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***  CELL CYCLE/DNA 04-APR-20 6WG6  ***

elNémo ID: 2005271047146311

Job options:

ID        	=	 2005271047146311
JOBID     	=	 CELL CYCLE/DNA 04-APR-20 6WG6
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    CELL CYCLE/DNA                          04-APR-20   6WG6              
TITLE     CRYSTAL STRUCTURE OF HUMAN SMC1-SMC3 HINGE DOMAIN HETERODIMER IN      
TITLE    2 NORTH-OPEN CONFORMATION                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN;             
COMPND   3 CHAIN: A, C, E, G, I, K;                                             
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3;           
COMPND   7 CHAIN: B, D, F, H, J, L;                                             
COMPND   8 SYNONYM: SMC-3,BASEMENT MEMBRANE-ASSOCIATED CHONDROITIN PROTEOGLYCAN,
COMPND   9 BAMACAN,CHONDROITIN SULFATE PROTEOGLYCAN 6,CHROMOSOME-ASSOCIATED     
COMPND  10 POLYPEPTIDE,HCAP;                                                    
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MOL_ID: 3;                                                           
COMPND  13 MOLECULE: POLY(DT);                                                  
COMPND  14 CHAIN: M, N;                                                         
COMPND  15 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: SMC1A;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: SMC3, BAM, BMH, CSPG6, SMC3L1;                                 
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 SYNTHETIC: YES;                                                      
SOURCE  17 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  18 ORGANISM_TAXID: 9606                                                 
KEYWDS    PROTEIN-DNA COMPLEX, ATPASE, DNA-BINDING PROTEIN,                     
KEYWDS   2 GENOME ORGANIZATION, SISTER CHROMATID COHESION,                      
KEYWDS   3 TRANSCRIPTION REGU CELL CYCLE, CELL CYCLE-DNA COMPLEX                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Z.B.SHI,H.YU                                                          
REVDAT   1   20-MAY-20 6WG6    0                                                
JRNL        AUTH   Z.B.SHI,H.GAO,X.C.BAI,H.YU                                   
JRNL        TITL   CRYO-EM STRUCTURE OF HUMAN COHESIN-NIPBL-DNA COMPLEX         
JRNL        REF    SCIENCE                                    2020              
JRNL        REFN                   ESSN 1095-9203                               
JRNL        DOI    10.1126/SCIENCE.ABB0981                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.54 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.17.1_3660                                   
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) : 3.54                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.50                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 87.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 60986                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.253                           
REMARK   3   R VALUE            (WORKING SET) : 0.252                           
REMARK   3   FREE R VALUE                     : 0.288                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.250                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1982                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 49.5000 -  8.5300    0.91     4666   153  0.1854 0.2222        
REMARK   3     2  8.5300 -  6.7800    1.00     4917   166  0.2252 0.2273        
REMARK   3     3  6.7800 -  5.9200    1.00     4860   164  0.2674 0.3309        
REMARK   3     4  5.9200 -  5.3800    0.99     4793   160  0.2776 0.3211        
REMARK   3     5  5.3800 -  5.0000    0.99     4769   161  0.2478 0.3120        
REMARK   3     6  5.0000 -  4.7000    0.99     4777   161  0.2334 0.2860        
REMARK   3     7  4.7000 -  4.4700    0.99     4763   161  0.2300 0.2726        
REMARK   3     8  4.4700 -  4.2700    0.99     4711   158  0.2572 0.2616        
REMARK   3     9  4.2700 -  4.1100    0.96     4589   155  0.2705 0.2925        
REMARK   3    10  4.1100 -  3.9700    0.89     4254   142  0.2811 0.3511        
REMARK   3    11  3.9700 -  3.8400    0.84     4007   135  0.2941 0.2980        
REMARK   3    12  3.8400 -  3.7300    0.77     3642   122  0.2971 0.3285        
REMARK   3    13  3.7300 -  3.6300    0.62     2972   101  0.3126 0.3520        
REMARK   3    14  3.6300 -  3.5400    0.27     1284    43  0.3246 0.4863        
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)     : 0.438            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.246           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 51.35                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 79.61                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.004          20356                                  
REMARK   3   ANGLE     :  0.742          27371                                  
REMARK   3   CHIRALITY :  0.046           3002                                  
REMARK   3   PLANARITY :  0.005           3565                                  
REMARK   3   DIHEDRAL  : 22.765           2783                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 73                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'K' AND (RESID 496 THROUGH 510 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.7816  -5.5734  28.6114              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.5248 T22:   1.7015                                     
REMARK   3      T33:   1.0205 T12:   0.8558                                     
REMARK   3      T13:   0.2000 T23:  -0.1639                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2021 L22:   0.5766                                     
REMARK   3      L33:   0.1026 L12:   0.3418                                     
REMARK   3      L13:  -0.1443 L23:  -0.2438                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1487 S12:   0.0552 S13:   0.1188                       
REMARK   3      S21:  -0.6331 S22:  -0.7558 S23:   0.1704                       
REMARK   3      S31:  -0.6589 S32:  -0.8649 S33:   0.3458                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'K' AND (RESID 511 THROUGH 563 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -10.1686 -15.9450  21.6593              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1695 T22:   2.1281                                     
REMARK   3      T33:   0.6072 T12:   0.4367                                     
REMARK   3      T13:  -0.1287 T23:  -0.2728                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9151 L22:   1.0523                                     
REMARK   3      L33:   1.7845 L12:   0.2325                                     
REMARK   3      L13:   0.0898 L23:   0.2014                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5376 S12:  -0.4237 S13:   0.3580                       
REMARK   3      S21:  -0.1321 S22:   0.1153 S23:   0.5416                       
REMARK   3      S31:  -0.4848 S32:  -1.3357 S33:   0.3805                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'K' AND (RESID 564 THROUGH 670 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -10.8361 -31.1042  20.0189              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1420 T22:   2.2505                                     
REMARK   3      T33:   0.9495 T12:   0.0196                                     
REMARK   3      T13:   0.0849 T23:  -0.1154                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0846 L22:   2.1418                                     
REMARK   3      L33:   1.8303 L12:   0.2110                                     
REMARK   3      L13:   0.6370 L23:  -0.8747                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3385 S12:   0.7434 S13:   0.0766                       
REMARK   3      S21:   0.7161 S22:   0.4465 S23:   0.3692                       
REMARK   3      S31:   0.3528 S32:  -1.2591 S33:  -0.1167                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'L' AND (RESID 468 THROUGH 499 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  33.1239  -6.0530  43.7639              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7126 T22:   0.6367                                     
REMARK   3      T33:   0.6271 T12:  -0.0007                                     
REMARK   3      T13:  -0.2932 T23:   0.0224                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.5917 L22:   2.7851                                     
REMARK   3      L33:   4.9298 L12:   2.7906                                     
REMARK   3      L13:   4.2850 L23:   2.6085                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4215 S12:  -0.5557 S13:   0.3237                       
REMARK   3      S21:  -0.1288 S22:  -0.9169 S23:   0.0274                       
REMARK   3      S31:  -0.3679 S32:  -0.6057 S33:   0.5234                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'L' AND (RESID 500 THROUGH 673 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  15.7743 -25.7676  19.5281              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6435 T22:   0.8648                                     
REMARK   3      T33:   0.2092 T12:   0.0247                                     
REMARK   3      T13:  -0.3223 T23:  -0.0047                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4646 L22:   1.9941                                     
REMARK   3      L33:   3.1723 L12:  -0.4708                                     
REMARK   3      L13:  -0.0793 L23:  -0.9664                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3644 S12:   0.3713 S13:   0.1974                       
REMARK   3      S21:  -0.3001 S22:  -0.1622 S23:   0.2362                       
REMARK   3      S31:  -0.2260 S32:   0.0548 S33:   0.2727                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'L' AND (RESID 674 THROUGH 706 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  37.8500  -9.5366  35.3074              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7355 T22:   0.8948                                     
REMARK   3      T33:   0.9180 T12:  -0.1835                                     
REMARK   3      T13:  -0.0033 T23:  -0.1763                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2805 L22:   2.4372                                     
REMARK   3      L33:   2.7213 L12:   0.0805                                     
REMARK   3      L13:   0.2318 L23:  -0.4718                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1603 S12:   0.7579 S13:  -0.1200                       
REMARK   3      S21:  -0.7600 S22:  -0.1149 S23:  -0.7276                       
REMARK   3      S31:  -0.4610 S32:   0.7504 S33:   0.0270                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'M' AND (RESID 9 THROUGH 10 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): -14.7826 -17.6773  98.3362              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0528 T22:   1.1621                                     
REMARK   3      T33:   1.0740 T12:  -0.2150                                     
REMARK   3      T13:  -0.1578 T23:  -0.0121                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.2109 L22:   9.1952                                     
REMARK   3      L33:   7.0011 L12:   1.9404                                     
REMARK   3      L13:  -3.6087 L23:  -1.5456                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1691 S12:  -0.4777 S13:   0.2273                       
REMARK   3      S21:   0.2966 S22:   0.4410 S23:  -0.3024                       
REMARK   3      S31:  -0.2159 S32:   0.7883 S33:  -0.5123                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'N' AND (RESID 3 THROUGH 4 )                     
REMARK   3    ORIGIN FOR THE GROUP (A): -47.6648 -50.3313  98.5305              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3119 T22:   1.3793                                     
REMARK   3      T33:   0.9747 T12:   0.0521                                     
REMARK   3      T13:   0.1848 T23:   0.2896                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.4658 L22:   8.6725                                     
REMARK   3      L33:   5.4903 L12:   5.5819                                     
REMARK   3      L13:  -2.7799 L23:  -1.7939                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2154 S12:  -1.4312 S13:   0.1331                       
REMARK   3      S21:   0.9255 S22:  -0.4502 S23:   0.7579                       
REMARK   3      S31:   0.1310 S32:  -0.7516 S33:   0.1402                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 495 THROUGH 510 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -16.6601 -16.6088  67.7732              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7472 T22:   0.1957                                     
REMARK   3      T33:   0.6921 T12:   0.0312                                     
REMARK   3      T13:   0.1091 T23:  -0.0715                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0411 L22:   2.0507                                     
REMARK   3      L33:   2.8380 L12:   0.3859                                     
REMARK   3      L13:  -0.0156 L23:   0.2342                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2015 S12:  -0.1253 S13:   1.0287                       
REMARK   3      S21:  -0.4129 S22:  -0.0996 S23:  -0.2886                       
REMARK   3      S31:  -1.2439 S32:   0.0151 S33:  -0.1634                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 511 THROUGH 543 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.0901 -18.1379  83.2796              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3977 T22:   0.3329                                     
REMARK   3      T33:   1.0407 T12:   0.0104                                     
REMARK   3      T13:  -0.1297 T23:  -0.2783                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2364 L22:   0.5055                                     
REMARK   3      L33:   2.0620 L12:  -0.6326                                     
REMARK   3      L13:   0.5885 L23:  -0.8623                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4347 S12:  -0.5965 S13:   0.8577                       
REMARK   3      S21:   0.1008 S22:  -0.0149 S23:  -0.4052                       
REMARK   3      S31:  -0.8228 S32:   0.0108 S33:   0.2472                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 544 THROUGH 587 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -16.5965 -28.3120  80.4038              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1344 T22:   0.0541                                     
REMARK   3      T33:   0.5326 T12:   0.1093                                     
REMARK   3      T13:   0.1551 T23:  -0.0810                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7195 L22:   2.0748                                     
REMARK   3      L33:6.4749403 L12:  -1.1162                                     
REMARK   3      L13:   1.3425 L23:   0.5371                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1189 S12:  -0.3643 S13:  -0.1101                       
REMARK   3      S21:  -0.0070 S22:   0.1758 S23:  -0.0181                       
REMARK   3      S31:   0.4227 S32:  -0.0579 S33:   0.1420                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 588 THROUGH 621 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.6561 -22.0790  93.4514              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5866 T22:   0.3135                                     
REMARK   3      T33:   0.7682 T12:   0.2289                                     
REMARK   3      T13:  -0.2556 T23:  -0.2965                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3305 L22:   2.4350                                     
REMARK   3      L33:   1.9375 L12:  -0.6196                                     
REMARK   3      L13:  -1.5861 L23:   0.4579                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4137 S12:  -0.8093 S13:   0.8049                       
REMARK   3      S21:   0.8495 S22:   0.4749 S23:  -0.9220                       
REMARK   3      S31:  -0.1464 S32:   0.5216 S33:  -0.1233                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 622 THROUGH 676 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   3.8679 -21.7501  87.0997              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5130 T22:   0.7765                                     
REMARK   3      T33:   1.1755 T12:   0.0438                                     
REMARK   3      T13:  -0.0600 T23:  -0.2535                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0841 L22:   3.2251                                     
REMARK   3      L33:   1.9761 L12:  -1.1307                                     
REMARK   3      L13:   0.2276 L23:  -0.2193                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1196 S12:   0.1500 S13:  -0.1236                       
REMARK   3      S21:   0.0927 S22:   0.4014 S23:  -0.5937                       
REMARK   3      S31:  -0.0627 S32:   0.8347 S33:  -0.3379                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 469 THROUGH 500 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   6.8033 -36.8729  36.4907              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3363 T22:   0.7254                                     
REMARK   3      T33:   0.6485 T12:  -0.1822                                     
REMARK   3      T13:   0.2057 T23:  -0.1735                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9078 L22:   1.0385                                     
REMARK   3      L33:   5.1703 L12:  -0.5335                                     
REMARK   3      L13:  -1.6091 L23:   0.5413                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1161 S12:   0.6143 S13:  -0.1101                       
REMARK   3      S21:  -0.3782 S22:   0.0167 S23:   0.1937                       
REMARK   3      S31:  -0.3776 S32:  -0.1833 S33:  -0.1299                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 501 THROUGH 604 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  10.0402 -43.4448  69.1123              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0904 T22:   0.1105                                     
REMARK   3      T33:   0.9627 T12:  -0.1770                                     
REMARK   3      T13:   0.1333 T23:  -0.1847                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3184 L22:   0.7703                                     
REMARK   3      L33:   1.0468 L12:   0.5445                                     
REMARK   3      L13:   0.1608 L23:   0.4010                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0123 S12:  -0.0324 S13:  -0.6057                       
REMARK   3      S21:   0.1134 S22:   0.0014 S23:  -0.5136                       
REMARK   3      S31:   0.1451 S32:   0.2212 S33:  -0.0512                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 605 THROUGH 673 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -10.2574 -43.1384  71.5711              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2099 T22:   0.2155                                     
REMARK   3      T33:   0.6007 T12:  -0.0178                                     
REMARK   3      T13:   0.1267 T23:  -0.3240                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3692 L22:   2.3555                                     
REMARK   3      L33:   1.3980 L12:  -0.4643                                     
REMARK   3      L13:   0.1153 L23:   0.6428                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0805 S12:   0.1204 S13:  -0.5270                       
REMARK   3      S21:  -0.1711 S22:  -0.1678 S23:   0.1968                       
REMARK   3      S31:   0.0706 S32:  -0.3023 S33:   0.2354                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 674 THROUGH 704 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   6.3059 -46.4549  40.7883              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7654 T22:   0.5810                                     
REMARK   3      T33:   0.6875 T12:  -0.1756                                     
REMARK   3      T13:   0.3416 T23:  -0.1393                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1313 L22:   2.8083                                     
REMARK   3      L33:   1.3566 L12:  -1.6456                                     
REMARK   3      L13:  -0.4651 L23:   0.4613                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0915 S12:   0.4503 S13:  -0.1378                       
REMARK   3      S21:  -0.5619 S22:  -0.3024 S23:   0.1004                       
REMARK   3      S31:   0.6520 S32:  -0.3423 S33:   0.1845                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 495 THROUGH 510 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -45.1740 -51.0591  67.8011              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6863 T22:   0.3439                                     
REMARK   3      T33:   1.1196 T12:  -0.1056                                     
REMARK   3      T13:   0.1076 T23:  -0.3806                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9162 L22:   1.7313                                     
REMARK   3      L33:   1.2597 L12:   0.3936                                     
REMARK   3      L13:   0.7500 L23:  -0.4580                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0936 S12:   0.0927 S13:  -0.1762                       
REMARK   3      S21:  -1.0410 S22:  -0.1569 S23:   0.1908                       
REMARK   3      S31:   0.3118 S32:  -0.1411 S33:  -0.0265                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 511 THROUGH 527 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -47.3099 -50.6453  82.1678              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2927 T22:   0.3562                                     
REMARK   3      T33:   0.6162 T12:   0.1282                                     
REMARK   3      T13:   0.3025 T23:   0.2444                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7622 L22:   0.2243                                     
REMARK   3      L33:   3.8754 L12:  -0.4025                                     
REMARK   3      L13:  -0.6553 L23:   0.5678                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2168 S12:  -0.5128 S13:  -0.4258                       
REMARK   3      S21:   0.0918 S22:  -0.0565 S23:   0.3163                       
REMARK   3      S31:   0.6347 S32:   0.0007 S33:   0.1591                       
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 528 THROUGH 563 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -49.3398 -43.9519  77.5232              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0923 T22:   0.2598                                     
REMARK   3      T33:   0.6561 T12:   0.2565                                     
REMARK   3      T13:   0.1227 T23:   0.2472                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5587 L22:   0.9767                                     
REMARK   3      L33:   0.5531 L12:  -0.7299                                     
REMARK   3      L13:   0.0388 L23:  -0.0526                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0176 S12:  -0.0211 S13:  -0.2125                       
REMARK   3      S21:  -0.0521 S22:  -0.0418 S23:   0.0921                       
REMARK   3      S31:   0.0747 S32:   0.0132 S33:  -0.1283                       
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 564 THROUGH 573 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -47.0883 -41.1682  72.1691              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2909 T22:   0.1328                                     
REMARK   3      T33:   0.3763 T12:   0.0552                                     
REMARK   3      T13:   0.0536 T23:   0.1695                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2350 L22:   2.5400                                     
REMARK   3      L33:   3.6268 L12:  -0.7838                                     
REMARK   3      L13:   1.0707 L23:  -1.2124                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1799 S12:   0.0627 S13:  -0.0162                       
REMARK   3      S21:  -0.3469 S22:  -0.0128 S23:  -0.1372                       
REMARK   3      S31:   0.3909 S32:  -0.0904 S33:  -0.0749                       
REMARK   3   TLS GROUP : 22                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 574 THROUGH 586 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -50.3633 -36.8377  95.2650              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8629 T22:   0.9852                                     
REMARK   3      T33:   0.2910 T12:   0.1704                                     
REMARK   3      T13:  -0.0921 T23:  -0.0535                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0248 L22:   2.1499                                     
REMARK   3      L33:   2.1467 L12:  -0.2363                                     
REMARK   3      L13:  -0.9783 L23:   0.6725                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4010 S12:  -1.1005 S13:   0.0306                       
REMARK   3      S21:   1.1080 S22:   0.0080 S23:   0.2571                       
REMARK   3      S31:  -0.2990 S32:  -0.2949 S33:   0.2107                       
REMARK   3   TLS GROUP : 23                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 587 THROUGH 602 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -56.4291 -48.0741  95.8903              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7119 T22:   0.6202                                     
REMARK   3      T33:   0.5372 T12:   0.2351                                     
REMARK   3      T13:   0.2898 T23:   0.2865                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.7616 L22:   1.9847                                     
REMARK   3      L33:   2.6028 L12:   2.3091                                     
REMARK   3      L13:  -0.2064 L23:  -0.6825                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1529 S12:  -0.2947 S13:  -0.0774                       
REMARK   3      S21:   0.4803 S22:   0.4248 S23:   0.4848                       
REMARK   3      S31:   0.4442 S32:   0.0092 S33:   0.1676                       
REMARK   3   TLS GROUP : 24                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 603 THROUGH 630 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -61.1535 -42.6801  93.6380              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2354 T22:   0.7343                                     
REMARK   3      T33:   0.7731 T12:   0.3848                                     
REMARK   3      T13:   0.1766 T23:   0.3882                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6924 L22:   0.9402                                     
REMARK   3      L33:   0.8309 L12:   0.5150                                     
REMARK   3      L13:   1.0438 L23:  -0.0716                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3123 S12:  -0.9115 S13:   0.2325                       
REMARK   3      S21:   0.4503 S22:   0.4464 S23:   0.5582                       
REMARK   3      S31:  -0.1186 S32:  -0.7118 S33:   0.0220                       
REMARK   3   TLS GROUP : 25                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 631 THROUGH 645 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -67.9164 -39.1212  94.0147              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5810 T22:   0.7806                                     
REMARK   3      T33:   1.0411 T12:   0.1978                                     
REMARK   3      T13:   0.2477 T23:  -0.0689                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6192 L22:   4.7765                                     
REMARK   3      L33:   4.6522 L12:  -1.4199                                     
REMARK   3      L13:  -1.3946 L23:  -1.6687                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1429 S12:  -1.0352 S13:  -0.0919                       
REMARK   3      S21:   0.7612 S22:   0.1537 S23:   0.0421                       
REMARK   3      S31:  -0.0852 S32:  -0.8223 S33:   0.1044                       
REMARK   3   TLS GROUP : 26                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 646 THROUGH 658 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -69.7610 -38.5254  85.0275              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0266 T22:   0.7637                                     
REMARK   3      T33:   0.9791 T12:   0.2710                                     
REMARK   3      T13:   0.1385 T23:   0.4372                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0491 L22:   0.6884                                     
REMARK   3      L33:   2.2926 L12:  -0.7675                                     
REMARK   3      L13:  -0.9186 L23:  -0.1153                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5031 S12:   0.3380 S13:  -0.0399                       
REMARK   3      S21:  -0.5008 S22:   0.0085 S23:  -0.5961                       
REMARK   3      S31:  -0.2657 S32:  -0.0163 S33:   0.4573                       
REMARK   3   TLS GROUP : 27                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 659 THROUGH 676 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -58.1064 -58.4134  77.4439              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8774 T22:   0.4260                                     
REMARK   3      T33:   1.1757 T12:  -0.2461                                     
REMARK   3      T13:  -0.1184 T23:  -0.0754                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4973 L22:   1.1690                                     
REMARK   3      L33:   2.8339 L12:   0.8992                                     
REMARK   3      L13:   2.3290 L23:   0.0870                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3836 S12:   0.3913 S13:  -0.9467                       
REMARK   3      S21:   0.1859 S22:  -0.2299 S23:  -0.4321                       
REMARK   3      S31:   0.8585 S32:   0.2667 S33:  -0.3696                       
REMARK   3   TLS GROUP : 28                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 468 THROUGH 500 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -69.4830 -30.4505  36.0646              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6272 T22:   0.4194                                     
REMARK   3      T33:   0.4421 T12:  -0.0689                                     
REMARK   3      T13:   0.0379 T23:  -0.1139                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5434 L22:   0.2916                                     
REMARK   3      L33:   2.6967 L12:  -0.1080                                     
REMARK   3      L13:   1.1382 L23:   0.0893                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1103 S12:   0.6289 S13:   0.1024                       
REMARK   3      S21:  -0.6383 S22:   0.3214 S23:   0.2185                       
REMARK   3      S31:   0.5185 S32:   0.1397 S33:  -0.2403                       
REMARK   3   TLS GROUP : 29                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 501 THROUGH 578 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -74.7068 -25.3784  66.6101              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0220 T22:   0.2421                                     
REMARK   3      T33:   0.7226 T12:  -0.2457                                     
REMARK   3      T13:   0.1002 T23:   0.4850                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3277 L22:   0.4276                                     
REMARK   3      L33:   0.7635 L12:   0.0746                                     
REMARK   3      L13:  -0.1163 L23:  -0.3493                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0551 S12:   0.2595 S13:   0.1991                       
REMARK   3      S21:   0.1970 S22:   0.3415 S23:   0.6124                       
REMARK   3      S31:  -0.0317 S32:  -0.4393 S33:   0.2683                       
REMARK   3   TLS GROUP : 30                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 579 THROUGH 591 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -75.6447 -28.1868  73.1227              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2576 T22:   0.0689                                     
REMARK   3      T33:   0.5344 T12:  -0.0352                                     
REMARK   3      T13:   0.0098 T23:  -0.0266                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2366 L22:   5.1582                                     
REMARK   3      L33:   2.9834 L12:   1.7224                                     
REMARK   3      L13:   1.0108 L23:   0.6147                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0066 S12:  -0.0162 S13:   0.0700                       
REMARK   3      S21:   0.3977 S22:   0.2555 S23:   0.2217                       
REMARK   3      S31:  -0.0880 S32:  -0.0503 S33:   0.2948                       
REMARK   3   TLS GROUP : 31                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 592 THROUGH 604 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -52.5327 -15.5322  78.6973              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5102 T22:   0.5382                                     
REMARK   3      T33:   1.1478 T12:  -0.3156                                     
REMARK   3      T13:  -0.0268 T23:   0.1087                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6047 L22:   0.7738                                     
REMARK   3      L33:   0.5554 L12:   0.5890                                     
REMARK   3      L13:   0.4045 L23:   0.1525                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4490 S12:  -0.5284 S13:   0.4703                       
REMARK   3      S21:  -0.0732 S22:  -0.1176 S23:   0.0127                       
REMARK   3      S31:  -0.1830 S32:   0.0115 S33:  -0.1081                       
REMARK   3   TLS GROUP : 32                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 605 THROUGH 626 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -60.0457 -16.7316  70.1525              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2839 T22:  -0.1160                                     
REMARK   3      T33:   0.4312 T12:   0.0397                                     
REMARK   3      T13:  -0.0287 T23:   0.0252                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1320 L22:   1.4214                                     
REMARK   3      L33:   0.8000 L12:   0.4075                                     
REMARK   3      L13:   0.0479 L23:  -0.2310                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0127 S12:   0.0398 S13:   0.2787                       
REMARK   3      S21:   0.2073 S22:   0.0242 S23:   0.0536                       
REMARK   3      S31:  -0.3899 S32:  -0.0441 S33:   0.1173                       
REMARK   3   TLS GROUP : 33                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 627 THROUGH 673 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -47.3143 -28.8928  72.1909              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2329 T22:  -0.0668                                     
REMARK   3      T33:   0.5447 T12:  -0.1028                                     
REMARK   3      T13:  -0.0850 T23:   0.2054                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9748 L22:   2.9393                                     
REMARK   3      L33:   2.2465 L12:  -0.5625                                     
REMARK   3      L13:  -0.4571 L23:   0.1335                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1808 S12:   0.0548 S13:  -0.1302                       
REMARK   3      S21:   0.2170 S22:  -0.1972 S23:  -0.3820                       
REMARK   3      S31:   0.0332 S32:   0.0799 S33:   0.1718                       
REMARK   3   TLS GROUP : 34                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 674 THROUGH 702 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -67.6914 -21.9200  42.2585              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8693 T22:   0.3703                                     
REMARK   3      T33:   0.3422 T12:   0.3047                                     
REMARK   3      T13:  -0.2801 T23:   0.0404                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4711 L22:   1.0745                                     
REMARK   3      L33:   4.0109 L12:  -0.9018                                     
REMARK   3      L13:   2.7481 L23:  -1.9547                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2963 S12:   0.9251 S13:   0.5155                       
REMARK   3      S21:  -0.4049 S22:  -0.4372 S23:  -0.0945                       
REMARK   3      S31:  -0.2193 S32:   0.3994 S33:   0.2366                       
REMARK   3   TLS GROUP : 35                                                     
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 494 THROUGH 510 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -54.7966  -9.4328 101.5351              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7878 T22:   0.7888                                     
REMARK   3      T33:   0.9077 T12:  -0.1609                                     
REMARK   3      T13:   0.1966 T23:  -0.0444                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5617 L22:   1.9977                                     
REMARK   3      L33:   3.7532 L12:  -0.4600                                     
REMARK   3      L13:  -0.7547 L23:  -0.0594                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1890 S12:  -0.2546 S13:  -0.2442                       
REMARK   3      S21:   1.6013 S22:  -0.6700 S23:   0.9478                       
REMARK   3      S31:  -0.1231 S32:  -0.8485 S33:   0.4243                       
REMARK   3   TLS GROUP : 36                                                     
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 511 THROUGH 547 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -41.9294 -14.5483 111.1589              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0397 T22:   1.0561                                     
REMARK   3      T33:   0.5335 T12:  -0.5021                                     
REMARK   3      T13:   0.3781 T23:  -0.1140                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3855 L22:   2.2473                                     
REMARK   3      L33:   1.2638 L12:  -1.0082                                     
REMARK   3      L13:  -0.1793 L23:  -0.1673                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1158 S12:  -1.4448 S13:  -0.2058                       
REMARK   3      S21:   1.2153 S22:  -0.0889 S23:   0.1342                       
REMARK   3      S31:  -0.0675 S32:  -0.0398 S33:   0.1216                       
REMARK   3   TLS GROUP : 37                                                     
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 548 THROUGH 562 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -46.9422 -15.0811  91.1619              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3159 T22:   0.6005                                     
REMARK   3      T33:   0.4811 T12:  -0.0823                                     
REMARK   3      T13:   0.2296 T23:  -0.0390                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.3243 L22:   6.2027                                     
REMARK   3      L33:   2.7178 L12:  -3.1994                                     
REMARK   3      L13:  -1.8076 L23:   2.9205                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0967 S12:  -0.0963 S13:  -0.7928                       
REMARK   3      S21:   0.1831 S22:  -0.2548 S23:   0.6318                       
REMARK   3      S31:   0.4598 S32:  -0.6432 S33:   0.2390                       
REMARK   3   TLS GROUP : 38                                                     
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 563 THROUGH 582 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -38.4435 -15.7444  98.8912              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5979 T22:   0.1671                                     
REMARK   3      T33:   0.4931 T12:  -0.1548                                     
REMARK   3      T13:   0.1096 T23:   0.0099                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.3231 L22:   4.8424                                     
REMARK   3      L33:   4.1395 L12:  -3.6320                                     
REMARK   3      L13:   3.8466 L23:  -2.0431                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1211 S12:  -0.4507 S13:  -0.3404                       
REMARK   3      S21:   0.2492 S22:  -0.1825 S23:  -0.0538                       
REMARK   3      S31:   0.4771 S32:   0.0339 S33:   0.1548                       
REMARK   3   TLS GROUP : 39                                                     
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 583 THROUGH 594 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -23.4531 -22.4117 119.6350              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.1300 T22:   0.7614                                     
REMARK   3      T33:   0.8733 T12:   0.0834                                     
REMARK   3      T13:  -0.2730 T23:  -0.1294                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4529 L22:   0.0626                                     
REMARK   3      L33:   0.6565 L12:   0.2778                                     
REMARK   3      L13:   0.9033 L23:   0.2030                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0968 S12:  -0.3313 S13:  -0.5719                       
REMARK   3      S21:  -0.3625 S22:   0.1367 S23:   0.1168                       
REMARK   3      S31:   0.1433 S32:  -0.4616 S33:   0.1594                       
REMARK   3   TLS GROUP : 40                                                     
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 595 THROUGH 630 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -30.5240 -16.9268 115.8192              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9660 T22:   0.9818                                     
REMARK   3      T33:   0.5796 T12:  -0.2020                                     
REMARK   3      T13:   0.0632 T23:   0.0127                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9258 L22:   2.0594                                     
REMARK   3      L33:   4.3343 L12:  -1.6540                                     
REMARK   3      L13:   0.1379 L23:   0.1005                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1847 S12:  -1.4493 S13:   0.1749                       
REMARK   3      S21:   1.2864 S22:  -0.2997 S23:   0.1897                       
REMARK   3      S31:   0.2928 S32:   0.2864 S33:   0.5535                       
REMARK   3   TLS GROUP : 41                                                     
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 631 THROUGH 655 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -22.1947  -8.2059 116.1018              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9191 T22:   0.9210                                     
REMARK   3      T33:   1.0407 T12:   0.0813                                     
REMARK   3      T13:  -0.0404 T23:  -0.1140                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1973 L22:   5.5778                                     
REMARK   3      L33:   6.4603 L12:   1.6030                                     
REMARK   3      L13:   0.3528 L23:  -2.5212                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1157 S12:  -0.6501 S13:  -0.4174                       
REMARK   3      S21:   0.3108 S22:  -1.1913 S23:  -0.7065                       
REMARK   3      S31:  -0.1546 S32:   0.0409 S33:   1.0006                       
REMARK   3   TLS GROUP : 42                                                     
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 656 THROUGH 671 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -44.4632  -5.0352 117.8997              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2652 T22:   1.3285                                     
REMARK   3      T33:   1.0983 T12:  -0.2224                                     
REMARK   3      T13:   0.0683 T23:  -0.5291                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9282 L22:   1.3465                                     
REMARK   3      L33:   0.9390 L12:  -1.0715                                     
REMARK   3      L13:   0.8819 L23:  -1.1227                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5595 S12:  -0.3245 S13:   0.2996                       
REMARK   3      S21:   0.6519 S22:  -0.7870 S23:   0.5657                       
REMARK   3      S31:   0.8066 S32:  -0.6053 S33:   1.0040                       
REMARK   3   TLS GROUP : 43                                                     
REMARK   3    SELECTION: CHAIN 'F' AND (RESID 469 THROUGH 500 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -46.0562  31.2868  84.9512              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5118 T22:   0.0524                                     
REMARK   3      T33:   0.6741 T12:  -0.0747                                     
REMARK   3      T13:  -0.1008 T23:  -0.0065                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0156 L22:   2.1608                                     
REMARK   3      L33:   1.2569 L12:  -0.6858                                     
REMARK   3      L13:   0.0419 L23:  -0.8208                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2935 S12:   0.3201 S13:   0.2087                       
REMARK   3      S21:   0.0575 S22:   0.5483 S23:   0.3312                       
REMARK   3      S31:  -0.2385 S32:   0.0195 S33:  -0.0331                       
REMARK   3   TLS GROUP : 44                                                     
REMARK   3    SELECTION: CHAIN 'F' AND (RESID 501 THROUGH 577 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -23.7569  14.8236  98.9053              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3510 T22:   0.0121                                     
REMARK   3      T33:   0.6880 T12:  -0.1209                                     
REMARK   3      T13:   0.2250 T23:  -0.0649                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8414 L22:   1.3601                                     
REMARK   3      L33:   1.7984 L12:  -0.0698                                     
REMARK   3      L13:   0.1644 L23:  -0.1838                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0283 S12:  -0.1602 S13:   0.3547                       
REMARK   3      S21:  -0.0170 S22:  -0.2551 S23:  -0.0038                       
REMARK   3      S31:  -0.6505 S32:   0.4406 S33:  -0.0471                       
REMARK   3   TLS GROUP : 45                                                     
REMARK   3    SELECTION: CHAIN 'F' AND (RESID 578 THROUGH 591 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -21.9863  11.9368 105.3391              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3752 T22:   0.1856                                     
REMARK   3      T33:   0.3287 T12:   0.0534                                     
REMARK   3      T13:   0.2022 T23:   0.1802                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4272 L22:   4.9995                                     
REMARK   3      L33:   3.8861 L12:   1.3720                                     
REMARK   3      L13:  -2.5565 L23:   0.4050                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2718 S12:   0.0133 S13:  -0.1612                       
REMARK   3      S21:   0.3298 S22:   0.2144 S23:   0.0282                       
REMARK   3      S31:  -0.0141 S32:  -0.1276 S33:   0.4728                       
REMARK   3   TLS GROUP : 46                                                     
REMARK   3    SELECTION: CHAIN 'F' AND (RESID 592 THROUGH 661 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -27.0491  -6.0758  87.0303              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2800 T22:  -0.2963                                     
REMARK   3      T33:   0.5114 T12:   0.0020                                     
REMARK   3      T13:   0.1359 T23:  -0.3551                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5007 L22:   2.3623                                     
REMARK   3      L33:   0.5851 L12:   0.1446                                     
REMARK   3      L13:   0.0328 L23:   0.6462                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0062 S12:  -0.0060 S13:  -0.0894                       
REMARK   3      S21:  -0.2458 S22:   0.1560 S23:  -0.3862                       
REMARK   3      S31:  -0.3412 S32:   0.1692 S33:  -0.0173                       
REMARK   3   TLS GROUP : 47                                                     
REMARK   3    SELECTION: CHAIN 'F' AND (RESID 662 THROUGH 703 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -39.3785  20.4142  83.5331              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7310 T22:   0.1757                                     
REMARK   3      T33:   0.7271 T12:   0.0561                                     
REMARK   3      T13:  -0.0136 T23:  -0.0115                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1828 L22:   4.7562                                     
REMARK   3      L33:   0.7992 L12:  -0.2100                                     
REMARK   3      L13:   0.2342 L23:  -1.7929                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1180 S12:   0.1027 S13:   0.1330                       
REMARK   3      S21:  -1.1866 S22:  -0.0437 S23:   0.6431                       
REMARK   3      S31:   0.0390 S32:  -0.1307 S33:   0.0320                       
REMARK   3   TLS GROUP : 48                                                     
REMARK   3    SELECTION: CHAIN 'G' AND (RESID 494 THROUGH 510 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.9652 -58.9162 101.5397              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8255 T22:   1.2614                                     
REMARK   3      T33:   1.0697 T12:  -0.1644                                     
REMARK   3      T13:  -0.3649 T23:   0.2343                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3969 L22:   0.6703                                     
REMARK   3      L33:   1.6498 L12:  -0.9634                                     
REMARK   3      L13:  -0.0937 L23:   0.0389                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4182 S12:   0.1125 S13:   0.3068                       
REMARK   3      S21:   0.1045 S22:   0.0464 S23:  -0.1012                       
REMARK   3      S31:  -0.1124 S32:   0.5909 S33:   0.1945                       
REMARK   3   TLS GROUP : 49                                                     
REMARK   3    SELECTION: CHAIN 'G' AND (RESID 511 THROUGH 586 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -21.1675 -52.3216 104.2642              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7443 T22:   0.4639                                     
REMARK   3      T33:   0.8803 T12:  -0.1614                                     
REMARK   3      T13:  -0.0456 T23:  -0.0026                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9648 L22:   3.8098                                     
REMARK   3      L33:   5.0345 L12:  -0.1447                                     
REMARK   3      L13:  -1.6232 L23:  -0.1329                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.7920 S12:  -0.9059 S13:   0.2732                       
REMARK   3      S21:   0.8571 S22:  -0.4647 S23:  -0.9780                       
REMARK   3      S31:  -0.6638 S32:   0.4739 S33:  -0.2315                       
REMARK   3   TLS GROUP : 50                                                     
REMARK   3    SELECTION: CHAIN 'G' AND (RESID 587 THROUGH 671 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -31.7847 -55.1510 116.8474              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3546 T22:   1.1842                                     
REMARK   3      T33:   0.7039 T12:  -0.2913                                     
REMARK   3      T13:  -0.1057 T23:  -0.0041                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9524 L22:   2.5654                                     
REMARK   3      L33:   1.2550 L12:   0.8286                                     
REMARK   3      L13:   0.1947 L23:  -0.8982                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4258 S12:  -1.0090 S13:   0.0228                       
REMARK   3      S21:   1.2678 S22:  -0.1823 S23:   0.0081                       
REMARK   3      S31:  -0.6397 S32:   0.6922 S33:  -0.2500                       
REMARK   3   TLS GROUP : 51                                                     
REMARK   3    SELECTION: CHAIN 'H' AND (RESID 469 THROUGH 500 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -16.0317 -98.9254  85.2987              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4358 T22:   0.2217                                     
REMARK   3      T33:   0.8403 T12:   0.1729                                     
REMARK   3      T13:   0.2148 T23:   0.1401                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2403 L22:   6.0730                                     
REMARK   3      L33:   1.3568 L12:  -1.5720                                     
REMARK   3      L13:  -0.2725 L23:   1.5408                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3387 S12:   0.0271 S13:   0.3727                       
REMARK   3      S21:   0.0409 S22:   0.0564 S23:  -0.5650                       
REMARK   3      S31:   0.3008 S32:   0.2379 S33:   0.1298                       
REMARK   3   TLS GROUP : 52                                                     
REMARK   3    SELECTION: CHAIN 'H' AND (RESID 501 THROUGH 577 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -38.3045 -82.6212  98.8484              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2766 T22:  -0.0138                                     
REMARK   3      T33:   0.4343 T12:  -0.0793                                     
REMARK   3      T13:  -0.0317 T23:   0.0695                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7983 L22:   2.1173                                     
REMARK   3      L33:   1.2389 L12:   0.1941                                     
REMARK   3      L13:   0.3857 L23:  -0.1247                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2416 S12:  -0.3575 S13:  -0.2443                       
REMARK   3      S21:  -0.0170 S22:  -0.1003 S23:  -0.2267                       
REMARK   3      S31:   0.0558 S32:  -0.1090 S33:   0.0312                       
REMARK   3   TLS GROUP : 53                                                     
REMARK   3    SELECTION: CHAIN 'H' AND (RESID 578 THROUGH 591 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -40.1279 -79.7899 105.3457              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0166 T22:   0.1604                                     
REMARK   3      T33:   0.3072 T12:  -0.0535                                     
REMARK   3      T13:  -0.0073 T23:  -0.0358                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5244 L22:   5.2482                                     
REMARK   3      L33:   5.0653 L12:   0.4633                                     
REMARK   3      L13:   2.9536 L23:  -0.8039                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2730 S12:  -0.0417 S13:  -0.2540                       
REMARK   3      S21:   0.4423 S22:   0.3467 S23:  -0.0310                       
REMARK   3      S31:   0.0755 S32:   0.0144 S33:   0.0699                       
REMARK   3   TLS GROUP : 54                                                     
REMARK   3    SELECTION: CHAIN 'H' AND (RESID 592 THROUGH 634 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -38.4769 -65.5870  85.7344              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2321 T22:   0.0741                                     
REMARK   3      T33:   0.4932 T12:   0.0158                                     
REMARK   3      T13:  -0.1016 T23:  -0.0180                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.2065 L22:   5.3743                                     
REMARK   3      L33:   3.5961 L12:   2.8281                                     
REMARK   3      L13:  -3.3400 L23:  -0.6760                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1757 S12:   0.5102 S13:   0.8993                       
REMARK   3      S21:  -0.6314 S22:   0.2492 S23:   0.7882                       
REMARK   3      S31:  -0.2318 S32:  -0.4846 S33:   0.0686                       
REMARK   3   TLS GROUP : 55                                                     
REMARK   3    SELECTION: CHAIN 'H' AND (RESID 635 THROUGH 673 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -25.4009 -59.0845  89.8884              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3217 T22:  -0.0389                                     
REMARK   3      T33:   0.7957 T12:   0.0287                                     
REMARK   3      T13:   0.2153 T23:   0.1550                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5228 L22:   1.2502                                     
REMARK   3      L33:   1.5507 L12:   0.1982                                     
REMARK   3      L13:  -0.0232 L23:   0.3756                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0092 S12:  -0.0271 S13:  -0.1226                       
REMARK   3      S21:   0.2267 S22:  -0.0235 S23:  -0.4285                       
REMARK   3      S31:   0.4208 S32:   0.0741 S33:   0.3596                       
REMARK   3   TLS GROUP : 56                                                     
REMARK   3    SELECTION: CHAIN 'H' AND (RESID 674 THROUGH 704 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -24.3324 -96.7289  80.4088              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4922 T22:   0.2613                                     
REMARK   3      T33:   0.6839 T12:   0.3457                                     
REMARK   3      T13:   0.0881 T23:   0.0149                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0578 L22:   4.4428                                     
REMARK   3      L33:   0.7474 L12:   0.1453                                     
REMARK   3      L13:   0.3595 L23:   0.2746                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1296 S12:   0.1902 S13:  -0.3151                       
REMARK   3      S21:  -1.0480 S22:  -0.4051 S23:   0.3469                       
REMARK   3      S31:  -0.1911 S32:  -0.2643 S33:   0.5110                       
REMARK   3   TLS GROUP : 57                                                     
REMARK   3    SELECTION: CHAIN 'I' AND (RESID 496 THROUGH 510 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -52.6700 -61.2114  27.1347              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3666 T22:   1.7100                                     
REMARK   3      T33:   0.5323 T12:   0.2292                                     
REMARK   3      T13:  -0.1224 T23:   0.2333                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5125 L22:   1.2868                                     
REMARK   3      L33:   0.0481 L12:   1.4563                                     
REMARK   3      L13:  -0.1214 L23:   0.1235                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1081 S12:  -0.1143 S13:   0.3124                       
REMARK   3      S21:  -0.0510 S22:  -0.5109 S23:  -0.0783                       
REMARK   3      S31:  -0.1557 S32:   0.7830 S33:   0.2938                       
REMARK   3   TLS GROUP : 58                                                     
REMARK   3    SELECTION: CHAIN 'I' AND (RESID 511 THROUGH 528 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -45.5581 -48.7883  21.7224              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8293 T22:   2.4670                                     
REMARK   3      T33:   1.0604 T12:   0.6061                                     
REMARK   3      T13:   0.0193 T23:  -0.2164                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3248 L22:   1.1370                                     
REMARK   3      L33:   1.9858 L12:  -1.1665                                     
REMARK   3      L13:  -0.4636 L23:  -0.0836                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4307 S12:  -0.8091 S13:   0.0803                       
REMARK   3      S21:   0.1571 S22:   0.0261 S23:  -0.3496                       
REMARK   3      S31:  -0.0676 S32:   0.4074 S33:   0.2551                       
REMARK   3   TLS GROUP : 59                                                     
REMARK   3    SELECTION: CHAIN 'I' AND (RESID 529 THROUGH 543 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -51.9591 -38.4649  25.7668              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0122 T22:   1.8095                                     
REMARK   3      T33:   0.9359 T12:  -0.0205                                     
REMARK   3      T13:  -0.1583 T23:   0.3191                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0572 L22:   2.3551                                     
REMARK   3      L33:   1.3997 L12:  -0.2757                                     
REMARK   3      L13:  -0.1652 L23:   0.9635                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3215 S12:  -0.7514 S13:   0.0880                       
REMARK   3      S21:   1.1322 S22:  -0.3044 S23:  -0.6020                       
REMARK   3      S31:  -0.4699 S32:   1.0346 S33:   0.4343                       
REMARK   3   TLS GROUP : 60                                                     
REMARK   3    SELECTION: CHAIN 'I' AND (RESID 544 THROUGH 572 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -57.6916 -58.9506  17.0345              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8695 T22:   1.1739                                     
REMARK   3      T33:   0.4879 T12:   0.3415                                     
REMARK   3      T13:   0.4909 T23:   0.1760                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6235 L22:   0.7870                                     
REMARK   3      L33:   0.8239 L12:   0.2464                                     
REMARK   3      L13:   0.0945 L23:   0.2430                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3834 S12:   0.0713 S13:  -0.3767                       
REMARK   3      S21:   0.0302 S22:  -0.0191 S23:  -0.0145                       
REMARK   3      S31:   0.6634 S32:  -0.1033 S33:   0.2445                       
REMARK   3   TLS GROUP : 61                                                     
REMARK   3    SELECTION: CHAIN 'I' AND (RESID 573 THROUGH 591 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -48.9356 -34.6804   8.3940              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1232 T22:   1.6715                                     
REMARK   3      T33:   0.9432 T12:  -0.4770                                     
REMARK   3      T13:   0.3930 T23:  -0.4244                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4014 L22:   2.8197                                     
REMARK   3      L33:   0.5626 L12:   2.0795                                     
REMARK   3      L13:   0.2955 L23:  -0.1956                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1066 S12:   0.0182 S13:   1.0423                       
REMARK   3      S21:  -0.1982 S22:   0.5438 S23:  -0.1260                       
REMARK   3      S31:  -0.8400 S32:   0.7617 S33:  -0.7479                       
REMARK   3   TLS GROUP : 62                                                     
REMARK   3    SELECTION: CHAIN 'I' AND (RESID 592 THROUGH 605 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -42.5825 -40.5682  16.5700              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8165 T22:   2.1668                                     
REMARK   3      T33:   1.2837 T12:   0.0148                                     
REMARK   3      T13:  -0.1698 T23:  -0.1184                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8358 L22:   0.9677                                     
REMARK   3      L33:   0.5619 L12:   0.8867                                     
REMARK   3      L13:   0.5148 L23:   0.5382                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0049 S12:  -0.0749 S13:   0.0026                       
REMARK   3      S21:  -0.3968 S22:   0.2217 S23:  -0.2298                       
REMARK   3      S31:  -0.1143 S32:   0.6939 S33:  -0.0136                       
REMARK   3   TLS GROUP : 63                                                     
REMARK   3    SELECTION: CHAIN 'I' AND (RESID 606 THROUGH 630 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -51.8493 -28.9244  18.1005              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2825 T22:   1.9195                                     
REMARK   3      T33:   0.7058 T12:  -0.3372                                     
REMARK   3      T13:   0.0725 T23:  -0.4091                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4847 L22:   1.8704                                     
REMARK   3      L33:   0.4505 L12:   0.1952                                     
REMARK   3      L13:   0.0376 L23:  -0.8767                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0770 S12:   0.2386 S13:   0.1364                       
REMARK   3      S21:   0.5510 S22:   0.3598 S23:  -0.9346                       
REMARK   3      S31:  -1.0857 S32:   1.0050 S33:  -0.2535                       
REMARK   3   TLS GROUP : 64                                                     
REMARK   3    SELECTION: CHAIN 'I' AND (RESID 631 THROUGH 640 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -55.7495 -23.4555  14.3814              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.8753 T22:   1.4924                                     
REMARK   3      T33:   0.9948 T12:  -0.6977                                     
REMARK   3      T13:  -0.0659 T23:   0.3878                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3361 L22:   3.6840                                     
REMARK   3      L33:   0.7771 L12:   0.0506                                     
REMARK   3      L13:  -0.9234 L23:   1.2128                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0023 S12:   0.5253 S13:   0.9327                       
REMARK   3      S21:  -0.2930 S22:  -0.5918 S23:  -0.5748                       
REMARK   3      S31:  -1.1035 S32:   0.5249 S33:   0.4160                       
REMARK   3   TLS GROUP : 65                                                     
REMARK   3    SELECTION: CHAIN 'I' AND (RESID 641 THROUGH 656 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -59.6639 -28.1420  24.0743              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3473 T22:   1.9830                                     
REMARK   3      T33:   0.6386 T12:  -0.2433                                     
REMARK   3      T13:  -0.1777 T23:   0.1745                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4091 L22:   1.9011                                     
REMARK   3      L33:   1.4696 L12:   0.2494                                     
REMARK   3      L13:  -1.6329 L23:   0.5468                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0336 S12:   0.0331 S13:  -0.0369                       
REMARK   3      S21:  -0.3455 S22:   0.0381 S23:   0.0140                       
REMARK   3      S31:  -0.0036 S32:   0.2382 S33:  -0.0604                       
REMARK   3   TLS GROUP : 66                                                     
REMARK   3    SELECTION: CHAIN 'I' AND (RESID 657 THROUGH 668 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -52.0110 -41.1638  33.9071              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.8740 T22:   1.0219                                     
REMARK   3      T33:   1.0232 T12:  -0.3219                                     
REMARK   3      T13:  -0.3350 T23:   0.0488                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8161 L22:   3.4954                                     
REMARK   3      L33:   3.7213 L12:   1.4200                                     
REMARK   3      L13:  -0.2095 L23:   2.7843                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4240 S12:  -0.1133 S13:   0.0328                       
REMARK   3      S21:   0.2095 S22:   0.3593 S23:  -0.6384                       
REMARK   3      S31:  -0.1628 S32:   0.7335 S33:  -0.5873                       
REMARK   3   TLS GROUP : 67                                                     
REMARK   3    SELECTION: CHAIN 'J' AND (RESID 469 THROUGH 500 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -93.6750 -61.0515  43.1628              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5979 T22:   0.3008                                     
REMARK   3      T33:   0.4361 T12:  -0.0363                                     
REMARK   3      T13:   0.3441 T23:  -0.3661                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3449 L22:   1.0034                                     
REMARK   3      L33:   2.6385 L12:  -0.7781                                     
REMARK   3      L13:  -1.6294 L23:   0.4766                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1216 S12:  -0.1102 S13:  -0.1588                       
REMARK   3      S21:   0.2815 S22:   0.2365 S23:   0.0847                       
REMARK   3      S31:   0.2784 S32:   0.2003 S33:   2.3336                       
REMARK   3   TLS GROUP : 68                                                     
REMARK   3    SELECTION: CHAIN 'J' AND (RESID 501 THROUGH 542 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -86.9331 -35.2628  30.6681              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5816 T22:   0.7705                                     
REMARK   3      T33:   0.4484 T12:   0.1283                                     
REMARK   3      T13:   0.0379 T23:  -0.4751                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4180 L22:   2.0894                                     
REMARK   3      L33:   0.7243 L12:  -1.1064                                     
REMARK   3      L13:  -0.5118 L23:   1.1448                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1969 S12:  -0.0613 S13:  -0.0485                       
REMARK   3      S21:  -0.0226 S22:  -0.2680 S23:   0.5684                       
REMARK   3      S31:  -0.4201 S32:  -0.5225 S33:   0.1409                       
REMARK   3   TLS GROUP : 69                                                     
REMARK   3    SELECTION: CHAIN 'J' AND (RESID 543 THROUGH 578 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -79.5114 -36.9698  25.2719              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6226 T22:   0.5502                                     
REMARK   3      T33:   0.3360 T12:   0.1209                                     
REMARK   3      T13:  -0.1119 T23:  -0.2976                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5099 L22:   1.5078                                     
REMARK   3      L33:   2.2435 L12:  -0.2116                                     
REMARK   3      L13:  -0.1557 L23:   0.3200                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5807 S12:   0.0424 S13:   0.0792                       
REMARK   3      S21:  -0.2626 S22:  -0.2863 S23:   0.4687                       
REMARK   3      S31:  -0.5183 S32:  -0.2077 S33:  -0.2792                       
REMARK   3   TLS GROUP : 70                                                     
REMARK   3    SELECTION: CHAIN 'J' AND (RESID 579 THROUGH 591 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -78.2990 -31.4632  27.0513              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3176 T22:   0.3410                                     
REMARK   3      T33:   0.7302 T12:   0.1742                                     
REMARK   3      T13:  -0.1882 T23:  -0.2962                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1062 L22:   8.1446                                     
REMARK   3      L33:   5.8591 L12:  -1.5337                                     
REMARK   3      L13:   1.8401 L23:   1.8388                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2293 S12:   0.3093 S13:   0.1461                       
REMARK   3      S21:  -1.2278 S22:  -0.3497 S23:   0.3944                       
REMARK   3      S31:  -0.2531 S32:   0.1443 S33:   0.3201                       
REMARK   3   TLS GROUP : 71                                                     
REMARK   3    SELECTION: CHAIN 'J' AND (RESID 592 THROUGH 604 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -76.1837 -43.3056   2.7930              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0266 T22:   1.2379                                     
REMARK   3      T33:   1.1453 T12:  -0.2074                                     
REMARK   3      T13:   0.0295 T23:  -0.2971                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3012 L22:   8.4322                                     
REMARK   3      L33:   4.8253 L12:  -1.7653                                     
REMARK   3      L13:  -0.2778 L23:   5.5919                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1466 S12:   0.2549 S13:  -0.1303                       
REMARK   3      S21:  -0.3246 S22:  -0.7582 S23:   0.8388                       
REMARK   3      S31:  -0.7070 S32:  -0.0364 S33:   0.8376                       
REMARK   3   TLS GROUP : 72                                                     
REMARK   3    SELECTION: CHAIN 'J' AND (RESID 605 THROUGH 673 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -72.9677 -49.9935  11.8763              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5316 T22:   0.7632                                     
REMARK   3      T33:   0.2515 T12:  -0.0064                                     
REMARK   3      T13:   0.2800 T23:  -0.1884                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1685 L22:   2.7552                                     
REMARK   3      L33:   1.6650 L12:  -0.1962                                     
REMARK   3      L13:   0.6117 L23:   0.5523                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5521 S12:   0.1076 S13:  -0.2527                       
REMARK   3      S21:  -0.4463 S22:  -0.1897 S23:   0.0500                       
REMARK   3      S31:   0.2359 S32:   0.1030 S33:   0.2173                       
REMARK   3   TLS GROUP : 73                                                     
REMARK   3    SELECTION: CHAIN 'J' AND (RESID 674 THROUGH 706 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -99.6776 -58.3988  35.3378              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7928 T22:   0.8926                                     
REMARK   3      T33:   0.2219 T12:  -0.2041                                     
REMARK   3      T13:   0.1990 T23:  -0.1412                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6752 L22:   1.3758                                     
REMARK   3      L33:   3.8892 L12:   0.4680                                     
REMARK   3      L13:  -1.7515 L23:  -0.8875                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0445 S12:   0.7202 S13:  -0.1331                       
REMARK   3      S21:   0.0430 S22:   0.2999 S23:   0.1478                       
REMARK   3      S31:   0.0610 S32:  -1.0637 S33:   0.2750                       
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 6WG6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-APR-20.                  
REMARK 100 THE DEPOSITION ID IS D_1000248140.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-OCT-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9792                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 61430                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.540                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 12.80                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 5.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.54                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.61                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 13.00                              
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: 2WD5                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 70.31                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.14                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM ACETATE PH 4.0, 15%         
REMARK 280  POLYETHYLENE GLYCOL 400, VAPOR DIFFUSION, SITTING DROP,             
REMARK 280  TEMPERATURE 293.15K                                                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       61.99250            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      157.97450            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       72.51050            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      157.97450            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       61.99250            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       72.51050            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: HEPTAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEPTAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 12800 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 65830 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -50.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, K, L, M                         
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H                                  
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000       72.51050            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      157.97450            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEPTAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEPTAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 12470 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 65730 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -55.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, I, J, N                         
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F                                  
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000     -123.98500            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000      -72.51050            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      157.97450            
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     GLY A   470                                                      
REMARK 465     PRO A   471                                                      
REMARK 465     GLU A   472                                                      
REMARK 465     ILE A   473                                                      
REMARK 465     ASN A   474                                                      
REMARK 465     LYS A   475                                                      
REMARK 465     GLU A   476                                                      
REMARK 465     LEU A   477                                                      
REMARK 465     ASN A   478                                                      
REMARK 465     GLN A   479                                                      
REMARK 465     VAL A   480                                                      
REMARK 465     MET A   481                                                      
REMARK 465     GLU A   482                                                      
REMARK 465     GLN A   483                                                      
REMARK 465     LEU A   484                                                      
REMARK 465     GLY A   485                                                      
REMARK 465     ASP A   486                                                      
REMARK 465     ALA A   487                                                      
REMARK 465     ARG A   488                                                      
REMARK 465     ILE A   489                                                      
REMARK 465     ASP A   490                                                      
REMARK 465     ARG A   491                                                      
REMARK 465     GLN A   492                                                      
REMARK 465     GLU A   493                                                      
REMARK 465     SER A   494                                                      
REMARK 465     LYS A   677                                                      
REMARK 465     LYS A   678                                                      
REMARK 465     GLU A   679                                                      
REMARK 465     ARG A   680                                                      
REMARK 465     LEU A   681                                                      
REMARK 465     THR A   682                                                      
REMARK 465     GLU A   683                                                      
REMARK 465     GLU A   684                                                      
REMARK 465     LEU A   685                                                      
REMARK 465     LYS A   686                                                      
REMARK 465     GLU A   687                                                      
REMARK 465     GLN A   688                                                      
REMARK 465     MET A   689                                                      
REMARK 465     LYS A   690                                                      
REMARK 465     ALA A   691                                                      
REMARK 465     LYS A   692                                                      
REMARK 465     ARG A   693                                                      
REMARK 465     LYS A   694                                                      
REMARK 465     GLU A   695                                                      
REMARK 465     ALA A   696                                                      
REMARK 465     GLU A   697                                                      
REMARK 465     LEU A   698                                                      
REMARK 465     ARG A   699                                                      
REMARK 465     GLN A   700                                                      
REMARK 465     VAL A   701                                                      
REMARK 465     GLN A   702                                                      
REMARK 465     GLY B   457                                                      
REMARK 465     PRO B   458                                                      
REMARK 465     LEU B   459                                                      
REMARK 465     GLY B   460                                                      
REMARK 465     SER B   461                                                      
REMARK 465     GLY B   462                                                      
REMARK 465     ARG B   463                                                      
REMARK 465     PRO B   464                                                      
REMARK 465     GLN B   465                                                      
REMARK 465     SER B   466                                                      
REMARK 465     GLU B   467                                                      
REMARK 465     ARG B   468                                                      
REMARK 465     ARG B   705                                                      
REMARK 465     ILE B   706                                                      
REMARK 465     ASN B   707                                                      
REMARK 465     ASN B   708                                                      
REMARK 465     GLU B   709                                                      
REMARK 465     ILE B   710                                                      
REMARK 465     ASP B   711                                                      
REMARK 465     GLN B   712                                                      
REMARK 465     GLY C   470                                                      
REMARK 465     PRO C   471                                                      
REMARK 465     GLU C   472                                                      
REMARK 465     ILE C   473                                                      
REMARK 465     ASN C   474                                                      
REMARK 465     LYS C   475                                                      
REMARK 465     GLU C   476                                                      
REMARK 465     LEU C   477                                                      
REMARK 465     ASN C   478                                                      
REMARK 465     GLN C   479                                                      
REMARK 465     VAL C   480                                                      
REMARK 465     MET C   481                                                      
REMARK 465     GLU C   482                                                      
REMARK 465     GLN C   483                                                      
REMARK 465     LEU C   484                                                      
REMARK 465     GLY C   485                                                      
REMARK 465     ASP C   486                                                      
REMARK 465     ALA C   487                                                      
REMARK 465     ARG C   488                                                      
REMARK 465     ILE C   489                                                      
REMARK 465     ASP C   490                                                      
REMARK 465     ARG C   491                                                      
REMARK 465     GLN C   492                                                      
REMARK 465     GLU C   493                                                      
REMARK 465     SER C   494                                                      
REMARK 465     LYS C   677                                                      
REMARK 465     LYS C   678                                                      
REMARK 465     GLU C   679                                                      
REMARK 465     ARG C   680                                                      
REMARK 465     LEU C   681                                                      
REMARK 465     THR C   682                                                      
REMARK 465     GLU C   683                                                      
REMARK 465     GLU C   684                                                      
REMARK 465     LEU C   685                                                      
REMARK 465     LYS C   686                                                      
REMARK 465     GLU C   687                                                      
REMARK 465     GLN C   688                                                      
REMARK 465     MET C   689                                                      
REMARK 465     LYS C   690                                                      
REMARK 465     ALA C   691                                                      
REMARK 465     LYS C   692                                                      
REMARK 465     ARG C   693                                                      
REMARK 465     LYS C   694                                                      
REMARK 465     GLU C   695                                                      
REMARK 465     ALA C   696                                                      
REMARK 465     GLU C   697                                                      
REMARK 465     LEU C   698                                                      
REMARK 465     ARG C   699                                                      
REMARK 465     GLN C   700                                                      
REMARK 465     VAL C   701                                                      
REMARK 465     GLN C   702                                                      
REMARK 465     GLY D   457                                                      
REMARK 465     PRO D   458                                                      
REMARK 465     LEU D   459                                                      
REMARK 465     GLY D   460                                                      
REMARK 465     SER D   461                                                      
REMARK 465     GLY D   462                                                      
REMARK 465     ARG D   463                                                      
REMARK 465     PRO D   464                                                      
REMARK 465     GLN D   465                                                      
REMARK 465     SER D   466                                                      
REMARK 465     GLU D   467                                                      
REMARK 465     ILE D   703                                                      
REMARK 465     GLU D   704                                                      
REMARK 465     ARG D   705                                                      
REMARK 465     ILE D   706                                                      
REMARK 465     ASN D   707                                                      
REMARK 465     ASN D   708                                                      
REMARK 465     GLU D   709                                                      
REMARK 465     ILE D   710                                                      
REMARK 465     ASP D   711                                                      
REMARK 465     GLN D   712                                                      
REMARK 465     GLY E   470                                                      
REMARK 465     PRO E   471                                                      
REMARK 465     GLU E   472                                                      
REMARK 465     ILE E   473                                                      
REMARK 465     ASN E   474                                                      
REMARK 465     LYS E   475                                                      
REMARK 465     GLU E   476                                                      
REMARK 465     LEU E   477                                                      
REMARK 465     ASN E   478                                                      
REMARK 465     GLN E   479                                                      
REMARK 465     VAL E   480                                                      
REMARK 465     MET E   481                                                      
REMARK 465     GLU E   482                                                      
REMARK 465     GLN E   483                                                      
REMARK 465     LEU E   484                                                      
REMARK 465     GLY E   485                                                      
REMARK 465     ASP E   486                                                      
REMARK 465     ALA E   487                                                      
REMARK 465     ARG E   488                                                      
REMARK 465     ILE E   489                                                      
REMARK 465     ASP E   490                                                      
REMARK 465     ARG E   491                                                      
REMARK 465     GLN E   492                                                      
REMARK 465     GLU E   493                                                      
REMARK 465     ASP E   672                                                      
REMARK 465     LYS E   673                                                      
REMARK 465     LEU E   674                                                      
REMARK 465     LYS E   675                                                      
REMARK 465     GLU E   676                                                      
REMARK 465     LYS E   677                                                      
REMARK 465     LYS E   678                                                      
REMARK 465     GLU E   679                                                      
REMARK 465     ARG E   680                                                      
REMARK 465     LEU E   681                                                      
REMARK 465     THR E   682                                                      
REMARK 465     GLU E   683                                                      
REMARK 465     GLU E   684                                                      
REMARK 465     LEU E   685                                                      
REMARK 465     LYS E   686                                                      
REMARK 465     GLU E   687                                                      
REMARK 465     GLN E   688                                                      
REMARK 465     MET E   689                                                      
REMARK 465     LYS E   690                                                      
REMARK 465     ALA E   691                                                      
REMARK 465     LYS E   692                                                      
REMARK 465     ARG E   693                                                      
REMARK 465     LYS E   694                                                      
REMARK 465     GLU E   695                                                      
REMARK 465     ALA E   696                                                      
REMARK 465     GLU E   697                                                      
REMARK 465     LEU E   698                                                      
REMARK 465     ARG E   699                                                      
REMARK 465     GLN E   700                                                      
REMARK 465     VAL E   701                                                      
REMARK 465     GLN E   702                                                      
REMARK 465     GLY F   457                                                      
REMARK 465     PRO F   458                                                      
REMARK 465     LEU F   459                                                      
REMARK 465     GLY F   460                                                      
REMARK 465     SER F   461                                                      
REMARK 465     GLY F   462                                                      
REMARK 465     ARG F   463                                                      
REMARK 465     PRO F   464                                                      
REMARK 465     GLN F   465                                                      
REMARK 465     SER F   466                                                      
REMARK 465     GLU F   467                                                      
REMARK 465     ARG F   468                                                      
REMARK 465     GLU F   704                                                      
REMARK 465     ARG F   705                                                      
REMARK 465     ILE F   706                                                      
REMARK 465     ASN F   707                                                      
REMARK 465     ASN F   708                                                      
REMARK 465     GLU F   709                                                      
REMARK 465     ILE F   710                                                      
REMARK 465     ASP F   711                                                      
REMARK 465     GLN F   712                                                      
REMARK 465     GLY G   470                                                      
REMARK 465     PRO G   471                                                      
REMARK 465     GLU G   472                                                      
REMARK 465     ILE G   473                                                      
REMARK 465     ASN G   474                                                      
REMARK 465     LYS G   475                                                      
REMARK 465     GLU G   476                                                      
REMARK 465     LEU G   477                                                      
REMARK 465     ASN G   478                                                      
REMARK 465     GLN G   479                                                      
REMARK 465     VAL G   480                                                      
REMARK 465     MET G   481                                                      
REMARK 465     GLU G   482                                                      
REMARK 465     GLN G   483                                                      
REMARK 465     LEU G   484                                                      
REMARK 465     GLY G   485                                                      
REMARK 465     ASP G   486                                                      
REMARK 465     ALA G   487                                                      
REMARK 465     ARG G   488                                                      
REMARK 465     ILE G   489                                                      
REMARK 465     ASP G   490                                                      
REMARK 465     ARG G   491                                                      
REMARK 465     GLN G   492                                                      
REMARK 465     GLU G   493                                                      
REMARK 465     ASP G   672                                                      
REMARK 465     LYS G   673                                                      
REMARK 465     LEU G   674                                                      
REMARK 465     LYS G   675                                                      
REMARK 465     GLU G   676                                                      
REMARK 465     LYS G   677                                                      
REMARK 465     LYS G   678                                                      
REMARK 465     GLU G   679                                                      
REMARK 465     ARG G   680                                                      
REMARK 465     LEU G   681                                                      
REMARK 465     THR G   682                                                      
REMARK 465     GLU G   683                                                      
REMARK 465     GLU G   684                                                      
REMARK 465     LEU G   685                                                      
REMARK 465     LYS G   686                                                      
REMARK 465     GLU G   687                                                      
REMARK 465     GLN G   688                                                      
REMARK 465     MET G   689                                                      
REMARK 465     LYS G   690                                                      
REMARK 465     ALA G   691                                                      
REMARK 465     LYS G   692                                                      
REMARK 465     ARG G   693                                                      
REMARK 465     LYS G   694                                                      
REMARK 465     GLU G   695                                                      
REMARK 465     ALA G   696                                                      
REMARK 465     GLU G   697                                                      
REMARK 465     LEU G   698                                                      
REMARK 465     ARG G   699                                                      
REMARK 465     GLN G   700                                                      
REMARK 465     VAL G   701                                                      
REMARK 465     GLN G   702                                                      
REMARK 465     GLY H   457                                                      
REMARK 465     PRO H   458                                                      
REMARK 465     LEU H   459                                                      
REMARK 465     GLY H   460                                                      
REMARK 465     SER H   461                                                      
REMARK 465     GLY H   462                                                      
REMARK 465     ARG H   463                                                      
REMARK 465     PRO H   464                                                      
REMARK 465     GLN H   465                                                      
REMARK 465     SER H   466                                                      
REMARK 465     GLU H   467                                                      
REMARK 465     ARG H   468                                                      
REMARK 465     ARG H   705                                                      
REMARK 465     ILE H   706                                                      
REMARK 465     ASN H   707                                                      
REMARK 465     ASN H   708                                                      
REMARK 465     GLU H   709                                                      
REMARK 465     ILE H   710                                                      
REMARK 465     ASP H   711                                                      
REMARK 465     GLN H   712                                                      
REMARK 465     GLY I   470                                                      
REMARK 465     PRO I   471                                                      
REMARK 465     GLU I   472                                                      
REMARK 465     ILE I   473                                                      
REMARK 465     ASN I   474                                                      
REMARK 465     LYS I   475                                                      
REMARK 465     GLU I   476                                                      
REMARK 465     LEU I   477                                                      
REMARK 465     ASN I   478                                                      
REMARK 465     GLN I   479                                                      
REMARK 465     VAL I   480                                                      
REMARK 465     MET I   481                                                      
REMARK 465     GLU I   482                                                      
REMARK 465     GLN I   483                                                      
REMARK 465     LEU I   484                                                      
REMARK 465     GLY I   485                                                      
REMARK 465     ASP I   486                                                      
REMARK 465     ALA I   487                                                      
REMARK 465     ARG I   488                                                      
REMARK 465     ILE I   489                                                      
REMARK 465     ASP I   490                                                      
REMARK 465     ARG I   491                                                      
REMARK 465     GLN I   492                                                      
REMARK 465     GLU I   493                                                      
REMARK 465     SER I   494                                                      
REMARK 465     SER I   495                                                      
REMARK 465     LYS I   669                                                      
REMARK 465     ALA I   670                                                      
REMARK 465     VAL I   671                                                      
REMARK 465     ASP I   672                                                      
REMARK 465     LYS I   673                                                      
REMARK 465     LEU I   674                                                      
REMARK 465     LYS I   675                                                      
REMARK 465     GLU I   676                                                      
REMARK 465     LYS I   677                                                      
REMARK 465     LYS I   678                                                      
REMARK 465     GLU I   679                                                      
REMARK 465     ARG I   680                                                      
REMARK 465     LEU I   681                                                      
REMARK 465     THR I   682                                                      
REMARK 465     GLU I   683                                                      
REMARK 465     GLU I   684                                                      
REMARK 465     LEU I   685                                                      
REMARK 465     LYS I   686                                                      
REMARK 465     GLU I   687                                                      
REMARK 465     GLN I   688                                                      
REMARK 465     MET I   689                                                      
REMARK 465     LYS I   690                                                      
REMARK 465     ALA I   691                                                      
REMARK 465     LYS I   692                                                      
REMARK 465     ARG I   693                                                      
REMARK 465     LYS I   694                                                      
REMARK 465     GLU I   695                                                      
REMARK 465     ALA I   696                                                      
REMARK 465     GLU I   697                                                      
REMARK 465     LEU I   698                                                      
REMARK 465     ARG I   699                                                      
REMARK 465     GLN I   700                                                      
REMARK 465     VAL I   701                                                      
REMARK 465     GLN I   702                                                      
REMARK 465     GLY J   457                                                      
REMARK 465     PRO J   458                                                      
REMARK 465     LEU J   459                                                      
REMARK 465     GLY J   460                                                      
REMARK 465     SER J   461                                                      
REMARK 465     GLY J   462                                                      
REMARK 465     ARG J   463                                                      
REMARK 465     PRO J   464                                                      
REMARK 465     GLN J   465                                                      
REMARK 465     SER J   466                                                      
REMARK 465     GLU J   467                                                      
REMARK 465     ARG J   468                                                      
REMARK 465     ASN J   707                                                      
REMARK 465     ASN J   708                                                      
REMARK 465     GLU J   709                                                      
REMARK 465     ILE J   710                                                      
REMARK 465     ASP J   711                                                      
REMARK 465     GLN J   712                                                      
REMARK 465     GLY K   470                                                      
REMARK 465     PRO K   471                                                      
REMARK 465     GLU K   472                                                      
REMARK 465     ILE K   473                                                      
REMARK 465     ASN K   474                                                      
REMARK 465     LYS K   475                                                      
REMARK 465     GLU K   476                                                      
REMARK 465     LEU K   477                                                      
REMARK 465     ASN K   478                                                      
REMARK 465     GLN K   479                                                      
REMARK 465     VAL K   480                                                      
REMARK 465     MET K   481                                                      
REMARK 465     GLU K   482                                                      
REMARK 465     GLN K   483                                                      
REMARK 465     LEU K   484                                                      
REMARK 465     GLY K   485                                                      
REMARK 465     ASP K   486                                                      
REMARK 465     ALA K   487                                                      
REMARK 465     ARG K   488                                                      
REMARK 465     ILE K   489                                                      
REMARK 465     ASP K   490                                                      
REMARK 465     ARG K   491                                                      
REMARK 465     GLN K   492                                                      
REMARK 465     GLU K   493                                                      
REMARK 465     SER K   494                                                      
REMARK 465     SER K   495                                                      
REMARK 465     VAL K   671                                                      
REMARK 465     ASP K   672                                                      
REMARK 465     LYS K   673                                                      
REMARK 465     LEU K   674                                                      
REMARK 465     LYS K   675                                                      
REMARK 465     GLU K   676                                                      
REMARK 465     LYS K   677                                                      
REMARK 465     LYS K   678                                                      
REMARK 465     GLU K   679                                                      
REMARK 465     ARG K   680                                                      
REMARK 465     LEU K   681                                                      
REMARK 465     THR K   682                                                      
REMARK 465     GLU K   683                                                      
REMARK 465     GLU K   684                                                      
REMARK 465     LEU K   685                                                      
REMARK 465     LYS K   686                                                      
REMARK 465     GLU K   687                                                      
REMARK 465     GLN K   688                                                      
REMARK 465     MET K   689                                                      
REMARK 465     LYS K   690                                                      
REMARK 465     ALA K   691                                                      
REMARK 465     LYS K   692                                                      
REMARK 465     ARG K   693                                                      
REMARK 465     LYS K   694                                                      
REMARK 465     GLU K   695                                                      
REMARK 465     ALA K   696                                                      
REMARK 465     GLU K   697                                                      
REMARK 465     LEU K   698                                                      
REMARK 465     ARG K   699                                                      
REMARK 465     GLN K   700                                                      
REMARK 465     VAL K   701                                                      
REMARK 465     GLN K   702                                                      
REMARK 465     GLY L   457                                                      
REMARK 465     PRO L   458                                                      
REMARK 465     LEU L   459                                                      
REMARK 465     GLY L   460                                                      
REMARK 465     SER L   461                                                      
REMARK 465     GLY L   462                                                      
REMARK 465     ARG L   463                                                      
REMARK 465     PRO L   464                                                      
REMARK 465     GLN L   465                                                      
REMARK 465     SER L   466                                                      
REMARK 465     GLU L   467                                                      
REMARK 465     ASN L   707                                                      
REMARK 465     ASN L   708                                                      
REMARK 465     GLU L   709                                                      
REMARK 465     ILE L   710                                                      
REMARK 465     ASP L   711                                                      
REMARK 465     GLN L   712                                                      
REMARK 465      DT M    11                                                      
REMARK 465      DT M    12                                                      
REMARK 465      DT M    13                                                      
REMARK 465      DT M    14                                                      
REMARK 465      DT M    15                                                      
REMARK 465      DT M    16                                                      
REMARK 465      DT M    17                                                      
REMARK 465      DT M    18                                                      
REMARK 465      DT N     5                                                      
REMARK 465      DT N     6                                                      
REMARK 465      DT N     7                                                      
REMARK 465      DT N     8                                                      
REMARK 465      DT N     9                                                      
REMARK 465      DT N    10                                                      
REMARK 465      DT N    11                                                      
REMARK 465      DT N    12                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500     DT M   9   O4' -  C1' -  N1  ANGL. DEV. =   2.5 DEGREES          
REMARK 500     DT M  10   O4' -  C1' -  N1  ANGL. DEV. =   2.0 DEGREES          
REMARK 500     DT N   3   O4' -  C1' -  N1  ANGL. DEV. =   5.2 DEGREES          
REMARK 500     DT N   4   O4' -  C1' -  N1  ANGL. DEV. =   1.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A 514       -2.52   -144.67                                   
REMARK 500    GLN A 527     -158.98   -110.04                                   
REMARK 500    TYR A 600     -155.31    -87.92                                   
REMARK 500    GLU A 601      -45.78   -141.34                                   
REMARK 500    ASN A 615       43.29   -106.88                                   
REMARK 500    ASN B 524       90.48     55.40                                   
REMARK 500    GLU B 601       40.26    -96.99                                   
REMARK 500    TYR C 511       79.36   -117.82                                   
REMARK 500    SER C 514       -3.55   -140.12                                   
REMARK 500    ASN C 615       36.27    -93.11                                   
REMARK 500    ALA C 656       63.69   -118.06                                   
REMARK 500    ASN D 524       65.90   -155.57                                   
REMARK 500    ASN D 579       80.49     57.77                                   
REMARK 500    GLU D 601       47.48   -103.41                                   
REMARK 500    THR D 646       83.43    -58.80                                   
REMARK 500    GLU E 587       41.77    -91.75                                   
REMARK 500    ASN F 579       77.09     56.79                                   
REMARK 500    GLU F 601       51.05    -94.99                                   
REMARK 500    SER G 514       -6.19   -140.80                                   
REMARK 500    GLN G 527     -159.91   -108.63                                   
REMARK 500    GLU G 587       57.23    -93.07                                   
REMARK 500    HIS G 604      -14.73     69.40                                   
REMARK 500    ASN G 615       38.25    -91.86                                   
REMARK 500    ASN H 579       79.12     60.59                                   
REMARK 500    GLU H 601       58.90   -104.32                                   
REMARK 500    GLN I 524      137.70   -172.27                                   
REMARK 500    GLN I 527     -167.43   -100.97                                   
REMARK 500    GLU I 587       37.90    -89.21                                   
REMARK 500    HIS I 604       11.41     50.12                                   
REMARK 500    ASN I 615       42.37    -99.00                                   
REMARK 500    ASN J 579       78.77     53.81                                   
REMARK 500    ASP J 593       99.58    -67.99                                   
REMARK 500    GLU J 601       46.49    -99.29                                   
REMARK 500    PHE J 645     -144.36   -111.23                                   
REMARK 500    ARG J 705       32.46    -90.88                                   
REMARK 500    LEU K 641      -37.59     71.71                                   
REMARK 500    ALA K 656       37.90   -150.94                                   
REMARK 500    ASN L 524       63.12     63.50                                   
REMARK 500    ASN L 579       72.17     60.89                                   
REMARK 500    GLU L 601       53.66   -101.09                                   
REMARK 500    PHE L 645     -141.40    -97.37                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 6WG3   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6WG4   RELATED DB: PDB                                   
DBREF  6WG6 D  465   712  UNP    Q9UQE7   SMC3_HUMAN     466    713             
DBREF  6WG6 I  472   702  UNP    G8JLG1   G8JLG1_HUMAN   450    680             
DBREF  6WG6 J  465   712  UNP    Q9UQE7   SMC3_HUMAN     466    713             
SEQADV 6WG6 GLY D  457  UNP  Q9UQE7              EXPRESSION TAG                 
SEQADV 6WG6 PRO D  458  UNP  Q9UQE7              EXPRESSION TAG                 
SEQADV 6WG6 LEU D  459  UNP  Q9UQE7              EXPRESSION TAG                 
SEQADV 6WG6 GLY D  460  UNP  Q9UQE7              EXPRESSION TAG                 
SEQADV 6WG6 SER D  461  UNP  Q9UQE7              EXPRESSION TAG                 
SEQADV 6WG6 GLY D  462  UNP  Q9UQE7              EXPRESSION TAG                 
SEQADV 6WG6 ARG D  463  UNP  Q9UQE7              EXPRESSION TAG                 
SEQADV 6WG6 PRO D  464  UNP  Q9UQE7              EXPRESSION TAG                 
SEQADV 6WG6 GLY I  470  UNP  G8JLG1              EXPRESSION TAG                 
SEQADV 6WG6 PRO I  471  UNP  G8JLG1              EXPRESSION TAG                 
SEQADV 6WG6 GLY J  457  UNP  Q9UQE7              EXPRESSION TAG                 
SEQADV 6WG6 PRO J  458  UNP  Q9UQE7              EXPRESSION TAG                 
SEQADV 6WG6 LEU J  459  UNP  Q9UQE7              EXPRESSION TAG                 
SEQADV 6WG6 GLY J  460  UNP  Q9UQE7              EXPRESSION TAG                 
SEQADV 6WG6 SER J  461  UNP  Q9UQE7              EXPRESSION TAG                 
SEQADV 6WG6 GLY J  462  UNP  Q9UQE7              EXPRESSION TAG                 
SEQADV 6WG6 ARG J  463  UNP  Q9UQE7              EXPRESSION TAG                 
SEQADV 6WG6 PRO J  464  UNP  Q9UQE7              EXPRESSION TAG                 
SEQRES   1 D  256  GLY PRO LEU GLY SER GLY ARG PRO GLN SER GLU ARG ASN          
SEQRES   2 D  256  TYR LEU TRP ARG GLU GLU ASN ALA GLU GLN GLN ALA LEU          
SEQRES   3 D  256  ALA ALA LYS ARG GLU ASP LEU GLU LYS LYS GLN GLN LEU          
SEQRES   4 D  256  LEU ARG ALA ALA THR GLY LYS ALA ILE LEU ASN GLY ILE          
SEQRES   5 D  256  ASP SER ILE ASN LYS VAL LEU ASP HIS PHE ARG ARG LYS          
SEQRES   6 D  256  GLY ILE ASN GLN HIS VAL GLN ASN GLY TYR HIS GLY ILE          
SEQRES   7 D  256  VAL MET ASN ASN PHE GLU CYS GLU PRO ALA PHE TYR THR          
SEQRES   8 D  256  CYS VAL GLU VAL THR ALA GLY ASN ARG LEU PHE TYR HIS          
SEQRES   9 D  256  ILE VAL ASP SER ASP GLU VAL SER THR LYS ILE LEU MET          
SEQRES  10 D  256  GLU PHE ASN LYS MET ASN LEU PRO GLY GLU VAL THR PHE          
SEQRES  11 D  256  LEU PRO LEU ASN LYS LEU ASP VAL ARG ASP THR ALA TYR          
