B 162     6365  10447   7771    948    461   -750       C  
ATOM   3492  C   LYS B 162      76.770  34.435  30.141  1.00 63.17           C  
ANISOU 3492  C   LYS B 162     6318  10230   7453   1202    496   -621       C  
ATOM   3493  O   LYS B 162      77.564  34.110  29.247  1.00 58.59           O  
ANISOU 3493  O   LYS B 162     5694   9711   6855   1285    603   -546       O  
ATOM   3494  CB  LYS B 162      77.557  35.821  32.121  1.00 68.32           C  
ANISOU 3494  CB  LYS B 162     6581  11189   8188    931    357   -853       C  
ATOM   3495  CG  LYS B 162      78.944  35.223  32.089  1.00 83.56           C  
ANISOU 3495  CG  LYS B 162     8278  13411  10059   1057    381   -804       C  
ATOM   3496  CD  LYS B 162      79.808  35.835  33.191  1.00 91.50           C  
ANISOU 3496  CD  LYS B 162     8980  14707  11078    920    291   -937       C  
ATOM   3497  CE  LYS B 162      81.290  35.512  32.985  1.00 99.82           C  
ANISOU 3497  CE  LYS B 162     9748  16064  12115    999    333   -886       C  
ATOM   3498  NZ  LYS B 162      82.163  36.313  33.898  1.00102.24           N  
ANISOU 3498  NZ  LYS B 162     9734  16656  12458    804    248  -1033       N  
ATOM   3499  N   LEU B 163      75.796  33.627  30.552  1.00 59.95           N  
ANISOU 3499  N   LEU B 163     6097   9714   6966   1320    421   -598       N  
ATOM   3500  CA  LEU B 163      75.636  32.299  29.975  1.00 64.88           C  
ANISOU 3500  CA  LEU B 163     6892  10276   7486   1543    459   -495       C  
ATOM   3501  C   LEU B 163      75.275  32.361  28.485  1.00 71.63           C  
ANISOU 3501  C   LEU B 163     7930  10935   8353   1526    563   -431       C  
ATOM   3502  O   LEU B 163      75.716  31.510  27.702  1.00 70.45           O  
ANISOU 3502  O   LEU B 163     7848  10793   8128   1682    650   -363       O  
ATOM   3503  CB  LEU B 163      74.572  31.545  30.771  1.00 64.07           C  
ANISOU 3503  CB  LEU B 163     6950  10074   7319   1629    363   -491       C  
ATOM   3504  CG  LEU B 163      74.134  30.153  30.342  1.00 61.58           C  
ANISOU 3504  CG  LEU B 163     6850   9635   6911   1831    392   -403       C  
ATOM   3505  CD1 LEU B 163      75.351  29.199  30.271  1.00 56.82           C  
ANISOU 3505  CD1 LEU B 163     6144   9209   6234   2050    460   -337       C  
ATOM   3506  CD2 LEU B 163      73.034  29.655  31.282  1.00 55.50           C  
ANISOU 3506  CD2 LEU B 163     6209   8770   6110   1860    296   -408       C  
ATOM   3507  N   ALA B 164      74.481  33.358  28.066  1.00 65.71           N  
ANISOU 3507  N   ALA B 164     7266  10012   7687   1348    562   -450       N  
ATOM   3508  CA  ALA B 164      74.173  33.484  26.638  1.00 64.87           C  
ANISOU 3508  CA  ALA B 164     7323   9754   7573   1331    652   -376       C  
ATOM   3509  C   ALA B 164      75.375  33.986  25.834  1.00 64.54           C  
ANISOU 3509  C   ALA B 164     7136   9827   7560   1295    788   -342       C  
ATOM   3510  O   ALA B 164      75.555  33.588  24.676  1.00 62.13           O  
ANISOU 3510  O   ALA B 164     6942   9484   7182   1373    888   -269       O  
ATOM   3511  CB  ALA B 164      72.967  34.399  26.428  1.00 61.53           C  
ANISOU 3511  CB  ALA B 164     7022   9126   7231   1174    611   -378       C  
ATOM   3512  N   ARG B 165      76.198  34.858  26.424  1.00 65.89           N  
ANISOU 3512  N   ARG B 165     7060  10142   7834   1168    798   -399       N  
ATOM   3513  CA  ARG B 165      77.410  35.321  25.749  1.00 70.22           C  
ANISOU 3513  CA  ARG B 165     7435  10819   8425   1122    934   -366       C  
ATOM   3514  C   ARG B 165      78.380  34.169  25.488  1.00 71.56           C  
ANISOU 3514  C   ARG B 165     7539  11166   8485   1342   1002   -315       C  
ATOM   3515  O   ARG B 165      79.080  34.163  24.471  1.00 74.21           O  
ANISOU 3515  O   ARG B 165     7849  11544   8804   1377   1148   -247       O  
ATOM   3516  CB  ARG B 165      78.093  36.411  26.578  1.00 67.69           C  
ANISOU 3516  CB  ARG B 165     6847  10630   8244    925    916   -461       C  
ATOM   3517  CG  ARG B 165      79.093  37.260  25.804  1.00 66.47           C  
ANISOU 3517  CG  ARG B 165     6529  10539   8186    794   1069   -426       C  
ATOM   3518  CD  ARG B 165      80.012  38.040  26.763  1.00 69.67           C  
ANISOU 3518  CD  ARG B 165     6622  11140   8709    620   1039   -543       C  
ATOM   3519  NE  ARG B 165      80.485  37.167  27.838  1.00 79.11           N  
ANISOU 3519  NE  ARG B 165     7667  12579   9810    759    919   -599       N  
ATOM   3520  CZ  ARG B 165      81.250  37.550  28.858  1.00 82.46           C  
ANISOU 3520  CZ  ARG B 165     7815  13235  10280    652    845   -711       C  
ATOM   3521  NH1 ARG B 165      81.664  38.813  28.957  1.00 85.41           N  
ANISOU 3521  NH1 ARG B 165     8028  13614  10810    381    886   -801       N  
ATOM   3522  NH2 ARG B 165      81.604  36.660  29.782  1.00 77.40           N  
ANISOU 3522  NH2 ARG B 165     7060  12824   9526    815    730   -730       N  
ATOM   3523  N   ASP B 166      78.464  33.204  26.414  1.00 67.61           N  
ANISOU 3523  N   ASP B 166     7003  10774   7913   1502    911   -339       N  
ATOM   3524  CA  ASP B 166      79.383  32.077  26.265  1.00 68.10           C  
ANISOU 3524  CA  ASP B 166     6996  10996   7883   1740    981   -281       C  
ATOM   3525  C   ASP B 166      78.838  31.017  25.312  1.00 68.60           C  
ANISOU 3525  C   ASP B 166     7352  10883   7832   1916   1051   -217       C  
ATOM   3526  O   ASP B 166      79.608  30.386  24.581  1.00 74.57           O  
ANISOU 3526  O   ASP B 166     8099  11707   8527   2073   1186   -162       O  
ATOM   3527  CB  ASP B 166      79.684  31.446  27.624  1.00 71.63           C  
ANISOU 3527  CB  ASP B 166     7299  11624   8293   1860    862   -308       C  
ATOM   3528  CG  ASP B 166      80.420  32.391  28.571  1.00 81.81           C  
ANISOU 3528  CG  ASP B 166     8270  13147   9668   1696    790   -387       C  
ATOM   3529  OD1 ASP B 166      80.907  33.457  28.127  1.00 88.63           O  
ANISOU 3529  OD1 ASP B 166     8996  14042  10636   1501    859   -418       O  
ATOM   3530  OD2 ASP B 166      80.509  32.064  29.772  1.00 83.35           O  
ANISOU 3530  OD2 ASP B 166     8354  13496   9819   1755    665   -422       O  
ATOM   3531  N   GLN B 167      77.525  30.779  25.325  1.00 64.35           N  
ANISOU 3531  N   GLN B 167     7067  10123   7259   1893    966   -233       N  
ATOM   3532  CA  GLN B 167      76.943  29.726  24.493  1.00 60.88           C  
ANISOU 3532  CA  GLN B 167     6909   9516   6707   2036   1015   -199       C  
ATOM   3533  C   GLN B 167      76.765  30.146  23.040  1.00 66.52           C  
ANISOU 3533  C   GLN B 167     7767  10123   7385   1963   1121   -166       C  
ATOM   3534  O   GLN B 167      76.778  29.288  22.149  1.00 63.49           O  
ANISOU 3534  O   GLN B 167     7563   9674   6888   2097   1213   -145       O  
ATOM   3535  CB  GLN B 167      75.595  29.268  25.048  1.00 56.52           C  
ANISOU 3535  CB  GLN B 167     6559   8783   6134   2028    882   -228       C  
ATOM   3536  CG  GLN B 167      75.721  28.594  26.386  1.00 73.09           C  
ANISOU 3536  CG  GLN B 167     8568  10974   8228   2145    798   -237       C  
ATOM   3537  CD  GLN B 167      74.556  27.687  26.696  1.00 77.83           C  
ANISOU 3537  CD  GLN B 167     9406  11384   8782   2207    726   -239       C  
ATOM   3538  OE1 GLN B 167      74.730  26.650  27.353  1.00 89.42           O  
ANISOU 3538  OE1 GLN B 167    10891  12879  10206   2385    721   -210       O  
ATOM   3539  NE2 GLN B 167      73.364  28.058  26.227  1.00 64.47           N  
ANISOU 3539  NE2 GLN B 167     7892   9501   7103   2065    674   -262       N  
ATOM   3540  N   TYR B 168      76.517  31.428  22.791  1.00 62.85           N  
ANISOU 3540  N   TYR B 168     7251   9624   7006   1754   1111   -162       N  
ATOM   3541  CA  TYR B 168      76.180  31.899  21.462  1.00 62.51           C  
ANISOU 3541  CA  TYR B 168     7359   9473   6918   1680   1194   -109       C  
ATOM   3542  C   TYR B 168      77.071  33.035  20.977  1.00 61.45           C  
ANISOU 3542  C   TYR B 168     7040   9439   6869   1554   1317    -62       C  
ATOM   3543  O   TYR B 168      76.820  33.568  19.896  1.00 65.11           O  
ANISOU 3543  O   TYR B 168     7617   9822   7299   1483   1394      4       O  
ATOM   3544  CB  TYR B 168      74.717  32.380  21.408  1.00 59.99           C  
ANISOU 3544  CB  TYR B 168     7218   8957   6618   1549   1072   -111       C  
ATOM   3545  CG  TYR B 168      73.668  31.402  21.865  1.00 57.61           C  
ANISOU 3545  CG  TYR B 168     7097   8536   6255   1626    948   -154       C  
ATOM   3546  CD1 TYR B 168      73.195  30.406  21.017  1.00 51.21           C  
ANISOU 3546  CD1 TYR B 168     6528   7630   5300   1728    968   -150       C  
ATOM   3547  CD2 TYR B 168      73.090  31.518  23.127  1.00 56.77           C  
ANISOU 3547  CD2 TYR B 168     6930   8405   6235   1579    816   -203       C  
ATOM   3548  CE1 TYR B 168      72.183  29.520  21.425  1.00 49.94           C  
ANISOU 3548  CE1 TYR B 168     6533   7343   5101   1772    859   -193       C  
ATOM   3549  CE2 TYR B 168      72.094  30.636  23.549  1.00 56.49           C  
ANISOU 3549  CE2 TYR B 168     7056   8254   6153   1638    715   -230       C  
ATOM   3550  CZ  TYR B 168      71.647  29.641  22.700  1.00 58.19           C  
ANISOU 3550  CZ  TYR B 168     7499   8365   6244   1728    737   -223       C  
ATOM   3551  OH  TYR B 168      70.666  28.783  23.140  1.00 59.05           O  
ANISOU 3551  OH  TYR B 168     7757   8352   6326   1764    645   -253       O  
ATOM   3552  N   GLY B 169      78.071  33.446  21.749  1.00 69.64           N  
ANISOU 3552  N   GLY B 169     7794  10652   8013   1513   1334    -91       N  
ATOM   3553  CA  GLY B 169      78.794  34.669  21.437  1.00 68.12           C  
ANISOU 3553  CA  GLY B 169     7414  10528   7941   1341   1437    -60       C  
ATOM   3554  C   GLY B 169      77.907  35.889  21.329  1.00 71.28           C  
ANISOU 3554  C   GLY B 169     7889  10748   8445   1128   1395    -49       C  
ATOM   3555  O   GLY B 169      78.261  36.848  20.637  1.00 70.65           O  
ANISOU 3555  O   GLY B 169     7758  10649   8438    999   1516     16       O  
ATOM   3556  N   ASP B 170      76.779  35.901  22.041  1.00 70.69           N  
ANISOU 3556  N   ASP B 170     7926  10541   8391   1094   1238   -102       N  
ATOM   3557  CA  ASP B 170      75.804  36.986  21.940  1.00 62.63           C  
ANISOU 3557  CA  ASP B 170     6995   9330   7470    926   1199    -82       C  
ATOM   3558  C   ASP B 170      76.251  38.110  22.866  1.00 65.43           C  
ANISOU 3558  C   ASP B 170     7124   9722   8014    737   1192   -160       C  
ATOM   3559  O   ASP B 170      75.716  38.314  23.957  1.00 70.16           O  
ANISOU 3559  O   ASP B 170     7694  10285   8679    679   1070   -256       O  
ATOM   3560  CB  ASP B 170      74.410  36.482  22.294  1.00 61.75           C  
ANISOU 3560  CB  ASP B 170     7085   9071   7304    977   1047   -106       C  
ATOM   3561  CG  ASP B 170      73.307  37.440  21.871  1.00 65.12           C  
ANISOU 3561  CG  ASP B 170     7641   9299   7802    855   1023    -45       C  
ATOM   3562  OD1 ASP B 170      73.594  38.639  21.645  1.00 61.40           O  
ANISOU 3562  OD1 ASP B 170     7084   8783   7463    710   1110     -6       O  
ATOM   3563  OD2 ASP B 170      72.137  36.984  21.778  1.00 66.03           O  
ANISOU 3563  OD2 ASP B 170     7938   9300   7850    907    920    -30       O  
ATOM   3564  N   SER B 171      77.272  38.845  22.418  1.00 69.18           N  
ANISOU 3564  N   SER B 171     7436  10275   8575    631   1336   -126       N  
ATOM   3565  CA  SER B 171      77.778  39.980  23.180  1.00 70.13           C  
ANISOU 3565  CA  SER B 171     7339  10422   8887    417   1350   -213       C  
ATOM   3566  C   SER B 171      76.868  41.195  23.097  1.00 69.75           C  
ANISOU 3566  C   SER B 171     7398  10123   8982    248   1358   -195       C  
ATOM   3567  O   SER B 171      76.988  42.100  23.930  1.00 78.01           O  
ANISOU 3567  O   SER B 171     8313  11137  10189     69   1342   -304       O  
ATOM   3568  CB  SER B 171      79.176  40.370  22.697  1.00 74.60           C  
ANISOU 3568  CB  SER B 171     7683  11145   9515    343   1514   -178       C  
ATOM   3569  OG  SER B 171      79.161  40.634  21.308  1.00 71.92           O  
ANISOU 3569  OG  SER B 171     7473  10709   9143    353   1671    -22       O  
ATOM   3570  N   ALA B 172      75.994  41.262  22.096  1.00 63.11           N  
ANISOU 3570  N   ALA B 172     6785   9108   8084    299   1390    -61       N  
ATOM   3571  CA  ALA B 172      75.055  42.376  22.023  1.00 60.45           C  
ANISOU 3571  CA  ALA B 172     6552   8530   7885    172   1396    -20       C  
ATOM   3572  C   ALA B 172      74.041  42.323  23.164  1.00 64.32           C  
ANISOU 3572  C   ALA B 172     7091   8934   8413    171   1232   -137       C  
ATOM   3573  O   ALA B 172      73.811  43.329  23.845  1.00 73.00           O  
ANISOU 3573  O   ALA B 172     8134   9916   9687     17   1236   -215       O  
ATOM   3574  CB  ALA B 172      74.353  42.384  20.668  1.00 59.77           C  
ANISOU 3574  CB  ALA B 172     6687   8319   7703    250   1451    168       C  
ATOM   3575  N   ILE B 173      73.401  41.164  23.376  1.00 60.80           N  
ANISOU 3575  N   ILE B 173     6760   8532   7810    336   1102   -153       N  
ATOM   3576  CA  ILE B 173      72.443  41.059  24.480  1.00 61.99           C  
ANISOU 3576  CA  ILE B 173     6950   8614   7989    340    960   -254       C  
ATOM   3577  C   ILE B 173      73.156  41.214  25.812  1.00 64.19           C  
ANISOU 3577  C   ILE B 173     7023   9031   8334    257    918   -428       C  
ATOM   3578  O   ILE B 173      72.593  41.763  26.767  1.00 69.27           O  
ANISOU 3578  O   ILE B 173     7652   9594   9073    171    858   -533       O  
ATOM   3579  CB  ILE B 173      71.630  39.747  24.410  1.00 60.18           C  
ANISOU 3579  CB  ILE B 173     6883   8397   7584    522    842   -228       C  
ATOM   3580  CG1 ILE B 173      70.286  39.926  25.135  1.00 60.82           C  
ANISOU 3580  CG1 ILE B 173     7055   8334   7720    508    731   -266       C  
ATOM   3581  CG2 ILE B 173      72.391  38.579  25.009  1.00 49.74           C  
ANISOU 3581  CG2 ILE B 173     5474   7281   6143    642    795   -304       C  
ATOM   3582  CD1 ILE B 173      69.220  38.867  24.774  1.00 54.93           C  
ANISOU 3582  CD1 ILE B 173     6497   7540   6835    646    632   -205       C  
ATOM   3583  N   TYR B 174      74.413  40.771  25.889  1.00 62.10           N  
ANISOU 3583  N   TYR B 174     6590   8987   8018    281    953   -462       N  
ATOM   3584  CA  TYR B 174      75.184  40.908  27.118  1.00 60.69           C  
ANISOU 3584  CA  TYR B 174     6190   8988   7883    200    899   -622       C  
ATOM   3585  C   TYR B 174      75.441  42.370  27.459  1.00 68.32           C  
ANISOU 3585  C   TYR B 174     7040   9866   9053    -51    968   -715       C  
ATOM   3586  O   TYR B 174      75.381  42.761  28.632  1.00 71.39           O  
ANISOU 3586  O   TYR B 174     7339  10289   9496   -153    892   -878       O  
ATOM   3587  CB  TYR B 174      76.510  40.159  26.986  1.00 64.00           C  
ANISOU 3587  CB  TYR B 174     6431   9674   8211    289    933   -610       C  
ATOM   3588  CG  TYR B 174      77.373  40.264  28.215  1.00 67.24           C  
ANISOU 3588  CG  TYR B 174     6585  10317   8645    212    862   -763       C  
ATOM   3589  CD1 TYR B 174      78.263  41.323  28.377  1.00 66.08           C  
ANISOU 3589  CD1 TYR B 174     6223  10239   8648    -10    933   -846       C  
ATOM   3590  CD2 TYR B 174      77.284  39.309  29.231  1.00 63.62           C  
ANISOU 3590  CD2 TYR B 174     6099  10017   8058    353    721   -822       C  
ATOM   3591  CE1 TYR B 174      79.054  41.424  29.516  1.00 69.51           C  
ANISOU 3591  CE1 TYR B 174     6407  10915   9087    -97    849  -1001       C  
ATOM   3592  CE2 TYR B 174      78.065  39.399  30.372  1.00 62.71           C  
ANISOU 3592  CE2 TYR B 174     5743  10148   7936    289    640   -955       C  
ATOM   3593  CZ  TYR B 174      78.952  40.457  30.508  1.00 72.56           C  
ANISOU 3593  CZ  TYR B 174     6768  11483   9320     60    695  -1052       C  
ATOM   3594  OH  TYR B 174      79.730  40.550  31.638  1.00 82.51           O  
ANISOU 3594  OH  TYR B 174     7776  13015  10559    -18    598  -1197       O  
ATOM   3595  N   GLN B 175      75.728  43.195  26.453  1.00 67.75           N  
ANISOU 3595  N   GLN B 175     6975   9674   9091   -155   1120   -617       N  
ATOM   3596  CA  GLN B 175      76.036  44.592  26.727  1.00 67.79           C  
ANISOU 3596  CA  GLN B 175     6876   9568   9313   -405   1211   -702       C  
ATOM   3597  C   GLN B 175      74.767  45.385  27.012  1.00 69.49           C  
ANISOU 3597  C   GLN B 175     7259   9499   9643   -465   1197   -723       C  
ATOM   3598  O   GLN B 175      74.701  46.129  27.997  1.00 65.25           O  
ANISOU 3598  O   GLN B 175     6654   8909   9228   -621   1177   -894       O  
ATOM   3599  CB  GLN B 175      76.791  45.209  25.548  1.00 73.61           C  
ANISOU 3599  CB  GLN B 175     7567  10262  10141   -494   1400   -569       C  
ATOM   3600  CG  GLN B 175      77.285  46.629  25.798  1.00 96.02           C  
ANISOU 3600  CG  GLN B 175    10277  12984  13221   -774   1520   -658       C  
ATOM   3601  CD  GLN B 175      78.175  47.150  24.676  1.00110.85           C  
ANISOU 3601  CD  GLN B 175    12081  14852  15185   -865   1721   -518       C  
ATOM   3602  OE1 GLN B 175      78.507  46.419  23.739  1.00115.00           O  
ANISOU 3602  OE1 GLN B 175    12636  15490  15570   -712   1771   -365       O  
ATOM   3603  NE2 GLN B 175      78.580  48.412  24.778  1.00112.20           N  
ANISOU 3603  NE2 GLN B 175    12158  14884  15587  -1121   1851   -576       N  
ATOM   3604  N   LYS B 176      73.759  45.260  26.142  1.00 69.20           N  
ANISOU 3604  N   LYS B 176     7439   9285   9568   -345   1211   -552       N  
ATOM   3605  CA  LYS B 176      72.502  45.961  26.382  1.00 66.55           C  
ANISOU 3605  CA  LYS B 176     7251   8691   9343   -371   1198   -548       C  
ATOM   3606  C   LYS B 176      71.865  45.511  27.686  1.00 66.65           C  
ANISOU 3606  C   LYS B 176     7269   8754   9303   -327   1047   -709       C  
ATOM   3607  O   LYS B 176      71.351  46.338  28.446  1.00 65.07           O  
ANISOU 3607  O   LYS B 176     7079   8406   9239   -433   1055   -823       O  
ATOM   3608  CB  LYS B 176      71.551  45.785  25.199  1.00 61.64           C  
ANISOU 3608  CB  LYS B 176     6836   7924   8661   -233   1215   -324       C  
ATOM   3609  CG  LYS B 176      72.024  46.584  23.989  1.00 68.44           C  
ANISOU 3609  CG  LYS B 176     7713   8683   9610   -305   1392   -157       C  
ATOM   3610  CD  LYS B 176      70.925  46.893  22.992  1.00 76.24           C  
ANISOU 3610  CD  LYS B 176     8899   9475  10595   -215   1419     57       C  
ATOM   3611  CE  LYS B 176      70.877  45.880  21.869  1.00 86.05           C  
ANISOU 3611  CE  LYS B 176    10245  10844  11605    -48   1386    214       C  
ATOM   3612  NZ  LYS B 176      69.693  46.101  20.977  1.00 89.97           N  
ANISOU 3612  NZ  LYS B 176    10927  11189  12067     45   1371    412       N  
ATOM   3613  N   GLY B 177      71.942  44.214  27.991  1.00 66.15           N  
ANISOU 3613  N   GLY B 177     7195   8895   9043   -171    923   -724       N  
ATOM   3614  CA  GLY B 177      71.417  43.735  29.260  1.00 62.16           C  
ANISOU 3614  CA  GLY B 177     6687   8459   8472   -125    790   -863       C  
ATOM   3615  C   GLY B 177      72.093  44.375  30.459  1.00 65.32           C  
ANISOU 3615  C   GLY B 177     6913   8958   8949   -294    780  -1082       C  
ATOM   3616  O   GLY B 177      71.433  44.711  31.448  1.00 69.43           O  
ANISOU 3616  O   GLY B 177     7461   9414   9505   -337    732  -1211       O  
ATOM   3617  N   HIS B 178      73.418  44.557  30.394  1.00 68.65           N  
ANISOU 3617  N   HIS B 178     7144   9549   9391   -398    828  -1134       N  
ATOM   3618  CA  HIS B 178      74.128  45.133  31.531  1.00 71.00           C  
ANISOU 3618  CA  HIS B 178     7255   9978   9743   -578    800  -1360       C  
ATOM   3619  C   HIS B 178      73.930  46.629  31.642  1.00 69.29           C  
ANISOU 3619  C   HIS B 178     7053   9514   9759   -809    916  -1461       C  
ATOM   3620  O   HIS B 178      74.096  47.176  32.735  1.00 72.37           O  
ANISOU 3620  O   HIS B 178     7355   9947  10195   -961    882  -1681       O  
ATOM   3621  CB  HIS B 178      75.624  44.812  31.486  1.00 73.03           C  
ANISOU 3621  CB  HIS B 178     7270  10528   9949   -620    801  -1389       C  
ATOM   3622  CG  HIS B 178      75.990  43.600  32.286  1.00 81.58           C  
ANISOU 3622  CG  HIS B 178     8255  11919  10822   -461    649  -1429       C  
ATOM   3623  ND1 HIS B 178      76.084  42.338  31.733  1.00 83.05           N  
ANISOU 3623  ND1 HIS B 178     8488  12217  10852   -222    618  -1269       N  
ATOM   3624  CD2 HIS B 178      76.240  43.448  33.608  1.00 83.96           C  
ANISOU 3624  CD2 HIS B 178     8430  12432  11038   -495    525  -1604       C  
ATOM   3625  CE1 HIS B 178      76.396  41.465  32.674  1.00 81.28           C  
ANISOU 3625  CE1 HIS B 178     8165  12245  10471   -109    490  -1328       C  
ATOM   3626  NE2 HIS B 178      76.493  42.113  33.822  1.00 84.97           N  
ANISOU 3626  NE2 HIS B 178     8523  12793  10968   -268    424  -1524       N  
ATOM   3627  N   THR B 179      73.565  47.304  30.555  1.00 70.63           N  
ANISOU 3627  N   THR B 179     7342   9423  10070   -836   1055  -1306       N  
ATOM   3628  CA  THR B 179      73.083  48.674  30.689  1.00 72.37           C  
ANISOU 3628  CA  THR B 179     7632   9346  10521  -1010   1173  -1376       C  
ATOM   3629  C   THR B 179      71.791  48.702  31.494  1.00 72.02           C  
ANISOU 3629  C   THR B 179     7730   9166  10467   -934   1103  -1448       C  
ATOM   3630  O   THR B 179      71.623  49.530  32.399  1.00 77.91           O  
ANISOU 3630  O   THR B 179     8465   9810  11329  -1082   1132  -1648       O  
ATOM   3631  CB  THR B 179      72.862  49.300  29.320  1.00 70.01           C  
ANISOU 3631  CB  THR B 179     7446   8800  10356  -1010   1334  -1149       C  
ATOM   3632  OG1 THR B 179      74.076  49.216  28.566  1.00 74.52           O  
ANISOU 3632  OG1 THR B 179     7880   9513  10921  -1071   1412  -1074       O  
ATOM   3633  CG2 THR B 179      72.429  50.783  29.483  1.00 61.80           C  
ANISOU 3633  CG2 THR B 179     6474   7423   9582  -1187   1481  -1214       C  
ATOM   3634  N   LEU B 180      70.870  47.786  31.178  1.00 62.95           N  
ANISOU 3634  N   LEU B 180     6717   8020   9181   -709   1017  -1296       N  
ATOM   3635  CA  LEU B 180      69.626  47.682  31.932  1.00 61.63           C  
ANISOU 3635  CA  LEU B 180     6668   7754   8994   -621    950  -1347       C  
ATOM   3636  C   LEU B 180      69.904  47.408  33.402  1.00 60.31           C  
ANISOU 3636  C   LEU B 180     6400   7789   8727   -671    846  -1590       C  
ATOM   3637  O   LEU B 180      69.412  48.127  34.275  1.00 63.91           O  
ANISOU 3637  O   LEU B 180     6885   8128   9271   -761    873  -1755       O  
ATOM   3638  CB  LEU B 180      68.738  46.578  31.348  1.00 59.13           C  
ANISOU 3638  CB  LEU B 180     6481   7458   8528   -388    861  -1151       C  
ATOM   3639  CG  LEU B 180      67.453  46.244  32.119  1.00 54.94           C  
ANISOU 3639  CG  LEU B 180     6052   6869   7954   -280    780  -1183       C  
ATOM   3640  CD1 LEU B 180      66.605  47.492  32.299  1.00 52.06           C  
ANISOU 3640  CD1 LEU B 180     5764   6214   7802   -356    889  -1216       C  
ATOM   3641  CD2 LEU B 180      66.669  45.172  31.395  1.00 60.79           C  
ANISOU 3641  CD2 LEU B 180     6907   7627   8565    -84    699   -986       C  
ATOM   3642  N   ILE B 181      70.730  46.395  33.692  1.00 61.07           N  
ANISOU 3642  N   ILE B 181     6372   8196   8635   -610    735  -1615       N  
ATOM   3643  CA  ILE B 181      71.004  46.035  35.082  1.00 64.98           C  
ANISOU 3643  CA  ILE B 181     6767   8924   8998   -632    620  -1817       C  
ATOM   3644  C   ILE B 181      71.520  47.240  35.850  1.00 71.45           C  
ANISOU 3644  C   ILE B 181     7484   9715   9948   -887    678  -2068       C  
ATOM   3645  O   ILE B 181      71.180  47.438  37.025  1.00 74.32           O  
ANISOU 3645  O   ILE B 181     7852  10121  10266   -935    629  -2260       O  
ATOM   3646  CB  ILE B 181      71.993  44.857  35.154  1.00 67.34           C  
ANISOU 3646  CB  ILE B 181     6925   9565   9097   -526    511  -1779       C  
ATOM   3647  CG1 ILE B 181      71.358  43.581  34.588  1.00 68.10           C  
ANISOU 3647  CG1 ILE B 181     7151   9670   9052   -273    453  -1569       C  
ATOM   3648  CG2 ILE B 181      72.487  44.657  36.582  1.00 56.28           C  
ANISOU 3648  CG2 ILE B 181     5383   8439   7562   -576    396  -1988       C  
ATOM   3649  CD1 ILE B 181      72.279  42.378  34.582  1.00 63.22           C  
ANISOU 3649  CD1 ILE B 181     6419   9348   8254   -137    371  -1510       C  
ATOM   3650  N   GLN B 182      72.329  48.080  35.192  1.00 72.65           N  
ANISOU 3650  N   GLN B 182     7551   9786  10266  -1063    793  -2074       N  
ATOM   3651  CA  GLN B 182      72.902  49.247  35.859  1.00 79.88           C  
ANISOU 3651  CA  GLN B 182     8364  10660  11324  -1339    858  -2327       C  
ATOM   3652  C   GLN B 182      71.903  50.389  36.027  1.00 75.60           C  
ANISOU 3652  C   GLN B 182     7992   9746  10986  -1426    987  -2403       C  
