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***  CELL ADHESION 21-MAR-11 3R6B  ***

elNémo ID: 200204170153128465

Job options:

ID        	=	 200204170153128465
JOBID     	=	 CELL ADHESION 21-MAR-11 3R6B
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 ADHESION                           21-MAR-11   3R6B              
TITLE     CRYSTAL STRUCTURE OF THROMBOSPONDIN-1 TSR DOMAINS 2 AND 3             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: THROMBOSPONDIN-1;                                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 434-547;                                      
COMPND   5 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: THBS1, TSP, TSP1;                                              
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PGST PARALLEL 1                           
KEYWDS    CELL ADHESION, DISULFIDE BOND, EGF-LIKE DOMAIN, TSP-1 TYPE 1 REPEAT   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.C.PAGE,P.A.KLENOTIC,S.MISRA,R.L.SILVERSTEIN                         
REVDAT   3   16-NOV-11 3R6B    1       JRNL                                     
REVDAT   2   17-AUG-11 3R6B    1       JRNL                                     
REVDAT   1   10-AUG-11 3R6B    0                                                
JRNL        AUTH   P.A.KLENOTIC,R.C.PAGE,S.MISRA,R.L.SILVERSTEIN                
JRNL        TITL   EXPRESSION, PURIFICATION AND STRUCTURAL CHARACTERIZATION OF  
JRNL        TITL 2 FUNCTIONALLY REPLETE THROMBOSPONDIN-1 TYPE 1 REPEATS IN A    
JRNL        TITL 3 BACTERIAL EXPRESSION SYSTEM.                                 
JRNL        REF    PROTEIN EXPR.PURIF.           V.  80   253 2011              
JRNL        REFN                   ISSN 1046-5928                               
JRNL        PMID   21821127                                                     
JRNL        DOI    10.1016/J.PEP.2011.07.010                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7_650)                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MLHL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.35                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 6519                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.239                           
REMARK   3   R VALUE            (WORKING SET) : 0.235                           
REMARK   3   FREE R VALUE                     : 0.273                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.020                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 653                             
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 30.3559 -  4.1016    0.97     1273   142  0.2024 0.2286        
REMARK   3     2  4.1016 -  3.2568    0.92     1151   127  0.2270 0.2507        
REMARK   3     3  3.2568 -  2.8454    0.94     1164   129  0.2466 0.3082        
REMARK   3     4  2.8454 -  2.5854    0.95     1169   130  0.2911 0.3810        
REMARK   3     5  2.5854 -  2.4002    0.90     1109   125  0.3241 0.3781        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 0.90                                          
REMARK   3   SHRINKAGE RADIUS   : 0.61                                          
REMARK   3   K_SOL              : 0.35                                          
REMARK   3   B_SOL              : 58.09                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.390            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 39.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -5.46040                                             
REMARK   3    B22 (A**2) : -3.25010                                             
REMARK   3    B33 (A**2) : 8.71050                                              
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.008            916                                  
REMARK   3   ANGLE     :  1.286           1209                                  
REMARK   3   CHIRALITY :  0.088            119                                  
REMARK   3   PLANARITY :  0.006            161                                  
REMARK   3   DIHEDRAL  : 13.171            330                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 13                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (chain A and resid 415:423)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -23.0210 -10.5834 -24.6556              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4918 T22:   0.2435                                     
REMARK   3      T33:   0.2912 T12:  -0.1169                                     
REMARK   3      T13:   0.0427 T23:  -0.1235                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2391 L22:   0.1060                                     
REMARK   3      L33:   0.0022 L12:  -0.1587                                     
REMARK   3      L13:   0.0056 L23:  -0.0056                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2100 S12:  -0.0548 S13:  -0.1907                       
REMARK   3      S21:   0.0042 S22:  -0.1173 S23:   0.0365                       
REMARK   3      S31:   0.2295 S32:  -0.3345 S33:  -0.0960                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (chain A and resid 424:435)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -13.1023   9.4181 -13.5351              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2778 T22:  -0.0530                                     
REMARK   3      T33:   0.3483 T12:  -0.3251                                     
REMARK   3      T13:  -0.1290 T23:   0.1449                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1451 L22:   0.3520                                     
REMARK   3      L33:   0.1055 L12:   0.0967                                     
REMARK   3      L13:   0.0464 L23:  -0.1525                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0761 S12:  -0.1098 S13:  -0.1413                       
REMARK   3      S21:  -0.1700 S22:   0.1375 S23:   0.0435                       
REMARK   3      S31:   0.2257 S32:  -0.0323 S33:   0.2395                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (chain A and resid 436:442)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -16.5351   2.7880 -19.0645              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5060 T22:   0.2463                                     
REMARK   3      T33:   0.2445 T12:  -0.0944                                     
REMARK   3      T13:  -0.0145 T23:  -0.0138                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1289 L22:   3.2964                                     
REMARK   3      L33:   2.6046 L12:   0.1310                                     
REMARK   3      L13:   0.7177 L23:   2.3361                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2475 S12:   0.0937 S13:   0.0821                       
REMARK   3      S21:   0.0267 S22:  -0.3173 S23:   0.2751                       
REMARK   3      S31:  -0.6098 S32:   0.4376 S33:  -0.1083                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (chain A and resid 443:449)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -19.8946 -13.9251 -23.6273              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3363 T22:   0.2063                                     
REMARK   3      T33:   0.4489 T12:   0.0086                                     
REMARK   3      T13:   0.0432 T23:  -0.1038                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3511 L22:   0.5731                                     
REMARK   3      L33:   0.7634 L12:  -0.4117                                     
REMARK   3      L13:  -0.5186 L23:   0.5934                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0660 S12:   0.3879 S13:  -0.5880                       
REMARK   3      S21:   0.2833 S22:   0.1087 S23:   0.4057                       
REMARK   3      S31:   0.4637 S32:  -0.0526 S33:   0.1007                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: (chain A and resid 450:457)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -19.9091 -15.9873 -32.6103              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9453 T22:   0.5901                                     
REMARK   3      T33:   0.3781 T12:   0.0116                                     
REMARK   3      T13:   0.1717 T23:  -0.1407                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1514 L22:   0.7349                                     
REMARK   3      L33:   0.5338 L12:  -0.0417                                     
REMARK   3      L13:   0.2806 L23:  -0.5903                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0107 S12:   0.7232 S13:  -0.3833                       
REMARK   3      S21:  -0.2373 S22:  -0.4028 S23:   0.1545                       
REMARK   3      S31:  -0.3603 S32:   0.1163 S33:   0.1970                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: (chain A and resid 458:464)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -16.9267   2.5313 -23.9940              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7949 T22:   0.4229                                     
REMARK   3      T33:   0.3859 T12:  -0.3084                                     
REMARK   3      T13:  -0.0296 T23:   0.3254                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1528 L22:   0.1543                                     
REMARK   3      L33:   0.1179 L12:  -0.1440                                     
REMARK   3      L13:  -0.1096 L23:   0.1305                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1266 S12:   0.0142 S13:   0.0303                       
REMARK   3      S21:  -0.0479 S22:  -0.0489 S23:  -0.1691                       
REMARK   3      S31:  -0.1151 S32:   0.1328 S33:  -0.2113                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: (chain A and resid 465:470)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -13.2139  18.1956 -13.9244              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2439 T22:   0.4534                                     
REMARK   3      T33:   0.7550 T12:  -0.1997                                     
REMARK   3      T13:  -0.1916 T23:   0.1446                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8565 L22:   1.9873                                     
REMARK   3      L33:   1.7824 L12:   0.2692                                     
REMARK   3      L13:  -0.0216 L23:   0.6440                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1244 S12:  -0.0428 S13:  -0.0680                       
REMARK   3      S21:  -0.2119 S22:   0.2209 S23:   0.1706                       
REMARK   3      S31:   0.2029 S32:  -0.0278 S33:   0.0399                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: (chain A and resid 471:484)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  12.4244  33.4341 -10.7244              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2873 T22:   0.2393                                     
REMARK   3      T33:   0.3055 T12:  -0.0201                                     
REMARK   3      T13:  -0.0455 T23:   0.0078                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.7507 L22:   1.9307                                     
REMARK   3      L33:   0.6717 L12:   3.0514                                     
REMARK   3      L13:  -1.0679 L23:  -0.7752                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0975 S12:   0.6041 S13:  -0.2930                       
REMARK   3      S21:   0.1539 S22:   0.0594 S23:  -0.2198                       
REMARK   3      S31:  -0.2641 S32:  -0.0027 S33:  -0.0496                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: (chain A and resid 485:491)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  31.9323  49.9219  -5.9953              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3211 T22:   0.4196                                     
REMARK   3      T33:   1.0472 T12:  -0.1695                                     
REMARK   3      T13:  -0.1648 T23:   0.0476                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3056 L22:   0.2497                                     
REMARK   3      L33:   0.1950 L12:   0.2597                                     
REMARK   3      L13:   0.0771 L23:   0.1336                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1663 S12:  -0.0058 S13:  -0.0139                       
REMARK   3      S21:  -0.0301 S22:  -0.0782 S23:   0.0120                       
REMARK   3      S31:  -0.0945 S32:   0.0323 S33:  -0.2794                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: (chain A and resid 492:497)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  25.5603  43.0904  -5.3973              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2864 T22:   0.4395                                     
REMARK   3      T33:   0.3229 T12:  -0.1480                                     
REMARK   3      T13:  -0.1048 T23:   0.0514                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1600 L22:   1.3619                                     
REMARK   3      L33:   0.3167 L12:   1.0490                                     
REMARK   3      L13:   0.2671 L23:   0.5601                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0411 S12:  -0.0108 S13:  -0.0707                       
REMARK   3      S21:   0.1280 S22:   0.0854 S23:   0.0318                       
REMARK   3      S31:  -0.0506 S32:   0.0525 S33:   0.0049                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: (chain A and resid 498:510)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   5.0404  32.2961 -10.0954              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0905 T22:   0.2189                                     
REMARK   3      T33:   0.4029 T12:  -0.0970                                     
REMARK   3      T13:  -0.1090 T23:  -0.0285                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4838 L22:   0.7091                                     
REMARK   3      L33:   0.0033 L12:   0.8329                                     
REMARK   3      L13:   0.0937 L23:   0.0247                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0515 S12:   0.0073 S13:  -0.2593                       
REMARK   3      S21:   0.0617 S22:  -0.3130 S23:   0.1941                       
REMARK   3      S31:   0.2311 S32:  -0.2701 S33:  -1.2369                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: (chain A and resid 511:523)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  17.7165  35.1047  -3.7926              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3986 T22:   0.3790                                     
REMARK   3      T33:   0.3829 T12:  -0.1029                                     
REMARK   3      T13:  -0.1631 T23:   0.1251                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1919 L22:   0.4221                                     
REMARK   3      L33:   0.8628 L12:   0.0512                                     
REMARK   3      L13:  -0.2474 L23:   0.4198                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2893 S12:  -0.3744 S13:  -0.4563                       
REMARK   3      S21:   0.3815 S22:  -0.1297 S23:  -0.2000                       
REMARK   3      S31:   0.3378 S32:   0.1344 S33:  -0.0989                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: (chain A and resid 524:529)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  40.0513  47.7230  -4.4711              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3444 T22:   0.8081                                     
REMARK   3      T33:   0.6351 T12:  -0.2607                                     
REMARK   3      T13:  -0.1008 T23:   0.1924                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0891 L22:   0.7102                                     
REMARK   3      L33:   0.2605 L12:  -0.2507                                     
REMARK   3      L13:  -0.0733 L23:   0.1876                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0902 S12:   0.1938 S13:  -0.2881                       
REMARK   3      S21:   0.1165 S22:  -0.1527 S23:   0.2780                       
REMARK   3      S31:  -0.1091 S32:   0.0558 S33:   0.0150                       
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 3R6B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-MAR-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB064543.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-MAR-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 93.0                               
REMARK 200  PH                             : 5.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007 HF             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU SATURN 944+                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : D*TREK                             
REMARK 200  DATA SCALING SOFTWARE          : D*TREK                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 6564                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.354                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.0                               
REMARK 200  DATA REDUNDANCY                : 5.800                              
REMARK 200  R MERGE                    (I) : 0.06500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 16.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.49                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 87.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.84                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.22700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 4.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX (PHENIX.REFINE: 1.7_650)                       
REMARK 200 STARTING MODEL: PDB ENTRY 1LSL                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.64                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.9M SODIUM POTASSIUM PHOSPHATE, PH      
REMARK 280  5.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293.0K              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       30.35350            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       30.35350            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       33.18200            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       42.40850            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       33.18200            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       42.40850            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       30.35350            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       33.18200            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       42.40850            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       30.35350            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       33.18200            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       42.40850            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A   425                                                      
REMARK 465     ALA A   426                                                      
REMARK 465     MET A   427                                                      
REMARK 465     ASP A   428                                                      
REMARK 465     PRO A   429                                                      
REMARK 465     GLU A   430                                                      
REMARK 465     PHE A   431                                                      
REMARK 465     GLU A   432                                                      
REMARK 465     LEU A   548                                                      
REMARK 465     GLU A   549                                                      
REMARK 465     PRO A   550                                                      
REMARK 465     TYR A   551                                                      
REMARK 465     THR A   552                                                      
REMARK 465     TYR A   553                                                      
REMARK 465     ARG A   554                                                      
REMARK 465     VAL A   555                                                      
REMARK 465     ARG A   556                                                      
REMARK 465     PHE A   557                                                      
REMARK 465     LEU A   558                                                      
REMARK 465     ALA A   559                                                      
REMARK 465     LYS A   560                                                      
REMARK 465     GLU A   561                                                      
REMARK 465     ASN A   562                                                      
REMARK 465     VAL A   563                                                      
REMARK 465     THR A   564                                                      
REMARK 465     GLN A   565                                                      
REMARK 465     ASP A   566                                                      
REMARK 465     ALA A   567                                                      
REMARK 465     GLU A   568                                                      
REMARK 465     ASP A   569                                                      
REMARK 465     ASN A   570                                                      
REMARK 465     THR A   571                                                      
REMARK 465     VAL A   572                                                      
REMARK 465     SER A   573                                                      
REMARK 465     PHE A   574                                                      
REMARK 465     LEU A   575                                                      
REMARK 465     GLN A   576                                                      
REMARK 465     PRO A   577                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LEU A 433    CG   CD1  CD2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   CB   CYS A   508     SG   CYS A   546              1.74            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 2                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 3                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 4                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 5                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 6                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 7                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 8                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1LSL   RELATED DB: PDB                                   