SEQRES  12 D  256  PRO GLU THR ASN ASP ALA ILE PRO MET ILE SER LYS LEU          
SEQRES  13 D  256  ARG TYR ASN PRO ARG PHE ASP LYS ALA PHE LYS HIS VAL          
SEQRES  14 D  256  PHE GLY LYS THR LEU ILE CYS ARG SER MET GLU VAL SER          
SEQRES  15 D  256  THR GLN LEU ALA ARG ALA PHE THR MET ASP CYS ILE THR          
SEQRES  16 D  256  LEU GLU GLY ASP GLN VAL SER HIS ARG GLY ALA LEU THR          
SEQRES  17 D  256  GLY GLY TYR TYR ASP THR ARG LYS SER ARG LEU GLU LEU          
SEQRES  18 D  256  GLN LYS ASP VAL ARG LYS ALA GLU GLU GLU LEU GLY GLU          
SEQRES  19 D  256  LEU GLU ALA LYS LEU ASN GLU ASN LEU ARG ARG ASN ILE          
SEQRES  20 D  256  GLU ARG ILE ASN ASN GLU ILE ASP GLN                          
SEQRES   1 I  233  GLY PRO GLU ILE ASN LYS GLU LEU ASN GLN VAL MET GLU          
SEQRES   2 I  233  GLN LEU GLY ASP ALA ARG ILE ASP ARG GLN GLU SER SER          
SEQRES   3 I  233  ARG GLN GLN ARG LYS ALA GLU ILE MET GLU SER ILE LYS          
SEQRES   4 I  233  ARG LEU TYR PRO GLY SER VAL TYR GLY ARG LEU ILE ASP          
SEQRES   5 I  233  LEU CYS GLN PRO THR GLN LYS LYS TYR GLN ILE ALA VAL          
SEQRES   6 I  233  THR LYS VAL LEU GLY LYS ASN MET ASP ALA ILE ILE VAL          
SEQRES   7 I  233  ASP SER GLU LYS THR GLY ARG ASP CYS ILE GLN TYR ILE          
SEQRES   8 I  233  LYS GLU GLN ARG GLY GLU PRO GLU THR PHE LEU PRO LEU          
SEQRES   9 I  233  ASP TYR LEU GLU VAL LYS PRO THR ASP GLU LYS LEU ARG          
SEQRES  10 I  233  GLU LEU LYS GLY ALA LYS LEU VAL ILE ASP VAL ILE ARG          
SEQRES  11 I  233  TYR GLU PRO PRO HIS ILE LYS LYS ALA LEU GLN TYR ALA          
SEQRES  12 I  233  CYS GLY ASN ALA LEU VAL CYS ASP ASN VAL GLU ASP ALA          
SEQRES  13 I  233  ARG ARG ILE ALA PHE GLY GLY HIS GLN ARG HIS LYS THR          
SEQRES  14 I  233  VAL ALA LEU ASP GLY THR LEU PHE GLN LYS SER GLY VAL          
SEQRES  15 I  233  ILE SER GLY GLY ALA SER ASP LEU LYS ALA LYS ALA ARG          
SEQRES  16 I  233  ARG TRP ASP GLU LYS ALA VAL ASP LYS LEU LYS GLU LYS          
SEQRES  17 I  233  LYS GLU ARG LEU THR GLU GLU LEU LYS GLU GLN MET LYS          
SEQRES  18 I  233  ALA LYS ARG LYS GLU ALA GLU LEU ARG GLN VAL GLN              
SEQRES   1 J  256  GLY PRO LEU GLY SER GLY ARG PRO GLN SER GLU ARG ASN          
SEQRES   2 J  256  TYR LEU TRP ARG GLU GLU ASN ALA GLU GLN GLN ALA LEU          
SEQRES   3 J  256  ALA ALA LYS ARG GLU ASP LEU GLU LYS LYS GLN GLN LEU          
SEQRES   4 J  256  LEU ARG ALA ALA THR GLY LYS ALA ILE LEU ASN GLY ILE          
SEQRES   5 J  256  ASP SER ILE ASN LYS VAL LEU ASP HIS PHE ARG ARG LYS          
SEQRES   6 J  256  GLY ILE ASN GLN HIS VAL GLN ASN GLY TYR HIS GLY ILE          
SEQRES   7 J  256  VAL MET ASN ASN PHE GLU CYS GLU PRO ALA PHE TYR THR          
SEQRES   8 J  256  CYS VAL GLU VAL THR ALA GLY ASN ARG LEU PHE TYR HIS          
SEQRES   9 J  256  ILE VAL ASP SER ASP GLU VAL SER THR LYS ILE LEU MET          
SEQRES  10 J  256  GLU PHE ASN LYS MET ASN LEU PRO GLY GLU VAL THR PHE          
SEQRES  11 J  256  LEU PRO LEU ASN LYS LEU ASP VAL ARG ASP THR ALA TYR          
SEQRES  12 J  256  PRO GLU THR ASN ASP ALA ILE PRO MET ILE SER LYS LEU          
SEQRES  13 J  256  ARG TYR ASN PRO ARG PHE ASP LYS ALA PHE LYS HIS VAL          
SEQRES  14 J  256  PHE GLY LYS THR LEU ILE CYS ARG SER MET GLU VAL SER          
SEQRES  15 J  256  THR GLN LEU ALA ARG ALA PHE THR MET ASP CYS ILE THR          
SEQRES  16 J  256  LEU GLU GLY ASP GLN VAL SER HIS ARG GLY ALA LEU THR          
SEQRES  17 J  256  GLY GLY TYR TYR ASP THR ARG LYS SER ARG LEU GLU LEU          
SEQRES  18 J  256  GLN LYS ASP VAL ARG LYS ALA GLU GLU GLU LEU GLY GLU          
SEQRES  19 J  256  LEU GLU ALA LYS LEU ASN GLU ASN LEU ARG ARG ASN ILE          
SEQRES  20 J  256  GLU ARG ILE ASN ASN GLU ILE ASP GLN                          
HELIX    1 AA1 SER A  495  TYR A  511  1                                  17    
HELIX    2 AA2 ILE A  520  CYS A  523  5                                   4    
HELIX    3 AA3 TYR A  530  GLY A  539  1                                  10    
HELIX    4 AA4 LYS A  540  ASP A  543  5                                   4    
HELIX    5 AA5 SER A  549  GLN A  563  1                                  15    
HELIX    6 AA6 ASP A  582  GLU A  587  5                                   6    
HELIX    7 AA7 PRO A  602  HIS A  604  5                                   3    
HELIX    8 AA8 ILE A  605  GLY A  614  1                                  10    
HELIX    9 AA9 ASN A  621  GLY A  631  1                                  11    
HELIX   10 AB1 ASP A  658  GLU A  676  1                                  19    
HELIX   11 AB2 TYR B  470  GLY B  501  1                                  32    
HELIX   12 AB3 GLY B  501  ARG B  520  1                                  20    
HELIX   13 AB4 ASN B  524  ASN B  529  1                                   6    
HELIX   14 AB5 GLU B  542  ALA B  544  5                                   3    
HELIX   15 AB6 PHE B  545  GLY B  554  1                                  10    
HELIX   16 AB7 ASN B  555  PHE B  558  5                                   4    
HELIX   17 AB8 SER B  564  ASN B  579  1                                  16    
HELIX   18 AB9 ASN B  590  LEU B  592  5                                   3    
HELIX   19 AC1 ILE B  609  LEU B  612  5                                   4    
HELIX   20 AC2 PHE B  618  PHE B  626  1                                   9    
HELIX   21 AC3 SER B  634  THR B  646  1                                  13    
HELIX   22 AC4 SER B  673  ARG B  701  1                                  29    
HELIX   23 AC5 ARG C  496  TYR C  511  1                                  16    
HELIX   24 AC6 LEU C  519  LEU C  522  1                                   4    
HELIX   25 AC7 TYR C  530  GLY C  539  1                                  10    
HELIX   26 AC8 LYS C  540  ASP C  543  5                                   4    
HELIX   27 AC9 SER C  549  GLN C  563  1                                  15    
HELIX   28 AD1 ASP C  582  ARG C  586  5                                   5    
HELIX   29 AD2 PRO C  602  HIS C  604  5                                   3    
HELIX   30 AD3 ILE C  605  CYS C  613  1                                   9    
HELIX   31 AD4 ASN C  621  GLY C  631  1                                  11    
HELIX   32 AD5 ASP C  658  GLU C  676  1                                  19    
HELIX   33 AD6 ASN D  469  GLY D  501  1                                  33    
HELIX   34 AD7 GLY D  501  LYS D  521  1                                  21    
HELIX   35 AD8 ASN D  524  ASN D  529  1                                   6    
HELIX   36 AD9 GLU D  542  ALA D  544  5                                   3    
HELIX   37 AE1 PHE D  545  GLY D  554  1                                  10    
HELIX   38 AE2 ASN D  555  PHE D  558  5                                   4    
HELIX   39 AE3 SER D  564  ASN D  579  1                                  16    
HELIX   40 AE4 ASN D  590  LEU D  592  5                                   3    
HELIX   41 AE5 ILE D  609  LEU D  612  5                                   4    
HELIX   42 AE6 PHE D  618  PHE D  626  1                                   9    
HELIX   43 AE7 SER D  634  PHE D  645  1                                  12    
HELIX   44 AE8 SER D  673  ARG D  701  1                                  29    
HELIX   45 AE9 SER E  495  TYR E  511  1                                  17    
HELIX   46 AF1 LEU E  519  LEU E  522  1                                   4    
HELIX   47 AF2 TYR E  530  GLY E  539  1                                  10    
HELIX   48 AF3 LYS E  540  ASP E  543  5                                   4    
HELIX   49 AF4 SER E  549  ARG E  564  1                                  16    
HELIX   50 AF5 ASP E  582  LEU E  588  5                                   7    
HELIX   51 AF6 ILE E  605  GLY E  614  1                                  10    
HELIX   52 AF7 ASN E  621  GLY E  632  1                                  12    
HELIX   53 AF8 GLY E  655  VAL E  671  1                                  17    
HELIX   54 AF9 TYR F  470  GLY F  501  1                                  32    
HELIX   55 AG1 GLY F  501  LYS F  521  1                                  21    
HELIX   56 AG2 ASN F  524  GLY F  530  1                                   7    
HELIX   57 AG3 GLU F  542  ALA F  544  5                                   3    
HELIX   58 AG4 PHE F  545  GLY F  554  1                                  10    
HELIX   59 AG5 ASN F  555  LEU F  557  5                                   3    
HELIX   60 AG6 SER F  564  MET F  578  1                                  15    
HELIX   61 AG7 ASN F  590  LEU F  592  5                                   3    
HELIX   62 AG8 ILE F  609  LEU F  612  5                                   4    
HELIX   63 AG9 PHE F  618  PHE F  626  1                                   9    
HELIX   64 AH1 SER F  634  THR F  646  1                                  13    
HELIX   65 AH2 SER F  673  ARG F  701  1                                  29    
HELIX   66 AH3 SER G  495  TYR G  511  1                                  17    
HELIX   67 AH4 LEU G  519  LEU G  522  1                                   4    
HELIX   68 AH5 TYR G  530  GLY G  539  1                                  10    
HELIX   69 AH6 LYS G  540  ASP G  543  5                                   4    
HELIX   70 AH7 SER G  549  ARG G  564  1                                  16    
HELIX   71 AH8 ASP G  582  GLU G  587  5                                   6    
HELIX   72 AH9 ILE G  605  GLY G  614  1                                  10    
HELIX   73 AI1 ASN G  621  GLY G  631  1                                  11    
HELIX   74 AI2 ASP G  658  ALA G  670  1                                  13    
HELIX   75 AI3 TYR H  470  GLY H  501  1                                  32    
HELIX   76 AI4 GLY H  501  LYS H  521  1                                  21    
HELIX   77 AI5 ASN H  524  GLY H  530  1                                   7    
HELIX   78 AI6 GLU H  542  ALA H  544  5                                   3    
HELIX   79 AI7 PHE H  545  GLY H  554  1                                  10    
HELIX   80 AI8 ASN H  555  PHE H  558  5                                   4    
HELIX   81 AI9 SER H  564  ASN H  579  1                                  16    
HELIX   82 AJ1 ASN H  590  LEU H  592  5                                   3    
HELIX   83 AJ2 ILE H  609  LEU H  612  5                                   4    
HELIX   84 AJ3 PHE H  618  GLY H  627  1                                  10    
HELIX   85 AJ4 SER H  634  THR H  646  1                                  13    
HELIX   86 AJ5 SER H  673  ARG H  701  1                                  29    
HELIX   87 AJ6 GLN I  497  TYR I  511  1                                  15    
HELIX   88 AJ7 ILE I  520  CYS I  523  5                                   4    
HELIX   89 AJ8 LYS I  528  GLY I  539  1                                  12    
HELIX   90 AJ9 LYS I  540  ASP I  543  5                                   4    
HELIX   91 AK1 SER I  549  GLN I  563  1                                  15    
HELIX   92 AK2 ASP I  582  LEU I  588  5                                   7    
HELIX   93 AK3 VAL I  594  ILE I  598  1                                   5    
HELIX   94 AK4 ILE I  605  GLY I  614  1                                  10    
HELIX   95 AK5 ASN I  621  GLY I  631  1                                  11    
HELIX   96 AK6 ALA I  656  GLU I  668  1                                  13    
HELIX   97 AK7 TYR J  470  GLY J  501  1                                  32    
HELIX   98 AK8 GLY J  501  LYS J  521  1                                  21    
HELIX   99 AK9 ASN J  524  ASN J  529  1                                   6    
HELIX  100 AL1 MET J  536  PHE J  539  5                                   4    
HELIX  101 AL2 GLU J  542  ALA J  544  5                                   3    
HELIX  102 AL3 PHE J  545  GLY J  554  1                                  10    
HELIX  103 AL4 ASN J  555  PHE J  558  5                                   4    
HELIX  104 AL5 SER J  564  ASN J  579  1                                  16    
HELIX  105 AL6 ASN J  590  LEU J  592  5                                   3    
HELIX  106 AL7 ILE J  609  LEU J  612  5                                   4    
HELIX  107 AL8 ASN J  615  ARG J  617  5                                   3    
HELIX  108 AL9 PHE J  618  GLY J  627  1                                  10    
HELIX  109 AM1 SER J  634  PHE J  645  1                                  12    
HELIX  110 AM2 SER J  673  GLU J  704  1                                  32    
HELIX  111 AM3 GLN K  497  TYR K  511  1                                  15    
HELIX  112 AM4 LEU K  519  LEU K  522  1                                   4    
HELIX  113 AM5 TYR K  530  GLY K  539  1                                  10    
HELIX  114 AM6 LYS K  540  ASP K  543  5                                   4    
HELIX  115 AM7 SER K  549  ARG K  564  1                                  16    
HELIX  116 AM8 GLU K  583  LEU K  588  5                                   6    
HELIX  117 AM9 VAL K  594  ASP K  596  5                                   3    
HELIX  118 AN1 PRO K  602  ILE K  605  5                                   4    
HELIX  119 AN2 LYS K  606  CYS K  613  1                                   8    
HELIX  120 AN3 ASN K  621  PHE K  630  1                                  10    
HELIX  121 AN4 ALA K  656  ALA K  670  1                                  15    
HELIX  122 AN5 ASN L  469  GLY L  501  1                                  33    
HELIX  123 AN6 GLY L  501  GLY L  522  1                                  22    
HELIX  124 AN7 ASN L  524  ASN L  529  1                                   6    
HELIX  125 AN8 GLU L  542  ALA L  544  5                                   3    
HELIX  126 AN9 PHE L  545  GLY L  554  1                                  10    
HELIX  127 AO1 ASN L  555  PHE L  558  5                                   4    
HELIX  128 AO2 SER L  564  MET L  578  1                                  15    
HELIX  129 AO3 ASN L  590  LEU L  592  5                                   3    
HELIX  130 AO4 ILE L  609  LEU L  612  5                                   4    
HELIX  131 AO5 PHE L  618  PHE L  626  1                                   9    
HELIX  132 AO6 SER L  634  PHE L  645  1                                  12    
HELIX  133 AO7 SER L  673  ILE L  706  1                                  34    
SHEET    1 AA1 8 VAL A 515  ARG A 518  0                                        
SHEET    2 AA1 8 ILE A 545  VAL A 547 -1  O  ILE A 546   N  GLY A 517           
SHEET    3 AA1 8 GLU A 568  PRO A 572  1  O  THR A 569   N  ILE A 545           
SHEET    4 AA1 8 LEU B 663  GLY B 665 -1  O  LEU B 663   N  PHE A 570           
SHEET    5 AA1 8 GLN B 656  VAL B 657 -1  N  GLN B 656   O  THR B 664           
SHEET    6 AA1 8 ASP B 648  ILE B 650 -1  N  CYS B 649   O  VAL B 657           
SHEET    7 AA1 8 THR B 629  CYS B 632  1  N  LEU B 630   O  ASP B 648           
SHEET    8 AA1 8 ALA B 605  PRO B 607 -1  N  ILE B 606   O  ILE B 631           
SHEET    1 AA2 2 GLN A 524  PRO A 525  0                                        
SHEET    2 AA2 2 ILE A 598  ARG A 599 -1  O  ARG A 599   N  GLN A 524           
SHEET    1 AA3 5 LYS A 592  LEU A 593  0                                        
SHEET    2 AA3 5 LEU A 617  CYS A 619 -1  O  VAL A 618   N  LYS A 592           
SHEET    3 AA3 5 THR A 638  ALA A 640  1  O  VAL A 639   N  LEU A 617           
SHEET    4 AA3 5 LEU A 645  PHE A 646 -1  O  PHE A 646   N  THR A 638           
SHEET    5 AA3 5 ILE A 652  SER A 653 -1  O  SER A 653   N  LEU A 645           
SHEET    1 AA4 3 TYR B 531  ILE B 534  0                                        
SHEET    2 AA4 3 HIS B 560  VAL B 562 -1  O  ILE B 561   N  GLY B 533           
SHEET    3 AA4 3 PHE B 586  PRO B 588  1  O  LEU B 587   N  HIS B 560           
SHEET    1 AA5 2 PHE B 539  GLU B 540  0                                        
SHEET    2 AA5 2 ARG B 613  TYR B 614 -1  O  ARG B 613   N  GLU B 540           
SHEET    1 AA6 8 VAL C 515  ARG C 518  0                                        
SHEET    2 AA6 8 ILE C 545  VAL C 547 -1  O  ILE C 546   N  GLY C 517           
SHEET    3 AA6 8 GLU C 568  LEU C 571  1  O  THR C 569   N  ILE C 545           
SHEET    4 AA6 8 LEU D 663  GLY D 665 -1  O  LEU D 663   N  PHE C 570           
SHEET    5 AA6 8 GLN D 656  VAL D 657 -1  N  GLN D 656   O  THR D 664           
SHEET    6 AA6 8 CYS D 649  THR D 651 -1  N  CYS D 649   O  VAL D 657           
SHEET    7 AA6 8 LEU D 630  CYS D 632  1  N  CYS D 632   O  ILE D 650           
SHEET    8 AA6 8 ALA D 605  PRO D 607 -1  N  ILE D 606   O  ILE D 631           
SHEET    1 AA7 2 CYS C 523  PRO C 525  0                                        
SHEET    2 AA7 2 ILE C 598  TYR C 600 -1  O  ARG C 599   N  GLN C 524           
SHEET    1 AA8 5 LYS C 592  LEU C 593  0                                        
SHEET    2 AA8 5 LEU C 617  CYS C 619 -1  O  VAL C 618   N  LYS C 592           
SHEET    3 AA8 5 THR C 638  ALA C 640  1  O  VAL C 639   N  LEU C 617           
SHEET    4 AA8 5 LEU C 645  PHE C 646 -1  O  PHE C 646   N  THR C 638           
SHEET    5 AA8 5 ILE C 652  SER C 653 -1  O  SER C 653   N  LEU C 645           
SHEET    1 AA9 3 TYR D 531  ILE D 534  0                                        
SHEET    2 AA9 3 HIS D 560  VAL D 562 -1  O  ILE D 561   N  GLY D 533           
SHEET    3 AA9 3 PHE D 586  PRO D 588  1  O  LEU D 587   N  HIS D 560           
SHEET    1 AB1 2 PHE D 539  GLU D 540  0                                        
SHEET    2 AB1 2 ARG D 613  TYR D 614 -1  O  ARG D 613   N  GLU D 540           
SHEET    1 AB2 8 VAL E 515  ARG E 518  0                                        
SHEET    2 AB2 8 ILE E 545  VAL E 547 -1  O  ILE E 546   N  GLY E 517           
SHEET    3 AB2 8 GLU E 568  LEU E 571  1  O  LEU E 571   N  VAL E 547           
SHEET    4 AB2 8 LEU F 663  GLY F 665 -1  O  LEU F 663   N  PHE E 570           
SHEET    5 AB2 8 GLN F 656  VAL F 657 -1  N  GLN F 656   O  THR F 664           
SHEET    6 AB2 8 ASP F 648  THR F 651 -1  N  CYS F 649   O  VAL F 657           
SHEET    7 AB2 8 THR F 629  CYS F 632  1  N  LEU F 630   O  ASP F 648           
SHEET    8 AB2 8 ALA F 605  PRO F 607 -1  N  ILE F 606   O  ILE F 631           
SHEET    1 AB3 2 CYS E 523  PRO E 525  0                                        
SHEET    2 AB3 2 ILE E 598  TYR E 600 -1  O  ARG E 599   N  GLN E 524           
SHEET    1 AB4 5 LYS E 592  LEU E 593  0                                        
SHEET    2 AB4 5 LEU E 617  VAL E 618 -1  O  VAL E 618   N  LYS E 592           
SHEET    3 AB4 5 THR E 638  VAL E 639  1  O  VAL E 639   N  LEU E 617           
SHEET    4 AB4 5 LEU E 645  PHE E 646 -1  O  PHE E 646   N  THR E 638           
SHEET    5 AB4 5 ILE E 652  SER E 653 -1  O  SER E 653   N  LEU E 645           
SHEET    1 AB5 3 TYR F 531  ILE F 534  0                                        
SHEET    2 AB5 3 TYR F 559  VAL F 562 -1  O  ILE F 561   N  GLY F 533           
SHEET    3 AB5 3 THR F 585  PRO F 588  1  O  LEU F 587   N  HIS F 560           
SHEET    1 AB6 2 PHE F 539  GLU F 540  0                                        
SHEET    2 AB6 2 ARG F 613  TYR F 614 -1  O  ARG F 613   N  GLU F 540           
SHEET    1 AB7 8 VAL G 515  ARG G 518  0                                        
SHEET    2 AB7 8 ILE G 545  VAL G 547 -1  O  ILE G 546   N  GLY G 517           
SHEET    3 AB7 8 GLU G 568  LEU G 571  1  O  LEU G 571   N  ILE G 545           
SHEET    4 AB7 8 LEU H 663  GLY H 665 -1  O  LEU H 663   N  PHE G 570           
SHEET    5 AB7 8 GLN H 656  VAL H 657 -1  N  GLN H 656   O  THR H 664           
SHEET    6 AB7 8 ASP H 648  ILE H 650 -1  N  CYS H 649   O  VAL H 657           
SHEET    7 AB7 8 THR H 629  CYS H 632  1  N  LEU H 630   O  ASP H 648           
SHEET    8 AB7 8 ALA H 605  PRO H 607 -1  N  ILE H 606   O  ILE H 631           
SHEET    1 AB8 2 CYS G 523  PRO G 525  0                                        
SHEET    2 AB8 2 ILE G 598  TYR G 600 -1  O  ARG G 599   N  GLN G 524           
SHEET    1 AB9 5 LYS G 592  LEU G 593  0                                        
SHEET    2 AB9 5 LEU G 617  VAL G 618 -1  O  VAL G 618   N  LYS G 592           
SHEET    3 AB9 5 THR G 638  VAL G 639  1  O  VAL G 639   N  LEU G 617           
SHEET    4 AB9 5 LEU G 645  PHE G 646 -1  O  PHE G 646   N  THR G 638           
SHEET    5 AB9 5 ILE G 652  SER G 653 -1  O  SER G 653   N  LEU G 645           
SHEET    1 AC1 3 TYR H 531  ILE H 534  0                                        
SHEET    2 AC1 3 HIS H 560  VAL H 562 -1  O  ILE H 561   N  GLY H 533           
SHEET    3 AC1 3 PHE H 586  PRO H 588  1  O  LEU H 587   N  HIS H 560           
SHEET    1 AC2 2 PHE H 539  GLU H 540  0                                        
SHEET    2 AC2 2 ARG H 613  TYR H 614 -1  O  ARG H 613   N  GLU H 540           
SHEET    1 AC3 8 VAL I 515  ARG I 518  0                                        
SHEET    2 AC3 8 ILE I 545  VAL I 547 -1  O  ILE I 546   N  GLY I 517           
SHEET    3 AC3 8 GLU I 568  LEU I 571  1  O  LEU I 571   N  ILE I 545           
SHEET    4 AC3 8 LEU J 663  GLY J 665 -1  O  LEU J 663   N  PHE I 570           
SHEET    5 AC3 8 GLN J 656  VAL J 657 -1  N  GLN J 656   O  THR J 664           
SHEET    6 AC3 8 ASP J 648  ILE J 650 -1  N  CYS J 649   O  VAL J 657           
SHEET    7 AC3 8 THR J 629  CYS J 632  1  N  LEU J 630   O  ASP J 648           
SHEET    8 AC3 8 ALA J 605  PRO J 607 -1  N  ILE J 606   O  ILE J 631           
SHEET    1 AC4 5 LYS I 592  LEU I 593  0                                        
SHEET    2 AC4 5 LEU I 617  VAL I 618 -1  O  VAL I 618   N  LYS I 592           
SHEET    3 AC4 5 THR I 638  VAL I 639  1  O  VAL I 639   N  LEU I 617           
SHEET    4 AC4 5 LEU I 645  PHE I 646 -1  O  PHE I 646   N  THR I 638           
SHEET    5 AC4 5 ILE I 652  SER I 653 -1  O  SER I 653   N  LEU I 645           
SHEET    1 AC5 3 TYR J 531  ILE J 534  0                                        
SHEET    2 AC5 3 HIS J 560  VAL J 562 -1  O  ILE J 561   N  GLY J 533           
SHEET    3 AC5 3 PHE J 586  PRO J 588  1  O  LEU J 587   N  HIS J 560           
SHEET    1 AC6 8 VAL K 515  ARG K 518  0                                        
SHEET    2 AC6 8 ILE K 545  VAL K 547 -1  O  ILE K 546   N  GLY K 517           
SHEET    3 AC6 8 GLU K 568  LEU K 571  1  O  LEU K 571   N  ILE K 545           
SHEET    4 AC6 8 LEU L 663  GLY L 665 -1  O  LEU L 663   N  PHE K 570           
SHEET    5 AC6 8 GLN L 656  VAL L 657 -1  N  GLN L 656   O  THR L 664           
SHEET    6 AC6 8 ASP L 648  ILE L 650 -1  N  CYS L 649   O  VAL L 657           
SHEET    7 AC6 8 THR L 629  CYS L 632  1  N  LEU L 630   O  ASP L 648           
SHEET    8 AC6 8 ALA L 605  PRO L 607 -1  N  ILE L 606   O  ILE L 631           
SHEET    1 AC7 2 CYS K 523  PRO K 525  0                                        
SHEET    2 AC7 2 ILE K 598  TYR K 600 -1  O  ARG K 599   N  GLN K 524           
SHEET    1 AC8 3 LEU K 617  VAL K 618  0                                        
SHEET    2 AC8 3 THR K 638  VAL K 639  1  O  VAL K 639   N  LEU K 617           
SHEET    3 AC8 3 LEU K 645  PHE K 646 -1  O  PHE K 646   N  THR K 638           
SHEET    1 AC9 3 TYR L 531  ILE L 534  0                                        
SHEET    2 AC9 3 HIS L 560  VAL L 562 -1  O  ILE L 561   N  GLY L 533           
SHEET    3 AC9 3 PHE L 586  PRO L 588  1  O  LEU L 587   N  VAL L 562           
SHEET    1 AD1 2 PHE L 539  GLU L 540  0                                        
SHEET    2 AD1 2 ARG L 613  TYR L 614 -1  O  ARG L 613   N  GLU L 540           
CRYST1  123.985  145.021  315.949  90.00  90.00  90.00 P 21 21 21   24          
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      0.008065  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006896  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003165        0.00000                         
ATOM      1  N   ARG D 468      12.299 -45.990  89.216  1.00140.81           N  
ANISOU    1  N   ARG D 468    19667  19528  14305  -2275   -382   1502       N  
ATOM      2  CA  ARG D 468      12.621 -46.168  87.805  1.00139.54           C  
ANISOU    2  CA  ARG D 468    19522  19137  14360  -2209   -514   1423       C  
ATOM      3  C   ARG D 468      11.625 -45.450  86.899  1.00138.86           C  
ANISOU    3  C   ARG D 468    19509  19056  14196  -2101   -516   1092       C  
ATOM      4  O   ARG D 468      11.932 -45.139  85.749  1.00137.75           O  
ANISOU    4  O   ARG D 468    19367  18712  14261  -2044   -574    991       O  
ATOM      5  CB  ARG D 468      12.667 -47.653  87.451  1.00140.46           C  
ANISOU    5  CB  ARG D 468    19686  19249  14434  -2269   -722   1585       C  
ATOM      6  CG  ARG D 468      13.840 -48.416  88.042  1.00141.25           C  
ANISOU    6  CG  ARG D 468    19720  19272  14677  -2346   -763   1910       C  
ATOM      7  CD  ARG D 468      13.566 -49.909  88.007  1.00143.85           C  
ANISOU    7  CD  ARG D 468    20106  19694  14854  -2409   -952   2060       C  
ATOM      8  NE  ARG D 468      14.729 -50.704  88.391  1.00143.21           N  
ANISOU    8  NE  ARG D 468    19971  19514  14930  -2455  -1025   2361       N  
ATOM      9  CZ  ARG D 468      14.794 -52.026  88.272  1.00142.10           C  
ANISOU    9  CZ  ARG D 468    19855  19414  14723  -2496  -1201   2525       C  
ATOM     10  NH1 ARG D 468      13.763 -52.701  87.782  1.00141.86           N  
ANISOU   10  NH1 ARG D 468    19903  19522  14476  -2512  -1320   2417       N  
ATOM     11  NH2 ARG D 468      15.890 -52.675  88.643  1.00141.28           N  
ANISOU   11  NH2 ARG D 468    19702  19210  14766  -2514  -1268   2789       N  
ATOM     12  N   ASN D 469      10.422 -45.194  87.423  1.00137.75           N  
ANISOU   12  N   ASN D 469    19434  19157  13749  -2070   -461    924       N  
ATOM     13  CA  ASN D 469       9.439 -44.413  86.682  1.00131.12           C  
ANISOU   13  CA  ASN D 469    18676  18324  12819  -1943   -461    594       C  
ATOM     14  C   ASN D 469       9.799 -42.934  86.640  1.00126.67           C  
ANISOU   14  C   ASN D 469    18035  17676  12418  -1857   -284    455       C  
ATOM     15  O   ASN D 469       9.263 -42.198  85.804  1.00126.81           O  
ANISOU   15  O   ASN D 469    18115  17617  12451  -1741   -296    197       O  
ATOM     16  CB  ASN D 469       8.049 -44.601  87.295  1.00126.48           C  
ANISOU   16  CB  ASN D 469    18177  18044  11837  -1909   -461    443       C  
ATOM     17  CG  ASN D 469       7.788 -43.656  88.453  1.00123.21           C  
ANISOU   17  CG  ASN D 469    17681  17866  11268  -1884   -244    386       C  
ATOM     18  OD1 ASN D 469       7.156 -42.611  88.290  1.00119.71           O  
ANISOU   18  OD1 ASN D 469    17252  17482  10751  -1755   -158    120       O  
ATOM     19  ND2 ASN D 469       8.271 -44.022  89.636  1.00125.08           N  
ANISOU   19  ND2 ASN D 469    17831  18246  11447  -2011   -161    642       N  
ATOM     20  N   TYR D 470      10.695 -42.491  87.521  1.00127.02           N  
ANISOU   20  N   TYR D 470    17954  17724  12583  -1914   -131    621       N  
ATOM     21  CA  TYR D 470      11.130 -41.101  87.543  1.00122.70           C  
ANISOU   21  CA  TYR D 470    17320  17101  12200  -1844     40    507       C  
ATOM     22  C   TYR D 470      12.207 -40.819  86.501  1.00123.70           C  
ANISOU   22  C   TYR D 470    17399  16911  12692  -1815     -1    537       C  
ATOM     23  O   TYR D 470      12.232 -39.731  85.913  1.00127.69           O  
ANISOU   23  O   TYR D 470    17884  17315  13316  -1714     71    346       O  
ATOM     24  CB  TYR D 470      11.632 -40.750  88.944  1.00120.79           C  
ANISOU   24  CB  TYR D 470    16968  16999  11926  -1937    210    676       C  
ATOM     25  CG  TYR D 470      12.343 -39.423  89.038  1.00119.60           C  
ANISOU   25  CG  TYR D 470    16710  16744  11987  -1895    377    615       C  
ATOM     26  CD2 TYR D 470      13.721 -39.367  89.218  1.00119.23           C  
ANISOU   26  CD2 TYR D 470    16575  16493  12232  -1963    406    827       C  
ATOM     27  CD1 TYR D 470      11.648 -38.230  88.930  1.00117.28           C  
ANISOU   27  CD1 TYR D 470    16405  16555  11602  -1776    497    338       C  
ATOM     28  CE2 TYR D 470      14.382 -38.159  89.304  1.00115.16           C  
ANISOU   28  CE2 TYR D 470    15963  15883  11910  -1926    552    766       C  
ATOM     29  CE1 TYR D 470      12.302 -37.016  89.013  1.00114.22           C  
ANISOU   29  CE1 TYR D 470    15913  16082  11405  -1738    647    280       C  
ATOM     30  CZ  TYR D 470      13.666 -36.985  89.199  1.00112.40           C  
ANISOU   30  CZ  TYR D 470    15595  15649  11462  -1820    676    495       C  
ATOM     31  OH  TYR D 470      14.319 -35.777  89.281  1.00108.81           O  
ANISOU   31  OH  TYR D 470    15039  15110  11194  -1783    820    431       O  
ATOM     32  N   LEU D 471      13.088 -41.795  86.254  1.00116.53           N  
ANISOU   32  N   LEU D 471    16467  15860  11949  -1893   -120    771       N  
ATOM     33  CA  LEU D 471      14.311 -41.544  85.494  1.00112.97           C  
ANISOU   33  CA  LEU D 471    15931  15148  11843  -1872   -137    842       C  
ATOM     34  C   LEU D 471      14.022 -41.221  84.033  1.00112.28           C  
ANISOU   34  C   LEU D 471    15892  14918  11852  -1788   -227    642       C  
ATOM     35  O   LEU D 471      14.532 -40.228  83.496  1.00110.79           O  
ANISOU   35  O   LEU D 471    15641  14589  11865  -1717   -150    543       O  
ATOM     36  CB  LEU D 471      15.243 -42.750  85.600  1.00112.09           C  
ANISOU   36  CB  LEU D 471    15783  14956  11851  -1957   -259   1131       C  
ATOM     37  CG  LEU D 471      16.425 -42.765  84.625  1.00110.22           C  
ANISOU   37  CG  LEU D 471    15460  14480  11938  -1921   -325   1198       C  
ATOM     38  CD1 LEU D 471      17.565 -41.904  85.145  1.00105.66           C  
ANISOU   38  CD1 LEU D 471    14767  13787  11591  -1896   -181   1268       C  
ATOM     39  CD2 LEU D 471      16.892 -44.190  84.368  1.00110.40           C  
ANISOU   39  CD2 LEU D 471    15481  14474  11994  -1980   -509   1414       C  
ATOM     40  N   TRP D 472      13.205 -42.048  83.371  1.00107.08           N  
ANISOU   40  N   TRP D 472    15349  14292  11045  -1805   -398    585       N  
ATOM     41  CA  TRP D 472      12.963 -41.854  81.944  1.00 98.16           C  
ANISOU   41  CA  TRP D 472    14279  13010  10007  -1758   -514    428       C  
ATOM     42  C   TRP D 472      12.151 -40.589  81.684  1.00 90.46           C  
ANISOU   42  C   TRP D 472    13370  12041   8959  -1640   -424    135       C  
ATOM     43  O   TRP D 472      12.432 -39.850  80.731  1.00 88.13           O  
ANISOU   43  O   TRP D 472    13063  11580   8844  -1583   -426     26       O  
ATOM     44  CB  TRP D 472      12.286 -43.094  81.352  1.00101.54           C  
ANISOU   44  CB  TRP D 472    14823  13470  10286  -1826   -734    449       C  
ATOM     45  CG  TRP D 472      10.887 -43.364  81.831  1.00107.59           C  
ANISOU   45  CG  TRP D 472    15734  14430  10714  -1810   -770    307       C  
ATOM     46  CD1 TRP D 472      10.519 -43.902  83.031  1.00113.89           C  
ANISOU   46  CD1 TRP D 472    16536  15447  11289  -1849   -725    400       C  
ATOM     47  CD2 TRP D 472       9.675 -43.155  81.097  1.00107.42           C  
ANISOU   47  CD2 TRP D 472    15879  14406  10531  -1747   -875     47       C  
ATOM     48  NE1 TRP D 472       9.150 -44.017  83.099  1.00115.54           N  
ANISOU   48  NE1 TRP D 472    16888  15811  11200  -1804   -784    202       N  
ATOM     49  CE2 TRP D 472       8.609 -43.567  81.923  1.00111.02           C  
ANISOU   49  CE2 TRP D 472    16425  15094  10663  -1733   -883    -23       C  
ATOM     50  CE3 TRP D 472       9.386 -42.650  79.826  1.00104.61           C  
ANISOU   50  CE3 TRP D 472    15611  13869  10267  -1700   -972   -133       C  
ATOM     51  CZ2 TRP D 472       7.278 -43.489  81.519  1.00108.84           C  
ANISOU   51  CZ2 TRP D 472    16327  14871  10157  -1655   -988   -283       C  
ATOM     52  CZ3 TRP D 472       8.064 -42.573  79.426  1.00105.68           C  
ANISOU   52  CZ3 TRP D 472    15938  14033  10182  -1636  -1084   -378       C  
ATOM     53  CH2 TRP D 472       7.027 -42.990  80.270  1.00106.74           C  
ANISOU   53  CH2 TRP D 472    16162  14397   9998  -1604  -1093   -460       C  
ATOM     54  N   ARG D 473      11.182 -40.291  82.551  1.00 90.71           N  
ANISOU   54  N   ARG D 473    13461  12277   8727  -1596   -341      8       N  
ATOM     55  CA  ARG D 473      10.388 -39.080  82.371  1.00 93.71           C  
ANISOU   55  CA  ARG D 473    13899  12686   9020  -1459   -257   -282       C  
ATOM     56  C   ARG D 473      11.220 -37.830  82.642  1.00 99.32           C  
ANISOU   56  C   ARG D 473    14469  13335   9933  -1405    -60   -297       C  
ATOM     57  O   ARG D 473      11.109 -36.832  81.913  1.00101.47           O  
ANISOU   57  O   ARG D 473    14761  13495  10298  -1300    -31   -488       O  
ATOM     58  CB  ARG D 473       9.151 -39.130  83.268  1.00 86.52           C  
ANISOU   58  CB  ARG D 473    13068  12053   7754  -1412   -220   -415       C  
ATOM     59  CG  ARG D 473       7.954 -39.793  82.596  1.00 88.72           C  
ANISOU   59  CG  ARG D 473    13538  12352   7820  -1379   -422   -573       C  
ATOM     60  CD  ARG D 473       6.623 -39.281  83.123  1.00 91.84           C  
ANISOU   60  CD  ARG D 473    14024  12980   7892  -1244   -375   -838       C  
ATOM     61  NE  ARG D 473       5.617 -39.216  82.065  1.00 93.84           N  
ANISOU   61  NE  ARG D 473    14476  13127   8053  -1140   -552  -1094       N  
ATOM     62  CZ  ARG D 473       4.546 -40.000  81.997  1.00 95.29           C  
ANISOU   62  CZ  ARG D 473    14816  13415   7976  -1124   -712  -1196       C  
ATOM     63  NH1 ARG D 473       4.333 -40.920  82.931  1.00 95.51           N  
ANISOU   63  NH1 ARG D 473    14812  13677   7800  -1203   -707  -1060       N  
ATOM     64  NH2 ARG D 473       3.685 -39.868  80.997  1.00 94.18           N  
ANISOU   64  NH2 ARG D 473    14873  13138   7774  -1030   -886  -1433       N  
ATOM     65  N   GLU D 474      12.101 -37.880  83.651  1.00 99.87           N  
ANISOU   65  N   GLU D 474    14404  13460  10083  -1480     64    -91       N  
ATOM     66  CA  GLU D 474      12.942 -36.725  83.943  1.00101.57           C  
ANISOU   66  CA  GLU D 474    14486  13610  10494  -1442    242    -99       C  
ATOM     67  C   GLU D 474      13.974 -36.498  82.847  1.00 95.61           C  
ANISOU   67  C   GLU D 474    13672  12590  10064  -1424    194    -58       C  
ATOM     68  O   GLU D 474      14.277 -35.349  82.511  1.00100.33           O  
ANISOU   68  O   GLU D 474    14214  13104  10804  -1338    296   -188       O  
ATOM     69  CB  GLU D 474      13.627 -36.893  85.301  1.00108.49           C  
ANISOU   69  CB  GLU D 474    15254  14594  11373  -1545    362    123       C  
ATOM     70  CG  GLU D 474      14.180 -35.591  85.883  1.00111.44           C  
ANISOU   70  CG  GLU D 474    15506  14976  11862  -1511    565     74       C  
ATOM     71  CD  GLU D 474      15.690 -35.453  85.742  1.00115.38           C  
ANISOU   71  CD  GLU D 474    15892  15250  12698  -1547    587    246       C  
ATOM     72  OE1 GLU D 474      16.270 -36.017  84.792  1.00117.05           O  
ANISOU   72  OE1 GLU D 474    16109  15273  13092  -1542    456    319       O  
ATOM     73  OE2 GLU D 474      16.300 -34.762  86.586  1.00117.40           O  
ANISOU   73  OE2 GLU D 474    16049  15528  13029  -1578    734    304       O  
ATOM     74  N   GLU D 475      14.520 -37.572  82.264  1.00 96.13           N  
ANISOU   74  N   GLU D 475    13740  12542  10244  -1500     39    117       N  
ATOM     75  CA  GLU D 475      15.489 -37.368  81.192  1.00 83.55           C  
ANISOU   75  CA  GLU D 475    12071  10735   8938  -1481     -9    152       C  
ATOM     76  C   GLU D 475      14.815 -36.923  79.896  1.00 72.86           C  
ANISOU   76  C   GLU D 475    10816   9288   7579  -1415    -99    -61       C  
ATOM     77  O   GLU D 475      15.413 -36.154  79.131  1.00 68.18           O  
ANISOU   77  O   GLU D 475    10158   8555   7193  -1363    -67   -117       O  
ATOM     78  CB  GLU D 475      16.341 -38.628  80.994  1.00 78.38           C  
ANISOU   78  CB  GLU D 475    11364  10016   8400  -1574   -143    406       C  
ATOM     79  CG  GLU D 475      15.643 -39.842  80.418  1.00 79.49           C  
ANISOU   79  CG  GLU D 475    11617  10195   8392  -1642   -346    439       C  
ATOM     80  CD  GLU D 475      16.539 -41.068  80.404  1.00 85.85           C  
ANISOU   80  CD  GLU D 475    12348  10972   9300  -1724   -462    701       C  
ATOM     81  OE1 GLU D 475      17.459 -41.139  81.249  1.00 87.32           O  
ANISOU   81  OE1 GLU D 475    12435  11152   9592  -1732   -383    868       O  
ATOM     82  OE2 GLU D 475      16.320 -41.965  79.562  1.00 88.48           O  
ANISOU   82  OE2 GLU D 475    12724  11291   9602  -1778   -641    738       O  
ATOM     83  N   ASN D 476      13.562 -37.337  79.663  1.00 70.51           N  
ANISOU   83  N   ASN D 476    10682   9066   7043  -1413   -213   -188       N  
ATOM     84  CA  ASN D 476      12.787 -36.770  78.559  1.00 73.13           C  
ANISOU   84  CA  ASN D 476    11141   9302   7344  -1341   -298   -415       C  
ATOM     85  C   ASN D 476      12.572 -35.271  78.747  1.00 77.97           C  
ANISOU   85  C   ASN D 476    11736   9922   7966  -1202   -131   -628       C  
ATOM     86  O   ASN D 476      12.747 -34.481  77.808  1.00 86.25           O  
ANISOU   86  O   ASN D 476    12791  10822   9158  -1141   -140   -737       O  
ATOM     87  CB  ASN D 476      11.442 -37.490  78.435  1.00 69.37           C  
ANISOU   87  CB  ASN D 476    10858   8909   6589  -1352   -456   -525       C  
ATOM     88  CG  ASN D 476      11.557 -38.834  77.742  1.00 69.77           C  
ANISOU   88  CG  ASN D 476    10953   8901   6656  -1485   -669   -366       C  
ATOM     89  OD1 ASN D 476      12.658 -39.334  77.512  1.00 74.51           O  
ANISOU   89  OD1 ASN D 476    11421   9434   7454  -1566   -689   -155       O  
ATOM     90  ND2 ASN D 476      10.416 -39.426  77.407  1.00 62.74           N  
ANISOU   90  ND2 ASN D 476    10244   8044   5549  -1500   -835   -476       N  
ATOM     91  N   ALA D 477      12.206 -34.857  79.966  1.00 81.47           N  
ANISOU   91  N   ALA D 477    12150  10555   8251  -1155     23   -681       N  
ATOM     92  CA  ALA D 477      11.987 -33.433  80.227  1.00 81.69           C  
ANISOU   92  CA  ALA D 477    12144  10626   8268  -1021    189   -884       C  
ATOM     93  C   ALA D 477      13.287 -32.638  80.130  1.00 77.90           C  
ANISOU   93  C   ALA D 477    11494  10022   8083  -1016    319   -804       C  
ATOM     94  O   ALA D 477      13.293 -31.497  79.644  1.00 77.36           O  
ANISOU   94  O   ALA D 477    11412   9881   8099   -906    386   -972       O  
ATOM     95  CB  ALA D 477      11.345 -33.246  81.600  1.00 82.32           C  
ANISOU   95  CB  ALA D 477    12204  10979   8095   -995    325   -937       C  
ATOM     96  N   GLU D 478      14.398 -33.230  80.574  1.00 75.00           N  
ANISOU   96  N   GLU D 478    11001   9624   7873  -1123    344   -554       N  
ATOM     97  CA  GLU D 478      15.691 -32.561  80.499  1.00 77.06           C  
ANISOU   97  CA  GLU D 478    11102   9761   8415  -1112    450   -475       C  
ATOM     98  C   GLU D 478      16.135 -32.388  79.051  1.00 73.51           C  
ANISOU   98  C   GLU D 478    10650   9114   8167  -1082    349   -507       C  
ATOM     99  O   GLU D 478      16.670 -31.334  78.679  1.00 71.47           O  
ANISOU   99  O   GLU D 478    10310   8771   8074  -1006    442   -591       O  
ATOM    100  CB  GLU D 478      16.718 -33.356  81.309  1.00 83.80           C  
ANISOU  100  CB  GLU D 478    11851  10619   9371  -1222    466   -203       C  
ATOM    101  CG  GLU D 478      17.631 -32.511  82.182  1.00 89.67           C  
ANISOU  101  CG  GLU D 478    12452  11363  10255  -1214    648   -154       C  
ATOM    102  CD  GLU D 478      18.030 -33.223  83.466  1.00 95.42           C  
ANISOU  102  CD  GLU D 478    13145  12179  10932  -1329    678     68       C  
ATOM    103  OE1 GLU D 478      18.753 -34.238  83.399  1.00 94.06           O  
ANISOU  103  OE1 GLU D 478    12954  11920  10865  -1397    569    278       O  
ATOM    104  OE2 GLU D 478      17.615 -32.762  84.550  1.00 98.44           O  
ANISOU  104  OE2 GLU D 478    13516  12726  11160  -1353    806     36       O  
ATOM    105  N   GLN D 479      15.887 -33.397  78.209  1.00 66.00           N  
ANISOU  105  N   GLN D 479     9785   8102   7191  -1150    155   -443       N  
ATOM    106  CA  GLN D 479      16.173 -33.251  76.786  1.00 68.79           C  
ANISOU  106  CA  GLN D 479    10144   8293   7698  -1145     45   -473       C  
ATOM    107  C   GLN D 479      15.269 -32.213  76.128  1.00 76.29           C  
ANISOU  107  C   GLN D 479    11216   9197   8574  -1039     44   -732       C  
ATOM    108  O   GLN D 479      15.716 -31.496  75.224  1.00 79.70           O  
ANISOU  108  O   GLN D 479    11606   9505   9172   -998     46   -784       O  
ATOM    109  CB  GLN D 479      16.035 -34.600  76.084  1.00 67.36           C  
ANISOU  109  CB  GLN D 479    10030   8084   7482  -1262   -170   -341       C  
ATOM    110  CG  GLN D 479      17.143 -34.883  75.087  1.00 65.30           C  
ANISOU  110  CG  GLN D 479     9642   7711   7457  -1315   -246   -200       C  
ATOM    111  CD  GLN D 479      17.107 -33.962  73.884  1.00 60.66           C  
ANISOU  111  CD  GLN D 479     9074   7003   6971  -1269   -270   -336       C  
ATOM    112  OE1 GLN D 479      16.041 -33.673  73.341  1.00 60.83           O  
ANISOU  112  OE1 GLN D 479     9268   6985   6859  -1251   -352   -503       O  
ATOM    113  NE2 GLN D 479      18.276 -33.494  73.462  1.00 59.14           N  
ANISOU  113  NE2 GLN D 479     8710   6750   7011  -1244   -206   -269       N  
ATOM    114  N   GLN D 480      14.010 -32.116  76.568  1.00 79.28           N  
ANISOU  114  N   GLN D 480    11745   9679   8700   -983     36   -897       N  
ATOM    115  CA  GLN D 480      13.120 -31.078  76.049  1.00 79.97           C  
ANISOU  115  CA  GLN D 480    11957   9726   8702   -851     34  -1162       C  
ATOM    116  C   GLN D 480      13.640 -29.682  76.388  1.00 77.37           C  
ANISOU  116  C   GLN D 480    11499   9407   8491   -736    239  -1259       C  
ATOM    117  O   GLN D 480      13.639 -28.779  75.535  1.00 77.23           O  
ANISOU  117  O   GLN D 480    11508   9270   8566   -653    233  -1390       O  
ATOM    118  CB  GLN D 480      11.709 -31.281  76.605  1.00 81.77           C  
ANISOU  118  CB  GLN D 480    12354  10098   8618   -790     -9  -1326       C  
ATOM    119  CG  GLN D 480      10.784 -30.085  76.441  1.00 80.58           C  
ANISOU  119  CG  GLN D 480    12312   9958   8346   -608     30  -1621       C  
ATOM    120  CD  GLN D 480      10.133 -30.032  75.073  1.00 80.10           C  
ANISOU  120  CD  GLN D 480    12453   9701   8280   -579   -179  -1750       C  
ATOM    121  OE1 GLN D 480       9.188 -30.769  74.791  1.00 81.19           O  
ANISOU  121  OE1 GLN D 480    12779   9831   8241   -600   -358  -1810       O  
ATOM    122  NE2 GLN D 480      10.641 -29.158  74.210  1.00 77.78           N  
ANISOU  122  NE2 GLN D 480    12129   9246   8179   -538   -165  -1791       N  
ATOM    123  N   ALA D 481      14.109 -29.496  77.627  1.00 76.87           N  
ANISOU  123  N   ALA D 481    11297   9483   8426   -740    415  -1188       N  
ATOM    124  CA  ALA D 481      14.687 -28.212  78.021  1.00 72.51           C  
ANISOU  124  CA  ALA D 481    10607   8950   7992   -651    611  -1265       C  
ATOM    125  C   ALA D 481      15.956 -27.907  77.229  1.00 70.77           C  
ANISOU  125  C   ALA D 481    10259   8555   8075   -671    619  -1163       C  
ATOM    126  O   ALA D 481      16.199 -26.751  76.842  1.00 70.70           O  
ANISOU  126  O   ALA D 481    10199   8491   8172   -570    704  -1290       O  
ATOM    127  CB  ALA D 481      14.976 -28.208  79.522  1.00 71.20           C  
ANISOU  127  CB  ALA D 481    10325   8966   7764   -693    776  -1176       C  
ATOM    128  N   LEU D 482      16.766 -28.937  76.961  1.00 64.49           N  
ANISOU  128  N   LEU D 482     9405   7688   7411   -789    526   -939       N  
ATOM    129  CA  LEU D 482      17.963 -28.744  76.148  1.00 62.71           C  
ANISOU  129  CA  LEU D 482     9050   7324   7454   -800    517   -845       C  
ATOM    130  C   LEU D 482      17.610 -28.315  74.729  1.00 65.29           C  
ANISOU  130  C   LEU D 482     9460   7529   7817   -762    406   -963       C  
ATOM    131  O   LEU D 482      18.258 -27.426  74.163  1.00 69.18           O  
ANISOU  131  O   LEU D 482     9860   7946   8479   -701    468  -1008       O  
ATOM    132  CB  LEU D 482      18.798 -30.021  76.121  1.00 60.81           C  
ANISOU  132  CB  LEU D 482     8734   7058   7312   -919    418   -593       C  
ATOM    133  CG  LEU D 482      20.129 -29.985  76.876  1.00 64.67           C  
ANISOU  133  CG  LEU D 482     9041   7543   7988   -926    531   -440       C  
ATOM    134  CD1 LEU D 482      21.012 -31.119  76.411  1.00 68.51           C  
ANISOU  134  CD1 LEU D 482     9452   7978   8603  -1004    400   -226       C  
ATOM    135  CD2 LEU D 482      20.836 -28.655  76.694  1.00 62.75           C  
ANISOU  135  CD2 LEU D 482     8678   7242   7923   -825    671   -543       C  
ATOM    136  N   ALA D 483      16.575 -28.928  74.142  1.00 69.96           N  
ANISOU  136  N   ALA D 483    10237   8099   8246   -802    235  -1014       N  
ATOM    137  CA  ALA D 483      16.158 -28.560  72.790  1.00 71.40           C  
ANISOU  137  CA  ALA D 483    10532   8148   8448   -786    104  -1116       C  
ATOM    138  C   ALA D 483      15.622 -27.132  72.742  1.00 65.23           C  
ANISOU  138  C   ALA D 483     9808   7349   7628   -626    202  -1358       C  
ATOM    139  O   ALA D 483      15.844 -26.409  71.759  1.00 60.71           O  
ANISOU  139  O   ALA D 483     9236   6661   7170   -589    175  -1417       O  
ATOM    140  CB  ALA D 483      15.109 -29.546  72.277  1.00 79.01           C  
ANISOU  140  CB  ALA D 483    11703   9084   9232   -871   -114  -1124       C  
ATOM    141  N   ALA D 484      14.920 -26.712  73.802  1.00 65.86           N  
ANISOU  141  N   ALA D 484     9927   7559   7536   -528    316  -1498       N  
ATOM    142  CA  ALA D 484      14.481 -25.321  73.892  1.00 64.95           C  
ANISOU  142  CA  ALA D 484     9836   7464   7379   -358    429  -1730       C  
ATOM    143  C   ALA D 484      15.670 -24.367  73.921  1.00 56.75           C  
ANISOU  143  C   ALA D 484     8590   6403   6571   -316    595  -1698       C  
ATOM    144  O   ALA D 484      15.676 -23.345  73.216  1.00 60.36           O  
ANISOU  144  O   ALA D 484     9059   6778   7098   -218    612  -1827       O  
ATOM    145  CB  ALA D 484      13.605 -25.125  75.128  1.00 71.78           C  
ANISOU  145  CB  ALA D 484    10740   8529   8006   -272    533  -1865       C  
ATOM    146  N   LYS D 485      16.697 -24.697  74.713  1.00 51.41           N  
ANISOU  146  N   LYS D 485     7731   5788   6014   -389    707  -1526       N  
ATOM    147  CA  LYS D 485      17.888 -23.849  74.760  1.00 53.93           C  
ANISOU  147  CA  LYS D 485     7855   6078   6558   -351    852  -1494       C  
ATOM    148  C   LYS D 485      18.622 -23.819  73.420  1.00 58.79           C  
ANISOU  148  C   LYS D 485     8424   6542   7370   -378    757  -1424       C  
ATOM    149  O   LYS D 485      19.176 -22.779  73.038  1.00 63.81           O  
ANISOU  149  O   LYS D 485     8966   7137   8143   -296    844  -1495       O  
ATOM    150  CB  LYS D 485      18.825 -24.320  75.871  1.00 54.49           C  
ANISOU  150  CB  LYS D 485     7769   6221   6713   -429    957  -1316       C  
ATOM    151  CG  LYS D 485      19.542 -23.183  76.577  1.00 57.10           C  
ANISOU  151  CG  LYS D 485     7940   6597   7156   -357   1158  -1373       C  
ATOM    152  CD  LYS D 485      18.771 -22.746  77.812  1.00 64.63           C  
ANISOU  152  CD  LYS D 485     8918   7730   7909   -322   1285  -1485       C  
ATOM    153  CE  LYS D 485      19.192 -21.362  78.276  1.00 67.18           C  
ANISOU  153  CE  LYS D 485     9110   8108   8308   -230   1472  -1608       C  
ATOM    154  NZ  LYS D 485      18.910 -21.151  79.724  1.00 67.34           N  
ANISOU  154  NZ  LYS D 485     9081   8322   8182   -259   1612  -1621       N  
ATOM    155  N   ARG D 486      18.614 -24.934  72.685  1.00 56.07           N  
ANISOU  155  N   ARG D 486     8140   6134   7029   -497    578  -1285       N  
ATOM    156  CA  ARG D 486      19.286 -24.970  71.388  1.00 56.39           C  
ANISOU  156  CA  ARG D 486     8123   6067   7234   -544    480  -1204       C  
ATOM    157  C   ARG D 486      18.550 -24.129  70.354  1.00 59.71           C  
ANISOU  157  C   ARG D 486     8685   6392   7609   -480    407  -1372       C  
ATOM    158  O   ARG D 486      19.185 -23.448  69.535  1.00 61.11           O  
ANISOU  158  O   ARG D 486     8775   6509   7934   -454    423  -1374       O  
ATOM    159  CB  ARG D 486      19.423 -26.412  70.913  1.00 59.06           C  
ANISOU  159  CB  ARG D 486     8481   6392   7567   -700    303  -1009       C  
ATOM    160  CG  ARG D 486      20.351 -27.210  71.785  1.00 60.26           C  
ANISOU  160  CG  ARG D 486     8479   6618   7800   -751    360   -826       C  
ATOM    161  CD  ARG D 486      20.644 -28.576  71.235  1.00 64.70           C  
ANISOU  161  CD  ARG D 486     9024   7181   8378   -888    190   -631       C  
ATOM    162  NE  ARG D 486      21.230 -29.390  72.291  1.00 70.84           N  
ANISOU  162  NE  ARG D 486     9710   8029   9174   -918    233   -480       N  
ATOM    163  CZ  ARG D 486      21.573 -30.664  72.160  1.00 83.27           C  
ANISOU  163  CZ  ARG D 486    11250   9634  10754  -1020    107   -296       C  
ATOM    164  NH1 ARG D 486      21.392 -31.293  71.008  1.00 94.62           N  
ANISOU  164  NH1 ARG D 486    12723  11053  12174  -1115    -67   -237       N  
ATOM    165  NH2 ARG D 486      22.090 -31.306  73.191  1.00 81.31           N  
ANISOU  165  NH2 ARG D 486    10934   9438  10522  -1031    150   -167       N  
ATOM    166  N   GLU D 487      17.213 -24.160  70.371  1.00 61.21           N  
ANISOU  166  N   GLU D 487     9098   6568   7589   -446    319  -1516       N  
ATOM    167  CA  GLU D 487      16.463 -23.265  69.493  1.00 65.69           C  
ANISOU  167  CA  GLU D 487     9825   7030   8105   -358    247  -1696       C  
ATOM    168  C   GLU D 487      16.689 -21.802  69.863  1.00 64.02           C  
ANISOU  168  C   GLU D 487     9522   6855   7948   -185    437  -1858       C  
ATOM    169  O   GLU D 487      16.768 -20.947  68.969  1.00 65.54           O  
ANISOU  169  O   GLU D 487     9735   6952   8214   -127    414  -1931       O  
ATOM    170  CB  GLU D 487      14.974 -23.610  69.523  1.00 71.45           C  
ANISOU  170  CB  GLU D 487    10822   7737   8589   -331    105  -1836       C  
ATOM    171  CG  GLU D 487      14.140 -22.844  68.497  1.00 73.08           C  
ANISOU  171  CG  GLU D 487    11238   7794   8736   -248    -25  -2011       C  
ATOM    172  CD  GLU D 487      14.445 -23.251  67.065  1.00 74.48           C  
ANISOU  172  CD  GLU D 487    11466   7814   9021   -404   -217  -1873       C  
ATOM    173  OE1 GLU D 487      14.106 -24.388  66.677  1.00 77.84           O  
ANISOU  173  OE1 GLU D 487    11997   8197   9380   -557   -399  -1765       O  
ATOM    174  OE2 GLU D 487      15.026 -22.428  66.325  1.00 71.81           O  
ANISOU  174  OE2 GLU D 487    11037   7419   8829   -378   -188  -1861       O  
ATOM    175  N   ASP D 488      16.825 -21.504  71.161  1.00 65.01           N  
ANISOU  175  N   ASP D 488     9540   7124   8037   -115    622  -1902       N  
ATOM    176  CA  ASP D 488      17.176 -20.150  71.594  1.00 63.01           C  
ANISOU  176  CA  ASP D 488     9130   6964   7846     45    768  -1968       C  
ATOM    177  C   ASP D 488      18.519 -19.710  71.020  1.00 46.56           C  
ANISOU  177  C   ASP D 488     6855   4830   6006     22    824  -1854       C  
ATOM    178  O   ASP D 488      18.657 -18.590  70.502  1.00 43.93           O  
ANISOU  178  O   ASP D 488     6449   4540   5702    144    776  -1813       O  
ATOM    179  CB  ASP D 488      17.216 -20.083  73.122  1.00 75.92           C  
ANISOU  179  CB  ASP D 488    10669   8770   9409     68    945  -1989       C  
ATOM    180  CG  ASP D 488      15.878 -19.730  73.733  1.00 89.37           C  
ANISOU  180  CG  ASP D 488    12469  10621  10866    207    890  -2091       C  
ATOM    181  OD1 ASP D 488      14.837 -20.090  73.146  1.00 95.45           O  
ANISOU  181  OD1 ASP D 488    13430  11337  11500    238    722  -2174       O  
ATOM    182  OD2 ASP D 488      15.872 -19.088  74.806  1.00 92.50           O  
ANISOU  182  OD2 ASP D 488    12747  11189  11210    285   1002  -2084       O  
ATOM    183  N   LEU D 489      19.524 -20.587  71.112  1.00 45.38           N  
ANISOU  183  N   LEU D 489     6598   4640   6004   -116    867  -1719       N  
ATOM    184  CA  LEU D 489      20.858 -20.259  70.612  1.00 48.28           C  
ANISOU  184  CA  LEU D 489     6766   4974   6603   -124    921  -1621       C  
ATOM    185  C   LEU D 489      20.838 -20.059  69.101  1.00 51.47           C  
ANISOU  185  C   LEU D 489     7224   5273   7061   -146    784  -1616       C  
ATOM    186  O   LEU D 489      21.479 -19.137  68.581  1.00 48.70           O  
ANISOU  186  O   LEU D 489     6748   4943   6815    -72    820  -1603       O  
ATOM    187  CB  LEU D 489      21.845 -21.365  71.004  1.00 45.96           C  
ANISOU  187  CB  LEU D 489     6333   4711   6419   -237    909  -1399       C  
ATOM    188  CG  LEU D 489      23.358 -21.143  71.195  1.00 43.91           C  
ANISOU  188  CG  LEU D 489     5833   4467   6384   -217   1015  -1300       C  
ATOM    189  CD1 LEU D 489      24.018 -22.469  71.560  1.00 46.94           C  
ANISOU  189  CD1 LEU D 489     6145   4870   6819   -324    950  -1088       C  
ATOM    190  CD2 LEU D 489      24.088 -20.516  70.007  1.00 32.28           C  
ANISOU  190  CD2 LEU D 489     4252   2951   5064   -180    999  -1304       C  
ATOM    191  N   GLU D 490      20.091 -20.904  68.383  1.00 57.38           N  
ANISOU  191  N   GLU D 490     8145   5955   7703   -251    587  -1564       N  
ATOM    192  CA  GLU D 490      20.046 -20.782  66.930  1.00 61.34           C  
ANISOU  192  CA  GLU D 490     8709   6353   8243   -308    438  -1535       C  
ATOM    193  C   GLU D 490      19.317 -19.511  66.504  1.00 57.02           C  
ANISOU  193  C   GLU D 490     8278   5766   7620   -160    421  -1698       C  
ATOM    194  O   GLU D 490      19.712 -18.867  65.526  1.00 53.62           O  
ANISOU  194  O   GLU D 490     7795   5313   7263   -143    372  -1650       O  
ATOM    195  CB  GLU D 490      19.392 -22.019  66.314  1.00 71.11           C  
ANISOU  195  CB  GLU D 490    10110   7534   9374   -472    212  -1427       C  
ATOM    196  CG  GLU D 490      19.484 -22.065  64.798  1.00 82.43           C  
ANISOU  196  CG  GLU D 490    11586   8878  10857   -585     42  -1345       C  
ATOM    197  CD  GLU D 490      18.527 -23.063  64.180  1.00 97.43           C  
ANISOU  197  CD  GLU D 490    13711  10695  12615   -737   -198  -1293       C  
ATOM    198  OE1 GLU D 490      18.024 -22.794  63.068  1.00101.19           O  
ANISOU  198  OE1 GLU D 490    14342  11049  13058   -796   -355  -1315       O  
ATOM    199  OE2 GLU D 490      18.276 -24.116  64.804  1.00101.76           O  
ANISOU  199  OE2 GLU D 490    14288  11294  13082   -803   -238  -1227       O  
ATOM    200  N   LYS D 491      18.281 -19.106  67.250  1.00 58.60           N  
ANISOU  200  N   LYS D 491     8578   6049   7638    -15    402  -1788       N  
ATOM    201  CA  LYS D 491      17.598 -17.852  66.935  1.00 58.27           C  
ANISOU  201  CA  LYS D 491     8589   6061   7489    182    309  -1820       C  
ATOM    202  C   LYS D 491      18.494 -16.642  67.189  1.00 51.01           C  
ANISOU  202  C   LYS D 491     7476   5274   6632    288    442  -1729       C  
ATOM    203  O   LYS D 491      18.511 -15.697  66.387  1.00 49.48           O  
ANISOU  203  O   LYS D 491     7309   5070   6421    362    382  -1689       O  
ATOM    204  CB  LYS D 491      16.305 -17.727  67.741  1.00 64.40           C  
ANISOU  204  CB  LYS D 491     9479   6918   8072    326    248  -1943       C  
ATOM    205  CG  LYS D 491      15.148 -18.576  67.239  1.00 68.14           C  
ANISOU  205  CG  LYS D 491    10015   7336   8541    212    116  -2082       C  
ATOM    206  CD  LYS D 491      13.962 -18.474  68.188  1.00 71.86           C  
ANISOU  206  CD  LYS D 491    10460   7964   8878    266    190  -2220       C  
ATOM    207  CE  LYS D 491      12.827 -19.400  67.782  1.00 74.70           C  
ANISOU  207  CE  LYS D 491    11089   8208   9084    149     97  -2283       C  
ATOM    208  NZ  LYS D 491      11.571 -19.083  68.519  1.00 76.43           N  
ANISOU  208  NZ  LYS D 491    11338   8560   9141    222    164  -2410       N  
ATOM    209  N   LYS D 492      19.243 -16.649  68.299  1.00 48.47           N  
ANISOU  209  N   LYS D 492     6966   5073   6378    281    612  -1690       N  
ATOM    210  CA  LYS D 492      20.144 -15.531  68.579  1.00 39.09           C  
ANISOU  210  CA  LYS D 492     5585   4014   5254    351    701  -1595       C  
ATOM    211  C   LYS D 492      21.266 -15.454  67.546  1.00 40.92           C  
ANISOU  211  C   LYS D 492     5688   4202   5656    278    710  -1517       C  
ATOM    212  O   LYS D 492      21.636 -14.358  67.093  1.00 42.94           O  
ANISOU  212  O   LYS D 492     5884   4523   5908    344    695  -1456       O  
ATOM    213  CB  LYS D 492      20.712 -15.661  69.991  1.00 26.95           C  
ANISOU  213  CB  LYS D 492     3894   2586   3760    330    846  -1570       C  
ATOM    214  CG  LYS D 492      19.738 -15.259  71.089  1.00 29.96           C  
ANISOU  214  CG  LYS D 492     4348   3073   3964    431    858  -1627       C  
ATOM    215  CD  LYS D 492      20.349 -15.438  72.471  1.00 31.43           C  
ANISOU  215  CD  LYS D 492     4387   3351   4205    375   1004  -1604       C  
ATOM    216  CE  LYS D 492      19.291 -15.333  73.558  1.00 35.79           C  
ANISOU  216  CE  LYS D 492     5016   4008   4574    445   1030  -1682       C  
ATOM    217  NZ  LYS D 492      18.469 -16.573  73.649  1.00 30.35           N  
ANISOU  217  NZ  LYS D 492     4473   3264   3796    386   1025  -1792       N  
ATOM    218  N   GLN D 493      21.800 -16.611  67.145  1.00 42.59           N  
ANISOU  218  N   GLN D 493     5865   4304   6011    137    729  -1518       N  
ATOM    219  CA  GLN D 493      22.816 -16.647  66.100  1.00 42.01           C  
ANISOU  219  CA  GLN D 493     5664   4190   6108     68    732  -1457       C  
ATOM    220  C   GLN D 493      22.255 -16.196  64.757  1.00 51.99           C  
ANISOU  220  C   GLN D 493     7069   5371   7314     65    594  -1473       C  
ATOM    221  O   GLN D 493      22.971 -15.565  63.974  1.00 55.45           O  
ANISOU  221  O   GLN D 493     7392   5841   7835     71    606  -1424       O  
ATOM    222  CB  GLN D 493      23.392 -18.057  65.995  1.00 41.31           C  
ANISOU  222  CB  GLN D 493     5528   3981   6188    -87    756  -1449       C  
ATOM    223  CG  GLN D 493      24.642 -18.280  66.827  1.00 42.10           C  
ANISOU  223  CG  GLN D 493     5397   4152   6450    -71    902  -1389       C  
ATOM    224  CD  GLN D 493      25.190 -19.685  66.680  1.00 51.30           C  
ANISOU  224  CD  GLN D 493     6497   5299   7694   -206    828  -1235       C  
ATOM    225  OE1 GLN D 493      24.434 -20.656  66.642  1.00 52.51           O  
ANISOU  225  OE1 GLN D 493     6798   5428   7725   -314    696  -1170       O  
ATOM    226  NE2 GLN D 493      26.512 -19.801  66.608  1.00 54.56           N  
ANISOU  226  NE2 GLN D 493     6680   5779   8273   -190    877  -1134       N  
ATOM    227  N   GLN D 494      20.980 -16.490  64.486  1.00 54.88           N  
ANISOU  227  N   GLN D 494     7691   5628   7533     55    451  -1541       N  
ATOM    228  CA  GLN D 494      20.343 -16.012  63.264  1.00 55.35           C  
ANISOU  228  CA  GLN D 494     7927   5584   7519     56    291  -1552       C  
ATOM    229  C   GLN D 494      20.184 -14.497  63.284  1.00 42.29           C  
ANISOU  229  C   GLN D 494     6273   4036   5758    241    313  -1533       C  
ATOM    230  O   GLN D 494      20.383 -13.835  62.257  1.00 39.85           O  
ANISOU  230  O   GLN D 494     5981   3691   5467    238    269  -1501       O  
ATOM    231  CB  GLN D 494      18.989 -16.706  63.087  1.00 66.38           C  
ANISOU  231  CB  GLN D 494     9602   6838   8780     17     98  -1631       C  
ATOM    232  CG  GLN D 494      18.005 -16.020  62.143  1.00 65.75           C  
ANISOU  232  CG  GLN D 494     9654   6710   8617     88    -98  -1649       C  
ATOM    233  CD  GLN D 494      18.536 -15.890  60.728  1.00 64.01           C  
ANISOU  233  CD  GLN D 494     9407   6392   8523    -44   -176  -1589       C  
ATOM    234  OE1 GLN D 494      19.035 -16.856  60.149  1.00 64.98           O  
ANISOU  234  OE1 GLN D 494     9469   6420   8801   -280   -185  -1563       O  
ATOM    235  NE2 GLN D 494      18.422 -14.694  60.161  1.00 58.95           N  
ANISOU  235  NE2 GLN D 494     8921   5756   7722    -66     47  -1509       N  
ATOM    236  N   LEU D 495      19.836 -13.934  64.447  1.00 43.69           N  
ANISOU  236  N   LEU D 495     6437   4342   5821    382    378  -1539       N  
ATOM    237  CA  LEU D 495      19.773 -12.480  64.592  1.00 39.42           C  
ANISOU  237  CA  LEU D 495     5883   3907   5189    524    413  -1495       C  
ATOM    238  C   LEU D 495      21.127 -11.838  64.311  1.00 40.17           C  
ANISOU  238  C   LEU D 495     5710   4104   5447    480    514  -1424       C  
ATOM    239  O   LEU D 495      21.219 -10.848  63.569  1.00 25.16           O  
ANISOU  239  O   LEU D 495     3794   2207   3557    508    510  -1420       O  
ATOM    240  CB  LEU D 495      19.296 -12.109  65.997  1.00 27.06           C  
ANISOU  240  CB  LEU D 495     4272   2455   3554    606    508  -1544       C  
ATOM    241  CG  LEU D 495      17.802 -12.202  66.298  1.00 31.32           C  
ANISOU  241  CG  LEU D 495     5049   2942   3910    675    450  -1608       C  
ATOM    242  CD1 LEU D 495      17.502 -11.544  67.636  1.00 30.52           C  
ANISOU  242  CD1 LEU D 495     4870   2973   3754    758    575  -1655       C  
ATOM    243  CD2 LEU D 495      16.991 -11.562  65.182  1.00 36.42           C  
ANISOU  243  CD2 LEU D 495     5887   3469   4481    657    417  -1592       C  
ATOM    244  N   LEU D 496      22.195 -12.408  64.885  1.00 40.35           N  
ANISOU  244  N   LEU D 496     5537   4202   5592    410    599  -1367       N  
ATOM    245  CA  LEU D 496      23.541 -11.905  64.613  1.00 40.91           C  
ANISOU  245  CA  LEU D 496     5370   4359   5815    360    678  -1300       C  
ATOM    246  C   LEU D 496      23.886 -12.006  63.132  1.00 38.61           C  
ANISOU  246  C   LEU D 496     5084   3991   5595    309    626  -1288       C  
ATOM    247  O   LEU D 496      24.360 -11.037  62.531  1.00 37.52           O  
ANISOU  247  O   LEU D 496     4870   3909   5478    331    632  -1254       O  
ATOM    248  CB  LEU D 496      24.581 -12.651  65.449  1.00 22.27           C  
ANISOU  248  CB  LEU D 496     2844   2054   3564    298    758  -1245       C  
ATOM    249  CG  LEU D 496      26.000 -12.089  65.278  1.00 23.04           C  
ANISOU  249  CG  LEU D 496     2717   2229   3808    245    818  -1183       C  
ATOM    250  CD1 LEU D 496      26.647 -11.836  66.612  1.00 21.39           C  
ANISOU  250  CD1 LEU D 496     2390   2081   3655    211    893  -1168       C  
ATOM    251  CD2 LEU D 496      26.885 -13.028  64.453  1.00 28.44           C  
ANISOU  251  CD2 LEU D 496     3295   2870   4642    176    829  -1157       C  
ATOM    252  N   ARG D 497      23.643 -13.173  62.528  1.00 43.23           N  
ANISOU  252  N   ARG D 497     5734   4426   6264    201    588  -1345       N  
ATOM    253  CA  ARG D 497      24.031 -13.404  61.141  1.00 39.27           C  
ANISOU  253  CA  ARG D 497     5207   3825   5890     96    544  -1350       C  
ATOM    254  C   ARG D 497      23.248 -12.525  60.176  1.00 33.75           C  
ANISOU  254  C   ARG D 497     4702   3052   5071    137    427  -1367       C  
ATOM    255  O   ARG D 497      23.779 -12.130  59.131  1.00 35.46           O  
ANISOU  255  O   ARG D 497     4844   3250   5379     89    419  -1352       O  
ATOM    256  CB  ARG D 497      23.848 -14.883  60.804  1.00 39.40           C  
ANISOU  256  CB  ARG D 497     5295   3674   6002    -81    474  -1374       C  
ATOM    257  CG  ARG D 497      24.944 -15.781  61.381  1.00 40.19           C  
ANISOU  257  CG  ARG D 497     5164   3815   6291   -140    591  -1345       C  
ATOM    258  CD  ARG D 497      25.265 -17.038  60.554  1.00 36.42           C  
ANISOU  258  CD  ARG D 497     4646   3308   5883   -356    457  -1198       C  
ATOM    259  NE  ARG D 497      24.329 -17.337  59.468  1.00 45.82           N  
ANISOU  259  NE  ARG D 497     6061   4392   6957   -512    239  -1141       N  
ATOM    260  CZ  ARG D 497      23.154 -17.945  59.627  1.00 58.55           C  
ANISOU  260  CZ  ARG D 497     7934   5882   8428   -581    106  -1170       C  
ATOM    261  NH1 ARG D 497      22.761 -18.326  60.835  1.00 60.80           N  
ANISOU  261  NH1 ARG D 497     8276   6163   8664   -507    178  -1249       N  
ATOM    262  NH2 ARG D 497      22.375 -18.170  58.579  1.00 63.42           N  
ANISOU  262  NH2 ARG D 497     8759   6386   8950   -728   -107  -1117       N  
ATOM    263  N   ALA D 498      21.999 -12.199  60.511  1.00 33.85           N  
ANISOU  263  N   ALA D 498     4965   3015   4881    231    338  -1400       N  
ATOM    264  CA  ALA D 498      21.261 -11.223  59.719  1.00 38.75           C  
ANISOU  264  CA  ALA D 498     5794   3562   5365    300    246  -1405       C  
ATOM    265  C   ALA D 498      21.830  -9.824  59.911  1.00 26.26           C  
ANISOU  265  C   ALA D 498     4065   2149   3763    424    342  -1352       C  
ATOM    266  O   ALA D 498      21.895  -9.039  58.957  1.00 24.88           O  
ANISOU  266  O   ALA D 498     3926   1940   3588    431    316  -1344       O  
ATOM    267  CB  ALA D 498      19.777 -11.258  60.084  1.00 45.47           C  
ANISOU  267  CB  ALA D 498     6939   4334   6005    354    172  -1427       C  
ATOM    268  N   ALA D 499      22.263  -9.498  61.130  1.00 27.17           N  
ANISOU  268  N   ALA D 499     3966   2427   3929    468    468  -1355       N  
ATOM    269  CA  ALA D 499      22.842  -8.184  61.381  1.00 35.34           C  
ANISOU  269  CA  ALA D 499     4808   3598   5022    504    558  -1349       C  
ATOM    270  C   ALA D 499      24.251  -8.020  60.817  1.00 35.42           C  
ANISOU  270  C   ALA D 499     4590   3687   5180    427    607  -1285       C  
ATOM    271  O   ALA D 499      24.727  -6.885  60.717  1.00 38.89           O  
ANISOU  271  O   ALA D 499     4913   4206   5659    437    644  -1281       O  
ATOM    272  CB  ALA D 499      22.854  -7.896  62.883  1.00 39.33           C  
ANISOU  272  CB  ALA D 499     5201   4213   5528    524    643  -1368       C  
ATOM    273  N   THR D 500      24.932  -9.111  60.454  1.00 30.24           N  
ANISOU  273  N   THR D 500     3877   3010   4604    351    603  -1239       N  
ATOM    274  CA  THR D 500      26.286  -8.998  59.916  1.00 35.74           C  
ANISOU  274  CA  THR D 500     4360   3788   5433    291    651  -1182       C  
ATOM    275  C   THR D 500      26.273  -8.631  58.435  1.00 34.67           C  
ANISOU  275  C   THR D 500     4265   3587   5322    280    603  -1197       C  
ATOM    276  O   THR D 500      26.952  -7.687  58.018  1.00 35.60           O  
ANISOU  276  O   THR D 500     4274   3793   5460    294    626  -1163       O  
ATOM    277  CB  THR D 500      27.062 -10.304  60.118  1.00 45.41           C  
ANISOU  277  CB  THR D 500     5448   5006   6798    207    698  -1167       C  
ATOM    278  OG1 THR D 500      26.311 -11.397  59.575  1.00 54.34           O  
ANISOU  278  OG1 THR D 500     6689   5961   7996    136    661  -1252       O  
ATOM    279  CG2 THR D 500      27.369 -10.557  61.592  1.00 40.54           C  
ANISOU  279  CG2 THR D 500     4785   4464   6156    215    739  -1128       C  
ATOM    280  N   GLY D 501      25.520  -9.378  57.628  1.00 32.58           N  
ANISOU  280  N   GLY D 501     2933   4039   5405  -1041   -878   2016       N  
ATOM    281  CA  GLY D 501      25.482  -9.170  56.192  1.00 40.91           C  
ANISOU  281  CA  GLY D 501     3978   5048   6517  -1065   -853   2011       C  
ATOM    282  C   GLY D 501      25.850 -10.405  55.393  1.00 43.42           C  
ANISOU  282  C   GLY D 501     4206   5376   6915  -1087   -869   2124       C  
ATOM    283  O   GLY D 501      26.597 -11.258  55.875  1.00 48.38           O  
ANISOU  283  O   GLY D 501     4768   6038   7578  -1058   -874   2212       O  
ATOM    284  N   LYS D 502      25.337 -10.502  54.162  1.00 45.28           N  
ANISOU  284  N   LYS D 502     4438   5582   7184  -1140   -877   2126       N  
ATOM    285  CA  LYS D 502      25.570 -11.684  53.331  1.00 53.62           C  
ANISOU  285  CA  LYS D 502     5410   6650   8314  -1173   -899   2234       C  
ATOM    286  C   LYS D 502      26.992 -11.718  52.773  1.00 47.23           C  
ANISOU  286  C   LYS D 502     4528   5821   7596  -1108   -830   2302       C  
ATOM    287  O   LYS D 502      27.628 -12.782  52.752  1.00 48.80           O  
ANISOU  287  O   LYS D 502     4642   6049   7850  -1096   -839   2411       O  
ATOM    288  CB  LYS D 502      24.533 -11.778  52.192  1.00 74.85           C  
ANISOU  288  CB  LYS D 502     8115   9309  11014  -1257   -930   2212       C  
ATOM    289  CG  LYS D 502      24.491 -10.668  51.089  1.00 88.43           C  
ANISOU  289  CG  LYS D 502     9871  10963  12767  -1253   -879   2151       C  
ATOM    290  CD  LYS D 502      23.999  -9.288  51.568  1.00 94.32           C  
ANISOU  290  CD  LYS D 502    10714  11682  13442  -1232   -856   2029       C  
ATOM    291  CE  LYS D 502      24.185  -8.197  50.520  1.00 95.29           C  
ANISOU  291  CE  LYS D 502    10861  11745  13599  -1218   -799   1987       C  
ATOM    292  NZ  LYS D 502      23.775  -6.850  51.028  1.00 90.96           N  
ANISOU  292  NZ  LYS D 502    10403  11177  12982  -1194   -775   1877       N  
ATOM    293  N   ALA D 503      27.512 -10.568  52.328  1.00 45.71           N  
ANISOU  293  N   ALA D 503     4366   5581   7420  -1065   -757   2242       N  
ATOM    294  CA  ALA D 503      28.841 -10.535  51.721  1.00 40.73           C  
ANISOU  294  CA  ALA D 503     3672   4928   6874  -1008   -680   2298       C  
ATOM    295  C   ALA D 503      29.926 -10.816  52.750  1.00 43.54           C  
ANISOU  295  C   ALA D 503     3987   5306   7248   -935   -646   2338       C  
ATOM    296  O   ALA D 503      30.868 -11.569  52.480  1.00 52.73           O  
ANISOU  296  O   ALA D 503     5066   6477   8492   -901   -617   2436       O  
ATOM    297  CB  ALA D 503      29.081  -9.184  51.049  1.00 35.15           C  
ANISOU  297  CB  ALA D 503     3019   4171   6167   -987   -607   2220       C  
ATOM    298  N   ILE D 504      29.791 -10.241  53.945  1.00 35.97           N  
ANISOU  298  N   ILE D 504     3087   4359   6222   -911   -649   2266       N  
ATOM    299  CA  ILE D 504      30.792 -10.435  54.988  1.00 37.77           C  
ANISOU  299  CA  ILE D 504     3279   4601   6470   -844   -615   2296       C  
ATOM    300  C   ILE D 504      30.773 -11.873  55.498  1.00 31.54           C  
ANISOU  300  C   ILE D 504     2416   3865   5705   -853   -679   2410       C  
ATOM    301  O   ILE D 504      31.829 -12.490  55.691  1.00 32.11           O  
ANISOU  301  O   ILE D 504     2410   3940   5850   -799   -643   2495       O  
ATOM    302  CB  ILE D 504      30.567  -9.417  56.119  1.00 29.43           C  
ANISOU  302  CB  ILE D 504     2306   3544   5332   -825   -607   2189       C  
ATOM    303  CG1 ILE D 504      30.903  -8.004  55.637  1.00 28.77           C  
ANISOU  303  CG1 ILE D 504     2284   3410   5236   -805   -527   2093       C  
ATOM    304  CG2 ILE D 504      31.392  -9.772  57.320  1.00 42.37           C  
ANISOU  304  CG2 ILE D 504     3908   5202   6989   -769   -590   2226       C  
ATOM    305  CD1 ILE D 504      30.535  -6.920  56.625  1.00 44.35           C  
ANISOU  305  CD1 ILE D 504     4345   5384   7121   -798   -524   1985       C  
ATOM    306  N   LEU D 505      29.576 -12.432  55.712  1.00 31.68           N  
ANISOU  306  N   LEU D 505     2456   3921   5659   -922   -770   2416       N  
ATOM    307  CA  LEU D 505      29.460 -13.823  56.143  1.00 32.54           C  
ANISOU  307  CA  LEU D 505     2498   4087   5777   -943   -835   2529       C  
ATOM    308  C   LEU D 505      30.025 -14.779  55.099  1.00 41.83           C  
ANISOU  308  C   LEU D 505     3580   5265   7050   -947   -827   2646       C  
ATOM    309  O   LEU D 505      30.713 -15.750  55.443  1.00 42.56           O  
ANISOU  309  O   LEU D 505     3588   5388   7194   -915   -832   2759       O  
ATOM    310  CB  LEU D 505      27.997 -14.161  56.426  1.00 32.51           C  
ANISOU  310  CB  LEU D 505     2549   4123   5681  -1030   -924   2501       C  
ATOM    311  CG  LEU D 505      27.501 -14.110  57.867  1.00 31.74           C  
ANISOU  311  CG  LEU D 505     2499   4068   5492  -1030   -965   2470       C  
ATOM    312  CD1 LEU D 505      25.997 -14.265  57.880  1.00 31.77           C  
ANISOU  312  CD1 LEU D 505     2568   4099   5406  -1123  -1033   2423       C  
ATOM    313  CD2 LEU D 505      28.158 -15.209  58.687  1.00 39.00           C  
ANISOU  313  CD2 LEU D 505     3338   5039   6440   -999   -988   2593       C  
ATOM    314  N   ASN D 506      29.746 -14.512  53.818  1.00 40.49           N  
ANISOU  314  N   ASN D 506     3418   5061   6907   -985   -813   2626       N  
ATOM    315  CA  ASN D 506      30.296 -15.341  52.750  1.00 47.16           C  
ANISOU  315  CA  ASN D 506     4170   5904   7843   -990   -800   2737       C  
ATOM    316  C   ASN D 506      31.815 -15.239  52.697  1.00 46.02           C  
ANISOU  316  C   ASN D 506     3963   5736   7788   -895   -708   2788       C  
ATOM    317  O   ASN D 506      32.498 -16.250  52.511  1.00 54.31           O  
ANISOU  317  O   ASN D 506     4916   6807   8911   -871   -705   2912       O  
ATOM    318  CB  ASN D 506      29.677 -14.946  51.409  1.00 54.24           C  
ANISOU  318  CB  ASN D 506     5094   6765   8750  -1049   -800   2698       C  
ATOM    319  CG  ASN D 506      28.296 -15.541  51.207  1.00 57.93           C  
ANISOU  319  CG  ASN D 506     5587   7259   9165  -1153   -891   2692       C  
ATOM    320  OD1 ASN D 506      27.931 -16.523  51.854  1.00 63.90           O  
ANISOU  320  OD1 ASN D 506     6317   8071   9891  -1187   -954   2750       O  
ATOM    321  ND2 ASN D 506      27.519 -14.946  50.309  1.00 57.09           N  
ANISOU  321  ND2 ASN D 506     5531   7113   9049  -1208   -894   2622       N  
ATOM    322  N   GLY D 507      32.361 -14.035  52.891  1.00 43.43           N  
ANISOU  322  N   GLY D 507     3687   5363   7453   -841   -630   2694       N  
ATOM    323  CA  GLY D 507      33.807 -13.883  52.905  1.00 43.57           C  
ANISOU  323  CA  GLY D 507     3653   5351   7551   -753   -530   2730       C  
ATOM    324  C   GLY D 507      34.468 -14.583  54.079  1.00 47.12           C  
ANISOU  324  C   GLY D 507     4048   5828   8028   -697   -532   2798       C  
ATOM    325  O   GLY D 507      35.550 -15.159  53.936  1.00 39.12           O  
ANISOU  325  O   GLY D 507     2951   4807   7107   -639   -478   2893       O  
ATOM    326  N   ILE D 508      33.820 -14.559  55.246  1.00 49.93           N  
ANISOU  326  N   ILE D 508     4449   6214   8307   -714   -592   2758       N  
ATOM    327  CA  ILE D 508      34.374 -15.232  56.421  1.00 34.51           C  
ANISOU  327  CA  ILE D 508     2444   4289   6378   -664   -601   2828       C  
ATOM    328  C   ILE D 508      34.353 -16.745  56.232  1.00 59.47           C  
ANISOU  328  C   ILE D 508     5508   7502   9585   -683   -662   2984       C  
ATOM    329  O   ILE D 508      35.354 -17.430  56.487  1.00 64.32           O  
ANISOU  329  O   ILE D 508     6035   8119  10285   -619   -626   3088       O  
ATOM    330  CB  ILE D 508      33.621 -14.801  57.692  1.00 33.41           C  
ANISOU  330  CB  ILE D 508     2380   4176   6138   -683   -654   2750       C  
ATOM    331  CG1 ILE D 508      33.914 -13.334  58.012  1.00 32.19           C  
ANISOU  331  CG1 ILE D 508     2308   3971   5952   -650   -580   2612       C  
ATOM    332  CG2 ILE D 508      33.990 -15.686  58.874  1.00 33.74           C  
ANISOU  332  CG2 ILE D 508     2361   4258   6198   -647   -685   2843       C  
ATOM    333  CD1 ILE D 508      33.169 -12.820  59.216  1.00 31.11           C  
ANISOU  333  CD1 ILE D 508     2246   3859   5714   -668   -629   2532       C  
ATOM    334  N   ASP D 509      33.221 -17.287  55.762  1.00 54.65           N  
ANISOU  334  N   ASP D 509     4912   6932   8921   -772   -751   3003       N  
ATOM    335  CA  ASP D 509      33.145 -18.720  55.477  1.00 66.33           C  
ANISOU  335  CA  ASP D 509     6302   8465  10436   -804   -809   3151       C  
ATOM    336  C   ASP D 509      34.122 -19.126  54.378  1.00 56.43           C  
ANISOU  336  C   ASP D 509     4958   7185   9297   -765   -748   3243       C  
ATOM    337  O   ASP D 509      34.702 -20.220  54.425  1.00 51.28           O  
ANISOU  337  O   ASP D 509     4208   6566   8712   -739   -756   3384       O  
ATOM    338  CB  ASP D 509      31.717 -19.105  55.084  1.00 77.46           C  
ANISOU  338  CB  ASP D 509     7755   9915  11762   -918   -903   3134       C  
ATOM    339  CG  ASP D 509      30.851 -19.443  56.285  1.00 87.47           C  
ANISOU  339  CG  ASP D 509     9065  11240  12928   -960   -981   3125       C  
ATOM    340  OD1 ASP D 509      30.239 -18.519  56.863  1.00 90.10           O  
ANISOU  340  OD1 ASP D 509     9493  11560  13181   -971   -986   3002       O  
ATOM    341  OD2 ASP D 509      30.774 -20.639  56.646  1.00 89.68           O  
ANISOU  341  OD2 ASP D 509     9283  11584  13206   -985  -1037   3246       O  
ATOM    342  N   SER D 510      34.362 -18.237  53.415  1.00 56.68           N  
ANISOU  342  N   SER D 510     5020   7161   9355   -757   -680   3170       N  
ATOM    343  CA  SER D 510      35.278 -18.551  52.329  1.00 54.46           C  
ANISOU  343  CA  SER D 510     4658   6856   9178   -722   -615   3255       C  
ATOM    344  C   SER D 510      36.730 -18.541  52.791  1.00 49.94           C  
ANISOU  344  C   SER D 510     4028   6254   8694   -611   -518   3303       C  
ATOM    345  O   SER D 510      37.522 -19.383  52.360  1.00 43.86           O  
ANISOU  345  O   SER D 510     3158   5491   8016   -572   -488   3431       O  
ATOM    346  CB  SER D 510      35.084 -17.567  51.185  1.00 51.99           C  
ANISOU  346  CB  SER D 510     4399   6494   8860   -748   -570   3166       C  
ATOM    347  OG  SER D 510      36.250 -17.553  50.402  1.00 51.78           O  
ANISOU  347  OG  SER D 510     4309   6435   8931   -686   -476   3225       O  
ATOM    348  N   ILE D 511      37.108 -17.587  53.645  1.00 57.13           N  
ANISOU  348  N   ILE D 511     4998   7128   9579   -560   -461   3201       N  
ATOM    349  CA  ILE D 511      38.459 -17.598  54.202  1.00 50.34           C  
ANISOU  349  CA  ILE D 511     4087   6235   8804   -458   -366   3240       C  
ATOM    350  C   ILE D 511      38.646 -18.808  55.112  1.00 43.56           C  
ANISOU  350  C   ILE D 511     3146   5423   7980   -431   -418   3368       C  
ATOM    351  O   ILE D 511      39.739 -19.395  55.164  1.00 43.63           O  
ANISOU  351  O   ILE D 511     3067   5417   8094   -355   -355   3473       O  
ATOM    352  CB  ILE D 511      38.748 -16.261  54.917  1.00 43.43           C  
ANISOU  352  CB  ILE D 511     3304   5310   7887   -423   -296   3094       C  
ATOM    353  CG1 ILE D 511      38.847 -15.136  53.879  1.00 40.47           C  
ANISOU  353  CG1 ILE D 511     2992   4886   7496   -436   -224   2997       C  
ATOM    354  CG2 ILE D 511      40.011 -16.332  55.786  1.00 43.75           C  
ANISOU  354  CG2 ILE D 511     3300   5317   8006   -326   -208   3127       C  
ATOM    355  CD1 ILE D 511      39.612 -13.917  54.339  1.00 36.12           C  
ANISOU  355  CD1 ILE D 511     2508   4278   6936   -384   -117   2885       C  
ATOM    356  N   ASN D 512      37.580 -19.228  55.804  1.00 45.34           N  
ANISOU  356  N   ASN D 512     3399   5707   8121   -494   -530   3371       N  
ATOM    357  CA  ASN D 512      37.635 -20.474  56.562  1.00 52.79           C  
ANISOU  357  CA  ASN D 512     4263   6708   9086   -483   -592   3510       C  
ATOM    358  C   ASN D 512      37.897 -21.668  55.649  1.00 67.48           C  
ANISOU  358  C   ASN D 512     6019   8600  11020   -492   -610   3668       C  
ATOM    359  O   ASN D 512      38.712 -22.539  55.976  1.00 82.26           O  
ANISOU  359  O   ASN D 512     7794  10485  12976   -429   -591   3804       O  
ATOM    360  CB  ASN D 512      36.338 -20.663  57.349  1.00 47.52           C  
ANISOU  360  CB  ASN D 512     3656   6103   8296   -562   -708   3479       C  
ATOM    361  CG  ASN D 512      36.212 -19.687  58.502  1.00 38.22           C  
ANISOU  361  CG  ASN D 512     2560   4904   7056   -540   -694   3357       C  
ATOM    362  OD1 ASN D 512      37.164 -18.987  58.845  1.00 37.76           O  
ANISOU  362  OD1 ASN D 512     2505   4789   7054   -462   -600   3308       O  
ATOM    363  ND2 ASN D 512      35.029 -19.631  59.103  1.00 37.59           N  
ANISOU  363  ND2 ASN D 512     2550   4871   6860   -610   -783   3307       N  
ATOM    364  N   LYS D 513      37.249 -21.705  54.479  1.00 56.43           N  
ANISOU  364  N   LYS D 513     4635   7210   9596   -567   -642   3657       N  
ATOM    365  CA  LYS D 513      37.526 -22.774  53.518  1.00 51.95           C  
ANISOU  365  CA  LYS D 513     3967   6671   9100   -580   -654   3805       C  
ATOM    366  C   LYS D 513      38.935 -22.678  52.934  1.00 55.48           C  
ANISOU  366  C   LYS D 513     4343   7064   9673   -481   -533   3859       C  
ATOM    367  O   LYS D 513      39.563 -23.709  52.663  1.00 54.22           O  
ANISOU  367  O   LYS D 513     4076   6927   9597   -447   -525   4015       O  
ATOM    368  CB  LYS D 513      36.493 -22.761  52.392  1.00 45.81           C  
ANISOU  368  CB  LYS D 513     3225   5910   8271   -688   -712   3770       C  
ATOM    369  CG  LYS D 513      35.129 -23.294  52.791  1.00 46.93           C  
ANISOU  369  CG  LYS D 513     3409   6119   8305   -795   -834   3765       C  
ATOM    370  CD  LYS D 513      34.153 -23.221  51.630  1.00 49.35           C  
ANISOU  370  CD  LYS D 513     3751   6427   8573   -900   -878   3721       C  
ATOM    371  CE  LYS D 513      32.719 -23.384  52.102  1.00 54.48           C  
ANISOU  371  CE  LYS D 513     4475   7123   9102  -1007   -978   3662       C  
ATOM    372  NZ  LYS D 513      31.753 -23.271  50.976  1.00 56.55           N  
ANISOU  372  NZ  LYS D 513     4773   7377   9338  -1110  -1013   3609       N  
ATOM    373  N   VAL D 514      39.442 -21.458  52.736  1.00 52.49           N  
ANISOU  373  N   VAL D 514     4024   6614   9306   -437   -435   3737       N  
ATOM    374  CA  VAL D 514      40.790 -21.278  52.197  1.00 43.81           C  
ANISOU  374  CA  VAL D 514     2870   5459   8317   -346   -306   3776       C  
ATOM    375  C   VAL D 514      41.833 -21.798  53.177  1.00 44.23           C  
ANISOU  375  C   VAL D 514     2853   5501   8453   -245   -254   3863       C  
ATOM    376  O   VAL D 514      42.743 -22.548  52.803  1.00 51.76           O  
ANISOU  376  O   VAL D 514     3707   6449   9512   -184   -201   3996       O  
ATOM    377  CB  VAL D 514      41.033 -19.800  51.836  1.00 46.09           C  
ANISOU  377  CB  VAL D 514     3252   5680   8580   -331   -213   3619       C  
ATOM    378  CG1 VAL D 514      42.503 -19.549  51.552  1.00 43.27           C  
ANISOU  378  CG1 VAL D 514     2852   5262   8325   -230    -68   3648       C  
ATOM    379  CG2 VAL D 514      40.222 -19.419  50.610  1.00 46.51           C  
ANISOU  379  CG2 VAL D 514     3348   5739   8586   -416   -248   3570       C  
ATOM    380  N   LEU D 515      41.703 -21.441  54.454  1.00 43.26           N  
ANISOU  380  N   LEU D 515     2778   5373   8287   -228   -268   3796       N  
ATOM    381  CA  LEU D 515      42.633 -21.972  55.445  1.00 67.87           C  
ANISOU  381  CA  LEU D 515     5837   8477  11474   -145   -217   3867       C  
ATOM    382  C   LEU D 515      42.390 -23.450  55.735  1.00 74.32           C  
ANISOU  382  C   LEU D 515     6591   9368  12278   -185   -286   3991       C  
ATOM    383  O   LEU D 515      43.318 -24.140  56.172  1.00 57.83           O  
ANISOU  383  O   LEU D 515     4445   7272  10257   -128   -220   4063       O  
ATOM    384  CB  LEU D 515      42.570 -21.146  56.727  1.00 69.54           C  
ANISOU  384  CB  LEU D 515     6131   8662  11628   -131   -200   3738       C  
ATOM    385  CG  LEU D 515      43.272 -19.787  56.628  1.00 54.27           C  
ANISOU  385  CG  LEU D 515     4255   6644   9723    -73    -84   3618       C  
ATOM    386  CD1 LEU D 515      43.256 -19.079  57.966  1.00 51.19           C  
ANISOU  386  CD1 LEU D 515     3930   6233   9289    -55    -74   3515       C  
ATOM    387  CD2 LEU D 515      44.702 -19.945  56.125  1.00 52.43           C  
ANISOU  387  CD2 LEU D 515     3952   6350   9621     23     53   3688       C  
ATOM    388  N   ASP D 516      41.182 -23.958  55.467  1.00 83.90           N  
ANISOU  388  N   ASP D 516     7813  10654  13411   -283   -414   4022       N  
ATOM    389  CA  ASP D 516      40.954 -25.400  55.496  1.00 94.96           C  
ANISOU  389  CA  ASP D 516     9143  12132  14805   -328   -479   4159       C  
ATOM    390  C   ASP D 516      41.770 -26.103  54.416  1.00 98.19           C  
ANISOU  390  C   ASP D 516     9447  12535  15325   -289   -427   4296       C  
ATOM    391  O   ASP D 516      42.410 -27.129  54.672  1.00101.37           O  
ANISOU  391  O   ASP D 516     9774  12962  15778   -259   -399   4408       O  
ATOM    392  CB  ASP D 516      39.461 -25.689  55.323  1.00 96.76           C  
ANISOU  392  CB  ASP D 516     9408  12433  14922   -446   -621   4158       C  
ATOM    393  CG  ASP D 516      39.135 -27.174  55.365  1.00 97.25           C  
ANISOU  393  CG  ASP D 516     9401  12584  14967   -504   -694   4302       C  
ATOM    394  OD2 ASP D 516      37.967 -27.528  55.098  1.00 96.04           O  
ANISOU  394  OD2 ASP D 516     9267  12492  14732   -606   -806   4322       O  
ATOM    395  OD1 ASP D 516      40.035 -27.987  55.663  1.00 99.72           O1-
ANISOU  395  OD1 ASP D 516     9638  12904  15346   -451   -639   4399       O1-
ATOM    396  N   HIS D 517      41.755 -25.559  53.197  1.00102.48           N  
ANISOU  396  N   HIS D 517     9982  13047  15908   -288   -413   4294       N  
ATOM    397  CA  HIS D 517      42.566 -26.102  52.111  1.00 78.17           C  
ANISOU  397  CA  HIS D 517     6806   9959  12937   -246   -354   4420       C  
ATOM    398  C   HIS D 517      44.056 -25.886  52.358  1.00 52.15           C  
ANISOU  398  C   HIS D 517     3481   6593   9743   -127   -200   4423       C  
ATOM    399  O   HIS D 517      44.879 -26.631  51.815  1.00 50.98           O  
ANISOU  399  O   HIS D 517     3242   6444   9683    -82   -142   4547       O  
ATOM    400  CB  HIS D 517      42.117 -25.469  50.784  1.00 83.90           C  
ANISOU  400  CB  HIS D 517     7556  10668  13653   -295   -362   4375       C  
ATOM    401  CG  HIS D 517      42.842 -25.977  49.571  1.00 69.64           C  
ANISOU  401  CG  HIS D 517     5658   8857  11944   -267   -304   4494       C  
ATOM    402  ND1 HIS D 517      44.131 -25.607  49.252  1.00 63.05           N  
ANISOU  402  ND1 HIS D 517     4790   7958  11209   -161   -164   4509       N  
ATOM    403  CD2 HIS D 517      42.439 -26.815  48.586  1.00 65.62           C  
ANISOU  403  CD2 HIS D 517     5085   8402  11443   -335   -365   4602       C  
ATOM    404  CE1 HIS D 517      44.495 -26.202  48.130  1.00 62.92           C  
ANISOU  404  CE1 HIS D 517     4692   7958  11259   -161   -142   4626       C  
ATOM    405  NE2 HIS D 517      43.486 -26.940  47.706  1.00 64.89           N  
ANISOU  405  NE2 HIS D 517     4920   8280  11457   -266   -264   4686       N  
ATOM    406  N   PHE D 518      44.416 -24.888  53.170  1.00 57.36           N  
ANISOU  406  N   PHE D 518     4214   7191  10390    -77   -132   4292       N  
ATOM    407  CA  PHE D 518      45.817 -24.662  53.510  1.00 65.48           C  
ANISOU  407  CA  PHE D 518     5223   8145  11510     31     18   4288       C  
ATOM    408  C   PHE D 518      46.316 -25.651  54.563  1.00 70.36           C  
ANISOU  408  C   PHE D 518     5802   8785  12149     57     32   4355       C  
ATOM    409  O   PHE D 518      47.455 -26.124  54.481  1.00 64.69           O  
ANISOU  409  O   PHE D 518     5019   8032  11528    134    135   4435       O  
ATOM    410  CB  PHE D 518      46.018 -23.228  54.005  1.00 66.75           C  
ANISOU  410  CB  PHE D 518     5476   8233  11651     70     85   4127       C  
ATOM    411  CG  PHE D 518      46.467 -22.269  52.934  1.00 64.09           C  
ANISOU  411  CG  PHE D 518     5149   7836  11366    112    169   4092       C  
ATOM    412  CD1 PHE D 518      47.752 -22.332  52.426  1.00 63.98           C  
ANISOU  412  CD1 PHE D 518     5084   7765  11460    201    307   4151       C  
ATOM    413  CD2 PHE D 518      45.616 -21.280  52.469  1.00 62.58           C  
ANISOU  413  CD2 PHE D 518     5062   7648  11070     30    136   3947       C  
ATOM    414  CE1 PHE D 518      48.174 -21.445  51.450  1.00 62.30           C  
ANISOU  414  CE1 PHE D 518     4917   7505  11250    209    404   4078       C  
ATOM    415  CE2 PHE D 518      46.033 -20.388  51.496  1.00 61.62           C  
ANISOU  415  CE2 PHE D 518     4986   7478  10949     35    232   3871       C  
ATOM    416  CZ  PHE D 518      47.312 -20.471  50.985  1.00 62.12           C  
ANISOU  416  CZ  PHE D 518     4996   7490  11117    123    365   3936       C  
ATOM    417  N   ARG D 519      45.488 -25.962  55.565  1.00 68.80           N  
ANISOU  417  N   ARG D 519     5640   8641  11859     -3    -64   4326       N  
ATOM    418  CA  ARG D 519      45.888 -26.917  56.596  1.00 69.70           C  
ANISOU  418  CA  ARG D 519     5714   8782  11988     16    -58   4396       C  
ATOM    419  C   ARG D 519      45.780 -28.361  56.119  1.00 71.11           C  
ANISOU  419  C   ARG D 519     5795   9038  12188    -17   -114   4567       C  
ATOM    420  O   ARG D 519      46.599 -29.205  56.504  1.00 70.25           O  
ANISOU  420  O   ARG D 519     5618   8930  12146     33    -60   4666       O  
ATOM    421  CB  ARG D 519      45.045 -26.734  57.860  1.00 68.05           C  
ANISOU  421  CB  ARG D 519     5576   8608  11670    -36   -138   4309       C  
ATOM    422  CG  ARG D 519      45.247 -25.433  58.613  1.00 61.79           C  
ANISOU  422  CG  ARG D 519     4873   7745  10860      1    -80   4152       C  
ATOM    423  CD  ARG D 519      44.830 -25.633  60.065  1.00 55.17           C  
ANISOU  423  CD  ARG D 519     4072   6942   9950    -25   -131   4115       C  
ATOM    424  NE  ARG D 519      44.551 -24.384  60.764  1.00 54.81           N  
ANISOU  424  NE  ARG D 519     4122   6855   9848    -25   -123   3961       N  
ATOM    425  CZ  ARG D 519      45.434 -23.747  61.525  1.00 63.93           C  
ANISOU  425  CZ  ARG D 519     5298   7937  11054     45    -23   3897       C  
ATOM    426  NH1 ARG D 519      46.652 -24.248  61.686  1.00 67.07           N  
ANISOU  426  NH1 ARG D 519     5631   8290  11561    122     80   3971       N  
ATOM    427  NH2 ARG D 519      45.101 -22.616  62.130  1.00 65.85           N  
ANISOU  427  NH2 ARG D 519     5626   8152  11240     37    -25   3762       N  
ATOM    428  N   ARG D 520      44.776 -28.668  55.294  1.00 68.77           N  
ANISOU  428  N   ARG D 520     5488   8805  11835   -104   -221   4608       N  
ATOM    429  CA  ARG D 520      44.493 -30.055  54.936  1.00 74.01           C  
ANISOU  429  CA  ARG D 520     6065   9556  12501   -155   -293   4770       C  
ATOM    430  C   ARG D 520      45.558 -30.612  53.996  1.00 81.84           C  
ANISOU  430  C   ARG D 520     6954  10525  13614    -89   -207   4901       C  
ATOM    431  O   ARG D 520      46.240 -31.590  54.320  1.00 84.80           O  
ANISOU  431  O   ARG D 520     7254  10921  14046    -51   -171   5018       O  
ATOM    432  CB  ARG D 520      43.101 -30.148  54.304  1.00 75.84           C  
ANISOU  432  CB  ARG D 520     6320   9856  12638   -272   -430   4771       C  
ATOM    433  CG  ARG D 520      42.795 -31.471  53.619  1.00 82.48           C  
ANISOU  433  CG  ARG D 520     7066  10784  13488   -333   -503   4944       C  
ATOM    434  CD  ARG D 520      41.299 -31.630  53.385  1.00 88.23           C  
ANISOU  434  CD  ARG D 520     7834  11587  14103   -462   -649   4934       C  
ATOM    435  NE  ARG D 520      40.794 -32.915  53.863  1.00 94.69           N  
ANISOU  435  NE  ARG D 520     8604  12507  14864   -532   -733   5050       N  
ATOM    436  CZ  ARG D 520      39.513 -33.165  54.121  1.00 94.68           C  
ANISOU  436  CZ  ARG D 520     8648  12580  14745   -645   -853   5036       C  
ATOM    437  NH1 ARG D 520      38.602 -32.217  53.948  1.00 86.99           N  
ANISOU  437  NH1 ARG D 520     7768  11584  13700   -697   -904   4909       N  
ATOM    438  NH2 ARG D 520      39.145 -34.364  54.552  1.00 98.19           N  
ANISOU  438  NH2 ARG D 520     9043  13123  15143   -706   -919   5152       N  
ATOM    439  N   LYS D 521      45.717 -29.995  52.829  1.00 87.40           N  
ANISOU  439  N   LYS D 521     7655  11190  14363    -73   -171   4888       N  
ATOM    440  CA  LYS D 521      46.695 -30.427  51.837  1.00 85.56           C  
ANISOU  440  CA  LYS D 521     7329  10935  14243    -11    -85   5009       C  
ATOM    441  C   LYS D 521      47.902 -29.500  51.904  1.00 76.27           C  
ANISOU  441  C   LYS D 521     6179   9651  13148    102     73   4932       C  
ATOM    442  O   LYS D 521      47.770 -28.288  51.695  1.00 65.37           O  
ANISOU  442  O   LYS D 521     4874   8216  11749    111    102   4804       O  
ATOM    443  CB  LYS D 521      46.088 -30.426  50.435  1.00 89.14           C  
ANISOU  443  CB  LYS D 521     7751  11421  14696    -71   -148   5062       C  
ATOM    444  CG  LYS D 521      44.804 -31.234  50.310  1.00 91.06           C  
ANISOU  444  CG  LYS D 521     7979  11766  14853   -194   -308   5127       C  
ATOM    445  CD  LYS D 521      44.384 -31.374  48.856  1.00 90.27           C  
ANISOU  445  CD  LYS D 521     7829  11694  14777   -247   -360   5209       C  
ATOM    446  CE  LYS D 521      43.180 -32.292  48.714  1.00 89.78           C  
ANISOU  446  CE  LYS D 521     7742  11733  14635   -374   -514   5292       C  
ATOM    447  NZ  LYS D 521      43.341 -33.551  49.493  1.00 88.10           N  
ANISOU  447  NZ  LYS D 521     7471  11591  14412   -384   -538   5404       N  
ATOM    448  N   GLY D 522      49.067 -30.065  52.199  1.00 79.41           N  
ANISOU  448  N   GLY D 522     6518  10019  13636    186    178   5012       N  
ATOM    449  CA  GLY D 522      50.269 -29.268  52.329  1.00 77.93           C  
ANISOU  449  CA  GLY D 522     6357   9727  13527    292    336   4947       C  
ATOM    450  C   GLY D 522      50.269 -28.415  53.588  1.00 68.22           C  
ANISOU  450  C   GLY D 522     5223   8446  12252    309    361   4792       C  
ATOM    451  O   GLY D 522      49.405 -28.520  54.462  1.00 67.87           O  
ANISOU  451  O   GLY D 522     5220   8449  12120    245    260   4744       O  
ATOM    452  N   ILE D 523      51.291 -27.561  53.671  1.00 72.17           N  
ANISOU  452  N   ILE D 523     5758   8847  12815    396    504   4719       N  
ATOM    453  CA  ILE D 523      51.481 -26.647  54.789  1.00 71.75           C  
ANISOU  453  CA  ILE D 523     5793   8733  12737    422    551   4574       C  
ATOM    454  C   ILE D 523      51.814 -25.278  54.203  1.00 72.90           C  
ANISOU  454  C   ILE D 523     6004   8800  12894    459    641   4459       C  
ATOM    455  O   ILE D 523      52.368 -25.172  53.104  1.00 69.60           O  
ANISOU  455  O   ILE D 523     5552   8354  12538    499    716   4510       O  
ATOM    456  CB  ILE D 523      52.605 -27.093  55.776  1.00 65.90           C  
ANISOU  456  CB  ILE D 523     5026   7940  12071    500    655   4608       C  
ATOM    457  CG1 ILE D 523      52.601 -28.603  56.057  1.00 73.20           C  
ANISOU  457  CG1 ILE D 523     5859   8937  13018    486    600   4766       C  
ATOM    458  CG2 ILE D 523      52.459 -26.397  57.126  1.00 53.38           C  
ANISOU  458  CG2 ILE D 523     3522   6322  10436    497    654   4475       C  
ATOM    459  CD1 ILE D 523      53.499 -29.436  55.134  1.00 74.06           C  
ANISOU  459  CD1 ILE D 523     5869   9040  13232    543    678   4921       C  
ATOM    460  N   ASN D 524      51.449 -24.222  54.938  1.00 66.30           N  
ANISOU  460  N   ASN D 524     5262   7933  11996    444    633   4308       N  
ATOM    461  CA  ASN D 524      51.875 -22.842  54.702  1.00 69.03           C  
ANISOU  461  CA  ASN D 524     5682   8196  12351    486    734   4185       C  
ATOM    462  C   ASN D 524      51.751 -22.136  56.054  1.00 72.95           C  
ANISOU  462  C   ASN D 524     6259   8662  12797    482    734   4055       C  
ATOM    463  O   ASN D 524      50.944 -21.226  56.243  1.00 66.90           O  
ANISOU  463  O   ASN D 524     5565   7904  11950    435    674   3942       O  
ATOM    464  CB  ASN D 524      51.056 -22.151  53.608  1.00 58.89           C  
ANISOU  464  CB  ASN D 524     4422   6936  11016    436    674   4148       C  
ATOM    465  CG  ASN D 524      51.847 -21.083  52.860  1.00 55.73           C  
ANISOU  465  CG  ASN D 524     4056   6454  10666    500    811   4092       C  
ATOM    466  OD1 ASN D 524      52.717 -20.422  53.429  1.00 54.07           O  
ANISOU  466  OD1 ASN D 524     3893   6162  10487    564    934   4016       O  
ATOM    467  ND2 ASN D 524      51.537 -20.905  51.579  1.00 49.23           N  
ANISOU  467  ND2 ASN D 524     3223   5654   9829    468    796   4114       N  
ATOM    468  N   GLN D 525      52.594 -22.585  56.994  1.00 78.35           N  
ANISOU  468  N   GLN D 525     6924   9308  13537    534    806   4080       N  
ATOM    469  CA  GLN D 525      52.481 -22.206  58.401  1.00 82.33           C  
ANISOU  469  CA  GLN D 525     7484   9796  14002    526    794   3988       C  
ATOM    470  C   GLN D 525      52.707 -20.717  58.626  1.00 81.22           C  
ANISOU  470  C   GLN D 525     7437   9579  13844    548    872   3834       C  
ATOM    471  O   GLN D 525      52.135 -20.140  59.563  1.00 89.63           O  
ANISOU  471  O   GLN D 525     8562  10651  14840    513    818   3737       O  
ATOM    472  CB  GLN D 525      53.480 -23.014  59.231  1.00 82.64           C  
ANISOU  472  CB  GLN D 525     7473   9802  14125    586    872   4061       C  
ATOM    473  CG  GLN D 525      53.074 -23.217  60.679  1.00 80.33           C  
ANISOU  473  CG  GLN D 525     7199   9537  13786    556    805   4029       C  
ATOM    474  CD  GLN D 525      52.267 -24.481  60.890  1.00 79.37           C  
ANISOU  474  CD  GLN D 525     7016   9522  13620    496    669   4140       C  
ATOM    475  OE1 GLN D 525      51.049 -24.429  61.054  1.00 80.97           O  
ANISOU  475  OE1 GLN D 525     7250   9798  13716    415    535   4105       O  
ATOM    476  NE2 GLN D 525      52.944 -25.625  60.908  1.00 76.39           N  
ANISOU  476  NE2 GLN D 525     6553   9152  13321    535    705   4275       N  
ATOM    477  N   HIS D 526      53.542 -20.089  57.789  1.00 83.52           N  
ANISOU  477  N   HIS D 526     7742   9797  14195    607   1001   3815       N  
ATOM    478  CA  HIS D 526      53.801 -18.656  57.907  1.00 84.86           C  
ANISOU  478  CA  HIS D 526     8002   9893  14348    628   1085   3674       C  
ATOM    479  C   HIS D 526      52.521 -17.857  57.704  1.00 78.48           C  
ANISOU  479  C   HIS D 526     7249   9136  13433    553    967   3588       C  
ATOM    480  O   HIS D 526      52.305 -16.831  58.360  1.00 71.06           O  
ANISOU  480  O   HIS D 526     6392   8169  12440    538    974   3461       O  
ATOM    481  CB  HIS D 526      54.842 -18.220  56.876  1.00 92.50           C  
ANISOU  481  CB  HIS D 526     8972  10784  15389    697   1238   3683       C  
ATOM    482  CG  HIS D 526      55.759 -19.316  56.427  1.00107.68           C  
ANISOU  482  CG  HIS D 526    10812  12695  17409    753   1310   3821       C  
ATOM    483  ND1 HIS D 526      56.526 -20.060  57.296  1.00113.24           N  
ANISOU  483  ND1 HIS D 526    11480  13369  18176    794   1364   3872       N  
ATOM    484  CD2 HIS D 526      56.012 -19.803  55.189  1.00111.90           C  
ANISOU  484  CD2 HIS D 526    11285  13244  17989    774   1336   3926       C  
ATOM    485  CE1 HIS D 526      57.223 -20.951  56.611  1.00114.44           C  
ANISOU  485  CE1 HIS D 526    11557  13518  18408    840   1422   4001       C  
ATOM    486  NE2 HIS D 526      56.928 -20.817  55.332  1.00113.24           N  
ANISOU  486  NE2 HIS D 526    11387  13393  18245    828   1406   4037       N  
ATOM    487  N   VAL D 527      51.664 -18.320  56.796  1.00 83.69           N  
ANISOU  487  N   VAL D 527     7871   9871  14058    501    859   3653       N  
ATOM    488  CA  VAL D 527      50.369 -17.692  56.572  1.00 75.16           C  
ANISOU  488  CA  VAL D 527     6863   8849  12846    400    741   3557       C  
ATOM    489  C   VAL D 527      49.375 -18.131  57.641  1.00 66.77           C  
ANISOU  489  C   VAL D 527     5788   7850  11729    355    597   3568       C  
ATOM    490  O   VAL D 527      48.570 -17.324  58.125  1.00 66.14           O  
ANISOU  490  O   VAL D 527     5802   7790  11538    290    538   3440       O  
ATOM    491  CB  VAL D 527      49.884 -18.027  55.144  1.00 76.26           C  
ANISOU  491  CB  VAL D 527     6974   9038  12963    352    692   3615       C  
ATOM    492  CG1 VAL D 527      48.359 -18.019  55.033  1.00 71.29           C  
ANISOU  492  CG1 VAL D 527     6381   8492  12214    241    529   3575       C  
ATOM    493  CG2 VAL D 527      50.515 -17.087  54.133  1.00 78.53           C  
ANISOU  493  CG2 VAL D 527     7324   9271  13241    361    815   3539       C  
ATOM    494  N   GLN D 528      49.452 -19.404  58.050  1.00 67.13           N  
ANISOU  494  N   GLN D 528     5770   7940  11798    350    557   3673       N  
ATOM    495  CA  GLN D 528      48.472 -19.977  58.972  1.00 63.60           C  
ANISOU  495  CA  GLN D 528     5329   7569  11266    281    423   3677       C  
ATOM    496  C   GLN D 528      48.512 -19.300  60.336  1.00 59.72           C  
ANISOU  496  C   GLN D 528     4903   7049  10741    288    438   3572       C  
ATOM    497  O   GLN D 528      47.461 -18.994  60.913  1.00 52.90           O  
ANISOU  497  O   GLN D 528     4091   6234   9776    224    332   3508       O  
ATOM    498  CB  GLN D 528      48.719 -21.478  59.119  1.00 60.71           C  
ANISOU  498  CB  GLN D 528     4876   7250  10942    284    398   3820       C  
ATOM    499  CG  GLN D 528      48.418 -22.283  57.873  1.00 66.91           C  
ANISOU  499  CG  GLN D 528     5594   8086  11743    256    348   3934       C  
ATOM    500  CD  GLN D 528      48.963 -23.694  57.957  1.00 77.35           C  
ANISOU  500  CD  GLN D 528     6823   9438  13130    279    358   4084       C  
ATOM    501  OE1 GLN D 528      49.171 -24.356  56.939  1.00 79.19           O  
ANISOU  501  OE1 GLN D 528     6986   9691  13412    286    364   4193       O  
ATOM    502  NE2 GLN D 528      49.202 -24.162  59.175  1.00 81.95           N  
ANISOU  502  NE2 GLN D 528     7398  10025  13714    292    360   4095       N  
ATOM    503  N   ASN D 529      49.707 -19.043  60.865  1.00 64.84           N  
ANISOU  503  N   ASN D 529     5551   7616  11471    364    572   3554       N  
ATOM    504  CA  ASN D 529      49.799 -18.300  62.117  1.00 61.71           C  
ANISOU  504  CA  ASN D 529     5214   7183  11050    372    595   3452       C  
ATOM    505  C   ASN D 529      49.621 -16.799  61.931  1.00 65.34           C  
ANISOU  505  C   ASN D 529     5759   7598  11471    369    629   3318       C  
ATOM    506  O   ASN D 529      49.644 -16.062  62.923  1.00 68.48           O  
ANISOU  506  O   ASN D 529     6210   7966  11843    371    646   3229       O  
ATOM    507  CB  ASN D 529      51.136 -18.578  62.809  1.00 60.79           C  
ANISOU  507  CB  ASN D 529     5069   6992  11038    449    727   3482       C  
ATOM    508  CG  ASN D 529      51.447 -20.055  62.899  1.00 64.02           C  
ANISOU  508  CG  ASN D 529     5386   7438  11500    462    710   3625       C  
ATOM    509  OD1 ASN D 529      50.550 -20.895  62.831  1.00 67.99           O  
ANISOU  509  OD1 ASN D 529     5856   8032  11944    403    583   3693       O  
ATOM    510  ND2 ASN D 529      52.724 -20.382  63.064  1.00 60.79           N  
ANISOU  510  ND2 ASN D 529     4939   6958  11201    538    841   3673       N  
ATOM    511  N   GLY D 530      49.433 -16.331  60.696  1.00 65.08           N  
ANISOU  511  N   GLY D 530     5741   7562  11423    358    639   3301       N  
ATOM    512  CA  GLY D 530      49.323 -14.915  60.422  1.00 64.91           C  
ANISOU  512  CA  GLY D 530     5851   7507  11303    311    689   3130       C  
ATOM    513  C   GLY D 530      47.922 -14.359  60.329  1.00 60.99           C  
ANISOU  513  C   GLY D 530     5436   7078  10660    209    563   3038       C  
ATOM    514  O   GLY D 530      47.765 -13.147  60.171  1.00 53.14           O  
ANISOU  514  O   GLY D 530     4552   6060   9577    168    597   2898       O  
ATOM    515  N   TYR D 531      46.897 -15.200  60.416  1.00 63.05           N  
ANISOU  515  N   TYR D 531     5647   7421  10889    165    420   3114       N  
ATOM    516  CA  TYR D 531      45.511 -14.757  60.351  1.00 57.75           C  
ANISOU  516  CA  TYR D 531     5049   6811  10081     70    298   3032       C  
ATOM    517  C   TYR D 531      44.885 -14.915  61.729  1.00 51.83           C  
ANISOU  517  C   TYR D 531     4306   6101   9284     51    208   3024       C  
ATOM    518  O   TYR D 531      44.953 -15.994  62.326  1.00 51.24           O  
ANISOU  518  O   TYR D 531     4139   6058   9271     83    160   3148       O  
ATOM    519  CB  TYR D 531      44.730 -15.551  59.302  1.00 49.80           C  
ANISOU  519  CB  TYR D 531     3994   5868   9059     21    203   3119       C  
ATOM    520  CG  TYR D 531      43.242 -15.283  59.297  1.00 39.43           C  
ANISOU  520  CG  TYR D 531     2748   4619   7615    -75     72   3052       C  
ATOM    521  CD1 TYR D 531      42.732 -14.126  58.721  1.00 35.84           C  
ANISOU  521  CD1 TYR D 531     2398   4151   7069   -129     82   2918       C  
ATOM    522  CD2 TYR D 531      42.345 -16.187  59.853  1.00 37.33           C  
ANISOU  522  CD2 TYR D 531     2442   4426   7315   -112    -60   3128       C  
ATOM    523  CE1 TYR D 531      41.375 -13.871  58.704  1.00 35.02           C  
ANISOU  523  CE1 TYR D 531     2356   4098   6852   -213    -30   2857       C  
ATOM    524  CE2 TYR D 531      40.983 -15.943  59.841  1.00 36.08           C  
ANISOU  524  CE2 TYR D 531     2352   4322   7036   -200   -171   3065       C  
ATOM    525  CZ  TYR D 531      40.505 -14.782  59.265  1.00 35.14           C  
ANISOU  525  CZ  TYR D 531     2335   4182   6836   -247   -154   2928       C  
ATOM    526  OH  TYR D 531      39.152 -14.531  59.250  1.00 34.39           O  
ANISOU  526  OH  TYR D 531     2307   4133   6627   -330   -258   2866       O  
ATOM    527  N   HIS D 532      44.278 -13.840  62.232  1.00 47.82           N  
ANISOU  527  N   HIS D 532     3906   5595   8667      1    186   2883       N  
ATOM    528  CA  HIS D 532      43.796 -13.802  63.604  1.00 45.97           C  
ANISOU  528  CA  HIS D 532     3690   5390   8387    -12    119   2861       C  
ATOM    529  C   HIS D 532      42.296 -13.585  63.728  1.00 43.40           C  
ANISOU  529  C   HIS D 532     3428   5137   7926    -99    -15   2806       C  
ATOM    530  O   HIS D 532      41.778 -13.590  64.850  1.00 43.72           O  
ANISOU  530  O   HIS D 532     3484   5212   7917   -116    -82   2793       O  
ATOM    531  CB  HIS D 532      44.539 -12.711  64.385  1.00 47.78           C  
ANISOU  531  CB  HIS D 532     3990   5549   8615     15    224   2747       C  
ATOM    532  CG  HIS D 532      46.026 -12.790  64.248  1.00 52.23           C  
ANISOU  532  CG  HIS D 532     4510   6030   9305     98    371   2783       C  
ATOM    533  ND1 HIS D 532      46.761 -13.853  64.726  1.00 55.42           N  
ANISOU  533  ND1 HIS D 532     4801   6421   9835    171    397   2916       N  
ATOM    534  CD2 HIS D 532      46.915 -11.946  63.675  1.00 53.73           C  
ANISOU  534  CD2 HIS D 532     4756   6146   9513    121    504   2707       C  
ATOM    535  CE1 HIS D 532      48.040 -13.656  64.462  1.00 55.82           C  
ANISOU  535  CE1 HIS D 532     4840   6387   9981    238    544   2916       C  
ATOM    536  NE2 HIS D 532      48.160 -12.504  63.826  1.00 54.73           N  
ANISOU  536  NE2 HIS D 532     4807   6212   9776    207    611   2789       N  
ATOM    537  N   GLY D 533      41.587 -13.400  62.624  1.00 37.91           N  
ANISOU  537  N   GLY D 533     2768   4464   7171   -155    -54   2776       N  
ATOM    538  CA  GLY D 533      40.148 -13.241  62.665  1.00 35.79           C  
ANISOU  538  CA  GLY D 533     2559   4258   6780   -236   -175   2727       C  
ATOM    539  C   GLY D 533      39.719 -11.804  62.464  1.00 37.55           C  
ANISOU  539  C   GLY D 533     2904   4456   6906   -277   -150   2567       C  
ATOM    540  O   GLY D 533      40.512 -10.910  62.153  1.00 35.94           O  
ANISOU  540  O   GLY D 533     2745   4191   6722   -252    -40   2493       O  
ATOM    541  N   ILE D 534      38.420 -11.586  62.663  1.00 30.76           N  
ANISOU  541  N   ILE D 534     2103   3647   5936   -344   -252   2517       N  
ATOM    542  CA  ILE D 534      37.826 -10.269  62.473  1.00 29.63           C  
ANISOU  542  CA  ILE D 534     2075   3491   5694   -388   -244   2374       C  
ATOM    543  C   ILE D 534      38.109  -9.400  63.690  1.00 40.22           C  
ANISOU  543  C   ILE D 534     3474   4811   6997   -369   -208   2288       C  
ATOM    544  O   ILE D 534      38.540  -9.897  64.738  1.00 49.99           O  
ANISOU  544  O   ILE D 534     4663   6054   8276   -333   -210   2341       O  
ATOM    545  CB  ILE D 534      36.314 -10.373  62.203  1.00 29.21           C  
ANISOU  545  CB  ILE D 534     2063   3495   5542   -463   -361   2355       C  
ATOM    546  CG1 ILE D 534      35.572 -10.838  63.455  1.00 28.90           C  
ANISOU  546  CG1 ILE D 534     2023   3513   5443   -481   -456   2380       C  
ATOM    547  CG2 ILE D 534      36.048 -11.333  61.068  1.00 35.09           C  
ANISOU  547  CG2 ILE D 534     2745   4260   6327   -487   -400   2449       C  
ATOM    548  CD1 ILE D 534      34.071 -10.914  63.271  1.00 28.51           C  
ANISOU  548  CD1 ILE D 534     2026   3517   5289   -556   -563   2355       C  
ATOM    549  N   VAL D 535      37.879  -8.093  63.548  1.00 33.76           N  
ANISOU  549  N   VAL D 535     2756   3968   6102   -396   -173   2161       N  
ATOM    550  CA  VAL D 535      38.105  -7.164  64.651  1.00 27.07           C  
ANISOU  550  CA  VAL D 535     1974   3101   5209   -388   -139   2072       C  
ATOM    551  C   VAL D 535      37.120  -7.427  65.781  1.00 26.54           C  
ANISOU  551  C   VAL D 535     1916   3096   5073   -414   -247   2078       C  
ATOM    552  O   VAL D 535      37.489  -7.392  66.961  1.00 26.41           O  
ANISOU  552  O   VAL D 535     1892   3077   5067   -390   -237   2079       O  
ATOM    553  CB  VAL D 535      38.021  -5.713  64.135  1.00 26.26           C  
ANISOU  553  CB  VAL D 535     1979   2966   5033   -416    -83   1944       C  
ATOM    554  CG1 VAL D 535      38.019  -4.715  65.280  1.00 25.37           C  
ANISOU  554  CG1 VAL D 535     1943   2844   4852   -423    -68   1850       C  
ATOM    555  CG2 VAL D 535      39.179  -5.426  63.194  1.00 26.85           C  
ANISOU  555  CG2 VAL D 535     2048   2978   5175   -384     36   1944       C  
ATOM    556  N   MET D 536      35.870  -7.759  65.436  1.00 26.35           N  
ANISOU  556  N   MET D 536     1904   3127   4981   -465   -349   2090       N  
ATOM    557  CA  MET D 536      34.811  -7.936  66.428  1.00 25.83           C  
ANISOU  557  CA  MET D 536     1862   3123   4831   -497   -452   2089       C  
ATOM    558  C   MET D 536      35.098  -9.088  67.387  1.00 26.50           C  
ANISOU  558  C   MET D 536     1860   3242   4967   -468   -493   2205       C  
ATOM    559  O   MET D 536      34.631  -9.075  68.532  1.00 26.08           O  
ANISOU  559  O   MET D 536     1824   3228   4858   -477   -548   2202       O  
ATOM    560  CB  MET D 536      33.478  -8.166  65.714  1.00 25.71           C  
ANISOU  560  CB  MET D 536     1876   3151   4741   -558   -540   2086       C  
ATOM    561  CG  MET D 536      32.249  -8.127  66.605  1.00 34.66           C  
ANISOU  561  CG  MET D 536     3060   4344   5764   -600   -637   2064       C  
ATOM    562  SD  MET D 536      30.727  -8.100  65.647  1.00 38.18           S  
ANISOU  562  SD  MET D 536     3565   4819   6121   -674   -711   2031       S  
ATOM    563  CE  MET D 536      30.755  -9.748  64.945  1.00 54.87           C  
ANISOU  563  CE  MET D 536     5582   6962   8305   -688   -757   2176       C  
ATOM    564  N   ASN D 537      35.876 -10.077  66.955  1.00 27.57           N  
ANISOU  564  N   ASN D 537     1901   3365   5210   -431   -467   2313       N  
ATOM    565  CA  ASN D 537      36.175 -11.238  67.780  1.00 28.35           C  
ANISOU  565  CA  ASN D 537     1908   3498   5366   -400   -506   2440       C  
ATOM    566  C   ASN D 537      37.529 -11.154  68.472  1.00 29.52           C  
ANISOU  566  C   ASN D 537     2008   3590   5616   -329   -410   2459       C  
ATOM    567  O   ASN D 537      37.929 -12.117  69.133  1.00 35.29           O  
ANISOU  567  O   ASN D 537     2653   4340   6416   -293   -429   2573       O  
ATOM    568  CB  ASN D 537      36.109 -12.515  66.935  1.00 32.08           C  
ANISOU  568  CB  ASN D 537     2296   3999   5892   -404   -547   2568       C  
ATOM    569  CG  ASN D 537      34.705 -12.825  66.460  1.00 33.98           C  
ANISOU  569  CG  ASN D 537     2578   4301   6031   -482   -653   2569       C  
ATOM    570  OD1 ASN D 537      33.722 -12.417  67.079  1.00 39.09           O  
ANISOU  570  OD1 ASN D 537     3296   4986   6569   -525   -716   2510       O  
ATOM    571  ND2 ASN D 537      34.604 -13.561  65.360  1.00 37.73           N  
ANISOU  571  ND2 ASN D 537     3009   4784   6542   -501   -670   2638       N  
ATOM    572  N   ASN D 538      38.242 -10.036  68.344  1.00 28.26           N  
ANISOU  572  N   ASN D 538     1907   3361   5468   -311   -304   2353       N  
ATOM    573  CA  ASN D 538      39.548  -9.870  68.970  1.00 28.65           C  
ANISOU  573  CA  ASN D 538     1926   3347   5612   -250   -199   2359       C  
ATOM    574  C   ASN D 538      39.562  -8.799  70.052  1.00 38.25           C  
ANISOU  574  C   ASN D 538     3221   4545   6768   -260   -176   2254       C  
ATOM    575  O   ASN D 538      40.646  -8.395  70.489  1.00 49.86           O  
ANISOU  575  O   ASN D 538     4693   5950   8303   -221    -74   2230       O  
ATOM    576  CB  ASN D 538      40.607  -9.560  67.908  1.00 29.12           C  
ANISOU  576  CB  ASN D 538     1984   3333   5748   -216    -76   2339       C  
ATOM    577  CG  ASN D 538      40.958 -10.770  67.070  1.00 38.51           C  
ANISOU  577  CG  ASN D 538     3070   4529   7034   -184    -78   2469       C  
ATOM    578  OD1 ASN D 538      40.612 -11.899  67.418  1.00 50.26           O  
ANISOU  578  OD1 ASN D 538     4477   6070   8548   -178   -160   2586       O  
ATOM    579  ND2 ASN D 538      41.639 -10.540  65.953  1.00 44.33           N  
ANISOU  579  ND2 ASN D 538     3808   5216   7819   -165     11   2457       N  
ATOM    580  N   PHE D 539      38.397  -8.325  70.496  1.00 39.85           N  
ANISOU  580  N   PHE D 539     3490   4802   6849   -314   -264   2195       N  
ATOM    581  CA  PHE D 539      38.337  -7.444  71.653  1.00 31.32           C  
ANISOU  581  CA  PHE D 539     2472   3716   5713   -324   -257   2116       C  
ATOM    582  C   PHE D 539      36.982  -7.612  72.324  1.00 35.24           C  
ANISOU  582  C   PHE D 539     2990   4297   6101   -369   -387   2123       C  
ATOM    583  O   PHE D 539      36.074  -8.257  71.795  1.00 40.93           O  
ANISOU  583  O   PHE D 539     3697   5074   6780   -399   -472   2171       O  
ATOM    584  CB  PHE D 539      38.604  -5.970  71.272  1.00 27.84           C  
ANISOU  584  CB  PHE D 539     2140   3221   5219   -344   -173   1973       C  
ATOM    585  CG  PHE D 539      37.443  -5.267  70.596  1.00 24.44           C  
ANISOU  585  CG  PHE D 539     1792   2825   4670   -400   -229   1892       C  
ATOM    586  CD2 PHE D 539      36.492  -4.564  71.331  1.00 24.60           C  
ANISOU  586  CD2 PHE D 539     1882   2886   4578   -439   -292   1824       C  
ATOM    587  CD1 PHE D 539      37.297  -5.325  69.225  1.00 24.61           C  
ANISOU  587  CD1 PHE D 539     1817   2838   4697   -412   -217   1890       C  
ATOM    588  CE2 PHE D 539      35.436  -3.926  70.702  1.00 22.76           C  
ANISOU  588  CE2 PHE D 539     1721   2681   4245   -484   -338   1754       C  
ATOM    589  CE1 PHE D 539      36.245  -4.692  68.590  1.00 26.53           C  
ANISOU  589  CE1 PHE D 539     2131   3108   4842   -461   -264   1821       C  
ATOM    590  CZ  PHE D 539      35.313  -3.993  69.330  1.00 22.97           C  
ANISOU  590  CZ  PHE D 539     1749   2693   4284   -495   -323   1752       C  
ATOM    591  N   GLU D 540      36.861  -7.015  73.505  1.00 24.97           N  
ANISOU  591  N   GLU D 540     1729   3006   4754   -377   -397   2078       N  
ATOM    592  CA  GLU D 540      35.579  -6.868  74.174  1.00 27.35           C  
ANISOU  592  CA  GLU D 540     2075   3382   4936   -421   -505   2060       C  
ATOM    593  C   GLU D 540      35.650  -5.632  75.054  1.00 37.74           C  
ANISOU  593  C   GLU D 540     3468   4677   6194   -432   -471   1956       C  
ATOM    594  O   GLU D 540      36.733  -5.210  75.469  1.00 30.31           O  
ANISOU  594  O   GLU D 540     2526   3673   5320   -403   -379   1930       O  
ATOM    595  CB  GLU D 540      35.206  -8.103  75.002  1.00 40.49           C  
ANISOU  595  CB  GLU D 540     3668   5113   6603   -419   -590   2179       C  
ATOM    596  CG  GLU D 540      36.390  -8.850  75.582  1.00 61.07           C  
ANISOU  596  CG  GLU D 540     6184   7685   9334   -366   -531   2264       C  
ATOM    597  CD  GLU D 540      35.980 -10.134  76.280  1.00 77.08           C  
ANISOU  597  CD  GLU D 540     8188   9776  11323   -392   -575   2330       C  
ATOM    598  OE1 GLU D 540      35.062 -10.085  77.124  1.00 79.23           O  
ANISOU  598  OE1 GLU D 540     8517  10107  11479   -436   -630   2293       O  
ATOM    599  OE2 GLU D 540      36.580 -11.189  75.984  1.00 83.19           O  
ANISOU  599  OE2 GLU D 540     8886  10542  12181   -366   -550   2421       O  
ATOM    600  N   CYS D 541      34.486  -5.049  75.320  1.00 42.09           N  
ANISOU  600  N   CYS D 541     4092   5280   6620   -476   -543   1897       N  
ATOM    601  CA  CYS D 541      34.389  -3.844  76.126  1.00 21.78           C  
ANISOU  601  CA  CYS D 541     1597   2698   3979   -492   -524   1800       C  
ATOM    602  C   CYS D 541      33.119  -3.914  76.958  1.00 24.29           C  
ANISOU  602  C   CYS D 541     1941   3103   4187   -524   -636   1814       C  
ATOM    603  O   CYS D 541      32.294  -4.816  76.797  1.00 21.50           O  
ANISOU  603  O   CYS D 541     1569   2807   3793   -544   -710   1872       O  
ATOM    604  CB  CYS D 541      34.397  -2.585  75.255  1.00 21.09           C  
ANISOU  604  CB  CYS D 541     1603   2567   3845   -513   -460   1676       C  
ATOM    605  SG  CYS D 541      32.941  -2.422  74.203  1.00 43.96           S  
ANISOU  605  SG  CYS D 541     4553   5513   6637   -556   -536   1641       S  
ATOM    606  N   GLU D 542      32.971  -2.942  77.851  1.00 27.23           N  
ANISOU  606  N   GLU D 542     2372   3478   4496   -537   -632   1745       N  
ATOM    607  CA  GLU D 542      31.818  -2.914  78.737  1.00 37.56           C  
ANISOU  607  CA  GLU D 542     3717   4864   5690   -567   -721   1746       C  
ATOM    608  C   GLU D 542      30.558  -2.567  77.943  1.00 37.87           C  
ANISOU  608  C   GLU D 542     3840   4935   5615   -608   -753   1674       C  
ATOM    609  O   GLU D 542      30.625  -1.779  76.993  1.00 39.76           O  
ANISOU  609  O   GLU D 542     4112   5140   5857   -609   -730   1622       O  
ATOM    610  CB  GLU D 542      32.047  -1.906  79.864  1.00 52.67           C  
ANISOU  610  CB  GLU D 542     5666   6771   7575   -568   -707   1697       C  
ATOM    611  CG  GLU D 542      31.806  -2.470  81.261  1.00 69.97           C  
ANISOU  611  CG  GLU D 542     7848   9005   9732   -577   -728   1725       C  
ATOM    612  CD  GLU D 542      32.633  -3.715  81.554  1.00 83.71           C  
ANISOU  612  CD  GLU D 542     9490  10733  11585   -546   -710   1831       C  
ATOM    613  OE1 GLU D 542      33.817  -3.766  81.159  1.00 89.72           O  
ANISOU  613  OE1 GLU D 542    10176  11431  12483   -502   -665   1886       O  
ATOM    614  OE2 GLU D 542      32.089  -4.650  82.180  1.00 88.32           O  
ANISOU  614  OE2 GLU D 542    10069  11367  12121   -565   -733   1860       O  
ATOM    615  N   PRO D 543      29.407  -3.155  78.293  1.00 37.40           N  
ANISOU  615  N   PRO D 543     3826   4931   5455   -643   -783   1654       N  
ATOM    616  CA  PRO D 543      28.208  -3.004  77.448  1.00 37.15           C  
ANISOU  616  CA  PRO D 543     3860   4919   5334   -678   -806   1600       C  
ATOM    617  C   PRO D 543      27.683  -1.585  77.337  1.00 34.29           C  