ATOM   3653  O   GLN B 182      72.059  51.190  36.946  1.00 76.03           O  
ANISOU 3653  O   GLN B 182     8009   9766  11111  -1620   1015  -2665       O  
ATOM   3654  CB  GLN B 182      74.117  49.763  35.086  1.00 87.77           C  
ANISOU 3654  CB  GLN B 182     9208  11686  12453  -1514    956  -2301       C  
ATOM   3655  CG  GLN B 182      75.361  48.902  35.183  1.00 94.01           C  
ANISOU 3655  CG  GLN B 182     9765  12876  13077  -1493    845  -2305       C  
ATOM   3656  CD  GLN B 182      76.397  49.285  34.135  1.00108.61           C  
ANISOU 3656  CD  GLN B 182    11485  14724  15059  -1613    969  -2203       C  
ATOM   3657  OE1 GLN B 182      76.544  50.463  33.793  1.00112.76           O  
ANISOU 3657  OE1 GLN B 182    12019  15009  15816  -1829   1126  -2251       O  
ATOM   3658  NE2 GLN B 182      77.100  48.287  33.598  1.00112.50           N  
ANISOU 3658  NE2 GLN B 182    11864  15470  15411  -1464    919  -2052       N  
ATOM   3659  N   ASN B 183      70.895  50.505  35.156  1.00 76.96           N  
ANISOU 3659  N   ASN B 183     8346   9641  11254  -1288   1071  -2183       N  
ATOM   3660  CA  ASN B 183      69.911  51.583  35.231  1.00 79.07           C  
ANISOU 3660  CA  ASN B 183     8769   9542  11730  -1334   1208  -2217       C  
ATOM   3661  C   ASN B 183      68.551  51.113  35.748  1.00 77.67           C  
ANISOU 3661  C   ASN B 183     8734   9311  11466  -1136   1144  -2184       C  
ATOM   3662  O   ASN B 183      67.525  51.736  35.471  1.00 76.18           O  
ANISOU 3662  O   ASN B 183     8689   8823  11434  -1080   1250  -2101       O  
ATOM   3663  CB  ASN B 183      69.758  52.234  33.860  1.00 79.80           C  
ANISOU 3663  CB  ASN B 183     8948   9350  12022  -1331   1367  -1979       C  
ATOM   3664  CG  ASN B 183      71.088  52.664  33.286  1.00 86.46           C  
ANISOU 3664  CG  ASN B 183     9649  10245  12956  -1523   1450  -1984       C  
ATOM   3665  OD1 ASN B 183      72.081  52.725  34.004  1.00 88.68           O  
ANISOU 3665  OD1 ASN B 183     9763  10731  13202  -1700   1405  -2207       O  
ATOM   3666  ND2 ASN B 183      71.120  52.951  31.993  1.00 84.74           N  
ANISOU 3666  ND2 ASN B 183     9489   9863  12846  -1490   1569  -1735       N  
ATOM   3667  N   MET B 184      68.542  50.032  36.525  1.00 72.34           N  
ANISOU 3667  N   MET B 184     8010   8927  10549  -1028    980  -2243       N  
ATOM   3668  CA  MET B 184      67.326  49.296  36.862  1.00 70.11           C  
ANISOU 3668  CA  MET B 184     7844   8643  10153   -818    906  -2158       C  
ATOM   3669  C   MET B 184      66.534  49.939  37.995  1.00 76.42           C  
ANISOU 3669  C   MET B 184     8714   9318  11003   -861    956  -2362       C  
ATOM   3670  O   MET B 184      65.310  49.769  38.066  1.00 72.77           O  
ANISOU 3670  O   MET B 184     8370   8728  10552   -710    968  -2268       O  
ATOM   3671  CB  MET B 184      67.712  47.881  37.270  1.00 66.81           C  
ANISOU 3671  CB  MET B 184     7347   8576   9460   -690    731  -2134       C  
ATOM   3672  CG  MET B 184      66.826  46.804  36.811  1.00 63.48           C  
ANISOU 3672  CG  MET B 184     7026   8164   8930   -459    660  -1912       C  
ATOM   3673  SD  MET B 184      67.621  45.229  37.186  1.00 74.01           S  
ANISOU 3673  SD  MET B 184     8255   9890   9976   -335    488  -1884       S  
ATOM   3674  CE  MET B 184      67.733  45.252  38.969  1.00 77.71           C  
ANISOU 3674  CE  MET B 184     8655  10568  10305   -397    416  -2153       C  
ATOM   3675  N   ALA B 185      67.222  50.621  38.909  1.00 73.85           N  
ANISOU 3675  N   ALA B 185     8311   9053  10695  -1065    980  -2647       N  
ATOM   3676  CA  ALA B 185      66.617  51.064  40.162  1.00 71.54           C  
ANISOU 3676  CA  ALA B 185     8078   8720  10385  -1107   1008  -2885       C  
ATOM   3677  C   ALA B 185      65.310  51.847  40.025  1.00 77.25           C  
ANISOU 3677  C   ALA B 185     8968   9070  11313  -1038   1165  -2835       C  
ATOM   3678  O   ALA B 185      64.376  51.550  40.788  1.00 79.83           O  
ANISOU 3678  O   ALA B 185     9366   9413  11553   -918   1148  -2876       O  
ATOM   3679  CB  ALA B 185      67.661  51.882  40.934  1.00 65.42           C  
ANISOU 3679  CB  ALA B 185     7196   8025   9635  -1383   1033  -3210       C  
ATOM   3680  N   PRO B 186      65.152  52.811  39.105  1.00 73.98           N  
ANISOU 3680  N   PRO B 186     8618   8325  11165  -1089   1324  -2731       N  
ATOM   3681  CA  PRO B 186      63.864  53.536  39.025  1.00 66.00           C  
ANISOU 3681  CA  PRO B 186     7757   6970  10350   -991   1474  -2667       C  
ATOM   3682  C   PRO B 186      62.658  52.629  38.819  1.00 67.60           C  
ANISOU 3682  C   PRO B 186     8019   7211  10454   -727   1397  -2436       C  
ATOM   3683  O   PRO B 186      61.533  53.043  39.125  1.00 67.83           O  
ANISOU 3683  O   PRO B 186     8142   7043  10588   -630   1492  -2429       O  
ATOM   3684  CB  PRO B 186      64.056  54.478  37.828  1.00 64.25           C  
ANISOU 3684  CB  PRO B 186     7574   6442  10397  -1056   1630  -2508       C  
ATOM   3685  CG  PRO B 186      65.518  54.667  37.721  1.00 63.41           C  
ANISOU 3685  CG  PRO B 186     7343   6467  10282  -1283   1614  -2634       C  
ATOM   3686  CD  PRO B 186      66.138  53.357  38.148  1.00 65.61           C  
ANISOU 3686  CD  PRO B 186     7495   7181  10252  -1238   1395  -2667       C  
ATOM   3687  N   LEU B 187      62.847  51.418  38.277  1.00 67.98           N  
ANISOU 3687  N   LEU B 187     8015   7496  10317   -610   1238  -2246       N  
ATOM   3688  CA  LEU B 187      61.726  50.496  38.121  1.00 63.61           C  
ANISOU 3688  CA  LEU B 187     7513   6990   9666   -386   1157  -2048       C  
ATOM   3689  C   LEU B 187      61.178  50.035  39.458  1.00 70.96           C  
ANISOU 3689  C   LEU B 187     8452   8064  10446   -333   1110  -2209       C  
ATOM   3690  O   LEU B 187      60.056  49.517  39.507  1.00 70.13           O  
ANISOU 3690  O   LEU B 187     8395   7939  10312   -168   1088  -2078       O  
ATOM   3691  CB  LEU B 187      62.124  49.268  37.312  1.00 56.21           C  
ANISOU 3691  CB  LEU B 187     6530   6269   8557   -292   1006  -1845       C  
ATOM   3692  CG  LEU B 187      62.578  49.517  35.880  1.00 53.25           C  
ANISOU 3692  CG  LEU B 187     6156   5791   8285   -308   1042  -1645       C  
ATOM   3693  CD1 LEU B 187      62.890  48.202  35.193  1.00 51.55           C  
ANISOU 3693  CD1 LEU B 187     5914   5801   7873   -200    898  -1474       C  
ATOM   3694  CD2 LEU B 187      61.527  50.319  35.123  1.00 54.15           C  
ANISOU 3694  CD2 LEU B 187     6366   5594   8614   -232   1161  -1466       C  
ATOM   3695  N   PHE B 188      61.936  50.210  40.539  1.00 68.19           N  
ANISOU 3695  N   PHE B 188     8049   7870   9992   -474   1094  -2487       N  
ATOM   3696  CA  PHE B 188      61.485  49.726  41.828  1.00 70.71           C  
ANISOU 3696  CA  PHE B 188     8378   8360  10129   -420   1047  -2634       C  
ATOM   3697  C   PHE B 188      60.810  50.791  42.681  1.00 83.41           C  
ANISOU 3697  C   PHE B 188    10067   9763  11864   -472   1208  -2845       C  
ATOM   3698  O   PHE B 188      60.152  50.434  43.661  1.00 85.40           O  
ANISOU 3698  O   PHE B 188    10350  10114  11984   -392   1202  -2927       O  
ATOM   3699  CB  PHE B 188      62.659  49.081  42.555  1.00 67.44           C  
ANISOU 3699  CB  PHE B 188     7854   8303   9466   -506    905  -2790       C  
ATOM   3700  CG  PHE B 188      63.032  47.758  41.962  1.00 67.50           C  
ANISOU 3700  CG  PHE B 188     7804   8534   9310   -382    751  -2570       C  
ATOM   3701  CD1 PHE B 188      63.948  47.679  40.928  1.00 68.54           C  
ANISOU 3701  CD1 PHE B 188     7867   8688   9488   -432    719  -2460       C  
ATOM   3702  CD2 PHE B 188      62.402  46.595  42.386  1.00 63.82           C  
ANISOU 3702  CD2 PHE B 188     7363   8227   8659   -209    660  -2461       C  
ATOM   3703  CE1 PHE B 188      64.264  46.459  40.356  1.00 67.85           C  
ANISOU 3703  CE1 PHE B 188     7742   8784   9255   -306    597  -2266       C  
ATOM   3704  CE2 PHE B 188      62.713  45.376  41.827  1.00 63.65           C  
ANISOU 3704  CE2 PHE B 188     7308   8373   8504    -93    537  -2265       C  
ATOM   3705  CZ  PHE B 188      63.647  45.303  40.809  1.00 64.84           C  
ANISOU 3705  CZ  PHE B 188     7396   8545   8694   -137    506  -2174       C  
ATOM   3706  N   GLU B 189      60.902  52.069  42.295  1.00 90.26           N  
ANISOU 3706  N   GLU B 189    10977  10328  12988   -590   1369  -2917       N  
ATOM   3707  CA  GLU B 189      60.105  53.161  42.876  1.00 93.21           C  
ANISOU 3707  CA  GLU B 189    11453  10420  13541   -607   1564  -3074       C  
ATOM   3708  C   GLU B 189      60.198  53.214  44.400  1.00 91.20           C  
ANISOU 3708  C   GLU B 189    11210  10334  13109   -686   1565  -3404       C  
ATOM   3709  O   GLU B 189      59.242  53.604  45.084  1.00 91.73           O  
ANISOU 3709  O   GLU B 189    11363  10269  13221   -613   1690  -3497       O  
ATOM   3710  CB  GLU B 189      58.642  53.072  42.432  1.00 93.68           C  
ANISOU 3710  CB  GLU B 189    11582  10287  13723   -378   1634  -2826       C  
ATOM   3711  CG  GLU B 189      58.484  52.900  40.934  1.00 96.18           C  
ANISOU 3711  CG  GLU B 189    11888  10492  14165   -284   1604  -2488       C  
ATOM   3712  CD  GLU B 189      57.070  53.136  40.466  1.00101.28           C  
ANISOU 3712  CD  GLU B 189    12590  10909  14983    -88   1698  -2267       C  
ATOM   3713  OE1 GLU B 189      56.804  52.946  39.260  1.00101.50           O  
ANISOU 3713  OE1 GLU B 189    12609  10871  15087      7   1659  -1979       O  
ATOM   3714  OE2 GLU B 189      56.221  53.507  41.304  1.00105.85           O  
ANISOU 3714  OE2 GLU B 189    13216  11391  15612    -25   1810  -2379       O  
ATOM   3715  N   ASN B 190      61.352  52.820  44.936  1.00 84.84           N  
ANISOU 3715  N   ASN B 190    10309   9836  12090   -830   1428  -3579       N  
ATOM   3716  CA  ASN B 190      61.682  52.956  46.349  1.00 88.44           C  
ANISOU 3716  CA  ASN B 190    10761  10491  12352   -947   1411  -3918       C  
ATOM   3717  C   ASN B 190      60.809  52.099  47.259  1.00 86.94           C  
ANISOU 3717  C   ASN B 190    10607  10495  11932   -764   1362  -3894       C  
ATOM   3718  O   ASN B 190      60.755  52.343  48.475  1.00 86.75           O  
ANISOU 3718  O   ASN B 190    10618  10581  11760   -826   1395  -4168       O  
ATOM   3719  CB  ASN B 190      61.612  54.424  46.787  1.00 98.50           C  
ANISOU 3719  CB  ASN B 190    12128  11464  13833  -1121   1620  -4214       C  
ATOM   3720  CG  ASN B 190      62.821  55.219  46.332  1.00111.87           C  
ANISOU 3720  CG  ASN B 190    13759  13075  15673  -1383   1643  -4352       C  
ATOM   3721  OD1 ASN B 190      63.962  54.771  46.470  1.00114.60           O  
ANISOU 3721  OD1 ASN B 190    13968  13730  15844  -1513   1481  -4430       O  
ATOM   3722  ND2 ASN B 190      62.579  56.402  45.785  1.00117.27           N  
ANISOU 3722  ND2 ASN B 190    14534  13339  16683  -1458   1852  -4370       N  
ATOM   3723  N   VAL B 191      60.103  51.111  46.700  1.00 80.19           N  
ANISOU 3723  N   VAL B 191     9748   9680  11041   -548   1293  -3577       N  
ATOM   3724  CA  VAL B 191      59.302  50.216  47.525  1.00 78.98           C  
ANISOU 3724  CA  VAL B 191     9619   9713  10675   -382   1251  -3529       C  
ATOM   3725  C   VAL B 191      60.230  49.322  48.349  1.00 78.69           C  
ANISOU 3725  C   VAL B 191     9498  10100  10299   -422   1070  -3629       C  
ATOM   3726  O   VAL B 191      61.358  48.996  47.943  1.00 80.94           O  
ANISOU 3726  O   VAL B 191     9681  10556  10517   -505    937  -3607       O  
ATOM   3727  CB  VAL B 191      58.328  49.380  46.665  1.00 75.03           C  
ANISOU 3727  CB  VAL B 191     9129   9139  10239   -167   1221  -3168       C  
ATOM   3728  CG1 VAL B 191      57.515  50.287  45.768  1.00 77.63           C  
ANISOU 3728  CG1 VAL B 191     9517   9081  10896   -124   1379  -3047       C  
ATOM   3729  CG2 VAL B 191      59.063  48.301  45.828  1.00 65.23           C  
ANISOU 3729  CG2 VAL B 191     7804   8089   8893   -131   1035  -2950       C  
ATOM   3730  N   VAL B 192      59.764  48.940  49.517  1.00 75.22           N  
ANISOU 3730  N   VAL B 192     9096   9841   9644   -354   1071  -3730       N  
ATOM   3731  CA  VAL B 192      60.485  48.029  50.390  1.00 72.47           C  
ANISOU 3731  CA  VAL B 192     8676   9909   8951   -350    906  -3790       C  
ATOM   3732  C   VAL B 192      60.085  46.612  50.020  1.00 76.82           C  
ANISOU 3732  C   VAL B 192     9208  10587   9394   -140    801  -3460       C  
ATOM   3733  O   VAL B 192      58.908  46.330  49.758  1.00 84.72           O  
ANISOU 3733  O   VAL B 192    10276  11420  10495      7    881  -3276       O  
ATOM   3734  CB  VAL B 192      60.183  48.341  51.867  1.00 84.65           C  
ANISOU 3734  CB  VAL B 192    10282  11592  10291   -381    971  -4064       C  
ATOM   3735  CG1 VAL B 192      60.826  49.659  52.261  1.00 79.52           C  
ANISOU 3735  CG1 VAL B 192     9643  10859   9712   -626   1047  -4432       C  
ATOM   3736  CG2 VAL B 192      58.676  48.404  52.098  1.00 91.79           C  
ANISOU 3736  CG2 VAL B 192    11301  12288  11286   -222   1141  -3979       C  
ATOM   3737  N   ILE B 193      61.070  45.722  49.964  1.00 75.17           N  
ANISOU 3737  N   ILE B 193     8899  10666   8994   -129    626  -3381       N  
ATOM   3738  CA  ILE B 193      60.889  44.388  49.419  1.00 65.43           C  
ANISOU 3738  CA  ILE B 193     7650   9519   7692     50    528  -3068       C  
ATOM   3739  C   ILE B 193      61.303  43.384  50.479  1.00 69.83           C  
ANISOU 3739  C   ILE B 193     8168  10455   7908    131    410  -3069       C  
ATOM   3740  O   ILE B 193      62.474  43.335  50.871  1.00 74.86           O  
ANISOU 3740  O   ILE B 193     8704  11363   8378     50    294  -3191       O  
ATOM   3741  CB  ILE B 193      61.690  44.199  48.117  1.00 68.72           C  
ANISOU 3741  CB  ILE B 193     7992   9882   8236     22    449  -2919       C  
ATOM   3742  CG1 ILE B 193      61.074  45.058  47.006  1.00 73.86           C  
ANISOU 3742  CG1 ILE B 193     8700  10150   9213    -14    573  -2850       C  
ATOM   3743  CG2 ILE B 193      61.733  42.737  47.692  1.00 58.17           C  
ANISOU 3743  CG2 ILE B 193     6639   8683   6781    196    337  -2642       C  
ATOM   3744  CD1 ILE B 193      61.885  45.086  45.753  1.00 70.50           C  
ANISOU 3744  CD1 ILE B 193     8211   9663   8913    -65    523  -2735       C  
ATOM   3745  N   GLU B 194      60.351  42.582  50.931  1.00 73.72           N  
ANISOU 3745  N   GLU B 194     8733  10976   8301    293    441  -2920       N  
ATOM   3746  CA  GLU B 194      60.511  41.513  51.908  1.00 81.05           C  
ANISOU 3746  CA  GLU B 194     9651  12228   8915    411    357  -2855       C  
ATOM   3747  C   GLU B 194      60.759  40.189  51.192  1.00 73.89           C  
ANISOU 3747  C   GLU B 194     8717  11381   7979    555    253  -2556       C  
ATOM   3748  O   GLU B 194      60.133  39.911  50.166  1.00 77.30           O  
ANISOU 3748  O   GLU B 194     9191  11566   8613    612    291  -2366       O  
ATOM   3749  CB  GLU B 194      59.267  41.382  52.786  1.00 91.12           C  
ANISOU 3749  CB  GLU B 194    11030  13473  10118    505    481  -2846       C  
ATOM   3750  CG  GLU B 194      59.105  42.463  53.858  1.00108.90           C  
ANISOU 3750  CG  GLU B 194    13323  15762  12292    394    582  -3163       C  
ATOM   3751  CD  GLU B 194      60.114  42.338  54.987  1.00120.59           C  
ANISOU 3751  CD  GLU B 194    14746  17642  13429    342    466  -3346       C  
ATOM   3752  OE1 GLU B 194      60.451  41.196  55.365  1.00124.92           O  
ANISOU 3752  OE1 GLU B 194    15262  18464  13740    470    355  -3175       O  
ATOM   3753  OE2 GLU B 194      60.573  43.380  55.497  1.00124.09           O  
ANISOU 3753  OE2 GLU B 194    15179  18130  13839    172    486  -3659       O  
ATOM   3754  N   PRO B 195      61.679  39.374  51.689  1.00 69.58           N  
ANISOU 3754  N   PRO B 195     8100  11156   7183    618    123  -2512       N  
ATOM   3755  CA  PRO B 195      61.894  38.054  51.078  1.00 64.19           C  
ANISOU 3755  CA  PRO B 195     7408  10513   6467    775     46  -2227       C  
ATOM   3756  C   PRO B 195      60.653  37.182  51.233  1.00 61.99           C  
ANISOU 3756  C   PRO B 195     7247  10121   6187    923    126  -2020       C  
ATOM   3757  O   PRO B 195      60.082  37.085  52.321  1.00 62.36           O  
ANISOU 3757  O   PRO B 195     7343  10275   6076    968    182  -2057       O  
ATOM   3758  CB  PRO B 195      63.085  37.487  51.864  1.00 63.34           C  
ANISOU 3758  CB  PRO B 195     7195  10803   6067    823    -91  -2247       C  
ATOM   3759  CG  PRO B 195      63.713  38.689  52.570  1.00 64.19           C  
ANISOU 3759  CG  PRO B 195     7224  11066   6098    635   -114  -2573       C  
ATOM   3760  CD  PRO B 195      62.571  39.624  52.837  1.00 61.26           C  
ANISOU 3760  CD  PRO B 195     6967  10450   5858    552     41  -2721       C  
ATOM   3761  N   CYS B 196      60.231  36.553  50.133  1.00 54.34           N  
ANISOU 3761  N   CYS B 196     6319   8938   5391    989    135  -1807       N  
ATOM   3762  CA  CYS B 196      59.126  35.602  50.151  1.00 53.55           C  
ANISOU 3762  CA  CYS B 196     6314   8726   5306   1113    198  -1596       C  
ATOM   3763  C   CYS B 196      59.563  34.276  49.548  1.00 57.71           C  
ANISOU 3763  C   CYS B 196     6852   9280   5793   1236    123  -1365       C  
ATOM   3764  O   CYS B 196      60.268  34.250  48.536  1.00 58.55           O  
ANISOU 3764  O   CYS B 196     6919   9332   5996   1214     60  -1336       O  
ATOM   3765  CB  CYS B 196      57.924  36.130  49.360  1.00 60.24           C  
ANISOU 3765  CB  CYS B 196     7215   9247   6429   1062    298  -1565       C  
ATOM   3766  SG  CYS B 196      57.171  37.611  50.063  1.00 67.34           S  
ANISOU 3766  SG  CYS B 196     8124  10054   7409    956    431  -1805       S  
ATOM   3767  N   LEU B 197      59.116  33.174  50.148  1.00 59.52           N  
ANISOU 3767  N   LEU B 197     7147   9577   5892   1369    148  -1197       N  
ATOM   3768  CA  LEU B 197      59.337  31.864  49.543  1.00 56.95           C  
ANISOU 3768  CA  LEU B 197     6863   9211   5564   1490    110   -970       C  
ATOM   3769  C   LEU B 197      58.576  31.789  48.225  1.00 59.71           C  
ANISOU 3769  C   LEU B 197     7269   9246   6174   1443    143   -884       C  
ATOM   3770  O   LEU B 197      57.342  31.823  48.215  1.00 64.22           O  
ANISOU 3770  O   LEU B 197     7894   9648   6857   1418    226   -840       O  
ATOM   3771  CB  LEU B 197      58.906  30.724  50.481  1.00 51.46           C  
ANISOU 3771  CB  LEU B 197     6241   8615   4696   1634    156   -797       C  
ATOM   3772  CG  LEU B 197      59.174  29.278  50.017  1.00 51.98           C  
ANISOU 3772  CG  LEU B 197     6369   8635   4745   1776    137   -559       C  
ATOM   3773  CD1 LEU B 197      60.658  29.025  49.759  1.00 48.67           C  
ANISOU 3773  CD1 LEU B 197     5869   8399   4225   1847     27   -555       C  
ATOM   3774  CD2 LEU B 197      58.605  28.249  50.986  1.00 53.25           C  
ANISOU 3774  CD2 LEU B 197     6615   8854   4762   1904    213   -381       C  
ATOM   3775  N   LEU B 198      59.314  31.689  47.121  1.00 51.37           N  
ANISOU 3775  N   LEU B 198     6188   8129   5201   1432     78   -859       N  
ATOM   3776  CA  LEU B 198      58.787  31.585  45.772  1.00 49.81           C  
ANISOU 3776  CA  LEU B 198     6041   7672   5213   1390     86   -782       C  
ATOM   3777  C   LEU B 198      58.806  30.135  45.301  1.00 54.21           C  
ANISOU 3777  C   LEU B 198     6684   8169   5746   1503     76   -587       C  
ATOM   3778  O   LEU B 198      59.679  29.350  45.677  1.00 51.52           O  
ANISOU 3778  O   LEU B 198     6339   7985   5253   1620     43   -520       O  
ATOM   3779  CB  LEU B 198      59.608  32.436  44.795  1.00 50.05           C  
ANISOU 3779  CB  LEU B 198     6003   7670   5345   1300     37   -882       C  
ATOM   3780  CG  LEU B 198      59.797  33.904  45.149  1.00 48.91           C  
ANISOU 3780  CG  LEU B 198     5777   7563   5245   1173     54  -1088       C  
ATOM   3781  CD1 LEU B 198      60.563  34.617  44.050  1.00 46.32           C  
ANISOU 3781  CD1 LEU B 198     5392   7168   5038   1085     22  -1147       C  
ATOM   3782  CD2 LEU B 198      58.457  34.569  45.382  1.00 37.09           C  
ANISOU 3782  CD2 LEU B 198     4319   5899   3873   1116    142  -1126       C  
ATOM   3783  N   HIS B 199      57.809  29.775  44.492  1.00 52.01           N  
ANISOU 3783  N   HIS B 199     6482   7659   5621   1469    107   -497       N  
ATOM   3784  CA  HIS B 199      57.861  28.494  43.797  1.00 49.52           C  
ANISOU 3784  CA  HIS B 199     6261   7240   5314   1544     99   -347       C  
ATOM   3785  C   HIS B 199      58.983  28.497  42.768  1.00 51.78           C  
ANISOU 3785  C   HIS B 199     6528   7537   5609   1558     39   -368       C  
ATOM   3786  O   HIS B 199      59.774  27.550  42.700  1.00 52.43           O  
ANISOU 3786  O   HIS B 199     6644   7678   5599   1676     28   -286       O  
ATOM   3787  CB  HIS B 199      56.511  28.179  43.147  1.00 40.60           C  
ANISOU 3787  CB  HIS B 199     5205   5877   4345   1474    134   -272       C  
ATOM   3788  CG  HIS B 199      56.514  26.918  42.331  1.00 51.20           C  
ANISOU 3788  CG  HIS B 199     6658   7084   5710   1517    129   -151       C  
ATOM   3789  ND1 HIS B 199      57.042  26.857  41.058  1.00 46.38           N  
ANISOU 3789  ND1 HIS B 199     6075   6394   5151   1498     78   -166       N  
ATOM   3790  CD2 HIS B 199      56.083  25.664  42.620  1.00 53.08           C  
ANISOU 3790  CD2 HIS B 199     6998   7245   5925   1578    180    -21       C  
ATOM   3791  CE1 HIS B 199      56.905  25.630  40.586  1.00 47.23           C  
ANISOU 3791  CE1 HIS B 199     6302   6378   5264   1541     96    -67       C  
ATOM   3792  NE2 HIS B 199      56.339  24.884  41.517  1.00 49.19           N  
ANISOU 3792  NE2 HIS B 199     6598   6616   5477   1587    159     23       N  
ATOM   3793  N   GLY B 200      59.082  29.570  41.976  1.00 38.90           N  
ANISOU 3793  N   GLY B 200     4841   5850   4090   1448     12   -470       N  
ATOM   3794  CA  GLY B 200      60.220  29.800  41.104  1.00 40.04           C  
ANISOU 3794  CA  GLY B 200     4942   6036   4235   1448    -30   -506       C  
ATOM   3795  C   GLY B 200      60.079  29.314  39.669  1.00 45.37           C  
ANISOU 3795  C   GLY B 200     5704   6536   5000   1437    -38   -436       C  
ATOM   3796  O   GLY B 200      60.927  29.661  38.837  1.00 48.17           O  
ANISOU 3796  O   GLY B 200     6023   6911   5369   1422    -59   -469       O  
ATOM   3797  N   ASP B 201      59.051  28.521  39.350  1.00 40.65           N  
ANISOU 3797  N   ASP B 201     5217   5774   4453   1437    -21   -345       N  
ATOM   3798  CA  ASP B 201      58.852  28.024  37.988  1.00 47.99           C  
ANISOU 3798  CA  ASP B 201     6241   6546   5447   1412    -36   -296       C  
ATOM   3799  C   ASP B 201      57.388  27.664  37.765  1.00 45.44           C  
ANISOU 3799  C   ASP B 201     5991   6053   5219   1340    -31   -241       C  
ATOM   3800  O   ASP B 201      57.073  26.511  37.453  1.00 50.44           O  
ANISOU 3800  O   ASP B 201     6738   6584   5845   1367    -19   -169       O  
ATOM   3801  CB  ASP B 201      59.742  26.794  37.701  1.00 50.41           C  
ANISOU 3801  CB  ASP B 201     6629   6866   5657   1541    -21   -232       C  
ATOM   3802  CG  ASP B 201      59.725  26.374  36.205  1.00 57.52           C  
ANISOU 3802  CG  ASP B 201     7634   7622   6601   1512    -32   -217       C  
ATOM   3803  OD1 ASP B 201      59.488  27.232  35.310  1.00 58.03           O  
ANISOU 3803  OD1 ASP B 201     7671   7640   6737   1408    -65   -261       O  
ATOM   3804  OD2 ASP B 201      59.927  25.175  35.918  1.00 60.42           O  
ANISOU 3804  OD2 ASP B 201     8118   7915   6925   1596      0   -160       O  
ATOM   3805  N   LEU B 202      56.484  28.627  37.933  1.00 43.94           N  
ANISOU 3805  N   LEU B 202     5733   5832   5130   1247    -33   -274       N  
ATOM   3806  CA  LEU B 202      55.054  28.342  38.075  1.00 46.80           C  
ANISOU 3806  CA  LEU B 202     6119   6082   5582   1187    -19   -217       C  
ATOM   3807  C   LEU B 202      54.328  28.541  36.740  1.00 48.30           C  
ANISOU 3807  C   LEU B 202     6329   6144   5880   1091    -75   -196       C  
ATOM   3808  O   LEU B 202      54.013  29.667  36.349  1.00 48.61           O  
ANISOU 3808  O   LEU B 202     6291   6171   6007   1033    -95   -225       O  
ATOM   3809  CB  LEU B 202      54.476  29.209  39.184  1.00 42.56           C  
ANISOU 3809  CB  LEU B 202     5486   5604   5080   1168     28   -258       C  
ATOM   3810  CG  LEU B 202      53.094  28.802  39.676  1.00 56.76           C  
ANISOU 3810  CG  LEU B 202     7289   7328   6951   1133     71   -188       C  
ATOM   3811  CD1 LEU B 202      53.081  27.338  40.183  1.00 46.92           C  
ANISOU 3811  CD1 LEU B 202     6141   6067   5622   1194    109    -97       C  
ATOM   3812  CD2 LEU B 202      52.649  29.765  40.764  1.00 55.61           C  
ANISOU 3812  CD2 LEU B 202     7049   7252   6827   1130    135   -246       C  
ATOM   3813  N   TRP B 203      54.069  27.438  36.039  1.00 44.86           N  
ANISOU 3813  N   TRP B 203     6000   5612   5434   1076    -99   -145       N  
ATOM   3814  CA  TRP B 203      53.309  27.443  34.801  1.00 42.08           C  