REMARK 900 GLYCOSYLATED TSR DOMAINS 2 AND 3 FROM A DROSOPHILA                   
REMARK 900 EXPRESSION SYSTEM                                                    
DBREF  3R6B A  434   547  UNP    P07996   TSP1_HUMAN     434    547             
SEQADV 3R6B GLY A  425  UNP  P07996              EXPRESSION TAG                 
SEQADV 3R6B ALA A  426  UNP  P07996              EXPRESSION TAG                 
SEQADV 3R6B MET A  427  UNP  P07996              EXPRESSION TAG                 
SEQADV 3R6B ASP A  428  UNP  P07996              EXPRESSION TAG                 
SEQADV 3R6B PRO A  429  UNP  P07996              EXPRESSION TAG                 
SEQADV 3R6B GLU A  430  UNP  P07996              EXPRESSION TAG                 
SEQADV 3R6B PHE A  431  UNP  P07996              EXPRESSION TAG                 
SEQADV 3R6B GLU A  432  UNP  P07996              EXPRESSION TAG                 
SEQADV 3R6B LEU A  433  UNP  P07996              EXPRESSION TAG                 
SEQADV 3R6B LEU A  548  UNP  P07996              EXPRESSION TAG                 
SEQADV 3R6B GLU A  549  UNP  P07996              EXPRESSION TAG                 
SEQADV 3R6B PRO A  550  UNP  P07996              EXPRESSION TAG                 
SEQADV 3R6B TYR A  551  UNP  P07996              EXPRESSION TAG                 
SEQADV 3R6B THR A  552  UNP  P07996              EXPRESSION TAG                 
SEQADV 3R6B TYR A  553  UNP  P07996              EXPRESSION TAG                 
SEQADV 3R6B ARG A  554  UNP  P07996              EXPRESSION TAG                 
SEQADV 3R6B VAL A  555  UNP  P07996              EXPRESSION TAG                 
SEQADV 3R6B ARG A  556  UNP  P07996              EXPRESSION TAG                 
SEQADV 3R6B PHE A  557  UNP  P07996              EXPRESSION TAG                 
SEQADV 3R6B LEU A  558  UNP  P07996              EXPRESSION TAG                 
SEQADV 3R6B ALA A  559  UNP  P07996              EXPRESSION TAG                 
SEQADV 3R6B LYS A  560  UNP  P07996              EXPRESSION TAG                 
SEQADV 3R6B GLU A  561  UNP  P07996              EXPRESSION TAG                 
SEQADV 3R6B ASN A  562  UNP  P07996              EXPRESSION TAG                 
SEQADV 3R6B VAL A  563  UNP  P07996              EXPRESSION TAG                 
SEQADV 3R6B THR A  564  UNP  P07996              EXPRESSION TAG                 
SEQADV 3R6B GLN A  565  UNP  P07996              EXPRESSION TAG                 
SEQADV 3R6B ASP A  566  UNP  P07996              EXPRESSION TAG                 
SEQADV 3R6B ALA A  567  UNP  P07996              EXPRESSION TAG                 
SEQADV 3R6B GLU A  568  UNP  P07996              EXPRESSION TAG                 
SEQADV 3R6B ASP A  569  UNP  P07996              EXPRESSION TAG                 
SEQADV 3R6B ASN A  570  UNP  P07996              EXPRESSION TAG                 
SEQADV 3R6B THR A  571  UNP  P07996              EXPRESSION TAG                 
SEQADV 3R6B VAL A  572  UNP  P07996              EXPRESSION TAG                 
SEQADV 3R6B SER A  573  UNP  P07996              EXPRESSION TAG                 
SEQADV 3R6B PHE A  574  UNP  P07996              EXPRESSION TAG                 
SEQADV 3R6B LEU A  575  UNP  P07996              EXPRESSION TAG                 
SEQADV 3R6B GLN A  576  UNP  P07996              EXPRESSION TAG                 
SEQADV 3R6B PRO A  577  UNP  P07996              EXPRESSION TAG                 
SEQRES   1 A  153  GLY ALA MET ASP PRO GLU PHE GLU LEU GLN ASP GLY GLY          
SEQRES   2 A  153  TRP SER HIS TRP SER PRO TRP SER SER CYS SER VAL THR          
SEQRES   3 A  153  CYS GLY ASP GLY VAL ILE THR ARG ILE ARG LEU CYS ASN          
SEQRES   4 A  153  SER PRO SER PRO GLN MET ASN GLY LYS PRO CYS GLU GLY          
SEQRES   5 A  153  GLU ALA ARG GLU THR LYS ALA CYS LYS LYS ASP ALA CYS          
SEQRES   6 A  153  PRO ILE ASN GLY GLY TRP GLY PRO TRP SER PRO TRP ASP          
SEQRES   7 A  153  ILE CYS SER VAL THR CYS GLY GLY GLY VAL GLN LYS ARG          
SEQRES   8 A  153  SER ARG LEU CYS ASN ASN PRO THR PRO GLN PHE GLY GLY          
SEQRES   9 A  153  LYS ASP CYS VAL GLY ASP VAL THR GLU ASN GLN ILE CYS          
SEQRES  10 A  153  ASN LYS GLN ASP CYS PRO LEU GLU PRO TYR THR TYR ARG          
SEQRES  11 A  153  VAL ARG PHE LEU ALA LYS GLU ASN VAL THR GLN ASP ALA          
SEQRES  12 A  153  GLU ASP ASN THR VAL SER PHE LEU GLN PRO                      
HET    EDO  A   1       4                                                       
HET    EDO  A   2       4                                                       
HET    EDO  A   3       4                                                       
HET    EDO  A   4       4                                                       
HET    EDO  A   5       4                                                       
HET    EDO  A   6       4                                                       
HET    EDO  A   7       4                                                       
HET    EDO  A   8       4                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   2  EDO    8(C2 H6 O2)                                                  
FORMUL  10  HOH   *94(H2 O)                                                     
SHEET    1   A 2 ASP A 453  GLY A 454  0                                        
SHEET    2   A 2 CYS A 484  LYS A 485 -1  O  CYS A 484   N  GLY A 454           
SHEET    1   B 2 THR A 457  ILE A 459  0                                        
SHEET    2   B 2 ARG A 479  THR A 481 -1  O  GLU A 480   N  ARG A 458           
SHEET    1   C 2 GLY A 511  SER A 516  0                                        
SHEET    2   C 2 THR A 536  CYS A 541 -1  O  GLU A 537   N  ARG A 515           
SSBOND   1 CYS A  447    CYS A  484                          1555   1555  2.03  
SSBOND   2 CYS A  451    CYS A  489                          1555   1555  2.03  
SSBOND   3 CYS A  462    CYS A  474                          1555   1555  2.03  
SSBOND   4 CYS A  504    CYS A  541                          1555   1555  2.03  
SSBOND   5 CYS A  508    CYS A  546                          1555   1555  2.03  
SSBOND   6 CYS A  519    CYS A  531                          1555   1555  2.03  
CISPEP   1 SER A  464    PRO A  465          0         0.27                     
CISPEP   2 ASN A  521    PRO A  522          0         4.15                     
SITE     1 AC1  3 EDO A   2  HOH A  34  HOH A  35                               
SITE     1 AC2  6 EDO A   1  SER A 442  TRP A 444  ARG A 458                    
SITE     2 AC2  6 LEU A 518  HOH A 583                                          
SITE     1 AC3  3 CYS A 447  ILE A 456  LYS A 486                               
SITE     1 AC4  4 ASN A 463  ASP A 487  ALA A 488  ASN A 521                    
SITE     1 AC5  2 ARG A 460  GLU A 475                                          
SITE     1 AC6  2 HIS A 440  GLN A 525                                          
SITE     1 AC7  2 MET A 469  ARG A 517                                          
SITE     1 AC8  3 HOH A  39  PRO A 497  TRP A 498                               
CRYST1   66.364   84.817   60.707  90.00  90.00  90.00 C 2 2 21      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.015068  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011790  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016473        0.00000                         
ATOM      1  N   LEU A 433     -23.006 -23.980 -32.527  1.00 79.20           N  
ANISOU    1  N   LEU A 433    11595   8690   9806  -1677   1405  -1144       N  
ATOM      2  CA  LEU A 433     -22.638 -22.608 -32.855  1.00 79.09           C  
ANISOU    2  CA  LEU A 433    11571   8701   9779  -1609   1291  -1134       C  
ATOM      3  C   LEU A 433     -23.575 -21.598 -32.203  1.00 80.19           C  
ANISOU    3  C   LEU A 433    11669   8911   9888  -1613   1227  -1193       C  
ATOM      4  O   LEU A 433     -24.697 -21.384 -32.661  1.00 82.31           O  
ANISOU    4  O   LEU A 433    11883   9253  10139  -1642   1202  -1278       O  
ATOM      5  CB  LEU A 433     -22.630 -22.408 -34.373  1.00 78.22           C  
ANISOU    5  CB  LEU A 433    11439   8611   9670  -1588   1246  -1164       C  
ATOM      6  N   GLN A 434     -23.098 -20.980 -31.130  1.00 77.81           N  
ANISOU    6  N   GLN A 434    11391   8592   9582  -1578   1198  -1147       N  
ATOM      7  CA  GLN A 434     -23.869 -19.987 -30.395  1.00 75.89           C  
ANISOU    7  CA  GLN A 434    11113   8415   9308  -1574   1133  -1196       C  
ATOM      8  C   GLN A 434     -23.267 -18.594 -30.524  1.00 69.22           C  
ANISOU    8  C   GLN A 434    10265   7584   8453  -1488   1015  -1171       C  
ATOM      9  O   GLN A 434     -22.056 -18.404 -30.386  1.00 65.30           O  
ANISOU    9  O   GLN A 434     9814   7022   7976  -1435   1001  -1087       O  
ATOM     10  CB  GLN A 434     -24.014 -20.378 -28.926  1.00 78.73           C  
ANISOU   10  CB  GLN A 434    11496   8753   9664  -1610   1196  -1178       C  
ATOM     11  CG  GLN A 434     -22.966 -19.783 -28.017  1.00 80.29           C  
ANISOU   11  CG  GLN A 434    11740   8901   9866  -1550   1162  -1096       C  
ATOM     12  CD  GLN A 434     -22.813 -20.567 -26.731  1.00 82.43           C  
ANISOU   12  CD  GLN A 434    12050   9122  10146  -1585   1252  -1052       C  
ATOM     13  OE1 GLN A 434     -23.246 -21.718 -26.640  1.00 83.64           O  
ANISOU   13  OE1 GLN A 434    12205   9263  10311  -1650   1350  -1067       O  
ATOM     14  NE2 GLN A 434     -22.197 -19.951 -25.729  1.00 82.29           N  
ANISOU   14  NE2 GLN A 434    12063   9077  10125  -1540   1218   -997       N  
ATOM     15  N   ASP A 435     -24.128 -17.624 -30.805  1.00 66.04           N  
ANISOU   15  N   ASP A 435     9801   7269   8021  -1470    928  -1242       N  
ATOM     16  CA  ASP A 435     -23.708 -16.239 -30.925  1.00 60.56           C  
ANISOU   16  CA  ASP A 435     9093   6601   7316  -1387    810  -1229       C  
ATOM     17  C   ASP A 435     -23.287 -15.706 -29.565  1.00 51.70           C  
ANISOU   17  C   ASP A 435     8001   5459   6186  -1360    789  -1188       C  
ATOM     18  O   ASP A 435     -23.825 -16.110 -28.538  1.00 50.96           O  
ANISOU   18  O   ASP A 435     7910   5374   6079  -1408    841  -1207       O  
ATOM     19  CB  ASP A 435     -24.847 -15.390 -31.489  1.00 65.65           C  
ANISOU   19  CB  ASP A 435     9658   7356   7931  -1373    724  -1316       C  
ATOM     20  CG  ASP A 435     -25.285 -15.847 -32.868  1.00 70.53           C  
ANISOU   20  CG  ASP A 435    10247   7995   8556  -1393    737  -1357       C  
ATOM     21  OD1 ASP A 435     -24.422 -16.324 -33.633  1.00 69.36           O  
ANISOU   21  OD1 ASP A 435    10138   7782   8435  -1384    767  -1311       O  
ATOM     22  OD2 ASP A 435     -26.491 -15.732 -33.181  1.00 74.09           O  
ANISOU   22  OD2 ASP A 435    10635   8529   8987  -1415    717  -1432       O  
ATOM     23  N   GLY A 436     -22.315 -14.805 -29.556  1.00 44.31           N  
ANISOU   23  N   GLY A 436     7085   4493   5257  -1283    713  -1133       N  
ATOM     24  CA  GLY A 436     -21.901 -14.185 -28.319  1.00 44.30           C  
ANISOU   24  CA  GLY A 436     7110   4475   5246  -1248    680  -1095       C  
ATOM     25  C   GLY A 436     -23.023 -13.310 -27.799  1.00 44.20           C  
ANISOU   25  C   GLY A 436     7037   4568   5191  -1244    610  -1175       C  
ATOM     26  O   GLY A 436     -23.961 -12.988 -28.534  1.00 43.41           O  
ANISOU   26  O   GLY A 436     6870   4552   5073  -1249    568  -1247       O  
ATOM     27  N   GLY A 437     -22.938 -12.933 -26.530  1.00 40.09           N  
ANISOU   27  N   GLY A 437     6534   4044   4652  -1231    597  -1160       N  
ATOM     28  CA  GLY A 437     -23.814 -11.909 -26.006  1.00 36.22           C  
ANISOU   28  CA  GLY A 437     5984   3658   4119  -1206    511  -1224       C  
ATOM     29  C   GLY A 437     -23.104 -11.227 -24.872  1.00 35.05           C  
ANISOU   29  C   GLY A 437     5876   3478   3962  -1154    467  -1175       C  
ATOM     30  O   GLY A 437     -22.313 -11.856 -24.173  1.00 39.10           O  
ANISOU   30  O   GLY A 437     6463   3899   4496  -1168    535  -1107       O  
ATOM     31  N   TRP A 438     -23.422  -9.952 -24.670  1.00 31.64           N  
ANISOU   31  N   TRP A 438     5393   3127   3500  -1092    351  -1208       N  
ATOM     32  CA  TRP A 438     -22.695  -9.096 -23.745  1.00 29.33           C  
ANISOU   32  CA  TRP A 438     5134   2812   3197  -1026    285  -1163       C  
ATOM     33  C   TRP A 438     -23.171  -9.343 -22.335  1.00 32.16           C  
ANISOU   33  C   TRP A 438     5508   3191   3521  -1060    324  -1181       C  
ATOM     34  O   TRP A 438     -24.333  -9.669 -22.112  1.00 34.84           O  
ANISOU   34  O   TRP A 438     5798   3608   3832  -1115    356  -1250       O  
ATOM     35  CB  TRP A 438     -22.939  -7.613 -24.063  1.00 34.85           C  
ANISOU   35  CB  TRP A 438     5762   3603   3878   -944    143  -1195       C  
ATOM     36  CG  TRP A 438     -22.343  -7.104 -25.338  1.00 40.79           C  
ANISOU   36  CG  TRP A 438     6500   4336   4662   -893     86  -1173       C  
ATOM     37  CD1 TRP A 438     -23.017  -6.741 -26.464  1.00 44.21           C  
ANISOU   37  CD1 TRP A 438     6860   4843   5096   -882     42  -1226       C  
ATOM     38  CD2 TRP A 438     -20.950  -6.882 -25.615  1.00 42.19           C  
ANISOU   38  CD2 TRP A 438     6738   4415   4879   -839     67  -1087       C  
ATOM     39  NE1 TRP A 438     -22.134  -6.317 -27.428  1.00 44.62           N  
ANISOU   39  NE1 TRP A 438     6923   4849   5180   -831      0  -1185       N  
ATOM     40  CE2 TRP A 438     -20.860  -6.394 -26.931  1.00 42.61           C  
ANISOU   40  CE2 TRP A 438     6749   4491   4951   -805     15  -1099       C  
ATOM     41  CE3 TRP A 438     -19.774  -7.061 -24.883  1.00 43.01           C  
ANISOU   41  CE3 TRP A 438     6924   4412   5005   -814     90   -997       C  
ATOM     42  CZ2 TRP A 438     -19.642  -6.076 -27.526  1.00 42.09           C  
ANISOU   42  CZ2 TRP A 438     6719   4349   4924   -750    -13  -1026       C  
ATOM     43  CZ3 TRP A 438     -18.565  -6.749 -25.479  1.00 41.39           C  
ANISOU   43  CZ3 TRP A 438     6751   4132   4843   -754     58   -919       C  
ATOM     44  CH2 TRP A 438     -18.511  -6.256 -26.783  1.00 41.14           C  
ANISOU   44  CH2 TRP A 438     6675   4129   4828   -724      8   -936       C  
ATOM     45  N   SER A 439     -22.279  -9.167 -21.373  1.00 29.69           N  
ANISOU   45  N   SER A 439     5225   2831   3223   -998    312  -1086       N  
ATOM     46  CA  SER A 439     -22.707  -9.129 -20.000  1.00 28.31           C  
ANISOU   46  CA  SER A 439     5024   2712   3022   -986    316  -1075       C  
ATOM     47  C   SER A 439     -23.309  -7.743 -19.824  1.00 33.05           C  
ANISOU   47  C   SER A 439     5552   3426   3579   -925    186  -1133       C  
ATOM     48  O   SER A 439     -23.220  -6.907 -20.726  1.00 33.78           O  
ANISOU   48  O   SER A 439     5626   3537   3671   -891    101  -1165       O  
ATOM     49  CB  SER A 439     -21.498  -9.298 -19.081  1.00 31.62           C  
ANISOU   49  CB  SER A 439     5494   3047   3472   -928    335   -953       C  
ATOM     50  OG  SER A 439     -20.626  -8.180 -19.173  1.00 33.62           O  
ANISOU   50  OG  SER A 439     5748   3287   3738   -830    224   -905       O  
ATOM     51  N   HIS A 440     -23.889  -7.484 -18.660  1.00 31.74           N  
ANISOU   51  N   HIS A 440     5347   3335   3379   -908    168  -1144       N  
ATOM     52  CA  HIS A 440     -24.273  -6.134 -18.314  1.00 32.26           C  
ANISOU   52  CA  HIS A 440     5351   3499   3408   -837     40  -1180       C  
ATOM     53  C   HIS A 440     -22.994  -5.322 -18.143  1.00 33.28           C  
ANISOU   53  C   HIS A 440     5506   3573   3567   -735    -42  -1092       C  
ATOM     54  O   HIS A 440     -21.910  -5.893 -18.009  1.00 33.60           O  
ANISOU   54  O   HIS A 440     5610   3507   3650   -722     11   -999       O  
ATOM     55  CB  HIS A 440     -25.082  -6.116 -17.022  1.00 32.31           C  
ANISOU   55  CB  HIS A 440     5315   3589   3372   -838     47  -1201       C  
ATOM     56  CG  HIS A 440     -26.478  -6.628 -17.182  1.00 36.73           C  
ANISOU   56  CG  HIS A 440     5833   4226   3897   -928    100  -1301       C  
ATOM     57  ND1 HIS A 440     -27.568  -5.791 -17.255  1.00 38.63           N  
ANISOU   57  ND1 HIS A 440     6001   4586   4090   -924     22  -1397       N  
ATOM     58  CD2 HIS A 440     -26.958  -7.888 -17.292  1.00 36.22           C  
ANISOU   58  CD2 HIS A 440     5788   4133   3840  -1023    224  -1322       C  
ATOM     59  CE1 HIS A 440     -28.666  -6.515 -17.399  1.00 36.52           C  
ANISOU   59  CE1 HIS A 440     5710   4363   3803  -1014     95  -1472       C  
ATOM     60  NE2 HIS A 440     -28.322  -7.790 -17.426  1.00 34.17           N  
ANISOU   60  NE2 HIS A 440     5467   3977   3539  -1075    218  -1428       N  
ATOM     61  N   TRP A 441     -23.118  -3.999 -18.187  1.00 25.06           N  
ANISOU   61  N   TRP A 441     4415   2601   2506   -663   -170  -1121       N  
ATOM     62  CA  TRP A 441     -21.971  -3.121 -18.018  1.00 24.39           C  
ANISOU   62  CA  TRP A 441     4346   2471   2450   -562   -258  -1043       C  
ATOM     63  C   TRP A 441     -21.492  -3.156 -16.587  1.00 28.92           C  
ANISOU   63  C   TRP A 441     4932   3032   3024   -512   -253   -968       C  
ATOM     64  O   TRP A 441     -22.297  -3.177 -15.659  1.00 28.45           O  
ANISOU   64  O   TRP A 441     4835   3050   2924   -522   -246  -1002       O  
ATOM     65  CB  TRP A 441     -22.331  -1.661 -18.341  1.00 34.10           C  
ANISOU   65  CB  TRP A 441     5512   3788   3658   -498   -400  -1100       C  
ATOM     66  CG  TRP A 441     -22.496  -1.369 -19.790  1.00 34.86           C  
ANISOU   66  CG  TRP A 441     5598   3886   3760   -519   -430  -1154       C  
ATOM     67  CD1 TRP A 441     -23.666  -1.160 -20.451  1.00 34.42           C  
ANISOU   67  CD1 TRP A 441     5461   3932   3685   -553   -442  -1246       C  
ATOM     68  CD2 TRP A 441     -21.453  -1.245 -20.766  1.00 35.98           C  
ANISOU   68  CD2 TRP A 441     5782   3938   3949   -491   -446  -1102       C  
ATOM     69  NE1 TRP A 441     -23.420  -0.916 -21.779  1.00 36.48           N  
ANISOU   69  NE1 TRP A 441     5689   4182   3987   -537   -458  -1245       N  
ATOM     70  CE2 TRP A 441     -22.070  -0.963 -22.000  1.00 35.71           C  
ANISOU   70  CE2 TRP A 441     5675   3968   3926   -506   -460  -1162       C  
ATOM     71  CE3 TRP A 441     -20.058  -1.343 -20.715  1.00 36.40           C  
ANISOU   71  CE3 TRP A 441     5894   3880   4055   -440   -440   -994       C  
ATOM     72  CZ2 TRP A 441     -21.343  -0.787 -23.175  1.00 36.24           C  
ANISOU   72  CZ2 TRP A 441     5748   3984   4038   -482   -470  -1126       C  
ATOM     73  CZ3 TRP A 441     -19.337  -1.166 -21.882  1.00 34.37           C  
ANISOU   73  CZ3 TRP A 441     5665   3558   3835   -423   -459   -970       C  
ATOM     74  CH2 TRP A 441     -19.981  -0.887 -23.095  1.00 36.13           C  
ANISOU   74  CH2 TRP A 441     5822   3847   4059   -444   -473  -1034       C  
ATOM     75  N   SER A 442     -20.174  -3.113 -16.416  1.00 27.46           N  
ANISOU   75  N   SER A 442     4120   2563   3750  -1483  -1792   1187       N  
ATOM     76  CA  SER A 442     -19.581  -2.868 -15.116  1.00 27.07           C  
ANISOU   76  CA  SER A 442     4027   2536   3724  -1461  -1753   1182       C  
ATOM     77  C   SER A 442     -20.008  -1.487 -14.644  1.00 28.71           C  
ANISOU   77  C   SER A 442     4187   2788   3933  -1448  -1712   1185       C  
ATOM     78  O   SER A 442     -20.466  -0.670 -15.438  1.00 26.55           O  
ANISOU   78  O   SER A 442     3921   2522   3644  -1453  -1698   1178       O  
ATOM     79  CB  SER A 442     -18.058  -2.886 -15.233  1.00 38.02           C  
ANISOU   79  CB  SER A 442     5436   3892   5120  -1439  -1688   1126       C  
ATOM     80  OG  SER A 442     -17.591  -1.719 -15.881  1.00 35.61           O  
ANISOU   80  OG  SER A 442     5137   3588   4805  -1425  -1619   1083       O  
ATOM     81  N   PRO A 443     -19.877  -1.232 -13.341  1.00 28.53           N  
ANISOU   81  N   PRO A 443     4118   2795   3929  -1434  -1693   1196       N  
ATOM     82  CA  PRO A 443     -20.072   0.122 -12.825  1.00 30.10           C  
ANISOU   82  CA  PRO A 443     4274   3033   4130  -1419  -1641   1190       C  
ATOM     83  C   PRO A 443     -19.091   1.079 -13.509  1.00 34.11           C  
ANISOU   83  C   PRO A 443     4800   3528   4631  -1400  -1562   1131       C  
ATOM     84  O   PRO A 443     -18.078   0.648 -14.071  1.00 33.74           O  
ANISOU   84  O   PRO A 443     4791   3444   4583  -1395  -1540   1094       O  
ATOM     85  CB  PRO A 443     -19.710  -0.012 -11.340  1.00 29.66           C  
ANISOU   85  CB  PRO A 443     4178   2998   4095  -1405  -1629   1201       C  
ATOM     86  CG  PRO A 443     -19.871  -1.459 -11.025  1.00 29.76           C  
ANISOU   86  CG  PRO A 443     4200   2992   4114  -1421  -1698   1234       C  
ATOM     87  CD  PRO A 443     -19.565  -2.205 -12.280  1.00 29.36           C  
ANISOU   87  CD  PRO A 443     4206   2897   4052  -1433  -1720   1215       C  
ATOM     88  N   TRP A 444     -19.406   2.367 -13.492  1.00 36.00           N  
ANISOU   88  N   TRP A 444     5014   3796   4866  -1391  -1521   1123       N  
ATOM     89  CA  TRP A 444     -18.470   3.370 -13.987  1.00 33.95           C  
ANISOU   89  CA  TRP A 444     4765   3531   4604  -1372  -1443   1068       C  
ATOM     90  C   TRP A 444     -17.349   3.504 -12.973  1.00 28.01           C  
ANISOU   90  C   TRP A 444     3992   2782   3870  -1349  -1392   1041       C  
ATOM     91  O   TRP A 444     -17.594   3.496 -11.774  1.00 29.96           O  
ANISOU   91  O   TRP A 444     4200   3055   4128  -1344  -1400   1067       O  
ATOM     92  CB  TRP A 444     -19.161   4.725 -14.153  1.00 33.72           C  
ANISOU   92  CB  TRP A 444     4711   3534   4568  -1368  -1415   1070       C  
ATOM     93  CG  TRP A 444     -20.116   4.803 -15.305  1.00 34.64           C  
ANISOU   93  CG  TRP A 444     4851   3646   4666  -1388  -1454   1088       C  
ATOM     94  CD1 TRP A 444     -21.457   4.563 -15.275  1.00 35.62           C  
ANISOU   94  CD1 TRP A 444     4960   3786   4787  -1408  -1519   1140       C  
ATOM     95  CD2 TRP A 444     -19.804   5.167 -16.655  1.00 33.82           C  