ANISOU  617  C   PRO D 543     3582   4550   4896   -689   -801   1503       C  
ATOM    618  O   PRO D 543      27.040  -1.262  76.328  1.00 43.52           O  
ANISOU  618  O   PRO D 543     4790   5713   6031   -706   -812   1469       O  
ATOM    619  CB  PRO D 543      27.182  -3.924  78.127  1.00 43.39           C  
ANISOU  619  CB  PRO D 543     4673   5769   6045   -710   -828   1607       C  
ATOM    620  CG  PRO D 543      28.004  -4.917  78.873  1.00 48.14           C  
ANISOU  620  CG  PRO D 543     5195   6378   6718   -690   -824   1694       C  
ATOM    621  CD  PRO D 543      29.207  -4.163  79.348  1.00 47.95           C  
ANISOU  621  CD  PRO D 543     5138   6310   6773   -651   -794   1698       C  
ATOM    622  N   ALA D 544      27.963  -0.718  78.315  1.00 32.01           N  
ANISOU  622  N   ALA D 544     3319   4260   4582   -680   -786   1462       N  
ATOM    623  CA  ALA D 544      27.559   0.682  78.220  1.00 41.98           C  
ANISOU  623  CA  ALA D 544     4659   5517   5776   -688   -779   1374       C  
ATOM    624  C   ALA D 544      28.240   1.404  77.064  1.00 41.29           C  
ANISOU  624  C   ALA D 544     4556   5384   5747   -677   -772   1377       C  
ATOM    625  O   ALA D 544      27.759   2.459  76.637  1.00 44.36           O  
ANISOU  625  O   ALA D 544     5016   5766   6073   -690   -758   1297       O  
ATOM    626  CB  ALA D 544      27.856   1.406  79.534  1.00 50.00           C  
ANISOU  626  CB  ALA D 544     5695   6541   6763   -682   -766   1344       C  
ATOM    627  N   PHE D 545      29.337   0.861  76.545  1.00 32.95           N  
ANISOU  627  N   PHE D 545     3439   4275   4804   -655   -714   1407       N  
ATOM    628  CA  PHE D 545      30.008   1.414  75.380  1.00 32.07           C  
ANISOU  628  CA  PHE D 545     3345   4096   4743   -649   -629   1350       C  
ATOM    629  C   PHE D 545      29.573   0.765  74.068  1.00 40.82           C  
ANISOU  629  C   PHE D 545     4435   5202   5872   -657   -646   1378       C  
ATOM    630  O   PHE D 545      29.995   1.245  73.009  1.00 45.35           O  
ANISOU  630  O   PHE D 545     5026   5726   6478   -656   -583   1334       O  
ATOM    631  CB  PHE D 545      31.530   1.282  75.531  1.00 25.17           C  
ANISOU  631  CB  PHE D 545     2427   3158   3978   -621   -538   1364       C  
ATOM    632  CG  PHE D 545      32.081   1.922  76.777  1.00 27.68           C  
ANISOU  632  CG  PHE D 545     2765   3464   4288   -617   -509   1335       C  
ATOM    633  CD2 PHE D 545      32.250   1.186  77.942  1.00 38.00           C  
ANISOU  633  CD2 PHE D 545     4015   4799   5626   -604   -547   1409       C  
ATOM    634  CD1 PHE D 545      32.423   3.264  76.784  1.00 28.65           C  
ANISOU  634  CD1 PHE D 545     2963   3549   4373   -630   -444   1239       C  
ATOM    635  CE2 PHE D 545      32.758   1.779  79.087  1.00 45.18           C  
ANISOU  635  CE2 PHE D 545     4940   5693   6532   -604   -519   1384       C  
ATOM    636  CE1 PHE D 545      32.930   3.862  77.923  1.00 34.76           C  
ANISOU  636  CE1 PHE D 545     3759   4310   5139   -633   -415   1212       C  
ATOM    637  CZ  PHE D 545      33.096   3.119  79.076  1.00 41.84           C  
ANISOU  637  CZ  PHE D 545     4597   5230   6071   -620   -452   1284       C  
ATOM    638  N   TYR D 546      28.720  -0.276  74.119  1.00 41.97           N  
ANISOU  638  N   TYR D 546     4551   5402   5994   -671   -729   1452       N  
ATOM    639  CA  TYR D 546      28.455  -1.120  72.947  1.00 39.33           C  
ANISOU  639  CA  TYR D 546     4184   5062   5697   -681   -745   1497       C  
ATOM    640  C   TYR D 546      27.935  -0.323  71.755  1.00 44.03           C  
ANISOU  640  C   TYR D 546     4838   5631   6261   -700   -722   1422       C  
ATOM    641  O   TYR D 546      28.235  -0.656  70.603  1.00 51.05           O  
ANISOU  641  O   TYR D 546     5699   6485   7211   -700   -692   1437       O  
ATOM    642  CB  TYR D 546      27.454  -2.230  73.277  1.00 35.01           C  
ANISOU  642  CB  TYR D 546     3620   4581   5102   -707   -834   1574       C  
ATOM    643  CG  TYR D 546      28.046  -3.465  73.909  1.00 31.03           C  
ANISOU  643  CG  TYR D 546     3044   4091   4656   -692   -830   1654       C  
ATOM    644  CD1 TYR D 546      29.421  -3.652  73.965  1.00 34.19           C  
ANISOU  644  CD1 TYR D 546     3360   4452   5177   -646   -796   1716       C  
ATOM    645  CD2 TYR D 546      27.225  -4.482  74.384  1.00 34.50           C  
ANISOU  645  CD2 TYR D 546     3493   4580   5038   -724   -856   1676       C  
ATOM    646  CE1 TYR D 546      29.964  -4.792  74.528  1.00 48.97           C  
ANISOU  646  CE1 TYR D 546     5164   6335   7107   -630   -789   1794       C  
ATOM    647  CE2 TYR D 546      27.758  -5.628  74.947  1.00 44.51           C  
ANISOU  647  CE2 TYR D 546     4692   5865   6356   -712   -855   1756       C  
ATOM    648  CZ  TYR D 546      29.129  -5.778  75.015  1.00 51.00           C  
ANISOU  648  CZ  TYR D 546     5434   6647   7297   -664   -822   1814       C  
ATOM    649  OH  TYR D 546      29.670  -6.916  75.571  1.00 48.95           O  
ANISOU  649  OH  TYR D 546     5104   6402   7092   -650   -817   1898       O  
ATOM    650  N   THR D 547      27.157   0.727  72.010  1.00 35.45           N  
ANISOU  650  N   THR D 547     3829   4560   5082   -716   -736   1349       N  
ATOM    651  CA  THR D 547      26.727   1.592  70.919  1.00 28.18           C  
ANISOU  651  CA  THR D 547     2961   3609   4137   -730   -709   1280       C  
ATOM    652  C   THR D 547      27.897   2.405  70.380  1.00 22.26           C  
ANISOU  652  C   THR D 547     2215   2798   3444   -710   -613   1230       C  
ATOM    653  O   THR D 547      28.240   2.312  69.194  1.00 22.86           O  
ANISOU  653  O   THR D 547     2277   2835   3576   -711   -572   1232       O  
ATOM    654  CB  THR D 547      25.595   2.508  71.389  1.00 23.95           C  
ANISOU  654  CB  THR D 547     2504   3108   3489   -748   -746   1222       C  
ATOM    655  OG1 THR D 547      24.511   1.713  71.885  1.00 31.47           O  
ANISOU  655  OG1 THR D 547     3461   4114   4381   -771   -823   1272       O  
ATOM    656  CG2 THR D 547      25.098   3.377  70.244  1.00 15.94           C  
ANISOU  656  CG2 THR D 547     1538   2062   2456   -760   -722   1160       C  
ATOM    657  N   CYS D 548      28.564   3.164  71.257  1.00 18.92           N  
ANISOU  657  N   CYS D 548     1815   2365   3008   -696   -572   1189       N  
ATOM    658  CA  CYS D 548      29.505   4.182  70.801  1.00 16.85           C  
ANISOU  658  CA  CYS D 548     1587   2047   2770   -689   -477   1126       C  
ATOM    659  C   CYS D 548      30.770   3.588  70.199  1.00 28.52           C  
ANISOU  659  C   CYS D 548     3011   3471   4352   -671   -402   1164       C  
ATOM    660  O   CYS D 548      31.446   4.268  69.422  1.00 29.63           O  
ANISOU  660  O   CYS D 548     3182   3563   4514   -671   -322   1122       O  
ATOM    661  CB  CYS D 548      29.869   5.122  71.950  1.00 24.87           C  
ANISOU  661  CB  CYS D 548     2645   3064   3740   -687   -453   1075       C  
ATOM    662  SG  CYS D 548      30.832   4.356  73.257  1.00 48.74           S  
ANISOU  662  SG  CYS D 548     5611   6084   6825   -666   -441   1130       S  
ATOM    663  N   VAL D 549      31.100   2.339  70.529  1.00 31.57           N  
ANISOU  663  N   VAL D 549     3323   3868   4805   -654   -426   1246       N  
ATOM    664  CA  VAL D 549      32.173   1.652  69.821  1.00 27.53           C  
ANISOU  664  CA  VAL D 549     2753   3311   4397   -633   -362   1296       C  
ATOM    665  C   VAL D 549      31.718   1.260  68.421  1.00 28.65           C  
ANISOU  665  C   VAL D 549     2878   3448   4558   -646   -377   1319       C  
ATOM    666  O   VAL D 549      32.405   1.545  67.429  1.00 27.90           O  
ANISOU  666  O   VAL D 549     2788   3307   4506   -641   -303   1305       O  
ATOM    667  CB  VAL D 549      32.650   0.428  70.624  1.00 19.32           C  
ANISOU  667  CB  VAL D 549     1630   2285   3426   -608   -386   1387       C  
ATOM    668  CG1 VAL D 549      33.788  -0.264  69.903  1.00 20.22           C  
ANISOU  668  CG1 VAL D 549     1680   2350   3651   -579   -315   1443       C  
ATOM    669  CG2 VAL D 549      33.100   0.853  72.011  1.00 19.06           C  
ANISOU  669  CG2 VAL D 549     1612   2250   3378   -598   -369   1365       C  
ATOM    670  N   GLU D 550      30.528   0.648  68.324  1.00 21.32           N  
ANISOU  670  N   GLU D 550     1938   2569   3592   -666   -471   1352       N  
ATOM    671  CA  GLU D 550      30.080   0.021  67.079  1.00 19.49           C  
ANISOU  671  CA  GLU D 550     1680   2335   3391   -682   -494   1392       C  
ATOM    672  C   GLU D 550      29.972   1.036  65.952  1.00 19.26           C  
ANISOU  672  C   GLU D 550     1704   2270   3345   -696   -446   1325       C  
ATOM    673  O   GLU D 550      30.628   0.901  64.911  1.00 24.49           O  
ANISOU  673  O   GLU D 550     2341   2894   4071   -690   -391   1345       O  
ATOM    674  CB  GLU D 550      28.736  -0.673  67.295  1.00 23.77           C  
ANISOU  674  CB  GLU D 550     2221   2934   3878   -712   -599   1427       C  
ATOM    675  CG  GLU D 550      28.288  -1.518  66.114  1.00 43.99           C  
ANISOU  675  CG  GLU D 550     4746   5491   6476   -735   -628   1480       C  
ATOM    676  CD  GLU D 550      27.078  -2.375  66.430  1.00 61.17           C  
ANISOU  676  CD  GLU D 550     6922   7721   8601   -770   -723   1524       C  
ATOM    677  OE1 GLU D 550      26.227  -2.552  65.533  1.00 64.55           O  
ANISOU  677  OE1 GLU D 550     7365   8146   9014   -806   -752   1523       O  
ATOM    678  OE2 GLU D 550      26.975  -2.869  67.574  1.00 62.35           O  
ANISOU  678  OE2 GLU D 550     7057   7914   8721   -765   -766   1562       O  
ATOM    679  N   VAL D 551      29.195   2.100  66.172  1.00 18.48           N  
ANISOU  679  N   VAL D 551     1679   2184   3160   -714   -463   1251       N  
ATOM    680  CA  VAL D 551      29.033   3.150  65.173  1.00 26.10           C  
ANISOU  680  CA  VAL D 551     2697   3118   4103   -727   -422   1192       C  
ATOM    681  C   VAL D 551      30.307   3.942  64.924  1.00 21.43           C  
ANISOU  681  C   VAL D 551     2127   2477   3539   -711   -316   1155       C  
ATOM    682  O   VAL D 551      30.357   4.720  63.965  1.00 18.63           O  
ANISOU  682  O   VAL D 551     1808   2094   3177   -721   -272   1120       O  
ATOM    683  CB  VAL D 551      27.882   4.084  65.597  1.00 25.92           C  
ANISOU  683  CB  VAL D 551     2744   3123   3981   -744   -468   1129       C  
ATOM    684  CG1 VAL D 551      26.596   3.297  65.683  1.00 46.24           C  
ANISOU  684  CG1 VAL D 551     5308   5738   6525   -766   -561   1164       C  
ATOM    685  CG2 VAL D 551      28.182   4.712  66.933  1.00 16.83           C  
ANISOU  685  CG2 VAL D 551     1624   1990   2780   -731   -460   1091       C  
ATOM    686  N   THR D 552      31.343   3.765  65.749  1.00 22.03           N  
ANISOU  686  N   THR D 552     2184   2540   3646   -688   -272   1166       N  
ATOM    687  CA  THR D 552      32.635   4.353  65.420  1.00 18.67           C  
ANISOU  687  CA  THR D 552     1780   2061   3253   -677   -164   1140       C  
ATOM    688  C   THR D 552      33.351   3.541  64.348  1.00 19.58           C  
ANISOU  688  C   THR D 552     1835   2145   3458   -664   -121   1204       C  
ATOM    689  O   THR D 552      34.017   4.111  63.475  1.00 22.03           O  
ANISOU  689  O   THR D 552     2174   2416   3782   -666    -44   1184       O  
ATOM    690  CB  THR D 552      33.502   4.463  66.672  1.00 18.58           C  
ANISOU  690  CB  THR D 552     1774   2038   3247   -661   -125   1127       C  
ATOM    691  OG1 THR D 552      32.742   5.067  67.724  1.00 19.45           O  
ANISOU  691  OG1 THR D 552     1926   2186   3276   -672   -178   1082       O  
ATOM    692  CG2 THR D 552      34.732   5.307  66.402  1.00 18.75           C  
ANISOU  692  CG2 THR D 552     1845   2003   3276   -661    -11   1083       C  
ATOM    693  N   ALA D 553      33.207   2.219  64.378  1.00 20.12           N  
ANISOU  693  N   ALA D 553     1824   2234   3586   -652   -172   1285       N  
ATOM    694  CA  ALA D 553      33.962   1.354  63.482  1.00 21.06           C  
ANISOU  694  CA  ALA D 553     1874   2327   3799   -633   -133   1358       C  
ATOM    695  C   ALA D 553      33.144   0.847  62.305  1.00 21.43           C  
ANISOU  695  C   ALA D 553     1893   2388   3861   -655   -184   1397       C  
ATOM    696  O   ALA D 553      33.671   0.759  61.193  1.00 22.03           O  
ANISOU  696  O   ALA D 553     1949   2434   3989   -651   -133   1424       O  
ATOM    697  CB  ALA D 553      34.534   0.165  64.257  1.00 27.13           C  
ANISOU  697  CB  ALA D 553     2564   3105   4641   -601   -145   1437       C  
ATOM    698  N   GLY D 554      31.878   0.500  62.524  1.00 21.15           N  
ANISOU  698  N   GLY D 554     1858   2396   3781   -680   -282   1404       N  
ATOM    699  CA  GLY D 554      31.020   0.068  61.429  1.00 23.97           C  
ANISOU  699  CA  GLY D 554     2198   2760   4148   -709   -331   1435       C  
ATOM    700  C   GLY D 554      31.513  -1.221  60.801  1.00 32.32           C  
ANISOU  700  C   GLY D 554     3166   3815   5300   -699   -332   1534       C  
ATOM    701  O   GLY D 554      31.710  -2.238  61.478  1.00 43.76           O  
ANISOU  701  O   GLY D 554     4556   5288   6783   -683   -366   1600       O  
ATOM    702  N   ASN D 555      31.756  -1.169  59.489  1.00 36.88           N  
ANISOU  702  N   ASN D 555     3730   4362   5921   -706   -293   1553       N  
ATOM    703  CA  ASN D 555      32.290  -2.323  58.777  1.00 42.25           C  
ANISOU  703  CA  ASN D 555     4322   5036   6694   -695   -286   1651       C  
ATOM    704  C   ASN D 555      33.737  -2.633  59.145  1.00 37.55           C  
ANISOU  704  C   ASN D 555     3680   4418   6169   -644   -207   1691       C  
ATOM    705  O   ASN D 555      34.200  -3.742  58.855  1.00 39.44           O  
ANISOU  705  O   ASN D 555     3836   4661   6489   -625   -209   1785       O  
ATOM    706  CB  ASN D 555      32.159  -2.115  57.268  1.00 49.40           C  
ANISOU  706  CB  ASN D 555     5227   5916   7627   -717   -263   1662       C  
ATOM    707  CG  ASN D 555      30.714  -2.087  56.811  1.00 50.04           C  
ANISOU  707  CG  ASN D 555     5338   6014   7662   -769   -345   1643       C  
ATOM    708  OD1 ASN D 555      30.113  -3.130  56.549  1.00 47.08           O  
ANISOU  708  OD1 ASN D 555     4916   5659   7312   -795   -413   1706       O  
ATOM    709  ND2 ASN D 555      30.145  -0.890  56.720  1.00 54.45           N  
ANISOU  709  ND2 ASN D 555     5975   6560   8153   -786   -338   1558       N  
ATOM    710  N   ARG D 556      34.450  -1.708  59.805  1.00 40.00           N  
ANISOU  710  N   ARG D 556     4042   4703   6452   -621   -137   1625       N  
ATOM    711  CA  ARG D 556      35.736  -2.063  60.394  1.00 24.47           C  
ANISOU  711  CA  ARG D 556     2034   2712   4550   -573    -68   1659       C  
ATOM    712  C   ARG D 556      35.606  -3.106  61.498  1.00 24.60           C  
ANISOU  712  C   ARG D 556     1990   2765   4592   -556   -131   1720       C  
ATOM    713  O   ARG D 556      36.616  -3.705  61.881  1.00 25.18           O  
ANISOU  713  O   ARG D 556     2006   2820   4743   -512    -83   1777       O  
ATOM    714  CB  ARG D 556      36.457  -0.835  60.953  1.00 23.88           C  
ANISOU  714  CB  ARG D 556     2038   2603   4432   -562     16   1571       C  
ATOM    715  CG  ARG D 556      37.157   0.073  59.947  1.00 24.05           C  
ANISOU  715  CG  ARG D 556     2106   2580   4451   -564    112   1533       C  
ATOM    716  CD  ARG D 556      36.262   1.178  59.445  1.00 23.37           C  
ANISOU  716  CD  ARG D 556     2101   2502   4275   -608     89   1457       C  
ATOM    717  NE  ARG D 556      36.979   2.442  59.346  1.00 48.87           N  
ANISOU  717  NE  ARG D 556     5413   5697   7459   -612    178   1386       N  
ATOM    718  CZ  ARG D 556      37.068   3.311  60.347  1.00 41.68           C  
ANISOU  718  CZ  ARG D 556     4572   4783   6480   -620    193   1311       C  
ATOM    719  NH1 ARG D 556      36.493   3.039  61.511  1.00 21.84           N  
ANISOU  719  NH1 ARG D 556     2053   2302   3943   -619    127   1300       N  
ATOM    720  NH2 ARG D 556      37.735   4.446  60.194  1.00 52.27           N  
ANISOU  720  NH2 ARG D 556     5990   6094   7776   -631    272   1251       N  
ATOM    721  N   LEU D 557      34.392  -3.328  62.023  1.00 24.13           N  
ANISOU  721  N   LEU D 557     1945   2754   4470   -588   -234   1714       N  
ATOM    722  CA  LEU D 557      34.142  -4.482  62.885  1.00 24.43           C  
ANISOU  722  CA  LEU D 557     1918   2835   4529   -580   -307   1792       C  
ATOM    723  C   LEU D 557      34.491  -5.797  62.204  1.00 35.47           C  
ANISOU  723  C   LEU D 557     3218   4238   6020   -566   -319   1910       C  
ATOM    724  O   LEU D 557      34.853  -6.765  62.880  1.00 46.51           O  
ANISOU  724  O   LEU D 557     4546   5656   7468   -539   -341   1994       O  
ATOM    725  CB  LEU D 557      32.678  -4.516  63.317  1.00 23.85           C  
ANISOU  725  CB  LEU D 557     1885   2816   4363   -626   -415   1770       C  
ATOM    726  CG  LEU D 557      32.261  -3.978  64.682  1.00 22.99           C  
ANISOU  726  CG  LEU D 557     1826   2733   4176   -628   -448   1715       C  
ATOM    727  CD1 LEU D 557      32.965  -2.687  65.012  1.00 22.37           C  
ANISOU  727  CD1 LEU D 557     1810   2613   4076   -610   -362   1623       C  
ATOM    728  CD2 LEU D 557      30.754  -3.780  64.681  1.00 26.39           C  
ANISOU  728  CD2 LEU D 557     2313   3205   4510   -677   -536   1678       C  
ATOM    729  N   PHE D 558      34.385  -5.859  60.876  1.00 33.23           N  
ANISOU  729  N   PHE D 558     2925   3940   5761   -585   -306   1926       N  
ATOM    730  CA  PHE D 558      34.609  -7.100  60.152  1.00 33.85           C  
ANISOU  730  CA  PHE D 558     2911   4028   5923   -579   -324   2042       C  
ATOM    731  C   PHE D 558      35.867  -7.049  59.294  1.00 36.43           C  
ANISOU  731  C   PHE D 558     3198   4305   6339   -537   -217   2073       C  
ATOM    732  O   PHE D 558      36.009  -7.841  58.356  1.00 43.91           O  
ANISOU  732  O   PHE D 558     4080   5254   7351   -538   -221   2157       O  
ATOM    733  CB  PHE D 558      33.388  -7.440  59.304  1.00 27.33           C  
ANISOU  733  CB  PHE D 558     2094   3231   5060   -640   -407   2055       C  
ATOM    734  CG  PHE D 558      32.136  -7.634  60.109  1.00 26.81           C  
ANISOU  734  CG  PHE D 558     2064   3214   4907   -683   -509   2036       C  
ATOM    735  CD2 PHE D 558      31.293  -6.565  60.363  1.00 26.51           C  
ANISOU  735  CD2 PHE D 558     2121   3177   4775   -711   -527   1929       C  
ATOM    736  CD1 PHE D 558      31.834  -8.868  60.664  1.00 27.34           C  
ANISOU  736  CD1 PHE D 558     2075   3331   4984   -692   -584   2129       C  
ATOM    737  CE2 PHE D 558      30.149  -6.732  61.114  1.00 25.37           C  
ANISOU  737  CE2 PHE D 558     2013   3078   4548   -748   -613   1913       C  
ATOM    738  CE1 PHE D 558      30.688  -9.041  61.413  1.00 26.92           C  
ANISOU  738  CE1 PHE D 558     2061   3325   4840   -734   -672   2113       C  
ATOM    739  CZ  PHE D 558      29.848  -7.969  61.642  1.00 25.92           C  
ANISOU  739  CZ  PHE D 558     2031   3196   4622   -761   -684   2003       C  
ATOM    740  N   TYR D 559      36.777  -6.127  59.593  1.00 28.25           N  
ANISOU  740  N   TYR D 559     2205   3224   5305   -503   -120   2008       N  
ATOM    741  CA  TYR D 559      38.087  -6.147  58.966  1.00 28.22           C  
ANISOU  741  CA  TYR D 559     2165   3172   5387   -457     -9   2043       C  
ATOM    742  C   TYR D 559      38.898  -7.317  59.510  1.00 30.51           C  
ANISOU  742  C   TYR D 559     2355   3462   5776   -403      5   2151       C  
ATOM    743  O   TYR D 559      38.768  -7.705  60.673  1.00 28.87           O  
ANISOU  743  O   TYR D 559     2129   3277   5562   -391    -39   2167       O  
ATOM    744  CB  TYR D 559      38.829  -4.832  59.212  1.00 27.64           C  
ANISOU  744  CB  TYR D 559     2175   3049   5278   -442     93   1942       C  
ATOM    745  CG  TYR D 559      38.445  -3.697  58.283  1.00 29.47           C  
ANISOU  745  CG  TYR D 559     2488   3267   5441   -481    115   1862       C  
ATOM    746  CD1 TYR D 559      37.281  -3.748  57.521  1.00 37.00           C  
ANISOU  746  CD1 TYR D 559     3450   4251   6356   -530     36   1862       C  
ATOM    747  CD2 TYR D 559      39.258  -2.576  58.158  1.00 32.22           C  
ANISOU  747  CD2 TYR D 559     2906   3570   5765   -470    218   1790       C  
ATOM    748  CE1 TYR D 559      36.933  -2.708  56.672  1.00 40.06           C  
ANISOU  748  CE1 TYR D 559     3908   4624   6689   -563     58   1797       C  
ATOM    749  CE2 TYR D 559      38.922  -1.536  57.309  1.00 35.21           C  
ANISOU  749  CE2 TYR D 559     3357   3940   6081   -506    237   1727       C  
ATOM    750  CZ  TYR D 559      37.759  -1.607  56.570  1.00 34.78           C  
ANISOU  750  CZ  TYR D 559     3304   3916   5996   -550    157   1733       C  
ATOM    751  OH  TYR D 559      37.420  -0.574  55.726  1.00 30.66           O  
ANISOU  751  OH  TYR D 559     2848   3382   5418   -582    176   1677       O  
ATOM    752  N   HIS D 560      39.742  -7.882  58.654  1.00 41.80           N  
ANISOU  752  N   HIS D 560     3717   4867   7298   -368     66   2231       N  
ATOM    753  CA  HIS D 560      40.493  -9.091  58.974  1.00 39.28           C  
ANISOU  753  CA  HIS D 560     3291   4549   7086   -313     80   2352       C  
ATOM    754  C   HIS D 560      41.877  -8.695  59.474  1.00 31.72           C  
ANISOU  754  C   HIS D 560     2336   3528   6188   -247    207   2333       C  
ATOM    755  O   HIS D 560      42.691  -8.162  58.713  1.00 31.61           O  
ANISOU  755  O   HIS D 560     2343   3466   6201   -226    311   2311       O  
ATOM    756  CB  HIS D 560      40.584  -9.997  57.750  1.00 36.96           C  
ANISOU  756  CB  HIS D 560     2915   4266   6862   -312     72   2460       C  
ATOM    757  CG  HIS D 560      39.313 -10.727  57.449  1.00 32.31           C  
ANISOU  757  CG  HIS D 560     2303   3740   6234   -373    -60   2507       C  
ATOM    758  ND1 HIS D 560      38.400 -11.065  58.424  1.00 31.81           N  
ANISOU  758  ND1 HIS D 560     2251   3725   6110   -404   -163   2504       N  
ATOM    759  CD2 HIS D 560      38.791 -11.159  56.279  1.00 33.71           C  
ANISOU  759  CD2 HIS D 560     2453   3936   6419   -414   -101   2556       C  
ATOM    760  CE1 HIS D 560      37.377 -11.690  57.868  1.00 32.10           C  
ANISOU  760  CE1 HIS D 560     2272   3807   6117   -462   -260   2547       C  
ATOM    761  NE2 HIS D 560      37.589 -11.760  56.568  1.00 33.09           N  
ANISOU  761  NE2 HIS D 560     2373   3915   6286   -470   -226   2578       N  
ATOM    762  N   ILE D 561      42.141  -8.949  60.753  1.00 31.18           N  
ANISOU  762  N   ILE D 561     2249   3459   6138   -217    202   2344       N  
ATOM    763  CA  ILE D 561      43.429  -8.617  61.349  1.00 31.43           C  
ANISOU  763  CA  ILE D 561     2284   3425   6231   -157    322   2326       C  
ATOM    764  C   ILE D 561      44.434  -9.688  60.944  1.00 32.79           C  
ANISOU  764  C   ILE D 561     2346   3572   6540    -88    384   2455       C  
ATOM    765  O   ILE D 561      44.271 -10.866  61.277  1.00 33.42           O  
ANISOU  765  O   ILE D 561     2330   3689   6678    -68    319   2569       O  
ATOM    766  CB  ILE D 561      43.320  -8.508  62.877  1.00 30.88           C  
ANISOU  766  CB  ILE D 561     2231   3362   6138   -152    292   2296       C  
ATOM    767  CG1 ILE D 561      42.552  -7.246  63.270  1.00 29.56           C  
ANISOU  767  CG1 ILE D 561     2185   3208   5840   -211    261   2158       C  
ATOM    768  CG2 ILE D 561      44.699  -8.478  63.509  1.00 33.18           C  
ANISOU  768  CG2 ILE D 561     2501   3584   6521    -83    413   2308       C  
ATOM    769  CD1 ILE D 561      42.300  -7.129  64.757  1.00 29.00           C  
ANISOU  769  CD1 ILE D 561     2131   3152   5736   -214    218   2131       C  
ATOM    770  N   VAL D 562      45.467  -9.280  60.205  1.00 33.30           N  
ANISOU  770  N   VAL D 562     2423   3577   6653    -52    509   2443       N  
ATOM    771  CA  VAL D 562      46.534 -10.173  59.776  1.00 49.36           C  
ANISOU  771  CA  VAL D 562     4359   5577   8818     22    588   2560       C  
ATOM    772  C   VAL D 562      47.872  -9.491  60.025  1.00 46.28           C  
ANISOU  772  C   VAL D 562     4011   5100   8474     77    745   2507       C  
ATOM    773  O   VAL D 562      47.959  -8.269  60.146  1.00 50.56           O  
ANISOU  773  O   VAL D 562     4663   5613   8936     47    793   2383       O  
ATOM    774  CB  VAL D 562      46.406 -10.582  58.293  1.00 35.33           C  
ANISOU  774  CB  VAL D 562     2540   3819   7063     10    582   2626       C  
ATOM    775  CG1 VAL D 562      45.221 -11.515  58.090  1.00 35.40           C  
ANISOU  775  CG1 VAL D 562     2490   3909   7051    -37    433   2703       C  
ATOM    776  CG2 VAL D 562      46.268  -9.350  57.423  1.00 34.72           C  
ANISOU  776  CG2 VAL D 562     2566   3725   6901    -34    625   2516       C  
ATOM    777  N   ASP D 563      48.931 -10.307  60.094  1.00 53.25           N  
ANISOU  777  N   ASP D 563     4804   5940   9486    158    826   2608       N  
ATOM    778  CA  ASP D 563      50.250  -9.781  60.444  1.00 54.75           C  
ANISOU  778  CA  ASP D 563     5029   6040   9733    216    980   2567       C  
ATOM    779  C   ASP D 563      50.840  -8.935  59.324  1.00 50.58           C  
ANISOU  779  C   ASP D 563     4569   5469   9178    213   1087   2508       C  
ATOM    780  O   ASP D 563      51.430  -7.879  59.583  1.00 43.47           O  
ANISOU  780  O   ASP D 563     3766   4513   8237    211   1180   2403       O  
ATOM    781  CB  ASP D 563      51.206 -10.923  60.790  1.00 58.18           C  
ANISOU  781  CB  ASP D 563     5345   6438  10323    309   1042   2698       C  
ATOM    782  CG  ASP D 563      50.803 -11.661  62.046  1.00 62.20           C  
ANISOU  782  CG  ASP D 563     5790   6979  10863    319    955   2755       C  
ATOM    783  OD1 ASP D 563      49.660 -12.150  62.102  1.00 61.06           O  
ANISOU  783  OD1 ASP D 563     5616   6918  10666    269    810   2792       O  
ATOM    784  OD2 ASP D 563      51.632 -11.750  62.976  1.00 66.26           O  
ANISOU  784  OD2 ASP D 563     6284   7436  11456    376   1032   2764       O  
ATOM    785  N   SER D 564      50.702  -9.378  58.078  1.00 51.72           N  
ANISOU  785  N   SER D 564     4667   5642   9342    211   1074   2580       N  
ATOM    786  CA  SER D 564      51.436  -8.767  56.983  1.00 55.09           C  
ANISOU  786  CA  SER D 564     5137   6026   9767    224   1188   2555       C  
ATOM    787  C   SER D 564      50.618  -8.856  55.702  1.00 54.99           C  
ANISOU  787  C   SER D 564     5112   6075   9707    171   1113   2585       C  
ATOM    788  O   SER D 564      49.496  -9.365  55.687  1.00 60.43           O  
ANISOU  788  O   SER D 564     5764   6832  10364    123    977   2618       O  
ATOM    789  CB  SER D 564      52.803  -9.433  56.817  1.00 65.52           C  
ANISOU  789  CB  SER D 564     6387   7282  11228    321   1321   2649       C  
ATOM    790  OG  SER D 564      52.677 -10.679  56.156  1.00 70.78           O  
ANISOU  790  OG  SER D 564     6929   7987  11977    350   1275   2797       O  
ATOM    791  N   ASP D 565      51.188  -8.323  54.623  1.00 55.21           N  
ANISOU  791  N   ASP D 565     5174   6076   9728    176   1206   2573       N  
ATOM    792  CA  ASP D 565      50.603  -8.467  53.299  1.00 61.46           C  
ANISOU  792  CA  ASP D 565     5941   6917  10496    136   1155   2619       C  
ATOM    793  C   ASP D 565      50.951  -9.798  52.648  1.00 66.55           C  
ANISOU  793  C   ASP D 565     6452   7574  11258    187   1158   2779       C  
ATOM    794  O   ASP D 565      50.366 -10.127  51.612  1.00 71.05           O  
ANISOU  794  O   ASP D 565     6984   8193  11820    150   1098   2835       O  
ATOM    795  CB  ASP D 565      51.044  -7.310  52.395  1.00 63.53           C  
ANISOU  795  CB  ASP D 565     6294   7151  10695    117   1250   2545       C  
ATOM    796  CG  ASP D 565      52.528  -7.018  52.499  1.00 67.77           C  
ANISOU  796  CG  ASP D 565     6854   7608  11288    189   1417   2537       C  
ATOM    797  OD1 ASP D 565      53.155  -7.457  53.486  1.00 68.24           O  
ANISOU  797  OD1 ASP D 565     6884   7624  11419    246   1461   2555       O  
ATOM    798  OD2 ASP D 565      53.073  -6.360  51.587  1.00 71.07           O  
ANISOU  798  OD2 ASP D 565     7319   8005  11678    188   1506   2517       O  
ATOM    799  N   GLU D 566      51.884 -10.560  53.231  1.00 65.63           N  
ANISOU  799  N   GLU D 566     6266   7417  11255    270   1227   2856       N  
ATOM    800  CA  GLU D 566      52.174 -11.910  52.754  1.00 63.74           C  
ANISOU  800  CA  GLU D 566     5892   7195  11131    322   1219   3021       C  
ATOM    801  C   GLU D 566      50.942 -12.801  52.864  1.00 54.76           C  
ANISOU  801  C   GLU D 566     4686   6140   9979    270   1049   3088       C  
ATOM    802  O   GLU D 566      50.518 -13.433  51.884  1.00 53.09           O  
ANISOU  802  O   GLU D 566     4411   5978   9784    245    991   3178       O  
ATOM    803  CB  GLU D 566      53.330 -12.507  53.562  1.00 74.05           C  
ANISOU  803  CB  GLU D 566     7141   8436  12558    421   1319   3084       C  
ATOM    804  CG  GLU D 566      54.715 -11.958  53.238  1.00 80.63           C  
ANISOU  804  CG  GLU D 566     8016   9183  13438    488   1502   3060       C  
ATOM    805  CD  GLU D 566      55.418 -12.739  52.145  1.00 85.93           C  
ANISOU  805  CD  GLU D 566     8596   9847  14205    547   1571   3198       C  
ATOM    806  OE1 GLU D 566      55.526 -13.978  52.275  1.00 85.47           O  
ANISOU  806  OE1 GLU D 566     8418   9806  14250    596   1539   3338       O  
ATOM    807  OE2 GLU D 566      55.870 -12.118  51.161  1.00 87.73           O  
ANISOU  807  OE2 GLU D 566     8872  10057  14405    544   1658   3171       O  
ATOM    808  N   VAL D 567      50.342 -12.843  54.056  1.00 48.33           N  
ANISOU  808  N   VAL D 567     3889   5345   9129    248    966   3045       N  
ATOM    809  CA  VAL D 567      49.169 -13.680  54.283  1.00 52.46           C  
ANISOU  809  CA  VAL D 567     4356   5946   9629    197    805   3106       C  
ATOM    810  C   VAL D 567      47.965 -13.148  53.513  1.00 56.26           C  
ANISOU  810  C   VAL D 567     4897   6480  10000    100    710   3040       C  
ATOM    811  O   VAL D 567      47.194 -13.929  52.944  1.00 64.01           O  
ANISOU  811  O   VAL D 567     5820   7521  10982     59    608   3121       O  
ATOM    812  CB  VAL D 567      48.906 -13.811  55.798  1.00 47.10           C  
ANISOU  812  CB  VAL D 567     3683   5273   8939    203    752   3078       C  
ATOM    813  CG1 VAL D 567      48.955 -12.460  56.474  1.00 38.78           C  
ANISOU  813  CG1 VAL D 567     2756   4179   7801    182    800   2914       C  
ATOM    814  CG2 VAL D 567      47.569 -14.492  56.074  1.00 49.93           C  
ANISOU  814  CG2 VAL D 567     4009   5716   9244    137    580   3118       C  
ATOM    815  N   SER D 568      47.807 -11.819  53.438  1.00 49.92           N  
ANISOU  815  N   SER D 568     4212   5652   9101     62    745   2897       N  
ATOM    816  CA  SER D 568      46.727 -11.239  52.639  1.00 45.80           C  
ANISOU  816  CA  SER D 568     3748   5170   8482    -24    669   2836       C  
ATOM    817  C   SER D 568      46.849 -11.634  51.172  1.00 53.49           C  
ANISOU  817  C   SER D 568     4666   6158   9500    -30    686   2924       C  
ATOM    818  O   SER D 568      45.866 -12.063  50.553  1.00 59.27           O  
ANISOU  818  O   SER D 568     5370   6941  10207    -90    581   2962       O  
ATOM    819  CB  SER D 568      46.725  -9.716  52.775  1.00 45.65           C  
ANISOU  819  CB  SER D 568     3862   5118   8364    -53    722   2682       C  
ATOM    820  OG  SER D 568      46.806  -9.316  54.130  1.00 59.03           O  
ANISOU  820  OG  SER D 568     5606   6793  10028    -41    726   2605       O  
ATOM    821  N   THR D 569      48.061 -11.538  50.617  1.00 54.07           N  
ANISOU  821  N   THR D 569     4720   6184   9640     33    820   2961       N  
ATOM    822  CA  THR D 569      48.291 -11.898  49.222  1.00 41.25           C  
ANISOU  822  CA  THR D 569     3039   4573   8062     34    848   3051       C  
ATOM    823  C   THR D 569      48.052 -13.385  48.985  1.00 42.33           C  
ANISOU  823  C   THR D 569     3046   4755   8281     43    770   3207       C  
ATOM    824  O   THR D 569      47.480 -13.765  47.959  1.00 61.36           O  
ANISOU  824  O   THR D 569     5416   7207  10691     -5    710   3268       O  
ATOM    825  CB  THR D 569      49.712 -11.497  48.815  1.00 42.86           C  
ANISOU  825  CB  THR D 569     3252   4714   8318    107   1016   3060       C  
ATOM    826  OG1 THR D 569      49.879 -10.084  48.998  1.00 41.03           O  
ANISOU  826  OG1 THR D 569     3148   4446   7997     88   1082   2915       O  
ATOM    827  CG2 THR D 569      49.990 -11.844  47.353  1.00 45.99           C  
ANISOU  827  CG2 THR D 569     3588   5126   8760    111   1052   3158       C  
ATOM    828  N   LYS D 570      48.436 -14.242  49.937  1.00 43.82           N  
ANISOU  828  N   LYS D 570     3170   4940   8539     98    764   3276       N  
ATOM    829  CA  LYS D 570      48.254 -15.679  49.729  1.00 53.88           C  
ANISOU  829  CA  LYS D 570     4319   6262   9890    106    689   3436       C  
ATOM    830  C   LYS D 570      46.782 -16.086  49.812  1.00 49.11           C  
ANISOU  830  C   LYS D 570     3714   5730   9215     13    520   3436       C  
ATOM    831  O   LYS D 570      46.303 -16.872  48.977  1.00 60.70           O  
ANISOU  831  O   LYS D 570     5114   7246  10703    -26    450   3535       O  
ATOM    832  CB  LYS D 570      49.098 -16.471  50.727  1.00 66.94           C  
ANISOU  832  CB  LYS D 570     5902   7892  11641    195    732   3519       C  
ATOM    833  CG  LYS D 570      50.384 -17.030  50.122  1.00 76.40           C  
ANISOU  833  CG  LYS D 570     7017   9052  12960    285    855   3639       C  
ATOM    834  CD  LYS D 570      51.352 -15.919  49.745  1.00 78.97           C  
ANISOU  834  CD  LYS D 570     7421   9304  13280    325   1013   3548       C  
ATOM    835  CE  LYS D 570      52.490 -16.435  48.877  1.00 79.69           C  
ANISOU  835  CE  LYS D 570     7435   9365  13477    402   1131   3669       C  
ATOM    836  NZ  LYS D 570      51.991 -17.076  47.627  1.00 76.39           N  
ANISOU  836  NZ  LYS D 570     6944   9011  13069    357   1063   3775       N  
ATOM    837  N   ILE D 571      46.046 -15.563  50.803  1.00 41.98           N  
ANISOU  837  N   ILE D 571     2888   4836   8227    -25    454   3328       N  
ATOM    838  CA  ILE D 571      44.610 -15.842  50.881  1.00 43.90           C  
ANISOU  838  CA  ILE D 571     3146   5142   8392   -116    301   3314       C  
ATOM    839  C   ILE D 571      43.880 -15.280  49.666  1.00 55.41           C  
ANISOU  839  C   ILE D 571     4650   6611   9791   -192    273   3266       C  
ATOM    840  O   ILE D 571      42.951 -15.907  49.152  1.00 62.30           O  
ANISOU  840  O   ILE D 571     5491   7533  10646   -258    167   3319       O  
ATOM    841  CB  ILE D 571      44.000 -15.327  52.206  1.00 45.08           C  
ANISOU  841  CB  ILE D 571     3373   5297   8459   -138    246   3206       C  
ATOM    842  CG1 ILE D 571      44.786 -15.809  53.428  1.00 43.26           C  
ANISOU  842  CG1 ILE D 571     3096   5047   8292    -61    284   3252       C  
ATOM    843  CG2 ILE D 571      42.549 -15.758  52.350  1.00 39.71           C  
ANISOU  843  CG2 ILE D 571     2704   4682   7702   -226     91   3206       C  
ATOM    844  CD1 ILE D 571      45.031 -17.303  53.455  1.00 52.38           C  
ANISOU  844  CD1 ILE D 571     4123   6238   9540    -28    243   3428       C  
ATOM    845  N   LEU D 572      44.311 -14.122  49.153  1.00 55.74           N  
ANISOU  845  N   LEU D 572     4766   6608   9806   -183    369   3174       N  
ATOM    846  CA  LEU D 572      43.644 -13.575  47.974  1.00 55.25           C  
ANISOU  846  CA  LEU D 572     4743   6556   9696   -251    345   3138       C  
ATOM    847  C   LEU D 572      43.987 -14.361  46.711  1.00 51.22           C  
ANISOU  847  C   LEU D 572     4136   6061   9266   -246    362   3272       C  
ATOM    848  O   LEU D 572      43.144 -14.494  45.810  1.00 55.10           O  
ANISOU  848  O   LEU D 572     4620   6580   9734   -318    290   3292       O  
ATOM    849  CB  LEU D 572      44.006 -12.102  47.806  1.00 40.03           C  
ANISOU  849  CB  LEU D 572     2920   4580   7708   -245    440   3010       C  
ATOM    850  CG  LEU D 572      43.154 -11.121  48.612  1.00 38.49           C  
ANISOU  850  CG  LEU D 572     2837   4384   7403   -292    388   2866       C  
ATOM    851  CD1 LEU D 572      43.399  -9.698  48.135  1.00 37.90           C  
ANISOU  851  CD1 LEU D 572     2862   4272   7266   -301    471   2759       C  
ATOM    852  CD2 LEU D 572      41.676 -11.478  48.544  1.00 38.16           C  
ANISOU  852  CD2 LEU D 572     2801   4390   7307   -375    243   2861       C  
ATOM    853  N   MET D 573      45.207 -14.899  46.639  1.00 54.05           N  
ANISOU  853  N   MET D 573     4419   6398   9720   -164    457   3367       N  
ATOM    854  CA  MET D 573      45.591 -15.774  45.536  1.00 51.27           C  
ANISOU  854  CA  MET D 573     3963   6066   9451   -152    472   3511       C  
ATOM    855  C   MET D 573      44.717 -17.018  45.501  1.00 66.38           C  
ANISOU  855  C   MET D 573     5798   8042  11380   -205    335   3616       C  
ATOM    856  O   MET D 573      44.167 -17.375  44.452  1.00 75.51           O  
ANISOU  856  O   MET D 573     6919   9230  12542   -265    282   3673       O  
ATOM    857  CB  MET D 573      47.063 -16.161  45.676  1.00 48.04           C  
ANISOU  857  CB  MET D 573     3489   5619   9143    -44    600   3594       C  
ATOM    858  CG  MET D 573      47.850 -16.159  44.386  1.00 57.14           C  
ANISOU  858  CG  MET D 573     4597   6760  10354    -14    698   3670       C  
ATOM    859  SD  MET D 573      49.617 -16.215  44.731  1.00 69.34           S  
ANISOU  859  SD  MET D 573     6110   8240  11995    118    876   3717       S  
ATOM    860  CE  MET D 573      50.181 -14.732  43.908  1.00 66.25           C  
ANISOU  860  CE  MET D 573     5822   7803  11547    119   1006   3609       C  
ATOM    861  N   GLU D 574      44.562 -17.681  46.652  1.00 67.84           N  
ANISOU  861  N   GLU D 574     5959   8248  11571   -189    276   3642       N  
ATOM    862  CA  GLU D 574      43.682 -18.848  46.707  1.00 70.01           C  
ANISOU  862  CA  GLU D 574     6169   8588  11844   -248    141   3738       C  
ATOM    863  C   GLU D 574      42.222 -18.464  46.476  1.00 66.60           C  
ANISOU  863  C   GLU D 574     5812   8184  11310   -360     27   3650       C  
ATOM    864  O   GLU D 574      41.468 -19.235  45.857  1.00 72.22           O  
ANISOU  864  O   GLU D 574     6479   8941  12020   -431    -65   3724       O  
ATOM    865  CB  GLU D 574      43.849 -19.564  48.046  1.00 69.17           C  
ANISOU  865  CB  GLU D 574     6026   8497  11756   -205    106   3785       C  
ATOM    866  CG  GLU D 574      45.021 -20.527  48.062  1.00 67.20           C  
ANISOU  866  CG  GLU D 574     5662   8244  11629   -114    174   3940       C  
ATOM    867  CD  GLU D 574      44.633 -21.915  47.604  1.00 66.56           C  
ANISOU  867  CD  GLU D 574     5474   8230  11585   -152     80   4104       C  
ATOM    868  OE1 GLU D 574      45.517 -22.794  47.531  1.00 69.40           O  
ANISOU  868  OE1 GLU D 574     5731   8594  12045    -82    126   4248       O  
ATOM    869  OE2 GLU D 574      43.440 -22.127  47.317  1.00 64.79           O  
ANISOU  869  OE2 GLU D 574     5272   8055  11289   -254    -39   4089       O  
ATOM    870  N   PHE D 575      41.834 -17.268  46.939  1.00 60.34           N  
ANISOU  870  N   PHE D 575     5132   7360  10433   -376     39   3493       N  
ATOM    871  CA  PHE D 575      40.489 -16.738  46.748  1.00 59.86           C  
ANISOU  871  CA  PHE D 575     5155   7314  10277   -473    -53   3396       C  
ATOM    872  C   PHE D 575      40.133 -16.673  45.272  1.00 62.74           C  
ANISOU  872  C   PHE D 575     5504   7680  10654   -529    -60   3425       C  
ATOM    873  O   PHE D 575      39.067 -17.134  44.851  1.00 68.57           O  
ANISOU  873  O   PHE D 575     6238   8451  11365   -615   -162   3445       O  
ATOM    874  CB  PHE D 575      40.407 -15.332  47.342  1.00 53.10           C  
ANISOU  874  CB  PHE D 575     4416   6417   9342   -463     -8   3232       C  
ATOM    875  CG  PHE D 575      39.188 -15.075  48.162  1.00 48.52           C  
ANISOU  875  CG  PHE D 575     3912   5859   8663   -525   -110   3140       C  
ATOM    876  CD2 PHE D 575      38.092 -14.430  47.616  1.00 53.85           C  
ANISOU  876  CD2 PHE D 575     4661   6533   9267   -604   -163   3057       C  
ATOM    877  CD1 PHE D 575      39.184 -15.373  49.513  1.00 45.69           C  
ANISOU  877  CD1 PHE D 575     3558   5517   8285   -498   -142   3131       C  
ATOM    878  CE2 PHE D 575      36.974 -14.169  48.386  1.00 58.85           C  
ANISOU  878  CE2 PHE D 575     5367   7184   9808   -656   -250   2971       C  
ATOM    879  CE1 PHE D 575      38.084 -15.097  50.290  1.00 46.77           C  
ANISOU  879  CE1 PHE D 575     3768   5676   8327   -552   -230   3046       C  
ATOM    880  CZ  PHE D 575      36.973 -14.499  49.728  1.00 54.32           C  
ANISOU  880  CZ  PHE D 575     4797   6633   9211   -630   -283   2965       C  
ATOM    881  N   ASN D 576      41.023 -16.088  44.472  1.00 62.86           N  
ANISOU  881  N   ASN D 576     5515   7658  10712   -484     52   3428       N  
ATOM    882  CA  ASN D 576      40.755 -15.968  43.048  1.00 60.05           C  
ANISOU  882  CA  ASN D 576     5142   7302  10372   -534     53   3461       C  
ATOM    883  C   ASN D 576      41.065 -17.240  42.277  1.00 62.59           C  
ANISOU  883  C   ASN D 576     5339   7659  10784   -535     36   3629       C  
ATOM    884  O   ASN D 576      40.559 -17.406  41.162  1.00 70.08           O  
ANISOU  884  O   ASN D 576     6263   8620  11744   -599     -1   3671       O  
ATOM    885  CB  ASN D 576      41.542 -14.804  42.450  1.00 60.47           C  
ANISOU  885  CB  ASN D 576     5243   7308  10425   -492    179   3402       C  
ATOM    886  CG  ASN D 576      40.950 -13.468  42.816  1.00 63.39           C  
ANISOU  886  CG  ASN D 576     5740   7650  10696   -522    178   3241       C  
ATOM    887  OD1 ASN D 576      39.875 -13.400  43.412  1.00 60.72           O  
ANISOU  887  OD1 ASN D 576     5453   7326  10292   -577     82   3174       O  
ATOM    888  ND2 ASN D 576      41.628 -12.397  42.436  1.00 67.16           N  
ANISOU  888  ND2 ASN D 576     6269   8090  11158   -488    285   3183       N  
ATOM    889  N   LYS D 577      41.875 -18.142  42.835  1.00 59.24           N  
ANISOU  889  N   LYS D 577     4833   7250  10425   -468     60   3730       N  
ATOM    890  CA  LYS D 577      42.165 -19.374  42.114  1.00 57.41           C  
ANISOU  890  CA  LYS D 577     4478   7057  10277   -469     41   3899       C  
ATOM    891  C   LYS D 577      40.988 -20.341  42.179  1.00 65.37           C  
ANISOU  891  C   LYS D 577     5458   8121  11257   -564   -107   3950       C  
ATOM    892  O   LYS D 577      40.565 -20.873  41.146  1.00 80.10           O  
ANISOU  892  O   LYS D 577     7274  10013  13147   -628   -154   4027       O  
ATOM    893  CB  LYS D 577      43.444 -20.023  42.651  1.00 52.88           C  
ANISOU  893  CB  LYS D 577     3824   6478   9789   -361    121   4000       C  
ATOM    894  CG  LYS D 577      43.705 -21.415  42.089  1.00 57.39           C  
ANISOU  894  CG  LYS D 577     4263   7098  10445   -360     89   4187       C  
ATOM    895  CD  LYS D 577      45.184 -21.789  42.130  1.00 60.75           C  
ANISOU  895  CD  LYS D 577     4608   7502  10972   -241    212   4290       C  
ATOM    896  CE  LYS D 577      45.813 -21.492  43.479  1.00 59.49           C  
ANISOU  896  CE  LYS D 577     4485   7304  10815   -156    270   4232       C  
ATOM    897  NZ  LYS D 577      45.193 -22.314  44.548  1.00 56.27           N  
ANISOU  897  NZ  LYS D 577     4056   6939  10385   -180    157   4267       N  
ATOM    898  N   MET D 578      40.429 -20.575  43.371  1.00 57.01           N  
ANISOU  898  N   MET D 578     4434   7082  10143   -578   -181   3908       N  
ATOM    899  CA  MET D 578      39.244 -21.427  43.435  1.00 55.28           C  
ANISOU  899  CA  MET D 578     4204   6918   9882   -678   -318   3945       C  
ATOM    900  C   MET D 578      37.937 -20.666  43.231  1.00 52.91           C  
ANISOU  900  C   MET D 578     4009   6604   9488   -775   -385   3811       C  
ATOM    901  O   MET D 578      36.874 -21.295  43.265  1.00 52.74           O  
ANISOU  901  O   MET D 578     3991   6622   9425   -866   -494   3825       O  
ATOM    902  CB  MET D 578      39.174 -22.203  44.757  1.00 56.67           C  
ANISOU  902  CB  MET D 578     4359   7133  10038   -659   -376   3986       C  
ATOM    903  CG  MET D 578      40.065 -23.433  44.829  1.00 67.92           C  
ANISOU  903  CG  MET D 578     5656   8594  11555   -600   -360   4164       C  
ATOM    904  SD  MET D 578      40.825 -23.688  46.443  1.00 78.83           S  
ANISOU  904  SD  MET D 578     7023   9975  12956   -498   -330   4186       S  
ATOM    905  CE  MET D 578      39.425 -24.286  47.391  1.00 71.08           C  
ANISOU  905  CE  MET D 578     6082   9060  11866   -597   -486   4169       C  
ATOM    906  N   ASN D 579      37.999 -19.345  43.019  1.00 44.38           N  
ANISOU  906  N   ASN D 579     4308   4002   8552   -791    -74    731       N  
ATOM    907  CA  ASN D 579      36.853 -18.487  42.718  1.00 50.71           C  
ANISOU  907  CA  ASN D 579     5346   4808   9113   -856   -132    665       C  
ATOM    908  C   ASN D 579      35.793 -18.562  43.814  1.00 52.87           C  
ANISOU  908  C   ASN D 579     5736   5113   9240   -835   -298    593       C  
ATOM    909  O   ASN D 579      34.780 -19.255  43.667  1.00 47.69           O  
ANISOU  909  O   ASN D 579     5115   4468   8537   -917   -431    606       O  
ATOM    910  CB  ASN D 579      36.256 -18.851  41.352  1.00 61.65           C  
ANISOU  910  CB  ASN D 579     6742   6184  10498  -1003   -151    728       C  
ATOM    911  CG  ASN D 579      35.174 -17.883  40.895  1.00 66.88           C  
ANISOU  911  CG  ASN D 579     7655   6801  10955  -1062   -204    667       C  
ATOM    912  OD1 ASN D 579      34.943 -16.845  41.512  1.00 62.07           O  
ANISOU  912  OD1 ASN D 579     7192   6169  10223   -983   -213    576       O  
ATOM    913  ND2 ASN D 579      34.506 -18.225  39.797  1.00 73.22           N  
ANISOU  913  ND2 ASN D 579     8500   7578  11743  -1199   -247    716       N  
ATOM    914  N   LEU D 580      36.009 -17.830  44.903  1.00 55.07           N  
ANISOU  914  N   LEU D 580     6083   5402   9440   -744   -274    509       N  
ATOM    915  CA  LEU D 580      35.178 -17.862  46.095  1.00 50.41           C  
ANISOU  915  CA  LEU D 580     5588   4847   8719   -740   -376    430       C  
ATOM    916  C   LEU D 580      34.403 -16.555  46.257  1.00 45.98           C  
ANISOU  916  C   LEU D 580     5191   4274   8007   -717   -361    304       C  
ATOM    917  O   LEU D 580      34.859 -15.502  45.804  1.00 55.74           O  
ANISOU  917  O   LEU D 580     6471   5473   9234   -670   -284    281       O  
ATOM    918  CB  LEU D 580      36.037 -18.089  47.342  1.00 43.21           C  
ANISOU  918  CB  LEU D 580     4612   3952   7854   -671   -363    433       C  
ATOM    919  CG  LEU D 580      36.672 -19.446  47.640  1.00 28.27           C  
ANISOU  919  CG  LEU D 580     2564   2045   6132   -676   -443    551       C  
ATOM    920  CD1 LEU D 580      35.744 -20.605  47.285  1.00 29.48           C  
ANISOU  920  CD1 LEU D 580     2713   2208   6281   -789   -603    618       C  
ATOM    921  CD2 LEU D 580      38.019 -19.567  46.957  1.00 29.30           C  
ANISOU  921  CD2 LEU D 580     2506   2121   6506   -604   -324    624       C  
ATOM    922  N   PRO D 581      33.240 -16.574  46.908  1.00 33.53           N  
ANISOU  922  N   PRO D 581     3706   2711   6323   -753   -435    216       N  
ATOM    923  CA  PRO D 581      32.448 -15.355  47.051  1.00 34.22           C  
ANISOU  923  CA  PRO D 581     3904   2767   6332   -714   -431     87       C  
ATOM    924  C   PRO D 581      32.724 -14.622  48.365  1.00 25.63           C  
ANISOU  924  C   PRO D 581     2817   1716   5205   -647   -384     -9       C  
ATOM    925  O   PRO D 581      33.428 -15.108  49.250  1.00 25.31           O  
ANISOU  925  O   PRO D 581     2727   1722   5168   -650   -356     21       O  
ATOM    926  CB  PRO D 581      31.017 -15.896  47.037  1.00 37.78           C  
ANISOU  926  CB  PRO D 581     4433   3199   6724   -803   -513     27       C  
ATOM    927  CG  PRO D 581      31.138 -17.172  47.809  1.00 27.68           C  
ANISOU  927  CG  PRO D 581     3118   1977   5424   -885   -544     77       C  
ATOM    928  CD  PRO D 581      32.526 -17.729  47.492  1.00 27.74           C  
ANISOU  928  CD  PRO D 581     2987   2005   5547   -848   -526    223       C  
ATOM    929  N   GLY D 582      32.146 -13.438  48.461  1.00 31.38           N  
ANISOU  929  N   GLY D 582     3599   2412   5913   -591   -389   -124       N  
ATOM    930  CA  GLY D 582      32.133 -12.688  49.700  1.00 33.94           C  
ANISOU  930  CA  GLY D 582     3906   2771   6218   -545   -354   -241       C  
ATOM    931  C   GLY D 582      33.096 -11.516  49.686  1.00 35.04           C  
ANISOU  931  C   GLY D 582     4032   2898   6383   -451   -322   -246       C  
ATOM    932  O   GLY D 582      34.125 -11.519  49.001  1.00 37.93           O  
ANISOU  932  O   GLY D 582     4404   3244   6763   -437   -289   -146       O  
ATOM    933  N   GLU D 583      32.752 -10.487  50.460  1.00 27.58           N  
ANISOU  933  N   GLU D 583     3068   1959   5450   -398   -328   -375       N  
ATOM    934  CA  GLU D 583      33.619  -9.332  50.647  1.00 35.06           C  
ANISOU  934  CA  GLU D 583     4016   2898   6409   -328   -323   -393       C  
ATOM    935  C   GLU D 583      34.546  -9.572  51.830  1.00 35.91           C  
ANISOU  935  C   GLU D 583     4083   3067   6494   -348   -244   -388       C  
ATOM    936  O   GLU D 583      34.112 -10.048  52.884  1.00 24.24           O  
ANISOU  936  O   GLU D 583     2570   1641   5000   -404   -212   -445       O  
ATOM    937  CB  GLU D 583      32.798  -8.064  50.882  1.00 38.35           C  
ANISOU  937  CB  GLU D 583     4402   3282   6887   -257   -400   -536       C  
ATOM    938  CG  GLU D 583      32.649  -7.188  49.656  1.00 47.25           C  
ANISOU  938  CG  GLU D 583     5619   4310   8023   -202   -511   -506       C  
ATOM    939  CD  GLU D 583      31.805  -5.963  49.913  1.00 57.16           C  
ANISOU  939  CD  GLU D 583     6814   5522   9381   -114   -630   -646       C  
ATOM    940  OE1 GLU D 583      31.117  -5.928  50.955  1.00 60.48           O  
ANISOU  940  OE1 GLU D 583     7097   5994   9889   -100   -597   -792       O  
ATOM    941  OE2 GLU D 583      31.831  -5.040  49.072  1.00 62.37           O  
ANISOU  941  OE2 GLU D 583     7564   6088  10046    -63   -759   -618       O  
ATOM    942  N   VAL D 584      35.825  -9.244  51.650  1.00 38.45           N  
ANISOU  942  N   VAL D 584     4439   3370   6801   -320   -210   -323       N  
ATOM    943  CA  VAL D 584      36.818  -9.330  52.714  1.00 37.92           C  
ANISOU  943  CA  VAL D 584     4356   3334   6717   -331   -149   -320       C  
ATOM    944  C   VAL D 584      37.737  -8.121  52.614  1.00 39.78           C  
ANISOU  944  C   VAL D 584     4657   3523   6932   -282   -152   -342       C  
ATOM    945  O   VAL D 584      38.162  -7.744  51.516  1.00 34.06           O  
ANISOU  945  O   VAL D 584     4022   2732   6186   -260   -156   -294       O  
ATOM    946  CB  VAL D 584      37.628 -10.641  52.649  1.00 31.70           C  
ANISOU  946  CB  VAL D 584     3551   2549   5946   -359    -96   -202       C  
ATOM    947  CG1 VAL D 584      36.842 -11.780  53.272  1.00 30.15           C  
ANISOU  947  CG1 VAL D 584     3328   2396   5733   -436   -123   -188       C  
ATOM    948  CG2 VAL D 584      37.986 -10.979  51.217  1.00 34.17           C  
ANISOU  948  CG2 VAL D 584     3869   2812   6301   -343    -74   -110       C  
ATOM    949  N   THR D 585      38.025  -7.502  53.755  1.00 40.76           N  
ANISOU  949  N   THR D 585     4765   3671   7051   -286   -152   -418       N  
ATOM    950  CA  THR D 585      38.946  -6.378  53.840  1.00 38.03           C  
ANISOU  950  CA  THR D 585     4502   3274   6674   -258   -172   -445       C  
ATOM    951  C   THR D 585      40.030  -6.722  54.851  1.00 36.89           C  
ANISOU  951  C   THR D 585     4377   3136   6504   -290   -103   -429       C  
ATOM    952  O   THR D 585      39.726  -7.139  55.974  1.00 41.58           O  
ANISOU  952  O   THR D 585     4906   3784   7110   -344    -86   -458       O  
ATOM    953  CB  THR D 585      38.223  -5.090  54.242  1.00 40.52           C  
ANISOU  953  CB  THR D 585     4767   3588   7040   -234   -280   -566       C  
ATOM    954  OG1 THR D 585      37.050  -4.929  53.435  1.00 44.17           O  
ANISOU  954  OG1 THR D 585     5192   4035   7554   -196   -359   -590       O  
ATOM    955  CG2 THR D 585      39.131  -3.888  54.044  1.00 40.29           C  
ANISOU  955  CG2 THR D 585     4863   3478   6965   -211   -347   -578       C  
ATOM    956  N   PHE D 586      41.286  -6.549  54.452  1.00 34.38           N  
ANISOU  956  N   PHE D 586     4175   2746   6142   -266    -57   -387       N  
ATOM    957  CA  PHE D 586      42.421  -7.049  55.213  1.00 28.80           C  
ANISOU  957  CA  PHE D 586     3501   2013   5429   -278     11   -361       C  
ATOM    958  C   PHE D 586      43.134  -5.912  55.934  1.00 32.42           C  
ANISOU  958  C   PHE D 586     4064   2425   5830   -292    -23   -434       C  
ATOM    959  O   PHE D 586      43.315  -4.825  55.378  1.00 35.27           O  
ANISOU  959  O   PHE D 586     4533   2728   6142   -273    -72   -473       O  
ATOM    960  CB  PHE D 586      43.399  -7.774  54.286  1.00 33.51           C  
ANISOU  960  CB  PHE D 586     4136   2541   6056   -232    112   -284       C  
ATOM    961  CG  PHE D 586      43.104  -9.239  54.121  1.00 29.76           C  
ANISOU  961  CG  PHE D 586     3525   2100   5681   -234    142   -199       C  
ATOM    962  CD1 PHE D 586      43.297 -10.124  55.169  1.00 31.94           C  
ANISOU  962  CD1 PHE D 586     3750   2387   6000   -259    127   -167       C  
ATOM    963  CD2 PHE D 586      42.629  -9.729  52.914  1.00 27.97           C  
ANISOU  963  CD2 PHE D 586     3242   1876   5509   -227    165   -144       C  
ATOM    964  CE1 PHE D 586      43.024 -11.472  55.016  1.00 32.15           C  
ANISOU  964  CE1 PHE D 586     3669   2422   6123   -268    112    -80       C  
ATOM    965  CE2 PHE D 586      42.353 -11.075  52.755  1.00 30.23           C  
ANISOU  965  CE2 PHE D 586     3398   2184   5904   -237    166    -64       C  
ATOM    966  CZ  PHE D 586      42.553 -11.947  53.807  1.00 32.92           C  
ANISOU  966  CZ  PHE D 586     3688   2531   6289   -253    128    -31       C  
ATOM    967  N   LEU D 587      43.541  -6.175  57.179  1.00 31.74           N  
ANISOU  967  N   LEU D 587     3969   2345   5744   -341    -13   -445       N  
ATOM    968  CA  LEU D 587      44.284  -5.224  58.006  1.00 24.36           C  
ANISOU  968  CA  LEU D 587     3136   1359   4761   -378    -48   -509       C  
ATOM    969  C   LEU D 587      45.671  -5.798  58.289  1.00 31.82           C  
ANISOU  969  C   LEU D 587     4198   2208   5683   -360     19   -467       C  
ATOM    970  O   LEU D 587      45.862  -6.492  59.302  1.00 33.81           O  
ANISOU  970  O   LEU D 587     4434   2459   5955   -411     23   -438       O  
ATOM    971  CB  LEU D 587      43.540  -4.925  59.305  1.00 24.48           C  
ANISOU  971  CB  LEU D 587     3050   1448   4804   -475    -96   -573       C  
ATOM    972  CG  LEU D 587      42.634  -3.692  59.324  1.00 28.42           C  
ANISOU  972  CG  LEU D 587     3453   1991   5354   -482   -187   -678       C  
ATOM    973  CD1 LEU D 587      42.101  -3.433  60.727  1.00 30.70           C  
ANISOU  973  CD1 LEU D 587     3630   2350   5686   -593   -193   -757       C  
ATOM    974  CD2 LEU D 587      43.370  -2.474  58.793  1.00 34.30           C  
ANISOU  974  CD2 LEU D 587     4332   2644   6058   -448   -269   -714       C  
ATOM    975  N   PRO D 588      46.653  -5.543  57.431  1.00 36.37           N  
ANISOU  975  N   PRO D 588     4911   2686   6222   -292     72   -470       N  
ATOM    976  CA  PRO D 588      48.014  -6.057  57.662  1.00 34.78           C  
ANISOU  976  CA  PRO D 588     4810   2374   6029   -247    146   -458       C  
ATOM    977  C   PRO D 588      48.772  -5.187  58.663  1.00 33.73           C  
ANISOU  977  C   PRO D 588     4840   2160   5813   -303     88   -526       C  
ATOM    978  O   PRO D 588      49.006  -4.006  58.411  1.00 36.69           O  
ANISOU  978  O   PRO D 588     5358   2484   6097   -324     41   -596       O  
ATOM    979  CB  PRO D 588      48.660  -6.007  56.275  1.00 37.99           C  
ANISOU  979  CB  PRO D 588     5294   2706   6436   -163    253   -465       C  
ATOM    980  CG  PRO D 588      47.896  -4.969  55.521  1.00 41.64           C  
ANISOU  980  CG  PRO D 588     5814   3190   6817   -196    184   -492       C  
ATOM    981  CD  PRO D 588      46.531  -4.841  56.137  1.00 42.27           C  
ANISOU  981  CD  PRO D 588     5740   3400   6923   -254     73   -486       C  
ATOM    982  N   LEU D 589      49.175  -5.795  59.787  1.00 34.92           N  
ANISOU  982  N   LEU D 589     4995   2279   5995   -341     76   -501       N  
ATOM    983  CA  LEU D 589      49.813  -5.050  60.871  1.00 35.17           C  
ANISOU  983  CA  LEU D 589     5179   2230   5954   -426     13   -557       C  
ATOM    984  C   LEU D 589      51.162  -4.469  60.465  1.00 44.72           C  
ANISOU  984  C   LEU D 589     6615   3282   7093   -360     34   -623       C  
ATOM    985  O   LEU D 589      51.530  -3.386  60.935  1.00 53.01           O  
ANISOU  985  O   LEU D 589     7824   4271   8047   -439    -38   -694       O  
ATOM    986  CB  LEU D 589      49.994  -5.951  62.094  1.00 37.10           C  
ANISOU  986  CB  LEU D 589     5416   2441   6238   -493     -5   -499       C  
ATOM    987  CG  LEU D 589      48.739  -6.527  62.749  1.00 30.23           C  
ANISOU  987  CG  LEU D 589     4384   1701   5402   -601    -37   -446       C  
ATOM    988  CD1 LEU D 589      49.062  -7.151  64.095  1.00 35.17           C  
ANISOU  988  CD1 LEU D 589     5096   2254   6012   -721    -71   -397       C  
ATOM    989  CD2 LEU D 589      47.690  -5.453  62.892  1.00 34.85           C  
ANISOU  989  CD2 LEU D 589     4872   2412   5959   -690    -80   -520       C  
ATOM    990  N   ASN D 590      51.905  -5.162  59.601  1.00 43.07           N  
ANISOU  990  N   ASN D 590     6414   3006   6945   -226    138   -615       N  
ATOM    991  CA  ASN D 590      53.251  -4.734  59.241  1.00 46.56           C  
ANISOU  991  CA  ASN D 590     7046   3294   7353   -152    180   -707       C  
ATOM    992  C   ASN D 590      53.280  -3.482  58.372  1.00 39.24           C  
ANISOU  992  C   ASN D 590     6242   2345   6323   -171    148   -792       C  
ATOM    993  O   ASN D 590      54.353  -2.889  58.215  1.00 35.34           O  
ANISOU  993  O   ASN D 590     5900   1729   5798   -149    168   -900       O  
ATOM    994  CB  ASN D 590      53.983  -5.880  58.536  1.00 54.29           C  
ANISOU  994  CB  ASN D 590     7939   4220   8468     -7    363   -697       C  
ATOM    995  CG  ASN D 590      53.699  -5.936  57.044  1.00 60.34           C  
ANISOU  995  CG  ASN D 590     8627   5042   9259     43    522   -702       C  
ATOM    996  OD1 ASN D 590      52.558  -5.779  56.607  1.00 67.43           O  
ANISOU  996  OD1 ASN D 590     9430   6055  10134    -11    474   -645       O  
ATOM    997  ND2 ASN D 590      54.741  -6.164  56.253  1.00 64.79           N  
ANISOU  997  ND2 ASN D 590     9239   5512   9867    137    736   -777       N  
ATOM    998  N   LYS D 591      52.148  -3.070  57.801  1.00 39.27           N  
ANISOU  998  N   LYS D 591     6180   2450   6288   -217    103   -756       N  
ATOM    999  CA  LYS D 591      52.116  -1.946  56.875  1.00 47.56           C  
ANISOU  999  CA  LYS D 591     7354   3452   7266   -239     41   -823       C  
ATOM   1000  C   LYS D 591      51.164  -0.854  57.351  1.00 42.94           C  
ANISOU 1000  C   LYS D 591     6820   2936   6559   -360   -118   -815       C  
ATOM   1001  O   LYS D 591      50.596  -0.117  56.542  1.00 49.33           O  
ANISOU 1001  O   LYS D 591     7686   3765   7292   -409    -69   -824       O  
ATOM   1002  CB  LYS D 591      51.734  -2.417  55.473  1.00 56.34           C  
ANISOU 1002  CB  LYS D 591     8403   4602   8403   -189    201   -780       C  
ATOM   1003  CG  LYS D 591      52.863  -3.132  54.756  1.00 69.77           C  
ANISOU 1003  CG  LYS D 591    10146   6234  10127   -108    487   -816       C  
ATOM   1004  CD  LYS D 591      52.503  -3.472  53.324  1.00 78.94           C  
ANISOU 1004  CD  LYS D 591    11285   7414  11294    -99    675   -775       C  
ATOM   1005  CE  LYS D 591      53.712  -3.264  52.432  1.00 85.40           C  
ANISOU 1005  CE  LYS D 591    12336   8116  11995    -94    963   -875       C  
ATOM   1006  NZ  LYS D 591      53.754  -1.901  51.854  1.00 87.50           N  
ANISOU 1006  NZ  LYS D 591    12923   8315  12007   -210    900   -926       N  
ATOM   1007  N   LEU D 592      50.983  -0.741  58.662  1.00 59.83           N  
ANISOU 1007  N   LEU D 592     5131   6406  11198  -2669   -738   1555       N  
ATOM   1008  CA  LEU D 592      50.128   0.281  59.255  1.00 59.03           C  
ANISOU 1008  CA  LEU D 592     5129   6306  10992  -2670   -774   1564       C  
ATOM   1009  C   LEU D 592      51.015   1.423  59.732  1.00100.13           C  
ANISOU 1009  C   LEU D 592    10266  11586  16194  -2790   -624   1354       C  
ATOM   1010  O   LEU D 592      51.712   1.302  60.743  1.00 98.97           O  
ANISOU 1010  O   LEU D 592    10086  11302  16215  -2771   -484   1258       O  
ATOM   1011  CB  LEU D 592      49.300  -0.300  60.396  1.00 58.23           C  
ANISOU 1011  CB  LEU D 592     5143   5974  11006  -2521   -798   1681       C  
ATOM   1012  CG  LEU D 592      48.232  -1.305  59.969  1.00 57.23           C  
ANISOU 1012  CG  LEU D 592     5108   5783  10852  -2402   -964   1896       C  
ATOM   1013  CD1 LEU D 592      47.285  -1.590  61.099  1.00 56.41           C  
ANISOU 1013  CD1 LEU D 592     5134   5492  10807  -2273   -988   1989       C  
ATOM   1014  CD2 LEU D 592      47.463  -0.807  58.752  1.00 56.56           C  
ANISOU 1014  CD2 LEU D 592     5055   5893  10542  -2450  -1124   1977       C  
ATOM   1015  N   ASP D 593      50.995   2.528  58.988  1.00109.11           N  
ANISOU 1015  N   ASP D 593    11386  12936  17136  -2912   -656   1284       N  
ATOM   1016  CA  ASP D 593      51.702   3.737  59.385  1.00112.98           C  
ANISOU 1016  CA  ASP D 593    11825  13514  17589  -3035   -533   1094       C  
ATOM   1017  C   ASP D 593      51.107   4.281  60.676  1.00105.50           C  
ANISOU 1017  C   ASP D 593    10962  12432  16691  -2979   -508   1098       C  
ATOM   1018  O   ASP D 593      50.019   4.865  60.668  1.00103.69           O  
ANISOU 1018  O   ASP D 593    10822  12230  16347  -2952   -619   1180       O  
ATOM   1019  CB  ASP D 593      51.637   4.787  58.273  1.00115.81           C  
ANISOU 1019  CB  ASP D 593    12166  14117  17720  -3163   -595   1037       C  
ATOM   1020  CG  ASP D 593      52.692   4.573  57.206  1.00116.65           C  
ANISOU 1020  CG  ASP D 593    12154  14382  17787  -3271   -541    938       C  
ATOM   1021  OD1 ASP D 593      53.544   3.675  57.381  1.00118.94           O  
ANISOU 1021  OD1 ASP D 593    12362  14597  18234  -3254   -446    899       O  
ATOM   1022  OD2 ASP D 593      52.668   5.301  56.192  1.00116.24           O  
ANISOU 1022  OD2 ASP D 593    12090  14520  17554  -3365   -594    896       O  
ATOM   1023  N   VAL D 594      51.805   4.084  61.788  1.00105.03           N  
ANISOU 1023  N   VAL D 594    10877  12223  16807  -2954   -365   1010       N  
ATOM   1024  CA  VAL D 594      51.305   4.453  63.106  1.00104.00           C  
ANISOU 1024  CA  VAL D 594    10828  11946  16742  -2892   -326   1014       C  
ATOM   1025  C   VAL D 594      52.043   5.704  63.575  1.00104.85           C  
ANISOU 1025  C   VAL D 594    10887  12141  16810  -3018   -207    828       C  
ATOM   1026  O   VAL D 594      53.236   5.663  63.907  1.00105.95           O  
ANISOU 1026  O   VAL D 594    10946  12259  17053  -3067    -67    690       O  
ATOM   1027  CB  VAL D 594      51.427   3.293  64.107  1.00 98.95           C  
ANISOU 1027  CB  VAL D 594    10221  11054  16323  -2755   -264   1066       C  
ATOM   1028  CG1 VAL D 594      50.309   2.296  63.870  1.00 94.85           C  
ANISOU 1028  CG1 VAL D 594     9794  10442  15804  -2623   -408   1274       C  
ATOM   1029  CG2 VAL D 594      52.762   2.566  63.955  1.00 97.62           C  
ANISOU 1029  CG2 VAL D 594     9938  10846  16306  -2771   -148    968       C  
ATOM   1030  N   ARG D 595      51.339   6.831  63.579  1.00107.76           N  
ANISOU 1030  N   ARG D 595    11303  12609  17031  -3068   -267    822       N  
ATOM   1031  CA  ARG D 595      51.844   8.032  64.227  1.00110.53           C  
ANISOU 1031  CA  ARG D 595    11632  13016  17350  -3171   -167    669       C  
ATOM   1032  C   ARG D 595      51.480   7.977  65.705  1.00114.61           C  
ANISOU 1032  C   ARG D 595    12219  13334  17993  -3077   -108    686       C  
ATOM   1033  O   ARG D 595      50.347   7.637  66.059  1.00119.10           O  
ANISOU 1033  O   ARG D 595    12878  13799  18574  -2966   -194    820       O  
ATOM   1034  CB  ARG D 595      51.265   9.289  63.578  1.00108.38           C  
ANISOU 1034  CB  ARG D 595    11374  12932  16874  -3263   -255    647       C  
ATOM   1035  CG  ARG D 595      51.119   9.210  62.064  1.00107.18           C  
ANISOU 1035  CG  ARG D 595    11194  12945  16583  -3304   -365    689       C  
ATOM   1036  CD  ARG D 595      50.665  10.543  61.477  1.00104.27           C  
ANISOU 1036  CD  ARG D 595    10835  12742  16040  -3384   -440    644       C  
ATOM   1037  NE  ARG D 595      49.225  10.590  61.233  1.00 95.74           N  
ANISOU 1037  NE  ARG D 595     9850  11641  14888  -3282   -614    810       N  
ATOM   1038  CZ  ARG D 595      48.673  10.788  60.039  1.00 82.34           C  
ANISOU 1038  CZ  ARG D 595     8173  10067  13046  -3285   -760    887       C  
ATOM   1039  NH1 ARG D 595      49.441  10.956  58.970  1.00 74.01           N  
ANISOU 1039  NH1 ARG D 595     7051   9163  11907  -3381   -748    809       N  
ATOM   1040  NH2 ARG D 595      47.354  10.817  59.912  1.00 76.87           N  
ANISOU 1040  NH2 ARG D 595     7571   9344  12294  -3190   -920   1041       N  
ATOM   1041  N   ASP D 596      52.448   8.288  66.567  1.00114.76           N  
ANISOU 1041  N   ASP D 596    12199  13299  18104  -3120     38    549       N  
ATOM   1042  CA  ASP D 596      52.228   8.233  68.009  1.00113.37           C  
ANISOU 1042  CA  ASP D 596    12088  12934  18052  -3035    110    547       C  
ATOM   1043  C   ASP D 596      51.276   9.352  68.414  1.00110.58           C  
ANISOU 1043  C   ASP D 596    11797  12639  17582  -3063     54    561       C  
ATOM   1044  O   ASP D 596      51.650  10.529  68.415  1.00111.12           O  
ANISOU 1044  O   ASP D 596    11829  12840  17553  -3184     86    451       O  
ATOM   1045  CB  ASP D 596      53.556   8.340  68.753  1.00118.44           C  
ANISOU 1045  CB  ASP D 596    12671  13513  18816  -3073    276    388       C  
ATOM   1046  CG  ASP D 596      53.541   7.602  70.080  1.00120.94           C  
ANISOU 1046  CG  ASP D 596    13050  13581  19319  -2946    358    407       C  
ATOM   1047  OD1 ASP D 596      52.537   6.918  70.372  1.00119.79           O  
ANISOU 1047  OD1 ASP D 596    12992  13318  19204  -2832    285    550       O  
ATOM   1048  OD2 ASP D 596      54.536   7.705  70.830  1.00121.17           O  
ANISOU 1048  OD2 ASP D 596    13046  13535  19458  -2960    493    277       O  
ATOM   1049  N   THR D 597      50.044   8.984  68.750  1.00106.48           N  
ANISOU 1049  N   THR D 597    11367  12019  17070  -2951    -32    698       N  
ATOM   1050  CA  THR D 597      48.995   9.953  69.023  1.00 96.13           C  
ANISOU 1050  CA  THR D 597    10108  10760  15658  -2961   -102    725       C  
ATOM   1051  C   THR D 597      49.179  10.592  70.395  1.00 87.96           C  
ANISOU 1051  C   THR D 597     9094   9643  14684  -2974     10    635       C  
ATOM   1052  O   THR D 597      49.766  10.004  71.308  1.00 85.12           O  
ANISOU 1052  O   THR D 597     8746   9130  14464  -2924    121    600       O  
ATOM   1053  CB  THR D 597      47.622   9.288  68.947  1.00 93.48           C  
ANISOU 1053  CB  THR D 597     9860  10340  15318  -2831   -230    901       C  
ATOM   1054  OG1 THR D 597      47.343   8.635  70.190  1.00 96.28           O  
ANISOU 1054  OG1 THR D 597    10286  10493  15803  -2725   -165    941       O  
ATOM   1055  CG2 THR D 597      47.586   8.259  67.823  1.00 89.19           C  
ANISOU 1055  CG2 THR D 597     9307   9817  14763  -2785   -321   1008       C  
ATOM   1056  N   ALA D 598      48.659  11.811  70.531  1.00 79.35           N  
ANISOU 1056  N   ALA D 598     8007   8653  13488  -3039    -24    597       N  
ATOM   1057  CA  ALA D 598      48.729  12.574  71.777  1.00 76.03           C  
ANISOU 1057  CA  ALA D 598     7603   8181  13103  -3062     65    516       C  
ATOM   1058  C   ALA D 598      47.315  13.022  72.134  1.00 63.30           C  
ANISOU 1058  C   ALA D 598     6051   6552  11447  -3008    -21    595       C  
ATOM   1059  O   ALA D 598      46.785  13.963  71.536  1.00 61.07           O  
ANISOU 1059  O   ALA D 598     5749   6411  11044  -3066   -110    589       O  
ATOM   1060  CB  ALA D 598      49.675  13.763  71.644  1.00 76.19           C  
ANISOU 1060  CB  ALA D 598     7553   8355  13042  -3215    121    370       C  
ATOM   1061  N   TYR D 599      46.715  12.348  73.108  1.00 58.97           N  
ANISOU 1061  N   TYR D 599     5577   5831  10999  -2896      6    665       N  
ATOM   1062  CA  TYR D 599      45.354  12.519  73.600  1.00 59.97           C  
ANISOU 1062  CA  TYR D 599     5767   5907  11113  -2824    -62    749       C  
ATOM   1063  C   TYR D 599      45.293  13.613  74.664  1.00 66.64           C  
ANISOU 1063  C   TYR D 599     6605   6757  11957  -2879     12    653       C  
ATOM   1064  O   TYR D 599      46.201  13.723  75.495  1.00 71.42           O  
ANISOU 1064  O   TYR D 599     7199   7309  12627  -2916    139    558       O  
ATOM   1065  CB  TYR D 599      44.831  11.210  74.178  1.00 60.13           C  
ANISOU 1065  CB  TYR D 599     5874   5741  11232  -2686    -55    862       C  
ATOM   1066  CG  TYR D 599      44.729  10.099  73.159  1.00 61.82           C  
ANISOU 1066  CG  TYR D 599     6102   5943  11443  -2619   -145    976       C  
ATOM   1067  CD1 TYR D 599      44.249  10.352  71.880  1.00 67.12           C  
ANISOU 1067  CD1 TYR D 599     6745   6753  12004  -2640   -286   1037       C  
ATOM   1068  CD2 TYR D 599      45.121   8.802  73.467  1.00 67.91           C  
ANISOU 1068  CD2 TYR D 599     6917   6567  12320  -2535    -95   1026       C  
ATOM   1069  CE1 TYR D 599      44.151   9.345  70.941  1.00 73.54           C  
ANISOU 1069  CE1 TYR D 599     7571   7562  12809  -2581   -374   1146       C  
ATOM   1070  CE2 TYR D 599      45.027   7.784  72.532  1.00 73.65           C  
ANISOU 1070  CE2 TYR D 599     7653   7287  13045  -2474   -182   1134       C  
ATOM   1071  CZ  TYR D 599      44.539   8.061  71.271  1.00 75.11           C  
ANISOU 1071  CZ  TYR D 599     7807   7614  13115  -2500   -321   1195       C  
ATOM   1072  OH  TYR D 599      44.447   7.055  70.335  1.00 75.28           O  
ANISOU 1072  OH  TYR D 599     7839   7635  13130  -2442   -411   1306       O  
ATOM   1073  N   PRO D 600      44.236  14.423  74.652  1.00 65.45           N  
ANISOU 1073  N   PRO D 600     6459   6668  11742  -2883    -72    678       N  
ATOM   1074  CA  PRO D 600      44.117  15.499  75.641  1.00 76.19           C  
ANISOU 1074  CA  PRO D 600     7806   8041  13103  -2937    -10    590       C  
ATOM   1075  C   PRO D 600      43.777  14.965  77.024  1.00 83.16           C  
ANISOU 1075  C   PRO D 600     8757   8750  14091  -2858     81    611       C  
ATOM   1076  O   PRO D 600      43.223  13.875  77.189  1.00 86.56           O  
ANISOU 1076  O   PRO D 600     9258   9057  14576  -2750     63    714       O  
ATOM   1077  CB  PRO D 600      42.981  16.361  75.084  1.00 70.15           C  
ANISOU 1077  CB  PRO D 600     7022   7382  12250  -2944   -144    628       C  
ATOM   1078  CG  PRO D 600      42.135  15.394  74.330  1.00 57.25           C  
ANISOU 1078  CG  PRO D 600     5433   5705  10613  -2838   -264    773       C  
ATOM   1079  CD  PRO D 600      43.103  14.418  73.709  1.00 64.10           C  
ANISOU 1079  CD  PRO D 600     6299   6558  11498  -2834   -234    788       C  
ATOM   1080  N   GLU D 601      44.124  15.762  78.028  1.00 83.79           N  
ANISOU 1080  N   GLU D 601     8820   8825  14191  -2916    176    512       N  
ATOM   1081  CA  GLU D 601      43.916  15.407  79.433  1.00 90.35           C  
ANISOU 1081  CA  GLU D 601     9712   9504  15112  -2861    276    510       C  
ATOM   1082  C   GLU D 601      42.722  16.144  80.027  1.00 83.99           C  
ANISOU 1082  C   GLU D 601     8915   8709  14290  -2853    243    522       C  
ATOM   1083  O   GLU D 601      42.800  16.708  81.117  1.00 94.51           O  
ANISOU 1083  O   GLU D 601    10246  10011  15652  -2885    329    454       O  
ATOM   1084  CB  GLU D 601      45.180  15.688  80.239  1.00102.50           C  
ANISOU 1084  CB  GLU D 601    11230  11014  16700  -2923    411    392       C  
ATOM   1085  CG  GLU D 601      46.108  14.493  80.392  1.00103.40           C  
ANISOU 1085  CG  GLU D 601    11379  11004  16905  -2871    489    397       C  
ATOM   1086  CD  GLU D 601      47.315  14.797  81.259  1.00101.45           C  
ANISOU 1086  CD  GLU D 601    11111  10716  16719  -2923    622    276       C  
ATOM   1087  OE1 GLU D 601      47.571  15.990  81.531  1.00 98.97           O  
ANISOU 1087  OE1 GLU D 601    10746  10497  16361  -3012    644    187       O  
ATOM   1088  OE2 GLU D 601      48.007  13.843  81.672  1.00 99.55           O  
ANISOU 1088  OE2 GLU D 601    10906  10344  16575  -2871    699    271       O  
ATOM   1089  N   THR D 602      41.600  16.143  79.318  1.00 74.03           N  
ANISOU 1089  N   THR D 602     7656   7487  12983  -2808    116    610       N  
ATOM   1090  CA  THR D 602      40.395  16.793  79.804  1.00 58.41           C  
ANISOU 1090  CA  THR D 602     5676   5514  11003  -2792     75    624       C  
ATOM   1091  C   THR D 602      39.593  15.850  80.696  1.00 58.11           C  
ANISOU 1091  C   THR D 602     5729   5317  11034  -2690    114    702       C  
ATOM   1092  O   THR D 602      39.796  14.634  80.704  1.00 57.87           O  
ANISOU 1092  O   THR D 602     5769   5182  11036  -2619    136    770       O  
ATOM   1093  CB  THR D 602      39.529  17.270  78.640  1.00 70.93           C  
ANISOU 1093  CB  THR D 602     7222   7213  12516  -2786    -90    681       C  
ATOM   1094  OG1 THR D 602      38.292  17.784  79.146  1.00 75.87           O  
ANISOU 1094  OG1 THR D 602     7844   7823  13161  -2755   -133    701       O  
ATOM   1095  CG2 THR D 602      39.244  16.122  77.692  1.00 57.01           C  
ANISOU 1095  CG2 THR D 602     5506   5415  10742  -2700   -184    806       C  
ATOM   1096  N   ASN D 603      38.664  16.433  81.451  1.00 58.20           N  
ANISOU 1096  N   ASN D 603     5736   5314  11062  -2687    121    690       N  
ATOM   1097  CA  ASN D 603      37.875  15.686  82.420  1.00 60.20           C  
ANISOU 1097  CA  ASN D 603     6075   5429  11368  -2609    171    747       C  
ATOM   1098  C   ASN D 603      36.550  15.185  81.859  1.00 60.68           C  
ANISOU 1098  C   ASN D 603     6173   5467  11414  -2520     47    868       C  
ATOM   1099  O   ASN D 603      35.871  14.401  82.529  1.00 57.07           O  
ANISOU 1099  O   ASN D 603     5801   4896  10986  -2450     79    929       O  
ATOM   1100  CB  ASN D 603      37.610  16.553  83.657  1.00 66.11           C  
ANISOU 1100  CB  ASN D 603     6800   6169  12150  -2659    262    661       C  
ATOM   1101  CG  ASN D 603      37.752  15.780  84.955  1.00 67.57           C  
ANISOU 1101  CG  ASN D 603     7076   6210  12386  -2627    394    661       C  
ATOM   1102  OD1 ASN D 603      38.569  14.864  85.059  1.00 74.41           O  
ANISOU 1102  OD1 ASN D 603     8003   7000  13269  -2601    447    679       O  
ATOM   1103  ND2 ASN D 603      36.961  16.151  85.956  1.00 66.46           N  
ANISOU 1103  ND2 ASN D 603     6944   6034  12273  -2632    444    639       N  
ATOM   1104  N   ASP D 604      36.168  15.610  80.653  1.00 57.19           N  
ANISOU 1104  N   ASP D 604     5676   5132  10922  -2522    -98    906       N  
ATOM   1105  CA  ASP D 604      34.875  15.254  80.080  1.00 63.98           C  
ANISOU 1105  CA  ASP D 604     6562   5978  11767  -2440   -234   1021       C  
ATOM   1106  C   ASP D 604      35.009  14.442  78.795  1.00 65.94           C  
ANISOU 1106  C   ASP D 604     6837   6252  11965  -2389   -351   1124       C  
ATOM   1107  O   ASP D 604      34.038  14.321  78.039  1.00 63.95           O  
ANISOU 1107  O   ASP D 604     6593   6024  11682  -2333   -497   1219       O  
ATOM   1108  CB  ASP D 604      34.039  16.511  79.827  1.00 65.47           C  
ANISOU 1108  CB  ASP D 604     6665   6266  11944  -2475   -331    989       C  
ATOM   1109  CG  ASP D 604      34.875  17.683  79.350  1.00 68.57           C  
ANISOU 1109  CG  ASP D 604     6961   6802  12290  -2579   -342    886       C  
ATOM   1110  OD1 ASP D 604      36.027  17.460  78.921  1.00 71.54           O  
ANISOU 1110  OD1 ASP D 604     7335   7215  12632  -2621   -304    857       O  
ATOM   1111  OD2 ASP D 604      34.381  18.830  79.411  1.00 66.10           O  
ANISOU 1111  OD2 ASP D 604     6576   6567  11974  -2622   -389    831       O  
ATOM   1112  N   ALA D 605      36.185  13.879  78.531  1.00 45.92           N  
ANISOU 1112  N   ALA D 605     5774   4310   7365   -326   -644    147       N  
ATOM   1113  CA  ALA D 605      36.383  13.060  77.344  1.00 44.00           C  
ANISOU 1113  CA  ALA D 605     5561   4103   7053   -278   -615    126       C  
ATOM   1114  C   ALA D 605      37.493  12.055  77.603  1.00 51.73           C  
ANISOU 1114  C   ALA D 605     6640   5044   7972   -274   -565    120       C  
ATOM   1115  O   ALA D 605      38.537  12.405  78.162  1.00 59.37           O  
ANISOU 1115  O   ALA D 605     7686   5946   8924   -307   -575    118       O  
ATOM   1116  CB  ALA D 605      36.719  13.923  76.122  1.00 42.29           C  
ANISOU 1116  CB  ALA D 605     5366   3892   6809   -270   -671    106       C  
ATOM   1117  N   ILE D 606      37.257  10.812  77.197  1.00 42.19           N  
ANISOU 1117  N   ILE D 606     5428   3872   6730   -234   -512    119       N  
ATOM   1118  CA  ILE D 606      38.256   9.751  77.303  1.00 20.12           C  
ANISOU 1118  CA  ILE D 606     2720   1043   3882   -219   -464    116       C  
ATOM   1119  C   ILE D 606      38.507   9.185  75.911  1.00 23.83           C  
ANISOU 1119  C   ILE D 606     3210   1546   4300   -174   -445     97       C  
ATOM   1120  O   ILE D 606      37.577   9.114  75.100  1.00 37.66           O  
ANISOU 1120  O   ILE D 606     4891   3361   6056   -152   -451     94       O  
ATOM   1121  CB  ILE D 606      37.805   8.643  78.267  1.00 32.92           C  
ANISOU 1121  CB  ILE D 606     4325   2668   5515   -216   -418    140       C  
ATOM   1122  CG1 ILE D 606      36.303   8.399  78.120  1.00 45.70           C  
ANISOU 1122  CG1 ILE D 606     5840   4356   7167   -202   -409    152       C  
ATOM   1123  CG2 ILE D 606      38.164   9.002  79.700  1.00 38.47           C  
ANISOU 1123  CG2 ILE D 606     5062   3310   6246   -265   -421    155       C  
ATOM   1124  CD1 ILE D 606      35.791   7.233  78.931  1.00 55.19           C  
ANISOU 1124  CD1 ILE D 606     7035   5563   8370   -200   -361    175       C  
ATOM   1125  N   PRO D 607      39.735   8.794  75.584  1.00 19.83           N  
ANISOU 1125  N   PRO D 607     2797    992   3744   -160   -417     84       N  
ATOM   1126  CA  PRO D 607      39.973   8.111  74.307  1.00 48.13           C  
ANISOU 1126  CA  PRO D 607     6399   4604   7284   -116   -387     69       C  
ATOM   1127  C   PRO D 607      39.262   6.764  74.262  1.00 44.59           C  
ANISOU 1127  C   PRO D 607     5900   4206   6838    -84   -353     87       C  
ATOM   1128  O   PRO D 607      39.191   6.048  75.263  1.00 61.78           O  
ANISOU 1128  O   PRO D 607     8077   6367   9029    -88   -333    108       O  
ATOM   1129  CB  PRO D 607      41.495   7.950  74.278  1.00 20.01           C  
ANISOU 1129  CB  PRO D 607     2957    964   3683   -110   -352     56       C  
ATOM   1130  CG  PRO D 607      41.990   9.085  75.102  1.00 20.82           C  
ANISOU 1130  CG  PRO D 607     3100   1007   3802   -159   -386     52       C  
ATOM   1131  CD  PRO D 607      40.983   9.268  76.199  1.00 20.76           C  
ANISOU 1131  CD  PRO D 607     3013   1025   3849   -188   -417     77       C  
ATOM   1132  N   MET D 608      38.722   6.432  73.082  1.00 33.30           N  
ANISOU 1132  N   MET D 608     4428   2836   5390    -57   -348     79       N  
ATOM   1133  CA  MET D 608      37.921   5.217  72.942  1.00 27.95           C  
ANISOU 1133  CA  MET D 608     3695   2210   4715    -33   -323     97       C  
ATOM   1134  C   MET D 608      38.774   3.964  73.103  1.00 33.85           C  
ANISOU 1134  C   MET D 608     4498   2923   5440     -6   -282    108       C  
ATOM   1135  O   MET D 608      38.339   2.987  73.729  1.00 34.93           O  
ANISOU 1135  O   MET D 608     4611   3071   5589     -1   -267    132       O  
ATOM   1136  CB  MET D 608      37.206   5.207  71.588  1.00 16.64           C  
ANISOU 1136  CB  MET D 608     2212    844   3266    -16   -330     85       C  
ATOM   1137  CG  MET D 608      36.527   3.879  71.248  1.00 16.08           C  
ANISOU 1137  CG  MET D 608     2100    822   3189      7   -302    101       C  
ATOM   1138  SD  MET D 608      35.273   4.000  69.965  1.00 15.20           S  
ANISOU 1138  SD  MET D 608     1915    792   3068     12   -315     92       S  
ATOM   1139  CE  MET D 608      34.286   5.334  70.628  1.00 20.92           C  
ANISOU 1139  CE  MET D 608     2582   1528   3838    -17   -354     91       C  
ATOM   1140  N   ILE D 609      40.001   3.993  72.571  1.00 29.42           N  
ANISOU 1140  N   ILE D 609     4017   2313   4847     12   -263     91       N  
ATOM   1141  CA  ILE D 609      40.926   2.864  72.647  1.00 18.45           C  
ANISOU 1141  CA  ILE D 609     2687    882   3443     46   -224    101       C  
ATOM   1142  C   ILE D 609      41.206   2.468  74.095  1.00 26.40           C  
ANISOU 1142  C   ILE D 609     3724   1840   4468     33   -218    123       C  
ATOM   1143  O   ILE D 609      41.422   1.287  74.396  1.00 31.23           O  
ANISOU 1143  O   ILE D 609     4347   2438   5080     59   -198    144       O  
ATOM   1144  CB  ILE D 609      42.217   3.223  71.878  1.00 19.87           C  
ANISOU 1144  CB  ILE D 609     2960   1005   3586     66   -198     77       C  
ATOM   1145  CG1 ILE D 609      43.259   2.106  71.967  1.00 26.11           C  
ANISOU 1145  CG1 ILE D 609     3816   1741   4365    110   -156     87       C  
ATOM   1146  CG2 ILE D 609      42.779   4.563  72.345  1.00 23.90           C  
ANISOU 1146  CG2 ILE D 609     3528   1459   4092     29   -213     59       C  
ATOM   1147  CD1 ILE D 609      44.569   2.460  71.327  1.00 34.20           C  
ANISOU 1147  CD1 ILE D 609     4948   2694   5352    132   -118     63       C  
ATOM   1148  N   SER D 610      41.135   3.428  75.020  1.00 19.38           N  
ANISOU 1148  N   SER D 610     2844    924   3596     -9   -241    122       N  
ATOM   1149  CA  SER D 610      41.355   3.173  76.438  1.00 28.11           C  
ANISOU 1149  CA  SER D 610     3984   1980   4718    -30   -236    142       C  
ATOM   1150  C   SER D 610      40.261   2.327  77.079  1.00 23.02           C  
ANISOU 1150  C   SER D 610     3273   1377   4095    -35   -236    171       C  
ATOM   1151  O   SER D 610      40.438   1.887  78.220  1.00 26.77           O  
ANISOU 1151  O   SER D 610     3783   1810   4578    -50   -227    191       O  
ATOM   1152  CB  SER D 610      41.477   4.501  77.184  1.00 38.07           C  
ANISOU 1152  CB  SER D 610     5263   3205   5997    -81   -263    133       C  
ATOM   1153  OG  SER D 610      40.236   5.188  77.199  1.00 41.07           O  
ANISOU 1153  OG  SER D 610     5550   3644   6409   -107   -297    135       O  
ATOM   1154  N   LYS D 611      39.140   2.092  76.395  1.00 18.82           N  
ANISOU 1154  N   LYS D 611     2659    922   3571    -27   -243    173       N  
ATOM   1155  CA  LYS D 611      38.071   1.256  76.926  1.00 20.59           C  
ANISOU 1155  CA  LYS D 611     2833   1182   3809    -32   -236    200       C  
ATOM   1156  C   LYS D 611      37.979  -0.086  76.208  1.00 20.88           C  
ANISOU 1156  C   LYS D 611     2858   1248   3829      6   -220    213       C  
ATOM   1157  O   LYS D 611      36.942  -0.753  76.278  1.00 17.78           O  
ANISOU 1157  O   LYS D 611     2418    897   3439      3   -216    231       O  
ATOM   1158  CB  LYS D 611      36.732   1.993  76.849  1.00 27.18           C  
ANISOU 1158  CB  LYS D 611     3586   2073   4668    -55   -251    196       C  
ATOM   1159  CG  LYS D 611      36.591   3.139  77.840  1.00 36.78           C  
ANISOU 1159  CG  LYS D 611     4799   3259   5916    -98   -267    195       C  
ATOM   1160  CD  LYS D 611      36.664   2.644  79.278  1.00 53.55           C  
ANISOU 1160  CD  LYS D 611     6963   5334   8049   -123   -249    220       C  
ATOM   1161  CE  LYS D 611      36.520   3.792  80.267  1.00 57.97           C  
ANISOU 1161  CE  LYS D 611     7517   5863   8647   -171   -264    220       C  
ATOM   1162  NZ  LYS D 611      36.876   3.387  81.656  1.00 58.45           N  
ANISOU 1162  NZ  LYS D 611     7638   5862   8707   -203   -246    241       N  
ATOM   1163  N   LEU D 612      39.046  -0.499  75.527  1.00 22.35           N  
ANISOU 1163  N   LEU D 612     3089   1408   3996     41   -209    204       N  
ATOM   1164  CA  LEU D 612      39.037  -1.685  74.677  1.00 23.47           C  
ANISOU 1164  CA  LEU D 612     3211   1577   4129     78   -197    216       C  
ATOM   1165  C   LEU D 612      40.091  -2.667  75.174  1.00 28.14           C  
ANISOU 1165  C   LEU D 612     3867   2104   4720    107   -182    235       C  
ATOM   1166  O   LEU D 612      41.273  -2.320  75.261  1.00 21.89           O  
ANISOU 1166  O   LEU D 612     3147   1251   3921    122   -170    222       O  
ATOM   1167  CB  LEU D 612      39.301  -1.305  73.218  1.00 20.94           C  
ANISOU 1167  CB  LEU D 612     2878   1286   3793    100   -194    189       C  
ATOM   1168  CG  LEU D 612      38.103  -1.212  72.267  1.00 20.68           C  
ANISOU 1168  CG  LEU D 612     2767   1334   3757     92   -205    184       C  
ATOM   1169  CD1 LEU D 612      37.040  -0.257  72.791  1.00 16.57           C  
ANISOU 1169  CD1 LEU D 612     2204    844   3250     54   -225    179       C  
ATOM   1170  CD2 LEU D 612      38.563  -0.784  70.883  1.00 23.41           C  
ANISOU 1170  CD2 LEU D 612     3120   1694   4082    111   -199    157       C  
ATOM   1171  N   ARG D 613      39.662  -3.889  75.490  1.00 34.80           N  
ANISOU 1171  N   ARG D 613     4693   2957   5572    116   -183    267       N  
ATOM   1172  CA  ARG D 613      40.557  -4.944  75.966  1.00 40.11           C  
ANISOU 1172  CA  ARG D 613     5419   3570   6251    148   -175    291       C  
ATOM   1173  C   ARG D 613      40.923  -5.824  74.776  1.00 40.04           C  
ANISOU 1173  C   ARG D 613     5386   3580   6248    194   -168    296       C  
ATOM   1174  O   ARG D 613      40.125  -6.653  74.331  1.00 40.58           O  
ANISOU 1174  O   ARG D 613     5397   3697   6323    196   -178    316       O  
ATOM   1175  CB  ARG D 613      39.911  -5.764  77.077  1.00 45.78           C  
ANISOU 1175  CB  ARG D 613     6141   4279   6975    127   -184    327       C  
ATOM   1176  CG  ARG D 613      39.094  -4.957  78.070  1.00 54.13           C  
ANISOU 1176  CG  ARG D 613     7196   5341   8029     75   -187    325       C  
ATOM   1177  CD  ARG D 613      38.046  -5.815  78.779  1.00 59.48           C  
ANISOU 1177  CD  ARG D 613     7863   6033   8703     53   -191    358       C  
ATOM   1178  NE  ARG D 613      38.640  -6.792  79.692  1.00 65.88           N  
ANISOU 1178  NE  ARG D 613     8739   6779   9514     62   -191    390       N  
ATOM   1179  CZ  ARG D 613      38.822  -8.081  79.416  1.00 63.21           C  
ANISOU 1179  CZ  ARG D 613     8404   6434   9179     94   -200    419       C  
ATOM   1180  NH1 ARG D 613      38.450  -8.577  78.243  1.00 60.49           N  
ANISOU 1180  NH1 ARG D 613     7999   6145   8838    117   -209    420       N  
ATOM   1181  NH2 ARG D 613      39.374  -8.880  80.319  1.00 65.13           N  
ANISOU 1181  NH2 ARG D 613     8710   6611   9423    101   -203    449       N  
ATOM   1182  N   TYR D 614      42.140  -5.648  74.272  1.00 48.47           N  
ANISOU 1182  N   TYR D 614     6502   4602   7313    231   -150    279       N  
ATOM   1183  CA  TYR D 614      42.611  -6.360  73.094  1.00 42.07           C  
ANISOU 1183  CA  TYR D 614     5671   3802   6514    278   -137    280       C  
ATOM   1184  C   TYR D 614      44.065  -6.759  73.297  1.00 35.41           C  
ANISOU 1184  C   TYR D 614     4904   2872   5678    328   -118    283       C  
ATOM   1185  O   TYR D 614      44.764  -6.221  74.161  1.00 39.71           O  
ANISOU 1185  O   TYR D 614     5528   3351   6209    323   -111    275       O  
ATOM   1186  CB  TYR D 614      42.435  -5.507  71.825  1.00 35.80           C  
ANISOU 1186  CB  TYR D 614     4849   3053   5701    274   -128    245       C  
ATOM   1187  CG  TYR D 614      43.217  -4.208  71.840  1.00 27.90           C  
ANISOU 1187  CG  TYR D 614     3920   2007   4673    268   -115    209       C  
ATOM   1188  CD2 TYR D 614      44.494  -4.130  71.303  1.00 31.54           C  
ANISOU 1188  CD2 TYR D 614     4452   2409   5123    310    -88    192       C  
ATOM   1189  CD1 TYR D 614      42.668  -3.055  72.393  1.00 20.92           C  
ANISOU 1189  CD1 TYR D 614     3037   1136   3776    219   -130    194       C  
ATOM   1190  CE2 TYR D 614      45.206  -2.952  71.325  1.00 26.92           C  
ANISOU 1190  CE2 TYR D 614     3949   1774   4505    300    -76    160       C  
ATOM   1191  CE1 TYR D 614      43.375  -1.870  72.416  1.00 19.75           C  
ANISOU 1191  CE1 TYR D 614     2957    942   3604    207   -123    164       C  
ATOM   1192  CZ  TYR D 614      44.643  -1.826  71.879  1.00 20.36           C  
ANISOU 1192  CZ  TYR D 614     3116    957   3661    246    -94    148       C  
ATOM   1193  OH  TYR D 614      45.360  -0.655  71.895  1.00 20.75           O  
ANISOU 1193  OH  TYR D 614     3249    953   3681    231    -83    119       O  
ATOM   1194  N   ASN D 615      44.515  -7.714  72.488  1.00 29.08           N  
ANISOU 1194  N   ASN D 615     4078   2068   4901    377   -108    296       N  
ATOM   1195  CA  ASN D 615      45.890  -8.180  72.581  1.00 35.18           C  
ANISOU 1195  CA  ASN D 615     4918   2760   5690    436    -89    300       C  
ATOM   1196  C   ASN D 615      46.831  -7.108  72.037  1.00 34.02           C  
ANISOU 1196  C   ASN D 615     4843   2571   5511    451    -63    256       C  
ATOM   1197  O   ASN D 615      46.566  -6.532  70.976  1.00 39.88           O  
ANISOU 1197  O   ASN D 615     5556   3357   6238    442    -53    230       O  
ATOM   1198  CB  ASN D 615      46.053  -9.496  71.810  1.00 43.39           C  
ANISOU 1198  CB  ASN D 615     5898   3812   6775    485    -87    328       C  
ATOM   1199  CG  ASN D 615      47.456 -10.085  71.916  1.00 45.51           C  
ANISOU 1199  CG  ASN D 615     6224   3994   7072    554    -70    336       C  
ATOM   1200  OD1 ASN D 615      48.423  -9.544  71.381  1.00 41.37           O  
ANISOU 1200  OD1 ASN D 615     5753   3427   6538    588    -42    303       O  
ATOM   1201  ND2 ASN D 615      47.567 -11.206  72.621  1.00 47.47           N  
ANISOU 1201  ND2 ASN D 615     6468   4213   7357    578    -88    379       N  
ATOM   1202  N   PRO D 616      47.938  -6.824  72.734  1.00 27.23           N  
ANISOU 1202  N   PRO D 616     4088   1620   4637    473    -53    246       N  
ATOM   1203  CA  PRO D 616      48.790  -5.684  72.347  1.00 36.71           C  
ANISOU 1203  CA  PRO D 616     5380   2771   5797    476    -35    202       C  
ATOM   1204  C   PRO D 616      49.485  -5.842  71.003  1.00 42.92           C  
ANISOU 1204  C   PRO D 616     6166   3551   6592    528    -15    180       C  
ATOM   1205  O   PRO D 616      49.852  -4.820  70.406  1.00 57.02           O  
ANISOU 1205  O   PRO D 616     8008   5319   8337    519     -8    141       O  
ATOM   1206  CB  PRO D 616      49.812  -5.599  73.492  1.00 34.94           C  
ANISOU 1206  CB  PRO D 616     5274   2443   5558    490    -34    204       C  
ATOM   1207  CG  PRO D 616      49.192  -6.369  74.623  1.00 30.56           C  
ANISOU 1207  CG  PRO D 616     4682   1899   5029    471    -50    246       C  
ATOM   1208  CD  PRO D 616      48.410  -7.460  73.976  1.00 27.55           C  
ANISOU 1208  CD  PRO D 616     4183   1594   4692    487    -61    274       C  
ATOM   1209  N   ARG D 617      49.670  -7.074  70.510  1.00 37.76           N  
ANISOU 1209  N   ARG D 617     5449   2907   5993    580     -6    204       N  
ATOM   1210  CA  ARG D 617      50.197  -7.278  69.162  1.00 47.45           C  
ANISOU 1210  CA  ARG D 617     6650   4137   7242    625     21    185       C  
ATOM   1211  C   ARG D 617      49.320  -6.609  68.113  1.00 42.49           C  
ANISOU 1211  C   ARG D 617     5968   3590   6586    584     26    165       C  
ATOM   1212  O   ARG D 617      49.829  -6.087  67.115  1.00 45.66           O  
ANISOU 1212  O   ARG D 617     6397   3978   6972    600     46    131       O  
ATOM   1213  CB  ARG D 617      50.316  -8.773  68.859  1.00 62.12           C  
ANISOU 1213  CB  ARG D 617     8425   6006   9173    678     32    225       C  
ATOM   1214  CG  ARG D 617      51.088  -9.109  67.588  1.00 73.65           C  
ANISOU 1214  CG  ARG D 617     9858   7452  10673    734     74    210       C  
ATOM   1215  CD  ARG D 617      52.491  -8.533  67.609  1.00 79.85           C  
ANISOU 1215  CD  ARG D 617    10749   8140  11451    775     93    168       C  
ATOM   1216  NE  ARG D 617      53.249  -9.015  68.760  1.00 85.21           N  
ANISOU 1216  NE  ARG D 617    11488   8737  12150    810     77    186       N  
ATOM   1217  CZ  ARG D 617      54.262  -9.872  68.680  1.00 84.45           C  
ANISOU 1217  CZ  ARG D 617    11389   8579  12120    885    102    196       C  
ATOM   1218  NH1 ARG D 617      54.894 -10.259  69.780  1.00 79.38           N  
ANISOU 1218  NH1 ARG D 617    10810   7861  11491    914     81    211       N  
ATOM   1219  NH2 ARG D 617      54.646 -10.340  67.501  1.00 87.92           N  
ANISOU 1219  NH2 ARG D 617    11761   9031  12613    931    152    192       N  
ATOM   1220  N   PHE D 618      48.011  -6.587  68.338  1.00 44.69           N  
ANISOU 1220  N   PHE D 618     6176   3947   6857    532      4    184       N  
ATOM   1221  CA  PHE D 618      47.066  -5.947  67.438  1.00 38.96           C  
ANISOU 1221  CA  PHE D 618     5400   3298   6106    491      1    167       C  
ATOM   1222  C   PHE D 618      46.948  -4.444  67.679  1.00 34.69           C  
ANISOU 1222  C   PHE D 618     4927   2748   5506    445     -8    133       C  
ATOM   1223  O   PHE D 618      46.042  -3.822  67.113  1.00 33.39           O  
ANISOU 1223  O   PHE D 618     4720   2647   5320    406    -17    121       O  
ATOM   1224  CB  PHE D 618      45.680  -6.591  67.576  1.00 33.23           C  
ANISOU 1224  CB  PHE D 618     4569   2656   5401    455    -24    201       C  
ATOM   1225  CG  PHE D 618      45.678  -8.098  67.477  1.00 21.10           C  
ANISOU 1225  CG  PHE D 618     2968   1128   3921    490    -25    243       C  
ATOM   1226  CD1 PHE D 618      46.564  -8.774  66.648  1.00 21.78           C  
ANISOU 1226  CD1 PHE D 618     3046   1185   4045    548      6    246       C  
ATOM   1227  CD2 PHE D 618      44.780  -8.840  68.231  1.00 20.83           C  
ANISOU 1227  CD2 PHE D 618     2883   1126   3905    464    -57    281       C  
ATOM   1228  CE1 PHE D 618      46.550 -10.154  66.574  1.00 22.19           C  
ANISOU 1228  CE1 PHE D 618     3032   1242   4156    578      2    290       C  
ATOM   1229  CE2 PHE D 618      44.762 -10.220  68.158  1.00 21.22           C  
ANISOU 1229  CE2 PHE D 618     2880   1179   4005    492    -65    323       C  
ATOM   1230  CZ  PHE D 618      45.646 -10.877  67.330  1.00 21.91           C  
ANISOU 1230  CZ  PHE D 618     2952   1238   4134    549    -38    330       C  
ATOM   1231  N   ASP D 619      47.830  -3.854  68.498  1.00 31.30           N  
ANISOU 1231  N   ASP D 619     4603   2237   5053    448     -8    119       N  
ATOM   1232  CA  ASP D 619      47.716  -2.437  68.837  1.00 32.76           C  
ANISOU 1232  CA  ASP D 619     4853   2407   5187    398    -16     93       C  
ATOM   1233  C   ASP D 619      47.889  -1.527  67.629  1.00 38.90           C  
ANISOU 1233  C   ASP D 619     5669   3189   5923    393     -6     56       C  
ATOM   1234  O   ASP D 619      47.401  -0.391  67.648  1.00 53.24           O  
ANISOU 1234  O   ASP D 619     7500   5023   7706    343    -12     40       O  
ATOM   1235  CB  ASP D 619      48.738  -2.067  69.915  1.00 35.44           C  
ANISOU 1235  CB  ASP D 619     5312   2647   5506    401    -14     87       C  
ATOM   1236  CG  ASP D 619      48.346  -0.820  70.688  1.00 38.22           C  
ANISOU 1236  CG  ASP D 619     5697   2994   5830    334    -17     78       C  
ATOM   1237  OD1 ASP D 619      48.669   0.295  70.224  1.00 36.54           O  
ANISOU 1237  OD1 ASP D 619     5552   2757   5575    312     -4     48       O  
ATOM   1238  OD2 ASP D 619      47.709  -0.953  71.754  1.00 36.40           O  
ANISOU 1238  OD2 ASP D 619     5419   2784   5626    302    -33    102       O  
ATOM   1239  N   LYS D 620      48.565  -2.002  66.584  1.00 33.87           N  
ANISOU 1239  N   LYS D 620     5041   2533   5294    442      8     42       N  
ATOM   1240  CA  LYS D 620      48.661  -1.233  65.351  1.00 36.90           C  
ANISOU 1240  CA  LYS D 620     5457   2924   5639    436     11      7       C  
ATOM   1241  C   LYS D 620      47.310  -1.165  64.646  1.00 34.47           C  
ANISOU 1241  C   LYS D 620     5046   2719   5332    402     11     17       C  
ATOM   1242  O   LYS D 620      46.975  -0.142  64.036  1.00 28.30           O  
ANISOU 1242  O   LYS D 620     4294   1955   4505    370      6     -7       O  
ATOM   1243  CB  LYS D 620      49.720  -1.858  64.444  1.00 30.63           C  
ANISOU 1243  CB  LYS D 620     4674   2085   4877    496     27    -11       C  
ATOM   1244  CG  LYS D 620      51.124  -1.809  65.026  1.00 40.16           C  
ANISOU 1244  CG  LYS D 620     5977   3184   6099    530     14    -31       C  
ATOM   1245  CD  LYS D 620      52.181  -2.146  63.987  1.00 55.29           C  
ANISOU 1245  CD  LYS D 620     7885   5056   8065    581     44    -60       C  
ATOM   1246  CE  LYS D 620      52.471  -0.965  63.078  1.00 65.75           C  
ANISOU 1246  CE  LYS D 620     9262   6359   9361    552     22   -110       C  
ATOM   1247  NZ  LYS D 620      53.589  -1.243  62.132  1.00 72.89           N  
ANISOU 1247  NZ  LYS D 620    10155   7214  10324    596     84   -140       N  
ATOM   1248  N   ALA D 621      46.517  -2.236  64.737  1.00 32.63           N  
ANISOU 1248  N   ALA D 621     4698   2551   5148    407      9     51       N  
ATOM   1249  CA  ALA D 621      45.229  -2.281  64.051  1.00 31.93           C  
ANISOU 1249  CA  ALA D 621     4514   2556   5061    377     -2     59       C  
ATOM   1250  C   ALA D 621      44.220  -1.354  64.707  1.00 34.35           C  
ANISOU 1250  C   ALA D 621     4799   2903   5351    319    -34     58       C  
ATOM   1251  O   ALA D 621      43.589  -0.530  64.034  1.00 41.76           O  
ANISOU 1251  O   ALA D 621     5726   3881   6261    290    -44     40       O  
ATOM   1252  CB  ALA D 621      44.694  -3.712  64.027  1.00 28.73           C  
ANISOU 1252  CB  ALA D 621     4006   2198   4711    394     -2     98       C  
ATOM   1253  N   PHE D 622      44.058  -1.476  66.027  1.00 23.53           N  
ANISOU 1253  N   PHE D 622     3420   1520   4001    304    -51     77       N  
ATOM   1254  CA  PHE D 622      42.999  -0.756  66.724  1.00 28.45           C  
ANISOU 1254  CA  PHE D 622     3997   2186   4626    252    -85     79       C  
ATOM   1255  C   PHE D 622      43.244   0.749  66.704  1.00 37.37           C  
ANISOU 1255  C   PHE D 622     5191   3287   5721    222    -91     49       C  
ATOM   1256  O   PHE D 622      42.299   1.532  66.543  1.00 43.42           O  
ANISOU 1256  O   PHE D 622     5908   4105   6485    185   -120     41       O  
ATOM   1257  CB  PHE D 622      42.875  -1.278  68.156  1.00 28.79           C  
ANISOU 1257  CB  PHE D 622     4027   2213   4700    243    -99    107       C  
ATOM   1258  CG  PHE D 622      42.273  -2.659  68.250  1.00 21.48           C  
ANISOU 1258  CG  PHE D 622     3026   1328   3808    257   -104    141       C  
ATOM   1259  CD1 PHE D 622      43.013  -3.786  67.924  1.00 22.27           C  
ANISOU 1259  CD1 PHE D 622     3134   1400   3927    304    -82    157       C  
ATOM   1260  CD2 PHE D 622      40.964  -2.826  68.659  1.00 17.43           C  
ANISOU 1260  CD2 PHE D 622     2438    877   3308    223   -131    158       C  
ATOM   1261  CE1 PHE D 622      42.459  -5.050  68.007  1.00 18.43           C  
ANISOU 1261  CE1 PHE D 622     2581    948   3475    313    -90    192       C  
ATOM   1262  CE2 PHE D 622      40.408  -4.085  68.745  1.00 17.28           C  
ANISOU 1262  CE2 PHE D 622     2365    889   3314    231   -136    190       C  
ATOM   1263  CZ  PHE D 622      41.155  -5.200  68.419  1.00 17.78           C  
ANISOU 1263  CZ  PHE D 622     2436    924   3397    273   -118    209       C  
ATOM   1264  N   LYS D 623      44.510   1.167  66.812  1.00 38.26           N  
ANISOU 1264  N   LYS D 623     5416   3314   5807    236    -64     32       N  
ATOM   1265  CA  LYS D 623      44.848   2.579  66.662  1.00 38.85           C  
ANISOU 1265  CA  LYS D 623     5563   3352   5848    204    -60      4       C  
ATOM   1266  C   LYS D 623      44.527   3.092  65.263  1.00 36.10           C  
ANISOU 1266  C   LYS D 623     5210   3039   5469    200    -56    -18       C  
ATOM   1267  O   LYS D 623      44.252   4.285  65.088  1.00 35.35           O  
ANISOU 1267  O   LYS D 623     5123   2948   5362    160    -71    -36       O  
ATOM   1268  CB  LYS D 623      46.327   2.812  66.980  1.00 42.92           C  
ANISOU 1268  CB  LYS D 623     6218   3757   6333    221    -20    -10       C  
ATOM   1269  CG  LYS D 623      46.599   3.199  68.422  1.00 41.26           C  
ANISOU 1269  CG  LYS D 623     6036   3498   6142    191    -25     -1       C  
ATOM   1270  CD  LYS D 623      48.088   3.299  68.715  1.00 43.55           C  
ANISOU 1270  CD  LYS D 623     6455   3693   6400    207     21    -14       C  
ATOM   1271  CE  LYS D 623      48.341   3.623  70.181  1.00 44.38           C  
ANISOU 1271  CE  LYS D 623     6583   3748   6533    174     22     -3       C  
ATOM   1272  NZ  LYS D 623      49.634   4.337  70.378  1.00 46.93           N  
ANISOU 1272  NZ  LYS D 623     6996   3998   6839    157     83    -24       N  
ATOM   1273  N   HIS D 624      44.551   2.215  64.256  1.00 31.50           N  
ANISOU 1273  N   HIS D 624     4609   2481   4880    238    -40    -16       N  
ATOM   1274  CA  HIS D 624      44.133   2.639  62.927  1.00 30.81           C  
ANISOU 1274  CA  HIS D 624     4513   2431   4762    232    -37    -33       C  
ATOM   1275  C   HIS D 624      42.620   2.813  62.855  1.00 33.66           C  
ANISOU 1275  C   HIS D 624     4756   2886   5146    198    -80    -23       C  
ATOM   1276  O   HIS D 624      42.127   3.638  62.075  1.00 39.90           O  
ANISOU 1276  O   HIS D 624     5542   3705   5913    176    -94    -40       O  
ATOM   1277  CB  HIS D 624      44.614   1.637  61.874  1.00 37.33           C  
ANISOU 1277  CB  HIS D 624     5347   3254   5582    281    -12    -34       C  
ATOM   1278  CG  HIS D 624      44.027   1.857  60.513  1.00 43.30           C  
ANISOU 1278  CG  HIS D 624     6081   4059   6314    274    -11    -47       C  
ATOM   1279  ND1 HIS D 624      44.336   2.954  59.740  1.00 46.02           N  
ANISOU 1279  ND1 HIS D 624     6516   4370   6601    255      2    -77       N  
ATOM   1280  CD2 HIS D 624      43.144   1.125  59.793  1.00 44.41           C  
ANISOU 1280  CD2 HIS D 624     6126   4274   6475    278    -18    -33       C  
ATOM   1281  CE1 HIS D 624      43.672   2.888  58.599  1.00 47.51           C  
ANISOU 1281  CE1 HIS D 624     6665   4612   6776    251      0    -81       C  
ATOM   1282  NE2 HIS D 624      42.942   1.788  58.606  1.00 44.44           N  
ANISOU 1282  NE2 HIS D 624     6163   4290   6434    265    -13    -55       N  
ATOM   1283  N   VAL D 625      41.872   2.080  63.673  1.00 31.08           N  
ANISOU 1283  N   VAL D 625     4342   2605   4863    195   -105      4       N  
ATOM   1284  CA  VAL D 625      40.414   2.100  63.624  1.00 23.99           C  
ANISOU 1284  CA  VAL D 625     3342   1791   3982    169   -144     15       C  
ATOM   1285  C   VAL D 625      39.830   3.028  64.680  1.00 32.25           C  
ANISOU 1285  C   VAL D 625     4362   2845   5048    131   -187     15       C  
ATOM   1286  O   VAL D 625      39.012   3.895  64.372  1.00 39.94           O  
ANISOU 1286  O   VAL D 625     5300   3858   6018    106   -224      5       O  
ATOM   1287  CB  VAL D 625      39.854   0.667  63.766  1.00 15.62           C  
ANISOU 1287  CB  VAL D 625     2207    774   2953    184   -140     45       C  
ATOM   1288  CG1 VAL D 625      38.339   0.694  63.760  1.00 14.82           C  
ANISOU 1288  CG1 VAL D 625     2018    750   2863    156   -175     54       C  
ATOM   1289  CG2 VAL D 625      40.381  -0.223  62.653  1.00 15.71           C  
ANISOU 1289  CG2 VAL D 625     2230    782   2958    220   -105     46       C  
ATOM   1290  N   PHE D 626      40.247   2.865  65.936  1.00 28.54           N  
ANISOU 1290  N   PHE D 626     3909   2334   4602    128   -187     28       N  
ATOM   1291  CA  PHE D 626      39.664   3.604  67.046  1.00 30.60           C  
ANISOU 1291  CA  PHE D 626     4137   2600   4890     93   -226     33       C  
ATOM   1292  C   PHE D 626      40.588   4.673  67.612  1.00 33.35           C  
ANISOU 1292  C   PHE D 626     4564   2877   5231     74   -232     18       C  
ATOM   1293  O   PHE D 626      40.171   5.411  68.512  1.00 40.18           O  
ANISOU 1293  O   PHE D 626     5403   3740   6122     42   -269     22       O  
ATOM   1294  CB  PHE D 626      39.279   2.650  68.188  1.00 22.25           C  
ANISOU 1294  CB  PHE D 626     3037   1550   3866     94   -224     63       C  
ATOM   1295  CG  PHE D 626      38.447   1.472  67.762  1.00 15.77           C  
ANISOU 1295  CG  PHE D 626     2150    789   3053    108   -216     83       C  
ATOM   1296  CD2 PHE D 626      37.065   1.521  67.828  1.00 26.91           C  
ANISOU 1296  CD2 PHE D 626     3484   2263   4478     87   -239     92       C  
ATOM   1297  CD1 PHE D 626      39.050   0.288  67.368  1.00 15.95           C  
ANISOU 1297  CD1 PHE D 626     2190    798   3072    142   -184     95       C  
ATOM   1298  CE2 PHE D 626      36.303   0.430  67.453  1.00 27.08           C  
ANISOU 1298  CE2 PHE D 626     3456   2331   4500     95   -230    110       C  
ATOM   1299  CE1 PHE D 626      38.295  -0.806  67.000  1.00 16.49           C  
ANISOU 1299  CE1 PHE D 626     2198    916   3150    149   -182    116       C  
ATOM   1300  CZ  PHE D 626      36.919  -0.735  67.041  1.00 14.86           C  
ANISOU 1300  CZ  PHE D 626     1925    771   2949    124   -204    123       C  
ATOM   1301  N   GLY D 627      41.820   4.778  67.115  1.00 37.07           N  
ANISOU 1301  N   GLY D 627     4870   3328   5888   -398    -89    911       N  
ATOM   1302  CA  GLY D 627      42.847   5.559  67.783  1.00 43.61           C  
ANISOU 1302  CA  GLY D 627     5823   4083   6663   -419    -62    906       C  
ATOM   1303  C   GLY D 627      42.723   7.062  67.633  1.00 45.70           C  
ANISOU 1303  C   GLY D 627     6131   4330   6904   -483   -106    896       C  
ATOM   1304  O   GLY D 627      43.491   7.786  68.276  1.00 55.14           O  
ANISOU 1304  O   GLY D 627     7423   5458   8070   -508    -93    889       O  
ATOM   1305  N   LYS D 628      41.796   7.552  66.813  1.00 34.78           N  
ANISOU 1305  N   LYS D 628     4683   2993   5538   -509   -162    897       N  
ATOM   1306  CA  LYS D 628      41.641   8.988  66.636  1.00 38.66           C  
ANISOU 1306  CA  LYS D 628     5208   3467   6014   -560   -222    901       C  
ATOM   1307  C   LYS D 628      40.372   9.554  67.261  1.00 39.84           C  
ANISOU 1307  C   LYS D 628     5235   3672   6230   -551   -322    918       C  
ATOM   1308  O   LYS D 628      40.278  10.775  67.414  1.00 44.24           O  
ANISOU 1308  O   LYS D 628     5806   4212   6792   -588   -393    930       O  
ATOM   1309  CB  LYS D 628      41.671   9.355  65.143  1.00 48.67           C  
ANISOU 1309  CB  LYS D 628     6534   4718   7242   -602   -204    901       C  
ATOM   1310  CG  LYS D 628      42.321  10.708  64.859  1.00 62.31           C  
ANISOU 1310  CG  LYS D 628     8378   6378   8918   -656   -218    907       C  
ATOM   1311  CD  LYS D 628      42.169  11.122  63.401  1.00 75.47           C  
ANISOU 1311  CD  LYS D 628    10101   8023  10550   -693   -196    923       C  
ATOM   1312  CE  LYS D 628      42.783  12.496  63.152  1.00 80.73           C  
ANISOU 1312  CE  LYS D 628    10880   8623  11172   -739   -226    942       C  
ATOM   1313  NZ  LYS D 628      43.108  12.724  61.716  1.00 82.57           N  
ANISOU 1313  NZ  LYS D 628    11214   8800  11358   -770   -140    966       N  
ATOM   1314  N   THR D 629      39.409   8.720  67.637  1.00 41.87           N  
ANISOU 1314  N   THR D 629     5379   3987   6541   -503   -330    924       N  
ATOM   1315  CA  THR D 629      38.118   9.205  68.106  1.00 35.71           C  
ANISOU 1315  CA  THR D 629     4492   3249   5826   -491   -404    941       C  
ATOM   1316  C   THR D 629      38.047   9.208  69.630  1.00 42.19           C  
ANISOU 1316  C   THR D 629     5276   4065   6690   -469   -397    956       C  
ATOM   1317  O   THR D 629      38.700   8.408  70.306  1.00 34.69           O  
ANISOU 1317  O   THR D 629     4362   3094   5724   -444   -328    954       O  
ATOM   1318  CB  THR D 629      36.976   8.366  67.530  1.00 24.71           C  
ANISOU 1318  CB  THR D 629     3016   1904   4468   -459   -407    936       C  
ATOM   1319  OG1 THR D 629      36.723   7.249  68.389  1.00 21.27           O  
ANISOU 1319  OG1 THR D 629     2535   1491   4057   -410   -366    936       O  
ATOM   1320  CG2 THR D 629      37.338   7.869  66.136  1.00 23.49           C  
ANISOU 1320  CG2 THR D 629     2909   1740   4278   -479   -372    922       C  
ATOM   1321  N   LEU D 630      37.228  10.119  70.163  1.00 38.96           N  
ANISOU 1321  N   LEU D 630     4796   3665   6341   -477   -461    977       N  
ATOM   1322  CA  LEU D 630      37.115  10.371  71.595  1.00 32.41           C  
ANISOU 1322  CA  LEU D 630     3928   2816   5569   -470   -449   1000       C  
ATOM   1323  C   LEU D 630      35.670  10.213  72.051  1.00 22.86           C  
ANISOU 1323  C   LEU D 630     2607   1646   4433   -432   -454   1020       C  
ATOM   1324  O   LEU D 630      34.742  10.647  71.363  1.00 37.71           O  
ANISOU 1324  O   LEU D 630     4433   3553   6343   -431   -511   1023       O  
ATOM   1325  CB  LEU D 630      37.597  11.788  71.943  1.00 23.66           C  
ANISOU 1325  CB  LEU D 630     2844   1660   4487   -527   -518   1014       C  
ATOM   1326  CG  LEU D 630      38.980  12.269  71.500  1.00 24.18           C  
ANISOU 1326  CG  LEU D 630     3042   1667   4480   -581   -523    993       C  
ATOM   1327  CD1 LEU D 630      39.200  13.695  71.971  1.00 25.15           C  
ANISOU 1327  CD1 LEU D 630     3167   1741   4649   -640   -614   1011       C  
ATOM   1328  CD2 LEU D 630      40.066  11.367  72.053  1.00 31.74           C  
ANISOU 1328  CD2 LEU D 630     4090   2576   5392   -569   -416    974       C  
ATOM   1329  N   ILE D 631      35.485   9.600  73.218  1.00 22.68           N  
ANISOU 1329  N   ILE D 631     2566   1615   4438   -400   -383   1039       N  
ATOM   1330  CA  ILE D 631      34.184   9.520  73.872  1.00 22.70           C  
ANISOU 1330  CA  ILE D 631     2482   1633   4508   -366   -362   1064       C  
ATOM   1331  C   ILE D 631      34.017  10.773  74.721  1.00 25.65           C  
ANISOU 1331  C   ILE D 631     2798   1972   4976   -394   -393   1100       C  
ATOM   1332  O   ILE D 631      34.796  11.004  75.652  1.00 47.85           O  
ANISOU 1332  O   ILE D 631     5643   4734   7804   -418   -360   1117       O  
ATOM   1333  CB  ILE D 631      34.076   8.259  74.742  1.00 22.65           C  
ANISOU 1333  CB  ILE D 631     2506   1623   4477   -319   -259   1078       C  
ATOM   1334  CG1 ILE D 631      34.397   7.009  73.921  1.00 21.99           C  
ANISOU 1334  CG1 ILE D 631     2478   1565   4313   -294   -242   1048       C  
ATOM   1335  CG2 ILE D 631      32.689   8.175  75.372  1.00 22.78           C  
ANISOU 1335  CG2 ILE D 631     2459   1646   4550   -285   -220   1105       C  
ATOM   1336  CD1 ILE D 631      33.951   5.710  74.564  1.00 21.95           C  
ANISOU 1336  CD1 ILE D 631     2504   1560   4277   -237   -167   1068       C  
ATOM   1337  N   CYS D 632      33.004  11.577  74.410  1.00 32.87           N  
ANISOU 1337  N   CYS D 632     3626   2901   5961   -394   -455   1113       N  
ATOM   1338  CA  CYS D 632      32.739  12.810  75.135  1.00 35.36           C  
ANISOU 1338  CA  CYS D 632     3865   3182   6390   -417   -498   1154       C  
ATOM   1339  C   CYS D 632      31.427  12.712  75.906  1.00 33.91           C  
ANISOU 1339  C   CYS D 632     3587   2996   6300   -374   -432   1188       C  
ATOM   1340  O   CYS D 632      30.589  11.843  75.652  1.00 24.19           O  
ANISOU 1340  O   CYS D 632     2360   1793   5038   -331   -376   1173       O  
ATOM   1341  CB  CYS D 632      32.703  14.010  74.183  1.00 39.85           C  
ANISOU 1341  CB  CYS D 632     4411   3750   6979   -452   -632   1157       C  
ATOM   1342  SG  CYS D 632      34.198  14.208  73.186  1.00 45.63           S  
ANISOU 1342  SG  CYS D 632     5280   4472   7588   -506   -696   1122       S  
ATOM   1343  N   ARG D 633      31.260  13.633  76.859  1.00 32.07           N  
ANISOU 1343  N   ARG D 633     3276   2719   6190   -390   -435   1234       N  
ATOM   1344  CA  ARG D 633      30.129  13.547  77.780  1.00 32.94           C  
ANISOU 1344  CA  ARG D 633     3304   2814   6400   -350   -340   1276       C  
ATOM   1345  C   ARG D 633      28.831  13.988  77.114  1.00 30.85           C  
ANISOU 1345  C   ARG D 633     2956   2565   6199   -319   -380   1279       C  
ATOM   1346  O   ARG D 633      27.800  13.320  77.251  1.00 28.57           O  
ANISOU 1346  O   ARG D 633     2662   2283   5910   -272   -289   1278       O  
ATOM   1347  CB  ARG D 633      30.408  14.380  79.031  1.00 43.55           C  
ANISOU 1347  CB  ARG D 633     4582   4092   7873   -383   -316   1328       C  
ATOM   1348  CG  ARG D 633      29.498  14.048  80.201  1.00 51.20           C  
ANISOU 1348  CG  ARG D 633     5495   5032   8927   -343   -168   1379       C  
ATOM   1349  CD  ARG D 633      30.232  14.156  81.532  1.00 58.23           C  
ANISOU 1349  CD  ARG D 633     6398   5854   9875   -385    -86   1419       C  
ATOM   1350  NE  ARG D 633      30.809  15.479  81.748  1.00 69.16           N  
ANISOU 1350  NE  ARG D 633     7715   7185  11376   -457   -190   1433       N  
ATOM   1351  CZ  ARG D 633      31.867  15.717  82.518  1.00 71.60           C  
ANISOU 1351  CZ  ARG D 633     8070   7429  11708   -530   -174   1440       C  
ATOM   1352  NH1 ARG D 633      32.476  14.718  83.143  1.00 65.17           N  
ANISOU 1352  NH1 ARG D 633     7365   6589  10806   -532    -54   1439       N  
ATOM   1353  NH2 ARG D 633      32.317  16.957  82.663  1.00 81.76           N  
ANISOU 1353  NH2 ARG D 633     9299   8663  13104   -607   -282   1446       N  
ATOM   1354  N   SER D 634      28.858  15.109  76.396  1.00 32.41           N  
ANISOU 1354  N   SER D 634     3107   2760   6449   -347   -514   1284       N  
ATOM   1355  CA  SER D 634      27.686  15.610  75.693  1.00 38.88           C  
ANISOU 1355  CA  SER D 634     3857   3580   7335   -323   -560   1290       C  
ATOM   1356  C   SER D 634      28.112  16.100  74.317  1.00 38.30           C  
ANISOU 1356  C   SER D 634     3835   3525   7193   -356   -697   1266       C  
ATOM   1357  O   SER D 634      29.296  16.077  73.965  1.00 41.32           O  
ANISOU 1357  O   SER D 634     4301   3918   7479   -396   -749   1246       O  
ATOM   1358  CB  SER D 634      26.992  16.722  76.486  1.00 56.37           C  
ANISOU 1358  CB  SER D 634     5930   5747   9741   -314   -569   1354       C  
ATOM   1359  OG  SER D 634      27.681  17.951  76.341  1.00 66.18           O  
ANISOU 1359  OG  SER D 634     7137   6965  11044   -362   -717   1382       O  
ATOM   1360  N   MET D 635      27.135  16.560  73.534  1.00 37.36           N  
ANISOU 1360  N   MET D 635     3677   3396   7122   -343   -743   1270       N  
ATOM   1361  CA  MET D 635      27.419  16.907  72.147  1.00 45.95           C  
ANISOU 1361  CA  MET D 635     4835   4490   8132   -374   -849   1251       C  
ATOM   1362  C   MET D 635      28.155  18.238  72.024  1.00 55.97           C  
ANISOU 1362  C   MET D 635     6092   5735   9440   -424   -995   1292       C  
ATOM   1363  O   MET D 635      29.040  18.376  71.173  1.00 58.75           O  
ANISOU 1363  O   MET D 635     6548   6093   9681   -464  -1064   1275       O  
ATOM   1364  CB  MET D 635      26.133  16.932  71.325  1.00 46.08           C  
ANISOU 1364  CB  MET D 635     4840   4484   8185   -348   -842   1244       C  
ATOM   1365  CG  MET D 635      25.649  15.553  70.931  1.00 45.21           C  
ANISOU 1365  CG  MET D 635     4804   4390   7985   -318   -738   1188       C  
ATOM   1366  SD  MET D 635      25.198  15.492  69.191  1.00 45.87           S  
ANISOU 1366  SD  MET D 635     4978   4445   8005   -330   -784   1158       S  
ATOM   1367  CE  MET D 635      26.825  15.379  68.450  1.00 28.52           C  
ANISOU 1367  CE  MET D 635     2882   2287   5669   -382   -844   1145       C  
ATOM   1368  N   GLU D 636      27.803  19.222  72.857  1.00 57.74           N  
ANISOU 1368  N   GLU D 636     6196   5922   9822   -423  -1040   1347       N  
ATOM   1369  CA  GLU D 636      28.479  20.517  72.813  1.00 58.14           C  
ANISOU 1369  CA  GLU D 636     6233   5938   9920   -474  -1199   1388       C  
ATOM   1370  C   GLU D 636      29.938  20.392  73.237  1.00 56.94           C  
ANISOU 1370  C   GLU D 636     6172   5785   9676   -520  -1214   1371       C  
ATOM   1371  O   GLU D 636      30.829  21.024  72.644  1.00 61.49           O  
ANISOU 1371  O   GLU D 636     6839   6346  10180   -576  -1332   1372       O  
ATOM   1372  CB  GLU D 636      27.726  21.520  73.685  1.00 65.89           C  
ANISOU 1372  CB  GLU D 636     7047   6871  11118   -459  -1240   1454       C  
ATOM   1373  CG  GLU D 636      27.151  20.920  74.956  1.00 75.02           C  
ANISOU 1373  CG  GLU D 636     8110   8022  12374   -410  -1079   1464       C  
ATOM   1374  CD  GLU D 636      26.138  21.830  75.622  1.00 82.83           C  
ANISOU 1374  CD  GLU D 636     8923   8957  13593   -381  -1088   1530       C  
ATOM   1375  OE1 GLU D 636      26.053  23.014  75.231  1.00 83.37           O  
ANISOU 1375  OE1 GLU D 636     8887   8975  13814   -406  -1273   1598       O  
ATOM   1376  OE2 GLU D 636      25.422  21.359  76.530  1.00 85.19           O  
ANISOU 1376  OE2 GLU D 636     9136   9240  13991   -334   -939   1548       O  
ATOM   1377  N   VAL D 637      30.198  19.551  74.243  1.00 54.24           N  
ANISOU 1377  N   VAL D 637     5827   5452   9331   -503  -1084   1354       N  
ATOM   1378  CA  VAL D 637      31.565  19.224  74.633  1.00 44.95           C  
ANISOU 1378  CA  VAL D 637     4756   4265   8060   -549  -1063   1326       C  
ATOM   1379  C   VAL D 637      32.325  18.622  73.458  1.00 41.31           C  
ANISOU 1379  C   VAL D 637     4444   3838   7414   -566  -1069   1274       C  
ATOM   1380  O   VAL D 637      33.477  18.984  73.193  1.00 45.07           O  
ANISOU 1380  O   VAL D 637     5024   4289   7810   -622  -1130   1259       O  
ATOM   1381  CB  VAL D 637      31.550  18.272  75.845  1.00 46.84           C  
ANISOU 1381  CB  VAL D 637     4974   4500   8322   -523   -900   1319       C  
ATOM   1382  CG1 VAL D 637      32.963  17.859  76.228  1.00 54.91           C  