ANISOU 3814  CA  TRP B 203     5674   5160   5153    977   -167   -126       C  
ATOM   3815  C   TRP B 203      52.369  26.234  34.799  1.00 47.87           C  
ANISOU 3815  C   TRP B 203     6486   5787   5917    923   -165    -73       C  
ATOM   3816  O   TRP B 203      52.319  25.466  35.764  1.00 54.30           O  
ANISOU 3816  O   TRP B 203     7336   6589   6705    969    -96    -38       O  
ATOM   3817  CB  TRP B 203      54.251  27.479  33.595  1.00 38.64           C  
ANISOU 3817  CB  TRP B 203     5301   4730   4652    991   -207   -157       C  
ATOM   3818  CG  TRP B 203      55.020  26.211  33.395  1.00 43.98           C  
ANISOU 3818  CG  TRP B 203     6111   5374   5225   1061   -179   -157       C  
ATOM   3819  CD1 TRP B 203      56.088  25.779  34.115  1.00 42.95           C  
ANISOU 3819  CD1 TRP B 203     5998   5314   5008   1185   -119   -160       C  
ATOM   3820  CD2 TRP B 203      54.778  25.213  32.390  1.00 43.40           C  
ANISOU 3820  CD2 TRP B 203     6176   5189   5126   1019   -206   -156       C  
ATOM   3821  NE1 TRP B 203      56.520  24.566  33.639  1.00 48.24           N  
ANISOU 3821  NE1 TRP B 203     6809   5906   5614   1241    -93   -146       N  
ATOM   3822  CE2 TRP B 203      55.738  24.195  32.578  1.00 47.57           C  
ANISOU 3822  CE2 TRP B 203     6811   5699   5565   1133   -140   -157       C  
ATOM   3823  CE3 TRP B 203      53.843  25.087  31.345  1.00 38.95           C  
ANISOU 3823  CE3 TRP B 203     5653   4547   4601    894   -283   -159       C  
ATOM   3824  CZ2 TRP B 203      55.801  23.062  31.758  1.00 52.30           C  
ANISOU 3824  CZ2 TRP B 203     7574   6175   6121   1127   -128   -174       C  
ATOM   3825  CZ3 TRP B 203      53.892  23.955  30.532  1.00 45.56           C  
ANISOU 3825  CZ3 TRP B 203     6649   5283   5379    867   -289   -189       C  
ATOM   3826  CH2 TRP B 203      54.874  22.957  30.742  1.00 52.75           C  
ANISOU 3826  CH2 TRP B 203     7683   6149   6211    984   -202   -202       C  
ATOM   3827  N   SER B 204      51.618  26.067  33.696  1.00 46.85           N  
ANISOU 3827  N   SER B 204     6382   5582   5837    816   -241    -65       N  
ATOM   3828  CA  SER B 204      50.515  25.097  33.642  1.00 50.36           C  
ANISOU 3828  CA  SER B 204     6867   5925   6341    718   -252    -28       C  
ATOM   3829  C   SER B 204      50.967  23.669  33.947  1.00 53.26           C  
ANISOU 3829  C   SER B 204     7390   6203   6644    760   -183    -21       C  
ATOM   3830  O   SER B 204      50.246  22.919  34.611  1.00 57.90           O  
ANISOU 3830  O   SER B 204     7996   6718   7287    720   -130     27       O  
ATOM   3831  CB  SER B 204      49.836  25.146  32.263  1.00 44.95           C  
ANISOU 3831  CB  SER B 204     6188   5206   5685    593   -367    -39       C  
ATOM   3832  OG  SER B 204      48.939  26.233  32.204  1.00 61.18           O  
ANISOU 3832  OG  SER B 204     8082   7319   7844    545   -417     -1       O  
ATOM   3833  N   GLY B 205      52.138  23.267  33.452  1.00 51.35           N  
ANISOU 3833  N   GLY B 205     7261   5954   6296    845   -171    -60       N  
ATOM   3834  CA  GLY B 205      52.664  21.924  33.678  1.00 52.59           C  
ANISOU 3834  CA  GLY B 205     7575   6009   6397    915    -92    -46       C  
ATOM   3835  C   GLY B 205      53.024  21.601  35.118  1.00 51.55           C  
ANISOU 3835  C   GLY B 205     7430   5918   6240   1040     11     25       C  
ATOM   3836  O   GLY B 205      53.320  20.439  35.416  1.00 59.99           O  
ANISOU 3836  O   GLY B 205     8628   6886   7280   1108     91     68       O  
ATOM   3837  N   ASN B 206      53.045  22.593  36.005  1.00 49.86           N  
ANISOU 3837  N   ASN B 206     7073   5847   6026   1081     16     38       N  
ATOM   3838  CA  ASN B 206      53.433  22.391  37.395  1.00 50.66           C  
ANISOU 3838  CA  ASN B 206     7152   6029   6066   1203    101     98       C  
ATOM   3839  C   ASN B 206      52.277  22.571  38.361  1.00 53.36           C  
ANISOU 3839  C   ASN B 206     7415   6377   6481   1141    144    151       C  
ATOM   3840  O   ASN B 206      52.505  22.601  39.574  1.00 54.06           O  
ANISOU 3840  O   ASN B 206     7471   6565   6503   1236    211    196       O  
ATOM   3841  CB  ASN B 206      54.550  23.361  37.770  1.00 47.94           C  
ANISOU 3841  CB  ASN B 206     6710   5873   5631   1306     83     50       C  
ATOM   3842  CG  ASN B 206      55.834  22.981  37.158  1.00 61.77           C  
ANISOU 3842  CG  ASN B 206     8529   7646   7295   1408     78     29       C  
ATOM   3843  OD1 ASN B 206      56.023  21.823  36.801  1.00 69.38           O  
ANISOU 3843  OD1 ASN B 206     9631   8489   8241   1454    119     68       O  
ATOM   3844  ND2 ASN B 206      56.750  23.926  37.050  1.00 63.66           N  
ANISOU 3844  ND2 ASN B 206     8672   8031   7486   1447     43    -33       N  
ATOM   3845  N   ILE B 207      51.055  22.720  37.853  1.00 49.05           N  
ANISOU 3845  N   ILE B 207     6829   5747   6061    990    106    147       N  
ATOM   3846  CA  ILE B 207      49.878  22.995  38.663  1.00 50.69           C  
ANISOU 3846  CA  ILE B 207     6935   5967   6358    925    151    196       C  
ATOM   3847  C   ILE B 207      48.865  21.886  38.426  1.00 54.19           C  
ANISOU 3847  C   ILE B 207     7443   6248   6899    804    178    255       C  
ATOM   3848  O   ILE B 207      48.699  21.417  37.297  1.00 60.58           O  
ANISOU 3848  O   ILE B 207     8322   6950   7745    706    109    216       O  
ATOM   3849  CB  ILE B 207      49.270  24.379  38.332  1.00 50.04           C  
ANISOU 3849  CB  ILE B 207     6695   5955   6362    856     86    146       C  
ATOM   3850  CG1 ILE B 207      50.283  25.501  38.575  1.00 50.34           C  
ANISOU 3850  CG1 ILE B 207     6676   6129   6321    953     73     74       C  
ATOM   3851  CG2 ILE B 207      48.047  24.646  39.160  1.00 48.69           C  
ANISOU 3851  CG2 ILE B 207     6411   5798   6291    805    150    198       C  
ATOM   3852  CD1 ILE B 207      49.893  26.824  37.930  1.00 44.92           C  
ANISOU 3852  CD1 ILE B 207     5873   5468   5728    894      8     25       C  
ATOM   3853  N   ALA B 208      48.200  21.459  39.497  1.00 56.92           N  
ANISOU 3853  N   ALA B 208     7769   6580   7279    801    285    343       N  
ATOM   3854  CA  ALA B 208      47.205  20.404  39.426  1.00 49.92           C  
ANISOU 3854  CA  ALA B 208     6931   5535   6501    671    333    407       C  
ATOM   3855  C   ALA B 208      46.178  20.642  40.522  1.00 54.46           C  
ANISOU 3855  C   ALA B 208     7382   6161   7147    642    430    489       C  
ATOM   3856  O   ALA B 208      46.343  21.513  41.378  1.00 55.03           O  
ANISOU 3856  O   ALA B 208     7364   6383   7161    740    468    490       O  
ATOM   3857  CB  ALA B 208      47.849  19.018  39.560  1.00 52.63           C  
ANISOU 3857  CB  ALA B 208     7474   5737   6788    735    418    461       C  
ATOM   3858  N   TYR B 209      45.112  19.846  40.493  1.00 55.75           N  
ANISOU 3858  N   TYR B 209     7545   6199   7439    496    478    550       N  
ATOM   3859  CA  TYR B 209      44.032  19.937  41.462  1.00 52.91           C  
ANISOU 3859  CA  TYR B 209     7063   5874   7165    450    588    641       C  
ATOM   3860  C   TYR B 209      43.709  18.552  42.006  1.00 59.00           C  
ANISOU 3860  C   TYR B 209     7952   6489   7974    404    727    757       C  
ATOM   3861  O   TYR B 209      43.645  17.580  41.250  1.00 61.94           O  
ANISOU 3861  O   TYR B 209     8442   6683   8408    294    705    742       O  
ATOM   3862  CB  TYR B 209      42.798  20.590  40.817  1.00 52.07           C  
ANISOU 3862  CB  TYR B 209     6768   5794   7223    288    503    611       C  
ATOM   3863  CG  TYR B 209      43.044  22.048  40.500  1.00 54.03           C  
ANISOU 3863  CG  TYR B 209     6895   6190   7446    359    406    530       C  
ATOM   3864  CD1 TYR B 209      43.703  22.427  39.335  1.00 56.64           C  
ANISOU 3864  CD1 TYR B 209     7267   6521   7733    359    259    437       C  
ATOM   3865  CD2 TYR B 209      42.650  23.047  41.388  1.00 50.23           C  
ANISOU 3865  CD2 TYR B 209     6269   5834   6980    433    480    548       C  
ATOM   3866  CE1 TYR B 209      43.950  23.770  39.056  1.00 55.00           C  
ANISOU 3866  CE1 TYR B 209     6957   6428   7513    425    189    378       C  
ATOM   3867  CE2 TYR B 209      42.881  24.378  41.124  1.00 47.78           C  
ANISOU 3867  CE2 TYR B 209     5864   5625   6664    497    413    473       C  
ATOM   3868  CZ  TYR B 209      43.538  24.738  39.958  1.00 55.10           C  
ANISOU 3868  CZ  TYR B 209     6833   6542   7562    491    268    395       C  
ATOM   3869  OH  TYR B 209      43.787  26.068  39.700  1.00 60.32           O  
ANISOU 3869  OH  TYR B 209     7407   7283   8227    554    218    334       O  
ATOM   3870  N   ASP B 210      43.502  18.461  43.320  1.00 58.48           N  
ANISOU 3870  N   ASP B 210     7867   6485   7870    487    881    870       N  
ATOM   3871  CA  ASP B 210      43.286  17.167  43.951  1.00 59.79           C  
ANISOU 3871  CA  ASP B 210     8157   6503   8060    470   1040   1009       C  
ATOM   3872  C   ASP B 210      41.783  16.876  44.014  1.00 68.45           C  
ANISOU 3872  C   ASP B 210     9131   7523   9355    262   1108   1069       C  
ATOM   3873  O   ASP B 210      40.970  17.588  43.419  1.00 70.51           O  
ANISOU 3873  O   ASP B 210     9215   7842   9733    134   1009    998       O  
ATOM   3874  CB  ASP B 210      43.988  17.126  45.317  1.00 54.57           C  
ANISOU 3874  CB  ASP B 210     7558   5959   7216    686   1171   1118       C  
ATOM   3875  CG  ASP B 210      43.331  18.025  46.371  1.00 63.32           C  
ANISOU 3875  CG  ASP B 210     8501   7257   8300    721   1253   1152       C  
ATOM   3876  OD1 ASP B 210      42.259  18.605  46.122  1.00 69.17           O  
ANISOU 3876  OD1 ASP B 210     9074   8018   9188    585   1234   1116       O  
ATOM   3877  OD2 ASP B 210      43.899  18.155  47.473  1.00 69.73           O  
ANISOU 3877  OD2 ASP B 210     9350   8209   8935    893   1340   1216       O  
ATOM   3878  N   LYS B 211      41.400  15.839  44.768  1.00 78.51           N  
ANISOU 3878  N   LYS B 211    10485   8675  10671    233   1285   1217       N  
ATOM   3879  CA  LYS B 211      40.011  15.378  44.778  1.00 83.56           C  
ANISOU 3879  CA  LYS B 211    11015   9216  11518      9   1363   1280       C  
ATOM   3880  C   LYS B 211      39.063  16.392  45.415  1.00 80.89           C  
ANISOU 3880  C   LYS B 211    10432   9072  11232     -2   1406   1308       C  
ATOM   3881  O   LYS B 211      37.882  16.428  45.058  1.00 80.66           O  
ANISOU 3881  O   LYS B 211    10233   9023  11392   -197   1393   1308       O  
ATOM   3882  CB  LYS B 211      39.901  14.022  45.483  1.00 93.14           C  
ANISOU 3882  CB  LYS B 211    12387  10236  12765    -11   1568   1447       C  
ATOM   3883  CG  LYS B 211      40.209  14.034  46.978  1.00101.46           C  
ANISOU 3883  CG  LYS B 211    13478  11406  13665    195   1754   1612       C  
ATOM   3884  CD  LYS B 211      40.052  12.641  47.583  1.00105.90           C  
ANISOU 3884  CD  LYS B 211    14206  11753  14278    169   1965   1802       C  
ATOM   3885  CE  LYS B 211      40.432  12.637  49.052  1.00110.78           C  
ANISOU 3885  CE  LYS B 211    14874  12511  14706    395   2141   1982       C  
ATOM   3886  NZ  LYS B 211      41.860  13.003  49.252  1.00112.51           N  
ANISOU 3886  NZ  LYS B 211    15200  12874  14676    660   2057   1948       N  
ATOM   3887  N   ASN B 212      39.541  17.196  46.368  1.00 78.39           N  
ANISOU 3887  N   ASN B 212    10089   8944  10751    203   1464   1328       N  
ATOM   3888  CA  ASN B 212      38.756  18.293  46.930  1.00 73.69           C  
ANISOU 3888  CA  ASN B 212     9276   8532  10190    221   1508   1324       C  
ATOM   3889  C   ASN B 212      38.816  19.552  46.077  1.00 74.25           C  
ANISOU 3889  C   ASN B 212     9214   8712  10288    226   1321   1167       C  
ATOM   3890  O   ASN B 212      38.435  20.624  46.558  1.00 66.39           O  
ANISOU 3890  O   ASN B 212     8066   7869   9290    295   1356   1142       O  
ATOM   3891  CB  ASN B 212      39.239  18.629  48.341  1.00 75.15           C  
ANISOU 3891  CB  ASN B 212     9506   8875  10174    431   1657   1393       C  
ATOM   3892  CG  ASN B 212      39.388  17.405  49.206  1.00 86.86           C  
ANISOU 3892  CG  ASN B 212    11150  10266  11588    471   1839   1571       C  
ATOM   3893  OD1 ASN B 212      38.446  16.632  49.374  1.00 85.73           O  
ANISOU 3893  OD1 ASN B 212    10975  10000  11597    327   1968   1691       O  
ATOM   3894  ND2 ASN B 212      40.591  17.196  49.733  1.00 94.54           N  
ANISOU 3894  ND2 ASN B 212    12291  11294  12336    666   1851   1599       N  
ATOM   3895  N   ASN B 213      39.314  19.446  44.842  1.00 76.49           N  
ANISOU 3895  N   ASN B 213     9562   8913  10587    166   1139   1064       N  
ATOM   3896  CA  ASN B 213      39.488  20.584  43.945  1.00 72.74           C  
ANISOU 3896  CA  ASN B 213     8987   8528  10122    180    962    932       C  
ATOM   3897  C   ASN B 213      40.326  21.693  44.572  1.00 65.37           C  
ANISOU 3897  C   ASN B 213     8055   7754   9028    383    972    871       C  
ATOM   3898  O   ASN B 213      40.117  22.874  44.297  1.00 67.31           O  
ANISOU 3898  O   ASN B 213     8164   8095   9314    409    906    797       O  
ATOM   3899  CB  ASN B 213      38.135  21.120  43.481  1.00 83.78           C  
ANISOU 3899  CB  ASN B 213    10142   9967  11722     35    917    937       C  
ATOM   3900  CG  ASN B 213      37.433  20.160  42.544  1.00 99.41           C  
ANISOU 3900  CG  ASN B 213    12108  11811  13852   -197    839    948       C  
ATOM   3901  OD1 ASN B 213      37.654  20.190  41.333  1.00104.90           O  
ANISOU 3901  OD1 ASN B 213    12828  12472  14556   -273    659    855       O  
ATOM   3902  ND2 ASN B 213      36.582  19.301  43.099  1.00104.37           N  
ANISOU 3902  ND2 ASN B 213    12699  12364  14593   -319    979   1055       N  
ATOM   3903  N   GLU B 214      41.300  21.320  45.382  1.00 59.72           N  
ANISOU 3903  N   GLU B 214     7495   7066   8131    527   1051    899       N  
ATOM   3904  CA  GLU B 214      42.291  22.238  45.922  1.00 55.54           C  
ANISOU 3904  CA  GLU B 214     6989   6691   7423    702   1039    819       C  
ATOM   3905  C   GLU B 214      43.550  22.198  45.077  1.00 56.20           C  
ANISOU 3905  C   GLU B 214     7194   6748   7412    754    893    730       C  
ATOM   3906  O   GLU B 214      43.906  21.143  44.548  1.00 58.26           O  
ANISOU 3906  O   GLU B 214     7587   6876   7672    718    865    765       O  
ATOM   3907  CB  GLU B 214      42.640  21.886  47.371  1.00 59.75           C  
ANISOU 3907  CB  GLU B 214     7601   7317   7786    837   1202    907       C  
ATOM   3908  CG  GLU B 214      41.502  22.215  48.343  1.00 65.90           C  
ANISOU 3908  CG  GLU B 214     8249   8169   8621    820   1366    974       C  
ATOM   3909  CD  GLU B 214      41.240  23.718  48.411  1.00 75.67           C  
ANISOU 3909  CD  GLU B 214     9334   9532   9884    857   1343    849       C  
ATOM   3910  OE1 GLU B 214      42.191  24.481  48.692  1.00 78.72           O  
ANISOU 3910  OE1 GLU B 214     9761  10033  10114    974   1300    737       O  
ATOM   3911  OE2 GLU B 214      40.094  24.142  48.154  1.00 78.94           O  
ANISOU 3911  OE2 GLU B 214     9584   9925  10485    766   1369    860       O  
ATOM   3912  N   PRO B 215      44.228  23.339  44.931  1.00 55.74           N  
ANISOU 3912  N   PRO B 215     7093   6805   7281    834    812    611       N  
ATOM   3913  CA  PRO B 215      45.424  23.389  44.075  1.00 48.98           C  
ANISOU 3913  CA  PRO B 215     6329   5937   6345    878    680    527       C  
ATOM   3914  C   PRO B 215      46.623  22.679  44.690  1.00 56.44           C  
ANISOU 3914  C   PRO B 215     7421   6923   7099   1018    719    563       C  
ATOM   3915  O   PRO B 215      46.805  22.644  45.907  1.00 59.56           O  
ANISOU 3915  O   PRO B 215     7828   7432   7371   1120    823    614       O  
ATOM   3916  CB  PRO B 215      45.696  24.890  43.927  1.00 44.75           C  
ANISOU 3916  CB  PRO B 215     5686   5515   5803    916    617    403       C  
ATOM   3917  CG  PRO B 215      45.104  25.496  45.157  1.00 49.51           C  
ANISOU 3917  CG  PRO B 215     6198   6223   6391    962    747    413       C  
ATOM   3918  CD  PRO B 215      43.883  24.657  45.491  1.00 50.14           C  
ANISOU 3918  CD  PRO B 215     6246   6226   6581    878    851    544       C  
ATOM   3919  N   VAL B 216      47.457  22.120  43.815  1.00 51.72           N  
ANISOU 3919  N   VAL B 216     6933   6245   6471   1031    634    541       N  
ATOM   3920  CA  VAL B 216      48.706  21.465  44.180  1.00 45.66           C  
ANISOU 3920  CA  VAL B 216     6294   5517   5539   1181    653    577       C  
ATOM   3921  C   VAL B 216      49.769  21.949  43.210  1.00 49.15           C  
ANISOU 3921  C   VAL B 216     6748   5990   5937   1214    524    463       C  
ATOM   3922  O   VAL B 216      49.530  21.984  41.997  1.00 54.06           O  
ANISOU 3922  O   VAL B 216     7376   6501   6664   1108    439    408       O  
ATOM   3923  CB  VAL B 216      48.575  19.929  44.112  1.00 50.02           C  
ANISOU 3923  CB  VAL B 216     6998   5886   6122   1173    730    704       C  
ATOM   3924  CG1 VAL B 216      49.852  19.250  44.594  1.00 49.54           C  
ANISOU 3924  CG1 VAL B 216     7059   5873   5891   1364    766    771       C  
ATOM   3925  CG2 VAL B 216      47.351  19.442  44.920  1.00 44.70           C  
ANISOU 3925  CG2 VAL B 216     6300   5152   5532   1098    867    825       C  
ATOM   3926  N   ILE B 217      50.935  22.326  43.720  1.00 45.36           N  
ANISOU 3926  N   ILE B 217     6263   5673   5297   1354    509    428       N  
ATOM   3927  CA  ILE B 217      51.999  22.769  42.823  1.00 48.06           C  
ANISOU 3927  CA  ILE B 217     6605   6052   5602   1384    403    329       C  
ATOM   3928  C   ILE B 217      53.220  21.864  42.974  1.00 55.04           C  
ANISOU 3928  C   ILE B 217     7593   6966   6352   1540    419    390       C  
ATOM   3929  O   ILE B 217      53.477  21.307  44.045  1.00 51.56           O  
ANISOU 3929  O   ILE B 217     7186   6604   5799   1658    496    491       O  
ATOM   3930  CB  ILE B 217      52.352  24.251  43.046  1.00 45.04           C  
ANISOU 3930  CB  ILE B 217     6090   5839   5186   1383    351    204       C  
ATOM   3931  CG1 ILE B 217      52.795  24.508  44.484  1.00 45.65           C  
ANISOU 3931  CG1 ILE B 217     6127   6115   5102   1492    408    208       C  
ATOM   3932  CG2 ILE B 217      51.131  25.141  42.697  1.00 41.24           C  
ANISOU 3932  CG2 ILE B 217     5510   5295   4866   1245    339    156       C  
ATOM   3933  CD1 ILE B 217      53.064  25.993  44.722  1.00 46.10           C  
ANISOU 3933  CD1 ILE B 217     6062   6313   5141   1464    369     57       C  
ATOM   3934  N   LEU B 218      53.968  21.721  41.874  1.00 54.77           N  
ANISOU 3934  N   LEU B 218     7608   6876   6327   1550    353    338       N  
ATOM   3935  CA  LEU B 218      54.984  20.684  41.703  1.00 57.11           C  
ANISOU 3935  CA  LEU B 218     8020   7138   6543   1691    381    403       C  
ATOM   3936  C   LEU B 218      56.246  21.271  41.084  1.00 55.79           C  
ANISOU 3936  C   LEU B 218     7800   7091   6306   1757    303    312       C  
ATOM   3937  O   LEU B 218      56.266  22.409  40.603  1.00 52.12           O  
ANISOU 3937  O   LEU B 218     7233   6694   5876   1668    227    198       O  
ATOM   3938  CB  LEU B 218      54.481  19.545  40.797  1.00 60.26           C  
ANISOU 3938  CB  LEU B 218     8575   7273   7049   1623    416    441       C  
ATOM   3939  CG  LEU B 218      53.062  19.016  40.998  1.00 62.53           C  
ANISOU 3939  CG  LEU B 218     8902   7396   7461   1485    477    502       C  
ATOM   3940  CD1 LEU B 218      52.542  18.352  39.744  1.00 58.56           C  
ANISOU 3940  CD1 LEU B 218     8508   6663   7077   1346    455    457       C  
ATOM   3941  CD2 LEU B 218      53.071  18.040  42.144  1.00 59.29           C  
ANISOU 3941  CD2 LEU B 218     8571   6961   6995   1602    607    661       C  
ATOM   3942  N   ASP B 219      57.308  20.469  41.094  1.00 58.04           N  
ANISOU 3942  N   ASP B 219     8153   7397   6502   1920    334    375       N  
ATOM   3943  CA  ASP B 219      58.543  20.765  40.374  1.00 59.40           C  
ANISOU 3943  CA  ASP B 219     8288   7659   6622   1992    282    308       C  
ATOM   3944  C   ASP B 219      59.105  22.161  40.659  1.00 60.99           C  
ANISOU 3944  C   ASP B 219     8309   8096   6769   1966    203    201       C  
ATOM   3945  O   ASP B 219      59.323  22.943  39.733  1.00 62.68           O  
ANISOU 3945  O   ASP B 219     8473   8308   7035   1878    145     98       O  
ATOM   3946  CB  ASP B 219      58.325  20.600  38.876  1.00 57.27           C  
ANISOU 3946  CB  ASP B 219     8108   7199   6452   1889    258    239       C  
ATOM   3947  CG  ASP B 219      57.889  19.220  38.502  1.00 70.61           C  
ANISOU 3947  CG  ASP B 219     9987   8647   8196   1900    337    310       C  
ATOM   3948  OD1 ASP B 219      58.549  18.252  38.932  1.00 78.08           O  
ANISOU 3948  OD1 ASP B 219    11014   9571   9081   2073    418    411       O  
ATOM   3949  OD2 ASP B 219      56.885  19.114  37.765  1.00 78.69           O  
ANISOU 3949  OD2 ASP B 219    11074   9500   9325   1733    317    263       O  
ATOM   3950  N   PRO B 220      59.389  22.481  41.917  1.00 60.81           N  
ANISOU 3950  N   PRO B 220     8193   8277   6635   2038    204    222       N  
ATOM   3951  CA  PRO B 220      59.800  23.848  42.243  1.00 61.33           C  
ANISOU 3951  CA  PRO B 220     8096   8545   6661   1977    136     94       C  
ATOM   3952  C   PRO B 220      61.220  24.161  41.797  1.00 60.25           C  
ANISOU 3952  C   PRO B 220     7870   8558   6463   2045     85     39       C  
ATOM   3953  O   PRO B 220      62.011  23.283  41.452  1.00 66.34           O  
ANISOU 3953  O   PRO B 220     8690   9324   7192   2182    107    117       O  
ATOM   3954  CB  PRO B 220      59.684  23.884  43.767  1.00 59.69           C  
ANISOU 3954  CB  PRO B 220     7839   8517   6324   2043    160    135       C  
ATOM   3955  CG  PRO B 220      59.942  22.473  44.174  1.00 60.07           C  
ANISOU 3955  CG  PRO B 220     7994   8539   6293   2216    224    311       C  
ATOM   3956  CD  PRO B 220      59.274  21.644  43.123  1.00 57.49           C  
ANISOU 3956  CD  PRO B 220     7818   7910   6115   2165    273    362       C  
ATOM   3957  N   ALA B 221      61.514  25.463  41.776  1.00 54.71           N  
ANISOU 3957  N   ALA B 221     7036   7978   5775   1942     29    -98       N  
ATOM   3958  CA  ALA B 221      62.867  26.010  41.725  1.00 51.94           C  
ANISOU 3958  CA  ALA B 221     6547   7835   5352   1979    -21   -169       C  
ATOM   3959  C   ALA B 221      62.990  27.102  42.796  1.00 56.05           C  
ANISOU 3959  C   ALA B 221     6929   8566   5803   1909    -62   -286       C  
ATOM   3960  O   ALA B 221      63.252  28.268  42.499  1.00 57.80           O  
ANISOU 3960  O   ALA B 221     7052   8825   6084   1782    -94   -425       O  
ATOM   3961  CB  ALA B 221      63.176  26.551  40.328  1.00 49.97           C  
ANISOU 3961  CB  ALA B 221     6287   7483   5216   1888    -36   -238       C  
ATOM   3962  N   CYS B 222      62.799  26.712  44.060  1.00 57.24           N  
ANISOU 3962  N   CYS B 222     7081   8848   5821   1990    -51   -233       N  
ATOM   3963  CA  CYS B 222      62.490  27.667  45.125  1.00 56.12           C  
ANISOU 3963  CA  CYS B 222     6858   8851   5614   1905    -66   -352       C  
ATOM   3964  C   CYS B 222      63.641  28.605  45.446  1.00 53.04           C  
ANISOU 3964  C   CYS B 222     6296   8715   5140   1860   -141   -501       C  
ATOM   3965  O   CYS B 222      64.812  28.263  45.312  1.00 56.21           O  
ANISOU 3965  O   CYS B 222     6613   9279   5463   1953   -188   -468       O  
ATOM   3966  CB  CYS B 222      62.113  26.957  46.429  1.00 57.25           C  
ANISOU 3966  CB  CYS B 222     7046   9110   5597   2019    -32   -248       C  
ATOM   3967  SG  CYS B 222      60.569  26.053  46.439  1.00 63.36           S  
ANISOU 3967  SG  CYS B 222     7997   9613   6465   2027     74    -97       S  
ATOM   3968  N   TYR B 223      63.274  29.783  45.940  1.00 53.42           N  
ANISOU 3968  N   TYR B 223     6289   8801   5207   1714   -145   -669       N  
ATOM   3969  CA  TYR B 223      64.176  30.685  46.644  1.00 54.48           C  
ANISOU 3969  CA  TYR B 223     6269   9200   5230   1648   -209   -838       C  
ATOM   3970  C   TYR B 223      63.326  31.783  47.273  1.00 51.57           C  
ANISOU 3970  C   TYR B 223     5910   8787   4898   1502   -169  -1005       C  
ATOM   3971  O   TYR B 223      62.117  31.863  47.049  1.00 51.09           O  
ANISOU 3971  O   TYR B 223     5953   8495   4962   1464    -93   -974       O  
ATOM   3972  CB  TYR B 223      65.252  31.268  45.721  1.00 58.83           C  
ANISOU 3972  CB  TYR B 223     6703   9781   5868   1573   -255   -920       C  
ATOM   3973  CG  TYR B 223      64.769  32.219  44.628  1.00 59.36           C  
ANISOU 3973  CG  TYR B 223     6801   9588   6167   1409   -210  -1005       C  
ATOM   3974  CD1 TYR B 223      64.157  31.746  43.464  1.00 53.56           C  
ANISOU 3974  CD1 TYR B 223     6185   8591   5576   1432   -166   -883       C  
ATOM   3975  CD2 TYR B 223      64.972  33.589  44.748  1.00 59.71           C  
ANISOU 3975  CD2 TYR B 223     6756   9652   6278   1233   -212  -1205       C  