ANISOU   95  CD2 TRP A 444     4788   3518   4544  -1392  -1432   1054       C  
ATOM     96  NE1 TRP A 444     -22.001   4.743 -16.528  1.00 34.98           N  
ANISOU   96  NE1 TRP A 444     4909   3694   4688  -1425  -1540   1142       N  
ATOM     97  CE2 TRP A 444     -21.005   5.112 -17.392  1.00 34.82           C  
ANISOU   97  CE2 TRP A 444     4925   3648   4656  -1415  -1488   1089       C  
ATOM     98  CE3 TRP A 444     -18.624   5.522 -17.314  1.00 36.35           C  
ANISOU   98  CE3 TRP A 444     5137   3815   4860  -1378  -1371    998       C  
ATOM     99  CZ2 TRP A 444     -21.060   5.405 -18.756  1.00 36.11           C  
ANISOU   99  CZ2 TRP A 444     5129   3793   4798  -1425  -1485   1070       C  
ATOM    100  CZ3 TRP A 444     -18.683   5.815 -18.672  1.00 37.92           C  
ANISOU  100  CZ3 TRP A 444     5375   3994   5038  -1388  -1366    979       C  
ATOM    101  CH2 TRP A 444     -19.891   5.750 -19.375  1.00 35.27           C  
ANISOU  101  CH2 TRP A 444     5052   3664   4686  -1412  -1424   1015       C  
ATOM    102  N   SER A 445     -16.119   3.638 -13.438  1.00 27.21           N  
ANISOU  102  N   SER A 445     3914   2654   3770  -1335  -1339    990       N  
ATOM    103  CA  SER A 445     -15.045   3.954 -12.509  1.00 33.06           C  
ANISOU  103  CA  SER A 445     4632   3401   4529  -1312  -1286    962       C  
ATOM    104  C   SER A 445     -15.185   5.395 -12.041  1.00 32.10           C  
ANISOU  104  C   SER A 445     4473   3317   4407  -1298  -1233    951       C  
ATOM    105  O   SER A 445     -16.063   6.135 -12.492  1.00 29.24           O  
ANISOU  105  O   SER A 445     4104   2973   4033  -1304  -1236    963       O  
ATOM    106  CB  SER A 445     -13.690   3.808 -13.192  1.00 36.45           C  
ANISOU  106  CB  SER A 445     5093   3791   4964  -1301  -1239    908       C  
ATOM    107  OG  SER A 445     -13.558   4.776 -14.213  1.00 36.99           O  
ANISOU  107  OG  SER A 445     5178   3858   5020  -1297  -1195    874       O  
ATOM    108  N   SER A 446     -14.297   5.779 -11.136  1.00 34.73           N  
ANISOU  108  N   SER A 446     4783   3660   4755  -1278  -1186    928       N  
ATOM    109  CA  SER A 446     -14.111   7.170 -10.735  1.00 35.56           C  
ANISOU  109  CA  SER A 446     4858   3793   4861  -1261  -1124    905       C  
ATOM    110  C   SER A 446     -13.489   7.977 -11.861  1.00 33.85           C  
ANISOU  110  C   SER A 446     4664   3561   4638  -1253  -1071    856       C  
ATOM    111  O   SER A 446     -13.003   7.425 -12.832  1.00 32.70           O  
ANISOU  111  O   SER A 446     4555   3380   4488  -1257  -1073    835       O  
ATOM    112  CB  SER A 446     -13.213   7.255  -9.509  1.00 38.29           C  
ANISOU  112  CB  SER A 446     5177   4148   5223  -1245  -1091    892       C  
ATOM    113  OG  SER A 446     -13.908   6.810  -8.367  1.00 43.79           O  
ANISOU  113  OG  SER A 446     5847   4869   5924  -1252  -1133    939       O  
ATOM    114  N   CYS A 447     -13.552   9.295 -11.748  1.00 37.84           N  
ANISOU  114  N   CYS A 447     5145   4091   5140  -1241  -1022    838       N  
ATOM    115  CA  CYS A 447     -12.828  10.153 -12.669  1.00 35.92           C  
ANISOU  115  CA  CYS A 447     4918   3837   4893  -1230   -964    789       C  
ATOM    116  C   CYS A 447     -11.338   9.822 -12.622  1.00 33.28           C  
ANISOU  116  C   CYS A 447     4595   3475   4575  -1216   -924    746       C  
ATOM    117  O   CYS A 447     -10.769   9.664 -11.548  1.00 33.83           O  
ANISOU  117  O   CYS A 447     4642   3552   4659  -1206   -913    745       O  
ATOM    118  CB  CYS A 447     -13.052  11.615 -12.305  1.00 35.72           C  
ANISOU  118  CB  CYS A 447     4859   3845   4866  -1217   -917    777       C  
ATOM    119  SG  CYS A 447     -12.468  12.751 -13.562  1.00 39.02           S  
ANISOU  119  SG  CYS A 447     5296   4254   5278  -1208   -855    724       S  
ATOM    120  N   SER A 448     -10.712   9.704 -13.786  1.00 34.89           N  
ANISOU  120  N   SER A 448     4833   3646   4776  -1217   -904    711       N  
ATOM    121  CA  SER A 448      -9.276   9.413 -13.853  1.00 40.09           C  
ANISOU  121  CA  SER A 448     5503   4277   5453  -1204   -863    668       C  
ATOM    122  C   SER A 448      -8.367  10.565 -13.372  1.00 44.15           C  
ANISOU  122  C   SER A 448     5988   4807   5980  -1182   -792    629       C  
ATOM    123  O   SER A 448      -7.159  10.385 -13.251  1.00 48.15           O  
ANISOU  123  O   SER A 448     6496   5293   6505  -1170   -757    595       O  
ATOM    124  CB  SER A 448      -8.876   8.987 -15.270  1.00 39.30           C  
ANISOU  124  CB  SER A 448     5448   4136   5347  -1211   -859    642       C  
ATOM    125  OG  SER A 448      -9.116  10.025 -16.204  1.00 42.28           O  
ANISOU  125  OG  SER A 448     5833   4521   5710  -1211   -828    622       O  
ATOM    126  N   VAL A 449      -8.937  11.741 -13.118  1.00 41.04           N  
ANISOU  126  N   VAL A 449     5569   4448   5577  -1176   -771    632       N  
ATOM    127  CA  VAL A 449      -8.173  12.841 -12.517  1.00 40.19           C  
ANISOU  127  CA  VAL A 449     5432   4359   5481  -1156   -708    599       C  
ATOM    128  C   VAL A 449      -8.899  13.424 -11.318  1.00 41.85           C  
ANISOU  128  C   VAL A 449     5605   4609   5688  -1154   -715    628       C  
ATOM    129  O   VAL A 449     -10.129  13.342 -11.226  1.00 43.66           O  
ANISOU  129  O   VAL A 449     5829   4856   5903  -1166   -758    669       O  
ATOM    130  CB  VAL A 449      -7.915  13.992 -13.511  1.00 34.68           C  
ANISOU  130  CB  VAL A 449     4740   3661   4777  -1149   -657    560       C  
ATOM    131  CG1 VAL A 449      -7.064  13.511 -14.675  1.00 34.44           C  
ANISOU  131  CG1 VAL A 449     4744   3589   4752  -1150   -640    525       C  
ATOM    132  CG2 VAL A 449      -9.233  14.589 -14.005  1.00 31.09           C  
ANISOU  132  CG2 VAL A 449     4285   3227   4301  -1160   -679    586       C  
ATOM    133  N   THR A 450      -8.137  13.985 -10.386  1.00 37.63           N  
ANISOU  133  N   THR A 450     5044   4089   5166  -1138   -674    608       N  
ATOM    134  CA  THR A 450      -8.731  14.742  -9.292  1.00 39.86           C  
ANISOU  134  CA  THR A 450     5292   4410   5444  -1134   -668    627       C  
ATOM    135  C   THR A 450      -8.688  16.236  -9.583  1.00 38.77           C  
ANISOU  135  C   THR A 450     5140   4289   5302  -1122   -614    596       C  
ATOM    136  O   THR A 450      -9.172  17.039  -8.795  1.00 40.99           O  
ANISOU  136  O   THR A 450     5395   4601   5580  -1117   -601    607       O  
ATOM    137  CB  THR A 450      -8.024  14.480  -7.960  1.00 45.38           C  
ANISOU  137  CB  THR A 450     5970   5116   6156  -1126   -661    628       C  
ATOM    138  OG1 THR A 450      -6.659  14.910  -8.050  1.00 47.41           O  
ANISOU  138  OG1 THR A 450     6226   5360   6428  -1110   -606    579       O  
ATOM    139  CG2 THR A 450      -8.082  12.995  -7.608  1.00 47.43           C  
ANISOU  139  CG2 THR A 450     6242   5359   6422  -1137   -717    661       C  
ATOM    140  N   CYS A 451      -8.081  16.598 -10.708  1.00 35.05           N  
ANISOU  140  N   CYS A 451     4687   3798   4832  -1117   -580    558       N  
ATOM    141  CA  CYS A 451      -8.095  17.969 -11.197  1.00 37.35           C  
ANISOU  141  CA  CYS A 451     4969   4103   5119  -1107   -533    530       C  
ATOM    142  C   CYS A 451      -7.939  17.964 -12.710  1.00 39.51           C  
ANISOU  142  C   CYS A 451     5273   4351   5387  -1111   -526    507       C  
ATOM    143  O   CYS A 451      -7.368  17.031 -13.280  1.00 40.88           O  
ANISOU  143  O   CYS A 451     5474   4494   5566  -1116   -538    498       O  
ATOM    144  CB  CYS A 451      -7.014  18.843 -10.526  1.00 36.89           C  
ANISOU  144  CB  CYS A 451     4887   4054   5075  -1087   -474    490       C  
ATOM    145  SG  CYS A 451      -5.324  18.151 -10.424  1.00 33.14           S  
ANISOU  145  SG  CYS A 451     4420   3548   4623  -1077   -448    454       S  
ATOM    146  N   GLY A 452      -8.448  19.000 -13.363  1.00 35.72           N  
ANISOU  146  N   GLY A 452     4791   3884   4897  -1110   -507    499       N  
ATOM    147  CA  GLY A 452      -8.431  19.033 -14.809  1.00 39.59           C  
ANISOU  147  CA  GLY A 452     5311   4353   5378  -1117   -504    482       C  
ATOM    148  C   GLY A 452      -9.472  18.099 -15.408  1.00 43.51           C  
ANISOU  148  C   GLY A 452     5834   4840   5859  -1139   -568    522       C  
ATOM    149  O   GLY A 452     -10.468  17.761 -14.758  1.00 40.78           O  
ANISOU  149  O   GLY A 452     5477   4511   5507  -1148   -612    566       O  
ATOM    150  N   ASP A 453      -9.239  17.689 -16.654  1.00 46.04           N  
ANISOU  150  N   ASP A 453     6191   5132   6172  -1148   -573    508       N  
ATOM    151  CA  ASP A 453     -10.194  16.869 -17.396  1.00 48.01           C  
ANISOU  151  CA  ASP A 453     6470   5368   6403  -1170   -632    543       C  
ATOM    152  C   ASP A 453      -9.740  15.415 -17.494  1.00 50.37           C  
ANISOU  152  C   ASP A 453     6797   5634   6706  -1179   -664    548       C  
ATOM    153  O   ASP A 453      -8.547  15.128 -17.577  1.00 53.78           O  
ANISOU  153  O   ASP A 453     7238   6043   7154  -1169   -631    513       O  
ATOM    154  CB  ASP A 453     -10.409  17.433 -18.802  1.00 52.19           C  
ANISOU  154  CB  ASP A 453     7025   5888   6916  -1178   -622    527       C  
ATOM    155  CG  ASP A 453     -10.926  18.865 -18.791  1.00 60.26           C  
ANISOU  155  CG  ASP A 453     8020   6941   7934  -1170   -594    523       C  
ATOM    156  OD1 ASP A 453     -11.598  19.262 -17.816  1.00 64.82           O  
ANISOU  156  OD1 ASP A 453     8565   7548   8515  -1166   -603    548       O  
ATOM    157  OD2 ASP A 453     -10.664  19.596 -19.769  1.00 62.12           O  
ANISOU  157  OD2 ASP A 453     8269   7172   8164  -1168   -563    494       O  
ATOM    158  N   GLY A 454     -10.701  14.499 -17.484  1.00 65.84           N  
ANISOU  158  N   GLY A 454    11596   7100   6321  -2688  -1591    744       N  
ATOM    159  CA  GLY A 454     -10.405  13.083 -17.588  1.00 62.77           C  
ANISOU  159  CA  GLY A 454    10971   6876   6003  -2688  -1412    724       C  
ATOM    160  C   GLY A 454     -11.636  12.272 -17.952  1.00 62.33           C  
ANISOU  160  C   GLY A 454    10918   6705   6060  -2451  -1362    638       C  
ATOM    161  O   GLY A 454     -12.674  12.823 -18.334  1.00 59.74           O  
ANISOU  161  O   GLY A 454    10745   6186   5768  -2287  -1472    578       O  
ATOM    162  N   VAL A 455     -11.530  10.954 -17.828  1.00 61.96           N  
ANISOU  162  N   VAL A 455    10651   6804   6087  -2374  -1180    627       N  
ATOM    163  CA  VAL A 455     -12.650  10.097 -18.178  1.00 63.99           C  
ANISOU  163  CA  VAL A 455    10837   7008   6468  -2113  -1104    501       C  
ATOM    164  C   VAL A 455     -13.026   9.083 -17.102  1.00 63.23           C  
ANISOU  164  C   VAL A 455    10556   6976   6492  -1923   -954    398       C  
ATOM    165  O   VAL A 455     -12.171   8.540 -16.401  1.00 65.48           O  
ANISOU  165  O   VAL A 455    10695   7437   6746  -1966   -858    461       O  
ATOM    166  CB  VAL A 455     -12.389   9.348 -19.499  1.00 66.52           C  
ANISOU  166  CB  VAL A 455    11053   7472   6751  -2116   -999    560       C  
ATOM    167  CG1 VAL A 455     -12.152  10.343 -20.625  1.00 70.23           C  
ANISOU  167  CG1 VAL A 455    11768   7843   7073  -2306  -1137    656       C  
ATOM    168  CG2 VAL A 455     -11.202   8.409 -19.351  1.00 65.29           C  
ANISOU  168  CG2 VAL A 455    10627   7618   6563  -2190   -822    647       C  
ATOM    169  N   ILE A 456     -14.327   8.849 -16.977  1.00 57.72           N  
ANISOU  169  N   ILE A 456     9881   6122   5928  -1715   -941    224       N  
ATOM    170  CA  ILE A 456     -14.834   7.701 -16.251  1.00 48.55           C  
ANISOU  170  CA  ILE A 456     8558   5011   4879  -1540   -751    116       C  
ATOM    171  C   ILE A 456     -15.062   6.633 -17.295  1.00 43.83           C  
ANISOU  171  C   ILE A 456     7807   4506   4342  -1429   -628    101       C  
ATOM    172  O   ILE A 456     -15.456   6.948 -18.415  1.00 43.26           O  
ANISOU  172  O   ILE A 456     7801   4360   4275  -1409   -721     80       O  
ATOM    173  CB  ILE A 456     -16.155   8.008 -15.562  1.00 45.51           C  
ANISOU  173  CB  ILE A 456     8254   4414   4622  -1397   -771   -103       C  
ATOM    174  CG1 ILE A 456     -17.200   8.431 -16.597  1.00 44.69           C  
ANISOU  174  CG1 ILE A 456     8206   4156   4619  -1275   -890   -235       C  
ATOM    175  CG2 ILE A 456     -15.960   9.086 -14.503  1.00 45.28           C  
ANISOU  175  CG2 ILE A 456     8380   4293   4533  -1494   -896   -102       C  
ATOM    176  CD1 ILE A 456     -18.548   8.732 -15.999  1.00 30.52           C  
ANISOU  176  CD1 ILE A 456     6310   2273   3013  -1052   -864   -449       C  
ATOM    177  N   THR A 457     -14.799   5.379 -16.936  1.00 41.40           N  
ANISOU  177  N   THR A 457     7317   4347   4067  -1352   -436    112       N  
ATOM    178  CA  THR A 457     -14.854   4.274 -17.888  1.00 40.74           C  
ANISOU  178  CA  THR A 457     7069   4375   4036  -1253   -314    109       C  
ATOM    179  C   THR A 457     -15.641   3.074 -17.351  1.00 41.73           C  
ANISOU  179  C   THR A 457     7083   4476   4298  -1073   -121    -26       C  
ATOM    180  O   THR A 457     -15.616   2.796 -16.153  1.00 40.57           O  
ANISOU  180  O   THR A 457     6954   4313   4146  -1062    -38    -43       O  
ATOM    181  CB  THR A 457     -13.440   3.818 -18.271  1.00 41.13           C  
ANISOU  181  CB  THR A 457     6985   4672   3970  -1368   -272    281       C  
ATOM    182  OG1 THR A 457     -12.723   4.927 -18.829  1.00 50.53           O  
ANISOU  182  OG1 THR A 457     8283   5884   5031  -1573   -416    394       O  
ATOM    183  CG2 THR A 457     -13.492   2.703 -19.296  1.00 39.44           C  
ANISOU  183  CG2 THR A 457     6603   4575   3806  -1261   -153    266       C  
ATOM    184  N   ARG A 458     -16.349   2.380 -18.239  1.00 40.55           N  
ANISOU  184  N   ARG A 458     6837   4309   4260   -942    -51   -127       N  
ATOM    185  CA  ARG A 458     -17.082   1.177 -17.854  1.00 40.82           C  
ANISOU  185  CA  ARG A 458     6759   4318   4431   -794    150   -259       C  
ATOM    186  C   ARG A 458     -16.969   0.109 -18.934  1.00 40.50           C  
ANISOU  186  C   ARG A 458     6555   4396   4437   -705    236   -248       C  
ATOM    187  O   ARG A 458     -16.952   0.417 -20.124  1.00 45.28           O  
ANISOU  187  O   ARG A 458     7153   5025   5025   -705    133   -233       O  
ATOM    188  CB  ARG A 458     -18.547   1.495 -17.522  1.00 42.24           C  
ANISOU  188  CB  ARG A 458     6991   4286   4772   -698    167   -508       C  
ATOM    189  CG  ARG A 458     -19.479   1.651 -18.714  1.00 40.39           C  
ANISOU  189  CG  ARG A 458     6721   3958   4667   -583     77   -668       C  
ATOM    190  CD  ARG A 458     -20.917   1.914 -18.244  1.00 40.24           C  
ANISOU  190  CD  ARG A 458     6709   3742   4838   -478    100   -966       C  
ATOM    191  NE  ARG A 458     -21.854   2.041 -19.362  1.00 39.91           N  
ANISOU  191  NE  ARG A 458     6584   3630   4950   -328    -20  -1140       N  
ATOM    192  CZ  ARG A 458     -23.176   2.113 -19.228  1.00 39.73           C  
ANISOU  192  CZ  ARG A 458     6313   3597   5184   -173    -29  -1368       C  
ATOM    193  NH1 ARG A 458     -23.730   2.060 -18.027  1.00 37.11           N  
ANISOU  193  NH1 ARG A 458     5909   3269   4921   -144     38  -1443       N  
ATOM    194  NH2 ARG A 458     -23.945   2.226 -20.299  1.00 43.32           N  
ANISOU  194  NH2 ARG A 458     6647   4043   5771    -93    -61  -1493       N  
ATOM    195  N   ILE A 459     -16.863  -1.148 -18.521  1.00 35.59           N  
ANISOU  195  N   ILE A 459     5825   3839   3858   -631    416   -251       N  
ATOM    196  CA  ILE A 459     -16.605  -2.218 -19.476  1.00 33.32           C  
ANISOU  196  CA  ILE A 459     5374   3678   3607   -547    493   -231       C  
ATOM    197  C   ILE A 459     -17.634  -3.351 -19.424  1.00 30.75           C  
ANISOU  197  C   ILE A 459     4965   3261   3457   -399    675   -403       C  
ATOM    198  O   ILE A 459     -18.406  -3.462 -18.468  1.00 30.29           O  
ANISOU  198  O   ILE A 459     4972   3062   3476   -384    785   -524       O  
ATOM    199  CB  ILE A 459     -15.177  -2.795 -19.306  1.00 37.37           C  
ANISOU  199  CB  ILE A 459     5804   4400   3993   -598    510    -51       C  
ATOM    200  CG1 ILE A 459     -15.037  -3.516 -17.963  1.00 38.50           C  
ANISOU  200  CG1 ILE A 459     5994   4509   4126   -564    621    -38       C  
ATOM    201  CG2 ILE A 459     -14.128  -1.696 -19.458  1.00 38.49           C  
ANISOU  201  CG2 ILE A 459     5995   4651   3979   -770    350     94       C  
ATOM    202  CD1 ILE A 459     -15.076  -5.033 -18.076  1.00 38.17           C  
ANISOU  202  CD1 ILE A 459     5844   4501   4156   -430    771    -68       C  
ATOM    203  N   ARG A 460     -17.640  -4.169 -20.475  1.00 28.27           N  
ANISOU  203  N   ARG A 460     4509   3028   3203   -307    715   -426       N  
ATOM    204  CA  ARG A 460     -18.481  -5.356 -20.557  1.00 32.15           C  
ANISOU  204  CA  ARG A 460     4901   3452   3865   -176    890   -582       C  
ATOM    205  C   ARG A 460     -17.758  -6.476 -21.322  1.00 33.78           C  
ANISOU  205  C   ARG A 460     4957   3823   4054   -105    939   -502       C  
ATOM    206  O   ARG A 460     -16.757  -6.228 -21.992  1.00 34.13           O  
ANISOU  206  O   ARG A 460     4956   4039   3974   -153    834   -364       O  
ATOM    207  CB  ARG A 460     -19.829  -5.032 -21.207  1.00 36.53           C  
ANISOU  207  CB  ARG A 460     5426   3858   4594    -89    861   -818       C  
ATOM    208  CG  ARG A 460     -19.748  -4.650 -22.665  1.00 41.33           C  
ANISOU  208  CG  ARG A 460     5995   4530   5179    -44    695   -811       C  
ATOM    209  CD  ARG A 460     -21.109  -4.261 -23.220  1.00 47.58           C  
ANISOU  209  CD  ARG A 460     6780   5151   6146     69    617  -1069       C  
ATOM    210  NE  ARG A 460     -20.995  -3.712 -24.571  1.00 54.39           N  
ANISOU  210  NE  ARG A 460     7683   6044   6937    105    414  -1043       N  
ATOM    211  CZ  ARG A 460     -22.026  -3.441 -25.365  1.00 57.85           C  
ANISOU  211  CZ  ARG A 460     8123   6354   7503    238    287  -1256       C  
ATOM    212  NH1 ARG A 460     -23.265  -3.679 -24.957  1.00 57.89           N  
ANISOU  212  NH1 ARG A 460     8040   6284   7670    337    313  -1394       N  
ATOM    213  NH2 ARG A 460     -21.818  -2.942 -26.574  1.00 59.01           N  
ANISOU  213  NH2 ARG A 460     8363   6522   7536    261     93  -1202       N  
ATOM    214  N   LEU A 461     -18.266  -7.701 -21.216  1.00 30.61           N  
ANISOU  214  N   LEU A 461     4043   3133   4455    315    551   -454       N  
ATOM    215  CA  LEU A 461     -17.580  -8.871 -21.749  1.00 34.92           C  
ANISOU  215  CA  LEU A 461     4602   3635   5030    347    472   -608       C  
ATOM    216  C   LEU A 461     -18.507  -9.668 -22.654  1.00 35.25           C  
ANISOU  216  C   LEU A 461     4540   3656   5198    250    447   -705       C  
ATOM    217  O   LEU A 461     -19.720  -9.674 -22.442  1.00 34.78           O  
ANISOU  217  O   LEU A 461     4446   3528   5241    167    513   -640       O  
ATOM    218  CB  LEU A 461     -17.131  -9.778 -20.597  1.00 37.90           C  
ANISOU  218  CB  LEU A 461     5147   3800   5452    420    511   -575       C  
ATOM    219  CG  LEU A 461     -16.267  -9.175 -19.484  1.00 39.56           C  
ANISOU  219  CG  LEU A 461     5480   3996   5556    527    543   -478       C  
ATOM    220  CD1 LEU A 461     -15.998 -10.209 -18.405  1.00 40.00           C  
ANISOU  220  CD1 LEU A 461     5703   3828   5668    601    582   -450       C  
ATOM    221  CD2 LEU A 461     -14.961  -8.652 -20.049  1.00 37.12           C  
ANISOU  221  CD2 LEU A 461     5137   3868   5100    600    457   -571       C  
ATOM    222  N   CYS A 462     -17.964 -10.381 -23.638  1.00 30.08           N  
ANISOU  222  N   CYS A 462     3835   3054   4542    258    354   -868       N  
ATOM    223  CA  CYS A 462     -18.870 -11.191 -24.402  1.00 34.42           C  
ANISOU  223  CA  CYS A 462     4290   3568   5219    166    336   -962       C  
ATOM    224  C   CYS A 462     -18.674 -12.551 -23.768  1.00 37.94           C  
ANISOU  224  C   CYS A 462     4859   3789   5770    189    363   -996       C  
ATOM    225  O   CYS A 462     -18.017 -13.447 -24.314  1.00 35.53           O  
ANISOU  225  O   CYS A 462     4561   3466   5474    218    293  -1131       O  
ATOM    226  CB  CYS A 462     -18.365 -11.188 -25.848  1.00 33.21           C  
ANISOU  226  CB  CYS A 462     4015   3602   5000    167    221  -1121       C  
ATOM    227  SG  CYS A 462     -19.356 -12.044 -27.070  1.00 43.79           S  
ANISOU  227  SG  CYS A 462     5207   4962   6470     61    173  -1271       S  
ATOM    228  N   ASN A 463     -19.314 -12.688 -22.609  1.00 37.60           N  
ANISOU  228  N   ASN A 463     4914   3567   5806    174    472   -869       N  
ATOM    229  CA  ASN A 463     -19.376 -13.916 -21.836  1.00 35.99           C  
ANISOU  229  CA  ASN A 463     4844   3117   5714    188    532   -869       C  
ATOM    230  C   ASN A 463     -20.777 -14.498 -21.630  1.00 39.92           C  
ANISOU  230  C   ASN A 463     5318   3462   6388     72    626   -847       C  
ATOM    231  O   ASN A 463     -20.943 -15.479 -20.915  1.00 44.72           O  
ANISOU  231  O   ASN A 463     6048   3847   7096     76    699   -834       O  
ATOM    232  CB  ASN A 463     -18.586 -13.789 -20.524  1.00 31.60           C  
ANISOU  232  CB  ASN A 463     4470   2451   5085    306    579   -754       C  
ATOM    233  CG  ASN A 463     -19.161 -12.763 -19.589  1.00 36.23           C  
ANISOU  233  CG  ASN A 463     5088   3029   5650    295    670   -575       C  
ATOM    234  OD1 ASN A 463     -20.184 -12.149 -19.875  1.00 41.36           O  
ANISOU  234  OD1 ASN A 463     5628   3745   6342    199    703   -530       O  
ATOM    235  ND2 ASN A 463     -18.508 -12.575 -18.446  1.00 38.47           N  
ANISOU  235  ND2 ASN A 463     5522   3230   5865    399    710   -474       N  
ATOM    236  N   SER A 464     -21.787 -13.849 -22.193  1.00 39.61           N  