ANISOU 1382  CG1 VAL D 637     6116   5499   9247   -573   -864   1286       C  
ATOM   1383  CG2 VAL D 637      30.842  18.924  77.023  1.00 55.94           C  
ANISOU 1383  CG2 VAL D 637     5984   5605   9667   -513   -875   1377       C  
ATOM   1384  N   SER D 638      31.672  17.733  72.706  1.00 42.20           N  
ANISOU 1384  N   SER D 638     4572   3997   7464   -522  -1002   1245       N  
ATOM   1385  CA  SER D 638      32.377  17.046  71.632  1.00 34.51           C  
ANISOU 1385  CA  SER D 638     3730   3049   6335   -535   -984   1198       C  
ATOM   1386  C   SER D 638      32.639  17.965  70.447  1.00 34.78           C  
ANISOU 1386  C   SER D 638     3833   3064   6319   -578  -1104   1210       C  
ATOM   1387  O   SER D 638      33.691  17.850  69.815  1.00 42.88           O  
ANISOU 1387  O   SER D 638     4985   4081   7226   -615  -1108   1185       O  
ATOM   1388  CB  SER D 638      31.602  15.812  71.183  1.00 33.42           C  
ANISOU 1388  CB  SER D 638     3590   2952   6157   -484   -883   1165       C  
ATOM   1389  OG  SER D 638      30.245  16.111  70.959  1.00 41.46           O  
ANISOU 1389  OG  SER D 638     4523   3967   7264   -453   -897   1184       O  
ATOM   1390  N   THR D 639      31.718  18.883  70.127  1.00 30.69           N  
ANISOU 1390  N   THR D 639     3243   2527   5890   -575  -1193   1251       N  
ATOM   1391  CA  THR D 639      32.024  19.813  69.043  1.00 34.37           C  
ANISOU 1391  CA  THR D 639     3794   2962   6302   -621  -1311   1271       C  
ATOM   1392  C   THR D 639      33.031  20.877  69.454  1.00 33.24           C  
ANISOU 1392  C   THR D 639     3693   2776   6160   -682  -1432   1296       C  
ATOM   1393  O   THR D 639      33.655  21.483  68.578  1.00 31.29           O  
ANISOU 1393  O   THR D 639     3569   2498   5821   -731  -1515   1303       O  
ATOM   1394  CB  THR D 639      30.770  20.504  68.485  1.00 44.63           C  
ANISOU 1394  CB  THR D 639     5025   4238   7693   -604  -1374   1310       C  
ATOM   1395  OG1 THR D 639      31.173  21.611  67.670  1.00 54.49           O  
ANISOU 1395  OG1 THR D 639     6363   5440   8902   -655  -1508   1345       O  
ATOM   1396  CG2 THR D 639      29.908  21.042  69.570  1.00 48.76           C  
ANISOU 1396  CG2 THR D 639     5381   4749   8398   -576  -1399   1349       C  
ATOM   1397  N   GLN D 640      33.208  21.123  70.754  1.00 34.79           N  
ANISOU 1397  N   GLN D 640     3805   2957   6458   -686  -1440   1311       N  
ATOM   1398  CA  GLN D 640      34.354  21.928  71.168  1.00 39.36           C  
ANISOU 1398  CA  GLN D 640     4453   3482   7020   -755  -1538   1317       C  
ATOM   1399  C   GLN D 640      35.658  21.151  70.987  1.00 38.46           C  
ANISOU 1399  C   GLN D 640     4497   3367   6749   -785  -1448   1258       C  
ATOM   1400  O   GLN D 640      36.605  21.635  70.345  1.00 35.46           O  
ANISOU 1400  O   GLN D 640     4259   2950   6262   -843  -1514   1246       O  
ATOM   1401  CB  GLN D 640      34.179  22.381  72.619  1.00 48.52           C  
ANISOU 1401  CB  GLN D 640     5482   4606   8348   -759  -1552   1348       C  
ATOM   1402  CG  GLN D 640      35.471  22.737  73.340  1.00 64.36           C  
ANISOU 1402  CG  GLN D 640     7569   6550  10336   -835  -1580   1328       C  
ATOM   1403  CD  GLN D 640      35.291  22.764  74.844  1.00 78.51           C  
ANISOU 1403  CD  GLN D 640     9240   8304  12287   -840  -1517   1343       C  
ATOM   1404  OE1 GLN D 640      34.165  22.770  75.342  1.00 85.44           O  
ANISOU 1404  OE1 GLN D 640     9964   9195  13304   -784  -1481   1384       O  
ATOM   1405  NE2 GLN D 640      36.400  22.777  75.575  1.00 76.40           N  
ANISOU 1405  NE2 GLN D 640     9048   7979  12004   -913  -1488   1306       N  
ATOM   1406  N   LEU D 641      35.705  19.922  71.520  1.00 40.23           N  
ANISOU 1406  N   LEU D 641     4705   3624   6957   -745  -1290   1222       N  
ATOM   1407  CA  LEU D 641      36.937  19.129  71.519  1.00 27.95           C  
ANISOU 1407  CA  LEU D 641     3283   2056   5282   -767  -1191   1168       C  
ATOM   1408  C   LEU D 641      37.372  18.730  70.112  1.00 38.15           C  
ANISOU 1408  C   LEU D 641     4704   3363   6427   -770  -1164   1140       C  
ATOM   1409  O   LEU D 641      38.575  18.682  69.825  1.00 45.89           O  
ANISOU 1409  O   LEU D 641     5826   4302   7307   -812  -1137   1109       O  
ATOM   1410  CB  LEU D 641      36.760  17.881  72.390  1.00 27.25           C  
ANISOU 1410  CB  LEU D 641     3142   1994   5217   -716  -1038   1147       C  
ATOM   1411  CG  LEU D 641      37.027  17.857  73.903  1.00 27.93           C  
ANISOU 1411  CG  LEU D 641     3182   2035   5395   -732   -985   1155       C  
ATOM   1412  CD1 LEU D 641      38.516  17.965  74.144  1.00 28.62           C  
ANISOU 1412  CD1 LEU D 641     3410   2051   5414   -800   -968   1118       C  
ATOM   1413  CD2 LEU D 641      36.320  18.959  74.667  1.00 28.96           C  
ANISOU 1413  CD2 LEU D 641     3181   2137   5687   -748  -1076   1207       C  
ATOM   1414  N   ALA D 642      36.417  18.435  69.221  1.00 36.24           N  
ANISOU 1414  N   ALA D 642     4424   3166   6180   -729  -1154   1150       N  
ATOM   1415  CA  ALA D 642      36.758  17.896  67.907  1.00 26.43           C  
ANISOU 1415  CA  ALA D 642     3295   1929   4816   -731  -1094   1126       C  
ATOM   1416  C   ALA D 642      37.463  18.930  67.043  1.00 27.35           C  
ANISOU 1416  C   ALA D 642     3549   1991   4852   -793  -1183   1144       C  
ATOM   1417  O   ALA D 642      38.382  18.594  66.289  1.00 27.38           O  
ANISOU 1417  O   ALA D 642     3692   1968   4743   -814  -1112   1119       O  
ATOM   1418  CB  ALA D 642      35.499  17.391  67.203  1.00 25.86           C  
ANISOU 1418  CB  ALA D 642     3151   1898   4775   -683  -1063   1133       C  
ATOM   1419  N   ARG D 643      37.049  20.191  67.134  1.00 30.74           N  
ANISOU 1419  N   ARG D 643     3946   2394   5340   -820  -1336   1191       N  
ATOM   1420  CA  ARG D 643      37.763  21.229  66.404  1.00 45.04           C  
ANISOU 1420  CA  ARG D 643     5904   4143   7065   -882  -1440   1212       C  
ATOM   1421  C   ARG D 643      39.021  21.653  67.147  1.00 46.17           C  
ANISOU 1421  C   ARG D 643     6132   4234   7177   -940  -1482   1188       C  
ATOM   1422  O   ARG D 643      40.042  21.942  66.510  1.00 42.14           O  
ANISOU 1422  O   ARG D 643     5795   3670   6545   -987  -1486   1174       O  
ATOM   1423  CB  ARG D 643      36.854  22.434  66.157  1.00 55.08           C  
ANISOU 1423  CB  ARG D 643     7122   5395   8412   -891  -1605   1275       C  
ATOM   1424  CG  ARG D 643      37.490  23.553  65.325  1.00 59.96           C  
ANISOU 1424  CG  ARG D 643     7910   5941   8931   -950  -1730   1308       C  
ATOM   1425  CD  ARG D 643      38.125  23.035  64.028  1.00 52.14           C  
ANISOU 1425  CD  ARG D 643     7102   4929   7779   -955  -1606   1294       C  
ATOM   1426  NE  ARG D 643      37.215  22.215  63.231  1.00 41.37           N  
ANISOU 1426  NE  ARG D 643     5692   3599   6427   -901  -1481   1298       N  
ATOM   1427  CZ  ARG D 643      36.264  22.702  62.442  1.00 41.23           C  
ANISOU 1427  CZ  ARG D 643     5674   3558   6435   -883  -1523   1351       C  
ATOM   1428  NH1 ARG D 643      35.482  21.880  61.758  1.00 49.74           N  
ANISOU 1428  NH1 ARG D 643     6718   4652   7528   -841  -1400   1346       N  
ATOM   1429  NH2 ARG D 643      36.106  24.013  62.317  1.00 45.44           N  
ANISOU 1429  NH2 ARG D 643     6250   4037   6980   -906  -1691   1410       N  
ATOM   1430  N   ALA D 644      38.967  21.682  68.488  1.00 50.87           N  
ANISOU 1430  N   ALA D 644     6614   4830   7883   -940  -1499   1182       N  
ATOM   1431  CA  ALA D 644      40.113  22.128  69.279  1.00 58.45           C  
ANISOU 1431  CA  ALA D 644     7651   5721   8837  -1006  -1536   1154       C  
ATOM   1432  C   ALA D 644      41.338  21.256  69.025  1.00 50.51           C  
ANISOU 1432  C   ALA D 644     6796   4688   7708  -1017  -1384   1092       C  
ATOM   1433  O   ALA D 644      42.409  21.759  68.663  1.00 50.97           O  
ANISOU 1433  O   ALA D 644     7017   4675   7673  -1077  -1419   1068       O  
ATOM   1434  CB  ALA D 644      39.751  22.137  70.765  1.00 70.17           C  
ANISOU 1434  CB  ALA D 644     8981   7202  10477  -1001  -1533   1160       C  
ATOM   1435  N   PHE D 645      41.195  19.946  69.189  1.00 43.93           N  
ANISOU 1435  N   PHE D 645     5915   3901   6875   -956  -1216   1066       N  
ATOM   1436  CA  PHE D 645      42.214  18.984  68.794  1.00 49.75           C  
ANISOU 1436  CA  PHE D 645     6776   4614   7512   -947  -1058   1016       C  
ATOM   1437  C   PHE D 645      41.629  18.161  67.660  1.00 54.53           C  
ANISOU 1437  C   PHE D 645     7370   5281   8068   -891   -972   1024       C  
ATOM   1438  O   PHE D 645      40.604  17.497  67.849  1.00 66.65           O  
ANISOU 1438  O   PHE D 645     8772   6885   9666   -834   -940   1034       O  
ATOM   1439  CB  PHE D 645      42.648  18.086  69.961  1.00 52.39           C  
ANISOU 1439  CB  PHE D 645     7079   4932   7894   -927   -935    981       C  
ATOM   1440  CG  PHE D 645      42.695  18.787  71.296  1.00 55.69           C  
ANISOU 1440  CG  PHE D 645     7438   5304   8418   -974  -1009    986       C  
ATOM   1441  CD2 PHE D 645      43.900  19.251  71.793  1.00 67.70           C  
ANISOU 1441  CD2 PHE D 645     9076   6720   9926  -1049  -1013    945       C  
ATOM   1442  CD1 PHE D 645      41.553  18.931  72.075  1.00 46.92           C  
ANISOU 1442  CD1 PHE D 645     6157   4241   7432   -946  -1056   1027       C  
ATOM   1443  CE2 PHE D 645      43.963  19.889  73.017  1.00 69.72           C  
ANISOU 1443  CE2 PHE D 645     9276   6920  10294  -1107  -1072    942       C  
ATOM   1444  CE1 PHE D 645      41.608  19.570  73.293  1.00 50.21           C  
ANISOU 1444  CE1 PHE D 645     6513   4602   7963   -996  -1105   1035       C  
ATOM   1445  CZ  PHE D 645      42.814  20.045  73.769  1.00 63.53           C  
ANISOU 1445  CZ  PHE D 645     8314   6185   9639  -1082  -1114    991       C  
ATOM   1446  N   THR D 646      42.260  18.232  66.484  1.00 50.76           N  
ANISOU 1446  N   THR D 646     7033   4768   7485   -910   -931   1020       N  
ATOM   1447  CA  THR D 646      41.733  17.624  65.264  1.00 42.43           C  
ANISOU 1447  CA  THR D 646     5980   3748   6392   -874   -851   1034       C  
ATOM   1448  C   THR D 646      41.534  16.121  65.410  1.00 37.04           C  
ANISOU 1448  C   THR D 646     5224   3114   5736   -815   -705   1003       C  
ATOM   1449  O   THR D 646      42.387  15.320  65.013  1.00 40.25           O  
ANISOU 1449  O   THR D 646     5712   3489   6092   -805   -567    976       O  
ATOM   1450  CB  THR D 646      42.646  17.920  64.073  1.00 39.95           C  
ANISOU 1450  CB  THR D 646     5845   3367   5968   -907   -798   1042       C  
ATOM   1451  OG1 THR D 646      43.952  17.382  64.315  1.00 49.17           O  
ANISOU 1451  OG1 THR D 646     7106   4478   7099   -912   -676   1000       O  
ATOM   1452  CG2 THR D 646      42.730  19.411  63.819  1.00 30.73           C  
ANISOU 1452  CG2 THR D 646     4766   2153   4756   -964   -968   1081       C  
ATOM   1453  N   MET D 647      40.393  15.749  65.982  1.00 37.20           N  
ANISOU 1453  N   MET D 647     5092   3203   5840   -773   -739   1011       N  
ATOM   1454  CA  MET D 647      40.048  14.368  66.268  1.00 35.89           C  
ANISOU 1454  CA  MET D 647     4846   3086   5703   -716   -638    987       C  
ATOM   1455  C   MET D 647      38.549  14.204  66.091  1.00 33.75           C  
ANISOU 1455  C   MET D 647     4442   2879   5502   -679   -686   1007       C  
ATOM   1456  O   MET D 647      37.780  15.140  66.327  1.00 26.30           O  
ANISOU 1456  O   MET D 647     3435   1943   4615   -687   -795   1039       O  
ATOM   1457  CB  MET D 647      40.442  13.975  67.695  1.00 26.37           C  
ANISOU 1457  CB  MET D 647     3605   1876   4540   -699   -610    970       C  
ATOM   1458  CG  MET D 647      41.910  13.670  67.892  1.00 33.63           C  
ANISOU 1458  CG  MET D 647     4657   2722   5399   -718   -514    939       C  
ATOM   1459  SD  MET D 647      42.246  13.184  69.593  1.00 27.87           S  
ANISOU 1459  SD  MET D 647     3895   1968   4727   -700   -470    928       S  
ATOM   1460  CE  MET D 647      44.036  13.187  69.590  1.00 38.54           C  
ANISOU 1460  CE  MET D 647     5437   3199   6009   -735   -368    891       C  
ATOM   1461  N   ASP D 648      38.138  13.011  65.678  1.00 28.46           N  
ANISOU 1461  N   ASP D 648     3733   2246   4836   -641   -606    989       N  
ATOM   1462  CA  ASP D 648      36.721  12.684  65.698  1.00 28.29           C  
ANISOU 1462  CA  ASP D 648     3589   2274   4888   -602   -636    998       C  
ATOM   1463  C   ASP D 648      36.244  12.556  67.140  1.00 30.35           C  
ANISOU 1463  C   ASP D 648     3744   2564   5223   -566   -655   1002       C  
ATOM   1464  O   ASP D 648      37.022  12.269  68.052  1.00 37.09           O  
ANISOU 1464  O   ASP D 648     4618   3405   6068   -562   -615    992       O  
ATOM   1465  CB  ASP D 648      36.455  11.392  64.926  1.00 31.23           C  
ANISOU 1465  CB  ASP D 648     3951   2666   5250   -578   -554    975       C  
ATOM   1466  CG  ASP D 648      37.090  11.396  63.548  1.00 38.48           C  
ANISOU 1466  CG  ASP D 648     4980   3540   6102   -620   -499    974       C  
ATOM   1467  OD1 ASP D 648      38.170  12.003  63.392  1.00 42.78           O  
ANISOU 1467  OD1 ASP D 648     5635   4037   6581   -656   -480    978       O  
ATOM   1468  OD2 ASP D 648      36.506  10.799  62.619  1.00 41.91           O  
ANISOU 1468  OD2 ASP D 648     5399   3975   6551   -621   -464    970       O  
ATOM   1469  N   CYS D 649      34.955  12.803  67.349  1.00 29.78           N  
ANISOU 1469  N   CYS D 649     3570   2516   5229   -540   -702   1021       N  
ATOM   1470  CA  CYS D 649      34.364  12.708  68.674  1.00 22.93           C  
ANISOU 1470  CA  CYS D 649     2605   1666   4442   -506   -697   1032       C  
ATOM   1471  C   CYS D 649      33.014  12.022  68.566  1.00 22.49           C  
ANISOU 1471  C   CYS D 649     2471   1640   4436   -461   -670   1026       C  
ATOM   1472  O   CYS D 649      32.405  11.976  67.494  1.00 30.58           O  
ANISOU 1472  O   CYS D 649     3504   2661   5454   -464   -686   1020       O  
ATOM   1473  CB  CYS D 649      34.210  14.084  69.330  1.00 27.97           C  
ANISOU 1473  CB  CYS D 649     3198   2279   5150   -531   -788   1070       C  
ATOM   1474  SG  CYS D 649      35.763  14.871  69.801  1.00 31.12           S  
ANISOU 1474  SG  CYS D 649     3692   2625   5506   -592   -823   1073       S  
ATOM   1475  N   ILE D 650      32.549  11.491  69.694  1.00 22.29           N  
ANISOU 1475  N   ILE D 650     2384   1628   4459   -424   -621   1029       N  
ATOM   1476  CA  ILE D 650      31.309  10.727  69.731  1.00 21.96           C  
ANISOU 1476  CA  ILE D 650     2291   1601   4452   -383   -580   1018       C  
ATOM   1477  C   ILE D 650      30.837  10.667  71.178  1.00 22.14           C  
ANISOU 1477  C   ILE D 650     2256   1620   4537   -354   -530   1042       C  
ATOM   1478  O   ILE D 650      31.645  10.545  72.102  1.00 22.97           O  
ANISOU 1478  O   ILE D 650     2379   1718   4632   -357   -491   1054       O  
ATOM   1479  CB  ILE D 650      31.513   9.318  69.119  1.00 21.39           C  
ANISOU 1479  CB  ILE D 650     2267   1546   4314   -370   -528    982       C  
ATOM   1480  CG1 ILE D 650      30.251   8.470  69.227  1.00 28.82           C  
ANISOU 1480  CG1 ILE D 650     3178   2489   5284   -334   -493    966       C  
ATOM   1481  CG2 ILE D 650      32.693   8.603  69.762  1.00 21.20           C  
ANISOU 1481  CG2 ILE D 650     2288   1528   4239   -364   -473    978       C  
ATOM   1482  CD1 ILE D 650      30.342   7.204  68.454  1.00 32.53           C  
ANISOU 1482  CD1 ILE D 650     3687   2965   5709   -331   -471    933       C  
ATOM   1483  N   THR D 651      29.527  10.790  71.375  1.00 22.30           N  
ANISOU 1483  N   THR D 651     2216   1631   4626   -328   -517   1051       N  
ATOM   1484  CA  THR D 651      28.970  10.657  72.711  1.00 24.03           C  
ANISOU 1484  CA  THR D 651     2391   1837   4903   -297   -442   1079       C  
ATOM   1485  C   THR D 651      28.700   9.188  73.030  1.00 23.34           C  
ANISOU 1485  C   THR D 651     2360   1756   4751   -262   -352   1060       C  
ATOM   1486  O   THR D 651      28.835   8.302  72.185  1.00 21.67           O  
ANISOU 1486  O   THR D 651     2203   1560   4470   -262   -361   1022       O  
ATOM   1487  CB  THR D 651      27.683  11.468  72.858  1.00 35.93           C  
ANISOU 1487  CB  THR D 651     3817   3317   6517   -281   -451   1103       C  
ATOM   1488  OG1 THR D 651      27.218  11.376  74.210  1.00 50.18           O  
ANISOU 1488  OG1 THR D 651     5583   5101   8384   -251   -358   1140       O  
ATOM   1489  CG2 THR D 651      26.606  10.921  71.940  1.00 35.75           C  
ANISOU 1489  CG2 THR D 651     3823   3283   6476   -262   -445   1067       C  
ATOM   1490  N   LEU D 652      28.305   8.942  74.280  1.00 25.58           N  
ANISOU 1490  N   LEU D 652     2637   2020   5062   -231   -264   1094       N  
ATOM   1491  CA  LEU D 652      27.966   7.597  74.727  1.00 29.23           C  
ANISOU 1491  CA  LEU D 652     3177   2475   5453   -190   -179   1091       C  
ATOM   1492  C   LEU D 652      26.723   7.057  74.028  1.00 25.42           C  
ANISOU 1492  C   LEU D 652     2726   1978   4955   -167   -183   1057       C  
ATOM   1493  O   LEU D 652      26.583   5.838  73.892  1.00 21.98           O  
ANISOU 1493  O   LEU D 652     2377   1536   4438   -141   -160   1037       O  
ATOM   1494  CB  LEU D 652      27.797   7.614  76.255  1.00 32.63           C  
ANISOU 1494  CB  LEU D 652     3608   2874   5914   -161    -75   1151       C  
ATOM   1495  CG  LEU D 652      27.906   6.385  77.167  1.00 23.44           C  
ANISOU 1495  CG  LEU D 652     2551   1693   4664   -112     24   1183       C  
ATOM   1496  CD1 LEU D 652      26.656   5.513  77.142  1.00 33.68           C  
ANISOU 1496  CD1 LEU D 652     3926   2967   5904    -54     67   1180       C  
ATOM   1497  CD2 LEU D 652      29.128   5.565  76.783  1.00 22.97           C  
ANISOU 1497  CD2 LEU D 652     2559   1654   4515   -119     -5   1162       C  
ATOM   1498  N   GLU D 653      25.838   7.934  73.554  1.00 28.67           N  
ANISOU 1498  N   GLU D 653     3080   2371   5444   -175   -218   1050       N  
ATOM   1499  CA  GLU D 653      24.591   7.536  72.919  1.00 34.19           C  
ANISOU 1499  CA  GLU D 653     3821   3030   6140   -154   -217   1013       C  
ATOM   1500  C   GLU D 653      24.682   7.478  71.397  1.00 28.48           C  
ANISOU 1500  C   GLU D 653     3107   2312   5400   -190   -305    962       C  
ATOM   1501  O   GLU D 653      23.643   7.422  70.729  1.00 36.60           O  
ANISOU 1501  O   GLU D 653     4163   3292   6450   -184   -316    929       O  
ATOM   1502  CB  GLU D 653      23.462   8.479  73.341  1.00 51.00           C  
ANISOU 1502  CB  GLU D 653     5892   5113   8371   -131   -184   1039       C  
ATOM   1503  CG  GLU D 653      23.651   9.075  74.727  1.00 66.57           C  
ANISOU 1503  CG  GLU D 653     7797   7085  10410   -116   -113   1106       C  
ATOM   1504  CD  GLU D 653      22.399   9.752  75.256  1.00 79.09           C  
ANISOU 1504  CD  GLU D 653     9331   8616  12103    -78    -50   1138       C  
ATOM   1505  OE1 GLU D 653      22.450  10.289  76.384  1.00 83.65           O  
ANISOU 1505  OE1 GLU D 653     9836   9185  12761    -66     19   1200       O  
ATOM   1506  OE2 GLU D 653      21.370   9.754  74.548  1.00 81.80           O  
ANISOU 1506  OE2 GLU D 653     9708   8914  12459    -58    -63   1102       O  
ATOM   1507  N   GLY D 654      25.889   7.501  70.831  1.00 21.76           N  
ANISOU 1507  N   GLY D 654     2247   1507   4514   -226   -358    957       N  
ATOM   1508  CA  GLY D 654      26.095   7.207  69.430  1.00 22.44           C  
ANISOU 1508  CA  GLY D 654     2359   1594   4573   -257   -417    918       C  
ATOM   1509  C   GLY D 654      26.280   8.409  68.525  1.00 21.84           C  
ANISOU 1509  C   GLY D 654     2250   1514   4534   -290   -486    930       C  
ATOM   1510  O   GLY D 654      26.829   8.254  67.428  1.00 39.08           O  
ANISOU 1510  O   GLY D 654     4466   3701   6682   -320   -520    914       O  
ATOM   1511  N   ASP D 655      25.829   9.591  68.936  1.00 23.03           N  
ANISOU 1511  N   ASP D 655     2345   1647   4756   -284   -504    965       N  
ATOM   1512  CA  ASP D 655      25.960  10.769  68.089  1.00 29.06           C  
ANISOU 1512  CA  ASP D 655     3095   2395   5551   -313   -580    986       C  
ATOM   1513  C   ASP D 655      27.411  11.220  68.020  1.00 24.94           C  
ANISOU 1513  C   ASP D 655     2586   1910   4979   -346   -624   1006       C  
ATOM   1514  O   ASP D 655      28.117  11.263  69.030  1.00 22.46           O  
ANISOU 1514  O   ASP D 655     2250   1622   4662   -342   -607   1022       O  
ATOM   1515  CB  ASP D 655      25.091  11.908  68.612  1.00 39.73           C  
ANISOU 1515  CB  ASP D 655     4375   3711   7008   -297   -596   1024       C  
ATOM   1516  CG  ASP D 655      23.778  11.424  69.172  1.00 50.73           C  
ANISOU 1516  CG  ASP D 655     5762   5064   8450   -254   -519   1008       C  
ATOM   1517  OD1 ASP D 655      23.060  10.682  68.467  1.00 47.60           O  
ANISOU 1517  OD1 ASP D 655     5432   4628   8026   -246   -498    963       O  
ATOM   1518  OD2 ASP D 655      23.473  11.782  70.328  1.00 59.03           O  
ANISOU 1518  OD2 ASP D 655     6751   6112   9566   -228   -475   1041       O  
ATOM   1519  N   GLN D 656      27.854  11.566  66.816  1.00 30.60           N  
ANISOU 1519  N   GLN D 656     3357   2613   5657   -381   -670   1006       N  
ATOM   1520  CA  GLN D 656      29.249  11.879  66.565  1.00 30.54           C  
ANISOU 1520  CA  GLN D 656     3399   2624   5581   -416   -698   1016       C  
ATOM   1521  C   GLN D 656      29.394  13.308  66.061  1.00 32.25           C  
ANISOU 1521  C   GLN D 656     3633   2808   5812   -450   -782   1056       C  
ATOM   1522  O   GLN D 656      28.417  13.994  65.747  1.00 38.09           O  
ANISOU 1522  O   GLN D 656     4345   3509   6617   -445   -820   1078       O  
ATOM   1523  CB  GLN D 656      29.854  10.907  65.543  1.00 34.55           C  
ANISOU 1523  CB  GLN D 656     3982   3134   6011   -435   -658    984       C  
ATOM   1524  CG  GLN D 656      29.339   9.486  65.664  1.00 38.48           C  
ANISOU 1524  CG  GLN D 656     4465   3645   6511   -406   -599    946       C  
ATOM   1525  CD  GLN D 656      29.587   8.670  64.416  1.00 41.25           C  
ANISOU 1525  CD  GLN D 656     4869   3978   6827   -432   -573    919       C  
ATOM   1526  OE1 GLN D 656      30.702   8.637  63.897  1.00 54.04           O  
ANISOU 1526  OE1 GLN D 656     6538   5602   8393   -461   -558    923       O  
ATOM   1527  NE2 GLN D 656      28.547   8.012  63.920  1.00 33.45           N  
ANISOU 1527  NE2 GLN D 656     3878   2958   5875   -429   -561    891       N  
ATOM   1528  N   VAL D 657      30.647  13.747  66.001  1.00 37.92           N  
ANISOU 1528  N   VAL D 657     4409   3530   6467   -486   -811   1067       N  
ATOM   1529  CA  VAL D 657      31.035  14.957  65.288  1.00 33.18           C  
ANISOU 1529  CA  VAL D 657     3872   2891   5845   -530   -890   1103       C  
ATOM   1530  C   VAL D 657      32.476  14.781  64.818  1.00 24.38           C  
ANISOU 1530  C   VAL D 657     2872   1772   4618   -570   -863   1090       C  
ATOM   1531  O   VAL D 657      33.384  14.513  65.613  1.00 24.06           O  
ANISOU 1531  O   VAL D 657     2839   1751   4550   -572   -840   1074       O  
ATOM   1532  CB  VAL D 657      30.832  16.221  66.152  1.00 25.02           C  
ANISOU 1532  CB  VAL D 657     2767   1844   4894   -536   -987   1147       C  
ATOM   1533  CG1 VAL D 657      31.406  16.041  67.540  1.00 24.70           C  
ANISOU 1533  CG1 VAL D 657     2673   1833   4880   -527   -970   1141       C  
ATOM   1534  CG2 VAL D 657      31.457  17.428  65.476  1.00 25.91           C  
ANISOU 1534  CG2 VAL D 657     2968   1914   4965   -589  -1084   1184       C  
ATOM   1535  N   SER D 658      32.683  14.880  63.507  1.00 24.83           N  
ANISOU 1535  N   SER D 658     3031   1790   4614   -602   -845   1097       N  
ATOM   1536  CA  SER D 658      33.979  14.581  62.924  1.00 24.89           C  
ANISOU 1536  CA  SER D 658     3157   1782   4520   -637   -784   1082       C  
ATOM   1537  C   SER D 658      34.972  15.701  63.210  1.00 25.51           C  
ANISOU 1537  C   SER D 658     3311   1831   4551   -678   -852   1106       C  
ATOM   1538  O   SER D 658      34.623  16.781  63.695  1.00 26.00           O  
ANISOU 1538  O   SER D 658     3335   1883   4662   -686   -964   1140       O  
ATOM   1539  CB  SER D 658      33.852  14.379  61.417  1.00 58.60           C  
ANISOU 1539  CB  SER D 658     7517   6001   8748   -664   -722   1091       C  
ATOM   1540  OG  SER D 658      34.155  15.579  60.725  1.00 60.02           O  
ANISOU 1540  OG  SER D 658     7804   6120   8882   -705   -768   1138       O  
ATOM   1541  N   HIS D 659      36.237  15.432  62.878  1.00 33.37           N  
ANISOU 1541  N   HIS D 659     4420   2802   5456   -707   -782   1088       N  
ATOM   1542  CA  HIS D 659      37.277  16.446  63.007  1.00 37.31           C  
ANISOU 1542  CA  HIS D 659     5026   3256   5895   -753   -837   1105       C  
ATOM   1543  C   HIS D 659      37.116  17.569  61.990  1.00 39.53           C  
ANISOU 1543  C   HIS D 659     5404   3480   6137   -788   -904   1158       C  
ATOM   1544  O   HIS D 659      37.700  18.642  62.173  1.00 46.08           O  
ANISOU 1544  O   HIS D 659     6307   4271   6930   -826  -1002   1183       O  
ATOM   1545  CB  HIS D 659      38.661  15.807  62.866  1.00 38.22           C  
ANISOU 1545  CB  HIS D 659     5250   3345   5928   -768   -719   1071       C  
ATOM   1546  CG  HIS D 659      38.820  14.969  61.635  1.00 42.69           C  
ANISOU 1546  CG  HIS D 659     5881   3889   6451   -769   -583   1064       C  
ATOM   1547  ND1 HIS D 659      38.330  13.684  61.536  1.00 43.84           N  
ANISOU 1547  ND1 HIS D 659     5944   4076   6636   -736   -505   1034       N  
ATOM   1548  CD2 HIS D 659      39.421  15.233  60.450  1.00 45.70           C  
ANISOU 1548  CD2 HIS D 659     6401   4202   6761   -804   -507   1088       C  
ATOM   1549  CE1 HIS D 659      38.620  13.193  60.345  1.00 45.94           C  
ANISOU 1549  CE1 HIS D 659     6288   4301   6865   -758   -393   1036       C  
ATOM   1550  NE2 HIS D 659      39.282  14.113  59.666  1.00 46.56           N  
ANISOU 1550  NE2 HIS D 659     6503   4311   6878   -797   -376   1071       N  
ATOM   1551  N   ARG D 660      36.344  17.342  60.927  1.00 41.29           N  
ANISOU 1551  N   ARG D 660     5638   3684   6366   -780   -856   1178       N  
ATOM   1552  CA  ARG D 660      36.025  18.374  59.951  1.00 37.25           C  
ANISOU 1552  CA  ARG D 660     5223   3106   5826   -802   -909   1241       C  
ATOM   1553  C   ARG D 660      34.754  19.135  60.291  1.00 30.83           C  
ANISOU 1553  C   ARG D 660     4306   2296   5111   -780  -1038   1277       C  
ATOM   1554  O   ARG D 660      34.494  20.179  59.682  1.00 30.42           O  
ANISOU 1554  O   ARG D 660     4332   2182   5043   -793  -1113   1339       O  
ATOM   1555  CB  ARG D 660      35.883  17.753  58.560  1.00 47.05           C  
ANISOU 1555  CB  ARG D 660     6548   4297   7032   -809   -765   1254       C  
ATOM   1556  CG  ARG D 660      37.201  17.507  57.858  1.00 55.75           C  
ANISOU 1556  CG  ARG D 660     7798   5352   8034   -840   -638   1255       C  
ATOM   1557  CD  ARG D 660      37.000  17.251  56.377  1.00 71.82           C  
ANISOU 1557  CD  ARG D 660     9930   7312  10048   -856   -502   1296       C  
ATOM   1558  NE  ARG D 660      38.252  16.870  55.733  1.00 96.69           N  
ANISOU 1558  NE  ARG D 660    13196  10415  13127   -881   -345   1301       N  
ATOM   1559  CZ  ARG D 660      38.690  15.618  55.635  1.00115.31           C  
ANISOU 1559  CZ  ARG D 660    15522  12789  15503   -885   -202   1247       C  
ATOM   1560  NH1 ARG D 660      37.973  14.621  56.138  1.00120.52           N  
ANISOU 1560  NH1 ARG D 660    16045  13516  16230   -868   -217   1185       N  
ATOM   1561  NH2 ARG D 660      39.843  15.362  55.035  1.00118.91           N  
ANISOU 1561  NH2 ARG D 660    16077  13189  15916   -902    -47   1263       N  
ATOM   1562  N   GLY D 661      33.961  18.644  61.233  1.00 29.46           N  
ANISOU 1562  N   GLY D 661     3970   2184   5040   -741  -1055   1246       N  
ATOM   1563  CA  GLY D 661      32.728  19.280  61.625  1.00 35.00           C  
ANISOU 1563  CA  GLY D 661     4560   2883   5855   -713  -1151   1277       C  
ATOM   1564  C   GLY D 661      31.445  18.601  61.166  1.00 31.51           C  
ANISOU 1564  C   GLY D 661     4057   2435   5480   -673  -1082   1268       C  
ATOM   1565  O   GLY D 661      30.406  19.270  61.108  1.00 37.68           O  
ANISOU 1565  O   GLY D 661     4793   3179   6344   -652  -1144   1305       O  
ATOM   1566  N   ALA D 662      31.482  17.310  60.850  1.00 27.64           N  
ANISOU 1566  N   ALA D 662     3568   1970   4964   -662   -961   1219       N  
ATOM   1567  CA  ALA D 662      30.313  16.602  60.328  1.00 27.61           C  
ANISOU 1567  CA  ALA D 662     3528   1945   5018   -636   -898   1203       C  
ATOM   1568  C   ALA D 662      29.490  16.071  61.494  1.00 26.74           C  
ANISOU 1568  C   ALA D 662     3266   1893   5002   -585   -907   1169       C  
ATOM   1569  O   ALA D 662      29.851  15.074  62.125  1.00 25.76           O  
ANISOU 1569  O   ALA D 662     3095   1829   4864   -568   -855   1124       O  
ATOM   1570  CB  ALA D 662      30.741  15.481  59.389  1.00 36.36           C  
ANISOU 1570  CB  ALA D 662     4711   3041   6065   -659   -775   1170       C  
ATOM   1571  N   LEU D 663      28.373  16.734  61.779  1.00 27.25           N  
ANISOU 1571  N   LEU D 663     3264   1927   5162   -557   -962   1195       N  
ATOM   1572  CA  LEU D 663      27.454  16.254  62.800  1.00 26.66           C  
ANISOU 1572  CA  LEU D 663     3062   1886   5181   -508   -943   1167       C  
ATOM   1573  C   LEU D 663      26.693  15.039  62.287  1.00 26.37           C  
ANISOU 1573  C   LEU D 663     3039   1833   5148   -489   -852   1119       C  
ATOM   1574  O   LEU D 663      26.143  15.058  61.182  1.00 62.01           O  
ANISOU 1574  O   LEU D 663     7626   6271   9662   -503   -829   1126       O  
ATOM   1575  CB  LEU D 663      26.477  17.356  63.212  1.00 27.49           C  
ANISOU 1575  CB  LEU D 663     3095   1949   5401   -484  -1014   1212       C  
ATOM   1576  CG  LEU D 663      26.865  18.397  64.272  1.00 27.70           C  
ANISOU 1576  CG  LEU D 663     3038   2000   5489   -491  -1110   1251       C  
ATOM   1577  CD1 LEU D 663      27.091  17.711  65.606  1.00 41.11           C  
ANISOU 1577  CD1 LEU D 663     4638   3769   7214   -469  -1062   1219       C  
ATOM   1578  CD2 LEU D 663      28.080  19.232  63.893  1.00 28.17           C  
ANISOU 1578  CD2 LEU D 663     3186   2051   5466   -545  -1197   1284       C  
ATOM   1579  N   THR D 664      26.666  13.977  63.088  1.00 25.41           N  
ANISOU 1579  N   THR D 664     2858   1769   5029   -462   -800   1073       N  
ATOM   1580  CA  THR D 664      25.990  12.739  62.721  1.00 25.16           C  
ANISOU 1580  CA  THR D 664     2840   1721   5000   -449   -729   1022       C  
ATOM   1581  C   THR D 664      25.376  12.152  63.980  1.00 34.25           C  
ANISOU 1581  C   THR D 664     3909   2906   6197   -402   -699    995       C  
ATOM   1582  O   THR D 664      26.084  11.928  64.967  1.00 40.36           O  
ANISOU 1582  O   THR D 664     4642   3745   6950   -390   -692    996       O  
ATOM   1583  CB  THR D 664      26.963  11.746  62.076  1.00 24.73           C  
ANISOU 1583  CB  THR D 664     2843   1690   4862   -482   -682    993       C  
ATOM   1584  OG1 THR D 664      27.149  12.090  60.700  1.00 25.98           O  
ANISOU 1584  OG1 THR D 664     3096   1783   4991   -530   -671   1013       O  
ATOM   1585  CG2 THR D 664      26.420  10.326  62.150  1.00 24.29           C  
ANISOU 1585  CG2 THR D 664     2770   1639   4819   -466   -628    936       C  
ATOM   1586  N   GLY D 665      24.071  11.919  63.956  1.00 24.95           N  
ANISOU 1586  N   GLY D 665     2727   1673   5080   -376   -671    973       N  
ATOM   1587  CA  GLY D 665      23.406  11.369  65.121  1.00 32.41           C  
ANISOU 1587  CA  GLY D 665     3622   2632   6060   -332   -624    950       C  
ATOM   1588  C   GLY D 665      21.933  11.159  64.854  1.00 30.23           C  
ANISOU 1588  C   GLY D 665     3379   2266   5841   -307   -589    918       C  
ATOM   1589  O   GLY D 665      21.395  11.563  63.818  1.00 26.14           O  
ANISOU 1589  O   GLY D 665     2912   1670   5350   -322   -606    920       O  
ATOM   1590  N   GLY D 666      21.289  10.515  65.822  1.00 32.43           N  
ANISOU 1590  N   GLY D 666     3648   2542   6132   -268   -532    891       N  
ATOM   1591  CA  GLY D 666      19.879  10.196  65.759  1.00 33.95           C  
ANISOU 1591  CA  GLY D 666     3896   2638   6366   -234   -487    850       C  
ATOM   1592  C   GLY D 666      19.515   9.198  66.838  1.00 39.22           C  
ANISOU 1592  C   GLY D 666     4589   3312   6999   -195   -419    818       C  
ATOM   1593  O   GLY D 666      19.974   9.316  67.979  1.00 40.21           O  
ANISOU 1593  O   GLY D 666     4659   3499   7120   -174   -390    857       O  
ATOM   1594  N   TYR D 667      18.705   8.205  66.490  1.00 38.63           N  
ANISOU 1594  N   TYR D 667     4615   3162   6899   -186   -393    748       N  
ATOM   1595  CA  TYR D 667      18.315   7.145  67.412  1.00 44.45           C  
ANISOU 1595  CA  TYR D 667     5423   3884   7583   -140   -336    713       C  
ATOM   1596  C   TYR D 667      19.000   5.853  66.991  1.00 46.42           C  
ANISOU 1596  C   TYR D 667     5715   4167   7757   -181   -364    668       C  
ATOM   1597  O   TYR D 667      18.763   5.353  65.887  1.00 49.81           O  
ANISOU 1597  O   TYR D 667     6188   4543   8193   -227   -398    606       O  
ATOM   1598  CB  TYR D 667      16.798   6.972  67.432  1.00 55.28           C  
ANISOU 1598  CB  TYR D 667     6901   5121   8980    -79   -293    656       C  
ATOM   1599  CG  TYR D 667      16.291   5.851  68.320  1.00 58.52           C  
ANISOU 1599  CG  TYR D 667     7353   5460   9424    -10   -262    636       C  
ATOM   1600  CD1 TYR D 667      16.105   6.049  69.684  1.00 61.33           C  
ANISOU 1600  CD1 TYR D 667     7681   5820   9801     73   -186    700       C  
ATOM   1601  CD2 TYR D 667      15.969   4.606  67.788  1.00 59.77           C  
ANISOU 1601  CD2 TYR D 667     7577   5530   9604    -21   -310    550       C  
ATOM   1602  CE1 TYR D 667      15.634   5.031  70.496  1.00 64.03           C  
ANISOU 1602  CE1 TYR D 667     8086   6085  10156    168   -143    692       C  
ATOM   1603  CE2 TYR D 667      15.498   3.584  68.592  1.00 61.42           C  
ANISOU 1603  CE2 TYR D 667     7841   5653   9843     69   -297    522       C  
ATOM   1604  CZ  TYR D 667      15.332   3.803  69.943  1.00 65.44           C  
ANISOU 1604  CZ  TYR D 667     8349   6171  10344    177   -204    601       C  
ATOM   1605  OH  TYR D 667      14.861   2.787  70.743  1.00 73.01           O  
ANISOU 1605  OH  TYR D 667     9387   7042  11313    306   -174    583       O  
ATOM   1606  N   TYR D 668      19.842   5.319  67.869  1.00 50.86           N  
ANISOU 1606  N   TYR D 668     6261   4806   8256   -166   -347    700       N  
ATOM   1607  CA  TYR D 668      20.476   4.025  67.661  1.00 45.27           C  
ANISOU 1607  CA  TYR D 668     5591   4122   7488   -187   -372    667       C  
ATOM   1608  C   TYR D 668      19.790   3.010  68.564  1.00 49.03           C  
ANISOU 1608  C   TYR D 668     6105   4506   8018   -114   -368    670       C  
ATOM   1609  O   TYR D 668      19.755   3.186  69.788  1.00 52.36           O  
ANISOU 1609  O   TYR D 668     6537   4941   8415    -45   -301    733       O  
ATOM   1610  CB  TYR D 668      21.976   4.087  67.945  1.00 34.26           C  
ANISOU 1610  CB  TYR D 668     4119   2841   6056   -209   -384    723       C  
ATOM   1611  CG  TYR D 668      22.749   4.858  66.901  1.00 28.42           C  
ANISOU 1611  CG  TYR D 668     3304   2144   5350   -266   -435    739       C  
ATOM   1612  CD2 TYR D 668      23.178   6.156  67.146  1.00 38.02           C  
ANISOU 1612  CD2 TYR D 668     4450   3399   6596   -266   -442    795       C  
ATOM   1613  CD1 TYR D 668      23.017   4.301  65.658  1.00 22.69           C  
ANISOU 1613  CD1 TYR D 668     2590   1404   4627   -317   -474    698       C  
ATOM   1614  CE2 TYR D 668      23.881   6.869  66.188  1.00 39.27           C  
ANISOU 1614  CE2 TYR D 668     4579   3579   6764   -306   -490    813       C  
ATOM   1615  CE1 TYR D 668      23.708   5.010  64.692  1.00 23.23           C  
ANISOU 1615  CE1 TYR D 668     2624   1494   4710   -358   -502    722       C  
ATOM   1616  CZ  TYR D 668      24.143   6.289  64.963  1.00 28.74           C  
ANISOU 1616  CZ  TYR D 668     3278   2226   5415   -348   -511    780       C  
ATOM   1617  OH  TYR D 668      24.837   6.990  64.004  1.00 26.14           O  
ANISOU 1617  OH  TYR D 668     2948   1902   5081   -386   -539    806       O  
ATOM   1618  N   ASP D 669      19.240   1.962  67.960  1.00 52.88           N  
ANISOU 1618  N   ASP D 669     6622   4888   8583   -121   -441    597       N  
ATOM   1619  CA  ASP D 669      18.538   0.933  68.708  1.00 53.10           C  
ANISOU 1619  CA  ASP D 669     6714   4798   8664    -22   -465    577       C  
ATOM   1620  C   ASP D 669      19.538  -0.035  69.340  1.00 57.60           C  
ANISOU 1620  C   ASP D 669     7276   5424   9187     19   -500    641       C  
ATOM   1621  O   ASP D 669      20.736  -0.020  69.046  1.00 56.66           O  
ANISOU 1621  O   ASP D 669     7093   5417   9017    -50   -510    677       O  
ATOM   1622  CB  ASP D 669      17.567   0.185  67.792  1.00 57.76           C  
ANISOU 1622  CB  ASP D 669     7344   5234   9369    -45   -572    428       C  
ATOM   1623  CG  ASP D 669      16.418  -0.458  68.552  1.00 62.54           C  
ANISOU 1623  CG  ASP D 669     8057   5682  10024    105   -588    355       C  
ATOM   1624  OD1 ASP D 669      16.476  -0.505  69.799  1.00 60.81           O  
ANISOU 1624  OD1 ASP D 669     7875   5484   9744    243   -507    457       O  
ATOM   1625  OD2 ASP D 669      15.462  -0.927  67.897  1.00 61.33           O  
ANISOU 1625  OD2 ASP D 669     7960   5387   9954     97   -676    178       O  
ATOM   1626  N   THR D 670      19.028  -0.879  70.236  1.00 56.59           N  
ANISOU 1626  N   THR D 670     7227   5212   9062    166   -514    658       N  
ATOM   1627  CA  THR D 670      19.806  -1.962  70.814  1.00 58.24           C  
ANISOU 1627  CA  THR D 670     7454   5460   9216    257   -576    727       C  
ATOM   1628  C   THR D 670      19.473  -3.306  70.166  1.00 62.08           C  
ANISOU 1628  C   THR D 670     7949   5985   9654    283   -753    554       C  
ATOM   1629  O   THR D 670      20.233  -4.268  70.327  1.00 57.07           O  
ANISOU 1629  O   THR D 670     7292   5493   8898    332   -825    561       O  
ATOM   1630  CB  THR D 670      19.571  -2.008  72.335  1.00 56.45           C  
ANISOU 1630  CB  THR D 670     7313   5254   8881    437   -446    850       C  
ATOM   1631  OG1 THR D 670      19.619  -0.674  72.851  1.00 63.18           O  
ANISOU 1631  OG1 THR D 670     8139   6171   9694    371   -280    904       O  
ATOM   1632  CG2 THR D 670      20.668  -2.794  73.052  1.00 52.06           C  
ANISOU 1632  CG2 THR D 670     6772   4806   8202    521   -451    968       C  
ATOM   1633  N   ARG D 671      18.378  -3.377  69.403  1.00 72.64           N  
ANISOU 1633  N   ARG D 671     9309   7255  11035    236   -815    369       N  
ATOM   1634  CA  ARG D 671      18.036  -4.600  68.681  1.00 83.30           C  
ANISOU 1634  CA  ARG D 671    10647   8701  12300    217   -982    151       C  
ATOM   1635  C   ARG D 671      19.057  -4.918  67.594  1.00 74.87           C  
ANISOU 1635  C   ARG D 671     9440   7648  11359     54  -1093    138       C  
ATOM   1636  O   ARG D 671      19.403  -6.086  67.384  1.00 75.24           O  
ANISOU 1636  O   ARG D 671     9430   7849  11308     75  -1224     40       O  
ATOM   1637  CB  ARG D 671      16.640  -4.478  68.068  1.00 96.27           C  
ANISOU 1637  CB  ARG D 671    12354  10229  13996    182  -1009    -48       C  
ATOM   1638  CG  ARG D 671      15.494  -4.909  68.972  1.00106.23           C  
ANISOU 1638  CG  ARG D 671    13763  11557  15043    371   -966   -149       C  
ATOM   1639  CD  ARG D 671      14.192  -4.994  68.183  1.00111.17           C  
ANISOU 1639  CD  ARG D 671    14453  12067  15718    322  -1025   -392       C  
ATOM   1640  NE  ARG D 671      13.107  -5.591  68.958  1.00112.67           N  
ANISOU 1640  NE  ARG D 671    14801  12341  15669    506  -1004   -529       N  
ATOM   1641  CZ  ARG D 671      11.945  -5.980  68.439  1.00110.92           C  
ANISOU 1641  CZ  ARG D 671    14670  12060  15417    500  -1076   -783       C  
ATOM   1642  NH1 ARG D 671      11.715  -5.839  67.140  1.00107.37           N  
ANISOU 1642  NH1 ARG D 671    14160  11454  15180    308  -1172   -921       N  
ATOM   1643  NH2 ARG D 671      11.014  -6.514  69.218  1.00112.15           N  
ANISOU 1643  NH2 ARG D 671    14986  12302  15322    685  -1045   -901       N  
ATOM   1644  N   LYS D 672      19.547  -3.897  66.890  1.00 70.11           N  
ANISOU 1644  N   LYS D 672     8778   6892  10969   -100  -1041    235       N  
ATOM   1645  CA  LYS D 672      20.504  -4.086  65.808  1.00 67.33           C  
ANISOU 1645  CA  LYS D 672     8301   6536  10744   -261  -1109    233       C  
ATOM   1646  C   LYS D 672      21.931  -3.735  66.210  1.00 63.41           C  
ANISOU 1646  C   LYS D 672     7755   6119  10219   -250  -1029    430       C  
ATOM   1647  O   LYS D 672      22.773  -3.500  65.336  1.00 70.50           O  
ANISOU 1647  O   LYS D 672     8560   7112  11115   -352   -990    444       O  
ATOM   1648  CB  LYS D 672      20.089  -3.275  64.579  1.00 70.07           C  
ANISOU 1648  CB  LYS D 672     8622   6854  11149   -404  -1040    180       C  
ATOM   1649  CG  LYS D 672      18.817  -3.760  63.908  1.00 68.64           C  
ANISOU 1649  CG  LYS D 672     8477   6554  11049   -462  -1138    -37       C  
ATOM   1650  CD  LYS D 672      18.564  -3.003  62.614  1.00 60.65           C  
ANISOU 1650  CD  LYS D 672     7453   5572  10021   -570  -1026    -45       C  
ATOM   1651  CE  LYS D 672      17.302  -3.493  61.927  1.00 55.89           C  
ANISOU 1651  CE  LYS D 672     6893   4853   9488   -634  -1101   -258       C  
ATOM   1652  NZ  LYS D 672      17.173  -2.942  60.551  1.00 54.07           N  
ANISOU 1652  NZ  LYS D 672     6663   4629   9252   -748   -997   -253       N  
ATOM   1653  N   SER D 673      22.224  -3.690  67.506  1.00 54.73           N  
ANISOU 1653  N   SER D 673     6722   5060   9014   -100   -964    562       N  
ATOM   1654  CA  SER D 673      23.602  -3.563  67.962  1.00 51.33           C  
ANISOU 1654  CA  SER D 673     6250   4768   8484    -81   -879    695       C  
ATOM   1655  C   SER D 673      24.290  -4.915  67.821  1.00 49.37           C  
ANISOU 1655  C   SER D 673     5938   4585   8234    -22  -1018    674       C  
ATOM   1656  O   SER D 673      23.891  -5.891  68.468  1.00 49.20           O  
ANISOU 1656  O   SER D 673     5956   4704   8034    132  -1076    613       O  
ATOM   1657  CB  SER D 673      23.650  -3.069  69.405  1.00 54.38           C  
ANISOU 1657  CB  SER D 673     6727   5226   8708     39   -728    806       C  
ATOM   1658  OG  SER D 673      22.574  -3.601  70.151  1.00 64.58           O  
ANISOU 1658  OG  SER D 673     8115   6432   9989    195   -772    807       O  
ATOM   1659  N   ARG D 674      25.316  -4.970  66.964  1.00 50.63           N  
ANISOU 1659  N   ARG D 674     8038   5271   5930   1457   -652    -39       N  
ATOM   1660  CA  ARG D 674      25.961  -6.238  66.632  1.00 41.92           C  
ANISOU 1660  CA  ARG D 674     6996   4183   4749   1469   -773   -172       C  
ATOM   1661  C   ARG D 674      26.708  -6.820  67.826  1.00 47.33           C  
ANISOU 1661  C   ARG D 674     7737   4834   5410   1472   -874   -161       C  
ATOM   1662  O   ARG D 674      26.692  -8.039  68.039  1.00 47.18           O  
ANISOU 1662  O   ARG D 674     7788   4824   5313   1516   -941   -229       O  
ATOM   1663  CB  ARG D 674      26.923  -6.047  65.459  1.00 31.29           C  
ANISOU 1663  CB  ARG D 674     5593   2868   3428   1429   -836   -251       C  
ATOM   1664  CG  ARG D 674      26.293  -5.564  64.159  1.00 30.99           C  
ANISOU 1664  CG  ARG D 674     5484   2844   3448   1411   -760   -251       C  
ATOM   1665  CD  ARG D 674      27.306  -5.664  63.023  1.00 42.67           C  
ANISOU 1665  CD  ARG D 674     6898   4369   4944   1398   -832   -320       C  
ATOM   1666  NE  ARG D 674      26.821  -5.116  61.758  1.00 46.90           N  
ANISOU 1666  NE  ARG D 674     7347   4901   5573   1367   -768   -298       N  
ATOM   1667  CZ  ARG D 674      27.480  -4.217  61.031  1.00 48.50           C  
ANISOU 1667  CZ  ARG D 674     7453   5131   5844   1341   -750   -275       C  
ATOM   1668  NH1 ARG D 674      28.657  -3.761  61.440  1.00 46.95           N  
ANISOU 1668  NH1 ARG D 674     7252   4972   5614   1352   -801   -291       N  
ATOM   1669  NH2 ARG D 674      26.964  -3.776  59.892  1.00 49.55           N  
ANISOU 1669  NH2 ARG D 674     7502   5245   6081   1311   -697   -236       N  
ATOM   1670  N   LEU D 675      27.374  -5.969  68.611  1.00 44.75           N  
ANISOU 1670  N   LEU D 675     7380   4457   5167   1420   -906    -63       N  
ATOM   1671  CA  LEU D 675      28.117  -6.463  69.765  1.00 52.56           C  
ANISOU 1671  CA  LEU D 675     8422   5382   6166   1406  -1036    -29       C  
ATOM   1672  C   LEU D 675      27.183  -6.930  70.873  1.00 51.00           C  
ANISOU 1672  C   LEU D 675     8228   5183   5967   1444   -982    118       C  
ATOM   1673  O   LEU D 675      27.515  -7.867  71.608  1.00 61.52           O  
ANISOU 1673  O   LEU D 675     9616   6483   7276   1456  -1081    117       O  
ATOM   1674  CB  LEU D 675      29.073  -5.388  70.289  1.00 27.71           C  
ANISOU 1674  CB  LEU D 675     5247   2165   3118   1326  -1123     59       C  
ATOM   1675  CG  LEU D 675      30.302  -5.066  69.432  1.00 27.35           C  
ANISOU 1675  CG  LEU D 675     5226   2119   3046   1315  -1236   -100       C  
ATOM   1676  CD1 LEU D 675      30.022  -3.934  68.469  1.00 26.34           C  
ANISOU 1676  CD1 LEU D 675     5006   2043   2958   1295  -1115    -76       C  
ATOM   1677  CD2 LEU D 675      31.500  -4.734  70.303  1.00 28.66           C  
ANISOU 1677  CD2 LEU D 675     5457   2176   3259   1265  -1437    -88       C  
ATOM   1678  N   GLU D 676      26.005  -6.314  70.994  1.00 49.01           N  
ANISOU 1678  N   GLU D 676     7910   4981   5729   1480   -834    251       N  
ATOM   1679  CA  GLU D 676      25.025  -6.791  71.964  1.00 52.62           C  
ANISOU 1679  CA  GLU D 676     8371   5488   6136   1560   -786    397       C  
ATOM   1680  C   GLU D 676      24.452  -8.140  71.545  1.00 60.48           C  
ANISOU 1680  C   GLU D 676     9516   6502   6961   1686   -788    203       C  
ATOM   1681  O   GLU D 676      24.226  -9.016  72.392  1.00 71.10           O  
ANISOU 1681  O   GLU D 676    10927   7860   8229   1758   -834    252       O  
ATOM   1682  CB  GLU D 676      23.921  -5.749  72.141  1.00 46.17           C  
ANISOU 1682  CB  GLU D 676     7483   4746   5313   1614   -651    567       C  
ATOM   1683  CG  GLU D 676      22.718  -6.217  72.941  1.00 43.94           C  
ANISOU 1683  CG  GLU D 676     7261   4570   4865   1787   -585    678       C  
ATOM   1684  CD  GLU D 676      22.861  -5.931  74.421  1.00 47.62           C  
ANISOU 1684  CD  GLU D 676     7588   5120   5386   1702   -662   1031       C  
ATOM   1685  OE1 GLU D 676      23.121  -4.763  74.779  1.00 49.11           O  
ANISOU 1685  OE1 GLU D 676     7616   5333   5709   1556   -689   1257       O  
ATOM   1686  OE2 GLU D 676      22.714  -6.876  75.224  1.00 52.13           O  
ANISOU 1686  OE2 GLU D 676     8193   5749   5864   1752   -719   1109       O  
ATOM   1687  N   LEU D 677      24.234  -8.337  70.240  1.00 50.80           N  
ANISOU 1687  N   LEU D 677     8324   5291   5686   1694   -759     17       N  
ATOM   1688  CA  LEU D 677      23.828  -9.651  69.749  1.00 44.71           C  
ANISOU 1688  CA  LEU D 677     7672   4542   4775   1773   -808   -140       C  
ATOM   1689  C   LEU D 677      24.926 -10.684  69.969  1.00 45.63           C  
ANISOU 1689  C   LEU D 677     7817   4630   4890   1729   -956   -215       C  
ATOM   1690  O   LEU D 677      24.638 -11.843  70.284  1.00 50.24           O  
ANISOU 1690  O   LEU D 677     8507   5220   5360   1811  -1016   -272       O  
ATOM   1691  CB  LEU D 677      23.456  -9.568  68.269  1.00 41.62           C  
ANISOU 1691  CB  LEU D 677     7250   4173   4392   1741   -786   -242       C  
ATOM   1692  CG  LEU D 677      22.125  -8.883  67.949  1.00 41.97           C  
ANISOU 1692  CG  LEU D 677     7313   4230   4404   1820   -669   -212       C  
ATOM   1693  CD1 LEU D 677      21.925  -8.756  66.448  1.00 49.12           C  
ANISOU 1693  CD1 LEU D 677     8164   5117   5381   1750   -683   -288       C  
ATOM   1694  CD2 LEU D 677      20.975  -9.644  68.581  1.00 44.18           C  
ANISOU 1694  CD2 LEU D 677     7758   4541   4487   2014   -656   -232       C  
ATOM   1695  N   GLN D 678      26.190 -10.273  69.825  1.00 41.92           N  
ANISOU 1695  N   GLN D 678     7270   4132   4525   1621  -1027   -223       N  
ATOM   1696  CA  GLN D 678      27.312 -11.160  70.117  1.00 35.75           C  
ANISOU 1696  CA  GLN D 678     6536   3320   3728   1608  -1186   -300       C  
ATOM   1697  C   GLN D 678      27.337 -11.551  71.589  1.00 42.68           C  
ANISOU 1697  C   GLN D 678     7454   4131   4633   1620  -1238   -182       C  
ATOM   1698  O   GLN D 678      27.593 -12.714  71.926  1.00 48.07           O  
ANISOU 1698  O   GLN D 678     8214   4793   5256   1660  -1340   -244       O  
ATOM   1699  CB  GLN D 678      28.621 -10.481  69.708  1.00 39.91           C  
ANISOU 1699  CB  GLN D 678     7033   3825   4305   1550  -1283   -351       C  
ATOM   1700  CG  GLN D 678      29.848 -10.895  70.507  1.00 44.88           C  
ANISOU 1700  CG  GLN D 678     7721   4375   4954   1536  -1465   -382       C  
ATOM   1701  CD  GLN D 678      31.139 -10.407  69.884  1.00 47.20           C  
ANISOU 1701  CD  GLN D 678     8015   4675   5244   1531  -1588   -488       C  
ATOM   1702  OE1 GLN D 678      31.392 -10.626  68.699  1.00 45.07           O  
ANISOU 1702  OE1 GLN D 678     7709   4507   4907   1578  -1589   -587       O  
ATOM   1703  NE2 GLN D 678      31.960  -9.730  70.679  1.00 50.30           N  
ANISOU 1703  NE2 GLN D 678     8442   4959   5711   1482  -1706   -449       N  
ATOM   1704  N   LYS D 679      27.055 -10.597  72.476  1.00 43.48           N  
ANISOU 1704  N   LYS D 679     7485   4207   4826   1586  -1182     29       N  
ATOM   1705  CA  LYS D 679      27.017 -10.898  73.904  1.00 52.47           C  
ANISOU 1705  CA  LYS D 679     8612   5323   6003   1578  -1247    242       C  
ATOM   1706  C   LYS D 679      25.852 -11.819  74.244  1.00 48.29           C  
ANISOU 1706  C   LYS D 679     8158   4867   5325   1719  -1191    265       C  
ATOM   1707  O   LYS D 679      25.993 -12.718  75.081  1.00 61.04           O  
ANISOU 1707  O   LYS D 679     9798   6477   6917   1731  -1284    342       O  
ATOM   1708  CB  LYS D 679      26.938  -9.606  74.716  1.00 64.64           C  
ANISOU 1708  CB  LYS D 679    10005   6888   7667   1489  -1210    542       C  
ATOM   1709  CG  LYS D 679      27.809  -9.611  75.964  1.00 76.10           C  
ANISOU 1709  CG  LYS D 679    11409   8288   9218   1382  -1369    757       C  
ATOM   1710  CD  LYS D 679      29.188 -10.187  75.669  1.00 82.98           C  
ANISOU 1710  CD  LYS D 679    12422   9004  10102   1351  -1565    502       C  
ATOM   1711  CE  LYS D 679      30.034 -10.284  76.922  1.00 84.51           C  
ANISOU 1711  CE  LYS D 679    12629   9101  10379   1253  -1771    671       C  
ATOM   1712  NZ  LYS D 679      31.391 -10.810  76.612  1.00 82.26           N  
ANISOU 1712  NZ  LYS D 679    12499   8657  10098   1242  -1996    394       N  
ATOM   1713  N   ASP D 680      24.701 -11.615  73.596  1.00 44.67           N  
ANISOU 1713  N   ASP D 680     7747   4480   4748   1839  -1049    192       N  
ATOM   1714  CA  ASP D 680      23.563 -12.512  73.779  1.00 45.10           C  
ANISOU 1714  CA  ASP D 680     7921   4610   4604   2026   -998    151       C  
ATOM   1715  C   ASP D 680      23.898 -13.929  73.327  1.00 33.27           C  
ANISOU 1715  C   ASP D 680     6550   3069   3023   2056  -1109    -68       C  
ATOM   1716  O   ASP D 680      23.600 -14.904  74.034  1.00 34.60           O  
ANISOU 1716  O   ASP D 680     6783   3264   3097   2149  -1153    -34       O  
ATOM   1717  CB  ASP D 680      22.353 -11.981  73.006  1.00 45.83           C  
ANISOU 1717  CB  ASP D 680     8074   4768   4571   2164   -848     67       C  
ATOM   1718  CG  ASP D 680      21.803 -10.695  73.593  1.00 50.65           C  
ANISOU 1718  CG  ASP D 680     8565   5462   5216   2190   -724    305       C  
ATOM   1719  OD1 ASP D 680      22.242 -10.304  74.695  1.00 55.65           O  
ANISOU 1719  OD1 ASP D 680     9053   6138   5955   2083   -773    583       O  
ATOM   1720  OD2 ASP D 680      20.935 -10.070  72.946  1.00 52.60           O  
ANISOU 1720  OD2 ASP D 680     8848   5752   5388   2294   -600    242       O  
ATOM   1721  N   VAL D 681      24.545 -14.054  72.162  1.00 48.92           N  
ANISOU 1721  N   VAL D 681     8532   5020   5035   1971  -1165   -253       N  
ATOM   1722  CA  VAL D 681      24.936 -15.361  71.636  1.00 31.76           C  
ANISOU 1722  CA  VAL D 681     6434   2848   2786   1982  -1289   -417       C  
ATOM   1723  C   VAL D 681      25.922 -16.045  72.574  1.00 36.38           C  
ANISOU 1723  C   VAL D 681     7022   3364   3439   1942  -1415   -380       C  
ATOM   1724  O   VAL D 681      25.769 -17.225  72.904  1.00 33.40           O  
ANISOU 1724  O   VAL D 681     6734   2982   2976   2017  -1486   -428       O  
ATOM   1725  CB  VAL D 681      25.514 -15.217  70.216  1.00 30.34           C  
ANISOU 1725  CB  VAL D 681     6175   2706   2648   1890  -1328   -518       C  
ATOM   1726  CG1 VAL D 681      26.224 -16.489  69.789  1.00 30.88           C  
ANISOU 1726  CG1 VAL D 681     6267   2793   2673   1895  -1478   -624       C  
ATOM   1727  CG2 VAL D 681      24.406 -14.906  69.226  1.00 35.63           C  
ANISOU 1727  CG2 VAL D 681     6842   3425   3272   1922  -1247   -533       C  
ATOM   1728  N   ARG D 682      26.930 -15.308  73.046  1.00 34.57           N  
ANISOU 1728  N   ARG D 682     6699   3071   3367   1825  -1461   -285       N  
ATOM   1729  CA  ARG D 682      27.958 -15.928  73.877  1.00 41.58           C  
ANISOU 1729  CA  ARG D 682     7593   3875   4330   1775  -1618   -248       C  
ATOM   1730  C   ARG D 682      27.434 -16.284  75.266  1.00 50.51           C  
ANISOU 1730  C   ARG D 682     8710   5008   5473   1794  -1631     -9       C  
ATOM   1731  O   ARG D 682      27.826 -17.316  75.826  1.00 54.96           O  
ANISOU 1731  O   ARG D 682     9313   5536   6034   1799  -1750      0       O  
ATOM   1732  CB  ARG D 682      29.177 -15.009  73.958  1.00 46.23           C  
ANISOU 1732  CB  ARG D 682     8114   4394   5059   1658  -1698   -224       C  
ATOM   1733  CG  ARG D 682      30.004 -15.047  72.680  1.00 52.55           C  
ANISOU 1733  CG  ARG D 682     8917   5238   5812   1662  -1745   -442       C  
ATOM   1734  CD  ARG D 682      30.953 -13.870  72.545  1.00 60.94           C  
ANISOU 1734  CD  ARG D 682     9945   6256   6952   1596  -1804   -444       C  
ATOM   1735  NE  ARG D 682      31.972 -14.135  71.532  1.00 69.97           N  
ANISOU 1735  NE  ARG D 682    11110   7459   8018   1647  -1915   -632       N  
ATOM   1736  CZ  ARG D 682      33.014 -13.347  71.289  1.00 76.55           C  
ANISOU 1736  CZ  ARG D 682    11951   8266   8867   1641  -2022   -691       C  
ATOM   1737  NH1 ARG D 682      33.182 -12.233  71.988  1.00 77.78           N  
ANISOU 1737  NH1 ARG D 682    12108   8316   9128   1559  -2045   -588       N  
ATOM   1738  NH2 ARG D 682      33.887 -13.672  70.344  1.00 76.70           N  
ANISOU 1738  NH2 ARG D 682    11969   8377   8795   1728  -2114   -837       N  
ATOM   1739  N   LYS D 683      26.520 -15.477  75.817  1.00 53.08           N  
ANISOU 1739  N   LYS D 683     8956   5417   5794   1808  -1514    216       N  
ATOM   1740  CA  LYS D 683      25.893 -15.833  77.085  1.00 62.85           C  
ANISOU 1740  CA  LYS D 683    10129   6766   6986   1830  -1522    508       C  
ATOM   1741  C   LYS D 683      25.023 -17.077  76.934  1.00 67.05           C  
ANISOU 1741  C   LYS D 683    10790   7370   7318   2005  -1494    380       C  
ATOM   1742  O   LYS D 683      25.056 -17.973  77.791  1.00 75.18           O  
ANISOU 1742  O   LYS D 683    11800   8453   8312   2002  -1582    516       O  
ATOM   1743  CB  LYS D 683      25.068 -14.657  77.610  1.00 67.14           C  
ANISOU 1743  CB  LYS D 683    10532   7456   7524   1821  -1402    794       C  
ATOM   1744  CG  LYS D 683      25.583 -14.048  78.911  1.00 71.50           C  
ANISOU 1744  CG  LYS D 683    10875   8076   8216   1642  -1492   1207       C  
ATOM   1745  CD  LYS D 683      27.086 -13.799  78.854  1.00 77.53           C  
ANISOU 1745  CD  LYS D 683    11655   8636   9165   1504  -1629   1118       C  
ATOM   1746  CE  LYS D 683      27.611 -13.234  80.164  1.00 83.69           C  
ANISOU 1746  CE  LYS D 683    12274   9474  10050   1367  -1715   1502       C  
ATOM   1747  NZ  LYS D 683      26.900 -11.984  80.552  1.00 88.59           N  
ANISOU 1747  NZ  LYS D 683    12700  10292  10666   1344  -1577   1825       N  
ATOM   1748  N   ALA D 684      24.257 -17.159  75.838  1.00 62.57           N  
ANISOU 1748  N   ALA D 684    10353   6810   6612   2152  -1388    125       N  
ATOM   1749  CA  ALA D 684      23.468 -18.359  75.579  1.00 57.76           C  
ANISOU 1749  CA  ALA D 684     9897   6247   5804   2332  -1385    -38       C  
ATOM   1750  C   ALA D 684      24.355 -19.576  75.347  1.00 53.29           C  
ANISOU 1750  C   ALA D 684     9392   5581   5274   2281  -1541   -193       C  
ATOM   1751  O   ALA D 684      23.984 -20.691  75.726  1.00 58.43           O  
ANISOU 1751  O   ALA D 684    10110   6275   5817   2376  -1587   -202       O  
ATOM   1752  CB  ALA D 684      22.547 -18.133  74.380  1.00 57.27           C  
ANISOU 1752  CB  ALA D 684     9967   6196   5596   2471  -1287   -272       C  
ATOM   1753  N   GLU D 685      25.538 -19.379  74.758  1.00 46.34           N  
ANISOU 1753  N   GLU D 685     8477   4599   4530   2144  -1624   -304       N  
ATOM   1754  CA  GLU D 685      26.467 -20.488  74.562  1.00 54.14           C  
ANISOU 1754  CA  GLU D 685     9506   5522   5541   2114  -1774   -438       C  
ATOM   1755  C   GLU D 685      27.044 -20.974  75.887  1.00 62.41           C  
ANISOU 1755  C   GLU D 685    10499   6530   6686   2054  -1883   -236       C  
ATOM   1756  O   GLU D 685      27.227 -22.182  76.080  1.00 66.22           O  
ANISOU 1756  O   GLU D 685    11034   6996   7129   2094  -1978   -285       O  
ATOM   1757  CB  GLU D 685      27.589 -20.078  73.605  1.00 51.40           C  
ANISOU 1757  CB  GLU D 685     9114   5149   5268   2019  -1834   -580       C  
ATOM   1758  CG  GLU D 685      27.169 -19.998  72.144  1.00 53.67           C  
ANISOU 1758  CG  GLU D 685     9410   5537   5446   2046  -1794   -726       C  
ATOM   1759  CD  GLU D 685      28.281 -19.500  71.238  1.00 54.95           C  
ANISOU 1759  CD  GLU D 685     9466   5736   5677   1964  -1844   -781       C  
ATOM   1760  OE1 GLU D 685      29.281 -18.959  71.760  1.00 60.02           O  
ANISOU 1760  OE1 GLU D 685    10065   6310   6431   1900  -1890   -746       O  
ATOM   1761  OE2 GLU D 685      28.155 -19.642  70.004  1.00 56.57           O  
ANISOU 1761  OE2 GLU D 685     9576   6031   5887   1957  -1812   -806       O  
ATOM   1762  N   GLU D 686      27.332 -20.052  76.813  1.00 70.72           N  
ANISOU 1762  N   GLU D 686    11430   7576   7864   1941  -1889     20       N  
ATOM   1763  CA  GLU D 686      27.780 -20.463  78.144  1.00 72.66           C  
ANISOU 1763  CA  GLU D 686    11596   7821   8191   1853  -2015    284       C  
ATOM   1764  C   GLU D 686      26.688 -21.232  78.885  1.00 61.67           C  
ANISOU 1764  C   GLU D 686    10179   6609   6645   1936  -1975    473       C  
ATOM   1765  O   GLU D 686      26.965 -22.255  79.532  1.00 60.17           O  
ANISOU 1765  O   GLU D 686     9981   6433   6449   1917  -2090    558       O  
ATOM   1766  CB  GLU D 686      28.223 -19.247  78.957  1.00 89.44           C  
ANISOU 1766  CB  GLU D 686    13580   9935  10467   1704  -2040    559       C  
ATOM   1767  CG  GLU D 686      29.465 -18.545  78.426  1.00103.03           C  
ANISOU 1767  CG  GLU D 686    15337  11485  12325   1622  -2125    383       C  
ATOM   1768  CD  GLU D 686      30.152 -17.700  79.483  1.00114.07           C  
ANISOU 1768  CD  GLU D 686    16639  12825  13875   1470  -2234    647       C  
ATOM   1769  OE1 GLU D 686      29.797 -17.831  80.674  1.00118.25           O  
ANISOU 1769  OE1 GLU D 686    17059  13460  14412   1416  -2261    988       O  
ATOM   1770  OE2 GLU D 686      31.047 -16.904  79.124  1.00115.43           O  
ANISOU 1770  OE2 GLU D 686    16845  12875  14139   1409  -2303    523       O  
ATOM   1771  N   GLU D 687      25.439 -20.758  78.791  1.00 56.93           N  
ANISOU 1771  N   GLU D 687     9568   6167   5895   2042  -1817    531       N  
ATOM   1772  CA  GLU D 687      24.315 -21.472  79.400  1.00 61.84           C  
ANISOU 1772  CA  GLU D 687    10182   7013   6302   2165  -1769    666       C  
ATOM   1773  C   GLU D 687      24.140 -22.862  78.791  1.00 63.92           C  
ANISOU 1773  C   GLU D 687    10615   7229   6443   2301  -1809    385       C  
ATOM   1774  O   GLU D 687      23.906 -23.844  79.513  1.00 68.51           O  
ANISOU 1774  O   GLU D 687    11168   7937   6925   2320  -1870    510       O  
ATOM   1775  CB  GLU D 687      23.032 -20.654  79.242  1.00 67.24           C  
ANISOU 1775  CB  GLU D 687    10864   7869   6814   2312  -1582    698       C  
ATOM   1776  CG  GLU D 687      23.051 -19.303  79.942  1.00 76.84           C  
ANISOU 1776  CG  GLU D 687    11881   9187   8128   2175  -1543   1031       C  
ATOM   1777  CD  GLU D 687      21.962 -18.368  79.441  1.00 83.37           C  
ANISOU 1777  CD  GLU D 687    12741  10120   8815   2344  -1346    963       C  
ATOM   1778  OE1 GLU D 687      21.188 -18.776  78.548  1.00 81.56           O  
ANISOU 1778  OE1 GLU D 687    12703   9873   8414   2580  -1247    651       O  
ATOM   1779  OE2 GLU D 687      21.880 -17.224  79.938  1.00 84.48           O  
ANISOU 1779  OE2 GLU D 687    12719  10358   9022   2241  -1305   1229       O  
ATOM   1780  N   LEU D 688      24.266 -22.962  77.465  1.00 64.70           N  
ANISOU 1780  N   LEU D 688    10867   7170   6548   2374  -1789     32       N  
ATOM   1781  CA  LEU D 688      24.123 -24.240  76.777  1.00 62.27           C  
ANISOU 1781  CA  LEU D 688    10706   6813   6143   2485  -1848   -220       C  
ATOM   1782  C   LEU D 688      25.247 -25.197  77.155  1.00 62.49           C  
ANISOU 1782  C   LEU D 688    10698   6758   6288   2376  -2011   -196       C  
ATOM   1783  O   LEU D 688      25.017 -26.401  77.304  1.00 68.67           O  
ANISOU 1783  O   LEU D 688    11528   7585   6980   2442  -2072   -228       O  
ATOM   1784  CB  LEU D 688      24.081 -24.001  75.265  1.00 43.83           C  
ANISOU 1784  CB  LEU D 688     8494   4364   3797   2534  -1820   -535       C  
ATOM   1785  CG  LEU D 688      23.651 -25.087  74.270  1.00 43.82           C  
ANISOU 1785  CG  LEU D 688     8649   4316   3685   2655  -1878   -798       C  
ATOM   1786  CD1 LEU D 688      24.805 -25.985  73.832  1.00 55.21           C  
ANISOU 1786  CD1 LEU D 688    10076   5674   5228   2566  -2020   -908       C  
ATOM   1787  CD2 LEU D 688      22.515 -25.912  74.848  1.00 46.25           C  
ANISOU 1787  CD2 LEU D 688     9025   4719   3827   2836  -1853   -752       C  
ATOM   1788  N   GLY D 689      26.464 -24.674  77.328  1.00 60.35           N  
ANISOU 1788  N   GLY D 689    10348   6369   6211   2223  -2091   -146       N  
ATOM   1789  CA  GLY D 689      27.565 -25.514  77.769  1.00 63.98           C  
ANISOU 1789  CA  GLY D 689    10789   6742   6780   2147  -2257   -124       C  
ATOM   1790  C   GLY D 689      27.374 -26.036  79.180  1.00 70.64           C  
ANISOU 1790  C   GLY D 689    11532   7697   7609   2091  -2324    200       C  
ATOM   1791  O   GLY D 689      27.674 -27.203  79.462  1.00 66.29           O  
ANISOU 1791  O   GLY D 689    11000   7143   7045   2100  -2431    198       O  
ATOM   1792  N   GLU D 690      26.860 -25.189  80.081  1.00 72.06           N  
ANISOU 1792  N   GLU D 690    11580   8017   7781   2025  -2266    512       N  
ATOM   1793  CA  GLU D 690      26.568 -25.640  81.441  1.00 82.39           C  
ANISOU 1793  CA  GLU D 690    12743   9524   9039   1958  -2325    887       C  
ATOM   1794  C   GLU D 690      25.502 -26.732  81.446  1.00 78.68           C  
ANISOU 1794  C   GLU D 690    12321   9251   8321   2097  -2278    852       C  
ATOM   1795  O   GLU D 690      25.641 -27.750  82.141  1.00 77.89           O  
ANISOU 1795  O   GLU D 690    12170   9238   8186   2062  -2381    994       O  
ATOM   1796  CB  GLU D 690      26.129 -24.463  82.313  1.00 93.21           C  
ANISOU 1796  CB  GLU D 690    13924  11076  10414   1866  -2258   1260       C  
ATOM   1797  CG  GLU D 690      27.222 -23.454  82.610  1.00103.14           C  
ANISOU 1797  CG  GLU D 690    15112  12166  11911   1714  -2332   1365       C  
ATOM   1798  CD  GLU D 690      26.711 -22.268  83.402  1.00111.08           C  
ANISOU 1798  CD  GLU D 690    15911  13388  12908   1640  -2247   1752       C  
ATOM   1799  OE1 GLU D 690      25.564 -22.329  83.893  1.00113.41           O  
ANISOU 1799  OE1 GLU D 690    16081  13999  13012   1680  -2160   1996       O  
ATOM   1800  OE2 GLU D 690      27.454 -21.271  83.529  1.00111.31           O  
ANISOU 1800  OE2 GLU D 690    15905  13285  13102   1543  -2277   1806       O  
ATOM   1801  N   LEU D 691      24.433 -26.540  80.662  1.00 73.61           N  
ANISOU 1801  N   LEU D 691    11791   8680   7499   2270  -2126    646       N  
ATOM   1802  CA  LEU D 691      23.373 -27.544  80.600  1.00 70.94           C  
ANISOU 1802  CA  LEU D 691    11531   8522   6901   2438  -2080    558       C  
ATOM   1803  C   LEU D 691      23.867 -28.853  79.993  1.00 71.79           C  
ANISOU 1803  C   LEU D 691    11758   8482   7036   2468  -2190    315       C  
ATOM   1804  O   LEU D 691      23.523 -29.940  80.478  1.00 81.83           O  
ANISOU 1804  O   LEU D 691    13016   9903   8172   2498  -2241    384       O  
ATOM   1805  CB  LEU D 691      22.184 -27.005  79.805  1.00 61.20           C  
ANISOU 1805  CB  LEU D 691    10420   7348   5485   2650  -1907    345       C  
ATOM   1806  CG  LEU D 691      21.189 -26.134  80.569  1.00 62.40           C  
ANISOU 1806  CG  LEU D 691    10454   7787   5468   2715  -1767    592       C  
ATOM   1807  CD1 LEU D 691      20.077 -25.679  79.643  1.00 55.57           C  
ANISOU 1807  CD1 LEU D 691     9746   6932   4434   2975  -1606    315       C  
ATOM   1808  CD2 LEU D 691      20.621 -26.894  81.758  1.00 65.32           C  
ANISOU 1808  CD2 LEU D 691    10696   8492   5632   2719  -1787    864       C  
ATOM   1809  N   GLU D 692      24.684 -28.766  78.935  1.00 69.93           N  
ANISOU 1809  N   GLU D 692    11620   7987   6962   2456  -2230     46       N  
ATOM   1810  CA  GLU D 692      25.223 -29.968  78.304  1.00 74.70           C  
ANISOU 1810  CA  GLU D 692    12308   8474   7600   2481  -2336   -161       C  
ATOM   1811  C   GLU D 692      26.142 -30.726  79.249  1.00 75.70           C  
ANISOU 1811  C   GLU D 692    12338   8598   7828   2360  -2486     31       C  
ATOM   1812  O   GLU D 692      26.068 -31.957  79.336  1.00 73.56           O  
ANISOU 1812  O   GLU D 692    12086   8381   7483   2394  -2558     10       O  
ATOM   1813  CB  GLU D 692      25.964 -29.602  77.018  1.00 80.82           C  
ANISOU 1813  CB  GLU D 692    13159   9040   8510   2483  -2344   -438       C  
ATOM   1814  CG  GLU D 692      25.110 -29.647  75.763  1.00 88.74           C  
ANISOU 1814  CG  GLU D 692    14288  10014   9413   2621  -2272   -689       C  
ATOM   1815  CD  GLU D 692      25.906 -29.340  74.508  1.00 94.89           C  
ANISOU 1815  CD  GLU D 692    15093  10651  10310   2594  -2298   -907       C  
ATOM   1816  OE1 GLU D 692      27.105 -29.011  74.630  1.00 95.70           O  
ANISOU 1816  OE1 GLU D 692    15122  10702  10537   2489  -2354   -889       O  
ATOM   1817  OE2 GLU D 692      25.335 -29.434  73.402  1.00 98.69           O  
ANISOU 1817  OE2 GLU D 692    15625  11103  10768   2662  -2266  -1054       O  
ATOM   1818  N   ALA D 693      27.004 -30.007  79.978  1.00 83.04           N  
ANISOU 1818  N   ALA D 693    13164   9457   8931   2218  -2548    227       N  
ATOM   1819  CA  ALA D 693      27.895 -30.657  80.934  1.00 88.25           C  
ANISOU 1819  CA  ALA D 693    13742  10086   9704   2109  -2712    423       C  
ATOM   1820  C   ALA D 693      27.115 -31.327  82.059  1.00 93.81           C  
ANISOU 1820  C   ALA D 693    14330  11059  10253   2084  -2726    737       C  
ATOM   1821  O   ALA D 693      27.423 -32.466  82.437  1.00 95.43           O  
ANISOU 1821  O   ALA D 693    14520  11289  10449   2070  -2838    790       O  
ATOM   1822  CB  ALA D 693      28.888 -29.643  81.502  1.00 90.40           C  
ANISOU 1822  CB  ALA D 693    13943  10218  10188   1970  -2787    568       C  
ATOM   1823  N   LYS D 694      26.086 -30.649  82.584  1.00 93.67           N  
ANISOU 1823  N   LYS D 694    14219  11280  10092   2087  -2611    955       N  
ATOM   1824  CA  LYS D 694      25.295 -31.228  83.668  1.00 96.42           C  
ANISOU 1824  CA  LYS D 694    14426  11962  10248   2065  -2619   1280       C  
ATOM   1825  C   LYS D 694      24.545 -32.476  83.211  1.00 98.09           C  
ANISOU 1825  C   LYS D 694    14753  12282  10236   2207  -2598   1072       C  
ATOM   1826  O   LYS D 694      24.566 -33.506  83.900  1.00103.68           O  
ANISOU 1826  O   LYS D 694    15384  13135  10873   2161  -2693   1240       O  
ATOM   1827  CB  LYS D 694      24.323 -30.191  84.232  1.00 96.23           C  
ANISOU 1827  CB  LYS D 694    14272  12203  10085   2056  -2494   1538       C  
ATOM   1828  CG  LYS D 694      24.889 -29.391  85.397  1.00 95.34           C  
ANISOU 1828  CG  LYS D 694    13917  12179  10130   1863  -2563   1994       C  
ATOM   1829  CD  LYS D 694      23.841 -28.469  85.999  1.00 92.09           C  
ANISOU 1829  CD  LYS D 694    13346  12085   9559   1826  -2465   2300       C  
ATOM   1830  CE  LYS D 694      24.470 -27.453  86.938  1.00 87.18           C  
ANISOU 1830  CE  LYS D 694    12464  11546   9113   1671  -2493   2736       C  
ATOM   1831  NZ  LYS D 694      23.464 -26.476  87.439  1.00 86.06           N  
ANISOU 1831  NZ  LYS D 694    12190  11644   8863   1540  -2460   3015       N  
ATOM   1832  N   LEU D 695      23.900 -32.418  82.037  1.00 95.79           N  
ANISOU 1832  N   LEU D 695    14640  11918   9838   2378  -2484    710       N  
ATOM   1833  CA  LEU D 695      23.166 -33.588  81.559  1.00 96.45           C  
ANISOU 1833  CA  LEU D 695    14838  12092   9719   2515  -2475    503       C  
ATOM   1834  C   LEU D 695      24.110 -34.732  81.207  1.00 96.74           C  
ANISOU 1834  C   LEU D 695    14913  11954   9888   2464  -2622    386       C  
ATOM   1835  O   LEU D 695      23.805 -35.896  81.489  1.00101.16           O  
ANISOU 1835  O   LEU D 695    15464  12657  10316   2480  -2680    418       O  
ATOM   1836  CB  LEU D 695      22.289 -33.226  80.358  1.00 99.69           C  
ANISOU 1836  CB  LEU D 695    15423  12433  10021   2703  -2347    163       C  
ATOM   1837  CG  LEU D 695      21.509 -34.411  79.766  1.00104.58           C  
ANISOU 1837  CG  LEU D 695    16167  13109  10461   2836  -2361    -65       C  
ATOM   1838  CD1 LEU D 695      20.241 -34.676  80.550  1.00105.73           C  
ANISOU 1838  CD1 LEU D 695    16277  13603  10293   2952  -2280     46       C  
ATOM   1839  CD2 LEU D 695      21.174 -34.211  78.305  1.00104.92           C  
ANISOU 1839  CD2 LEU D 695    16379  12935  10552   2949  -2327   -406       C  
ATOM   1840  N   ASN D 696      25.277 -34.426  80.628  1.00 94.90           N  
ANISOU 1840  N   ASN D 696    14713  11440   9905   2408  -2684    259       N  
ATOM   1841  CA  ASN D 696      26.205 -35.485  80.247  1.00 99.90           C  
ANISOU 1841  CA  ASN D 696    15376  11930  10652   2390  -2815    139       C  
ATOM   1842  C   ASN D 696      26.811 -36.163  81.472  1.00107.18           C  
ANISOU 1842  C   ASN D 696    16171  12924  11628   2276  -2952    430       C  
ATOM   1843  O   ASN D 696      26.990 -37.387  81.481  1.00111.19           O  
ANISOU 1843  O   ASN D 696    16681  13465  12101   2286  -3041    409       O  
ATOM   1844  CB  ASN D 696      27.301 -34.922  79.342  1.00 96.95           C  
ANISOU 1844  CB  ASN D 696    15056  11286  10492   2387  -2838    -74       C  
ATOM   1845  CG  ASN D 696      27.832 -35.952  78.364  1.00 95.34           C  
ANISOU 1845  CG  ASN D 696    14910  10990  10325   2451  -2906   -302       C  
ATOM   1846  OD1 ASN D 696      27.100 -36.835  77.915  1.00 95.97           O  
ANISOU 1846  OD1 ASN D 696    15029  11166  10268   2515  -2895   -386       O  
ATOM   1847  ND2 ASN D 696      29.111 -35.841  78.024  1.00 94.77           N  
ANISOU 1847  ND2 ASN D 696    14832  10750  10425   2438  -2982   -397       N  
ATOM   1848  N   GLU D 697      27.110 -35.396  82.526  1.00108.94           N  
ANISOU 1848  N   GLU D 697    16269  13184  11941   2159  -2980    730       N  
ATOM   1849  CA  GLU D 697      27.623 -36.025  83.738  1.00109.09           C  
ANISOU 1849  CA  GLU D 697    16151  13284  12013   2047  -3121   1048       C  
ATOM   1850  C   GLU D 697      26.528 -36.759  84.504  1.00110.35           C  
ANISOU 1850  C   GLU D 697    16204  13812  11914   2047  -3096   1288       C  
ATOM   1851  O   GLU D 697      26.824 -37.720  85.222  1.00110.40           O  
ANISOU 1851  O   GLU D 697    16121  13913  11911   1992  -3213   1479       O  
ATOM   1852  CB  GLU D 697      28.306 -34.997  84.637  1.00110.45           C  
ANISOU 1852  CB  GLU D 697    16212  13384  12369   1918  -3176   1317       C  
ATOM   1853  CG  GLU D 697      29.734 -34.687  84.224  1.00112.05           C  
ANISOU 1853  CG  GLU D 697    16518  13219  12837   1896  -3292   1115       C  
ATOM   1854  CD  GLU D 697      30.587 -34.215  85.385  1.00120.13           C  
ANISOU 1854  CD  GLU D 697    17458  14148  14040   1761  -3436   1395       C  
ATOM   1855  OE1 GLU D 697      30.027 -33.639  86.342  1.00124.70           O  
ANISOU 1855  OE1 GLU D 697    17882  14941  14557   1686  -3390   1745       O  
ATOM   1856  OE2 GLU D 697      31.817 -34.427  85.342  1.00122.27           O  
ANISOU 1856  OE2 GLU D 697    17822  14139  14496   1744  -3604   1262       O  
ATOM   1857  N   ASN D 698      25.266 -36.335  84.369  1.00112.46           N  
ANISOU 1857  N   ASN D 698    16482  14297  11949   2121  -2949   1273       N  
ATOM   1858  CA  ASN D 698      24.185 -37.110  84.974  1.00112.86           C  
ANISOU 1858  CA  ASN D 698    16465  14709  11706   2147  -2928   1430       C  
ATOM   1859  C   ASN D 698      23.925 -38.406  84.213  1.00105.92           C  
ANISOU 1859  C   ASN D 698    15728  13807  10709   2253  -2950   1135       C  
ATOM   1860  O   ASN D 698      23.526 -39.407  84.818  1.00105.10           O  
ANISOU 1860  O   ASN D 698    15556  13942  10436   2231  -3006   1282       O  
ATOM   1861  CB  ASN D 698      22.910 -36.273  85.056  1.00121.34           C  
ANISOU 1861  CB  ASN D 698    17539  16019  12544   2235  -2762   1454       C  
ATOM   1862  CG  ASN D 698      22.905 -35.334  86.246  1.00129.38           C  
ANISOU 1862  CG  ASN D 698    18331  17232  13595   2077  -2776   1914       C  
ATOM   1863  OD1 ASN D 698      22.283 -35.616  87.270  1.00133.12           O  
ANISOU 1863  OD1 ASN D 698    18665  18034  13881   1995  -2814   2241       O  
ATOM   1864  ND2 ASN D 698      23.604 -34.212  86.119  1.00130.69           N  
ANISOU 1864  ND2 ASN D 698    18465  17192  14000   2011  -2765   1952       N  
ATOM   1865  N   LEU D 699      24.138 -38.406  82.895  1.00103.58           N  
ANISOU 1865  N   LEU D 699    15609  13247  10499   2353  -2918    748       N  
ATOM   1866  CA  LEU D 699      23.997 -39.642  82.130  1.00104.43           C  
ANISOU 1866  CA  LEU D 699    15821  13325  10533   2422  -2963    507       C  
ATOM   1867  C   LEU D 699      25.181 -40.577  82.347  1.00113.93           C  
ANISOU 1867  C   LEU D 699    16964  14412  11912   2331  -3126    584       C  
ATOM   1868  O   LEU D 699      25.013 -41.801  82.312  1.00119.71           O  
ANISOU 1868  O   LEU D 699    17697  15246  12540   2338  -3192    561       O  
ATOM   1869  CB  LEU D 699      23.833 -39.337  80.640  1.00 93.95           C  
ANISOU 1869  CB  LEU D 699    14661  11783   9254   2533  -2894    130       C  
ATOM   1870  CG  LEU D 699      22.576 -38.594  80.179  1.00 91.25           C  
ANISOU 1870  CG  LEU D 699    14418  11514   8736   2666  -2744    -21       C  
ATOM   1871  CD1 LEU D 699      22.417 -38.700  78.671  1.00 88.26           C  
ANISOU 1871  CD1 LEU D 699    14186  10928   8421   2743  -2735   -356       C  
ATOM   1872  CD2 LEU D 699      21.335 -39.120  80.886  1.00 92.21           C  
ANISOU 1872  CD2 LEU D 699    14524  11968   8544   2740  -2697     67       C  
ATOM   1873  N   ARG D 700      26.381 -40.026  82.565  1.00113.94           N  
ANISOU 1873  N   ARG D 700    16920  14199  12174   2257  -3196    662       N  
ATOM   1874  CA  ARG D 700      27.552 -40.872  82.787  1.00120.95           C  
ANISOU 1874  CA  ARG D 700    17769  14956  13229   2208  -3354    711       C  
ATOM   1875  C   ARG D 700      27.493 -41.589  84.130  1.00125.97           C  
ANISOU 1875  C   ARG D 700    18251  15814  13797   2112  -3452   1075       C  
ATOM   1876  O   ARG D 700      28.094 -42.658  84.284  1.00132.09           O  
ANISOU 1876  O   ARG D 700    19002  16562  14623   2100  -3575   1105       O  
ATOM   1877  CB  ARG D 700      28.835 -40.045  82.694  1.00123.79           C  
ANISOU 1877  CB  ARG D 700    18148  15020  13866   2178  -3411    664       C  
ATOM   1878  CG  ARG D 700      29.361 -39.854  81.282  1.00124.45           C  
ANISOU 1878  CG  ARG D 700    18354  14888  14044   2279  -3376    301       C  
ATOM   1879  CD  ARG D 700      30.594 -38.966  81.281  1.00124.13           C  
ANISOU 1879  CD  ARG D 700    18334  14595  14233   2257  -3435    250       C  
ATOM   1880  NE  ARG D 700      30.910 -38.455  79.951  1.00122.00           N  
ANISOU 1880  NE  ARG D 700    18153  14195  14009   2351  -3362    -62       N  
ATOM   1881  CZ  ARG D 700      31.717 -37.426  79.720  1.00117.29           C  
ANISOU 1881  CZ  ARG D 700    17588  13425  13550   2347  -3367   -160       C  
ATOM   1882  NH1 ARG D 700      32.288 -36.792  80.735  1.00120.74           N  
ANISOU 1882  NH1 ARG D 700    17996  13766  14114   2247  -3455     21       N  
ATOM   1883  NH2 ARG D 700      31.952 -37.027  78.477  1.00110.77           N  
ANISOU 1883  NH2 ARG D 700    16815  12540  12732   2436  -3295   -423       N  
ATOM   1884  N   ARG D 701      26.771 -41.030  85.105  1.00128.09           N  
ANISOU 1884  N   ARG D 701    18395  16334  13941   2050  -3399   1375       N  
ATOM   1885  CA  ARG D 701      26.666 -41.638  86.426  1.00129.02           C  
ANISOU 1885  CA  ARG D 701    18320  16729  13973   1957  -3484   1780       C  
ATOM   1886  C   ARG D 701      25.831 -42.913  86.430  1.00131.92           C  
ANISOU 1886  C   ARG D 701    18680  17365  14076   1984  -3494   1770       C  
ATOM   1887  O   ARG D 701      25.825 -43.624  87.441  1.00139.25           O  
ANISOU 1887  O   ARG D 701    19444  18536  14929   1911  -3579   2093       O  
ATOM   1888  CB  ARG D 701      26.082 -40.629  87.418  1.00130.19           C  
ANISOU 1888  CB  ARG D 701    18293  17140  14033   1887  -3413   2141       C  
ATOM   1889  CG  ARG D 701      27.079 -39.584  87.904  1.00132.35           C  
ANISOU 1889  CG  ARG D 701    18512  17202  14572   1831  -3452   2290       C  
ATOM   1890  CD  ARG D 701      26.382 -38.447  88.640  1.00137.12           C  
ANISOU 1890  CD  ARG D 701    18944  18088  15067   1798  -3338   2608       C  
ATOM   1891  NE  ARG D 701      27.284 -37.331  88.912  1.00139.32           N  
ANISOU 1891  NE  ARG D 701    19232  18112  15592   1765  -3362   2663       N  
ATOM   1892  CZ  ARG D 701      26.918 -36.205  89.518  1.00138.54           C  
ANISOU 1892  CZ  ARG D 701    19007  18194  15438   1770  -3261   2913       C  
ATOM   1893  NH1 ARG D 701      25.662 -36.040  89.911  1.00137.72           N  
ANISOU 1893  NH1 ARG D 701    18719  18572  15036   1812  -3120   3162       N  
ATOM   1894  NH2 ARG D 701      27.805 -35.241  89.724  1.00138.13           N  
ANISOU 1894  NH2 ARG D 701    19017  17842  15623   1716  -3319   2911       N  
ATOM   1895  N   ASN D 702      25.131 -43.218  85.340  1.00128.93           N  
ANISOU 1895  N   ASN D 702    18472  16960  13554   2096  -3410   1414       N  
ATOM   1896  CA  ASN D 702      24.393 -44.468  85.223  1.00120.34           C  
ANISOU 1896  CA  ASN D 702    17413  16085  12227   2129  -3430   1345       C  
ATOM   1897  C   ASN D 702      25.185 -45.479  84.398  1.00109.72           C  
ANISOU 1897  C   ASN D 702    16145  14524  11019   2154  -3525   1124       C  
ATOM   1898  O   ASN D 702      24.624 -46.196  83.569  1.00102.12           O  
ANISOU 1898  O   ASN D 702    15289  13590   9922   2220  -3505    879       O  
ATOM   1899  CB  ASN D 702      23.020 -44.227  84.594  1.00114.39           C  
ANISOU 1899  CB  ASN D 702    16798  15461  11205   2259  -3281   1094       C  
ATOM   1900  CG  ASN D 702      22.118 -43.381  85.471  1.00113.23           C  
ANISOU 1900  CG  ASN D 702    16568  15592  10864   2260  -3183   1319       C  
ATOM   1901  OD1 ASN D 702      22.025 -43.600  86.680  1.00114.64           O  
ANISOU 1901  OD1 ASN D 702    16571  16033  10954   2139  -3251   1702       O  
ATOM   1902  ND2 ASN D 702      21.447 -42.406  84.868  1.00110.72           N  
ANISOU 1902  ND2 ASN D 702    16364  15223  10479   2392  -3030   1103       N  
TER    1903      ASN D 702                                                      
ATOM   1904  N   ARG I 496      -8.412 -16.666  61.529  1.00138.27           N  
ANISOU 1904  N   ARG I 496    19411  21873  11252    929  -1219    344       N  
ATOM   1905  CA  ARG I 496      -8.646 -17.760  62.463  1.00142.53           C  
ANISOU 1905  CA  ARG I 496    19997  22156  12002   1092  -1256    386       C  
ATOM   1906  C   ARG I 496      -8.874 -17.233  63.877  1.00145.10           C  
ANISOU 1906  C   ARG I 496    20218  22610  12303   1056  -1304    627       C  
ATOM   1907  O   ARG I 496      -9.707 -17.758  64.616  1.00145.80           O  
ANISOU 1907  O   ARG I 496    20330  22647  12420   1253  -1333    827       O  
ATOM   1908  CB  ARG I 496      -7.472 -18.739  62.450  1.00146.07           C  
ANISOU 1908  CB  ARG I 496    20480  22274  12746    976  -1254     62       C  
ATOM   1909  CG  ARG I 496      -7.376 -19.581  61.188  1.00148.43           C  
ANISOU 1909  CG  ARG I 496    20900  22376  13120   1069  -1211   -168       C  
ATOM   1910  CD  ARG I 496      -6.190 -20.532  61.254  1.00151.99           C  
ANISOU 1910  CD  ARG I 496    21361  22484  13906    948  -1211   -488       C  
ATOM   1911  NE  ARG I 496      -5.923 -21.175  59.970  1.00153.14           N  
ANISOU 1911  NE  ARG I 496    21604  22464  14119    983  -1156   -751       N  
ATOM   1912  CZ  ARG I 496      -4.864 -21.943  59.727  1.00151.53           C  
ANISOU 1912  CZ  ARG I 496    21403  21964  14206    867  -1136  -1078       C  
ATOM   1913  NH1 ARG I 496      -3.972 -22.166  60.683  1.00152.38           N  
ANISOU 1913  NH1 ARG I 496    21413  21898  14586    710  -1168  -1178       N  
ATOM   1914  NH2 ARG I 496      -4.697 -22.487  58.530  1.00149.07           N  
ANISOU 1914  NH2 ARG I 496    21181  21520  13940    908  -1080  -1306       N  
ATOM   1915  N   GLN I 497      -8.118 -16.194  64.242  1.00145.89           N  
ANISOU 1915  N   GLN I 497    20197  22892  12343    789  -1308    597       N  
ATOM   1916  CA  GLN I 497      -8.269 -15.585  65.562  1.00145.74           C  
ANISOU 1916  CA  GLN I 497    20066  23011  12300    731  -1351    818       C  
ATOM   1917  C   GLN I 497      -9.610 -14.869  65.680  1.00142.87           C  
ANISOU 1917  C   GLN I 497    19672  22913  11700    906  -1355   1158       C  
ATOM   1918  O   GLN I 497     -10.263 -14.923  66.729  1.00142.39           O  
ANISOU 1918  O   GLN I 497    19576  22882  11645   1015  -1382   1384       O  
ATOM   1919  CB  GLN I 497      -7.099 -14.627  65.818  1.00149.41           C  
ANISOU 1919  CB  GLN I 497    20401  23611  12757    388  -1347    670       C  
ATOM   1920  CG  GLN I 497      -7.331 -13.517  66.846  1.00152.16           C  
ANISOU 1920  CG  GLN I 497    20613  24226  12976    293  -1381    917       C  
ATOM   1921  CD  GLN I 497      -7.712 -14.040  68.222  1.00151.20           C  
ANISOU 1921  CD  GLN I 497    20469  23977  13002    411  -1425   1107       C  
ATOM   1922  OE1 GLN I 497      -7.204 -15.067  68.674  1.00151.33           O  
ANISOU 1922  OE1 GLN I 497    20518  23696  13284    420  -1444    984       O  
ATOM   1923  NE2 GLN I 497      -8.615 -13.335  68.892  1.00149.20           N  
ANISOU 1923  NE2 GLN I 497    20151  23952  12586    494  -1445   1417       N  
ATOM   1924  N   GLN I 498     -10.044 -14.209  64.606  1.00137.67           N  
ANISOU 1924  N   GLN I 498    19016  22444  10849    932  -1328   1202       N  
ATOM   1925  CA  GLN I 498     -11.346 -13.549  64.604  1.00130.00           C  
ANISOU 1925  CA  GLN I 498    17997  21694   9704   1110  -1327   1515       C  
ATOM   1926  C   GLN I 498     -12.480 -14.570  64.612  1.00126.96           C  
ANISOU 1926  C   GLN I 498    17706  21149   9381   1433  -1303   1606       C  
ATOM   1927  O   GLN I 498     -13.510 -14.363  65.270  1.00127.96           O  
ANISOU 1927  O   GLN I 498    17782  21384   9453   1585  -1300   1851       O  
ATOM   1928  CB  GLN I 498     -11.442 -12.629  63.386  1.00124.79           C  
ANISOU 1928  CB  GLN I 498    17300  21252   8863   1039  -1315   1542       C  
ATOM   1929  CG  GLN I 498     -12.679 -11.755  63.313  1.00123.04           C  
ANISOU 1929  CG  GLN I 498    16985  21268   8497   1183  -1322   1872       C  
ATOM   1930  CD  GLN I 498     -12.581 -10.724  62.202  1.00122.54           C  
ANISOU 1930  CD  GLN I 498    16854  21431   8276   1047  -1335   1925       C  
ATOM   1931  OE1 GLN I 498     -11.581 -10.666  61.484  1.00121.34           O  
ANISOU 1931  OE1 GLN I 498    16733  21297   8075    837  -1333   1706       O  
ATOM   1932  NE2 GLN I 498     -13.617  -9.907  62.053  1.00122.37           N  
ANISOU 1932  NE2 GLN I 498    16726  21447   8322   1126  -1327   2173       N  
ATOM   1933  N   ARG I 499     -12.287 -15.694  63.915  1.00127.20           N  
ANISOU 1933  N   ARG I 499    17869  20927   9533   1529  -1282   1396       N  
ATOM   1934  CA  ARG I 499     -13.358 -16.669  63.739  1.00126.32           C  
ANISOU 1934  CA  ARG I 499    17851  20683   9463   1824  -1254   1452       C  
ATOM   1935  C   ARG I 499     -13.675 -17.411  65.034  1.00126.70           C  
ANISOU 1935  C   ARG I 499    17906  20633   9600   1909  -1283   1554       C  
ATOM   1936  O   ARG I 499     -14.840 -17.742  65.281  1.00123.74           O  
ANISOU 1936  O   ARG I 499    17544  20295   9178   2125  -1257   1709       O  
ATOM   1937  CB  ARG I 499     -12.991 -17.640  62.606  1.00123.44           C  
ANISOU 1937  CB  ARG I 499    17619  20079   9203   1883  -1230   1190       C  
ATOM   1938  CG  ARG I 499     -12.590 -19.055  63.021  1.00121.22           C  
ANISOU 1938  CG  ARG I 499    17437  19491   9132   1936  -1256   1036       C  
ATOM   1939  CD  ARG I 499     -11.851 -19.790  61.913  1.00121.65           C  
ANISOU 1939  CD  ARG I 499    17593  19316   9312   1908  -1237    735       C  
ATOM   1940  NE  ARG I 499     -12.631 -19.885  60.683  1.00119.66           N  
ANISOU 1940  NE  ARG I 499    17406  19085   8973   2088  -1182    723       N  
ATOM   1941  CZ  ARG I 499     -12.358 -20.730  59.693  1.00116.39           C  
ANISOU 1941  CZ  ARG I 499    17099  18459   8664   2147  -1156    496       C  
ATOM   1942  NH1 ARG I 499     -11.325 -21.555  59.790  1.00115.42           N  
ANISOU 1942  NH1 ARG I 499    17026  18082   8746   2042  -1182    260       N  
ATOM   1943  NH2 ARG I 499     -13.119 -20.751  58.607  1.00113.99           N  
ANISOU 1943  NH2 ARG I 499    16840  18184   8287   2312  -1105    506       N  
ATOM   1944  N   LYS I 500     -12.680 -17.632  65.899  1.00129.15           N  
ANISOU 1944  N   LYS I 500    18194  20834  10043   1731  -1334   1480       N  
ATOM   1945  CA  LYS I 500     -12.953 -18.368  67.128  1.00133.82           C  
ANISOU 1945  CA  LYS I 500    18786  21335  10725   1796  -1374   1605       C  
ATOM   1946  C   LYS I 500     -13.683 -17.497  68.145  1.00129.45           C  
ANISOU 1946  C   LYS I 500    18117  21038  10030   1803  -1372   1888       C  
ATOM   1947  O   LYS I 500     -14.595 -17.976  68.829  1.00134.05           O  
ANISOU 1947  O   LYS I 500    18706  21646  10579   1954  -1367   2053       O  
ATOM   1948  CB  LYS I 500     -11.654 -18.945  67.703  1.00139.96           C  
ANISOU 1948  CB  LYS I 500    19559  21877  11741   1610  -1435   1446       C  
ATOM   1949  CG  LYS I 500     -10.539 -17.946  67.957  1.00143.37           C  
ANISOU 1949  CG  LYS I 500    19879  22392  12204   1326  -1445   1358       C  
ATOM   1950  CD  LYS I 500      -9.250 -18.647  68.367  1.00142.27           C  
ANISOU 1950  CD  LYS I 500    19726  21966  12365   1156  -1489   1151       C  
ATOM   1951  CE  LYS I 500      -9.463 -19.575  69.553  1.00139.48           C  
ANISOU 1951  CE  LYS I 500    19370  21453  12174   1232  -1559   1314       C  
ATOM   1952  NZ  LYS I 500      -8.203 -20.269  69.936  1.00138.04           N  
ANISOU 1952  NZ  LYS I 500    19149  20959  12340   1070  -1611   1128       N  
ATOM   1953  N   ALA I 501     -13.342 -16.208  68.222  1.00125.93           N  
ANISOU 1953  N   ALA I 501    17558  20801   9488   1636  -1372   1945       N  
ATOM   1954  CA  ALA I 501     -14.108 -15.297  69.067  1.00121.53           C  
ANISOU 1954  CA  ALA I 501    16882  20496   8798   1653  -1365   2215       C  
ATOM   1955  C   ALA I 501     -15.507 -15.063  68.512  1.00120.23           C  
ANISOU 1955  C   ALA I 501    16710  20472   8498   1885  -1302   2360       C  
ATOM   1956  O   ALA I 501     -16.458 -14.890  69.285  1.00 97.08           O  
ANISOU 1956  O   ALA I 501    13712  17658   5516   1987  -1275   2560       O  
ATOM   1957  CB  ALA I 501     -13.366 -13.971  69.227  1.00114.62           C  
ANISOU 1957  CB  ALA I 501    15880  19813   7857   1407  -1389   2235       C  
ATOM   1958  N   GLU I 502     -15.659 -15.074  67.181  1.00122.20           N  
ANISOU 1958  N   GLU I 502    17016  20694   8722   1963  -1270   2250       N  
ATOM   1959  CA  GLU I 502     -16.990 -14.969  66.587  1.00121.72           C  
ANISOU 1959  CA  GLU I 502    16926  20630   8690   2154  -1191   2331       C  
ATOM   1960  C   GLU I 502     -17.848 -16.187  66.922  1.00118.64           C  
ANISOU 1960  C   GLU I 502    16612  20089   8376   2356  -1147   2315       C  
ATOM   1961  O   GLU I 502     -19.027 -16.046  67.275  1.00119.85           O  
ANISOU 1961  O   GLU I 502    16684  20283   8569   2466  -1078   2433       O  
ATOM   1962  CB  GLU I 502     -16.860 -14.783  65.074  1.00121.36           C  
ANISOU 1962  CB  GLU I 502    16919  20548   8645   2167  -1171   2208       C  
ATOM   1963  CG  GLU I 502     -18.094 -15.141  64.268  1.00118.09           C  
ANISOU 1963  CG  GLU I 502    16510  20033   8326   2391  -1088   2212       C  
ATOM   1964  CD  GLU I 502     -17.844 -15.073  62.773  1.00113.72           C  
ANISOU 1964  CD  GLU I 502    16004  19432   7773   2398  -1078   2092       C  
ATOM   1965  OE1 GLU I 502     -16.884 -14.388  62.361  1.00111.50           O  
ANISOU 1965  OE1 GLU I 502    15708  19250   7405   2199  -1127   2054       O  
ATOM   1966  OE2 GLU I 502     -18.604 -15.707  62.012  1.00110.68           O  
ANISOU 1966  OE2 GLU I 502    15666  18924   7466   2592  -1019   2032       O  
ATOM   1967  N   ILE I 503     -17.264 -17.388  66.840  1.00117.42           N  
ANISOU 1967  N   ILE I 503    16603  19781   8232   2401  -1189   2168       N  
ATOM   1968  CA  ILE I 503     -17.968 -18.611  67.226  1.00112.84           C  
ANISOU 1968  CA  ILE I 503    16094  19070   7709   2558  -1167   2158       C  
ATOM   1969  C   ILE I 503     -18.305 -18.584  68.715  1.00113.41           C  
ANISOU 1969  C   ILE I 503    16091  19237   7764   2510  -1180   2343       C  
ATOM   1970  O   ILE I 503     -19.383 -19.030  69.133  1.00115.75           O  
ANISOU 1970  O   ILE I 503    16364  19535   8082   2616  -1118   2404       O  
ATOM   1971  CB  ILE I 503     -17.121 -19.841  66.838  1.00106.32           C  
ANISOU 1971  CB  ILE I 503    15420  18006   6970   2565  -1226   1956       C  
ATOM   1972  CG1 ILE I 503     -17.171 -20.068  65.326  1.00103.42           C  
ANISOU 1972  CG1 ILE I 503    15135  17533   6626   2667  -1183   1771       C  
ATOM   1973  CG2 ILE I 503     -17.575 -21.104  67.564  1.00 94.11           C  
ANISOU 1973  CG2 ILE I 503    13938  16361   5460   2666  -1248   1992       C  
ATOM   1974  CD1 ILE I 503     -18.556 -20.367  64.796  1.00 99.95           C  
ANISOU 1974  CD1 ILE I 503    14688  17090   6199   2878  -1087   1789       C  
ATOM   1975  N   MET I 504     -17.403 -18.030  69.530  1.00115.04           N  
ANISOU 1975  N   MET I 504    16246  19545   7919   2341  -1256   2431       N  
ATOM   1976  CA  MET I 504     -17.649 -17.889  70.963  1.00122.74           C  
ANISOU 1976  CA  MET I 504    17137  20625   8874   2277  -1273   2626       C  
ATOM   1977  C   MET I 504     -18.845 -16.984  71.243  1.00125.68           C  
ANISOU 1977  C   MET I 504    17373  21131   9248   2309  -1174   2755       C  
ATOM   1978  O   MET I 504     -19.716 -17.319  72.057  1.00126.66           O  
ANISOU 1978  O   MET I 504    17459  21293   9372   2364  -1128   2854       O  
ATOM   1979  CB  MET I 504     -16.390 -17.352  71.646  1.00129.08           C  
ANISOU 1979  CB  MET I 504    17877  21415   9750   2033  -1352   2634       C  
ATOM   1980  CG  MET I 504     -16.631 -16.752  73.012  1.00130.68           C  
ANISOU 1980  CG  MET I 504    17959  21796   9899   1951  -1362   2863       C  
ATOM   1981  SD  MET I 504     -16.569 -17.958  74.343  1.00129.68           S  
ANISOU 1981  SD  MET I 504    17861  21549   9862   1928  -1425   2972       S  
ATOM   1982  CE  MET I 504     -17.149 -16.939  75.692  1.00130.96           C  
ANISOU 1982  CE  MET I 504    17863  21994   9901   1862  -1399   3250       C  
ATOM   1983  N   GLU I 505     -18.907 -15.833  70.568  1.00126.56           N  
ANISOU 1983  N   GLU I 505    17400  21334   9352   2275  -1143   2761       N  
ATOM   1984  CA  GLU I 505     -20.039 -14.927  70.757  1.00123.88           C  
ANISOU 1984  CA  GLU I 505    16916  21130   9022   2329  -1059   2896       C  
ATOM   1985  C   GLU I 505     -21.336 -15.556  70.252  1.00120.11           C  
ANISOU 1985  C   GLU I 505    16450  20601   8585   2545   -955   2847       C  
ATOM   1986  O   GLU I 505     -22.396 -15.382  70.867  1.00116.85           O  
ANISOU 1986  O   GLU I 505    15938  20298   8161   2623   -877   2950       O  
ATOM   1987  CB  GLU I 505     -19.766 -13.590  70.063  1.00121.44           C  
ANISOU 1987  CB  GLU I 505    16508  20930   8702   2241  -1071   2934       C  
ATOM   1988  CG  GLU I 505     -20.977 -12.670  69.959  1.00119.42           C  
ANISOU 1988  CG  GLU I 505    16094  20804   8475   2337   -992   3075       C  
ATOM   1989  CD  GLU I 505     -20.819 -11.600  68.899  1.00118.44           C  
ANISOU 1989  CD  GLU I 505    15894  20749   8359   2288  -1013   3104       C  
ATOM   1990  OE1 GLU I 505     -19.689 -11.102  68.714  1.00118.33           O  
ANISOU 1990  OE1 GLU I 505    15896  20771   8293   2097  -1093   3072       O  
ATOM   1991  OE2 GLU I 505     -21.831 -11.250  68.254  1.00118.21           O  
ANISOU 1991  OE2 GLU I 505    15777  20758   8380   2437   -949   3169       O  
ATOM   1992  N   SER I 506     -21.260 -16.334  69.166  1.00121.81           N  
ANISOU 1992  N   SER I 506    16782  20666   8836   2646   -948   2680       N  
ATOM   1993  CA  SER I 506     -22.451 -17.004  68.648  1.00120.97           C  
ANISOU 1993  CA  SER I 506    16687  20517   8761   2856   -848   2613       C  
ATOM   1994  C   SER I 506     -22.981 -18.055  69.623  1.00128.93           C  
ANISOU 1994  C   SER I 506    17733  21518   9736   2900   -823   2620       C  
ATOM   1995  O   SER I 506     -24.191 -18.108  69.884  1.00130.86           O  
ANISOU 1995  O   SER I 506    17899  21869   9955   3020   -720   2659       O  
ATOM   1996  CB  SER I 506     -22.148 -17.633  67.287  1.00113.62           C  
ANISOU 1996  CB  SER I 506    15876  19418   7876   2943   -854   2427       C  
ATOM   1997  OG  SER I 506     -21.825 -16.643  66.325  1.00111.21           O  
ANISOU 1997  OG  SER I 506    15521  19147   7586   2903   -866   2436       O  
ATOM   1998  N   ILE I 507     -22.098 -18.890  70.182  1.00130.40           N  
ANISOU 1998  N   ILE I 507    18030  21604   9913   2800   -918   2595       N  
ATOM   1999  CA  ILE I 507     -22.556 -19.903  71.134  1.00130.19           C  
ANISOU 1999  CA  ILE I 507    18034  21585   9848   2812   -914   2633       C  
ATOM   2000  C   ILE I 507     -22.956 -19.286  72.471  1.00130.48           C  
ANISOU 2000  C   ILE I 507    17946  21805   9824   2721   -891   2824       C  
ATOM   2001  O   ILE I 507     -23.733 -19.892  73.217  1.00127.72           O  
ANISOU 2001  O   ILE I 507    17578  21530   9418   2746   -844   2870       O  
ATOM   2002  CB  ILE I 507     -21.508 -21.015  71.356  1.00126.17           C  
ANISOU 2002  CB  ILE I 507    17665  20918   9355   2744  -1040   2590       C  
ATOM   2003  CG1 ILE I 507     -20.295 -20.500  72.136  1.00127.01           C  
ANISOU 2003  CG1 ILE I 507    17752  21053   9452   2567  -1154   2706       C  
ATOM   2004  CG2 ILE I 507     -21.088 -21.642  70.044  1.00119.97           C  
ANISOU 2004  CG2 ILE I 507    17005  19951   8627   2838  -1061   2390       C  
ATOM   2005  CD1 ILE I 507     -19.393 -21.598  72.650  1.00127.30           C  
ANISOU 2005  CD1 ILE I 507    17889  20977   9502   2515  -1286   2729       C  
ATOM   2006  N   LYS I 508     -22.449 -18.092  72.799  1.00129.23           N  
ANISOU 2006  N   LYS I 508    17696  21737   9667   2608   -922   2934       N  
ATOM   2007  CA  LYS I 508     -22.966 -17.380  73.963  1.00133.04           C  
ANISOU 2007  CA  LYS I 508    18043  22407  10101   2544   -881   3109       C  
ATOM   2008  C   LYS I 508     -24.366 -16.842  73.685  1.00137.22           C  
ANISOU 2008  C   LYS I 508    18448  23080  10608   2694   -739   3125       C  
ATOM   2009  O   LYS I 508     -25.230 -16.839  74.570  1.00140.07           O  
ANISOU 2009  O   LYS I 508    18722  23593  10903   2712   -663   3214       O  
ATOM   2010  CB  LYS I 508     -22.005 -16.251  74.350  1.00133.02           C  
ANISOU 2010  CB  LYS I 508    17970  22466  10104   2380   -958   3215       C  
ATOM   2011  CG  LYS I 508     -22.570 -15.218  75.320  1.00132.78           C  
ANISOU 2011  CG  LYS I 508    17775  22637  10039   2329   -907   3392       C  
ATOM   2012  CD  LYS I 508     -21.512 -14.210  75.740  1.00127.04           C  
ANISOU 2012  CD  LYS I 508    16986  21970   9314   2150   -995   3486       C  
ATOM   2013  CE  LYS I 508     -22.081 -13.176  76.702  1.00121.76           C  
ANISOU 2013  CE  LYS I 508    16146  21500   8616   2102   -947   3664       C  
ATOM   2014  NZ  LYS I 508     -21.016 -12.322  77.297  1.00118.80           N  
ANISOU 2014  NZ  LYS I 508    15710  21194   8234   1910  -1038   3761       N  
ATOM   2015  N   ARG I 509     -24.616 -16.413  72.445  1.00137.69           N  
ANISOU 2015  N   ARG I 509    18490  23109  10717   2810   -699   3044       N  
ATOM   2016  CA  ARG I 509     -25.931 -15.888  72.090  1.00134.59           C  
ANISOU 2016  CA  ARG I 509    17962  22862  10313   2983   -569   3077       C  
ATOM   2017  C   ARG I 509     -26.975 -16.991  71.955  1.00129.46           C  
ANISOU 2017  C   ARG I 509    17353  22223   9615   3150   -464   2963       C  
ATOM   2018  O   ARG I 509     -28.169 -16.735  72.152  1.00125.31           O  
ANISOU 2018  O   ARG I 509    16701  21879   9032   3279   -337   3005       O  
ATOM   2019  CB  ARG I 509     -25.837 -15.088  70.790  1.00136.67           C  
ANISOU 2019  CB  ARG I 509    18185  23094  10649   3052   -574   3058       C  
ATOM   2020  CG  ARG I 509     -26.882 -13.996  70.657  1.00140.05           C  
ANISOU 2020  CG  ARG I 509    18413  23718  11082   3173   -484   3199       C  
ATOM   2021  CD  ARG I 509     -26.300 -12.766  69.981  1.00139.16           C  
ANISOU 2021  CD  ARG I 509    18222  23620  11032   3092   -559   3296       C  
ATOM   2022  NE  ARG I 509     -25.111 -12.277  70.674  1.00137.90           N  
ANISOU 2022  NE  ARG I 509    18086  23455  10856   2845   -673   3352       N  
ATOM   2023  CZ  ARG I 509     -25.140 -11.446  71.711  1.00136.78           C  
ANISOU 2023  CZ  ARG I 509    17819  23466  10685   2742   -682   3514       C  
ATOM   2024  NH1 ARG I 509     -24.008 -11.053  72.280  1.00136.48           N  
ANISOU 2024  NH1 ARG I 509    17807  23422  10627   2526   -784   3547       N  
ATOM   2025  NH2 ARG I 509     -26.300 -11.007  72.180  1.00136.17           N  
ANISOU 2025  NH2 ARG I 509    17582  23564  10594   2861   -584   3641       N  
ATOM   2026  N   LEU I 510     -26.558 -18.215  71.621  1.00130.86           N  
ANISOU 2026  N   LEU I 510    17693  22226   9802   3151   -512   2818       N  
ATOM   2027  CA  LEU I 510     -27.537 -19.282  71.423  1.00129.37           C  
ANISOU 2027  CA  LEU I 510    17543  22055   9558   3300   -416   2695       C  
ATOM   2028  C   LEU I 510     -28.014 -19.879  72.745  1.00133.02           C  
ANISOU 2028  C   LEU I 510    17984  22652   9903   3220   -386   2760       C  
ATOM   2029  O   LEU I 510     -29.212 -20.134  72.914  1.00136.82           O  
ANISOU 2029  O   LEU I 510    18393  23302  10290   3332   -252   2723       O  
ATOM   2030  CB  LEU I 510     -26.959 -20.373  70.523  1.00120.53           C  
ANISOU 2030  CB  LEU I 510    16596  20706   8496   3334   -481   2520       C  
ATOM   2031  CG  LEU I 510     -27.472 -20.346  69.079  1.00116.90           C  
ANISOU 2031  CG  LEU I 510    16140  20185   8091   3539   -406   2382       C  
ATOM   2032  CD1 LEU I 510     -26.954 -19.128  68.327  1.00115.95           C  
ANISOU 2032  CD1 LEU I 510    15962  20040   8053   3525   -443   2446       C  
ATOM   2033  CD2 LEU I 510     -27.104 -21.629  68.351  1.00116.13           C  
ANISOU 2033  CD2 LEU I 510    16210  19883   8032   3585   -451   2197       C  
ATOM   2034  N   TYR I 511     -27.101 -20.113  73.691  1.00135.46           N  
ANISOU 2034  N   TYR I 511    12173  24823  14473   5955   2571   -693       N  
ATOM   2035  CA  TYR I 511     -27.433 -20.672  75.001  1.00134.22           C  
ANISOU 2035  CA  TYR I 511    12047  24629  14322   5890   2461   -831       C  
ATOM   2036  C   TYR I 511     -26.921 -19.705  76.063  1.00132.55           C  
ANISOU 2036  C   TYR I 511    11780  24602  13981   5918   2291   -760       C  
ATOM   2037  O   TYR I 511     -25.850 -19.921  76.649  1.00135.37           O  
ANISOU 2037  O   TYR I 511    12101  25086  14246   5851   2103   -874       O  
ATOM   2038  CB  TYR I 511     -26.840 -22.069  75.191  1.00134.21           C  
ANISOU 2038  CB  TYR I 511    12066  24597  14329   5761   2357  -1077       C  
ATOM   2039  CG  TYR I 511     -26.994 -22.993  73.996  1.00135.28           C  
ANISOU 2039  CG  TYR I 511    12217  24611  14574   5720   2496  -1166       C  
ATOM   2040  CD1 TYR I 511     -26.029 -23.036  72.994  1.00136.65           C  
ANISOU 2040  CD1 TYR I 511    12343  24864  14713   5702   2496  -1156       C  
ATOM   2041  CD2 TYR I 511     -28.105 -23.820  73.871  1.00137.17           C  
ANISOU 2041  CD2 TYR I 511    12506  24664  14948   5703   2632  -1267       C  
ATOM   2042  CE1 TYR I 511     -26.165 -23.876  71.903  1.00138.98           C  
ANISOU 2042  CE1 TYR I 511    12627  25058  15119   5658   2634  -1233       C  
ATOM   2043  CE2 TYR I 511     -28.249 -24.664  72.781  1.00137.96           C  
ANISOU 2043  CE2 TYR I 511    12595  24664  15159   5660   2763  -1367       C  
ATOM   2044  CZ  TYR I 511     -27.277 -24.688  71.802  1.00139.42           C  
ANISOU 2044  CZ  TYR I 511    12719  24933  15323   5632   2768  -1344       C  
ATOM   2045  OH  TYR I 511     -27.414 -25.524  70.718  1.00141.35           O  
ANISOU 2045  OH  TYR I 511    12929  25089  15690   5583   2909  -1439       O  
ATOM   2046  N   PRO I 512     -27.663 -18.627  76.342  1.00126.65           N  
ANISOU 2046  N   PRO I 512    11016  23878  13228   6020   2354   -577       N  
ATOM   2047  CA  PRO I 512     -27.124 -17.578  77.222  1.00121.75           C  
ANISOU 2047  CA  PRO I 512    10311  23465  12485   6052   2199   -501       C  
ATOM   2048  C   PRO I 512     -27.071 -17.973  78.686  1.00114.56           C  
ANISOU 2048  C   PRO I 512     9385  22576  11567   5974   2061   -621       C  
ATOM   2049  O   PRO I 512     -26.145 -17.554  79.393  1.00114.23           O  
ANISOU 2049  O   PRO I 512     9262  22709  11430   5945   1889   -658       O  
ATOM   2050  CB  PRO I 512     -28.083 -16.396  76.994  1.00117.22           C  
ANISOU 2050  CB  PRO I 512     9724  22893  11919   6193   2334   -266       C  
ATOM   2051  CG  PRO I 512     -28.934 -16.784  75.800  1.00118.10           C  
ANISOU 2051  CG  PRO I 512     9917  22802  12153   6243   2566   -209       C  
ATOM   2052  CD  PRO I 512     -28.994 -18.273  75.824  1.00126.21           C  
ANISOU 2052  CD  PRO I 512    11007  23672  13275   6122   2573   -432       C  
ATOM   2053  N   GLY I 513     -28.027 -18.762  79.168  1.00114.16           N  
ANISOU 2053  N   GLY I 513     9405  22358  11612   5946   2137   -684       N  
ATOM   2054  CA  GLY I 513     -28.007 -19.203  80.544  1.00113.26           C  
ANISOU 2054  CA  GLY I 513     9281  22260  11491   5882   2026   -781       C  
ATOM   2055  C   GLY I 513     -27.154 -20.417  80.825  1.00111.95           C  
ANISOU 2055  C   GLY I 513     9144  22082  11311   5772   1906   -997       C  
ATOM   2056  O   GLY I 513     -27.270 -21.003  81.904  1.00111.29           O  
ANISOU 2056  O   GLY I 513     9074  21975  11235   5728   1846  -1082       O  
ATOM   2057  N   SER I 514     -26.284 -20.813  79.888  1.00118.81           N  
ANISOU 2057  N   SER I 514    10019  22971  12151   5736   1874  -1080       N  
ATOM   2058  CA  SER I 514     -25.517 -22.041  80.053  1.00119.20           C  
ANISOU 2058  CA  SER I 514    10103  23000  12186   5641   1770  -1286       C  
ATOM   2059  C   SER I 514     -24.075 -21.943  79.565  1.00124.57           C  
ANISOU 2059  C   SER I 514    10737  23820  12772   5614   1645  -1347       C  
ATOM   2060  O   SER I 514     -23.366 -22.957  79.587  1.00122.46           O  
ANISOU 2060  O   SER I 514    10500  23544  12487   5546   1560  -1515       O  
ATOM   2061  CB  SER I 514     -26.215 -23.205  79.336  1.00116.95           C  
ANISOU 2061  CB  SER I 514     9905  22535  11994   5612   1893  -1389       C  
ATOM   2062  OG  SER I 514     -27.349 -23.646  80.060  1.00117.71           O  
ANISOU 2062  OG  SER I 514    10058  22514  12152   5624   1960  -1409       O  
ATOM   2063  N   VAL I 515     -23.616 -20.776  79.124  1.00126.31           N  
ANISOU 2063  N   VAL I 515    10889  24181  12923   5677   1627  -1221       N  
ATOM   2064  CA  VAL I 515     -22.243 -20.587  78.658  1.00129.59           C  
ANISOU 2064  CA  VAL I 515    11259  24750  13228   5674   1506  -1277       C  
ATOM   2065  C   VAL I 515     -21.624 -19.514  79.545  1.00131.84           C  
ANISOU 2065  C   VAL I 515    11447  25227  13421   5706   1361  -1243       C  
ATOM   2066  O   VAL I 515     -21.913 -18.321  79.382  1.00132.33           O  
ANISOU 2066  O   VAL I 515    11449  25384  13446   5788   1395  -1082       O  
ATOM   2067  CB  VAL I 515     -22.177 -20.196  77.177  1.00130.23           C  
ANISOU 2067  CB  VAL I 515    11340  24845  13295   5735   1620  -1166       C  
ATOM   2068  CG1 VAL I 515     -20.737 -19.934  76.756  1.00128.46           C  
ANISOU 2068  CG1 VAL I 515    11070  24805  12934   5750   1488  -1218       C  
ATOM   2069  CG2 VAL I 515     -22.800 -21.281  76.310  1.00130.13           C  
ANISOU 2069  CG2 VAL I 515    11401  24643  13402   5692   1772  -1216       C  
ATOM   2070  N   TYR I 516     -20.778 -19.924  80.492  1.00129.33           N  
ANISOU 2070  N   TYR I 516    11103  24971  13067   5648   1202  -1397       N  
ATOM   2071  CA  TYR I 516     -20.227 -18.982  81.457  1.00128.16           C  
ANISOU 2071  CA  TYR I 516    10841  24994  12859   5664   1066  -1394       C  
ATOM   2072  C   TYR I 516     -19.001 -18.248  80.935  1.00125.18           C  
ANISOU 2072  C   TYR I 516    10395  24822  12346   5713    947  -1425       C  
ATOM   2073  O   TYR I 516     -18.518 -17.330  81.607  1.00120.12           O  
ANISOU 2073  O   TYR I 516     9641  24349  11650   5736    829  -1431       O  
ATOM   2074  CB  TYR I 516     -19.879 -19.712  82.759  1.00129.36           C  
ANISOU 2074  CB  TYR I 516    10985  25116  13050   5590    961  -1542       C  
ATOM   2075  CG  TYR I 516     -21.079 -20.247  83.517  1.00133.02           C  
ANISOU 2075  CG  TYR I 516    11497  25422  13624   5563   1063  -1498       C  
ATOM   2076  CD1 TYR I 516     -22.370 -19.826  83.211  1.00137.36           C  
ANISOU 2076  CD1 TYR I 516    12070  25890  14229   5608   1218  -1333       C  
ATOM   2077  CD2 TYR I 516     -20.921 -21.187  84.525  1.00133.71           C  
ANISOU 2077  CD2 TYR I 516    11610  25443  13750   5508   1010  -1618       C  
ATOM   2078  CE1 TYR I 516     -23.463 -20.316  83.895  1.00139.43           C  
ANISOU 2078  CE1 TYR I 516    12382  26019  14578   5598   1310  -1300       C  
ATOM   2079  CE2 TYR I 516     -22.011 -21.683  85.216  1.00137.09           C  
ANISOU 2079  CE2 TYR I 516    12086  25744  14258   5500   1105  -1573       C  
ATOM   2080  CZ  TYR I 516     -23.279 -21.244  84.896  1.00140.00           C  
ANISOU 2080  CZ  TYR I 516    12478  26040  14674   5544   1251  -1420       C  
ATOM   2081  OH  TYR I 516     -24.368 -21.736  85.579  1.00141.10           O  
ANISOU 2081  OH  TYR I 516    12670  26062  14880   5550   1344  -1383       O  
ATOM   2082  N   GLY I 517     -18.494 -18.619  79.769  1.00128.38           N  
ANISOU 2082  N   GLY I 517    10855  25226  12696   5733    974  -1450       N  
ATOM   2083  CA  GLY I 517     -17.352 -17.963  79.168  1.00136.82           C  
ANISOU 2083  CA  GLY I 517    11871  26496  13618   5799    874  -1474       C  
ATOM   2084  C   GLY I 517     -16.091 -18.808  79.258  1.00141.81           C  
ANISOU 2084  C   GLY I 517    12527  27162  14191   5757    738  -1687       C  
ATOM   2085  O   GLY I 517     -16.044 -19.858  79.901  1.00145.47           O  
ANISOU 2085  O   GLY I 517    13040  27506  14725   5677    706  -1818       O  
ATOM   2086  N   ARG I 518     -15.053 -18.320  78.581  1.00140.50           N  
ANISOU 2086  N   ARG I 518    12329  27174  13881   5830    659  -1716       N  
ATOM   2087  CA  ARG I 518     -13.741 -18.939  78.684  1.00135.83           C  
ANISOU 2087  CA  ARG I 518    11751  26650  13209   5817    514  -1921       C  
ATOM   2088  C   ARG I 518     -13.138 -18.678  80.063  1.00129.94           C  
ANISOU 2088  C   ARG I 518    10925  25985  12461   5794    340  -2074       C  
ATOM   2089  O   ARG I 518     -13.635 -17.871  80.852  1.00131.54           O  
ANISOU 2089  O   ARG I 518    11040  26230  12708   5791    322  -2012       O  
ATOM   2090  CB  ARG I 518     -12.799 -18.421  77.597  1.00140.45           C  
ANISOU 2090  CB  ARG I 518    12320  27419  13625   5920    478  -1908       C  
ATOM   2091  CG  ARG I 518     -13.430 -18.233  76.231  1.00140.28           C  
ANISOU 2091  CG  ARG I 518    12334  27364  13604   5972    662  -1703       C  
ATOM   2092  CD  ARG I 518     -12.385 -17.787  75.222  1.00137.93           C  
ANISOU 2092  CD  ARG I 518    12019  27265  13124   6084    621  -1692       C  
ATOM   2093  NE  ARG I 518     -11.620 -18.920  74.712  1.00134.56           N  
ANISOU 2093  NE  ARG I 518    11655  26792  12680   6047    604  -1818       N  
ATOM   2094  CZ  ARG I 518     -11.854 -19.521  73.551  1.00133.23           C  
ANISOU 2094  CZ  ARG I 518    11532  26534  12553   6038    754  -1725       C  
ATOM   2095  NH1 ARG I 518     -12.838 -19.098  72.769  1.00130.93           N  
ANISOU 2095  NH1 ARG I 518    11239  26177  12333   6068    942  -1507       N  
ATOM   2096  NH2 ARG I 518     -11.105 -20.550  73.173  1.00134.21           N  
ANISOU 2096  NH2 ARG I 518    11699  26637  12659   6002    722  -1850       N  
ATOM   2097  N   LEU I 519     -12.037 -19.375  80.346  1.00131.91           N  
ANISOU 2097  N   LEU I 519    11196  26256  12668   5781    214  -2277       N  
ATOM   2098  CA  LEU I 519     -11.438 -19.278  81.670  1.00123.06           C  
ANISOU 2098  CA  LEU I 519     9999  25180  11579   5756     59  -2439       C  
ATOM   2099  C   LEU I 519     -10.716 -17.947  81.858  1.00120.48           C  
ANISOU 2099  C   LEU I 519     9538  25093  11147   5831    -82  -2482       C  
ATOM   2100  O   LEU I 519     -10.843 -17.323  82.915  1.00121.26           O  
ANISOU 2100  O   LEU I 519     9519  25237  11317   5801   -158  -2506       O  
ATOM   2101  CB  LEU I 519     -10.514 -20.479  81.907  1.00119.98           C  
ANISOU 2101  CB  LEU I 519     9682  24722  11182   5736    -22  -2642       C  
ATOM   2102  CG  LEU I 519     -10.340 -21.038  83.328  1.00117.18           C  
ANISOU 2102  CG  LEU I 519     9304  24279  10940   5682   -101  -2777       C  
ATOM   2103  CD1 LEU I 519      -9.781 -22.447  83.297  1.00119.29           C  
ANISOU 2103  CD1 LEU I 519     9687  24433  11203   5670   -116  -2915       C  
ATOM   2104  CD2 LEU I 519      -9.401 -20.168  84.134  1.00117.92           C  
ANISOU 2104  CD2 LEU I 519     9258  24533  11013   5718   -281  -2917       C  
ATOM   2105  N   ILE I 520      -9.994 -17.472  80.836  1.00121.60           N  
ANISOU 2105  N   ILE I 520     9682  25399  11121   5929   -117  -2487       N  
ATOM   2106  CA  ILE I 520      -9.202 -16.250  80.992  1.00125.34           C  
ANISOU 2106  CA  ILE I 520    10030  26124  11469   6014   -272  -2562       C  
ATOM   2107  C   ILE I 520     -10.084 -15.016  81.146  1.00130.90           C  
ANISOU 2107  C   ILE I 520    10632  26918  12186   6031   -229  -2383       C  
ATOM   2108  O   ILE I 520      -9.674 -14.031  81.773  1.00136.20           O  
ANISOU 2108  O   ILE I 520    11164  27764  12822   6054   -374  -2459       O  
ATOM   2109  CB  ILE I 520      -8.227 -16.078  79.813  1.00119.27           C  
ANISOU 2109  CB  ILE I 520     9300  25524  10492   6136   -309  -2602       C  
ATOM   2110  CG1 ILE I 520      -8.959 -16.252  78.481  1.00120.71           C  
ANISOU 2110  CG1 ILE I 520     9575  25645  10645   6168   -108  -2370       C  
ATOM   2111  CG2 ILE I 520      -7.052 -17.026  79.947  1.00118.89           C  
ANISOU 2111  CG2 ILE I 520     9311  25454  10408   6141   -420  -2838       C  
ATOM   2112  CD1 ILE I 520      -8.193 -15.725  77.291  1.00122.25           C  
ANISOU 2112  CD1 ILE I 520     9776  26048  10627   6310   -120  -2335       C  
ATOM   2113  N   ASP I 521     -11.299 -15.038  80.596  1.00129.29           N  
ANISOU 2113  N   ASP I 521    10487  26598  12039   6022    -37  -2151       N  
ATOM   2114  CA  ASP I 521     -12.183 -13.883  80.706  1.00131.17           C  
ANISOU 2114  CA  ASP I 521    10637  26916  12284   6057     17  -1965       C  
ATOM   2115  C   ASP I 521     -12.806 -13.738  82.088  1.00134.23           C  
ANISOU 2115  C   ASP I 521    10934  27233  12835   5958    -13  -1972       C  
ATOM   2116  O   ASP I 521     -13.488 -12.738  82.336  1.00134.74           O  
ANISOU 2116  O   ASP I 521    10906  27380  12909   5982     12  -1832       O  
ATOM   2117  CB  ASP I 521     -13.296 -13.964  79.660  1.00130.34           C  
ANISOU 2117  CB  ASP I 521    10628  26693  12201   6092    239  -1716       C  
ATOM   2118  CG  ASP I 521     -12.770 -14.238  78.268  1.00129.68           C  
ANISOU 2118  CG  ASP I 521    10630  26649  11993   6175    297  -1683       C  
ATOM   2119  OD2 ASP I 521     -13.263 -15.186  77.624  1.00126.49           O  
ANISOU 2119  OD2 ASP I 521    10336  26049  11674   6131    443  -1620       O  
ATOM   2120  OD1 ASP I 521     -11.861 -13.509  77.820  1.00131.03           O  
ANISOU 2120  OD1 ASP I 521    10749  27053  11982   6284    197  -1723       O  
ATOM   2121  N   LEU I 522     -12.590 -14.693  82.989  1.00133.49           N  
ANISOU 2121  N   LEU I 522    10859  26997  12865   5858    -60  -2119       N  
ATOM   2122  CA  LEU I 522     -13.264 -14.706  84.276  1.00136.01           C  
ANISOU 2122  CA  LEU I 522    11100  27226  13352   5765    -56  -2098       C  
ATOM   2123  C   LEU I 522     -12.333 -14.497  85.463  1.00144.03           C  
ANISOU 2123  C   LEU I 522    11973  28331  14423   5714   -257  -2303       C  
ATOM   2124  O   LEU I 522     -12.817 -14.470  86.600  1.00151.09           O  
ANISOU 2124  O   LEU I 522    12777  29164  15468   5633   -260  -2282       O  
ATOM   2125  CB  LEU I 522     -14.031 -16.022  84.455  1.00126.55           C  
ANISOU 2125  CB  LEU I 522    10038  25764  12280   5694     87  -2062       C  
ATOM   2126  CG  LEU I 522     -15.504 -16.044  84.033  1.00121.54           C  
ANISOU 2126  CG  LEU I 522     9478  24996  11706   5698    291  -1833       C  
ATOM   2127  CD1 LEU I 522     -15.670 -15.902  82.528  1.00117.94           C  
ANISOU 2127  CD1 LEU I 522     9112  24553  11146   5779    395  -1720       C  
ATOM   2128  CD2 LEU I 522     -16.174 -17.318  84.521  1.00120.50           C  
ANISOU 2128  CD2 LEU I 522     9453  24629  11702   5622    390  -1847       C  
ATOM   2129  N   CYS I 523     -11.026 -14.334  85.249  1.00144.72           N  
ANISOU 2129  N   CYS I 523    12027  28559  14400   5760   -425  -2499       N  
ATOM   2130  CA  CYS I 523     -10.126 -14.262  86.390  1.00144.56           C  
ANISOU 2130  CA  CYS I 523    11875  28587  14463   5704   -624  -2718       C  
ATOM   2131  C   CYS I 523      -8.830 -13.545  86.038  1.00147.39           C  
ANISOU 2131  C   CYS I 523    12164  29170  14669   5781   -826  -2907       C  
ATOM   2132  O   CYS I 523      -8.563 -13.209  84.881  1.00148.20           O  
ANISOU 2132  O   CYS I 523    12334  29396  14581   5891   -802  -2868       O  
ATOM   2133  CB  CYS I 523      -9.786 -15.649  86.918  1.00141.53           C  
ANISOU 2133  CB  CYS I 523    11592  27998  14185   5647   -618  -2845       C  
ATOM   2134  SG  CYS I 523      -9.620 -16.943  85.721  1.00138.49           S  
ANISOU 2134  SG  CYS I 523    11435  27494  13693   5709   -495  -2852       S  
ATOM   2135  N   GLN I 524      -8.013 -13.349  87.079  1.00151.43           N  
ANISOU 2135  N   GLN I 524    12590  29676  15270   5688  -1026  -3108       N  
ATOM   2136  CA  GLN I 524      -6.688 -12.746  87.093  1.00150.90           C  
ANISOU 2136  CA  GLN I 524    12480  29754  15100   5708  -1261  -3345       C  
ATOM   2137  C   GLN I 524      -6.103 -12.932  88.490  1.00154.80           C  
ANISOU 2137  C   GLN I 524    12988  30038  15790   5505  -1416  -3521       C  
ATOM   2138  O   GLN I 524      -6.824 -12.774  89.484  1.00158.55           O  
ANISOU 2138  O   GLN I 524    13390  30396  16455   5363  -1379  -3422       O  
ATOM   2139  CB  GLN I 524      -6.751 -11.264  86.728  1.00149.76           C  
ANISOU 2139  CB  GLN I 524    12138  29940  14825   5812  -1344  -3306       C  
ATOM   2140  CG  GLN I 524      -5.451 -10.710  86.186  1.00149.17           C  
ANISOU 2140  CG  GLN I 524    12039  30089  14548   5926  -1542  -3525       C  
ATOM   2141  CD  GLN I 524      -5.229  -9.269  86.584  1.00154.83           C  
ANISOU 2141  CD  GLN I 524    12570  31034  15224   5908  -1722  -3595       C  
ATOM   2142  OE1 GLN I 524      -5.786  -8.352  85.980  1.00159.01           O  
ANISOU 2142  OE1 GLN I 524    13072  31724  15621   5985  -1645  -3421       O  
ATOM   2143  NE2 GLN I 524      -4.420  -9.059  87.617  1.00155.28           N  
ANISOU 2143  NE2 GLN I 524    12564  31035  15399   5765  -1946  -3841       N  
ATOM   2144  N   PRO I 525      -4.826 -13.285  88.613  1.00155.33           N  
ANISOU 2144  N   PRO I 525    13151  30043  15826   5489  -1576  -3771       N  
ATOM   2145  CA  PRO I 525      -4.236 -13.498  89.942  1.00154.16           C  
ANISOU 2145  CA  PRO I 525    13031  29660  15883   5294  -1712  -3936       C  
ATOM   2146  C   PRO I 525      -4.073 -12.196  90.719  1.00154.75           C  
ANISOU 2146  C   PRO I 525    12903  29854  16042   5184  -1888  -4019       C  
ATOM   2147  O   PRO I 525      -4.275 -11.092  90.210  1.00152.86           O  
ANISOU 2147  O   PRO I 525    12498  29910  15672   5277  -1936  -3979       O  