ATOM   3976  CE1 TYR B 223      63.739  32.632  42.463  1.00 53.54           C  
ANISOU 3976  CE1 TYR B 223     6202   8377   5764   1297   -133   -940       C  
ATOM   3977  CE2 TYR B 223      64.559  34.471  43.770  1.00 53.85           C  
ANISOU 3977  CE2 TYR B 223     6044   8671   5747   1102   -161  -1257       C  
ATOM   3978  CZ  TYR B 223      63.954  33.994  42.631  1.00 54.35           C  
ANISOU 3978  CZ  TYR B 223     6215   8500   5935   1142   -126  -1115       C  
ATOM   3979  OH  TYR B 223      63.580  34.905  41.673  1.00 52.77           O  
ANISOU 3979  OH  TYR B 223     6035   8089   5925   1022    -83  -1152       O  
ATOM   3980  N   TYR B 224      63.974  32.619  48.078  1.00 50.93           N  
ANISOU 3980  N   TYR B 224     5713   8937   4702   1421   -217  -1187       N  
ATOM   3981  CA  TYR B 224      63.331  33.747  48.734  1.00 53.89           C  
ANISOU 3981  CA  TYR B 224     6094   9283   5098   1280   -170  -1383       C  
ATOM   3982  C   TYR B 224      63.602  34.997  47.919  1.00 55.84           C  
ANISOU 3982  C   TYR B 224     6283   9389   5546   1098   -158  -1550       C  
ATOM   3983  O   TYR B 224      64.766  35.358  47.713  1.00 53.45           O  
ANISOU 3983  O   TYR B 224     5853   9233   5221   1036   -228  -1637       O  
ATOM   3984  CB  TYR B 224      63.846  33.925  50.161  1.00 60.02           C  
ANISOU 3984  CB  TYR B 224     6796  10399   5612   1286   -224  -1507       C  
ATOM   3985  CG  TYR B 224      63.469  32.792  51.073  1.00 60.60           C  
ANISOU 3985  CG  TYR B 224     6940  10610   5478   1467   -214  -1333       C  
ATOM   3986  CD1 TYR B 224      62.265  32.799  51.757  1.00 62.02           C  
ANISOU 3986  CD1 TYR B 224     7230  10703   5632   1476   -114  -1324       C  
ATOM   3987  CD2 TYR B 224      64.310  31.703  51.234  1.00 62.62           C  
ANISOU 3987  CD2 TYR B 224     7149  11072   5570   1638   -290  -1160       C  
ATOM   3988  CE1 TYR B 224      61.918  31.763  52.583  1.00 67.52           C  
ANISOU 3988  CE1 TYR B 224     7994  11517   6143   1637    -88  -1149       C  
ATOM   3989  CE2 TYR B 224      63.971  30.661  52.063  1.00 63.05           C  
ANISOU 3989  CE2 TYR B 224     7278  11236   5442   1812   -266   -978       C  
ATOM   3990  CZ  TYR B 224      62.778  30.697  52.737  1.00 67.00           C  
ANISOU 3990  CZ  TYR B 224     7893  11648   5916   1804   -165   -973       C  
ATOM   3991  OH  TYR B 224      62.433  29.658  53.566  1.00 68.95           O  
ANISOU 3991  OH  TYR B 224     8217  11997   5982   1973   -125   -776       O  
ATOM   3992  N   GLY B 225      62.536  35.649  47.458  1.00 56.38           N  
ANISOU 3992  N   GLY B 225     6435   9175   5813   1017    -66  -1581       N  
ATOM   3993  CA  GLY B 225      62.695  36.790  46.589  1.00 50.97           C  
ANISOU 3993  CA  GLY B 225     5715   8313   5337    864    -36  -1696       C  
ATOM   3994  C   GLY B 225      61.506  37.722  46.633  1.00 53.78           C  
ANISOU 3994  C   GLY B 225     6146   8431   5858    782     75  -1779       C  
ATOM   3995  O   GLY B 225      60.636  37.617  47.501  1.00 55.74           O  
ANISOU 3995  O   GLY B 225     6453   8687   6039    825    130  -1791       O  
ATOM   3996  N   HIS B 226      61.501  38.659  45.689  1.00 50.41           N  
ANISOU 3996  N   HIS B 226     5710   7795   5648    671    117  -1827       N  
ATOM   3997  CA  HIS B 226      60.360  39.537  45.512  1.00 52.14           C  
ANISOU 3997  CA  HIS B 226     5996   7754   6062    619    230  -1865       C  
ATOM   3998  C   HIS B 226      59.171  38.706  45.060  1.00 54.61           C  
ANISOU 3998  C   HIS B 226     6394   7922   6435    737    253  -1649       C  
ATOM   3999  O   HIS B 226      59.266  37.968  44.073  1.00 56.00           O  
ANISOU 3999  O   HIS B 226     6588   8045   6646    792    201  -1481       O  
ATOM   4000  CB  HIS B 226      60.673  40.614  44.482  1.00 51.97           C  
ANISOU 4000  CB  HIS B 226     5949   7536   6260    496    270  -1915       C  
ATOM   4001  CG  HIS B 226      59.673  41.723  44.459  1.00 54.45           C  
ANISOU 4001  CG  HIS B 226     6317   7598   6773    440    398  -1985       C  
ATOM   4002  ND1 HIS B 226      59.666  42.702  43.489  1.00 55.27           N  
ANISOU 4002  ND1 HIS B 226     6424   7473   7105    358    461  -1984       N  
ATOM   4003  CD2 HIS B 226      58.640  42.004  45.285  1.00 57.16           C  
ANISOU 4003  CD2 HIS B 226     6711   7881   7125    470    487  -2046       C  
ATOM   4004  CE1 HIS B 226      58.684  43.555  43.733  1.00 57.38           C  
ANISOU 4004  CE1 HIS B 226     6741   7541   7519    346    583  -2040       C  
ATOM   4005  NE2 HIS B 226      58.037  43.147  44.810  1.00 57.09           N  
ANISOU 4005  NE2 HIS B 226     6731   7604   7356    414    603  -2083       N  
ATOM   4006  N   ASN B 227      58.075  38.782  45.774  1.00 52.92           N  
ANISOU 4006  N   ASN B 227     6228   7654   6226    772    332  -1659       N  
ATOM   4007  CA  ASN B 227      56.921  37.992  45.446  1.00 49.61           C  
ANISOU 4007  CA  ASN B 227     5868   7118   5865    865    354  -1465       C  
ATOM   4008  C   ASN B 227      56.460  38.101  44.017  1.00 52.03           C  
ANISOU 4008  C   ASN B 227     6190   7202   6378    853    347  -1330       C  
ATOM   4009  O   ASN B 227      55.962  37.170  43.483  1.00 49.86           O  
ANISOU 4009  O   ASN B 227     5951   6883   6112    916    311  -1161       O  
ATOM   4010  CB  ASN B 227      55.792  38.298  46.411  1.00 42.86           C  
ANISOU 4010  CB  ASN B 227     5040   6229   5017    887    465  -1513       C  
ATOM   4011  CG  ASN B 227      55.091  39.576  46.092  1.00 49.10           C  
ANISOU 4011  CG  ASN B 227     5827   6798   6032    825    570  -1593       C  
ATOM   4012  OD1 ASN B 227      55.651  40.617  46.161  1.00 51.56           O  
ANISOU 4012  OD1 ASN B 227     6117   7078   6394    734    601  -1764       O  
ATOM   4013  ND2 ASN B 227      53.867  39.481  45.737  1.00 49.55           N  
ANISOU 4013  ND2 ASN B 227     5896   6699   6230    874    627  -1462       N  
ATOM   4014  N   GLU B 228      56.611  39.258  43.414  1.00 54.18           N  
ANISOU 4014  N   GLU B 228     6439   7334   6813    767    385  -1406       N  
ATOM   4015  CA  GLU B 228      56.187  39.461  42.030  1.00 47.91           C  
ANISOU 4015  CA  GLU B 228     5658   6344   6201    761    377  -1268       C  
ATOM   4016  C   GLU B 228      56.983  38.629  41.035  1.00 51.65           C  
ANISOU 4016  C   GLU B 228     6140   6872   6613    780    275  -1154       C  
ATOM   4017  O   GLU B 228      56.554  38.503  39.882  1.00 51.39           O  
ANISOU 4017  O   GLU B 228     6134   6710   6682    791    251  -1018       O  
ATOM   4018  CB  GLU B 228      56.312  40.925  41.616  1.00 46.38           C  
ANISOU 4018  CB  GLU B 228     5444   5988   6191    671    454  -1364       C  
ATOM   4019  CG  GLU B 228      55.452  41.935  42.386  1.00 45.10           C  
ANISOU 4019  CG  GLU B 228     5285   5707   6143    657    586  -1477       C  
ATOM   4020  CD  GLU B 228      55.785  43.364  41.951  1.00 56.68           C  
ANISOU 4020  CD  GLU B 228     6745   6995   7796    562    672  -1577       C  
ATOM   4021  OE1 GLU B 228      56.587  43.514  40.986  1.00 58.93           O  
ANISOU 4021  OE1 GLU B 228     7016   7252   8122    510    625  -1529       O  
ATOM   4022  OE2 GLU B 228      55.263  44.331  42.561  1.00 55.55           O  
ANISOU 4022  OE2 GLU B 228     6615   6731   7761    542    799  -1700       O  
ATOM   4023  N   ALA B 229      58.152  38.110  41.426  1.00 46.55           N  
ANISOU 4023  N   ALA B 229     5467   6419   5800    787    216  -1211       N  
ATOM   4024  CA  ALA B 229      58.944  37.314  40.496  1.00 46.70           C  
ANISOU 4024  CA  ALA B 229     5494   6487   5763    822    140  -1107       C  
ATOM   4025  C   ALA B 229      58.309  35.960  40.225  1.00 43.34           C  
ANISOU 4025  C   ALA B 229     5143   6046   5278    923     99   -942       C  
ATOM   4026  O   ALA B 229      58.663  35.321  39.232  1.00 45.68           O  
ANISOU 4026  O   ALA B 229     5475   6318   5563    952     53   -844       O  
ATOM   4027  CB  ALA B 229      60.380  37.137  41.009  1.00 43.11           C  
ANISOU 4027  CB  ALA B 229     4967   6258   5156    817     94  -1202       C  
ATOM   4028  N   ASP B 230      57.356  35.522  41.058  1.00 45.75           N  
ANISOU 4028  N   ASP B 230     5478   6352   5552    967    128   -913       N  
ATOM   4029  CA  ASP B 230      56.711  34.235  40.809  1.00 42.40           C  
ANISOU 4029  CA  ASP B 230     5126   5890   5093   1040    101   -760       C  
ATOM   4030  C   ASP B 230      55.706  34.278  39.651  1.00 44.27           C  
ANISOU 4030  C   ASP B 230     5396   5937   5486   1007     91   -655       C  
ATOM   4031  O   ASP B 230      55.149  33.235  39.307  1.00 52.52           O  
ANISOU 4031  O   ASP B 230     6501   6936   6517   1038     63   -542       O  
ATOM   4032  CB  ASP B 230      56.021  33.722  42.081  1.00 49.49           C  
ANISOU 4032  CB  ASP B 230     6040   6855   5909   1091    148   -749       C  
ATOM   4033  CG  ASP B 230      56.464  32.281  42.471  1.00 54.94           C  
ANISOU 4033  CG  ASP B 230     6785   7655   6434   1193    118   -653       C  
ATOM   4034  OD1 ASP B 230      57.269  31.679  41.737  1.00 47.68           O  
ANISOU 4034  OD1 ASP B 230     5892   6749   5475   1228     65   -604       O  
ATOM   4035  OD2 ASP B 230      56.013  31.746  43.516  1.00 52.54           O  
ANISOU 4035  OD2 ASP B 230     6502   7420   6041   1246    161   -619       O  
ATOM   4036  N   PHE B 231      55.453  35.432  39.044  1.00 42.96           N  
ANISOU 4036  N   PHE B 231     5194   5664   5465    943    113   -683       N  
ATOM   4037  CA  PHE B 231      54.626  35.518  37.845  1.00 46.82           C  
ANISOU 4037  CA  PHE B 231     5701   6008   6080    921     84   -569       C  
ATOM   4038  C   PHE B 231      55.439  35.492  36.547  1.00 46.77           C  
ANISOU 4038  C   PHE B 231     5725   5984   6061    903     29   -530       C  
ATOM   4039  O   PHE B 231      54.855  35.630  35.471  1.00 52.75           O  
ANISOU 4039  O   PHE B 231     6500   6644   6898    883     -5   -437       O  
ATOM   4040  CB  PHE B 231      53.772  36.790  37.870  1.00 46.38           C  
ANISOU 4040  CB  PHE B 231     5588   5835   6198    888    149   -586       C  
ATOM   4041  CG  PHE B 231      52.922  36.922  39.092  1.00 51.22           C  
ANISOU 4041  CG  PHE B 231     6170   6459   6834    910    226   -630       C  
ATOM   4042  CD1 PHE B 231      52.315  35.812  39.648  1.00 54.63           C  
ANISOU 4042  CD1 PHE B 231     6623   6942   7190    949    217   -567       C  
ATOM   4043  CD2 PHE B 231      52.729  38.163  39.687  1.00 60.58           C  
ANISOU 4043  CD2 PHE B 231     7310   7589   8117    892    324   -736       C  
ATOM   4044  CE1 PHE B 231      51.542  35.927  40.785  1.00 58.52           C  
ANISOU 4044  CE1 PHE B 231     7086   7455   7692    973    304   -600       C  
ATOM   4045  CE2 PHE B 231      51.941  38.294  40.827  1.00 64.06           C  
ANISOU 4045  CE2 PHE B 231     7728   8045   8567    920    412   -785       C  
ATOM   4046  CZ  PHE B 231      51.355  37.171  41.379  1.00 62.65           C  
ANISOU 4046  CZ  PHE B 231     7564   7942   8300    963    402   -712       C  
ATOM   4047  N   GLY B 232      56.753  35.284  36.620  1.00 50.42           N  
ANISOU 4047  N   GLY B 232     6187   6556   6415    916     18   -590       N  
ATOM   4048  CA  GLY B 232      57.631  35.348  35.457  1.00 51.52           C  
ANISOU 4048  CA  GLY B 232     6343   6693   6538    902     -9   -562       C  
ATOM   4049  C   GLY B 232      57.448  34.248  34.419  1.00 46.76           C  
ANISOU 4049  C   GLY B 232     5833   6057   5877    937    -69   -454       C  
ATOM   4050  O   GLY B 232      58.078  34.323  33.364  1.00 49.05           O  
ANISOU 4050  O   GLY B 232     6148   6341   6148    929    -81   -425       O  
ATOM   4051  N   MET B 233      56.610  33.246  34.683  1.00 46.72           N  
ANISOU 4051  N   MET B 233     5883   6027   5843    968    -95   -399       N  
ATOM   4052  CA  MET B 233      56.260  32.212  33.709  1.00 43.00           C  
ANISOU 4052  CA  MET B 233     5510   5499   5330    976   -149   -317       C  
ATOM   4053  C   MET B 233      54.799  32.345  33.278  1.00 52.49           C  
ANISOU 4053  C   MET B 233     6709   6600   6635    920   -187   -245       C  
ATOM   4054  O   MET B 233      54.227  31.386  32.752  1.00 51.32           O  
ANISOU 4054  O   MET B 233     6634   6407   6458    904   -237   -193       O  
ATOM   4055  CB  MET B 233      56.513  30.804  34.274  1.00 45.90           C  
ANISOU 4055  CB  MET B 233     5950   5904   5585   1045   -146   -308       C  
ATOM   4056  CG  MET B 233      57.984  30.347  34.198  1.00 45.13           C  
ANISOU 4056  CG  MET B 233     5874   5904   5370   1124   -129   -338       C  
ATOM   4057  SD  MET B 233      58.561  30.186  32.470  1.00 53.99           S  
ANISOU 4057  SD  MET B 233     7075   6984   6457   1114   -153   -312       S  
ATOM   4058  CE  MET B 233      57.667  28.738  31.961  1.00 53.23           C  
ANISOU 4058  CE  MET B 233     7131   6768   6327   1114   -186   -257       C  
ATOM   4059  N   SER B 234      54.170  33.506  33.524  1.00 43.49           N  
ANISOU 4059  N   SER B 234     5482   5423   5622    889   -160   -245       N  
ATOM   4060  CA  SER B 234      52.732  33.636  33.306  1.00 48.61           C  
ANISOU 4060  CA  SER B 234     6092   5998   6377    855   -190   -167       C  
ATOM   4061  C   SER B 234      52.343  33.483  31.834  1.00 48.46           C  
ANISOU 4061  C   SER B 234     6113   5944   6356    817   -279    -80       C  
ATOM   4062  O   SER B 234      51.192  33.149  31.536  1.00 45.66           O  
ANISOU 4062  O   SER B 234     5737   5560   6050    781   -336    -11       O  
ATOM   4063  CB  SER B 234      52.237  34.987  33.833  1.00 47.38           C  
ANISOU 4063  CB  SER B 234     5836   5802   6366    854   -123   -182       C  
ATOM   4064  OG  SER B 234      52.769  36.048  33.058  1.00 48.16           O  
ANISOU 4064  OG  SER B 234     5920   5864   6515    842   -111   -174       O  
ATOM   4065  N   TRP B 235      53.273  33.703  30.906  1.00 49.10           N  
ANISOU 4065  N   TRP B 235     6244   6042   6371    821   -294    -81       N  
ATOM   4066  CA  TRP B 235      52.967  33.565  29.489  1.00 47.31           C  
ANISOU 4066  CA  TRP B 235     6066   5803   6105    789   -378     -2       C  
ATOM   4067  C   TRP B 235      52.615  32.128  29.102  1.00 57.68           C  
ANISOU 4067  C   TRP B 235     7476   7121   7319    759   -450     -4       C  
ATOM   4068  O   TRP B 235      52.153  31.909  27.981  1.00 59.18           O  
ANISOU 4068  O   TRP B 235     7707   7313   7466    715   -536     47       O  
ATOM   4069  CB  TRP B 235      54.152  34.073  28.659  1.00 46.12           C  
ANISOU 4069  CB  TRP B 235     5955   5678   5889    805   -351     -6       C  
ATOM   4070  CG  TRP B 235      55.436  33.338  28.932  1.00 48.53           C  
ANISOU 4070  CG  TRP B 235     6324   6038   6076    843   -308    -91       C  
ATOM   4071  CD1 TRP B 235      56.374  33.648  29.867  1.00 56.16           C  
ANISOU 4071  CD1 TRP B 235     7240   7049   7049    874   -232   -170       C  
ATOM   4072  CD2 TRP B 235      55.919  32.167  28.252  1.00 52.68           C  
ANISOU 4072  CD2 TRP B 235     6969   6587   6459    861   -337   -106       C  
ATOM   4073  NE1 TRP B 235      57.415  32.751  29.821  1.00 58.01           N  
ANISOU 4073  NE1 TRP B 235     7537   7347   7158    923   -216   -213       N  
ATOM   4074  CE2 TRP B 235      57.167  31.832  28.834  1.00 58.12           C  
ANISOU 4074  CE2 TRP B 235     7663   7335   7084    923   -268   -176       C  
ATOM   4075  CE3 TRP B 235      55.415  31.364  27.211  1.00 52.62           C  
ANISOU 4075  CE3 TRP B 235     7065   6561   6368    829   -413    -75       C  
ATOM   4076  CZ2 TRP B 235      57.931  30.722  28.412  1.00 57.11           C  
ANISOU 4076  CZ2 TRP B 235     7641   7231   6826    976   -256   -201       C  
ATOM   4077  CZ3 TRP B 235      56.178  30.259  26.785  1.00 53.07           C  
ANISOU 4077  CZ3 TRP B 235     7248   6629   6289    865   -397   -124       C  
ATOM   4078  CH2 TRP B 235      57.422  29.951  27.395  1.00 52.92           C  
ANISOU 4078  CH2 TRP B 235     7231   6652   6224    949   -311   -180       C  
ATOM   4079  N   CYS B 236      52.813  31.146  29.996  1.00 51.28           N  
ANISOU 4079  N   CYS B 236     6708   6308   6467    780   -414    -60       N  
ATOM   4080  CA  CYS B 236      52.358  29.778  29.766  1.00 48.58           C  
ANISOU 4080  CA  CYS B 236     6462   5930   6064    741   -460    -64       C  
ATOM   4081  C   CYS B 236      51.516  29.258  30.934  1.00 45.72           C  
ANISOU 4081  C   CYS B 236     6058   5537   5775    727   -429    -57       C  
ATOM   4082  O   CYS B 236      51.594  28.074  31.284  1.00 58.84           O  
ANISOU 4082  O   CYS B 236     7809   7161   7386    730   -406    -77       O  
ATOM   4083  CB  CYS B 236      53.551  28.844  29.495  1.00 50.82           C  
ANISOU 4083  CB  CYS B 236     6881   6218   6210    795   -427   -121       C  
ATOM   4084  SG  CYS B 236      53.063  27.262  28.632  1.00 64.69           S  
ANISOU 4084  SG  CYS B 236     8804   7894   7882    725   -487   -142       S  
ATOM   4085  N   ALA B 237      50.730  30.132  31.582  1.00 53.09           N  
ANISOU 4085  N   ALA B 237     6860   6479   6833    720   -408    -23       N  
ATOM   4086  CA  ALA B 237      50.001  29.765  32.789  1.00 44.75           C  
ANISOU 4086  CA  ALA B 237     5753   5409   5840    718   -351    -14       C  
ATOM   4087  C   ALA B 237      48.488  29.943  32.710  1.00 55.99           C  
ANISOU 4087  C   ALA B 237     7068   6812   7394    646   -391     57       C  
ATOM   4088  O   ALA B 237      47.772  29.311  33.495  1.00 62.77           O  
ANISOU 4088  O   ALA B 237     7901   7651   8296    619   -351     76       O  
ATOM   4089  CB  ALA B 237      50.523  30.569  33.986  1.00 42.29           C  
ANISOU 4089  CB  ALA B 237     5378   5144   5546    794   -252    -60       C  
ATOM   4090  N   GLY B 238      47.982  30.781  31.815  1.00 57.53           N  
ANISOU 4090  N   GLY B 238     7187   7019   7653    620   -462    110       N  
ATOM   4091  CA  GLY B 238      46.552  31.067  31.798  1.00 64.80           C  
ANISOU 4091  CA  GLY B 238     7967   7944   8708    572   -498    192       C  
ATOM   4092  C   GLY B 238      45.966  31.624  33.083  1.00 65.89           C  
ANISOU 4092  C   GLY B 238     7989   8079   8968    620   -385    202       C  
ATOM   4093  O   GLY B 238      44.870  31.218  33.484  1.00 70.61           O  
ANISOU 4093  O   GLY B 238     8500   8678   9650    573   -378    250       O  
ATOM   4094  N   PHE B 239      46.651  32.572  33.718  1.00 64.23           N  
ANISOU 4094  N   PHE B 239     7770   7867   8768    704   -291    152       N  
ATOM   4095  CA  PHE B 239      46.156  33.222  34.930  1.00 56.65           C  
ANISOU 4095  CA  PHE B 239     6714   6903   7908    755   -169    138       C  
ATOM   4096  C   PHE B 239      45.098  34.270  34.558  1.00 58.69           C  
ANISOU 4096  C   PHE B 239     6824   7141   8336    774   -173    227       C  
ATOM   4097  O   PHE B 239      45.385  35.216  33.810  1.00 52.98           O  
ANISOU 4097  O   PHE B 239     6089   6392   7649    806   -198    253       O  
ATOM   4098  CB  PHE B 239      47.298  33.905  35.693  1.00 48.31           C  
ANISOU 4098  CB  PHE B 239     5706   5855   6795    822    -74     28       C  
ATOM   4099  CG  PHE B 239      48.319  32.968  36.327  1.00 46.12           C  
ANISOU 4099  CG  PHE B 239     5542   5627   6356    834    -53    -48       C  
ATOM   4100  CD1 PHE B 239      47.963  31.729  36.845  1.00 47.14           C  
ANISOU 4100  CD1 PHE B 239     5711   5768   6431    816    -44    -19       C  
ATOM   4101  CD2 PHE B 239      49.651  33.365  36.427  1.00 40.74           C  
ANISOU 4101  CD2 PHE B 239     4915   4980   5584    869    -35   -137       C  
ATOM   4102  CE1 PHE B 239      48.928  30.882  37.440  1.00 41.19           C  
ANISOU 4102  CE1 PHE B 239     5063   5058   5531    855    -17    -65       C  
ATOM   4103  CE2 PHE B 239      50.630  32.527  37.029  1.00 41.38           C  
ANISOU 4103  CE2 PHE B 239     5079   5130   5513    903    -20   -192       C  
ATOM   4104  CZ  PHE B 239      50.265  31.302  37.534  1.00 40.14           C  
ANISOU 4104  CZ  PHE B 239     4970   4982   5300    907    -10   -148       C  
ATOM   4105  N   GLY B 240      43.874  34.094  35.074  1.00 64.97           N  
ANISOU 4105  N   GLY B 240     7500   7947   9238    763   -138    287       N  
ATOM   4106  CA  GLY B 240      42.803  35.053  34.900  1.00 66.80           C  
ANISOU 4106  CA  GLY B 240     7568   8169   9645    807   -120    382       C  
ATOM   4107  C   GLY B 240      42.779  36.188  35.923  1.00 65.44           C  
ANISOU 4107  C   GLY B 240     7346   7949   9571    907     50    330       C  
ATOM   4108  O   GLY B 240      43.575  36.260  36.863  1.00 58.96           O  
ANISOU 4108  O   GLY B 240     6613   7119   8671    932    149    207       O  
ATOM   4109  N   GLU B 241      41.790  37.072  35.734  1.00 61.30           N  
ANISOU 4109  N   GLU B 241     6671   7398   9220    969     82    428       N  
ATOM   4110  CA  GLU B 241      41.552  38.162  36.673  1.00 58.79           C  
ANISOU 4110  CA  GLU B 241     6298   7015   9023   1070    261    383       C  
ATOM   4111  C   GLU B 241      41.123  37.637  38.041  1.00 57.26           C  
ANISOU 4111  C   GLU B 241     6082   6862   8814   1071    388    320       C  
ATOM   4112  O   GLU B 241      41.444  38.247  39.068  1.00 52.58           O  
ANISOU 4112  O   GLU B 241     5526   6234   8217   1130    541    203       O  
ATOM   4113  CB  GLU B 241      40.485  39.114  36.108  1.00 59.10           C  
ANISOU 4113  CB  GLU B 241     6170   7018   9266   1155    271    530       C  
ATOM   4114  CG  GLU B 241      40.307  40.412  36.895  1.00 71.79           C  
ANISOU 4114  CG  GLU B 241     7740   8517  11021   1277    471    482       C  
ATOM   4115  CD  GLU B 241      39.037  41.195  36.517  1.00 82.99           C  
ANISOU 4115  CD  GLU B 241     8963   9907  12660   1387    507    653       C  
ATOM   4116  OE1 GLU B 241      37.913  40.679  36.696  1.00 87.83           O  
ANISOU 4116  OE1 GLU B 241     9419  10609  13344   1386    495    748       O  
ATOM   4117  OE2 GLU B 241      39.161  42.345  36.057  1.00 90.79           O  
ANISOU 4117  OE2 GLU B 241     9950  10784  13763   1481    556    700       O  
ATOM   4118  N   SER B 242      40.422  36.498  38.087  1.00 49.42           N  
ANISOU 4118  N   SER B 242     5035   5943   7801    999    333    389       N  
ATOM   4119  CA  SER B 242      40.074  35.934  39.387  1.00 48.07           C  
ANISOU 4119  CA  SER B 242     4855   5810   7598    998    465    346       C  
ATOM   4120  C   SER B 242      41.302  35.412  40.128  1.00 51.31           C  
ANISOU 4120  C   SER B 242     5448   6241   7806    983    498    211       C  
ATOM   4121  O   SER B 242      41.331  35.455  41.363  1.00 54.70           O  
ANISOU 4121  O   SER B 242     5899   6698   8185   1026    643    138       O  
ATOM   4122  CB  SER B 242      39.035  34.820  39.224  1.00 56.30           C  
ANISOU 4122  CB  SER B 242     5794   6913   8684    906    406    462       C  
ATOM   4123  OG  SER B 242      39.553  33.764  38.433  1.00 80.02           O  
ANISOU 4123  OG  SER B 242     8905   9929  11571    796    248    467       O  
ATOM   4124  N   PHE B 243      42.333  34.950  39.401  1.00 48.78           N  
ANISOU 4124  N   PHE B 243     5256   5920   7361    933    370    179       N  
ATOM   4125  CA  PHE B 243      43.598  34.577  40.042  1.00 46.78           C  
ANISOU 4125  CA  PHE B 243     5155   5699   6920    940    395     59       C  
ATOM   4126  C   PHE B 243      44.262  35.790  40.688  1.00 48.30           C  
ANISOU 4126  C   PHE B 243     5371   5876   7103   1009    499    -73       C  
ATOM   4127  O   PHE B 243      44.643  35.753  41.860  1.00 55.96           O  
ANISOU 4127  O   PHE B 243     6390   6904   7969   1040    600   -172       O  
ATOM   4128  CB  PHE B 243      44.557  33.942  39.018  1.00 43.50           C  
ANISOU 4128  CB  PHE B 243     4852   5281   6394    887    247     58       C  
ATOM   4129  CG  PHE B 243      45.967  33.726  39.537  1.00 40.21           C  
ANISOU 4129  CG  PHE B 243     4567   4910   5800    913    262    -55       C  
ATOM   4130  CD1 PHE B 243      46.301  32.572  40.252  1.00 40.42           C  
ANISOU 4130  CD1 PHE B 243     4675   4993   5690    913    283    -59       C  
ATOM   4131  CD2 PHE B 243      46.961  34.671  39.313  1.00 40.48           C  
ANISOU 4131  CD2 PHE B 243     4634   4936   5811    938    259   -148       C  
ATOM   4132  CE1 PHE B 243      47.613  32.365  40.726  1.00 40.27           C  
ANISOU 4132  CE1 PHE B 243     4757   5043   5503    953    287   -146       C  
ATOM   4133  CE2 PHE B 243      48.271  34.479  39.784  1.00 43.20           C  
ANISOU 4133  CE2 PHE B 243     5069   5349   5994    955    263   -252       C  
ATOM   4134  CZ  PHE B 243      48.598  33.329  40.498  1.00 41.12           C  
ANISOU 4134  CZ  PHE B 243     4874   5165   5585    971    271   -248       C  
ATOM   4135  N   TYR B 244      44.442  36.866  39.918  1.00 51.41           N  
ANISOU 4135  N   TYR B 244     5741   6195   7599   1028    475    -79       N  
ATOM   4136  CA  TYR B 244      45.169  38.025  40.428  1.00 52.80           C  
ANISOU 4136  CA  TYR B 244     5954   6330   7778   1067    573   -221       C  
ATOM   4137  C   TYR B 244      44.409  38.728  41.550  1.00 55.38           C  