ANISOU  236  N   SER A 464     5130   3539   6381    -25    631   -838       N  
ATOM    237  CA  SER A 464     -23.164 -14.137 -21.804  1.00 39.94           C  
ANISOU  237  CA  SER A 464     5148   3448   6579   -133    736   -791       C  
ATOM    238  C   SER A 464     -24.099 -14.475 -22.963  1.00 39.87           C  
ANISOU  238  C   SER A 464     4958   3519   6671   -249    699   -927       C  
ATOM    239  O   SER A 464     -25.114 -13.794 -23.159  1.00 40.38           O  
ANISOU  239  O   SER A 464     4907   3670   6766   -324    726   -888       O  
ATOM    240  CB  SER A 464     -23.747 -12.948 -21.043  1.00 40.02           C  
ANISOU  240  CB  SER A 464     5164   3492   6550   -143    811   -616       C  
ATOM    241  OG  SER A 464     -22.873 -12.513 -20.022  1.00 40.28           O  
ANISOU  241  OG  SER A 464     5349   3478   6477    -34    837   -495       O  
ATOM    242  N   PRO A 465     -23.808 -15.567 -23.683  1.00 34.84           N  
ANISOU  242  N   PRO A 465     4297   2846   6094   -263    644  -1090       N  
ATOM    243  CA  PRO A 465     -22.666 -16.437 -23.416  1.00 40.15           C  
ANISOU  243  CA  PRO A 465     5112   3405   6739   -172    619  -1137       C  
ATOM    244  C   PRO A 465     -21.459 -16.061 -24.258  1.00 44.78           C  
ANISOU  244  C   PRO A 465     5656   4189   7170    -88    483  -1218       C  
ATOM    245  O   PRO A 465     -21.533 -15.156 -25.086  1.00 43.53           O  
ANISOU  245  O   PRO A 465     5362   4250   6929   -103    415  -1241       O  
ATOM    246  CB  PRO A 465     -23.181 -17.807 -23.859  1.00 31.59           C  
ANISOU  246  CB  PRO A 465     4001   2182   5818   -253    638  -1279       C  
ATOM    247  CG  PRO A 465     -24.067 -17.488 -25.011  1.00 37.48           C  
ANISOU  247  CG  PRO A 465     4533   3102   6607   -357    586  -1378       C  
ATOM    248  CD  PRO A 465     -24.723 -16.160 -24.676  1.00 37.43           C  
ANISOU  248  CD  PRO A 465     4469   3207   6547   -376    621  -1237       C  
ATOM    249  N   SER A 466     -20.362 -16.783 -24.065  1.00 47.69           N  
ANISOU  249  N   SER A 466     6143   4478   7500      4    449  -1268       N  
ATOM    250  CA  SER A 466     -19.222 -16.643 -24.944  1.00 49.40           C  
ANISOU  250  CA  SER A 466     6316   4864   7591     74    322  -1375       C  
ATOM    251  C   SER A 466     -19.611 -17.235 -26.282  1.00 53.23           C  
ANISOU  251  C   SER A 466     6650   5430   8146     -7    250  -1549       C  
ATOM    252  O   SER A 466     -20.354 -18.215 -26.329  1.00 55.61           O  
ANISOU  252  O   SER A 466     6943   5588   8598    -85    297  -1611       O  
ATOM    253  CB  SER A 466     -18.019 -17.386 -24.375  1.00 51.09           C  
ANISOU  253  CB  SER A 466     6694   4958   7761    192    307  -1396       C  
ATOM    254  OG  SER A 466     -17.498 -16.709 -23.250  1.00 53.06           O  
ANISOU  254  OG  SER A 466     7067   5178   7917    284    352  -1251       O  
ATOM    255  N   PRO A 467     -19.128 -16.637 -27.381  1.00 53.10           N  
ANISOU  255  N   PRO A 467     6514   5642   8019      9    140  -1632       N  
ATOM    256  CA  PRO A 467     -19.344 -17.274 -28.680  1.00 56.07           C  
ANISOU  256  CA  PRO A 467     6757   6097   8448    -50     59  -1810       C  
ATOM    257  C   PRO A 467     -18.781 -18.690 -28.642  1.00 64.38           C  
ANISOU  257  C   PRO A 467     7901   6985   9574    -25     47  -1917       C  
ATOM    258  O   PRO A 467     -17.757 -18.933 -28.001  1.00 66.06           O  
ANISOU  258  O   PRO A 467     8257   7120   9725     77     46  -1885       O  
ATOM    259  CB  PRO A 467     -18.527 -16.406 -29.637  1.00 51.30           C  
ANISOU  259  CB  PRO A 467     6068   5742   7680      5    -52  -1862       C  
ATOM    260  CG  PRO A 467     -18.435 -15.089 -28.966  1.00 50.16           C  
ANISOU  260  CG  PRO A 467     5959   5674   7427     46     -8  -1701       C  
ATOM    261  CD  PRO A 467     -18.383 -15.373 -27.496  1.00 50.10           C  
ANISOU  261  CD  PRO A 467     6118   5453   7465     81     92  -1572       C  
ATOM    262  N   GLN A 468     -19.531 -19.556 -29.320  1.00 85.93           N  
ANISOU  262  N   GLN A 468    13572   9959   9120    -81   2049  -1545       N  
ATOM    263  CA  GLN A 468     -19.274 -20.968 -29.519  1.00 91.64           C  
ANISOU  263  CA  GLN A 468    14099  10699  10022    -56   2140  -1689       C  
ATOM    264  C   GLN A 468     -18.740 -21.148 -30.933  1.00 93.94           C  
ANISOU  264  C   GLN A 468    14341  11191  10161     26   2139  -1757       C  
ATOM    265  O   GLN A 468     -18.651 -20.190 -31.700  1.00 95.92           O  
ANISOU  265  O   GLN A 468    14704  11564  10178     60   2065  -1691       O  
ATOM    266  CB  GLN A 468     -20.548 -21.787 -29.318  1.00 97.53           C  
ANISOU  266  CB  GLN A 468    14727  11352  10977     19   2137  -1936       C  
ATOM    267  CG  GLN A 468     -20.301 -23.277 -29.170  1.00103.42           C  
ANISOU  267  CG  GLN A 468    15273  12059  11964     18   2234  -2061       C  
ATOM    268  CD  GLN A 468     -19.278 -23.590 -28.097  1.00105.34           C  
ANISOU  268  CD  GLN A 468    15494  12209  12322   -119   2328  -1861       C  
ATOM    269  OE1 GLN A 468     -18.453 -22.746 -27.746  1.00105.37           O  
ANISOU  269  OE1 GLN A 468    15626  12223  12186   -211   2325  -1623       O  
ATOM    270  NE2 GLN A 468     -19.324 -24.808 -27.570  1.00105.74           N  
ANISOU  270  NE2 GLN A 468    15379  12166  12631   -137   2406  -1950       N  
ATOM    271  N   MET A 469     -18.372 -22.376 -31.265  1.00 94.39           N  
ANISOU  271  N   MET A 469    14230  11283  10351     57   2221  -1884       N  
ATOM    272  CA  MET A 469     -17.758 -22.693 -32.548  1.00 96.25           C  
ANISOU  272  CA  MET A 469    14406  11709  10456    135   2241  -1953       C  
ATOM    273  C   MET A 469     -18.545 -22.083 -33.708  1.00 96.64           C  
ANISOU  273  C   MET A 469    14517  11896  10308    256   2135  -2088       C  
ATOM    274  O   MET A 469     -19.694 -22.414 -33.928  1.00 97.38           O  
ANISOU  274  O   MET A 469    14562  11956  10481    339   2084  -2307       O  
ATOM    275  CB  MET A 469     -17.803 -24.208 -32.667  1.00 97.72           C  
ANISOU  275  CB  MET A 469    14394  11867  10869    184   2323  -2165       C  
ATOM    276  CG  MET A 469     -16.916 -24.932 -31.696  1.00 96.56           C  
ANISOU  276  CG  MET A 469    14161  11611  10916     75   2435  -2038       C  
ATOM    277  SD  MET A 469     -17.169 -26.676 -31.927  1.00145.28           S  
ANISOU  277  SD  MET A 469    20100  17738  17361    150   2512  -2316       S  
ATOM    278  CE  MET A 469     -16.356 -26.937 -33.501  1.00 78.48           C  
ANISOU  278  CE  MET A 469    11597   9514   8709    257   2542  -2400       C  
ATOM    279  N   ASN A 470     -17.899 -21.174 -34.426  1.00 96.13           N  
ANISOU  279  N   ASN A 470    14555  11984   9986    258   2099  -1939       N  
ATOM    280  CA  ASN A 470     -18.518 -20.515 -35.563  1.00 96.28           C  
ANISOU  280  CA  ASN A 470    14636  12151   9794    364   1997  -2031       C  
ATOM    281  C   ASN A 470     -19.725 -19.687 -35.149  1.00 91.77           C  
ANISOU  281  C   ASN A 470    14173  11478   9219    374   1891  -2052       C  
ATOM    282  O   ASN A 470     -20.635 -19.464 -35.946  1.00 93.49           O  
ANISOU  282  O   ASN A 470    14400  11771   9351    476   1806  -2208       O  
ATOM    283  CB  ASN A 470     -18.914 -21.536 -36.631  1.00 99.56           C  
ANISOU  283  CB  ASN A 470    14913  12679  10236    494   2008  -2319       C  
ATOM    284  CG  ASN A 470     -17.714 -22.147 -37.325  1.00102.81           C  
ANISOU  284  CG  ASN A 470    15241  13239  10583    512   2102  -2299       C  
ATOM    285  OD1 ASN A 470     -16.571 -21.792 -37.039  1.00104.12           O  
ANISOU  285  OD1 ASN A 470    15447  13433  10682    426   2158  -2058       O  
ATOM    286  ND2 ASN A 470     -17.968 -23.072 -38.244  1.00103.76           N  
ANISOU  286  ND2 ASN A 470    15243  13456  10724    625   2118  -2552       N  
ATOM    287  N   GLY A 471     -19.728 -19.222 -33.904  1.00 85.21           N  
ANISOU  287  N   GLY A 471    13424  10476   8475    269   1897  -1892       N  
ATOM    288  CA  GLY A 471     -20.805 -18.366 -33.445  1.00 79.41           C  
ANISOU  288  CA  GLY A 471    12802   9639   7731    278   1805  -1891       C  
ATOM    289  C   GLY A 471     -20.497 -16.911 -33.725  1.00 74.57           C  
ANISOU  289  C   GLY A 471    12369   9094   6872    251   1720  -1682       C  
ATOM    290  O   GLY A 471     -19.333 -16.527 -33.825  1.00 72.99           O  
ANISOU  290  O   GLY A 471    12218   8964   6550    181   1745  -1478       O  
ATOM    291  N   LYS A 472     -21.537 -16.094 -33.846  1.00 71.38           N  
ANISOU  291  N   LYS A 472    12057   8664   6400    306   1618  -1725       N  
ATOM    292  CA  LYS A 472     -21.344 -14.669 -34.076  1.00 70.08           C  
ANISOU  292  CA  LYS A 472    12066   8545   6017    283   1527  -1529       C  
ATOM    293  C   LYS A 472     -20.753 -14.013 -32.837  1.00 66.13           C  
ANISOU  293  C   LYS A 472    11691   7891   5543    148   1543  -1289       C  
ATOM    294  O   LYS A 472     -21.108 -14.359 -31.716  1.00 66.13           O  
ANISOU  294  O   LYS A 472    11681   7719   5725    100   1586  -1312       O  
ATOM    295  CB  LYS A 472     -22.659 -13.989 -34.476  1.00 73.51           C  
ANISOU  295  CB  LYS A 472    12561   8977   6392    380   1415  -1640       C  
ATOM    296  CG  LYS A 472     -23.196 -14.440 -35.827  1.00 78.50           C  
ANISOU  296  CG  LYS A 472    13092   9784   6952    510   1375  -1852       C  
ATOM    297  CD  LYS A 472     -24.465 -13.695 -36.232  1.00 82.06           C  
ANISOU  297  CD  LYS A 472    13587  10240   7350    597   1250  -1930       C  
ATOM    298  CE  LYS A 472     -24.985 -14.205 -37.579  1.00 85.63           C  
ANISOU  298  CE  LYS A 472    13902  10878   7756    712   1196  -2133       C  
ATOM    299  NZ  LYS A 472     -26.216 -13.501 -38.040  1.00 86.36           N  
ANISOU  299  NZ  LYS A 472    14018  10990   7806    791   1071  -2200       N  
ATOM    300  N   PRO A 473     -19.823 -13.077 -33.038  1.00 63.33           N  
ANISOU  300  N   PRO A 473    11453   7602   5006     81   1507  -1052       N  
ATOM    301  CA  PRO A 473     -19.222 -12.333 -31.930  1.00 60.42           C  
ANISOU  301  CA  PRO A 473    11223   7094   4639    -53   1503   -811       C  
ATOM    302  C   PRO A 473     -20.147 -11.224 -31.454  1.00 56.87           C  
ANISOU  302  C   PRO A 473    10933   6522   4153    -42   1403   -782       C  
ATOM    303  O   PRO A 473     -21.004 -10.767 -32.208  1.00 57.99           O  
ANISOU  303  O   PRO A 473    11097   6727   4207     62   1322   -883       O  
ATOM    304  CB  PRO A 473     -17.978 -11.725 -32.570  1.00 61.78           C  
ANISOU  304  CB  PRO A 473    11450   7409   4615   -108   1483   -585       C  
ATOM    305  CG  PRO A 473     -18.376 -11.512 -33.991  1.00 61.73           C  
ANISOU  305  CG  PRO A 473    11414   7595   4446     16   1421   -690       C  
ATOM    306  CD  PRO A 473     -19.305 -12.638 -34.345  1.00 61.92           C  
ANISOU  306  CD  PRO A 473    11284   7638   4603    129   1462   -994       C  
ATOM    307  N   CYS A 474     -19.973 -10.782 -30.219  1.00 54.49           N  
ANISOU  307  N   CYS A 474    10743   6047   3914   -146   1408   -643       N  
ATOM    308  CA  CYS A 474     -20.736  -9.647 -29.741  1.00 53.64           C  
ANISOU  308  CA  CYS A 474    10803   5818   3760   -138   1316   -596       C  
ATOM    309  C   CYS A 474     -20.410  -8.448 -30.620  1.00 56.64           C  
ANISOU  309  C   CYS A 474    11304   6307   3911   -128   1206   -447       C  
ATOM    310  O   CYS A 474     -19.293  -8.333 -31.123  1.00 57.20           O  
ANISOU  310  O   CYS A 474    11371   6495   3868   -185   1211   -291       O  
ATOM    311  CB  CYS A 474     -20.383  -9.345 -28.291  1.00 52.27           C  
ANISOU  311  CB  CYS A 474    10740   5454   3665   -265   1340   -448       C  
ATOM    312  SG  CYS A 474     -20.819 -10.645 -27.137  1.00 48.41           S  
ANISOU  312  SG  CYS A 474    10120   4827   3446   -284   1463   -597       S  
ATOM    313  N   GLU A 475     -21.377  -7.559 -30.819  1.00 57.71           N  
ANISOU  313  N   GLU A 475    11539   6406   3981    -54   1109   -486       N  
ATOM    314  CA  GLU A 475     -21.131  -6.385 -31.650  1.00 60.26           C  
ANISOU  314  CA  GLU A 475    11975   6826   4095    -42    996   -340       C  
ATOM    315  C   GLU A 475     -21.202  -5.086 -30.861  1.00 56.98           C  
ANISOU  315  C   GLU A 475    11721   6247   3681   -106    900   -166       C  
ATOM    316  O   GLU A 475     -22.061  -4.919 -29.994  1.00 54.32           O  
ANISOU  316  O   GLU A 475    11469   5744   3427    -87    902   -244       O  
ATOM    317  CB  GLU A 475     -22.085  -6.341 -32.841  1.00 67.22           C  
ANISOU  317  CB  GLU A 475    12794   7843   4904    105    936   -509       C  
ATOM    318  CG  GLU A 475     -21.437  -6.763 -34.155  1.00 76.65           C  
ANISOU  318  CG  GLU A 475    13875   9279   5971    143    947   -516       C  
ATOM    319  CD  GLU A 475     -20.277  -5.862 -34.560  1.00 83.86           C  
ANISOU  319  CD  GLU A 475    14820  10282   6759     62    881   -240       C  
ATOM    320  OE1 GLU A 475     -19.495  -6.264 -35.449  1.00 85.29           O  
ANISOU  320  OE1 GLU A 475    14897  10654   6855     69    911   -208       O  
ATOM    321  OE2 GLU A 475     -20.148  -4.754 -33.997  1.00 87.40           O  
ANISOU  321  OE2 GLU A 475    15380  10612   7215     -6    797    -61       O  
ATOM    322  N   GLY A 476     -20.290  -4.168 -31.168  1.00 49.56           N  
ANISOU  322  N   GLY A 476     7866   5596   5371  -1749    252   1996       N  
ATOM    323  CA  GLY A 476     -20.216  -2.899 -30.467  1.00 49.03           C  
ANISOU  323  CA  GLY A 476     7823   5519   5288  -1777    183   1995       C  
ATOM    324  C   GLY A 476     -19.036  -2.823 -29.516  1.00 48.60           C  
ANISOU  324  C   GLY A 476     7743   5467   5257  -1782    178   2026       C  
ATOM    325  O   GLY A 476     -18.290  -3.795 -29.366  1.00 46.44           O  
ANISOU  325  O   GLY A 476     7433   5201   5010  -1763    229   2048       O  
ATOM    326  N   GLU A 477     -18.866  -1.660 -28.886  1.00 49.67           N  
ANISOU  326  N   GLU A 477     7898   5596   5380  -1810    115   2028       N  
ATOM    327  CA  GLU A 477     -17.752  -1.405 -27.976  1.00 54.86           C  
ANISOU  327  CA  GLU A 477     8536   6254   6055  -1823     99   2057       C  
ATOM    328  C   GLU A 477     -17.829  -2.244 -26.705  1.00 55.37           C  
ANISOU  328  C   GLU A 477     8585   6323   6130  -1801    110   2056       C  
ATOM    329  O   GLU A 477     -18.887  -2.366 -26.088  1.00 54.89           O  
ANISOU  329  O   GLU A 477     8544   6259   6054  -1790     92   2027       O  
ATOM    330  CB  GLU A 477     -17.691   0.083 -27.608  1.00 62.52           C  
ANISOU  330  CB  GLU A 477     9534   7215   7007  -1859     25   2056       C  
ATOM    331  CG  GLU A 477     -17.032   0.974 -28.660  1.00 70.10           C  
ANISOU  331  CG  GLU A 477    10498   8170   7966  -1885     18   2074       C  
ATOM    332  CD  GLU A 477     -15.523   0.761 -28.764  1.00 76.04           C  
ANISOU  332  CD  GLU A 477    11214   8929   8748  -1893     49   2115       C  
ATOM    333  OE1 GLU A 477     -14.942   0.113 -27.865  1.00 80.13           O  
ANISOU  333  OE1 GLU A 477    11707   9454   9284  -1883     63   2130       O  
ATOM    334  OE2 GLU A 477     -14.915   1.240 -29.745  1.00 75.29           O  
ANISOU  334  OE2 GLU A 477    11118   8831   8659  -1908     59   2133       O  
ATOM    335  N   ALA A 478     -16.698  -2.822 -26.315  1.00 54.00           N  
ANISOU  335  N   ALA A 478     8377   6158   5982  -1794    142   2087       N  
ATOM    336  CA  ALA A 478     -16.622  -3.568 -25.069  1.00 48.87           C  
ANISOU  336  CA  ALA A 478     7713   5512   5342  -1773    152   2092       C  
ATOM    337  C   ALA A 478     -16.318  -2.622 -23.910  1.00 46.85           C  
ANISOU  337  C   ALA A 478     7470   5253   5078  -1799     86   2099       C  
ATOM    338  O   ALA A 478     -16.270  -3.041 -22.755  1.00 43.71           O  
ANISOU  338  O   ALA A 478     7066   4859   4684  -1786     82   2103       O  
ATOM    339  CB  ALA A 478     -15.571  -4.650 -25.164  1.00 47.66           C  
ANISOU  339  CB  ALA A 478     7520   5369   5220  -1753    217   2122       C  
ATOM    340  N   ARG A 479     -16.110  -1.345 -24.220  1.00 45.90           N  
ANISOU  340  N   ARG A 479     7368   5127   4945  -1835     34   2101       N  
ATOM    341  CA  ARG A 479     -15.964  -0.337 -23.172  1.00 50.90           C  
ANISOU  341  CA  ARG A 479     8017   5756   5567  -1863    -36   2104       C  
ATOM    342  C   ARG A 479     -16.437   1.053 -23.599  1.00 49.80           C  
ANISOU  342  C   ARG A 479     7912   5605   5405  -1895    -95   2087       C  
ATOM    343  O   ARG A 479     -16.421   1.403 -24.777  1.00 50.48           O  
ANISOU  343  O   ARG A 479     8004   5688   5489  -1904    -84   2087       O  
ATOM    344  CB  ARG A 479     -14.522  -0.272 -22.670  1.00 55.33           C  
ANISOU  344  CB  ARG A 479     8551   6325   6149  -1880    -38   2143       C  
ATOM    345  CG  ARG A 479     -13.532   0.222 -23.696  1.00 57.38           C  
ANISOU  345  CG  ARG A 479     8798   6584   6420  -1905    -27   2168       C  
ATOM    346  CD  ARG A 479     -12.112   0.179 -23.152  1.00 61.29           C  
ANISOU  346  CD  ARG A 479     9264   7087   6936  -1921    -26   2206       C  
ATOM    347  NE  ARG A 479     -11.733   1.407 -22.459  1.00 63.87           N  
ANISOU  347  NE  ARG A 479     9603   7409   7254  -1962    -98   2216       N  
ATOM    348  CZ  ARG A 479     -11.562   2.584 -23.061  1.00 67.10           C  
ANISOU  348  CZ  ARG A 479    10027   7809   7658  -1996   -134   2218       C  
ATOM    349  NH1 ARG A 479     -11.758   2.703 -24.371  1.00 67.44           N  
ANISOU  349  NH1 ARG A 479    10078   7847   7701  -1994   -105   2211       N  
ATOM    350  NH2 ARG A 479     -11.204   3.649 -22.352  1.00 67.21           N  
ANISOU  350  NH2 ARG A 479    10051   7818   7667  -2033   -199   2227       N  
ATOM    351  N   GLU A 480     -16.875   1.837 -22.625  1.00 49.29           N  
ANISOU  351  N   GLU A 480     7870   5533   5323  -1911   -159   2074       N  
ATOM    352  CA  GLU A 480     -17.305   3.199 -22.883  1.00 52.14           C  
ANISOU  352  CA  GLU A 480     8266   5883   5664  -1942   -220   2059       C  
ATOM    353  C   GLU A 480     -16.606   4.148 -21.926  1.00 53.48           C  
ANISOU  353  C   GLU A 480     8436   6050   5834  -1975   -280   2077       C  
ATOM    354  O   GLU A 480     -16.187   3.760 -20.828  1.00 51.57           O  
ANISOU  354  O   GLU A 480     8178   5814   5600  -1970   -286   2091       O  
ATOM    355  CB  GLU A 480     -18.820   3.338 -22.719  1.00 51.97           C  
ANISOU  355  CB  GLU A 480     8280   5853   5615  -1931   -245   2016       C  
ATOM    356  CG  GLU A 480     -19.621   2.889 -23.920  1.00 53.43           C  
ANISOU  356  CG  GLU A 480     8474   6036   5791  -1913   -205   1994       C  
ATOM    357  CD  GLU A 480     -21.111   2.796 -23.630  1.00 54.58           C  
ANISOU  357  CD  GLU A 480     8652   6175   5912  -1898   -224   1951       C  
ATOM    358  OE1 GLU A 480     -21.491   2.812 -22.435  1.00 52.11           O  
ANISOU  358  OE1 GLU A 480     8346   5859   5593  -1895   -255   1940       O  
ATOM    359  OE2 GLU A 480     -21.900   2.703 -24.601  1.00 54.55           O  
ANISOU  359  OE2 GLU A 480     8665   6167   5893  -1892   -208   1929       O  
ATOM    360  N   THR A 481     -16.481   5.394 -22.359  1.00 58.56           N  
ANISOU  360  N   THR A 481     9100   6683   6468  -2009   -324   2078       N  
ATOM    361  CA  THR A 481     -15.880   6.443 -21.550  1.00 63.59           C  
ANISOU  361  CA  THR A 481     9741   7315   7105  -2046   -387   2094       C  
ATOM    362  C   THR A 481     -16.798   7.656 -21.535  1.00 69.51           C  
ANISOU  362  C   THR A 481    10534   8050   7829  -2066   -449   2065       C  
ATOM    363  O   THR A 481     -17.734   7.747 -22.330  1.00 70.79           O  
ANISOU  363  O   THR A 481    10719   8204   7973  -2055   -441   2038       O  
ATOM    364  CB  THR A 481     -14.535   6.872 -22.123  1.00 59.93           C  
ANISOU  364  CB  THR A 481     9256   6853   6662  -2074   -377   2131       C  
ATOM    365  OG1 THR A 481     -14.731   7.347 -23.459  1.00 60.37           O  
ANISOU  365  OG1 THR A 481     9327   6900   6712  -2081   -362   2126       O  
ATOM    366  CG2 THR A 481     -13.579   5.697 -22.144  1.00 56.58           C  
ANISOU  366  CG2 THR A 481     8791   6444   6265  -2056   -316   2159       C  
ATOM    367  N   LYS A 482     -16.551   8.577 -20.615  1.00 72.07           N  
ANISOU  367  N   LYS A 482    10867   8368   8148  -2095   -513   2071       N  
ATOM    368  CA  LYS A 482     -17.291   9.824 -20.607  1.00 72.89           C  
ANISOU  368  CA  LYS A 482    11010   8456   8228  -2117   -575   2047       C  
ATOM    369  C   LYS A 482     -16.341  10.949 -20.256  1.00 73.77           C  
ANISOU  369  C   LYS A 482    11120   8561   8348  -2161   -625   2073       C  
ATOM    370  O   LYS A 482     -15.129  10.746 -20.143  1.00 76.17           O  
ANISOU  370  O   LYS A 482    11392   8873   8677  -2174   -608   2109       O  
ATOM    371  CB  LYS A 482     -18.455   9.774 -19.613  1.00 73.69           C  
ANISOU  371  CB  LYS A 482    11137   8554   8309  -2102   -611   2012       C  
ATOM    372  CG  LYS A 482     -19.805   9.411 -20.211  1.00 74.17           C  
ANISOU  372  CG  LYS A 482    11223   8610   8349  -2075   -592   1973       C  
ATOM    373  CD  LYS A 482     -20.878   9.394 -19.116  1.00 76.06           C  
ANISOU  373  CD  LYS A 482    11485   8845   8570  -2063   -630   1940       C  
ATOM    374  CE  LYS A 482     -22.286   9.223 -19.696  1.00 75.78           C  
ANISOU  374  CE  LYS A 482    11480   8802   8510  -2043   -621   1898       C  
ATOM    375  NZ  LYS A 482     -23.339   9.210 -18.638  1.00 75.21           N  
ANISOU  375  NZ  LYS A 482    11431   8724   8420  -2032   -656   1865       N  
ATOM    376  N   ALA A 483     -16.898  12.141 -20.095  1.00 69.65           N  
ANISOU  376  N   ALA A 483     7461   8115  10889  -1791  -2265   1474       N  
ATOM    377  CA  ALA A 483     -16.115  13.296 -19.708  1.00 66.16           C  