ATOM   2148  CB  PRO I 525      -2.878 -14.133  89.628  1.00152.93           C  
ANISOU 2148  CB  PRO I 525    13033  29444  15628   5354  -1833  -4185       C  
ATOM   2149  CG  PRO I 525      -3.045 -14.737  88.280  1.00151.72           C  
ANISOU 2149  CG  PRO I 525    12970  29402  15273   5547  -1688  -4088       C  
ATOM   2150  CD  PRO I 525      -3.973 -13.824  87.541  1.00154.38           C  
ANISOU 2150  CD  PRO I 525    13156  29999  15503   5649  -1590  -3883       C  
ATOM   2151  N   THR I 526      -3.694 -12.350  91.993  1.00156.48           N  
ANISOU 2151  N   THR I 526    13130  29835  16491   4980  -1984  -4135       N  
ATOM   2152  CA  THR I 526      -3.547 -11.200  92.882  1.00162.97           C  
ANISOU 2152  CA  THR I 526    13748  30728  17444   4832  -2152  -4224       C  
ATOM   2153  C   THR I 526      -2.259 -10.429  92.614  1.00171.65           C  
ANISOU 2153  C   THR I 526    14797  32009  18414   4878  -2414  -4528       C  
ATOM   2154  O   THR I 526      -2.267  -9.193  92.604  1.00173.44           O  
ANISOU 2154  O   THR I 526    14814  32499  18588   4884  -2544  -4575       O  
ATOM   2155  CB  THR I 526      -3.596 -11.649  94.345  1.00158.72           C  
ANISOU 2155  CB  THR I 526    13234  29854  17220   4588  -2148  -4231       C  
ATOM   2156  OG1 THR I 526      -2.393 -12.356  94.676  1.00160.54           O  
ANISOU 2156  OG1 THR I 526    13640  29855  17504   4538  -2262  -4471       O  
ATOM   2157  CG2 THR I 526      -4.804 -12.540  94.602  1.00152.18           C  
ANISOU 2157  CG2 THR I 526    12481  28846  16493   4569  -1888  -3946       C  
ATOM   2158  N   GLN I 527      -1.147 -11.129  92.407  1.00175.60           N  
ANISOU 2158  N   GLN I 527    15481  32385  18853   4922  -2499  -4744       N  
ATOM   2159  CA  GLN I 527       0.123 -10.491  92.103  1.00176.12           C  
ANISOU 2159  CA  GLN I 527    15525  32617  18774   4991  -2745  -5051       C  
ATOM   2160  C   GLN I 527       0.400 -10.572  90.603  1.00170.76           C  
ANISOU 2160  C   GLN I 527    14913  32206  17762   5271  -2706  -5042       C  
ATOM   2161  O   GLN I 527      -0.475 -10.912  89.800  1.00169.76           O  
ANISOU 2161  O   GLN I 527    14809  32162  17531   5394  -2496  -4788       O  
ATOM   2162  CB  GLN I 527       1.253 -11.124  92.919  1.00178.62           C  
ANISOU 2162  CB  GLN I 527    15998  32620  19248   4863  -2877  -5316       C  
ATOM   2163  CG  GLN I 527       1.777 -10.260  94.059  1.00181.39           C  
ANISOU 2163  CG  GLN I 527    16209  32899  19811   4646  -3097  -5532       C  
ATOM   2164  CD  GLN I 527       0.830 -10.212  95.243  1.00180.69           C  
ANISOU 2164  CD  GLN I 527    16011  32608  20035   4406  -2996  -5341       C  
ATOM   2165  OE1 GLN I 527       0.108 -11.170  95.513  1.00179.36           O  
ANISOU 2165  OE1 GLN I 527    15954  32218  19977   4371  -2782  -5115       O  
ATOM   2166  NE2 GLN I 527       0.835  -9.093  95.959  1.00180.90           N  
ANISOU 2166  NE2 GLN I 527    15810  32724  20199   4245  -3150  -5433       N  
ATOM   2167  N   LYS I 528       1.637 -10.262  90.218  1.00169.83           N  
ANISOU 2167  N   LYS I 528    14828  32221  17478   5375  -2904  -5324       N  
ATOM   2168  CA  LYS I 528       2.037 -10.191  88.819  1.00165.12           C  
ANISOU 2168  CA  LYS I 528    14272  31916  16551   5651  -2889  -5335       C  
ATOM   2169  C   LYS I 528       2.859 -11.395  88.379  1.00164.50           C  
ANISOU 2169  C   LYS I 528    14432  31678  16394   5746  -2853  -5443       C  
ATOM   2170  O   LYS I 528       2.687 -11.883  87.259  1.00162.26           O  
ANISOU 2170  O   LYS I 528    14217  31517  15916   5935  -2703  -5307       O  
ATOM   2171  CB  LYS I 528       2.841  -8.911  88.573  1.00159.76           C  
ANISOU 2171  CB  LYS I 528    13446  31570  15688   5749  -3138  -5570       C  
ATOM   2172  CG  LYS I 528       2.654  -8.301  87.198  1.00153.14           C  
ANISOU 2172  CG  LYS I 528    12527  31143  14518   6030  -3081  -5444       C  
ATOM   2173  CD  LYS I 528       1.179  -8.235  86.839  1.00147.99           C  
ANISOU 2173  CD  LYS I 528    11790  30548  13891   6050  -2833  -5064       C  
ATOM   2174  CE  LYS I 528       0.970  -7.522  85.525  1.00149.28           C  
ANISOU 2174  CE  LYS I 528    11916  31055  13749   6296  -2740  -4910       C  
ATOM   2175  NZ  LYS I 528      -0.368  -7.821  84.942  1.00139.57           N  
ANISOU 2175  NZ  LYS I 528    10722  29773  12535   6324  -2436  -4529       N  
ATOM   2176  N   LYS I 529       3.762 -11.869  89.240  1.00155.81           N  
ANISOU 2176  N   LYS I 529    17337  26346  15518  -1962  -4734   3277       N  
ATOM   2177  CA  LYS I 529       4.489 -13.109  88.983  1.00158.80           C  
ANISOU 2177  CA  LYS I 529    18055  26438  15843  -1955  -4483   3055       C  
ATOM   2178  C   LYS I 529       3.544 -14.304  88.988  1.00164.26           C  
ANISOU 2178  C   LYS I 529    18572  27021  16817  -1817  -4086   3087       C  
ATOM   2179  O   LYS I 529       3.756 -15.292  88.263  1.00163.27           O  
ANISOU 2179  O   LYS I 529    18682  26692  16660  -1662  -3787   2959       O  
ATOM   2180  CB  LYS I 529       5.568 -13.284  90.052  1.00158.29           C  
ANISOU 2180  CB  LYS I 529    18142  26261  15740  -2282  -4710   2859       C  
ATOM   2181  CG  LYS I 529       5.128 -12.717  91.403  1.00156.06           C  
ANISOU 2181  CG  LYS I 529    17482  26144  15668  -2538  -4957   2959       C  
ATOM   2182  CD  LYS I 529       6.278 -12.405  92.343  1.00155.31           C  
ANISOU 2182  CD  LYS I 529    17549  26000  15460  -2873  -5285   2794       C  
ATOM   2183  CE  LYS I 529       7.117 -11.249  91.825  1.00155.83           C  
ANISOU 2183  CE  LYS I 529    17831  26170  15205  -2892  -5617   2771       C  
ATOM   2184  NZ  LYS I 529       8.198 -10.879  92.781  1.00156.38           N  
ANISOU 2184  NZ  LYS I 529    18039  26206  15174  -3230  -5955   2618       N  
ATOM   2185  N   TYR I 530       2.483 -14.218  89.789  1.00163.72           N  
ANISOU 2185  N   TYR I 530    18087  27086  17033  -1867  -4078   3252       N  
ATOM   2186  CA  TYR I 530       1.519 -15.303  89.868  1.00160.59           C  
ANISOU 2186  CA  TYR I 530    17514  26593  16910  -1741  -3720   3297       C  
ATOM   2187  C   TYR I 530       0.669 -15.391  88.609  1.00160.24           C  
ANISOU 2187  C   TYR I 530    17430  26589  16864  -1398  -3438   3432       C  
ATOM   2188  O   TYR I 530       0.034 -16.420  88.387  1.00159.54           O  
ANISOU 2188  O   TYR I 530    17289  26376  16952  -1251  -3104   3427       O  
ATOM   2189  CB  TYR I 530       0.626 -15.163  91.113  1.00158.58           C  
ANISOU 2189  CB  TYR I 530    16836  26463  16955  -1903  -3782   3436       C  
ATOM   2190  CG  TYR I 530       1.326 -14.952  92.460  1.00157.92           C  
ANISOU 2190  CG  TYR I 530    16741  26363  16899  -2268  -4063   3330       C  
ATOM   2191  CD2 TYR I 530       0.600 -14.526  93.565  1.00157.64           C  
ANISOU 2191  CD2 TYR I 530    16315  26477  17103  -2445  -4168   3461       C  
ATOM   2192  CD1 TYR I 530       2.680 -15.243  92.648  1.00158.54           C  
ANISOU 2192  CD1 TYR I 530    17198  26262  16779  -2439  -4195   3093       C  
ATOM   2193  CE2 TYR I 530       1.208 -14.337  94.795  1.00160.35           C  
ANISOU 2193  CE2 TYR I 530    16647  26799  17481  -2789  -4402   3362       C  
ATOM   2194  CE1 TYR I 530       3.294 -15.054  93.872  1.00160.53           C  
ANISOU 2194  CE1 TYR I 530    17448  26492  17053  -2774  -4440   2999       C  
ATOM   2195  CZ  TYR I 530       2.552 -14.605  94.942  1.00161.91           C  
ANISOU 2195  CZ  TYR I 530    17234  26818  17466  -2953  -4538   3133       C  
ATOM   2196  OH  TYR I 530       3.154 -14.423  96.166  1.00164.45           O  
ANISOU 2196  OH  TYR I 530    17558  27107  17817  -3300  -4763   3033       O  
ATOM   2197  N   GLN I 531       0.674 -14.356  87.760  1.00159.54           N  
ANISOU 2197  N   GLN I 531    17393  26656  16569  -1263  -3565   3541       N  
ATOM   2198  CA  GLN I 531       0.097 -14.491  86.424  1.00153.66           C  
ANISOU 2198  CA  GLN I 531    16722  25901  15761   -940  -3281   3628       C  
ATOM   2199  C   GLN I 531       0.866 -15.517  85.602  1.00144.21           C  
ANISOU 2199  C   GLN I 531    15919  24437  14437   -846  -3014   3401       C  
ATOM   2200  O   GLN I 531       0.270 -16.385  84.954  1.00139.97           O  
ANISOU 2200  O   GLN I 531    15375  23790  14017   -642  -2652   3400       O  
ATOM   2201  CB  GLN I 531       0.084 -13.141  85.709  1.00161.64           C  
ANISOU 2201  CB  GLN I 531    17773  27109  16535   -827  -3501   3771       C  
ATOM   2202  CG  GLN I 531      -0.927 -12.147  86.245  1.00168.20           C  
ANISOU 2202  CG  GLN I 531    18175  28216  17517   -827  -3703   4017       C  
ATOM   2203  CD  GLN I 531      -1.136 -10.978  85.305  1.00172.86           C  
ANISOU 2203  CD  GLN I 531    18824  28975  17881   -625  -3847   4169       C  
ATOM   2204  OE1 GLN I 531      -0.344 -10.756  84.388  1.00173.71           O  
ANISOU 2204  OE1 GLN I 531    19323  28997  17683   -541  -3862   4081       O  
ATOM   2205  NE2 GLN I 531      -2.204 -10.224  85.525  1.00174.13           N  
ANISOU 2205  NE2 GLN I 531    18607  29368  18188   -541  -3950   4395       N  
ATOM   2206  N   ILE I 532       2.199 -15.437  85.630  1.00147.68           N  
ANISOU 2206  N   ILE I 532    16699  24767  14644   -997  -3189   3199       N  
ATOM   2207  CA  ILE I 532       3.030 -16.416  84.936  1.00138.79           C  
ANISOU 2207  CA  ILE I 532    15944  23382  13407   -931  -2953   2954       C  
ATOM   2208  C   ILE I 532       2.881 -17.790  85.577  1.00134.57           C  
ANISOU 2208  C   ILE I 532    15338  22658  13133   -981  -2742   2817       C  
ATOM   2209  O   ILE I 532       2.834 -18.816  84.882  1.00135.16           O  
ANISOU 2209  O   ILE I 532    15540  22552  13264   -814  -2411   2692       O  
ATOM   2210  CB  ILE I 532       4.496 -15.950  84.928  1.00136.89           C  
ANISOU 2210  CB  ILE I 532    16075  23077  12860  -1096  -3217   2773       C  
ATOM   2211  CG1 ILE I 532       4.565 -14.425  84.811  1.00136.78           C  
ANISOU 2211  CG1 ILE I 532    16044  23293  12635  -1125  -3558   2936       C  
ATOM   2212  CG2 ILE I 532       5.259 -16.609  83.788  1.00136.30           C  
ANISOU 2212  CG2 ILE I 532    16399  22784  12605   -954  -2958   2566       C  
ATOM   2213  CD1 ILE I 532       5.963 -13.861  84.939  1.00136.59           C  
ANISOU 2213  CD1 ILE I 532    16362  23224  12314  -1310  -3865   2776       C  
ATOM   2214  N   ALA I 533       2.787 -17.831  86.912  1.00134.94           N  
ANISOU 2214  N   ALA I 533    15184  22740  13346  -1209  -2927   2833       N  
ATOM   2215  CA  ALA I 533       2.584 -19.108  87.601  1.00130.93           C  
ANISOU 2215  CA  ALA I 533    14620  22047  13081  -1254  -2743   2717       C  
ATOM   2216  C   ALA I 533       1.249 -19.747  87.222  1.00126.40           C  
ANISOU 2216  C   ALA I 533    13792  21477  12756  -1020  -2405   2853       C  
ATOM   2217  O   ALA I 533       1.176 -20.959  86.986  1.00121.36           O  
ANISOU 2217  O   ALA I 533    13240  20633  12236   -909  -2132   2710       O  
ATOM   2218  CB  ALA I 533       2.674 -18.908  89.113  1.00132.55           C  
ANISOU 2218  CB  ALA I 533    14663  22296  13403  -1551  -3003   2732       C  
ATOM   2219  N   VAL I 534       0.189 -18.941  87.136  1.00126.01           N  
ANISOU 2219  N   VAL I 534    13434  21658  12787   -934  -2426   3121       N  
ATOM   2220  CA  VAL I 534      -1.132 -19.440  86.777  1.00126.06           C  
ANISOU 2220  CA  VAL I 534    13190  21686  13022   -712  -2118   3272       C  
ATOM   2221  C   VAL I 534      -1.168 -19.863  85.312  1.00125.84           C  
ANISOU 2221  C   VAL I 534    13360  21559  12894   -436  -1816   3216       C  
ATOM   2222  O   VAL I 534      -1.836 -20.843  84.961  1.00123.95           O  
ANISOU 2222  O   VAL I 534    13057  21201  12836   -266  -1496   3196       O  
ATOM   2223  CB  VAL I 534      -2.180 -18.361  87.128  1.00128.56           C  
ANISOU 2223  CB  VAL I 534    13126  22285  13437   -707  -2256   3568       C  
ATOM   2224  CG1 VAL I 534      -3.417 -18.435  86.242  1.00128.00           C  
ANISOU 2224  CG1 VAL I 534    12875  22285  13472   -412  -1969   3756       C  
ATOM   2225  CG2 VAL I 534      -2.570 -18.471  88.594  1.00127.76           C  
ANISOU 2225  CG2 VAL I 534    12752  22220  13570   -932  -2375   3618       C  
ATOM   2226  N   THR I 535      -0.428 -19.161  84.445  1.00125.22           N  
ANISOU 2226  N   THR I 535    13538  21512  12526   -392  -1905   3177       N  
ATOM   2227  CA  THR I 535      -0.251 -19.613  83.065  1.00128.33           C  
ANISOU 2227  CA  THR I 535    14182  21774  12803   -167  -1607   3075       C  
ATOM   2228  C   THR I 535       0.378 -21.003  83.022  1.00126.42           C  
ANISOU 2228  C   THR I 535    14143  21252  12638   -171  -1398   2783       C  
ATOM   2229  O   THR I 535      -0.101 -21.892  82.306  1.00122.97           O  
ANISOU 2229  O   THR I 535    13705  20690  12326     26  -1053   2725       O  
ATOM   2230  CB  THR I 535       0.605 -18.602  82.289  1.00134.50           C  
ANISOU 2230  CB  THR I 535    15255  22614  13234   -163  -1771   3058       C  
ATOM   2231  OG1 THR I 535      -0.207 -17.497  81.886  1.00135.50           O  
ANISOU 2231  OG1 THR I 535    15218  22969  13297    -40  -1848   3330       O  
ATOM   2232  CG2 THR I 535       1.234 -19.230  81.050  1.00135.46           C  
ANISOU 2232  CG2 THR I 535    15728  22532  13209    -13  -1481   2855       C  
ATOM   2233  N   LYS I 536       1.435 -21.213  83.818  1.00126.05           N  
ANISOU 2233  N   LYS I 536    14262  21103  12529   -393  -1610   2592       N  
ATOM   2234  CA  LYS I 536       2.091 -22.520  83.865  1.00122.38           C  
ANISOU 2234  CA  LYS I 536    13996  20368  12134   -399  -1451   2299       C  
ATOM   2235  C   LYS I 536       1.156 -23.605  84.394  1.00114.21           C  
ANISOU 2235  C   LYS I 536    12727  19243  11425   -331  -1250   2309       C  
ATOM   2236  O   LYS I 536       1.169 -24.737  83.897  1.00109.39           O  
ANISOU 2236  O   LYS I 536    12208  18434  10921   -188   -980   2127       O  
ATOM   2237  CB  LYS I 536       3.358 -22.442  84.722  1.00123.92           C  
ANISOU 2237  CB  LYS I 536    14407  20483  12192   -659  -1750   2115       C  
ATOM   2238  CG  LYS I 536       4.162 -23.744  84.807  1.00119.17           C  
ANISOU 2238  CG  LYS I 536    14042  19597  11639   -668  -1627   1793       C  
ATOM   2239  CD  LYS I 536       4.391 -24.355  83.435  1.00116.25           C  
ANISOU 2239  CD  LYS I 536    13866  19086  11219   -439  -1304   1627       C  
ATOM   2240  CE  LYS I 536       5.207 -25.631  83.492  1.00114.53           C  
ANISOU 2240  CE  LYS I 536    13866  18590  11059   -433  -1195   1287       C  
ATOM   2241  NZ  LYS I 536       5.525 -26.122  82.121  1.00113.72           N  
ANISOU 2241  NZ  LYS I 536    13951  18358  10898   -231   -887   1107       N  
ATOM   2242  N   VAL I 537       0.337 -23.282  85.398  1.00115.51           N  
ANISOU 2242  N   VAL I 537    12590  19546  11754   -431  -1378   2513       N  
ATOM   2243  CA  VAL I 537      -0.556 -24.292  85.965  1.00111.74           C  
ANISOU 2243  CA  VAL I 537    11910  18972  11573   -375  -1195   2529       C  
ATOM   2244  C   VAL I 537      -1.684 -24.632  84.993  1.00111.49           C  
ANISOU 2244  C   VAL I 537    11721  18963  11678    -91   -857   2649       C  
ATOM   2245  O   VAL I 537      -2.018 -25.808  84.800  1.00103.98           O  
ANISOU 2245  O   VAL I 537    10774  17832  10902     44   -604   2526       O  
ATOM   2246  CB  VAL I 537      -1.098 -23.835  87.332  1.00115.50           C  
ANISOU 2246  CB  VAL I 537    12120  19581  12185   -576  -1407   2708       C  
ATOM   2247  CG1 VAL I 537      -2.080 -24.854  87.886  1.00114.35           C  
ANISOU 2247  CG1 VAL I 537    11786  19330  12334   -506  -1202   2740       C  
ATOM   2248  CG2 VAL I 537       0.041 -23.665  88.312  1.00117.22           C  
ANISOU 2248  CG2 VAL I 537    12518  19736  12283   -862  -1711   2558       C  
ATOM   2249  N   LEU I 538      -2.276 -23.622  84.353  1.00114.50           N  
ANISOU 2249  N   LEU I 538    11972  19555  11977     10   -854   2880       N  
ATOM   2250  CA  LEU I 538      -3.420 -23.864  83.480  1.00111.18           C  
ANISOU 2250  CA  LEU I 538    11393  19168  11684    271   -540   3019       C  
ATOM   2251  C   LEU I 538      -2.991 -24.499  82.160  1.00109.87           C  
ANISOU 2251  C   LEU I 538    11482  18833  11432    457   -259   2823       C  
ATOM   2252  O   LEU I 538      -3.459 -25.587  81.804  1.00101.77           O  
ANISOU 2252  O   LEU I 538    10424  17653  10591    610     30   2726       O  
ATOM   2253  CB  LEU I 538      -4.182 -22.557  83.239  1.00103.83           C  
ANISOU 2253  CB  LEU I 538    10256  18511  10684    326   -640   3327       C  
ATOM   2254  CG  LEU I 538      -4.882 -21.940  84.455  1.00102.76           C  
ANISOU 2254  CG  LEU I 538     9789  18563  10693    180   -860   3545       C  
ATOM   2255  CD1 LEU I 538      -5.680 -20.706  84.065  1.00 97.02           C  
ANISOU 2255  CD1 LEU I 538     8855  18101   9909    282   -935   3832       C  
ATOM   2256  CD2 LEU I 538      -5.780 -22.957  85.144  1.00101.10           C  
ANISOU 2256  CD2 LEU I 538     9366  18256  10791    207   -675   3567       C  
ATOM   2257  N   GLY I 539      -2.102 -23.838  81.415  1.00116.40           N  
ANISOU 2257  N   GLY I 539    12566  19679  11980    445   -334   2754       N  
ATOM   2258  CA  GLY I 539      -1.664 -24.374  80.140  1.00118.07           C  
ANISOU 2258  CA  GLY I 539    13028  19731  12103    606    -50   2563       C  
ATOM   2259  C   GLY I 539      -2.738 -24.339  79.074  1.00119.27           C  
ANISOU 2259  C   GLY I 539    13066  19935  12316    855    263   2721       C  
ATOM   2260  O   GLY I 539      -3.113 -23.263  78.594  1.00125.54           O  
ANISOU 2260  O   GLY I 539    13834  20906  12958    917    210   2941       O  
ATOM   2261  N   LYS I 540      -3.250 -25.512  78.697  1.00114.22           N  
ANISOU 2261  N   LYS I 540    12364  19135  11898   1006    584   2607       N  
ATOM   2262  CA  LYS I 540      -4.345 -25.581  77.739  1.00107.80           C  
ANISOU 2262  CA  LYS I 540    11429  18357  11173   1239    900   2753       C  
ATOM   2263  C   LYS I 540      -5.684 -25.197  78.352  1.00105.92           C  
ANISOU 2263  C   LYS I 540    10838  18301  11105   1281    850   3066       C  
ATOM   2264  O   LYS I 540      -6.656 -25.012  77.612  1.00106.22           O  
ANISOU 2264  O   LYS I 540    10765  18409  11186   1469   1067   3239       O  
ATOM   2265  CB  LYS I 540      -4.432 -26.988  77.142  1.00103.20           C  
ANISOU 2265  CB  LYS I 540    10890  17538  10785   1380   1252   2507       C  
ATOM   2266  CG  LYS I 540      -3.099 -27.535  76.654  1.00103.60           C  
ANISOU 2266  CG  LYS I 540    11259  17388  10718   1334   1309   2158       C  
ATOM   2267  CD  LYS I 540      -3.283 -28.656  75.641  1.00 99.78           C  
ANISOU 2267  CD  LYS I 540    10818  16705  10388   1520   1714   1943       C  
ATOM   2268  CE  LYS I 540      -4.108 -29.797  76.218  1.00 95.52           C  
ANISOU 2268  CE  LYS I 540    10040  16070  10184   1594   1818   1903       C  
ATOM   2269  NZ  LYS I 540      -4.299 -30.897  75.233  1.00 92.62           N  
ANISOU 2269  NZ  LYS I 540     9696  15510   9984   1776   2199   1678       N  
ATOM   2270  N   ASN I 541      -5.757 -25.067  79.680  1.00107.59           N  
ANISOU 2270  N   ASN I 541    10879  18587  11414   1108    583   3138       N  
ATOM   2271  CA  ASN I 541      -7.001 -24.679  80.331  1.00103.69           C  
ANISOU 2271  CA  ASN I 541    10041  18268  11091   1132    535   3427       C  
ATOM   2272  C   ASN I 541      -7.323 -23.202  80.150  1.00104.39           C  
ANISOU 2272  C   ASN I 541    10041  18616  11007   1139    351   3699       C  
ATOM   2273  O   ASN I 541      -8.470 -22.806  80.374  1.00100.29           O  
ANISOU 2273  O   ASN I 541     9237  18253  10616   1219    369   3953       O  
ATOM   2274  CB  ASN I 541      -6.941 -25.013  81.824  1.00 98.13           C  
ANISOU 2274  CB  ASN I 541     9198  17545  10544    929    324   3404       C  
ATOM   2275  CG  ASN I 541      -7.064 -26.499  82.097  1.00 91.86           C  
ANISOU 2275  CG  ASN I 541     8416  16510   9976    975    523   3204       C  
ATOM   2276  OD1 ASN I 541      -7.808 -27.208  81.419  1.00 87.89           O  
ANISOU 2276  OD1 ASN I 541     7853  15924   9618   1180    827   3200       O  
ATOM   2277  ND2 ASN I 541      -6.332 -26.978  83.095  1.00 91.52           N  
ANISOU 2277  ND2 ASN I 541     8463  16348   9961    786    344   3033       N  
ATOM   2278  N   MET I 542      -6.345 -22.382  79.751  1.00100.03           N  
ANISOU 2278  N   MET I 542     9732  18110  10167   1067    169   3647       N  
ATOM   2279  CA  MET I 542      -6.598 -20.951  79.602  1.00107.11           C  
ANISOU 2279  CA  MET I 542    10563  19248  10886   1080    -45   3891       C  
ATOM   2280  C   MET I 542      -7.573 -20.664  78.466  1.00110.80           C  
ANISOU 2280  C   MET I 542    10988  19779  11330   1347    212   4074       C  
ATOM   2281  O   MET I 542      -8.344 -19.701  78.542  1.00119.98           O  
ANISOU 2281  O   MET I 542    11955  21155  12476   1411     88   4336       O  
ATOM   2282  CB  MET I 542      -5.285 -20.200  79.375  1.00109.73           C  
ANISOU 2282  CB  MET I 542    11207  19587  10897    955   -292   3774       C  
ATOM   2283  CG  MET I 542      -4.472 -19.976  80.642  1.00114.44           C  
ANISOU 2283  CG  MET I 542    11789  20213  11481    672   -653   3689       C  
ATOM   2284  SD  MET I 542      -3.098 -18.809  80.496  1.00120.21           S  
ANISOU 2284  SD  MET I 542    12835  21010  11828    520  -1013   3618       S  
ATOM   2285  CE  MET I 542      -3.350 -18.135  78.856  1.00119.83           C  
ANISOU 2285  CE  MET I 542    12997  21002  11532    787   -824   3729       C  
ATOM   2286  N   ASP I 543      -7.567 -21.488  77.421  1.00107.33           N  
ANISOU 2286  N   ASP I 543    10726  19158  10899   1505    570   3934       N  
ATOM   2287  CA  ASP I 543      -8.505 -21.355  76.317  1.00112.31           C  
ANISOU 2287  CA  ASP I 543    11336  19815  11521   1756    859   4087       C  
ATOM   2288  C   ASP I 543      -9.719 -22.265  76.467  1.00114.77           C  
ANISOU 2288  C   ASP I 543    11372  20082  12154   1883   1127   4159       C  
ATOM   2289  O   ASP I 543     -10.509 -22.387  75.525  1.00112.02           O  
ANISOU 2289  O   ASP I 543    11014  19715  11832   2094   1419   4251       O  
ATOM   2290  CB  ASP I 543      -7.799 -21.637  74.988  1.00105.85           C  
ANISOU 2290  CB  ASP I 543    10888  18822  10508   1852   1116   3895       C  
ATOM   2291  CG  ASP I 543      -6.643 -20.689  74.729  1.00104.15           C  
ANISOU 2291  CG  ASP I 543    10981  18643   9948   1748    873   3838       C  
ATOM   2292  OD1 ASP I 543      -5.763 -20.564  75.608  1.00104.18           O  
ANISOU 2292  OD1 ASP I 543    11023  18656   9905   1536    576   3729       O  
ATOM   2293  OD2 ASP I 543      -6.614 -20.068  73.645  1.00102.63           O  
ANISOU 2293  OD2 ASP I 543    11011  18462   9522   1880    981   3902       O  
ATOM   2294  N   ALA I 544      -9.887 -22.900  77.625  1.00106.02           N  
ANISOU 2294  N   ALA I 544    12888  16468  10928   3367   2240   1962       N  
ATOM   2295  CA  ALA I 544     -11.003 -23.810  77.843  1.00114.68           C  
ANISOU 2295  CA  ALA I 544    14016  17535  12023   3260   2321   1881       C  
ATOM   2296  C   ALA I 544     -12.264 -23.030  78.192  1.00120.59           C  
ANISOU 2296  C   ALA I 544    14826  18204  12790   3327   2394   1936       C  
ATOM   2297  O   ALA I 544     -12.252 -22.179  79.087  1.00124.08           O  
ANISOU 2297  O   ALA I 544    15231  18670  13243   3444   2319   2026       O  
ATOM   2298  CB  ALA I 544     -10.673 -24.808  78.952  1.00115.17           C  
ANISOU 2298  CB  ALA I 544    13984  17705  12069   3206   2213   1836       C  
ATOM   2299  N   ILE I 545     -13.350 -23.327  77.488  1.00119.20           N  
ANISOU 2299  N   ILE I 545    14741  17936  12615   3255   2543   1880       N  
ATOM   2300  CA  ILE I 545     -14.633 -22.664  77.693  1.00113.40           C  
ANISOU 2300  CA  ILE I 545    14074  17118  11897   3314   2634   1920       C  
ATOM   2301  C   ILE I 545     -15.390 -23.390  78.796  1.00108.85           C  
ANISOU 2301  C   ILE I 545    13464  16578  11315   3252   2621   1867       C  
ATOM   2302  O   ILE I 545     -15.412 -24.626  78.845  1.00106.20           O  
ANISOU 2302  O   ILE I 545    13109  16282  10959   3118   2627   1766       O  
ATOM   2303  CB  ILE I 545     -15.437 -22.630  76.377  1.00109.91           C  
ANISOU 2303  CB  ILE I 545    13749  16557  11455   3269   2805   1885       C  
ATOM   2304  CG1 ILE I 545     -14.637 -21.909  75.289  1.00110.37           C  
ANISOU 2304  CG1 ILE I 545    13842  16583  11511   3327   2817   1941       C  
ATOM   2305  CG2 ILE I 545     -16.794 -21.961  76.575  1.00109.08           C  
ANISOU 2305  CG2 ILE I 545    13715  16362  11368   3338   2905   1925       C  
ATOM   2306  CD1 ILE I 545     -15.417 -21.648  74.014  1.00111.64           C  
ANISOU 2306  CD1 ILE I 545    14127  16622  11670   3311   2985   1933       C  
ATOM   2307  N   ILE I 546     -16.000 -22.627  79.700  1.00109.23           N  
ANISOU 2307  N   ILE I 546    13503  16619  11379   3348   2604   1936       N  
ATOM   2308  CA  ILE I 546     -16.774 -23.181  80.804  1.00 97.56           C  
ANISOU 2308  CA  ILE I 546    11998  15176   9895   3298   2599   1894       C  
ATOM   2309  C   ILE I 546     -18.251 -23.121  80.433  1.00 99.86           C  
ANISOU 2309  C   ILE I 546    12385  15363  10194   3273   2760   1857       C  
ATOM   2310  O   ILE I 546     -18.794 -22.041  80.162  1.00102.50           O  
ANISOU 2310  O   ILE I 546    12772  15622  10552   3386   2824   1931       O  
ATOM   2311  CB  ILE I 546     -16.493 -22.429  82.115  1.00 86.81           C  
ANISOU 2311  CB  ILE I 546    10558  13885   8542   3412   2478   1987       C  
ATOM   2312  CG1 ILE I 546     -15.103 -22.787  82.640  1.00 89.23           C  
ANISOU 2312  CG1 ILE I 546    10763  14308   8833   3410   2317   2001       C  
ATOM   2313  CG2 ILE I 546     -17.547 -22.760  83.160  1.00 91.99           C  
ANISOU 2313  CG2 ILE I 546    11206  14554   9193   3373   2507   1953       C  
ATOM   2314  CD1 ILE I 546     -14.688 -22.001  83.863  1.00 87.19           C  
ANISOU 2314  CD1 ILE I 546    10424  14125   8580   3523   2192   2097       C  
ATOM   2315  N   VAL I 547     -18.902 -24.283  80.402  1.00 95.40           N  
ANISOU 2315  N   VAL I 547    11844  14797   9608   3130   2830   1743       N  
ATOM   2316  CA  VAL I 547     -20.332 -24.357  80.121  1.00105.48           C  
ANISOU 2316  CA  VAL I 547    13206  15983  10887   3094   2984   1693       C  
ATOM   2317  C   VAL I 547     -21.055 -24.913  81.340  1.00112.93           C  
ANISOU 2317  C   VAL I 547    14116  16977  11815   3039   2972   1645       C  
ATOM   2318  O   VAL I 547     -20.430 -25.237  82.356  1.00111.79           O  
ANISOU 2318  O   VAL I 547    13885  16934  11656   3030   2846   1656       O  
ATOM   2319  CB  VAL I 547     -20.625 -25.204  78.870  1.00109.70           C  
ANISOU 2319  CB  VAL I 547    13816  16461  11405   2966   3103   1593       C  
ATOM   2320  CG1 VAL I 547     -19.907 -24.633  77.665  1.00111.49           C  
ANISOU 2320  CG1 VAL I 547    14078  16639  11642   3016   3120   1641       C  
ATOM   2321  CG2 VAL I 547     -20.219 -26.651  79.099  1.00110.47           C  
ANISOU 2321  CG2 VAL I 547    13863  16645  11463   2811   3057   1488       C  
ATOM   2322  N   ASP I 548     -22.378 -25.032  81.242  1.00114.82           N  
ANISOU 2322  N   ASP I 548    14426  17147  12054   3002   3107   1591       N  
ATOM   2323  CA  ASP I 548     -23.198 -25.426  82.382  1.00118.95           C  
ANISOU 2323  CA  ASP I 548    14925  17709  12561   2957   3115   1548       C  
ATOM   2324  C   ASP I 548     -23.475 -26.928  82.398  1.00120.86           C  
ANISOU 2324  C   ASP I 548    15176  17991  12754   2778   3148   1418       C  
ATOM   2325  O   ASP I 548     -23.126 -27.618  83.360  1.00115.61           O  
ANISOU 2325  O   ASP I 548    14444  17423  12058   2719   3056   1395       O  
ATOM   2326  CB  ASP I 548     -24.511 -24.636  82.372  1.00121.98           C  
ANISOU 2326  CB  ASP I 548    15376  18001  12971   3031   3242   1565       C  
ATOM   2327  CG  ASP I 548     -25.605 -25.307  83.171  1.00124.65           C  
ANISOU 2327  CG  ASP I 548    15720  18357  13283   2940   3306   1477       C  
ATOM   2328  OD1 ASP I 548     -25.438 -25.442  84.399  1.00124.90           O  
ANISOU 2328  OD1 ASP I 548    15678  18477  13300   2935   3216   1490       O  
ATOM   2329  OD2 ASP I 548     -26.630 -25.698  82.571  1.00124.25           O  
ANISOU 2329  OD2 ASP I 548    15750  18235  13224   2874   3448   1396       O  
ATOM   2330  N   SER I 549     -24.101 -27.444  81.345  1.00123.35           N  
ANISOU 2330  N   SER I 549    15574  18236  13059   2691   3280   1336       N  
ATOM   2331  CA  SER I 549     -24.530 -28.831  81.319  1.00119.42           C  
ANISOU 2331  CA  SER I 549    15092  17771  12510   2522   3330   1208       C  
ATOM   2332  C   SER I 549     -23.770 -29.621  80.261  1.00107.25           C  
ANISOU 2332  C   SER I 549    13558  16243  10950   2429   3330   1155       C  
ATOM   2333  O   SER I 549     -23.219 -29.067  79.304  1.00106.74           O  
ANISOU 2333  O   SER I 549    13514  16130  10912   2484   3339   1200       O  
ATOM   2334  CB  SER I 549     -26.040 -28.936  81.073  1.00126.71           C  
ANISOU 2334  CB  SER I 549    16102  18615  13425   2476   3495   1136       C  
ATOM   2335  OG  SER I 549     -26.392 -28.443  79.795  1.00130.76           O  
ANISOU 2335  OG  SER I 549    16698  19018  13965   2512   3610   1143       O  
ATOM   2336  N   GLU I 550     -23.738 -30.940  80.471  1.00102.17           N  
ANISOU 2336  N   GLU I 550    12895  15670  10253   2286   3320   1058       N  
ATOM   2337  CA  GLU I 550     -23.152 -31.856  79.498  1.00100.37           C  
ANISOU 2337  CA  GLU I 550    12673  15463  10001   2180   3336    987       C  
ATOM   2338  C   GLU I 550     -23.919 -31.826  78.179  1.00101.20           C  
ANISOU 2338  C   GLU I 550    12875  15466  10110   2132   3500    932       C  
ATOM   2339  O   GLU I 550     -23.321 -31.916  77.096  1.00107.21           O  
ANISOU 2339  O   GLU I 550    13650  16209  10877   2108   3522    922       O  
ATOM   2340  CB  GLU I 550     -23.116 -33.265  80.103  1.00 94.95           C  
ANISOU 2340  CB  GLU I 550    11950  14874   9251   2046   3299    899       C  
ATOM   2341  CG  GLU I 550     -23.013 -34.431  79.131  1.00 98.72           C  
ANISOU 2341  CG  GLU I 550    12451  15369   9689   1903   3365    791       C  
ATOM   2342  CD  GLU I 550     -24.374 -35.005  78.767  1.00101.23           C  
ANISOU 2342  CD  GLU I 550    12854  15638   9970   1790   3523    685       C  
ATOM   2343  OE1 GLU I 550     -24.769 -34.903  77.588  1.00105.37           O  
ANISOU 2343  OE1 GLU I 550    13444  16088  10504   1757   3642    646       O  
ATOM   2344  OE2 GLU I 550     -25.050 -35.553  79.666  1.00102.05           O  
ANISOU 2344  OE2 GLU I 550    12962  15782  10032   1734   3528    642       O  
ATOM   2345  N   LYS I 551     -25.248 -31.691  78.258  1.00103.12           N  
ANISOU 2345  N   LYS I 551    13187  15645  10349   2120   3619    895       N  
ATOM   2346  CA  LYS I 551     -26.075 -31.595  77.058  1.00104.45           C  
ANISOU 2346  CA  LYS I 551    13453  15711  10521   2090   3779    850       C  
ATOM   2347  C   LYS I 551     -25.724 -30.358  76.240  1.00107.78           C  
ANISOU 2347  C   LYS I 551    13912  16044  10997   2225   3797    953       C  
ATOM   2348  O   LYS I 551     -25.573 -30.440  75.014  1.00113.38           O  
ANISOU 2348  O   LYS I 551    14672  16702  11704   2188   3871    933       O  
ATOM   2349  CB  LYS I 551     -27.552 -31.587  77.447  1.00102.21           C  
ANISOU 2349  CB  LYS I 551    13230  15379  10227   2076   3892    802       C  
ATOM   2350  CG  LYS I 551     -28.511 -31.753  76.283  1.00101.98           C  
ANISOU 2350  CG  LYS I 551    13303  15255  10188   2022   4062    734       C  
ATOM   2351  CD  LYS I 551     -29.884 -31.198  76.630  1.00104.64           C  
ANISOU 2351  CD  LYS I 551    13704  15514  10542   2084   4168    733       C  
ATOM   2352  CE  LYS I 551     -29.948 -29.693  76.419  1.00104.90           C  
ANISOU 2352  CE  LYS I 551    13772  15442  10643   2273   4185    860       C  
ATOM   2353  NZ  LYS I 551     -29.835 -29.318  74.983  1.00108.02           N  
ANISOU 2353  NZ  LYS I 551    14249  15736  11057   2301   4272    887       N  
ATOM   2354  N   THR I 552     -25.568 -29.205  76.904  1.00111.16           N  
ANISOU 2354  N   THR I 552    14314  16455  11468   2380   3730   1067       N  
ATOM   2355  CA  THR I 552     -25.097 -28.008  76.214  1.00111.84           C  
ANISOU 2355  CA  THR I 552    14429  16469  11597   2518   3728   1177       C  
ATOM   2356  C   THR I 552     -23.677 -28.188  75.699  1.00110.00           C  
ANISOU 2356  C   THR I 552    14144  16291  11359   2499   3633   1198       C  
ATOM   2357  O   THR I 552     -23.314 -27.595  74.680  1.00110.41           O  
ANISOU 2357  O   THR I 552    14241  16281  11427   2549   3672   1247       O  
ATOM   2358  CB  THR I 552     -25.166 -26.789  77.134  1.00116.06           C  
ANISOU 2358  CB  THR I 552    14933  16993  12170   2687   3664   1294       C  
ATOM   2359  OG1 THR I 552     -24.599 -27.113  78.411  1.00115.51           O  
ANISOU 2359  OG1 THR I 552    14760  17039  12089   2676   3523   1300       O  
ATOM   2360  CG2 THR I 552     -26.605 -26.322  77.305  1.00117.04           C  
ANISOU 2360  CG2 THR I 552    15129  17030  12311   2738   3790   1289       C  
ATOM   2361  N   GLY I 553     -22.877 -29.018  76.372  1.00104.37           N  
ANISOU 2361  N   GLY I 553    13340  15695  10622   2427   3515   1161       N  
ATOM   2362  CA  GLY I 553     -21.543 -29.316  75.877  1.00100.93           C  
ANISOU 2362  CA  GLY I 553    12851  15317  10181   2401   3432   1166       C  
ATOM   2363  C   GLY I 553     -21.560 -30.003  74.526  1.00102.48           C  
ANISOU 2363  C   GLY I 553    13102  15482  10355   2281   3540   1080       C  
ATOM   2364  O   GLY I 553     -20.921 -29.543  73.574  1.00102.44           O  
ANISOU 2364  O   GLY I 553    13116  15442  10362   2312   3554   1118       O  
ATOM   2365  N   ARG I 554     -22.312 -31.105  74.414  1.00 98.75           N  
ANISOU 2365  N   ARG I 554    12655  15022   9844   2139   3624    963       N  
ATOM   2366  CA  ARG I 554     -22.347 -31.802  73.130  1.00102.32           C  
ANISOU 2366  CA  ARG I 554    13154  15452  10270   2017   3731    877       C  
ATOM   2367  C   ARG I 554     -23.131 -31.022  72.075  1.00111.37           C  
ANISOU 2367  C   ARG I 554    14413  16468  11435   2061   3876    906       C  
ATOM   2368  O   ARG I 554     -22.819 -31.122  70.878  1.00111.65           O  
ANISOU 2368  O   ARG I 554    14487  16474  11462   2011   3944    885       O  
ATOM   2369  CB  ARG I 554     -22.893 -33.225  73.291  1.00 91.63           C  
ANISOU 2369  CB  ARG I 554    11794  14159   8864   1852   3778    743       C  
ATOM   2370  CG  ARG I 554     -23.999 -33.428  74.311  1.00 88.98           C  
ANISOU 2370  CG  ARG I 554    11473  13824   8511   1842   3800    715       C  
ATOM   2371  CD  ARG I 554     -24.477 -34.878  74.265  1.00 84.15           C  
ANISOU 2371  CD  ARG I 554    10864  13273   7836   1669   3857    578       C  
ATOM   2372  NE  ARG I 554     -25.670 -35.119  75.069  1.00 88.13           N  
ANISOU 2372  NE  ARG I 554    11400  13772   8314   1640   3906    536       N  
ATOM   2373  CZ  ARG I 554     -26.916 -34.945  74.639  1.00 94.19           C  
ANISOU 2373  CZ  ARG I 554    12254  14457   9076   1625   4046    497       C  
ATOM   2374  NH1 ARG I 554     -27.140 -34.527  73.400  1.00 99.16           N  
ANISOU 2374  NH1 ARG I 554    12954  14998   9725   1639   4151    503       N  
ATOM   2375  NH2 ARG I 554     -27.939 -35.197  75.446  1.00 94.05           N  
ANISOU 2375  NH2 ARG I 554    12256  14447   9031   1599   4083    454       N  
ATOM   2376  N   ASP I 555     -24.106 -30.203  72.491  1.00120.71           N  
ANISOU 2376  N   ASP I 555    15652  17571  12642   2162   3925    961       N  
ATOM   2377  CA  ASP I 555     -24.789 -29.329  71.540  1.00122.43           C  
ANISOU 2377  CA  ASP I 555    15982  17653  12882   2237   4055   1011       C  
ATOM   2378  C   ASP I 555     -23.840 -28.284  70.958  1.00115.33           C  
ANISOU 2378  C   ASP I 555    15088  16719  12011   2353   4011   1125       C  
ATOM   2379  O   ASP I 555     -23.826 -28.062  69.739  1.00120.34           O  
ANISOU 2379  O   ASP I 555    15800  17280  12642   2342   4107   1135       O  
ATOM   2380  CB  ASP I 555     -25.987 -28.651  72.207  1.00123.71           C  
ANISOU 2380  CB  ASP I 555    16194  17742  13069   2337   4110   1050       C  
ATOM   2381  CG  ASP I 555     -27.137 -29.610  72.458  1.00127.69           C  
ANISOU 2381  CG  ASP I 555    16727  18251  13540   2219   4200    930       C  
ATOM   2382  OD1 ASP I 555     -26.954 -30.828  72.251  1.00129.42           O  
ANISOU 2382  OD1 ASP I 555    16916  18545  13713   2060   4203    822       O  
ATOM   2383  OD2 ASP I 555     -28.224 -29.145  72.861  1.00130.26           O  
ANISOU 2383  OD2 ASP I 555    17104  18508  13882   2286   4271    944       O  
ATOM   2384  N   CYS I 556     -23.031 -27.643  71.812  1.00115.24           N  
ANISOU 2384  N   CYS I 556    14998  16764  12024   2463   3868   1213       N  
ATOM   2385  CA  CYS I 556     -22.033 -26.693  71.331  1.00104.28           C  
ANISOU 2385  CA  CYS I 556    13605  15361  10655   2570   3812   1318       C  
ATOM   2386  C   CYS I 556     -20.975 -27.374  70.476  1.00 96.08           C  
ANISOU 2386  C   CYS I 556    12536  14379   9592   2461   3792   1264       C  
ATOM   2387  O   CYS I 556     -20.496 -26.778  69.505  1.00 95.89           O  
ANISOU 2387  O   CYS I 556    12558  14306   9570   2500   3828   1316       O  
ATOM   2388  CB  CYS I 556     -21.375 -25.980  72.512  1.00 99.86           C  
ANISOU 2388  CB  CYS I 556    12956  14866  10121   2700   3655   1413       C  
ATOM   2389  SG  CYS I 556     -22.369 -24.666  73.248  1.00103.40           S  
ANISOU 2389  SG  CYS I 556    13446  15234  10606   2883   3681   1523       S  
ATOM   2390  N   ILE I 557     -20.614 -28.617  70.811  1.00 98.43           N  
ANISOU 2390  N   ILE I 557    12758  14779   9863   2325   3742   1160       N  
ATOM   2391  CA  ILE I 557     -19.634 -29.354  70.015  1.00100.37           C  
ANISOU 2391  CA  ILE I 557    12966  15086  10085   2216   3731   1096       C  
ATOM   2392  C   ILE I 557     -20.171 -29.611  68.610  1.00109.15           C  
ANISOU 2392  C   ILE I 557    14175  16122  11176   2123   3895   1040       C  
ATOM   2393  O   ILE I 557     -19.467 -29.396  67.613  1.00109.96           O  
ANISOU 2393  O   ILE I 557    14295  16214  11272   2109   3921   1055       O  
ATOM   2394  CB  ILE I 557     -19.245 -30.661  70.734  1.00100.29           C  
ANISOU 2394  CB  ILE I 557    12857  15197  10050   2102   3650    999       C  
ATOM   2395  CG1 ILE I 557     -18.220 -30.376  71.835  1.00 94.32           C  
ANISOU 2395  CG1 ILE I 557    11997  14527   9312   2197   3470   1068       C  
ATOM   2396  CG2 ILE I 557     -18.694 -31.691  69.754  1.00103.59           C  
ANISOU 2396  CG2 ILE I 557    13258  15664  10437   1953   3697    896       C  
ATOM   2397  CD1 ILE I 557     -17.797 -31.605  72.614  1.00 92.63           C  
ANISOU 2397  CD1 ILE I 557    11691  14430   9073   2108   3382    991       C  
ATOM   2398  N   GLN I 558     -21.434 -30.041  68.503  1.00108.23           N  
ANISOU 2398  N   GLN I 558    14126  15953  11045   2059   4013    977       N  
ATOM   2399  CA  GLN I 558     -22.002 -30.285  67.179  1.00112.25           C  
ANISOU 2399  CA  GLN I 558    14733  16386  11532   1973   4173    928       C  
ATOM   2400  C   GLN I 558     -22.220 -28.987  66.405  1.00113.58           C  
ANISOU 2400  C   GLN I 558    15010  16422  11724   2100   4250   1043       C  
ATOM   2401  O   GLN I 558     -22.060 -28.969  65.177  1.00113.83           O  
ANISOU 2401  O   GLN I 558    15105  16406  11738   2050   4343   1036       O  
ATOM   2402  CB  GLN I 558     -23.310 -31.069  67.289  1.00110.42           C  
ANISOU 2402  CB  GLN I 558    14548  16131  11276   1879   4278    832       C  
ATOM   2403  CG  GLN I 558     -23.782 -31.641  65.954  1.00110.07           C  
ANISOU 2403  CG  GLN I 558    14584  16037  11199   1756   4432    757       C  
ATOM   2404  CD  GLN I 558     -25.002 -32.531  66.080  1.00112.01           C  
ANISOU 2404  CD  GLN I 558    14866  16277  11415   1655   4527    652       C  
ATOM   2405  OE1 GLN I 558     -25.789 -32.401  67.018  1.00111.63           O  
ANISOU 2405  OE1 GLN I 558    14824  16211  11377   1706   4516    658       O  
ATOM   2406  NE2 GLN I 558     -25.166 -33.445  65.130  1.00113.21           N  
ANISOU 2406  NE2 GLN I 558    15041  16448  11527   1509   4623    556       N  
ATOM   2407  N   TYR I 559     -22.560 -27.891  67.096  1.00112.99           N  
ANISOU 2407  N   TYR I 559    14959  16288  11686   2267   4215   1152       N  
ATOM   2408  CA  TYR I 559     -22.693 -26.611  66.403  1.00112.37           C  
ANISOU 2408  CA  TYR I 559    14983  16085  11627   2405   4282   1273       C  
ATOM   2409  C   TYR I 559     -21.347 -26.114  65.885  1.00110.11           C  
ANISOU 2409  C   TYR I 559    14664  15837  11337   2441   4208   1336       C  
ATOM   2410  O   TYR I 559     -21.276 -25.528  64.798  1.00111.09           O  
ANISOU 2410  O   TYR I 559    14881  15875  11452   2470   4296   1390       O  
ATOM   2411  CB  TYR I 559     -23.326 -25.562  67.318  1.00117.41           C  
ANISOU 2411  CB  TYR I 559    15641  16665  12304   2582   4256   1374       C  
ATOM   2412  CG  TYR I 559     -23.334 -24.176  66.708  1.00121.87           C  
ANISOU 2412  CG  TYR I 559    16303  17115  12890   2747   4307   1513       C  
ATOM   2413  CD1 TYR I 559     -24.145 -23.874  65.620  1.00124.30           C  
ANISOU 2413  CD1 TYR I 559    16758  17277  13192   2758   4477   1532       C  
ATOM   2414  CD2 TYR I 559     -22.513 -23.174  67.207  1.00121.65           C  
ANISOU 2414  CD2 TYR I 559    16221  17120  12880   2893   4188   1629       C  
ATOM   2415  CE1 TYR I 559     -24.145 -22.606  65.056  1.00122.88           C  
ANISOU 2415  CE1 TYR I 559    16675  16987  13025   2915   4528   1666       C  
ATOM   2416  CE2 TYR I 559     -22.505 -21.907  66.652  1.00120.13           C  
ANISOU 2416  CE2 TYR I 559    16118  16828  12698   3049   4233   1760       C  
ATOM   2417  CZ  TYR I 559     -23.322 -21.628  65.579  1.00118.78           C  
ANISOU 2417  CZ  TYR I 559    16098  16512  12522   3060   4404   1780       C  
ATOM   2418  OH  TYR I 559     -23.312 -20.366  65.027  1.00114.85           O  
ANISOU 2418  OH  TYR I 559    15696  15911  12030   3222   4454   1916       O  
ATOM   2419  N   ILE I 560     -20.271 -26.337  66.645  1.00111.27           N  
ANISOU 2419  N   ILE I 560    14682  16108  11487   2440   4051   1332       N  
ATOM   2420  CA  ILE I 560     -18.937 -25.981  66.169  1.00102.51           C  
ANISOU 2420  CA  ILE I 560    13533  15047  10371   2461   3979   1375       C  
ATOM   2421  C   ILE I 560     -18.544 -26.851  64.979  1.00 98.68           C  
ANISOU 2421  C   ILE I 560    13061  14585   9849   2295   4059   1278       C  
ATOM   2422  O   ILE I 560     -17.966 -26.361  64.000  1.00 96.19           O  
ANISOU 2422  O   ILE I 560    12790  14238   9519   2306   4098   1321       O  
ATOM   2423  CB  ILE I 560     -17.916 -26.075  67.321  1.00 96.45           C  
ANISOU 2423  CB  ILE I 560    12626  14403   9616   2501   3794   1389       C  
ATOM   2424  CG1 ILE I 560     -18.100 -24.908  68.292  1.00 87.92           C  
ANISOU 2424  CG1 ILE I 560    11540  13297   8570   2687   3716   1513       C  
ATOM   2425  CG2 ILE I 560     -16.478 -26.110  66.808  1.00 96.43           C  
ANISOU 2425  CG2 ILE I 560    12566  14474   9600   2476   3723   1390       C  
ATOM   2426  CD1 ILE I 560     -17.146 -24.934  69.457  1.00 89.59           C  
ANISOU 2426  CD1 ILE I 560    11622  13625   8793   2735   3536   1537       C  
ATOM   2427  N   LYS I 561     -18.884 -28.143  65.027  1.00 95.03           N  
ANISOU 2427  N   LYS I 561    12562  14180   9367   2139   4091   1148       N  
ATOM   2428  CA  LYS I 561     -18.564 -29.038  63.917  1.00 98.76           C  
ANISOU 2428  CA  LYS I 561    13037  14685   9802   1976   4173   1047       C  
ATOM   2429  C   LYS I 561     -19.327 -28.671  62.648  1.00111.00           C  
ANISOU 2429  C   LYS I 561    14729  16108  11336   1956   4345   1067       C  
ATOM   2430  O   LYS I 561     -18.793 -28.825  61.542  1.00114.07           O  
ANISOU 2430  O   LYS I 561    15140  16503  11697   1876   4406   1043       O  
ATOM   2431  CB  LYS I 561     -18.850 -30.486  64.310  1.00 92.94           C  
ANISOU 2431  CB  LYS I 561    12230  14038   9044   1824   4172    907       C  
ATOM   2432  CG  LYS I 561     -18.364 -31.521  63.303  1.00 86.40           C  
ANISOU 2432  CG  LYS I 561    11373  13278   8178   1652   4235    793       C  
ATOM   2433  CD  LYS I 561     -18.881 -32.894  63.667  1.00 85.41           C  
ANISOU 2433  CD  LYS I 561    11198  13228   8028   1513   4255    661       C  
ATOM   2434  CE  LYS I 561     -18.396 -33.283  65.047  1.00 85.39           C  
ANISOU 2434  CE  LYS I 561    11085  13318   8041   1547   4101    652       C  
ATOM   2435  NZ  LYS I 561     -19.085 -34.487  65.576  1.00 86.03           N  
ANISOU 2435  NZ  LYS I 561    11136  13457   8095   1436   4120    542       N  
ATOM   2436  N   GLU I 562     -20.562 -28.179  62.777  1.00109.24           N  
ANISOU 2436  N   GLU I 562    14608  15768  11129   2030   4430   1112       N  
ATOM   2437  CA  GLU I 562     -21.284 -27.721  61.591  1.00109.13           C  
ANISOU 2437  CA  GLU I 562    14748  15612  11105   2035   4596   1149       C  
ATOM   2438  C   GLU I 562     -20.705 -26.424  61.037  1.00103.40           C  
ANISOU 2438  C   GLU I 562    14088  14813  10386   2167   4595   1285       C  
ATOM   2439  O   GLU I 562     -20.729 -26.210  59.819  1.00105.58           O  
ANISOU 2439  O   GLU I 562    14466  15011  10639   2130   4711   1305       O  
ATOM   2440  CB  GLU I 562     -22.770 -27.539  61.902  1.00116.28           C  
ANISOU 2440  CB  GLU I 562    15751  16401  12030   2089   4692   1160       C  
ATOM   2441  CG  GLU I 562     -23.506 -28.826  62.227  1.00120.29           C  
ANISOU 2441  CG  GLU I 562    16222  16961  12519   1946   4728   1021       C  
ATOM   2442  CD  GLU I 562     -24.996 -28.612  62.411  1.00125.93           C  
ANISOU 2442  CD  GLU I 562    17047  17548  13252   1998   4841   1028       C  
ATOM   2443  OE1 GLU I 562     -25.545 -27.672  61.798  1.00128.84           O  
ANISOU 2443  OE1 GLU I 562    17553  17762  13639   2102   4947   1119       O  
ATOM   2444  OE2 GLU I 562     -25.618 -29.388  63.166  1.00126.84           O  
ANISOU 2444  OE2 GLU I 562    17116  17715  13361   1937   4828    941       O  
ATOM   2445  N   GLN I 563     -20.182 -25.555  61.901  1.00 99.16           N  
ANISOU 2445  N   GLN I 563    13498  14303   9877   2318   4468   1381       N  
ATOM   2446  CA  GLN I 563     -19.658 -24.264  61.469  1.00101.69           C  
ANISOU 2446  CA  GLN I 563    13878  14560  10199   2460   4460   1518       C  
ATOM   2447  C   GLN I 563     -18.236 -24.339  60.924  1.00108.29           C  
ANISOU 2447  C   GLN I 563    14650  15489  11008   2403   4394   1508       C  
ATOM   2448  O   GLN I 563     -17.712 -23.299  60.506  1.00115.89           O  
ANISOU 2448  O   GLN I 563    15660  16409  11962   2509   4386   1617       O  
ATOM   2449  CB  GLN I 563     -19.707 -23.261  62.625  1.00 94.35           C  
ANISOU 2449  CB  GLN I 563    12916  13626   9308   2653   4352   1628       C  
ATOM   2450  CG  GLN I 563     -21.108 -22.797  62.998  1.00 98.11           C  
ANISOU 2450  CG  GLN I 563    13483  13983   9813   2754   4438   1672       C  
ATOM   2451  CD  GLN I 563     -21.595 -21.644  62.137  1.00102.58           C  
ANISOU 2451  CD  GLN I 563    14208  14388  10378   2884   4560   1794       C  
ATOM   2452  OE1 GLN I 563     -21.175 -20.501  62.317  1.00102.70           O  
ANISOU 2452  OE1 GLN I 563    14233  14385  10403   3047   4505   1920       O  
ATOM   2453  NE2 GLN I 563     -22.487 -21.941  61.201  1.00102.97           N  
ANISOU 2453  NE2 GLN I 563    14390  14320  10416   2814   4730   1760       N  
ATOM   2454  N   ARG I 564     -17.617 -25.528  60.924  1.00107.54           N  
ANISOU 2454  N   ARG I 564    14447  15518  10895   2243   4351   1382       N  
ATOM   2455  CA  ARG I 564     -16.265 -25.755  60.393  1.00111.03           C  
ANISOU 2455  CA  ARG I 564    14818  16056  11311   2171   4298   1351       C  
ATOM   2456  C   ARG I 564     -15.231 -24.859  61.077  1.00111.74           C  
ANISOU 2456  C   ARG I 564    14841  16197  11419   2316   4147   1447       C  
ATOM   2457  O   ARG I 564     -14.380 -24.244  60.431  1.00111.15           O  
ANISOU 2457  O   ARG I 564    14784  16125  11323   2346   4140   1502       O  
ATOM   2458  CB  ARG I 564     -16.225 -25.572  58.871  1.00113.98           C  
ANISOU 2458  CB  ARG I 564    15302  16361  11645   2101   4440   1359       C  
ATOM   2459  CG  ARG I 564     -17.309 -26.315  58.107  1.00115.11           C  
ANISOU 2459  CG  ARG I 564    15532  16436  11770   1973   4602   1282       C  
ATOM   2460  CD  ARG I 564     -17.126 -26.146  56.606  1.00115.76           C  
ANISOU 2460  CD  ARG I 564    15716  16458  11809   1897   4734   1294       C  
ATOM   2461  NE  ARG I 564     -16.107 -27.043  56.070  1.00118.16           N  
ANISOU 2461  NE  ARG I 564    15918  16897  12081   1737   4716   1186       N  
ATOM   2462  CZ  ARG I 564     -15.747 -27.089  54.791  1.00121.58           C  
ANISOU 2462  CZ  ARG I 564    16406  17319  12471   1640   4817   1173       C  
ATOM   2463  NH1 ARG I 564     -16.326 -26.286  53.908  1.00124.09           N  
ANISOU 2463  NH1 ARG I 564    16890  17485  12772   1685   4942   1267       N  
ATOM   2464  NH2 ARG I 564     -14.807 -27.937  54.394  1.00120.71           N  
ANISOU 2464  NH2 ARG I 564    16186  17344  12333   1499   4797   1068       N  
ATOM   2465  N   GLY I 565     -15.310 -24.789  62.408  1.00111.76           N  
ANISOU 2465  N   GLY I 565    14764  16243  11456   2403   4026   1468       N  
ATOM   2466  CA  GLY I 565     -14.476 -23.898  63.183  1.00106.54           C  
ANISOU 2466  CA  GLY I 565    14040  15625  10815   2553   3882   1567       C  
ATOM   2467  C   GLY I 565     -13.351 -24.614  63.919  1.00 99.07           C  
ANISOU 2467  C   GLY I 565    12943  14824   9875   2505   3734   1503       C  
ATOM   2468  O   GLY I 565     -13.129 -25.815  63.783  1.00 93.87           O  
ANISOU 2468  O   GLY I 565    12224  14236   9204   2356   3743   1380       O  
ATOM   2469  N   GLU I 566     -12.632 -23.830  64.714  1.00 99.22           N  
ANISOU 2469  N   GLU I 566    12901  14884   9912   2644   3597   1592       N  
ATOM   2470  CA  GLU I 566     -11.533 -24.344  65.525  1.00 99.23           C  
ANISOU 2470  CA  GLU I 566    12765  15015   9922   2633   3444   1554       C  
ATOM   2471  C   GLU I 566     -12.077 -25.265  66.610  1.00 97.98           C  
ANISOU 2471  C   GLU I 566    12539  14905   9785   2586   3393   1487       C  
ATOM   2472  O   GLU I 566     -12.958 -24.850  67.374  1.00 99.29           O  
ANISOU 2472  O   GLU I 566    12729  15025   9971   2668   3385   1539       O  
ATOM   2473  CB  GLU I 566     -10.759 -23.187  66.156  1.00102.51           C  
ANISOU 2473  CB  GLU I 566    13142  15457  10351   2805   3316   1677       C  
ATOM   2474  CG  GLU I 566      -9.656 -22.604  65.285  1.00105.64           C  
ANISOU 2474  CG  GLU I 566    13549  15869  10719   2825   3312   1713       C  
ATOM   2475  CD  GLU I 566      -8.326 -23.311  65.463  1.00108.62           C  
ANISOU 2475  CD  GLU I 566    13808  16372  11091   2762   3208   1642       C  
ATOM   2476  OE1 GLU I 566      -8.271 -24.302  66.221  1.00108.81           O  
ANISOU 2476  OE1 GLU I 566    13743  16468  11132   2702   3142   1565       O  
ATOM   2477  OE2 GLU I 566      -7.332 -22.872  64.847  1.00109.64           O  
ANISOU 2477  OE2 GLU I 566    13933  16529  11198   2778   3194   1664       O  
ATOM   2478  N   PRO I 567     -11.610 -26.511  66.705  1.00 96.62           N  
ANISOU 2478  N   PRO I 567    12284  14822   9603   2458   3363   1372       N  
ATOM   2479  CA  PRO I 567     -12.070 -27.391  67.789  1.00 90.38           C  
ANISOU 2479  CA  PRO I 567    11430  14084   8825   2418   3306   1314       C  
ATOM   2480  C   PRO I 567     -11.548 -26.910  69.134  1.00 84.40           C  
ANISOU 2480  C   PRO I 567    10588  13388   8091   2550   3137   1394       C  
ATOM   2481  O   PRO I 567     -10.356 -26.631  69.288  1.00 81.67           O  
ANISOU 2481  O   PRO I 567    10174  13110   7746   2606   3030   1429       O  
ATOM   2482  CB  PRO I 567     -11.485 -28.759  67.411  1.00 91.51           C  
ANISOU 2482  CB  PRO I 567    11506  14314   8950   2264   3314   1182       C  
ATOM   2483  CG  PRO I 567     -11.160 -28.653  65.953  1.00 96.43           C  
ANISOU 2483  CG  PRO I 567    12186  14903   9550   2192   3428   1155       C  
ATOM   2484  CD  PRO I 567     -10.756 -27.227  65.744  1.00 97.91           C  
ANISOU 2484  CD  PRO I 567    12419  15040   9743   2334   3400   1283       C  
ATOM   2485  N   GLU I 568     -12.451 -26.809  70.108  1.00 83.37           N  
ANISOU 2485  N   GLU I 568    10464  13237   7976   2597   3118   1420       N  
ATOM   2486  CA  GLU I 568     -12.127 -26.294  71.430  1.00 81.90           C  
ANISOU 2486  CA  GLU I 568    10205  13104   7809   2721   2970   1501       C  
ATOM   2487  C   GLU I 568     -12.531 -27.308  72.493  1.00 82.56           C  
ANISOU 2487  C   GLU I 568    10228  13251   7890   2658   2918   1436       C  
ATOM   2488  O   GLU I 568     -13.141 -28.340  72.202  1.00 73.52           O  
ANISOU 2488  O   GLU I 568     9104  12102   6729   2527   3002   1334       O  
ATOM   2489  CB  GLU I 568     -12.810 -24.942  71.684  1.00 76.24           C  
ANISOU 2489  CB  GLU I 568     9553  12302   7112   2868   2990   1620       C  
ATOM   2490  CG  GLU I 568     -12.583 -23.929  70.573  1.00 76.51           C  
ANISOU 2490  CG  GLU I 568     9666  12262   7142   2933   3060   1690       C  
ATOM   2491  CD  GLU I 568     -12.892 -22.511  70.995  1.00 80.90           C  
ANISOU 2491  CD  GLU I 568    10256  12765   7716   3111   3036   1826       C  
ATOM   2492  OE1 GLU I 568     -12.667 -22.182  72.177  1.00 81.74           O  
ANISOU 2492  OE1 GLU I 568    10287  12930   7839   3200   2913   1879       O  
ATOM   2493  OE2 GLU I 568     -13.355 -21.725  70.140  1.00 77.05           O  
ANISOU 2493  OE2 GLU I 568     9870  12179   7225   3165   3141   1882       O  
ATOM   2494  N   THR I 569     -12.182 -27.000  73.740  1.00 79.35           N  
ANISOU 2494  N   THR I 569     9747  12907   7495   2752   2780   1500       N  
ATOM   2495  CA  THR I 569     -12.412 -27.889  74.870  1.00 63.57           C  
ANISOU 2495  CA  THR I 569     7684  10982   5488   2707   2710   1454       C  
ATOM   2496  C   THR I 569     -13.369 -27.220  75.847  1.00 89.38           C  
ANISOU 2496  C   THR I 569    10975  14214   8773   2791   2703   1520       C  
ATOM   2497  O   THR I 569     -13.134 -26.083  76.272  1.00 90.81           O  
ANISOU 2497  O   THR I 569    11145  14384   8973   2928   2641   1628       O  
ATOM   2498  CB  THR I 569     -11.090 -28.246  75.559  1.00 62.47           C  
ANISOU 2498  CB  THR I 569     7427  10969   5341   2736   2546   1465       C  
ATOM   2499  OG1 THR I 569     -10.388 -29.215  74.770  1.00 62.63           O  
ANISOU 2499  OG1 THR I 569     7416  11037   5343   2631   2564   1373       O  
ATOM   2500  CG2 THR I 569     -11.332 -28.824  76.949  1.00 61.85           C  
ANISOU 2500  CG2 THR I 569     7283  10965   5252   2734   2454   1459       C  
ATOM   2501  N   PHE I 570     -14.446 -27.920  76.192  1.00 87.34           N  
ANISOU 2501  N   PHE I 570    10745  13937   8503   2708   2772   1454       N  
ATOM   2502  CA  PHE I 570     -15.460 -27.407  77.099  1.00 90.86           C  
ANISOU 2502  CA  PHE I 570    11214  14349   8962   2770   2783   1499       C  
ATOM   2503  C   PHE I 570     -15.358 -28.074  78.464  1.00 96.69           C  
ANISOU 2503  C   PHE I 570    11869  15186   9682   2750   2673   1483       C  
ATOM   2504  O   PHE I 570     -14.942 -29.230  78.587  1.00100.76           O  
ANISOU 2504  O   PHE I 570    12337  15779  10170   2652   2634   1408       O  
ATOM   2505  CB  PHE I 570     -16.866 -27.613  76.531  1.00 88.06           C  
ANISOU 2505  CB  PHE I 570    10961  13895   8602   2699   2952   1439       C  
ATOM   2506  CG  PHE I 570     -17.122 -26.845  75.272  1.00 92.39           C  
ANISOU 2506  CG  PHE I 570    11602  14337   9165   2735   3068   1469       C  
ATOM   2507  CD1 PHE I 570     -17.361 -25.483  75.319  1.00 93.14           C  
ANISOU 2507  CD1 PHE I 570    11735  14367   9288   2885   3075   1583       C  
ATOM   2508  CD2 PHE I 570     -17.127 -27.481  74.043  1.00 98.84           C  
ANISOU 2508  CD2 PHE I 570    12470  15122   9964   2621   3171   1388       C  
ATOM   2509  CE1 PHE I 570     -17.600 -24.765  74.167  1.00 96.63           C  
ANISOU 2509  CE1 PHE I 570    12269  14710   9738   2928   3182   1621       C  
ATOM   2510  CE2 PHE I 570     -17.365 -26.769  72.883  1.00102.15           C  
ANISOU 2510  CE2 PHE I 570    12980  15443  10390   2654   3280   1423       C  
ATOM   2511  CZ  PHE I 570     -17.602 -25.408  72.949  1.00100.53           C  
ANISOU 2511  CZ  PHE I 570    12818  15169  10212   2811   3285   1542       C  
ATOM   2512  N   LEU I 571     -15.746 -27.324  79.490  1.00 98.96           N  
ANISOU 2512  N   LEU I 571    12140  15476   9986   2847   2625   1559       N  
ATOM   2513  CA  LEU I 571     -15.768 -27.814  80.867  1.00102.95           C  
ANISOU 2513  CA  LEU I 571    12574  16070  10472   2836   2529   1557       C  
ATOM   2514  C   LEU I 571     -17.193 -27.730  81.392  1.00109.75           C  
ANISOU 2514  C   LEU I 571    13489  16879  11334   2819   2620   1539       C  
ATOM   2515  O   LEU I 571     -17.648 -26.640  81.783  1.00115.96           O  
ANISOU 2515  O   LEU I 571    14290  17622  12147   2929   2630   1618       O  
ATOM   2516  CB  LEU I 571     -14.823 -27.003  81.752  1.00103.04           C  
ANISOU 2516  CB  LEU I 571    12502  16152  10498   2966   2375   1664       C  
ATOM   2517  CG  LEU I 571     -13.396 -26.790  81.244  1.00101.94           C  
ANISOU 2517  CG  LEU I 571    12311  16058  10363   3014   2284   1698       C  
ATOM   2518  CD1 LEU I 571     -12.587 -26.012  82.267  1.00101.51           C  
ANISOU 2518  CD1 LEU I 571    12174  16079  10318   3139   2134   1800       C  
ATOM   2519  CD2 LEU I 571     -12.731 -28.121  80.933  1.00102.96           C  
ANISOU 2519  CD2 LEU I 571    12399  16259  10462   2899   2255   1606       C  
ATOM   2520  N   PRO I 572     -17.936 -28.832  81.418  1.00104.52           N  
ANISOU 2520  N   PRO I 572    12854  16219  10638   2688   2693   1436       N  
ATOM   2521  CA  PRO I 572     -19.264 -28.812  82.036  1.00103.01           C  
ANISOU 2521  CA  PRO I 572    12707  15991  10441   2666   2775   1412       C  
ATOM   2522  C   PRO I 572     -19.149 -28.720  83.549  1.00106.99           C  
ANISOU 2522  C   PRO I 572    13137  16581  10935   2710   2661   1460       C  
ATOM   2523  O   PRO I 572     -18.075 -28.879  84.131  1.00100.64           O  
ANISOU 2523  O   PRO I 572    12248  15870  10121   2739   2520   1499       O  
ATOM   2524  CB  PRO I 572     -19.863 -30.145  81.589  1.00 96.72           C  
ANISOU 2524  CB  PRO I 572    11954  15193   9601   2502   2869   1283       C  
ATOM   2525  CG  PRO I 572     -18.679 -31.052  81.593  1.00 96.73           C  
ANISOU 2525  CG  PRO I 572    11883  15295   9576   2449   2761   1257       C  
ATOM   2526  CD  PRO I 572     -17.545 -30.201  81.033  1.00101.76           C  
ANISOU 2526  CD  PRO I 572    12488  15927  10250   2554   2691   1337       C  
ATOM   2527  N   LEU I 573     -20.277 -28.437  84.192  1.00117.27           N  
ANISOU 2527  N   LEU I 573    12286  20698  11576  -2011   2008  -3428       N  
ATOM   2528  CA  LEU I 573     -20.319 -28.346  85.648  1.00100.35           C  
ANISOU 2528  CA  LEU I 573    10173  18522   9432  -2275   2175  -3564       C  
ATOM   2529  C   LEU I 573     -21.103 -29.467  86.305  1.00 95.91           C  
ANISOU 2529  C   LEU I 573     9742  17852   8846  -2376   2278  -3463       C  
ATOM   2530  O   LEU I 573     -20.697 -29.954  87.358  1.00 77.97           O  
ANISOU 2530  O   LEU I 573     7626  15488   6512  -2575   2424  -3448       O  
ATOM   2531  CB  LEU I 573     -20.893 -26.995  86.094  1.00108.72           C  
ANISOU 2531  CB  LEU I 573    10953  19777  10579  -2393   2166  -3837       C  
ATOM   2532  CG  LEU I 573     -19.877 -25.886  86.400  1.00 79.58           C  
ANISOU 2532  CG  LEU I 573     7189  16182   6866  -2498   2173  -4008       C  
ATOM   2533  CD1 LEU I 573     -18.863 -25.659  85.286  1.00 80.35           C  
ANISOU 2533  CD1 LEU I 573     7331  16304   6894  -2329   2049  -3924       C  
ATOM   2534  CD2 LEU I 573     -20.578 -24.591  86.741  1.00 81.20           C  
ANISOU 2534  CD2 LEU I 573     7081  16607   7166  -2604   2150  -4270       C  
ATOM   2535  N   ASP I 574     -22.216 -29.896  85.714  1.00 95.26           N  
ANISOU 2535  N   ASP I 574     9602  17793   8799  -2265   2209  -3399       N  
ATOM   2536  CA  ASP I 574     -22.948 -31.027  86.273  1.00 94.02           C  
ANISOU 2536  CA  ASP I 574     9589  17548   8586  -2379   2302  -3298       C  
ATOM   2537  C   ASP I 574     -22.180 -32.326  86.076  1.00100.82           C  
ANISOU 2537  C   ASP I 574    10724  18253   9328  -2336   2321  -3027       C  
ATOM   2538  O   ASP I 574     -22.194 -33.205  86.946  1.00103.93           O  
ANISOU 2538  O   ASP I 574    11290  18572   9625  -2528   2437  -2940       O  
ATOM   2539  CB  ASP I 574     -24.327 -31.117  85.626  1.00 89.08           C  
ANISOU 2539  CB  ASP I 574     8822  16989   8033  -2273   2228  -3327       C  
ATOM   2540  CG  ASP I 574     -24.256 -31.043  84.117  1.00 84.19           C  
ANISOU 2540  CG  ASP I 574     8130  16403   7455  -1981   2048  -3219       C  
ATOM   2541  OD1 ASP I 574     -23.171 -30.702  83.596  1.00 83.39           O  
ANISOU 2541  OD1 ASP I 574     8054  16299   7332  -1870   1980  -3158       O  
ATOM   2542  OD2 ASP I 574     -25.277 -31.315  83.453  1.00 83.68           O  
ANISOU 2542  OD2 ASP I 574     7981  16372   7442  -1873   1982  -3204       O  
ATOM   2543  N   TYR I 575     -21.481 -32.451  84.949  1.00 96.38           N  
ANISOU 2543  N   TYR I 575    10198  17656   8769  -2102   2210  -2894       N  
ATOM   2544  CA  TYR I 575     -20.831 -33.696  84.565  1.00 91.41           C  
ANISOU 2544  CA  TYR I 575     9792  16888   8051  -2026   2218  -2637       C  
ATOM   2545  C   TYR I 575     -19.392 -33.802  85.052  1.00 90.45           C  
ANISOU 2545  C   TYR I 575     9812  16672   7884  -2108   2324  -2613       C  
ATOM   2546  O   TYR I 575     -18.876 -34.920  85.180  1.00 88.75           O  
ANISOU 2546  O   TYR I 575     9786  16345   7590  -2147   2393  -2421       O  
ATOM   2547  CB  TYR I 575     -20.885 -33.844  83.041  1.00 89.79           C  
ANISOU 2547  CB  TYR I 575     9542  16691   7882  -1731   2055  -2507       C  
ATOM   2548  CG  TYR I 575     -20.331 -35.144  82.528  1.00 88.95           C  
ANISOU 2548  CG  TYR I 575     9637  16458   7702  -1635   2055  -2240       C  
ATOM   2549  CD2 TYR I 575     -19.170 -35.171  81.769  1.00 89.17           C  
ANISOU 2549  CD2 TYR I 575     9718  16428   7736  -1474   2029  -2157       C  
ATOM   2550  CD1 TYR I 575     -20.952 -36.347  82.825  1.00 89.60           C  
ANISOU 2550  CD1 TYR I 575     9854  16490   7701  -1728   2089  -2078       C  
ATOM   2551  CE2 TYR I 575     -18.654 -36.359  81.302  1.00 88.37           C  
ANISOU 2551  CE2 TYR I 575     9774  16221   7581  -1389   2045  -1919       C  
ATOM   2552  CE1 TYR I 575     -20.442 -37.540  82.366  1.00 89.03           C  
ANISOU 2552  CE1 TYR I 575     9948  16322   7557  -1658   2084  -1820       C  
ATOM   2553  CZ  TYR I 575     -19.287 -37.540  81.609  1.00 88.05           C  
ANISOU 2553  CZ  TYR I 575     9852  16143   7461  -1482   2067  -1741       C  
ATOM   2554  OH  TYR I 575     -18.769 -38.724  81.136  1.00 89.72           O  
ANISOU 2554  OH  TYR I 575    10201  16272   7615  -1414   2074  -1483       O  
ATOM   2555  N   LEU I 576     -18.740 -32.679  85.340  1.00 94.11           N  
ANISOU 2555  N   LEU I 576    10179  17185   8394  -2154   2347  -2810       N  
ATOM   2556  CA  LEU I 576     -17.358 -32.706  85.802  1.00 93.03           C  
ANISOU 2556  CA  LEU I 576    10163  16955   8229  -2242   2467  -2833       C  
ATOM   2557  C   LEU I 576     -17.281 -33.261  87.218  1.00 95.13           C  
ANISOU 2557  C   LEU I 576    10552  17160   8433  -2541   2645  -2829       C  
ATOM   2558  O   LEU I 576     -18.013 -32.823  88.111  1.00100.99           O  
ANISOU 2558  O   LEU I 576    11214  17979   9179  -2728   2688  -2960       O  
ATOM   2559  CB  LEU I 576     -16.766 -31.302  85.754  1.00 84.81           C  
ANISOU 2559  CB  LEU I 576     8982  16003   7240  -2243   2437  -3066       C  
ATOM   2560  CG  LEU I 576     -15.257 -31.103  85.892  1.00 83.62           C  
ANISOU 2560  CG  LEU I 576     8926  15766   7079  -2283   2536  -3141       C  
ATOM   2561  CD1 LEU I 576     -14.538 -31.416  84.587  1.00 81.26           C  
ANISOU 2561  CD1 LEU I 576     8686  15410   6780  -2036   2463  -3021       C  
ATOM   2562  CD2 LEU I 576     -14.988 -29.675  86.325  1.00 84.74           C  
ANISOU 2562  CD2 LEU I 576     8920  16029   7247  -2403   2529  -3409       C  
ATOM   2563  N   GLU I 577     -16.397 -34.234  87.423  1.00 97.00           N  
ANISOU 2563  N   GLU I 577    10972  17268   8615  -2604   2757  -2675       N  
ATOM   2564  CA  GLU I 577     -16.152 -34.807  88.739  1.00108.21           C  
ANISOU 2564  CA  GLU I 577    12520  18629   9968  -2922   2935  -2636       C  
ATOM   2565  C   GLU I 577     -14.764 -34.417  89.220  1.00108.32           C  
ANISOU 2565  C   GLU I 577    12572  18559  10025  -3031   3088  -2769       C  
ATOM   2566  O   GLU I 577     -13.768 -34.659  88.528  1.00100.97           O  
ANISOU 2566  O   GLU I 577    11693  17537   9135  -2889   3120  -2732       O  
ATOM   2567  CB  GLU I 577     -16.289 -36.330  88.731  1.00116.15           C  
ANISOU 2567  CB  GLU I 577    13703  19554  10873  -2992   2966  -2322       C  
ATOM   2568  CG  GLU I 577     -16.193 -36.931  90.129  1.00127.60           C  
ANISOU 2568  CG  GLU I 577    15286  20959  12236  -3378   3128  -2232       C  
ATOM   2569  CD  GLU I 577     -17.000 -38.199  90.293  1.00134.91           C  
ANISOU 2569  CD  GLU I 577    16351  21880  13030  -3513   3086  -1937       C  
ATOM   2570  OE1 GLU I 577     -17.686 -38.596  89.330  1.00136.47           O  
ANISOU 2570  OE1 GLU I 577    16533  22111  13210  -3295   2939  -1834       O  
ATOM   2571  OE2 GLU I 577     -16.949 -38.798  91.388  1.00138.69           O  
ANISOU 2571  OE2 GLU I 577    16961  22270  13466  -3827   3149  -1784       O  
ATOM   2572  N   VAL I 578     -14.705 -33.808  90.404  1.00118.24           N  
ANISOU 2572  N   VAL I 578    13797  19845  11285  -3291   3198  -2943       N  
ATOM   2573  CA  VAL I 578     -13.457 -33.454  91.060  1.00120.96           C  
ANISOU 2573  CA  VAL I 578    14183  20082  11694  -3445   3356  -3082       C  
ATOM   2574  C   VAL I 578     -13.485 -34.008  92.478  1.00122.79           C  
ANISOU 2574  C   VAL I 578    14527  20178  11950  -3776   3453  -2965       C  
ATOM   2575  O   VAL I 578     -14.521 -34.444  92.983  1.00120.70           O  
ANISOU 2575  O   VAL I 578    14278  20038  11546  -3944   3478  -2873       O  
ATOM   2576  CB  VAL I 578     -13.213 -31.929  91.093  1.00119.46           C  
ANISOU 2576  CB  VAL I 578    13829  20006  11553  -3424   3325  -3408       C  
ATOM   2577  CG1 VAL I 578     -13.249 -31.338  89.696  1.00114.67           C  
ANISOU 2577  CG1 VAL I 578    13119  19467  10981  -3098   3128  -3440       C  
ATOM   2578  CG2 VAL I 578     -14.233 -31.246  91.995  1.00119.88           C  
ANISOU 2578  CG2 VAL I 578    13759  20198  11594  -3607   3308  -3532       C  
ATOM   2579  N   LYS I 579     -12.320 -33.991  93.110  1.00126.65           N  
ANISOU 2579  N   LYS I 579    15096  20406  12620  -3881   3511  -2973       N  
ATOM   2580  CA  LYS I 579     -12.148 -34.179  94.541  1.00129.99           C  
ANISOU 2580  CA  LYS I 579    15592  20700  13099  -4217   3606  -2924       C  
ATOM   2581  C   LYS I 579     -12.059 -32.814  95.211  1.00130.97           C  
ANISOU 2581  C   LYS I 579    15574  20981  13208  -4364   3701  -3284       C  
ATOM   2582  O   LYS I 579     -11.495 -31.880  94.625  1.00130.29           O  
ANISOU 2582  O   LYS I 579    15392  20948  13164  -4208   3686  -3527       O  
ATOM   2583  CB  LYS I 579     -10.881 -34.986  94.832  1.00132.78           C  
ANISOU 2583  CB  LYS I 579    16098  20632  13722  -4241   3601  -2711       C  
ATOM   2584  CG  LYS I 579     -10.910 -35.794  96.125  1.00133.70           C  
ANISOU 2584  CG  LYS I 579    16338  20565  13896  -4574   3630  -2457       C  
ATOM   2585  CD  LYS I 579     -11.983 -36.875  96.087  1.00127.21           C  
ANISOU 2585  CD  LYS I 579    15607  19837  12891  -4652   3555  -2140       C  
ATOM   2586  CE  LYS I 579     -12.132 -37.553  97.441  1.00121.23           C  
ANISOU 2586  CE  LYS I 579    14969  18967  12128  -5045   3582  -1898       C  
ATOM   2587  NZ  LYS I 579     -13.298 -38.477  97.478  1.00115.21           N  
ANISOU 2587  NZ  LYS I 579    14294  18367  11112  -5183   3525  -1637       N  
ATOM   2588  N   PRO I 580     -12.641 -32.641  96.401  1.00131.40           N  
ANISOU 2588  N   PRO I 580    15605  21132  13188  -4674   3795  -3326       N  
ATOM   2589  CA  PRO I 580     -12.579 -31.334  97.067  1.00129.23           C  
ANISOU 2589  CA  PRO I 580    15179  21004  12920  -4822   3881  -3662       C  
ATOM   2590  C   PRO I 580     -11.152 -30.931  97.407  1.00128.73           C  
ANISOU 2590  C   PRO I 580    15161  20682  13069  -4857   3909  -3771       C  
ATOM   2591  O   PRO I 580     -10.282 -31.777  97.632  1.00126.58           O  
ANISOU 2591  O   PRO I 580    15046  20076  12973  -4882   3907  -3562       O  
ATOM   2592  CB  PRO I 580     -13.416 -31.542  98.335  1.00128.33           C  
ANISOU 2592  CB  PRO I 580    15069  20989  12703  -5174   3992  -3614       C  
ATOM   2593  CG  PRO I 580     -14.348 -32.646  97.988  1.00126.84           C  
ANISOU 2593  CG  PRO I 580    14969  20866  12359  -5152   3952  -3348       C  
ATOM   2594  CD  PRO I 580     -13.579 -33.556  97.076  1.00127.69           C  
ANISOU 2594  CD  PRO I 580    15223  20713  12582  -4903   3825  -3091       C  
ATOM   2595  N   THR I 581     -10.919 -29.618  97.407  1.00127.77           N  
ANISOU 2595  N   THR I 581    14889  20710  12948  -4858   3928  -4105       N  
ATOM   2596  CA  THR I 581      -9.603 -29.084  97.728  1.00126.77           C  
ANISOU 2596  CA  THR I 581    14792  20373  13000  -4912   3966  -4272       C  
ATOM   2597  C   THR I 581      -9.221 -29.424  99.160  1.00133.07           C  
ANISOU 2597  C   THR I 581    15678  20947  13937  -5233   4064  -4187       C  
ATOM   2598  O   THR I 581     -10.010 -29.231 100.091  1.00136.19           O  
ANISOU 2598  O   THR I 581    16011  21494  14242  -5479   4128  -4202       O  
ATOM   2599  CB  THR I 581      -9.572 -27.568  97.526  1.00118.38           C  
ANISOU 2599  CB  THR I 581    13546  19558  11874  -4902   3948  -4637       C  
ATOM   2600  OG1 THR I 581     -10.723 -26.972  98.141  1.00115.35           O  
ANISOU 2600  OG1 THR I 581    12998  19455  11375  -5067   3979  -4739       O  
ATOM   2601  CG2 THR I 581      -9.521 -27.221  96.052  1.00113.44           C  
ANISOU 2601  CG2 THR I 581    12864  19077  11160  -4591   3832  -4707       C  
ATOM   2602  N   ASP I 582      -8.012 -29.954  99.322  1.00133.07           N  
ANISOU 2602  N   ASP I 582    15811  20575  14175  -5234   4080  -4094       N  
ATOM   2603  CA  ASP I 582      -7.491 -30.331 100.631  1.00138.03           C  
ANISOU 2603  CA  ASP I 582    16523  20929  14993  -5527   4151  -3984       C  
ATOM   2604  C   ASP I 582      -7.303 -29.057 101.442  1.00140.15           C  
ANISOU 2604  C   ASP I 582    16672  21312  15266  -5736   4227  -4317       C  
ATOM   2605  O   ASP I 582      -6.329 -28.323 101.258  1.00139.36           O  
ANISOU 2605  O   ASP I 582    16547  21118  15287  -5687   4244  -4573       O  
ATOM   2606  CB  ASP I 582      -6.187 -31.104 100.474  1.00141.45           C  
ANISOU 2606  CB  ASP I 582    17089  20913  15742  -5440   4144  -3842       C  
ATOM   2607  CG  ASP I 582      -5.867 -31.970 101.679  1.00146.47           C  
ANISOU 2607  CG  ASP I 582    17834  21224  16595  -5714   4165  -3559       C  
ATOM   2608  OD1 ASP I 582      -6.346 -31.665 102.790  1.00149.07           O  
ANISOU 2608  OD1 ASP I 582    18132  21660  16848  -6014   4216  -3572       O  
ATOM   2609  OD2 ASP I 582      -5.134 -32.968 101.511  1.00148.36           O  
ANISOU 2609  OD2 ASP I 582    18178  21093  17099  -5636   4124  -3310       O  
ATOM   2610  N   GLU I 583      -8.260 -28.778 102.332  1.00137.81           N  
ANISOU 2610  N   GLU I 583    16297  21234  14832  -5983   4279  -4327       N  
ATOM   2611  CA  GLU I 583      -8.208 -27.568 103.145  1.00132.74           C  
ANISOU 2611  CA  GLU I 583    15517  20722  14197  -6195   4348  -4628       C  
ATOM   2612  C   GLU I 583      -7.070 -27.602 104.155  1.00138.13           C  
ANISOU 2612  C   GLU I 583    16282  21058  15142  -6416   4406  -4637       C  
ATOM   2613  O   GLU I 583      -6.643 -26.541 104.627  1.00140.02           O  
ANISOU 2613  O   GLU I 583    16426  21336  15441  -6542   4445  -4926       O  
ATOM   2614  CB  GLU I 583      -9.548 -27.366 103.849  1.00124.67           C  
ANISOU 2614  CB  GLU I 583    14381  20003  12986  -6408   4413  -4624       C  
ATOM   2615  CG  GLU I 583     -10.732 -27.403 102.898  1.00120.85           C  
ANISOU 2615  CG  GLU I 583    13804  19833  12281  -6201   4365  -4615       C  
ATOM   2616  CD  GLU I 583     -11.952 -26.703 103.454  1.00124.95           C  
ANISOU 2616  CD  GLU I 583    14126  20689  12662  -6377   4450  -4780       C  
ATOM   2617  OE1 GLU I 583     -11.797 -25.905 104.402  1.00128.21           O  
ANISOU 2617  OE1 GLU I 583    14437  21131  13145  -6614   4526  -4963       O  
ATOM   2618  OE2 GLU I 583     -13.065 -26.950 102.943  1.00123.99           O  
ANISOU 2618  OE2 GLU I 583    13938  20792  12379  -6280   4447  -4735       O  
ATOM   2619  N   LYS I 584      -6.548 -28.796 104.466  1.00143.49           N  
ANISOU 2619  N   LYS I 584    17129  21386  16005  -6464   4399  -4321       N  
ATOM   2620  CA  LYS I 584      -5.345 -28.922 105.283  1.00148.32           C  
ANISOU 2620  CA  LYS I 584    17816  21601  16939  -6630   4439  -4312       C  
ATOM   2621  C   LYS I 584      -4.137 -28.244 104.650  1.00152.40           C  
ANISOU 2621  C   LYS I 584    18316  21963  17624  -6452   4448  -4623       C  
ATOM   2622  O   LYS I 584      -3.178 -27.922 105.359  1.00153.36           O  
ANISOU 2622  O   LYS I 584    18450  21827  17991  -6612   4503  -4758       O  
ATOM   2623  CB  LYS I 584      -5.026 -30.400 105.528  1.00147.12           C  
ANISOU 2623  CB  LYS I 584    17827  21082  16989  -6668   4393  -3879       C  
ATOM   2624  CG  LYS I 584      -6.177 -31.220 106.085  1.00144.70           C  
ANISOU 2624  CG  LYS I 584    17573  20924  16484  -6867   4372  -3535       C  
ATOM   2625  CD  LYS I 584      -5.745 -32.659 106.329  1.00142.37           C  
ANISOU 2625  CD  LYS I 584    17438  20240  16416  -6927   4289  -3079       C  
ATOM   2626  CE  LYS I 584      -5.347 -32.884 107.778  1.00143.26           C  
ANISOU 2626  CE  LYS I 584    17594  20103  16734  -7309   4314  -2914       C  
ATOM   2627  NZ  LYS I 584      -6.502 -32.711 108.698  1.00139.80           N  
ANISOU 2627  NZ  LYS I 584    17129  20000  15990  -7640   4375  -2860       N  
ATOM   2628  N   LEU I 585      -4.162 -28.013 103.337  1.00149.23           N  
ANISOU 2628  N   LEU I 585    17890  21721  17092  -6145   4399  -4745       N  
ATOM   2629  CA  LEU I 585      -3.099 -27.287 102.658  1.00148.35           C  
ANISOU 2629  CA  LEU I 585    17763  21535  17069  -6000   4417  -5068       C  
ATOM   2630  C   LEU I 585      -3.173 -25.781 102.877  1.00148.08           C  
ANISOU 2630  C   LEU I 585    17588  21788  16886  -6122   4427  -5452       C  
ATOM   2631  O   LEU I 585      -2.328 -25.056 102.341  1.00148.88           O  
ANISOU 2631  O   LEU I 585    17679  21879  17010  -6047   4435  -5746       O  
ATOM   2632  CB  LEU I 585      -3.120 -27.610 101.159  1.00142.13           C  
ANISOU 2632  CB  LEU I 585    17001  20829  16173  -5650   4356  -5033       C  
ATOM   2633  CG  LEU I 585      -3.042 -29.087 100.756  1.00137.58           C  
ANISOU 2633  CG  LEU I 585    16548  19978  15746  -5493   4326  -4653       C  
ATOM   2634  CD1 LEU I 585      -2.673 -29.231  99.297  1.00134.46           C  
ANISOU 2634  CD1 LEU I 585    16172  19600  15317  -5160   4296  -4705       C  
ATOM   2635  CD2 LEU I 585      -2.026 -29.840 101.607  1.00139.93           C  
ANISOU 2635  CD2 LEU I 585    16943  19778  16447  -5638   4384  -4509       C  
ATOM   2636  N   ARG I 586      -4.152 -25.286 103.645  1.00147.23           N  
ANISOU 2636  N   ARG I 586    17367  21941  16632  -6322   4427  -5461       N  
ATOM   2637  CA  ARG I 586      -4.094 -23.895 104.081  1.00144.34           C  
ANISOU 2637  CA  ARG I 586    16860  21777  16208  -6488   4434  -5803       C  
ATOM   2638  C   ARG I 586      -3.092 -23.706 105.215  1.00149.15           C  
ANISOU 2638  C   ARG I 586    17515  22077  17080  -6754   4517  -5912       C  
ATOM   2639  O   ARG I 586      -2.567 -22.601 105.392  1.00153.34           O  
ANISOU 2639  O   ARG I 586    17970  22670  17621  -6860   4519  -6237       O  
ATOM   2640  CB  ARG I 586      -5.478 -23.407 104.514  1.00135.98           C  
ANISOU 2640  CB  ARG I 586    15632  21085  14948  -6610   4422  -5795       C  
ATOM   2641  CG  ARG I 586      -6.541 -23.516 103.438  1.00127.42           C  
ANISOU 2641  CG  ARG I 586    14474  20307  13634  -6360   4341  -5713       C  
ATOM   2642  CD  ARG I 586      -6.411 -22.425 102.388  1.00122.70           C  
ANISOU 2642  CD  ARG I 586    13759  19949  12914  -6182   4233  -5981       C  
ATOM   2643  NE  ARG I 586      -7.446 -22.540 101.365  1.00118.54           N  
ANISOU 2643  NE  ARG I 586    13147  19693  12200  -5945   4144  -5885       N  
ATOM   2644  CZ  ARG I 586      -8.702 -22.124 101.508  1.00118.98           C  
ANISOU 2644  CZ  ARG I 586    13014  20044  12147  -5985   4126  -5899       C  
ATOM   2645  NH1 ARG I 586      -9.093 -21.534 102.629  1.00121.49           N  
ANISOU 2645  NH1 ARG I 586    13204  20446  12512  -6256   4196  -6011       N  
ATOM   2646  NH2 ARG I 586      -9.567 -22.285 100.516  1.00114.72           N  
ANISOU 2646  NH2 ARG I 586    12402  19710  11475  -5754   4042  -5814       N  
ATOM   2647  N   GLU I 587      -2.815 -24.768 105.979  1.00148.02           N  
ANISOU 2647  N   GLU I 587    17491  21593  17156  -6874   4570  -5635       N  
ATOM   2648  CA  GLU I 587      -1.857 -24.741 107.088  1.00145.25           C  
ANISOU 2648  CA  GLU I 587    17186  20893  17109  -7128   4640  -5688       C  
ATOM   2649  C   GLU I 587      -0.436 -25.075 106.653  1.00142.69           C  
ANISOU 2649  C   GLU I 587    16973  20163  17079  -7001   4675  -5782       C  
ATOM   2650  O   GLU I 587       0.293 -25.755 107.382  1.00143.61           O  
ANISOU 2650  O   GLU I 587    17170  19861  17533  -7127   4719  -5638       O  
ATOM   2651  CB  GLU I 587      -2.306 -25.710 108.179  1.00144.04           C  
ANISOU 2651  CB  GLU I 587    17092  20576  17062  -7355   4663  -5312       C  
ATOM   2652  CG  GLU I 587      -3.612 -25.375 108.866  1.00141.02           C  
ANISOU 2652  CG  GLU I 587    16599  20554  16429  -7561   4680  -5255       C  
ATOM   2653  CD  GLU I 587      -4.160 -26.557 109.645  1.00141.23           C  
ANISOU 2653  CD  GLU I 587    16720  20464  16478  -7749   4693  -4829       C  
ATOM   2654  OE1 GLU I 587      -3.362 -27.257 110.304  1.00143.11           O  
ANISOU 2654  OE1 GLU I 587    17066  20297  17010  -7887   4694  -4630       O  
ATOM   2655  OE2 GLU I 587      -5.386 -26.787 109.599  1.00139.28           O  
ANISOU 2655  OE2 GLU I 587    16435  20524  15961  -7774   4697  -4692       O  
ATOM   2656  N   LEU I 588      -0.020 -24.619 105.480  1.00137.29           N  
ANISOU 2656  N   LEU I 588    16286  19587  16291  -6763   4659  -6021       N  
ATOM   2657  CA  LEU I 588       1.275 -24.969 104.915  1.00136.63           C  
ANISOU 2657  CA  LEU I 588    16300  19146  16466  -6621   4722  -6138       C  
ATOM   2658  C   LEU I 588       2.297 -23.865 105.152  1.00129.51           C  
ANISOU 2658  C   LEU I 588    15372  18185  15650  -6765   4789  -6583       C  
ATOM   2659  O   LEU I 588       1.961 -22.676 105.163  1.00129.44           O  
ANISOU 2659  O   LEU I 588    15266  18527  15388  -6863   4746  -6840       O  
ATOM   2660  CB  LEU I 588       1.134 -25.291 103.426  1.00128.74           C  
ANISOU 2660  CB  LEU I 588    15330  18289  15296  -6280   4681  -6103       C  
ATOM   2661  CG  LEU I 588       1.128 -26.781 103.065  1.00122.90           C  
ANISOU 2661  CG  LEU I 588    14687  17264  14744  -6097   4670  -5712       C  
ATOM   2662  CD1 LEU I 588       2.566 -27.259 103.082  1.00125.47           C  
ANISOU 2662  CD1 LEU I 588    15087  17084  15503  -6068   4778  -5799       C  
ATOM   2663  CD2 LEU I 588       0.313 -27.621 104.046  1.00123.04           C  
ANISOU 2663  CD2 LEU I 588    14724  17215  14812  -6264   4622  -5304       C  
ATOM   2664  N   LYS I 589       3.553 -24.279 105.338  1.00132.06           N  
ANISOU 2664  N   LYS I 589    15776  18047  16352  -6784   4892  -6673       N  
ATOM   2665  CA  LYS I 589       4.570 -23.394 105.897  1.00135.37           C  
ANISOU 2665  CA  LYS I 589    16184  18318  16933  -6993   4976  -7067       C  
ATOM   2666  C   LYS I 589       5.085 -22.393 104.870  1.00135.19           C  
ANISOU 2666  C   LYS I 589    16157  18537  16673  -6902   4996  -7494       C  
ATOM   2667  O   LYS I 589       5.373 -21.240 105.214  1.00136.97           O  
ANISOU 2667  O   LYS I 589    16334  18914  16793  -7104   4995  -7832       O  
ATOM   2668  CB  LYS I 589       5.723 -24.229 106.453  1.00138.44           C  
ANISOU 2668  CB  LYS I 589    16646  18099  17855  -7046   5088  -7020       C  
ATOM   2669  CG  LYS I 589       5.290 -25.549 107.089  1.00138.29           C  
ANISOU 2669  CG  LYS I 589    16659  17802  18084  -7060   5040  -6503       C  
ATOM   2670  CD  LYS I 589       6.325 -26.089 108.076  1.00142.22           C  
ANISOU 2670  CD  LYS I 589    17182  17713  19141  -7233   5113  -6454       C  
ATOM   2671  CE  LYS I 589       6.929 -24.995 108.948  1.00145.32           C  
ANISOU 2671  CE  LYS I 589    17531  18065  19620  -7515   5177  -6834       C  
ATOM   2672  NZ  LYS I 589       7.178 -25.463 110.339  1.00148.42           N  
ANISOU 2672  NZ  LYS I 589    17916  18067  20411  -7785   5171  -6607       N  
ATOM   2673  N   GLY I 590       5.211 -22.804 103.611  1.00145.77           N  
ANISOU 2673  N   GLY I 590    17546  19923  17916  -6622   5007  -7477       N  
ATOM   2674  CA  GLY I 590       5.878 -21.953 102.647  1.00151.24           C  
ANISOU 2674  CA  GLY I 590    18258  20795  18412  -6567   5048  -7881       C  
ATOM   2675  C   GLY I 590       5.185 -21.724 101.319  1.00156.34           C  
ANISOU 2675  C   GLY I 590    18882  21872  18649  -6335   4943  -7840       C  
ATOM   2676  O   GLY I 590       5.857 -21.406 100.333  1.00158.77           O  
ANISOU 2676  O   GLY I 590    19237  22247  18841  -6241   4999  -8096       O  
ATOM   2677  N   ALA I 591       3.861 -21.860 101.266  1.00160.51           N  
ANISOU 2677  N   ALA I 591    19336  22696  18956  -6256   4799  -7535       N  
ATOM   2678  CA  ALA I 591       3.141 -21.603 100.025  1.00160.62           C  
ANISOU 2678  CA  ALA I 591    19308  23115  18604  -6042   4681  -7486       C  
ATOM   2679  C   ALA I 591       1.691 -21.261 100.328  1.00158.78           C  
ANISOU 2679  C   ALA I 591    18944  23245  18140  -6075   4526  -7287       C  
ATOM   2680  O   ALA I 591       1.214 -21.399 101.457  1.00162.05           O  
ANISOU 2680  O   ALA I 591    19314  23588  18671  -6246   4530  -7151       O  
ATOM   2681  CB  ALA I 591       3.209 -22.797  99.071  1.00159.16           C  
ANISOU 2681  CB  ALA I 591    19204  22765  18504  -5739   4719  -7245       C  
ATOM   2682  N   LYS I 592       0.996 -20.816  99.285  1.00152.78           N  
ANISOU 2682  N   LYS I 592    13649  26114  18286  -1330  -1652  -1320       N  
ATOM   2683  CA  LYS I 592      -0.432 -20.547  99.322  1.00147.27           C  
ANISOU 2683  CA  LYS I 592    12953  25531  17474  -1266  -1590  -1306       C  
ATOM   2684  C   LYS I 592      -1.070 -21.231  98.121  1.00147.65           C  
ANISOU 2684  C   LYS I 592    13064  25477  17558  -1102  -1673  -1230       C  
ATOM   2685  O   LYS I 592      -0.406 -21.476  97.110  1.00148.83           O  
ANISOU 2685  O   LYS I 592    13190  25550  17809  -1018  -1755  -1211       O  
ATOM   2686  CB  LYS I 592      -0.709 -19.037  99.313  1.00130.32           C  
ANISOU 2686  CB  LYS I 592    10593  23661  15263  -1229  -1488  -1390       C  
ATOM   2687  CG  LYS I 592      -0.895 -18.444 100.703  1.00122.48           C  
ANISOU 2687  CG  LYS I 592     9571  22795  14171  -1383  -1374  -1456       C  
ATOM   2688  CD  LYS I 592       0.117 -17.335 100.969  1.00118.63           C  
ANISOU 2688  CD  LYS I 592     8912  22458  13704  -1446  -1324  -1540       C  
ATOM   2689  CE  LYS I 592       0.132 -16.930 102.436  1.00117.16           C  
ANISOU 2689  CE  LYS I 592     8723  22360  13430  -1627  -1220  -1601       C  
ATOM   2690  NZ  LYS I 592       0.668 -15.555 102.634  1.00117.53           N  
ANISOU 2690  NZ  LYS I 592     8566  22626  13466  -1654  -1145  -1694       N  
ATOM   2691  N   LEU I 593      -2.356 -21.556  98.247  1.00147.67           N  
ANISOU 2691  N   LEU I 593    13150  25482  17477  -1064  -1649  -1193       N  
ATOM   2692  CA  LEU I 593      -3.041 -22.336  97.221  1.00148.36           C  
ANISOU 2692  CA  LEU I 593    13325  25454  17592   -921  -1730  -1114       C  
ATOM   2693  C   LEU I 593      -3.169 -21.541  95.928  1.00147.60           C  
ANISOU 2693  C   LEU I 593    13070  25485  17526   -748  -1749  -1127       C  
ATOM   2694  O   LEU I 593      -3.373 -20.325  95.946  1.00147.44           O  
ANISOU 2694  O   LEU I 593    12882  25677  17461   -721  -1678  -1194       O  
ATOM   2695  CB  LEU I 593      -4.425 -22.767  97.710  1.00146.33           C  
ANISOU 2695  CB  LEU I 593    13181  25189  17230   -929  -1688  -1085       C  
ATOM   2696  CG  LEU I 593      -4.588 -24.195  98.242  1.00143.20           C  
ANISOU 2696  CG  LEU I 593    13024  24560  16825  -1024  -1747  -1005       C  
ATOM   2697  CD1 LEU I 593      -4.658 -25.197  97.097  1.00140.99           C  
ANISOU 2697  CD1 LEU I 593    12845  24095  16630   -894  -1871   -915       C  
ATOM   2698  CD2 LEU I 593      -3.458 -24.551  99.186  1.00143.26           C  
ANISOU 2698  CD2 LEU I 593    13102  24458  16870  -1202  -1769  -1010       C  
ATOM   2699  N   VAL I 594      -3.034 -22.239  94.795  1.00147.57           N  
ANISOU 2699  N   VAL I 594    13122  25348  17600   -638  -1852  -1063       N  
ATOM   2700  CA  VAL I 594      -3.091 -21.548  93.513  1.00142.12           C  
ANISOU 2700  CA  VAL I 594    12298  24766  16936   -490  -1883  -1067       C  
ATOM   2701  C   VAL I 594      -4.512 -21.089  93.219  1.00142.34           C  
ANISOU 2701  C   VAL I 594    12288  24911  16884   -375  -1853  -1057       C  
ATOM   2702  O   VAL I 594      -4.708 -20.030  92.617  1.00139.92           O  
ANISOU 2702  O   VAL I 594    11826  24773  16566   -289  -1842  -1090       O  
ATOM   2703  CB  VAL I 594      -2.532 -22.425  92.374  1.00133.94           C  
ANISOU 2703  CB  VAL I 594    11330  23560  16002   -414  -1999  -1008       C  
ATOM   2704  CG1 VAL I 594      -1.046 -22.678  92.573  1.00132.38           C  
ANISOU 2704  CG1 VAL I 594    11124  23273  15902   -518  -2026  -1045       C  
ATOM   2705  CG2 VAL I 594      -3.297 -23.731  92.241  1.00130.83           C  
ANISOU 2705  CG2 VAL I 594    11128  22970  15611   -372  -2061   -919       C  
ATOM   2706  N   ILE I 595      -5.520 -21.842  93.668  1.00139.94           N  
ANISOU 2706  N   ILE I 595    12122  24521  16528   -379  -1841  -1018       N  
ATOM   2707  CA  ILE I 595      -6.905 -21.494  93.369  1.00143.82           C  
ANISOU 2707  CA  ILE I 595    12582  25108  16957   -265  -1814  -1018       C  
ATOM   2708  C   ILE I 595      -7.325 -20.255  94.153  1.00147.42           C  
ANISOU 2708  C   ILE I 595    12883  25787  17343   -305  -1702  -1117       C  
ATOM   2709  O   ILE I 595      -8.098 -19.427  93.656  1.00148.30           O  
ANISOU 2709  O   ILE I 595    12870  26038  17438   -189  -1691  -1147       O  
ATOM   2710  CB  ILE I 595      -7.820 -22.708  93.641  1.00147.55           C  
ANISOU 2710  CB  ILE I 595    13250  25420  17391   -272  -1830   -955       C  
ATOM   2711  CG1 ILE I 595      -9.301 -22.344  93.478  1.00150.29           C  
ANISOU 2711  CG1 ILE I 595    13560  25870  17674   -168  -1788   -975       C  
ATOM   2712  CG2 ILE I 595      -7.527 -23.315  95.015  1.00149.32           C  
ANISOU 2712  CG2 ILE I 595    13601  25562  17574   -463  -1780   -964       C  
ATOM   2713  CD1 ILE I 595     -10.261 -23.438  93.884  1.00150.71           C  
ANISOU 2713  CD1 ILE I 595    13798  25792  17672   -196  -1781   -930       C  
ATOM   2714  N   ASP I 596      -6.786 -20.074  95.360  1.00148.47           N  
ANISOU 2714  N   ASP I 596    13013  25957  17443   -469  -1623  -1171       N  
ATOM   2715  CA  ASP I 596      -7.064 -18.874  96.138  1.00145.15           C  
ANISOU 2715  CA  ASP I 596    12435  25753  16961   -520  -1513  -1274       C  
ATOM   2716  C   ASP I 596      -6.356 -17.640  95.591  1.00143.23           C  
ANISOU 2716  C   ASP I 596    11991  25668  16760   -471  -1522  -1320       C  
ATOM   2717  O   ASP I 596      -6.707 -16.522  95.984  1.00149.70           O  
ANISOU 2717  O   ASP I 596    12656  26681  17543   -472  -1449  -1403       O  
ATOM   2718  CB  ASP I 596      -6.667 -19.103  97.596  1.00142.05           C  
ANISOU 2718  CB  ASP I 596    12113  25346  16515   -724  -1430  -1313       C  
ATOM   2719  CG  ASP I 596      -7.537 -20.138  98.276  1.00136.62           C  
ANISOU 2719  CG  ASP I 596    11612  24542  15757   -796  -1405  -1280       C  
ATOM   2720  OD2 ASP I 596      -7.064 -20.767  99.244  1.00136.42           O  
ANISOU 2720  OD2 ASP I 596    11713  24418  15703   -966  -1388  -1268       O  
ATOM   2721  OD1 ASP I 596      -8.694 -20.323  97.841  1.00134.37           O  
ANISOU 2721  OD1 ASP I 596    11348  24262  15445   -690  -1406  -1267       O  
ATOM   2722  N   VAL I 597      -5.369 -17.813  94.710  1.00144.21           N  
ANISOU 2722  N   VAL I 597    12114  25718  16961   -435  -1609  -1275       N  
ATOM   2723  CA  VAL I 597      -4.757 -16.670  94.041  1.00137.16           C  
ANISOU 2723  CA  VAL I 597    11040  24975  16099   -386  -1628  -1312       C  
ATOM   2724  C   VAL I 597      -5.643 -16.202  92.886  1.00135.51           C  
ANISOU 2724  C   VAL I 597    10758  24835  15896   -210  -1690  -1284       C  
ATOM   2725  O   VAL I 597      -5.696 -15.006  92.575  1.00139.85           O  
ANISOU 2725  O   VAL I 597    11140  25558  16440   -162  -1687  -1328       O  
ATOM   2726  CB  VAL I 597      -3.335 -17.051  93.577  1.00131.23           C  
ANISOU 2726  CB  VAL I 597    10315  24123  15425   -435  -1688  -1289       C  
ATOM   2727  CG1 VAL I 597      -2.679 -15.935  92.785  1.00129.67           C  
ANISOU 2727  CG1 VAL I 597     9943  24075  15251   -397  -1713  -1322       C  
ATOM   2728  CG2 VAL I 597      -2.469 -17.425  94.769  1.00129.32           C  
ANISOU 2728  CG2 VAL I 597    10134  23815  15188   -610  -1635  -1323       C  
ATOM   2729  N   ILE I 598      -6.385 -17.116  92.278  1.00130.78           N  
ANISOU 2729  N   ILE I 598    10286  24101  15306   -114  -1751  -1210       N  
ATOM   2730  CA  ILE I 598      -7.258 -16.830  91.146  1.00129.65           C  
ANISOU 2730  CA  ILE I 598    10099  23992  15172     56  -1824  -1172       C  
ATOM   2731  C   ILE I 598      -8.635 -16.428  91.667  1.00132.28           C  
ANISOU 2731  C   ILE I 598    10387  24418  15455    106  -1764  -1221       C  
ATOM   2732  O   ILE I 598      -9.129 -16.998  92.644  1.00130.30           O  
ANISOU 2732  O   ILE I 598    10227  24120  15159     31  -1688  -1243       O  
ATOM   2733  CB  ILE I 598      -7.330 -18.061  90.225  1.00132.91           C  
ANISOU 2733  CB  ILE I 598    10672  24204  15623    129  -1921  -1072       C  
ATOM   2734  CG1 ILE I 598      -5.952 -18.696  90.089  1.00134.21           C  
ANISOU 2734  CG1 ILE I 598    10902  24249  15844     41  -1955  -1048       C  
ATOM   2735  CG2 ILE I 598      -7.718 -17.680  88.858  1.00134.45           C  
ANISOU 2735  CG2 ILE I 598    10810  24433  15841    280  -2018  -1026       C  
ATOM   2736  CD1 ILE I 598      -5.939 -20.000  89.323  1.00132.21           C  
ANISOU 2736  CD1 ILE I 598    10810  23786  15638     96  -2045   -959       C  
ATOM   2737  N   ARG I 599      -9.264 -15.441  91.023  1.00129.48           N  
ANISOU 2737  N   ARG I 599     9891  24196  15111    227  -1801  -1242       N  
ATOM   2738  CA  ARG I 599     -10.534 -14.883  91.492  1.00138.56           C  
ANISOU 2738  CA  ARG I 599    10960  25455  16234    283  -1745  -1313       C  
ATOM   2739  C   ARG I 599     -11.645 -15.152  90.480  1.00140.31           C  
ANISOU 2739  C   ARG I 599    11215  25618  16480    455  -1834  -1260       C  
ATOM   2740  O   ARG I 599     -11.545 -14.764  89.314  1.00138.21           O  
ANISOU 2740  O   ARG I 599    10898  25363  16254    563  -1945  -1208       O  
ATOM   2741  CB  ARG I 599     -10.403 -13.381  91.792  1.00140.57           C  
ANISOU 2741  CB  ARG I 599    10996  25923  16490    273  -1710  -1406       C  
ATOM   2742  CG  ARG I 599      -9.917 -12.490  90.644  1.00141.17           C  
ANISOU 2742  CG  ARG I 599    10952  26075  16610    357  -1821  -1372       C  
ATOM   2743  CD  ARG I 599     -10.515 -11.096  90.743  1.00144.02           C  
ANISOU 2743  CD  ARG I 599    11109  26627  16984    417  -1819  -1455       C  
ATOM   2744  NE  ARG I 599     -10.719 -10.490  89.428  1.00145.21           N  
ANISOU 2744  NE  ARG I 599    11189  26807  17179    553  -1961  -1400       N  
ATOM   2745  CZ  ARG I 599     -10.825  -9.182  89.217  1.00148.20           C  
ANISOU 2745  CZ  ARG I 599    11386  27341  17581    595  -2006  -1444       C  
ATOM   2746  NH1 ARG I 599     -11.011  -8.718  87.989  1.00149.80           N  
ANISOU 2746  NH1 ARG I 599    11548  27552  17819    709  -2151  -1380       N  
ATOM   2747  NH2 ARG I 599     -10.752  -8.337  90.237  1.00147.60           N  
ANISOU 2747  NH2 ARG I 599    11175  27411  17494    520  -1912  -1551       N  
ATOM   2748  N   TYR I 600     -12.717 -15.795  90.932  1.00140.81           N  
ANISOU 2748  N   TYR I 600    11364  25622  16515    474  -1786  -1277       N  
ATOM   2749  CA  TYR I 600     -13.793 -16.255  90.053  1.00148.00           C  
ANISOU 2749  CA  TYR I 600    12335  26450  17448    627  -1864  -1225       C  
ATOM   2750  C   TYR I 600     -15.090 -15.564  90.468  1.00160.48           C  
ANISOU 2750  C   TYR I 600    13797  28152  19027    695  -1810  -1329       C  
ATOM   2751  O   TYR I 600     -15.692 -15.919  91.485  1.00167.30           O  
ANISOU 2751  O   TYR I 600    14703  29022  19843    618  -1698  -1398       O  
ATOM   2752  CB  TYR I 600     -13.917 -17.781  90.096  1.00143.91           C  
ANISOU 2752  CB  TYR I 600    12043  25731  16906    594  -1868  -1146       C  
ATOM   2753  CG  TYR I 600     -13.534 -18.408  91.426  1.00144.73           C  
ANISOU 2753  CG  TYR I 600    12248  25792  16951    411  -1756  -1178       C  
ATOM   2754  CD1 TYR I 600     -12.217 -18.776  91.695  1.00143.68           C  
ANISOU 2754  CD1 TYR I 600    12176  25591  16824    289  -1759  -1142       C  
ATOM   2755  CD2 TYR I 600     -14.489 -18.641  92.408  1.00147.86           C  
ANISOU 2755  CD2 TYR I 600    12681  26212  17288    353  -1652  -1247       C  
ATOM   2756  CE1 TYR I 600     -11.864 -19.339  92.902  1.00145.07           C  
ANISOU 2756  CE1 TYR I 600    12451  25718  16951    118  -1674  -1164       C  
ATOM   2757  CE2 TYR I 600     -14.144 -19.208  93.621  1.00149.29           C  
ANISOU 2757  CE2 TYR I 600    12965  26353  17404    170  -1558  -1270       C  
ATOM   2758  CZ  TYR I 600     -12.829 -19.556  93.861  1.00148.01           C  
ANISOU 2758  CZ  TYR I 600    12868  26116  17253     54  -1577  -1222       C  
ATOM   2759  OH  TYR I 600     -12.476 -20.123  95.064  1.00149.24           O  
ANISOU 2759  OH  TYR I 600    13134  26221  17348   -132  -1500  -1237       O  
ATOM   2760  N   GLU I 601     -15.524 -14.577  89.672  1.00168.19           N  
ANISOU 2760  N   GLU I 601    14623  29223  20059    833  -1894  -1345       N  
ATOM   2761  CA  GLU I 601     -16.702 -13.795  90.056  1.00168.57           C  
ANISOU 2761  CA  GLU I 601    14526  29393  20129    904  -1851  -1462       C  
ATOM   2762  C   GLU I 601     -18.007 -14.586  89.963  1.00162.45           C  
ANISOU 2762  C   GLU I 601    13846  28524  19353    987  -1843  -1468       C  
ATOM   2763  O   GLU I 601     -18.804 -14.511  90.916  1.00166.55           O  
ANISOU 2763  O   GLU I 601    14325  29110  19848    945  -1726  -1585       O  
ATOM   2764  CB  GLU I 601     -16.762 -12.489  89.253  1.00168.88           C  
ANISOU 2764  CB  GLU I 601    14376  29551  20239   1024  -1961  -1475       C  
ATOM   2765  CG  GLU I 601     -17.935 -11.592  89.645  1.00165.55           C  
ANISOU 2765  CG  GLU I 601    13781  29257  19866   1105  -1930  -1610       C  
ATOM   2766  CD  GLU I 601     -18.966 -11.443  88.541  1.00161.48           C  
ANISOU 2766  CD  GLU I 601    13234  28694  19425   1300  -2068  -1579       C  
ATOM   2767  OE1 GLU I 601     -18.610 -10.950  87.451  1.00159.58           O  
ANISOU 2767  OE1 GLU I 601    12956  28449  19227   1384  -2217  -1495       O  
ATOM   2768  OE2 GLU I 601     -20.138 -11.816  88.766  1.00159.84           O  
ANISOU 2768  OE2 GLU I 601    13043  28454  19233   1363  -2027  -1642       O  
ATOM   2769  N   PRO I 602     -18.313 -15.334  88.895  1.00153.59           N  
ANISOU 2769  N   PRO I 602    12847  27259  18253   1098  -1954  -1358       N  
ATOM   2770  CA  PRO I 602     -19.507 -16.187  88.951  1.00149.99           C  
ANISOU 2770  CA  PRO I 602    12497  26708  17784   1152  -1928  -1368       C  
ATOM   2771  C   PRO I 602     -19.303 -17.340  89.918  1.00147.22           C  
ANISOU 2771  C   PRO I 602    12325  26265  17348    992  -1814  -1360       C  
ATOM   2772  O   PRO I 602     -18.301 -18.062  89.835  1.00145.04           O  
ANISOU 2772  O   PRO I 602    12181  25882  17045    909  -1838  -1262       O  
ATOM   2773  CB  PRO I 602     -19.669 -16.693  87.507  1.00139.39           C  
ANISOU 2773  CB  PRO I 602    11248  25231  16484   1297  -2086  -1237       C  
ATOM   2774  CG  PRO I 602     -18.875 -15.783  86.686  1.00137.87           C  
ANISOU 2774  CG  PRO I 602    10943  25104  16336   1343  -2196  -1191       C  
ATOM   2775  CD  PRO I 602     -17.724 -15.388  87.540  1.00144.73           C  
ANISOU 2775  CD  PRO I 602    11762  26062  17168   1184  -2109  -1229       C  
ATOM   2776  N   PRO I 603     -20.234 -17.541  90.840  1.00149.41           N  
ANISOU 2776  N   PRO I 603    12610  26577  17583    940  -1695  -1463       N  
ATOM   2777  CA  PRO I 603     -20.119 -18.630  91.812  1.00149.39           C  
ANISOU 2777  CA  PRO I 603    12786  26487  17487    770  -1592  -1454       C  
ATOM   2778  C   PRO I 603     -20.423 -19.967  91.151  1.00150.43           C  
ANISOU 2778  C   PRO I 603    13132  26418  17606    816  -1664  -1332       C  
ATOM   2779  O   PRO I 603     -20.694 -20.052  89.957  1.00147.12           O  
ANISOU 2779  O   PRO I 603    12721  25931  17247    976  -1787  -1257       O  
ATOM   2780  CB  PRO I 603     -21.181 -18.278  92.852  1.00151.02           C  
ANISOU 2780  CB  PRO I 603    12908  26817  17655    716  -1448  -1617       C  
ATOM   2781  CG  PRO I 603     -22.230 -17.574  92.065  1.00151.23           C  
ANISOU 2781  CG  PRO I 603    12788  26904  17771    915  -1512  -1676       C  
ATOM   2782  CD  PRO I 603     -21.520 -16.834  90.955  1.00150.61           C  
ANISOU 2782  CD  PRO I 603    12612  26839  17776   1040  -1661  -1594       C  
ATOM   2783  N   HIS I 604     -20.341 -21.023  91.964  1.00144.92           N  
ANISOU 2783  N   HIS I 604    12614  25623  16826    663  -1592  -1309       N  
ATOM   2784  CA  HIS I 604     -20.568 -22.433  91.631  1.00146.75           C  
ANISOU 2784  CA  HIS I 604    13074  25655  17028    658  -1641  -1198       C  
ATOM   2785  C   HIS I 604     -19.816 -22.946  90.397  1.00145.54           C  
ANISOU 2785  C   HIS I 604    13005  25356  16936    754  -1795  -1047       C  
ATOM   2786  O   HIS I 604     -20.062 -24.069  89.945  1.00144.82           O  
ANISOU 2786  O   HIS I 604    13090  25100  16837    779  -1854   -952       O  
ATOM   2787  CB  HIS I 604     -22.083 -22.727  91.533  1.00149.02           C  
ANISOU 2787  CB  HIS I 604    13386  25936  17300    739  -1610  -1253       C  
ATOM   2788  CG  HIS I 604     -22.682 -22.580  90.166  1.00150.05           C  
ANISOU 2788  CG  HIS I 604    13473  26026  17515    960  -1736  -1204       C  
ATOM   2789  ND1 HIS I 604     -22.842 -23.652  89.313  1.00148.64           N  
ANISOU 2789  ND1 HIS I 604    13467  25667  17344   1030  -1835  -1078       N  
ATOM   2790  CD2 HIS I 604     -23.275 -21.527  89.556  1.00150.82           C  
ANISOU 2790  CD2 HIS I 604    13381  26233  17690   1120  -1779  -1271       C  
ATOM   2791  CE1 HIS I 604     -23.444 -23.248  88.208  1.00148.25           C  
ANISOU 2791  CE1 HIS I 604    13339  25622  17369   1221  -1934  -1063       C  
ATOM   2792  NE2 HIS I 604     -23.716 -21.961  88.329  1.00149.77           N  
ANISOU 2792  NE2 HIS I 604    13314  25984  17608   1280  -1908  -1176       N  
ATOM   2793  N   ILE I 605     -18.860 -22.164  89.880  1.00147.41           N  
ANISOU 2793  N   ILE I 605    13122  25656  17231    793  -1857  -1027       N  
ATOM   2794  CA  ILE I 605     -17.877 -22.659  88.923  1.00142.60           C  
ANISOU 2794  CA  ILE I 605    12592  24920  16668    830  -1978   -901       C  
ATOM   2795  C   ILE I 605     -16.622 -23.180  89.611  1.00141.52           C  
ANISOU 2795  C   ILE I 605    12545  24714  16512    660  -1952   -868       C  
ATOM   2796  O   ILE I 605     -15.660 -23.557  88.925  1.00139.04           O  
ANISOU 2796  O   ILE I 605    12280  24303  16245    670  -2041   -784       O  
ATOM   2797  CB  ILE I 605     -17.531 -21.561  87.894  1.00137.69           C  
ANISOU 2797  CB  ILE I 605    11800  24401  16116    957  -2067   -896       C  
ATOM   2798  CG1 ILE I 605     -16.499 -20.579  88.468  1.00133.31           C  
ANISOU 2798  CG1 ILE I 605    11103  23985  15564    859  -2017   -958       C  
ATOM   2799  CG2 ILE I 605     -18.791 -20.852  87.419  1.00139.54           C  
ANISOU 2799  CG2 ILE I 605    11917  24723  16378   1112  -2091   -950       C  
ATOM   2800  CD1 ILE I 605     -16.233 -19.379  87.602  1.00130.46           C  
ANISOU 2800  CD1 ILE I 605    10565  23746  15258    963  -2095   -966       C  
ATOM   2801  N   LYS I 606     -16.626 -23.249  90.950  1.00141.77           N  
ANISOU 2801  N   LYS I 606    11576  27329  14962  -1903    335  -5940       N  
ATOM   2802  CA  LYS I 606     -15.464 -23.667  91.736  1.00137.20           C  
ANISOU 2802  CA  LYS I 606    11408  26623  14097  -2124    446  -5804       C  
ATOM   2803  C   LYS I 606     -14.964 -25.053  91.346  1.00127.74           C  
ANISOU 2803  C   LYS I 606    10621  25291  12623  -1977    574  -5635       C  
ATOM   2804  O   LYS I 606     -13.772 -25.344  91.486  1.00123.17           O  
ANISOU 2804  O   LYS I 606    10451  24529  11820  -2058    580  -5475       O  
ATOM   2805  CB  LYS I 606     -15.819 -23.637  93.228  1.00138.97           C  
ANISOU 2805  CB  LYS I 606    11471  27008  14322  -2438    682  -5898       C  
ATOM   2806  CG  LYS I 606     -14.655 -23.864  94.182  1.00134.89           C  
ANISOU 2806  CG  LYS I 606    11319  26371  13563  -2711    784  -5773       C  
ATOM   2807  CD  LYS I 606     -15.060 -23.571  95.618  1.00130.07           C  
ANISOU 2807  CD  LYS I 606    10474  25928  13017  -3027    973  -5872       C  
ATOM   2808  CE  LYS I 606     -14.171 -24.305  96.609  1.00125.70           C  
ANISOU 2808  CE  LYS I 606    10284  25287  12189  -3258   1174  -5738       C  
ATOM   2809  NZ  LYS I 606     -12.750 -23.868  96.518  1.00122.17           N  
ANISOU 2809  NZ  LYS I 606    10199  24598  11623  -3360    998  -5610       N  
ATOM   2810  N   LYS I 607     -15.852 -25.909  90.835  1.00122.16           N  
ANISOU 2810  N   LYS I 607     9813  24664  11937  -1758    670  -5665       N  
ATOM   2811  CA  LYS I 607     -15.433 -27.229  90.383  1.00121.35           C  
ANISOU 2811  CA  LYS I 607    10077  24432  11598  -1604    769  -5491       C  
ATOM   2812  C   LYS I 607     -14.551 -27.150  89.141  1.00120.34           C  
ANISOU 2812  C   LYS I 607    10218  24076  11429  -1375    543  -5326       C  
ATOM   2813  O   LYS I 607     -13.661 -27.990  88.966  1.00120.65           O  
ANISOU 2813  O   LYS I 607    10662  23940  11240  -1332    605  -5131       O  
ATOM   2814  CB  LYS I 607     -16.663 -28.093  90.131  1.00119.50           C  
ANISOU 2814  CB  LYS I 607     9646  24345  11414  -1433    902  -5578       C  
ATOM   2815  CG  LYS I 607     -17.111 -28.884  91.356  1.00116.80           C  
ANISOU 2815  CG  LYS I 607     9333  24081  10965  -1643   1165  -5584       C  
ATOM   2816  CD  LYS I 607     -17.932 -30.097  90.965  1.00112.44           C  
ANISOU 2816  CD  LYS I 607     8888  23369  10464  -1465   1153  -5458       C  
ATOM   2817  CE  LYS I 607     -19.112 -29.677  90.114  1.00110.17           C  
ANISOU 2817  CE  LYS I 607     8314  23123  10421  -1241    990  -5614       C  
ATOM   2818  NZ  LYS I 607     -19.913 -30.831  89.616  1.00108.07           N  
ANISOU 2818  NZ  LYS I 607     8164  22710  10187  -1062    962  -5512       N  
ATOM   2819  N   ALA I 608     -14.744 -26.134  88.294  1.00118.04           N  
ANISOU 2819  N   ALA I 608     9712  23780  11359  -1235    287  -5388       N  
ATOM   2820  CA  ALA I 608     -13.918 -25.997  87.096  1.00105.70           C  
ANISOU 2820  CA  ALA I 608     8394  22009   9756  -1015     72  -5229       C  
ATOM   2821  C   ALA I 608     -12.482 -25.627  87.451  1.00104.30           C  
ANISOU 2821  C   ALA I 608     8595  21649   9385  -1192     25  -5104       C  
ATOM   2822  O   ALA I 608     -11.526 -26.230  86.944  1.00107.38           O  
ANISOU 2822  O   ALA I 608     9383  21834   9580  -1081     28  -4911       O  
ATOM   2823  CB  ALA I 608     -14.527 -24.958  86.153  1.00 95.66           C  
ANISOU 2823  CB  ALA I 608     6777  20794   8776   -837   -192  -5326       C  
ATOM   2824  N   LEU I 609     -12.305 -24.644  88.337  1.00 98.24           N  
ANISOU 2824  N   LEU I 609     7709  20944   8672  -1469    -14  -5212       N  
ATOM   2825  CA  LEU I 609     -10.961 -24.310  88.789  1.00107.51           C  
ANISOU 2825  CA  LEU I 609     9248  21944   9658  -1666    -48  -5113       C  
ATOM   2826  C   LEU I 609     -10.400 -25.354  89.745  1.00113.77           C  
ANISOU 2826  C   LEU I 609    10354  22671  10201  -1839    227  -5013       C  
ATOM   2827  O   LEU I 609      -9.179 -25.437  89.899  1.00117.79           O  
ANISOU 2827  O   LEU I 609    11260  22980  10514  -1928    230  -4883       O  
ATOM   2828  CB  LEU I 609     -10.947 -22.923  89.437  1.00108.50           C  
ANISOU 2828  CB  LEU I 609     9143  22149   9932  -1919   -196  -5252       C  
ATOM   2829  CG  LEU I 609     -11.061 -21.734  88.473  1.00107.42           C  
ANISOU 2829  CG  LEU I 609     8807  22010   9995  -1784   -520  -5299       C  
ATOM   2830  CD1 LEU I 609     -10.480 -20.470  89.085  1.00102.84           C  
ANISOU 2830  CD1 LEU I 609     8206  21413   9458  -2062   -690  -5360       C  
ATOM   2831  CD2 LEU I 609     -10.388 -22.030  87.140  1.00102.54           C  
ANISOU 2831  CD2 LEU I 609     8495  21202   9266  -1489   -655  -5135       C  
ATOM   2832  N   GLN I 610     -11.258 -26.160  90.377  1.00112.01           N  
ANISOU 2832  N   GLN I 610     9972  22609   9979  -1886    458  -5068       N  
ATOM   2833  CA  GLN I 610     -10.774 -27.303  91.145  1.00122.80           C  
ANISOU 2833  CA  GLN I 610    11644  23913  11104  -2011    718  -4943       C  
ATOM   2834  C   GLN I 610     -10.219 -28.380  90.221  1.00120.69           C  
ANISOU 2834  C   GLN I 610    11729  23455  10672  -1756    743  -4732       C  
ATOM   2835  O   GLN I 610      -9.241 -29.056  90.559  1.00121.19           O  
ANISOU 2835  O   GLN I 610    12177  23350  10520  -1834    866  -4564       O  
ATOM   2836  CB  GLN I 610     -11.901 -27.870  92.010  1.00128.60           C  
ANISOU 2836  CB  GLN I 610    12104  24884  11875  -2119    951  -5057       C  
ATOM   2837  CG  GLN I 610     -11.996 -27.254  93.396  1.00135.90           C  
ANISOU 2837  CG  GLN I 610    12860  25936  12840  -2468   1054  -5173       C  
ATOM   2838  CD  GLN I 610     -13.300 -27.584  94.104  1.00140.90           C  
ANISOU 2838  CD  GLN I 610    13139  26835  13561  -2538   1258  -5322       C  
ATOM   2839  OE1 GLN I 610     -14.366 -27.600  93.490  1.00140.53           O  
ANISOU 2839  OE1 GLN I 610    12804  26921  13671  -2340   1224  -5436       O  
ATOM   2840  NE2 GLN I 610     -13.218 -27.839  95.404  1.00143.60           N  
ANISOU 2840  NE2 GLN I 610    13504  27254  13804  -2822   1476  -5322       N  
ATOM   2841  N   TYR I 611     -10.843 -28.558  89.058  1.00125.41           N  
ANISOU 2841  N   TYR I 611    12190  24074  11387  -1450    628  -4731       N  
ATOM   2842  CA  TYR I 611     -10.329 -29.490  88.062  1.00114.67           C  
ANISOU 2842  CA  TYR I 611    11136  22454   9979  -1180    612  -4470       C  
ATOM   2843  C   TYR I 611      -9.031 -28.977  87.453  1.00106.37           C  
ANISOU 2843  C   TYR I 611    10413  21173   8829  -1121    461  -4344       C  
ATOM   2844  O   TYR I 611      -8.077 -29.742  87.270  1.00112.12           O  
ANISOU 2844  O   TYR I 611    11537  21611   9451  -1058    536  -4084       O  
ATOM   2845  CB  TYR I 611     -11.389 -29.712  86.981  1.00110.82           C  
ANISOU 2845  CB  TYR I 611    10380  22040   9685   -877    510  -4503       C  
ATOM   2846  CG  TYR I 611     -10.867 -30.183  85.643  1.00105.17           C  
ANISOU 2846  CG  TYR I 611     9898  21065   8996   -563    390  -4262       C  
ATOM   2847  CD1 TYR I 611     -10.225 -31.410  85.511  1.00102.79           C  
ANISOU 2847  CD1 TYR I 611     9960  20477   8617   -488    504  -3962       C  
ATOM   2848  CD2 TYR I 611     -11.012 -29.393  84.509  1.00105.11           C  
ANISOU 2848  CD2 TYR I 611     9741  21096   9099   -344    155  -4329       C  
ATOM   2849  CE1 TYR I 611      -9.748 -31.838  84.287  1.00102.35           C  
ANISOU 2849  CE1 TYR I 611    10107  20196   8587   -204    406  -3744       C  
ATOM   2850  CE2 TYR I 611     -10.536 -29.811  83.283  1.00103.70           C  
ANISOU 2850  CE2 TYR I 611     9768  20692   8943    -56     57  -4104       C  
ATOM   2851  CZ  TYR I 611      -9.906 -31.032  83.177  1.00101.52           C  
ANISOU 2851  CZ  TYR I 611     9846  20146   8582     13    190  -3816       C  
ATOM   2852  OH  TYR I 611      -9.430 -31.451  81.955  1.00 97.90           O  
ANISOU 2852  OH  TYR I 611     9579  19472   8147    297    102  -3594       O  
ATOM   2853  N   ALA I 612      -8.977 -27.681  87.135  1.00105.06           N  
ANISOU 2853  N   ALA I 612    10091  21083   8743  -1139    237  -4493       N  
ATOM   2854  CA  ALA I 612      -7.802 -27.136  86.463  1.00102.55           C  
ANISOU 2854  CA  ALA I 612    10081  20545   8337  -1065     71  -4377       C  
ATOM   2855  C   ALA I 612      -6.620 -26.991  87.417  1.00102.23           C  
ANISOU 2855  C   ALA I 612    10382  20361   8098  -1345    159  -4329       C  
ATOM   2856  O   ALA I 612      -5.467 -27.192  87.016  1.00102.65           O  
ANISOU 2856  O   ALA I 612    10841  20162   7997  -1275    152  -4155       O  
ATOM   2857  CB  ALA I 612      -8.143 -25.792  85.822  1.00 96.17           C  
ANISOU 2857  CB  ALA I 612     8994  19811   7734   -998   -215  -4504       C  
ATOM   2858  N   CYS I 613      -6.881 -26.651  88.678  1.00111.97           N  
ANISOU 2858  N   CYS I 613    11460  21728   9356  -1656    249  -4465       N  
ATOM   2859  CA  CYS I 613      -5.836 -26.381  89.659  1.00115.71           C  
ANISOU 2859  CA  CYS I 613    12210  22077   9677  -1950    312  -4443       C  
ATOM   2860  C   CYS I 613      -5.581 -27.557  90.592  1.00115.99           C  
ANISOU 2860  C   CYS I 613    12451  22075   9544  -2093    608  -4338       C  
ATOM   2861  O   CYS I 613      -4.433 -27.982  90.753  1.00115.93           O  
ANISOU 2861  O   CYS I 613    12858  21843   9346  -2143    692  -4186       O  
ATOM   2862  CB  CYS I 613      -6.203 -25.139  90.480  1.00116.39           C  
ANISOU 2862  CB  CYS I 613    11988  22319   9916  -2224    199  -4645       C  
ATOM   2863  SG  CYS I 613      -6.466 -23.644  89.504  1.00115.60           S  
ANISOU 2863  SG  CYS I 613    11630  22267  10024  -2102   -169  -4762       S  
ATOM   2864  N   GLY I 614      -6.628 -28.086  91.220  1.00114.21           N  
ANISOU 2864  N   GLY I 614    11944  22064   9386  -2161    770  -4414       N  
ATOM   2865  CA  GLY I 614      -6.441 -29.181  92.156  1.00113.99           C  
ANISOU 2865  CA  GLY I 614    12090  22022   9198  -2313   1047  -4311       C  
ATOM   2866  C   GLY I 614      -5.827 -28.699  93.455  1.00116.21           C  
ANISOU 2866  C   GLY I 614    12454  22278   9421  -2677   1119  -4353       C  
ATOM   2867  O   GLY I 614      -6.162 -27.628  93.975  1.00120.14           O  
ANISOU 2867  O   GLY I 614    12686  22902  10060  -2860   1016  -4524       O  
ATOM   2868  N   ASN I 615      -4.914 -29.505  93.992  1.00117.47           N  
ANISOU 2868  N   ASN I 615    12980  22265   9387  -2784   1297  -4184       N  
ATOM   2869  CA  ASN I 615      -4.175 -29.174  95.207  1.00117.56           C  
ANISOU 2869  CA  ASN I 615    13131  22206   9329  -3124   1377  -4190       C  
ATOM   2870  C   ASN I 615      -2.789 -28.628  94.891  1.00119.04           C  
ANISOU 2870  C   ASN I 615    13701  22107   9421  -3143   1244  -4120       C  
ATOM   2871  O   ASN I 615      -1.804 -28.987  95.543  1.00118.86           O  
ANISOU 2871  O   ASN I 615    14005  21899   9255  -3310   1370  -4008       O  
ATOM   2872  CB  ASN I 615      -4.078 -30.396  96.116  1.00118.37           C  
ANISOU 2872  CB  ASN I 615    13378  22307   9291  -3259   1670  -4053       C  
ATOM   2873  CG  ASN I 615      -5.427 -31.045  96.363  1.00119.72           C  
ANISOU 2873  CG  ASN I 615    13212  22712   9564  -3210   1797  -4088       C  
ATOM   2874  OD1 ASN I 615      -6.469 -30.484  96.027  1.00119.64           O  
ANISOU 2874  OD1 ASN I 615    12833  22948   9676  -3136   1706  -4285       O  
ATOM   2875  ND2 ASN I 615      -5.412 -32.230  96.960  1.00121.05           N  
ANISOU 2875  ND2 ASN I 615    13510  22767   9717  -3243   1990  -3882       N  
ATOM   2876  N   ALA I 616      -2.688 -27.758  93.892  1.00117.55           N  
ANISOU 2876  N   ALA I 616    13484  21874   9304  -2974    992  -4184       N  
ATOM   2877  CA  ALA I 616      -1.409 -27.180  93.504  1.00117.97           C  
ANISOU 2877  CA  ALA I 616    13906  21664   9253  -2976    852  -4133       C  
ATOM   2878  C   ALA I 616      -1.113 -25.935  94.336  1.00120.85           C  
ANISOU 2878  C   ALA I 616    14192  22047   9680  -3292    714  -4289       C  
ATOM   2879  O   ALA I 616      -2.022 -25.250  94.807  1.00125.28           O  
ANISOU 2879  O   ALA I 616    14343  22839  10419  -3426    642  -4453       O  
ATOM   2880  CB  ALA I 616      -1.399 -26.841  92.011  1.00111.33           C  
ANISOU 2880  CB  ALA I 616    13092  20765   8444  -2644    643  -4112       C  
ATOM   2881  N   LEU I 617       0.180 -25.667  94.534  1.00124.41           N  
ANISOU 2881  N   LEU I 617    15041  22242   9988  -3414    682  -4234       N  
ATOM   2882  CA  LEU I 617       0.647 -24.576  95.376  1.00133.65           C  
ANISOU 2882  CA  LEU I 617    16209  23381  11191  -3736    554  -4359       C  
ATOM   2883  C   LEU I 617       1.681 -23.759  94.609  1.00141.83           C  
ANISOU 2883  C   LEU I 617    17563  24195  12132  -3668    322  -4366       C  
ATOM   2884  O   LEU I 617       2.443 -24.296  93.792  1.00144.33           O  
ANISOU 2884  O   LEU I 617    18248  24300  12292  -3445    362  -4227       O  
ATOM   2885  CB  LEU I 617       1.259 -25.111  96.692  1.00133.48           C  
ANISOU 2885  CB  LEU I 617    16384  23257  11076  -4032    780  -4294       C  
ATOM   2886  CG  LEU I 617       0.387 -25.502  97.904  1.00135.67           C  
ANISOU 2886  CG  LEU I 617    16335  23761  11452  -4255    976  -4330       C  
ATOM   2887  CD1 LEU I 617      -0.554 -26.667  97.631  1.00132.35           C  
ANISOU 2887  CD1 LEU I 617    15748  23504  11035  -4047   1175  -4250       C  
ATOM   2888  CD2 LEU I 617       1.254 -25.846  99.101  1.00139.42           C  
ANISOU 2888  CD2 LEU I 617    17069  24078  11826  -4551   1149  -4252       C  
ATOM   2889  N   VAL I 618       1.709 -22.453  94.897  1.00147.83           N  
ANISOU 2889  N   VAL I 618    18178  25004  12986  -3868     82  -4522       N  
ATOM   2890  CA  VAL I 618       2.619 -21.501  94.257  1.00150.43           C  
ANISOU 2890  CA  VAL I 618    18776  25152  13227  -3848   -175  -4558       C  
ATOM   2891  C   VAL I 618       3.582 -20.945  95.320  1.00155.78           C  
ANISOU 2891  C   VAL I 618    19691  25666  13831  -4209   -206  -4611       C  
ATOM   2892  O   VAL I 618       3.152 -20.574  96.418  1.00159.24           O  
ANISOU 2892  O   VAL I 618    19861  26238  14404  -4501   -196  -4704       O  
ATOM   2893  CB  VAL I 618       1.839 -20.377  93.536  1.00151.67           C  
ANISOU 2893  CB  VAL I 618    18567  25498  13562  -3756   -479  -4688       C  
ATOM   2894  CG1 VAL I 618       0.727 -19.808  94.424  1.00150.28           C  
ANISOU 2894  CG1 VAL I 618    17864  25599  13636  -3981   -517  -4832       C  
ATOM   2895  CG2 VAL I 618       2.776 -19.279  93.041  1.00155.98           C  
ANISOU 2895  CG2 VAL I 618    19379  25877  14011  -3795   -764  -4736       C  
ATOM   2896  N   CYS I 619       4.882 -20.917  95.003  1.00155.02           N  
ANISOU 2896  N   CYS I 619    20100  25275  13526  -4188   -233  -4550       N  
ATOM   2897  CA  CYS I 619       5.963 -20.641  95.945  1.00154.32           C  
ANISOU 2897  CA  CYS I 619    20335  24969  13331  -4498   -217  -4574       C  
ATOM   2898  C   CYS I 619       6.755 -19.394  95.560  1.00152.55           C  
ANISOU 2898  C   CYS I 619    20331  24604  13028  -4578   -528  -4680       C  
ATOM   2899  O   CYS I 619       6.508 -18.783  94.537  1.00149.71           O  
ANISOU 2899  O   CYS I 619    19889  24311  12683  -4384   -747  -4718       O  
ATOM   2900  CB  CYS I 619       6.871 -21.857  96.078  1.00153.11           C  
ANISOU 2900  CB  CYS I 619    20625  24561  12989  -4430     77  -4401       C  
ATOM   2901  SG  CYS I 619       6.287 -23.111  97.237  1.00155.13           S  
ANISOU 2901  SG  CYS I 619    20694  24931  13319  -4562    433  -4298       S  
ATOM   2902  N   ASP I 620       7.728 -19.023  96.398  1.00155.44           N  
ANISOU 2902  N   ASP I 620    20987  24768  13305  -4873   -550  -4725       N  
ATOM   2903  CA  ASP I 620       8.453 -17.762  96.270  1.00161.20           C  
ANISOU 2903  CA  ASP I 620    21908  25375  13967  -5026   -862  -4849       C  
ATOM   2904  C   ASP I 620       9.717 -17.935  95.429  1.00165.92           C  
ANISOU 2904  C   ASP I 620    23091  25661  14289  -4843   -854  -4782       C  
ATOM   2905  O   ASP I 620      10.185 -16.966  94.787  1.00167.25           O  
ANISOU 2905  O   ASP I 620    23425  25758  14363  -4823  -1129  -4864       O  
ATOM   2906  CB  ASP I 620       8.815 -17.211  97.664  1.00164.47           C  
ANISOU 2906  CB  ASP I 620    22314  25732  14446  -5464   -908  -4944       C  
ATOM   2907  CG  ASP I 620       7.595 -16.802  98.518  1.00166.47           C  
ANISOU 2907  CG  ASP I 620    21970  26294  14986  -5675   -955  -5025       C  
ATOM   2908  OD1 ASP I 620       6.559 -16.415  97.941  1.00166.04           O  
ANISOU 2908  OD1 ASP I 620    21511  26491  15087  -5529  -1086  -5068       O  
ATOM   2909  OD2 ASP I 620       7.677 -16.849  99.777  1.00168.85           O  
ANISOU 2909  OD2 ASP I 620    22205  26583  15368  -5989   -857  -5042       O  
ATOM   2910  N   ASN I 621      10.284 -19.162  95.440  1.00163.52           N  
ANISOU 2910  N   ASN I 621    23107  25169  13855  -4712   -537  -4628       N  
ATOM   2911  CA  ASN I 621      11.445 -19.442  94.604  1.00166.24           C  
ANISOU 2911  CA  ASN I 621    23998  25216  13951  -4503   -484  -4545       C  
ATOM   2912  C   ASN I 621      11.444 -20.919  94.236  1.00162.19           C  
ANISOU 2912  C   ASN I 621    23603  24632  13391  -4226   -144  -4336       C  