ANISOU 4137  C   TYR B 244     6216   6635   8190   1132    750   -280       C  
ATOM   4138  O   TYR B 244      45.004  39.132  42.560  1.00 54.39           O  
ANISOU 4138  O   TYR B 244     6150   6538   7976   1145    851   -440       O  
ATOM   4139  CB  TYR B 244      45.466  38.996  39.287  1.00 43.81           C  
ANISOU 4139  CB  TYR B 244     4807   5090   6749   1070    525   -189       C  
ATOM   4140  CG  TYR B 244      46.548  38.502  38.356  1.00 51.11           C  
ANISOU 4140  CG  TYR B 244     5822   6044   7554   1013    387   -184       C  
ATOM   4141  CD1 TYR B 244      47.875  38.433  38.785  1.00 50.16           C  
ANISOU 4141  CD1 TYR B 244     5795   5976   7288    988    393   -322       C  
ATOM   4142  CD2 TYR B 244      46.258  38.126  37.044  1.00 46.33           C  
ANISOU 4142  CD2 TYR B 244     5201   5430   6974    987    255    -45       C  
ATOM   4143  CE1 TYR B 244      48.885  37.978  37.946  1.00 51.90           C  
ANISOU 4143  CE1 TYR B 244     6087   6229   7404    948    285   -314       C  
ATOM   4144  CE2 TYR B 244      47.263  37.661  36.194  1.00 43.10           C  
ANISOU 4144  CE2 TYR B 244     4884   5050   6443    942    148    -48       C  
ATOM   4145  CZ  TYR B 244      48.574  37.593  36.648  1.00 49.32           C  
ANISOU 4145  CZ  TYR B 244     5759   5878   7102    929    172   -179       C  
ATOM   4146  OH  TYR B 244      49.579  37.159  35.810  1.00 51.58           O  
ANISOU 4146  OH  TYR B 244     6124   6196   7277    898     84   -179       O  
ATOM   4147  N   ASN B 245      43.098  38.877  41.403  1.00 48.76           N  
ANISOU 4147  N   ASN B 245     5250   5760   7516   1172    793   -158       N  
ATOM   4148  CA  ASN B 245      42.360  39.583  42.432  1.00 50.57           C  
ANISOU 4148  CA  ASN B 245     5416   5962   7836   1249    983   -212       C  
ATOM   4149  C   ASN B 245      42.320  38.793  43.727  1.00 51.38           C  
ANISOU 4149  C   ASN B 245     5558   6183   7783   1244   1068   -278       C  
ATOM   4150  O   ASN B 245      42.360  39.400  44.804  1.00 47.51           O  
ANISOU 4150  O   ASN B 245     5093   5698   7260   1292   1227   -413       O  
ATOM   4151  CB  ASN B 245      40.957  39.936  41.935  1.00 44.38           C  
ANISOU 4151  CB  ASN B 245     4461   5125   7276   1309   1012    -47       C  
ATOM   4152  CG  ASN B 245      40.979  41.118  40.991  1.00 54.19           C  
ANISOU 4152  CG  ASN B 245     5671   6235   8683   1362    999     -2       C  
ATOM   4153  OD1 ASN B 245      42.056  41.663  40.692  1.00 54.52           O  
ANISOU 4153  OD1 ASN B 245     5826   6213   8677   1338    975    -98       O  
ATOM   4154  ND2 ASN B 245      39.806  41.530  40.515  1.00 53.02           N  
ANISOU 4154  ND2 ASN B 245     5363   6049   8734   1438   1019    157       N  
ATOM   4155  N   ALA B 246      42.291  37.452  43.659  1.00 45.21           N  
ANISOU 4155  N   ALA B 246     4795   5490   6893   1185    975   -190       N  
ATOM   4156  CA  ALA B 246      42.378  36.682  44.900  1.00 48.86           C  
ANISOU 4156  CA  ALA B 246     5313   6064   7188   1189   1062   -235       C  
ATOM   4157  C   ALA B 246      43.785  36.757  45.474  1.00 51.27           C  
ANISOU 4157  C   ALA B 246     5760   6439   7282   1185   1049   -399       C  
ATOM   4158  O   ALA B 246      43.954  36.819  46.694  1.00 55.40           O  
ANISOU 4158  O   ALA B 246     6326   7050   7672   1220   1165   -502       O  
ATOM   4159  CB  ALA B 246      41.949  35.229  44.682  1.00 40.54           C  
ANISOU 4159  CB  ALA B 246     4249   5058   6096   1127    986    -87       C  
ATOM   4160  N   TYR B 247      44.801  36.762  44.602  1.00 48.40           N  
ANISOU 4160  N   TYR B 247     5460   6053   6878   1143    908   -424       N  
ATOM   4161  CA  TYR B 247      46.181  36.948  45.035  1.00 47.50           C  
ANISOU 4161  CA  TYR B 247     5448   6014   6587   1133    884   -580       C  
ATOM   4162  C   TYR B 247      46.364  38.287  45.752  1.00 50.16           C  
ANISOU 4162  C   TYR B 247     5785   6325   6949   1156   1012   -764       C  
ATOM   4163  O   TYR B 247      46.822  38.332  46.900  1.00 51.54           O  
ANISOU 4163  O   TYR B 247     6012   6616   6956   1169   1083   -900       O  
ATOM   4164  CB  TYR B 247      47.134  36.855  43.828  1.00 42.10           C  
ANISOU 4164  CB  TYR B 247     4807   5294   5897   1085    728   -562       C  
ATOM   4165  CG  TYR B 247      48.564  36.967  44.278  1.00 45.43           C  
ANISOU 4165  CG  TYR B 247     5304   5817   6140   1071    699   -711       C  
ATOM   4166  CD1 TYR B 247      49.156  38.220  44.457  1.00 44.24           C  
ANISOU 4166  CD1 TYR B 247     5154   5633   6022   1050    750   -876       C  
ATOM   4167  CD2 TYR B 247      49.314  35.832  44.588  1.00 44.42           C  
ANISOU 4167  CD2 TYR B 247     5241   5822   5816   1080    630   -688       C  
ATOM   4168  CE1 TYR B 247      50.436  38.343  44.925  1.00 43.92           C  
ANISOU 4168  CE1 TYR B 247     5159   5710   5820   1021    718  -1023       C  
ATOM   4169  CE2 TYR B 247      50.615  35.949  45.041  1.00 40.78           C  
ANISOU 4169  CE2 TYR B 247     4821   5485   5189   1076    597   -815       C  
ATOM   4170  CZ  TYR B 247      51.163  37.203  45.216  1.00 43.63           C  
ANISOU 4170  CZ  TYR B 247     5163   5833   5581   1038    635   -988       C  
ATOM   4171  OH  TYR B 247      52.431  37.345  45.689  1.00 47.21           O  
ANISOU 4171  OH  TYR B 247     5634   6429   5873   1015    595  -1125       O  
ATOM   4172  N   PHE B 248      45.986  39.396  45.098  1.00 48.08           N  
ANISOU 4172  N   PHE B 248     5470   5907   6892   1164   1049   -770       N  
ATOM   4173  CA  PHE B 248      46.258  40.716  45.677  1.00 49.48           C  
ANISOU 4173  CA  PHE B 248     5669   6018   7114   1174   1178   -962       C  
ATOM   4174  C   PHE B 248      45.410  41.007  46.906  1.00 56.10           C  
ANISOU 4174  C   PHE B 248     6486   6881   7948   1237   1365  -1034       C  
ATOM   4175  O   PHE B 248      45.725  41.944  47.645  1.00 53.64           O  
ANISOU 4175  O   PHE B 248     6220   6546   7615   1237   1484  -1235       O  
ATOM   4176  CB  PHE B 248      45.976  41.843  44.681  1.00 42.53           C  
ANISOU 4176  CB  PHE B 248     4744   4936   6478   1186   1200   -924       C  
ATOM   4177  CG  PHE B 248      46.878  41.840  43.489  1.00 48.14           C  
ANISOU 4177  CG  PHE B 248     5485   5609   7197   1124   1050   -878       C  
ATOM   4178  CD1 PHE B 248      48.258  41.770  43.634  1.00 46.94           C  
ANISOU 4178  CD1 PHE B 248     5410   5540   6886   1051    985  -1014       C  
ATOM   4179  CD2 PHE B 248      46.341  41.923  42.199  1.00 47.62           C  
ANISOU 4179  CD2 PHE B 248     5360   5441   7293   1143    976   -691       C  
ATOM   4180  CE1 PHE B 248      49.111  41.767  42.496  1.00 45.40           C  
ANISOU 4180  CE1 PHE B 248     5237   5314   6701    998    863   -964       C  
ATOM   4181  CE2 PHE B 248      47.174  41.937  41.066  1.00 47.82           C  
ANISOU 4181  CE2 PHE B 248     5422   5438   7311   1091    850   -644       C  
ATOM   4182  CZ  PHE B 248      48.559  41.856  41.210  1.00 46.01           C  
ANISOU 4182  CZ  PHE B 248     5272   5278   6931   1019    803   -779       C  
ATOM   4183  N   LYS B 249      44.389  40.196  47.182  1.00 53.61           N  
ANISOU 4183  N   LYS B 249     6109   6622   7640   1281   1400   -889       N  
ATOM   4184  CA  LYS B 249      43.635  40.376  48.414  1.00 50.94           C  
ANISOU 4184  CA  LYS B 249     5753   6333   7268   1345   1591   -953       C  
ATOM   4185  C   LYS B 249      44.487  40.047  49.627  1.00 51.34           C  
ANISOU 4185  C   LYS B 249     5912   6565   7031   1327   1617  -1115       C  
ATOM   4186  O   LYS B 249      44.349  40.692  50.672  1.00 57.11           O  
ANISOU 4186  O   LYS B 249     6674   7327   7697   1361   1778  -1280       O  
ATOM   4187  CB  LYS B 249      42.375  39.521  48.375  1.00 48.16           C  
ANISOU 4187  CB  LYS B 249     5295   6007   6997   1381   1622   -742       C  
ATOM   4188  CG  LYS B 249      41.443  39.725  49.504  1.00 56.46           C  
ANISOU 4188  CG  LYS B 249     6303   7098   8051   1456   1836   -773       C  
ATOM   4189  CD  LYS B 249      40.065  39.323  49.064  1.00 69.20           C  
ANISOU 4189  CD  LYS B 249     7757   8673   9864   1488   1868   -555       C  
ATOM   4190  CE  LYS B 249      39.191  39.000  50.237  1.00 77.67           C  
ANISOU 4190  CE  LYS B 249     8786   9841  10885   1544   2064   -534       C  
ATOM   4191  NZ  LYS B 249      39.353  37.574  50.614  1.00 80.88           N  
ANISOU 4191  NZ  LYS B 249     9237  10389  11104   1487   2003   -432       N  
ATOM   4192  N   VAL B 250      45.362  39.047  49.501  1.00 57.31           N  
ANISOU 4192  N   VAL B 250     6724   7447   7605   1281   1464  -1070       N  
ATOM   4193  CA  VAL B 250      46.302  38.644  50.548  1.00 54.48           C  
ANISOU 4193  CA  VAL B 250     6455   7291   6952   1273   1451  -1194       C  
ATOM   4194  C   VAL B 250      47.616  39.432  50.456  1.00 56.31           C  
ANISOU 4194  C   VAL B 250     6741   7543   7113   1207   1376  -1400       C  
ATOM   4195  O   VAL B 250      48.190  39.809  51.477  1.00 63.13           O  
ANISOU 4195  O   VAL B 250     7657   8539   7790   1195   1426  -1596       O  
ATOM   4196  CB  VAL B 250      46.542  37.113  50.443  1.00 55.91           C  
ANISOU 4196  CB  VAL B 250     6662   7590   6992   1278   1335  -1011       C  
ATOM   4197  CG1 VAL B 250      47.582  36.588  51.471  1.00 47.15           C  
ANISOU 4197  CG1 VAL B 250     5637   6714   5565   1293   1301  -1097       C  
ATOM   4198  CG2 VAL B 250      45.233  36.353  50.574  1.00 51.23           C  
ANISOU 4198  CG2 VAL B 250     6012   6970   6484   1316   1421   -818       C  
ATOM   4199  N   MET B 251      48.121  39.687  49.245  1.00 50.83           N  
ANISOU 4199  N   MET B 251     6029   6729   6555   1156   1257  -1365       N  
ATOM   4200  CA  MET B 251      49.403  40.373  49.033  1.00 51.61           C  
ANISOU 4200  CA  MET B 251     6162   6841   6608   1077   1184  -1538       C  
ATOM   4201  C   MET B 251      49.138  41.555  48.109  1.00 54.37           C  
ANISOU 4201  C   MET B 251     6481   6945   7231   1048   1229  -1561       C  
ATOM   4202  O   MET B 251      49.277  41.433  46.879  1.00 52.00           O  
ANISOU 4202  O   MET B 251     6155   6547   7055   1030   1125  -1427       O  
ATOM   4203  CB  MET B 251      50.459  39.437  48.423  1.00 45.89           C  
ANISOU 4203  CB  MET B 251     5450   6224   5761   1049    999  -1451       C  
ATOM   4204  CG  MET B 251      50.934  38.297  49.329  1.00 55.92           C  
ANISOU 4204  CG  MET B 251     6756   7738   6752   1091    950  -1422       C  
ATOM   4205  SD  MET B 251      52.144  38.754  50.611  1.00 66.44           S  
ANISOU 4205  SD  MET B 251     8118   9319   7806   1051    944  -1685       S  
ATOM   4206  CE  MET B 251      53.557  39.313  49.649  1.00 50.33           C  
ANISOU 4206  CE  MET B 251     6046   7254   5821    947    808  -1783       C  
ATOM   4207  N   PRO B 252      48.880  42.740  48.669  1.00 48.72           N  
ANISOU 4207  N   PRO B 252     5780   6130   6599   1043   1384  -1741       N  
ATOM   4208  CA  PRO B 252      48.415  43.867  47.851  1.00 48.15           C  
ANISOU 4208  CA  PRO B 252     5682   5797   6815   1048   1464  -1727       C  
ATOM   4209  C   PRO B 252      49.429  44.352  46.825  1.00 52.63           C  
ANISOU 4209  C   PRO B 252     6262   6273   7463    959   1362  -1746       C  
ATOM   4210  O   PRO B 252      50.645  44.281  47.013  1.00 56.54           O  
ANISOU 4210  O   PRO B 252     6790   6889   7805    868   1278  -1878       O  
ATOM   4211  CB  PRO B 252      48.104  44.954  48.891  1.00 51.77           C  
ANISOU 4211  CB  PRO B 252     6182   6185   7304   1057   1669  -1958       C  
ATOM   4212  CG  PRO B 252      47.780  44.174  50.137  1.00 53.25           C  
ANISOU 4212  CG  PRO B 252     6387   6591   7256   1103   1715  -1993       C  
ATOM   4213  CD  PRO B 252      48.719  43.000  50.111  1.00 46.93           C  
ANISOU 4213  CD  PRO B 252     5597   6017   6216   1060   1521  -1930       C  
ATOM   4214  N   LYS B 253      48.889  44.817  45.706  1.00 55.68           N  
ANISOU 4214  N   LYS B 253     6608   6457   8090    993   1370  -1592       N  
ATOM   4215  CA  LYS B 253      49.687  45.240  44.564  1.00 53.44           C  
ANISOU 4215  CA  LYS B 253     6332   6071   7902    925   1286  -1553       C  
ATOM   4216  C   LYS B 253      50.487  46.515  44.869  1.00 50.98           C  
ANISOU 4216  C   LYS B 253     6074   5643   7654    829   1388  -1794       C  
ATOM   4217  O   LYS B 253      49.933  47.552  45.261  1.00 55.61           O  
ANISOU 4217  O   LYS B 253     6681   6052   8397    856   1564  -1895       O  
ATOM   4218  CB  LYS B 253      48.738  45.420  43.372  1.00 50.35           C  
ANISOU 4218  CB  LYS B 253     5883   5512   7737   1005   1280  -1309       C  
ATOM   4219  CG  LYS B 253      49.357  45.888  42.097  1.00 57.11           C  
ANISOU 4219  CG  LYS B 253     6747   6249   8702    959   1212  -1224       C  
ATOM   4220  CD  LYS B 253      48.340  45.845  40.947  1.00 65.67           C  
ANISOU 4220  CD  LYS B 253     7766   7232   9955   1051   1173   -955       C  
ATOM   4221  CE  LYS B 253      47.294  46.926  41.073  1.00 76.25           C  
ANISOU 4221  CE  LYS B 253     9067   8370  11533   1150   1347   -925       C  
ATOM   4222  NZ  LYS B 253      46.466  47.007  39.844  1.00 82.31           N  
ANISOU 4222  NZ  LYS B 253     9758   9055  12461   1238   1291   -654       N  
ATOM   4223  N   GLN B 254      51.790  46.445  44.625  1.00 51.19           N  
ANISOU 4223  N   GLN B 254     6117   5755   7577    715   1285  -1879       N  
ATOM   4224  CA  GLN B 254      52.742  47.493  44.981  1.00 56.02           C  
ANISOU 4224  CA  GLN B 254     6768   6303   8215    583   1356  -2131       C  
ATOM   4225  C   GLN B 254      52.997  48.417  43.801  1.00 53.60           C  
ANISOU 4225  C   GLN B 254     6466   5751   8149    539   1394  -2056       C  
ATOM   4226  O   GLN B 254      52.863  48.019  42.641  1.00 59.65           O  
ANISOU 4226  O   GLN B 254     7203   6483   8978    588   1304  -1818       O  
ATOM   4227  CB  GLN B 254      54.063  46.867  45.423  1.00 58.53           C  
ANISOU 4227  CB  GLN B 254     7074   6887   8278    479   1218  -2260       C  
ATOM   4228  CG  GLN B 254      53.968  46.026  46.678  1.00 67.65           C  
ANISOU 4228  CG  GLN B 254     8234   8302   9170    519   1186  -2342       C  
ATOM   4229  CD  GLN B 254      55.217  45.153  46.876  1.00 78.78           C  
ANISOU 4229  CD  GLN B 254     9609   9998  10327    463   1015  -2375       C  
ATOM   4230  OE1 GLN B 254      55.309  44.040  46.313  1.00 70.86           O  
ANISOU 4230  OE1 GLN B 254     8580   9097   9246    531    890  -2170       O  
ATOM   4231  NE2 GLN B 254      56.182  45.652  47.665  1.00 79.44           N  
ANISOU 4231  NE2 GLN B 254     9687  10211  10286    339   1011  -2636       N  
ATOM   4232  N   ALA B 255      53.358  49.659  44.114  1.00 51.35           N  
ANISOU 4232  N   ALA B 255     6227   5290   7992    443   1536  -2265       N  
ATOM   4233  CA  ALA B 255      53.676  50.640  43.084  1.00 53.96           C  
ANISOU 4233  CA  ALA B 255     6574   5366   8560    389   1602  -2205       C  
ATOM   4234  C   ALA B 255      54.718  50.098  42.111  1.00 59.63           C  
ANISOU 4234  C   ALA B 255     7253   6201   9203    315   1440  -2089       C  
ATOM   4235  O   ALA B 255      55.705  49.475  42.513  1.00 59.30           O  
ANISOU 4235  O   ALA B 255     7181   6399   8950    225   1322  -2203       O  
ATOM   4236  CB  ALA B 255      54.206  51.911  43.734  1.00 53.32           C  
ANISOU 4236  CB  ALA B 255     6556   5119   8584    247   1766  -2504       C  
ATOM   4237  N   GLY B 256      54.477  50.312  40.819  1.00 60.58           N  
ANISOU 4237  N   GLY B 256     7369   6163   9487    369   1436  -1849       N  
ATOM   4238  CA  GLY B 256      55.367  49.780  39.808  1.00 56.98           C  
ANISOU 4238  CA  GLY B 256     6881   5811   8957    319   1300  -1718       C  
ATOM   4239  C   GLY B 256      55.134  48.330  39.443  1.00 58.92           C  
ANISOU 4239  C   GLY B 256     7090   6281   9014    415   1121  -1536       C  
ATOM   4240  O   GLY B 256      55.960  47.746  38.723  1.00 58.09           O  
ANISOU 4240  O   GLY B 256     6965   6295   8810    378   1007  -1457       O  
ATOM   4241  N   TYR B 257      54.036  47.725  39.907  1.00 54.07           N  
ANISOU 4241  N   TYR B 257     6469   5722   8355    535   1106  -1469       N  
ATOM   4242  CA  TYR B 257      53.807  46.310  39.628  1.00 53.81           C  
ANISOU 4242  CA  TYR B 257     6411   5885   8151    607    948  -1313       C  
ATOM   4243  C   TYR B 257      53.712  46.050  38.126  1.00 55.74           C  
ANISOU 4243  C   TYR B 257     6650   6078   8451    646    863  -1068       C  
ATOM   4244  O   TYR B 257      54.337  45.118  37.604  1.00 57.22           O  
ANISOU 4244  O   TYR B 257     6837   6414   8488    632    734  -1002       O  
ATOM   4245  CB  TYR B 257      52.543  45.812  40.334  1.00 55.39           C  
ANISOU 4245  CB  TYR B 257     6595   6120   8331    716    971  -1270       C  
ATOM   4246  CG  TYR B 257      52.041  44.531  39.696  1.00 55.43           C  
ANISOU 4246  CG  TYR B 257     6577   6240   8244    788    829  -1058       C  
ATOM   4247  CD1 TYR B 257      52.645  43.300  39.984  1.00 49.76           C  
ANISOU 4247  CD1 TYR B 257     5869   5736   7302    773    710  -1073       C  
ATOM   4248  CD2 TYR B 257      51.009  44.559  38.757  1.00 54.72           C  
ANISOU 4248  CD2 TYR B 257     6456   6043   8291    867    811   -842       C  
ATOM   4249  CE1 TYR B 257      52.200  42.127  39.377  1.00 54.33           C  
ANISOU 4249  CE1 TYR B 257     6443   6389   7810    825    594   -895       C  
ATOM   4250  CE2 TYR B 257      50.563  43.406  38.140  1.00 53.41           C  
ANISOU 4250  CE2 TYR B 257     6272   5981   8042    906    677   -672       C  
ATOM   4251  CZ  TYR B 257      51.154  42.196  38.445  1.00 59.03           C  
ANISOU 4251  CZ  TYR B 257     7012   6874   8545    878    576   -707       C  
ATOM   4252  OH  TYR B 257      50.681  41.066  37.819  1.00 60.54           O  
ANISOU 4252  OH  TYR B 257     7199   7134   8669    906    458   -552       O  
ATOM   4253  N   GLU B 258      52.911  46.852  37.421  1.00 55.73           N  
ANISOU 4253  N   GLU B 258     6648   5873   8655    707    938   -927       N  
ATOM   4254  CA  GLU B 258      52.749  46.688  35.977  1.00 59.68           C  
ANISOU 4254  CA  GLU B 258     7145   6338   9194    749    858   -687       C  
ATOM   4255  C   GLU B 258      54.046  46.966  35.235  1.00 58.28           C  
ANISOU 4255  C   GLU B 258     6996   6157   8991    651    844   -700       C  
ATOM   4256  O   GLU B 258      54.368  46.292  34.252  1.00 58.24           O  
ANISOU 4256  O   GLU B 258     6998   6243   8885    659    732   -563       O  
ATOM   4257  CB  GLU B 258      51.648  47.619  35.462  1.00 64.77           C  
ANISOU 4257  CB  GLU B 258     7772   6773  10067    847    952   -528       C  
ATOM   4258  CG  GLU B 258      50.258  47.071  35.660  1.00 80.57           C  
ANISOU 4258  CG  GLU B 258     9711   8819  12082    964    914   -411       C  
ATOM   4259  CD  GLU B 258      50.004  45.824  34.835  1.00 98.27           C  
ANISOU 4259  CD  GLU B 258    11931  11231  14176    985    726   -244       C  
ATOM   4260  OE1 GLU B 258      50.745  45.582  33.843  1.00 99.74           O  
ANISOU 4260  OE1 GLU B 258    12154  11459  14283    942    639   -169       O  
ATOM   4261  OE2 GLU B 258      49.060  45.082  35.191  1.00106.67           O  
ANISOU 4261  OE2 GLU B 258    12942  12383  15205   1038    675   -195       O  
ATOM   4262  N   LYS B 259      54.794  47.967  35.689  1.00 59.67           N  
ANISOU 4262  N   LYS B 259     7187   6225   9259    551    966   -871       N  
ATOM   4263  CA  LYS B 259      56.032  48.370  35.034  1.00 58.43           C  
ANISOU 4263  CA  LYS B 259     7040   6050   9110    441    981   -889       C  
ATOM   4264  C   LYS B 259      57.097  47.280  35.095  1.00 59.37           C  
ANISOU 4264  C   LYS B 259     7134   6426   8999    385    848   -954       C  
ATOM   4265  O   LYS B 259      57.950  47.201  34.201  1.00 61.18           O  
ANISOU 4265  O   LYS B 259     7361   6691   9194    339    819   -881       O  
ATOM   4266  CB  LYS B 259      56.512  49.662  35.690  1.00 63.83           C  
ANISOU 4266  CB  LYS B 259     7738   6558   9955    325   1148  -1093       C  
ATOM   4267  CG  LYS B 259      57.886  50.089  35.359  1.00 77.97           C  
ANISOU 4267  CG  LYS B 259     9518   8352  11754    170   1178  -1178       C  
ATOM   4268  CD  LYS B 259      58.281  51.258  36.245  1.00 88.90           C  
ANISOU 4268  CD  LYS B 259    10915   9579  13282     31   1335  -1432       C  
ATOM   4269  CE  LYS B 259      57.481  52.502  35.919  1.00 89.08           C  
ANISOU 4269  CE  LYS B 259    11003   9260  13584     78   1517  -1349       C  
ATOM   4270  NZ  LYS B 259      57.898  53.614  36.807  1.00 97.11           N  
ANISOU 4270  NZ  LYS B 259    12050  10105  14743    -73   1682  -1628       N  
ATOM   4271  N   ARG B 260      57.073  46.440  36.137  1.00 54.88           N  
ANISOU 4271  N   ARG B 260     6544   6038   8269    399    780  -1079       N  
ATOM   4272  CA  ARG B 260      58.089  45.412  36.356  1.00 47.65           C  
ANISOU 4272  CA  ARG B 260     5598   5368   7137    367    666  -1143       C  
ATOM   4273  C   ARG B 260      57.724  44.044  35.785  1.00 51.42           C  
ANISOU 4273  C   ARG B 260     6096   5972   7469    473    534   -972       C  
ATOM   4274  O   ARG B 260      58.576  43.147  35.806  1.00 51.26           O  
ANISOU 4274  O   ARG B 260     6061   6135   7282    470    450   -994       O  
ATOM   4275  CB  ARG B 260      58.366  45.228  37.854  1.00 42.53           C  
ANISOU 4275  CB  ARG B 260     4921   4865   6373    328    666  -1367       C  
ATOM   4276  CG  ARG B 260      59.100  46.383  38.526  1.00 45.12           C  
ANISOU 4276  CG  ARG B 260     5223   5138   6783    182    768  -1600       C  
ATOM   4277  CD  ARG B 260      59.449  46.043  39.963  1.00 52.37           C  
ANISOU 4277  CD  ARG B 260     6108   6262   7527    147    735  -1817       C  
ATOM   4278  NE  ARG B 260      58.284  45.856  40.836  1.00 55.87           N  
ANISOU 4278  NE  ARG B 260     6593   6690   7946    239    770  -1838       N  
ATOM   4279  CZ  ARG B 260      57.655  46.846  41.481  1.00 60.43           C  
ANISOU 4279  CZ  ARG B 260     7205   7105   8651    213    906  -1971       C  
ATOM   4280  NH1 ARG B 260      58.048  48.105  41.338  1.00 53.47           N  
ANISOU 4280  NH1 ARG B 260     6334   6036   7944     93   1022  -2095       N  
ATOM   4281  NH2 ARG B 260      56.608  46.585  42.255  1.00 59.31           N  
ANISOU 4281  NH2 ARG B 260     7091   6971   8474    309    944  -1977       N  
ATOM   4282  N   ARG B 261      56.506  43.850  35.266  1.00 45.34           N  
ANISOU 4282  N   ARG B 261     5355   5113   6760    565    514   -806       N  
ATOM   4283  CA  ARG B 261      56.109  42.502  34.863  1.00 52.18           C  
ANISOU 4283  CA  ARG B 261     6243   6096   7485    641    390   -681       C  
ATOM   4284  C   ARG B 261      57.092  41.911  33.860  1.00 55.16           C  
ANISOU 4284  C   ARG B 261     6644   6563   7751    626    320   -614       C  
ATOM   4285  O   ARG B 261      57.474  40.734  33.970  1.00 47.58           O  
ANISOU 4285  O   ARG B 261     5700   5751   6626    658    238   -618       O  
ATOM   4286  CB  ARG B 261      54.699  42.514  34.289  1.00 44.87           C  
ANISOU 4286  CB  ARG B 261     5325   5066   6658    716    373   -511       C  
ATOM   4287  CG  ARG B 261      53.661  42.576  35.369  1.00 55.62           C  
ANISOU 4287  CG  ARG B 261     6656   6401   8075    758    422   -562       C  
ATOM   4288  CD  ARG B 261      52.296  42.853  34.808  1.00 62.79           C  
ANISOU 4288  CD  ARG B 261     7537   7199   9122    829    425   -394       C  
ATOM   4289  NE  ARG B 261      51.651  41.649  34.313  1.00 75.59           N  
ANISOU 4289  NE  ARG B 261     9158   8916  10647    865    298   -266       N  
ATOM   4290  CZ  ARG B 261      50.544  41.654  33.582  1.00 83.18           C  
ANISOU 4290  CZ  ARG B 261    10081   9833  11691    914    251    -98       C  
ATOM   4291  NH1 ARG B 261      49.977  42.814  33.264  1.00 85.11           N  
ANISOU 4291  NH1 ARG B 261    10282   9938  12116    958    328    -17       N  
ATOM   4292  NH2 ARG B 261      50.004  40.505  33.178  1.00 83.56           N  
ANISOU 4292  NH2 ARG B 261    10130   9976  11644    917    131    -11       N  
ATOM   4293  N   ASP B 262      57.514  42.721  32.877  1.00 51.86           N  
ANISOU 4293  N   ASP B 262     6233   6049   7424    587    366   -546       N  
ATOM   4294  CA  ASP B 262      58.449  42.260  31.857  1.00 52.50           C  
ANISOU 4294  CA  ASP B 262     6336   6210   7402    576    324   -478       C  
ATOM   4295  C   ASP B 262      59.823  41.940  32.443  1.00 53.93           C  
ANISOU 4295  C   ASP B 262     6469   6546   7477    523    325   -626       C  
ATOM   4296  O   ASP B 262      60.529  41.062  31.932  1.00 51.94           O  
ANISOU 4296  O   ASP B 262     6230   6418   7087    553    270   -589       O  
ATOM   4297  CB  ASP B 262      58.565  43.313  30.755  1.00 57.08           C  
ANISOU 4297  CB  ASP B 262     6931   6649   8110    545    397   -362       C  
ATOM   4298  CG  ASP B 262      57.384  43.285  29.798  1.00 68.41           C  
ANISOU 4298  CG  ASP B 262     8411   8003   9580    623    351   -161       C  
ATOM   4299  OD1 ASP B 262      56.532  42.383  29.925  1.00 77.51           O  