ANISOU  377  CA  ALA A 483     6962   7733  10442  -1741  -2147   1421       C  
ATOM    378  C   ALA A 483     -16.340  13.553 -18.233  1.00 58.93           C  
ANISOU  378  C   ALA A 483     5971   6865   9553  -1691  -2061   1449       C  
ATOM    379  O   ALA A 483     -17.482  13.613 -17.773  1.00 56.45           O  
ANISOU  379  O   ALA A 483     5622   6565   9263  -1695  -2062   1530       O  
ATOM    380  CB  ALA A 483     -16.528  14.512 -20.520  1.00 68.67           C  
ANISOU  380  CB  ALA A 483     7269   8074  10749  -1752  -2134   1449       C  
ATOM    381  N   CYS A 484     -15.248  13.672 -17.489  1.00 53.62           N  
ANISOU  381  N   CYS A 484     5272   6221   8881  -1651  -1990   1376       N  
ATOM    382  CA  CYS A 484     -15.327  14.146 -16.120  1.00 52.31           C  
ANISOU  382  CA  CYS A 484     5039   6109   8728  -1608  -1901   1390       C  
ATOM    383  C   CYS A 484     -14.412  15.358 -16.001  1.00 52.12           C  
ANISOU  383  C   CYS A 484     4969   6144   8689  -1570  -1791   1308       C  
ATOM    384  O   CYS A 484     -13.235  15.308 -16.360  1.00 49.54           O  
ANISOU  384  O   CYS A 484     4651   5820   8353  -1567  -1782   1212       O  
ATOM    385  CB  CYS A 484     -14.936  13.053 -15.128  1.00 40.58           C  
ANISOU  385  CB  CYS A 484     3564   4598   7259  -1604  -1939   1391       C  
ATOM    386  SG  CYS A 484     -13.287  12.395 -15.384  1.00 40.58           S  
ANISOU  386  SG  CYS A 484     3588   4567   7263  -1586  -1982   1274       S  
ATOM    387  N   LYS A 485     -14.969  16.456 -15.516  1.00 54.67           N  
ANISOU  387  N   LYS A 485     5241   6514   9017  -1548  -1709   1338       N  
ATOM    388  CA  LYS A 485     -14.199  17.675 -15.373  1.00 57.54           C  
ANISOU  388  CA  LYS A 485     5565   6928   9368  -1522  -1602   1265       C  
ATOM    389  C   LYS A 485     -14.137  18.056 -13.908  1.00 55.54           C  
ANISOU  389  C   LYS A 485     5256   6728   9120  -1484  -1519   1255       C  
ATOM    390  O   LYS A 485     -15.126  17.931 -13.179  1.00 55.35           O  
ANISOU  390  O   LYS A 485     5210   6707   9112  -1482  -1520   1332       O  
ATOM    391  CB  LYS A 485     -14.802  18.801 -16.212  1.00 61.21           C  
ANISOU  391  CB  LYS A 485     6025   7390   9840  -1537  -1585   1304       C  
ATOM    392  CG  LYS A 485     -14.827  18.501 -17.708  1.00 66.46           C  
ANISOU  392  CG  LYS A 485     6754   8004  10494  -1588  -1678   1316       C  
ATOM    393  CD  LYS A 485     -15.487  19.627 -18.501  1.00 69.62           C  
ANISOU  393  CD  LYS A 485     7152   8392  10908  -1608  -1687   1377       C  
ATOM    394  CE  LYS A 485     -16.986  19.717 -18.234  1.00 70.49           C  
ANISOU  394  CE  LYS A 485     7226   8497  11062  -1592  -1734   1489       C  
ATOM    395  NZ  LYS A 485     -17.761  18.629 -18.906  1.00 71.53           N  
ANISOU  395  NZ  LYS A 485     7400   8584  11194  -1629  -1866   1549       N  
ATOM    396  N   LYS A 486     -12.956  18.498 -13.488  1.00 49.47           N  
ANISOU  396  N   LYS A 486     4459   6002   8335  -1464  -1449   1155       N  
ATOM    397  CA  LYS A 486     -12.715  18.922 -12.122  1.00 45.67           C  
ANISOU  397  CA  LYS A 486     3928   5575   7851  -1435  -1375   1130       C  
ATOM    398  C   LYS A 486     -12.043  20.275 -12.193  1.00 43.54           C  
ANISOU  398  C   LYS A 486     3623   5353   7569  -1428  -1266   1045       C  
ATOM    399  O   LYS A 486     -11.611  20.701 -13.263  1.00 39.39           O  
ANISOU  399  O   LYS A 486     3113   4815   7038  -1452  -1255   1003       O  
ATOM    400  CB  LYS A 486     -11.794  17.934 -11.407  1.00 47.26           C  
ANISOU  400  CB  LYS A 486     4125   5781   8052  -1421  -1422   1082       C  
ATOM    401  CG  LYS A 486     -12.327  16.503 -11.317  1.00 51.18           C  
ANISOU  401  CG  LYS A 486     4665   6214   8567  -1440  -1540   1166       C  
ATOM    402  CD  LYS A 486     -13.292  16.332 -10.163  1.00 53.87           C  
ANISOU  402  CD  LYS A 486     4992   6560   8916  -1452  -1534   1261       C  
ATOM    403  CE  LYS A 486     -13.546  14.859  -9.880  1.00 56.88           C  
ANISOU  403  CE  LYS A 486     5417   6876   9317  -1483  -1652   1334       C  
ATOM    404  NZ  LYS A 486     -15.007  14.539  -9.884  1.00 57.72           N  
ANISOU  404  NZ  LYS A 486     5537   6956   9437  -1528  -1670   1445       N  
ATOM    405  N   ASP A 487     -11.947  20.951 -11.056  1.00 46.00           N  
ANISOU  405  N   ASP A 487     3888   5715   7874  -1409  -1187   1020       N  
ATOM    406  CA  ASP A 487     -11.294  22.248 -11.022  1.00 49.64           C  
ANISOU  406  CA  ASP A 487     4316   6219   8324  -1412  -1081    935       C  
ATOM    407  C   ASP A 487      -9.832  22.079 -11.421  1.00 49.90           C  
ANISOU  407  C   ASP A 487     4338   6279   8342  -1423  -1071    809       C  
ATOM    408  O   ASP A 487      -9.274  20.979 -11.335  1.00 50.97           O  
ANISOU  408  O   ASP A 487     4475   6412   8480  -1411  -1145    782       O  
ATOM    409  CB  ASP A 487     -11.413  22.894  -9.637  1.00 52.18           C  
ANISOU  409  CB  ASP A 487     4593   6592   8643  -1396  -1006    924       C  
ATOM    410  CG  ASP A 487     -12.832  23.336  -9.317  1.00 55.09           C  
ANISOU  410  CG  ASP A 487     4952   6942   9038  -1391   -989   1028       C  
ATOM    411  OD1 ASP A 487     -13.639  23.481 -10.263  1.00 53.04           O  
ANISOU  411  OD1 ASP A 487     4713   6637   8805  -1396  -1022   1097       O  
ATOM    412  OD2 ASP A 487     -13.134  23.549  -8.122  1.00 56.23           O  
ANISOU  412  OD2 ASP A 487     5061   7120   9183  -1384   -946   1038       O  
ATOM    413  N   ALA A 488      -9.231  23.170 -11.883  1.00 44.57           N  
ANISOU  413  N   ALA A 488     3647   5627   7660  -1452   -982    732       N  
ATOM    414  CA  ALA A 488      -7.866  23.151 -12.388  1.00 40.30           C  
ANISOU  414  CA  ALA A 488     3083   5119   7110  -1480   -953    601       C  
ATOM    415  C   ALA A 488      -6.878  22.613 -11.363  1.00 40.01           C  
ANISOU  415  C   ALA A 488     2986   5149   7066  -1447   -966    509       C  
ATOM    416  O   ALA A 488      -7.013  22.875 -10.168  1.00 39.74           O  
ANISOU  416  O   ALA A 488     2923   5153   7023  -1422   -945    515       O  
ATOM    417  CB  ALA A 488      -7.460  24.546 -12.827  1.00 42.45           C  
ANISOU  417  CB  ALA A 488     3346   5407   7376  -1533   -836    540       C  
ATOM    418  N   CYS A 489      -5.891  21.856 -11.839  1.00 27.47           N  
ANISOU  418  N   CYS A 489     2638   4036   3763    110   -499   -442       N  
ATOM    419  CA  CYS A 489      -4.788  21.397 -10.993  1.00 30.59           C  
ANISOU  419  CA  CYS A 489     3082   4124   4415    143   -532   -542       C  
ATOM    420  C   CYS A 489      -3.930  22.584 -10.545  1.00 37.24           C  
ANISOU  420  C   CYS A 489     4077   4862   5210    196   -541   -378       C  
ATOM    421  O   CYS A 489      -3.744  23.553 -11.295  1.00 35.62           O  
ANISOU  421  O   CYS A 489     3873   4843   4817    173   -499   -297       O  
ATOM    422  CB  CYS A 489      -3.918  20.366 -11.731  1.00 27.87           C  
ANISOU  422  CB  CYS A 489     2543   3803   4242     25   -481   -875       C  
ATOM    423  SG  CYS A 489      -4.792  18.828 -12.261  1.00 38.03           S  
ANISOU  423  SG  CYS A 489     3622   5174   5655    -76   -429  -1155       S  
ATOM    424  N   PRO A 490      -3.412  22.523  -9.312  1.00 35.05           N  
ANISOU  424  N   PRO A 490     3917   4304   5096    245   -601   -310       N  
ATOM    425  CA  PRO A 490      -2.502  23.574  -8.866  1.00 32.60           C  
ANISOU  425  CA  PRO A 490     3744   3899   4744    262   -601   -192       C  
ATOM    426  C   PRO A 490      -1.371  23.803  -9.861  1.00 31.38           C  
ANISOU  426  C   PRO A 490     3497   3859   4566    201   -564   -320       C  
ATOM    427  O   PRO A 490      -0.907  22.860 -10.495  1.00 29.09           O  
ANISOU  427  O   PRO A 490     3037   3610   4406    133   -549   -546       O  
ATOM    428  CB  PRO A 490      -1.960  23.033  -7.536  1.00 30.28           C  
ANISOU  428  CB  PRO A 490     3514   3342   4651    252   -692   -155       C  
ATOM    429  CG  PRO A 490      -2.506  21.633  -7.403  1.00 31.59           C  
ANISOU  429  CG  PRO A 490     3545   3450   5008    241   -741   -253       C  
ATOM    430  CD  PRO A 490      -3.735  21.587  -8.228  1.00 31.77           C  
ANISOU  430  CD  PRO A 490     3514   3678   4878    264   -676   -296       C  
ATOM    431  N   ILE A 491      -0.979  25.063 -10.018  1.00 30.78           N  
ANISOU  431  N   ILE A 491     3519   3832   4343    216   -530   -187       N  
ATOM    432  CA  ILE A 491       0.185  25.426 -10.809  1.00 32.62           C  
ANISOU  432  CA  ILE A 491     3690   4161   4543    155   -501   -275       C  
ATOM    433  C   ILE A 491       1.219  26.007  -9.852  1.00 28.01           C  
ANISOU  433  C   ILE A 491     3249   3353   4040    173   -537   -188       C  
ATOM    434  O   ILE A 491       0.997  27.062  -9.257  1.00 26.36           O  
ANISOU  434  O   ILE A 491     3200   3074   3740    214   -515     -7       O  
ATOM    435  CB  ILE A 491      -0.176  26.461 -11.895  1.00 37.06           C  
ANISOU  435  CB  ILE A 491     4220   5003   4860    130   -441   -158       C  
ATOM    436  CG1 ILE A 491      -1.153  25.841 -12.900  1.00 36.56           C  
ANISOU  436  CG1 ILE A 491     3989   5226   4677     57   -420   -236       C  
ATOM    437  CG2 ILE A 491       1.084  26.995 -12.592  1.00 22.56           C  
ANISOU  437  CG2 ILE A 491     2341   3260   2969     60   -415   -215       C  
ATOM    438  CD1 ILE A 491      -1.862  26.850 -13.781  1.00 35.14           C  
ANISOU  438  CD1 ILE A 491     3758   5334   4261     27   -397     -3       C  
ATOM    439  N   ASN A 492       2.335  25.305  -9.683  1.00 26.17           N  
ANISOU  439  N   ASN A 492     2940   3000   4003    128   -580   -320       N  
ATOM    440  CA  ASN A 492       3.352  25.725  -8.739  1.00 27.18           C  
ANISOU  440  CA  ASN A 492     3178   2939   4209    113   -638   -223       C  
ATOM    441  C   ASN A 492       4.233  26.844  -9.300  1.00 28.95           C  
ANISOU  441  C   ASN A 492     3449   3248   4303     93   -587   -195       C  
ATOM    442  O   ASN A 492       4.498  26.892 -10.499  1.00 32.77           O  
ANISOU  442  O   ASN A 492     3811   3919   4719     62   -528   -312       O  
ATOM    443  CB  ASN A 492       4.206  24.526  -8.330  1.00 28.73           C  
ANISOU  443  CB  ASN A 492     3233   2964   4720     71   -719   -316       C  
ATOM    444  CG  ASN A 492       3.393  23.432  -7.670  1.00 33.87           C  
ANISOU  444  CG  ASN A 492     3828   3506   5536     83   -783   -301       C  
ATOM    445  OD1 ASN A 492       2.629  23.688  -6.741  1.00 34.38           O  
ANISOU  445  OD1 ASN A 492     4038   3527   5499     95   -825   -142       O  
ATOM    446  ND2 ASN A 492       3.544  22.203  -8.159  1.00 36.88           N  
ANISOU  446  ND2 ASN A 492     3985   3838   6191     68   -772   -484       N  
ATOM    447  N   GLY A 493       4.689  27.739  -8.432  1.00 27.55           N  
ANISOU  447  N   GLY A 493     3440   2949   4078     83   -603    -51       N  
ATOM    448  CA  GLY A 493       5.533  28.837  -8.860  1.00 26.55           C  
ANISOU  448  CA  GLY A 493     3364   2873   3849     63   -556    -11       C  
ATOM    449  C   GLY A 493       6.865  28.395  -9.441  1.00 27.26           C  
ANISOU  449  C   GLY A 493     3318   2982   4059     10   -580   -148       C  
ATOM    450  O   GLY A 493       7.582  27.632  -8.813  1.00 32.57           O  
ANISOU  450  O   GLY A 493     3935   3502   4938    -27   -661   -180       O  
ATOM    451  N   GLY A 494       7.169  28.819 -10.665  1.00 24.85           N  
ANISOU  451  N   GLY A 494     2926   2873   3642     -9   -510   -218       N  
ATOM    452  CA  GLY A 494       8.532  28.781 -11.171  1.00 27.44           C  
ANISOU  452  CA  GLY A 494     3158   3219   4047    -71   -503   -331       C  
ATOM    453  C   GLY A 494       9.220  30.138 -11.038  1.00 29.79           C  
ANISOU  453  C   GLY A 494     3595   3506   4216    -81   -489   -183       C  
ATOM    454  O   GLY A 494       8.553  31.169 -11.120  1.00 31.84           O  
ANISOU  454  O   GLY A 494     3962   3827   4308    -47   -441    -29       O  
ATOM    455  N   TRP A 495      10.546  30.147 -10.889  1.00 28.11           N  
ANISOU  455  N   TRP A 495     3357   3210   4113   -130   -520   -224       N  
ATOM    456  CA  TRP A 495      11.314  31.395 -10.833  1.00 26.10           C  
ANISOU  456  CA  TRP A 495     3219   2951   3747   -156   -502   -107       C  
ATOM    457  C   TRP A 495      11.567  31.907 -12.243  1.00 26.05           C  
ANISOU  457  C   TRP A 495     3109   3193   3595   -187   -423   -159       C  
ATOM    458  O   TRP A 495      11.942  31.138 -13.123  1.00 24.73           O  
ANISOU  458  O   TRP A 495     2756   3161   3479   -240   -393   -357       O  
ATOM    459  CB  TRP A 495      12.684  31.179 -10.178  1.00 24.79           C  
ANISOU  459  CB  TRP A 495     3043   2626   3748   -216   -577   -116       C  
ATOM    460  CG  TRP A 495      12.709  31.066  -8.670  1.00 28.00           C  
ANISOU  460  CG  TRP A 495     3576   2835   4228   -252   -675     16       C  
ATOM    461  CD1 TRP A 495      13.086  29.975  -7.943  1.00 29.53           C  
ANISOU  461  CD1 TRP A 495     3669   2896   4656   -292   -789     25       C  
ATOM    462  CD2 TRP A 495      12.381  32.091  -7.714  1.00 27.76           C  
ANISOU  462  CD2 TRP A 495     3770   2737   4041   -291   -660    162       C  
ATOM    463  NE1 TRP A 495      13.001  30.248  -6.600  1.00 31.06           N  
ANISOU  463  NE1 TRP A 495     4015   2992   4794   -374   -869    191       N  
ATOM    464  CE2 TRP A 495      12.569  31.540  -6.432  1.00 29.86           C  
ANISOU  464  CE2 TRP A 495     4072   2880   4394   -383   -774    242       C  
ATOM    465  CE3 TRP A 495      11.921  33.408  -7.817  1.00 27.67           C  
ANISOU  465  CE3 TRP A 495     3908   2751   3852   -272   -546    232       C  
ATOM    466  CZ2 TRP A 495      12.327  32.267  -5.260  1.00 27.84           C  
ANISOU  466  CZ2 TRP A 495     4014   2567   3995   -489   -766    345       C  
ATOM    467  CZ3 TRP A 495      11.681  34.123  -6.656  1.00 28.05           C  
ANISOU  467  CZ3 TRP A 495     4145   2685   3827   -348   -514    313       C  
ATOM    468  CH2 TRP A 495      11.883  33.550  -5.392  1.00 24.69           C  
ANISOU  468  CH2 TRP A 495     3769   2178   3434   -471   -617    347       C  
ATOM    469  N   GLY A 496      11.385  33.205 -12.465  1.00 25.38           N  
ANISOU  469  N   GLY A 496     3124   3173   3347   -176   -378     16       N  
ATOM    470  CA  GLY A 496      11.849  33.800 -13.709  1.00 25.54           C  
ANISOU  470  CA  GLY A 496     3040   3437   3228   -237   -328     23       C  
ATOM    471  C   GLY A 496      13.352  34.015 -13.605  1.00 28.69           C  
ANISOU  471  C   GLY A 496     3444   3760   3698   -291   -344    -38       C  
ATOM    472  O   GLY A 496      13.953  33.712 -12.569  1.00 23.15           O  
ANISOU  472  O   GLY A 496     2818   2827   3151   -283   -402    -57       O  
ATOM    473  N   PRO A 497      13.974  34.539 -14.670  1.00 28.47           N  
ANISOU  473  N   PRO A 497     3322   3947   3550   -365   -301    -46       N  
ATOM    474  CA  PRO A 497      15.414  34.797 -14.638  1.00 27.31           C  
ANISOU  474  CA  PRO A 497     3170   3739   3468   -418   -309    -98       C  
ATOM    475  C   PRO A 497      15.824  35.912 -13.678  1.00 31.31           C  
ANISOU  475  C   PRO A 497     3878   4030   3987   -388   -332     95       C  
ATOM    476  O   PRO A 497      15.051  36.824 -13.392  1.00 30.81           O  
ANISOU  476  O   PRO A 497     3934   3915   3855   -341   -299    281       O  
ATOM    477  CB  PRO A 497      15.723  35.212 -16.078  1.00 31.70           C  
ANISOU  477  CB  PRO A 497     3580   4629   3837   -522   -247   -123       C  
ATOM    478  CG  PRO A 497      14.406  35.626 -16.659  1.00 29.77           C  
ANISOU  478  CG  PRO A 497     3312   4591   3410   -518   -230     45       C  
ATOM    479  CD  PRO A 497      13.409  34.742 -16.012  1.00 31.45           C  
ANISOU  479  CD  PRO A 497     3556   4676   3720   -438   -252    -20       C  
ATOM    480  N   TRP A 498      17.053  35.824 -13.186  1.00 32.54           N  
ANISOU  480  N   TRP A 498     4052   4055   4257   -430   -374     41       N  
ATOM    481  CA  TRP A 498      17.647  36.888 -12.400  1.00 28.68           C  
ANISOU  481  CA  TRP A 498     3734   3408   3755   -453   -384    185       C  
ATOM    482  C   TRP A 498      17.798  38.132 -13.256  1.00 30.29           C  
ANISOU  482  C   TRP A 498     3942   3749   3819   -470   -312    309       C  
ATOM    483  O   TRP A 498      18.103  38.034 -14.441  1.00 28.24           O  
ANISOU  483  O   TRP A 498     3526   3726   3479   -512   -288    253       O  
ATOM    484  CB  TRP A 498      19.041  36.478 -11.936  1.00 29.87           C  
ANISOU  484  CB  TRP A 498     3849   3455   4047   -521   -456    115       C  
ATOM    485  CG  TRP A 498      19.074  35.410 -10.897  1.00 31.13           C  
ANISOU  485  CG  TRP A 498     3994   3448   4388   -529   -554     84       C  
ATOM    486  CD1 TRP A 498      19.493  34.123 -11.057  1.00 28.16           C  
ANISOU  486  CD1 TRP A 498     3418   3044   4238   -529   -600    -49       C  
ATOM    487  CD2 TRP A 498      18.686  35.541  -9.526  1.00 30.27           C  
ANISOU  487  CD2 TRP A 498     4050   3178   4272   -563   -613    201       C  
ATOM    488  NE1 TRP A 498      19.387  33.443  -9.871  1.00 30.36           N  
ANISOU  488  NE1 TRP A 498     3718   3151   4666   -549   -709     29       N  
ATOM    489  CE2 TRP A 498      18.891  34.289  -8.915  1.00 29.93           C  
ANISOU  489  CE2 TRP A 498     3894   3041   4437   -585   -725    179       C  
ATOM    490  CE3 TRP A 498      18.167  36.590  -8.759  1.00 29.06           C  
ANISOU  490  CE3 TRP A 498     4114   2953   3976   -597   -564    310       C  
ATOM    491  CZ2 TRP A 498      18.599  34.057  -7.571  1.00 30.14           C  
ANISOU  491  CZ2 TRP A 498     4021   2953   4477   -659   -818    296       C  
ATOM    492  CZ3 TRP A 498      17.882  36.357  -7.420  1.00 28.34           C  
ANISOU  492  CZ3 TRP A 498     4133   2746   3889   -681   -625    366       C  
ATOM    493  CH2 TRP A 498      18.104  35.105  -6.841  1.00 28.43           C  
ANISOU  493  CH2 TRP A 498     4034   2715   4055   -721   -765    375       C  
ATOM    494  N   SER A 499      17.601  39.301 -12.655  1.00 24.34           N  
ANISOU  494  N   SER A 499     3349   2850   3048   -461   -266    473       N  
ATOM    495  CA  SER A 499      18.046  40.544 -13.279  1.00 28.49           C  
ANISOU  495  CA  SER A 499     3873   3437   3513   -489   -207    614       C  
ATOM    496  C   SER A 499      19.566  40.556 -13.397  1.00 30.94           C  
ANISOU  496  C   SER A 499     4156   3769   3831   -573   -248    534       C  
ATOM    497  O   SER A 499      20.261  39.811 -12.699  1.00 30.09           O  
ANISOU  497  O   SER A 499     4064   3558   3811   -607   -318    413       O  
ATOM    498  CB  SER A 499      17.625  41.752 -12.443  1.00 28.33           C  
ANISOU  498  CB  SER A 499     4024   3184   3555   -474   -117    762       C  
ATOM    499  OG  SER A 499      18.186  41.664 -11.144  1.00 28.98           O  
ANISOU  499  OG  SER A 499     4264   3062   3687   -542   -138    669       O  
ATOM    500  N   PRO A 500      20.088  41.407 -14.288  1.00 34.61           N  
ANISOU  500  N   PRO A 500     4558   4373   4221   -613   -211    631       N  
ATOM    501  CA  PRO A 500      21.524  41.678 -14.324  1.00 35.40           C  
ANISOU  501  CA  PRO A 500     4654   4466   4332   -693   -234    587       C  
ATOM    502  C   PRO A 500      21.972  42.175 -12.954  1.00 37.33           C  
ANISOU  502  C   PRO A 500     5095   4431   4659   -726   -242    613       C  
ATOM    503  O   PRO A 500      21.213  42.877 -12.285  1.00 37.87           O  
ANISOU  503  O   PRO A 500     5300   4339   4750   -704   -174    705       O  
ATOM    504  CB  PRO A 500      21.634  42.823 -15.335  1.00 34.33           C  
ANISOU  504  CB  PRO A 500     4455   4489   4100   -724   -179    767       C  
ATOM    505  CG  PRO A 500      20.419  42.710 -16.189  1.00 36.56           C  
ANISOU  505  CG  PRO A 500     4618   4978   4295   -690   -158    867       C  
ATOM    506  CD  PRO A 500      19.342  42.189 -15.291  1.00 35.61           C  
ANISOU  506  CD  PRO A 500     4595   4677   4258   -599   -156    829       C  
ATOM    507  N   TRP A 501      23.175  41.816 -12.528  1.00 35.07           N  
ANISOU  507  N   TRP A 501     4806   4096   4423   -800   -313    528       N  
ATOM    508  CA  TRP A 501      23.707  42.383 -11.299  1.00 36.00           C  
ANISOU  508  CA  TRP A 501     5096   4015   4567   -891   -326    568       C  
ATOM    509  C   TRP A 501      23.680  43.905 -11.364  1.00 37.34           C  
ANISOU  509  C   TRP A 501     5376   4114   4699   -917   -209    691       C  
ATOM    510  O   TRP A 501      24.010  44.478 -12.395  1.00 42.75           O  
ANISOU  510  O   TRP A 501     5971   4922   5352   -901   -175    764       O  
ATOM    511  CB  TRP A 501      25.144  41.926 -11.096  1.00 35.43           C  
ANISOU  511  CB  TRP A 501     4956   3949   4556   -982   -427    516       C  
ATOM    512  CG  TRP A 501      25.268  40.531 -10.617  1.00 36.38           C  
ANISOU  512  CG  TRP A 501     4975   4040   4808   -983   -541    440       C  
ATOM    513  CD1 TRP A 501      25.675  39.449 -11.334  1.00 36.14           C  
ANISOU  513  CD1 TRP A 501     4725   4093   4912   -941   -577    325       C  
ATOM    514  CD2 TRP A 501      24.990  40.060  -9.295  1.00 37.10           C  
ANISOU  514  CD2 TRP A 501     5155   4003   4939  -1049   -624    479       C  
ATOM    515  NE1 TRP A 501      25.672  38.328 -10.536  1.00 36.12           N  
ANISOU  515  NE1 TRP A 501     4655   3984   5085   -953   -682    314       N  
ATOM    516  CE2 TRP A 501      25.256  38.680  -9.279  1.00 33.00           C  
ANISOU  516  CE2 TRP A 501     4448   3480   4612  -1025   -730    430       C  
ATOM    517  CE3 TRP A 501      24.550  40.676  -8.119  1.00 40.68           C  
ANISOU  517  CE3 TRP A 501     5813   4354   5292  -1153   -606    542       C  
ATOM    518  CZ2 TRP A 501      25.091  37.904  -8.143  1.00 34.20           C  
ANISOU  518  CZ2 TRP A 501     4602   3538   4854  -1093   -849    500       C  