ATOM   2913  O   ASN I 621      10.515 -21.655  94.571  1.00161.73           O  
ANISOU 2913  O   ASN I 621    23203  24769  13479  -4195     17  -4270       O  
ATOM   2914  CB  ASN I 621      12.762 -18.994  95.276  1.00170.73           C  
ANISOU 2914  CB  ASN I 621    25026  25481  14362  -4777   -519  -4618       C  
ATOM   2915  CG  ASN I 621      13.001 -19.683  96.613  1.00173.12           C  
ANISOU 2915  CG  ASN I 621    25366  25692  14718  -5041   -271  -4574       C  
ATOM   2916  OD1 ASN I 621      13.248 -20.911  96.675  1.00170.42           O  
ANISOU 2916  OD1 ASN I 621    25191  25233  14327  -4909     45  -4406       O  
ATOM   2917  ND2 ASN I 621      12.964 -18.924  97.669  1.00177.64           N  
ANISOU 2917  ND2 ASN I 621    25794  26307  15394  -5410   -411  -4706       N  
ATOM   2918  N   VAL I 622      12.503 -21.346  93.548  1.00164.91           N  
ANISOU 2918  N   VAL I 622    24440  24691  13528  -4027    -36  -4230       N  
ATOM   2919  CA  VAL I 622      12.582 -22.725  93.101  1.00160.95           C  
ANISOU 2919  CA  VAL I 622    24073  24098  12985  -3747    271  -4011       C  
ATOM   2920  C   VAL I 622      12.829 -23.660  94.277  1.00162.49           C  
ANISOU 2920  C   VAL I 622    24338  24193  13208  -3946    558  -3922       C  
ATOM   2921  O   VAL I 622      12.201 -24.719  94.386  1.00161.10           O  
ANISOU 2921  O   VAL I 622    23968  24124  13117  -3839    773  -3781       O  
ATOM   2922  CB  VAL I 622      13.674 -22.847  92.029  1.00157.75           C  
ANISOU 2922  CB  VAL I 622    24116  23360  12462  -3420    297  -3867       C  
ATOM   2923  CG1 VAL I 622      13.689 -24.253  91.451  1.00154.38           C  
ANISOU 2923  CG1 VAL I 622    23762  22829  12065  -3082    585  -3602       C  
ATOM   2924  CG2 VAL I 622      13.478 -21.811  90.931  1.00154.97           C  
ANISOU 2924  CG2 VAL I 622    23680  23084  12116  -3229     -9  -3937       C  
ATOM   2925  N   GLU I 623      13.728 -23.278  95.186  1.00160.04           N  
ANISOU 2925  N   GLU I 623    24300  23678  12829  -4247    559  -4001       N  
ATOM   2926  CA  GLU I 623      14.100 -24.166  96.277  1.00159.94           C  
ANISOU 2926  CA  GLU I 623    24400  23533  12836  -4433    836  -3900       C  
ATOM   2927  C   GLU I 623      13.026 -24.249  97.356  1.00165.14           C  
ANISOU 2927  C   GLU I 623    24571  24478  13697  -4677    863  -3942       C  
ATOM   2928  O   GLU I 623      12.951 -25.264  98.052  1.00166.31           O  
ANISOU 2928  O   GLU I 623    24695  24608  13885  -4739   1126  -3806       O  
ATOM   2929  CB  GLU I 623      15.441 -23.722  96.870  1.00160.50           C  
ANISOU 2929  CB  GLU I 623    24933  23274  12777  -4671    825  -3973       C  
ATOM   2930  CG  GLU I 623      16.097 -24.753  97.788  1.00160.78           C  
ANISOU 2930  CG  GLU I 623    25199  23086  12804  -4800   1142  -3829       C  
ATOM   2931  CD  GLU I 623      17.600 -24.578  97.890  1.00164.98           C  
ANISOU 2931  CD  GLU I 623    26308  23212  13164  -4878   1187  -3850       C  
ATOM   2932  OE1 GLU I 623      18.072 -23.423  97.830  1.00168.55           O  
ANISOU 2932  OE1 GLU I 623    26915  23590  13537  -5015    932  -4040       O  
ATOM   2933  OE2 GLU I 623      18.309 -25.597  98.023  1.00164.69           O  
ANISOU 2933  OE2 GLU I 623    26572  22927  13076  -4801   1476  -3675       O  
ATOM   2934  N   ASP I 624      12.158 -23.240  97.480  1.00163.69           N  
ANISOU 2934  N   ASP I 624    23987  24564  13645  -4802    606  -4114       N  
ATOM   2935  CA  ASP I 624      11.034 -23.346  98.409  1.00165.15           C  
ANISOU 2935  CA  ASP I 624    23678  25042  14029  -4994    651  -4147       C  
ATOM   2936  C   ASP I 624      10.032 -24.401  97.942  1.00160.32           C  
ANISOU 2936  C   ASP I 624    22794  24637  13483  -4727    832  -4010       C  
ATOM   2937  O   ASP I 624       9.597 -25.256  98.728  1.00160.17           O  
ANISOU 2937  O   ASP I 624    22618  24709  13531  -4820   1059  -3918       O  
ATOM   2938  CB  ASP I 624      10.353 -21.987  98.569  1.00163.01           C  
ANISOU 2938  CB  ASP I 624    23041  24998  13899  -5170    331  -4355       C  
ATOM   2939  CG  ASP I 624      11.204 -20.997  99.338  1.00164.97           C  
ANISOU 2939  CG  ASP I 624    23488  25074  14119  -5514    158  -4490       C  
ATOM   2940  OD1 ASP I 624      12.406 -21.273  99.536  1.00165.37           O  
ANISOU 2940  OD1 ASP I 624    24013  24805  14013  -5574    261  -4440       O  
ATOM   2941  OD2 ASP I 624      10.673 -19.941  99.742  1.00167.25           O  
ANISOU 2941  OD2 ASP I 624    23458  25539  14551  -5726    -82  -4642       O  
ATOM   2942  N   ALA I 625       9.661 -24.356  96.658  1.00161.60           N  
ANISOU 2942  N   ALA I 625    22902  24872  13624  -4394    729  -3992       N  
ATOM   2943  CA  ALA I 625       8.818 -25.403  96.092  1.00158.19           C  
ANISOU 2943  CA  ALA I 625    22268  24595  13241  -4114    892  -3852       C  
ATOM   2944  C   ALA I 625       9.521 -26.751  96.105  1.00149.40           C  
ANISOU 2944  C   ALA I 625    21503  23251  12011  -3997   1197  -3623       C  
ATOM   2945  O   ALA I 625       8.869 -27.787  96.262  1.00148.30           O  
ANISOU 2945  O   ALA I 625    21188  23235  11925  -3918   1394  -3496       O  
ATOM   2946  CB  ALA I 625       8.400 -25.033  94.668  1.00160.36           C  
ANISOU 2946  CB  ALA I 625    22450  24958  13522  -3782    705  -3870       C  
ATOM   2947  N   ARG I 626      10.850 -26.751  95.968  1.00146.14           N  
ANISOU 2947  N   ARG I 626    21583  22502  11442  -3994   1241  -3568       N  
ATOM   2948  CA  ARG I 626      11.622 -27.982  96.105  1.00141.72           C  
ANISOU 2948  CA  ARG I 626    21366  21692  10790  -3918   1539  -3346       C  
ATOM   2949  C   ARG I 626      11.516 -28.547  97.517  1.00139.25           C  
ANISOU 2949  C   ARG I 626    20955  21409  10542  -4220   1734  -3301       C  
ATOM   2950  O   ARG I 626      11.441 -29.766  97.701  1.00141.04           O  
ANISOU 2950  O   ARG I 626    21212  21609  10770  -4145   1985  -3101       O  
ATOM   2951  CB  ARG I 626      13.082 -27.713  95.745  1.00135.52           C  
ANISOU 2951  CB  ARG I 626    21124  20533   9834  -3880   1538  -3328       C  
ATOM   2952  CG  ARG I 626      13.837 -28.900  95.186  1.00127.78           C  
ANISOU 2952  CG  ARG I 626    20491  19275   8786  -3608   1791  -3065       C  
ATOM   2953  CD  ARG I 626      15.149 -28.436  94.581  1.00120.75           C  
ANISOU 2953  CD  ARG I 626    20062  18030   7787  -3484   1736  -3058       C  
ATOM   2954  NE  ARG I 626      15.703 -29.402  93.641  1.00122.23           N  
ANISOU 2954  NE  ARG I 626    20455  17972   8017  -3085   1900  -2782       N  
ATOM   2955  CZ  ARG I 626      16.622 -29.107  92.729  1.00108.46           C  
ANISOU 2955  CZ  ARG I 626    19021  15973   6214  -2846   1850  -2736       C  
ATOM   2956  NH1 ARG I 626      17.091 -27.870  92.635  1.00110.66           N  
ANISOU 2956  NH1 ARG I 626    19460  16204   6384  -2963   1633  -2946       N  
ATOM   2957  NH2 ARG I 626      17.074 -30.047  91.910  1.00106.54           N  
ANISOU 2957  NH2 ARG I 626    18914  15534   6034  -2494   2011  -2475       N  
ATOM   2958  N   ARG I 627      11.504 -27.671  98.526  1.00144.61           N  
ANISOU 2958  N   ARG I 627    21513  22148  11284  -4567   1616  -3473       N  
ATOM   2959  CA  ARG I 627      11.366 -28.117  99.910  1.00148.44           C  
ANISOU 2959  CA  ARG I 627    21877  22679  11844  -4872   1790  -3433       C  
ATOM   2960  C   ARG I 627       9.974 -28.679 100.176  1.00145.10           C  
ANISOU 2960  C   ARG I 627    20978  22609  11546  -4850   1877  -3399       C  
ATOM   2961  O   ARG I 627       9.835 -29.711 100.844  1.00144.47           O  
ANISOU 2961  O   ARG I 627    20871  22546  11475  -4916   2122  -3244       O  
ATOM   2962  CB  ARG I 627      11.686 -26.965 100.870  1.00153.46           C  
ANISOU 2962  CB  ARG I 627    22486  23289  12531  -5245   1619  -3626       C  
ATOM   2963  CG  ARG I 627      10.998 -27.056 102.231  1.00154.91           C  
ANISOU 2963  CG  ARG I 627    22321  23679  12860  -5563   1708  -3647       C  
ATOM   2964  CD  ARG I 627      11.784 -26.362 103.332  1.00156.58           C  
ANISOU 2964  CD  ARG I 627    22679  23718  13095  -5941   1647  -3740       C  
ATOM   2965  NE  ARG I 627      12.684 -27.288 104.014  1.00158.51           N  
ANISOU 2965  NE  ARG I 627    23252  23697  13279  -6043   1910  -3567       N  
ATOM   2966  CZ  ARG I 627      13.173 -27.097 105.235  1.00163.40           C  
ANISOU 2966  CZ  ARG I 627    23928  24202  13954  -6392   1955  -3584       C  
ATOM   2967  NH1 ARG I 627      12.851 -26.008 105.918  1.00168.01           N  
ANISOU 2967  NH1 ARG I 627    24262  24917  14657  -6676   1750  -3765       N  
ATOM   2968  NH2 ARG I 627      13.982 -27.998 105.776  1.00162.94           N  
ANISOU 2968  NH2 ARG I 627    24167  23894  13848  -6458   2202  -3411       N  
ATOM   2969  N   ILE I 628       8.930 -28.027  99.658  1.00145.54           N  
ANISOU 2969  N   ILE I 628    20658  22946  11696  -4754   1682  -3540       N  
ATOM   2970  CA  ILE I 628       7.586 -28.559  99.894  1.00135.98           C  
ANISOU 2970  CA  ILE I 628    19002  22066  10598  -4724   1774  -3524       C  
ATOM   2971  C   ILE I 628       7.326 -29.821  99.068  1.00132.92           C  
ANISOU 2971  C   ILE I 628    18677  21675  10151  -4395   1944  -3324       C  
ATOM   2972  O   ILE I 628       6.561 -30.697  99.492  1.00132.02           O  
ANISOU 2972  O   ILE I 628    18347  21738  10075  -4404   2120  -3235       O  
ATOM   2973  CB  ILE I 628       6.507 -27.485  99.655  1.00132.02           C  
ANISOU 2973  CB  ILE I 628    18057  21863  10241  -4733   1527  -3737       C  
ATOM   2974  CG1 ILE I 628       6.949 -26.148 100.246  1.00130.31           C  
ANISOU 2974  CG1 ILE I 628    17842  21595  10075  -5025   1310  -3919       C  
ATOM   2975  CG2 ILE I 628       5.170 -27.907 100.259  1.00133.59           C  
ANISOU 2975  CG2 ILE I 628    17793  22398  10569  -4799   1644  -3755       C  
ATOM   2976  CD1 ILE I 628       5.883 -25.086 100.234  1.00132.07           C  
ANISOU 2976  CD1 ILE I 628    17594  22114  10474  -5089   1083  -4114       C  
ATOM   2977  N   ALA I 629       7.973 -29.967  97.911  1.00128.90           N  
ANISOU 2977  N   ALA I 629    18470  20961   9544  -4107   1902  -3240       N  
ATOM   2978  CA  ALA I 629       7.727 -31.134  97.074  1.00127.48           C  
ANISOU 2978  CA  ALA I 629    18338  20771   9328  -3788   2045  -3039       C  
ATOM   2979  C   ALA I 629       8.618 -32.323  97.418  1.00131.02           C  
ANISOU 2979  C   ALA I 629    19132  20942   9708  -3777   2308  -2782       C  
ATOM   2980  O   ALA I 629       8.243 -33.465  97.128  1.00124.90           O  
ANISOU 2980  O   ALA I 629    18282  20136   9040  -3549   2427  -2554       O  
ATOM   2981  CB  ALA I 629       7.914 -30.771  95.597  1.00123.34           C  
ANISOU 2981  CB  ALA I 629    17923  20149   8790  -3441   1871  -3031       C  
ATOM   2982  N   PHE I 630       9.781 -32.092  98.028  1.00135.34           N  
ANISOU 2982  N   PHE I 630    20030  21233  10160  -3985   2370  -2783       N  
ATOM   2983  CA  PHE I 630      10.727 -33.159  98.329  1.00142.12           C  
ANISOU 2983  CA  PHE I 630    21236  21794  10971  -3970   2616  -2536       C  
ATOM   2984  C   PHE I 630      11.013 -33.332  99.816  1.00139.76           C  
ANISOU 2984  C   PHE I 630    20962  21472  10668  -4352   2770  -2530       C  
ATOM   2985  O   PHE I 630      11.773 -34.238 100.179  1.00138.57           O  
ANISOU 2985  O   PHE I 630    21087  21090  10473  -4378   2992  -2324       O  
ATOM   2986  CB  PHE I 630      12.064 -32.925  97.602  1.00151.11           C  
ANISOU 2986  CB  PHE I 630    22838  22551  12027  -3807   2587  -2480       C  
ATOM   2987  CG  PHE I 630      12.000 -33.097  96.105  1.00151.78           C  
ANISOU 2987  CG  PHE I 630    22935  22551  12184  -3352   2483  -2366       C  
ATOM   2988  CD1 PHE I 630      11.474 -32.106  95.290  1.00151.79           C  
ANISOU 2988  CD1 PHE I 630    22768  22720  12184  -3235   2233  -2549       C  
ATOM   2989  CD2 PHE I 630      12.483 -34.255  95.514  1.00149.44           C  
ANISOU 2989  CD2 PHE I 630    22809  22009  11964  -3045   2633  -2065       C  
ATOM   2990  CE1 PHE I 630      11.424 -32.272  93.916  1.00147.04           C  
ANISOU 2990  CE1 PHE I 630    22183  22044  11643  -2824   2148  -2433       C  
ATOM   2991  CE2 PHE I 630      12.436 -34.426  94.144  1.00144.98           C  
ANISOU 2991  CE2 PHE I 630    22248  21376  11460  -2636   2546  -1953       C  
ATOM   2992  CZ  PHE I 630      11.907 -33.434  93.344  1.00144.29           C  
ANISOU 2992  CZ  PHE I 630    22009  21458  11358  -2527   2309  -2137       C  
ATOM   2993  N   GLY I 631      10.437 -32.506 100.684  1.00144.52           N  
ANISOU 2993  N   GLY I 631    23446  16970  14494  -7558  -1359   4058       N  
ATOM   2994  CA  GLY I 631      10.801 -32.536 102.089  1.00145.04           C  
ANISOU 2994  CA  GLY I 631    23610  16781  14719  -7729  -1347   4393       C  
ATOM   2995  C   GLY I 631       9.845 -33.288 102.989  1.00140.21           C  
ANISOU 2995  C   GLY I 631    23026  16295  13951  -7598  -1176   4759       C  
ATOM   2996  O   GLY I 631      10.264 -33.875 103.992  1.00143.59           O  
ANISOU 2996  O   GLY I 631    23645  16466  14446  -7599  -1175   4999       O  
ATOM   2997  N   GLY I 632       8.556 -33.272 102.656  1.00148.09           N  
ANISOU 2997  N   GLY I 632    23847  17680  14739  -7487  -1018   4811       N  
ATOM   2998  CA  GLY I 632       7.572 -33.974 103.451  1.00152.00           C  
ANISOU 2998  CA  GLY I 632    24376  18328  15049  -7363   -834   5137       C  
ATOM   2999  C   GLY I 632       7.449 -35.438 103.069  1.00154.79           C  
ANISOU 2999  C   GLY I 632    24916  18734  15162  -6976   -881   5044       C  
ATOM   3000  O   GLY I 632       7.961 -35.888 102.046  1.00155.06           O  
ANISOU 3000  O   GLY I 632    25000  18737  15180  -6787  -1028   4692       O  
ATOM   3001  N   HIS I 633       6.749 -36.186 103.922  1.00153.43           N  
ANISOU 3001  N   HIS I 633    24852  18640  14803  -6861   -748   5359       N  
ATOM   3002  CA  HIS I 633       6.478 -37.591 103.647  1.00157.32           C  
ANISOU 3002  CA  HIS I 633    25513  19227  15033  -6482   -801   5297       C  
ATOM   3003  C   HIS I 633       5.374 -37.787 102.616  1.00155.26           C  
ANISOU 3003  C   HIS I 633    25056  19391  14545  -6278   -706   5070       C  
ATOM   3004  O   HIS I 633       5.140 -38.924 102.191  1.00153.64           O  
ANISOU 3004  O   HIS I 633    24949  19293  14135  -5951   -771   4935       O  
ATOM   3005  CB  HIS I 633       6.115 -38.321 104.942  1.00164.63           C  
ANISOU 3005  CB  HIS I 633    26660  20090  15800  -6428   -697   5727       C  
ATOM   3006  CG  HIS I 633       7.282 -38.982 105.607  1.00171.51           C  
ANISOU 3006  CG  HIS I 633    27838  20536  16793  -6379   -873   5846       C  
ATOM   3007  ND1 HIS I 633       8.215 -38.281 106.340  1.00174.51           N  
ANISOU 3007  ND1 HIS I 633    28270  20551  17482  -6675   -894   5988       N  
ATOM   3008  CD2 HIS I 633       7.670 -40.279 105.645  1.00173.52           C  
ANISOU 3008  CD2 HIS I 633    28351  20660  16920  -6064  -1042   5837       C  
ATOM   3009  CE1 HIS I 633       9.127 -39.118 106.804  1.00176.66           C  
ANISOU 3009  CE1 HIS I 633    28826  20478  17818  -6547  -1049   6071       C  
ATOM   3010  NE2 HIS I 633       8.819 -40.336 106.396  1.00176.36           N  
ANISOU 3010  NE2 HIS I 633    28918  20572  17517  -6170  -1152   5989       N  
ATOM   3011  N   GLN I 634       4.695 -36.716 102.213  1.00155.39           N  
ANISOU 3011  N   GLN I 634    24789  19642  14609  -6458   -561   5020       N  
ATOM   3012  CA  GLN I 634       3.713 -36.747 101.138  1.00151.77           C  
ANISOU 3012  CA  GLN I 634    24117  19558  13992  -6292   -458   4776       C  
ATOM   3013  C   GLN I 634       4.091 -35.691 100.111  1.00154.39           C  
ANISOU 3013  C   GLN I 634    24260  19891  14511  -6433   -517   4482       C  
ATOM   3014  O   GLN I 634       4.349 -34.538 100.472  1.00156.24           O  
ANISOU 3014  O   GLN I 634    24392  20031  14942  -6738   -512   4597       O  
ATOM   3015  CB  GLN I 634       2.297 -36.500 101.670  1.00149.05           C  
ANISOU 3015  CB  GLN I 634    23604  19534  13495  -6352   -180   5040       C  
ATOM   3016  CG  GLN I 634       2.245 -35.572 102.875  1.00150.05           C  
ANISOU 3016  CG  GLN I 634    23675  19540  13798  -6686    -55   5400       C  
ATOM   3017  CD  GLN I 634       0.838 -35.109 103.194  1.00148.71           C  
ANISOU 3017  CD  GLN I 634    23170  19673  13661  -6633    228   5457       C  
ATOM   3018  OE1 GLN I 634      -0.092 -35.329 102.418  1.00146.10           O  
ANISOU 3018  OE1 GLN I 634    22680  19655  13178  -6456    334   5286       O  
ATOM   3019  NE2 GLN I 634       0.675 -34.463 104.343  1.00149.80           N  
ANISOU 3019  NE2 GLN I 634    23199  19702  14016  -6790    365   5687       N  
ATOM   3020  N   ARG I 635       4.133 -36.083  98.842  1.00148.79           N  
ANISOU 3020  N   ARG I 635    23511  19280  13742  -6213   -573   4097       N  
ATOM   3021  CA  ARG I 635       4.525 -35.163  97.785  1.00144.70           C  
ANISOU 3021  CA  ARG I 635    22863  18751  13364  -6320   -621   3805       C  
ATOM   3022  C   ARG I 635       3.330 -34.337  97.324  1.00143.96           C  
ANISOU 3022  C   ARG I 635    22474  19004  13221  -6384   -422   3820       C  
ATOM   3023  O   ARG I 635       2.182 -34.790  97.360  1.00149.15           O  
ANISOU 3023  O   ARG I 635    23019  19944  13707  -6239   -243   3896       O  
ATOM   3024  CB  ARG I 635       5.127 -35.923  96.600  1.00135.21           C  
ANISOU 3024  CB  ARG I 635    21755  17471  12149  -6067   -734   3374       C  
ATOM   3025  CG  ARG I 635       6.110 -37.028  96.979  1.00133.59           C  
ANISOU 3025  CG  ARG I 635    21817  16963  11977  -5914   -919   3333       C  
ATOM   3026  CD  ARG I 635       7.253 -36.505  97.842  1.00136.26           C  
ANISOU 3026  CD  ARG I 635    22310  16935  12527  -6178  -1059   3507       C  
ATOM   3027  NE  ARG I 635       8.173 -37.564  98.248  1.00139.17           N  
ANISOU 3027  NE  ARG I 635    22930  16996  12952  -6026  -1229   3492       N  
ATOM   3028  CZ  ARG I 635       9.209 -37.382  99.060  1.00139.04           C  
ANISOU 3028  CZ  ARG I 635    23078  16623  13127  -6204  -1349   3640       C  
ATOM   3029  NH1 ARG I 635       9.461 -36.180  99.558  1.00139.84           N  
ANISOU 3029  NH1 ARG I 635    23114  16640  13379  -6548  -1323   3797       N  
ATOM   3030  NH2 ARG I 635       9.993 -38.404  99.377  1.00138.58           N  
ANISOU 3030  NH2 ARG I 635    23240  16285  13128  -6035  -1502   3623       N  
ATOM   3031  N   HIS I 636       3.609 -33.108  96.892  1.00144.00           N  
ANISOU 3031  N   HIS I 636    22356  18979  13379  -6602   -460   3746       N  
ATOM   3032  CA  HIS I 636       2.566 -32.192  96.457  1.00141.66           C  
ANISOU 3032  CA  HIS I 636    21773  18973  13078  -6677   -299   3773       C  
ATOM   3033  C   HIS I 636       3.010 -31.447  95.208  1.00138.24           C  
ANISOU 3033  C   HIS I 636    21294  18521  12711  -6705   -378   3463       C  
ATOM   3034  O   HIS I 636       4.170 -31.042  95.093  1.00141.99           O  
ANISOU 3034  O   HIS I 636    21916  18734  13301  -6838   -566   3350       O  
ATOM   3035  CB  HIS I 636       2.198 -31.193  97.562  1.00140.59           C  
ANISOU 3035  CB  HIS I 636    21490  18851  13078  -6978   -242   4136       C  
ATOM   3036  CG  HIS I 636       1.755 -31.841  98.837  1.00138.86           C  
ANISOU 3036  CG  HIS I 636    21337  18632  12793  -6981   -124   4464       C  
ATOM   3037  ND1 HIS I 636       2.577 -31.959  99.937  1.00141.46           N  
ANISOU 3037  ND1 HIS I 636    21858  18666  13225  -7129   -223   4674       N  
ATOM   3038  CD2 HIS I 636       0.581 -32.419  99.182  1.00138.63           C  
ANISOU 3038  CD2 HIS I 636    21206  18847  12619  -6822     95   4589       C  
ATOM   3039  CE1 HIS I 636       1.924 -32.575 100.907  1.00144.24           C  
ANISOU 3039  CE1 HIS I 636    22239  19079  13487  -7059    -64   4932       C  
ATOM   3040  NE2 HIS I 636       0.711 -32.865 100.474  1.00141.75           N  
ANISOU 3040  NE2 HIS I 636    21734  19090  13033  -6845    122   4855       N  
ATOM   3041  N   LYS I 637       2.070 -31.274  94.281  1.00131.11           N  
ANISOU 3041  N   LYS I 637    20196  17891  11728  -6579   -218   3328       N  
ATOM   3042  CA  LYS I 637       2.308 -30.555  93.033  1.00125.15           C  
ANISOU 3042  CA  LYS I 637    19398  17148  11005  -6584   -246   3056       C  
ATOM   3043  C   LYS I 637       2.510 -29.076  93.341  1.00111.14           C  
ANISOU 3043  C   LYS I 637    17521  15332   9374  -6891   -352   3224       C  
ATOM   3044  O   LYS I 637       1.588 -28.402  93.812  1.00107.58           O  
ANISOU 3044  O   LYS I 637    16831  15068   8976  -7002   -250   3467       O  
ATOM   3045  CB  LYS I 637       1.125 -30.775  92.093  1.00101.92           C  
ANISOU 3045  CB  LYS I 637    16257  14509   7958  -6371    -14   2915       C  
ATOM   3046  CG  LYS I 637       1.406 -30.584  90.613  1.00 99.56           C  
ANISOU 3046  CG  LYS I 637    15988  14196   7645  -6261      8   2554       C  
ATOM   3047  CD  LYS I 637       0.157 -30.909  89.802  1.00 97.50           C  
ANISOU 3047  CD  LYS I 637    15515  14227   7304  -6042    271   2432       C  
ATOM   3048  CE  LYS I 637       0.213 -30.325  88.401  1.00 95.51           C  
ANISOU 3048  CE  LYS I 637    15240  13985   7065  -5994    340   2162       C  
ATOM   3049  NZ  LYS I 637      -0.966 -30.738  87.590  1.00 93.60           N  
ANISOU 3049  NZ  LYS I 637    14793  13998   6772  -5769    618   2017       N  
ATOM   3050  N   THR I 638       3.715 -28.566  93.090  1.00122.35           N  
ANISOU 3050  N   THR I 638    19115  16504  10869  -7030   -559   3083       N  
ATOM   3051  CA  THR I 638       4.071 -27.207  93.476  1.00124.22           C  
ANISOU 3051  CA  THR I 638    19282  16671  11243  -7330   -714   3223       C  
ATOM   3052  C   THR I 638       4.801 -26.502  92.340  1.00121.99           C  
ANISOU 3052  C   THR I 638    19112  16303  10934  -7370   -842   2943       C  
ATOM   3053  O   THR I 638       5.635 -27.104  91.658  1.00118.47           O  
ANISOU 3053  O   THR I 638    18898  15687  10428  -7259   -880   2654       O  
ATOM   3054  CB  THR I 638       4.945 -27.204  94.736  1.00129.53           C  
ANISOU 3054  CB  THR I 638    20080  17079  12057  -7542   -870   3401       C  
ATOM   3055  OG1 THR I 638       4.542 -28.270  95.606  1.00130.02           O  
ANISOU 3055  OG1 THR I 638    20169  17150  12082  -7429   -747   3586       O  
ATOM   3056  CG2 THR I 638       4.786 -25.900  95.471  1.00130.93           C  
ANISOU 3056  CG2 THR I 638    20065  17277  12405  -7841   -955   3639       C  
ATOM   3057  N   VAL I 639       4.489 -25.219  92.150  1.00124.71           N  
ANISOU 3057  N   VAL I 639    19298  16759  11326  -7528   -907   3028       N  
ATOM   3058  CA  VAL I 639       5.085 -24.394  91.105  1.00132.46           C  
ANISOU 3058  CA  VAL I 639    20393  17685  12249  -7581  -1034   2806       C  
ATOM   3059  C   VAL I 639       5.709 -23.171  91.773  1.00149.09           C  
ANISOU 3059  C   VAL I 639    22482  19678  14487  -7897  -1296   2938       C  
ATOM   3060  O   VAL I 639       5.258 -22.728  92.832  1.00156.67           O  
ANISOU 3060  O   VAL I 639    23232  20694  15601  -8054  -1325   3220       O  
ATOM   3061  CB  VAL I 639       4.020 -24.009  90.043  1.00125.51           C  
ANISOU 3061  CB  VAL I 639    19341  17072  11275  -7424   -868   2762       C  
ATOM   3062  CG1 VAL I 639       2.867 -23.226  90.668  1.00125.91           C  
ANISOU 3062  CG1 VAL I 639    19047  17352  11441  -7516   -823   3080       C  
ATOM   3063  CG2 VAL I 639       4.624 -23.280  88.839  1.00122.21           C  
ANISOU 3063  CG2 VAL I 639    19096  16588  10749  -7439   -964   2523       C  
ATOM   3064  N   ALA I 640       6.784 -22.653  91.178  1.00148.47           N  
ANISOU 3064  N   ALA I 640    22630  19427  14354  -7999  -1482   2715       N  
ATOM   3065  CA  ALA I 640       7.480 -21.475  91.677  1.00150.83           C  
ANISOU 3065  CA  ALA I 640    22938  19616  14757  -8296  -1759   2777       C  
ATOM   3066  C   ALA I 640       7.001 -20.235  90.906  1.00148.87           C  
ANISOU 3066  C   ALA I 640    22576  19555  14433  -8330  -1850   2786       C  
ATOM   3067  O   ALA I 640       6.011 -20.295  90.163  1.00145.44           O  
ANISOU 3067  O   ALA I 640    22014  19338  13907  -8133  -1669   2802       O  
ATOM   3068  CB  ALA I 640       8.988 -21.701  91.566  1.00151.98           C  
ANISOU 3068  CB  ALA I 640    23416  19446  14884  -8396  -1910   2520       C  
ATOM   3069  N   LEU I 641       7.699 -19.092  91.073  1.00151.59           N  
ANISOU 3069  N   LEU I 641    18557  26788  12254  -2475  -1374   1424       N  
ATOM   3070  CA  LEU I 641       7.309 -17.897  90.324  1.00150.58           C  
ANISOU 3070  CA  LEU I 641    18270  26827  12115  -2367  -1436   1469       C  
ATOM   3071  C   LEU I 641       7.743 -18.042  88.878  1.00143.01           C  
ANISOU 3071  C   LEU I 641    17341  25854  11142  -2302  -1536   1577       C  
ATOM   3072  O   LEU I 641       7.170 -17.408  87.985  1.00137.63           O  
ANISOU 3072  O   LEU I 641    16597  25235  10462  -2173  -1585   1668       O  
ATOM   3073  CB  LEU I 641       7.967 -16.641  90.886  1.00155.56           C  
ANISOU 3073  CB  LEU I 641    18699  27697  12709  -2431  -1424   1370       C  
ATOM   3074  CG  LEU I 641       9.450 -16.428  90.605  1.00154.58           C  
ANISOU 3074  CG  LEU I 641    18526  27674  12534  -2535  -1458   1325       C  
ATOM   3075  CD1 LEU I 641       9.744 -14.996  90.423  1.00154.43           C  
ANISOU 3075  CD1 LEU I 641    18287  27940  12449  -2520  -1512   1288       C  
ATOM   3076  CD2 LEU I 641      10.397 -17.119  91.510  1.00154.32           C  
ANISOU 3076  CD2 LEU I 641    18570  27543  12524  -2698  -1362   1222       C  
ATOM   3077  N   ASP I 642       8.797 -18.823  88.666  1.00136.51           N  
ANISOU 3077  N   ASP I 642    16606  24949  10314  -2390  -1551   1567       N  
ATOM   3078  CA  ASP I 642       9.412 -19.145  87.407  1.00134.12           C  
ANISOU 3078  CA  ASP I 642    16347  24603  10008  -2365  -1621   1645       C  
ATOM   3079  C   ASP I 642       8.581 -20.201  86.705  1.00131.78           C  
ANISOU 3079  C   ASP I 642    16196  24108   9768  -2288  -1641   1724       C  
ATOM   3080  O   ASP I 642       7.616 -20.736  87.255  1.00132.40           O  
ANISOU 3080  O   ASP I 642    16348  24087   9871  -2268  -1602   1710       O  
ATOM   3081  CB  ASP I 642      10.835 -19.637  87.651  1.00129.70           C  
ANISOU 3081  CB  ASP I 642    15818  24015   9448  -2502  -1602   1581       C  
ATOM   3082  CG  ASP I 642      11.834 -19.020  86.698  1.00123.94           C  
ANISOU 3082  CG  ASP I 642    15013  23404   8674  -2519  -1650   1597       C  
ATOM   3083  OD1 ASP I 642      11.674 -19.216  85.465  1.00125.73           O  
ANISOU 3083  OD1 ASP I 642    15287  23576   8910  -2435  -1705   1697       O  
ATOM   3084  OD2 ASP I 642      12.795 -18.373  87.175  1.00122.40           O  
ANISOU 3084  OD2 ASP I 642    14719  23352   8436  -2627  -1618   1501       O  
ATOM   3085  N   GLY I 643       8.997 -20.537  85.489  1.00130.67           N  
ANISOU 3085  N   GLY I 643    16097  23907   9644  -2258  -1692   1792       N  
ATOM   3086  CA  GLY I 643       8.277 -21.542  84.732  1.00129.46           C  
ANISOU 3086  CA  GLY I 643    16065  23571   9553  -2200  -1705   1844       C  
ATOM   3087  C   GLY I 643       8.443 -22.954  85.259  1.00129.96           C  
ANISOU 3087  C   GLY I 643    16252  23483   9642  -2278  -1705   1798       C  
ATOM   3088  O   GLY I 643       7.671 -23.847  84.883  1.00131.91           O  
ANISOU 3088  O   GLY I 643    16593  23599   9926  -2244  -1716   1812       O  
ATOM   3089  N   THR I 644       9.417 -23.169  86.143  1.00129.13           N  
ANISOU 3089  N   THR I 644    16145  23399   9518  -2380  -1687   1743       N  
ATOM   3090  CA  THR I 644       9.703 -24.505  86.650  1.00128.92           C  
ANISOU 3090  CA  THR I 644    16232  23239   9512  -2438  -1690   1727       C  
ATOM   3091  C   THR I 644       8.535 -25.043  87.473  1.00129.51           C  
ANISOU 3091  C   THR I 644    16392  23257   9558  -2419  -1663   1711       C  
ATOM   3092  O   THR I 644       8.006 -24.364  88.359  1.00127.71           O  
ANISOU 3092  O   THR I 644    16129  23100   9296  -2423  -1598   1674       O  
ATOM   3093  CB  THR I 644      10.994 -24.500  87.478  1.00128.68           C  
ANISOU 3093  CB  THR I 644    16178  23233   9483  -2542  -1643   1681       C  
ATOM   3094  OG1 THR I 644      11.120 -25.737  88.193  1.00128.50           O  
ANISOU 3094  OG1 THR I 644    16266  23084   9473  -2574  -1633   1688       O  
ATOM   3095  CG2 THR I 644      11.037 -23.319  88.449  1.00129.98           C  
ANISOU 3095  CG2 THR I 644    16242  23543   9603  -2587  -1566   1612       C  
ATOM   3096  N   LEU I 645       8.114 -26.259  87.141  1.00125.87           N  
ANISOU 3096  N   LEU I 645    16039  22678   9109  -2403  -1710   1730       N  
ATOM   3097  CA  LEU I 645       6.995 -26.927  87.788  1.00125.05           C  
ANISOU 3097  CA  LEU I 645    16033  22522   8957  -2393  -1692   1710       C  
ATOM   3098  C   LEU I 645       7.482 -28.245  88.373  1.00123.60           C  
ANISOU 3098  C   LEU I 645    15955  22266   8742  -2439  -1727   1722       C  
ATOM   3099  O   LEU I 645       8.258 -28.965  87.737  1.00123.83           O  
ANISOU 3099  O   LEU I 645    15990  22244   8817  -2445  -1798   1752       O  
ATOM   3100  CB  LEU I 645       5.854 -27.174  86.791  1.00125.36           C  
ANISOU 3100  CB  LEU I 645    16100  22506   9024  -2330  -1717   1709       C  
ATOM   3101  CG  LEU I 645       4.670 -28.042  87.221  1.00128.37           C  
ANISOU 3101  CG  LEU I 645    16592  22831   9352  -2334  -1704   1667       C  
ATOM   3102  CD1 LEU I 645       3.985 -27.458  88.448  1.00129.61           C  
ANISOU 3102  CD1 LEU I 645    16759  23035   9450  -2346  -1606   1633       C  
ATOM   3103  CD2 LEU I 645       3.684 -28.209  86.075  1.00131.43           C  
ANISOU 3103  CD2 LEU I 645    16988  23154   9796  -2286  -1706   1647       C  
ATOM   3104  N   PHE I 646       7.035 -28.553  89.585  1.00126.30           N  
ANISOU 3104  N   PHE I 646    16377  22604   9009  -2464  -1671   1708       N  
ATOM   3105  CA  PHE I 646       7.473 -29.744  90.306  1.00128.63           C  
ANISOU 3105  CA  PHE I 646    16778  22840   9253  -2491  -1692   1746       C  
ATOM   3106  C   PHE I 646       6.292 -30.707  90.378  1.00132.04           C  
ANISOU 3106  C   PHE I 646    17326  23249   9596  -2471  -1735   1735       C  
ATOM   3107  O   PHE I 646       5.379 -30.525  91.188  1.00137.02           O  
ANISOU 3107  O   PHE I 646    18016  23896  10149  -2483  -1657   1701       O  
ATOM   3108  CB  PHE I 646       7.984 -29.375  91.695  1.00128.71           C  
ANISOU 3108  CB  PHE I 646    16806  22861   9236  -2543  -1573   1745       C  
ATOM   3109  CG  PHE I 646       9.368 -28.795  91.693  1.00129.07           C  
ANISOU 3109  CG  PHE I 646    16757  22918   9366  -2586  -1533   1744       C  
ATOM   3110  CD1 PHE I 646       9.566 -27.452  91.411  1.00129.61           C  
ANISOU 3110  CD1 PHE I 646    16690  23079   9476  -2606  -1492   1687       C  
ATOM   3111  CD2 PHE I 646      10.470 -29.589  91.963  1.00130.34           C  
ANISOU 3111  CD2 PHE I 646    16957  23003   9564  -2606  -1532   1800       C  
ATOM   3112  CE1 PHE I 646      10.837 -26.910  91.405  1.00130.35           C  
ANISOU 3112  CE1 PHE I 646    16695  23201   9630  -2664  -1449   1664       C  
ATOM   3113  CE2 PHE I 646      11.746 -29.053  91.958  1.00132.00           C  
ANISOU 3113  CE2 PHE I 646    17080  23213   9862  -2661  -1471   1780       C  
ATOM   3114  CZ  PHE I 646      11.927 -27.711  91.679  1.00131.51           C  
ANISOU 3114  CZ  PHE I 646    16889  23255   9824  -2700  -1429   1702       C  
ATOM   3115  N   GLN I 647       6.314 -31.729  89.526  1.00130.54           N  
ANISOU 3115  N   GLN I 647    17160  23025   9416  -2451  -1853   1750       N  
ATOM   3116  CA  GLN I 647       5.252 -32.722  89.507  1.00126.92           C  
ANISOU 3116  CA  GLN I 647    16799  22565   8861  -2448  -1907   1718       C  
ATOM   3117  C   GLN I 647       5.352 -33.637  90.729  1.00121.51           C  
ANISOU 3117  C   GLN I 647    16237  21888   8043  -2460  -1911   1773       C  
ATOM   3118  O   GLN I 647       6.327 -33.609  91.487  1.00116.81           O  
ANISOU 3118  O   GLN I 647    15652  21274   7458  -2464  -1870   1844       O  
ATOM   3119  CB  GLN I 647       5.314 -33.546  88.221  1.00131.26           C  
ANISOU 3119  CB  GLN I 647    17316  23090   9468  -2433  -2032   1700       C  
ATOM   3120  CG  GLN I 647       5.144 -32.734  86.947  1.00134.69           C  
ANISOU 3120  CG  GLN I 647    17649  23497  10029  -2414  -2011   1659       C  
ATOM   3121  CD  GLN I 647       4.697 -33.584  85.773  1.00139.64           C  
ANISOU 3121  CD  GLN I 647    18270  24089  10700  -2416  -2092   1600       C  
ATOM   3122  OE1 GLN I 647       4.135 -34.664  85.954  1.00142.70           O  
ANISOU 3122  OE1 GLN I 647    18725  24497  10998  -2438  -2158   1557       O  
ATOM   3123  NE2 GLN I 647       4.945 -33.100  84.561  1.00139.70           N  
ANISOU 3123  NE2 GLN I 647    18193  24049  10836  -2398  -2081   1590       N  
ATOM   3124  N   LYS I 648       4.316 -34.461  90.914  1.00121.48           N  
ANISOU 3124  N   LYS I 648    16334  21913   7910  -2468  -1948   1737       N  
ATOM   3125  CA  LYS I 648       4.311 -35.405  92.028  1.00125.88           C  
ANISOU 3125  CA  LYS I 648    17026  22495   8309  -2470  -1960   1803       C  
ATOM   3126  C   LYS I 648       5.368 -36.486  91.855  1.00127.96           C  
ANISOU 3126  C   LYS I 648    17284  22753   8580  -2429  -2093   1905       C  
ATOM   3127  O   LYS I 648       5.925 -36.971  92.847  1.00130.81           O  
ANISOU 3127  O   LYS I 648    17726  23104   8870  -2407  -2072   2013       O  
ATOM   3128  CB  LYS I 648       2.930 -36.042  92.180  1.00125.21           C  
ANISOU 3128  CB  LYS I 648    17048  22464   8062  -2497  -1977   1726       C  
ATOM   3129  CG  LYS I 648       1.818 -35.063  92.516  1.00123.02           C  
ANISOU 3129  CG  LYS I 648    16787  22178   7777  -2533  -1823   1630       C  
ATOM   3130  CD  LYS I 648       1.371 -35.226  93.960  1.00117.83           C  
ANISOU 3130  CD  LYS I 648    16277  21539   6955  -2562  -1715   1653       C  
ATOM   3131  CE  LYS I 648       0.730 -36.585  94.191  1.00116.31           C  
ANISOU 3131  CE  LYS I 648    16224  21418   6552  -2578  -1807   1649       C  
ATOM   3132  NZ  LYS I 648      -0.536 -36.752  93.427  1.00115.51           N  
ANISOU 3132  NZ  LYS I 648    16120  21346   6423  -2623  -1822   1498       N  
ATOM   3133  N   SER I 649       5.661 -36.873  90.611  1.00127.76           N  
ANISOU 3133  N   SER I 649    17163  22725   8655  -2414  -2215   1876       N  
ATOM   3134  CA  SER I 649       6.741 -37.819  90.361  1.00129.24           C  
ANISOU 3134  CA  SER I 649    17313  22900   8890  -2371  -2335   1968       C  
ATOM   3135  C   SER I 649       8.111 -37.191  90.575  1.00125.65           C  
ANISOU 3135  C   SER I 649    16794  22367   8580  -2360  -2255   2045       C  
ATOM   3136  O   SER I 649       9.088 -37.919  90.775  1.00123.52           O  
ANISOU 3136  O   SER I 649    16518  22066   8348  -2317  -2304   2149       O  
ATOM   3137  CB  SER I 649       6.639 -38.369  88.938  1.00137.08           C  
ANISOU 3137  CB  SER I 649    18209  23907   9968  -2371  -2469   1891       C  
ATOM   3138  OG  SER I 649       5.353 -38.908  88.688  1.00142.69           O  
ANISOU 3138  OG  SER I 649    18969  24690  10557  -2402  -2524   1788       O  
ATOM   3139  N   GLY I 650       8.198 -35.863  90.550  1.00120.28           N  
ANISOU 3139  N   GLY I 650    16060  21660   7981  -2396  -2129   1995       N  
ATOM   3140  CA  GLY I 650       9.458 -35.163  90.652  1.00125.63           C  
ANISOU 3140  CA  GLY I 650    16662  22282   8791  -2410  -2045   2031       C  
ATOM   3141  C   GLY I 650       9.986 -34.625  89.342  1.00126.80           C  
ANISOU 3141  C   GLY I 650    16680  22412   9088  -2420  -2076   1980       C  
ATOM   3142  O   GLY I 650      11.087 -34.059  89.324  1.00130.08           O  
ANISOU 3142  O   GLY I 650    17026  22791   9609  -2443  -2010   1995       O  
ATOM   3143  N   VAL I 651       9.245 -34.795  88.247  1.00128.82           N  
ANISOU 3143  N   VAL I 651    16903  22687   9355  -2411  -2160   1915       N  
ATOM   3144  CA  VAL I 651       9.702 -34.341  86.940  1.00128.37           C  
ANISOU 3144  CA  VAL I 651    16738  22603   9435  -2417  -2178   1876       C  
ATOM   3145  C   VAL I 651       9.706 -32.818  86.910  1.00125.61           C  
ANISOU 3145  C   VAL I 651    16334  22279   9112  -2439  -2064   1845       C  
ATOM   3146  O   VAL I 651       8.750 -32.167  87.349  1.00131.14           O  
ANISOU 3146  O   VAL I 651    17062  23024   9740  -2438  -2004   1812       O  
ATOM   3147  CB  VAL I 651       8.817 -34.928  85.831  1.00129.91           C  
ANISOU 3147  CB  VAL I 651    16922  22798   9640  -2406  -2267   1808       C  
ATOM   3148  CG1 VAL I 651       9.480 -34.760  84.474  1.00131.12           C  
ANISOU 3148  CG1 VAL I 651    16975  22899   9946  -2410  -2285   1785       C  
ATOM   3149  CG2 VAL I 651       8.522 -36.398  86.112  1.00127.27           C  
ANISOU 3149  CG2 VAL I 651    16645  22489   9224  -2391  -2388   1821       C  
ATOM   3150  N   ILE I 652      10.792 -32.245  86.395  1.00121.39           N  
ANISOU 3150  N   ILE I 652    15715  21729   8681  -2458  -2034   1852       N  
ATOM   3151  CA  ILE I 652      11.030 -30.806  86.471  1.00117.41           C  
ANISOU 3151  CA  ILE I 652    15144  21282   8184  -2483  -1938   1829       C  
ATOM   3152  C   ILE I 652      10.648 -30.106  85.169  1.00108.98           C  
ANISOU 3152  C   ILE I 652    14014  20234   7160  -2457  -1950   1804       C  
ATOM   3153  O   ILE I 652      11.493 -29.509  84.492  1.00109.94           O  
ANISOU 3153  O   ILE I 652    14064  20366   7342  -2474  -1930   1806       O  
ATOM   3154  CB  ILE I 652      12.495 -30.536  86.873  1.00109.93           C  
ANISOU 3154  CB  ILE I 652    14149  20322   7299  -2536  -1875   1842       C  
ATOM   3155  CG1 ILE I 652      13.467 -31.397  86.051  1.00108.44           C  
ANISOU 3155  CG1 ILE I 652    13933  20047   7222  -2536  -1932   1867       C  
ATOM   3156  CG2 ILE I 652      12.697 -30.789  88.361  1.00104.41           C  
ANISOU 3156  CG2 ILE I 652    13513  19607   6550  -2560  -1802   1866       C  
ATOM   3157  CD1 ILE I 652      14.768 -30.699  85.712  1.00103.35           C  
ANISOU 3157  CD1 ILE I 652    13205  19401   6662  -2595  -1859   1845       C  
ATOM   3158  N   SER I 653       9.361 -30.149  84.825  1.00115.27           N  
ANISOU 3158  N   SER I 653    14844  21030   7924  -2416  -1966   1782       N  
ATOM   3159  CA  SER I 653       8.882 -29.485  83.619  1.00117.53           C  
ANISOU 3159  CA  SER I 653    15084  21313   8259  -2376  -1951   1775       C  
ATOM   3160  C   SER I 653       8.859 -27.971  83.807  1.00112.96           C  
ANISOU 3160  C   SER I 653    14437  20834   7651  -2356  -1878   1791       C  
ATOM   3161  O   SER I 653       8.747 -27.461  84.925  1.00108.43           O  
ANISOU 3161  O   SER I 653    13855  20329   7012  -2373  -1834   1779       O  
ATOM   3162  CB  SER I 653       7.484 -29.987  83.253  1.00122.78           C  
ANISOU 3162  CB  SER I 653    15804  21932   8914  -2344  -1960   1736       C  
ATOM   3163  OG  SER I 653       6.779 -29.032  82.476  1.00124.93           O  
ANISOU 3163  OG  SER I 653    16040  22206   9223  -2289  -1897   1744       O  
ATOM   3164  N   GLY I 654       8.974 -27.245  82.691  1.00105.02           N  
ANISOU 3164  N   GLY I 654    13374  19840   6689  -2318  -1864   1819       N  
ATOM   3165  CA  GLY I 654       8.906 -25.802  82.703  1.00103.76           C  
ANISOU 3165  CA  GLY I 654    13135  19799   6491  -2280  -1817   1848       C  
ATOM   3166  C   GLY I 654      10.060 -25.178  81.956  1.00103.59           C  
ANISOU 3166  C   GLY I 654    13047  19831   6481  -2298  -1818   1877       C  
ATOM   3167  O   GLY I 654      10.724 -25.826  81.143  1.00103.27           O  
ANISOU 3167  O   GLY I 654    13028  19706   6506  -2324  -1839   1880       O  
ATOM   3168  N   GLY I 655      10.298 -23.902  82.234  1.00106.52           N  
ANISOU 3168  N   GLY I 655    13331  20356   6786  -2287  -1794   1890       N  
ATOM   3169  CA  GLY I 655      11.347 -23.150  81.564  1.00113.45           C  
ANISOU 3169  CA  GLY I 655    14143  21325   7638  -2309  -1792   1912       C  
ATOM   3170  C   GLY I 655      11.070 -22.875  80.102  1.00120.01           C  
ANISOU 3170  C   GLY I 655    14984  22117   8496  -2225  -1787   1993       C  
ATOM   3171  O   GLY I 655      11.968 -23.028  79.265  1.00120.86           O  
ANISOU 3171  O   GLY I 655    15100  22192   8629  -2262  -1783   2003       O  
ATOM   3172  N   ALA I 656       9.848 -22.467  79.772  1.00121.21           N  
ANISOU 3172  N   ALA I 656    15140  22261   8655  -2113  -1768   2054       N  
ATOM   3173  CA  ALA I 656       9.432 -22.249  78.393  1.00122.25           C  
ANISOU 3173  CA  ALA I 656    15298  22323   8831  -2019  -1733   2144       C  
ATOM   3174  C   ALA I 656       9.231 -20.761  78.144  1.00128.93           C  
ANISOU 3174  C   ALA I 656    16058  23340   9589  -1915  -1722   2244       C  
ATOM   3175  O   ALA I 656       8.530 -20.089  78.908  1.00130.59           O  
ANISOU 3175  O   ALA I 656    16204  23653   9760  -1859  -1725   2253       O  
ATOM   3176  CB  ALA I 656       8.143 -23.014  78.084  1.00117.39           C  
ANISOU 3176  CB  ALA I 656    14756  21533   8313  -1965  -1694   2138       C  
ATOM   3177  N   SER I 657       9.846 -20.250  77.074  1.00128.92           N  
ANISOU 3177  N   SER I 657    23076  12498  13409  -3383  -2109   1320       N  
ATOM   3178  CA  SER I 657       9.634 -18.854  76.701  1.00131.33           C  
ANISOU 3178  CA  SER I 657    23305  12946  13650  -3523  -2216   1201       C  
ATOM   3179  C   SER I 657       8.243 -18.641  76.120  1.00136.33           C  
ANISOU 3179  C   SER I 657    23852  13715  14232  -3437  -2462   1238       C  
ATOM   3180  O   SER I 657       7.722 -17.518  76.152  1.00135.75           O  
ANISOU 3180  O   SER I 657    23702  13752  14124  -3499  -2590   1136       O  
ATOM   3181  CB  SER I 657      10.700 -18.405  75.702  1.00128.99           C  
ANISOU 3181  CB  SER I 657    23041  12649  13318  -3634  -2203   1140       C  
ATOM   3182  OG  SER I 657      11.801 -17.808  76.365  1.00128.70           O  
ANISOU 3182  OG  SER I 657    23043  12552  13306  -3794  -2011   1020       O  
ATOM   3183  N   ASP I 658       7.637 -19.708  75.589  1.00135.66           N  
ANISOU 3183  N   ASP I 658    23773  13621  14152  -3285  -2538   1365       N  
ATOM   3184  CA  ASP I 658       6.285 -19.636  75.042  1.00135.27           C  
ANISOU 3184  CA  ASP I 658    23658  13674  14063  -3197  -2751   1402       C  
ATOM   3185  C   ASP I 658       5.288 -19.264  76.136  1.00137.10           C  
ANISOU 3185  C   ASP I 658    23803  13965  14324  -3190  -2762   1338       C  
ATOM   3186  O   ASP I 658       4.404 -18.431  75.925  1.00141.39           O  
ANISOU 3186  O   ASP I 658    24254  14610  14858  -3180  -2937   1260       O  
ATOM   3187  CB  ASP I 658       5.948 -20.991  74.400  1.00129.73           C  
ANISOU 3187  CB  ASP I 658    22976  12949  13365  -3057  -2781   1530       C  
ATOM   3188  CG  ASP I 658       4.527 -21.082  73.823  1.00125.37           C  
ANISOU 3188  CG  ASP I 658    22372  12486  12776  -2969  -2975   1571       C  
ATOM   3189  OD1 ASP I 658       3.782 -20.083  73.753  1.00124.71           O  
ANISOU 3189  OD1 ASP I 658    22244  12470  12671  -2990  -3119   1505       O  
ATOM   3190  OD2 ASP I 658       4.148 -22.205  73.431  1.00123.44           O  
ANISOU 3190  OD2 ASP I 658    22126  12244  12533  -2865  -2990   1657       O  
ATOM   3191  N   LEU I 659       5.455 -19.825  77.330  1.00139.16           N  
ANISOU 3191  N   LEU I 659    24103  14153  14620  -3208  -2572   1349       N  
ATOM   3192  CA  LEU I 659       4.508 -19.598  78.417  1.00133.36           C  
ANISOU 3192  CA  LEU I 659    23299  13474  13898  -3246  -2531   1264       C  
ATOM   3193  C   LEU I 659       4.761 -18.251  79.093  1.00131.60           C  
ANISOU 3193  C   LEU I 659    22984  13320  13699  -3411  -2474   1050       C  
ATOM   3194  O   LEU I 659       3.815 -17.541  79.486  1.00132.35           O  
ANISOU 3194  O   LEU I 659    22924  13539  13822  -3438  -2547    895       O  
ATOM   3195  CB  LEU I 659       4.609 -20.760  79.410  1.00128.67           C  
ANISOU 3195  CB  LEU I 659    22847  12754  13290  -3232  -2344   1366       C  
ATOM   3196  CG  LEU I 659       3.933 -22.119  79.137  1.00121.81           C  
ANISOU 3196  CG  LEU I 659    22035  11860  12388  -3070  -2414   1537       C  
ATOM   3197  CD1 LEU I 659       4.027 -22.660  77.706  1.00120.39           C  
ANISOU 3197  CD1 LEU I 659    21824  11706  12212  -2927  -2579   1638       C  
ATOM   3198  CD2 LEU I 659       4.577 -23.125  80.053  1.00118.18           C  
ANISOU 3198  CD2 LEU I 659    21783  11222  11899  -3058  -2244   1646       C  
ATOM   3199  N   LYS I 660       6.040 -17.882  79.211  1.00130.54           N  
ANISOU 3199  N   LYS I 660    22923  13114  13562  -3522  -2344   1013       N  
ATOM   3200  CA  LYS I 660       6.413 -16.537  79.636  1.00130.77           C  
ANISOU 3200  CA  LYS I 660    22854  13231  13601  -3686  -2317    797       C  
ATOM   3201  C   LYS I 660       5.819 -15.481  78.707  1.00130.12           C  
ANISOU 3201  C   LYS I 660    22631  13304  13505  -3632  -2618    712       C  
ATOM   3202  O   LYS I 660       5.397 -14.411  79.163  1.00131.62           O  
ANISOU 3202  O   LYS I 660    22657  13627  13727  -3694  -2692    499       O  
ATOM   3203  CB  LYS I 660       7.941 -16.438  79.705  1.00127.85           C  
ANISOU 3203  CB  LYS I 660    22607  12747  13222  -3808  -2135    792       C  
ATOM   3204  CG  LYS I 660       8.553 -15.183  79.107  1.00124.65           C  
ANISOU 3204  CG  LYS I 660    22138  12441  12782  -3914  -2240    658       C  
ATOM   3205  CD  LYS I 660      10.041 -15.366  78.857  1.00121.04           C  
ANISOU 3205  CD  LYS I 660    21820  11856  12313  -4008  -2069    689       C  
ATOM   3206  CE  LYS I 660      10.547 -14.377  77.821  1.00120.31           C  
ANISOU 3206  CE  LYS I 660    21714  11857  12140  -4088  -2229    622       C  
ATOM   3207  NZ  LYS I 660      10.403 -12.967  78.275  1.00122.01           N  
ANISOU 3207  NZ  LYS I 660    21797  12232  12329  -4217  -2312    403       N  
ATOM   3208  N   ALA I 661       5.740 -15.777  77.405  1.00128.88           N  
ANISOU 3208  N   ALA I 661    22543  13127  13298  -3515  -2804    861       N  
ATOM   3209  CA  ALA I 661       5.060 -14.875  76.482  1.00130.14           C  
ANISOU 3209  CA  ALA I 661    22641  13386  13421  -3444  -3117    816       C  
ATOM   3210  C   ALA I 661       3.542 -15.011  76.558  1.00131.53           C  
ANISOU 3210  C   ALA I 661    22694  13628  13654  -3297  -3274    796       C  
ATOM   3211  O   ALA I 661       2.822 -14.066  76.222  1.00134.62           O  
ANISOU 3211  O   ALA I 661    22985  14107  14059  -3227  -3530    684       O  
ATOM   3212  CB  ALA I 661       5.538 -15.123  75.051  1.00127.41           C  
ANISOU 3212  CB  ALA I 661    22463  12975  12974  -3422  -3227    968       C  
ATOM   3213  N   LYS I 662       3.040 -16.175  76.978  1.00132.00           N  
ANISOU 3213  N   LYS I 662    22767  13640  13745  -3241  -3138    894       N  
ATOM   3214  CA  LYS I 662       1.607 -16.365  77.173  1.00127.63           C  
ANISOU 3214  CA  LYS I 662    22092  13153  13247  -3133  -3239    851       C  
ATOM   3215  C   LYS I 662       1.074 -15.541  78.338  1.00131.47           C  
ANISOU 3215  C   LYS I 662    22374  13757  13823  -3210  -3189    586       C  
ATOM   3216  O   LYS I 662      -0.137 -15.305  78.413  1.00130.13           O  
ANISOU 3216  O   LYS I 662    22047  13672  13726  -3123  -3320    468       O  
ATOM   3217  CB  LYS I 662       1.306 -17.851  77.390  1.00123.87           C  
ANISOU 3217  CB  LYS I 662    21703  12606  12755  -3084  -3092   1018       C  
ATOM   3218  CG  LYS I 662       0.134 -18.390  76.586  1.00119.77           C  
ANISOU 3218  CG  LYS I 662    21166  12108  12232  -2934  -3268   1102       C  
ATOM   3219  CD  LYS I 662       0.069 -19.910  76.674  1.00120.38           C  
ANISOU 3219  CD  LYS I 662    21346  12123  12268  -2890  -3139   1278       C  
ATOM   3220  CE  LYS I 662      -0.525 -20.383  77.989  1.00124.33           C  
ANISOU 3220  CE  LYS I 662    21814  12644  12781  -2948  -2968   1220       C  
ATOM   3221  NZ  LYS I 662      -0.407 -21.860  78.140  1.00124.35           N  
ANISOU 3221  NZ  LYS I 662    21962  12570  12717  -2901  -2865   1407       N  
ATOM   3222  N   ALA I 663       1.951 -15.126  79.256  1.00130.31           N  
ANISOU 3222  N   ALA I 663    22216  13615  13680  -3384  -2982    464       N  
ATOM   3223  CA  ALA I 663       1.555 -14.158  80.286  1.00132.99           C  
ANISOU 3223  CA  ALA I 663    22331  14095  14103  -3495  -2932    149       C  
ATOM   3224  C   ALA I 663       1.133 -12.799  79.705  1.00129.38           C  
ANISOU 3224  C   ALA I 663    21681  13775  13704  -3397  -3264    -41       C  
ATOM   3225  O   ALA I 663       0.382 -12.049  80.359  1.00129.30           O  
ANISOU 3225  O   ALA I 663    21412  13912  13804  -3409  -3313   -336       O  
ATOM   3226  CB  ALA I 663       2.695 -13.960  81.286  1.00127.86           C  
ANISOU 3226  CB  ALA I 663    21740  13410  13429  -3727  -2633     53       C  
ATOM   3227  N   ARG I 664       1.595 -12.461  78.492  1.00130.47           N  
ANISOU 3227  N   ARG I 664    21946  13864  13764  -3304  -3502    104       N  
ATOM   3228  CA  ARG I 664       1.135 -11.236  77.839  1.00134.88           C  
ANISOU 3228  CA  ARG I 664    22390  14514  14344  -3177  -3876    -33       C  
ATOM   3229  C   ARG I 664      -0.364 -11.266  77.577  1.00141.70           C  
ANISOU 3229  C   ARG I 664    23120  15410  15309  -2971  -4100    -90       C  
ATOM   3230  O   ARG I 664      -1.005 -10.210  77.538  1.00144.93           O  
ANISOU 3230  O   ARG I 664    23335  15922  15809  -2854  -4377   -315       O  
ATOM   3231  CB  ARG I 664       1.873 -11.007  76.519  1.00133.08           C  
ANISOU 3231  CB  ARG I 664    22408  14192  13966  -3146  -4073    170       C  
ATOM   3232  CG  ARG I 664       3.325 -10.572  76.628  1.00130.49           C  
ANISOU 3232  CG  ARG I 664    22176  13861  13544  -3341  -3936    155       C  
ATOM   3233  CD  ARG I 664       3.865 -10.290  75.234  1.00130.03           C  
ANISOU 3233  CD  ARG I 664    22368  13719  13317  -3325  -4153    329       C  
ATOM   3234  NE  ARG I 664       5.321 -10.257  75.166  1.00130.95           N  
ANISOU 3234  NE  ARG I 664    22628  13796  13330  -3530  -3955    368       N  
ATOM   3235  CZ  ARG I 664       6.004 -10.207  74.026  1.00131.50           C  
ANISOU 3235  CZ  ARG I 664    22943  13784  13235  -3591  -4036    512       C  
ATOM   3236  NH1 ARG I 664       7.330 -10.178  74.042  1.00133.39           N  
ANISOU 3236  NH1 ARG I 664    23285  13997  13402  -3792  -3826    508       N  
ATOM   3237  NH2 ARG I 664       5.358 -10.183  72.868  1.00128.85           N  
ANISOU 3237  NH2 ARG I 664    22767  13386  12804  -3472  -4310    646       N  
ATOM   3238  N   ARG I 665      -0.938 -12.459  77.387  1.00138.88           N  
ANISOU 3238  N   ARG I 665    22857  14966  14944  -2915  -3997     95       N  
ATOM   3239  CA  ARG I 665      -2.387 -12.579  77.266  1.00140.85           C  
ANISOU 3239  CA  ARG I 665    22970  15246  15300  -2748  -4152     17       C  
ATOM   3240  C   ARG I 665      -3.091 -12.203  78.562  1.00147.39           C  
ANISOU 3240  C   ARG I 665    23486  16229  16287  -2813  -4024   -324       C  
ATOM   3241  O   ARG I 665      -4.214 -11.686  78.527  1.00151.65           O  
ANISOU 3241  O   ARG I 665    23813  16843  16965  -2664  -4230   -530       O  
ATOM   3242  CB  ARG I 665      -2.772 -13.999  76.860  1.00129.66           C  
ANISOU 3242  CB  ARG I 665    21718  13722  13824  -2713  -4032    273       C  
ATOM   3243  CG  ARG I 665      -2.361 -14.396  75.457  1.00122.60           C  
ANISOU 3243  CG  ARG I 665    21092  12694  12794  -2643  -4173    553       C  
ATOM   3244  CD  ARG I 665      -2.347 -15.906  75.333  1.00116.28           C  
ANISOU 3244  CD  ARG I 665    20426  11822  11932  -2668  -3965    771       C  
ATOM   3245  NE  ARG I 665      -3.553 -16.490  75.913  1.00108.95           N  
ANISOU 3245  NE  ARG I 665    19364  10945  11087  -2621  -3899    697       N  
ATOM   3246  CZ  ARG I 665      -4.586 -16.937  75.208  1.00100.87           C  
ANISOU 3246  CZ  ARG I 665    18358   9894  10076  -2495  -4032    757       C  
ATOM   3247  NH1 ARG I 665      -5.638 -17.451  75.831  1.00100.75           N  
ANISOU 3247  NH1 ARG I 665    18212   9937  10132  -2483  -3943    664       N  
ATOM   3248  NH2 ARG I 665      -4.570 -16.872  73.885  1.00101.41           N  
ANISOU 3248  NH2 ARG I 665    18592   9869  10070  -2408  -4235    899       N  
ATOM   3249  N   TRP I 666      -2.461 -12.469  79.712  1.00143.16           N  
ANISOU 3249  N   TRP I 666    22928  15732  15735  -3044  -3674   -406       N  
ATOM   3250  CA  TRP I 666      -2.994 -11.956  80.969  1.00149.30           C  
ANISOU 3250  CA  TRP I 666    23413  16671  16643  -3170  -3520   -784       C  
ATOM   3251  C   TRP I 666      -2.915 -10.440  81.001  1.00152.85           C  
ANISOU 3251  C   TRP I 666    23607  17272  17199  -3124  -3760  -1100       C  
ATOM   3252  O   TRP I 666      -3.834  -9.772  81.489  1.00155.57           O  
ANISOU 3252  O   TRP I 666    23625  17771  17714  -3076  -3848  -1459       O  
ATOM   3253  CB  TRP I 666      -2.234 -12.530  82.162  1.00152.29           C  
ANISOU 3253  CB  TRP I 666    23894  17023  16945  -3462  -3082   -792       C  
ATOM   3254  CG  TRP I 666      -2.545 -13.950  82.501  1.00155.13           C  
ANISOU 3254  CG  TRP I 666    24451  17271  17221  -3522  -2840   -581       C  
ATOM   3255  CD1 TRP I 666      -1.640 -14.952  82.641  1.00157.22           C  
ANISOU 3255  CD1 TRP I 666    25021  17373  17343  -3614  -2623   -297       C  
ATOM   3256  CD2 TRP I 666      -3.834 -14.533  82.756  1.00156.69           C  
ANISOU 3256  CD2 TRP I 666    24561  17509  17464  -3492  -2803   -648       C  
ATOM   3257  NE1 TRP I 666      -2.273 -16.128  82.956  1.00158.16           N  
ANISOU 3257  NE1 TRP I 666    25262  17429  17401  -3629  -2482   -166       N  
ATOM   3258  CE2 TRP I 666      -3.621 -15.898  83.034  1.00157.35           C  
ANISOU 3258  CE2 TRP I 666    24929  17455  17403  -3575  -2573   -376       C  
ATOM   3259  CE3 TRP I 666      -5.144 -14.039  82.776  1.00157.27           C  
ANISOU 3259  CE3 TRP I 666    24342  17719  17695  -3396  -2949   -927       C  
ATOM   3260  CZ2 TRP I 666      -4.665 -16.773  83.325  1.00155.79           C  
ANISOU 3260  CZ2 TRP I 666    24748  17264  17181  -3589  -2482   -360       C  
ATOM   3261  CZ3 TRP I 666      -6.178 -14.911  83.063  1.00157.25           C  
ANISOU 3261  CZ3 TRP I 666    24342  17718  17687  -3419  -2830   -926       C  
ATOM   3262  CH2 TRP I 666      -5.932 -16.262  83.337  1.00156.02           C  
ANISOU 3262  CH2 TRP I 666    24490  17436  17356  -3528  -2596   -638       C  
ATOM   3263  N   ASP I 667      -1.816  -9.876  80.489  1.00156.86           N  
ANISOU 3263  N   ASP I 667    24245  17746  17608  -3139  -3874   -998       N  
ATOM   3264  CA  ASP I 667      -1.754  -8.418  80.396  1.00154.67           C  
ANISOU 3264  CA  ASP I 667    23745  17616  17407  -3065  -4170  -1281       C  
ATOM   3265  C   ASP I 667      -2.663  -7.860  79.304  1.00149.62           C  
ANISOU 3265  C   ASP I 667    23068  16954  16827  -2741  -4660  -1268       C  
ATOM   3266  O   ASP I 667      -3.156  -6.733  79.433  1.00149.32           O  
ANISOU 3266  O   ASP I 667    22748  17060  16928  -2610  -4941  -1593       O  
ATOM   3267  CB  ASP I 667      -0.318  -7.949  80.181  1.00152.80           C  
ANISOU 3267  CB  ASP I 667    23674  17356  17026  -3200  -4148  -1188       C  
ATOM   3268  CG  ASP I 667       0.512  -8.054  81.435  1.00151.98           C  
ANISOU 3268  CG  ASP I 667    23524  17308  16912  -3515  -3716  -1342       C  
ATOM   3269  OD2 ASP I 667       1.556  -8.736  81.420  1.00149.68           O  
ANISOU 3269  OD2 ASP I 667    23507  16875  16489  -3661  -3467  -1095       O  
ATOM   3270  OD1 ASP I 667       0.109  -7.438  82.441  1.00154.39           O  
ANISOU 3270  OD1 ASP I 667    23516  17796  17348  -3620  -3621  -1735       O  
ATOM   3271  N   GLU I 668      -2.903  -8.613  78.235  1.00150.34           N  
ANISOU 3271  N   GLU I 668    23440  16862  16820  -2604  -4774   -919       N  
ATOM   3272  CA  GLU I 668      -3.713  -8.111  77.125  1.00152.18           C  
ANISOU 3272  CA  GLU I 668    23721  17022  17080  -2311  -5233   -873       C  
ATOM   3273  C   GLU I 668      -5.204  -8.129  77.452  1.00148.63           C  
ANISOU 3273  C   GLU I 668    22993  16630  16849  -2138  -5324  -1111       C  
ATOM   3274  O   GLU I 668      -5.619  -8.648  78.488  1.00145.81           O  
ANISOU 3274  O   GLU I 668    22432  16372  16597  -2275  -5003  -1285       O  
ATOM   3275  CB  GLU I 668      -3.449  -8.927  75.857  1.00155.00           C  
ANISOU 3275  CB  GLU I 668    24487  17160  17245  -2269  -5284   -446       C  
ATOM   3276  CG  GLU I 668      -4.398  -8.631  74.710  1.00158.94           C  
ANISOU 3276  CG  GLU I 668    25107  17532  17750  -1995  -5699   -364       C  
ATOM   3277  CD  GLU I 668      -3.770  -8.897  73.355  1.00159.05           C  
ANISOU 3277  CD  GLU I 668    25558  17352  17520  -2011  -5814     -7       C  
ATOM   3278  OE1 GLU I 668      -4.193  -8.261  72.367  1.00160.66           O  
ANISOU 3278  OE1 GLU I 668    25939  17436  17666  -1828  -6209     51       O  
ATOM   3279  OE2 GLU I 668      -2.852  -9.740  73.281  1.00157.36           O  
ANISOU 3279  OE2 GLU I 668    25521  17097  17173  -2213  -5509    200       O  
TER    3280      GLU I 668                                                      
ATOM   3281  N   ASN J 469       9.741 -45.111  14.365  1.00 95.44           N  
ANISOU 3281  N   ASN J 469    13878   8975  13408  -1818   5261  -1734       N  
ATOM   3282  CA  ASN J 469       9.780 -43.656  14.451  1.00100.50           C  
ANISOU 3282  CA  ASN J 469    14720   9558  13907  -1569   5223  -1539       C  
ATOM   3283  C   ASN J 469       8.784 -43.142  15.486  1.00106.31           C  
ANISOU 3283  C   ASN J 469    15427  10414  14551  -1478   5026  -1551       C  
ATOM   3284  O   ASN J 469       8.837 -41.982  15.893  1.00109.01           O  
ANISOU 3284  O   ASN J 469    15882  10786  14751  -1250   4895  -1434       O  
ATOM   3285  CB  ASN J 469       9.488 -43.028  13.085  1.00102.83           C  
ANISOU 3285  CB  ASN J 469    15243   9565  14261  -1552   5562  -1421       C  
ATOM   3286  CG  ASN J 469      10.549 -43.353  12.050  1.00103.84           C  
ANISOU 3286  CG  ASN J 469    15411   9601  14444  -1544   5679  -1402       C  
ATOM   3287  OD1 ASN J 469      11.745 -43.313  12.337  1.00103.01           O  
ANISOU 3287  OD1 ASN J 469    15299   9559  14282  -1471   5572  -1352       O  
ATOM   3288  ND2 ASN J 469      10.114 -43.675  10.837  1.00107.39           N  
ANISOU 3288  ND2 ASN J 469    15902   9899  15003  -1614   5909  -1450       N  
ATOM   3289  N   TYR J 470       7.876 -44.020  15.913  1.00107.23           N  
ANISOU 3289  N   TYR J 470    15383  10611  14747  -1653   4999  -1710       N  
ATOM   3290  CA  TYR J 470       6.799 -43.665  16.826  1.00108.15           C  
ANISOU 3290  CA  TYR J 470    15470  10820  14804  -1586   4829  -1741       C  
ATOM   3291  C   TYR J 470       7.117 -44.016  18.275  1.00101.54           C  
ANISOU 3291  C   TYR J 470    14460  10238  13882  -1539   4499  -1798       C  
ATOM   3292  O   TYR J 470       6.234 -43.913  19.134  1.00 96.54           O  
ANISOU 3292  O   TYR J 470    13772   9697  13212  -1507   4347  -1844       O  
ATOM   3293  CB  TYR J 470       5.495 -44.358  16.411  1.00120.08           C  
ANISOU 3293  CB  TYR J 470    16920  12265  16441  -1785   5009  -1883       C  
ATOM   3294  CG  TYR J 470       5.130 -44.261  14.939  1.00131.80           C  
ANISOU 3294  CG  TYR J 470    18543  13500  18034  -1878   5392  -1859       C  
ATOM   3295  CD2 TYR J 470       4.262 -43.276  14.479  1.00135.49           C  
ANISOU 3295  CD2 TYR J 470    19212  13790  18478  -1758   5527  -1758       C  
ATOM   3296  CD1 TYR J 470       5.611 -45.190  14.017  1.00134.12           C  
ANISOU 3296  CD1 TYR J 470    18758  13764  18437  -2033   5558  -1959       C  
ATOM   3297  CE2 TYR J 470       3.914 -43.196  13.137  1.00137.87           C  
ANISOU 3297  CE2 TYR J 470    19650  13861  18874  -1827   5908  -1728       C  
ATOM   3298  CE1 TYR J 470       5.270 -45.117  12.677  1.00136.61           C  
ANISOU 3298  CE1 TYR J 470    19189  13886  18830  -2056   5840  -1960       C  
ATOM   3299  CZ  TYR J 470       4.420 -44.120  12.243  1.00139.51           C  
ANISOU 3299  CZ  TYR J 470    19766  14059  19181  -1956   6028  -1841       C  
ATOM   3300  OH  TYR J 470       4.078 -44.047  10.912  1.00143.24           O  
ANISOU 3300  OH  TYR J 470    20363  14327  19734  -1969   6334  -1840       O  
ATOM   3301  N   LEU J 471       8.352 -44.421  18.570  1.00 99.67           N  
ANISOU 3301  N   LEU J 471    14146  10110  13616  -1523   4397  -1790       N  
ATOM   3302  CA  LEU J 471       8.689 -44.995  19.869  1.00 96.07           C  
ANISOU 3302  CA  LEU J 471    13519   9882  13103  -1505   4138  -1850       C  
ATOM   3303  C   LEU J 471       9.223 -43.960  20.857  1.00 88.91           C  
ANISOU 3303  C   LEU J 471    12656   9086  12041  -1278   3904  -1742       C  
ATOM   3304  O   LEU J 471       8.851 -43.982  22.039  1.00 89.83           O  
ANISOU 3304  O   LEU J 471    12682   9346  12104  -1233   3703  -1775       O  
ATOM   3305  CB  LEU J 471       9.719 -46.117  19.692  1.00101.64           C  
ANISOU 3305  CB  LEU J 471    14104  10650  13863  -1611   4164  -1917       C  
ATOM   3306  CG  LEU J 471       9.448 -47.183  18.622  1.00107.34           C  
ANISOU 3306  CG  LEU J 471    14762  11275  14748  -1852   4404  -2056       C  
ATOM   3307  CD1 LEU J 471      10.190 -46.889  17.317  1.00106.56           C  
ANISOU 3307  CD1 LEU J 471    14801  10981  14704  -1860   4626  -1981       C  
ATOM   3308  CD2 LEU J 471       9.799 -48.570  19.140  1.00108.23           C  
ANISOU 3308  CD2 LEU J 471    14664  11566  14893  -1965   4308  -2213       C  
ATOM   3309  N   TRP J 472      10.093 -43.059  20.391  1.00 79.99           N  
ANISOU 3309  N   TRP J 472    11657   7897  10840  -1137   3936  -1623       N  
ATOM   3310  CA  TRP J 472      10.715 -42.083  21.280  1.00 72.18           C  
ANISOU 3310  CA  TRP J 472    10687   7033   9705   -938   3725  -1552       C  
ATOM   3311  C   TRP J 472       9.703 -41.092  21.845  1.00 73.53           C  
ANISOU 3311  C   TRP J 472    10908   7221   9807   -824   3621  -1543       C  
ATOM   3312  O   TRP J 472       9.866 -40.625  22.978  1.00 76.58           O  
ANISOU 3312  O   TRP J 472    11236   7759  10104   -719   3408  -1549       O  
ATOM   3313  CB  TRP J 472      11.834 -41.343  20.548  1.00 66.35           C  
ANISOU 3313  CB  TRP J 472    10072   6241   8899   -815   3798  -1448       C  
ATOM   3314  CG  TRP J 472      11.354 -40.514  19.397  1.00 67.78           C  
ANISOU 3314  CG  TRP J 472    10443   6231   9080   -753   3999  -1368       C  
ATOM   3315  CD1 TRP J 472      11.000 -40.960  18.156  1.00 73.87           C  
ANISOU 3315  CD1 TRP J 472    11296   6799   9970   -876   4271  -1357       C  
ATOM   3316  CD2 TRP J 472      11.140 -39.098  19.390  1.00 68.15           C  
ANISOU 3316  CD2 TRP J 472    10623   6267   9002   -546   3962  -1290       C  
ATOM   3317  NE1 TRP J 472      10.600 -39.906  17.372  1.00 77.69           N  
ANISOU 3317  NE1 TRP J 472    11979   7128  10412   -748   4418  -1251       N  
ATOM   3318  CE2 TRP J 472      10.673 -38.752  18.107  1.00 73.15           C  
ANISOU 3318  CE2 TRP J 472    11437   6676   9678   -533   4225  -1209       C  
ATOM   3319  CE3 TRP J 472      11.301 -38.088  20.343  1.00 67.29           C  
ANISOU 3319  CE3 TRP J 472    10496   6320   8751   -368   3744  -1289       C  
ATOM   3320  CZ2 TRP J 472      10.370 -37.439  17.750  1.00 73.60           C  
ANISOU 3320  CZ2 TRP J 472    11666   6672   9626   -322   4271  -1110       C  
ATOM   3321  CZ3 TRP J 472      11.002 -36.786  19.988  1.00 67.94           C  
ANISOU 3321  CZ3 TRP J 472    10725   6363   8726   -173   3778  -1221       C  
ATOM   3322  CH2 TRP J 472      10.541 -36.473  18.704  1.00 71.17           C  
ANISOU 3322  CH2 TRP J 472    11323   6552   9167   -138   4038  -1123       C  
ATOM   3323  N   ARG J 473       8.654 -40.770  21.084  1.00 73.38           N  
ANISOU 3323  N   ARG J 473    11000   7046   9836   -843   3778  -1533       N  
ATOM   3324  CA  ARG J 473       7.606 -39.894  21.600  1.00 66.38           C  
ANISOU 3324  CA  ARG J 473    10160   6171   8891   -730   3687  -1533       C  
ATOM   3325  C   ARG J 473       6.835 -40.569  22.731  1.00 63.07           C  
ANISOU 3325  C   ARG J 473     9583   5880   8499   -812   3524  -1635       C  
ATOM   3326  O   ARG J 473       6.501 -39.925  23.736  1.00 66.17           O  
ANISOU 3326  O   ARG J 473     9946   6384   8811   -695   3338  -1643       O  
ATOM   3327  CB  ARG J 473       6.663 -39.493  20.466  1.00 64.33           C  
ANISOU 3327  CB  ARG J 473    10068   5690   8685   -732   3924  -1491       C  
ATOM   3328  CG  ARG J 473       7.271 -38.566  19.422  1.00 63.87           C  
ANISOU 3328  CG  ARG J 473    10203   5497   8570   -589   4087  -1360       C  
ATOM   3329  CD  ARG J 473       6.197 -37.718  18.754  1.00 65.78           C  
ANISOU 3329  CD  ARG J 473    10631   5558   8806   -486   4250  -1291       C  
ATOM   3330  NE  ARG J 473       6.763 -36.676  17.901  1.00 71.13           N  
ANISOU 3330  NE  ARG J 473    11503   6133   9390   -291   4385  -1146       N  
ATOM   3331  CZ  ARG J 473       6.983 -36.816  16.597  1.00 83.85           C  
ANISOU 3331  CZ  ARG J 473    13261   7530  11068   -332   4676  -1053       C  
ATOM   3332  NH1 ARG J 473       6.686 -37.958  15.990  1.00 85.81           N  
ANISOU 3332  NH1 ARG J 473    13465   7652  11488   -583   4868  -1114       N  
ATOM   3333  NH2 ARG J 473       7.499 -35.814  15.898  1.00 90.44           N  
ANISOU 3333  NH2 ARG J 473    14278   8289  11795   -119   4786   -904       N  
ATOM   3334  N   GLU J 474       6.563 -41.871  22.588  1.00 64.97           N  
ANISOU 3334  N   GLU J 474     9716   6118   8852  -1009   3599  -1722       N  
ATOM   3335  CA  GLU J 474       5.946 -42.641  23.664  1.00 67.65           C  
ANISOU 3335  CA  GLU J 474     9899   6597   9208  -1082   3450  -1819       C  
ATOM   3336  C   GLU J 474       6.847 -42.693  24.892  1.00 68.20           C  
ANISOU 3336  C   GLU J 474     9868   6850   9195  -1002   3233  -1802       C  
ATOM   3337  O   GLU J 474       6.368 -42.598  26.032  1.00 67.11           O  
ANISOU 3337  O   GLU J 474     9661   6825   9012   -952   3065  -1827       O  
ATOM   3338  CB  GLU J 474       5.628 -44.055  23.169  1.00 70.59           C  
ANISOU 3338  CB  GLU J 474    10164   6952   9705  -1304   3588  -1934       C  
ATOM   3339  CG  GLU J 474       5.107 -45.009  24.237  1.00 74.73           C  
ANISOU 3339  CG  GLU J 474    10518   7640  10238  -1377   3446  -2042       C  
ATOM   3340  CD  GLU J 474       3.631 -44.821  24.528  1.00 78.45           C  
ANISOU 3340  CD  GLU J 474    10996   8094  10720  -1383   3423  -2099       C  
ATOM   3341  OE1 GLU J 474       3.195 -45.167  25.646  1.00 76.76           O  
ANISOU 3341  OE1 GLU J 474    10679   8017  10469  -1366   3260  -2146       O  
ATOM   3342  OE2 GLU J 474       2.905 -44.341  23.635  1.00 80.63           O  
ANISOU 3342  OE2 GLU J 474    11387   8207  11041  -1399   3579  -2092       O  
ATOM   3343  N   GLU J 475       8.160 -42.820  24.676  1.00 61.77           N  
ANISOU 3343  N   GLU J 475     9052   6055   8361   -985   3247  -1755       N  
ATOM   3344  CA  GLU J 475       9.100 -42.835  25.796  1.00 53.64           C  
ANISOU 3344  CA  GLU J 475     7944   5178   7260   -908   3070  -1733       C  
ATOM   3345  C   GLU J 475       9.120 -41.493  26.523  1.00 54.24           C  
ANISOU 3345  C   GLU J 475     8071   5312   7227   -735   2922  -1688       C  
ATOM   3346  O   GLU J 475       9.135 -41.449  27.761  1.00 49.88           O  
ANISOU 3346  O   GLU J 475     7438   4882   6631   -692   2761  -1704       O  
ATOM   3347  CB  GLU J 475      10.496 -43.202  25.296  1.00 48.36           C  
ANISOU 3347  CB  GLU J 475     7279   4502   6596   -918   3135  -1695       C  
ATOM   3348  CG  GLU J 475      10.726 -44.700  25.186  1.00 54.94           C  
ANISOU 3348  CG  GLU J 475     7996   5365   7513  -1065   3199  -1767       C  
ATOM   3349  CD  GLU J 475      12.104 -45.043  24.659  1.00 69.50           C  
ANISOU 3349  CD  GLU J 475     9848   7198   9359  -1058   3266  -1728       C  
ATOM   3350  OE1 GLU J 475      13.009 -44.187  24.747  1.00 70.39           O  
ANISOU 3350  OE1 GLU J 475    10031   7320   9392   -930   3216  -1645       O  
ATOM   3351  OE2 GLU J 475      12.278 -46.171  24.150  1.00 76.89           O  
ANISOU 3351  OE2 GLU J 475    10714   8128  10374  -1178   3368  -1795       O  
ATOM   3352  N   ASN J 476       9.101 -40.389  25.768  1.00 49.61           N  
ANISOU 3352  N   ASN J 476     7616   4641   6593   -632   2986  -1638       N  
ATOM   3353  CA  ASN J 476       9.063 -39.063  26.380  1.00 41.92           C  
ANISOU 3353  CA  ASN J 476     6680   3740   5508   -460   2854  -1624       C  
ATOM   3354  C   ASN J 476       7.767 -38.840  27.152  1.00 47.09           C  
ANISOU 3354  C   ASN J 476     7300   4432   6161   -440   2758  -1674       C  
ATOM   3355  O   ASN J 476       7.779 -38.250  28.242  1.00 54.67           O  
ANISOU 3355  O   ASN J 476     8206   5515   7051   -350   2596  -1697       O  
ATOM   3356  CB  ASN J 476       9.240 -37.981  25.312  1.00 43.34           C  
ANISOU 3356  CB  ASN J 476     7013   3824   5629   -338   2965  -1567       C  
ATOM   3357  CG  ASN J 476      10.655 -37.922  24.769  1.00 43.51           C  
ANISOU 3357  CG  ASN J 476     7069   3849   5616   -309   3019  -1516       C  
ATOM   3358  OD1 ASN J 476      11.609 -38.289  25.452  1.00 42.41           O  
ANISOU 3358  OD1 ASN J 476     6837   3817   5461   -328   2920  -1530       O  
ATOM   3359  ND2 ASN J 476      10.798 -37.445  23.538  1.00 45.06           N  
ANISOU 3359  ND2 ASN J 476     7406   3916   5796   -254   3188  -1450       N  
ATOM   3360  N   ALA J 477       6.640 -39.318  26.611  1.00 42.53           N  
ANISOU 3360  N   ALA J 477     6748   3748   5662   -529   2866  -1700       N  
ATOM   3361  CA  ALA J 477       5.365 -39.186  27.313  1.00 51.45           C  
ANISOU 3361  CA  ALA J 477     7846   4908   6793   -513   2782  -1750       C  
ATOM   3362  C   ALA J 477       5.356 -39.981  28.615  1.00 63.79           C  
ANISOU 3362  C   ALA J 477     9259   6614   8364   -574   2636  -1796       C  
ATOM   3363  O   ALA J 477       4.883 -39.488  29.650  1.00 73.97           O  
ANISOU 3363  O   ALA J 477    10513   7983   9607   -508   2514  -1821       O  
ATOM   3364  CB  ALA J 477       4.219 -39.631  26.405  1.00 46.33           C  
ANISOU 3364  CB  ALA J 477     7257   4108   6237   -613   2950  -1778       C  
ATOM   3365  N   GLU J 478       5.895 -41.204  28.590  1.00 65.14           N  
ANISOU 3365  N   GLU J 478     9348   6807   8595   -705   2676  -1812       N  
ATOM   3366  CA  GLU J 478       5.930 -42.008  29.808  1.00 64.66           C  
ANISOU 3366  CA  GLU J 478     9159   6874   8536   -747   2560  -1845       C  
ATOM   3367  C   GLU J 478       6.890 -41.419  30.837  1.00 59.19           C  
ANISOU 3367  C   GLU J 478     8446   6264   7777   -668   2461  -1813       C  
ATOM   3368  O   GLU J 478       6.633 -41.499  32.047  1.00 57.95           O  
ANISOU 3368  O   GLU J 478     8225   6185   7609   -671   2380  -1839       O  
ATOM   3369  CB  GLU J 478       6.307 -43.449  29.469  1.00 68.20           C  
ANISOU 3369  CB  GLU J 478     9528   7327   9057   -892   2648  -1884       C  
ATOM   3370  CG  GLU J 478       5.199 -44.224  28.768  1.00 80.56           C  
ANISOU 3370  CG  GLU J 478    11072   8831  10707  -1026   2764  -1970       C  
ATOM   3371  CD  GLU J 478       5.529 -45.692  28.566  1.00 86.10           C  
ANISOU 3371  CD  GLU J 478    11663   9579  11472  -1171   2835  -2047       C  
ATOM   3372  OE1 GLU J 478       5.656 -46.122  27.400  1.00 87.50           O  
ANISOU 3372  OE1 GLU J 478    11855   9670  11722  -1280   2998  -2085       O  
ATOM   3373  OE2 GLU J 478       5.612 -46.426  29.571  1.00 84.85           O  
ANISOU 3373  OE2 GLU J 478    11402   9545  11291  -1174   2738  -2081       O  
ATOM   3374  N   GLN J 479       7.978 -40.789  30.378  1.00 59.44           N  
ANISOU 3374  N   GLN J 479     8538   6280   7769   -602   2480  -1764       N  
ATOM   3375  CA  GLN J 479       8.876 -40.108  31.306  1.00 51.73           C  
ANISOU 3375  CA  GLN J 479     7546   5376   6731   -535   2401  -1754       C  
ATOM   3376  C   GLN J 479       8.214 -38.896  31.944  1.00 55.88           C  
ANISOU 3376  C   GLN J 479     8096   5940   7197   -438   2322  -1787       C  
ATOM   3377  O   GLN J 479       8.427 -38.623  33.130  1.00 59.20           O  
ANISOU 3377  O   GLN J 479     8462   6436   7595   -430   2248  -1813       O  
ATOM   3378  CB  GLN J 479      10.153 -39.670  30.602  1.00 43.64           C  
ANISOU 3378  CB  GLN J 479     6580   4332   5668   -480   2441  -1710       C  
ATOM   3379  CG  GLN J 479      11.331 -39.616  31.544  1.00 46.98           C  
ANISOU 3379  CG  GLN J 479     6960   4824   6067   -474   2393  -1709       C  
ATOM   3380  CD  GLN J 479      11.420 -38.340  32.357  1.00 54.96           C  
ANISOU 3380  CD  GLN J 479     7979   5900   7003   -385   2310  -1748       C  
ATOM   3381  OE1 GLN J 479      11.074 -37.259  31.882  1.00 64.70           O  
ANISOU 3381  OE1 GLN J 479     9274   7138   8169   -278   2292  -1764       O  
ATOM   3382  NE2 GLN J 479      11.880 -38.465  33.598  1.00 51.08           N  
ANISOU 3382  NE2 GLN J 479     7423   5462   6521   -422   2266  -1772       N  
ATOM   3383  N   GLN J 480       7.445 -38.132  31.165  1.00 57.72           N  
ANISOU 3383  N   GLN J 480     8412   6119   7401   -357   2347  -1788       N  
ATOM   3384  CA  GLN J 480       6.738 -36.997  31.748  1.00 63.18           C  
ANISOU 3384  CA  GLN J 480     9120   6859   8026   -243   2269  -1830       C  
ATOM   3385  C   GLN J 480       5.676 -37.457  32.739  1.00 61.90           C  
ANISOU 3385  C   GLN J 480     8887   6728   7905   -305   2219  -1873       C  
ATOM   3386  O   GLN J 480       5.443 -36.783  33.750  1.00 68.23           O  
ANISOU 3386  O   GLN J 480     9654   7608   8661   -250   2136  -1914       O  
ATOM   3387  CB  GLN J 480       6.131 -36.131  30.645  1.00 79.50           C  
ANISOU 3387  CB  GLN J 480    11300   8857  10050   -120   2321  -1817       C  
ATOM   3388  CG  GLN J 480       7.145 -35.215  29.967  1.00 95.43           C  
ANISOU 3388  CG  GLN J 480    13383  10896  11979      6   2337  -1792       C  
ATOM   3389  CD  GLN J 480       6.557 -34.451  28.795  1.00110.67           C  
ANISOU 3389  CD  GLN J 480    15432  12749  13870    135   2417  -1763       C  
ATOM   3390  OE1 GLN J 480       5.366 -34.556  28.505  1.00115.59           O  
ANISOU 3390  OE1 GLN J 480    16103  13278  14539    122   2478  -1764       O  
ATOM   3391  NE2 GLN J 480       7.395 -33.672  28.116  1.00114.28           N  
ANISOU 3391  NE2 GLN J 480    15959  13217  14245    245   2469  -1738       N  
ATOM   3392  N   ALA J 481       5.063 -38.620  32.492  1.00 62.07           N  
ANISOU 3392  N   ALA J 481     8876   6701   8006   -422   2272  -1874       N  
ATOM   3393  CA  ALA J 481       4.154 -39.202  33.480  1.00 57.23           C  
ANISOU 3393  CA  ALA J 481     8184   6134   7425   -484   2226  -1919       C  
ATOM   3394  C   ALA J 481       4.889 -39.571  34.768  1.00 54.24           C  
ANISOU 3394  C   ALA J 481     7714   5849   7045   -527   2167  -1921       C  
ATOM   3395  O   ALA J 481       4.391 -39.314  35.877  1.00 58.92           O  
ANISOU 3395  O   ALA J 481     8262   6502   7624   -514   2104  -1954       O  
ATOM   3396  CB  ALA J 481       3.457 -40.428  32.892  1.00 55.18           C  
ANISOU 3396  CB  ALA J 481     7899   5825   7240   -599   2296  -1939       C  
ATOM   3397  N   LEU J 482       6.076 -40.174  34.637  1.00 54.50           N  
ANISOU 3397  N   LEU J 482     7726   5886   7095   -574   2198  -1885       N  
ATOM   3398  CA  LEU J 482       6.882 -40.509  35.811  1.00 46.65           C  
ANISOU 3398  CA  LEU J 482     6665   4957   6104   -606   2165  -1880       C  
ATOM   3399  C   LEU J 482       7.280 -39.261  36.592  1.00 48.67           C  
ANISOU 3399  C   LEU J 482     6930   5256   6307   -535   2109  -1898       C  
ATOM   3400  O   LEU J 482       7.212 -39.243  37.826  1.00 56.83           O  
ANISOU 3400  O   LEU J 482     7907   6341   7346   -557   2074  -1922       O  
ATOM   3401  CB  LEU J 482       8.124 -41.290  35.387  1.00 50.19           C  
ANISOU 3401  CB  LEU J 482     7107   5388   6574   -646   2219  -1838       C  
ATOM   3402  CG  LEU J 482       8.009 -42.813  35.348  1.00 55.60           C  
ANISOU 3402  CG  LEU J 482     7731   6088   7307   -724   2252  -1843       C  
ATOM   3403  CD1 LEU J 482       9.366 -43.438  35.071  1.00 70.53           C  
ANISOU 3403  CD1 LEU J 482     9620   7972   9205   -735   2296  -1803       C  
ATOM   3404  CD2 LEU J 482       7.453 -43.323  36.661  1.00 52.20           C  
ANISOU 3404  CD2 LEU J 482     7231   5722   6881   -746   2206  -1872       C  
ATOM   3405  N   ALA J 483       7.685 -38.203  35.883  1.00 45.36           N  
ANISOU 3405  N   ALA J 483     6580   4823   5832   -446   2106  -1897       N  
ATOM   3406  CA  ALA J 483       8.067 -36.958  36.543  1.00 50.33           C  
ANISOU 3406  CA  ALA J 483     7211   5517   6397   -367   2048  -1940       C  
ATOM   3407  C   ALA J 483       6.880 -36.299  37.232  1.00 55.09           C  
ANISOU 3407  C   ALA J 483     7793   6165   6972   -318   1986  -1995       C  
ATOM   3408  O   ALA J 483       7.042 -35.703  38.304  1.00 62.70           O  
ANISOU 3408  O   ALA J 483     8710   7198   7915   -311   1942  -2044       O  
ATOM   3409  CB  ALA J 483       8.696 -35.996  35.537  1.00 55.70           C  
ANISOU 3409  CB  ALA J 483     7970   6193   7000   -255   2053  -1938       C  
ATOM   3410  N   ALA J 484       5.683 -36.408  36.645  1.00 50.42           N  
ANISOU 3410  N   ALA J 484     7238   5534   6388   -289   1993  -1993       N  
ATOM   3411  CA  ALA J 484       4.487 -35.891  37.300  1.00 54.77           C  
ANISOU 3411  CA  ALA J 484     7772   6123   6917   -239   1940  -2044       C  
ATOM   3412  C   ALA J 484       4.196 -36.644  38.593  1.00 57.14           C  
ANISOU 3412  C   ALA J 484     7978   6461   7272   -345   1926  -2058       C  
ATOM   3413  O   ALA J 484       3.888 -36.027  39.622  1.00 64.35           O  
ANISOU 3413  O   ALA J 484     8848   7439   8162   -321   1878  -2106       O  
ATOM   3414  CB  ALA J 484       3.291 -35.973  36.354  1.00 62.09           C  
ANISOU 3414  CB  ALA J 484     8764   6977   7850   -196   1971  -2038       C  
ATOM   3415  N   LYS J 485       4.302 -37.980  38.559  1.00 54.17           N  
ANISOU 3415  N   LYS J 485     7566   6053   6963   -454   1971  -2023       N  
ATOM   3416  CA  LYS J 485       4.074 -38.763  39.773  1.00 53.66           C  
ANISOU 3416  CA  LYS J 485     7419   6031   6938   -533   1964  -2033       C  
ATOM   3417  C   LYS J 485       5.117 -38.454  40.843  1.00 49.53           C  
ANISOU 3417  C   LYS J 485     6855   5549   6415   -558   1960  -2038       C  
ATOM   3418  O   LYS J 485       4.797 -38.407  42.038  1.00 50.58           O  
ANISOU 3418  O   LYS J 485     6933   5725   6559   -584   1945  -2068       O  
ATOM   3419  CB  LYS J 485       4.064 -40.257  39.452  1.00 56.56           C  
ANISOU 3419  CB  LYS J 485     7760   6375   7354   -616   2009  -2006       C  
ATOM   3420  CG  LYS J 485       2.677 -40.883  39.503  1.00 65.35           C  
ANISOU 3420  CG  LYS J 485     8850   7498   8484   -639   2001  -2042       C  
ATOM   3421  CD  LYS J 485       1.964 -40.542  40.805  1.00 72.74           C  
ANISOU 3421  CD  LYS J 485     9740   8492   9405   -623   1955  -2079       C  
ATOM   3422  CE  LYS J 485       0.491 -40.921  40.748  1.00 72.72           C  
ANISOU 3422  CE  LYS J 485     9730   8494   9408   -626   1943  -2125       C  
ATOM   3423  NZ  LYS J 485      -0.224 -40.545  42.001  1.00 71.37           N  
ANISOU 3423  NZ  LYS J 485     9519   8380   9219   -604   1902  -2160       N  
ATOM   3424  N   ARG J 486       6.361 -38.206  40.431  1.00 43.69           N  
ANISOU 3424  N   ARG J 486     6143   4791   5666   -553   1984  -2015       N  
ATOM   3425  CA  ARG J 486       7.413 -37.892  41.394  1.00 47.03           C  
ANISOU 3425  CA  ARG J 486     6534   5239   6097   -588   1998  -2031       C  
ATOM   3426  C   ARG J 486       7.220 -36.510  42.005  1.00 54.97           C  
ANISOU 3426  C   ARG J 486     7522   6306   7057   -537   1949  -2107       C  
ATOM   3427  O   ARG J 486       7.457 -36.323  43.204  1.00 63.98           O  
ANISOU 3427  O   ARG J 486     8606   7479   8223   -591   1961  -2146       O  
ATOM   3428  CB  ARG J 486       8.774 -38.015  40.719  1.00 41.01           C  
ANISOU 3428  CB  ARG J 486     5811   4438   5333   -592   2041  -1994       C  
ATOM   3429  CG  ARG J 486       9.098 -39.451  40.417  1.00 47.22           C  
ANISOU 3429  CG  ARG J 486     6595   5180   6166   -647   2095  -1930       C  
ATOM   3430  CD  ARG J 486      10.461 -39.663  39.820  1.00 53.84           C  
ANISOU 3430  CD  ARG J 486     7471   5980   7006   -650   2145  -1891       C  
ATOM   3431  NE  ARG J 486      10.467 -40.990  39.214  1.00 63.27           N  
ANISOU 3431  NE  ARG J 486     8665   7145   8231   -677   2184  -1842       N  
ATOM   3432  CZ  ARG J 486      11.393 -41.446  38.382  1.00 72.59           C  
ANISOU 3432  CZ  ARG J 486     9876   8289   9415   -674   2230  -1801       C  
ATOM   3433  NH1 ARG J 486      12.411 -40.681  38.018  1.00 77.64           N  
ANISOU 3433  NH1 ARG J 486    10560   8911  10029   -644   2245  -1797       N  
ATOM   3434  NH2 ARG J 486      11.278 -42.669  37.897  1.00 75.58           N  
ANISOU 3434  NH2 ARG J 486    10239   8661   9818   -696   2259  -1776       N  
ATOM   3435  N   GLU J 487       6.777 -35.535  41.205  1.00 57.89           N  
ANISOU 3435  N   GLU J 487     7942   6697   7357   -426   1901  -2134       N  
ATOM   3436  CA  GLU J 487       6.466 -34.218  41.752  1.00 62.66           C  
ANISOU 3436  CA  GLU J 487     8528   7383   7897   -352   1846  -2218       C  
ATOM   3437  C   GLU J 487       5.289 -34.286  42.720  1.00 62.24           C  
ANISOU 3437  C   GLU J 487     8418   7363   7869   -375   1824  -2250       C  
ATOM   3438  O   GLU J 487       5.296 -33.619  43.762  1.00 58.36           O  
ANISOU 3438  O   GLU J 487     7865   6939   7372   -394   1809  -2320       O  
ATOM   3439  CB  GLU J 487       6.177 -33.233  40.621  1.00 73.45           C  
ANISOU 3439  CB  GLU J 487     9977   8768   9161   -189   1805  -2232       C  
ATOM   3440  CG  GLU J 487       6.388 -31.777  41.001  1.00 85.58           C  
ANISOU 3440  CG  GLU J 487    11505  10414  10598    -85   1753  -2324       C  
ATOM   3441  CD  GLU J 487       7.853 -31.426  41.171  1.00 98.37           C  
ANISOU 3441  CD  GLU J 487    13107  12065  12205   -124   1771  -2359       C  
ATOM   3442  OE1 GLU J 487       8.695 -31.995  40.441  1.00101.68           O  
ANISOU 3442  OE1 GLU J 487    13567  12421  12646   -152   1812  -2300       O  
ATOM   3443  OE2 GLU J 487       8.164 -30.582  42.036  1.00102.86           O  
ANISOU 3443  OE2 GLU J 487    13617  12723  12744   -136   1752  -2452       O  
ATOM   3444  N   ASP J 488       4.285 -35.111  42.400  1.00 62.28           N  
ANISOU 3444  N   ASP J 488     8438   7324   7902   -384   1829  -2208       N  
ATOM   3445  CA  ASP J 488       3.158 -35.310  43.309  1.00 67.75           C  
ANISOU 3445  CA  ASP J 488     9080   8046   8617   -406   1813  -2236       C  
ATOM   3446  C   ASP J 488       3.604 -35.943  44.623  1.00 67.43           C  
ANISOU 3446  C   ASP J 488     8960   8020   8641   -525   1853  -2239       C  
ATOM   3447  O   ASP J 488       3.159 -35.533  45.706  1.00 72.95           O  
ANISOU 3447  O   ASP J 488     9601   8771   9346   -543   1843  -2292       O  
ATOM   3448  CB  ASP J 488       2.097 -36.179  42.630  1.00 70.30           C  
ANISOU 3448  CB  ASP J 488     9436   8316   8958   -402   1820  -2200       C  
ATOM   3449  CG  ASP J 488       0.854 -36.351  43.477  1.00 78.43           C  
ANISOU 3449  CG  ASP J 488    10423   9380   9998   -410   1800  -2235       C  
ATOM   3450  OD1 ASP J 488       0.155 -35.347  43.725  1.00 84.55           O  
ANISOU 3450  OD1 ASP J 488    11203  10197  10723   -322   1759  -2287       O  
ATOM   3451  OD2 ASP J 488       0.578 -37.495  43.898  1.00 80.46           O  
ANISOU 3451  OD2 ASP J 488    10642   9627  10301   -489   1826  -2215       O  
ATOM   3452  N   LEU J 489       4.493 -36.938  44.546  1.00 64.79           N  
ANISOU 3452  N   LEU J 489     8628   7636   8352   -599   1907  -2181       N  
ATOM   3453  CA  LEU J 489       4.984 -37.593  45.755  1.00 59.90           C  
ANISOU 3453  CA  LEU J 489     7960   7013   7787   -690   1963  -2174       C  
ATOM   3454  C   LEU J 489       5.819 -36.636  46.599  1.00 66.90           C  
ANISOU 3454  C   LEU J 489     8810   7926   8683   -727   1985  -2235       C  
ATOM   3455  O   LEU J 489       5.698 -36.627  47.831  1.00 72.34           O  
ANISOU 3455  O   LEU J 489     9446   8632   9408   -788   2020  -2271       O  
ATOM   3456  CB  LEU J 489       5.778 -38.847  45.375  1.00 36.08           C  
ANISOU 3456  CB  LEU J 489     4971   3938   4801   -730   2018  -2100       C  
ATOM   3457  CG  LEU J 489       6.139 -39.926  46.407  1.00 35.94           C  
ANISOU 3457  CG  LEU J 489     4934   3898   4824   -788   2083  -2068       C  
ATOM   3458  CD1 LEU J 489       6.350 -41.243  45.689  1.00 44.08           C  
ANISOU 3458  CD1 LEU J 489     5994   4900   5854   -778   2102  -2006       C  
ATOM   3459  CD2 LEU J 489       7.392 -39.594  47.200  1.00 36.35           C  
ANISOU 3459  CD2 LEU J 489     4986   3915   4910   -841   2154  -2076       C  
ATOM   3460  N   GLU J 490       6.656 -35.814  45.955  1.00 62.31           N  
ANISOU 3460  N   GLU J 490     8254   7352   8067   -694   1972  -2259       N  
ATOM   3461  CA  GLU J 490       7.434 -34.814  46.687  1.00 69.02           C  
ANISOU 3461  CA  GLU J 490     9061   8245   8920   -732   1989  -2344       C  
ATOM   3462  C   GLU J 490       6.529 -33.790  47.360  1.00 72.09           C  
ANISOU 3462  C   GLU J 490     9388   8724   9279   -704   1940  -2439       C  
ATOM   3463  O   GLU J 490       6.782 -33.387  48.503  1.00 82.65           O  
ANISOU 3463  O   GLU J 490    10653  10095  10656   -787   1980  -2515       O  
ATOM   3464  CB  GLU J 490       8.418 -34.107  45.753  1.00 79.43           C  
ANISOU 3464  CB  GLU J 490    10424   9571  10184   -679   1972  -2362       C  
ATOM   3465  CG  GLU J 490       9.544 -34.976  45.225  1.00 88.64           C  
ANISOU 3465  CG  GLU J 490    11641  10654  11383   -717   2034  -2285       C  
ATOM   3466  CD  GLU J 490      10.366 -34.271  44.161  1.00 89.39           C  
ANISOU 3466  CD  GLU J 490    11790  10764  11411   -643   2008  -2300       C  
ATOM   3467  OE1 GLU J 490      10.613 -33.055  44.308  1.00 90.10           O  
ANISOU 3467  OE1 GLU J 490    11858  10931  11443   -605   1972  -2397       O  
ATOM   3468  OE2 GLU J 490      10.755 -34.931  43.174  1.00 85.47           O  
ANISOU 3468  OE2 GLU J 490    11354  10209  10911   -618   2025  -2220       O  
ATOM   3469  N   LYS J 491       5.456 -33.375  46.679  1.00 76.31           N  
ANISOU 3469  N   LYS J 491     9953   9296   9747   -589   1863  -2441       N  
ATOM   3470  CA  LYS J 491       4.555 -32.385  47.262  1.00 64.72           C  
ANISOU 3470  CA  LYS J 491     8433   7920   8238   -540   1815  -2529       C  
ATOM   3471  C   LYS J 491       3.791 -32.956  48.452  1.00 54.34           C  
ANISOU 3471  C   LYS J 491     7053   6606   6989   -622   1848  -2535       C  
ATOM   3472  O   LYS J 491       3.627 -32.277  49.471  1.00 55.25           O  
ANISOU 3472  O   LYS J 491     7086   6792   7116   -664   1856  -2626       O  
ATOM   3473  CB  LYS J 491       3.592 -31.860  46.198  1.00 61.66           C  
ANISOU 3473  CB  LYS J 491     8120   7553   7756   -375   1742  -2517       C  
ATOM   3474  CG  LYS J 491       4.112 -30.633  45.464  1.00 65.44           C  
ANISOU 3474  CG  LYS J 491     8643   8095   8127   -251   1700  -2567       C  
ATOM   3475  CD  LYS J 491       3.226 -30.250  44.290  1.00 66.74           C  
ANISOU 3475  CD  LYS J 491     8916   8251   8193    -65   1655  -2532       C  
ATOM   3476  CE  LYS J 491       3.875 -29.159  43.448  1.00 64.23           C  
ANISOU 3476  CE  LYS J 491     8666   7990   7747     83   1630  -2561       C  
ATOM   3477  NZ  LYS J 491       3.048 -28.790  42.266  1.00 61.06           N  
ANISOU 3477  NZ  LYS J 491     8390   7569   7241    289   1610  -2517       N  
ATOM   3478  N   LYS J 492       3.345 -34.210  48.359  1.00 48.19           N  
ANISOU 3478  N   LYS J 492     6304   5758   6248   -648   1872  -2449       N  
ATOM   3479  CA  LYS J 492       2.613 -34.797  49.480  1.00 49.36           C  
ANISOU 3479  CA  LYS J 492     6402   5911   6441   -708   1904  -2453       C  
ATOM   3480  C   LYS J 492       3.538 -35.123  50.652  1.00 48.46           C  
ANISOU 3480  C   LYS J 492     6245   5768   6401   -834   2000  -2466       C  
ATOM   3481  O   LYS J 492       3.134 -34.991  51.821  1.00 55.86           O  
ANISOU 3481  O   LYS J 492     7122   6733   7369   -888   2036  -2517       O  
ATOM   3482  CB  LYS J 492       1.841 -36.024  48.994  1.00 38.80           C  
ANISOU 3482  CB  LYS J 492     5111   4525   5105   -685   1898  -2373       C  
ATOM   3483  CG  LYS J 492       0.645 -35.627  48.127  1.00 46.22           C  
ANISOU 3483  CG  LYS J 492     6089   5486   5985   -574   1826  -2384       C  
ATOM   3484  CD  LYS J 492      -0.358 -36.746  47.907  1.00 44.76           C  
ANISOU 3484  CD  LYS J 492     5925   5273   5807   -570   1824  -2343       C  
ATOM   3485  CE  LYS J 492       0.311 -38.005  47.389  1.00 44.90           C  
ANISOU 3485  CE  LYS J 492     5971   5233   5855   -621   1863  -2272       C  
ATOM   3486  NZ  LYS J 492      -0.683 -39.076  47.101  1.00 47.25           N  
ANISOU 3486  NZ  LYS J 492     6280   5524   6150   -616   1856  -2256       N  
ATOM   3487  N   GLN J 493       4.789 -35.503  50.368  1.00 44.82           N  
ANISOU 3487  N   GLN J 493     5818   5244   5967   -879   2053  -2425       N  
ATOM   3488  CA  GLN J 493       5.786 -35.631  51.427  1.00 48.68           C  
ANISOU 3488  CA  GLN J 493     6283   5689   6526   -993   2161  -2448       C  
ATOM   3489  C   GLN J 493       6.052 -34.289  52.098  1.00 52.99           C  
ANISOU 3489  C   GLN J 493     6746   6306   7081  -1045   2169  -2580       C  
ATOM   3490  O   GLN J 493       6.230 -34.225  53.319  1.00 61.78           O  
ANISOU 3490  O   GLN J 493     7809   7406   8258  -1148   2258  -2634       O  
ATOM   3491  CB  GLN J 493       7.084 -36.204  50.861  1.00 55.99           C  
ANISOU 3491  CB  GLN J 493     7271   6533   7470  -1013   2214  -2383       C  
ATOM   3492  CG  GLN J 493       7.150 -37.718  50.808  1.00 61.63           C  
ANISOU 3492  CG  GLN J 493     8047   7168   8201  -1006   2261  -2271       C  
ATOM   3493  CD  GLN J 493       8.472 -38.211  50.254  1.00 68.77           C  
ANISOU 3493  CD  GLN J 493     9012   7997   9120  -1016   2316  -2213       C  
ATOM   3494  OE1 GLN J 493       9.053 -37.590  49.363  1.00 71.44           O  
ANISOU 3494  OE1 GLN J 493     9362   8350   9432   -993   2280  -2229       O  
ATOM   3495  NE2 GLN J 493       8.954 -39.334  50.775  1.00 72.35           N  
ANISOU 3495  NE2 GLN J 493     9511   8370   9607  -1035   2406  -2144       N  
ATOM   3496  N   GLN J 494       6.076 -33.205  51.315  1.00 54.81           N  
ANISOU 3496  N   GLN J 494     6964   6617   7245   -972   2083  -2642       N  
ATOM   3497  CA  GLN J 494       6.245 -31.873  51.888  1.00 55.05           C  
ANISOU 3497  CA  GLN J 494     6901   6751   7265  -1006   2074  -2789       C  
ATOM   3498  C   GLN J 494       5.044 -31.474  52.739  1.00 53.46           C  
ANISOU 3498  C   GLN J 494     6622   6628   7064  -1005   2051  -2854       C  
ATOM   3499  O   GLN J 494       5.205 -30.778  53.747  1.00 51.01           O  
ANISOU 3499  O   GLN J 494     6211   6380   6793  -1099   2097  -2975       O  
ATOM   3500  CB  GLN J 494       6.481 -30.853  50.772  1.00 57.34           C  
ANISOU 3500  CB  GLN J 494     7213   7121   7454   -889   1978  -2832       C  
ATOM   3501  CG  GLN J 494       6.744 -29.430  51.245  1.00 63.45           C  
ANISOU 3501  CG  GLN J 494     7883   8032   8193   -908   1956  -3001       C  
ATOM   3502  CD  GLN J 494       8.207 -29.188  51.572  1.00 64.24           C  
ANISOU 3502  CD  GLN J 494     7949   8118   8342  -1029   2037  -3075       C  
ATOM   3503  OE1 GLN J 494       9.085 -29.409  50.739  1.00 71.28           O  
ANISOU 3503  OE1 GLN J 494     8918   8955   9209   -998   2039  -3022       O  
ATOM   3504  NE2 GLN J 494       8.474 -28.730  52.791  1.00 56.25           N  
ANISOU 3504  NE2 GLN J 494     6820   7151   7400  -1173   2113  -3205       N  
ATOM   3505  N   LEU J 495       3.843 -31.914  52.354  1.00 51.16           N  
ANISOU 3505  N   LEU J 495     6371   6335   6732   -908   1989  -2785       N  
ATOM   3506  CA  LEU J 495       2.663 -31.697  53.191  1.00 54.43           C  
ANISOU 3506  CA  LEU J 495     6722   6810   7149   -904   1977  -2834       C  
ATOM   3507  C   LEU J 495       2.807 -32.397  54.537  1.00 42.06           C  
ANISOU 3507  C   LEU J 495     5118   5186   5677  -1042   2093  -2835       C  
ATOM   3508  O   LEU J 495       2.511 -31.813  55.590  1.00 42.99           O  
ANISOU 3508  O   LEU J 495     5144   5366   5826  -1110   2129  -2937       O  
ATOM   3509  CB  LEU J 495       1.401 -32.183  52.474  1.00 41.10           C  
ANISOU 3509  CB  LEU J 495     5101   5110   5403   -778   1904  -2755       C  
ATOM   3510  CG  LEU J 495       0.985 -31.483  51.180  1.00 41.12           C  
ANISOU 3510  CG  LEU J 495     5166   5152   5307   -619   1807  -2749       C  
ATOM   3511  CD1 LEU J 495      -0.375 -31.984  50.715  1.00 56.06           C  
ANISOU 3511  CD1 LEU J 495     7118   7020   7163   -522   1766  -2690       C  
ATOM   3512  CD2 LEU J 495       0.977 -29.975  51.363  1.00 58.88           C  
ANISOU 3512  CD2 LEU J 495     7347   7532   7492   -566   1763  -2875       C  
ATOM   3513  N   LEU J 496       3.262 -33.656  54.520  1.00 41.29           N  
ANISOU 3513  N   LEU J 496     5097   4971   5621  -1078   2159  -2724       N  
ATOM   3514  CA  LEU J 496       3.498 -34.368  55.776  1.00 41.61           C  
ANISOU 3514  CA  LEU J 496     5135   4936   5739  -1187   2286  -2712       C  
ATOM   3515  C   LEU J 496       4.580 -33.686  56.608  1.00 46.48           C  
ANISOU 3515  C   LEU J 496     5692   5538   6430  -1325   2394  -2813       C  
ATOM   3516  O   LEU J 496       4.465 -33.596  57.837  1.00 48.74           O  
ANISOU 3516  O   LEU J 496     5931   5810   6780  -1424   2490  -2875       O  
ATOM   3517  CB  LEU J 496       3.875 -35.825  55.507  1.00 40.74           C  
ANISOU 3517  CB  LEU J 496     5129   4711   5639  -1169   2334  -2575       C  
ATOM   3518  CG  LEU J 496       3.862 -36.752  56.730  1.00 41.06           C  
ANISOU 3518  CG  LEU J 496     5201   4669   5730  -1226   2456  -2536       C  
ATOM   3519  CD1 LEU J 496       3.277 -38.091  56.358  1.00 40.16           C  
ANISOU 3519  CD1 LEU J 496     5162   4530   5566  -1130   2424  -2423       C  
ATOM   3520  CD2 LEU J 496       5.258 -36.956  57.319  1.00 41.77           C  
ANISOU 3520  CD2 LEU J 496     5330   4642   5897  -1329   2604  -2528       C  
ATOM   3521  N   ARG J 497       5.637 -33.201  55.952  1.00 48.45           N  
ANISOU 3521  N   ARG J 497     5945   5788   6674  -1339   2387  -2840       N  
ATOM   3522  CA  ARG J 497       6.728 -32.551  56.670  1.00 55.34           C  
ANISOU 3522  CA  ARG J 497     6759   6650   7618  -1480   2496  -2952       C  
ATOM   3523  C   ARG J 497       6.294 -31.219  57.273  1.00 58.09           C  
ANISOU 3523  C   ARG J 497     6965   7144   7964  -1527   2468  -3128       C  
ATOM   3524  O   ARG J 497       6.772 -30.841  58.348  1.00 56.45           O  
ANISOU 3524  O   ARG J 497     6683   6927   7840  -1679   2590  -3239       O  
ATOM   3525  CB  ARG J 497       7.920 -32.363  55.729  1.00 58.10           C  
ANISOU 3525  CB  ARG J 497     7151   6979   7947  -1466   2484  -2942       C  
ATOM   3526  CG  ARG J 497       8.635 -33.666  55.390  1.00 61.92           C  
ANISOU 3526  CG  ARG J 497     7760   7310   8456  -1457   2556  -2791       C  
ATOM   3527  CD  ARG J 497       9.952 -33.436  54.667  1.00 64.54           C  
ANISOU 3527  CD  ARG J 497     8127   7612   8782  -1468   2574  -2798       C  
ATOM   3528  NE  ARG J 497      10.995 -32.942  55.561  1.00 69.23           N  
ANISOU 3528  NE  ARG J 497     8677   8168   9459  -1619   2716  -2908       N  
ATOM   3529  CZ  ARG J 497      11.470 -31.702  55.538  1.00 71.43           C  
ANISOU 3529  CZ  ARG J 497     8862   8552   9724  -1669   2695  -3067       C  
ATOM   3530  NH1 ARG J 497      10.998 -30.825  54.661  1.00 75.05           N  
ANISOU 3530  NH1 ARG J 497     9277   9159  10079  -1557   2533  -3120       N  
ATOM   3531  NH2 ARG J 497      12.419 -31.339  56.390  1.00 70.06           N  
ANISOU 3531  NH2 ARG J 497     8646   8337   9636  -1825   2845  -3178       N  
ATOM   3532  N   ALA J 498       5.386 -30.505  56.608  1.00 60.93           N  
ANISOU 3532  N   ALA J 498     7285   7637   8227  -1400   2318  -3160       N  
ATOM   3533  CA  ALA J 498       4.851 -29.279  57.186  1.00 61.42           C  
ANISOU 3533  CA  ALA J 498     7206   7858   8271  -1422   2281  -3327       C  
ATOM   3534  C   ALA J 498       3.917 -29.584  58.349  1.00 60.15           C  
ANISOU 3534  C   ALA J 498     7001   7690   8164  -1480   2341  -3342       C  
ATOM   3535  O   ALA J 498       3.924 -28.871  59.358  1.00 68.43           O  
ANISOU 3535  O   ALA J 498     7926   8812   9264  -1598   2404  -3491       O  
ATOM   3536  CB  ALA J 498       4.126 -28.464  56.115  1.00 65.35           C  
ANISOU 3536  CB  ALA J 498     7701   8491   8638  -1239   2114  -3342       C  
ATOM   3537  N   ALA J 499       3.113 -30.643  58.232  1.00 62.71           N  
ANISOU 3537  N   ALA J 499     7421   7932   8474  -1404   2326  -3200       N  
ATOM   3538  CA  ALA J 499       2.196 -30.994  59.310  1.00 60.14           C  
ANISOU 3538  CA  ALA J 499     7069   7598   8185  -1441   2382  -3208       C  
ATOM   3539  C   ALA J 499       2.890 -31.676  60.484  1.00 46.56           C  
ANISOU 3539  C   ALA J 499     5374   5739   6577  -1600   2566  -3199       C  
ATOM   3540  O   ALA J 499       2.275 -31.813  61.546  1.00 47.14           O  
ANISOU 3540  O   ALA J 499     5420   5803   6690  -1653   2637  -3231       O  
ATOM   3541  CB  ALA J 499       1.078 -31.889  58.774  1.00 58.78           C  
ANISOU 3541  CB  ALA J 499     6988   7398   7946  -1299   2303  -3073       C  
ATOM   3542  N   THR J 500       4.145 -32.102  60.322  1.00 46.56           N  
ANISOU 3542  N   THR J 500     5440   5624   6628  -1667   2654  -3154       N  
ATOM   3543  CA  THR J 500       4.879 -32.741  61.412  1.00 50.07           C  
ANISOU 3543  CA  THR J 500     5936   5910   7180  -1805   2851  -3139       C  
ATOM   3544  C   THR J 500       5.424 -31.723  62.408  1.00 55.32           C  
ANISOU 3544  C   THR J 500     6477   6605   7938  -1989   2971  -3325       C  
ATOM   3545  O   THR J 500       5.253 -31.877  63.623  1.00 63.58           O  
ANISOU 3545  O   THR J 500     7515   7580   9064  -2098   3111  -3367       O  
ATOM   3546  CB  THR J 500       6.019 -33.591  60.846  1.00 53.84           C  
ANISOU 3546  CB  THR J 500     6537   6247   7674  -1796   2910  -3019       C  
ATOM   3547  OG1 THR J 500       5.503 -34.514  59.878  1.00 56.62           O  
ANISOU 3547  OG1 THR J 500     6982   6591   7940  -1635   2796  -2867       O  
ATOM   3548  CG2 THR J 500       6.733 -34.350  61.954  1.00 47.71           C  
ANISOU 3548  CG2 THR J 500     5846   5280   7000  -1908   3127  -2979       C  
ATOM   3549  N   GLY J 501       6.090 -30.682  61.914  1.00 48.62           N  
ANISOU 3549  N   GLY J 501     6433   7102   4937     24   1078  -2153       N  
ATOM   3550  CA  GLY J 501       6.725 -29.700  62.775  1.00 48.02           C  
ANISOU 3550  CA  GLY J 501     6496   6971   4778     81    986  -2132       C  
ATOM   3551  C   GLY J 501       8.222 -29.639  62.562  1.00 47.09           C  
ANISOU 3551  C   GLY J 501     6459   6852   4582    194    982  -2171       C  
ATOM   3552  O   GLY J 501       8.829 -30.635  62.159  1.00 53.87           O  
ANISOU 3552  O   GLY J 501     7260   7745   5461    220   1012  -2227       O  
ATOM   3553  N   LYS J 502       8.836 -28.485  62.830  1.00 51.21           N  
ANISOU 3553  N   LYS J 502     7106   7334   5017    258    945  -2154       N  
ATOM   3554  CA  LYS J 502      10.259 -28.334  62.543  1.00 59.54           C  
ANISOU 3554  CA  LYS J 502     8240   8387   5994    359    954  -2193       C  
ATOM   3555  C   LYS J 502      11.126 -29.018  63.600  1.00 55.01           C  
ANISOU 3555  C   LYS J 502     7683   7778   5439    360    843  -2256       C  
ATOM   3556  O   LYS J 502      12.161 -29.607  63.266  1.00 52.60           O  
ANISOU 3556  O   LYS J 502     7372   7497   5118    416    862  -2308       O  
ATOM   3557  CB  LYS J 502      10.623 -26.844  62.395  1.00 77.76           C  
ANISOU 3557  CB  LYS J 502    10680  10666   8202    425    959  -2166       C  
ATOM   3558  CG  LYS J 502      10.702 -25.996  63.677  1.00 90.20           C  
ANISOU 3558  CG  LYS J 502    12328  12170   9772    398    825  -2181       C  
ATOM   3559  CD  LYS J 502       9.336 -25.587  64.216  1.00 92.57           C  
ANISOU 3559  CD  LYS J 502    12593  12449  10129    317    786  -2137       C  
ATOM   3560  CE  LYS J 502       9.456 -24.948  65.591  1.00 91.26           C  
ANISOU 3560  CE  LYS J 502    12481  12207   9988    283    659  -2167       C  
ATOM   3561  NZ  LYS J 502       8.187 -25.039  66.365  1.00 88.66           N  
ANISOU 3561  NZ  LYS J 502    12088  11851   9747    186    617  -2137       N  
ATOM   3562  N   ALA J 503      10.704 -28.992  64.868  1.00 56.34           N  
ANISOU 3562  N   ALA J 503     7872   7886   5646    300    738  -2250       N  
ATOM   3563  CA  ALA J 503      11.513 -29.564  65.940  1.00 61.62           C  
ANISOU 3563  CA  ALA J 503     8581   8505   6327    307    643  -2301       C  
ATOM   3564  C   ALA J 503      11.479 -31.085  65.914  1.00 57.66           C  
ANISOU 3564  C   ALA J 503     7998   8036   5874    297    645  -2338       C  
ATOM   3565  O   ALA J 503      12.510 -31.734  66.122  1.00 64.33           O  
ANISOU 3565  O   ALA J 503     8855   8878   6709    346    611  -2397       O  
ATOM   3566  CB  ALA J 503      11.039 -29.044  67.297  1.00 70.04           C  
ANISOU 3566  CB  ALA J 503     9706   9485   7421    251    553  -2282       C  
ATOM   3567  N   ILE J 504      10.310 -31.666  65.640  1.00 51.63           N  
ANISOU 3567  N   ILE J 504     7143   7307   5167    235    681  -2314       N  
ATOM   3568  CA  ILE J 504      10.193 -33.118  65.555  1.00 57.03           C  
ANISOU 3568  CA  ILE J 504     7739   8030   5901    228    678  -2364       C  
ATOM   3569  C   ILE J 504      10.971 -33.650  64.355  1.00 56.49           C  
ANISOU 3569  C   ILE J 504     7592   8037   5834    290    754  -2426       C  
ATOM   3570  O   ILE J 504      11.635 -34.691  64.439  1.00 39.40           O  
ANISOU 3570  O   ILE J 504     5391   5893   3687    332    720  -2500       O  
ATOM   3571  CB  ILE J 504       8.705 -33.516  65.507  1.00 36.83           C  
ANISOU 3571  CB  ILE J 504     5092   5494   3408    140    703  -2334       C  
ATOM   3572  CG1 ILE J 504       7.998 -33.048  66.782  1.00 36.85           C  
ANISOU 3572  CG1 ILE J 504     5176   5416   3408     86    631  -2278       C  
ATOM   3573  CG2 ILE J 504       8.545 -35.013  65.330  1.00 37.27           C  
ANISOU 3573  CG2 ILE J 504     5046   5599   3516    142    696  -2404       C  
ATOM   3574  CD1 ILE J 504       6.502 -33.257  66.773  1.00 38.12           C  
ANISOU 3574  CD1 ILE J 504     5258   5597   3631     -6    658  -2241       C  
ATOM   3575  N   LEU J 505      10.940 -32.925  63.235  1.00 53.60           N  
ANISOU 3575  N   LEU J 505     7207   7709   5448    305    861  -2398       N  
ATOM   3576  CA  LEU J 505      11.684 -33.357  62.055  1.00 61.02           C  
ANISOU 3576  CA  LEU J 505     8083   8711   6392    366    958  -2452       C  
ATOM   3577  C   LEU J 505      13.186 -33.191  62.243  1.00 63.33           C  
ANISOU 3577  C   LEU J 505     8459   8987   6618    457    920  -2494       C  
ATOM   3578  O   LEU J 505      13.969 -34.024  61.770  1.00 68.30           O  
ANISOU 3578  O   LEU J 505     9024   9657   7270    507    942  -2571       O  
ATOM   3579  CB  LEU J 505      11.220 -32.587  60.822  1.00 60.23           C  
ANISOU 3579  CB  LEU J 505     7969   8639   6277    368   1104  -2396       C  
ATOM   3580  CG  LEU J 505      10.043 -33.181  60.057  1.00 49.10           C  
ANISOU 3580  CG  LEU J 505     6414   7274   4969    288   1196  -2396       C  
ATOM   3581  CD1 LEU J 505       9.661 -32.230  58.952  1.00 47.66           C  
ANISOU 3581  CD1 LEU J 505     6255   7098   4755    304   1343  -2319       C  
ATOM   3582  CD2 LEU J 505      10.396 -34.550  59.500  1.00 50.66           C  
ANISOU 3582  CD2 LEU J 505     6470   7523   5254    294   1232  -2502       C  
ATOM   3583  N   ASN J 506      13.611 -32.113  62.914  1.00 59.63           N  
ANISOU 3583  N   ASN J 506     8120   8459   6078    476    861  -2457       N  
ATOM   3584  CA  ASN J 506      15.023 -31.978  63.258  1.00 54.61           C  
ANISOU 3584  CA  ASN J 506     7552   7804   5393    547    808  -2509       C  
ATOM   3585  C   ASN J 506      15.462 -33.083  64.206  1.00 52.05           C  
ANISOU 3585  C   ASN J 506     7203   7460   5113    548    702  -2573       C  
ATOM   3586  O   ASN J 506      16.580 -33.596  64.090  1.00 63.35           O  
ANISOU 3586  O   ASN J 506     8618   8912   6538    614    684  -2644       O  
ATOM   3587  CB  ASN J 506      15.297 -30.605  63.870  1.00 57.13           C  
ANISOU 3587  CB  ASN J 506     7994   8064   5648    552    758  -2475       C  
ATOM   3588  CG  ASN J 506      15.251 -29.493  62.844  1.00 61.00           C  
ANISOU 3588  CG  ASN J 506     8536   8576   6066    590    863  -2430       C  
ATOM   3589  OD1 ASN J 506      15.276 -29.744  61.639  1.00 63.03           O  
ANISOU 3589  OD1 ASN J 506     8754   8885   6309    630    989  -2424       O  
ATOM   3590  ND2 ASN J 506      15.180 -28.254  63.316  1.00 62.91           N  
ANISOU 3590  ND2 ASN J 506     8867   8774   6261    583    818  -2404       N  
ATOM   3591  N   GLY J 507      14.581 -33.481  65.129  1.00 52.05           N  
ANISOU 3591  N   GLY J 507     7205   7418   5153    482    635  -2548       N  
ATOM   3592  CA  GLY J 507      14.877 -34.617  65.985  1.00 42.14           C  
ANISOU 3592  CA  GLY J 507     5944   6141   3928    495    547  -2602       C  
ATOM   3593  C   GLY J 507      15.047 -35.906  65.205  1.00 42.90           C  
ANISOU 3593  C   GLY J 507     5911   6319   4072    535    573  -2681       C  
ATOM   3594  O   GLY J 507      15.996 -36.654  65.432  1.00 45.39           O  
ANISOU 3594  O   GLY J 507     6214   6642   4390    601    518  -2756       O  
ATOM   3595  N   ILE J 508      14.139 -36.163  64.257  1.00 42.25           N  
ANISOU 3595  N   ILE J 508     5718   6298   4036    496    659  -2675       N  
ATOM   3596  CA  ILE J 508      14.219 -37.370  63.427  1.00 43.12           C  
ANISOU 3596  CA  ILE J 508     5678   6490   4216    525    694  -2770       C  
ATOM   3597  C   ILE J 508      15.509 -37.380  62.610  1.00 56.36           C  
ANISOU 3597  C   ILE J 508     7328   8206   5879    607    746  -2834       C  
ATOM   3598  O   ILE J 508      16.236 -38.385  62.568  1.00 60.56           O  
ANISOU 3598  O   ILE J 508     7792   8773   6446    669    700  -2934       O  
ATOM   3599  CB  ILE J 508      12.980 -37.474  62.515  1.00 42.77           C  
ANISOU 3599  CB  ILE J 508     5514   6497   4241    452    795  -2755       C  
ATOM   3600  CG1 ILE J 508      11.717 -37.769  63.334  1.00 50.17           C  
ANISOU 3600  CG1 ILE J 508     6451   7407   5204    378    732  -2717       C  
ATOM   3601  CG2 ILE J 508      13.194 -38.524  61.422  1.00 49.51           C  
ANISOU 3601  CG2 ILE J 508     6195   7432   5185    478    862  -2869       C  
ATOM   3602  CD1 ILE J 508      10.528 -38.231  62.498  1.00 54.15           C  
ANISOU 3602  CD1 ILE J 508     6800   7971   5803    305    811  -2740       C  
ATOM   3603  N   ASP J 509      15.820 -36.252  61.967  1.00 50.89           N  
ANISOU 3603  N   ASP J 509     6698   7509   5130    619    840  -2778       N  
ATOM   3604  CA  ASP J 509      16.994 -36.179  61.105  1.00 66.36           C  
ANISOU 3604  CA  ASP J 509     8646   9502   7065    700    913  -2829       C  
ATOM   3605  C   ASP J 509      18.284 -36.282  61.915  1.00 69.84           C  
ANISOU 3605  C   ASP J 509     9153   9916   7465    769    800  -2880       C  
ATOM   3606  O   ASP J 509      19.248 -36.929  61.483  1.00 76.77           O  
ANISOU 3606  O   ASP J 509     9971  10835   8364    839    807  -2968       O  
ATOM   3607  CB  ASP J 509      16.952 -34.884  60.294  1.00 79.81           C  
ANISOU 3607  CB  ASP J 509    10431  11197   8696    710   1042  -2745       C  
ATOM   3608  CG  ASP J 509      17.941 -34.879  59.147  1.00 94.32           C  
ANISOU 3608  CG  ASP J 509    12252  13073  10512    792   1168  -2785       C  
ATOM   3609  OD1 ASP J 509      17.794 -35.716  58.231  1.00 98.19           O  
ANISOU 3609  OD1 ASP J 509    12611  13611  11085    792   1267  -2839       O  
ATOM   3610  OD2 ASP J 509      18.851 -34.026  59.152  1.00 99.30           O  
ANISOU 3610  OD2 ASP J 509    12998  13682  11050    853   1176  -2767       O  
ATOM   3611  N   SER J 510      18.307 -35.698  63.115  1.00 69.41           N  
ANISOU 3611  N   SER J 510     9214   9791   7368    748    695  -2833       N  
ATOM   3612  CA  SER J 510      19.491 -35.809  63.955  1.00 63.95           C  
ANISOU 3612  CA  SER J 510     8579   9066   6654    808    589  -2884       C  
ATOM   3613  C   SER J 510      19.632 -37.205  64.553  1.00 55.36           C  
ANISOU 3613  C   SER J 510     7431   7983   5622    837    492  -2959       C  
ATOM   3614  O   SER J 510      20.756 -37.664  64.763  1.00 51.42           O  
ANISOU 3614  O   SER J 510     6925   7490   5123    915    431  -3034       O  
ATOM   3615  CB  SER J 510      19.458 -34.751  65.056  1.00 65.14           C  
ANISOU 3615  CB  SER J 510     8859   9130   6760    771    520  -2823       C  
ATOM   3616  OG  SER J 510      18.137 -34.497  65.491  1.00 69.13           O  
ANISOU 3616  OG  SER J 510     9390   9596   7279    683    520  -2747       O  
ATOM   3617  N   ILE J 511      18.517 -37.895  64.821  1.00 54.42           N  
ANISOU 3617  N   ILE J 511     7269   7863   5546    785    471  -2946       N  
ATOM   3618  CA  ILE J 511      18.590 -39.293  65.250  1.00 60.07           C  
ANISOU 3618  CA  ILE J 511     7922   8596   6307    832    381  -3026       C  
ATOM   3619  C   ILE J 511      19.185 -40.151  64.143  1.00 59.60           C  
ANISOU 3619  C   ILE J 511     7712   8629   6303    900    418  -3139       C  
ATOM   3620  O   ILE J 511      20.026 -41.029  64.394  1.00 59.05           O  
ANISOU 3620  O   ILE J 511     7608   8575   6253    988    333  -3231       O  
ATOM   3621  CB  ILE J 511      17.193 -39.799  65.669  1.00 62.03           C  
ANISOU 3621  CB  ILE J 511     8155   8832   6582    767    359  -2991       C  
ATOM   3622  CG1 ILE J 511      16.794 -39.229  67.027  1.00 56.82           C  
ANISOU 3622  CG1 ILE J 511     7654   8064   5872    717    302  -2903       C  
ATOM   3623  CG2 ILE J 511      17.150 -41.317  65.738  1.00 63.58           C  
ANISOU 3623  CG2 ILE J 511     8254   9076   6829    832    281  -3093       C  
ATOM   3624  CD1 ILE J 511      17.789 -39.486  68.083  1.00 58.75           C  
ANISOU 3624  CD1 ILE J 511     7993   8243   6086    782    206  -2936       C  
ATOM   3625  N   ASN J 512      18.769 -39.898  62.898  1.00 66.19           N  
ANISOU 3625  N   ASN J 512     8456   9522   7171    864    553  -3137       N  
ATOM   3626  CA  ASN J 512      19.342 -40.613  61.762  1.00 71.60           C  
ANISOU 3626  CA  ASN J 512     8996  10286   7924    917    620  -3248       C  
ATOM   3627  C   ASN J 512      20.833 -40.315  61.617  1.00 72.18           C  
ANISOU 3627  C   ASN J 512     9114  10358   7952   1002    619  -3287       C  
ATOM   3628  O   ASN J 512      21.624 -41.211  61.299  1.00 80.97           O  
ANISOU 3628  O   ASN J 512    10131  11517   9116   1077    590  -3403       O  
ATOM   3629  CB  ASN J 512      18.587 -40.250  60.483  1.00 69.66           C  
ANISOU 3629  CB  ASN J 512     8668  10079   7722    852    793  -3222       C  
ATOM   3630  CG  ASN J 512      17.116 -40.629  60.549  1.00 66.37           C  
ANISOU 3630  CG  ASN J 512     8179   9672   7368    766    793  -3202       C  
ATOM   3631  OD1 ASN J 512      16.713 -41.466  61.357  1.00 66.34           O  
ANISOU 3631  OD1 ASN J 512     8150   9667   7390    771    668  -3241       O  
ATOM   3632  ND2 ASN J 512      16.307 -40.005  59.701  1.00 66.41           N  
ANISOU 3632  ND2 ASN J 512     8156   9683   7393    694    936  -3139       N  
ATOM   3633  N   LYS J 513      21.236 -39.066  61.878  1.00 65.33           N  
ANISOU 3633  N   LYS J 513     8388   9442   6994    996    641  -3200       N  
ATOM   3634  CA  LYS J 513      22.657 -38.721  61.845  1.00 61.29           C  
ANISOU 3634  CA  LYS J 513     7926   8929   6434   1079    626  -3239       C  
ATOM   3635  C   LYS J 513      23.437 -39.428  62.951  1.00 60.27           C  
ANISOU 3635  C   LYS J 513     7813   8771   6314   1144    460  -3304       C  
ATOM   3636  O   LYS J 513      24.564 -39.887  62.722  1.00 66.93           O  
ANISOU 3636  O   LYS J 513     8613   9646   7171   1230    434  -3395       O  
ATOM   3637  CB  LYS J 513      22.837 -37.207  61.946  1.00 55.40           C  
ANISOU 3637  CB  LYS J 513     7320   8138   5592   1061    669  -3144       C  
ATOM   3638  CG  LYS J 513      22.416 -36.454  60.697  1.00 62.01           C  
ANISOU 3638  CG  LYS J 513     8162   9002   6398   1040    848  -3087       C  
ATOM   3639  CD  LYS J 513      22.607 -34.955  60.851  1.00 59.76           C  
ANISOU 3639  CD  LYS J 513     8022   8676   6010   1038    868  -3004       C  
ATOM   3640  CE  LYS J 513      22.065 -34.217  59.638  1.00 62.94           C  
ANISOU 3640  CE  LYS J 513     8453   9094   6370   1030   1051  -2933       C  
ATOM   3641  NZ  LYS J 513      21.890 -32.760  59.884  1.00 59.96           N  
ANISOU 3641  NZ  LYS J 513     8212   8673   5897   1016   1052  -2849       N  
ATOM   3642  N   VAL J 514      22.856 -39.516  64.155  1.00 58.28           N  
ANISOU 3642  N   VAL J 514     7634   8454   6055   1108    356  -3257       N  
ATOM   3643  CA  VAL J 514      23.487 -40.248  65.255  1.00 59.52           C  
ANISOU 3643  CA  VAL J 514     7826   8570   6220   1176    210  -3309       C  
ATOM   3644  C   VAL J 514      23.668 -41.716  64.894  1.00 59.61           C  
ANISOU 3644  C   VAL J 514     7702   8647   6299   1252    159  -3426       C  
ATOM   3645  O   VAL J 514      24.735 -42.291  65.122  1.00 61.55           O  
ANISOU 3645  O   VAL J 514     7931   8899   6556   1352     77  -3510       O  
ATOM   3646  CB  VAL J 514      22.681 -40.086  66.559  1.00 64.47           C  
ANISOU 3646  CB  VAL J 514     8567   9105   6824   1117    141  -3230       C  
ATOM   3647  CG1 VAL J 514      23.241 -40.978  67.653  1.00 56.26           C  
ANISOU 3647  CG1 VAL J 514     7572   8015   5789   1199      6  -3284       C  
ATOM   3648  CG2 VAL J 514      22.759 -38.659  67.044  1.00 72.38           C  
ANISOU 3648  CG2 VAL J 514     9690  10037   7776   1058    166  -3147       C  
ATOM   3649  N   LEU J 515      22.653 -42.334  64.290  1.00 60.26           N  
ANISOU 3649  N   LEU J 515     7677   8783   6437   1213    203  -3445       N  
ATOM   3650  CA  LEU J 515      22.768 -43.752  63.957  1.00 68.49           C  
ANISOU 3650  CA  LEU J 515     8572   9892   7558   1289    140  -3577       C  
ATOM   3651  C   LEU J 515      23.735 -43.997  62.801  1.00 72.90           C  
ANISOU 3651  C   LEU J 515     9005  10523   8169   1344    209  -3685       C  
ATOM   3652  O   LEU J 515      24.440 -45.015  62.794  1.00 73.88           O  
ANISOU 3652  O   LEU J 515     9043  10685   8344   1444    119  -3807       O  
ATOM   3653  CB  LEU J 515      21.388 -44.330  63.655  1.00 75.93           C  
ANISOU 3653  CB  LEU J 515     9418  10872   8559   1229    162  -3583       C  
ATOM   3654  CG  LEU J 515      20.462 -44.345  64.874  1.00 77.46           C  
ANISOU 3654  CG  LEU J 515     9734  10995   8702   1194     79  -3495       C  
ATOM   3655  CD1 LEU J 515      19.197 -45.114  64.582  1.00 75.55           C  
ANISOU 3655  CD1 LEU J 515     9379  10803   8522   1160     77  -3528       C  
ATOM   3656  CD2 LEU J 515      21.176 -44.955  66.075  1.00 78.92           C  
ANISOU 3656  CD2 LEU J 515    10017  11124   8844   1302    -76  -3522       C  
ATOM   3657  N   ASP J 516      23.813 -43.069  61.843  1.00 71.69           N  
ANISOU 3657  N   ASP J 516     8853  10386   8000   1290    369  -3640       N  
ATOM   3658  CA  ASP J 516      24.778 -43.209  60.756  1.00 80.15           C  
ANISOU 3658  CA  ASP J 516     9832  11512   9110   1342    461  -3731       C  
ATOM   3659  C   ASP J 516      26.208 -43.056  61.268  1.00 83.71           C  
ANISOU 3659  C   ASP J 516    10356  11941   9508   1437    376  -3763       C  
ATOM   3660  O   ASP J 516      27.084 -43.868  60.945  1.00 89.53           O  
ANISOU 3660  O   ASP J 516    10995  12722  10301   1522    339  -3888       O  
ATOM   3661  CB  ASP J 516      24.481 -42.186  59.658  1.00 89.48           C  
ANISOU 3661  CB  ASP J 516    11034  12700  10266   1275    667  -3654       C  
ATOM   3662  CG  ASP J 516      25.508 -42.207  58.539  1.00100.82           C  
ANISOU 3662  CG  ASP J 516    12407  14174  11724   1331    792  -3727       C  
ATOM   3663  OD2 ASP J 516      25.562 -41.227  57.768  1.00103.59           O  
ANISOU 3663  OD2 ASP J 516    12828  14515  12018   1311    958  -3649       O  
ATOM   3664  OD1 ASP J 516      26.249 -43.207  58.417  1.00105.41           O1-
ANISOU 3664  OD1 ASP J 516    12877  14796  12380   1402    729  -3862       O1-
ATOM   3665  N   HIS J 517      26.460 -42.025  62.083  1.00 81.91           N  
ANISOU 3665  N   HIS J 517    10292  11646   9185   1424    340  -3663       N  
ATOM   3666  CA  HIS J 517      27.769 -41.839  62.702  1.00 84.86           C  
ANISOU 3666  CA  HIS J 517    10735  11991   9518   1508    248  -3695       C  
ATOM   3667  C   HIS J 517      28.078 -42.931  63.722  1.00 76.81           C  
ANISOU 3667  C   HIS J 517     9704  10947   8534   1588     69  -3764       C  
ATOM   3668  O   HIS J 517      29.251 -43.173  64.028  1.00 77.98           O  
ANISOU 3668  O   HIS J 517     9859  11089   8681   1682    -11  -3832       O  
ATOM   3669  CB  HIS J 517      27.813 -40.442  63.342  1.00 92.34           C  
ANISOU 3669  CB  HIS J 517    11842  12868  10375   1463    253  -3582       C  
ATOM   3670  CG  HIS J 517      29.081 -40.131  64.075  1.00 94.04           C  
ANISOU 3670  CG  HIS J 517    12128  13044  10558   1539    155  -3614       C  
ATOM   3671  ND1 HIS J 517      29.279 -40.463  65.397  1.00 92.96           N  
ANISOU 3671  ND1 HIS J 517    12057  12835  10430   1570     10  -3618       N  
ATOM   3672  CD2 HIS J 517      30.210 -39.498  63.674  1.00 93.29           C  
ANISOU 3672  CD2 HIS J 517    12054  12970  10424   1594    187  -3646       C  
ATOM   3673  CE1 HIS J 517      30.478 -40.058  65.777  1.00 91.05           C  
ANISOU 3673  CE1 HIS J 517    11860  12567  10166   1637    -46  -3656       C  
ATOM   3674  NE2 HIS J 517      31.063 -39.469  64.750  1.00 93.57           N  
ANISOU 3674  NE2 HIS J 517    12150  12948  10455   1653     53  -3675       N  
ATOM   3675  N   PHE J 518      27.046 -43.614  64.218  1.00 73.84           N  
ANISOU 3675  N   PHE J 518     9313  10558   8186   1562      8  -3750       N  
ATOM   3676  CA  PHE J 518      27.172 -44.677  65.203  1.00 66.86           C  
ANISOU 3676  CA  PHE J 518     8441   9644   7318   1650   -157  -3803       C  
ATOM   3677  C   PHE J 518      27.587 -45.990  64.554  1.00 65.78           C  
ANISOU 3677  C   PHE J 518     8135   9591   7266   1749   -210  -3957       C  
ATOM   3678  O   PHE J 518      28.409 -46.731  65.109  1.00 65.41           O  