ANISOU 4299  OD1 ASP B 262     9578   9217  10657    684    254   -123       O  
ATOM   4300  OD2 ASP B 262      57.305  44.157  28.913  1.00 75.08           O  
ANISOU 4300  OD2 ASP B 262     9271   8730  10525    622    409    -33       O  
ATOM   4301  N   LEU B 263      60.224  42.651  33.494  1.00 51.55           N  
ANISOU 4301  N   LEU B 263     6107   6246   7234    447    389   -796       N  
ATOM   4302  CA  LEU B 263      61.520  42.404  34.103  1.00 51.64           C  
ANISOU 4302  CA  LEU B 263     6045   6435   7141    391    376   -939       C  
ATOM   4303  C   LEU B 263      61.596  41.004  34.676  1.00 48.50           C  
ANISOU 4303  C   LEU B 263     5652   6227   6549    484    275   -946       C  
ATOM   4304  O   LEU B 263      62.649  40.363  34.615  1.00 51.96           O  
ANISOU 4304  O   LEU B 263     6047   6830   6866    498    236   -964       O  
ATOM   4305  CB  LEU B 263      61.789  43.452  35.182  1.00 56.88           C  
ANISOU 4305  CB  LEU B 263     6649   7069   7895    278    453  -1140       C  
ATOM   4306  CG  LEU B 263      63.237  43.552  35.653  1.00 59.54           C  
ANISOU 4306  CG  LEU B 263     6879   7581   8162    176    447  -1295       C  
ATOM   4307  CD1 LEU B 263      64.106  44.180  34.542  1.00 51.64           C  
ANISOU 4307  CD1 LEU B 263     5846   6516   7259     90    513  -1235       C  
ATOM   4308  CD2 LEU B 263      63.317  44.354  36.940  1.00 62.24           C  
ANISOU 4308  CD2 LEU B 263     7174   7930   8543     69    494  -1525       C  
ATOM   4309  N   TYR B 264      60.490  40.497  35.201  1.00 50.95           N  
ANISOU 4309  N   TYR B 264     6011   6513   6836    556    242   -917       N  
ATOM   4310  CA  TYR B 264      60.467  39.147  35.745  1.00 50.65           C  
ANISOU 4310  CA  TYR B 264     5993   6625   6628    648    164   -902       C  
ATOM   4311  C   TYR B 264      60.195  38.069  34.686  1.00 46.30           C  
ANISOU 4311  C   TYR B 264     5522   6059   6010    729    102   -742       C  
ATOM   4312  O   TYR B 264      60.632  36.928  34.861  1.00 48.45           O  
ANISOU 4312  O   TYR B 264     5814   6453   6141    800     53   -725       O  
ATOM   4313  CB  TYR B 264      59.439  39.084  36.888  1.00 46.05           C  
ANISOU 4313  CB  TYR B 264     5422   6029   6048    676    175   -951       C  
ATOM   4314  CG  TYR B 264      59.881  39.975  38.021  1.00 50.77           C  
ANISOU 4314  CG  TYR B 264     5952   6681   6659    598    230  -1142       C  
ATOM   4315  CD1 TYR B 264      61.183  39.901  38.502  1.00 50.10           C  
ANISOU 4315  CD1 TYR B 264     5792   6783   6462    558    203  -1256       C  
ATOM   4316  CD2 TYR B 264      59.020  40.905  38.601  1.00 50.31           C  
ANISOU 4316  CD2 TYR B 264     5899   6494   6722    562    312  -1216       C  
ATOM   4317  CE1 TYR B 264      61.627  40.718  39.522  1.00 47.77           C  
ANISOU 4317  CE1 TYR B 264     5431   6558   6163    464    240  -1453       C  
ATOM   4318  CE2 TYR B 264      59.455  41.730  39.639  1.00 50.32           C  
ANISOU 4318  CE2 TYR B 264     5854   6541   6724    477    368  -1421       C  
ATOM   4319  CZ  TYR B 264      60.766  41.628  40.087  1.00 50.30           C  
ANISOU 4319  CZ  TYR B 264     5779   6737   6596    417    324  -1545       C  
ATOM   4320  OH  TYR B 264      61.224  42.425  41.107  1.00 54.72           O  
ANISOU 4320  OH  TYR B 264     6288   7365   7138    313    365  -1767       O  
ATOM   4321  N   LEU B 265      59.477  38.388  33.604  1.00 39.29           N  
ANISOU 4321  N   LEU B 265     4685   5028   5215    722    105   -625       N  
ATOM   4322  CA  LEU B 265      59.432  37.496  32.444  1.00 48.19           C  
ANISOU 4322  CA  LEU B 265     5890   6156   6262    772     48   -501       C  
ATOM   4323  C   LEU B 265      60.812  37.336  31.820  1.00 50.67           C  
ANISOU 4323  C   LEU B 265     6191   6563   6497    770     63   -510       C  
ATOM   4324  O   LEU B 265      61.155  36.252  31.334  1.00 46.58           O  
ANISOU 4324  O   LEU B 265     5732   6110   5857    836     25   -465       O  
ATOM   4325  CB  LEU B 265      58.447  38.026  31.391  1.00 44.11           C  
ANISOU 4325  CB  LEU B 265     5415   5498   5847    758     40   -375       C  
ATOM   4326  CG  LEU B 265      56.958  37.993  31.764  1.00 43.44           C  
ANISOU 4326  CG  LEU B 265     5334   5334   5838    777     13   -327       C  
ATOM   4327  CD1 LEU B 265      56.147  38.869  30.818  1.00 43.15           C  
ANISOU 4327  CD1 LEU B 265     5295   5173   5925    767     18   -204       C  
ATOM   4328  CD2 LEU B 265      56.446  36.569  31.700  1.00 47.05           C  
ANISOU 4328  CD2 LEU B 265     5855   5841   6183    822    -70   -283       C  
ATOM   4329  N   LEU B 266      61.617  38.414  31.829  1.00 46.30           N  
ANISOU 4329  N   LEU B 266     5559   6011   6022    692    131   -572       N  
ATOM   4330  CA  LEU B 266      62.879  38.430  31.099  1.00 46.16           C  
ANISOU 4330  CA  LEU B 266     5509   6071   5958    677    164   -563       C  
ATOM   4331  C   LEU B 266      63.820  37.329  31.581  1.00 49.86           C  
ANISOU 4331  C   LEU B 266     5944   6726   6275    751    130   -613       C  
ATOM   4332  O   LEU B 266      64.522  36.706  30.775  1.00 48.26           O  
ANISOU 4332  O   LEU B 266     5766   6586   5986    804    136   -557       O  
ATOM   4333  CB  LEU B 266      63.544  39.799  31.230  1.00 47.06           C  
ANISOU 4333  CB  LEU B 266     5528   6150   6203    557    252   -638       C  
ATOM   4334  CG  LEU B 266      64.979  39.931  30.681  1.00 49.77           C  
ANISOU 4334  CG  LEU B 266     5795   6598   6516    517    304   -649       C  
ATOM   4335  CD1 LEU B 266      65.044  39.657  29.186  1.00 39.34           C  
ANISOU 4335  CD1 LEU B 266     4559   5237   5152    562    324   -495       C  
ATOM   4336  CD2 LEU B 266      65.574  41.314  31.003  1.00 43.30           C  
ANISOU 4336  CD2 LEU B 266     4872   5731   5849    366    395   -749       C  
ATOM   4337  N   TYR B 267      63.849  37.073  32.888  1.00 51.00           N  
ANISOU 4337  N   TYR B 267     6034   6965   6378    767    101   -709       N  
ATOM   4338  CA  TYR B 267      64.685  35.989  33.407  1.00 50.09           C  
ANISOU 4338  CA  TYR B 267     5884   7034   6115    863     65   -729       C  
ATOM   4339  C   TYR B 267      64.334  34.646  32.759  1.00 45.94           C  
ANISOU 4339  C   TYR B 267     5488   6476   5492    984     34   -618       C  
ATOM   4340  O   TYR B 267      65.223  33.898  32.348  1.00 48.21           O  
ANISOU 4340  O   TYR B 267     5775   6856   5688   1066     43   -587       O  
ATOM   4341  CB  TYR B 267      64.539  35.910  34.921  1.00 44.74           C  
ANISOU 4341  CB  TYR B 267     5149   6459   5391    872     33   -826       C  
ATOM   4342  CG  TYR B 267      65.245  34.744  35.561  1.00 46.83           C  
ANISOU 4342  CG  TYR B 267     5385   6913   5497    997     -8   -817       C  
ATOM   4343  CD1 TYR B 267      66.635  34.663  35.569  1.00 50.99           C  
ANISOU 4343  CD1 TYR B 267     5787   7626   5960   1019     -6   -848       C  
ATOM   4344  CD2 TYR B 267      64.523  33.737  36.187  1.00 45.66           C  
ANISOU 4344  CD2 TYR B 267     5320   6759   5267   1098    -41   -765       C  
ATOM   4345  CE1 TYR B 267      67.289  33.587  36.178  1.00 51.72           C  
ANISOU 4345  CE1 TYR B 267     5842   7901   5907   1160    -43   -817       C  
ATOM   4346  CE2 TYR B 267      65.161  32.665  36.799  1.00 50.71           C  
ANISOU 4346  CE2 TYR B 267     5941   7561   5766   1231    -67   -732       C  
ATOM   4347  CZ  TYR B 267      66.539  32.597  36.791  1.00 48.57           C  
ANISOU 4347  CZ  TYR B 267     5546   7478   5429   1271    -71   -754       C  
ATOM   4348  OH  TYR B 267      67.156  31.539  37.411  1.00 45.49           O  
ANISOU 4348  OH  TYR B 267     5128   7254   4902   1427    -95   -701       O  
ATOM   4349  N   HIS B 268      63.037  34.328  32.650  1.00 40.67           N  
ANISOU 4349  N   HIS B 268     4929   5674   4851    993      2   -561       N  
ATOM   4350  CA  HIS B 268      62.630  33.058  32.061  1.00 44.00           C  
ANISOU 4350  CA  HIS B 268     5481   6047   5189   1079    -27   -478       C  
ATOM   4351  C   HIS B 268      62.748  33.051  30.540  1.00 47.74           C  
ANISOU 4351  C   HIS B 268     6031   6454   5652   1068    -15   -411       C  
ATOM   4352  O   HIS B 268      63.028  31.992  29.972  1.00 51.15           O  
ANISOU 4352  O   HIS B 268     6556   6894   5986   1147    -15   -377       O  
ATOM   4353  CB  HIS B 268      61.208  32.703  32.485  1.00 44.53           C  
ANISOU 4353  CB  HIS B 268     5618   6010   5292   1072    -67   -447       C  
ATOM   4354  CG  HIS B 268      61.087  32.444  33.950  1.00 49.35           C  
ANISOU 4354  CG  HIS B 268     6181   6697   5873   1107    -69   -496       C  
ATOM   4355  ND1 HIS B 268      61.585  31.301  34.549  1.00 46.14           N  
ANISOU 4355  ND1 HIS B 268     5800   6382   5350   1216    -72   -481       N  
ATOM   4356  CD2 HIS B 268      60.575  33.205  34.950  1.00 43.93           C  
ANISOU 4356  CD2 HIS B 268     5427   6017   5248   1057    -58   -556       C  
ATOM   4357  CE1 HIS B 268      61.360  31.361  35.851  1.00 49.09           C  
ANISOU 4357  CE1 HIS B 268     6122   6829   5702   1229    -72   -520       C  
ATOM   4358  NE2 HIS B 268      60.745  32.503  36.119  1.00 45.31           N  
ANISOU 4358  NE2 HIS B 268     5589   6302   5326   1130    -62   -576       N  
ATOM   4359  N   TYR B 269      62.555  34.196  29.862  1.00 40.56           N  
ANISOU 4359  N   TYR B 269     5097   5478   4837    979      7   -388       N  
ATOM   4360  CA  TYR B 269      62.860  34.247  28.427  1.00 45.25           C  
ANISOU 4360  CA  TYR B 269     5756   6046   5393    976     30   -318       C  
ATOM   4361  C   TYR B 269      64.346  34.024  28.158  1.00 44.44           C  
ANISOU 4361  C   TYR B 269     5601   6067   5215   1022     95   -342       C  
ATOM   4362  O   TYR B 269      64.707  33.356  27.187  1.00 48.94           O  
ANISOU 4362  O   TYR B 269     6259   6649   5687   1079    116   -299       O  
ATOM   4363  CB  TYR B 269      62.429  35.577  27.808  1.00 47.73           C  
ANISOU 4363  CB  TYR B 269     6046   6267   5823    884     54   -265       C  
ATOM   4364  CG  TYR B 269      60.950  35.689  27.589  1.00 55.80           C  
ANISOU 4364  CG  TYR B 269     7129   7175   6899    863    -11   -198       C  
ATOM   4365  CD1 TYR B 269      60.187  34.567  27.365  1.00 61.95           C  
ANISOU 4365  CD1 TYR B 269     8008   7936   7592    903    -87   -172       C  
ATOM   4366  CD2 TYR B 269      60.321  36.931  27.567  1.00 60.74           C  
ANISOU 4366  CD2 TYR B 269     7705   7704   7668    803     10   -156       C  
ATOM   4367  CE1 TYR B 269      58.824  34.668  27.157  1.00 72.83           C  
ANISOU 4367  CE1 TYR B 269     9415   9234   9025    873   -155   -109       C  
ATOM   4368  CE2 TYR B 269      58.967  37.045  27.353  1.00 53.40           C  
ANISOU 4368  CE2 TYR B 269     6807   6690   6794    799    -51    -79       C  
ATOM   4369  CZ  TYR B 269      58.224  35.908  27.160  1.00 66.60           C  
ANISOU 4369  CZ  TYR B 269     8556   8374   8374    829   -140    -57       C  
ATOM   4370  OH  TYR B 269      56.879  36.003  26.947  1.00 66.00           O  
ANISOU 4370  OH  TYR B 269     8484   8237   8355    815   -208     20       O  
ATOM   4371  N   LEU B 270      65.223  34.599  28.985  1.00 46.53           N  
ANISOU 4371  N   LEU B 270     5719   6434   5525    993    131   -415       N  
ATOM   4372  CA  LEU B 270      66.648  34.298  28.852  1.00 48.44           C  
ANISOU 4372  CA  LEU B 270     5878   6826   5701   1046    186   -435       C  
ATOM   4373  C   LEU B 270      66.909  32.823  29.110  1.00 50.41           C  
ANISOU 4373  C   LEU B 270     6187   7144   5821   1197    165   -426       C  
ATOM   4374  O   LEU B 270      67.680  32.181  28.390  1.00 52.01           O  
ANISOU 4374  O   LEU B 270     6419   7399   5942   1284    217   -394       O  
ATOM   4375  CB  LEU B 270      67.493  35.164  29.795  1.00 47.81           C  
ANISOU 4375  CB  LEU B 270     5608   6867   5691    970    208   -530       C  
ATOM   4376  CG  LEU B 270      67.625  36.650  29.424  1.00 51.83           C  
ANISOU 4376  CG  LEU B 270     6046   7306   6341    817    270   -545       C  
ATOM   4377  CD1 LEU B 270      68.379  37.441  30.474  1.00 50.10           C  
ANISOU 4377  CD1 LEU B 270     5647   7197   6190    718    283   -673       C  
ATOM   4378  CD2 LEU B 270      68.285  36.835  28.061  1.00 54.22           C  
ANISOU 4378  CD2 LEU B 270     6366   7602   6632    811    355   -459       C  
ATOM   4379  N   ASN B 271      66.269  32.262  30.128  1.00 50.37           N  
ANISOU 4379  N   ASN B 271     6207   7130   5801   1237    105   -448       N  
ATOM   4380  CA  ASN B 271      66.495  30.856  30.405  1.00 43.76           C  
ANISOU 4380  CA  ASN B 271     5439   6333   4856   1387    101   -423       C  
ATOM   4381  C   ASN B 271      66.046  29.986  29.236  1.00 47.18           C  
ANISOU 4381  C   ASN B 271     6060   6636   5231   1434    116   -367       C  
ATOM   4382  O   ASN B 271      66.690  28.981  28.915  1.00 52.73           O  
ANISOU 4382  O   ASN B 271     6822   7367   5847   1560    163   -347       O  
ATOM   4383  CB  ASN B 271      65.784  30.442  31.684  1.00 48.66           C  
ANISOU 4383  CB  ASN B 271     6067   6951   5472   1413     46   -437       C  
ATOM   4384  CG  ASN B 271      66.325  29.161  32.224  1.00 51.61           C  
ANISOU 4384  CG  ASN B 271     6463   7402   5743   1579     58   -403       C  
ATOM   4385  OD1 ASN B 271      67.538  29.008  32.311  1.00 55.12           O  
ANISOU 4385  OD1 ASN B 271     6804   8003   6138   1664     91   -404       O  
ATOM   4386  ND2 ASN B 271      65.452  28.198  32.509  1.00 49.57           N  
ANISOU 4386  ND2 ASN B 271     6342   7032   5462   1632     42   -360       N  
ATOM   4387  N   HIS B 272      64.931  30.338  28.599  1.00 49.68           N  
ANISOU 4387  N   HIS B 272     6472   6813   5590   1338     77   -346       N  
ATOM   4388  CA  HIS B 272      64.433  29.518  27.496  1.00 45.48           C  
ANISOU 4388  CA  HIS B 272     6120   6174   4986   1360     73   -313       C  
ATOM   4389  C   HIS B 272      65.334  29.643  26.281  1.00 50.74           C  
ANISOU 4389  C   HIS B 272     6810   6886   5585   1384    146   -297       C  
ATOM   4390  O   HIS B 272      65.604  28.653  25.598  1.00 51.56           O  
ANISOU 4390  O   HIS B 272     7041   6964   5586   1468    186   -298       O  
ATOM   4391  CB  HIS B 272      62.993  29.900  27.160  1.00 47.94           C  
ANISOU 4391  CB  HIS B 272     6498   6363   5353   1248     -4   -287       C  
ATOM   4392  CG  HIS B 272      61.978  29.157  27.970  1.00 49.79           C  
ANISOU 4392  CG  HIS B 272     6786   6520   5610   1250    -60   -292       C  
ATOM   4393  ND1 HIS B 272      61.884  29.280  29.340  1.00 49.26           N  
ANISOU 4393  ND1 HIS B 272     6623   6495   5598   1265    -65   -312       N  
ATOM   4394  CD2 HIS B 272      61.043  28.247  27.610  1.00 50.64           C  
ANISOU 4394  CD2 HIS B 272     7032   6520   5689   1232   -103   -283       C  
ATOM   4395  CE1 HIS B 272      60.918  28.499  29.787  1.00 48.74           C  
ANISOU 4395  CE1 HIS B 272     6634   6344   5541   1263   -100   -298       C  
ATOM   4396  NE2 HIS B 272      60.387  27.865  28.756  1.00 56.18           N  
ANISOU 4396  NE2 HIS B 272     7713   7188   6443   1234   -125   -283       N  
ATOM   4397  N   TYR B 273      65.816  30.856  26.015  1.00 46.63           N  
ANISOU 4397  N   TYR B 273     6171   6424   5123   1311    179   -284       N  
ATOM   4398  CA  TYR B 273      66.869  31.071  25.032  1.00 43.93           C  
ANISOU 4398  CA  TYR B 273     5811   6154   4726   1336    274   -262       C  
ATOM   4399  C   TYR B 273      68.072  30.155  25.307  1.00 51.70           C  
ANISOU 4399  C   TYR B 273     6754   7252   5639   1483    346   -286       C  
ATOM   4400  O   TYR B 273      68.500  29.384  24.436  1.00 49.81           O  
ANISOU 4400  O   TYR B 273     6621   7009   5294   1574    414   -275       O  
ATOM   4401  CB  TYR B 273      67.240  32.561  25.076  1.00 45.60           C  
ANISOU 4401  CB  TYR B 273     5868   6406   5050   1222    307   -249       C  
ATOM   4402  CG  TYR B 273      68.374  33.049  24.197  1.00 53.64           C  
ANISOU 4402  CG  TYR B 273     6824   7509   6048   1217    421   -215       C  
ATOM   4403  CD1 TYR B 273      68.773  32.365  23.045  1.00 53.26           C  
ANISOU 4403  CD1 TYR B 273     6893   7478   5867   1299    489   -179       C  
ATOM   4404  CD2 TYR B 273      69.059  34.203  24.535  1.00 56.52           C  
ANISOU 4404  CD2 TYR B 273     7012   7936   6529   1123    473   -226       C  
ATOM   4405  CE1 TYR B 273      69.827  32.833  22.259  1.00 46.86           C  
ANISOU 4405  CE1 TYR B 273     6016   6754   5036   1297    612   -139       C  
ATOM   4406  CE2 TYR B 273      70.110  34.675  23.755  1.00 57.61           C  
ANISOU 4406  CE2 TYR B 273     7076   8150   6662   1105    591   -187       C  
ATOM   4407  CZ  TYR B 273      70.492  33.984  22.629  1.00 55.03           C  
ANISOU 4407  CZ  TYR B 273     6859   7850   6199   1198    663   -136       C  
ATOM   4408  OH  TYR B 273      71.536  34.483  21.879  1.00 58.61           O  
ANISOU 4408  OH  TYR B 273     7230   8389   6651   1180    797    -89       O  
ATOM   4409  N   ASN B 274      68.591  30.185  26.541  1.00 52.46           N  
ANISOU 4409  N   ASN B 274     6696   7454   5781   1518    332   -318       N  
ATOM   4410  CA  ASN B 274      69.788  29.416  26.879  1.00 52.53           C  
ANISOU 4410  CA  ASN B 274     6625   7602   5731   1671    395   -320       C  
ATOM   4411  C   ASN B 274      69.536  27.914  26.862  1.00 51.73           C  
ANISOU 4411  C   ASN B 274     6694   7419   5541   1824    406   -306       C  
ATOM   4412  O   ASN B 274      70.455  27.146  26.576  1.00 61.93           O  
ANISOU 4412  O   ASN B 274     7990   8772   6767   1975    494   -289       O  
ATOM   4413  CB  ASN B 274      70.335  29.843  28.242  1.00 53.80           C  
ANISOU 4413  CB  ASN B 274     6574   7922   5946   1664    355   -356       C  
ATOM   4414  CG  ASN B 274      71.171  31.097  28.162  1.00 55.78           C  
ANISOU 4414  CG  ASN B 274     6627   8295   6272   1547    392   -384       C  
ATOM   4415  OD1 ASN B 274      71.952  31.274  27.227  1.00 62.70           O  
ANISOU 4415  OD1 ASN B 274     7470   9217   7135   1556    485   -355       O  
ATOM   4416  ND2 ASN B 274      71.026  31.972  29.148  1.00 52.02           N  
ANISOU 4416  ND2 ASN B 274     6020   7868   5875   1432    331   -446       N  
ATOM   4417  N   LEU B 275      68.317  27.476  27.151  1.00 50.47           N  
ANISOU 4417  N   LEU B 275     6674   7113   5390   1788    332   -311       N  
ATOM   4418  CA  LEU B 275      67.989  26.057  27.139  1.00 48.40           C  
ANISOU 4418  CA  LEU B 275     6589   6737   5064   1907    351   -302       C  
ATOM   4419  C   LEU B 275      67.537  25.557  25.770  1.00 56.15           C  
ANISOU 4419  C   LEU B 275     7782   7577   5974   1885    383   -319       C  
ATOM   4420  O   LEU B 275      67.935  24.463  25.360  1.00 56.25           O  
ANISOU 4420  O   LEU B 275     7923   7535   5914   2015    465   -328       O  
ATOM   4421  CB  LEU B 275      66.862  25.758  28.132  1.00 50.69           C  
ANISOU 4421  CB  LEU B 275     6925   6935   5400   1865    265   -299       C  
ATOM   4422  CG  LEU B 275      67.154  25.702  29.626  1.00 54.92           C  
ANISOU 4422  CG  LEU B 275     7322   7586   5958   1934    240   -280       C  
ATOM   4423  CD1 LEU B 275      65.853  25.430  30.381  1.00 52.00           C  
ANISOU 4423  CD1 LEU B 275     7031   7098   5628   1872    172   -271       C  
ATOM   4424  CD2 LEU B 275      68.171  24.637  29.927  1.00 49.78           C  
ANISOU 4424  CD2 LEU B 275     6667   7005   5240   2145    317   -236       C  
ATOM   4425  N   PHE B 276      66.688  26.315  25.064  1.00 55.75           N  
ANISOU 4425  N   PHE B 276     7777   7466   5938   1729    320   -326       N  
ATOM   4426  CA  PHE B 276      65.981  25.796  23.900  1.00 51.67           C  
ANISOU 4426  CA  PHE B 276     7469   6824   5338   1683    310   -350       C  
ATOM   4427  C   PHE B 276      66.316  26.475  22.580  1.00 58.87           C  
ANISOU 4427  C   PHE B 276     8403   7787   6177   1634    350   -338       C  
ATOM   4428  O   PHE B 276      65.748  26.084  21.557  1.00 62.90           O  
ANISOU 4428  O   PHE B 276     9088   8222   6589   1592    333   -364       O  
ATOM   4429  CB  PHE B 276      64.454  25.872  24.101  1.00 55.29           C  
ANISOU 4429  CB  PHE B 276     7992   7168   5849   1547    184   -354       C  
ATOM   4430  CG  PHE B 276      63.968  25.175  25.341  1.00 50.89           C  
ANISOU 4430  CG  PHE B 276     7433   6546   5358   1581    153   -355       C  
ATOM   4431  CD1 PHE B 276      64.156  23.811  25.504  1.00 56.16           C  
ANISOU 4431  CD1 PHE B 276     8234   7124   5980   1693    214   -376       C  
ATOM   4432  CD2 PHE B 276      63.308  25.875  26.334  1.00 43.52           C  
ANISOU 4432  CD2 PHE B 276     6375   5632   4530   1505     79   -330       C  
ATOM   4433  CE1 PHE B 276      63.703  23.158  26.655  1.00 56.43           C  
ANISOU 4433  CE1 PHE B 276     8273   7093   6074   1729    200   -354       C  
ATOM   4434  CE2 PHE B 276      62.841  25.237  27.485  1.00 53.40           C  
ANISOU 4434  CE2 PHE B 276     7628   6835   5827   1537     62   -321       C  
ATOM   4435  CZ  PHE B 276      63.040  23.867  27.639  1.00 56.06           C  
ANISOU 4435  CZ  PHE B 276     8098   7087   6117   1648    122   -324       C  
ATOM   4436  N   GLY B 277      67.202  27.456  22.556  1.00 57.88           N  
ANISOU 4436  N   GLY B 277     8113   7790   6088   1631    405   -301       N  
ATOM   4437  CA  GLY B 277      67.702  27.989  21.306  1.00 53.47           C  
ANISOU 4437  CA  GLY B 277     7578   7287   5451   1609    479   -273       C  
ATOM   4438  C   GLY B 277      67.247  29.419  21.038  1.00 53.25           C  
ANISOU 4438  C   GLY B 277     7463   7274   5495   1463    429   -210       C  
ATOM   4439  O   GLY B 277      66.341  29.963  21.672  1.00 58.45           O  
ANISOU 4439  O   GLY B 277     8073   7879   6258   1371    327   -197       O  
ATOM   4440  N   SER B 278      67.880  29.994  20.020  1.00 54.88           N  
ANISOU 4440  N   SER B 278     7664   7548   5642   1453    520   -161       N  
ATOM   4441  CA  SER B 278      67.798  31.407  19.684  1.00 63.11           C  
ANISOU 4441  CA  SER B 278     8611   8610   6759   1339    525    -78       C  
ATOM   4442  C   SER B 278      66.430  31.854  19.169  1.00 65.82           C  
ANISOU 4442  C   SER B 278     9053   8863   7091   1240    409    -24       C  
ATOM   4443  O   SER B 278      66.249  33.048  18.913  1.00 67.71           O  
ANISOU 4443  O   SER B 278     9224   9097   7407   1158    414     64       O  
ATOM   4444  CB  SER B 278      68.874  31.709  18.650  1.00 56.11           C  
ANISOU 4444  CB  SER B 278     7713   7819   5788   1371    674    -28       C  
ATOM   4445  OG  SER B 278      68.699  30.799  17.589  1.00 66.95           O  
ANISOU 4445  OG  SER B 278     9293   9179   6967   1436    695    -49       O  
ATOM   4446  N   GLY B 279      65.481  30.945  18.963  1.00 62.21           N  
ANISOU 4446  N   GLY B 279     8752   8338   6545   1245    311    -66       N  
ATOM   4447  CA  GLY B 279      64.126  31.389  18.696  1.00 57.76           C  
ANISOU 4447  CA  GLY B 279     8233   7713   6000   1149    179    -13       C  
ATOM   4448  C   GLY B 279      63.539  32.252  19.799  1.00 57.44           C  
ANISOU 4448  C   GLY B 279     8042   7621   6161   1085    118     15       C  
ATOM   4449  O   GLY B 279      62.611  33.027  19.545  1.00 56.51           O  
ANISOU 4449  O   GLY B 279     7910   7465   6095   1015     44     97       O  
ATOM   4450  N   TYR B 280      64.037  32.110  21.027  1.00 52.05           N  
ANISOU 4450  N   TYR B 280     7250   6943   5584   1117    147    -50       N  
ATOM   4451  CA  TYR B 280      63.582  32.900  22.156  1.00 49.07           C  
ANISOU 4451  CA  TYR B 280     6735   6525   5382   1060    106    -50       C  
ATOM   4452  C   TYR B 280      64.345  34.204  22.312  1.00 53.65           C  
ANISOU 4452  C   TYR B 280     7169   7138   6078   1013    194    -15       C  
ATOM   4453  O   TYR B 280      63.969  35.031  23.149  1.00 54.00           O  
ANISOU 4453  O   TYR B 280     7110   7134   6272    953    176    -22       O  
ATOM   4454  CB  TYR B 280      63.711  32.082  23.446  1.00 47.60           C  
ANISOU 4454  CB  TYR B 280     6510   6347   5230   1114     89   -140       C  
ATOM   4455  CG  TYR B 280      62.614  31.060  23.663  1.00 51.08           C  
ANISOU 4455  CG  TYR B 280     7064   6708   5635   1119     -6   -166       C  
ATOM   4456  CD1 TYR B 280      61.372  31.438  24.166  1.00 48.16           C  
ANISOU 4456  CD1 TYR B 280     6665   6269   5366   1048    -94   -144       C  
ATOM   4457  CD2 TYR B 280      62.813  29.722  23.359  1.00 53.30           C  
ANISOU 4457  CD2 TYR B 280     7481   6975   5795   1192      7   -213       C  
ATOM   4458  CE1 TYR B 280      60.369  30.508  24.364  1.00 53.23           C  
ANISOU 4458  CE1 TYR B 280     7393   6844   5987   1036   -173   -164       C  
ATOM   4459  CE2 TYR B 280      61.810  28.778  23.561  1.00 48.97           C  
ANISOU 4459  CE2 TYR B 280     7040   6337   5231   1175    -68   -242       C  
ATOM   4460  CZ  TYR B 280      60.598  29.179  24.064  1.00 56.73           C  
ANISOU 4460  CZ  TYR B 280     7973   7265   6314   1090   -161   -216       C  