ATOM    519  CZ3 TRP A 501      24.385  39.902  -6.989  1.00 41.37           C  
ANISOU  519  CZ3 TRP A 501     5918   4388   5413  -1246   -717    578       C  
ATOM    520  CH2 TRP A 501      24.656  38.528  -7.009  1.00 37.17           C  
ANISOU  520  CH2 TRP A 501     5188   3864   5071  -1212   -854    585       C  
ATOM    521  N   ASP A 502      23.279  44.555 -10.273  1.00 38.29           N  
ANISOU  521  N   ASP A 502     5673   4037   4838   -976   -135    707       N  
ATOM    522  CA  ASP A 502      23.427  46.008 -10.151  1.00 39.77           C  
ANISOU  522  CA  ASP A 502     5960   4093   5060  -1031      3    786       C  
ATOM    523  C   ASP A 502      24.908  46.373 -10.105  1.00 38.36           C  
ANISOU  523  C   ASP A 502     5792   3937   4846  -1153    -47    777       C  
ATOM    524  O   ASP A 502      25.739  45.548  -9.724  1.00 39.19           O  
ANISOU  524  O   ASP A 502     5872   4101   4917  -1226   -182    709       O  
ATOM    525  CB  ASP A 502      22.752  46.531  -8.877  1.00 42.55           C  
ANISOU  525  CB  ASP A 502     6492   4223   5452  -1116    130    729       C  
ATOM    526  CG  ASP A 502      21.243  46.460  -8.941  1.00 43.61           C  
ANISOU  526  CG  ASP A 502     6614   4294   5662   -991    222    759       C  
ATOM    527  OD1 ASP A 502      20.707  46.364 -10.056  1.00 43.60           O  
ANISOU  527  OD1 ASP A 502     6467   4409   5690   -846    210    877       O  
ATOM    528  OD2 ASP A 502      20.589  46.504  -7.878  1.00 45.81           O  
ANISOU  528  OD2 ASP A 502     7018   4429   5960  -1060    310    668       O  
ATOM    529  N   ILE A 503      25.231  47.607 -10.485  1.00 55.51           N  
ANISOU  529  N   ILE A 503     4728   5453  10909  -1299  -1301    100       N  
ATOM    530  CA  ILE A 503      26.600  48.122 -10.376  1.00 53.91           C  
ANISOU  530  CA  ILE A 503     4539   5257  10689  -1317  -1326    169       C  
ATOM    531  C   ILE A 503      27.091  48.121  -8.927  1.00 51.80           C  
ANISOU  531  C   ILE A 503     4257   4991  10433  -1303  -1320    193       C  
ATOM    532  O   ILE A 503      26.340  48.421  -8.003  1.00 46.96           O  
ANISOU  532  O   ILE A 503     3639   4371   9835  -1282  -1341    156       O  
ATOM    533  CB  ILE A 503      26.735  49.544 -10.983  1.00 58.02           C  
ANISOU  533  CB  ILE A 503     5096   5763  11185  -1330  -1418    180       C  
ATOM    534  CG1 ILE A 503      25.567  50.440 -10.555  1.00 60.64           C  
ANISOU  534  CG1 ILE A 503     5439   6074  11527  -1305  -1483    126       C  
ATOM    535  CG2 ILE A 503      26.774  49.470 -12.504  1.00 55.88           C  
ANISOU  535  CG2 ILE A 503     4842   5498  10894  -1357  -1417    183       C  
ATOM    536  CD1 ILE A 503      25.735  51.127  -9.216  1.00 60.58           C  
ANISOU  536  CD1 ILE A 503     5431   6059  11527  -1287  -1521    133       C  
ATOM    537  N   CYS A 504      28.359  47.786  -8.730  1.00 52.59           N  
ANISOU  537  N   CYS A 504     4350   5104  10527  -1317  -1292    255       N  
ATOM    538  CA  CYS A 504      28.904  47.685  -7.383  1.00 52.06           C  
ANISOU  538  CA  CYS A 504     4269   5042  10471  -1307  -1282    284       C  
ATOM    539  C   CYS A 504      28.671  48.991  -6.635  1.00 52.99           C  
ANISOU  539  C   CYS A 504     4405   5147  10582  -1298  -1363    275       C  
ATOM    540  O   CYS A 504      28.669  50.057  -7.238  1.00 55.47           O  
ANISOU  540  O   CYS A 504     4747   5450  10879  -1305  -1430    275       O  
ATOM    541  CB  CYS A 504      30.394  47.358  -7.440  1.00 49.48           C  
ANISOU  541  CB  CYS A 504     3936   4728  10135  -1325  -1255    356       C  
ATOM    542  SG  CYS A 504      31.128  46.958  -5.840  1.00 56.99           S  
ANISOU  542  SG  CYS A 504     4865   5688  11102  -1314  -1230    397       S  
ATOM    543  N   SER A 505      28.447  48.907  -5.329  1.00 46.94           N  
ANISOU  543  N   SER A 505     3624   4381   9829  -1282  -1357    265       N  
ATOM    544  CA  SER A 505      28.199  50.097  -4.522  1.00 48.75           C  
ANISOU  544  CA  SER A 505     3868   4600  10053  -1273  -1429    251       C  
ATOM    545  C   SER A 505      29.439  50.994  -4.446  1.00 49.74           C  
ANISOU  545  C   SER A 505     4015   4727  10158  -1289  -1478    314       C  
ATOM    546  O   SER A 505      29.334  52.193  -4.190  1.00 51.58           O  
ANISOU  546  O   SER A 505     4271   4948  10381  -1286  -1551    307       O  
ATOM    547  CB  SER A 505      27.740  49.708  -3.119  1.00 49.96           C  
ANISOU  547  CB  SER A 505     4000   4759  10224  -1259  -1403    226       C  
ATOM    548  OG  SER A 505      28.707  48.904  -2.469  1.00 48.91           O  
ANISOU  548  OG  SER A 505     3847   4641  10093  -1268  -1353    281       O  
ATOM    549  N   VAL A 506      30.607  50.403  -4.669  1.00 47.15           N  
ANISOU  549  N   VAL A 506     3679   4413   9824  -1306  -1439    374       N  
ATOM    550  CA  VAL A 506      31.842  51.156  -4.743  1.00 50.26           C  
ANISOU  550  CA  VAL A 506     4090   4810  10196  -1323  -1479    435       C  
ATOM    551  C   VAL A 506      32.632  50.710  -5.962  1.00 54.45           C  
ANISOU  551  C   VAL A 506     4623   5350  10714  -1345  -1449    471       C  
ATOM    552  O   VAL A 506      32.494  49.574  -6.424  1.00 50.68           O  
ANISOU  552  O   VAL A 506     4125   4881  10250  -1345  -1381    462       O  
ATOM    553  CB  VAL A 506      32.717  50.945  -3.499  1.00 49.88           C  
ANISOU  553  CB  VAL A 506     4027   4775  10152  -1323  -1464    482       C  
ATOM    554  CG1 VAL A 506      31.892  51.130  -2.240  1.00 51.21           C  
ANISOU  554  CG1 VAL A 506     4187   4939  10333  -1306  -1476    442       C  
ATOM    555  CG2 VAL A 506      33.351  49.559  -3.531  1.00 47.87           C  
ANISOU  555  CG2 VAL A 506     3743   4536   9911  -1327  -1381    515       C  
ATOM    556  N   THR A 507      33.461  51.608  -6.485  1.00 59.48           N  
ANISOU  556  N   THR A 507     5285   5987  11326  -1365  -1499    510       N  
ATOM    557  CA  THR A 507      34.321  51.258  -7.603  1.00 61.65           C  
ANISOU  557  CA  THR A 507     5562   6275  11586  -1390  -1472    546       C  
ATOM    558  C   THR A 507      35.525  50.502  -7.068  1.00 61.10           C  
ANISOU  558  C   THR A 507     5468   6223  11523  -1395  -1420    600       C  
ATOM    559  O   THR A 507      36.217  49.796  -7.805  1.00 62.82           O  
ANISOU  559  O   THR A 507     5675   6455  11739  -1411  -1371    625       O  
ATOM    560  CB  THR A 507      34.794  52.510  -8.362  1.00 65.11           C  
ANISOU  560  CB  THR A 507     6039   6708  11992  -1414  -1544    568       C  
ATOM    561  OG1 THR A 507      35.629  53.311  -7.510  1.00 66.69           O  
ANISOU  561  OG1 THR A 507     6248   6909  12182  -1416  -1588    611       O  
ATOM    562  CG2 THR A 507      33.588  53.326  -8.816  1.00 62.59           C  
ANISOU  562  CG2 THR A 507     5745   6367  11668  -1406  -1604    515       C  
ATOM    563  N   CYS A 508      35.769  50.654  -5.772  1.00 61.67           N  
ANISOU  563  N   CYS A 508     5531   6296  11605  -1382  -1431    619       N  
ATOM    564  CA  CYS A 508      36.982  50.123  -5.174  1.00 66.43           C  
ANISOU  564  CA  CYS A 508     6113   6914  12213  -1386  -1396    677       C  
ATOM    565  C   CYS A 508      36.833  49.825  -3.690  1.00 67.66           C  
ANISOU  565  C   CYS A 508     6250   7070  12387  -1368  -1385    680       C  
ATOM    566  O   CYS A 508      36.086  50.498  -2.984  1.00 68.20           O  
ANISOU  566  O   CYS A 508     6329   7129  12454  -1357  -1428    649       O  
ATOM    567  CB  CYS A 508      38.143  51.102  -5.386  1.00 66.61           C  
ANISOU  567  CB  CYS A 508     6158   6943  12208  -1408  -1447    728       C  
ATOM    568  SG  CYS A 508      37.705  52.836  -5.119  1.00 85.65           S  
ANISOU  568  SG  CYS A 508     8610   9337  14596  -1410  -1551    713       S  
ATOM    569  N   GLY A 509      37.597  48.845  -3.218  1.00 66.31           N  
ANISOU  569  N   GLY A 509     6052   6911  12232  -1366  -1329    719       N  
ATOM    570  CA  GLY A 509      37.710  48.581  -1.797  1.00 66.41           C  
ANISOU  570  CA  GLY A 509     6047   6927  12258  -1354  -1321    737       C  
ATOM    571  C   GLY A 509      36.559  47.825  -1.171  1.00 66.66           C  
ANISOU  571  C   GLY A 509     6062   6954  12312  -1336  -1284    689       C  
ATOM    572  O   GLY A 509      36.142  48.150  -0.061  1.00 63.94           O  
ANISOU  572  O   GLY A 509     5716   6608  11968  -1330  -1307    676       O  
ATOM    573  N   GLY A 510      36.078  46.782  -1.842  1.00 53.23           N  
ANISOU  573  N   GLY A 510     6156   7740   6328  -1583  -1214     78       N  
ATOM    574  CA  GLY A 510      35.030  45.967  -1.248  1.00 55.66           C  
ANISOU  574  CA  GLY A 510     6493   8022   6634  -1563  -1238    162       C  
ATOM    575  C   GLY A 510      33.600  46.481  -1.163  1.00 54.62           C  
ANISOU  575  C   GLY A 510     6411   7890   6452  -1563  -1164    232       C  
ATOM    576  O   GLY A 510      33.131  46.833  -0.084  1.00 57.97           O  
ANISOU  576  O   GLY A 510     6894   8308   6823  -1573  -1145    276       O  
ATOM    577  N   GLY A 511      32.938  46.628  -2.303  1.00 50.92           N  
ANISOU  577  N   GLY A 511     5916   7429   6001  -1562  -1118    235       N  
ATOM    578  CA  GLY A 511      31.526  46.955  -2.301  1.00 48.25           C  
ANISOU  578  CA  GLY A 511     5608   7079   5645  -1556  -1063    299       C  
ATOM    579  C   GLY A 511      30.602  45.749  -2.356  1.00 48.80           C  
ANISOU  579  C   GLY A 511     5663   7130   5751  -1535  -1087    348       C  
ATOM    580  O   GLY A 511      31.040  44.593  -2.325  1.00 49.81           O  
ANISOU  580  O   GLY A 511     5759   7248   5917  -1524  -1153    339       O  
ATOM    581  N   VAL A 512      29.304  46.031  -2.440  1.00 43.17           N  
ANISOU  581  N   VAL A 512     4964   6402   5034  -1530  -1036    396       N  
ATOM    582  CA  VAL A 512      28.291  45.004  -2.588  1.00 43.16           C  
ANISOU  582  CA  VAL A 512     4947   6385   5068  -1513  -1047    441       C  
ATOM    583  C   VAL A 512      27.435  45.276  -3.824  1.00 44.10           C  
ANISOU  583  C   VAL A 512     5035   6502   5219  -1509  -1016    454       C  
ATOM    584  O   VAL A 512      27.294  46.430  -4.252  1.00 45.63           O  
ANISOU  584  O   VAL A 512     5237   6696   5403  -1520   -978    450       O  
ATOM    585  CB  VAL A 512      27.361  44.956  -1.375  1.00 45.75           C  
ANISOU  585  CB  VAL A 512     5322   6693   5368  -1518  -1015    487       C  
ATOM    586  CG1 VAL A 512      28.140  44.565  -0.164  1.00 46.43           C  
ANISOU  586  CG1 VAL A 512     5450   6780   5412  -1538  -1060    488       C  
ATOM    587  CG2 VAL A 512      26.698  46.303  -1.155  1.00 51.40           C  
ANISOU  587  CG2 VAL A 512     6061   7402   6069  -1529   -935    486       C  
ATOM    588  N   GLN A 513      26.870  44.214  -4.398  1.00 39.57           N  
ANISOU  588  N   GLN A 513     4427   5923   4686  -1496  -1040    474       N  
ATOM    589  CA  GLN A 513      25.943  44.353  -5.515  1.00 36.58           C  
ANISOU  589  CA  GLN A 513     4021   5541   4336  -1497  -1021    496       C  
ATOM    590  C   GLN A 513      24.802  43.343  -5.400  1.00 37.80           C  
ANISOU  590  C   GLN A 513     4160   5674   4527  -1476  -1024    540       C  
ATOM    591  O   GLN A 513      24.928  42.298  -4.747  1.00 40.10           O  
ANISOU  591  O   GLN A 513     4453   5959   4826  -1465  -1053    547       O  
ATOM    592  CB  GLN A 513      26.656  44.222  -6.864  1.00 35.04           C  
ANISOU  592  CB  GLN A 513     3790   5378   4147  -1524  -1045    453       C  
ATOM    593  CG  GLN A 513      27.306  42.875  -7.093  1.00 37.07           C  
ANISOU  593  CG  GLN A 513     4002   5646   4437  -1520  -1090    413       C  
ATOM    594  CD  GLN A 513      28.088  42.815  -8.388  1.00 40.18           C  
ANISOU  594  CD  GLN A 513     4355   6076   4834  -1563  -1097    345       C  
ATOM    595  OE1 GLN A 513      28.890  41.904  -8.597  1.00 44.52           O  
ANISOU  595  OE1 GLN A 513     4861   6630   5425  -1560  -1121    283       O  
ATOM    596  NE2 GLN A 513      27.855  43.784  -9.271  1.00 35.97           N  
ANISOU  596  NE2 GLN A 513     3841   5561   4266  -1603  -1070    353       N  
ATOM    597  N   LYS A 514      23.693  43.656  -6.054  1.00 34.95           N  
ANISOU  597  N   LYS A 514     3785   5299   4196  -1472  -1002    572       N  
ATOM    598  CA  LYS A 514      22.453  42.964  -5.794  1.00 36.99           C  
ANISOU  598  CA  LYS A 514     4031   5532   4491  -1453   -989    612       C  
ATOM    599  C   LYS A 514      21.747  42.598  -7.087  1.00 38.93           C  
ANISOU  599  C   LYS A 514     4235   5779   4779  -1454  -1008    629       C  
ATOM    600  O   LYS A 514      21.829  43.323  -8.071  1.00 41.68           O  
ANISOU  600  O   LYS A 514     4577   6136   5125  -1475  -1018    628       O  
ATOM    601  CB  LYS A 514      21.562  43.854  -4.931  1.00 38.71           C  
ANISOU  601  CB  LYS A 514     4273   5718   4717  -1449   -931    629       C  
ATOM    602  CG  LYS A 514      20.137  43.390  -4.821  1.00 48.39           C  
ANISOU  602  CG  LYS A 514     5476   6913   5995  -1435   -905    659       C  
ATOM    603  CD  LYS A 514      19.464  44.007  -3.612  1.00 56.73           C  
ANISOU  603  CD  LYS A 514     6556   7943   7055  -1443   -835    651       C  
ATOM    604  CE  LYS A 514      19.262  45.490  -3.792  1.00 62.81           C  
ANISOU  604  CE  LYS A 514     7318   8687   7859  -1442   -805    636       C  
ATOM    605  NZ  LYS A 514      18.248  45.750  -4.852  1.00 67.54           N  
ANISOU  605  NZ  LYS A 514     7867   9251   8544  -1423   -822    661       N  
ATOM    606  N   ARG A 515      21.076  41.453  -7.088  1.00 36.80           N  
ANISOU  606  N   ARG A 515     3941   5500   4542  -1440  -1018    648       N  
ATOM    607  CA  ARG A 515      20.198  41.091  -8.190  1.00 35.06           C  
ANISOU  607  CA  ARG A 515     3680   5277   4363  -1441  -1032    669       C  
ATOM    608  C   ARG A 515      18.959  40.429  -7.634  1.00 33.97           C  
ANISOU  608  C   ARG A 515     3530   5108   4268  -1418  -1009    701       C  
ATOM    609  O   ARG A 515      18.936  40.021  -6.476  1.00 30.21           O  
ANISOU  609  O   ARG A 515     3079   4620   3779  -1410   -988    704       O  
ATOM    610  CB  ARG A 515      20.900  40.183  -9.202  1.00 40.11           C  
ANISOU  610  CB  ARG A 515     4286   5952   5000  -1462  -1072    636       C  
ATOM    611  CG  ARG A 515      21.318  38.814  -8.687  1.00 40.28           C  
ANISOU  611  CG  ARG A 515     4291   5973   5040  -1446  -1094    617       C  
ATOM    612  CD  ARG A 515      22.029  38.038  -9.788  1.00 41.17           C  
ANISOU  612  CD  ARG A 515     4356   6117   5170  -1471  -1125    564       C  
ATOM    613  NE  ARG A 515      22.242  36.644  -9.427  1.00 43.30           N  
ANISOU  613  NE  ARG A 515     4594   6371   5487  -1451  -1155    549       N  
ATOM    614  CZ  ARG A 515      22.562  35.686 -10.291  1.00 44.61           C  
ANISOU  614  CZ  ARG A 515     4712   6542   5693  -1453  -1165    496       C  
ATOM    615  NH1 ARG A 515      22.710  35.971 -11.578  1.00 39.70           N  
ANISOU  615  NH1 ARG A 515     4085   5944   5055  -1471  -1133    449       N  
ATOM    616  NH2 ARG A 515      22.726  34.438  -9.867  1.00 48.16           N  
ANISOU  616  NH2 ARG A 515     5135   6961   6202  -1427  -1196    484       N  
ATOM    617  N   SER A 516      17.918  40.342  -8.450  1.00 25.56           N  
ANISOU  617  N   SER A 516     2848   2799   4065   -312   -704    668       N  
ATOM    618  CA  SER A 516      16.640  39.821  -7.972  1.00 30.94           C  
ANISOU  618  CA  SER A 516     3515   3460   4781   -314   -739    681       C  
ATOM    619  C   SER A 516      15.832  39.105  -9.057  1.00 29.51           C  
ANISOU  619  C   SER A 516     3301   3293   4618   -267   -766    609       C  
ATOM    620  O   SER A 516      16.116  39.241 -10.254  1.00 28.09           O  
ANISOU  620  O   SER A 516     3121   3116   4437   -236   -771    569       O  
ATOM    621  CB  SER A 516      15.811  40.948  -7.337  1.00 33.93           C  
ANISOU  621  CB  SER A 516     3876   3889   5126   -294   -742    650       C  
ATOM    622  OG  SER A 516      15.543  41.974  -8.273  1.00 35.10           O  
ANISOU  622  OG  SER A 516     4009   4069   5259   -244   -746    578       O  
ATOM    623  N   ARG A 517      14.836  38.335  -8.622  1.00 27.07           N  
ANISOU  623  N   ARG A 517     2950   3020   4313   -268   -779    576       N  
ATOM    624  CA  ARG A 517      13.986  37.554  -9.520  1.00 29.43           C  
ANISOU  624  CA  ARG A 517     3196   3359   4628   -247   -792    484       C  
ATOM    625  C   ARG A 517      12.520  37.568  -9.054  1.00 32.79           C  
ANISOU  625  C   ARG A 517     3549   3873   5034   -272   -785    387       C  
ATOM    626  O   ARG A 517      12.222  37.977  -7.933  1.00 36.80           O  
ANISOU  626  O   ARG A 517     4048   4412   5520   -307   -771    396       O  
ATOM    627  CB  ARG A 517      14.487  36.115  -9.595  1.00 30.10           C  
ANISOU  627  CB  ARG A 517     3284   3378   4774   -270   -803    533       C  
ATOM    628  CG  ARG A 517      14.587  35.449  -8.235  1.00 32.71           C  
ANISOU  628  CG  ARG A 517     3616   3670   5143   -325   -819    632       C  
ATOM    629  CD  ARG A 517      15.098  34.022  -8.318  1.00 30.78           C  
ANISOU  629  CD  ARG A 517     3360   3339   4995   -337   -855    708       C  
ATOM    630  NE  ARG A 517      15.380  33.490  -6.990  1.00 32.85           N  
ANISOU  630  NE  ARG A 517     3623   3602   5258   -373   -875    814       N  
ATOM    631  CZ  ARG A 517      15.868  32.271  -6.757  1.00 34.56           C  
ANISOU  631  CZ  ARG A 517     3808   3787   5536   -379   -905    875       C  
ATOM    632  NH1 ARG A 517      16.123  31.451  -7.771  1.00 31.10           N  
ANISOU  632  NH1 ARG A 517     3340   3289   5188   -351   -915    849       N  
ATOM    633  NH2 ARG A 517      16.100  31.875  -5.508  1.00 31.10           N  
ANISOU  633  NH2 ARG A 517     3362   3390   5062   -425   -911    938       N  
ATOM    634  N   LEU A 518      11.612  37.121  -9.914  1.00 26.86           N  
ANISOU  634  N   LEU A 518     2745   3170   4291   -270   -788    288       N  
ATOM    635  CA  LEU A 518      10.199  37.079  -9.568  1.00 27.98           C  
ANISOU  635  CA  LEU A 518     2819   3392   4422   -316   -770    188       C  
ATOM    636  C   LEU A 518       9.708  35.646  -9.600  1.00 27.65           C  
ANISOU  636  C   LEU A 518     2745   3351   4411   -380   -753    145       C  
ATOM    637  O   LEU A 518      10.192  34.847 -10.399  1.00 28.25           O  
ANISOU  637  O   LEU A 518     2828   3369   4537   -365   -777    164       O  
ATOM    638  CB  LEU A 518       9.404  37.901 -10.578  1.00 30.22           C  
ANISOU  638  CB  LEU A 518     3066   3730   4687   -272   -785    110       C  
ATOM    639  CG  LEU A 518       9.758  39.389 -10.625  1.00 29.67           C  
ANISOU  639  CG  LEU A 518     3023   3655   4594   -217   -797    140       C  
ATOM    640  CD1 LEU A 518       9.114  40.065 -11.824  1.00 29.06           C  
ANISOU  640  CD1 LEU A 518     2916   3617   4509   -175   -819     81       C  
ATOM    641  CD2 LEU A 518       9.316  40.039  -9.343  1.00 27.53           C  
ANISOU  641  CD2 LEU A 518     2730   3416   4313   -251   -775    129       C  
ATOM    642  N   CYS A 519       8.730  35.293  -8.775  1.00 27.15           N  
ANISOU  642  N   CYS A 519     2641   3331   4343   -461   -721     88       N  
ATOM    643  CA  CYS A 519       8.195  33.966  -8.969  1.00 24.22           C  
ANISOU  643  CA  CYS A 519     2242   2936   4025   -526   -712     48       C  
ATOM    644  C   CYS A 519       6.940  34.201  -9.774  1.00 26.19           C  
ANISOU  644  C   CYS A 519     2442   3267   4244   -527   -704    -65       C  
ATOM    645  O   CYS A 519       5.824  34.194  -9.267  1.00 27.76           O  
ANISOU  645  O   CYS A 519     2605   3526   4416   -594   -672   -130       O  
ATOM    646  CB  CYS A 519       7.836  33.425  -7.585  1.00 23.62           C  
ANISOU  646  CB  CYS A 519     2164   2863   3948   -628   -669     55       C  
ATOM    647  SG  CYS A 519       6.815  31.922  -7.536  1.00 29.40           S  
ANISOU  647  SG  CYS A 519     2862   3587   4721   -735   -632    -17       S  
ATOM    648  N   ASN A 520       7.158  34.407 -11.061  1.00 29.14           N  
ANISOU  648  N   ASN A 520     2814   3641   4615   -458   -737    -77       N  
ATOM    649  CA  ASN A 520       6.104  34.571 -12.045  1.00 28.50           C  
ANISOU  649  CA  ASN A 520     2690   3620   4517   -452   -748   -159       C  
ATOM    650  C   ASN A 520       6.143  33.599 -13.205  1.00 26.51           C  
ANISOU  650  C   ASN A 520     2427   3346   4299   -452   -765   -193       C  
ATOM    651  O   ASN A 520       5.436  33.784 -14.191  1.00 29.73           O  
ANISOU  651  O   ASN A 520     2807   3808   4681   -440   -780   -247       O  
ATOM    652  CB  ASN A 520       5.960  36.035 -12.491  1.00 29.00           C  
ANISOU  652  CB  ASN A 520     2748   3717   4553   -379   -778   -157       C  
ATOM    653  CG  ASN A 520       7.133  36.520 -13.285  1.00 29.93           C  
ANISOU  653  CG  ASN A 520     2910   3803   4660   -299   -808    -98       C  
ATOM    654  OD1 ASN A 520       8.106  35.795 -13.497  1.00 32.32           O  
ANISOU  654  OD1 ASN A 520     3245   4057   4978   -292   -809    -56       O  
ATOM    655  ND2 ASN A 520       7.046  37.757 -13.752  1.00 28.68           N  
ANISOU  655  ND2 ASN A 520     2753   3665   4480   -244   -832    -93       N  
ATOM    656  N   ASN A 521       7.065  32.650 -13.158  1.00 23.89           N  
ANISOU  656  N   ASN A 521     2115   2925   4036   -460   -771   -152       N  
ATOM    657  CA  ASN A 521       7.347  31.847 -14.341  1.00 22.57           C  
ANISOU  657  CA  ASN A 521     1935   2726   3916   -449   -792   -185       C  
ATOM    658  C   ASN A 521       7.190  30.337 -14.124  1.00 25.75           C  
ANISOU  658  C   ASN A 521     2320   3054   4410   -521   -769   -214       C  
ATOM    659  O   ASN A 521       8.141  29.585 -14.273  1.00 28.24           O  
ANISOU  659  O   ASN A 521     2648   3280   4802   -515   -775   -174       O  