ANISOU 3678  O   PHE J 518     8092   9533   7228   1870   -344  -4034       O  
ATOM   3679  CB  PHE J 518      25.829 -44.826  65.919  1.00 71.35           C  
ANISOU 3679  CB  PHE J 518     9071  10168   7870   1587   -187  -3722       C  
ATOM   3680  CG  PHE J 518      25.937 -45.018  67.396  1.00 80.00           C  
ANISOU 3680  CG  PHE J 518    10316  11163   8917   1636   -314  -3683       C  
ATOM   3681  CD2 PHE J 518      25.426 -46.156  67.993  1.00 87.44           C  
ANISOU 3681  CD2 PHE J 518    11259  12098   9866   1706   -425  -3717       C  
ATOM   3682  CD1 PHE J 518      26.541 -44.061  68.193  1.00 81.12           C  
ANISOU 3682  CD1 PHE J 518    10600  11215   9009   1619   -319  -3619       C  
ATOM   3683  CE2 PHE J 518      25.506 -46.330  69.353  1.00 89.16           C  
ANISOU 3683  CE2 PHE J 518    11636  12211  10029   1760   -524  -3676       C  
ATOM   3684  CE1 PHE J 518      26.634 -44.239  69.559  1.00 85.54           C  
ANISOU 3684  CE1 PHE J 518    11299  11668   9536   1660   -416  -3590       C  
ATOM   3685  CZ  PHE J 518      26.116 -45.375  70.140  1.00 87.75           C  
ANISOU 3685  CZ  PHE J 518    11598  11932   9810   1732   -511  -3614       C  
ATOM   3686  N   ARG J 519      27.017 -46.300  63.387  1.00 71.93           N  
ANISOU 3686  N   ARG J 519     8761  10452   8118   1702   -108  -4012       N  
ATOM   3687  CA  ARG J 519      27.441 -47.487  62.655  1.00 72.27           C  
ANISOU 3687  CA  ARG J 519     8617  10578   8265   1784   -144  -4180       C  
ATOM   3688  C   ARG J 519      28.726 -47.253  61.876  1.00 70.52           C  
ANISOU 3688  C   ARG J 519     8345  10389   8062   1825    -73  -4252       C  
ATOM   3689  O   ARG J 519      29.464 -48.210  61.613  1.00 67.16           O  
ANISOU 3689  O   ARG J 519     7798  10010   7708   1923   -147  -4396       O  
ATOM   3690  CB  ARG J 519      26.359 -47.939  61.682  1.00 74.28           C  
ANISOU 3690  CB  ARG J 519     8708  10900   8616   1710    -52  -4231       C  
ATOM   3691  CG  ARG J 519      25.166 -48.592  62.318  1.00 72.95           C  
ANISOU 3691  CG  ARG J 519     8534  10727   8457   1704   -153  -4219       C  
ATOM   3692  CD  ARG J 519      24.587 -49.609  61.369  1.00 77.24           C  
ANISOU 3692  CD  ARG J 519     8846  11360   9142   1699   -137  -4367       C  
ATOM   3693  NE  ARG J 519      23.176 -49.370  61.124  1.00 76.78           N  
ANISOU 3693  NE  ARG J 519     8761  11307   9106   1583    -55  -4304       N  
ATOM   3694  CZ  ARG J 519      22.729 -48.533  60.196  1.00 77.22           C  
ANISOU 3694  CZ  ARG J 519     8789  11364   9186   1456    142  -4245       C  
ATOM   3695  NH1 ARG J 519      23.584 -47.859  59.437  1.00 73.55           N  
ANISOU 3695  NH1 ARG J 519     8334  10897   8717   1440    281  -4234       N  
ATOM   3696  NH2 ARG J 519      21.432 -48.365  60.025  1.00 78.59           N  
ANISOU 3696  NH2 ARG J 519     8936  11541   9386   1356    204  -4192       N  
ATOM   3697  N   ARG J 520      28.999 -46.001  61.489  1.00 69.73           N  
ANISOU 3697  N   ARG J 520     8334  10264   7895   1759     68  -4158       N  
ATOM   3698  CA  ARG J 520      30.180 -45.700  60.685  1.00 76.82           C  
ANISOU 3698  CA  ARG J 520     9199  11192   8796   1800    158  -4216       C  
ATOM   3699  C   ARG J 520      31.467 -45.992  61.444  1.00 80.04           C  
ANISOU 3699  C   ARG J 520     9651  11580   9182   1919      8  -4277       C  
ATOM   3700  O   ARG J 520      32.467 -46.394  60.839  1.00 85.08           O  
ANISOU 3700  O   ARG J 520    10200  12262   9866   1988     22  -4390       O  
ATOM   3701  CB  ARG J 520      30.143 -44.239  60.235  1.00 87.70           C  
ANISOU 3701  CB  ARG J 520    10694  12544  10083   1724    323  -4090       C  
ATOM   3702  CG  ARG J 520      29.639 -44.039  58.813  1.00101.42           C  
ANISOU 3702  CG  ARG J 520    12348  14323  11865   1657    541  -4089       C  
ATOM   3703  CD  ARG J 520      30.792 -43.860  57.839  1.00118.59           C  
ANISOU 3703  CD  ARG J 520    14492  16527  14042   1712    667  -4152       C  
ATOM   3704  NE  ARG J 520      30.392 -44.132  56.461  1.00129.42           N  
ANISOU 3704  NE  ARG J 520    15739  17932  15502   1668    870  -4192       N  
ATOM   3705  CZ  ARG J 520      31.215 -44.592  55.523  1.00133.24           C  
ANISOU 3705  CZ  ARG J 520    16119  18449  16058   1716    973  -4301       C  
ATOM   3706  NH1 ARG J 520      30.765 -44.812  54.294  1.00133.52           N  
ANISOU 3706  NH1 ARG J 520    16045  18498  16190   1667   1175  -4326       N  
ATOM   3707  NH2 ARG J 520      32.486 -44.835  55.813  1.00133.84           N  
ANISOU 3707  NH2 ARG J 520    16197  18538  16119   1812    879  -4384       N  
ATOM   3708  N   LYS J 521      31.460 -45.806  62.762  1.00 77.61           N  
ANISOU 3708  N   LYS J 521     9480  11198   8811   1944   -129  -4206       N  
ATOM   3709  CA  LYS J 521      32.564 -46.235  63.609  1.00 75.43           C  
ANISOU 3709  CA  LYS J 521     9245  10887   8527   2066   -286  -4266       C  
ATOM   3710  C   LYS J 521      32.276 -47.549  64.323  1.00 75.47           C  
ANISOU 3710  C   LYS J 521     9212  10885   8577   2156   -458  -4334       C  
ATOM   3711  O   LYS J 521      33.181 -48.104  64.955  1.00 80.15           O  
ANISOU 3711  O   LYS J 521     9828  11453   9174   2278   -595  -4399       O  
ATOM   3712  CB  LYS J 521      32.910 -45.150  64.642  1.00 73.20           C  
ANISOU 3712  CB  LYS J 521     9148  10511   8156   2049   -320  -4156       C  
ATOM   3713  CG  LYS J 521      34.030 -44.184  64.227  1.00 74.28           C  
ANISOU 3713  CG  LYS J 521     9318  10656   8251   2060   -249  -4160       C  
ATOM   3714  CD  LYS J 521      33.824 -43.575  62.845  1.00 72.64           C  
ANISOU 3714  CD  LYS J 521     9052  10516   8032   1991    -55  -4146       C  
ATOM   3715  CE  LYS J 521      34.846 -42.488  62.552  1.00 68.39           C  
ANISOU 3715  CE  LYS J 521     8583   9978   7426   2011     10  -4132       C  
ATOM   3716  NZ  LYS J 521      36.229 -43.031  62.457  1.00 67.02           N  
ANISOU 3716  NZ  LYS J 521     8350   9831   7282   2127    -56  -4256       N  
ATOM   3717  N   GLY J 522      31.045 -48.052  64.236  1.00 67.83           N  
ANISOU 3717  N   GLY J 522     8194   9940   7639   2110   -456  -4321       N  
ATOM   3718  CA  GLY J 522      30.707 -49.372  64.729  1.00 62.27           C  
ANISOU 3718  CA  GLY J 522     7436   9248   6975   2212   -616  -4402       C  
ATOM   3719  C   GLY J 522      30.774 -49.540  66.232  1.00 78.94           C  
ANISOU 3719  C   GLY J 522     9726  11257   9011   2292   -766  -4337       C  
ATOM   3720  O   GLY J 522      31.447 -50.449  66.726  1.00 83.46           O  
ANISOU 3720  O   GLY J 522    10296  11820   9594   2442   -920  -4423       O  
ATOM   3721  N   ILE J 523      30.083 -48.678  66.974  1.00 82.16           N  
ANISOU 3721  N   ILE J 523    10292  11580   9344   2198   -721  -4188       N  
ATOM   3722  CA  ILE J 523      30.035 -48.783  68.426  1.00 90.49           C  
ANISOU 3722  CA  ILE J 523    11531  12519  10330   2258   -835  -4120       C  
ATOM   3723  C   ILE J 523      28.603 -49.064  68.856  1.00 92.15           C  
ANISOU 3723  C   ILE J 523    11792  12710  10512   2210   -841  -4049       C  
ATOM   3724  O   ILE J 523      27.639 -48.650  68.198  1.00 86.98           O  
ANISOU 3724  O   ILE J 523    11074  12101   9874   2083   -727  -4004       O  
ATOM   3725  CB  ILE J 523      30.612 -47.522  69.125  1.00 92.79           C  
ANISOU 3725  CB  ILE J 523    11980  12708  10568   2199   -787  -4024       C  
ATOM   3726  CG1 ILE J 523      31.367 -47.916  70.397  1.00 95.52           C  
ANISOU 3726  CG1 ILE J 523    12466  12944  10883   2328   -925  -4036       C  
ATOM   3727  CG2 ILE J 523      29.541 -46.480  69.445  1.00 88.55           C  
ANISOU 3727  CG2 ILE J 523    11542  12115   9986   2042   -681  -3884       C  
ATOM   3728  CD1 ILE J 523      32.055 -46.754  71.082  1.00 93.75           C  
ANISOU 3728  CD1 ILE J 523    12370  12618  10633   2281   -889  -3976       C  
ATOM   3729  N   ASN J 524      28.484 -49.829  69.945  1.00 98.13           N  
ANISOU 3729  N   ASN J 524    12664  13398  11222   2326   -979  -4046       N  
ATOM   3730  CA  ASN J 524      27.220 -50.176  70.599  1.00101.69           C  
ANISOU 3730  CA  ASN J 524    13203  13812  11623   2312  -1007  -3976       C  
ATOM   3731  C   ASN J 524      26.218 -50.783  69.615  1.00110.69           C  
ANISOU 3731  C   ASN J 524    14163  15074  12821   2278   -984  -4035       C  
ATOM   3732  O   ASN J 524      25.136 -50.247  69.369  1.00113.96           O  
ANISOU 3732  O   ASN J 524    14571  15497  13233   2138   -878  -3957       O  
ATOM   3733  CB  ASN J 524      26.628 -48.957  71.311  1.00 95.86           C  
ANISOU 3733  CB  ASN J 524    12628  12967  10826   2162   -898  -3824       C  
ATOM   3734  CG  ASN J 524      27.282 -48.684  72.647  1.00 92.89           C  
ANISOU 3734  CG  ASN J 524    12457  12444  10392   2222   -953  -3777       C  
ATOM   3735  OD1 ASN J 524      27.783 -47.587  72.891  1.00 87.69           O  
ANISOU 3735  OD1 ASN J 524    11862  11721   9735   2138   -880  -3728       O  
ATOM   3736  ND2 ASN J 524      27.277 -49.680  73.525  1.00 95.10           N  
ANISOU 3736  ND2 ASN J 524    12845  12666  10621   2378  -1085  -3797       N  
ATOM   3737  N   GLN J 525      26.613 -51.917  69.032  1.00111.48           N  
ANISOU 3737  N   GLN J 525    14104  15267  12986   2410  -1088  -4187       N  
ATOM   3738  CA  GLN J 525      25.737 -52.616  68.097  1.00107.94           C  
ANISOU 3738  CA  GLN J 525    13458  14935  12618   2393  -1082  -4278       C  
ATOM   3739  C   GLN J 525      24.538 -53.229  68.811  1.00103.74           C  
ANISOU 3739  C   GLN J 525    13004  14384  12028   2436  -1165  -4238       C  
ATOM   3740  O   GLN J 525      23.491 -53.445  68.189  1.00 97.83           O  
ANISOU 3740  O   GLN J 525    12131  13709  11333   2368  -1122  -4265       O  
ATOM   3741  CB  GLN J 525      26.517 -53.691  67.334  1.00105.53           C  
ANISOU 3741  CB  GLN J 525    12950  14734  12414   2529  -1184  -4474       C  
ATOM   3742  CG  GLN J 525      27.874 -53.247  66.773  1.00101.34           C  
ANISOU 3742  CG  GLN J 525    12363  14216  11927   2524  -1127  -4526       C  
ATOM   3743  CD  GLN J 525      29.026 -53.392  67.759  1.00101.24           C  
ANISOU 3743  CD  GLN J 525    12500  14119  11848   2666  -1253  -4520       C  
ATOM   3744  OE1 GLN J 525      28.825 -53.419  68.974  1.00100.92           O  
ANISOU 3744  OE1 GLN J 525    12661  13976  11708   2727  -1332  -4427       O  
ATOM   3745  NE2 GLN J 525      30.243 -53.486  67.234  1.00102.18           N  
ANISOU 3745  NE2 GLN J 525    12526  14275  12024   2720  -1263  -4622       N  
ATOM   3746  N   HIS J 526      24.678 -53.519  70.108  1.00107.16           N  
ANISOU 3746  N   HIS J 526    13648  14716  12353   2555  -1278  -4177       N  
ATOM   3747  CA  HIS J 526      23.534 -53.903  70.928  1.00112.41           C  
ANISOU 3747  CA  HIS J 526    14441  15338  12931   2586  -1332  -4107       C  
ATOM   3748  C   HIS J 526      22.529 -52.762  71.051  1.00116.30           C  
ANISOU 3748  C   HIS J 526    15012  15780  13395   2372  -1164  -3957       C  
ATOM   3749  O   HIS J 526      21.320 -53.003  71.146  1.00117.98           O  
ANISOU 3749  O   HIS J 526    15230  16012  13585   2337  -1159  -3925       O  
ATOM   3750  CB  HIS J 526      24.031 -54.353  72.305  1.00113.79           C  
ANISOU 3750  CB  HIS J 526    14854  15394  12986   2764  -1467  -4066       C  
ATOM   3751  CG  HIS J 526      22.946 -54.577  73.311  1.00117.21           C  
ANISOU 3751  CG  HIS J 526    15477  15756  13303   2796  -1498  -3968       C  
ATOM   3752  ND1 HIS J 526      22.410 -53.557  74.069  1.00116.18           N  
ANISOU 3752  ND1 HIS J 526    15528  15510  13105   2649  -1372  -3813       N  
ATOM   3753  CD2 HIS J 526      22.298 -55.705  73.688  1.00118.82           C  
ANISOU 3753  CD2 HIS J 526    15718  15987  13442   2965  -1641  -4008       C  
ATOM   3754  CE1 HIS J 526      21.477 -54.046  74.866  1.00115.57           C  
ANISOU 3754  CE1 HIS J 526    15597  15389  12926   2718  -1424  -3757       C  
ATOM   3755  NE2 HIS J 526      21.389 -55.347  74.654  1.00118.09           N  
ANISOU 3755  NE2 HIS J 526    15838  15794  13236   2917  -1589  -3869       N  
ATOM   3756  N   VAL J 527      23.014 -51.521  71.049  1.00116.62           N  
ANISOU 3756  N   VAL J 527    15114  15760  13438   2235  -1034  -3872       N  
ATOM   3757  CA  VAL J 527      22.147 -50.349  71.111  1.00110.52           C  
ANISOU 3757  CA  VAL J 527    14406  14941  12645   2034   -879  -3739       C  
ATOM   3758  C   VAL J 527      21.525 -50.056  69.743  1.00 95.89           C  
ANISOU 3758  C   VAL J 527    12349  13201  10885   1906   -764  -3770       C  
ATOM   3759  O   VAL J 527      20.403 -49.537  69.662  1.00 85.76           O  
ANISOU 3759  O   VAL J 527    11078  11911   9594   1774   -673  -3687       O  
ATOM   3760  CB  VAL J 527      22.974 -49.166  71.659  1.00117.41           C  
ANISOU 3760  CB  VAL J 527    15416  15707  13488   1964   -808  -3656       C  
ATOM   3761  CG1 VAL J 527      22.263 -47.825  71.526  1.00116.29           C  
ANISOU 3761  CG1 VAL J 527    15309  15532  13344   1759   -649  -3538       C  
ATOM   3762  CG2 VAL J 527      23.357 -49.420  73.112  1.00118.13           C  
ANISOU 3762  CG2 VAL J 527    15725  15666  13493   2075   -901  -3618       C  
ATOM   3763  N   GLN J 528      22.209 -50.444  68.662  1.00 93.19           N  
ANISOU 3763  N   GLN J 528    11814  12958  10635   1950   -768  -3896       N  
ATOM   3764  CA  GLN J 528      21.824 -50.024  67.316  1.00 93.97           C  
ANISOU 3764  CA  GLN J 528    11731  13145  10826   1826   -630  -3928       C  
ATOM   3765  C   GLN J 528      20.497 -50.646  66.888  1.00 94.78           C  
ANISOU 3765  C   GLN J 528    11713  13319  10982   1794   -631  -3968       C  
ATOM   3766  O   GLN J 528      19.614 -49.949  66.373  1.00 87.18           O  
ANISOU 3766  O   GLN J 528    10715  12367  10044   1646   -499  -3902       O  
ATOM   3767  CB  GLN J 528      22.943 -50.380  66.335  1.00 88.95           C  
ANISOU 3767  CB  GLN J 528    10927  12590  10279   1890   -630  -4068       C  
ATOM   3768  CG  GLN J 528      23.038 -49.509  65.082  1.00 88.78           C  
ANISOU 3768  CG  GLN J 528    10795  12616  10322   1759   -446  -4065       C  
ATOM   3769  CD  GLN J 528      21.853 -49.639  64.142  1.00 91.77           C  
ANISOU 3769  CD  GLN J 528    11017  13065  10785   1659   -350  -4096       C  
ATOM   3770  OE1 GLN J 528      21.796 -50.554  63.321  1.00 93.58           O  
ANISOU 3770  OE1 GLN J 528    11041  13384  11130   1699   -371  -4250       O  
ATOM   3771  NE2 GLN J 528      20.900 -48.721  64.259  1.00 90.01           N  
ANISOU 3771  NE2 GLN J 528    10882  12800  10519   1526   -246  -3958       N  
ATOM   3772  N   ASN J 529      20.331 -51.951  67.096  1.00 98.68           N  
ANISOU 3772  N   ASN J 529    12140  13861  11493   1940   -786  -4080       N  
ATOM   3773  CA  ASN J 529      19.078 -52.604  66.733  1.00 99.66           C  
ANISOU 3773  CA  ASN J 529    12139  14056  11671   1926   -806  -4136       C  
ATOM   3774  C   ASN J 529      17.971 -52.385  67.759  1.00 96.28           C  
ANISOU 3774  C   ASN J 529    11895  13553  11134   1887   -816  -3998       C  
ATOM   3775  O   ASN J 529      16.877 -52.936  67.592  1.00 89.31           O  
ANISOU 3775  O   ASN J 529    10928  12724  10280   1884   -844  -4037       O  
ATOM   3776  CB  ASN J 529      19.302 -54.107  66.518  1.00105.31           C  
ANISOU 3776  CB  ASN J 529    12696  14863  12453   2113   -984  -4328       C  
ATOM   3777  CG  ASN J 529      19.982 -54.779  67.700  1.00107.57           C  
ANISOU 3777  CG  ASN J 529    13155  15089  12627   2312  -1165  -4324       C  
ATOM   3778  OD1 ASN J 529      20.272 -54.145  68.714  1.00110.27           O  
ANISOU 3778  OD1 ASN J 529    13735  15315  12850   2302  -1150  -4181       O  
ATOM   3779  ND2 ASN J 529      20.232 -56.077  67.574  1.00106.08           N  
ANISOU 3779  ND2 ASN J 529    12844  14978  12484   2499  -1340  -4491       N  
ATOM   3780  N   GLY J 530      18.226 -51.604  68.807  1.00 98.22           N  
ANISOU 3780  N   GLY J 530    12379  13677  11264   1854   -790  -3851       N  
ATOM   3781  CA  GLY J 530      17.253 -51.287  69.826  1.00 93.31           C  
ANISOU 3781  CA  GLY J 530    11946  12969  10540   1800   -776  -3718       C  
ATOM   3782  C   GLY J 530      16.419 -50.053  69.573  1.00 85.93           C  
ANISOU 3782  C   GLY J 530    11034  12002   9613   1589   -607  -3595       C  
ATOM   3783  O   GLY J 530      15.554 -49.729  70.392  1.00 78.75           O  
ANISOU 3783  O   GLY J 530    10273  11022   8629   1527   -584  -3488       O  
ATOM   3784  N   TYR J 531      16.651 -49.342  68.472  1.00 80.85           N  
ANISOU 3784  N   TYR J 531    10257  11408   9055   1483   -487  -3608       N  
ATOM   3785  CA  TYR J 531      15.839 -48.196  68.080  1.00 77.13           C  
ANISOU 3785  CA  TYR J 531     9790  10917   8597   1302   -334  -3501       C  
ATOM   3786  C   TYR J 531      14.976 -48.615  66.899  1.00 70.85           C  
ANISOU 3786  C   TYR J 531     8771  10234   7915   1256   -286  -3587       C  
ATOM   3787  O   TYR J 531      15.501 -49.036  65.862  1.00 74.66           O  
ANISOU 3787  O   TYR J 531     9067  10803   8498   1292   -273  -3713       O  
ATOM   3788  CB  TYR J 531      16.714 -46.994  67.717  1.00 76.13           C  
ANISOU 3788  CB  TYR J 531     9699  10757   8471   1229   -228  -3444       C  
ATOM   3789  CG  TYR J 531      15.951 -45.815  67.145  1.00 71.37           C  
ANISOU 3789  CG  TYR J 531     9085  10147   7884   1069    -79  -3346       C  
ATOM   3790  CD1 TYR J 531      15.305 -44.914  67.982  1.00 65.10           C  
ANISOU 3790  CD1 TYR J 531     8456   9258   7021    973    -41  -3209       C  
ATOM   3791  CD2 TYR J 531      15.882 -45.599  65.772  1.00 74.13           C  
ANISOU 3791  CD2 TYR J 531     9263  10581   8323   1018     28  -3397       C  
ATOM   3792  CE1 TYR J 531      14.608 -43.835  67.471  1.00 64.38           C  
ANISOU 3792  CE1 TYR J 531     8355   9161   6944    845     79  -3122       C  
ATOM   3793  CE2 TYR J 531      15.188 -44.522  65.252  1.00 71.67           C  
ANISOU 3793  CE2 TYR J 531     8953  10260   8018    890    160  -3304       C  
ATOM   3794  CZ  TYR J 531      14.552 -43.644  66.106  1.00 67.10           C  
ANISOU 3794  CZ  TYR J 531     8537   9593   7367    810    176  -3166       C  
ATOM   3795  OH  TYR J 531      13.862 -42.569  65.594  1.00 65.94           O  
ANISOU 3795  OH  TYR J 531     8389   9438   7226    699    292  -3077       O  
ATOM   3796  N   HIS J 532      13.659 -48.493  67.049  1.00 63.84           N  
ANISOU 3796  N   HIS J 532     7895   9340   7020   1173   -253  -3526       N  
ATOM   3797  CA  HIS J 532      12.726 -48.994  66.052  1.00 69.79           C  
ANISOU 3797  CA  HIS J 532     8432  10195   7890   1133   -220  -3620       C  
ATOM   3798  C   HIS J 532      11.932 -47.906  65.342  1.00 75.91           C  
ANISOU 3798  C   HIS J 532     9163  10968   8711    961    -54  -3535       C  
ATOM   3799  O   HIS J 532      11.150 -48.223  64.440  1.00 83.30           O  
ANISOU 3799  O   HIS J 532     9909  11981   9759    909     -5  -3614       O  
ATOM   3800  CB  HIS J 532      11.765 -50.003  66.689  1.00 80.27           C  
ANISOU 3800  CB  HIS J 532     9768  11542   9190   1207   -340  -3656       C  
ATOM   3801  CG  HIS J 532      12.453 -51.055  67.500  1.00 91.06           C  
ANISOU 3801  CG  HIS J 532    11210  12901  10487   1398   -514  -3723       C  
ATOM   3802  ND1 HIS J 532      13.245 -52.031  66.931  1.00 96.52           N  
ANISOU 3802  ND1 HIS J 532    11738  13677  11257   1533   -611  -3893       N  
ATOM   3803  CD2 HIS J 532      12.467 -51.289  68.833  1.00 93.90           C  
ANISOU 3803  CD2 HIS J 532    11793  13176  10708   1482   -606  -3647       C  
ATOM   3804  CE1 HIS J 532      13.718 -52.818  67.880  1.00 98.67           C  
ANISOU 3804  CE1 HIS J 532    12134  13920  11437   1705   -768  -3914       C  
ATOM   3805  NE2 HIS J 532      13.261 -52.390  69.043  1.00 96.39           N  
ANISOU 3805  NE2 HIS J 532    12085  13526  11012   1678   -763  -3764       N  
ATOM   3806  N   GLY J 533      12.107 -46.647  65.708  1.00 67.05           N  
ANISOU 3806  N   GLY J 533     8202   9760   7514    876     29  -3388       N  
ATOM   3807  CA  GLY J 533      11.452 -45.555  65.019  1.00 67.77           C  
ANISOU 3807  CA  GLY J 533     8262   9848   7640    734    177  -3305       C  
ATOM   3808  C   GLY J 533      10.312 -44.970  65.831  1.00 63.58           C  
ANISOU 3808  C   GLY J 533     7864   9247   7047    647    188  -3172       C  
ATOM   3809  O   GLY J 533      10.142 -45.246  67.023  1.00 65.59           O  
ANISOU 3809  O   GLY J 533     8271   9435   7214    685    101  -3126       O  
ATOM   3810  N   ILE J 534       9.508 -44.153  65.152  1.00 63.66           N  
ANISOU 3810  N   ILE J 534     7814   9270   7105    528    306  -3114       N  
ATOM   3811  CA  ILE J 534       8.417 -43.436  65.802  1.00 61.84           C  
ANISOU 3811  CA  ILE J 534     7692   8975   6828    435    331  -2987       C  
ATOM   3812  C   ILE J 534       7.195 -44.335  65.916  1.00 58.50           C  
ANISOU 3812  C   ILE J 534     7186   8596   6446    426    286  -3034       C  
ATOM   3813  O   ILE J 534       7.144 -45.418  65.320  1.00 67.10           O  
ANISOU 3813  O   ILE J 534     8104   9774   7616    482    247  -3174       O  
ATOM   3814  CB  ILE J 534       8.074 -42.135  65.053  1.00 64.93           C  
ANISOU 3814  CB  ILE J 534     8059   9361   7249    325    465  -2902       C  
ATOM   3815  CG1 ILE J 534       7.523 -42.441  63.659  1.00 73.03           C  
ANISOU 3815  CG1 ILE J 534     8861  10483   8404    272    561  -2988       C  
ATOM   3816  CG2 ILE J 534       9.302 -41.250  64.946  1.00 63.85           C  
ANISOU 3816  CG2 ILE J 534     8014   9187   7060    354    498  -2862       C  
ATOM   3817  CD1 ILE J 534       7.316 -41.206  62.799  1.00 78.13           C  
ANISOU 3817  CD1 ILE J 534     9492  11121   9071    182    705  -2909       C  
ATOM   3818  N   VAL J 535       6.204 -43.888  66.690  1.00 55.14           N  
ANISOU 3818  N   VAL J 535     6874   8108   5969    359    288  -2928       N  
ATOM   3819  CA  VAL J 535       4.977 -44.659  66.863  1.00 48.58           C  
ANISOU 3819  CA  VAL J 535     5981   7313   5163    349    249  -2962       C  
ATOM   3820  C   VAL J 535       4.169 -44.678  65.573  1.00 43.47           C  
ANISOU 3820  C   VAL J 535     5097   6761   4660    266    337  -3031       C  
ATOM   3821  O   VAL J 535       3.583 -45.705  65.210  1.00 42.18           O  
ANISOU 3821  O   VAL J 535     4779   6676   4571    296    293  -3150       O  
ATOM   3822  CB  VAL J 535       4.157 -44.090  68.038  1.00 50.04           C  
ANISOU 3822  CB  VAL J 535     6360   7397   5254    293    243  -2826       C  
ATOM   3823  CG1 VAL J 535       2.951 -44.969  68.333  1.00 40.64           C  
ANISOU 3823  CG1 VAL J 535     5134   6241   4068    304    192  -2864       C  
ATOM   3824  CG2 VAL J 535       5.026 -43.960  69.273  1.00 50.01           C  
ANISOU 3824  CG2 VAL J 535     6591   7284   5125    354    185  -2768       C  
ATOM   3825  N   MET J 536       4.142 -43.552  64.850  1.00 40.47           N  
ANISOU 3825  N   MET J 536     4682   6372   4321    164    461  -2965       N  
ATOM   3826  CA  MET J 536       3.312 -43.432  63.652  1.00 50.35           C  
ANISOU 3826  CA  MET J 536     5731   7691   5708     61    570  -3014       C  
ATOM   3827  C   MET J 536       3.773 -44.369  62.540  1.00 55.13           C  
ANISOU 3827  C   MET J 536     6121   8386   6439    101    587  -3190       C  
ATOM   3828  O   MET J 536       2.953 -44.821  61.732  1.00 63.96           O  
ANISOU 3828  O   MET J 536     7046   9566   7692     37    634  -3286       O  
ATOM   3829  CB  MET J 536       3.317 -41.983  63.161  1.00 45.03           C  
ANISOU 3829  CB  MET J 536     5103   6975   5031    -36    697  -2898       C  
ATOM   3830  CG  MET J 536       2.343 -41.692  62.029  1.00 52.12           C  
ANISOU 3830  CG  MET J 536     5836   7912   6057   -159    824  -2918       C  
ATOM   3831  SD  MET J 536       2.332 -39.959  61.553  1.00 57.35           S  
ANISOU 3831  SD  MET J 536     6591   8513   6685   -244    956  -2766       S  
ATOM   3832  CE  MET J 536       4.059 -39.727  61.141  1.00 57.99           C  
ANISOU 3832  CE  MET J 536     6737   8589   6706   -138    979  -2783       C  
ATOM   3833  N   ASN J 537       5.063 -44.689  62.492  1.00 55.02           N  
ANISOU 3833  N   ASN J 537     6130   8379   6397    200    548  -3245       N  
ATOM   3834  CA  ASN J 537       5.591 -45.607  61.494  1.00 58.37           C  
ANISOU 3834  CA  ASN J 537     6349   8883   6947    245    556  -3422       C  
ATOM   3835  C   ASN J 537       5.660 -47.046  61.990  1.00 62.22           C  
ANISOU 3835  C   ASN J 537     6771   9425   7445    374    390  -3561       C  
ATOM   3836  O   ASN J 537       6.264 -47.890  61.320  1.00 69.38           O  
ANISOU 3836  O   ASN J 537     7515  10396   8451    438    364  -3723       O  
ATOM   3837  CB  ASN J 537       6.981 -45.155  61.042  1.00 56.97           C  
ANISOU 3837  CB  ASN J 537     6215   8688   6743    287    614  -3416       C  
ATOM   3838  CG  ASN J 537       6.951 -43.849  60.280  1.00 57.26           C  
ANISOU 3838  CG  ASN J 537     6289   8686   6783    184    785  -3306       C  
ATOM   3839  OD1 ASN J 537       5.911 -43.438  59.766  1.00 60.44           O  
ANISOU 3839  OD1 ASN J 537     6627   9086   7252     72    880  -3271       O  
ATOM   3840  ND2 ASN J 537       8.105 -43.196  60.182  1.00 56.39           N  
ANISOU 3840  ND2 ASN J 537     6286   8543   6597    231    824  -3254       N  
ATOM   3841  N   ASN J 538       5.062 -47.349  63.145  1.00 54.04           N  
ANISOU 3841  N   ASN J 538     5865   8360   6308    422    278  -3503       N  
ATOM   3842  CA  ASN J 538       5.115 -48.688  63.720  1.00 60.13           C  
ANISOU 3842  CA  ASN J 538     6614   9174   7058    570    109  -3618       C  
ATOM   3843  C   ASN J 538       3.731 -49.308  63.883  1.00 59.95           C  
ANISOU 3843  C   ASN J 538     6511   9194   7074    559     58  -3663       C  
ATOM   3844  O   ASN J 538       3.581 -50.285  64.623  1.00 59.19           O  
ANISOU 3844  O   ASN J 538     6461   9116   6914    692    -91  -3716       O  
ATOM   3845  CB  ASN J 538       5.850 -48.668  65.061  1.00 71.69           C  
ANISOU 3845  CB  ASN J 538     8344  10552   8343    674      6  -3517       C  
ATOM   3846  CG  ASN J 538       7.354 -48.548  64.902  1.00 82.71           C  
ANISOU 3846  CG  ASN J 538     9772  11934   9722    740      2  -3541       C  
ATOM   3847  OD1 ASN J 538       7.858 -48.313  63.803  1.00 82.88           O  
ANISOU 3847  OD1 ASN J 538     9643  12000   9846    698     93  -3607       O  
ATOM   3848  ND2 ASN J 538       8.079 -48.706  66.003  1.00 90.50           N  
ANISOU 3848  ND2 ASN J 538    10958  12852  10576    841    -96  -3488       N  
ATOM   3849  N   PHE J 539       2.719 -48.765  63.209  1.00 66.66           N  
ANISOU 3849  N   PHE J 539     7246  10061   8022    412    176  -3645       N  
ATOM   3850  CA  PHE J 539       1.400 -49.384  63.193  1.00 72.60           C  
ANISOU 3850  CA  PHE J 539     7879  10866   8840    396    136  -3715       C  
ATOM   3851  C   PHE J 539       0.652 -48.930  61.947  1.00 84.53           C  
ANISOU 3851  C   PHE J 539     9173  12412  10531    228    287  -3764       C  
ATOM   3852  O   PHE J 539       0.979 -47.908  61.339  1.00 87.46           O  
ANISOU 3852  O   PHE J 539     9561  12739  10929    115    432  -3684       O  
ATOM   3853  CB  PHE J 539       0.581 -49.066  64.457  1.00 67.40           C  
ANISOU 3853  CB  PHE J 539     7451  10135   8024    394     93  -3557       C  
ATOM   3854  CG  PHE J 539      -0.027 -47.675  64.492  1.00 62.26           C  
ANISOU 3854  CG  PHE J 539     6892   9411   7353    227    233  -3385       C  
ATOM   3855  CD2 PHE J 539      -1.362 -47.517  64.833  1.00 58.90           C  
ANISOU 3855  CD2 PHE J 539     6480   8977   6923    156    246  -3329       C  
ATOM   3856  CD1 PHE J 539       0.729 -46.536  64.245  1.00 56.37           C  
ANISOU 3856  CD1 PHE J 539     6227   8606   6585    156    337  -3279       C  
ATOM   3857  CE2 PHE J 539      -1.939 -46.260  64.888  1.00 50.11           C  
ANISOU 3857  CE2 PHE J 539     5441   7799   5798     12    360  -3179       C  
ATOM   3858  CE1 PHE J 539       0.156 -45.276  64.297  1.00 46.90           C  
ANISOU 3858  CE1 PHE J 539     5107   7346   5369     23    444  -3131       C  
ATOM   3859  CZ  PHE J 539      -1.179 -45.140  64.622  1.00 43.46           C  
ANISOU 3859  CZ  PHE J 539     4670   6903   4940    -50    454  -3082       C  
ATOM   3860  N   GLU J 540      -0.350 -49.720  61.571  1.00 85.15           N  
ANISOU 3860  N   GLU J 540     9054  12565  10735    218    249  -3902       N  
ATOM   3861  CA  GLU J 540      -1.293 -49.362  60.523  1.00 84.77           C  
ANISOU 3861  CA  GLU J 540     8810  12534  10863     45    384  -3950       C  
ATOM   3862  C   GLU J 540      -2.703 -49.683  60.997  1.00 84.76           C  
ANISOU 3862  C   GLU J 540     8780  12562  10864     33    328  -3953       C  
ATOM   3863  O   GLU J 540      -2.920 -50.642  61.742  1.00 87.85           O  
ANISOU 3863  O   GLU J 540     9197  12996  11186    182    170  -4014       O  
ATOM   3864  CB  GLU J 540      -1.010 -50.102  59.201  1.00 89.89           C  
ANISOU 3864  CB  GLU J 540     9172  13243  11739     16    415  -4179       C  
ATOM   3865  CG  GLU J 540       0.390 -49.896  58.642  1.00 94.67           C  
ANISOU 3865  CG  GLU J 540     9793  13822  12355     35    476  -4194       C  
ATOM   3866  CD  GLU J 540       0.438 -49.968  57.127  1.00 98.90           C  
ANISOU 3866  CD  GLU J 540    10112  14344  13119    -96    617  -4334       C  
ATOM   3867  OE1 GLU J 540      -0.620 -50.194  56.502  1.00 99.91           O  
ANISOU 3867  OE1 GLU J 540    10078  14475  13408   -211    659  -4429       O  
ATOM   3868  OE2 GLU J 540       1.538 -49.790  56.561  1.00 98.17           O  
ANISOU 3868  OE2 GLU J 540    10032  14221  13046    -86    691  -4344       O  
ATOM   3869  N   CYS J 541      -3.656 -48.863  60.565  1.00 89.02           N  
ANISOU 3869  N   CYS J 541     9278  13069  11475   -140    459  -3884       N  
ATOM   3870  CA  CYS J 541      -5.059 -49.065  60.891  1.00 87.42           C  
ANISOU 3870  CA  CYS J 541     9029  12893  11294   -175    430  -3888       C  
ATOM   3871  C   CYS J 541      -5.902 -48.715  59.674  1.00 88.16           C  
ANISOU 3871  C   CYS J 541     8907  12986  11603   -372    567  -3964       C  
ATOM   3872  O   CYS J 541      -5.425 -48.108  58.711  1.00 95.48           O  
ANISOU 3872  O   CYS J 541     9799  13858  12622   -489    699  -3961       O  
ATOM   3873  CB  CYS J 541      -5.483 -48.229  62.105  1.00 78.22           C  
ANISOU 3873  CB  CYS J 541     8141  11649   9930   -183    429  -3660       C  
ATOM   3874  SG  CYS J 541      -5.252 -46.450  61.903  1.00 66.89           S  
ANISOU 3874  SG  CYS J 541     6852  10107   8455   -352    603  -3448       S  
ATOM   3875  N   GLU J 542      -7.168 -49.122  59.723  1.00 80.07           N  
ANISOU 3875  N   GLU J 542     7763  12005  10653   -404    535  -4030       N  
ATOM   3876  CA  GLU J 542      -8.101 -48.787  58.661  1.00 73.92           C  
ANISOU 3876  CA  GLU J 542     6810  11199  10077   -608    652  -4101       C  
ATOM   3877  C   GLU J 542      -8.378 -47.282  58.666  1.00 65.40           C  
ANISOU 3877  C   GLU J 542     5909  10010   8932   -763    796  -3883       C  
ATOM   3878  O   GLU J 542      -8.368 -46.650  59.726  1.00 67.53           O  
ANISOU 3878  O   GLU J 542     6388  10256   9013   -714    780  -3694       O  
ATOM   3879  CB  GLU J 542      -9.399 -49.578  58.828  1.00 72.78           C  
ANISOU 3879  CB  GLU J 542     6500  11135  10017   -590    568  -4222       C  
ATOM   3880  CG  GLU J 542      -9.457 -50.897  58.037  1.00 78.03           C  
ANISOU 3880  CG  GLU J 542     6900  11869  10878   -539    480  -4498       C  
ATOM   3881  CD  GLU J 542      -8.590 -52.027  58.601  1.00 80.99           C  
ANISOU 3881  CD  GLU J 542     7237  12353  11183   -296    303  -4613       C  
ATOM   3882  OE1 GLU J 542      -7.796 -51.811  59.542  1.00 79.70           O  
ANISOU 3882  OE1 GLU J 542     7319  12165  10796   -163    257  -4459       O  
ATOM   3883  OE2 GLU J 542      -8.706 -53.158  58.082  1.00 80.36           O  
ANISOU 3883  OE2 GLU J 542     6929  12345  11258   -230    203  -4847       O  
ATOM   3884  N   PRO J 543      -8.604 -46.685  57.488  1.00 73.02           N  
ANISOU 3884  N   PRO J 543     8808   9216   9719   -233   2265  -3391       N  
ATOM   3885  CA  PRO J 543      -8.604 -45.211  57.388  1.00 70.01           C  
ANISOU 3885  CA  PRO J 543     8520   8763   9318   -155   2403  -3118       C  
ATOM   3886  C   PRO J 543      -9.707 -44.509  58.167  1.00 64.75           C  
ANISOU 3886  C   PRO J 543     7975   8069   8556   -122   2475  -2986       C  
ATOM   3887  O   PRO J 543      -9.525 -43.339  58.529  1.00 65.37           O  
ANISOU 3887  O   PRO J 543     8137   8154   8545    -20   2504  -2754       O  
ATOM   3888  CB  PRO J 543      -8.757 -44.971  55.881  1.00 73.25           C  
ANISOU 3888  CB  PRO J 543     8827   9039   9966   -252   2628  -3134       C  
ATOM   3889  CG  PRO J 543      -8.156 -46.183  55.257  1.00 77.30           C  
ANISOU 3889  CG  PRO J 543     9181   9598  10590   -340   2555  -3382       C  
ATOM   3890  CD  PRO J 543      -8.555 -47.318  56.158  1.00 75.28           C  
ANISOU 3890  CD  PRO J 543     8919   9446  10239   -362   2376  -3573       C  
ATOM   3891  N   ALA J 544     -10.829 -45.180  58.448  1.00 68.93           N  
ANISOU 3891  N   ALA J 544     8508   8585   9099   -200   2500  -3131       N  
ATOM   3892  CA  ALA J 544     -11.929 -44.551  59.175  1.00 70.92           C  
ANISOU 3892  CA  ALA J 544     8865   8817   9264   -168   2578  -3022       C  
ATOM   3893  C   ALA J 544     -11.557 -44.182  60.605  1.00 69.27           C  
ANISOU 3893  C   ALA J 544     8778   8739   8804    -50   2416  -2894       C  
ATOM   3894  O   ALA J 544     -12.195 -43.299  61.191  1.00 68.28           O  
ANISOU 3894  O   ALA J 544     8730   8616   8599      4   2490  -2736       O  
ATOM   3895  CB  ALA J 544     -13.151 -45.472  59.179  1.00 73.64           C  
ANISOU 3895  CB  ALA J 544     9183   9134   9661   -276   2627  -3238       C  
ATOM   3896  N   PHE J 545     -10.546 -44.833  61.179  1.00 66.73           N  
ANISOU 3896  N   PHE J 545     8470   8523   8362    -17   2200  -2962       N  
ATOM   3897  CA  PHE J 545     -10.062 -44.476  62.505  1.00 64.37           C  
ANISOU 3897  CA  PHE J 545     8295   8329   7835     76   2050  -2846       C  
ATOM   3898  C   PHE J 545      -9.064 -43.326  62.480  1.00 63.89           C  
ANISOU 3898  C   PHE J 545     8257   8275   7743    173   2054  -2633       C  
ATOM   3899  O   PHE J 545      -8.673 -42.856  63.555  1.00 48.22           O  
ANISOU 3899  O   PHE J 545     6371   6369   5580    240   1957  -2524       O  
ATOM   3900  CB  PHE J 545      -9.411 -45.692  63.169  1.00 60.15           C  
ANISOU 3900  CB  PHE J 545     7783   7889   7183     68   1804  -3014       C  
ATOM   3901  CG  PHE J 545     -10.299 -46.902  63.230  1.00 63.06           C  
ANISOU 3901  CG  PHE J 545     8120   8284   7557    -19   1767  -3234       C  
ATOM   3902  CD2 PHE J 545     -10.074 -47.979  62.386  1.00 68.46           C  
ANISOU 3902  CD2 PHE J 545     8666   8965   8378    -89   1719  -3444       C  
ATOM   3903  CD1 PHE J 545     -11.348 -46.971  64.133  1.00 60.22           C  
ANISOU 3903  CD1 PHE J 545     7855   7968   7058    -31   1781  -3239       C  
ATOM   3904  CE2 PHE J 545     -10.882 -49.100  62.437  1.00 67.41           C  
ANISOU 3904  CE2 PHE J 545     8492   8875   8246   -167   1677  -3658       C  
ATOM   3905  CE1 PHE J 545     -12.162 -48.090  64.191  1.00 57.97           C  
ANISOU 3905  CE1 PHE J 545     7542   7720   6762   -105   1742  -3449       C  
ATOM   3906  CZ  PHE J 545     -11.927 -49.156  63.340  1.00 64.04           C  
ANISOU 3906  CZ  PHE J 545     8174   8487   7669   -173   1685  -3659       C  
ATOM   3907  N   TYR J 546      -8.679 -42.855  61.283  1.00 70.16           N  
ANISOU 3907  N   TYR J 546     8964   8995   8699    173   2170  -2578       N  
ATOM   3908  CA  TYR J 546      -7.558 -41.925  61.130  1.00 73.71           C  
ANISOU 3908  CA  TYR J 546     9421   9472   9115    267   2148  -2410       C  
ATOM   3909  C   TYR J 546      -7.765 -40.634  61.911  1.00 71.22           C  
ANISOU 3909  C   TYR J 546     9180   9207   8672    350   2188  -2182       C  
ATOM   3910  O   TYR J 546      -6.809 -40.071  62.459  1.00 73.15           O  
ANISOU 3910  O   TYR J 546     9470   9526   8797    428   2091  -2080       O  
ATOM   3911  CB  TYR J 546      -7.342 -41.602  59.652  1.00 77.71           C  
ANISOU 3911  CB  TYR J 546     9823   9892   9810    242   2298  -2384       C  
ATOM   3912  CG  TYR J 546      -6.412 -42.542  58.922  1.00 78.26           C  
ANISOU 3912  CG  TYR J 546     9802   9963   9970    203   2221  -2554       C  
ATOM   3913  CD1 TYR J 546      -5.699 -43.520  59.605  1.00 80.30           C  
ANISOU 3913  CD1 TYR J 546    10072  10301  10137    213   2005  -2702       C  
ATOM   3914  CD2 TYR J 546      -6.226 -42.432  57.550  1.00 78.71           C  
ANISOU 3914  CD2 TYR J 546     9757   9946  10204    155   2365  -2565       C  
ATOM   3915  CE1 TYR J 546      -4.839 -44.376  58.936  1.00 80.74           C  
ANISOU 3915  CE1 TYR J 546    10019  10375  10283    184   1927  -2862       C  
ATOM   3916  CE2 TYR J 546      -5.371 -43.280  56.873  1.00 80.10           C  
ANISOU 3916  CE2 TYR J 546     9828  10140  10466    116   2305  -2728       C  
ATOM   3917  CZ  TYR J 546      -4.679 -44.249  57.571  1.00 80.28           C  
ANISOU 3917  CZ  TYR J 546     9844  10256  10402    135   2082  -2878       C  
ATOM   3918  OH  TYR J 546      -3.825 -45.095  56.900  1.00 79.18           O  
ANISOU 3918  OH  TYR J 546     9577  10152  10356    103   2014  -3047       O  
ATOM   3919  N   THR J 547      -9.005 -40.149  61.977  1.00 74.57           N  
ANISOU 3919  N   THR J 547     9611   9597   9125    329   2330  -2110       N  
ATOM   3920  CA  THR J 547      -9.281 -38.955  62.764  1.00 68.74           C  
ANISOU 3920  CA  THR J 547     8916   8931   8270    398   2363  -1902       C  
ATOM   3921  C   THR J 547      -9.252 -39.260  64.256  1.00 68.06           C  
ANISOU 3921  C   THR J 547     8927   8954   7978    406   2228  -1927       C  
ATOM   3922  O   THR J 547      -8.687 -38.491  65.043  1.00 68.34           O  
ANISOU 3922  O   THR J 547     9003   9086   7877    461   2170  -1789       O  
ATOM   3923  CB  THR J 547     -10.635 -38.363  62.365  1.00 60.75           C  
ANISOU 3923  CB  THR J 547     7880   7844   7361    376   2553  -1827       C  
ATOM   3924  OG1 THR J 547     -10.631 -38.061  60.964  1.00 61.75           O  
ANISOU 3924  OG1 THR J 547     7939   7847   7675    354   2686  -1801       O  
ATOM   3925  CG2 THR J 547     -10.925 -37.089  63.151  1.00 54.27           C  
ANISOU 3925  CG2 THR J 547     7075   7116   6428    444   2581  -1611       C  
ATOM   3926  N   CYS J 548      -9.830 -40.393  64.663  1.00 69.74           N  
ANISOU 3926  N   CYS J 548     9179   9161   8158    340   2175  -2107       N  
ATOM   3927  CA  CYS J 548     -10.028 -40.637  66.086  1.00 63.35           C  
ANISOU 3927  CA  CYS J 548     8475   8457   7138    332   2072  -2118       C  
ATOM   3928  C   CYS J 548      -8.763 -41.131  66.774  1.00 63.00           C  
ANISOU 3928  C   CYS J 548     8511   8472   6954    340   1853  -2177       C  
ATOM   3929  O   CYS J 548      -8.609 -40.931  67.982  1.00 61.91           O  
ANISOU 3929  O   CYS J 548     8476   8429   6619    337   1764  -2118       O  
ATOM   3930  CB  CYS J 548     -11.165 -41.636  66.298  1.00 60.24           C  
ANISOU 3930  CB  CYS J 548     8100   8054   6735    260   2088  -2288       C  
ATOM   3931  SG  CYS J 548     -10.695 -43.362  66.090  1.00 62.16           S  
ANISOU 3931  SG  CYS J 548     8341   8287   6988    192   1900  -2568       S  
ATOM   3932  N   VAL J 549      -7.853 -41.770  66.039  1.00 60.01           N  
ANISOU 3932  N   VAL J 549     8091   8042   6670    341   1759  -2292       N  
ATOM   3933  CA  VAL J 549      -6.603 -42.216  66.645  1.00 57.88           C  
ANISOU 3933  CA  VAL J 549     7897   7812   6282    355   1532  -2351       C  
ATOM   3934  C   VAL J 549      -5.677 -41.030  66.889  1.00 58.76           C  
ANISOU 3934  C   VAL J 549     8041   7954   6330    422   1530  -2177       C  
ATOM   3935  O   VAL J 549      -5.168 -40.845  68.002  1.00 63.49           O  
ANISOU 3935  O   VAL J 549     8756   8622   6745    415   1394  -2139       O  
ATOM   3936  CB  VAL J 549      -5.930 -43.288  65.770  1.00 50.40           C  
ANISOU 3936  CB  VAL J 549     6869   6814   5466    338   1431  -2530       C  
ATOM   3937  CG1 VAL J 549      -4.607 -43.710  66.376  1.00 52.06           C  
ANISOU 3937  CG1 VAL J 549     7150   7059   5571    363   1179  -2581       C  
ATOM   3938  CG2 VAL J 549      -6.835 -44.499  65.639  1.00 44.36           C  
ANISOU 3938  CG2 VAL J 549     6066   6048   4741    262   1413  -2715       C  
ATOM   3939  N   GLU J 550      -5.481 -40.197  65.856  1.00 56.18           N  
ANISOU 3939  N   GLU J 550     7616   7587   6144    477   1676  -2069       N  
ATOM   3940  CA  GLU J 550      -4.495 -39.115  65.876  1.00 56.16           C  
ANISOU 3940  CA  GLU J 550     7621   7623   6095    550   1670  -1922       C  
ATOM   3941  C   GLU J 550      -4.698 -38.171  67.051  1.00 61.66           C  
ANISOU 3941  C   GLU J 550     8391   8422   6614    552   1678  -1765       C  
ATOM   3942  O   GLU J 550      -3.811 -38.013  67.897  1.00 71.38           O  
ANISOU 3942  O   GLU J 550     9726   9703   7692    544   1534  -1759       O  
ATOM   3943  CB  GLU J 550      -4.560 -38.330  64.569  1.00 62.18           C  
ANISOU 3943  CB  GLU J 550     8254   8353   7018    601   1839  -1810       C  
ATOM   3944  CG  GLU J 550      -3.420 -37.349  64.400  1.00 71.41           C  
ANISOU 3944  CG  GLU J 550     9414   9577   8144    685   1818  -1688       C  
ATOM   3945  CD  GLU J 550      -3.443 -36.665  63.055  1.00 82.58           C  
ANISOU 3945  CD  GLU J 550    10700  10980   9697    723   1959  -1592       C  
ATOM   3946  OE1 GLU J 550      -3.323 -35.422  63.017  1.00 85.78           O  
ANISOU 3946  OE1 GLU J 550    11056  11475  10062    767   2013  -1421       O  
ATOM   3947  OE2 GLU J 550      -3.586 -37.372  62.036  1.00 85.88           O  
ANISOU 3947  OE2 GLU J 550    11059  11310  10261    689   2010  -1694       O  
ATOM   3948  N   VAL J 551      -5.887 -37.569  67.143  1.00 68.87           N  
ANISOU 3948  N   VAL J 551     9253   9370   7544    541   1834  -1645       N  
ATOM   3949  CA  VAL J 551      -6.156 -36.615  68.211  1.00 62.74           C  
ANISOU 3949  CA  VAL J 551     8513   8714   6613    527   1859  -1473       C  
ATOM   3950  C   VAL J 551      -6.183 -37.284  69.581  1.00 65.19           C  
ANISOU 3950  C   VAL J 551     8976   9081   6712    446   1721  -1543       C  
ATOM   3951  O   VAL J 551      -6.098 -36.591  70.601  1.00 64.61           O  
ANISOU 3951  O   VAL J 551     8966   9117   6467    406   1698  -1402       O  
ATOM   3952  CB  VAL J 551      -7.470 -35.864  67.932  1.00 56.29           C  
ANISOU 3952  CB  VAL J 551     7590   7915   5884    531   2042  -1337       C  
ATOM   3953  CG1 VAL J 551      -7.367 -35.096  66.624  1.00 63.02           C  
ANISOU 3953  CG1 VAL J 551     8313   8722   6910    583   2143  -1253       C  
ATOM   3954  CG2 VAL J 551      -8.629 -36.828  67.884  1.00 48.73           C  
ANISOU 3954  CG2 VAL J 551     6649   6890   4976    487   2093  -1471       C  
ATOM   3955  N   THR J 552      -6.276 -38.617  69.640  1.00 62.89           N  
ANISOU 3955  N   THR J 552     8744   8736   6416    403   1606  -1748       N  
ATOM   3956  CA  THR J 552      -6.143 -39.288  70.927  1.00 56.71           C  
ANISOU 3956  CA  THR J 552     8112   8029   5407    320   1414  -1811       C  
ATOM   3957  C   THR J 552      -4.689 -39.330  71.382  1.00 48.60           C  
ANISOU 3957  C   THR J 552     7183   7018   4265    310   1174  -1836       C  
ATOM   3958  O   THR J 552      -4.408 -39.211  72.579  1.00 51.62           O  
ANISOU 3958  O   THR J 552     7692   7501   4423    237   1015  -1764       O  
ATOM   3959  CB  THR J 552      -6.720 -40.703  70.857  1.00 51.59           C  
ANISOU 3959  CB  THR J 552     7481   7342   4780    283   1334  -2012       C  
ATOM   3960  OG1 THR J 552      -7.939 -40.686  70.107  1.00 41.78           O  
ANISOU 3960  OG1 THR J 552     6129   6051   3696    298   1550  -2022       O  
ATOM   3961  CG2 THR J 552      -7.009 -41.221  72.248  1.00 41.82           C  
ANISOU 3961  CG2 THR J 552     6387   6216   3287    200   1176  -2014       C  
ATOM   3962  N   ALA J 553      -3.754 -39.480  70.446  1.00 41.83           N  
ANISOU 3962  N   ALA J 553     6268   6069   3558    376   1129  -1921       N  
ATOM   3963  CA  ALA J 553      -2.336 -39.519  70.783  1.00 53.99           C  
ANISOU 3963  CA  ALA J 553     7880   7612   5023    380    886  -1957       C  
ATOM   3964  C   ALA J 553      -1.624 -38.207  70.494  1.00 52.21           C  
ANISOU 3964  C   ALA J 553     7618   7415   4804    430    972  -1821       C  
ATOM   3965  O   ALA J 553      -0.737 -37.812  71.258  1.00 40.22           O  
ANISOU 3965  O   ALA J 553     6181   5967   3135    417    773  -1773       O  
ATOM   3966  CB  ALA J 553      -1.641 -40.654  70.027  1.00 51.34           C  
ANISOU 3966  CB  ALA J 553     7493   7173   4841    414    746  -2141       C  
ATOM   3967  N   GLY J 554      -1.996 -37.529  69.409  1.00 49.94           N  
ANISOU 3967  N   GLY J 554     7206   7084   4684    503   1230  -1739       N  
ATOM   3968  CA  GLY J 554      -1.405 -36.240  69.086  1.00 50.97           C  
ANISOU 3968  CA  GLY J 554     7297   7256   4814    562   1326  -1585       C  
ATOM   3969  C   GLY J 554       0.071 -36.371  68.786  1.00 55.38           C  
ANISOU 3969  C   GLY J 554     7868   7781   5393    588   1152  -1689       C  
ATOM   3970  O   GLY J 554       0.499 -37.207  67.979  1.00 64.18           O  
ANISOU 3970  O   GLY J 554     8932   8800   6655    621   1106  -1829       O  
ATOM   3971  N   ASN J 555       0.870 -35.565  69.487  1.00 53.08           N  
ANISOU 3971  N   ASN J 555     7626   7597   4943    587   1016  -1608       N  
ATOM   3972  CA  ASN J 555       2.319 -35.623  69.353  1.00 59.11           C  
ANISOU 3972  CA  ASN J 555     8403   8346   5711    648    791  -1692       C  
ATOM   3973  C   ASN J 555       2.907 -36.918  69.902  1.00 56.42           C  
ANISOU 3973  C   ASN J 555     8143   7930   5363    631    473  -1856       C  
ATOM   3974  O   ASN J 555       4.079 -37.206  69.634  1.00 60.39           O  
ANISOU 3974  O   ASN J 555     8634   8380   5934    685    300  -1941       O  
ATOM   3975  CB  ASN J 555       2.947 -34.414  70.043  1.00 70.37           C  
ANISOU 3975  CB  ASN J 555     9889   9881   6967    668    687  -1519       C  
ATOM   3976  CG  ASN J 555       2.596 -33.109  69.354  1.00 80.31           C  
ANISOU 3976  CG  ASN J 555    11041  11220   8252    709    981  -1343       C  
ATOM   3977  OD1 ASN J 555       1.536 -32.531  69.599  1.00 83.88           O  
ANISOU 3977  OD1 ASN J 555    11470  11723   8679    662   1170  -1172       O  
ATOM   3978  ND2 ASN J 555       3.476 -32.647  68.474  1.00 84.21           N  
ANISOU 3978  ND2 ASN J 555    11462  11704   8830    779   1014  -1360       N  
ATOM   3979  N   ARG J 556       2.117 -37.721  70.627  1.00 49.91           N  
ANISOU 3979  N   ARG J 556     7391   7101   4471    557    402  -1885       N  
ATOM   3980  CA  ARG J 556       2.517 -39.078  70.976  1.00 51.30           C  
ANISOU 3980  CA  ARG J 556     7616   7197   4679    540    139  -2018       C  
ATOM   3981  C   ARG J 556       2.681 -39.975  69.753  1.00 53.15           C  
ANISOU 3981  C   ARG J 556     7714   7347   5134    582    218  -2175       C  
ATOM   3982  O   ARG J 556       3.261 -41.058  69.878  1.00 48.25           O  
ANISOU 3982  O   ARG J 556     7094   6678   4560    596      0  -2279       O  
ATOM   3983  CB  ARG J 556       1.502 -39.698  71.939  1.00 56.49           C  
ANISOU 3983  CB  ARG J 556     8372   7890   5201    450     83  -1996       C  
ATOM   3984  CG  ARG J 556       1.469 -39.050  73.313  1.00 57.35           C  
ANISOU 3984  CG  ARG J 556     8643   8076   5073    393    -67  -1810       C  
ATOM   3985  CD  ARG J 556       0.216 -39.455  74.084  1.00 59.02           C  
ANISOU 3985  CD  ARG J 556     8922   8355   5146    296    -15  -1754       C  
ATOM   3986  NE  ARG J 556      -0.101 -38.524  75.165  1.00 68.88           N  
ANISOU 3986  NE  ARG J 556    10250   9666   6256    190    -12  -1467       N  
ATOM   3987  CZ  ARG J 556       0.517 -38.487  76.343  1.00 76.28           C  
ANISOU 3987  CZ  ARG J 556    11335  10580   7068    121   -289  -1319       C  
ATOM   3988  NH1 ARG J 556       1.499 -39.336  76.618  1.00 77.09           N  
ANISOU 3988  NH1 ARG J 556    11538  10585   7167    164   -603  -1425       N  
ATOM   3989  NH2 ARG J 556       0.145 -37.595  77.253  1.00 74.50           N  
ANISOU 3989  NH2 ARG J 556    11152  10425   6731      8   -248  -1062       N  
ATOM   3990  N   LEU J 557       2.182 -39.553  68.581  1.00 54.62           N  
ANISOU 3990  N   LEU J 557     7782   7515   5455    605    520  -2164       N  
ATOM   3991  CA  LEU J 557       2.542 -40.195  67.320  1.00 48.96           C  
ANISOU 3991  CA  LEU J 557     6934   6732   4936    650    586  -2271       C  
ATOM   3992  C   LEU J 557       4.042 -40.186  67.063  1.00 51.34           C  
ANISOU 3992  C   LEU J 557     7200   7029   5278    720    419  -2322       C  
ATOM   3993  O   LEU J 557       4.536 -41.049  66.330  1.00 65.18           O  
ANISOU 3993  O   LEU J 557     8854   8752   7161    752    372  -2440       O  
ATOM   3994  CB  LEU J 557       1.844 -39.501  66.146  1.00 39.29           C  
ANISOU 3994  CB  LEU J 557     5615   5482   3831    674    917  -2178       C  
ATOM   3995  CG  LEU J 557       0.574 -40.076  65.516  1.00 40.50           C  
ANISOU 3995  CG  LEU J 557     5701   5595   4094    646   1085  -2203       C  
ATOM   3996  CD1 LEU J 557      -0.400 -40.571  66.561  1.00 41.28           C  
ANISOU 3996  CD1 LEU J 557     5886   5719   4080    576   1022  -2231       C  
ATOM   3997  CD2 LEU J 557      -0.078 -39.024  64.633  1.00 42.38           C  
ANISOU 3997  CD2 LEU J 557     5867   5829   4408    696   1359  -2034       C  
ATOM   3998  N   PHE J 558       4.777 -39.230  67.635  1.00 47.75           N  
ANISOU 3998  N   PHE J 558     6813   6616   4712    750    324  -2237       N  
ATOM   3999  CA  PHE J 558       6.178 -39.024  67.300  1.00 37.59           C  
ANISOU 3999  CA  PHE J 558     5489   5327   3466    830    200  -2273       C  
ATOM   4000  C   PHE J 558       7.118 -39.391  68.442  1.00 38.03           C  
ANISOU 4000  C   PHE J 558     5655   5357   3436    850   -154  -2291       C  
ATOM   4001  O   PHE J 558       8.274 -38.956  68.453  1.00 45.85           O  
ANISOU 4001  O   PHE J 558     6652   6344   4424    915   -275  -2290       O  
ATOM   4002  CB  PHE J 558       6.399 -37.578  66.859  1.00 36.95           C  
ANISOU 4002  CB  PHE J 558     5385   5308   3346    865    379  -2154       C  
ATOM   4003  CG  PHE J 558       5.462 -37.134  65.773  1.00 49.78           C  
ANISOU 4003  CG  PHE J 558     6921   6926   5068    851    734  -2075       C  
ATOM   4004  CD2 PHE J 558       4.283 -36.468  66.078  1.00 54.54           C  
ANISOU 4004  CD2 PHE J 558     7559   7556   5608    806    921  -1937       C  
ATOM   4005  CD1 PHE J 558       5.740 -37.422  64.447  1.00 49.04           C  
ANISOU 4005  CD1 PHE J 558     6715   6789   5130    887    874  -2115       C  
ATOM   4006  CE2 PHE J 558       3.416 -36.074  65.078  1.00 54.34           C  
ANISOU 4006  CE2 PHE J 558     7470   7485   5691    823   1226  -1822       C  
ATOM   4007  CE1 PHE J 558       4.876 -37.033  63.444  1.00 46.18           C  
ANISOU 4007  CE1 PHE J 558     6299   6390   4856    894   1171  -2000       C  
ATOM   4008  CZ  PHE J 558       3.714 -36.358  63.759  1.00 51.81           C  
ANISOU 4008  CZ  PHE J 558     7057   7110   5519    878   1334  -1845       C  
ATOM   4009  N   TYR J 559       6.649 -40.179  69.403  1.00 37.76           N  
ANISOU 4009  N   TYR J 559     5716   5295   3337    793   -318  -2292       N  
ATOM   4010  CA  TYR J 559       7.538 -40.721  70.418  1.00 45.31           C  
ANISOU 4010  CA  TYR J 559     6775   6190   4251    813   -649  -2284       C  
ATOM   4011  C   TYR J 559       8.404 -41.821  69.812  1.00 50.89           C  
ANISOU 4011  C   TYR J 559     7375   6853   5110    908   -759  -2428       C  
ATOM   4012  O   TYR J 559       7.976 -42.557  68.922  1.00 48.91           O  
ANISOU 4012  O   TYR J 559     6994   6622   4966    915   -633  -2538       O  
ATOM   4013  CB  TYR J 559       6.741 -41.271  71.603  1.00 51.33           C  
ANISOU 4013  CB  TYR J 559     7670   6944   4890    722   -778  -2216       C  
ATOM   4014  CG  TYR J 559       6.124 -40.233  72.529  1.00 60.69           C  
ANISOU 4014  CG  TYR J 559     8988   8181   5891    632   -754  -2046       C  
ATOM   4015  CD1 TYR J 559       6.190 -38.872  72.243  1.00 67.60           C  
ANISOU 4015  CD1 TYR J 559     9852   9118   6715    644   -607  -1966       C  
ATOM   4016  CD2 TYR J 559       5.479 -40.622  73.698  1.00 60.78           C  
ANISOU 4016  CD2 TYR J 559     9131   8200   5764    538   -880  -1950       C  
ATOM   4017  CE1 TYR J 559       5.630 -37.932  73.094  1.00 66.51           C  
ANISOU 4017  CE1 TYR J 559     9824   9052   6395    568   -588  -1794       C  
ATOM   4018  CE2 TYR J 559       4.915 -39.689  74.552  1.00 60.81           C  
ANISOU 4018  CE2 TYR J 559     9249   8267   5590    449   -856  -1772       C  
ATOM   4019  CZ  TYR J 559       4.993 -38.346  74.246  1.00 62.21           C  
ANISOU 4019  CZ  TYR J 559     9408   8508   5721    466   -712  -1693       C  
ATOM   4020  OH  TYR J 559       4.434 -37.416  75.094  1.00 61.61           O  
ANISOU 4020  OH  TYR J 559     9438   8510   5460    379   -683  -1492       O  
ATOM   4021  N   HIS J 560       9.636 -41.924  70.296  1.00 52.73           N  
ANISOU 4021  N   HIS J 560     7657   7025   5355    983   -996  -2427       N  
ATOM   4022  CA  HIS J 560      10.592 -42.887  69.764  1.00 55.43           C  
ANISOU 4022  CA  HIS J 560     7892   7338   5830   1103  -1112  -2563       C  
ATOM   4023  C   HIS J 560      10.513 -44.176  70.577  1.00 57.57           C  
ANISOU 4023  C   HIS J 560     8225   7555   6093   1123  -1340  -2588       C  
ATOM   4024  O   HIS J 560      10.804 -44.176  71.779  1.00 50.95           O  
ANISOU 4024  O   HIS J 560     7550   6638   5172   1112  -1550  -2485       O  
ATOM   4025  CB  HIS J 560      12.008 -42.314  69.799  1.00 57.43           C  
ANISOU 4025  CB  HIS J 560     8161   7551   6108   1200  -1234  -2563       C  
ATOM   4026  CG  HIS J 560      12.260 -41.260  68.767  1.00 61.03           C  
ANISOU 4026  CG  HIS J 560     8519   8083   6585   1213  -1017  -2574       C  
ATOM   4027  ND1 HIS J 560      11.566 -41.197  67.578  1.00 59.98           N  
ANISOU 4027  ND1 HIS J 560     8247   8030   6514   1184   -742  -2620       N  
ATOM   4028  CD2 HIS J 560      13.132 -40.223  68.748  1.00 63.39           C  
ANISOU 4028  CD2 HIS J 560     8847   8390   6849   1252  -1032  -2538       C  
ATOM   4029  CE1 HIS J 560      11.998 -40.167  66.872  1.00 59.93           C  
ANISOU 4029  CE1 HIS J 560     8191   8077   6502   1209   -594  -2598       C  
ATOM   4030  NE2 HIS J 560      12.949 -39.561  67.559  1.00 62.60           N  
ANISOU 4030  NE2 HIS J 560     8624   8386   6773   1254   -769  -2557       N  
ATOM   4031  N   ILE J 561      10.115 -45.265  69.927  1.00 56.53           N  
ANISOU 4031  N   ILE J 561     7966   7467   6045   1150  -1300  -2717       N  
ATOM   4032  CA  ILE J 561       9.978 -46.558  70.589  1.00 60.12           C  
ANISOU 4032  CA  ILE J 561     8462   7896   6485   1184  -1508  -2756       C  
ATOM   4033  C   ILE J 561      11.338 -47.244  70.599  1.00 77.74           C  
ANISOU 4033  C   ILE J 561    10656  10070   8811   1360  -1738  -2844       C  
ATOM   4034  O   ILE J 561      11.904 -47.539  69.540  1.00 88.49           O  
ANISOU 4034  O   ILE J 561    11838  11483  10301   1453  -1683  -2985       O  
ATOM   4035  CB  ILE J 561       8.923 -47.429  69.893  1.00 55.79           C  
ANISOU 4035  CB  ILE J 561     7786   7430   5980   1136  -1373  -2872       C  
ATOM   4036  CG1 ILE J 561       7.530 -46.833  70.098  1.00 45.33           C  
ANISOU 4036  CG1 ILE J 561     6533   6141   4549    975  -1174  -2783       C  
ATOM   4037  CG2 ILE J 561       8.978 -48.855  70.417  1.00 60.49           C  
ANISOU 4037  CG2 ILE J 561     8392   8021   6570   1207  -1607  -2945       C  
ATOM   4038  CD1 ILE J 561       6.434 -47.576  69.367  1.00 48.02           C  
ANISOU 4038  CD1 ILE J 561     6757   6546   4942    918  -1015  -2899       C  
ATOM   4039  N   VAL J 562      11.868 -47.491  71.798  1.00 78.73           N  
ANISOU 4039  N   VAL J 562    10952  10086   8874   1409  -1995  -2759       N  
ATOM   4040  CA  VAL J 562      13.170 -48.118  71.979  1.00 76.30           C  
ANISOU 4040  CA  VAL J 562    10649   9690   8651   1596  -2238  -2833       C  
ATOM   4041  C   VAL J 562      13.046 -49.237  73.005  1.00 85.16           C  
ANISOU 4041  C   VAL J 562    11900  10736   9718   1648  -2489  -2807       C  
ATOM   4042  O   VAL J 562      12.078 -49.311  73.763  1.00 83.94           O  
ANISOU 4042  O   VAL J 562    11866  10590   9436   1518  -2488  -2693       O  
ATOM   4043  CB  VAL J 562      14.248 -47.106  72.417  1.00 72.60           C  
ANISOU 4043  CB  VAL J 562    10291   9114   8180   1632  -2318  -2751       C  
ATOM   4044  CG1 VAL J 562      14.585 -46.153  71.284  1.00 47.49           C  
ANISOU 4044  CG1 VAL J 562     6963   6023   5058   1625  -2098  -2807       C  
ATOM   4045  CG2 VAL J 562      13.769 -46.338  73.630  1.00 70.10           C  
ANISOU 4045  CG2 VAL J 562    10193   8722   7720   1483  -2355  -2547       C  
ATOM   4046  N   ASP J 563      14.065 -50.101  73.036  1.00 88.86           N  
ANISOU 4046  N   ASP J 563    12348  11135  10279   1849  -2712  -2913       N  
ATOM   4047  CA  ASP J 563      13.995 -51.314  73.851  1.00 94.10           C  
ANISOU 4047  CA  ASP J 563    13117  11733  10902   1935  -2959  -2916       C  
ATOM   4048  C   ASP J 563      14.109 -51.012  75.342  1.00 95.60           C  
ANISOU 4048  C   ASP J 563    13598  11753  10973   1880  -3144  -2713       C  
ATOM   4049  O   ASP J 563      13.342 -51.554  76.147  1.00 95.53           O  
ANISOU 4049  O   ASP J 563    13711  11744  10842   1805  -3224  -2619       O  
ATOM   4050  CB  ASP J 563      15.085 -52.300  73.431  1.00 98.49           C  
ANISOU 4050  CB  ASP J 563    13566  12258  11597   2192  -3154  -3101       C  
ATOM   4051  CG  ASP J 563      14.808 -52.939  72.085  1.00 99.94           C  
ANISOU 4051  CG  ASP J 563    13457  12629  11888   2237  -3012  -3308       C  
ATOM   4052  OD1 ASP J 563      14.232 -52.262  71.210  1.00 98.97           O  
ANISOU 4052  OD1 ASP J 563    13198  12625  11780   2096  -2735  -3321       O  
ATOM   4053  OD2 ASP J 563      15.162 -54.123  71.905  1.00102.46           O  
ANISOU 4053  OD2 ASP J 563    13683  12969  12277   2413  -3182  -3462       O  
ATOM   4054  N   SER J 564      15.057 -50.167  75.736  1.00 97.40           N  
ANISOU 4054  N   SER J 564    13939  11840  11229   1910  -3217  -2642       N  
ATOM   4055  CA  SER J 564      15.305 -49.909  77.148  1.00 99.35           C  
ANISOU 4055  CA  SER J 564    14467  11896  11387   1860  -3416  -2457       C  
ATOM   4056  C   SER J 564      15.674 -48.440  77.324  1.00 97.14           C  
ANISOU 4056  C   SER J 564    14250  11563  11094   1749  -3320  -2352       C  
ATOM   4057  O   SER J 564      15.601 -47.641  76.386  1.00 96.15           O  
ANISOU 4057  O   SER J 564    13961  11565  11005   1703  -3092  -2409       O  
ATOM   4058  CB  SER J 564      16.395 -50.849  77.681  1.00106.86           C  
ANISOU 4058  CB  SER J 564    15541  12650  12411   2087  -3743  -2516       C  
ATOM   4059  OG  SER J 564      17.623 -50.640  77.005  1.00110.94           O  
ANISOU 4059  OG  SER J 564    15957  13118  13077   2265  -3781  -2663       O  
ATOM   4060  N   ASP J 565      16.044 -48.077  78.552  1.00 96.69           N  
ANISOU 4060  N   ASP J 565    14440  11317  10979   1694  -3500  -2192       N  
ATOM   4061  CA  ASP J 565      16.590 -46.755  78.820  1.00 96.87           C  
ANISOU 4061  CA  ASP J 565    14538  11267  11003   1607  -3464  -2109       C  
ATOM   4062  C   ASP J 565      18.064 -46.657  78.453  1.00 93.34           C  
ANISOU 4062  C   ASP J 565    14069  10699  10698   1800  -3588  -2244       C  
ATOM   4063  O   ASP J 565      18.594 -45.543  78.358  1.00 90.27           O  
ANISOU 4063  O   ASP J 565    13679  10296  10322   1749  -3521  -2227       O  
ATOM   4064  CB  ASP J 565      16.394 -46.395  80.295  1.00100.62           C  
ANISOU 4064  CB  ASP J 565    15282  11583  11364   1450  -3612  -1884       C  
ATOM   4065  CG  ASP J 565      16.697 -47.557  81.222  1.00107.40           C  
ANISOU 4065  CG  ASP J 565    16345  12246  12216   1549  -3910  -1843       C  
ATOM   4066  OD1 ASP J 565      17.020 -48.653  80.715  1.00107.77           O  
ANISOU 4066  OD1 ASP J 565    16312  12294  12343   1751  -4004  -1999       O  
ATOM   4067  OD2 ASP J 565      16.621 -47.375  82.455  1.00110.32           O  
ANISOU 4067  OD2 ASP J 565    16957  12460  12499   1424  -4057  -1652       O  
ATOM   4068  N   GLU J 566      18.724 -47.798  78.235  1.00 94.85           N  
ANISOU 4068  N   GLU J 566    14235  10817  10987   2027  -3769  -2386       N  
ATOM   4069  CA  GLU J 566      20.141 -47.809  77.880  1.00 99.61           C  
ANISOU 4069  CA  GLU J 566    14807  11316  11724   2238  -3903  -2532       C  
ATOM   4070  C   GLU J 566      20.368 -47.194  76.505  1.00 95.51           C  
ANISOU 4070  C   GLU J 566    14015  11008  11266   2259  -3652  -2669       C  
ATOM   4071  O   GLU J 566      21.233 -46.322  76.332  1.00 93.22           O  
ANISOU 4071  O   GLU J 566    13719  10688  11011   2277  -3635  -2698       O  
ATOM   4072  CB  GLU J 566      20.667 -49.246  77.912  1.00108.98           C  
ANISOU 4072  CB  GLU J 566    16006  12405  12996   2490  -4153  -2663       C  
ATOM   4073  CG  GLU J 566      20.502 -49.962  79.245  1.00111.61           C  
ANISOU 4073  CG  GLU J 566    16630  12514  13264   2490  -4426  -2532       C  
ATOM   4074  CD  GLU J 566      21.697 -49.782  80.159  1.00113.85           C  
ANISOU 4074  CD  GLU J 566    17170  12482  13604   2591  -4720  -2498       C  
ATOM   4075  OE1 GLU J 566      22.841 -49.922  79.675  1.00113.82           O  
ANISOU 4075  OE1 GLU J 566    17094  12422  13729   2814  -4830  -2666       O  
ATOM   4076  OE2 GLU J 566      21.496 -49.509  81.361  1.00114.53           O  
ANISOU 4076  OE2 GLU J 566    17530  12380  13605   2443  -4847  -2304       O  
ATOM   4077  N   VAL J 567      19.602 -47.654  75.511  1.00 93.91           N  
ANISOU 4077  N   VAL J 567    13592  11018  11072   2251  -3460  -2756       N  
ATOM   4078  CA  VAL J 567      19.685 -47.111  74.159  1.00 93.93           C  
ANISOU 4078  CA  VAL J 567    13344  11221  11124   2248  -3209  -2870       C  
ATOM   4079  C   VAL J 567      19.299 -45.636  74.140  1.00 90.18           C  
ANISOU 4079  C   VAL J 567    12898  10806  10561   2046  -2998  -2746       C  
ATOM   4080  O   VAL J 567      19.945 -44.825  73.464  1.00 85.55           O  
ANISOU 4080  O   VAL J 567    12216  10284  10004   2066  -2890  -2806       O  
ATOM   4081  CB  VAL J 567      18.830 -47.969  73.200  1.00 88.77           C  
ANISOU 4081  CB  VAL J 567    12474  10755  10499   2254  -3062  -2977       C  
ATOM   4082  CG1 VAL J 567      17.465 -48.246  73.793  1.00 83.61           C  
ANISOU 4082  CG1 VAL J 567    11912  10122   9734   2091  -3015  -2852       C  
ATOM   4083  CG2 VAL J 567      18.661 -47.284  71.851  1.00 86.64           C  
ANISOU 4083  CG2 VAL J 567    11978  10682  10258   2191  -2769  -3052       C  
ATOM   4084  N   SER J 568      18.287 -45.252  74.930  1.00 88.09           N  
ANISOU 4084  N   SER J 568    12769  10524  10179   1856  -2954  -2573       N  
ATOM   4085  CA  SER J 568      17.892 -43.847  75.011  1.00 83.50           C  
ANISOU 4085  CA  SER J 568    12218  10001   9506   1674  -2781  -2454       C  
ATOM   4086  C   SER J 568      19.015 -42.986  75.573  1.00 82.00           C  
ANISOU 4086  C   SER J 568    12153   9676   9325   1690  -2909  -2421       C  
ATOM   4087  O   SER J 568      19.323 -41.922  75.023  1.00 85.85           O  
ANISOU 4087  O   SER J 568    12567  10251   9800   1654  -2768  -2441       O  
ATOM   4088  CB  SER J 568      16.638 -43.696  75.873  1.00 86.38           C  
ANISOU 4088  CB  SER J 568    12708  10374   9740   1480  -2746  -2277       C  
ATOM   4089  OG  SER J 568      15.756 -44.786  75.699  1.00 93.56           O  
ANISOU 4089  OG  SER J 568    13559  11351  10640   1489  -2723  -2312       O  
ATOM   4090  N   THR J 569      19.655 -43.444  76.651  1.00 86.51           N  
ANISOU 4090  N   THR J 569    12922  10030   9919   1749  -3185  -2379       N  
ATOM   4091  CA  THR J 569      20.707 -42.652  77.280  1.00 80.46           C  
ANISOU 4091  CA  THR J 569    12295   9109   9168   1749  -3325  -2352       C  
ATOM   4092  C   THR J 569      21.945 -42.559  76.396  1.00 74.80           C  
ANISOU 4092  C   THR J 569    11446   8419   8554   1934  -3330  -2540       C  
ATOM   4093  O   THR J 569      22.587 -41.505  76.336  1.00 77.34           O  
ANISOU 4093  O   THR J 569    11775   8746   8863   1896  -3294  -2551       O  
ATOM   4094  CB  THR J 569      21.061 -43.238  78.646  1.00 74.68           C  
ANISOU 4094  CB  THR J 569    11828   8106   8442   1768  -3633  -2260       C  
ATOM   4095  OG1 THR J 569      21.029 -44.669  78.574  1.00 75.97           O  
ANISOU 4095  OG1 THR J 569    11983   8221   8661   1936  -3768  -2337       O  
ATOM   4096  CG2 THR J 569      20.068 -42.766  79.700  1.00 69.45           C  
ANISOU 4096  CG2 THR J 569    11328   7413   7649   1524  -3623  -2037       C  
ATOM   4097  N   LYS J 570      22.287 -43.638  75.682  1.00 74.47           N  
ANISOU 4097  N   LYS J 570    11270   8417   8608   2130  -3372  -2695       N  
ATOM   4098  CA  LYS J 570      23.438 -43.580  74.781  1.00 74.79           C  
ANISOU 4098  CA  LYS J 570    11162   8518   8739   2302  -3366  -2878       C  
ATOM   4099  C   LYS J 570      23.159 -42.671  73.586  1.00 68.05           C  
ANISOU 4099  C   LYS J 570    10107   7904   7846   2221  -3060  -2917       C  
ATOM   4100  O   LYS J 570      24.048 -41.925  73.135  1.00 70.97           O  
ANISOU 4100  O   LYS J 570    10423   8316   8225   2264  -3020  -2995       O  
ATOM   4101  CB  LYS J 570      23.809 -44.987  74.315  1.00 88.25           C  
ANISOU 4101  CB  LYS J 570    12754  10228  10551   2527  -3493  -3035       C  
ATOM   4102  CG  LYS J 570      25.286 -45.171  74.004  1.00 98.76           C  
ANISOU 4102  CG  LYS J 570    14034  11510  11980   2744  -3646  -3208       C  
ATOM   4103  CD  LYS J 570      26.119 -45.081  75.276  1.00105.12           C  
ANISOU 4103  CD  LYS J 570    15107  12031  12802   2796  -3940  -3157       C  
ATOM   4104  CE  LYS J 570      27.586 -44.815  74.973  1.00105.10           C  
ANISOU 4104  CE  LYS J 570    15064  11997  12871   2957  -4042  -3317       C  
ATOM   4105  NZ  LYS J 570      28.325 -46.070  74.665  1.00104.80           N  
ANISOU 4105  NZ  LYS J 570    14938  11936  12943   3228  -4245  -3494       N  
ATOM   4106  N   ILE J 571      21.923 -42.712  73.076  1.00 65.78           N  
ANISOU 4106  N   ILE J 571     9718   7767   7509   2104  -2848  -2863       N  
ATOM   4107  CA  ILE J 571      21.505 -41.803  72.012  1.00 63.97           C  
ANISOU 4107  CA  ILE J 571     9333   7741   7233   2014  -2561  -2872       C  
ATOM   4108  C   ILE J 571      21.611 -40.354  72.470  1.00 64.66           C  
ANISOU 4108  C   ILE J 571     9531   7815   7221   1883  -2514  -2765       C  
ATOM   4109  O   ILE J 571      22.133 -39.499  71.748  1.00 64.29           O  
ANISOU 4109  O   ILE J 571     9398   7874   7154   1899  -2395  -2824       O  
ATOM   4110  CB  ILE J 571      20.078 -42.152  71.548  1.00 57.62           C  
ANISOU 4110  CB  ILE J 571     8436   7060   6396   1907  -2369  -2826       C  
ATOM   4111  CG1 ILE J 571      20.088 -43.379  70.625  1.00 65.45           C  
ANISOU 4111  CG1 ILE J 571     9239   8137   7494   2034  -2349  -2981       C  
ATOM   4112  CG2 ILE J 571      19.414 -40.965  70.905  1.00 53.13           C  
ANISOU 4112  CG2 ILE J 571     7804   6638   5743   1772  -2102  -2764       C  
ATOM   4113  CD1 ILE J 571      20.426 -43.066  69.181  1.00 71.93           C  
ANISOU 4113  CD1 ILE J 571     9843   9130   8358   2074  -2145  -3102       C  
ATOM   4114  N   LEU J 572      21.142 -40.059  73.685  1.00 66.49           N  
ANISOU 4114  N   LEU J 572     9954   7927   7383   1750  -2616  -2609       N  
ATOM   4115  CA  LEU J 572      21.200 -38.683  74.176  1.00 55.34           C  
ANISOU 4115  CA  LEU J 572     8635   6518   5875   1610  -2585  -2507       C  
ATOM   4116  C   LEU J 572      22.631 -38.249  74.480  1.00 68.45           C  
ANISOU 4116  C   LEU J 572    10367   8066   7575   1692  -2747  -2585       C  
ATOM   4117  O   LEU J 572      22.956 -37.060  74.363  1.00 70.98           O  
ANISOU 4117  O   LEU J 572    10684   8456   7830   1626  -2677  -2578       O  
ATOM   4118  CB  LEU J 572      20.319 -38.523  75.414  1.00 54.90           C  
ANISOU 4118  CB  LEU J 572     8751   6375   5734   1430  -2658  -2317       C  
ATOM   4119  CG  LEU J 572      18.817 -38.735  75.207  1.00 53.15           C  
ANISOU 4119  CG  LEU J 572     8472   6280   5443   1322  -2485  -2230       C  
ATOM   4120  CD1 LEU J 572      18.027 -38.229  76.406  1.00 52.78           C  
ANISOU 4120  CD1 LEU J 572     8581   6190   5282   1125  -2535  -2032       C  
ATOM   4121  CD2 LEU J 572      18.333 -38.103  73.909  1.00 51.56           C  
ANISOU 4121  CD2 LEU J 572     8086   6294   5210   1318  -2207  -2284       C  
ATOM   4122  N   MET J 573      23.493 -39.200  74.854  1.00 64.60           N  
ANISOU 4122  N   MET J 573     9943   7410   7191   1846  -2969  -2670       N  
ATOM   4123  CA  MET J 573      24.914 -38.914  75.018  1.00 69.47           C  
ANISOU 4123  CA  MET J 573    10613   7921   7862   1956  -3123  -2780       C  
ATOM   4124  C   MET J 573      25.535 -38.454  73.707  1.00 73.46           C  
ANISOU 4124  C   MET J 573    10920   8618   8373   2053  -2956  -2933       C  
ATOM   4125  O   MET J 573      26.184 -37.403  73.648  1.00 74.39           O  
ANISOU 4125  O   MET J 573    11053   8770   8442   2021  -2932  -2966       O  
ATOM   4126  CB  MET J 573      25.639 -40.157  75.534  1.00 76.02           C  
ANISOU 4126  CB  MET J 573    11531   8546   8806   2137  -3392  -2855       C  
ATOM   4127  CG  MET J 573      25.617 -40.339  77.036  1.00 83.75           C  
ANISOU 4127  CG  MET J 573    12778   9261   9781   2063  -3640  -2721       C  
ATOM   4128  SD  MET J 573      26.602 -41.773  77.501  1.00 91.84           S  
ANISOU 4128  SD  MET J 573    13912  10042  10942   2324  -3977  -2830       S  
ATOM   4129  CE  MET J 573      26.566 -41.650  79.282  1.00 95.56           C  
ANISOU 4129  CE  MET J 573    14736  10187  11385   2186  -4251  -2639       C  
ATOM   4130  N   GLU J 574      25.335 -39.228  72.636  1.00 77.58           N  
ANISOU 4130  N   GLU J 574    11254   9277   8947   2163  -2840  -3030       N  
ATOM   4131  CA  GLU J 574      25.858 -38.797  71.339  1.00 80.01           C  
ANISOU 4131  CA  GLU J 574    11372   9779   9250   2238  -2667  -3162       C  
ATOM   4132  C   GLU J 574      25.159 -37.534  70.842  1.00 76.79           C  
ANISOU 4132  C   GLU J 574    10919   9540   8718   2085  -2424  -3074       C  
ATOM   4133  O   GLU J 574      25.775 -36.714  70.147  1.00 80.47           O  
ANISOU 4133  O   GLU J 574    11311  10127   9136   2116  -2325  -3149       O  
ATOM   4134  CB  GLU J 574      25.729 -39.920  70.315  1.00 85.02           C  
ANISOU 4134  CB  GLU J 574    11808  10525   9969   2361  -2596  -3277       C  
ATOM   4135  CG  GLU J 574      26.946 -40.821  70.262  1.00 92.49           C  
ANISOU 4135  CG  GLU J 574    12717  11398  11026   2574  -2799  -3448       C  
ATOM   4136  CD  GLU J 574      28.128 -40.175  69.569  1.00 96.59           C  
ANISOU 4136  CD  GLU J 574    13154  12010  11536   2662  -2758  -3589       C  
ATOM   4137  OE1 GLU J 574      29.167 -39.969  70.232  1.00 98.20           O  
ANISOU 4137  OE1 GLU J 574    13478  12072  11760   2738  -2949  -3646       O  
ATOM   4138  OE2 GLU J 574      28.021 -39.873  68.363  1.00 96.83           O  
ANISOU 4138  OE2 GLU J 574    13006  12249  11537   2652  -2536  -3645       O  
ATOM   4139  N   PHE J 575      23.898 -37.347  71.241  1.00 75.16           N  
ANISOU 4139  N   PHE J 575    10767   9344   8448   1929  -2341  -2918       N  
ATOM   4140  CA  PHE J 575      23.108 -36.191  70.831  1.00 74.16           C  
ANISOU 4140  CA  PHE J 575    10604   9376   8198   1797  -2125  -2824       C  
ATOM   4141  C   PHE J 575      23.701 -34.900  71.378  1.00 71.52           C  
ANISOU 4141  C   PHE J 575    10374   9031   7771   1727  -2184  -2789       C  
ATOM   4142  O   PHE J 575      23.967 -33.957  70.624  1.00 68.38           O  
ANISOU 4142  O   PHE J 575     9896   8789   7295   1738  -2047  -2827       O  
ATOM   4143  CB  PHE J 575      21.672 -36.372  71.326  1.00 71.80           C  
ANISOU 4143  CB  PHE J 575    10358   9068   7854   1654  -2065  -2671       C  
ATOM   4144  CG  PHE J 575      20.617 -35.941  70.352  1.00 70.22           C  
ANISOU 4144  CG  PHE J 575    10033   9058   7590   1598  -1791  -2632       C  
ATOM   4145  CD1 PHE J 575      20.821 -34.878  69.488  1.00 72.28           C  
ANISOU 4145  CD1 PHE J 575    10210   9478   7775   1612  -1622  -2654       C  
ATOM   4146  CD2 PHE J 575      19.401 -36.602  70.315  1.00 69.89           C  
ANISOU 4146  CD2 PHE J 575     9967   9029   7559   1537  -1702  -2574       C  
ATOM   4147  CE1 PHE J 575      19.828 -34.496  68.603  1.00 75.94           C  
ANISOU 4147  CE1 PHE J 575    10571  10097   8184   1574  -1366  -2608       C  
ATOM   4148  CE2 PHE J 575      18.413 -36.223  69.433  1.00 71.86           C  
ANISOU 4148  CE2 PHE J 575    10112   9429   7762   1491  -1445  -2543       C  
ATOM   4149  CZ  PHE J 575      18.626 -35.169  68.577  1.00 75.90           C  
ANISOU 4149  CZ  PHE J 575    10546  10086   8208   1513  -1274  -2554       C  
ATOM   4150  N   ASN J 576      23.918 -34.838  72.695  1.00 75.35           N  
ANISOU 4150  N   ASN J 576    11037   9334   8258   1649  -2391  -2716       N  
ATOM   4151  CA  ASN J 576      24.479 -33.617  73.260  1.00 72.85           C  
ANISOU 4151  CA  ASN J 576    10812   9008   7859   1560  -2458  -2689       C  
ATOM   4152  C   ASN J 576      25.987 -33.516  73.066  1.00 70.57           C  
ANISOU 4152  C   ASN J 576    10522   8669   7622   1696  -2569  -2861       C  
ATOM   4153  O   ASN J 576      26.536 -32.414  73.183  1.00 69.41           O  
ANISOU 4153  O   ASN J 576    10405   8572   7394   1642  -2579  -2882       O  
ATOM   4154  CB  ASN J 576      24.092 -33.457  74.746  1.00 80.11           C  
ANISOU 4154  CB  ASN J 576    11918   9766   8755   1390  -2623  -2536       C  
ATOM   4155  CG  ASN J 576      24.661 -34.541  75.669  1.00 92.76           C  
ANISOU 4155  CG  ASN J 576    13663  11105  10478   1457  -2874  -2557       C  
ATOM   4156  OD1 ASN J 576      25.538 -35.317  75.313  1.00101.14           O  
ANISOU 4156  OD1 ASN J 576    14695  12092  11643   1640  -2960  -2701       O  
ATOM   4157  ND2 ASN J 576      24.156 -34.565  76.894  1.00 92.56           N  
ANISOU 4157  ND2 ASN J 576    13798  10939  10431   1309  -3002  -2404       N  
ATOM   4158  N   LYS J 577      26.668 -34.627  72.764  1.00 72.94           N  
ANISOU 4158  N   LYS J 577    10781   8886   8046   1874  -2657  -2991       N  
ATOM   4159  CA  LYS J 577      28.091 -34.539  72.458  1.00 77.56           C  
ANISOU 4159  CA  LYS J 577    11345   9452   8674   2020  -2746  -3170       C  
ATOM   4160  C   LYS J 577      28.315 -33.910  71.089  1.00 79.85           C  
ANISOU 4160  C   LYS J 577    11456   9991   8892   2081  -2528  -3265       C  
ATOM   4161  O   LYS J 577      29.117 -32.978  70.950  1.00 82.29           O  
ANISOU 4161  O   LYS J 577    11774  10362   9132   2088  -2530  -3341       O  
ATOM   4162  CB  LYS J 577      28.730 -35.925  72.538  1.00 80.16           C  
ANISOU 4162  CB  LYS J 577    11671   9635   9150   2204  -2916  -3281       C  
ATOM   4163  CG  LYS J 577      30.084 -36.023  71.857  1.00 81.47           C  
ANISOU 4163  CG  LYS J 577    11750   9843   9364   2389  -2957  -3491       C  
ATOM   4164  CD  LYS J 577      31.008 -36.973  72.604  1.00 81.71           C  
ANISOU 4164  CD  LYS J 577    11887   9638   9521   2537  -3238  -3582       C  
ATOM   4165  CE  LYS J 577      30.370 -38.334  72.818  1.00 71.66           C  
ANISOU 4165  CE  LYS J 577    10610   8280   8337   2601  -3322  -3531       C  
ATOM   4166  NZ  LYS J 577      31.367 -39.337  73.280  1.00 65.49           N  
ANISOU 4166  NZ  LYS J 577     9896   7309   7678   2798  -3594  -3652       N  
ATOM   4167  N   MET J 578      27.606 -34.392  70.064  1.00 79.79           N  
ANISOU 4167  N   MET J 578    11289  10134   8894   2118  -2340  -3261       N  
ATOM   4168  CA  MET J 578      27.733 -33.777  68.748  1.00 80.39           C  
ANISOU 4168  CA  MET J 578    11205  10446   8893   2164  -2121  -3328       C  
ATOM   4169  C   MET J 578      26.943 -32.479  68.623  1.00 76.81           C  
ANISOU 4169  C   MET J 578    10764  10138   8283   2024  -1958  -3197       C  
ATOM   4170  O   MET J 578      27.141 -31.750  67.643  1.00 79.96           O  
ANISOU 4170  O   MET J 578    11060  10732   8591   2062  -1794  -3239       O  
ATOM   4171  CB  MET J 578      27.303 -34.760  67.654  1.00 83.19           C  
ANISOU 4171  CB  MET J 578    11382  10905   9323   2242  -1974  -3377       C  
ATOM   4172  CG  MET J 578      28.237 -35.959  67.493  1.00 86.05           C  
ANISOU 4172  CG  MET J 578    11681  11194   9822   2410  -2118  -3539       C  
ATOM   4173  SD  MET J 578      27.582 -37.276  66.444  1.00 82.28           S  
ANISOU 4173  SD  MET J 578    11001  10816   9445   2461  -1987  -3585       S  
ATOM   4174  CE  MET J 578      27.726 -36.531  64.821  1.00 80.57           C  
ANISOU 4174  CE  MET J 578    10602  10865   9144   2466  -1694  -3644       C  
ATOM   4175  N   ASN J 579      26.081 -32.174  69.601  1.00 68.45           N  
ANISOU 4175  N   ASN J 579     6593   8368  11048    834  -1271  -3180       N  
ATOM   4176  CA  ASN J 579      25.212 -30.997  69.641  1.00 65.67           C  
ANISOU 4176  CA  ASN J 579     6308   8029  10615    822  -1264  -3098       C  
ATOM   4177  C   ASN J 579      24.365 -30.885  68.379  1.00 69.70           C  
ANISOU 4177  C   ASN J 579     6802   8613  11067    809  -1168  -3101       C  
ATOM   4178  O   ASN J 579      24.675 -30.109  67.467  1.00 69.96           O  
ANISOU 4178  O   ASN J 579     6819   8769  10992    938  -1104  -3162       O  
ATOM   4179  CB  ASN J 579      26.022 -29.715  69.862  1.00 66.35           C  
ANISOU 4179  CB  ASN J 579     6353   8179  10679    944  -1404  -3250       C  
ATOM   4180  CG  ASN J 579      25.136 -28.486  70.018  1.00 60.34           C  
ANISOU 4180  CG  ASN J 579     5651   7408   9868    959  -1450  -3196       C  
ATOM   4181  OD1 ASN J 579      24.956 -27.711  69.076  1.00 56.20           O  
ANISOU 4181  OD1 ASN J 579     5112   6999   9245   1065  -1508  -3309       O  
ATOM   4182  ND2 ASN J 579      24.563 -28.316  71.203  1.00 56.61           N  
ANISOU 4182  ND2 ASN J 579     5234   6792   9485    878  -1438  -3077       N  
ATOM   4183  N   LEU J 580      23.298 -31.672  68.317  1.00 69.80           N  
ANISOU 4183  N   LEU J 580     6870   8540  11113    718  -1098  -2957       N  
ATOM   4184  CA  LEU J 580      22.387 -31.660  67.192  1.00 72.56           C  
ANISOU 4184  CA  LEU J 580     7210   8918  11442    723   -990  -2884       C  
ATOM   4185  C   LEU J 580      21.009 -31.203  67.657  1.00 69.17           C  
ANISOU 4185  C   LEU J 580     6880   8412  10991    691  -1060  -2783       C  
ATOM   4186  O   LEU J 580      20.615 -31.479  68.794  1.00 67.76           O  
ANISOU 4186  O   LEU J 580     6782   8164  10801    654  -1071  -2672       O  
ATOM   4187  CB  LEU J 580      22.297 -33.052  66.551  1.00 74.82           C  
ANISOU 4187  CB  LEU J 580     7432   9164  11834    670   -884  -2859       C  
ATOM   4188  CG  LEU J 580      23.623 -33.780  66.320  1.00 76.94           C  
ANISOU 4188  CG  LEU J 580     7586   9491  12155    705   -819  -2975       C  
ATOM   4189  CD1 LEU J 580      23.360 -35.211  65.898  1.00 76.69           C  
ANISOU 4189  CD1 LEU J 580     7480   9385  12274    655   -783  -2975       C  
ATOM   4190  CD2 LEU J 580      24.479 -33.059  65.287  1.00 82.91           C  
ANISOU 4190  CD2 LEU J 580     8236  10420  12846    816   -632  -3074       C  
ATOM   4191  N   PRO J 581      20.264 -30.490  66.819  1.00 71.25           N  
ANISOU 4191  N   PRO J 581     7143   8710  11220    761  -1053  -2747       N  
ATOM   4192  CA  PRO J 581      18.998 -29.902  67.268  1.00 69.20           C  
ANISOU 4192  CA  PRO J 581     6962   8399  10931    775  -1140  -2680       C  
ATOM   4193  C   PRO J 581      17.811 -30.838  67.098  1.00 56.46           C  
ANISOU 4193  C   PRO J 581     5382   6701   9369    720  -1115  -2582       C  
ATOM   4194  O   PRO J 581      17.888 -31.882  66.446  1.00 48.89           O  
ANISOU 4194  O   PRO J 581     4376   5699   8501    673  -1054  -2578       O  
ATOM   4195  CB  PRO J 581      18.875 -28.671  66.362  1.00 79.86           C  
ANISOU 4195  CB  PRO J 581     8308   9809  12225    941  -1216  -2721       C  
ATOM   4196  CG  PRO J 581      19.458 -29.139  65.065  1.00 84.19           C  
ANISOU 4196  CG  PRO J 581     8786  10383  12818    990  -1059  -2748       C  
ATOM   4197  CD  PRO J 581      20.554 -30.136  65.416  1.00 79.30           C  
ANISOU 4197  CD  PRO J 581     8088   9806  12238    873   -949  -2790       C  
ATOM   4198  N   GLY J 582      16.697 -30.442  67.715  1.00 60.69           N  
ANISOU 4198  N   GLY J 582     5975   7218   9866    745  -1174  -2539       N  
ATOM   4199  CA  GLY J 582      15.452 -31.175  67.595  1.00 56.34           C  
ANISOU 4199  CA  GLY J 582     5456   6610   9342    740  -1196  -2482       C  
ATOM   4200  C   GLY J 582      14.901 -31.710  68.902  1.00 46.45           C  
ANISOU 4200  C   GLY J 582     4227   5362   8058    714  -1179  -2458       C  
ATOM   4201  O   GLY J 582      15.649 -31.953  69.853  1.00 40.63           O  
ANISOU 4201  O   GLY J 582     3477   4628   7332    668  -1130  -2464       O  
ATOM   4202  N   GLU J 583      13.585 -31.898  68.957  1.00 39.62           N  
ANISOU 4202  N   GLU J 583     3387   4498   7170    778  -1222  -2434       N  
ATOM   4203  CA  GLU J 583      12.934 -32.505  70.110  1.00 41.89           C  
ANISOU 4203  CA  GLU J 583     3672   4818   7427    810  -1188  -2419       C  
ATOM   4204  C   GLU J 583      12.829 -34.010  69.906  1.00 41.96           C  
ANISOU 4204  C   GLU J 583     3710   4765   7470    798  -1264  -2427       C  
ATOM   4205  O   GLU J 583      12.372 -34.470  68.855  1.00 47.50           O  
ANISOU 4205  O   GLU J 583     4422   5400   8225    806  -1369  -2453       O  
ATOM   4206  CB  GLU J 583      11.538 -31.921  70.325  1.00 53.84           C  
ANISOU 4206  CB  GLU J 583     5191   6387   8879    946  -1192  -2423       C  
ATOM   4207  CG  GLU J 583      11.502 -30.566  70.993  1.00 67.43           C  
ANISOU 4207  CG  GLU J 583     6826   8192  10603    986  -1124  -2448       C  
ATOM   4208  CD  GLU J 583      10.106 -29.978  70.993  1.00 78.03           C  
ANISOU 4208  CD  GLU J 583     8161   9589  11899   1153  -1145  -2481       C  
ATOM   4209  OE1 GLU J 583       9.370 -30.209  70.011  1.00 79.82           O  
ANISOU 4209  OE1 GLU J 583     8494   9746  12088   1233  -1268  -2484       O  
ATOM   4210  OE2 GLU J 583       9.741 -29.291  71.971  1.00 84.07           O  
ANISOU 4210  OE2 GLU J 583     8794  10455  12694   1215  -1040  -2518       O  
ATOM   4211  N   VAL J 584      13.253 -34.775  70.910  1.00 36.47           N  
ANISOU 4211  N   VAL J 584     3007   4069   6782    799  -1244  -2424       N  
ATOM   4212  CA  VAL J 584      13.057 -36.218  70.926  1.00 39.37           C  
ANISOU 4212  CA  VAL J 584     3409   4383   7167    852  -1374  -2449       C  
ATOM   4213  C   VAL J 584      12.420 -36.599  72.256  1.00 44.53           C  
ANISOU 4213  C   VAL J 584     4124   5057   7736   1012  -1323  -2429       C  
ATOM   4214  O   VAL J 584      12.827 -36.118  73.320  1.00 50.29           O  
ANISOU 4214  O   VAL J 584     4808   5806   8494   1016  -1178  -2407       O  
ATOM   4215  CB  VAL J 584      14.369 -37.001  70.668  1.00 35.24           C  
ANISOU 4215  CB  VAL J 584     2874   3801   6716    780  -1396  -2437       C  
ATOM   4216  CG1 VAL J 584      14.894 -36.717  69.271  1.00 32.03           C  
ANISOU 4216  CG1 VAL J 584     2450   3372   6349    706  -1316  -2401       C  
ATOM   4217  CG2 VAL J 584      15.446 -36.657  71.691  1.00 48.15           C  
ANISOU 4217  CG2 VAL J 584     4474   5437   8383    745  -1333  -2438       C  
ATOM   4218  N   THR J 585      11.385 -37.431  72.185  1.00 47.87           N  
ANISOU 4218  N   THR J 585     4668   5449   8071   1166  -1430  -2460       N  
ATOM   4219  CA  THR J 585      10.724 -37.977  73.363  1.00 57.37           C  
ANISOU 4219  CA  THR J 585     6042   6619   9137   1382  -1364  -2475       C  
ATOM   4220  C   THR J 585      10.764 -39.490  73.237  1.00 65.23           C  
ANISOU 4220  C   THR J 585     7205   7494  10086   1487  -1627  -2518       C  
ATOM   4221  O   THR J 585      10.297 -40.041  72.235  1.00 75.97           O  
ANISOU 4221  O   THR J 585     8564   8830  11471   1486  -1849  -2572       O  
ATOM   4222  CB  THR J 585       9.287 -37.465  73.480  1.00 58.98           C  
ANISOU 4222  CB  THR J 585     6330   6886   9195   1538  -1251  -2513       C  
ATOM   4223  OG1 THR J 585       9.226 -36.105  73.030  1.00 62.57           O  
ANISOU 4223  OG1 THR J 585     6608   7441   9725   1423  -1152  -2485       O  
ATOM   4224  CG2 THR J 585       8.807 -37.533  74.929  1.00 56.46           C  
ANISOU 4224  CG2 THR J 585     6140   6572   8740   1744  -1002  -2556       C  
ATOM   4225  N   PHE J 586      11.336 -40.156  74.233  1.00 64.78           N  
ANISOU 4225  N   PHE J 586     7296   7330   9988   1584  -1638  -2508       N  
ATOM   4226  CA  PHE J 586      11.667 -41.569  74.131  1.00 58.44           C  
ANISOU 4226  CA  PHE J 586     6645   6399   9159   1679  -1956  -2548       C  
ATOM   4227  C   PHE J 586      10.702 -42.411  74.953  1.00 56.33           C  
ANISOU 4227  C   PHE J 586     6818   5995   8590   1965  -2037  -2595       C  
ATOM   4228  O   PHE J 586      10.255 -41.997  76.027  1.00 60.10           O  
ANISOU 4228  O   PHE J 586     7516   6429   8888   2096  -1766  -2594       O  
ATOM   4229  CB  PHE J 586      13.108 -41.817  74.579  1.00 54.18           C  
ANISOU 4229  CB  PHE J 586     6047   5785   8756   1612  -1999  -2508       C  
ATOM   4230  CG  PHE J 586      14.112 -41.571  73.498  1.00 51.03           C  
ANISOU 4230  CG  PHE J 586     5305   5493   8590   1382  -2055  -2535       C  
ATOM   4231  CD1 PHE J 586      14.299 -42.498  72.486  1.00 53.11           C  
ANISOU 4231  CD1 PHE J 586     5458   5749   8971   1350  -2331  -2651       C  
ATOM   4232  CD2 PHE J 586      14.841 -40.395  73.465  1.00 47.50           C  
ANISOU 4232  CD2 PHE J 586     4676   5129   8244   1199  -1829  -2491       C  
ATOM   4233  CE1 PHE J 586      15.209 -42.266  71.475  1.00 48.85           C  
ANISOU 4233  CE1 PHE J 586     4757   5238   8566   1159  -2162  -2622       C  
ATOM   4234  CE2 PHE J 586      15.752 -40.160  72.458  1.00 44.82           C  
ANISOU 4234  CE2 PHE J 586     4157   4835   8038   1010  -1832  -2545       C  
ATOM   4235  CZ  PHE J 586      15.932 -41.096  71.460  1.00 41.95           C  
ANISOU 4235  CZ  PHE J 586     3799   4432   7709   1012  -1904  -2556       C  
ATOM   4236  N   LEU J 587      10.383 -43.596  74.426  1.00 61.81           N  
ANISOU 4236  N   LEU J 587     7643   6620   9221   2074  -2414  -2669       N  
ATOM   4237  CA  LEU J 587       9.516 -44.573  75.085  1.00 65.77           C  
ANISOU 4237  CA  LEU J 587     8644   6977   9367   2369  -2597  -2730       C  
ATOM   4238  C   LEU J 587      10.318 -45.851  75.285  1.00 71.03           C  
ANISOU 4238  C   LEU J 587     9474   7484  10029   2473  -2997  -2745       C  
ATOM   4239  O   LEU J 587      10.391 -46.700  74.383  1.00 76.01           O  
ANISOU 4239  O   LEU J 587     9935   8125  10820   2477  -3398  -2844       O  
ATOM   4240  CB  LEU J 587       8.254 -44.836  74.266  1.00 63.19           C  
ANISOU 4240  CB  LEU J 587     8355   6697   8956   2452  -2780  -2830       C  
ATOM   4241  CG  LEU J 587       7.058 -43.919  74.526  1.00 63.31           C  
ANISOU 4241  CG  LEU J 587     8483   6805   8767   2529  -2448  -2850       C  
ATOM   4242  CD1 LEU J 587       5.909 -44.262  73.592  1.00 67.59           C  
ANISOU 4242  CD1 LEU J 587     9062   7346   9275   2606  -2708  -2950       C  
ATOM   4243  CD2 LEU J 587       6.621 -44.021  75.975  1.00 64.13           C  
ANISOU 4243  CD2 LEU J 587     9081   6844   8441   2791  -2201  -2864       C  
ATOM   4244  N   PRO J 588      10.956 -46.024  76.448  1.00 73.23           N  
ANISOU 4244  N   PRO J 588    10078   7587  10159   2570  -2926  -2663       N  
ATOM   4245  CA  PRO J 588      11.709 -47.256  76.721  1.00 77.93           C  
ANISOU 4245  CA  PRO J 588    10899   8000  10711   2710  -3355  -2668       C  
ATOM   4246  C   PRO J 588      10.761 -48.388  77.117  1.00 87.57           C  
ANISOU 4246  C   PRO J 588    12721   9063  11488   3045  -3704  -2731       C  
ATOM   4247  O   PRO J 588      10.021 -48.271  78.090  1.00 93.89           O  
ANISOU 4247  O   PRO J 588    14094   9739  11842   3232  -3488  -2680       O  
ATOM   4248  CB  PRO J 588      12.625 -46.860  77.886  1.00 80.67           C  
ANISOU 4248  CB  PRO J 588    11469   8152  11032   2691  -3121  -2520       C  
ATOM   4249  CG  PRO J 588      11.936 -45.709  78.554  1.00 81.50           C  
ANISOU 4249  CG  PRO J 588    11696   8266  11002   2664  -2605  -2481       C  
ATOM   4250  CD  PRO J 588      11.047 -45.042  77.542  1.00 76.48           C  
ANISOU 4250  CD  PRO J 588    10647   7934  10481   2554  -2464  -2576       C  
ATOM   4251  N   LEU J 589      10.803 -49.488  76.353  1.00 86.11           N  
ANISOU 4251  N   LEU J 589    12420   8884  11415   3135  -4248  -2867       N  
ATOM   4252  CA  LEU J 589       9.897 -50.607  76.607  1.00 91.53           C  
ANISOU 4252  CA  LEU J 589    13655   9426  11697   3481  -4680  -2947       C  
ATOM   4253  C   LEU J 589      10.186 -51.300  77.930  1.00 96.98           C  
ANISOU 4253  C   LEU J 589    15118   9823  11907   3756  -4828  -2842       C  
ATOM   4254  O   LEU J 589       9.268 -51.848  78.552  1.00101.43           O  
ANISOU 4254  O   LEU J 589    16380  10239  11918   4066  -4949  -2835       O  
ATOM   4255  CB  LEU J 589       9.980 -51.634  75.475  1.00 90.05           C  
ANISOU 4255  CB  LEU J 589    13095   9275  11846   3529  -5267  -3134       C  
ATOM   4256  CG  LEU J 589       9.502 -51.243  74.079  1.00 84.23           C  
ANISOU 4256  CG  LEU J 589    11758   8691  11552   3280  -5081  -3199       C  
ATOM   4257  CD1 LEU J 589       9.338 -52.476  73.204  1.00 89.79           C  
ANISOU 4257  CD1 LEU J 589    12330   9254  12534   3333  -5368  -3322       C  
ATOM   4258  CD2 LEU J 589       8.207 -50.483  74.176  1.00 81.36           C  
ANISOU 4258  CD2 LEU J 589    11593   8407  10911   3361  -4895  -3177       C  
ATOM   4259  N   ASN J 590      11.443 -51.288  78.376  1.00 98.60           N  
ANISOU 4259  N   ASN J 590    15270   9915  12277   3661  -4813  -2746       N  
ATOM   4260  CA  ASN J 590      11.828 -52.049  79.557  1.00104.40           C  
ANISOU 4260  CA  ASN J 590    16775  10307  12585   3916  -5030  -2613       C  
ATOM   4261  C   ASN J 590      11.260 -51.479  80.852  1.00111.94           C  
ANISOU 4261  C   ASN J 590    18502  11019  13012   4028  -4530  -2381       C  
ATOM   4262  O   ASN J 590      11.238 -52.189  81.862  1.00121.77           O  
ANISOU 4262  O   ASN J 590    20589  11952  13725   4271  -4677  -2203       O  
ATOM   4263  CB  ASN J 590      13.357 -52.146  79.638  1.00102.57           C  
ANISOU 4263  CB  ASN J 590    16243  10012  12717   3763  -5134  -2570       C  
ATOM   4264  CG  ASN J 590      13.995 -50.950  80.336  1.00105.62           C  
ANISOU 4264  CG  ASN J 590    16574  10310  13246   3539  -4554  -2328       C  
ATOM   4265  OD1 ASN J 590      13.622 -49.797  80.103  1.00102.50           O  
ANISOU 4265  OD1 ASN J 590    15838  10086  13020   3336  -4067  -2317       O  
ATOM   4266  ND2 ASN J 590      14.963 -51.226  81.202  1.00110.27           N  
ANISOU 4266  ND2 ASN J 590    17512  10610  13774   3571  -4642  -2153       N  
ATOM   4267  N   LYS J 591      10.794 -50.232  80.849  1.00110.17           N  
ANISOU 4267  N   LYS J 591    17975  11016  12870   3784  -3894  -2331       N  
ATOM   4268  CA  LYS J 591      10.339 -49.568  82.066  1.00110.66           C  
ANISOU 4268  CA  LYS J 591    18421  11166  12460   3613  -3205  -1982       C  
ATOM   4269  C   LYS J 591       8.965 -48.942  81.864  1.00108.84           C  
ANISOU 4269  C   LYS J 591    18108  11246  12001   3621  -2800  -2078       C  
ATOM   4270  O   LYS J 591       8.739 -47.767  82.161  1.00108.37           O  
ANISOU 4270  O   LYS J 591    17716  11431  12028   3351  -2164  -1958       O  
ATOM   4271  CB  LYS J 591      11.349 -48.518  82.517  1.00111.75           C  
ANISOU 4271  CB  LYS J 591    18150  11334  12975   3214  -2744  -1756       C  
ATOM   4272  CG  LYS J 591      12.384 -49.042  83.500  1.00119.68           C  
ANISOU 4272  CG  LYS J 591    19638  11978  13855   3191  -2871  -1478       C  
ATOM   4273  CD  LYS J 591      11.720 -49.748  84.672  1.00128.51           C  
ANISOU 4273  CD  LYS J 591    21720  12924  14184   3347  -2754  -1187       C  
ATOM   4274  CE  LYS J 591      12.217 -51.179  84.822  1.00131.96           C  
ANISOU 4274  CE  LYS J 591    22803  12953  14384   3724  -3500  -1199       C  
ATOM   4275  NZ  LYS J 591      11.436 -51.923  85.848  1.00135.18           N  
ANISOU 4275  NZ  LYS J 591    24243  13200  13919   3935  -3432   -935       N  
ATOM   4276  N   LEU J 592       8.020 -49.730  81.361  1.00113.59           N  
ANISOU 4276  N   LEU J 592    15074  13916  14167  -2194  -1367  -3523       N  
ATOM   4277  CA  LEU J 592       6.625 -49.315  81.238  1.00106.89           C  
ANISOU 4277  CA  LEU J 592    14114  13223  13275  -2318  -1114  -3290       C  
ATOM   4278  C   LEU J 592       5.792 -50.189  82.168  1.00 99.03           C  
ANISOU 4278  C   LEU J 592    13210  12210  12208  -2252  -1340  -3223       C  
ATOM   4279  O   LEU J 592       5.400 -51.302  81.805  1.00 97.94           O  
ANISOU 4279  O   LEU J 592    12930  12061  12224  -2061  -1404  -3512       O  
ATOM   4280  CB  LEU J 592       6.141 -49.410  79.794  1.00106.19           C  
ANISOU 4280  CB  LEU J 592    13739  13210  13397  -2301   -708  -3520       C  
ATOM   4281  CG  LEU J 592       6.886 -48.535  78.786  1.00106.12           C  
ANISOU 4281  CG  LEU J 592    13769  13162  13392  -2367   -393  -3577       C  
ATOM   4282  CD1 LEU J 592       6.162 -48.501  77.460  1.00104.46           C  
ANISOU 4282  CD1 LEU J 592    13395  12975  13321  -2413    102  -3723       C  
ATOM   4283  CD2 LEU J 592       7.068 -47.120  79.321  1.00107.05           C  
ANISOU 4283  CD2 LEU J 592    14141  13303  13229  -2477   -459  -3194       C  
ATOM   4284  N   ASP J 593       5.534 -49.679  83.368  1.00103.41           N  
ANISOU 4284  N   ASP J 593    14018  12740  12532  -2411  -1444  -2880       N  
ATOM   4285  CA  ASP J 593       4.703 -50.369  84.351  1.00104.44           C  
ANISOU 4285  CA  ASP J 593    14358  12811  12511  -2393  -1578  -2760       C  
ATOM   4286  C   ASP J 593       3.273 -50.398  83.834  1.00101.80           C  
ANISOU 4286  C   ASP J 593    13760  12671  12249  -2414  -1319  -2721       C  
ATOM   4287  O   ASP J 593       2.538 -49.413  83.940  1.00102.74           O  
ANISOU 4287  O   ASP J 593    13779  12939  12318  -2623  -1086  -2474       O  
ATOM   4288  CB  ASP J 593       4.792 -49.670  85.703  1.00101.45           C  
ANISOU 4288  CB  ASP J 593    14302  12339  11905  -2646  -1612  -2432       C  
ATOM   4289  CG  ASP J 593       6.090 -49.963  86.427  1.00100.58           C  
ANISOU 4289  CG  ASP J 593    14570  11963  11684  -2594  -1920  -2477       C  
ATOM   4290  OD1 ASP J 593       7.163 -49.622  85.886  1.00100.37           O  
ANISOU 4290  OD1 ASP J 593    14443  11927  11766  -2544  -1990  -2614       O  
ATOM   4291  OD2 ASP J 593       6.040 -50.532  87.538  1.00102.70           O  
ANISOU 4291  OD2 ASP J 593    15290  12003  11729  -2600  -2076  -2375       O  
ATOM   4292  N   VAL J 594       2.872 -51.527  83.258  1.00106.08           N  
ANISOU 4292  N   VAL J 594    14164  13209  12931  -2174  -1386  -3013       N  
ATOM   4293  CA  VAL J 594       1.578 -51.658  82.597  1.00107.00           C  
ANISOU 4293  CA  VAL J 594    13996  13495  13163  -2167  -1144  -3044       C  
ATOM   4294  C   VAL J 594       0.600 -52.358  83.535  1.00112.98           C  
ANISOU 4294  C   VAL J 594    14985  14214  13727  -2094  -1291  -2931       C  
ATOM   4295  O   VAL J 594       0.815 -53.508  83.935  1.00116.05           O  
ANISOU 4295  O   VAL J 594    15609  14432  14053  -1828  -1629  -3136       O  
ATOM   4296  CB  VAL J 594       1.706 -52.403  81.256  1.00103.25           C  
ANISOU 4296  CB  VAL J 594    13164  13037  13029  -1980  -1059  -3507       C  
ATOM   4297  CG1 VAL J 594       2.165 -51.447  80.171  1.00100.44           C  
ANISOU 4297  CG1 VAL J 594    12616  12739  12808  -2140   -691  -3525       C  
ATOM   4298  CG2 VAL J 594       2.703 -53.554  81.364  1.00103.99           C  
ANISOU 4298  CG2 VAL J 594    13328  12953  13231  -1694  -1449  -3915       C  
ATOM   4299  N   ARG J 595      -0.468 -51.653  83.900  1.00116.73           N  
ANISOU 4299  N   ARG J 595    15434  14831  14088  -2303  -1053  -2628       N  
ATOM   4300  CA  ARG J 595      -1.598 -52.278  84.572  1.00126.79           C  
ANISOU 4300  CA  ARG J 595    16882  16098  15196  -2246  -1084  -2542       C  
ATOM   4301  C   ARG J 595      -2.534 -52.848  83.515  1.00133.46           C  
ANISOU 4301  C   ARG J 595    17363  17084  16264  -2073   -990  -2780       C  
ATOM   4302  O   ARG J 595      -2.990 -52.119  82.627  1.00135.24           O  
ANISOU 4302  O   ARG J 595    17239  17486  16661  -2196   -691  -2755       O  
ATOM   4303  CB  ARG J 595      -2.337 -51.273  85.456  1.00124.88           C  
ANISOU 4303  CB  ARG J 595    16723  15950  14777  -2568   -834  -2177       C  
ATOM   4304  CG  ARG J 595      -1.505 -50.654  86.569  1.00124.92           C  
ANISOU 4304  CG  ARG J 595    17051  15802  14610  -2803   -863  -1980       C  
ATOM   4305  CD  ARG J 595      -2.374 -49.768  87.453  1.00125.21           C  
ANISOU 4305  CD  ARG J 595    17089  15934  14551  -3136   -572  -1734       C  
ATOM   4306  NE  ARG J 595      -1.772 -48.463  87.708  1.00126.87           N  
ANISOU 4306  NE  ARG J 595    17154  16200  14853  -3403   -475  -1652       N  
ATOM   4307  CZ  ARG J 595      -1.245 -48.098  88.873  1.00130.10           C  
ANISOU 4307  CZ  ARG J 595    17845  16433  15154  -3661   -439  -1549       C  
ATOM   4308  NH1 ARG J 595      -1.247 -48.943  89.896  1.00133.94           N  
ANISOU 4308  NH1 ARG J 595    18867  16644  15381  -3697   -452  -1472       N  
ATOM   4309  NH2 ARG J 595      -0.719 -46.890  89.019  1.00128.65           N  
ANISOU 4309  NH2 ARG J 595    17452  16318  15110  -3872   -387  -1546       N  
ATOM   4310  N   ASP J 596      -2.809 -54.150  83.597  1.00139.02           N  
ANISOU 4310  N   ASP J 596    18184  17679  16958  -1763  -1263  -3038       N  
ATOM   4311  CA  ASP J 596      -3.687 -54.796  82.629  1.00139.07           C  
ANISOU 4311  CA  ASP J 596    17821  17797  17221  -1585  -1204  -3336       C  
ATOM   4312  C   ASP J 596      -5.120 -54.319  82.841  1.00136.16           C  
ANISOU 4312  C   ASP J 596    17400  17599  16734  -1740   -939  -3053       C  
ATOM   4313  O   ASP J 596      -5.712 -54.556  83.899  1.00139.01           O  
ANISOU 4313  O   ASP J 596    18128  17902  16789  -1730  -1020  -2851       O  
ATOM   4314  CB  ASP J 596      -3.593 -56.314  82.757  1.00143.70           C  
ANISOU 4314  CB  ASP J 596    18559  18212  17828  -1153  -1657  -3749       C  
ATOM   4315  CG  ASP J 596      -4.041 -57.035  81.499  1.00145.28           C  
ANISOU 4315  CG  ASP J 596    18234  18502  18464   -957  -1628  -4254       C  
ATOM   4316  OD1 ASP J 596      -3.233 -57.135  80.551  1.00144.75           O  
ANISOU 4316  OD1 ASP J 596    17812  18428  18761   -940  -1568  -4626       O  
ATOM   4317  OD2 ASP J 596      -5.199 -57.502  81.457  1.00147.08           O  
ANISOU 4317  OD2 ASP J 596    18401  18796  18687   -836  -1635  -4308       O  
ATOM   4318  N   THR J 597      -5.669 -53.640  81.840  1.00130.86           N  
ANISOU 4318  N   THR J 597    16325  17111  16285  -1881   -603  -3049       N  
ATOM   4319  CA  THR J 597      -6.962 -52.983  81.962  1.00119.70           C  
ANISOU 4319  CA  THR J 597    14822  15876  14782  -2035   -348  -2789       C  
ATOM   4320  C   THR J 597      -8.096 -53.923  81.570  1.00112.91           C  
ANISOU 4320  C   THR J 597    13812  15064  14026  -1823   -382  -3006       C  
ATOM   4321  O   THR J 597      -7.912 -54.871  80.802  1.00113.09           O  
ANISOU 4321  O   THR J 597    13640  15018  14311  -1595   -512  -3419       O  
ATOM   4322  CB  THR J 597      -7.007 -51.724  81.094  1.00109.24           C  
ANISOU 4322  CB  THR J 597    13236  14681  13587  -2240    -17  -2676       C  
ATOM   4323  OG1 THR J 597      -6.299 -51.959  79.870  1.00111.28           O  
ANISOU 4323  OG1 THR J 597    13295  14862  14124  -2173     73  -2980       O  
ATOM   4324  CG2 THR J 597      -6.368 -50.554  81.825  1.00102.04           C  
ANISOU 4324  CG2 THR J 597    12493  13780  12497  -2461      4  -2384       C  
ATOM   4325  N   ALA J 598      -9.282 -53.644  82.111  1.00112.47           N  
ANISOU 4325  N   ALA J 598    13814  15127  13791  -1900   -262  -2772       N  
ATOM   4326  CA  ALA J 598     -10.480 -54.442  81.871  1.00111.51           C  
ANISOU 4326  CA  ALA J 598    13589  15063  13718  -1704   -294  -2932       C  
ATOM   4327  C   ALA J 598     -11.519 -53.561  81.191  1.00106.39           C  
ANISOU 4327  C   ALA J 598    12616  14619  13189  -1868     51  -2809       C  
ATOM   4328  O   ALA J 598     -12.122 -52.693  81.833  1.00102.14           O  
ANISOU 4328  O   ALA J 598    12142  14205  12464  -2056    209  -2505       O  
ATOM   4329  CB  ALA J 598     -11.023 -55.027  83.174  1.00116.83           C  
ANISOU 4329  CB  ALA J 598    14719  15655  14016  -1605   -468  -2786       C  
ATOM   4330  N   TYR J 599     -11.735 -53.796  79.901  1.00100.98           N  
ANISOU 4330  N   TYR J 599    11592  13946  12830  -1794    176  -3087       N  
ATOM   4331  CA  TYR J 599     -12.616 -53.011  79.055  1.00 96.31           C  
ANISOU 4331  CA  TYR J 599    10758  13478  12356  -1914    501  -3013       C  
ATOM   4332  C   TYR J 599     -14.074 -53.441  79.236  1.00 89.49           C  
ANISOU 4332  C   TYR J 599     9825  12729  11450  -1802    495  -3019       C  
ATOM   4333  O   TYR J 599     -14.347 -54.603  79.542  1.00 90.73           O  
ANISOU 4333  O   TYR J 599    10036  12832  11605  -1574    253  -3230       O  
ATOM   4334  CB  TYR J 599     -12.199 -53.165  77.597  1.00 89.44           C  
ANISOU 4334  CB  TYR J 599     9638  12500  11843  -1915    711  -3335       C  
ATOM   4335  CG  TYR J 599     -10.792 -52.682  77.331  1.00 89.50           C  
ANISOU 4335  CG  TYR J 599     9733  12392  11881  -2028    769  -3338       C  
ATOM   4336  CD1 TYR J 599     -10.312 -51.524  77.928  1.00 88.50           C  
ANISOU 4336  CD1 TYR J 599     9823  12310  11495  -2182    776  -2977       C  
ATOM   4337  CD2 TYR J 599      -9.933 -53.401  76.510  1.00 90.96           C  
ANISOU 4337  CD2 TYR J 599     9758  12424  12378  -1974    808  -3754       C  
ATOM   4338  CE1 TYR J 599      -9.025 -51.080  77.695  1.00 88.69           C  
ANISOU 4338  CE1 TYR J 599     9949  12223  11527  -2262    807  -2984       C  
ATOM   4339  CE2 TYR J 599      -8.642 -52.966  76.271  1.00 91.21           C  
ANISOU 4339  CE2 TYR J 599     9884  12348  12424  -2075    880  -3767       C  
ATOM   4340  CZ  TYR J 599      -8.192 -51.805  76.866  1.00 89.95           C  
ANISOU 4340  CZ  TYR J 599     9988  12229  11958  -2209    868  -3358       C  
ATOM   4341  OH  TYR J 599      -6.908 -51.371  76.631  1.00 90.32           O  
ANISOU 4341  OH  TYR J 599    10150  12165  12003  -2286    919  -3377       O  
ATOM   4342  N   PRO J 600     -15.022 -52.518  79.064  1.00 91.81           N  
ANISOU 4342  N   PRO J 600    10023  13168  11691  -1920    721  -2815       N  
ATOM   4343  CA  PRO J 600     -16.435 -52.861  79.270  1.00 91.16           C  
ANISOU 4343  CA  PRO J 600     9872  13207  11558  -1820    726  -2814       C  
ATOM   4344  C   PRO J 600     -16.953 -53.837  78.223  1.00 95.87           C  
ANISOU 4344  C   PRO J 600    10226  13740  12460  -1636    733  -3188       C  
ATOM   4345  O   PRO J 600     -16.407 -53.978  77.126  1.00100.92           O  
ANISOU 4345  O   PRO J 600    10691  14255  13397  -1657    866  -3441       O  
ATOM   4346  CB  PRO J 600     -17.153 -51.511  79.161  1.00 88.17           C  
ANISOU 4346  CB  PRO J 600     9411  12985  11106  -1976    953  -2569       C  
ATOM   4347  CG  PRO J 600     -16.099 -50.488  79.406  1.00 86.83           C  
ANISOU 4347  CG  PRO J 600     9354  12790  10849  -2145    976  -2392       C  
ATOM   4348  CD  PRO J 600     -14.833 -51.070  78.867  1.00 87.09           C  
ANISOU 4348  CD  PRO J 600     9431  12631  11027  -2112    915  -2575       C  
ATOM   4349  N   GLU J 601     -18.034 -54.515  78.587  1.00 95.20           N  
ANISOU 4349  N   GLU J 601    10136  13727  12308  -1469    616  -3254       N  
ATOM   4350  CA  GLU J 601     -18.645 -55.549  77.750  1.00 96.64           C  
ANISOU 4350  CA  GLU J 601    10071  13857  12792  -1258    560  -3662       C  
ATOM   4351  C   GLU J 601     -19.847 -55.006  76.990  1.00 94.50           C  
ANISOU 4351  C   GLU J 601     9588  13681  12637  -1327    838  -3624       C  
ATOM   4352  O   GLU J 601     -20.911 -55.623  76.944  1.00 94.87           O  
ANISOU 4352  O   GLU J 601     9535  13781  12729  -1159    763  -3772       O  
ATOM   4353  CB  GLU J 601     -19.039 -56.745  78.608  1.00104.98           C  
ANISOU 4353  CB  GLU J 601    11319  14891  13678   -955    186  -3810       C  
ATOM   4354  CG  GLU J 601     -18.901 -58.087  77.913  1.00113.24           C  
ANISOU 4354  CG  GLU J 601    12144  15803  15081   -655    -71  -4391       C  
ATOM   4355  CD  GLU J 601     -18.480 -59.190  78.865  1.00120.34           C  
ANISOU 4355  CD  GLU J 601    13401  16577  15746   -310   -568  -4554       C  
ATOM   4356  OE1 GLU J 601     -17.827 -58.879  79.884  1.00122.51           O  
ANISOU 4356  OE1 GLU J 601    14100  16804  15645   -380   -648  -4228       O  
ATOM   4357  OE2 GLU J 601     -18.805 -60.366  78.595  1.00124.34           O  
ANISOU 4357  OE2 GLU J 601    13798  17007  16439     51   -894  -5033       O  
ATOM   4358  N   THR J 602     -19.692 -53.837  76.381  1.00 91.04           N  
ANISOU 4358  N   THR J 602     9129  13241  12222  -1541   1135  -3435       N  
ATOM   4359  CA  THR J 602     -20.777 -53.186  75.666  1.00 99.78           C  
ANISOU 4359  CA  THR J 602    10136  14396  13382  -1585   1381  -3372       C  
ATOM   4360  C   THR J 602     -20.651 -53.414  74.163  1.00104.60           C  
ANISOU 4360  C   THR J 602    10589  14790  14365  -1640   1671  -3688       C  
ATOM   4361  O   THR J 602     -19.629 -53.882  73.655  1.00104.35           O  
ANISOU 4361  O   THR J 602    10494  14592  14563  -1690   1734  -3945       O  
ATOM   4362  CB  THR J 602     -20.804 -51.688  75.979  1.00 87.04           C  
ANISOU 4362  CB  THR J 602     8683  12882  11508  -1726   1485  -2994       C  
ATOM   4363  OG1 THR J 602     -21.643 -51.013  75.033  1.00 87.07           O  
ANISOU 4363  OG1 THR J 602     8663  12849  11572  -1730   1711  -2982       O  
ATOM   4364  CG2 THR J 602     -19.402 -51.112  75.930  1.00 86.82           C  
ANISOU 4364  CG2 THR J 602     8809  12742  11437  -1860   1519  -2900       C  
ATOM   4365  N   ASN J 603     -21.726 -53.074  73.449  1.00108.36           N  
ANISOU 4365  N   ASN J 603    11013  15251  14908  -1645   1883  -3694       N  
ATOM   4366  CA  ASN J 603     -21.798 -53.263  72.008  1.00114.18           C  
ANISOU 4366  CA  ASN J 603    11657  15736  15991  -1740   2254  -3997       C  
ATOM   4367  C   ASN J 603     -21.607 -51.977  71.218  1.00109.06           C  
ANISOU 4367  C   ASN J 603    11327  14911  15199  -1901   2608  -3767       C  
ATOM   4368  O   ASN J 603     -21.296 -52.044  70.023  1.00113.83           O  
ANISOU 4368  O   ASN J 603    11987  15223  16042  -2048   3012  -3995       O  
ATOM   4369  CB  ASN J 603     -23.144 -53.890  71.624  1.00122.84           C  
ANISOU 4369  CB  ASN J 603    12536  16856  17281  -1622   2271  -4221       C  
ATOM   4370  CG  ASN J 603     -23.076 -54.667  70.325  1.00131.68           C  
ANISOU 4370  CG  ASN J 603    13421  17706  18906  -1714   2594  -4734       C  
ATOM   4371  OD1 ASN J 603     -22.047 -55.257  69.994  1.00134.66           O  
ANISOU 4371  OD1 ASN J 603    13656  17948  19563  -1789   2662  -5061       O  
ATOM   4372  ND2 ASN J 603     -24.176 -54.675  69.582  1.00137.46           N  
ANISOU 4372  ND2 ASN J 603    14092  18350  19788  -1723   2813  -4852       N  
ATOM   4373  N   ASP J 604     -21.786 -50.815  71.845  1.00101.72           N  
ANISOU 4373  N   ASP J 604    10635  14124  13890  -1866   2475  -3366       N  
ATOM   4374  CA  ASP J 604     -21.627 -49.533  71.170  1.00 99.60           C  
ANISOU 4374  CA  ASP J 604    10753  13674  13415  -1921   2700  -3161       C  
ATOM   4375  C   ASP J 604     -20.366 -48.796  71.613  1.00 96.27           C  
ANISOU 4375  C   ASP J 604    10550  13248  12780  -1978   2605  -2964       C  
ATOM   4376  O   ASP J 604     -20.278 -47.574  71.453  1.00 95.50           O  
ANISOU 4376  O   ASP J 604    10794  13081  12410  -1935   2615  -2748       O  
ATOM   4377  CB  ASP J 604     -22.868 -48.666  71.388  1.00 95.07           C  
ANISOU 4377  CB  ASP J 604    10278  13237  12608  -1771   2579  -2954       C  
ATOM   4378  CG  ASP J 604     -23.453 -48.820  72.778  1.00 92.60           C  
ANISOU 4378  CG  ASP J 604     9691  13304  12188  -1669   2209  -2845       C  
ATOM   4379  OD1 ASP J 604     -22.823 -49.497  73.618  1.00 92.51           O  
ANISOU 4379  OD1 ASP J 604     9525  13416  12210  -1711   2040  -2870       O  
ATOM   4380  OD2 ASP J 604     -24.549 -48.273  73.029  1.00 90.74           O  
ANISOU 4380  OD2 ASP J 604     9433  13219  11826  -1547   2109  -2754       O  
ATOM   4381  N   ALA J 605     -19.388 -49.516  72.158  1.00 78.64           N  
ANISOU 4381  N   ALA J 605    10919  11314   7648      9   2485  -1924       N  
ATOM   4382  CA  ALA J 605     -18.101 -48.926  72.511  1.00 76.40           C  
ANISOU 4382  CA  ALA J 605    10552  11090   7386     20   2390  -1796       C  
ATOM   4383  C   ALA J 605     -17.030 -49.997  72.385  1.00 74.89           C  
ANISOU 4383  C   ALA J 605    10394  10880   7182    -94   2204  -1954       C  
ATOM   4384  O   ALA J 605     -17.055 -50.995  73.111  1.00 74.67           O  
ANISOU 4384  O   ALA J 605    10486  10876   7010   -161   2091  -2060       O  
ATOM   4385  CB  ALA J 605     -18.121 -48.337  73.923  1.00 77.55           C  
ANISOU 4385  CB  ALA J 605    10714  11345   7405     64   2399  -1632       C  
ATOM   4386  N   ILE J 606     -16.099 -49.782  71.461  1.00 70.16           N  
ANISOU 4386  N   ILE J 606     9683  10250   6725   -109   2163  -1971       N  
ATOM   4387  CA  ILE J 606     -15.036 -50.734  71.154  1.00 72.10           C  
ANISOU 4387  CA  ILE J 606     9908  10491   6997   -209   1987  -2138       C  
ATOM   4388  C   ILE J 606     -13.723 -50.148  71.660  1.00 65.74           C  
ANISOU 4388  C   ILE J 606     9027   9761   6189   -198   1876  -2039       C  
ATOM   4389  O   ILE J 606     -13.516 -48.931  71.553  1.00 58.33           O  
ANISOU 4389  O   ILE J 606     8012   8840   5312   -113   1965  -1864       O  
ATOM   4390  CB  ILE J 606     -14.983 -51.028  69.645  1.00 83.97           C  
ANISOU 4390  CB  ILE J 606    11322  11912   8672   -252   2038  -2264       C  
ATOM   4391  CG1 ILE J 606     -16.383 -50.916  69.035  1.00 98.01           C  
ANISOU 4391  CG1 ILE J 606    13143  13607  10490   -229   2222  -2277       C  
ATOM   4392  CG2 ILE J 606     -14.420 -52.414  69.369  1.00 81.86           C  
ANISOU 4392  CG2 ILE J 606    11052  11632   8420   -364   1867  -2504       C  
ATOM   4393  CD1 ILE J 606     -16.418 -51.100  67.533  1.00105.65           C  
ANISOU 4393  CD1 ILE J 606    14027  14483  11633   -288   2306  -2388       C  
ATOM   4394  N   PRO J 607     -12.820 -50.945  72.233  1.00 65.93           N  
ANISOU 4394  N   PRO J 607     9074   9834   6143   -273   1667  -2148       N  
ATOM   4395  CA  PRO J 607     -11.518 -50.397  72.638  1.00 64.85           C  
ANISOU 4395  CA  PRO J 607     8852   9771   6016   -269   1548  -2083       C  
ATOM   4396  C   PRO J 607     -10.695 -49.962  71.435  1.00 69.69           C  
ANISOU 4396  C   PRO J 607     9307  10369   6804   -248   1569  -2104       C  
ATOM   4397  O   PRO J 607     -10.708 -50.610  70.385  1.00 73.38           O  
ANISOU 4397  O   PRO J 607     9721  10785   7374   -288   1578  -2248       O  
ATOM   4398  CB  PRO J 607     -10.857 -51.563  73.383  1.00 63.55           C  
ANISOU 4398  CB  PRO J 607     8754   9648   5745   -350   1286  -2229       C  
ATOM   4399  CG  PRO J 607     -11.993 -52.452  73.780  1.00 63.54           C  
ANISOU 4399  CG  PRO J 607     8921   9606   5617   -378   1298  -2294       C  
ATOM   4400  CD  PRO J 607     -12.991 -52.336  72.682  1.00 66.60           C  
ANISOU 4400  CD  PRO J 607     9279   9911   6114   -349   1505  -2322       C  
ATOM   4401  N   MET J 608      -9.997 -48.833  71.597  1.00 59.68           N  
ANISOU 4401  N   MET J 608     7965   9148   5562   -188   1585  -1958       N  
ATOM   4402  CA  MET J 608      -9.183 -48.291  70.512  1.00 56.49           C  
ANISOU 4402  CA  MET J 608     7430   8738   5296   -154   1611  -1952       C  
ATOM   4403  C   MET J 608      -8.051 -49.240  70.143  1.00 57.57           C  
ANISOU 4403  C   MET J 608     7470   8918   5486   -226   1423  -2160       C  
ATOM   4404  O   MET J 608      -7.812 -49.505  68.958  1.00 64.90           O  
ANISOU 4404  O   MET J 608     8307   9816   6537   -243   1468  -2252       O  
ATOM   4405  CB  MET J 608      -8.625 -46.924  70.912  1.00 41.08           C  
ANISOU 4405  CB  MET J 608     5437   6834   3337    -73   1636  -1765       C  
ATOM   4406  CG  MET J 608      -7.620 -46.344  69.928  1.00 40.48           C  
ANISOU 4406  CG  MET J 608     5247   6769   3366    -32   1635  -1758       C  
ATOM   4407  SD  MET J 608      -7.459 -44.551  70.035  1.00 46.21           S  
ANISOU 4407  SD  MET J 608     5962   7497   4099     95   1743  -1506       S  
ATOM   4408  CE  MET J 608      -9.081 -44.012  69.505  1.00 48.03           C  
ANISOU 4408  CE  MET J 608     6270   7624   4356    198   1980  -1342       C  
ATOM   4409  N   ILE J 609      -7.373 -49.798  71.152  1.00 58.13           N  
ANISOU 4409  N   ILE J 609     7555   9059   5471   -264   1204  -2236       N  
ATOM   4410  CA  ILE J 609      -6.245 -50.690  70.915  1.00 59.02           C  
ANISOU 4410  CA  ILE J 609     7565   9211   5649   -298    984  -2425       C  
ATOM   4411  C   ILE J 609      -6.677 -51.990  70.239  1.00 61.97           C  
ANISOU 4411  C   ILE J 609     7940   9519   6087   -360    957  -2613       C  
ATOM   4412  O   ILE J 609      -5.848 -52.665  69.615  1.00 64.38           O  
ANISOU 4412  O   ILE J 609     8112   9840   6508   -376    837  -2772       O  
ATOM   4413  CB  ILE J 609      -5.514 -50.947  72.249  1.00 57.18           C  
ANISOU 4413  CB  ILE J 609     7378   9039   5307   -304    727  -2430       C  
ATOM   4414  CG1 ILE J 609      -4.105 -51.487  72.000  1.00 58.35           C  
ANISOU 4414  CG1 ILE J 609     7388   9220   5563   -286    489  -2573       C  
ATOM   4415  CG2 ILE J 609      -6.322 -51.876  73.155  1.00 56.09           C  
ANISOU 4415  CG2 ILE J 609     7427   8855   5028   -357    637  -2454       C  
ATOM   4416  CD1 ILE J 609      -3.379 -51.859  73.247  1.00 59.95           C  
ANISOU 4416  CD1 ILE J 609     7658   9431   5690   -284    196  -2566       C  
ATOM   4417  N   SER J 610      -7.964 -52.344  70.312  1.00 60.17           N  
ANISOU 4417  N   SER J 610     7845   9221   5797   -388   1069  -2604       N  
ATOM   4418  CA  SER J 610      -8.468 -53.498  69.580  1.00 66.29           C  
ANISOU 4418  CA  SER J 610     8618   9929   6640   -449   1059  -2788       C  
ATOM   4419  C   SER J 610      -8.438 -53.288  68.071  1.00 59.58           C  
ANISOU 4419  C   SER J 610     7617   9052   5968   -469   1231  -2846       C  
ATOM   4420  O   SER J 610      -8.418 -54.272  67.323  1.00 54.11           O  
ANISOU 4420  O   SER J 610     6847   8330   5380   -532   1189  -3039       O  
ATOM   4421  CB  SER J 610      -9.896 -53.823  70.022  1.00 80.15           C  
ANISOU 4421  CB  SER J 610    10559  11619   8274   -464   1147  -2764       C  
ATOM   4422  OG  SER J 610     -10.619 -54.448  68.976  1.00 88.83           O  
ANISOU 4422  OG  SER J 610    11635  12642   9473   -513   1248  -2902       O  
ATOM   4423  N   LYS J 611      -8.437 -52.039  67.607  1.00 56.20           N  
ANISOU 4423  N   LYS J 611     7153   8625   5575   -415   1414  -2678       N  
ATOM   4424  CA  LYS J 611      -8.413 -51.742  66.180  1.00 61.52           C  
ANISOU 4424  CA  LYS J 611     7717   9262   6396   -433   1581  -2697       C  
ATOM   4425  C   LYS J 611      -7.050 -51.221  65.731  1.00 61.38           C  
ANISOU 4425  C   LYS J 611     7551   9321   6448   -400   1535  -2684       C  
ATOM   4426  O   LYS J 611      -6.959 -50.434  64.785  1.00 64.12           O  
ANISOU 4426  O   LYS J 611     7857   9647   6860   -371   1693  -2588       O  
ATOM   4427  CB  LYS J 611      -9.515 -50.747  65.823  1.00 52.65           C  
ANISOU 4427  CB  LYS J 611     6685   8058   5261   -376   1814  -2504       C  
ATOM   4428  CG  LYS J 611     -10.910 -51.279  66.095  1.00 46.60           C  
ANISOU 4428  CG  LYS J 611     6047   7216   4442   -406   1880  -2544       C  
ATOM   4429  CD  LYS J 611     -11.168 -52.535  65.281  1.00 58.54           C  
ANISOU 4429  CD  LYS J 611     7508   8678   6056   -526   1870  -2795       C  
ATOM   4430  CE  LYS J 611     -12.518 -53.144  65.607  1.00 64.02           C  
ANISOU 4430  CE  LYS J 611     8346   9297   6681   -554   1911  -2859       C  
ATOM   4431  NZ  LYS J 611     -12.754 -54.401  64.841  1.00 68.73           N  
ANISOU 4431  NZ  LYS J 611     8892   9840   7383   -670   1881  -3120       N  
ATOM   4432  N   LEU J 612      -5.986 -51.664  66.394  1.00 61.26           N  
ANISOU 4432  N   LEU J 612     7468   9395   6414   -395   1310  -2779       N  
ATOM   4433  CA  LEU J 612      -4.627 -51.241  66.091  1.00 67.45           C  
ANISOU 4433  CA  LEU J 612     8106  10266   7255   -354   1237  -2794       C  
ATOM   4434  C   LEU J 612      -3.779 -52.462  65.765  1.00 77.65           C  
ANISOU 4434  C   LEU J 612     9234  11610   8660   -400   1061  -3048       C  
ATOM   4435  O   LEU J 612      -3.695 -53.396  66.570  1.00 81.21           O  
ANISOU 4435  O   LEU J 612     9713  12060   9082   -406    851  -3148       O  
ATOM   4436  CB  LEU J 612      -4.023 -50.469  67.265  1.00 65.31           C  
ANISOU 4436  CB  LEU J 612     7883  10060   6873   -277   1111  -2662       C  
ATOM   4437  CG  LEU J 612      -3.848 -48.965  67.058  1.00 63.51           C  
ANISOU 4437  CG  LEU J 612     7675   9839   6617   -195   1249  -2448       C  
ATOM   4438  CD1 LEU J 612      -5.150 -48.315  66.616  1.00 54.51           C  
ANISOU 4438  CD1 LEU J 612     6657   8592   5464   -172   1492  -2274       C  
ATOM   4439  CD2 LEU J 612      -3.335 -48.327  68.330  1.00 68.04           C  
ANISOU 4439  CD2 LEU J 612     8282  10483   7086   -141   1110  -2354       C  
ATOM   4440  N   ARG J 613      -3.154 -52.451  64.591  1.00 75.85           N  
ANISOU 4440  N   ARG J 613     8843  11415   8560   -422   1142  -3139       N  
ATOM   4441  CA  ARG J 613      -2.333 -53.561  64.122  1.00 76.18           C  
ANISOU 4441  CA  ARG J 613     8686  11515   8745   -457   1004  -3392       C  
ATOM   4442  C   ARG J 613      -0.868 -53.189  64.317  1.00 74.36           C  
ANISOU 4442  C   ARG J 613     8327  11394   8532   -371    860  -3409       C  
ATOM   4443  O   ARG J 613      -0.362 -52.262  63.676  1.00 70.60           O  
ANISOU 4443  O   ARG J 613     7811  10957   8056   -344    986  -3325       O  