ATOM   4461  OH  TYR B 280      59.610  28.249  24.278  1.00 62.54           O  
ANISOU 4461  OH  TYR B 280     8797   7917   7047   1058   -228   -241       O  
ATOM   4462  N   ARG B 281      65.391  34.417  21.518  1.00 53.94           N  
ANISOU 4462  N   ARG B 281     7197   7245   6052   1031    301     17       N  
ATOM   4463  CA  ARG B 281      66.212  35.602  21.704  1.00 54.27           C  
ANISOU 4463  CA  ARG B 281     7090   7313   6218    968    399     40       C  
ATOM   4464  C   ARG B 281      65.451  36.890  21.384  1.00 55.02           C  
ANISOU 4464  C   ARG B 281     7175   7303   6430    877    393    140       C  
ATOM   4465  O   ARG B 281      65.702  37.923  22.010  1.00 56.48           O  
ANISOU 4465  O   ARG B 281     7235   7447   6778    800    444    126       O  
ATOM   4466  CB  ARG B 281      67.479  35.490  20.860  1.00 56.19           C  
ANISOU 4466  CB  ARG B 281     7322   7659   6368   1008    529     66       C  
ATOM   4467  CG  ARG B 281      68.372  36.713  20.985  1.00 61.50           C  
ANISOU 4467  CG  ARG B 281     7831   8357   7178    920    642     91       C  
ATOM   4468  CD  ARG B 281      69.417  36.763  19.920  1.00 57.93           C  
ANISOU 4468  CD  ARG B 281     7379   7993   6639    944    782    156       C  
ATOM   4469  NE  ARG B 281      70.380  37.832  20.178  1.00 58.96           N  
ANISOU 4469  NE  ARG B 281     7327   8156   6918    845    898    162       N  
ATOM   4470  CZ  ARG B 281      70.295  39.051  19.648  1.00 64.39           C  
ANISOU 4470  CZ  ARG B 281     8000   8758   7707    741    976    266       C  
ATOM   4471  NH1 ARG B 281      69.289  39.348  18.833  1.00 59.03           N  
ANISOU 4471  NH1 ARG B 281     7472   7977   6982    745    939    386       N  
ATOM   4472  NH2 ARG B 281      71.215  39.970  19.930  1.00 60.00           N  
ANISOU 4472  NH2 ARG B 281     7276   8221   7301    632   1090    255       N  
ATOM   4473  N   SER B 282      64.526  36.861  20.423  1.00 54.86           N  
ANISOU 4473  N   SER B 282     7281   7237   6328    884    334    240       N  
ATOM   4474  CA  SER B 282      63.818  38.091  20.077  1.00 55.75           C  
ANISOU 4474  CA  SER B 282     7376   7253   6552    824    335    365       C  
ATOM   4475  C   SER B 282      62.968  38.538  21.258  1.00 52.27           C  
ANISOU 4475  C   SER B 282     6857   6714   6288    787    272    318       C  
ATOM   4476  O   SER B 282      62.977  39.719  21.613  1.00 53.35           O  
ANISOU 4476  O   SER B 282     6910   6763   6599    728    338    348       O  
ATOM   4477  CB  SER B 282      62.995  37.907  18.803  1.00 57.48           C  
ANISOU 4477  CB  SER B 282     7734   7483   6622    852    266    491       C  
ATOM   4478  OG  SER B 282      62.323  36.667  18.833  1.00 77.17           O  
ANISOU 4478  OG  SER B 282    10322  10009   8989    889    141    417       O  
ATOM   4479  N   SER B 283      62.244  37.602  21.887  1.00 52.04           N  
ANISOU 4479  N   SER B 283     6860   6691   6221    819    161    240       N  
ATOM   4480  CA  SER B 283      61.432  37.939  23.055  1.00 52.18           C  
ANISOU 4480  CA  SER B 283     6804   6630   6391    793    113    191       C  
ATOM   4481  C   SER B 283      62.263  38.617  24.132  1.00 52.51           C  
ANISOU 4481  C   SER B 283     6718   6666   6568    746    202     90       C  
ATOM   4482  O   SER B 283      61.848  39.627  24.708  1.00 51.99           O  
ANISOU 4482  O   SER B 283     6585   6502   6667    695    232     87       O  
ATOM   4483  CB  SER B 283      60.774  36.687  23.626  1.00 57.40           C  
ANISOU 4483  CB  SER B 283     7514   7316   6979    832      7    116       C  
ATOM   4484  OG  SER B 283      59.864  36.124  22.706  1.00 63.95           O  
ANISOU 4484  OG  SER B 283     8451   8145   7702    845    -89    189       O  
ATOM   4485  N   ALA B 284      63.444  38.074  24.422  1.00 51.28           N  
ANISOU 4485  N   ALA B 284     6521   6620   6342    763    246      0       N  
ATOM   4486  CA  ALA B 284      64.276  38.677  25.454  1.00 49.23           C  
ANISOU 4486  CA  ALA B 284     6122   6391   6191    704    311   -109       C  
ATOM   4487  C   ALA B 284      64.779  40.044  25.010  1.00 52.93           C  
ANISOU 4487  C   ALA B 284     6530   6791   6790    611    426    -60       C  
ATOM   4488  O   ALA B 284      64.691  41.026  25.762  1.00 55.42           O  
ANISOU 4488  O   ALA B 284     6766   7024   7268    528    468   -119       O  
ATOM   4489  CB  ALA B 284      65.431  37.743  25.813  1.00 44.20           C  
ANISOU 4489  CB  ALA B 284     5437   5916   5442    759    323   -195       C  
ATOM   4490  N   MET B 285      65.267  40.138  23.768  1.00 50.35           N  
ANISOU 4490  N   MET B 285     6251   6484   6397    620    490     52       N  
ATOM   4491  CA  MET B 285      65.835  41.393  23.283  1.00 56.45           C  
ANISOU 4491  CA  MET B 285     6968   7186   7293    529    621    118       C  
ATOM   4492  C   MET B 285      64.767  42.479  23.172  1.00 54.29           C  
ANISOU 4492  C   MET B 285     6731   6724   7173    493    632    215       C  
ATOM   4493  O   MET B 285      65.026  43.655  23.469  1.00 56.31           O  
ANISOU 4493  O   MET B 285     6918   6865   7611    396    737    203       O  
ATOM   4494  CB  MET B 285      66.503  41.171  21.932  1.00 62.81           C  
ANISOU 4494  CB  MET B 285     7833   8064   7969    563    693    236       C  
ATOM   4495  CG  MET B 285      67.279  42.374  21.445  1.00 74.90           C  
ANISOU 4495  CG  MET B 285     9297   9539   9624    464    853    310       C  
ATOM   4496  SD  MET B 285      68.816  42.600  22.372  1.00 85.63           S  
ANISOU 4496  SD  MET B 285    10449  11007  11078    359    944    141       S  
ATOM   4497  CE  MET B 285      68.416  43.981  23.424  1.00 88.77           C  
ANISOU 4497  CE  MET B 285    10767  11220  11742    211    978     55       C  
ATOM   4498  N   SER B 286      63.555  42.100  22.769  1.00 55.13           N  
ANISOU 4498  N   SER B 286     6938   6793   7216    570    530    308       N  
ATOM   4499  CA  SER B 286      62.451  43.056  22.705  1.00 59.25           C  
ANISOU 4499  CA  SER B 286     7478   7151   7884    566    531    415       C  
ATOM   4500  C   SER B 286      62.204  43.727  24.057  1.00 60.23           C  
ANISOU 4500  C   SER B 286     7515   7167   8202    507    561    282       C  
ATOM   4501  O   SER B 286      62.018  44.943  24.135  1.00 62.55           O  
ANISOU 4501  O   SER B 286     7786   7297   8683    457    660    326       O  
ATOM   4502  CB  SER B 286      61.193  42.341  22.230  1.00 60.25           C  
ANISOU 4502  CB  SER B 286     7693   7302   7898    654    388    506       C  
ATOM   4503  OG  SER B 286      60.063  43.146  22.462  1.00 77.66           O  
ANISOU 4503  OG  SER B 286     9880   9368  10257    668    376    586       O  
ATOM   4504  N   ILE B 287      62.199  42.944  25.135  1.00 60.10           N  
ANISOU 4504  N   ILE B 287     7460   7236   8138    515    486    119       N  
ATOM   4505  CA  ILE B 287      61.992  43.493  26.471  1.00 54.71           C  
ANISOU 4505  CA  ILE B 287     6704   6483   7602    461    512    -27       C  
ATOM   4506  C   ILE B 287      63.141  44.398  26.882  1.00 55.70           C  
ANISOU 4506  C   ILE B 287     6738   6581   7843    337    637   -137       C  
ATOM   4507  O   ILE B 287      62.922  45.472  27.453  1.00 61.51           O  
ANISOU 4507  O   ILE B 287     7443   7166   8763    265    720   -196       O  
ATOM   4508  CB  ILE B 287      61.795  42.349  27.471  1.00 50.26           C  
ANISOU 4508  CB  ILE B 287     6125   6045   6924    508    405   -156       C  
ATOM   4509  CG1 ILE B 287      60.445  41.665  27.230  1.00 47.06           C  
ANISOU 4509  CG1 ILE B 287     5796   5621   6464    597    297    -61       C  
ATOM   4510  CG2 ILE B 287      61.952  42.860  28.887  1.00 46.30           C  
ANISOU 4510  CG2 ILE B 287     5540   5527   6526    440    443   -336       C  
ATOM   4511  CD1 ILE B 287      60.208  40.434  28.123  1.00 46.53           C  
ANISOU 4511  CD1 ILE B 287     5732   5664   6283    645    203   -161       C  
ATOM   4512  N   ILE B 288      64.384  43.985  26.614  1.00 59.81           N  
ANISOU 4512  N   ILE B 288     7210   7247   8267    306    660   -175       N  
ATOM   4513  CA  ILE B 288      65.533  44.796  27.014  1.00 59.84           C  
ANISOU 4513  CA  ILE B 288     7100   7254   8380    167    770   -289       C  
ATOM   4514  C   ILE B 288      65.521  46.138  26.290  1.00 63.69           C  
ANISOU 4514  C   ILE B 288     7611   7537   9052     86    914   -177       C  
ATOM   4515  O   ILE B 288      65.822  47.181  26.881  1.00 63.61           O  
ANISOU 4515  O   ILE B 288     7539   7406   9222    -44   1015   -282       O  
ATOM   4516  CB  ILE B 288      66.847  44.031  26.757  1.00 59.58           C  
ANISOU 4516  CB  ILE B 288     6993   7437   8206    169    767   -323       C  
ATOM   4517  CG1 ILE B 288      66.971  42.835  27.708  1.00 53.40           C  
ANISOU 4517  CG1 ILE B 288     6172   6843   7276    245    645   -448       C  
ATOM   4518  CG2 ILE B 288      68.055  44.976  26.870  1.00 55.71           C  
ANISOU 4518  CG2 ILE B 288     6372   6951   7846      6    895   -402       C  
ATOM   4519  CD1 ILE B 288      68.209  41.959  27.465  1.00 48.42           C  
ANISOU 4519  CD1 ILE B 288     5466   6430   6502    287    642   -464       C  
ATOM   4520  N   ASP B 289      65.142  46.138  25.009  1.00 67.23           N  
ANISOU 4520  N   ASP B 289     8156   7936   9454    162    931     41       N  
ATOM   4521  CA  ASP B 289      65.100  47.385  24.249  1.00 62.31           C  
ANISOU 4521  CA  ASP B 289     7565   7115   8995    108   1076    190       C  
ATOM   4522  C   ASP B 289      64.078  48.364  24.819  1.00 67.41           C  
ANISOU 4522  C   ASP B 289     8237   7526   9847     98   1118    187       C  
ATOM   4523  O   ASP B 289      64.370  49.559  24.947  1.00 66.93           O  
ANISOU 4523  O   ASP B 289     8155   7278   9996    -11   1270    171       O  
ATOM   4524  CB  ASP B 289      64.792  47.093  22.781  1.00 65.01           C  
ANISOU 4524  CB  ASP B 289     8013   7485   9204    214   1064    436       C  
ATOM   4525  CG  ASP B 289      66.009  46.583  22.012  1.00 71.63           C  
ANISOU 4525  CG  ASP B 289     8829   8492   9896    197   1113    464       C  
ATOM   4526  OD1 ASP B 289      67.154  46.811  22.485  1.00 70.76           O  
ANISOU 4526  OD1 ASP B 289     8601   8433   9851     81   1196    333       O  
ATOM   4527  OD2 ASP B 289      65.815  45.969  20.931  1.00 67.98           O  
ANISOU 4527  OD2 ASP B 289     8460   8118   9252    298   1070    614       O  
ATOM   4528  N   ASP B 290      62.877  47.880  25.171  1.00 68.82           N  
ANISOU 4528  N   ASP B 290     8461   7704   9983    210    998    199       N  
ATOM   4529  CA  ASP B 290      61.828  48.767  25.678  1.00 67.38           C  
ANISOU 4529  CA  ASP B 290     8300   7306   9996    230   1046    211       C  
ATOM   4530  C   ASP B 290      62.241  49.441  26.981  1.00 70.77           C  
ANISOU 4530  C   ASP B 290     8661   7646  10582    100   1132    -35       C  
ATOM   4531  O   ASP B 290      62.004  50.640  27.171  1.00 77.52           O  
ANISOU 4531  O   ASP B 290     9532   8263  11661     47   1272    -37       O  
ATOM   4532  CB  ASP B 290      60.530  47.990  25.883  1.00 68.50           C  
ANISOU 4532  CB  ASP B 290     8475   7505  10049    367    897    255       C  
ATOM   4533  CG  ASP B 290      59.978  47.438  24.596  1.00 80.81           C  
ANISOU 4533  CG  ASP B 290    10102   9139  11462    480    806    487       C  
ATOM   4534  OD1 ASP B 290      60.509  47.807  23.530  1.00 90.26           O  
ANISOU 4534  OD1 ASP B 290    11336  10321  12639    469    875    636       O  
ATOM   4535  OD2 ASP B 290      59.035  46.615  24.646  1.00 86.77           O  
ANISOU 4535  OD2 ASP B 290    10875   9980  12115    571    666    517       O  
ATOM   4536  N   TYR B 291      62.850  48.687  27.898  1.00 63.55           N  
ANISOU 4536  N   TYR B 291     7675   6921   9549     49   1052   -247       N  
ATOM   4537  CA  TYR B 291      63.260  49.278  29.168  1.00 60.73           C  
ANISOU 4537  CA  TYR B 291     7250   6521   9304    -83   1114   -500       C  
ATOM   4538  C   TYR B 291      64.356  50.315  28.965  1.00 68.55           C  
ANISOU 4538  C   TYR B 291     8191   7407  10447   -260   1269   -555       C  
ATOM   4539  O   TYR B 291      64.381  51.342  29.653  1.00 66.96           O  
ANISOU 4539  O   TYR B 291     7980   7027  10435   -379   1384   -701       O  
ATOM   4540  CB  TYR B 291      63.734  48.186  30.124  1.00 58.50           C  
ANISOU 4540  CB  TYR B 291     6895   6502   8830    -85    982   -684       C  
ATOM   4541  CG  TYR B 291      62.647  47.505  30.912  1.00 62.67           C  
ANISOU 4541  CG  TYR B 291     7456   7076   9279     29    876   -724       C  
ATOM   4542  CD1 TYR B 291      61.697  48.244  31.611  1.00 59.96           C  
ANISOU 4542  CD1 TYR B 291     7146   6554   9083     35    939   -785       C  
ATOM   4543  CD2 TYR B 291      62.558  46.116  30.947  1.00 66.10           C  
ANISOU 4543  CD2 TYR B 291     7895   7722   9500    134    731   -695       C  
ATOM   4544  CE1 TYR B 291      60.707  47.616  32.336  1.00 62.63           C  
ANISOU 4544  CE1 TYR B 291     7503   6944   9350    137    857   -814       C  
ATOM   4545  CE2 TYR B 291      61.555  45.474  31.667  1.00 59.42           C  
ANISOU 4545  CE2 TYR B 291     7077   6911   8589    228    648   -719       C  
ATOM   4546  CZ  TYR B 291      60.640  46.230  32.360  1.00 60.23           C  
ANISOU 4546  CZ  TYR B 291     7196   6855   8834    227    711   -776       C  
ATOM   4547  OH  TYR B 291      59.650  45.607  33.076  1.00 57.19           O  
ANISOU 4547  OH  TYR B 291     6828   6511   8389    317    644   -794       O  
ATOM   4548  N   LEU B 292      65.279  50.062  28.031  1.00 70.87           N  
ANISOU 4548  N   LEU B 292     8455   7806  10666   -288   1287   -450       N  
ATOM   4549  CA  LEU B 292      66.311  51.054  27.744  1.00 73.30           C  
ANISOU 4549  CA  LEU B 292     8707   8010  11133   -466   1450   -477       C  
ATOM   4550  C   LEU B 292      65.690  52.323  27.178  1.00 77.36           C  
ANISOU 4550  C   LEU B 292     9318   8191  11884   -475   1616   -323       C  
ATOM   4551  O   LEU B 292      66.112  53.434  27.508  1.00 82.91           O  
ANISOU 4551  O   LEU B 292    10000   8698  12803   -641   1773   -428       O  
ATOM   4552  CB  LEU B 292      67.349  50.491  26.773  1.00 64.34           C  
ANISOU 4552  CB  LEU B 292     7521   7060   9864   -471   1451   -364       C  
ATOM   4553  CG  LEU B 292      68.245  49.372  27.290  1.00 62.40           C  
ANISOU 4553  CG  LEU B 292     7155   7134   9421   -475   1328   -512       C  
ATOM   4554  CD1 LEU B 292      69.262  48.984  26.246  1.00 59.42           C  
ANISOU 4554  CD1 LEU B 292     6730   6902   8947   -474   1372   -387       C  
ATOM   4555  CD2 LEU B 292      68.917  49.770  28.586  1.00 69.34           C  
ANISOU 4555  CD2 LEU B 292     7902   8068  10377   -649   1333   -796       C  
ATOM   4556  N   ARG B 293      64.695  52.174  26.307  1.00 74.14           N  
ANISOU 4556  N   ARG B 293     9017   7716  11439   -299   1587    -70       N  
ATOM   4557  CA  ARG B 293      63.944  53.329  25.845  1.00 72.63           C  
ANISOU 4557  CA  ARG B 293     8915   7213  11466   -264   1731    101       C  
ATOM   4558  C   ARG B 293      63.256  54.021  27.023  1.00 71.62           C  
ANISOU 4558  C   ARG B 293     8801   6888  11525   -293   1785    -80       C  
ATOM   4559  O   ARG B 293      63.522  55.192  27.312  1.00 74.78           O  
ANISOU 4559  O   ARG B 293     9213   7035  12164   -423   1967   -159       O  
ATOM   4560  CB  ARG B 293      62.962  52.886  24.753  1.00 76.03           C  
ANISOU 4560  CB  ARG B 293     9434   7675  11779    -54   1647    401       C  
ATOM   4561  CG  ARG B 293      62.214  54.014  24.069  1.00 86.49           C  
ANISOU 4561  CG  ARG B 293    10846   8715  13303     20   1788    645       C  
ATOM   4562  CD  ARG B 293      61.703  53.583  22.694  1.00 94.21           C  
ANISOU 4562  CD  ARG B 293    11889   9792  14115    186   1711    965       C  
ATOM   4563  NE  ARG B 293      60.602  54.418  22.205  1.00106.73           N  
ANISOU 4563  NE  ARG B 293    13544  11159  15849    325   1778   1213       N  
ATOM   4564  CZ  ARG B 293      60.756  55.502  21.441  1.00114.52           C  
ANISOU 4564  CZ  ARG B 293    14589  11926  16998    323   1964   1431       C  
ATOM   4565  NH1 ARG B 293      61.970  55.899  21.075  1.00118.47           N  
ANISOU 4565  NH1 ARG B 293    15084  12390  17540    171   2108   1421       N  
ATOM   4566  NH2 ARG B 293      59.696  56.194  21.043  1.00113.69           N  
ANISOU 4566  NH2 ARG B 293    14538  11638  17021    479   2013   1671       N  
ATOM   4567  N   MET B 294      62.386  53.295  27.735  1.00 72.44           N  
ANISOU 4567  N   MET B 294     8904   7099  11521   -179   1642   -159       N  
ATOM   4568  CA  MET B 294      61.663  53.857  28.879  1.00 70.45           C  
ANISOU 4568  CA  MET B 294     8666   6684  11416   -185   1695   -332       C  
ATOM   4569  C   MET B 294      62.593  54.521  29.897  1.00 74.17           C  
ANISOU 4569  C   MET B 294     9086   7093  12002   -409   1799   -642       C  
ATOM   4570  O   MET B 294      62.280  55.592  30.425  1.00 76.79           O  
ANISOU 4570  O   MET B 294     9464   7155  12559   -470   1954   -745       O  
ATOM   4571  CB  MET B 294      60.849  52.758  29.564  1.00 69.24           C  
ANISOU 4571  CB  MET B 294     8497   6730  11082    -58   1514   -397       C  
ATOM   4572  CG  MET B 294      60.310  53.156  30.930  1.00 74.89           C  
ANISOU 4572  CG  MET B 294     9211   7348  11895    -82   1561   -630       C  
ATOM   4573  SD  MET B 294      59.615  51.774  31.870  1.00 78.54           S  
ANISOU 4573  SD  MET B 294     9638   8083  12121     30   1362   -732       S  
ATOM   4574  CE  MET B 294      58.470  51.079  30.670  1.00 77.55           C  
ANISOU 4574  CE  MET B 294     9550   7997  11919    245   1248   -388       C  
ATOM   4575  N   LEU B 295      63.738  53.909  30.187  1.00 74.00           N  
ANISOU 4575  N   LEU B 295     8965   7321  11830   -534   1718   -800       N  
ATOM   4576  CA  LEU B 295      64.714  54.525  31.085  1.00 68.65           C  
ANISOU 4576  CA  LEU B 295     8214   6626  11244   -770   1797  -1095       C  
ATOM   4577  C   LEU B 295      65.575  55.516  30.318  1.00 68.77           C  
ANISOU 4577  C   LEU B 295     8221   6455  11452   -933   1978  -1028       C  
ATOM   4578  O   LEU B 295      66.498  56.099  30.874  1.00 75.45           O  
ANISOU 4578  O   LEU B 295     8994   7277  12396  -1161   2057  -1256       O  
ATOM   4579  CB  LEU B 295      65.593  53.463  31.756  1.00 68.35           C  
ANISOU 4579  CB  LEU B 295     8048   6958  10964   -828   1628  -1281       C  
ATOM   4580  CG  LEU B 295      64.877  52.363  32.558  1.00 71.17           C  
ANISOU 4580  CG  LEU B 295     8407   7525  11109   -677   1451  -1344       C  
ATOM   4581  CD1 LEU B 295      65.808  51.221  32.907  1.00 67.19           C  
ANISOU 4581  CD1 LEU B 295     7784   7385  10360   -692   1292  -1438       C  
ATOM   4582  CD2 LEU B 295      64.277  52.924  33.834  1.00 71.37           C  
ANISOU 4582  CD2 LEU B 295     8464   7436  11216   -721   1497  -1579       C  
TER    4583      LEU B 295                                                      
HETATM 4584  PB  ADP A 301      62.776  19.434  18.724  1.00 94.59           P  
HETATM 4585  O1B ADP A 301      63.058  18.047  18.180  1.00 82.70           O  
HETATM 4586  O2B ADP A 301      63.470  19.717  20.047  1.00100.17           O  
HETATM 4587  O3B ADP A 301      61.299  19.774  18.681  1.00 96.19           O  
HETATM 4588  PA  ADP A 301      63.464  22.110  17.891  1.00 76.58           P  
HETATM 4589  O1A ADP A 301      62.710  22.703  16.710  1.00 72.25           O  
HETATM 4590  O2A ADP A 301      63.129  22.485  19.323  1.00 73.57           O  
HETATM 4591  O3A ADP A 301      63.477  20.498  17.713  1.00 84.28           O  
HETATM 4592  O5' ADP A 301      65.031  22.460  17.685  1.00 75.40           O  
HETATM 4593  C5' ADP A 301      65.996  22.544  18.737  1.00 69.21           C  
HETATM 4594  C4' ADP A 301      67.137  23.518  18.401  1.00 68.88           C  
HETATM 4595  O4' ADP A 301      67.388  23.665  16.991  1.00 70.02           O  
HETATM 4596  C3' ADP A 301      66.831  24.926  18.877  1.00 73.49           C  
HETATM 4597  O3' ADP A 301      68.079  25.439  19.370  1.00 73.03           O  
HETATM 4598  C2' ADP A 301      66.344  25.686  17.643  1.00 66.84           C  
HETATM 4599  O2' ADP A 301      66.624  27.093  17.703  1.00 61.08           O  
HETATM 4600  C1' ADP A 301      67.135  25.020  16.539  1.00 62.33           C  
HETATM 4601  N9  ADP A 301      66.481  24.914  15.213  1.00 50.95           N  
HETATM 4602  C8  ADP A 301      65.334  24.261  14.923  1.00 52.68           C  
HETATM 4603  N7  ADP A 301      65.055  24.305  13.595  1.00 48.33           N  
HETATM 4604  C5  ADP A 301      66.059  24.988  13.024  1.00 48.56           C  
HETATM 4605  C6  ADP A 301      66.408  25.398  11.655  1.00 41.65           C  
HETATM 4606  N6  ADP A 301      65.609  25.068  10.612  1.00 40.39           N  
HETATM 4607  N1  ADP A 301      67.547  26.094  11.487  1.00 44.64           N  
HETATM 4608  C2  ADP A 301      68.354  26.416  12.504  1.00 45.94           C  
HETATM 4609  N3  ADP A 301      68.106  26.075  13.769  1.00 52.98           N  
HETATM 4610  C4  ADP A 301      66.992  25.380  14.084  1.00 47.88           C  
HETATM 4611  S   SO4 A 302      30.666  35.033  18.401  1.00 75.72           S  
HETATM 4612  O1  SO4 A 302      32.063  35.300  17.998  1.00 75.57           O  
HETATM 4613  O2  SO4 A 302      29.817  34.914  17.218  1.00 77.61           O  
HETATM 4614  O3  SO4 A 302      30.523  33.797  19.199  1.00 76.15           O  
HETATM 4615  O4  SO4 A 302      30.232  36.180  19.189  1.00 72.22           O  
HETATM 4616  S   SO4 A 303      68.898  33.103   6.367  1.00 69.92           S  
HETATM 4617  O1  SO4 A 303      69.784  33.908   5.526  1.00 74.46           O  
HETATM 4618  O2  SO4 A 303      68.373  32.001   5.570  1.00 68.50           O  
HETATM 4619  O3  SO4 A 303      69.568  32.489   7.511  1.00 55.18           O  
HETATM 4620  O4  SO4 A 303      67.825  33.984   6.845  1.00 67.14           O  
HETATM 4621  S   SO4 A 304      34.784  13.471  37.599  1.00121.49           S  
HETATM 4622  O1  SO4 A 304      34.038  14.655  37.176  1.00103.79           O  
HETATM 4623  O2  SO4 A 304      35.064  12.593  36.463  1.00128.01           O  
HETATM 4624  O3  SO4 A 304      36.048  13.875  38.202  1.00127.81           O  
HETATM 4625  O4  SO4 A 304      34.007  12.733  38.590  1.00124.96           O  
HETATM 4626  S   SO4 A 305      54.393  39.470   1.422  1.00134.25           S  
HETATM 4627  O1  SO4 A 305      54.260  38.033   1.663  1.00135.63           O  
HETATM 4628  O2  SO4 A 305      54.782  39.700   0.035  1.00133.22           O  
HETATM 4629  O3  SO4 A 305      53.109  40.117   1.674  1.00137.89           O  
HETATM 4630  O4  SO4 A 305      55.415  40.038   2.302  1.00128.17           O  
HETATM 4631  S   SO4 A 306      35.501   1.271  21.957  1.00164.10           S  
HETATM 4632  O1  SO4 A 306      35.533   2.561  21.270  1.00163.16           O  
HETATM 4633  O2  SO4 A 306      35.057   0.225  21.042  1.00162.80           O  
HETATM 4634  O3  SO4 A 306      34.581   1.344  23.090  1.00162.26           O  
HETATM 4635  O4  SO4 A 306      36.842   0.943  22.433  1.00164.89           O  
HETATM 4636  S   SO4 A 307      77.177  26.290  16.088  1.00 96.59           S  
HETATM 4637  O1  SO4 A 307      77.933  25.138  15.589  1.00 79.19           O  
HETATM 4638  O2  SO4 A 307      76.521  27.016  15.003  1.00100.30           O  
HETATM 4639  O3  SO4 A 307      76.114  25.831  16.987  1.00101.60           O  
HETATM 4640  O4  SO4 A 307      78.106  27.181  16.790  1.00102.03           O  
HETATM 4641  S   SO4 A 308      67.368  25.706   0.149  1.00123.86           S  
HETATM 4642  O1  SO4 A 308      66.942  24.451  -0.473  1.00124.47           O  
HETATM 4643  O2  SO4 A 308      68.431  26.291  -0.661  1.00132.22           O  
HETATM 4644  O3  SO4 A 308      67.869  25.471   1.501  1.00118.52           O  
HETATM 4645  O4  SO4 A 308      66.239  26.629   0.203  1.00122.22           O  
HETATM 4646  S   SO4 A 309      32.874  11.273   3.646  1.00149.27           S  
HETATM 4647  O1  SO4 A 309      32.057  12.315   3.033  1.00148.20           O  
HETATM 4648  O2  SO4 A 309      33.647  10.604   2.605  1.00150.97           O  
HETATM 4649  O3  SO4 A 309      33.773  11.856   4.636  1.00147.97           O  
HETATM 4650  O4  SO4 A 309      32.006  10.303   4.304  1.00151.48           O  
HETATM 4651  S   SO4 A 310      54.542  43.792  17.378  1.00152.45           S  
HETATM 4652  O1  SO4 A 310      55.200  43.610  16.085  1.00152.41           O  
HETATM 4653  O2  SO4 A 310      53.098  43.722  17.186  1.00151.28           O  
HETATM 4654  O3  SO4 A 310      54.984  42.758  18.314  1.00147.67           O  
HETATM 4655  O4  SO4 A 310      54.879  45.105  17.921  1.00155.80           O  
HETATM 4656 CL    CL A 311      53.789  23.021  26.149  1.00 86.02          CL  
HETATM 4657  C1  EDO A 312      51.037  16.811  35.168  1.00 61.73           C  
HETATM 4658  O1  EDO A 312      50.055  16.027  35.854  1.00 63.55           O  
HETATM 4659  C2  EDO A 312      51.528  17.896  36.103  1.00 72.29           C  
HETATM 4660  O2  EDO A 312      50.627  18.999  35.965  1.00 83.25           O  
HETATM 4661  C1  EDO A 313      65.897  20.185  -2.642  1.00 82.00           C  