ATOM    660  CB  ASN A 521       8.766  32.159 -14.820  1.00 21.51           C  
ANISOU  660  CB  ASN A 521     1840   2544   3790   -378   -821   -112       C  
ATOM    661  CG  ASN A 521       8.956  31.899 -16.290  1.00 26.54           C  
ANISOU  661  CG  ASN A 521     2458   3200   4427   -351   -845   -163       C  
ATOM    662  OD1 ASN A 521       8.351  32.564 -17.132  1.00 30.33           O  
ANISOU  662  OD1 ASN A 521     2921   3774   4829   -332   -857   -209       O  
ATOM    663  ND2 ASN A 521       9.827  30.947 -16.616  1.00 27.34           N  
ANISOU  663  ND2 ASN A 521     2559   3213   4616   -355   -852   -151       N  
ATOM    664  N   PRO A 522       5.974  29.875 -13.827  1.00 26.61           N  
ANISOU  664  N   PRO A 522     2400   3195   4515   -590   -741   -281       N  
ATOM    665  CA  PRO A 522       4.733  30.642 -13.763  1.00 22.53           C  
ANISOU  665  CA  PRO A 522     1860   2774   3925   -602   -736   -331       C  
ATOM    666  C   PRO A 522       4.477  31.174 -12.368  1.00 25.08           C  
ANISOU  666  C   PRO A 522     2195   3122   4213   -638   -707   -295       C  
ATOM    667  O   PRO A 522       5.240  30.895 -11.448  1.00 27.64           O  
ANISOU  667  O   PRO A 522     2548   3393   4563   -659   -691   -230       O  
ATOM    668  CB  PRO A 522       3.674  29.580 -14.090  1.00 21.90           C  
ANISOU  668  CB  PRO A 522     1748   2689   3883   -668   -718   -415       C  
ATOM    669  CG  PRO A 522       4.227  28.338 -13.482  1.00 22.75           C  
ANISOU  669  CG  PRO A 522     1870   2701   4071   -721   -688   -388       C  
ATOM    670  CD  PRO A 522       5.726  28.424 -13.671  1.00 24.98           C  
ANISOU  670  CD  PRO A 522     2181   2919   4390   -662   -710   -313       C  
ATOM    671  N   THR A 523       3.390  31.925 -12.230  1.00 22.58           N  
ANISOU  671  N   THR A 523     1855   2883   3842   -649   -701   -335       N  
ATOM    672  CA  THR A 523       2.913  32.410 -10.949  1.00 21.74           C  
ANISOU  672  CA  THR A 523     1749   2813   3698   -700   -668   -324       C  
ATOM    673  C   THR A 523       2.117  31.298 -10.273  1.00 25.60           C  
ANISOU  673  C   THR A 523     2227   3286   4213   -806   -633   -355       C  
ATOM    674  O   THR A 523       1.353  30.593 -10.935  1.00 24.80           O  
ANISOU  674  O   THR A 523     2104   3174   4144   -826   -638   -411       O  
ATOM    675  CB  THR A 523       2.005  33.642 -11.159  1.00 24.71           C  
ANISOU  675  CB  THR A 523     2091   3248   4051   -663   -688   -358       C  
ATOM    676  OG1 THR A 523       2.795  34.739 -11.644  1.00 29.47           O  
ANISOU  676  OG1 THR A 523     2707   3853   4638   -568   -721   -320       O  
ATOM    677  CG2 THR A 523       1.334  34.045  -9.863  1.00 20.02           C  
ANISOU  677  CG2 THR A 523     1483   2682   3443   -726   -657   -365       C  
ATOM    678  N   PRO A 524       2.316  31.109  -8.961  1.00 23.78           N  
ANISOU  678  N   PRO A 524     2017   3054   3966   -877   -594   -320       N  
ATOM    679  CA  PRO A 524       1.535  30.060  -8.303  1.00 26.60           C  
ANISOU  679  CA  PRO A 524     2370   3402   4335   -988   -560   -341       C  
ATOM    680  C   PRO A 524       0.035  30.307  -8.539  1.00 33.92           C  
ANISOU  680  C   PRO A 524     3262   4376   5251  -1007   -569   -401       C  
ATOM    681  O   PRO A 524      -0.429  31.444  -8.406  1.00 34.60           O  
ANISOU  681  O   PRO A 524     3326   4506   5314   -975   -582   -413       O  
ATOM    682  CB  PRO A 524       1.905  30.213  -6.821  1.00 21.42           C  
ANISOU  682  CB  PRO A 524     1739   2767   3632  -1062   -516   -297       C  
ATOM    683  CG  PRO A 524       3.261  30.879  -6.835  1.00 20.52           C  
ANISOU  683  CG  PRO A 524     1649   2621   3526   -975   -532   -240       C  
ATOM    684  CD  PRO A 524       3.266  31.773  -8.050  1.00 19.93           C  
ANISOU  684  CD  PRO A 524     1557   2568   3448   -865   -581   -259       C  
ATOM    685  N   GLN A 525      -0.708  29.266  -8.903  1.00 22.73           N  
ANISOU  685  N   GLN A 525     1830   2925   3881  -1046   -566   -444       N  
ATOM    686  CA  GLN A 525      -2.120  29.433  -9.195  1.00 23.28           C  
ANISOU  686  CA  GLN A 525     1863   3019   3963  -1048   -575   -509       C  
ATOM    687  C   GLN A 525      -2.909  28.194  -8.780  1.00 29.63           C  
ANISOU  687  C   GLN A 525     2663   3790   4807  -1136   -550   -534       C  
ATOM    688  O   GLN A 525      -2.348  27.096  -8.659  1.00 29.22           O  
ANISOU  688  O   GLN A 525     2633   3687   4783  -1181   -532   -511       O  
ATOM    689  CB  GLN A 525      -2.335  29.720 -10.687  1.00 29.54           C  
ANISOU  689  CB  GLN A 525     2630   3815   4779   -959   -611   -565       C  
ATOM    690  CG  GLN A 525      -1.673  30.995 -11.179  1.00 37.52           C  
ANISOU  690  CG  GLN A 525     3639   4856   5761   -868   -642   -541       C  
ATOM    691  CD  GLN A 525      -1.711  31.140 -12.689  1.00 40.97           C  
ANISOU  691  CD  GLN A 525     4058   5300   6209   -796   -682   -578       C  
ATOM    692  OE1 GLN A 525      -2.737  31.506 -13.260  1.00 41.83           O  
ANISOU  692  OE1 GLN A 525     4127   5429   6336   -775   -701   -638       O  
ATOM    693  NE2 GLN A 525      -0.582  30.863 -13.343  1.00 39.61           N  
ANISOU  693  NE2 GLN A 525     3911   5108   6031   -761   -697   -547       N  
ATOM    694  N   PHE A 526      -4.212  28.378  -8.571  1.00 28.15           N  
ANISOU  694  N   PHE A 526     2441   3620   4636  -1153   -545   -590       N  
ATOM    695  CA  PHE A 526      -5.082  27.285  -8.159  1.00 28.13           C  
ANISOU  695  CA  PHE A 526     2430   3591   4668  -1231   -520   -617       C  
ATOM    696  C   PHE A 526      -4.453  26.508  -7.004  1.00 30.11           C  
ANISOU  696  C   PHE A 526     2722   3819   4900  -1332   -500   -529       C  
ATOM    697  O   PHE A 526      -4.397  25.288  -7.043  1.00 34.46           O  
ANISOU  697  O   PHE A 526     3283   4322   5488  -1382   -485   -527       O  
ATOM    698  CB  PHE A 526      -5.319  26.330  -9.330  1.00 30.76           C  
ANISOU  698  CB  PHE A 526     2748   3885   5054  -1206   -524   -682       C  
ATOM    699  CG  PHE A 526      -5.756  27.010 -10.597  1.00 35.80           C  
ANISOU  699  CG  PHE A 526     3354   4551   5698  -1116   -554   -751       C  
ATOM    700  CD1 PHE A 526      -5.008  26.896 -11.753  1.00 34.54           C  
ANISOU  700  CD1 PHE A 526     3198   4377   5549  -1057   -579   -761       C  
ATOM    701  CD2 PHE A 526      -6.916  27.759 -10.633  1.00 40.73           C  
ANISOU  701  CD2 PHE A 526     3933   5209   6333  -1092   -555   -817       C  
ATOM    702  CE1 PHE A 526      -5.406  27.508 -12.921  1.00 35.07           C  
ANISOU  702  CE1 PHE A 526     3237   4478   5610   -989   -613   -811       C  
ATOM    703  CE2 PHE A 526      -7.319  28.373 -11.797  1.00 42.03           C  
ANISOU  703  CE2 PHE A 526     4064   5399   6507  -1018   -586   -873       C  
ATOM    704  CZ  PHE A 526      -6.558  28.248 -12.944  1.00 39.58           C  
ANISOU  704  CZ  PHE A 526     3769   5086   6184   -972   -619   -861       C  
ATOM    705  N   GLY A 527      -3.945  27.217  -6.000  1.00 30.69           N  
ANISOU  705  N   GLY A 527     2817   3925   4919  -1364   -500   -458       N  
ATOM    706  CA  GLY A 527      -3.371  26.584  -4.825  1.00 30.56           C  
ANISOU  706  CA  GLY A 527     2842   3904   4865  -1475   -486   -362       C  
ATOM    707  C   GLY A 527      -1.956  26.035  -4.959  1.00 34.48           C  
ANISOU  707  C   GLY A 527     3381   4379   5340  -1484   -456   -327       C  
ATOM    708  O   GLY A 527      -1.426  25.448  -4.011  1.00 33.95           O  
ANISOU  708  O   GLY A 527     3359   4307   5234  -1548   -408   -279       O  
ATOM    709  N   GLY A 528      -1.323  26.222  -6.112  1.00 31.93           N  
ANISOU  709  N   GLY A 528     3049   4026   5057  -1377   -467   -365       N  
ATOM    710  CA  GLY A 528       0.046  25.752  -6.274  1.00 29.52           C  
ANISOU  710  CA  GLY A 528     2771   3660   4785  -1348   -447   -332       C  
ATOM    711  C   GLY A 528       0.996  26.352  -5.245  1.00 32.77           C  
ANISOU  711  C   GLY A 528     3212   4095   5145  -1364   -412   -283       C  
ATOM    712  O   GLY A 528       0.701  27.383  -4.622  1.00 35.03           O  
ANISOU  712  O   GLY A 528     3495   4464   5350  -1382   -405   -288       O  
ATOM    713  N   LYS A 529       2.142  25.705  -5.064  1.00 41.87           N  
ANISOU  713  N   LYS A 529     6015   4449   5443  -2002  -1056   1420       N  
ATOM    714  CA  LYS A 529       3.112  26.127  -4.062  1.00 43.57           C  
ANISOU  714  CA  LYS A 529     6276   4698   5581  -2001  -1129   1519       C  
ATOM    715  C   LYS A 529       3.833  27.417  -4.447  1.00 42.76           C  
ANISOU  715  C   LYS A 529     6079   4704   5463  -1892  -1116   1445       C  
ATOM    716  O   LYS A 529       3.935  27.770  -5.623  1.00 43.15           O  
ANISOU  716  O   LYS A 529     6037   4762   5597  -1779  -1085   1333       O  
ATOM    717  CB  LYS A 529       4.153  25.029  -3.829  1.00 47.99           C  
ANISOU  717  CB  LYS A 529     6911   5109   6215  -1948  -1265   1638       C  
ATOM    718  CG  LYS A 529       3.602  23.676  -3.389  1.00 50.95           C  
ANISOU  718  CG  LYS A 529     7401   5354   6604  -2050  -1289   1728       C  
ATOM    719  CD  LYS A 529       4.677  22.605  -3.553  1.00 55.41           C  
ANISOU  719  CD  LYS A 529     8017   5760   7276  -1952  -1421   1815       C  
ATOM    720  CE  LYS A 529       4.317  21.303  -2.856  1.00 61.07           C  
ANISOU  720  CE  LYS A 529     8863   6366   7976  -2032  -1448   1909       C  
ATOM    721  NZ  LYS A 529       3.092  20.689  -3.433  1.00 63.31           N  
ANISOU  721  NZ  LYS A 529     9144   6614   8298  -2096  -1351   1830       N  
ATOM    722  N   ASP A 530       4.335  28.110  -3.435  1.00 38.37           N  
ANISOU  722  N   ASP A 530     5552   4231   4797  -1930  -1138   1507       N  
ATOM    723  CA  ASP A 530       5.187  29.263  -3.629  1.00 34.09           C  
ANISOU  723  CA  ASP A 530     4937   3782   4232  -1836  -1138   1455       C  
ATOM    724  C   ASP A 530       6.525  28.793  -4.179  1.00 33.74           C  
ANISOU  724  C   ASP A 530     4869   3643   4307  -1694  -1252   1476       C  
ATOM    725  O   ASP A 530       6.881  27.629  -4.055  1.00 34.80           O  
ANISOU  725  O   ASP A 530     5064   3650   4511  -1684  -1344   1563       O  
ATOM    726  CB  ASP A 530       5.393  29.972  -2.293  1.00 38.31           C  
ANISOU  726  CB  ASP A 530     5521   4420   4616  -1929  -1142   1529       C  
ATOM    727  CG  ASP A 530       6.016  31.350  -2.442  1.00 43.84           C  
ANISOU  727  CG  ASP A 530     6148   5242   5268  -1861  -1107   1457       C  
ATOM    728  OD1 ASP A 530       6.030  31.901  -3.568  1.00 42.36           O  
ANISOU  728  OD1 ASP A 530     5873   5078   5144  -1760  -1053   1336       O  
ATOM    729  OD2 ASP A 530       6.485  31.886  -1.415  1.00 48.49           O  
ANISOU  729  OD2 ASP A 530     6771   5904   5749  -1913  -1131   1520       O  
ATOM    730  N   CYS A 531       7.261  29.690  -4.819  1.00 33.99           N  
ANISOU  730  N   CYS A 531     4815   3733   4365  -1582  -1242   1393       N  
ATOM    731  CA  CYS A 531       8.607  29.359  -5.224  1.00 35.80           C  
ANISOU  731  CA  CYS A 531     5018   3891   4694  -1454  -1348   1411       C  
ATOM    732  C   CYS A 531       9.399  29.177  -3.938  1.00 40.11           C  
ANISOU  732  C   CYS A 531     5633   4442   5163  -1498  -1448   1544       C  
ATOM    733  O   CYS A 531       9.074  29.791  -2.913  1.00 42.26           O  
ANISOU  733  O   CYS A 531     5945   4814   5299  -1605  -1413   1584       O  
ATOM    734  CB  CYS A 531       9.215  30.488  -6.065  1.00 30.64           C  
ANISOU  734  CB  CYS A 531     4263   3316   4064  -1342  -1304   1290       C  
ATOM    735  SG  CYS A 531       8.466  30.747  -7.688  1.00 29.29           S  
ANISOU  735  SG  CYS A 531     4007   3135   3985  -1262  -1198   1129       S  
ATOM    736  N   VAL A 532      10.423  28.330  -3.980  1.00 39.53           N  
ANISOU  736  N   VAL A 532     5577   4266   5178  -1415  -1573   1611       N  
ATOM    737  CA  VAL A 532      11.336  28.185  -2.848  1.00 43.64           C  
ANISOU  737  CA  VAL A 532     6153   4794   5633  -1431  -1682   1729       C  
ATOM    738  C   VAL A 532      12.657  28.909  -3.110  1.00 43.82           C  
ANISOU  738  C   VAL A 532     6092   4877   5680  -1315  -1731   1682       C  
ATOM    739  O   VAL A 532      13.352  28.624  -4.085  1.00 44.07           O  
ANISOU  739  O   VAL A 532     6061   4843   5840  -1187  -1771   1627       O  
ATOM    740  CB  VAL A 532      11.617  26.706  -2.523  1.00 49.79           C  
ANISOU  740  CB  VAL A 532     7023   5420   6476  -1421  -1800   1851       C  
ATOM    741  CG1 VAL A 532      12.124  25.976  -3.755  1.00 51.84           C  
ANISOU  741  CG1 VAL A 532     7230   5557   6908  -1281  -1847   1801       C  
ATOM    742  CG2 VAL A 532      12.621  26.595  -1.384  1.00 51.46           C  
ANISOU  742  CG2 VAL A 532     7287   5647   6618  -1421  -1920   1969       C  
ATOM    743  N   GLY A 533      12.973  29.891  -2.278  1.00 44.62           N  
ANISOU  743  N   GLY A 533     6189   5107   5657  -1365  -1716   1693       N  
ATOM    744  CA  GLY A 533      14.264  30.547  -2.372  1.00 45.65           C  
ANISOU  744  CA  GLY A 533     6247   5300   5797  -1272  -1767   1655       C  
ATOM    745  C   GLY A 533      14.240  32.033  -2.068  1.00 47.30           C  
ANISOU  745  C   GLY A 533     6414   5671   5887  -1320  -1673   1585       C  
ATOM    746  O   GLY A 533      13.206  32.592  -1.689  1.00 47.94           O  
ANISOU  746  O   GLY A 533     6525   5822   5867  -1428  -1570   1573       O  
ATOM    747  N   ASP A 534      15.384  32.679  -2.275  1.00 46.03           N  
ANISOU  747  N   ASP A 534     6181   5569   5741  -1237  -1703   1532       N  
ATOM    748  CA  ASP A 534      15.509  34.114  -2.061  1.00 44.88           C  
ANISOU  748  CA  ASP A 534     5994   5572   5488  -1272  -1614   1457       C  
ATOM    749  C   ASP A 534      14.998  34.856  -3.280  1.00 37.52           C  
ANISOU  749  C   ASP A 534     4996   4659   4600  -1224  -1485   1312       C  
ATOM    750  O   ASP A 534      15.277  34.466  -4.413  1.00 34.43           O  
ANISOU  750  O   ASP A 534     4553   4187   4342  -1115  -1496   1247       O  
ATOM    751  CB  ASP A 534      16.976  34.495  -1.839  1.00 51.33           C  
ANISOU  751  CB  ASP A 534     6757   6442   6305  -1204  -1695   1449       C  
ATOM    752  CG  ASP A 534      17.622  33.719  -0.707  1.00 60.31           C  
ANISOU  752  CG  ASP A 534     7951   7557   7406  -1226  -1840   1590       C  
ATOM    753  OD1 ASP A 534      18.686  33.104  -0.944  1.00 63.14           O  
ANISOU  753  OD1 ASP A 534     8275   7858   7858  -1121  -1956   1607       O  
ATOM    754  OD2 ASP A 534      17.071  33.728   0.418  1.00 62.86           O  
ANISOU  754  OD2 ASP A 534     8355   7921   7608  -1347  -1838   1681       O  
ATOM    755  N   VAL A 535      14.258  35.932  -3.049  1.00 36.86           N  
ANISOU  755  N   VAL A 535     4918   4683   4402  -1303  -1362   1260       N  
ATOM    756  CA  VAL A 535      13.884  36.834  -4.123  1.00 37.14           C  
ANISOU  756  CA  VAL A 535     4896   4757   4457  -1252  -1237   1118       C  
ATOM    757  C   VAL A 535      15.094  37.672  -4.544  1.00 35.64           C  
ANISOU  757  C   VAL A 535     4637   4622   4283  -1167  -1235   1034       C  
ATOM    758  O   VAL A 535      15.172  38.164  -5.675  1.00 34.06           O  
ANISOU  758  O   VAL A 535     4382   4415   4144  -1082  -1166    916       O  
ATOM    759  CB  VAL A 535      12.716  37.754  -3.701  1.00 42.73           C  
ANISOU  759  CB  VAL A 535     5637   5566   5032  -1358  -1105   1089       C  
ATOM    760  CG1 VAL A 535      12.833  39.107  -4.366  1.00 45.97           C  
ANISOU  760  CG1 VAL A 535     5996   6064   5407  -1312   -989    955       C  
ATOM    761  CG2 VAL A 535      11.372  37.108  -4.040  1.00 40.62           C  
ANISOU  761  CG2 VAL A 535     5399   5239   4796  -1396  -1058   1092       C  
ATOM    762  N   THR A 536      16.051  37.809  -3.636  1.00 36.62           N  
ANISOU  762  N   THR A 536     4765   4799   4350  -1191  -1313   1095       N  
ATOM    763  CA  THR A 536      17.214  38.651  -3.893  1.00 40.46           C  
ANISOU  763  CA  THR A 536     5186   5352   4835  -1129  -1309   1015       C  
ATOM    764  C   THR A 536      18.536  38.000  -3.499  1.00 39.56           C  
ANISOU  764  C   THR A 536     5047   5212   4773  -1076  -1460   1077       C  
ATOM    765  O   THR A 536      18.603  37.206  -2.567  1.00 39.36           O  
ANISOU  765  O   THR A 536     5072   5161   4723  -1121  -1563   1202       O  
ATOM    766  CB  THR A 536      17.100  40.004  -3.178  1.00 43.75           C  
ANISOU  766  CB  THR A 536     5617   5914   5092  -1220  -1212    982       C  
ATOM    767  OG1 THR A 536      15.856  40.618  -3.517  1.00 46.13           O  
ANISOU  767  OG1 THR A 536     5943   6242   5341  -1263  -1074    924       O  
ATOM    768  CG2 THR A 536      18.219  40.922  -3.616  1.00 46.83           C  
ANISOU  768  CG2 THR A 536     5940   6368   5487  -1157  -1186    879       C  
ATOM    769  N   GLU A 537      19.585  38.347  -4.234  1.00 37.43           N  
ANISOU  769  N   GLU A 537     4699   4951   4574   -978  -1469    985       N  
ATOM    770  CA  GLU A 537      20.936  37.906  -3.927  1.00 37.83           C  
ANISOU  770  CA  GLU A 537     4706   4997   4669   -919  -1603   1020       C  
ATOM    771  C   GLU A 537      21.861  39.094  -3.862  1.00 35.48           C  
ANISOU  771  C   GLU A 537     4350   4821   4310   -916  -1558    928       C  
ATOM    772  O   GLU A 537      21.740  40.040  -4.640  1.00 36.44           O  
ANISOU  772  O   GLU A 537     4440   4979   4425   -899  -1435    806       O  
ATOM    773  CB  GLU A 537      21.452  36.971  -5.010  1.00 37.54           C  
ANISOU  773  CB  GLU A 537     4620   4836   4809   -786  -1674    990       C  
ATOM    774  CG  GLU A 537      21.453  35.527  -4.635  1.00 37.33           C  
ANISOU  774  CG  GLU A 537     4636   4698   4850   -765  -1811   1117       C  
ATOM    775  CD  GLU A 537      21.758  34.650  -5.819  1.00 39.64           C  
ANISOU  775  CD  GLU A 537     4884   4859   5316   -638  -1856   1077       C  
ATOM    776  OE1 GLU A 537      22.182  35.190  -6.866  1.00 36.27           O  
ANISOU  776  OE1 GLU A 537     4383   4439   4957   -562  -1796    949       O  
ATOM    777  OE2 GLU A 537      21.559  33.423  -5.709  1.00 46.49           O  
ANISOU  777  OE2 GLU A 537     5797   5614   6252   -618  -1948   1171       O  
ATOM    778  N   ASN A 538      22.798  39.032  -2.935  1.00 37.98           N  
ANISOU  778  N   ASN A 538     4653   5199   4577   -933  -1659    986       N  
ATOM    779  CA  ASN A 538      23.847  40.019  -2.862  1.00 40.64           C  
ANISOU  779  CA  ASN A 538     4925   5649   4869   -926  -1636    899       C  
ATOM    780  C   ASN A 538      25.180  39.310  -2.970  1.00 41.79           C  
ANISOU  780  C   ASN A 538     4999   5765   5114   -825  -1781    906       C  
ATOM    781  O   ASN A 538      25.274  38.124  -2.672  1.00 39.83           O  
ANISOU  781  O   ASN A 538     4775   5434   4926   -788  -1911   1012       O  
ATOM    782  CB  ASN A 538      23.762  40.780  -1.539  1.00 45.15           C  
ANISOU  782  CB  ASN A 538     5539   6352   5266  -1053  -1615    950       C  
ATOM    783  CG  ASN A 538      22.464  41.556  -1.397  1.00 45.73           C  
ANISOU  783  CG  ASN A 538     5678   6463   5233  -1154  -1467    936       C  
ATOM    784  OD1 ASN A 538      22.418  42.767  -1.626  1.00 46.30           O  
ANISOU  784  OD1 ASN A 538     5737   6619   5236  -1185  -1339    834       O  
ATOM    785  ND2 ASN A 538      21.404  40.861  -1.013  1.00 45.56           N  
ANISOU  785  ND2 ASN A 538     5732   6381   5198  -1206  -1481   1035       N  
ATOM    786  N   GLN A 539      26.209  40.032  -3.408  1.00 43.06           N  
ANISOU  786  N   GLN A 539     5076   5994   5292   -779  -1756    791       N  
ATOM    787  CA  GLN A 539      27.569  39.504  -3.361  1.00 43.46           C  
ANISOU  787  CA  GLN A 539     5049   6049   5417   -693  -1893    789       C  
ATOM    788  C   GLN A 539      28.598  40.638  -3.372  1.00 42.60           C  
ANISOU  788  C   GLN A 539     4860   6070   5255   -702  -1842    668       C  
ATOM    789  O   GLN A 539      28.306  41.757  -3.811  1.00 38.68           O  
ANISOU  789  O   GLN A 539     4364   5628   4705   -744  -1691    563       O  
ATOM    790  CB  GLN A 539      27.824  38.543  -4.526  1.00 43.70           C  
ANISOU  790  CB  GLN A 539     5035   5940   5628   -559  -1946    758       C  
ATOM    791  CG  GLN A 539      27.879  39.227  -5.881  1.00 45.49           C  
ANISOU  791  CG  GLN A 539     5208   6150   5926   -505  -1819    600       C  
ATOM    792  CD  GLN A 539      28.263  38.281  -6.999  1.00 45.93           C  
ANISOU  792  CD  GLN A 539     5214   6077   6161   -372  -1880    566       C  
ATOM    793  OE1 GLN A 539      28.295  37.065  -6.810  1.00 48.28           O  
ANISOU  793  OE1 GLN A 539     5529   6282   6534   -323  -2007    667       O  
ATOM    794  NE2 GLN A 539      28.555  38.835  -8.173  1.00 42.45           N  
ANISOU  794  NE2 GLN A 539     4716   5625   5788   -314  -1787    423       N  
ATOM    795  N   ILE A 540      29.803  40.340  -2.898  1.00 38.70           N  
ANISOU  795  N   ILE A 540     4301   5627   4775   -661  -1968    681       N  
ATOM    796  CA  ILE A 540      30.869  41.320  -2.898  1.00 40.90           C  
ANISOU  796  CA  ILE A 540     4496   6033   5012   -669  -1932    563       C  
ATOM    797  C   ILE A 540      31.245  41.659  -4.331  1.00 41.72           C  
ANISOU  797  C   ILE A 540     4530   6091   5229   -585  -1845    409       C  
ATOM    798  O   ILE A 540      30.981  40.891  -5.258  1.00 41.66           O  
ANISOU  798  O   ILE A 540     4521   5955   5355   -496  -1863    406       O  
ATOM    799  CB  ILE A 540      32.118  40.799  -2.171  1.00 43.90           C  
ANISOU  799  CB  ILE A 540     4808   6473   5400   -625  -2100    604       C  
ATOM    800  CG1 ILE A 540      32.789  39.708  -3.002  1.00 45.15           C  
ANISOU  800  CG1 ILE A 540     4900   6520   5735   -476  -2212    591       C  