ATOM   4444  CB  ARG J 613      -2.647 -53.884  62.664  1.00 77.51           C  
ANISOU 4444  CB  ARG J 613     8741  11653   9057   -557   1205  -3513       C  
ATOM   4445  CG  ARG J 613      -4.128 -54.146  62.424  1.00 78.96           C  
ANISOU 4445  CG  ARG J 613     9054  11715   9232   -636   1360  -3494       C  
ATOM   4446  CD  ARG J 613      -4.513 -54.050  60.956  1.00 80.73           C  
ANISOU 4446  CD  ARG J 613     9207  11884   9584   -732   1612  -3542       C  
ATOM   4447  NE  ARG J 613      -4.172 -55.259  60.210  1.00 88.29           N  
ANISOU 4447  NE  ARG J 613     9950  12871  10727   -834   1570  -3838       N  
ATOM   4448  CZ  ARG J 613      -3.081 -55.401  59.463  1.00 92.78           C  
ANISOU 4448  CZ  ARG J 613    10307  13527  11417   -853   1568  -3970       C  
ATOM   4449  NH1 ARG J 613      -2.216 -54.403  59.348  1.00 91.56           N  
ANISOU 4449  NH1 ARG J 613    10156  13435  11198   -774   1600  -3823       N  
ATOM   4450  NH2 ARG J 613      -2.861 -56.541  58.823  1.00 95.18           N  
ANISOU 4450  NH2 ARG J 613    10396  13858  11911   -945   1532  -4255       N  
ATOM   4451  N   TYR J 614      -0.191 -53.919  65.200  1.00 70.48           N  
ANISOU 4451  N   TYR J 614     7794  10932   8051   -314    587  -3502       N  
ATOM   4452  CA  TYR J 614       1.156 -53.573  65.626  1.00 70.71           C  
ANISOU 4452  CA  TYR J 614     7728  11046   8091   -209    416  -3506       C  
ATOM   4453  C   TYR J 614       1.841 -54.824  66.155  1.00 71.99           C  
ANISOU 4453  C   TYR J 614     7813  11190   8349   -153    132  -3659       C  
ATOM   4454  O   TYR J 614       1.185 -55.793  66.550  1.00 73.24           O  
ANISOU 4454  O   TYR J 614     8069  11256   8504   -186     33  -3694       O  
ATOM   4455  CB  TYR J 614       1.137 -52.459  66.683  1.00 74.50           C  
ANISOU 4455  CB  TYR J 614     8369  11527   8411   -149    386  -3288       C  
ATOM   4456  CG  TYR J 614       0.489 -52.851  67.998  1.00 80.44           C  
ANISOU 4456  CG  TYR J 614     9314  12197   9052   -154    239  -3207       C  
ATOM   4457  CD2 TYR J 614       1.258 -53.143  69.116  1.00 82.31           C  
ANISOU 4457  CD2 TYR J 614     9591  12413   9270    -87    -37  -3191       C  
ATOM   4458  CD1 TYR J 614      -0.897 -52.895  68.127  1.00 86.43           C  
ANISOU 4458  CD1 TYR J 614    10236  12883   9721   -228    381  -3128       C  
ATOM   4459  CE2 TYR J 614       0.666 -53.493  70.315  1.00 84.78           C  
ANISOU 4459  CE2 TYR J 614    10113  12636   9465   -115   -172  -3094       C  
ATOM   4460  CE1 TYR J 614      -1.495 -53.244  69.320  1.00 88.78           C  
ANISOU 4460  CE1 TYR J 614    10723  13116   9894   -242    257  -3055       C  
ATOM   4461  CZ  TYR J 614      -0.709 -53.541  70.413  1.00 88.67           C  
ANISOU 4461  CZ  TYR J 614    10757  13085   9850   -194    -21  -3035       C  
ATOM   4462  OH  TYR J 614      -1.299 -53.886  71.605  1.00 91.94           O  
ANISOU 4462  OH  TYR J 614    11385  13426  10124   -228   -148  -2945       O  
ATOM   4463  N   ASN J 615       3.171 -54.789  66.149  1.00 75.91           N  
ANISOU 4463  N   ASN J 615     8155  11757   8928    -54     -3  -3734       N  
ATOM   4464  CA  ASN J 615       3.962 -55.940  66.577  1.00 78.86           C  
ANISOU 4464  CA  ASN J 615     8460  12083   9419     32   -271  -3857       C  
ATOM   4465  C   ASN J 615       3.778 -56.137  68.081  1.00 81.23           C  
ANISOU 4465  C   ASN J 615     9014  12248   9602     63   -498  -3690       C  
ATOM   4466  O   ASN J 615       3.944 -55.181  68.845  1.00 83.42           O  
ANISOU 4466  O   ASN J 615     9402  12530   9765     91   -520  -3530       O  
ATOM   4467  CB  ASN J 615       5.438 -55.723  66.218  1.00 79.57           C  
ANISOU 4467  CB  ASN J 615     8334  12276   9624    146   -338  -3968       C  
ATOM   4468  CG  ASN J 615       6.314 -56.953  66.465  1.00 82.99           C  
ANISOU 4468  CG  ASN J 615     8672  12646  10213    254   -586  -4113       C  
ATOM   4469  OD1 ASN J 615       6.334 -57.529  67.552  1.00 84.65           O  
ANISOU 4469  OD1 ASN J 615     9066  12708  10390    294   -815  -4017       O  
ATOM   4470  ND2 ASN J 615       7.051 -57.355  65.434  1.00 84.17           N  
ANISOU 4470  ND2 ASN J 615     8541  12905  10535    289   -536  -4340       N  
ATOM   4471  N   PRO J 616       3.428 -57.349  68.531  1.00 84.41           N  
ANISOU 4471  N   PRO J 616     9522  12527  10025     43   -673  -3718       N  
ATOM   4472  CA  PRO J 616       3.116 -57.549  69.960  1.00 83.87           C  
ANISOU 4472  CA  PRO J 616     9730  12322   9816     24   -876  -3538       C  
ATOM   4473  C   PRO J 616       4.288 -57.327  70.901  1.00 76.22           C  
ANISOU 4473  C   PRO J 616     8800  11303   8858    111  -1097  -3446       C  
ATOM   4474  O   PRO J 616       4.049 -57.085  72.091  1.00 74.35           O  
ANISOU 4474  O   PRO J 616     8782  10983   8486     68  -1214  -3268       O  
ATOM   4475  CB  PRO J 616       2.638 -59.007  70.011  1.00 87.88           C  
ANISOU 4475  CB  PRO J 616    10311  12718  10359    -20  -1022  -3616       C  
ATOM   4476  CG  PRO J 616       2.138 -59.283  68.633  1.00 87.69           C  
ANISOU 4476  CG  PRO J 616    10097  12774  10445    -61   -811  -3802       C  
ATOM   4477  CD  PRO J 616       3.062 -58.522  67.721  1.00 86.76           C  
ANISOU 4477  CD  PRO J 616     9713  12804  10448      2   -663  -3901       C  
ATOM   4478  N   ARG J 617       5.535 -57.404  70.413  1.00 75.39           N  
ANISOU 4478  N   ARG J 617     8488  11245   8912    226  -1152  -3570       N  
ATOM   4479  CA  ARG J 617       6.688 -57.010  71.220  1.00 84.63           C  
ANISOU 4479  CA  ARG J 617     9685  12368  10101    318  -1327  -3488       C  
ATOM   4480  C   ARG J 617       6.565 -55.571  71.707  1.00 81.00           C  
ANISOU 4480  C   ARG J 617     9307  11963   9508    301  -1232  -3328       C  
ATOM   4481  O   ARG J 617       6.974 -55.257  72.832  1.00 82.09           O  
ANISOU 4481  O   ARG J 617     9587  12013   9593    305  -1397  -3180       O  
ATOM   4482  CB  ARG J 617       7.985 -57.174  70.422  1.00 99.09           C  
ANISOU 4482  CB  ARG J 617    11256  14275  12121    460  -1344  -3683       C  
ATOM   4483  CG  ARG J 617       9.218 -56.637  71.148  1.00105.21           C  
ANISOU 4483  CG  ARG J 617    12047  15005  12921    568  -1496  -3619       C  
ATOM   4484  CD  ARG J 617      10.496 -56.769  70.334  1.00109.77           C  
ANISOU 4484  CD  ARG J 617    12364  15669  13675    724  -1500  -3838       C  
ATOM   4485  NE  ARG J 617      10.266 -56.654  68.896  1.00108.65           N  
ANISOU 4485  NE  ARG J 617    11973  15719  13591    713  -1260  -4027       N  
ATOM   4486  CZ  ARG J 617      11.232 -56.505  67.995  1.00 99.93           C  
ANISOU 4486  CZ  ARG J 617    10603  14757  12608    816  -1192  -4230       C  
ATOM   4487  NH1 ARG J 617      10.931 -56.417  66.707  1.00103.32           N  
ANISOU 4487  NH1 ARG J 617    10810  15366  13080    751   -968  -4386       N  
ATOM   4488  NH2 ARG J 617      12.498 -56.424  68.383  1.00 87.67           N  
ANISOU 4488  NH2 ARG J 617     9008  13170  11131    968  -1345  -4278       N  
ATOM   4489  N   PHE J 618       5.981 -54.695  70.895  1.00 80.48           N  
ANISOU 4489  N   PHE J 618     9154  12038   9387    271   -970  -3350       N  
ATOM   4490  CA  PHE J 618       5.741 -53.308  71.272  1.00 72.37           C  
ANISOU 4490  CA  PHE J 618     8195  11075   8226    257   -861  -3203       C  
ATOM   4491  C   PHE J 618       4.459 -53.124  72.078  1.00 77.24           C  
ANISOU 4491  C   PHE J 618     9036  11637   8673    146   -821  -3044       C  
ATOM   4492  O   PHE J 618       4.020 -51.979  72.243  1.00 78.16           O  
ANISOU 4492  O   PHE J 618     9193  11828   8676    128   -681  -2936       O  
ATOM   4493  CB  PHE J 618       5.681 -52.419  70.025  1.00 64.27           C  
ANISOU 4493  CB  PHE J 618     6994  10222   7204    263   -591  -3274       C  
ATOM   4494  CG  PHE J 618       6.896 -52.503  69.136  1.00 57.90           C  
ANISOU 4494  CG  PHE J 618     5952   9509   6541    360   -598  -3446       C  
ATOM   4495  CD1 PHE J 618       8.149 -52.825  69.646  1.00 61.82           C  
ANISOU 4495  CD1 PHE J 618     6405   9949   7134    481   -823  -3494       C  
ATOM   4496  CD2 PHE J 618       6.774 -52.274  67.774  1.00 64.46           C  
ANISOU 4496  CD2 PHE J 618     6615  10470   7408    316   -372  -3555       C  
ATOM   4497  CE1 PHE J 618       9.252 -52.902  68.816  1.00 61.15           C  
ANISOU 4497  CE1 PHE J 618     6092   9966   7177    581   -817  -3675       C  
ATOM   4498  CE2 PHE J 618       7.873 -52.350  66.940  1.00 63.38           C  
ANISOU 4498  CE2 PHE J 618     6255  10439   7388    386   -372  -3724       C  
ATOM   4499  CZ  PHE J 618       9.114 -52.665  67.461  1.00 62.41           C  
ANISOU 4499  CZ  PHE J 618     6063  10290   7359    531   -593  -3798       C  
ATOM   4500  N   ASP J 619       3.862 -54.213  72.582  1.00 76.64           N  
ANISOU 4500  N   ASP J 619     9106  11442   8570     76   -942  -3032       N  
ATOM   4501  CA  ASP J 619       2.577 -54.145  73.273  1.00 74.09           C  
ANISOU 4501  CA  ASP J 619     8994  11082   8073    -28   -888  -2912       C  
ATOM   4502  C   ASP J 619       2.656 -53.322  74.554  1.00 75.42           C  
ANISOU 4502  C   ASP J 619     9305  11232   8117    -48   -987  -2729       C  
ATOM   4503  O   ASP J 619       1.640 -52.770  74.990  1.00 74.18           O  
ANISOU 4503  O   ASP J 619     9267  11114   7803   -110   -860  -2632       O  
ATOM   4504  CB  ASP J 619       2.085 -55.566  73.573  1.00 77.71           C  
ANISOU 4504  CB  ASP J 619     9586  11417   8523    -94  -1039  -2947       C  
ATOM   4505  CG  ASP J 619       0.564 -55.677  73.611  1.00 80.27           C  
ANISOU 4505  CG  ASP J 619    10063  11739   8697   -187   -882  -2920       C  
ATOM   4506  OD1 ASP J 619      -0.101 -54.841  74.258  1.00 77.75           O  
ANISOU 4506  OD1 ASP J 619     9864  11457   8222   -223   -782  -2792       O  
ATOM   4507  OD2 ASP J 619       0.029 -56.617  72.983  1.00 80.91           O  
ANISOU 4507  OD2 ASP J 619    10137  11785   8822   -218   -854  -3037       O  
ATOM   4508  N   LYS J 620       3.844 -53.212  75.155  1.00 78.42           N  
ANISOU 4508  N   LYS J 620     9666  11558   8571      4  -1198  -2684       N  
ATOM   4509  CA  LYS J 620       4.014 -52.341  76.311  1.00 77.09           C  
ANISOU 4509  CA  LYS J 620     9603  11378   8311    -23  -1295  -2516       C  
ATOM   4510  C   LYS J 620       3.869 -50.869  75.940  1.00 71.37           C  
ANISOU 4510  C   LYS J 620     8777  10806   7534     26  -1083  -2487       C  
ATOM   4511  O   LYS J 620       3.356 -50.081  76.742  1.00 67.16           O  
ANISOU 4511  O   LYS J 620     8335  10314   6869    -21  -1059  -2356       O  
ATOM   4512  CB  LYS J 620       5.377 -52.597  76.957  1.00 83.49           C  
ANISOU 4512  CB  LYS J 620    10405  12080   9238     13  -1560  -2478       C  
ATOM   4513  CG  LYS J 620       5.476 -53.920  77.702  1.00 82.54           C  
ANISOU 4513  CG  LYS J 620    10421  11818   9125    -68  -1791  -2443       C  
ATOM   4514  CD  LYS J 620       6.828 -54.072  78.381  1.00 82.07           C  
ANISOU 4514  CD  LYS J 620    10337  11669   9178    -35  -2019  -2398       C  
ATOM   4515  CE  LYS J 620       6.694 -54.658  79.778  1.00 83.34           C  
ANISOU 4515  CE  LYS J 620    10676  11743   9244   -176  -2230  -2246       C  
ATOM   4516  NZ  LYS J 620       6.042 -53.712  80.726  1.00 83.42           N  
ANISOU 4516  NZ  LYS J 620    10803  11800   9094   -287  -2213  -2076       N  
ATOM   4517  N   ALA J 621       4.295 -50.483  74.733  1.00 72.43           N  
ANISOU 4517  N   ALA J 621     8720  11042   7758    112   -926  -2607       N  
ATOM   4518  CA  ALA J 621       4.258 -49.074  74.348  1.00 64.14           C  
ANISOU 4518  CA  ALA J 621     7581  10137   6650    157   -741  -2567       C  
ATOM   4519  C   ALA J 621       2.839 -48.620  74.042  1.00 56.67           C  
ANISOU 4519  C   ALA J 621     6690   9271   5572     87   -465  -2509       C  
ATOM   4520  O   ALA J 621       2.379 -47.599  74.567  1.00 48.40           O  
ANISOU 4520  O   ALA J 621     5692   8293   4406     75   -379  -2380       O  
ATOM   4521  CB  ALA J 621       5.157 -48.828  73.139  1.00 63.44           C  
ANISOU 4521  CB  ALA J 621     7290  10135   6678    256   -660  -2700       C  
ATOM   4522  N   PHE J 622       2.137 -49.367  73.187  1.00 53.68           N  
ANISOU 4522  N   PHE J 622     6301   8872   5221     42   -317  -2595       N  
ATOM   4523  CA  PHE J 622       0.838 -48.926  72.693  1.00 51.85           C  
ANISOU 4523  CA  PHE J 622     6122   8673   4906    -14    -22  -2529       C  
ATOM   4524  C   PHE J 622      -0.200 -48.919  73.808  1.00 59.58           C  
ANISOU 4524  C   PHE J 622     7286   9623   5730    -83    -12  -2407       C  
ATOM   4525  O   PHE J 622      -1.050 -48.020  73.867  1.00 65.86           O  
ANISOU 4525  O   PHE J 622     8128  10461   6437    -96    208  -2278       O  
ATOM   4526  CB  PHE J 622       0.397 -49.817  71.530  1.00 52.68           C  
ANISOU 4526  CB  PHE J 622     6177   8735   5105    -53    102  -2656       C  
ATOM   4527  CG  PHE J 622       1.084 -49.497  70.226  1.00 44.97           C  
ANISOU 4527  CG  PHE J 622     5023   7817   4246    -10    211  -2736       C  
ATOM   4528  CD1 PHE J 622       2.430 -49.784  70.044  1.00 45.38           C  
ANISOU 4528  CD1 PHE J 622     4928   7911   4405     60     33  -2859       C  
ATOM   4529  CD2 PHE J 622       0.388 -48.904  69.185  1.00 50.33           C  
ANISOU 4529  CD2 PHE J 622     5704   8488   4930    -37    491  -2668       C  
ATOM   4530  CE1 PHE J 622       3.066 -49.489  68.853  1.00 50.32           C  
ANISOU 4530  CE1 PHE J 622     5396   8607   5115     91    141  -2938       C  
ATOM   4531  CE2 PHE J 622       1.020 -48.607  67.989  1.00 49.13           C  
ANISOU 4531  CE2 PHE J 622     5427   8375   4865    -13    588  -2718       C  
ATOM   4532  CZ  PHE J 622       2.361 -48.901  67.823  1.00 49.33           C  
ANISOU 4532  CZ  PHE J 622     5292   8478   4972     43    418  -2864       C  
ATOM   4533  N   LYS J 623      -0.110 -49.886  74.730  1.00 57.98           N  
ANISOU 4533  N   LYS J 623     7197   9336   5495   -126   -251  -2425       N  
ATOM   4534  CA  LYS J 623      -0.965 -49.887  75.916  1.00 62.27           C  
ANISOU 4534  CA  LYS J 623     7925   9869   5866   -200   -270  -2305       C  
ATOM   4535  C   LYS J 623      -0.727 -48.652  76.776  1.00 60.51           C  
ANISOU 4535  C   LYS J 623     7694   9744   5553   -187   -281  -2161       C  
ATOM   4536  O   LYS J 623      -1.631 -48.210  77.493  1.00 60.76           O  
ANISOU 4536  O   LYS J 623     7823   9834   5429   -244   -157  -2039       O  
ATOM   4537  CB  LYS J 623      -0.721 -51.153  76.742  1.00 71.04           C  
ANISOU 4537  CB  LYS J 623     9179  10850   6965   -248   -570  -2328       C  
ATOM   4538  CG  LYS J 623      -1.404 -52.395  76.196  1.00 72.88           C  
ANISOU 4538  CG  LYS J 623     9481  10997   7214   -286   -545  -2438       C  
ATOM   4539  CD  LYS J 623      -1.507 -53.510  77.219  1.00 74.29           C  
ANISOU 4539  CD  LYS J 623     9867  11051   7307   -353   -811  -2408       C  
ATOM   4540  CE  LYS J 623      -2.494 -54.576  76.753  1.00 73.68           C  
ANISOU 4540  CE  LYS J 623     9888  10913   7193   -393   -745  -2504       C  
ATOM   4541  NZ  LYS J 623      -3.887 -54.057  76.645  1.00 72.46           N  
ANISOU 4541  NZ  LYS J 623     9800  10834   6897   -419   -437  -2466       N  
ATOM   4542  N   HIS J 624       0.481 -48.084  76.715  1.00 60.58           N  
ANISOU 4542  N   HIS J 624     7578   9778   5660   -113   -420  -2173       N  
ATOM   4543  CA  HIS J 624       0.753 -46.839  77.421  1.00 55.65           C  
ANISOU 4543  CA  HIS J 624     6921   9256   4967    -92   -440  -2049       C  
ATOM   4544  C   HIS J 624       0.020 -45.667  76.775  1.00 59.71           C  
ANISOU 4544  C   HIS J 624     7367   9896   5424    -59   -106  -1977       C  
ATOM   4545  O   HIS J 624      -0.378 -44.730  77.475  1.00 68.26           O  
ANISOU 4545  O   HIS J 624     8463  11078   6395    -74    -31  -1836       O  
ATOM   4546  CB  HIS J 624       2.263 -46.580  77.451  1.00 55.93           C  
ANISOU 4546  CB  HIS J 624     6853   9252   5147     -8   -682  -2086       C  
ATOM   4547  CG  HIS J 624       2.661 -45.318  78.157  1.00 61.08           C  
ANISOU 4547  CG  HIS J 624     7461   9992   5754     19   -750  -1969       C  
ATOM   4548  ND1 HIS J 624       1.831 -44.656  79.038  1.00 63.44           N  
ANISOU 4548  ND1 HIS J 624     7816  10399   5888    -51   -677  -1825       N  
ATOM   4549  CD2 HIS J 624       3.802 -44.590  78.100  1.00 61.51           C  
ANISOU 4549  CD2 HIS J 624     7413  10050   5910    109   -879  -1974       C  
ATOM   4550  CE1 HIS J 624       2.445 -43.581  79.498  1.00 64.14           C  
ANISOU 4550  CE1 HIS J 624     7825  10557   5989     -9   -782  -1745       C  
ATOM   4551  NE2 HIS J 624       3.642 -43.517  78.943  1.00 61.23           N  
ANISOU 4551  NE2 HIS J 624     7371  10110   5785     91   -911  -1836       N  
ATOM   4552  N   VAL J 625      -0.173 -45.699  75.460  1.00 52.92           N  
ANISOU 4552  N   VAL J 625     6439   9014   4655    -19     95  -2042       N  
ATOM   4553  CA  VAL J 625      -0.745 -44.570  74.728  1.00 53.60           C  
ANISOU 4553  CA  VAL J 625     6483   9136   4745     26    383  -1927       C  
ATOM   4554  C   VAL J 625      -2.245 -44.729  74.522  1.00 59.15           C  
ANISOU 4554  C   VAL J 625     7299   9752   5423    -27    645  -1833       C  
ATOM   4555  O   VAL J 625      -3.019 -43.821  74.825  1.00 63.12           O  
ANISOU 4555  O   VAL J 625     7838  10261   5884    -15    821  -1662       O  
ATOM   4556  CB  VAL J 625      -0.016 -44.377  73.379  1.00 45.37           C  
ANISOU 4556  CB  VAL J 625     5325   8082   3830     97    432  -2006       C  
ATOM   4557  CG1 VAL J 625      -0.261 -42.977  72.841  1.00 40.86           C  
ANISOU 4557  CG1 VAL J 625     4734   7531   3260    162    635  -1846       C  
ATOM   4558  CG2 VAL J 625       1.473 -44.620  73.540  1.00 46.52           C  
ANISOU 4558  CG2 VAL J 625     5367   8275   4033    153    153  -2141       C  
ATOM   4559  N   PHE J 626      -2.675 -45.878  74.007  1.00 52.59           N  
ANISOU 4559  N   PHE J 626     6521   8827   4634    -75    664  -1942       N  
ATOM   4560  CA  PHE J 626      -4.059 -46.082  73.611  1.00 62.99           C  
ANISOU 4560  CA  PHE J 626     7942  10038   5953   -103    899  -1876       C  
ATOM   4561  C   PHE J 626      -4.811 -47.029  74.533  1.00 66.99           C  
ANISOU 4561  C   PHE J 626     8588  10522   6342   -183    842  -1904       C  
ATOM   4562  O   PHE J 626      -5.982 -47.324  74.273  1.00 79.85           O  
ANISOU 4562  O   PHE J 626    10309  12065   7963   -199   1014  -1872       O  
ATOM   4563  CB  PHE J 626      -4.117 -46.619  72.175  1.00 57.23           C  
ANISOU 4563  CB  PHE J 626     7169   9222   5354    -96    987  -1977       C  
ATOM   4564  CG  PHE J 626      -3.357 -45.787  71.184  1.00 49.58           C  
ANISOU 4564  CG  PHE J 626     6090   8268   4481    -27   1045  -1948       C  
ATOM   4565  CD1 PHE J 626      -3.932 -44.663  70.612  1.00 46.06           C  
ANISOU 4565  CD1 PHE J 626     5682   7755   4064     38   1262  -1764       C  
ATOM   4566  CD2 PHE J 626      -2.063 -46.129  70.823  1.00 38.66           C  
ANISOU 4566  CD2 PHE J 626     4578   6953   3156    -13    874  -2097       C  
ATOM   4567  CE1 PHE J 626      -3.230 -43.898  69.701  1.00 38.34           C  
ANISOU 4567  CE1 PHE J 626     4639   6783   3147    102   1309  -1725       C  
ATOM   4568  CE2 PHE J 626      -1.358 -45.369  69.912  1.00 38.52           C  
ANISOU 4568  CE2 PHE J 626     4477   6958   3201     49    934  -2069       C  
ATOM   4569  CZ  PHE J 626      -1.942 -44.252  69.351  1.00 38.38           C  
ANISOU 4569  CZ  PHE J 626     4522   6874   3187    101   1152  -1879       C  
ATOM   4570  N   GLY J 627      -4.179 -47.503  75.606  1.00 70.04           N  
ANISOU 4570  N   GLY J 627     9009  10970   6634   -226    591  -1950       N  
ATOM   4571  CA  GLY J 627      -4.750 -48.555  76.428  1.00 65.85           C  
ANISOU 4571  CA  GLY J 627     8640  10400   5981   -306    490  -1981       C  
ATOM   4572  C   GLY J 627      -5.930 -48.141  77.282  1.00 65.17           C  
ANISOU 4572  C   GLY J 627     8677  10338   5747   -346    672  -1819       C  
ATOM   4573  O   GLY J 627      -6.617 -49.020  77.811  1.00 69.47           O  
ANISOU 4573  O   GLY J 627     9375  10843   6177   -406    642  -1840       O  
ATOM   4574  N   LYS J 628      -6.189 -46.841  77.432  1.00 63.74           N  
ANISOU 4574  N   LYS J 628     8432  10212   5573   -307    858  -1654       N  
ATOM   4575  CA  LYS J 628      -7.260 -46.378  78.301  1.00 66.82           C  
ANISOU 4575  CA  LYS J 628     8910  10622   5856   -335   1039  -1481       C  
ATOM   4576  C   LYS J 628      -8.409 -45.693  77.576  1.00 64.83           C  
ANISOU 4576  C   LYS J 628     8651  10267   5716   -247   1342  -1373       C  
ATOM   4577  O   LYS J 628      -9.400 -45.345  78.225  1.00 63.51           O  
ANISOU 4577  O   LYS J 628     8548  10091   5492   -243   1503  -1238       O  
ATOM   4578  CB  LYS J 628      -6.710 -45.416  79.366  1.00 75.85           C  
ANISOU 4578  CB  LYS J 628     9989  11912   6919   -366    978  -1341       C  
ATOM   4579  CG  LYS J 628      -7.198 -45.712  80.778  1.00 79.97           C  
ANISOU 4579  CG  LYS J 628    10641  12499   7244   -481    955  -1230       C  
ATOM   4580  CD  LYS J 628      -6.388 -46.802  81.454  1.00 79.90           C  
ANISOU 4580  CD  LYS J 628    10739  12512   7107   -577    610  -1328       C  
ATOM   4581  CE  LYS J 628      -6.578 -46.755  82.962  1.00 83.14           C  
ANISOU 4581  CE  LYS J 628    11260  13014   7315   -713    555  -1149       C  
ATOM   4582  NZ  LYS J 628      -5.431 -47.352  83.696  1.00 85.88           N  
ANISOU 4582  NZ  LYS J 628    11667  13367   7595   -793    140  -1176       N  
ATOM   4583  N   THR J 629      -8.318 -45.487  76.267  1.00 59.95           N  
ANISOU 4583  N   THR J 629     7963   9561   5253   -169   1413  -1418       N  
ATOM   4584  CA  THR J 629      -9.320 -44.726  75.535  1.00 60.71           C  
ANISOU 4584  CA  THR J 629     8062   9547   5458    -63   1658  -1292       C  
ATOM   4585  C   THR J 629     -10.189 -45.646  74.684  1.00 60.18           C  
ANISOU 4585  C   THR J 629     8065   9377   5422    -53   1730  -1392       C  
ATOM   4586  O   THR J 629      -9.720 -46.653  74.145  1.00 62.90           O  
ANISOU 4586  O   THR J 629     8406   9711   5784   -112   1607  -1570       O  
ATOM   4587  CB  THR J 629      -8.660 -43.656  74.662  1.00 58.72           C  
ANISOU 4587  CB  THR J 629     7699   9274   5338     22   1696  -1227       C  
ATOM   4588  OG1 THR J 629      -8.300 -44.219  73.395  1.00 66.45           O  
ANISOU 4588  OG1 THR J 629     8650  10193   6405     32   1668  -1352       O  
ATOM   4589  CG2 THR J 629      -7.416 -43.107  75.355  1.00 51.87           C  
ANISOU 4589  CG2 THR J 629     6731   8550   4427    -12   1529  -1226       C  
ATOM   4590  N   LEU J 630     -11.467 -45.283  74.570  1.00 61.37           N  
ANISOU 4590  N   LEU J 630     8260   9468   5588     28   1918  -1285       N  
ATOM   4591  CA  LEU J 630     -12.477 -46.094  73.907  1.00 66.89           C  
ANISOU 4591  CA  LEU J 630     9020  10100   6296     34   1988  -1380       C  
ATOM   4592  C   LEU J 630     -13.067 -45.339  72.720  1.00 67.95           C  
ANISOU 4592  C   LEU J 630     9088  10171   6558    152   2138  -1299       C  
ATOM   4593  O   LEU J 630     -13.000 -44.110  72.645  1.00 67.85           O  
ANISOU 4593  O   LEU J 630     9009  10174   6599    260   2213  -1129       O  
ATOM   4594  CB  LEU J 630     -13.608 -46.475  74.876  1.00 68.51           C  
ANISOU 4594  CB  LEU J 630     9332  10331   6368     21   2054  -1357       C  
ATOM   4595  CG  LEU J 630     -13.282 -47.321  76.109  1.00 70.18           C  
ANISOU 4595  CG  LEU J 630     9647  10613   6404    -99   1915  -1422       C  
ATOM   4596  CD1 LEU J 630     -14.538 -47.530  76.941  1.00 68.31           C  
ANISOU 4596  CD1 LEU J 630     9515  10402   6037    -88   2028  -1369       C  
ATOM   4597  CD2 LEU J 630     -12.676 -48.656  75.719  1.00 77.82           C  
ANISOU 4597  CD2 LEU J 630    10661  11561   7345   -197   1724  -1643       C  
ATOM   4598  N   ILE J 631     -13.673 -46.090  71.802  1.00 71.72           N  
ANISOU 4598  N   ILE J 631     9586  10587   7077    126   2175  -1427       N  
ATOM   4599  CA  ILE J 631     -14.322 -45.546  70.616  1.00 63.74           C  
ANISOU 4599  CA  ILE J 631     8516   9529   6171    204   2305  -1383       C  
ATOM   4600  C   ILE J 631     -15.809 -45.834  70.748  1.00 59.46           C  
ANISOU 4600  C   ILE J 631     8033   8971   5588    213   2413  -1416       C  
ATOM   4601  O   ILE J 631     -16.229 -46.996  70.705  1.00 61.59           O  
ANISOU 4601  O   ILE J 631     8390   9192   5820    120   2392  -1589       O  
ATOM   4602  CB  ILE J 631     -13.760 -46.156  69.326  1.00 45.37           C  
ANISOU 4602  CB  ILE J 631     6152   7139   3947    133   2276  -1526       C  
ATOM   4603  CG1 ILE J 631     -12.280 -45.811  69.171  1.00 48.01           C  
ANISOU 4603  CG1 ILE J 631     6416   7506   4319    131   2174  -1503       C  
ATOM   4604  CG2 ILE J 631     -14.548 -45.659  68.125  1.00 46.80           C  
ANISOU 4604  CG2 ILE J 631     6290   7270   4222    183   2422  -1492       C  
ATOM   4605  CD1 ILE J 631     -11.656 -46.372  67.912  1.00 48.62           C  
ANISOU 4605  CD1 ILE J 631     6430   7546   4500     62   2156  -1642       C  
ATOM   4606  N   CYS J 632     -16.609 -44.784  70.904  1.00 61.22           N  
ANISOU 4606  N   CYS J 632     8201   9246   5814    322   2522  -1270       N  
ATOM   4607  CA  CYS J 632     -18.042 -44.923  71.111  1.00 70.13           C  
ANISOU 4607  CA  CYS J 632     9371  10373   6903    333   2632  -1306       C  
ATOM   4608  C   CYS J 632     -18.809 -44.552  69.850  1.00 72.88           C  
ANISOU 4608  C   CYS J 632     9675  10653   7364    352   2748  -1340       C  
ATOM   4609  O   CYS J 632     -18.297 -43.877  68.952  1.00 73.71           O  
ANISOU 4609  O   CYS J 632     9695  10751   7561    381   2754  -1280       O  
ATOM   4610  CB  CYS J 632     -18.510 -44.061  72.286  1.00 75.12           C  
ANISOU 4610  CB  CYS J 632     9955  11128   7457    412   2679  -1153       C  
ATOM   4611  SG  CYS J 632     -17.573 -44.344  73.797  1.00 81.36           S  
ANISOU 4611  SG  CYS J 632    10808  11978   8126    368   2574  -1090       S  
ATOM   4612  N   ARG J 633     -20.063 -45.010  69.801  1.00 80.87           N  
ANISOU 4612  N   ARG J 633    10761  11608   8359    328   2849  -1444       N  
ATOM   4613  CA  ARG J 633     -20.886 -44.816  68.612  1.00 84.65           C  
ANISOU 4613  CA  ARG J 633    11236  11975   8952    318   2979  -1509       C  
ATOM   4614  C   ARG J 633     -21.371 -43.377  68.495  1.00 78.26           C  
ANISOU 4614  C   ARG J 633    10325  11215   8196    406   3075  -1370       C  
ATOM   4615  O   ARG J 633     -21.390 -42.810  67.396  1.00 76.25           O  
ANISOU 4615  O   ARG J 633    10032  10884   8055    406   3146  -1354       O  
ATOM   4616  CB  ARG J 633     -22.072 -45.781  68.641  1.00 95.37           C  
ANISOU 4616  CB  ARG J 633    12722  13240  10274    264   3061  -1684       C  
ATOM   4617  CG  ARG J 633     -22.797 -45.924  67.313  1.00105.80           C  
ANISOU 4617  CG  ARG J 633    14078  14392  11731    215   3194  -1802       C  
ATOM   4618  CD  ARG J 633     -23.698 -47.150  67.309  1.00114.04           C  
ANISOU 4618  CD  ARG J 633    15260  15339  12732    140   3235  -2016       C  
ATOM   4619  NE  ARG J 633     -24.671 -47.117  68.397  1.00121.37           N  
ANISOU 4619  NE  ARG J 633    16247  16341  13526    207   3278  -2011       N  
ATOM   4620  CZ  ARG J 633     -25.472 -48.130  68.714  1.00125.27           C  
ANISOU 4620  CZ  ARG J 633    16874  16799  13926    170   3295  -2181       C  
ATOM   4621  NH1 ARG J 633     -25.421 -49.261  68.023  1.00126.61           N  
ANISOU 4621  NH1 ARG J 633    17124  16855  14129     61   3258  -2378       N  
ATOM   4622  NH2 ARG J 633     -26.327 -48.012  69.722  1.00126.77           N  
ANISOU 4622  NH2 ARG J 633    17110  17074  13981    239   3347  -2163       N  
ATOM   4623  N   SER J 634     -21.769 -42.771  69.611  1.00 77.57           N  
ANISOU 4623  N   SER J 634    10198  11244   8031    460   3096  -1283       N  
ATOM   4624  CA  SER J 634     -22.287 -41.413  69.610  1.00 81.51           C  
ANISOU 4624  CA  SER J 634    10598  11787   8586    519   3196  -1184       C  
ATOM   4625  C   SER J 634     -21.672 -40.651  70.775  1.00 78.61           C  
ANISOU 4625  C   SER J 634    10120  11603   8145    554   3122  -1045       C  
ATOM   4626  O   SER J 634     -20.904 -41.201  71.572  1.00 76.98           O  
ANISOU 4626  O   SER J 634     9933  11469   7846    544   3008  -1015       O  
ATOM   4627  CB  SER J 634     -23.819 -41.404  69.683  1.00 90.46           C  
ANISOU 4627  CB  SER J 634    11787  12855   9728    542   3354  -1262       C  
ATOM   4628  OG  SER J 634     -24.296 -40.182  70.217  1.00 96.10           O  
ANISOU 4628  OG  SER J 634    12403  13652  10461    602   3433  -1168       O  
ATOM   4629  N   MET J 635     -22.019 -39.367  70.876  1.00 78.69           N  
ANISOU 4629  N   MET J 635    10021  11672   8207    590   3193   -967       N  
ATOM   4630  CA  MET J 635     -21.436 -38.532  71.918  1.00 80.43           C  
ANISOU 4630  CA  MET J 635    10111  12073   8377    598   3127   -852       C  
ATOM   4631  C   MET J 635     -22.170 -38.675  73.244  1.00 81.79           C  
ANISOU 4631  C   MET J 635    10279  12343   8454    599   3182   -842       C  
ATOM   4632  O   MET J 635     -21.538 -38.594  74.303  1.00 81.10           O  
ANISOU 4632  O   MET J 635    10136  12381   8296    580   3093   -754       O  
ATOM   4633  CB  MET J 635     -21.425 -37.070  71.480  1.00 85.05           C  
ANISOU 4633  CB  MET J 635    10581  12669   9067    608   3176   -796       C  
ATOM   4634  CG  MET J 635     -20.089 -36.621  70.925  1.00 86.31           C  
ANISOU 4634  CG  MET J 635    10676  12870   9249    588   3056   -746       C  
ATOM   4635  SD  MET J 635     -19.708 -34.922  71.362  1.00 90.51           S  
ANISOU 4635  SD  MET J 635    11063  13481   9847    550   3055   -676       S  
ATOM   4636  CE  MET J 635     -19.189 -35.157  73.056  1.00 81.59           C  
ANISOU 4636  CE  MET J 635     9877  12480   8643    469   2917   -634       C  
ATOM   4637  N   GLU J 636     -23.491 -38.877  73.208  1.00 85.57           N  
ANISOU 4637  N   GLU J 636    10824  12749   8940    618   3327   -924       N  
ATOM   4638  CA  GLU J 636     -24.233 -39.143  74.437  1.00 87.34           C  
ANISOU 4638  CA  GLU J 636    11060  13073   9054    620   3395   -927       C  
ATOM   4639  C   GLU J 636     -23.829 -40.486  75.033  1.00 86.39           C  
ANISOU 4639  C   GLU J 636    11066  12968   8792    589   3305   -950       C  
ATOM   4640  O   GLU J 636     -23.661 -40.611  76.254  1.00 82.48           O  
ANISOU 4640  O   GLU J 636    10556  12600   8181    578   3285   -875       O  
ATOM   4641  CB  GLU J 636     -25.738 -39.090  74.163  1.00 92.72           C  
ANISOU 4641  CB  GLU J 636    11794  13663   9772    663   3576  -1028       C  
ATOM   4642  CG  GLU J 636     -26.597 -39.828  75.178  1.00 99.31           C  
ANISOU 4642  CG  GLU J 636    12704  14567  10462    664   3654  -1083       C  
ATOM   4643  CD  GLU J 636     -27.929 -40.271  74.610  1.00110.37           C  
ANISOU 4643  CD  GLU J 636    14218  15837  11881    705   3796  -1236       C  
ATOM   4644  OE1 GLU J 636     -28.364 -39.697  73.589  1.00113.72           O  
ANISOU 4644  OE1 GLU J 636    14630  16128  12451    747   3871  -1272       O  
ATOM   4645  OE2 GLU J 636     -28.541 -41.196  75.185  1.00115.10           O  
ANISOU 4645  OE2 GLU J 636    14926  16463  12342    697   3836  -1320       O  
ATOM   4646  N   VAL J 637     -23.617 -41.488  74.176  1.00 84.00           N  
ANISOU 4646  N   VAL J 637    10890  12523   8502    568   3250  -1055       N  
ATOM   4647  CA  VAL J 637     -23.094 -42.774  74.630  1.00 85.38           C  
ANISOU 4647  CA  VAL J 637    11200  12682   8560    526   3144  -1100       C  
ATOM   4648  C   VAL J 637     -21.685 -42.606  75.194  1.00 78.92           C  
ANISOU 4648  C   VAL J 637    10335  11936   7717    524   3001   -968       C  
ATOM   4649  O   VAL J 637     -21.308 -43.267  76.169  1.00 78.34           O  
ANISOU 4649  O   VAL J 637    10354  11888   7525    484   2951   -950       O  
ATOM   4650  CB  VAL J 637     -23.134 -43.793  73.474  1.00 85.57           C  
ANISOU 4650  CB  VAL J 637    11343  12537   8631    486   3113  -1262       C  
ATOM   4651  CG1 VAL J 637     -22.658 -45.166  73.931  1.00 82.77           C  
ANISOU 4651  CG1 VAL J 637    11142  12149   8157    409   3009  -1357       C  
ATOM   4652  CG2 VAL J 637     -24.537 -43.875  72.889  1.00 90.55           C  
ANISOU 4652  CG2 VAL J 637    12026  13079   9302    499   3264  -1386       C  
ATOM   4653  N   SER J 638     -20.905 -41.683  74.623  1.00 83.72           N  
ANISOU 4653  N   SER J 638    10820  12560   8431    551   2954   -885       N  
ATOM   4654  CA  SER J 638     -19.533 -41.483  75.085  1.00 84.44           C  
ANISOU 4654  CA  SER J 638    10883  12676   8526    556   2813   -764       C  
ATOM   4655  C   SER J 638     -19.499 -40.815  76.456  1.00 84.35           C  
ANISOU 4655  C   SER J 638    10802  12770   8478    549   2819   -621       C  
ATOM   4656  O   SER J 638     -18.742 -41.236  77.340  1.00 85.26           O  
ANISOU 4656  O   SER J 638    11011  12857   8527    511   2775   -566       O  
ATOM   4657  CB  SER J 638     -18.744 -40.660  74.065  1.00 84.55           C  
ANISOU 4657  CB  SER J 638    10794  12665   8666    579   2754   -725       C  
ATOM   4658  OG  SER J 638     -19.096 -39.290  74.129  1.00 88.21           O  
ANISOU 4658  OG  SER J 638    11091  13231   9194    581   2794   -656       O  
ATOM   4659  N   THR J 639     -20.309 -39.769  76.656  1.00 89.72           N  
ANISOU 4659  N   THR J 639    11329  13562   9199    553   2899   -584       N  
ATOM   4660  CA  THR J 639     -20.352 -39.130  77.969  1.00 87.69           C  
ANISOU 4660  CA  THR J 639    10980  13428   8911    525   2916   -463       C  
ATOM   4661  C   THR J 639     -21.062 -40.004  78.993  1.00 78.41           C  
ANISOU 4661  C   THR J 639     9929  12274   7590    506   3015   -472       C  
ATOM   4662  O   THR J 639     -20.888 -39.800  80.198  1.00 76.98           O  
ANISOU 4662  O   THR J 639     9731  12160   7358    474   3040   -355       O  
ATOM   4663  CB  THR J 639     -21.020 -37.749  77.896  1.00 90.15           C  
ANISOU 4663  CB  THR J 639    11096  13846   9312    478   2992   -484       C  
ATOM   4664  OG1 THR J 639     -21.123 -37.195  79.212  1.00 92.00           O  
ANISOU 4664  OG1 THR J 639    11233  14207   9516    408   3028   -402       O  
ATOM   4665  CG2 THR J 639     -22.417 -37.849  77.345  1.00 89.47           C  
ANISOU 4665  CG2 THR J 639    11054  13714   9228    514   3180   -606       C  
ATOM   4666  N   GLN J 640     -21.853 -40.977  78.539  1.00 79.58           N  
ANISOU 4666  N   GLN J 640    10208  12367   7662    516   3081   -616       N  
ATOM   4667  CA  GLN J 640     -22.349 -42.006  79.442  1.00 77.21           C  
ANISOU 4667  CA  GLN J 640    10065  12087   7184    481   3149   -655       C  
ATOM   4668  C   GLN J 640     -21.223 -42.932  79.894  1.00 69.65           C  
ANISOU 4668  C   GLN J 640     9272  11060   6131    414   3041   -647       C  
ATOM   4669  O   GLN J 640     -20.984 -43.099  81.097  1.00 62.27           O  
ANISOU 4669  O   GLN J 640     8397  10176   5086    353   3059   -558       O  
ATOM   4670  CB  GLN J 640     -23.464 -42.792  78.753  1.00 75.51           C  
ANISOU 4670  CB  GLN J 640     9956  11817   6918    500   3231   -840       C  
ATOM   4671  CG  GLN J 640     -24.000 -43.976  79.526  1.00 77.05           C  
ANISOU 4671  CG  GLN J 640    10341  12009   6924    445   3268   -921       C  
ATOM   4672  CD  GLN J 640     -25.074 -44.714  78.755  1.00 78.47           C  
ANISOU 4672  CD  GLN J 640    10632  12097   7086    457   3330  -1119       C  
ATOM   4673  OE1 GLN J 640     -25.836 -44.110  78.000  1.00 73.20           O  
ANISOU 4673  OE1 GLN J 640     9879  11402   6531    517   3418  -1167       O  
ATOM   4674  NE2 GLN J 640     -25.126 -46.029  78.922  1.00 84.97           N  
ANISOU 4674  NE2 GLN J 640    11656  12861   7766    390   3279  -1247       N  
ATOM   4675  N   LEU J 641     -20.500 -43.513  78.934  1.00 70.84           N  
ANISOU 4675  N   LEU J 641     9498  11084   6334    395   2925   -752       N  
ATOM   4676  CA  LEU J 641     -19.546 -44.574  79.242  1.00 71.93           C  
ANISOU 4676  CA  LEU J 641     9803  11143   6385    279   2791   -824       C  
ATOM   4677  C   LEU J 641     -18.286 -44.047  79.916  1.00 72.09           C  
ANISOU 4677  C   LEU J 641     9794  11172   6424    232   2718   -695       C  
ATOM   4678  O   LEU J 641     -17.637 -44.789  80.662  1.00 71.50           O  
ANISOU 4678  O   LEU J 641     9844  11096   6226     99   2617   -731       O  
ATOM   4679  CB  LEU J 641     -19.176 -45.329  77.965  1.00 74.86           C  
ANISOU 4679  CB  LEU J 641    10229  11388   6826    254   2687   -998       C  
ATOM   4680  CG  LEU J 641     -19.921 -46.631  77.649  1.00 77.81           C  
ANISOU 4680  CG  LEU J 641    10752  11705   7106    197   2678  -1197       C  
ATOM   4681  CD1 LEU J 641     -19.841 -47.587  78.820  1.00 79.82           C  
ANISOU 4681  CD1 LEU J 641    11171  12008   7149     92   2615  -1234       C  
ATOM   4682  CD2 LEU J 641     -21.369 -46.366  77.272  1.00 79.64           C  
ANISOU 4682  CD2 LEU J 641    10951  11951   7360    276   2837  -1230       C  
ATOM   4683  N   ALA J 642     -17.917 -42.786  79.667  1.00 65.74           N  
ANISOU 4683  N   ALA J 642     8834  10383   5760    323   2753   -559       N  
ATOM   4684  CA  ALA J 642     -16.658 -42.271  80.200  1.00 73.04           C  
ANISOU 4684  CA  ALA J 642     9752  11277   6724    259   2688   -468       C  
ATOM   4685  C   ALA J 642     -16.718 -42.100  81.713  1.00 77.19           C  
ANISOU 4685  C   ALA J 642    10302  11878   7150    169   2752   -348       C  
ATOM   4686  O   ALA J 642     -15.746 -42.405  82.416  1.00 84.23           O  
ANISOU 4686  O   ALA J 642    11254  12782   7966     10   2635   -357       O  
ATOM   4687  CB  ALA J 642     -16.305 -40.946  79.524  1.00 68.19           C  
ANISOU 4687  CB  ALA J 642     8985  10608   6317    357   2693   -366       C  
ATOM   4688  N   ARG J 643     -17.844 -41.618  82.233  1.00 84.17           N  
ANISOU 4688  N   ARG J 643    11106  12838   8038    235   2893   -250       N  
ATOM   4689  CA  ARG J 643     -18.016 -41.499  83.673  1.00 85.63           C  
ANISOU 4689  CA  ARG J 643    11313  13099   8125    149   2987   -125       C  
ATOM   4690  C   ARG J 643     -18.620 -42.760  84.281  1.00 83.57           C  
ANISOU 4690  C   ARG J 643    11219  12907   7626     70   3000   -202       C  
ATOM   4691  O   ARG J 643     -18.433 -43.004  85.479  1.00 85.54           O  
ANISOU 4691  O   ARG J 643    11546  13206   7748    -62   3013   -120       O  
ATOM   4692  CB  ARG J 643     -18.886 -40.272  83.992  1.00 92.16           C  
ANISOU 4692  CB  ARG J 643    11940  13993   9084    247   3119     15       C  
ATOM   4693  CG  ARG J 643     -19.070 -39.924  85.468  1.00101.22           C  
ANISOU 4693  CG  ARG J 643    13074  15200  10185    165   3251    169       C  
ATOM   4694  CD  ARG J 643     -17.732 -39.869  86.201  1.00112.03           C  
ANISOU 4694  CD  ARG J 643    14528  16500  11537    -17   3209    223       C  
ATOM   4695  NE  ARG J 643     -17.857 -40.282  87.597  1.00124.94           N  
ANISOU 4695  NE  ARG J 643    16237  18239  12997   -162   3284    324       N  
ATOM   4696  CZ  ARG J 643     -17.388 -41.428  88.085  1.00128.51           C  
ANISOU 4696  CZ  ARG J 643    16857  18740  13229   -323   3141    274       C  
ATOM   4697  NH1 ARG J 643     -17.551 -41.719  89.369  1.00127.83           N  
ANISOU 4697  NH1 ARG J 643    16837  18737  12996   -464   3195    392       N  
ATOM   4698  NH2 ARG J 643     -16.749 -42.278  87.292  1.00128.45           N  
ANISOU 4698  NH2 ARG J 643    16953  18693  13160   -353   2929    108       N  
ATOM   4699  N   ALA J 644     -19.319 -43.573  83.475  1.00 86.32           N  
ANISOU 4699  N   ALA J 644    11634  13237   7925    118   2977   -367       N  
ATOM   4700  CA  ALA J 644     -19.786 -44.877  83.944  1.00 94.45           C  
ANISOU 4700  CA  ALA J 644    12860  14284   8742     23   2950   -477       C  
ATOM   4701  C   ALA J 644     -18.621 -45.748  84.391  1.00 91.12           C  
ANISOU 4701  C   ALA J 644    12597  13827   8196   -149   2752   -524       C  
ATOM   4702  O   ALA J 644     -18.694 -46.417  85.429  1.00 93.32           O  
ANISOU 4702  O   ALA J 644    13018  14167   8272   -267   2731   -492       O  
ATOM   4703  CB  ALA J 644     -20.576 -45.580  82.842  1.00 99.83           C  
ANISOU 4703  CB  ALA J 644    13592  14912   9427     89   2943   -672       C  
ATOM   4704  N   PHE J 645     -17.538 -45.746  83.622  1.00 93.03           N  
ANISOU 4704  N   PHE J 645    12810  13993   8544   -172   2591   -599       N  
ATOM   4705  CA  PHE J 645     -16.298 -46.380  84.037  1.00 91.96           C  
ANISOU 4705  CA  PHE J 645    12770  13868   8304   -338   2367   -642       C  
ATOM   4706  C   PHE J 645     -15.274 -45.279  84.284  1.00 92.28           C  
ANISOU 4706  C   PHE J 645    12664  13935   8462   -372   2334   -516       C  
ATOM   4707  O   PHE J 645     -15.636 -44.201  84.764  1.00 98.66           O  
ANISOU 4707  O   PHE J 645    13358  14772   9356   -321   2504   -350       O  
ATOM   4708  CB  PHE J 645     -15.841 -47.389  82.981  1.00 86.92           C  
ANISOU 4708  CB  PHE J 645    12201  13151   7674   -349   2183   -865       C  
ATOM   4709  CG  PHE J 645     -16.818 -48.518  82.772  1.00 86.35           C  
ANISOU 4709  CG  PHE J 645    12278  13052   7479   -336   2197  -1005       C  
ATOM   4710  CD1 PHE J 645     -16.730 -49.676  83.528  1.00 92.59           C  
ANISOU 4710  CD1 PHE J 645    13265  13880   8036   -455   2053  -1063       C  
ATOM   4711  CD2 PHE J 645     -17.842 -48.409  81.840  1.00 80.43           C  
ANISOU 4711  CD2 PHE J 645    11476  12247   6835   -208   2339  -1075       C  
ATOM   4712  CE1 PHE J 645     -17.633 -50.711  83.346  1.00 92.62           C  
ANISOU 4712  CE1 PHE J 645    13414  13862   7917   -439   2057  -1201       C  
ATOM   4713  CE2 PHE J 645     -18.748 -49.439  81.660  1.00 78.76           C  
ANISOU 4713  CE2 PHE J 645    11402  12018   6506   -207   2348  -1220       C  
ATOM   4714  CZ  PHE J 645     -18.642 -50.590  82.410  1.00 86.91           C  
ANISOU 4714  CZ  PHE J 645    12630  13084   7307   -318   2210  -1288       C  
ATOM   4715  N   THR J 646     -14.006 -45.520  83.970  1.00 85.48           N  
ANISOU 4715  N   THR J 646    11793  13079   7608   -455   2110   -602       N  
ATOM   4716  CA  THR J 646     -12.966 -44.513  84.172  1.00 83.61           C  
ANISOU 4716  CA  THR J 646    11405  12903   7462   -496   2046   -509       C  
ATOM   4717  C   THR J 646     -12.043 -44.464  82.959  1.00 76.48           C  
ANISOU 4717  C   THR J 646    10416  11955   6686   -442   1902   -654       C  
ATOM   4718  O   THR J 646     -10.821 -44.570  83.067  1.00 75.53           O  
ANISOU 4718  O   THR J 646    10255  11917   6524   -527   1678   -704       O  
ATOM   4719  CB  THR J 646     -12.180 -44.780  85.457  1.00 87.33           C  
ANISOU 4719  CB  THR J 646    11932  13503   7746   -694   1874   -417       C  
ATOM   4720  OG1 THR J 646     -12.018 -46.194  85.641  1.00 98.20           O  
ANISOU 4720  OG1 THR J 646    13511  14871   8928   -787   1680   -535       O  
ATOM   4721  CG2 THR J 646     -12.891 -44.179  86.666  1.00 77.35           C  
ANISOU 4721  CG2 THR J 646    10653  12294   6442   -744   2069   -199       C  
ATOM   4722  N   MET J 647     -12.633 -44.284  81.780  1.00 70.88           N  
ANISOU 4722  N   MET J 647     9673  11126   6132   -292   2024   -714       N  
ATOM   4723  CA  MET J 647     -11.900 -44.332  80.524  1.00 68.54           C  
ANISOU 4723  CA  MET J 647     9312  10769   5962   -238   1921   -845       C  
ATOM   4724  C   MET J 647     -12.228 -43.122  79.664  1.00 61.42           C  
ANISOU 4724  C   MET J 647     8295   9782   5260    -83   2089   -751       C  
ATOM   4725  O   MET J 647     -13.351 -42.609  79.683  1.00 63.49           O  
ANISOU 4725  O   MET J 647     8555   9999   5568     23   2285   -641       O  
ATOM   4726  CB  MET J 647     -12.216 -45.619  79.747  1.00 70.11           C  
ANISOU 4726  CB  MET J 647     9617  10890   6131   -238   1858  -1032       C  
ATOM   4727  CG  MET J 647     -11.853 -46.888  80.492  1.00 79.38           C  
ANISOU 4727  CG  MET J 647    10931  12122   7107   -377   1657  -1140       C  
ATOM   4728  SD  MET J 647     -12.014 -48.382  79.504  1.00 84.04           S  
ANISOU 4728  SD  MET J 647    11619  12615   7696   -380   1539  -1387       S  
ATOM   4729  CE  MET J 647     -12.020 -49.611  80.801  1.00 85.28           C  
ANISOU 4729  CE  MET J 647    11988  12833   7580   -513   1347  -1422       C  
ATOM   4730  N   ASP J 648     -11.229 -42.665  78.913  1.00 63.89           N  
ANISOU 4730  N   ASP J 648     8512  10087   5675    -62   1995   -793       N  
ATOM   4731  CA  ASP J 648     -11.468 -41.659  77.892  1.00 64.16           C  
ANISOU 4731  CA  ASP J 648     8478  10018   5882     81   2130   -718       C  
ATOM   4732  C   ASP J 648     -12.281 -42.264  76.755  1.00 66.43           C  
ANISOU 4732  C   ASP J 648     8822  10202   6216    174   2202   -784       C  
ATOM   4733  O   ASP J 648     -12.211 -43.464  76.478  1.00 72.81           O  
ANISOU 4733  O   ASP J 648     9693  11004   6965    104   2103   -944       O  
ATOM   4734  CB  ASP J 648     -10.147 -41.095  77.363  1.00 63.53           C  
ANISOU 4734  CB  ASP J 648     8290   9976   5872     73   2000   -757       C  
ATOM   4735  CG  ASP J 648      -9.329 -40.406  78.443  1.00 64.58           C  
ANISOU 4735  CG  ASP J 648     8313  10279   5945     -1   1892   -693       C  
ATOM   4736  OD1 ASP J 648      -9.426 -40.816  79.618  1.00 68.17           O  
ANISOU 4736  OD1 ASP J 648     8796  10838   6266   -103   1844   -666       O  
ATOM   4737  OD2 ASP J 648      -8.585 -39.456  78.117  1.00 65.92           O  
ANISOU 4737  OD2 ASP J 648     8363  10499   6185     44   1845   -663       O  
ATOM   4738  N   CYS J 649     -13.078 -41.422  76.109  1.00 57.72           N  
ANISOU 4738  N   CYS J 649     7676   9047   5209    330   2359   -666       N  
ATOM   4739  CA  CYS J 649     -13.954 -41.873  75.039  1.00 59.06           C  
ANISOU 4739  CA  CYS J 649     7842   9197   5402    413   2405   -723       C  
ATOM   4740  C   CYS J 649     -13.890 -40.871  73.901  1.00 57.58           C  
ANISOU 4740  C   CYS J 649     7546   8979   5351    525   2426   -637       C  
ATOM   4741  O   CYS J 649     -13.659 -39.681  74.121  1.00 54.29           O  
ANISOU 4741  O   CYS J 649     7067   8548   5011    578   2444   -493       O  
ATOM   4742  CB  CYS J 649     -15.395 -42.038  75.532  1.00 66.09           C  
ANISOU 4742  CB  CYS J 649     8731  10156   6223    449   2504   -700       C  
ATOM   4743  SG  CYS J 649     -15.624 -43.402  76.695  1.00 66.77           S  
ANISOU 4743  SG  CYS J 649     8974  10260   6138    298   2458   -817       S  
ATOM   4744  N   ILE J 650     -14.094 -41.363  72.682  1.00 49.69           N  
ANISOU 4744  N   ILE J 650     6536   7965   4377    541   2426   -737       N  
ATOM   4745  CA  ILE J 650     -13.978 -40.527  71.495  1.00 49.49           C  
ANISOU 4745  CA  ILE J 650     6406   7950   4448    616   2427   -678       C  
ATOM   4746  C   ILE J 650     -14.778 -41.177  70.374  1.00 53.89           C  
ANISOU 4746  C   ILE J 650     6961   8506   5009    590   2503   -816       C  
ATOM   4747  O   ILE J 650     -14.768 -42.399  70.211  1.00 50.48           O  
ANISOU 4747  O   ILE J 650     6626   7986   4568    504   2478   -963       O  
ATOM   4748  CB  ILE J 650     -12.490 -40.301  71.120  1.00 48.28           C  
ANISOU 4748  CB  ILE J 650     6285   7714   4346    605   2367   -668       C  
ATOM   4749  CG1 ILE J 650     -12.348 -39.457  69.855  1.00 59.25           C  
ANISOU 4749  CG1 ILE J 650     7578   9133   5802    683   2374   -604       C  
ATOM   4750  CG2 ILE J 650     -11.741 -41.617  70.987  1.00 49.25           C  
ANISOU 4750  CG2 ILE J 650     6482   7799   4432    484   2297   -863       C  
ATOM   4751  CD1 ILE J 650     -10.923 -39.107  69.548  1.00 57.09           C  
ANISOU 4751  CD1 ILE J 650     7358   8753   5581    673   2344   -585       C  
ATOM   4752  N   THR J 651     -15.499 -40.351  69.621  1.00 51.18           N  
ANISOU 4752  N   THR J 651     6517   8219   4710    607   2587   -799       N  
ATOM   4753  CA  THR J 651     -16.219 -40.812  68.446  1.00 56.96           C  
ANISOU 4753  CA  THR J 651     7282   8858   5504    552   2687   -920       C  
ATOM   4754  C   THR J 651     -15.261 -40.926  67.261  1.00 59.81           C  
ANISOU 4754  C   THR J 651     7634   9165   5925    535   2662   -946       C  
ATOM   4755  O   THR J 651     -14.082 -40.575  67.344  1.00 63.02           O  
ANISOU 4755  O   THR J 651     8009   9622   6312    585   2579   -873       O  
ATOM   4756  CB  THR J 651     -17.374 -39.866  68.129  1.00 71.00           C  
ANISOU 4756  CB  THR J 651     8999  10652   7324    557   2816   -899       C  
ATOM   4757  OG1 THR J 651     -16.848 -38.611  67.679  1.00 72.37           O  
ANISOU 4757  OG1 THR J 651     9059  10915   7523    584   2809   -813       O  
ATOM   4758  CG2 THR J 651     -18.236 -39.645  69.366  1.00 79.33           C  
ANISOU 4758  CG2 THR J 651    10040  11783   8319    573   2849   -872       C  
ATOM   4759  N   LEU J 652     -15.777 -41.418  66.131  1.00 56.63           N  
ANISOU 4759  N   LEU J 652     7268   8646   5602    465   2750  -1050       N  
ATOM   4760  CA  LEU J 652     -14.960 -41.522  64.926  1.00 46.28           C  
ANISOU 4760  CA  LEU J 652     5938   7293   4353    434   2756  -1077       C  
ATOM   4761  C   LEU J 652     -14.641 -40.162  64.321  1.00 59.19           C  
ANISOU 4761  C   LEU J 652     7482   9015   5991    494   2796   -953       C  
ATOM   4762  O   LEU J 652     -13.670 -40.046  63.566  1.00 59.33           O  
ANISOU 4762  O   LEU J 652     7471   9054   6020    498   2777   -938       O  
ATOM   4763  CB  LEU J 652     -15.659 -42.399  63.887  1.00 47.43           C  
ANISOU 4763  CB  LEU J 652     6142   7287   4592    332   2859  -1219       C  
ATOM   4764  CG  LEU J 652     -15.794 -43.885  64.224  1.00 47.49           C  
ANISOU 4764  CG  LEU J 652     6229   7215   4600    234   2810  -1396       C  
ATOM   4765  CD1 LEU J 652     -16.654 -44.586  63.188  1.00 49.24           C  
ANISOU 4765  CD1 LEU J 652     6503   7279   4929    116   2950  -1551       C  
ATOM   4766  CD2 LEU J 652     -14.424 -44.535  64.316  1.00 47.79           C  
ANISOU 4766  CD2 LEU J 652     6247   7280   4630    188   2679  -1460       C  
ATOM   4767  N   GLU J 653     -15.432 -39.135  64.633  1.00 59.11           N  
ANISOU 4767  N   GLU J 653     7427   9058   5972    526   2853   -882       N  
ATOM   4768  CA  GLU J 653     -15.201 -37.791  64.127  1.00 71.95           C  
ANISOU 4768  CA  GLU J 653     8975  10762   7601    546   2887   -794       C  
ATOM   4769  C   GLU J 653     -14.462 -36.906  65.126  1.00 78.02           C  
ANISOU 4769  C   GLU J 653     9636  11715   8293    579   2755   -723       C  
ATOM   4770  O   GLU J 653     -14.540 -35.676  65.035  1.00 83.16           O  
ANISOU 4770  O   GLU J 653    10232  12405   8961    549   2791   -686       O  
ATOM   4771  CB  GLU J 653     -16.527 -37.156  63.702  1.00 79.63           C  
ANISOU 4771  CB  GLU J 653     9989  11612   8656    532   3051   -782       C  
ATOM   4772  CG  GLU J 653     -17.706 -37.491  64.598  1.00 81.02           C  
ANISOU 4772  CG  GLU J 653    10205  11743   8838    540   3092   -822       C  
ATOM   4773  CD  GLU J 653     -19.038 -37.246  63.910  1.00 82.97           C  
ANISOU 4773  CD  GLU J 653    10531  11810   9185    543   3275   -839       C  
ATOM   4774  OE1 GLU J 653     -19.309 -37.907  62.886  1.00 82.80           O  
ANISOU 4774  OE1 GLU J 653    10586  11642   9231    499   3359   -904       O  
ATOM   4775  OE2 GLU J 653     -19.814 -36.395  64.391  1.00 84.33           O  
ANISOU 4775  OE2 GLU J 653    10686  11978   9378    592   3341   -792       O  
ATOM   4776  N   GLY J 654     -13.750 -37.509  66.080  1.00 78.85           N  
ANISOU 4776  N   GLY J 654     9756  11846   8360    617   2602   -700       N  
ATOM   4777  CA  GLY J 654     -12.767 -36.806  66.875  1.00 79.29           C  
ANISOU 4777  CA  GLY J 654     9735  12007   8384    640   2435   -623       C  
ATOM   4778  C   GLY J 654     -13.258 -36.203  68.174  1.00 74.67           C  
ANISOU 4778  C   GLY J 654     9072  11513   7787    573   2391   -621       C  
ATOM   4779  O   GLY J 654     -12.428 -35.759  68.977  1.00 73.01           O  
ANISOU 4779  O   GLY J 654     8779  11400   7561    507   2247   -628       O  
ATOM   4780  N   ASP J 655     -14.567 -36.163  68.411  1.00 72.93           N  
ANISOU 4780  N   ASP J 655     8871  11253   7585    544   2528   -651       N  
ATOM   4781  CA  ASP J 655     -15.089 -35.550  69.628  1.00 75.87           C  
ANISOU 4781  CA  ASP J 655     9184  11680   7962    470   2536   -652       C  
ATOM   4782  C   ASP J 655     -14.789 -36.437  70.828  1.00 75.92           C  
ANISOU 4782  C   ASP J 655     9220  11733   7892    548   2412   -578       C  
ATOM   4783  O   ASP J 655     -15.218 -37.594  70.874  1.00 75.47           O  
ANISOU 4783  O   ASP J 655     9306  11564   7806    632   2472   -568       O  
ATOM   4784  CB  ASP J 655     -16.589 -35.317  69.506  1.00 78.29           C  
ANISOU 4784  CB  ASP J 655     9524  11921   8300    500   2736   -662       C  
ATOM   4785  CG  ASP J 655     -16.983 -34.757  68.163  1.00 81.15           C  
ANISOU 4785  CG  ASP J 655     9917  12195   8722    535   2886   -666       C  
ATOM   4786  OD1 ASP J 655     -16.247 -33.897  67.634  1.00 77.52           O  
ANISOU 4786  OD1 ASP J 655     9430  11731   8293    511   2874   -639       O  
ATOM   4787  OD2 ASP J 655     -18.032 -35.184  67.639  1.00 87.07           O  
ANISOU 4787  OD2 ASP J 655    10749  12822   9512    578   3008   -688       O  
ATOM   4788  N   GLN J 656     -14.069 -35.895  71.804  1.00 74.90           N  
ANISOU 4788  N   GLN J 656     8992  11709   7758    431   2288   -591       N  
ATOM   4789  CA  GLN J 656     -13.616 -36.655  72.958  1.00 72.75           C  
ANISOU 4789  CA  GLN J 656     9077  11065   7501    807   2392   -223       C  
ATOM   4790  C   GLN J 656     -14.415 -36.293  74.203  1.00 75.45           C  
ANISOU 4790  C   GLN J 656     9190  11728   7750    675   2334   -280       C  
ATOM   4791  O   GLN J 656     -15.167 -35.315  74.240  1.00 79.07           O  
ANISOU 4791  O   GLN J 656     9512  12209   8324    124   2460   -676       O  
ATOM   4792  CB  GLN J 656     -12.124 -36.419  73.221  1.00 70.45           C  
ANISOU 4792  CB  GLN J 656     9132  10200   7436    471   2614   -364       C  
ATOM   4793  CG  GLN J 656     -11.269 -36.292  71.976  1.00 66.87           C  
ANISOU 4793  CG  GLN J 656     8678   9712   7017    473   2572   -413       C  
ATOM   4794  CD  GLN J 656      -9.848 -35.866  72.289  1.00 63.87           C  
ANISOU 4794  CD  GLN J 656     8191   9508   6568    380   2459   -504       C  
ATOM   4795  OE1 GLN J 656      -9.531 -35.505  73.422  1.00 60.96           O  
ANISOU 4795  OE1 GLN J 656     7732   9306   6122    352   2410   -492       O  
ATOM   4796  NE2 GLN J 656      -8.986 -35.901  71.281  1.00 67.21           N  
ANISOU 4796  NE2 GLN J 656     8614   9934   6988    410   2410   -544       N  
ATOM   4797  N   VAL J 657     -14.239 -37.120  75.231  1.00 78.24           N  
ANISOU 4797  N   VAL J 657     9991  11531   8207    691   2595   -174       N  
ATOM   4798  CA  VAL J 657     -14.680 -36.823  76.588  1.00 74.06           C  
ANISOU 4798  CA  VAL J 657     9524  10907   7709    587   2738   -137       C  
ATOM   4799  C   VAL J 657     -13.758 -37.572  77.545  1.00 76.33           C  
ANISOU 4799  C   VAL J 657     9858  11270   7875    391   2672   -248       C  
ATOM   4800  O   VAL J 657     -13.599 -38.796  77.455  1.00 77.69           O  
ANISOU 4800  O   VAL J 657    10074  11538   7905    392   2570   -332       O  
ATOM   4801  CB  VAL J 657     -16.170 -37.166  76.802  1.00 63.40           C  
ANISOU 4801  CB  VAL J 657     7793  10184   6114    647   2555   -186       C  
ATOM   4802  CG1 VAL J 657     -16.511 -38.557  76.279  1.00 68.05           C  
ANISOU 4802  CG1 VAL J 657     8552  10657   6646    627   2588   -318       C  
ATOM   4803  CG2 VAL J 657     -16.539 -37.043  78.273  1.00 56.39           C  
ANISOU 4803  CG2 VAL J 657     6948   9274   5203    639   2670    -67       C  
ATOM   4804  N   SER J 658     -13.111 -36.833  78.441  1.00 76.51           N  
ANISOU 4804  N   SER J 658     9799  11373   7899    240   2681   -254       N  
ATOM   4805  CA  SER J 658     -12.095 -37.411  79.303  1.00 75.62           C  
ANISOU 4805  CA  SER J 658     9650  11470   7613    155   2524   -276       C  
ATOM   4806  C   SER J 658     -12.737 -38.229  80.421  1.00 76.15           C  
ANISOU 4806  C   SER J 658     9790  11600   7544    102   2559   -239       C  
ATOM   4807  O   SER J 658     -13.948 -38.185  80.650  1.00 75.26           O  
ANISOU 4807  O   SER J 658     9721  11409   7463    170   2721   -170       O  
ATOM   4808  CB  SER J 658     -11.205 -36.313  79.885  1.00 75.56           C  
ANISOU 4808  CB  SER J 658     9442  11642   7626    106   2414   -216       C  
ATOM   4809  OG  SER J 658     -10.329 -36.830  80.871  1.00 76.50           O  
ANISOU 4809  OG  SER J 658     9501  11974   7590     10   2214   -208       O  
ATOM   4810  N   HIS J 659     -11.896 -38.990  81.127  1.00 75.46           N  
ANISOU 4810  N   HIS J 659     9697  11671   7302    -27   2357   -290       N  
ATOM   4811  CA  HIS J 659     -12.369 -39.750  82.278  1.00 80.12           C  
ANISOU 4811  CA  HIS J 659    10372  12334   7735   -126   2372   -252       C  
ATOM   4812  C   HIS J 659     -12.729 -38.848  83.450  1.00 81.80           C  
ANISOU 4812  C   HIS J 659    10489  12621   7970   -178   2500    -82       C  
ATOM   4813  O   HIS J 659     -13.462 -39.278  84.347  1.00 86.70           O  
ANISOU 4813  O   HIS J 659    11188  13262   8492   -227   2600    -16       O  
ATOM   4814  CB  HIS J 659     -11.316 -40.775  82.704  1.00 82.60           C  
ANISOU 4814  CB  HIS J 659    10730  12785   7870   -276   2111   -350       C  
ATOM   4815  CG  HIS J 659      -9.954 -40.191  82.920  1.00 86.50           C  
ANISOU 4815  CG  HIS J 659    11068  13445   8354   -335   1911   -334       C  
ATOM   4816  ND1 HIS J 659      -9.047 -40.015  81.896  1.00 87.27           N  
ANISOU 4816  ND1 HIS J 659    11092  13543   8525   -262   1779   -448       N  
ATOM   4817  CD2 HIS J 659      -9.342 -39.745  84.043  1.00 88.31           C  
ANISOU 4817  CD2 HIS J 659    11193  13864   8497   -451   1814   -206       C  
ATOM   4818  CE1 HIS J 659      -7.938 -39.485  82.378  1.00 86.60           C  
ANISOU 4818  CE1 HIS J 659    10865  13652   8387   -306   1600   -410       C  
ATOM   4819  NE2 HIS J 659      -8.090 -39.311  83.679  1.00 87.44           N  
ANISOU 4819  NE2 HIS J 659    10947  13881   8395   -426   1611   -254       N  
ATOM   4820  N   ARG J 660     -12.232 -37.613  83.462  1.00 83.61           N  
ANISOU 4820  N   ARG J 660    10537  12909   8323   -167   2491    -13       N  
ATOM   4821  CA  ARG J 660     -12.606 -36.618  84.456  1.00 85.16           C  
ANISOU 4821  CA  ARG J 660    10594  13177   8586   -209   2617    140       C  
ATOM   4822  C   ARG J 660     -13.808 -35.787  84.027  1.00 84.67           C  
ANISOU 4822  C   ARG J 660    10529  12936   8704   -116   2886    138       C  
ATOM   4823  O   ARG J 660     -14.277 -34.953  84.808  1.00 93.28           O  
ANISOU 4823  O   ARG J 660    11493  14076   9872   -160   3014    226       O  
ATOM   4824  CB  ARG J 660     -11.423 -35.691  84.743  1.00 89.34           C  
ANISOU 4824  CB  ARG J 660    10885  13914   9146   -237   2433    222       C  
ATOM   4825  CG  ARG J 660     -10.198 -36.404  85.281  1.00 94.59           C  
ANISOU 4825  CG  ARG J 660    11539  14776   9626   -367   2167    225       C  
ATOM   4826  CD  ARG J 660      -9.109 -35.413  85.650  1.00106.34           C  
ANISOU 4826  CD  ARG J 660    12776  16491  11139   -380   2002    339       C  
ATOM   4827  NE  ARG J 660      -7.992 -36.061  86.329  1.00118.64           N  
ANISOU 4827  NE  ARG J 660    14376  18088  12614   -516   1682    351       N  
ATOM   4828  CZ  ARG J 660      -6.935 -35.416  86.809  1.00125.67           C  
ANISOU 4828  CZ  ARG J 660    15134  18966  13649   -530   1394    430       C  
ATOM   4829  NH1 ARG J 660      -6.846 -34.098  86.687  1.00126.52           N  
ANISOU 4829  NH1 ARG J 660    15029  19122  13922   -426   1422    512       N  
ATOM   4830  NH2 ARG J 660      -5.965 -36.089  87.413  1.00127.75           N  
ANISOU 4830  NH2 ARG J 660    15482  19157  13898   -640   1062    421       N  
ATOM   4831  N   GLY J 661     -14.308 -35.988  82.812  1.00 79.02           N  
ANISOU 4831  N   GLY J 661     9934  12024   8066    -16   2953     28       N  
ATOM   4832  CA  GLY J 661     -15.439 -35.227  82.326  1.00 78.81           C  
ANISOU 4832  CA  GLY J 661     9886  11838   8221    -19   3106    -43       C  
ATOM   4833  C   GLY J 661     -15.092 -34.020  81.487  1.00 69.71           C  
ANISOU 4833  C   GLY J 661     8553  10746   7188    -19   3064   -109       C  
ATOM   4834  O   GLY J 661     -15.946 -33.143  81.313  1.00 69.42           O  
ANISOU 4834  O   GLY J 661     8370  10772   7233    -52   3141   -174       O  
ATOM   4835  N   ALA J 662     -13.872 -33.944  80.960  1.00 80.57           N  
ANISOU 4835  N   ALA J 662     9898  12181   8533     54   2924    -81       N  
ATOM   4836  CA  ALA J 662     -13.459 -32.815  80.133  1.00 79.22           C  
ANISOU 4836  CA  ALA J 662     9579  12065   8456    134   2860    -83       C  
ATOM   4837  C   ALA J 662     -13.982 -33.018  78.717  1.00 73.96           C  
ANISOU 4837  C   ALA J 662     9008  11245   7851    116   2889   -241       C  
ATOM   4838  O   ALA J 662     -13.541 -33.928  78.007  1.00 65.74           O  
ANISOU 4838  O   ALA J 662     8117  10077   6785    119   2816   -300       O  
ATOM   4839  CB  ALA J 662     -11.940 -32.670  80.145  1.00 80.76           C  
ANISOU 4839  CB  ALA J 662     9682  12415   8587    211   2615     -6       C  
ATOM   4840  N   LEU J 663     -14.917 -32.169  78.303  1.00 71.43           N  
ANISOU 4840  N   LEU J 663     8561  10983   7596    123   2962   -287       N  
ATOM   4841  CA  LEU J 663     -15.539 -32.301  76.993  1.00 72.29           C  
ANISOU 4841  CA  LEU J 663     8664  11091   7711    113   2930   -420       C  
ATOM   4842  C   LEU J 663     -14.673 -31.632  75.933  1.00 80.51           C  
ANISOU 4842  C   LEU J 663     9695  12104   8792    219   2887   -383       C  
ATOM   4843  O   LEU J 663     -14.288 -30.468  76.076  1.00 93.68           O  
ANISOU 4843  O   LEU J 663    11262  13827  10506    360   2893   -244       O  
ATOM   4844  CB  LEU J 663     -16.941 -31.689  77.007  1.00 65.49           C  
ANISOU 4844  CB  LEU J 663     7671  10353   6861    174   3036   -425       C  
ATOM   4845  CG  LEU J 663     -18.107 -32.638  77.303  1.00 64.60           C  
ANISOU 4845  CG  LEU J 663     7546  10364   6637    129   3026   -503       C  
ATOM   4846  CD1 LEU J 663     -18.145 -33.743  76.272  1.00 71.81           C  
ANISOU 4846  CD1 LEU J 663     8495  11337   7451    170   2881   -569       C  
ATOM   4847  CD2 LEU J 663     -18.044 -33.226  78.705  1.00 59.96           C  
ANISOU 4847  CD2 LEU J 663     6992   9809   5982      1   3031   -488       C  
ATOM   4848  N   THR J 664     -14.366 -32.369  74.866  1.00 75.19           N  
ANISOU 4848  N   THR J 664     9104  11364   8100    168   2799   -488       N  
ATOM   4849  CA  THR J 664     -13.486 -31.877  73.812  1.00 75.35           C  
ANISOU 4849  CA  THR J 664     9136  11358   8137    248   2762   -463       C  
ATOM   4850  C   THR J 664     -14.057 -32.285  72.464  1.00 77.78           C  
ANISOU 4850  C   THR J 664     9426  11700   8425    223   2729   -570       C  
ATOM   4851  O   THR J 664     -14.243 -33.477  72.205  1.00 74.63           O  
ANISOU 4851  O   THR J 664     9027  11360   7969    144   2621   -677       O  
ATOM   4852  CB  THR J 664     -12.064 -32.423  73.981  1.00 80.80           C  
ANISOU 4852  CB  THR J 664     9935  11969   8798    261   2675   -432       C  
ATOM   4853  OG1 THR J 664     -11.454 -31.825  75.132  1.00 85.39           O  
ANISOU 4853  OG1 THR J 664    10421  12683   9339    360   2613   -286       O  
ATOM   4854  CG2 THR J 664     -11.220 -32.116  72.751  1.00 82.23           C  
ANISOU 4854  CG2 THR J 664    10128  12144   8970    317   2627   -446       C  
ATOM   4855  N   GLY J 665     -14.330 -31.305  71.609  1.00 83.51           N  
ANISOU 4855  N   GLY J 665    10108  12454   9169    347   2811   -506       N  
ATOM   4856  CA  GLY J 665     -14.881 -31.607  70.300  1.00 85.71           C  
ANISOU 4856  CA  GLY J 665    10386  12758   9423    384   2823   -549       C  
ATOM   4857  C   GLY J 665     -14.774 -30.417  69.373  1.00 83.75           C  
ANISOU 4857  C   GLY J 665    10158  12445   9218    525   2910   -430       C  
ATOM   4858  O   GLY J 665     -14.381 -29.317  69.772  1.00 78.71           O  
ANISOU 4858  O   GLY J 665     9506  11781   8620    638   2920   -292       O  
ATOM   4859  N   GLY J 666     -15.136 -30.661  68.121  1.00 90.12           N  
ANISOU 4859  N   GLY J 666    11002  13224  10014    558   2950   -442       N  
ATOM   4860  CA  GLY J 666     -15.090 -29.625  67.107  1.00 93.95           C  
ANISOU 4860  CA  GLY J 666    11544  13616  10537    696   3036   -305       C  
ATOM   4861  C   GLY J 666     -15.050 -30.249  65.722  1.00 93.94           C  
ANISOU 4861  C   GLY J 666    11600  13586  10507    668   3061   -349       C  
ATOM   4862  O   GLY J 666     -15.468 -31.389  65.527  1.00 90.54           O  
ANISOU 4862  O   GLY J 666    11159  13189  10054    603   3040   -454       O  
ATOM   4863  N   TYR J 667     -14.538 -29.471  64.773  1.00 92.39           N  
ANISOU 4863  N   TYR J 667    11466  13334  10303    749   3112   -241       N  
ATOM   4864  CA  TYR J 667     -14.415 -29.903  63.383  1.00 97.25           C  
ANISOU 4864  CA  TYR J 667    12144  13909  10896    727   3168   -252       C  
ATOM   4865  C   TYR J 667     -12.959 -30.268  63.113  1.00 98.73           C  
ANISOU 4865  C   TYR J 667    12301  14215  10997    627   3047   -334       C  
ATOM   4866  O   TYR J 667     -12.117 -29.392  62.901  1.00 99.15           O  
ANISOU 4866  O   TYR J 667    12393  14270  11010    687   3043   -244       O  
ATOM   4867  CB  TYR J 667     -14.899 -28.819  62.425  1.00104.67           C  
ANISOU 4867  CB  TYR J 667    13194  14700  11878    887   3340    -65       C  
ATOM   4868  CG  TYR J 667     -14.592 -29.121  60.975  1.00109.10           C  
ANISOU 4868  CG  TYR J 667    13836  15208  12410    857   3420    -50       C  
ATOM   4869  CD1 TYR J 667     -15.236 -30.157  60.311  1.00110.90           C  
ANISOU 4869  CD1 TYR J 667    14092  15359  12685    785   3492   -134       C  
ATOM   4870  CD2 TYR J 667     -13.656 -28.371  60.272  1.00109.26           C  
ANISOU 4870  CD2 TYR J 667    13911  15252  12352    910   3435     56       C  
ATOM   4871  CE1 TYR J 667     -14.957 -30.440  58.985  1.00110.88           C  
ANISOU 4871  CE1 TYR J 667    14161  15294  12673    751   3589   -112       C  
ATOM   4872  CE2 TYR J 667     -13.370 -28.647  58.944  1.00109.57           C  
ANISOU 4872  CE2 TYR J 667    14022  15251  12359    869   3528     74       C  
ATOM   4873  CZ  TYR J 667     -14.025 -29.683  58.308  1.00109.14           C  
ANISOU 4873  CZ  TYR J 667    13984  15112  12372    784   3610     -9       C  
ATOM   4874  OH  TYR J 667     -13.748 -29.963  56.990  1.00106.59           O  
ANISOU 4874  OH  TYR J 667    13731  14736  12034    739   3724     18       O  
ATOM   4875  N   TYR J 668     -12.666 -31.565  63.123  1.00 97.88           N  
ANISOU 4875  N   TYR J 668    12123  14216  10851    512   2949   -490       N  
ATOM   4876  CA  TYR J 668     -11.357 -32.067  62.730  1.00 90.08           C  
ANISOU 4876  CA  TYR J 668    11096  13331   9800    429   2841   -580       C  
ATOM   4877  C   TYR J 668     -11.375 -32.364  61.236  1.00 78.03           C  
ANISOU 4877  C   TYR J 668     9600  11800   8246    460   2942   -549       C  
ATOM   4878  O   TYR J 668     -12.202 -33.153  60.765  1.00 71.03           O  
ANISOU 4878  O   TYR J 668     8743  10840   7407    492   3011   -544       O  
ATOM   4879  CB  TYR J 668     -10.987 -33.315  63.528  1.00 90.76           C  
ANISOU 4879  CB  TYR J 668    11118  13480   9888    384   2651   -680       C  
ATOM   4880  CG  TYR J 668     -10.701 -33.048  64.987  1.00 92.44           C  
ANISOU 4880  CG  TYR J 668    11336  13638  10150    287   2570   -729       C  
ATOM   4881  CD2 TYR J 668     -11.550 -33.523  65.979  1.00 96.49           C  
ANISOU 4881  CD2 TYR J 668    11814  14180  10667    303   2533   -730       C  
ATOM   4882  CD1 TYR J 668      -9.579 -32.325  65.375  1.00 92.03           C  
ANISOU 4882  CD1 TYR J 668    11387  13442  10137    242   2598   -716       C  
ATOM   4883  CE2 TYR J 668     -11.293 -33.282  67.317  1.00 95.97           C  
ANISOU 4883  CE2 TYR J 668    11794  14003  10666    198   2516   -759       C  
ATOM   4884  CE1 TYR J 668      -9.313 -32.078  66.713  1.00 91.20           C  
ANISOU 4884  CE1 TYR J 668    11345  13239  10068    272   2596   -661       C  
ATOM   4885  CZ  TYR J 668     -10.173 -32.560  67.678  1.00 90.51           C  
ANISOU 4885  CZ  TYR J 668    11228  13145  10017    220   2577   -690       C  
ATOM   4886  OH  TYR J 668      -9.917 -32.322  69.009  1.00 83.20           O  
ANISOU 4886  OH  TYR J 668    10341  12173   9097    282   2579   -604       O  
ATOM   4887  N   ASP J 669     -10.471 -31.730  60.498  1.00 84.48           N  
ANISOU 4887  N   ASP J 669    10456  12628   9014    451   2978   -511       N  
ATOM   4888  CA  ASP J 669     -10.411 -31.898  59.057  1.00 85.65           C  
ANISOU 4888  CA  ASP J 669    10652  12747   9144    466   3095   -459       C  
ATOM   4889  C   ASP J 669      -9.683 -33.189  58.693  1.00 87.26           C  
ANISOU 4889  C   ASP J 669    10760  13085   9309    438   3004   -570       C  
ATOM   4890  O   ASP J 669      -8.948 -33.771  59.497  1.00 88.43           O  
ANISOU 4890  O   ASP J 669    10843  13302   9456    438   2806   -644       O  
ATOM   4891  CB  ASP J 669      -9.707 -30.703  58.407  1.00 85.36           C  
ANISOU 4891  CB  ASP J 669    10710  12682   9042    504   3176   -344       C  
ATOM   4892  CG  ASP J 669     -10.106 -30.505  56.954  1.00 84.37           C  
ANISOU 4892  CG  ASP J 669    10692  12446   8920    542   3372   -216       C  
ATOM   4893  OD1 ASP J 669     -10.795 -31.385  56.394  1.00 82.58           O  
ANISOU 4893  OD1 ASP J 669    10467  12142   8769    510   3452   -245       O  
ATOM   4894  OD2 ASP J 669      -9.720 -29.472  56.368  1.00 83.14           O  
ANISOU 4894  OD2 ASP J 669    10641  12256   8692    613   3458    -74       O  
ATOM   4895  N   THR J 670      -9.908 -33.640  57.461  1.00 78.96           N  
ANISOU 4895  N   THR J 670     9756  11963   8283    446   3142   -530       N  
ATOM   4896  CA  THR J 670      -9.146 -34.740  56.890  1.00 80.06           C  
ANISOU 4896  CA  THR J 670     9851  12163   8406    464   3125   -585       C  
ATOM   4897  C   THR J 670      -7.913 -34.250  56.137  1.00 91.59           C  
ANISOU 4897  C   THR J 670    11280  13753   9765    449   3121   -574       C  
ATOM   4898  O   THR J 670      -7.016 -35.050  55.849  1.00 98.46           O  
ANISOU 4898  O   THR J 670    12115  14670  10627    504   3067   -605       O  
ATOM   4899  CB  THR J 670     -10.041 -35.570  55.958  1.00 74.19           C  
ANISOU 4899  CB  THR J 670     9192  11202   7794    415   3295   -585       C  
ATOM   4900  OG1 THR J 670     -11.371 -35.603  56.485  1.00 71.27           O  
ANISOU 4900  OG1 THR J 670     8884  10679   7518    407   3332   -583       O  
ATOM   4901  CG2 THR J 670      -9.539 -37.009  55.861  1.00 65.66           C  
ANISOU 4901  CG2 THR J 670     8093  10087   6768    409   3261   -690       C  
ATOM   4902  N   ARG J 671      -7.839 -32.949  55.839  1.00 93.94           N  
ANISOU 4902  N   ARG J 671    11631  14065   9998    398   3199   -515       N  
ATOM   4903  CA  ARG J 671      -6.689 -32.404  55.127  1.00101.74           C  
ANISOU 4903  CA  ARG J 671    12630  15144  10881    362   3221   -512       C  
ATOM   4904  C   ARG J 671      -5.439 -32.383  55.997  1.00 97.42           C  
ANISOU 4904  C   ARG J 671    12023  14672  10322    309   2994   -651       C  
ATOM   4905  O   ARG J 671      -4.324 -32.508  55.479  1.00 98.58           O  
ANISOU 4905  O   ARG J 671    12135  14911  10408    278   2965   -715       O  
ATOM   4906  CB  ARG J 671      -7.006 -30.993  54.629  1.00113.66           C  
ANISOU 4906  CB  ARG J 671    14317  16522  12346    386   3398   -340       C  
ATOM   4907  CG  ARG J 671      -7.964 -30.943  53.452  1.00120.40           C  
ANISOU 4907  CG  ARG J 671    15294  17190  13264    413   3625   -182       C  
ATOM   4908  CD  ARG J 671      -8.273 -29.509  53.057  1.00124.65           C  
ANISOU 4908  CD  ARG J 671    16022  17587  13751    516   3765     42       C  
ATOM   4909  NE  ARG J 671      -8.835 -29.419  51.713  1.00130.07           N  
ANISOU 4909  NE  ARG J 671    16842  18114  14467    515   4007    190       N  
ATOM   4910  CZ  ARG J 671      -9.179 -28.279  51.123  1.00133.64           C  
ANISOU 4910  CZ  ARG J 671    17479  18427  14869    626   4164    422       C  
ATOM   4911  NH1 ARG J 671      -9.021 -27.126  51.759  1.00134.20           N  
ANISOU 4911  NH1 ARG J 671    17619  18516  14856    778   4092    542       N  
ATOM   4912  NH2 ARG J 671      -9.684 -28.291  49.896  1.00134.90           N  
ANISOU 4912  NH2 ARG J 671    17766  18422  15068    603   4399    550       N  
ATOM   4913  N   LYS J 672      -5.598 -32.222  57.311  1.00 89.90           N  
ANISOU 4913  N   LYS J 672    11086  13628   9444    266   2882   -714       N  
ATOM   4914  CA  LYS J 672      -4.470 -32.178  58.234  1.00 92.49           C  
ANISOU 4914  CA  LYS J 672    11508  13779   9854    138   2814   -856       C  
ATOM   4915  C   LYS J 672      -4.352 -33.451  59.069  1.00 93.21           C  
ANISOU 4915  C   LYS J 672    11599  13706  10112     22   2729  -1014       C  
ATOM   4916  O   LYS J 672      -3.554 -33.492  60.011  1.00 99.84           O  
ANISOU 4916  O   LYS J 672    12829  14022  11082    234   2867   -818       O  
ATOM   4917  CB  LYS J 672      -4.576 -30.952  59.147  1.00 96.56           C  
ANISOU 4917  CB  LYS J 672    12166  14187  10336    264   2866   -710       C  
ATOM   4918  CG  LYS J 672      -3.229 -30.364  59.571  1.00 96.61           C  
ANISOU 4918  CG  LYS J 672    12291  14156  10260    381   2849   -666       C  
ATOM   4919  CD  LYS J 672      -3.239 -29.954  61.037  1.00 94.70           C  
ANISOU 4919  CD  LYS J 672    12042  13920  10021    523   2712   -585       C  
ATOM   4920  CE  LYS J 672      -1.825 -29.872  61.597  1.00 92.54           C  
ANISOU 4920  CE  LYS J 672    11772  13723   9667    659   2537   -583       C  
ATOM   4921  NZ  LYS J 672      -1.810 -29.494  63.037  1.00 90.38           N  
ANISOU 4921  NZ  LYS J 672    11415  13544   9379    788   2334   -515       N  
ATOM   4922  N   SER J 673      -5.127 -34.488  58.753  1.00 89.07           N  
ANISOU 4922  N   SER J 673    10792  13687   9363    614   2476   -687       N  
ATOM   4923  CA  SER J 673      -4.954 -35.778  59.412  1.00 80.43           C  
ANISOU 4923  CA  SER J 673    10057  12083   8421    944   2610   -452       C  
ATOM   4924  C   SER J 673      -3.623 -36.373  58.974  1.00 70.38           C  
ANISOU 4924  C   SER J 673     8933  10593   7215    883   2733   -546       C  
ATOM   4925  O   SER J 673      -3.433 -36.687  57.794  1.00 67.51           O  
ANISOU 4925  O   SER J 673     8462  10392   6798    877   2791   -586       O  
ATOM   4926  CB  SER J 673      -6.111 -36.714  59.083  1.00 84.57           C  
ANISOU 4926  CB  SER J 673    10468  12686   8978    795   2662   -597       C  
ATOM   4927  OG  SER J 673      -6.557 -36.514  57.758  1.00 88.88           O  
ANISOU 4927  OG  SER J 673    10936  13336   9499    682   2807   -640       O  
ATOM   4928  N   ARG J 674      -2.702 -36.516  59.930  1.00 69.46           N  
ANISOU 4928  N   ARG J 674    10399   9589   6403  -1682   1816  -1859       N  
ATOM   4929  CA  ARG J 674      -1.320 -36.861  59.611  1.00 61.01           C  
ANISOU 4929  CA  ARG J 674     9403   8466   5310  -1663   1769  -1773       C  
ATOM   4930  C   ARG J 674      -1.213 -38.282  59.073  1.00 65.49           C  
ANISOU 4930  C   ARG J 674     9974   9062   5848  -1571   1738  -1722       C  
ATOM   4931  O   ARG J 674      -0.399 -38.559  58.183  1.00 73.27           O  
ANISOU 4931  O   ARG J 674    10994  10020   6827  -1528   1693  -1671       O  
ATOM   4932  CB  ARG J 674      -0.457 -36.684  60.859  1.00 54.25           C  
ANISOU 4932  CB  ARG J 674     8612   7588   4415  -1728   1818  -1733       C  
ATOM   4933  CG  ARG J 674      -0.419 -35.249  61.371  1.00 53.80           C  
ANISOU 4933  CG  ARG J 674     8547   7535   4359  -1862   1846  -1787       C  
ATOM   4934  CD  ARG J 674       0.721 -35.033  62.347  1.00 58.40           C  
ANISOU 4934  CD  ARG J 674     9234   8061   4897  -1964   1891  -1746       C  
ATOM   4935  NE  ARG J 674       0.757 -33.666  62.857  1.00 63.22           N  
ANISOU 4935  NE  ARG J 674     9826   8713   5482  -2136   1914  -1806       N  
ATOM   4936  CZ  ARG J 674       0.369 -33.318  64.079  1.00 71.24           C  
ANISOU 4936  CZ  ARG J 674    10810   9792   6464  -2252   1990  -1848       C  
ATOM   4937  NH1 ARG J 674      -0.089 -34.240  64.917  1.00 75.21           N  
ANISOU 4937  NH1 ARG J 674    11311  10300   6966  -2200   2050  -1830       N  
ATOM   4938  NH2 ARG J 674       0.435 -32.052  64.465  1.00 75.65           N  
ANISOU 4938  NH2 ARG J 674    11332  10434   6976  -2432   2006  -1905       N  
ATOM   4939  N   LEU J 675      -2.043 -39.193  59.587  1.00 60.91           N  
ANISOU 4939  N   LEU J 675     9354   8557   5235  -1548   1765  -1736       N  
ATOM   4940  CA  LEU J 675      -2.036 -40.563  59.090  1.00 61.98           C  
ANISOU 4940  CA  LEU J 675     9476   8766   5310  -1484   1736  -1696       C  
ATOM   4941  C   LEU J 675      -2.630 -40.657  57.689  1.00 64.43           C  
ANISOU 4941  C   LEU J 675     9752   9077   5652  -1493   1690  -1746       C  
ATOM   4942  O   LEU J 675      -2.214 -41.513  56.899  1.00 70.14           O  
ANISOU 4942  O   LEU J 675    10471   9851   6329  -1462   1652  -1705       O  
ATOM   4943  CB  LEU J 675      -2.785 -41.481  60.058  1.00 55.95           C  
ANISOU 4943  CB  LEU J 675     8683   8097   4480  -1476   1777  -1701       C  
ATOM   4944  CG  LEU J 675      -2.187 -41.688  61.453  1.00 55.03           C  
ANISOU 4944  CG  LEU J 675     8611   7989   4308  -1455   1836  -1636       C  
ATOM   4945  CD1 LEU J 675      -2.741 -40.701  62.465  1.00 51.69           C  
ANISOU 4945  CD1 LEU J 675     8182   7524   3933  -1537   1896  -1697       C  
ATOM   4946  CD2 LEU J 675      -2.427 -43.113  61.918  1.00 56.84           C  
ANISOU 4946  CD2 LEU J 675     8824   8350   4423  -1392   1852  -1585       C  
ATOM   4947  N   GLU J 676      -3.582 -39.780  57.354  1.00 62.74           N  
ANISOU 4947  N   GLU J 676     9519   8811   5507  -1537   1709  -1834       N  
ATOM   4948  CA  GLU J 676      -4.081 -39.726  55.982  1.00 63.09           C  
ANISOU 4948  CA  GLU J 676     9562   8822   5586  -1551   1686  -1882       C  
ATOM   4949  C   GLU J 676      -2.998 -39.245  55.025  1.00 69.84           C  
ANISOU 4949  C   GLU J 676    10452   9619   6464  -1531   1634  -1832       C  
ATOM   4950  O   GLU J 676      -2.889 -39.744  53.901  1.00 79.13           O  
ANISOU 4950  O   GLU J 676    11632  10802   7633  -1534   1601  -1826       O  
ATOM   4951  CB  GLU J 676      -5.314 -38.825  55.901  1.00 63.23           C  
ANISOU 4951  CB  GLU J 676     9577   8784   5663  -1574   1749  -1980       C  
ATOM   4952  CG  GLU J 676      -5.839 -38.584  54.490  1.00 64.54           C  
ANISOU 4952  CG  GLU J 676     9773   8879   5869  -1585   1754  -2033       C  
ATOM   4953  CD  GLU J 676      -6.851 -39.623  54.053  1.00 78.35           C  
ANISOU 4953  CD  GLU J 676    11527  10654   7590  -1637   1782  -2093       C  
ATOM   4954  OE1 GLU J 676      -7.921 -39.717  54.687  1.00 85.00           O  
ANISOU 4954  OE1 GLU J 676    12367  11502   8427  -1652   1855  -2158       O  
ATOM   4955  OE2 GLU J 676      -6.574 -40.347  53.071  1.00 81.60           O  
ANISOU 4955  OE2 GLU J 676    11945  11086   7973  -1676   1739  -2079       O  
ATOM   4956  N   LEU J 677      -2.173 -38.290  55.461  1.00 62.15           N  
ANISOU 4956  N   LEU J 677     9509   8596   5510  -1527   1630  -1798       N  
ATOM   4957  CA  LEU J 677      -1.058 -37.844  54.629  1.00 59.51           C  
ANISOU 4957  CA  LEU J 677     9221   8204   5185  -1513   1585  -1748       C  
ATOM   4958  C   LEU J 677      -0.003 -38.936  54.495  1.00 59.66           C  
ANISOU 4958  C   LEU J 677     9262   8261   5144  -1460   1564  -1659       C  
ATOM   4959  O   LEU J 677       0.616 -39.088  53.431  1.00 59.17           O  
ANISOU 4959  O   LEU J 677     9220   8184   5078  -1437   1531  -1626       O  
ATOM   4960  CB  LEU J 677      -0.458 -36.567  55.214  1.00 48.81           C  
ANISOU 4960  CB  LEU J 677     7903   6801   3843  -1553   1593  -1743       C  
ATOM   4961  CG  LEU J 677      -1.327 -35.319  55.048  1.00 44.94           C  
ANISOU 4961  CG  LEU J 677     7389   6302   3386  -1590   1615  -1823       C  
ATOM   4962  CD1 LEU J 677      -0.881 -34.209  55.988  1.00 45.38           C  
ANISOU 4962  CD1 LEU J 677     7454   6373   3415  -1667   1633  -1829       C  
ATOM   4963  CD2 LEU J 677      -1.309 -34.839  53.601  1.00 58.25           C  
ANISOU 4963  CD2 LEU J 677     9102   7934   5096  -1569   1582  -1833       C  
ATOM   4964  N   GLN J 678       0.194 -39.723  55.559  1.00 62.35           N  
ANISOU 4964  N   GLN J 678     9601   8662   5427  -1432   1595  -1618       N  
ATOM   4965  CA  GLN J 678       1.071 -40.891  55.481  1.00 67.34           C  
ANISOU 4965  CA  GLN J 678    10248   9364   5974  -1352   1598  -1529       C  
ATOM   4966  C   GLN J 678       0.552 -41.903  54.466  1.00 74.00           C  
ANISOU 4966  C   GLN J 678    11028  10313   6774  -1349   1566  -1541       C  
ATOM   4967  O   GLN J 678       1.327 -42.450  53.668  1.00 80.94           O  
ANISOU 4967  O   GLN J 678    11912  11237   7604  -1301   1552  -1481       O  
ATOM   4968  CB  GLN J 678       1.198 -41.530  56.864  1.00 67.36           C  
ANISOU 4968  CB  GLN J 678    10265   9422   5908  -1314   1652  -1483       C  
ATOM   4969  CG  GLN J 678       1.796 -42.925  56.866  1.00 67.82           C  
ANISOU 4969  CG  GLN J 678    10317   9606   5846  -1205   1673  -1384       C  
ATOM   4970  CD  GLN J 678       2.095 -43.421  58.267  1.00 70.67           C  
ANISOU 4970  CD  GLN J 678    10716  10001   6133  -1147   1745  -1318       C  
ATOM   4971  OE1 GLN J 678       3.118 -44.062  58.507  1.00 74.15           O  
ANISOU 4971  OE1 GLN J 678    11205  10479   6488  -1035   1798  -1206       O  
ATOM   4972  NE2 GLN J 678       1.194 -43.133  59.199  1.00 67.83           N  
ANISOU 4972  NE2 GLN J 678    10339   9632   5802  -1215   1763  -1381       N  
ATOM   4973  N   LYS J 679      -0.760 -42.147  54.470  1.00 75.27           N  
ANISOU 4973  N   LYS J 679    11135  10518   6944  -1414   1566  -1623       N  
ATOM   4974  CA  LYS J 679      -1.351 -43.084  53.520  1.00 75.46           C  
ANISOU 4974  CA  LYS J 679    11109  10642   6920  -1462   1544  -1654       C  
ATOM   4975  C   LYS J 679      -1.274 -42.551  52.094  1.00 70.69           C  
ANISOU 4975  C   LYS J 679    10522   9962   6375  -1503   1517  -1686       C  
ATOM   4976  O   LYS J 679      -1.055 -43.324  51.153  1.00 78.18           O  
ANISOU 4976  O   LYS J 679    11444  10996   7266  -1529   1497  -1669       O  
ATOM   4977  CB  LYS J 679      -2.800 -43.377  53.906  1.00 83.71           C  
ANISOU 4977  CB  LYS J 679    12120  11724   7963  -1541   1568  -1747       C  
ATOM   4978  CG  LYS J 679      -3.353 -44.653  53.293  1.00 89.61           C  
ANISOU 4978  CG  LYS J 679    12816  12620   8614  -1620   1554  -1773       C  
ATOM   4979  CD  LYS J 679      -2.394 -45.815  53.506  1.00 93.14           C  
ANISOU 4979  CD  LYS J 679    13225  13241   8923  -1547   1536  -1660       C  
ATOM   4980  CE  LYS J 679      -3.032 -47.141  53.134  1.00 94.63           C  
ANISOU 4980  CE  LYS J 679    13340  13631   8984  -1650   1520  -1686       C  
ATOM   4981  NZ  LYS J 679      -2.127 -48.284  53.438  1.00 92.85           N  
ANISOU 4981  NZ  LYS J 679    13067  13611   8601  -1554   1514  -1552       N  
ATOM   4982  N   ASP J 680      -1.450 -41.236  51.922  1.00 65.16           N  
ANISOU 4982  N   ASP J 680     9862   9119   5776  -1514   1522  -1727       N  
ATOM   4983  CA  ASP J 680      -1.268 -40.601  50.618  1.00 59.51           C  
ANISOU 4983  CA  ASP J 680     9180   8320   5111  -1536   1504  -1743       C  
ATOM   4984  C   ASP J 680       0.141 -40.832  50.089  1.00 60.27           C  
ANISOU 4984  C   ASP J 680     9299   8434   5169  -1481   1475  -1651       C  
ATOM   4985  O   ASP J 680       0.325 -41.262  48.941  1.00 55.50           O  
ANISOU 4985  O   ASP J 680     8688   7860   4540  -1508   1462  -1646       O  
ATOM   4986  CB  ASP J 680      -1.548 -39.098  50.720  1.00 55.34           C  
ANISOU 4986  CB  ASP J 680     8694   7665   4668  -1533   1520  -1782       C  
ATOM   4987  CG  ASP J 680      -3.011 -38.782  50.965  1.00 58.74           C  
ANISOU 4987  CG  ASP J 680     9116   8068   5134  -1571   1574  -1879       C  
ATOM   4988  OD1 ASP J 680      -3.806 -39.727  51.151  1.00 62.37           O  
ANISOU 4988  OD1 ASP J 680     9546   8593   5561  -1612   1597  -1918       O  
ATOM   4989  OD2 ASP J 680      -3.363 -37.582  50.981  1.00 56.16           O  
ANISOU 4989  OD2 ASP J 680     8818   7663   4857  -1558   1604  -1916       O  
ATOM   4990  N   VAL J 681       1.147 -40.574  50.932  1.00 59.24           N  
ANISOU 4990  N   VAL J 681     9203   8282   5024  -1410   1481  -1581       N  
ATOM   4991  CA  VAL J 681       2.541 -40.727  50.525  1.00 59.01           C  
ANISOU 4991  CA  VAL J 681     9218   8248   4954  -1342   1479  -1492       C  
ATOM   4992  C   VAL J 681       2.852 -42.184  50.199  1.00 64.87           C  
ANISOU 4992  C   VAL J 681     9910   9150   5586  -1295   1489  -1433       C  
ATOM   4993  O   VAL J 681       3.497 -42.484  49.186  1.00 73.58           O  
ANISOU 4993  O   VAL J 681    11016  10286   6654  -1274   1486  -1392       O  
ATOM   4994  CB  VAL J 681       3.470 -40.166  51.621  1.00 43.56           C  
ANISOU 4994  CB  VAL J 681     7333   6218   2999  -1297   1507  -1440       C  
ATOM   4995  CG1 VAL J 681       4.887 -40.706  51.481  1.00 43.72           C  
ANISOU 4995  CG1 VAL J 681     7409   6252   2950  -1201   1542  -1336       C  
ATOM   4996  CG2 VAL J 681       3.470 -38.644  51.580  1.00 43.16           C  
ANISOU 4996  CG2 VAL J 681     7333   6039   3028  -1359   1489  -1484       C  
ATOM   4997  N   ARG J 682       2.351 -43.116  51.014  1.00 57.33           N  
ANISOU 4997  N   ARG J 682     8904   8319   4562  -1283   1506  -1426       N  
ATOM   4998  CA  ARG J 682       2.681 -44.524  50.807  1.00 68.35           C  
ANISOU 4998  CA  ARG J 682    10240   9910   5819  -1229   1520  -1349       C  
ATOM   4999  C   ARG J 682       1.993 -45.092  49.567  1.00 74.73           C  
ANISOU 4999  C   ARG J 682    10977  10818   6600  -1348   1486  -1408       C  
ATOM   5000  O   ARG J 682       2.601 -45.863  48.811  1.00 80.62           O  
ANISOU 5000  O   ARG J 682    11682  11699   7252  -1323   1491  -1340       O  
ATOM   5001  CB  ARG J 682       2.323 -45.328  52.056  1.00 77.27           C  
ANISOU 5001  CB  ARG J 682    11339  11154   6866  -1186   1548  -1317       C  
ATOM   5002  CG  ARG J 682       3.355 -45.182  53.167  1.00 83.99           C  
ANISOU 5002  CG  ARG J 682    12264  11956   7692  -1049   1610  -1217       C  
ATOM   5003  CD  ARG J 682       2.949 -45.897  54.445  1.00 90.54           C  
ANISOU 5003  CD  ARG J 682    13074  12885   8442  -1006   1648  -1183       C  
ATOM   5004  NE  ARG J 682       4.045 -45.913  55.410  1.00 93.06           N  
ANISOU 5004  NE  ARG J 682    13472  13169   8716   -870   1730  -1070       N  
ATOM   5005  CZ  ARG J 682       3.986 -46.487  56.609  1.00 92.87           C  
ANISOU 5005  CZ  ARG J 682    13456  13216   8614   -801   1789  -1008       C  
ATOM   5006  NH1 ARG J 682       2.878 -47.099  57.003  1.00 94.44           N  
ANISOU 5006  NH1 ARG J 682    13587  13530   8765   -852   1765  -1050       N  
ATOM   5007  NH2 ARG J 682       5.039 -46.447  57.415  1.00 89.86           N  
ANISOU 5007  NH2 ARG J 682    13159  12783   8200   -693   1880   -907       N  
ATOM   5008  N   LYS J 683       0.734 -44.708  49.321  1.00 75.60           N  
ANISOU 5008  N   LYS J 683    11075  10865   6784  -1483   1467  -1531       N  
ATOM   5009  CA  LYS J 683       0.060 -45.164  48.111  1.00 75.68           C  
ANISOU 5009  CA  LYS J 683    11041  10941   6773  -1628   1452  -1601       C  
ATOM   5010  C   LYS J 683       0.674 -44.540  46.863  1.00 75.77           C  
ANISOU 5010  C   LYS J 683    11096  10858   6835  -1636   1447  -1593       C  
ATOM   5011  O   LYS J 683       0.754 -45.201  45.817  1.00 86.98           O  
ANISOU 5011  O   LYS J 683    12471  12389   8189  -1720   1443  -1595       O  
ATOM   5012  CB  LYS J 683      -1.435 -44.855  48.190  1.00 74.26           C  
ANISOU 5012  CB  LYS J 683    10870  10686   6659  -1755   1466  -1730       C  
ATOM   5013  CG  LYS J 683      -2.324 -45.962  47.634  1.00 74.05           C  
ANISOU 5013  CG  LYS J 683    10778  10815   6541  -1926   1468  -1801       C  
ATOM   5014  CD  LYS J 683      -2.063 -47.284  48.344  1.00 74.16           C  
ANISOU 5014  CD  LYS J 683    10699  11079   6399  -1905   1448  -1731       C  
ATOM   5015  CE  LYS J 683      -3.215 -48.262  48.159  1.00 76.63           C  
ANISOU 5015  CE  LYS J 683    10948  11548   6621  -2104   1449  -1824       C  
ATOM   5016  NZ  LYS J 683      -3.568 -48.457  46.725  1.00 77.45           N  
ANISOU 5016  NZ  LYS J 683    11040  11675   6713  -2297   1453  -1900       N  
ATOM   5017  N   ALA J 684       1.136 -43.287  46.961  1.00 65.34           N  
ANISOU 5017  N   ALA J 684     9857   9352   5618  -1563   1447  -1582       N  
ATOM   5018  CA  ALA J 684       1.870 -42.686  45.854  1.00 59.35           C  
ANISOU 5018  CA  ALA J 684     9150   8508   4893  -1554   1443  -1557       C  
ATOM   5019  C   ALA J 684       3.180 -43.419  45.600  1.00 60.24           C  
ANISOU 5019  C   ALA J 684     9243   8739   4905  -1460   1454  -1444       C  
ATOM   5020  O   ALA J 684       3.592 -43.589  44.446  1.00 69.63           O  
ANISOU 5020  O   ALA J 684    10429   9961   6066  -1492   1459  -1426       O  
ATOM   5021  CB  ALA J 684       2.125 -41.206  46.136  1.00 43.90           C  
ANISOU 5021  CB  ALA J 684     7278   6360   3042  -1503   1438  -1561       C  
ATOM   5022  N   GLU J 685       3.838 -43.882  46.670  1.00 55.83           N  
ANISOU 5022  N   GLU J 685     8679   8251   4283  -1335   1476  -1358       N  
ATOM   5023  CA  GLU J 685       5.069 -44.657  46.519  1.00 57.32           C  
ANISOU 5023  CA  GLU J 685     8855   8564   4359  -1205   1519  -1226       C  
ATOM   5024  C   GLU J 685       4.812 -45.983  45.814  1.00 64.99           C  
ANISOU 5024  C   GLU J 685     9709   9784   5202  -1262   1520  -1199       C  
ATOM   5025  O   GLU J 685       5.593 -46.396  44.947  1.00 55.87           O  
ANISOU 5025  O   GLU J 685     8528   8724   3976  -1221   1548  -1121       O  
ATOM   5026  CB  GLU J 685       5.705 -44.900  47.888  1.00 67.33           C  
ANISOU 5026  CB  GLU J 685    10155   9849   5579  -1054   1567  -1134       C  
ATOM   5027  CG  GLU J 685       6.431 -43.703  48.466  1.00 82.29           C  
ANISOU 5027  CG  GLU J 685    12169  11529   7566  -1006   1584  -1131       C  
ATOM   5028  CD  GLU J 685       6.792 -43.895  49.925  1.00 90.84           C  
ANISOU 5028  CD  GLU J 685    13290  12609   8615   -913   1638  -1072       C  
ATOM   5029  OE1 GLU J 685       6.303 -44.868  50.536  1.00 91.93           O  
ANISOU 5029  OE1 GLU J 685    13359  12902   8666   -878   1653  -1042       O  
ATOM   5030  OE2 GLU J 685       7.564 -43.071  50.460  1.00 94.45           O  
ANISOU 5030  OE2 GLU J 685    13855  12907   9124   -891   1670  -1058       O  
ATOM   5031  N   GLU J 686       3.720 -46.665  46.174  1.00 65.86           N  
ANISOU 5031  N   GLU J 686     9739  10015   5270  -1372   1492  -1262       N  
ATOM   5032  CA  GLU J 686       3.392 -47.932  45.520  1.00 78.23           C  
ANISOU 5032  CA  GLU J 686    11172  11849   6702  -1481   1480  -1250       C  
ATOM   5033  C   GLU J 686       3.047 -47.728  44.046  1.00 83.27           C  
ANISOU 5033  C   GLU J 686    11794  12472   7374  -1662   1460  -1338       C  
ATOM   5034  O   GLU J 686       3.487 -48.506  43.184  1.00 88.40           O  
ANISOU 5034  O   GLU J 686    12351  13323   7916  -1704   1466  -1279       O  
ATOM   5035  CB  GLU J 686       2.242 -48.619  46.257  1.00 85.54           C  
ANISOU 5035  CB  GLU J 686    12027  12896   7577  -1589   1452  -1317       C  
ATOM   5036  CG  GLU J 686       2.544 -48.906  47.720  1.00 88.84           C  
ANISOU 5036  CG  GLU J 686    12464  13343   7947  -1418   1482  -1224       C  
ATOM   5037  CD  GLU J 686       1.685 -50.011  48.297  1.00 90.46           C  
ANISOU 5037  CD  GLU J 686    12565  13772   8035  -1508   1459  -1239       C  
ATOM   5038  OE1 GLU J 686       0.830 -50.550  47.564  1.00 91.79           O  
ANISOU 5038  OE1 GLU J 686    12640  14079   8158  -1724   1416  -1333       O  
ATOM   5039  OE2 GLU J 686       1.864 -50.339  49.490  1.00 89.81           O  
ANISOU 5039  OE2 GLU J 686    12499  13727   7898  -1374   1490  -1157       O  
ATOM   5040  N   GLU J 687       2.277 -46.676  43.740  1.00 76.89           N  
ANISOU 5040  N   GLU J 687    11075  11432   6708  -1762   1448  -1466       N  
ATOM   5041  CA  GLU J 687       1.954 -46.361  42.349  1.00 90.52           C  
ANISOU 5041  CA  GLU J 687    12822  13097   8473  -1921   1453  -1543       C  
ATOM   5042  C   GLU J 687       3.210 -46.024  41.549  1.00 90.11           C  
ANISOU 5042  C   GLU J 687    12806  13015   8417  -1822   1472  -1452       C  
ATOM   5043  O   GLU J 687       3.361 -46.456  40.395  1.00 95.66           O  
ANISOU 5043  O   GLU J 687    13461  13826   9060  -1932   1484  -1453       O  
ATOM   5044  CB  GLU J 687       0.960 -45.200  42.308  1.00 93.44           C  
ANISOU 5044  CB  GLU J 687    13303  13207   8996  -1987   1462  -1661       C  
ATOM   5045  CG  GLU J 687      -0.159 -45.348  41.294  1.00100.95           C  
ANISOU 5045  CG  GLU J 687    14265  14137   9955  -2217   1491  -1784       C  
ATOM   5046  CD  GLU J 687      -1.300 -44.385  41.558  1.00104.51           C  
ANISOU 5046  CD  GLU J 687    14820  14359  10532  -2241   1526  -1880       C  
ATOM   5047  OE1 GLU J 687      -1.110 -43.448  42.363  1.00101.77           O  
ANISOU 5047  OE1 GLU J 687    14524  13875  10271  -2085   1515  -1848       O  
ATOM   5048  OE2 GLU J 687      -2.386 -44.566  40.968  1.00107.35           O  
ANISOU 5048  OE2 GLU J 687    15213  14682  10894  -2419   1577  -1985       O  
ATOM   5049  N   LEU J 688       4.133 -45.274  42.160  1.00 86.88           N  
ANISOU 5049  N   LEU J 688    12482  12467   8063  -1627   1484  -1374       N  
ATOM   5050  CA  LEU J 688       5.374 -44.904  41.489  1.00 70.28           C  
ANISOU 5050  CA  LEU J 688    10432  10317   5955  -1521   1514  -1285       C  
ATOM   5051  C   LEU J 688       6.251 -46.125  41.242  1.00 58.38           C  
ANISOU 5051  C   LEU J 688     8822   9069   4291  -1436   1557  -1150       C  
ATOM   5052  O   LEU J 688       6.901 -46.224  40.194  1.00 60.73           O  
ANISOU 5052  O   LEU J 688     9109   9417   4550  -1438   1589  -1099       O  
ATOM   5053  CB  LEU J 688       6.108 -43.852  42.326  1.00 45.62           C  
ANISOU 5053  CB  LEU J 688     7425   6994   2915  -1364   1521  -1243       C  
ATOM   5054  CG  LEU J 688       7.288 -43.041  41.773  1.00 45.07           C  
ANISOU 5054  CG  LEU J 688     7456   6792   2878  -1274   1548  -1183       C  
ATOM   5055  CD1 LEU J 688       8.626 -43.761  41.893  1.00 45.72           C  
ANISOU 5055  CD1 LEU J 688     7525   6996   2852  -1099   1620  -1034       C  
ATOM   5056  CD2 LEU J 688       7.019 -42.648  40.331  1.00 60.90           C  
ANISOU 5056  CD2 LEU J 688     9482   8742   4915  -1400   1540  -1238       C  
ATOM   5057  N   GLY J 689       6.284 -47.063  42.192  1.00 61.68           N  
ANISOU 5057  N   GLY J 689     9160   9664   4610  -1352   1569  -1074       N  
ATOM   5058  CA  GLY J 689       7.039 -48.289  41.983  1.00 61.72           C  
ANISOU 5058  CA  GLY J 689     9048   9950   4454  -1256   1621   -916       C  
ATOM   5059  C   GLY J 689       6.475 -49.140  40.861  1.00 64.50           C  
ANISOU 5059  C   GLY J 689     9240  10549   4718  -1477   1586   -957       C  
ATOM   5060  O   GLY J 689       7.231 -49.704  40.059  1.00 63.33           O  
ANISOU 5060  O   GLY J 689     9004  10578   4479  -1442   1628   -843       O  
ATOM   5061  N   GLU J 690       5.141 -49.231  40.779  1.00 67.77           N  
ANISOU 5061  N   GLU J 690     9613  10981   5157  -1719   1519  -1118       N  
ATOM   5062  CA  GLU J 690       4.505 -49.940  39.667  1.00 77.65           C  
ANISOU 5062  CA  GLU J 690    10727  12447   6327  -1989   1488  -1191       C  
ATOM   5063  C   GLU J 690       4.857 -49.301  38.326  1.00 73.76           C  
ANISOU 5063  C   GLU J 690    10300  11835   5891  -2063   1517  -1223       C  
ATOM   5064  O   GLU J 690       5.206 -49.999  37.359  1.00 79.61           O  
ANISOU 5064  O   GLU J 690    10910  12812   6526  -2159   1528  -1169       O  
ATOM   5065  CB  GLU J 690       2.989 -49.963  39.864  1.00 90.15           C  
ANISOU 5065  CB  GLU J 690    12315  13990   7947  -2231   1442  -1373       C  
ATOM   5066  CG  GLU J 690       2.522 -50.803  41.038  1.00103.95           C  
ANISOU 5066  CG  GLU J 690    13970  15919   9608  -2210   1409  -1350       C  
ATOM   5067  CD  GLU J 690       1.014 -50.790  41.199  1.00114.94           C  
ANISOU 5067  CD  GLU J 690    15386  17248  11038  -2448   1386  -1532       C  
ATOM   5068  OE1 GLU J 690       0.335 -50.109  40.400  1.00118.13           O  
ANISOU 5068  OE1 GLU J 690    15891  17450  11542  -2614   1410  -1666       O  
ATOM   5069  OE2 GLU J 690       0.508 -51.458  42.125  1.00117.41           O  
ANISOU 5069  OE2 GLU J 690    15629  17702  11279  -2460   1359  -1530       O  
ATOM   5070  N   LEU J 691       4.785 -47.966  38.257  1.00 67.12           N  
ANISOU 5070  N   LEU J 691     9648  10645   5210  -2021   1529  -1298       N  
ATOM   5071  CA  LEU J 691       5.105 -47.264  37.015  1.00 65.84           C  
ANISOU 5071  CA  LEU J 691     9570  10343   5103  -2081   1561  -1324       C  
ATOM   5072  C   LEU J 691       6.571 -47.437  36.631  1.00 72.21           C  
ANISOU 5072  C   LEU J 691    10351  11241   5845  -1891   1613  -1155       C  
ATOM   5073  O   LEU J 691       6.888 -47.610  35.446  1.00 73.14           O  
ANISOU 5073  O   LEU J 691    10428  11442   5918  -1984   1644  -1136       O  
ATOM   5074  CB  LEU J 691       4.759 -45.782  37.146  1.00 49.70           C  
ANISOU 5074  CB  LEU J 691     7718   7933   3234  -2046   1558  -1410       C  
ATOM   5075  CG  LEU J 691       3.324 -45.371  36.818  1.00 63.11           C  
ANISOU 5075  CG  LEU J 691     9480   9486   5013  -2258   1557  -1573       C  
ATOM   5076  CD1 LEU J 691       3.190 -43.856  36.828  1.00 62.09           C  
ANISOU 5076  CD1 LEU J 691     9522   9030   5038  -2176   1566  -1606       C  
ATOM   5077  CD2 LEU J 691       2.895 -45.944  35.477  1.00 51.60           C  
ANISOU 5077  CD2 LEU J 691     7980   8140   3484  -2516   1590  -1640       C  
ATOM   5078  N   GLU J 692       7.476 -47.402  37.616  1.00 72.01           N  
ANISOU 5078  N   GLU J 692    10357  11192   5810  -1626   1642  -1026       N  
ATOM   5079  CA  GLU J 692       8.895 -47.593  37.333  1.00 74.11           C  
ANISOU 5079  CA  GLU J 692    10620  11524   6013  -1414   1725   -849       C  
ATOM   5080  C   GLU J 692       9.182 -49.000  36.830  1.00 76.58           C  
ANISOU 5080  C   GLU J 692    10718  12216   6163  -1437   1758   -722       C  
ATOM   5081  O   GLU J 692       9.995 -49.179  35.915  1.00 73.57           O  
ANISOU 5081  O   GLU J 692    10296  11922   5737  -1389   1823   -620       O  
ATOM   5082  CB  GLU J 692       9.733 -47.294  38.574  1.00 76.87           C  
ANISOU 5082  CB  GLU J 692    11071  11754   6381  -1138   1773   -744       C  
ATOM   5083  CG  GLU J 692      10.087 -45.832  38.738  1.00 79.75           C  
ANISOU 5083  CG  GLU J 692    11627  11789   6888  -1084   1762   -807       C  
ATOM   5084  CD  GLU J 692      11.251 -45.626  39.685  1.00 84.18           C  
ANISOU 5084  CD  GLU J 692    12270  12275   7439   -834   1833   -685       C  
ATOM   5085  OE1 GLU J 692      11.575 -46.566  40.442  1.00 85.90           O  
ANISOU 5085  OE1 GLU J 692    12419  12666   7554   -683   1894   -561       O  
ATOM   5086  OE2 GLU J 692      11.854 -44.534  39.657  1.00 85.26           O  
ANISOU 5086  OE2 GLU J 692    12545  12185   7667   -802   1836   -711       O  
ATOM   5087  N   ALA J 693       8.520 -50.010  37.409  1.00 86.84           N  
ANISOU 5087  N   ALA J 693    11860  13763   7372  -1516   1709   -720       N  
ATOM   5088  CA  ALA J 693       8.700 -51.378  36.930  1.00 80.39           C  
ANISOU 5088  CA  ALA J 693    10786  13366   6393  -1573   1711   -597       C  
ATOM   5089  C   ALA J 693       8.214 -51.533  35.493  1.00 71.62           C  
ANISOU 5089  C   ALA J 693     9570  12390   5253  -1873   1674   -696       C  
ATOM   5090  O   ALA J 693       8.892 -52.160  34.664  1.00 73.26           O  
ANISOU 5090  O   ALA J 693     9619  12846   5371  -1863   1713   -565       O  
ATOM   5091  CB  ALA J 693       7.973 -52.358  37.852  1.00 81.79           C  
ANISOU 5091  CB  ALA J 693    10812  13791   6475  -1632   1643   -593       C  
ATOM   5092  N   LYS J 694       7.055 -50.944  35.172  1.00 72.25           N  
ANISOU 5092  N   LYS J 694     9745  12293   5413  -2138   1616   -920       N  
ATOM   5093  CA  LYS J 694       6.537 -51.051  33.809  1.00 74.60           C  
ANISOU 5093  CA  LYS J 694     9988  12675   5682  -2450   1607  -1029       C  
ATOM   5094  C   LYS J 694       7.431 -50.324  32.806  1.00 78.84           C  
ANISOU 5094  C   LYS J 694    10629  13050   6276  -2366   1683   -974       C  
ATOM   5095  O   LYS J 694       7.686 -50.838  31.707  1.00 81.20           O  
ANISOU 5095  O   LYS J 694    10794  13567   6492  -2504   1705   -932       O  
ATOM   5096  CB  LYS J 694       5.105 -50.522  33.744  1.00 76.13           C  
ANISOU 5096  CB  LYS J 694    10312  12652   5962  -2722   1571  -1268       C  
ATOM   5097  CG  LYS J 694       4.055 -51.618  33.852  1.00 81.44           C  
ANISOU 5097  CG  LYS J 694    10810  13622   6510  -3008   1510  -1358       C  
ATOM   5098  CD  LYS J 694       2.645 -51.071  33.728  1.00 85.12           C  
ANISOU 5098  CD  LYS J 694    11440  13829   7072  -3265   1518  -1586       C  
ATOM   5099  CE  LYS J 694       1.678 -51.843  34.613  1.00 86.82           C  
ANISOU 5099  CE  LYS J 694    11562  14208   7220  -3391   1464  -1654       C  
ATOM   5100  NZ  LYS J 694       0.344 -51.188  34.681  1.00 85.36           N  
ANISOU 5100  NZ  LYS J 694    11570  13707   7156  -3564   1505  -1849       N  
ATOM   5101  N   LEU J 695       7.948 -49.147  33.177  1.00 78.96           N  
ANISOU 5101  N   LEU J 695    10870  12706   6425  -2146   1721   -966       N  
ATOM   5102  CA  LEU J 695       8.821 -48.416  32.261  1.00 79.33           C  
ANISOU 5102  CA  LEU J 695    11027  12593   6520  -2062   1791   -912       C  
ATOM   5103  C   LEU J 695      10.161 -49.127  32.091  1.00 79.41           C  
ANISOU 5103  C   LEU J 695    10908  12834   6431  -1838   1873   -681       C  
ATOM   5104  O   LEU J 695      10.733 -49.125  30.993  1.00 76.57           O  
ANISOU 5104  O   LEU J 695    10518  12528   6047  -1864   1933   -621       O  
ATOM   5105  CB  LEU J 695       9.007 -46.976  32.755  1.00 71.05           C  
ANISOU 5105  CB  LEU J 695    10234  11135   5627  -1908   1793   -964       C  
ATOM   5106  CG  LEU J 695       9.434 -45.871  31.771  1.00 63.22           C  
ANISOU 5106  CG  LEU J 695     9411   9892   4719  -1911   1834   -987       C  
ATOM   5107  CD1 LEU J 695      10.902 -45.858  31.425  1.00 59.48           C  
ANISOU 5107  CD1 LEU J 695     8945   9450   4204  -1687   1920   -814       C  
ATOM   5108  CD2 LEU J 695       8.656 -46.033  30.495  1.00 62.44           C  
ANISOU 5108  CD2 LEU J 695     9285   9842   4599  -2213   1842  -1095       C  
ATOM   5109  N   ASN J 696      10.666 -49.762  33.154  1.00 76.42           N  
ANISOU 5109  N   ASN J 696    10455  12587   5993  -1609   1894   -538       N  
ATOM   5110  CA  ASN J 696      11.909 -50.520  33.037  1.00 85.52           C  
ANISOU 5110  CA  ASN J 696    11489  13952   7054  -1372   2003   -296       C  
ATOM   5111  C   ASN J 696      11.733 -51.737  32.136  1.00 94.67           C  
ANISOU 5111  C   ASN J 696    12336  15552   8083  -1560   1976   -228       C  
ATOM   5112  O   ASN J 696      12.632 -52.067  31.353  1.00 95.24           O  
ANISOU 5112  O   ASN J 696    12311  15764   8112  -1467   2063    -75       O  
ATOM   5113  CB  ASN J 696      12.402 -50.938  34.421  1.00 89.33           C  
ANISOU 5113  CB  ASN J 696    11991  14446   7505  -1096   2052   -158       C  
ATOM   5114  CG  ASN J 696      13.619 -50.153  34.867  1.00 95.36           C  
ANISOU 5114  CG  ASN J 696    13002  14903   8328   -777   2192    -53       C  
ATOM   5115  OD1 ASN J 696      14.307 -49.537  34.052  1.00 92.88           O  
ANISOU 5115  OD1 ASN J 696    12785  14456   8050   -723   2260    -29       O  
ATOM   5116  ND2 ASN J 696      13.890 -50.169  36.167  1.00101.60           N  
ANISOU 5116  ND2 ASN J 696    13902  15583   9119   -575   2239      8       N  
ATOM   5117  N   GLU J 697      10.577 -52.406  32.222  1.00100.17           N  
ANISOU 5117  N   GLU J 697    12866  16483   8711  -1837   1855   -344       N  
ATOM   5118  CA  GLU J 697      10.310 -53.520  31.312  1.00101.33           C  
ANISOU 5118  CA  GLU J 697    12700  17080   8718  -2079   1805   -307       C  
ATOM   5119  C   GLU J 697      10.201 -53.042  29.868  1.00 98.17           C  
ANISOU 5119  C   GLU J 697    12345  16606   8348  -2314   1831   -407       C  
ATOM   5120  O   GLU J 697      10.703 -53.704  28.946  1.00 99.44           O  
ANISOU 5120  O   GLU J 697    12293  17068   8422  -2367   1859   -285       O  
ATOM   5121  CB  GLU J 697       9.036 -54.253  31.730  1.00104.73           C  
ANISOU 5121  CB  GLU J 697    12982  17751   9060  -2366   1674   -440       C  
ATOM   5122  CG  GLU J 697       9.286 -55.629  32.324  1.00110.76           C  
ANISOU 5122  CG  GLU J 697    13429  18990   9666  -2267   1627   -245       C  
ATOM   5123  CD  GLU J 697       8.032 -56.477  32.376  1.00117.50           C  
ANISOU 5123  CD  GLU J 697    14085  20170  10389  -2635   1490   -381       C  
ATOM   5124  OE1 GLU J 697       7.152 -56.292  31.509  1.00119.36           O  
ANISOU 5124  OE1 GLU J 697    14353  20380  10618  -3018   1453   -592       O  
ATOM   5125  OE2 GLU J 697       7.925 -57.328  33.285  1.00120.52           O1-
ANISOU 5125  OE2 GLU J 697    14297  20823  10673  -2550   1431   -280       O1-
ATOM   5126  N   ASN J 698       9.562 -51.885  29.654  1.00100.91           N  
ANISOU 5126  N   ASN J 698    12967  16553   8820  -2447   1827   -615       N  
ATOM   5127  CA  ASN J 698       9.468 -51.328  28.305  1.00 96.67           C  
ANISOU 5127  CA  ASN J 698    12519  15891   8321  -2653   1870   -706       C  
ATOM   5128  C   ASN J 698      10.842 -50.976  27.744  1.00 86.82           C  
ANISOU 5128  C   ASN J 698    11310  14574   7102  -2391   1983   -525       C  
ATOM   5129  O   ASN J 698      11.111 -51.202  26.561  1.00 79.87           O  
ANISOU 5129  O   ASN J 698    10334  13834   6179  -2524   2027   -488       O  
ATOM   5130  CB  ASN J 698       8.558 -50.099  28.301  1.00101.75           C  
ANISOU 5130  CB  ASN J 698    13464  16092   9104  -2789   1857   -934       C  
ATOM   5131  CG  ASN J 698       7.090 -50.462  28.399  1.00107.67           C  
ANISOU 5131  CG  ASN J 698    14190  16897   9822  -3134   1786  -1137       C  
ATOM   5132  OD1 ASN J 698       6.608 -51.345  27.690  1.00109.54           O  
ANISOU 5132  OD1 ASN J 698    14248  17437   9936  -3442   1765  -1184       O  
ATOM   5133  ND2 ASN J 698       6.369 -49.776  29.279  1.00110.68           N  
ANISOU 5133  ND2 ASN J 698    14754  16988  10313  -3093   1756  -1258       N  
ATOM   5134  N   LEU J 699      11.738 -50.454  28.583  1.00 79.72           N  
ANISOU 5134  N   LEU J 699    10557  13465   6269  -2027   2042   -411       N  
ATOM   5135  CA  LEU J 699      13.071 -50.113  28.093  1.00 88.78           C  
ANISOU 5135  CA  LEU J 699    11772  14524   7437  -1773   2172   -243       C  
ATOM   5136  C   LEU J 699      13.912 -51.358  27.831  1.00 99.63           C  
ANISOU 5136  C   LEU J 699    12859  16302   8694  -1645   2242     -5       C  
ATOM   5137  O   LEU J 699      14.698 -51.389  26.873  1.00104.33           O  
ANISOU 5137  O   LEU J 699    13412  16952   9278  -1592   2339    106       O  
ATOM   5138  CB  LEU J 699      13.774 -49.191  29.081  1.00 71.86           C  
ANISOU 5138  CB  LEU J 699     9888  12034   5382  -1453   2226   -206       C  
ATOM   5139  CG  LEU J 699      13.158 -47.802  29.217  1.00 60.79           C  
ANISOU 5139  CG  LEU J 699     8751  10232   4112  -1545   2157   -408       C  
ATOM   5140  CD1 LEU J 699      14.143 -46.910  29.903  1.00 55.37           C  
ANISOU 5140  CD1 LEU J 699     8273   9273   3493  -1246   2212   -340       C  
ATOM   5141  CD2 LEU J 699      12.765 -47.218  27.864  1.00 56.96           C  
ANISOU 5141  CD2 LEU J 699     8336   9639   3667  -1791   2154   -521       C  
ATOM   5142  N   ARG J 700      13.771 -52.389  28.674  1.00105.72           N  
ANISOU 5142  N   ARG J 700    13425  17364   9382  -1583   2194     86       N  
ATOM   5143  CA  ARG J 700      14.471 -53.646  28.420  1.00113.90           C  
ANISOU 5143  CA  ARG J 700    14137  18835  10306  -1473   2235    323       C  
ATOM   5144  C   ARG J 700      13.997 -54.299  27.130  1.00116.25           C  
ANISOU 5144  C   ARG J 700    14159  19498  10514  -1811   2168    293       C  
ATOM   5145  O   ARG J 700      14.795 -54.923  26.422  1.00116.63           O  
ANISOU 5145  O   ARG J 700    13993  19812  10508  -1724   2236    483       O  
ATOM   5146  CB  ARG J 700      14.289 -54.608  29.594  1.00119.14           C  
ANISOU 5146  CB  ARG J 700    14621  19757  10889  -1362   2172    422       C  
ATOM   5147  CG  ARG J 700      15.063 -54.231  30.843  1.00122.15           C  
ANISOU 5147  CG  ARG J 700    15235  19841  11337   -990   2281    519       C  
ATOM   5148  CD  ARG J 700      14.816 -55.229  31.960  1.00126.46           C  
ANISOU 5148  CD  ARG J 700    15594  20657  11798   -898   2216    620       C  
ATOM   5149  NE  ARG J 700      15.252 -54.720  33.256  1.00127.87           N  
ANISOU 5149  NE  ARG J 700    16052  20484  12048   -634   2305    640       N  
ATOM   5150  CZ  ARG J 700      15.184 -55.410  34.391  1.00129.56           C  
ANISOU 5150  CZ  ARG J 700    16183  20833  12211   -501   2283    735       C  
ATOM   5151  NH1 ARG J 700      14.694 -56.643  34.390  1.00132.20           N  
ANISOU 5151  NH1 ARG J 700    16147  21668  12414   -591   2163    829       N  
ATOM   5152  NH2 ARG J 700      15.604 -54.868  35.525  1.00127.48           N  
ANISOU 5152  NH2 ARG J 700    16204  20216  12015   -299   2378    735       N  
ATOM   5153  N   ARG J 701      12.711 -54.163  26.803  1.00117.74           N  
ANISOU 5153  N   ARG J 701    14361  19690  10686  -2207   2048     54       N  
ATOM   5154  CA  ARG J 701      12.233 -54.662  25.520  1.00122.88           C  
ANISOU 5154  CA  ARG J 701    14812  20627  11251  -2581   2005     -9       C  
ATOM   5155  C   ARG J 701      12.517 -53.708  24.365  1.00120.16           C  
ANISOU 5155  C   ARG J 701    14674  19984  10998  -2653   2102    -77       C  
ATOM   5156  O   ARG J 701      12.419 -54.122  23.206  1.00125.79           O  
ANISOU 5156  O   ARG J 701    15224  20925  11645  -2909   2104    -81       O  
ATOM   5157  CB  ARG J 701      10.734 -54.963  25.598  1.00128.90           C  
ANISOU 5157  CB  ARG J 701    15534  21497  11943  -3009   1866   -251       C  
ATOM   5158  CG  ARG J 701      10.407 -56.113  26.538  1.00135.17           C  
ANISOU 5158  CG  ARG J 701    16056  22698  12605  -3002   1755   -173       C  
ATOM   5159  CD  ARG J 701       8.946 -56.524  26.465  1.00139.56           C  
ANISOU 5159  CD  ARG J 701    16557  23407  13063  -3474   1631   -415       C  
ATOM   5160  NE  ARG J 701       8.576 -57.365  27.601  1.00144.85           N  
ANISOU 5160  NE  ARG J 701    17050  24355  13632  -3426   1528   -366       N  
ATOM   5161  CZ  ARG J 701       7.354 -57.835  27.820  1.00147.77           C  
ANISOU 5161  CZ  ARG J 701    17361  24880  13902  -3788   1422   -554       C  
ATOM   5162  NH1 ARG J 701       6.370 -57.552  26.977  1.00148.56           N  
ANISOU 5162  NH1 ARG J 701    17585  24866  13994  -4233   1418   -811       N  
ATOM   5163  NH2 ARG J 701       7.114 -58.593  28.882  1.00148.76           N  
ANISOU 5163  NH2 ARG J 701    17324  25262  13937  -3709   1334   -484       N  
ATOM   5164  N   ASN J 702      12.861 -52.447  24.646  1.00112.31           N  
ANISOU 5164  N   ASN J 702    14027  18500  10144  -2449   2176   -128       N  
ATOM   5165  CA  ASN J 702      13.247 -51.532  23.577  1.00110.82           C  
ANISOU 5165  CA  ASN J 702    14031  18041  10034  -2478   2269   -161       C  
ATOM   5166  C   ASN J 702      14.714 -51.674  23.188  1.00105.70           C  
ANISOU 5166  C   ASN J 702    13318  17460   9382  -2160   2411     88       C  
ATOM   5167  O   ASN J 702      15.058 -51.470  22.018  1.00102.40           O  
ANISOU 5167  O   ASN J 702    12902  17033   8971  -2248   2483    112       O  
ATOM   5168  CB  ASN J 702      12.953 -50.086  23.979  1.00115.34           C  
ANISOU 5168  CB  ASN J 702    14988  18090  10745  -2418   2270   -322       C  
ATOM   5169  CG  ASN J 702      11.516 -49.682  23.697  1.00121.41           C  
ANISOU 5169  CG  ASN J 702    15880  18704  11545  -2795   2190   -585       C  
ATOM   5170  OD1 ASN J 702      11.243 -48.948  22.747  1.00122.81           O  
ANISOU 5170  OD1 ASN J 702    16231  18656  11777  -2966   2232   -690       O  
ATOM   5171  ND2 ASN J 702      10.593 -50.153  24.524  1.00124.56           N  
ANISOU 5171  ND2 ASN J 702    16211  19207  11910  -2918   2092   -688       N  
ATOM   5172  N   ILE J 703      15.592 -52.011  24.136  1.00107.52           N  
ANISOU 5172  N   ILE J 703    13517  17730   9604  -1792   2472    273       N  
ATOM   5173  CA  ILE J 703      16.996 -52.202  23.776  1.00105.30           C  
ANISOU 5173  CA  ILE J 703    13198  17491   9322  -1489   2639    507       C  
ATOM   5174  C   ILE J 703      17.198 -53.535  23.064  1.00116.28           C  
ANISOU 5174  C   ILE J 703    14169  19410  10603  -1574   2630    672       C  
ATOM   5175  O   ILE J 703      17.936 -53.618  22.075  1.00117.92           O  
ANISOU 5175  O   ILE J 703    14305  19691  10809  -1532   2738    787       O  
ATOM   5176  CB  ILE J 703      17.899 -52.070  25.016  1.00 90.63           C  
ANISOU 5176  CB  ILE J 703    11503  15437   7497  -1085   2742    634       C  
ATOM   5177  CG1 ILE J 703      17.721 -50.689  25.648  1.00 85.34           C  
ANISOU 5177  CG1 ILE J 703    11229  14274   6924  -1020   2736    474       C  
ATOM   5178  CG2 ILE J 703      19.364 -52.308  24.654  1.00 88.87           C  
ANISOU 5178  CG2 ILE J 703    11272  15221   7274   -797   2940    855       C  
ATOM   5179  CD1 ILE J 703      18.690 -50.398  26.766  1.00 84.21           C  
ANISOU 5179  CD1 ILE J 703    11314  13873   6808   -666   2868    573       C  
ATOM   5180  N   GLU J 704      16.527 -54.593  23.528  1.00121.28           N  
ANISOU 5180  N   GLU J 704    14506  20439  11134  -1708   2492    686       N  
ATOM   5181  CA  GLU J 704      16.637 -55.895  22.877  1.00131.94           C  
ANISOU 5181  CA  GLU J 704    15415  22358  12357  -1815   2446    846       C  
ATOM   5182  C   GLU J 704      15.971 -55.933  21.507  1.00131.25           C  
ANISOU 5182  C   GLU J 704    15224  22420  12224  -2253   2392    710       C  
ATOM   5183  O   GLU J 704      16.189 -56.893  20.759  1.00138.65           O  
ANISOU 5183  O   GLU J 704    15808  23814  13058  -2357   2370    845       O  
ATOM   5184  CB  GLU J 704      16.052 -56.986  23.775  1.00140.66           C  
ANISOU 5184  CB  GLU J 704    16234  23867  13341  -1859   2296    893       C  
ATOM   5185  CG  GLU J 704      16.989 -57.432  24.888  1.00145.70           C  
ANISOU 5185  CG  GLU J 704    16828  24544  13987  -1396   2370   1134       C  
ATOM   5186  CD  GLU J 704      18.104 -58.335  24.390  1.00153.76           C  
ANISOU 5186  CD  GLU J 704    17534  25935  14953  -1152   2456   1440       C  
ATOM   5187  OE1 GLU J 704      18.053 -59.552  24.666  1.00158.06           O  
ANISOU 5187  OE1 GLU J 704    17690  27000  15366  -1116   2358   1617       O  
ATOM   5188  OE2 GLU J 704      19.031 -57.829  23.724  1.00155.03           O1-
ANISOU 5188  OE2 GLU J 704    17830  25879  15196   -991   2620   1511       O1-
ATOM   5189  N   ARG J 705      15.168 -54.923  21.160  1.00123.31           N  
ANISOU 5189  N   ARG J 705    14518  21045  11291  -2514   2372    451       N  
ATOM   5190  CA  ARG J 705      14.650 -54.757  19.807  1.00116.70           C  
ANISOU 5190  CA  ARG J 705    13676  20229  10436  -2906   2367    316       C  
ATOM   5191  C   ARG J 705      15.558 -53.894  18.938  1.00109.79           C  
ANISOU 5191  C   ARG J 705    13002  19051   9661  -2746   2532    381       C  
ATOM   5192  O   ARG J 705      15.068 -53.164  18.066  1.00112.83           O  
ANISOU 5192  O   ARG J 705    13583  19194  10092  -3007   2551    214       O  
ATOM   5193  CB  ARG J 705      13.236 -54.174  19.851  1.00116.15           C  
ANISOU 5193  CB  ARG J 705    13834  19912  10387  -3286   2274      2       C  
ATOM   5194  CG  ARG J 705      12.152 -55.209  20.108  1.00120.97           C  
ANISOU 5194  CG  ARG J 705    14198  20916  10850  -3638   2118   -105       C  
ATOM   5195  CD  ARG J 705      10.793 -54.561  20.329  1.00123.74           C  
ANISOU 5195  CD  ARG J 705    14832  20946  11240  -3956   2061   -416       C  
ATOM   5196  NE  ARG J 705       9.976 -55.334  21.263  1.00129.56           N  
ANISOU 5196  NE  ARG J 705    15418  21938  11870  -4088   1928   -486       N  
ATOM   5197  CZ  ARG J 705       8.793 -54.943  21.727  1.00130.41           C  
ANISOU 5197  CZ  ARG J 705    15740  21808  12002  -4316   1879   -735       C  
ATOM   5198  NH1 ARG J 705       8.279 -53.782  21.345  1.00129.85           N  
ANISOU 5198  NH1 ARG J 705    16038  21238  12061  -4423   1953   -928       N  
ATOM   5199  NH2 ARG J 705       8.125 -55.716  22.572  1.00130.01           N  
ANISOU 5199  NH2 ARG J 705    15534  22019  11846  -4424   1763   -781       N  
ATOM   5200  N   ILE J 706      16.870 -53.948  19.162  1.00108.20           N  
ANISOU 5200  N   ILE J 706    12780  18839   9492  -2324   2663    618       N  
ATOM   5201  CA  ILE J 706      17.832 -53.219  18.342  1.00 98.34           C  
ANISOU 5201  CA  ILE J 706    11710  17336   8318  -2158   2834    697       C  
ATOM   5202  C   ILE J 706      18.890 -54.173  17.802  1.00 95.00           C  
ANISOU 5202  C   ILE J 706    10970  17285   7840  -1978   2935    964       C  
ATOM   5203  O   ILE J 706      18.613 -55.003  16.935  1.00 94.32           O  
ANISOU 5203  O   ILE J 706    10565  17605   7667  -2239   2879    998       O  
ATOM   5204  CB  ILE J 706      18.495 -52.072  19.131  1.00 93.55           C  
ANISOU 5204  CB  ILE J 706    11498  16229   7818  -1804   2937    695       C  
ATOM   5205  CG1 ILE J 706      17.459 -51.019  19.535  1.00 74.49           C  
ANISOU 5205  CG1 ILE J 706     9386  13448   5470  -1984   2828    436       C  
ATOM   5206  CG2 ILE J 706      19.618 -51.448  18.315  1.00 77.52           C  
ANISOU 5206  CG2 ILE J 706     9633  13986   5837  -1611   3125    803       C  
ATOM   5207  CD1 ILE J 706      18.046 -49.841  20.282  1.00 71.73           C  
ANISOU 5207  CD1 ILE J 706     9402  12643   5210  -1676   2894    424       C  
TER    5208      ILE J 706                                                      
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.