HETATM 4662  O1  EDO A 313      65.566  19.565  -1.389  1.00 73.87           O  
HETATM 4663  C2  EDO A 313      65.051  21.437  -2.865  1.00 85.13           C  
HETATM 4664  O2  EDO A 313      64.067  21.184  -3.876  1.00 88.26           O  
HETATM 4665  C1  EDO A 314      49.758  43.423  23.604  1.00 90.86           C  
HETATM 4666  O1  EDO A 314      48.382  43.036  23.455  1.00 87.08           O  
HETATM 4667  C2  EDO A 314      50.596  42.971  22.410  1.00 91.91           C  
HETATM 4668  O2  EDO A 314      50.079  43.525  21.192  1.00 91.81           O  
HETATM 4669  C1  EDO A 315      63.526  27.040  19.036  1.00 67.28           C  
HETATM 4670  O1  EDO A 315      64.662  27.915  19.003  1.00 62.77           O  
HETATM 4671  C2  EDO A 315      62.413  27.696  19.839  1.00 76.09           C  
HETATM 4672  O2  EDO A 315      61.723  28.652  19.020  1.00 79.64           O  
HETATM 4673  S   DMS A 316      72.228  23.699  16.587  1.00 96.12           S  
HETATM 4674  O   DMS A 316      73.586  24.295  16.884  1.00102.40           O  
HETATM 4675  C1  DMS A 316      71.060  24.085  17.933  1.00 93.23           C  
HETATM 4676  C2  DMS A 316      71.377  24.637  15.281  1.00 93.49           C  
HETATM 4677  PB  ADP B 301      58.956  15.730  35.610  1.00 72.15           P  
HETATM 4678  O1B ADP B 301      58.855  14.734  34.482  1.00 74.18           O  
HETATM 4679  O2B ADP B 301      60.204  15.559  36.445  1.00 70.07           O  
HETATM 4680  O3B ADP B 301      58.665  17.158  35.206  1.00 80.45           O  
HETATM 4681  PA  ADP B 301      56.240  15.874  36.455  1.00 64.13           P  
HETATM 4682  O1A ADP B 301      56.011  16.477  35.083  1.00 80.42           O  
HETATM 4683  O2A ADP B 301      55.937  16.643  37.707  1.00 62.82           O  
HETATM 4684  O3A ADP B 301      57.748  15.330  36.600  1.00 69.76           O  
HETATM 4685  O5' ADP B 301      55.437  14.496  36.578  1.00 60.75           O  
HETATM 4686  C5' ADP B 301      55.371  13.492  35.580  1.00 59.97           C  
HETATM 4687  C4' ADP B 301      54.090  12.683  35.836  1.00 67.53           C  
HETATM 4688  O4' ADP B 301      53.957  12.338  37.214  1.00 74.42           O  
HETATM 4689  C3' ADP B 301      52.823  13.451  35.508  1.00 69.10           C  
HETATM 4690  O3' ADP B 301      51.918  12.480  34.982  1.00 72.37           O  
HETATM 4691  C2' ADP B 301      52.259  13.938  36.818  1.00 67.53           C  
HETATM 4692  O2' ADP B 301      50.840  13.892  36.790  1.00 66.76           O  
HETATM 4693  C1' ADP B 301      52.728  12.862  37.755  1.00 71.63           C  
HETATM 4694  N9  ADP B 301      53.053  13.329  39.112  1.00 61.40           N  
HETATM 4695  C8  ADP B 301      53.976  14.259  39.423  1.00 51.85           C  
HETATM 4696  N7  ADP B 301      54.065  14.408  40.763  1.00 50.54           N  
HETATM 4697  C5  ADP B 301      53.186  13.549  41.313  1.00 46.71           C  
HETATM 4698  C6  ADP B 301      52.779  13.190  42.675  1.00 41.04           C  
HETATM 4699  N6  ADP B 301      53.340  13.807  43.736  1.00 47.28           N  
HETATM 4700  N1  ADP B 301      51.822  12.248  42.814  1.00 44.64           N  
HETATM 4701  C2  ADP B 301      51.255  11.627  41.767  1.00 40.24           C  
HETATM 4702  N3  ADP B 301      51.588  11.905  40.501  1.00 54.44           N  
HETATM 4703  C4  ADP B 301      52.524  12.837  40.222  1.00 51.54           C  
HETATM 4704  S   SO4 B 302      52.239  50.522  38.094  1.00 81.94           S  
HETATM 4705  O1  SO4 B 302      53.461  50.153  37.355  1.00 83.86           O  
HETATM 4706  O2  SO4 B 302      51.373  51.270  37.188  1.00 83.76           O  
HETATM 4707  O3  SO4 B 302      51.497  49.352  38.589  1.00 69.39           O  
HETATM 4708  O4  SO4 B 302      52.596  51.374  39.233  1.00 84.26           O  
HETATM 4709  S   SO4 B 303      44.833  12.327  48.268  1.00 81.68           S  
HETATM 4710  O1  SO4 B 303      45.249  11.667  47.019  1.00 68.62           O  
HETATM 4711  O2  SO4 B 303      44.312  13.666  47.975  1.00 87.28           O  
HETATM 4712  O3  SO4 B 303      43.793  11.567  48.954  1.00 85.66           O  
HETATM 4713  O4  SO4 B 303      45.991  12.421  49.156  1.00 81.11           O  
HETATM 4714  S   SO4 B 304      42.757  27.743  54.254  1.00147.64           S  
HETATM 4715  O1  SO4 B 304      42.280  26.955  53.120  1.00148.43           O  
HETATM 4716  O2  SO4 B 304      43.358  28.984  53.772  1.00148.82           O  
HETATM 4717  O3  SO4 B 304      41.634  28.057  55.131  1.00146.62           O  
HETATM 4718  O4  SO4 B 304      43.759  26.976  54.986  1.00145.33           O  
HETATM 4719  S   SO4 B 305      70.636  43.078  17.801  1.00133.02           S  
HETATM 4720  O1  SO4 B 305      70.006  41.842  17.324  1.00131.85           O  
HETATM 4721  O2  SO4 B 305      70.917  43.961  16.672  1.00134.03           O  
HETATM 4722  O3  SO4 B 305      71.892  42.748  18.463  1.00131.17           O  
HETATM 4723  O4  SO4 B 305      69.747  43.775  18.732  1.00134.23           O  
HETATM 4724  S   SO4 B 306      48.666   2.722  37.410  1.00138.41           S  
HETATM 4725  O1  SO4 B 306      49.931   2.598  36.700  1.00138.10           O  
HETATM 4726  O2  SO4 B 306      47.732   1.723  36.898  1.00134.76           O  
HETATM 4727  O3  SO4 B 306      48.910   2.488  38.829  1.00141.84           O  
HETATM 4728  O4  SO4 B 306      48.111   4.062  37.226  1.00137.59           O  
HETATM 4729 CL    CL B 307      57.529  25.590  28.609  1.00 83.59          CL  
HETATM 4730  C1  EDO B 308      37.804  31.104  38.275  1.00 81.49           C  
HETATM 4731  O1  EDO B 308      37.617  30.831  39.679  1.00 78.52           O  
HETATM 4732  C2  EDO B 308      38.020  29.832  37.449  1.00 79.78           C  
HETATM 4733  O2  EDO B 308      38.820  28.886  38.169  1.00 78.71           O  
HETATM 4734  S   DMS B 309      83.611  16.682  11.578  1.00 90.95           S  
HETATM 4735  O   DMS B 309      82.817  16.078  10.457  1.00 89.31           O  
HETATM 4736  C1  DMS B 309      84.145  18.351  11.128  1.00 80.25           C  
HETATM 4737  C2  DMS B 309      82.617  17.023  13.049  1.00 84.06           C  
HETATM 4738  O   HOH A 401      69.366  24.227   2.665  1.00 57.84           O  
HETATM 4739  O   HOH A 402      63.987  22.954  21.489  1.00 54.39           O  
HETATM 4740  O   HOH A 403      68.113  34.711   9.427  1.00 58.23           O  
HETATM 4741  O   HOH A 404      36.460  31.023  10.348  1.00 55.83           O  
HETATM 4742  O   HOH A 405      43.954  20.729  15.861  1.00 50.99           O  
HETATM 4743  O   HOH A 406      45.592  17.851  -0.670  1.00 71.49           O  
HETATM 4744  O   HOH A 407      55.334  29.314   2.915  1.00 49.40           O  
HETATM 4745  O   HOH A 408      78.255  24.070  13.208  1.00 51.02           O  
HETATM 4746  O   HOH A 409      61.027   9.851  13.505  1.00 64.39           O  
HETATM 4747  O   HOH A 410      45.379  13.126  18.195  1.00 43.52           O  
HETATM 4748  O   HOH A 411      47.773  27.912  18.640  1.00 46.26           O  
HETATM 4749  O   HOH A 412      69.475  29.667  14.250  1.00 55.46           O  
HETATM 4750  O   HOH A 413      35.674  38.135  18.675  1.00 59.69           O  
HETATM 4751  O   HOH A 414      47.951  25.357  16.239  1.00 43.03           O  
HETATM 4752  O   HOH A 415      44.294  18.532  -4.093  1.00 74.42           O  
HETATM 4753  O   HOH A 416      51.090  23.167  -0.238  1.00 58.89           O  
HETATM 4754  O   HOH A 417      51.668  20.095  21.682  1.00 56.20           O  
HETATM 4755  O   HOH A 418      60.641  22.067  11.946  1.00 47.30           O  
HETATM 4756  O   HOH A 419      48.119  33.850  23.426  1.00 57.45           O  
HETATM 4757  O   HOH A 420      47.373  33.797   0.804  1.00 61.22           O  
HETATM 4758  O   HOH A 421      45.974  23.476  16.652  1.00 49.43           O  
HETATM 4759  O   HOH A 422      47.257  41.709   7.941  1.00 63.06           O  
HETATM 4760  O   HOH A 423      38.143  27.420   7.698  1.00 49.57           O  
HETATM 4761  O   HOH A 424      37.185  29.634  17.729  1.00 44.01           O  
HETATM 4762  O   HOH A 425      39.962  29.335  17.973  1.00 49.34           O  
HETATM 4763  O   HOH A 426      71.410  15.659  15.178  1.00 48.94           O  
HETATM 4764  O   HOH A 427      44.027  11.974  16.012  1.00 59.60           O  
HETATM 4765  O   HOH A 428      45.313  34.502  22.715  1.00 61.23           O  
HETATM 4766  O   HOH A 429      57.489  34.794   7.056  1.00 58.76           O  
HETATM 4767  O   HOH A 430      46.499  19.604  15.631  1.00 45.61           O  
HETATM 4768  O   HOH A 431      41.514  32.466  19.625  1.00 65.56           O  
HETATM 4769  O   HOH A 432      30.347  32.160   7.899  1.00 53.65           O  
HETATM 4770  O   HOH A 433      41.022  28.334  20.240  1.00 42.59           O  
HETATM 4771  O   HOH A 434      42.237  30.332  21.681  1.00 47.25           O  
HETATM 4772  O   HOH A 435      39.453  39.608  17.669  1.00 71.37           O  
HETATM 4773  O   HOH A 436      57.645  29.570   1.262  1.00 71.57           O  
HETATM 4774  O   HOH A 437      41.422  31.423  23.822  1.00 58.54           O  
HETATM 4775  O   HOH A 438      62.906  22.334  13.668  1.00 50.62           O  
HETATM 4776  O   HOH A 439      45.449   8.897   6.356  1.00 63.45           O  
HETATM 4777  O   HOH A 440      36.024  28.501   6.785  1.00 54.48           O  
HETATM 4778  O   HOH A 441      35.155  29.645  24.112  1.00 56.88           O  
HETATM 4779  O   HOH A 442      40.644  36.844  19.777  1.00 67.57           O  
HETATM 4780  O   HOH A 443      49.050  19.298  22.194  1.00 42.76           O  
HETATM 4781  O   HOH A 444      31.714  20.713   6.774  1.00 62.14           O  
HETATM 4782  O   HOH A 445      59.200  35.806   4.883  1.00 59.67           O  
HETATM 4783  O   HOH B 401      70.204  13.588  30.257  1.00 64.86           O  
HETATM 4784  O   HOH B 402      71.123  32.102  38.760  1.00 61.33           O  
HETATM 4785  O   HOH B 403      71.746  20.717  24.939  1.00 59.25           O  
HETATM 4786  O   HOH B 404      52.097  24.215  52.270  1.00 57.04           O  
HETATM 4787  O   HOH B 405      62.892  34.222  39.252  1.00 50.80           O  
HETATM 4788  O   HOH B 406      54.676  32.316  36.886  1.00 44.11           O  
HETATM 4789  O   HOH B 407      49.069  31.845  29.639  1.00 63.14           O  
HETATM 4790  O   HOH B 408      43.294  42.690  38.563  1.00 52.35           O  
HETATM 4791  O   HOH B 409      60.714   5.915  38.321  1.00 58.45           O  
HETATM 4792  O   HOH B 410      53.469  38.263  34.392  1.00 48.94           O  
HETATM 4793  O   HOH B 411      69.578  30.927  36.380  1.00 46.85           O  
HETATM 4794  O   HOH B 412      63.135  31.164  39.351  1.00 44.92           O  
HETATM 4795  O   HOH B 413      50.189  33.227  55.196  1.00 67.21           O  
HETATM 4796  O   HOH B 414      59.567  32.504  38.605  1.00 51.46           O  
HETATM 4797  O   HOH B 415      56.131  38.984  35.616  1.00 45.69           O  
HETATM 4798  O   HOH B 416      51.777  39.129  36.155  1.00 52.25           O  
HETATM 4799  O   HOH B 417      52.936  43.736  43.966  1.00 47.45           O  
HETATM 4800  O   HOH B 418      55.784  42.705  38.446  1.00 44.93           O  
HETATM 4801  O   HOH B 419      49.384  36.968  33.030  1.00 60.25           O  
HETATM 4802  O   HOH B 420      57.462  17.810  42.581  1.00 52.52           O  
HETATM 4803  O   HOH B 421      60.891  27.052  32.897  1.00 56.16           O  
HETATM 4804  O   HOH B 422      51.673  21.523  53.727  1.00 68.10           O  
HETATM 4805  O   HOH B 423      57.192  31.153  38.964  1.00 47.42           O  
HETATM 4806  O   HOH B 424      42.001  42.175  45.334  1.00 40.99           O  
HETATM 4807  O   HOH B 425      55.321  40.060  37.840  1.00 45.66           O  
HETATM 4808  O   HOH B 426      63.794  23.843  44.634  1.00 65.72           O  
HETATM 4809  O   HOH B 427      56.411  16.065  40.679  1.00 51.28           O  
HETATM 4810  O   HOH B 428      56.085  45.139  32.104  1.00 49.78           O  
HETATM 4811  O   HOH B 429      62.633  29.293  32.667  1.00 47.74           O  
HETATM 4812  O   HOH B 430      41.857  35.754  48.528  1.00 55.83           O  
HETATM 4813  O   HOH B 431      65.659  31.567  59.199  1.00 72.68           O  
HETATM 4814  O   HOH B 432      51.135  37.106  30.759  1.00 63.25           O  
HETATM 4815  O   HOH B 433      56.174  34.268  24.563  1.00 63.68           O  
HETATM 4816  O   HOH B 434      61.268  35.722  37.589  1.00 50.80           O  
HETATM 4817  O   HOH B 435      51.799  41.647  45.156  1.00 50.78           O  
HETATM 4818  O   HOH B 436      39.009  35.001  35.660  1.00 57.47           O  
HETATM 4819  O   HOH B 437      64.068  34.623  17.250  1.00 66.11           O  
HETATM 4820  O   HOH B 438      75.003  15.929  41.046  1.00 68.57           O  
HETATM 4821  O   HOH B 439      73.106  26.192  23.734  1.00 66.76           O  
HETATM 4822  O   HOH B 440      50.873  20.613  51.770  1.00 62.72           O  
HETATM 4823  O   HOH B 441      57.328  42.954  49.681  1.00 60.56           O  
HETATM 4824  O   HOH B 442      40.597  37.621  32.708  1.00 60.89           O  
HETATM 4825  O   HOH B 443      57.082  47.327  30.223  1.00 74.97           O  
HETATM 4826  O   HOH B 444      39.371  35.855  33.245  1.00 75.39           O  
CONECT  190 2485                                                                
CONECT 1796 4084                                                                
CONECT 2485  190                                                                
CONECT 4084 1796                                                                
CONECT 4584 4585 4586 4587 4591                                                 
CONECT 4585 4584                                                                
CONECT 4586 4584                                                                
CONECT 4587 4584                                                                
CONECT 4588 4589 4590 4591 4592                                                 
CONECT 4589 4588                                                                
CONECT 4590 4588                                                                
CONECT 4591 4584 4588                                                           
CONECT 4592 4588 4593                                                           
CONECT 4593 4592 4594                                                           
CONECT 4594 4593 4595 4596                                                      
CONECT 4595 4594 4600                                                           
CONECT 4596 4594 4597 4598                                                      
CONECT 4597 4596                                                                
CONECT 4598 4596 4599 4600                                                      
CONECT 4599 4598                                                                
CONECT 4600 4595 4598 4601                                                      
CONECT 4601 4600 4602 4610                                                      
CONECT 4602 4601 4603                                                           
CONECT 4603 4602 4604                                                           
CONECT 4604 4603 4605 4610                                                      
CONECT 4605 4604 4606 4607                                                      
CONECT 4606 4605                                                                
CONECT 4607 4605 4608                                                           
CONECT 4608 4607 4609                                                           
CONECT 4609 4608 4610                                                           
CONECT 4610 4601 4604 4609                                                      
CONECT 4611 4612 4613 4614 4615                                                 
CONECT 4612 4611                                                                
CONECT 4613 4611                                                                
CONECT 4614 4611                                                                
CONECT 4615 4611                                                                
CONECT 4616 4617 4618 4619 4620                                                 
CONECT 4617 4616                                                                
CONECT 4618 4616                                                                
CONECT 4619 4616                                                                
CONECT 4620 4616                                                                
CONECT 4621 4622 4623 4624 4625                                                 
CONECT 4622 4621                                                                
CONECT 4623 4621                                                                
CONECT 4624 4621                                                                
CONECT 4625 4621                                                                
CONECT 4626 4627 4628 4629 4630                                                 
CONECT 4627 4626                                                                
CONECT 4628 4626                                                                
CONECT 4629 4626                                                                
CONECT 4630 4626                                                                
CONECT 4631 4632 4633 4634 4635                                                 
CONECT 4632 4631                                                                
CONECT 4633 4631                                                                
CONECT 4634 4631                                                                
CONECT 4635 4631                                                                
CONECT 4636 4637 4638 4639 4640                                                 
CONECT 4637 4636                                                                
CONECT 4638 4636                                                                
CONECT 4639 4636                                                                
CONECT 4640 4636                                                                
CONECT 4641 4642 4643 4644 4645                                                 
CONECT 4642 4641                                                                
CONECT 4643 4641                                                                
CONECT 4644 4641                                                                
CONECT 4645 4641                                                                
CONECT 4646 4647 4648 4649 4650                                                 
CONECT 4647 4646                                                                
CONECT 4648 4646                                                                
CONECT 4649 4646                                                                
CONECT 4650 4646                                                                
CONECT 4651 4652 4653 4654 4655                                                 
CONECT 4652 4651                                                                
CONECT 4653 4651                                                                
CONECT 4654 4651                                                                
CONECT 4655 4651                                                                
CONECT 4657 4658 4659                                                           
CONECT 4658 4657                                                                
CONECT 4659 4657 4660                                                           
CONECT 4660 4659                                                                
CONECT 4661 4662 4663                                                           
CONECT 4662 4661                                                                
CONECT 4663 4661 4664                                                           
CONECT 4664 4663                                                                
CONECT 4665 4666 4667                                                           
CONECT 4666 4665                                                                
CONECT 4667 4665 4668                                                           
CONECT 4668 4667                                                                
CONECT 4669 4670 4671                                                           
CONECT 4670 4669                                                                
CONECT 4671 4669 4672                                                           
CONECT 4672 4671                                                                
CONECT 4673 4674 4675 4676                                                      
CONECT 4674 4673                                                                
CONECT 4675 4673                                                                
CONECT 4676 4673                                                                
CONECT 4677 4678 4679 4680 4684                                                 
CONECT 4678 4677                                                                
CONECT 4679 4677                                                                
CONECT 4680 4677                                                                
CONECT 4681 4682 4683 4684 4685                                                 
CONECT 4682 4681                                                                
CONECT 4683 4681                                                                
CONECT 4684 4677 4681                                                           
CONECT 4685 4681 4686                                                           
CONECT 4686 4685 4687                                                           
CONECT 4687 4686 4688 4689                                                      
CONECT 4688 4687 4693                                                           
CONECT 4689 4687 4690 4691                                                      
CONECT 4690 4689                                                                
CONECT 4691 4689 4692 4693                                                      
CONECT 4692 4691                                                                
CONECT 4693 4688 4691 4694                                                      
CONECT 4694 4693 4695 4703                                                      
CONECT 4695 4694 4696                                                           
CONECT 4696 4695 4697                                                           
CONECT 4697 4696 4698 4703                                                      
CONECT 4698 4697 4699 4700                                                      
CONECT 4699 4698                                                                
CONECT 4700 4698 4701                                                           
CONECT 4701 4700 4702                                                           
CONECT 4702 4701 4703                                                           
CONECT 4703 4694 4697 4702                                                      
CONECT 4704 4705 4706 4707 4708                                                 
CONECT 4705 4704                                                                
CONECT 4706 4704                                                                
CONECT 4707 4704                                                                
CONECT 4708 4704                                                                
CONECT 4709 4710 4711 4712 4713                                                 
CONECT 4710 4709                                                                
CONECT 4711 4709                                                                
CONECT 4712 4709                                                                
CONECT 4713 4709                                                                
CONECT 4714 4715 4716 4717 4718                                                 
CONECT 4715 4714                                                                
CONECT 4716 4714                                                                
CONECT 4717 4714                                                                
CONECT 4718 4714                                                                
CONECT 4719 4720 4721 4722 4723                                                 
CONECT 4720 4719                                                                
CONECT 4721 4719                                                                
CONECT 4722 4719                                                                
CONECT 4723 4719                                                                
CONECT 4724 4725 4726 4727 4728                                                 
CONECT 4725 4724                                                                
CONECT 4726 4724                                                                
CONECT 4727 4724                                                                
CONECT 4728 4724                                                                
CONECT 4730 4731 4732                                                           
CONECT 4731 4730                                                                
CONECT 4732 4730 4733                                                           
CONECT 4733 4732                                                                
CONECT 4734 4735 4736 4737                                                      
CONECT 4735 4734                                                                
CONECT 4736 4734                                                                
CONECT 4737 4734                                                                
MASTER      533    0   25   26   22    0   35    6 4817    2  156   50          
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.