ATOM    801  CG2 ILE A 540      31.744  40.267  -0.811  1.00 45.18           C  
ANISOU  801  CG2 ILE A 540     5048   6655   5463   -691  -2203    769       C  
ATOM    802  CD1 ILE A 540      34.107  39.253  -2.454  1.00 50.58           C  
ANISOU  802  CD1 ILE A 540     5504   7270   6442   -413  -2371    606       C  
ATOM    803  N   CYS A 541      31.842  42.829  -4.506  1.00 41.63           N  
ANISOU  803  N   CYS A 541     4470   6188   5160   -621  -1745    280       N  
ATOM    804  CA  CYS A 541      32.368  43.228  -5.796  1.00 40.70           C  
ANISOU  804  CA  CYS A 541     4285   6042   5139   -548  -1663    124       C  
ATOM    805  C   CYS A 541      33.514  44.202  -5.566  1.00 40.64           C  
ANISOU  805  C   CYS A 541     4199   6174   5066   -583  -1628     10       C  
ATOM    806  O   CYS A 541      33.553  44.879  -4.536  1.00 38.87           O  
ANISOU  806  O   CYS A 541     3998   6071   4700   -687  -1610     35       O  
ATOM    807  CB  CYS A 541      31.274  43.881  -6.628  1.00 39.72           C  
ANISOU  807  CB  CYS A 541     4228   5863   5000   -572  -1491     64       C  
ATOM    808  SG  CYS A 541      30.320  45.097  -5.707  1.00 40.69           S  
ANISOU  808  SG  CYS A 541     4448   6094   4920   -728  -1356     89       S  
ATOM    809  N   ASN A 542      34.443  44.257  -6.520  1.00 56.47           N  
ANISOU  809  N   ASN A 542     4320   8936   8199  -2307   -757   1198       N  
ATOM    810  CA  ASN A 542      35.583  45.163  -6.448  1.00 55.43           C  
ANISOU  810  CA  ASN A 542     4295   8871   7893  -2326   -825   1320       C  
ATOM    811  C   ASN A 542      36.298  45.111  -5.108  1.00 56.78           C  
ANISOU  811  C   ASN A 542     4545   9004   8023  -2361   -763   1445       C  
ATOM    812  O   ASN A 542      36.583  46.154  -4.521  1.00 54.68           O  
ANISOU  812  O   ASN A 542     4367   8752   7657  -2389   -802   1540       O  
ATOM    813  CB  ASN A 542      35.133  46.597  -6.708  1.00 48.65           C  
ANISOU  813  CB  ASN A 542     3480   8050   6953  -2334   -919   1332       C  
ATOM    814  CG  ASN A 542      34.556  46.782  -8.089  1.00 56.20           C  
ANISOU  814  CG  ASN A 542     4375   9053   7924  -2294   -997   1219       C  
ATOM    815  OD1 ASN A 542      34.886  46.042  -9.017  1.00 56.04           O  
ANISOU  815  OD1 ASN A 542     4306   9066   7921  -2263  -1005   1158       O  
ATOM    816  ND2 ASN A 542      33.687  47.775  -8.236  1.00 54.82           N  
ANISOU  816  ND2 ASN A 542     4205   8882   7740  -2293  -1057   1188       N  
ATOM    817  N   LYS A 543      36.592  43.909  -4.621  1.00 62.46           N  
ANISOU  817  N   LYS A 543     5238   9676   8818  -2357   -670   1444       N  
ATOM    818  CA  LYS A 543      37.192  43.781  -3.293  1.00 67.59           C  
ANISOU  818  CA  LYS A 543     5963  10279   9439  -2385   -606   1555       C  
ATOM    819  C   LYS A 543      38.645  44.261  -3.216  1.00 70.04           C  
ANISOU  819  C   LYS A 543     6364  10657   9592  -2397   -665   1672       C  
ATOM    820  O   LYS A 543      39.204  44.350  -2.128  1.00 69.73           O  
ANISOU  820  O   LYS A 543     6397  10587   9509  -2420   -634   1772       O  
ATOM    821  CB  LYS A 543      37.046  42.359  -2.730  1.00 68.60           C  
ANISOU  821  CB  LYS A 543     6041  10328   9695  -2377   -484   1521       C  
ATOM    822  CG  LYS A 543      37.916  41.302  -3.385  1.00 70.79           C  
ANISOU  822  CG  LYS A 543     6282  10642   9973  -2352   -474   1498       C  
ATOM    823  CD  LYS A 543      37.802  39.979  -2.635  1.00 72.56           C  
ANISOU  823  CD  LYS A 543     6474  10781  10313  -2349   -349   1481       C  
ATOM    824  CE  LYS A 543      38.503  38.843  -3.369  1.00 73.54           C  
ANISOU  824  CE  LYS A 543     6547  10937  10458  -2322   -335   1439       C  
ATOM    825  NZ  LYS A 543      38.229  37.526  -2.728  1.00 73.19           N  
ANISOU  825  NZ  LYS A 543     6463  10806  10540  -2318   -210   1407       N  
ATOM    826  N   GLN A 544      39.247  44.581  -4.360  1.00 74.66           N  
ANISOU  826  N   GLN A 544     6946  11330  10093  -2381   -750   1659       N  
ATOM    827  CA  GLN A 544      40.610  45.111  -4.388  1.00 80.85           C  
ANISOU  827  CA  GLN A 544     7809  12180  10730  -2394   -809   1764       C  
ATOM    828  C   GLN A 544      40.662  46.486  -3.718  1.00 86.61           C  
ANISOU  828  C   GLN A 544     8633  12917  11359  -2429   -862   1857       C  
ATOM    829  O   GLN A 544      39.655  47.186  -3.661  1.00 87.74           O  
ANISOU  829  O   GLN A 544     8772  13040  11526  -2437   -881   1826       O  
ATOM    830  CB  GLN A 544      41.123  45.214  -5.828  1.00 82.52           C  
ANISOU  830  CB  GLN A 544     7996  12478  10879  -2369   -881   1723       C  
ATOM    831  CG  GLN A 544      40.677  46.473  -6.575  1.00 85.06           C  
ANISOU  831  CG  GLN A 544     8340  12849  11129  -2371   -973   1705       C  
ATOM    832  CD  GLN A 544      39.212  46.439  -6.999  1.00 87.66           C  
ANISOU  832  CD  GLN A 544     8594  13146  11567  -2352   -971   1587       C  
ATOM    833  OE1 GLN A 544      38.676  45.386  -7.352  1.00 88.51           O  
ANISOU  833  OE1 GLN A 544     8613  13222  11794  -2325   -921   1490       O  
ATOM    834  NE2 GLN A 544      38.560  47.599  -6.968  1.00 87.46           N  
ANISOU  834  NE2 GLN A 544     8602  13127  11502  -2364  -1028   1592       N  
ATOM    835  N   ASP A 545      41.830  46.868  -3.206  1.00 90.60           N  
ANISOU  835  N   ASP A 545     9219  13451  11754  -2449   -889   1969       N  
ATOM    836  CA  ASP A 545      41.972  48.143  -2.494  1.00 94.50           C  
ANISOU  836  CA  ASP A 545     9807  13949  12150  -2484   -939   2064       C  
ATOM    837  C   ASP A 545      42.143  49.370  -3.392  1.00 91.29           C  
ANISOU  837  C   ASP A 545     9435  13619  11631  -2490  -1042   2074       C  
ATOM    838  O   ASP A 545      42.634  49.270  -4.517  1.00 91.34           O  
ANISOU  838  O   ASP A 545     9416  13690  11600  -2470  -1081   2041       O  
ATOM    839  CB  ASP A 545      43.084  48.061  -1.447  1.00102.35           C  
ANISOU  839  CB  ASP A 545    10875  14930  13081  -2503   -924   2177       C  
ATOM    840  CG  ASP A 545      44.452  47.856  -2.074  1.00110.67           C  
ANISOU  840  CG  ASP A 545    11938  16057  14054  -2494   -965   2212       C  
ATOM    841  OD1 ASP A 545      44.549  47.951  -3.317  1.00114.48           O  
ANISOU  841  OD1 ASP A 545    12384  16602  14513  -2477  -1008   2159       O  
ATOM    842  OD2 ASP A 545      45.428  47.621  -1.329  1.00112.06           O  
ANISOU  842  OD2 ASP A 545    12160  16228  14190  -2504   -954   2292       O  
ATOM    843  N   CYS A 546      41.741  50.530  -2.881  1.00 88.81           N  
ANISOU  843  N   CYS A 546     9184  13296  11264  -2519  -1083   2122       N  
ATOM    844  CA  CYS A 546      41.658  51.742  -3.694  1.00 89.19           C  
ANISOU  844  CA  CYS A 546     9265  13406  11218  -2524  -1175   2122       C  
ATOM    845  C   CYS A 546      42.858  52.667  -3.565  1.00 91.43           C  
ANISOU  845  C   CYS A 546     9643  13741  11354  -2552  -1239   2233       C  
ATOM    846  O   CYS A 546      43.391  52.865  -2.474  1.00 91.43           O  
ANISOU  846  O   CYS A 546     9707  13716  11318  -2580  -1229   2325       O  
ATOM    847  CB  CYS A 546      40.389  52.517  -3.342  1.00 88.61           C  
ANISOU  847  CB  CYS A 546     9197  13292  11177  -2537  -1188   2097       C  
ATOM    848  SG  CYS A 546      38.918  51.705  -3.949  1.00 73.93           S  
ANISOU  848  SG  CYS A 546     7217  11394   9480  -2500  -1143   1943       S  
ATOM    849  N   PRO A 547      43.282  53.235  -4.690  1.00 92.41           N  
ANISOU  849  N   PRO A 547     9778  13936  11397  -2543  -1302   2223       N  
ATOM    850  CA  PRO A 547      44.429  54.148  -4.707  1.00 91.59           C  
ANISOU  850  CA  PRO A 547     9761  13883  11157  -2570  -1359   2322       C  
ATOM    851  C   PRO A 547      44.081  55.506  -4.109  1.00 90.55           C  
ANISOU  851  C   PRO A 547     9711  13741  10954  -2605  -1410   2383       C  
ATOM    852  O   PRO A 547      44.897  56.424  -4.197  1.00 89.09           O  
ANISOU  852  O   PRO A 547     9600  13595  10655  -2629  -1462   2458       O  
ATOM    853  CB  PRO A 547      44.732  54.292  -6.199  1.00 92.02           C  
ANISOU  853  CB  PRO A 547     9794  14005  11166  -2546  -1397   2272       C  
ATOM    854  CG  PRO A 547      43.423  54.062  -6.867  1.00 92.32           C  
ANISOU  854  CG  PRO A 547     9761  14027  11288  -2513  -1394   2155       C  
ATOM    855  CD  PRO A 547      42.712  53.034  -6.033  1.00 92.51           C  
ANISOU  855  CD  PRO A 547     9724  13981  11443  -2506  -1321   2115       C  
TER     856      PRO A 547                                                      
HETATM  857  C1  EDO A   1     -27.514  -0.502 -18.878  1.00 74.11           C  
HETATM  858  O1  EDO A   1     -27.348  -0.092 -17.514  1.00 74.20           O  
HETATM  859  C2  EDO A   1     -27.483   0.713 -19.799  1.00 73.88           C  
HETATM  860  O2  EDO A   1     -27.454   0.261 -21.157  1.00 72.85           O  
HETATM  861  C1  EDO A   2     -23.549   0.808 -14.411  1.00 49.02           C  
HETATM  862  O1  EDO A   2     -22.638   1.204 -15.441  1.00 48.50           O  
HETATM  863  C2  EDO A   2     -24.863   0.384 -15.055  1.00 50.73           C  
HETATM  864  O2  EDO A   2     -25.690  -0.242 -14.067  1.00 52.61           O  
HETATM  865  C1  EDO A   3     -16.534  11.899 -10.334  1.00 69.97           C  
HETATM  866  O1  EDO A   3     -15.565  11.084  -9.670  1.00 68.51           O  
HETATM  867  C2  EDO A   3     -16.623  11.483 -11.797  1.00 71.71           C  
HETATM  868  O2  EDO A   3     -17.618  12.278 -12.455  1.00 72.66           O  
HETATM  869  C1  EDO A   4     -20.887 -15.427 -17.203  1.00 69.40           C  
HETATM  870  O1  EDO A   4     -21.107 -14.141 -16.608  1.00 69.84           O  
HETATM  871  C2  EDO A   4     -22.227 -16.002 -17.645  1.00 70.12           C  
HETATM  872  O2  EDO A   4     -22.045 -16.861 -18.778  1.00 71.39           O  
HETATM  873  C1  EDO A   5     -24.616  -2.833 -28.809  1.00 74.77           C  
HETATM  874  O1  EDO A   5     -24.491  -1.832 -27.794  1.00 73.78           O  
HETATM  875  C2  EDO A   5     -24.036  -2.300 -30.115  1.00 76.52           C  
HETATM  876  O2  EDO A   5     -24.282  -3.243 -31.168  1.00 78.16           O  
HETATM  877  C1  EDO A   6      -1.574  34.914 -12.906  1.00 77.07           C  
HETATM  878  O1  EDO A   6      -2.085  34.419 -11.730  1.00 79.19           O  
HETATM  879  C2  EDO A   6      -0.951  36.259 -12.849  1.00 75.53           C  
HETATM  880  O2  EDO A   6      -1.196  37.100 -13.906  1.00 76.09           O  
HETATM  881  C1  EDO A   7      17.698  28.946  -6.591  1.00 69.04           C  
HETATM  882  O1  EDO A   7      16.981  28.871  -5.366  1.00 68.22           O  
HETATM  883  C2  EDO A   7      16.929  28.197  -7.648  1.00 69.38           C  
HETATM  884  O2  EDO A   7      15.927  27.479  -6.940  1.00 71.08           O  
HETATM  885  C1  EDO A   8      19.758  33.582 -14.665  1.00 75.42           C  
HETATM  886  O1  EDO A   8      18.511  33.035 -14.497  1.00 75.46           O  
HETATM  887  C2  EDO A   8      19.912  34.676 -15.656  1.00 74.95           C  
HETATM  888  O2  EDO A   8      20.737  34.454 -16.727  1.00 73.78           O  
HETATM  889  O   HOH A   9       9.171  27.101 -14.631  1.00 29.85           O  
HETATM  890  O   HOH A  10       4.632  34.738  -6.970  1.00 30.48           O  
HETATM  891  O   HOH A  11      20.807  30.527  -9.101  1.00 45.20           O  
HETATM  892  O   HOH A  12      22.453  31.916  -7.652  1.00 43.39           O  
HETATM  893  O   HOH A  13       0.582  20.160 -10.108  1.00 49.83           O  
HETATM  894  O   HOH A  14     -16.604  16.310 -11.302  1.00 46.84           O  
HETATM  895  O   HOH A  15      -3.994  23.551 -13.927  1.00 39.39           O  
HETATM  896  O   HOH A  16       1.311  19.776  -7.517  1.00 49.54           O  
HETATM  897  O   HOH A  17     -16.450  -6.359 -30.435  1.00 45.30           O  
HETATM  898  O   HOH A  18     -24.679  -4.805 -22.376  1.00 27.01           O  
HETATM  899  O   HOH A  19     -25.821  -8.800 -26.520  1.00 51.09           O  
HETATM  900  O   HOH A  20     -19.668 -11.240 -16.474  1.00 39.76           O  
HETATM  901  O   HOH A  21       4.056  26.803  -0.687  1.00 44.17           O  
HETATM  902  O   HOH A  22      -2.425  32.701 -15.641  1.00 26.92           O  
HETATM  903  O   HOH A  23      11.137  27.437  -8.756  1.00 47.62           O  
HETATM  904  O   HOH A  24      12.390  27.767 -10.911  1.00 44.59           O  
HETATM  905  O   HOH A  25       8.697  33.635  -3.571  1.00 36.10           O  
HETATM  906  O   HOH A  26      -6.358  23.311  -7.330  1.00 44.30           O  
HETATM  907  O   HOH A  27     -22.995   0.967 -10.704  1.00 43.58           O  
HETATM  908  O   HOH A  28      -1.418  29.897  -4.857  1.00 58.30           O  
HETATM  909  O   HOH A  29      21.624  30.811 -11.474  1.00 58.67           O  
HETATM  910  O   HOH A  30     -17.591  15.824 -13.684  1.00 48.85           O  
HETATM  911  O   HOH A  31      29.655  37.559 -11.087  1.00 45.86           O  
HETATM  912  O   HOH A  32     -17.341 -11.607 -14.976  1.00 56.07           O  
HETATM  913  O   HOH A  33     -23.754 -12.387 -31.064  1.00 51.05           O  
HETATM  914  O   HOH A  34     -25.756  -2.851 -18.288  1.00 37.78           O  
HETATM  915  O   HOH A  35     -26.023   0.125 -23.464  1.00 45.95           O  
HETATM  916  O   HOH A  36     -16.696 -18.344 -21.097  1.00 55.92           O  
HETATM  917  O   HOH A  37       0.543  21.340  -5.487  1.00 52.95           O  
HETATM  918  O   HOH A  38      16.558  32.310 -11.343  1.00 58.12           O  
HETATM  919  O   HOH A  39      20.545  37.514 -14.989  1.00 49.96           O  
HETATM  920  O   HOH A  40      24.796  40.077 -14.993  1.00 55.70           O  
HETATM  921  O   HOH A  41      27.054  36.404 -12.735  1.00 60.12           O  
HETATM  922  O   HOH A  42      17.428  47.322  -7.377  1.00 52.42           O  
HETATM  923  O   HOH A  43      17.530  44.882  -8.288  1.00 51.94           O  
HETATM  924  O   HOH A  44      35.663  49.616 -10.351  1.00 52.86           O  
HETATM  925  O   HOH A  45      31.265  41.598  -9.791  1.00 46.64           O  
HETATM  926  O   HOH A  46      23.013  32.983 -13.678  1.00 60.90           O  
HETATM  927  O   HOH A  47      11.403  40.871  -6.716  1.00 35.07           O  
HETATM  928  O   HOH A  48       8.110  37.119  -6.403  1.00 37.21           O  
HETATM  929  O   HOH A  49       3.357  35.328 -14.380  1.00 35.03           O  
HETATM  930  O   HOH A  50       5.120  33.924   0.516  1.00 64.34           O  
HETATM  931  O   HOH A  51       7.964  29.770   0.358  1.00 61.96           O  
HETATM  932  O   HOH A  52      22.810  36.182  -1.008  1.00 45.67           O  
HETATM  933  O   HOH A  53      32.019  38.547  -7.045  1.00 63.16           O  
HETATM  934  O   HOH A  54     -20.964 -20.990 -23.455  1.00 54.26           O  
HETATM  935  O   HOH A  55     -18.205   7.487 -11.209  1.00 51.22           O  
HETATM  936  O   HOH A  56     -27.084  -4.501 -21.027  1.00 56.62           O  
HETATM  937  O   HOH A  57      19.773  43.843 -10.590  1.00 39.80           O  
HETATM  938  O   HOH A  58      11.195  29.956  -0.133  1.00 58.32           O  
HETATM  939  O   HOH A  59      19.413  31.352  -4.131  1.00 51.99           O  
HETATM  940  O   HOH A  60     -17.429   6.929  -8.164  1.00 50.40           O  
HETATM  941  O   HOH A  61     -19.662   3.870 -10.054  1.00 38.76           O  
HETATM  942  O   HOH A  62      -4.701  13.920 -10.273  1.00 54.12           O  
HETATM  943  O   HOH A  63      -6.211  21.857 -14.674  1.00 45.64           O  
HETATM  944  O   HOH A  64      -4.192  19.673 -15.986  1.00 52.58           O  
HETATM  945  O   HOH A  65     -14.975  -9.813 -23.880  1.00 56.84           O  
HETATM  946  O   HOH A  66     -16.592 -18.645 -32.085  1.00 43.00           O  
HETATM  947  O   HOH A  67     -15.437  11.903 -23.420  1.00 53.83           O  
HETATM  948  O   HOH A  68       2.643  22.970 -11.449  1.00 60.66           O  
HETATM  949  O   HOH A  69      30.281  46.874 -10.847  1.00 44.28           O  
HETATM  950  O   HOH A  70      37.994  54.599  -8.386  1.00 62.62           O  
HETATM  951  O   HOH A  71       0.054  33.499  -6.538  1.00 62.99           O  
HETATM  952  O   HOH A  72       7.206  26.080  -2.104  1.00 50.34           O  
HETATM  953  O   HOH A  73      -2.548  33.770  -8.295  1.00 51.15           O  
HETATM  954  O   HOH A  74     -25.555   2.808 -23.526  1.00 49.68           O  
HETATM  955  O   HOH A  75      -3.964  12.918  -7.635  1.00 70.07           O  
HETATM  956  O   HOH A  76       9.496  33.228  -1.320  1.00 88.58           O  
HETATM  957  O   HOH A  77       5.480  35.508  -2.369  1.00 59.53           O  
HETATM  958  O   HOH A  78     -27.044 -11.719 -22.265  1.00 56.34           O  
HETATM  959  O   HOH A  79      23.711  31.871 -11.389  1.00 72.65           O  
HETATM  960  O   HOH A  80       7.568  25.273 -10.618  1.00 54.81           O  
HETATM  961  O   HOH A  81      -6.822  18.861 -18.166  1.00 62.05           O  
HETATM  962  O   HOH A  82      19.353  40.357   0.849  1.00 62.25           O  
HETATM  963  O   HOH A  83      15.028  37.696  -0.912  1.00 68.24           O  
HETATM  964  O   HOH A  84      36.350  41.614  -6.406  1.00 52.99           O  
HETATM  965  O   HOH A  85     -13.080  19.628  -8.685  1.00 57.25           O  
HETATM  966  O   HOH A  86      41.079  50.202   0.059  1.00 66.52           O  
HETATM  967  O   HOH A  87     -20.243   1.594 -26.598  1.00 72.54           O  
HETATM  968  O   HOH A  88      23.707  46.504  -5.319  1.00 64.14           O  
HETATM  969  O   HOH A  89     -10.270   7.082 -10.727  1.00 60.57           O  
HETATM  970  O   HOH A  90      30.021  37.539  -1.913  1.00 49.52           O  
HETATM  971  O   HOH A  91      -5.318  16.494 -15.422  1.00 58.54           O  
HETATM  972  O   HOH A  92      11.060  27.260  -6.435  1.00 47.51           O  
HETATM  973  O   HOH A  93      -3.427  30.623  -5.663  1.00 70.29           O  
HETATM  974  O   HOH A  94       7.902  35.663  -4.508  1.00 53.23           O  
HETATM  975  O   HOH A 578      12.461  36.775 -12.645  1.00 15.98           O  
HETATM  976  O   HOH A 579      10.446  36.692 -14.360  1.00 21.32           O  
HETATM  977  O   HOH A 580       4.782  33.829  -4.487  1.00 34.50           O  
HETATM  978  O   HOH A 581     -21.562   2.943 -11.871  1.00 46.93           O  
HETATM  979  O   HOH A 582      22.719  38.070 -13.509  1.00 37.09           O  
HETATM  980  O   HOH A 583     -25.231  -2.701 -15.334  1.00 39.09           O  
HETATM  981  O   HOH A 584       3.131  37.150 -10.380  1.00 32.22           O  
HETATM  982  O   HOH A 585       6.935  26.007  -6.622  1.00 34.66           O  
CONECT  119  386                                                                
CONECT  145  423                                                                
CONECT  227  312                                                                
CONECT  312  227                                                                
CONECT  386  119                                                                
CONECT  423  145                                                                
CONECT  542  808                                                                
CONECT  568  848                                                                
CONECT  647  735                                                                
CONECT  735  647                                                                
CONECT  808  542                                                                
CONECT  848  568                                                                
CONECT  857  858  859                                                           
CONECT  858  857                                                                
CONECT  859  857  860                                                           
CONECT  860  859                                                                
CONECT  861  862  863                                                           
CONECT  862  861                                                                
CONECT  863  861  864                                                           
CONECT  864  863                                                                
CONECT  865  866  867                                                           
CONECT  866  865                                                                
CONECT  867  865  868                                                           
CONECT  868  867                                                                
CONECT  869  870  871                                                           
CONECT  870  869                                                                
CONECT  871  869  872                                                           
CONECT  872  871                                                                
CONECT  873  874  875                                                           
CONECT  874  873                                                                
CONECT  875  873  876                                                           
CONECT  876  875                                                                
CONECT  877  878  879                                                           
CONECT  878  877                                                                
CONECT  879  877  880                                                           
CONECT  880  879                                                                
CONECT  881  882  883                                                           
CONECT  882  881                                                                
CONECT  883  881  884                                                           
CONECT  884  883                                                                
CONECT  885  886  887                                                           
CONECT  886  885                                                                
CONECT  887  885  888                                                           
CONECT  888  887                                                                
MASTER      505    0    8    0    6    0    9    6  981    1   44   12          
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.