CNRS Nantes University UFIP UFIP
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***  HYDROLASE/LIGASE 18-JAN-12 4DDG  ***

elNémo ID: 22012115434913873

Job options:

ID        	=	 22012115434913873
JOBID     	=	 HYDROLASE/LIGASE 18-JAN-12 4DDG
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 on
DORMSD    	=	 on

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    HYDROLASE/LIGASE                        18-JAN-12   4DDG              
TITLE     CRYSTAL STRUCTURE OF HUMAN OTUB1/UBCH5B~UB/UB                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UBIQUITIN-CONJUGATING ENZYME E2 D2, UBIQUITIN THIOESTERASE 
COMPND   3 OTUB1;                                                               
COMPND   4 CHAIN: A, B, C, J, K, L;                                             
COMPND   5 SYNONYM: UBIQUITIN CARRIER PROTEIN D2, UBIQUITIN-CONJUGATING ENZYME  
COMPND   6 E2(17)KB 2, UBIQUITIN-CONJUGATING ENZYME E2-17 KDA 2, UBIQUITIN-     
COMPND   7 PROTEIN LIGASE D2, DEUBIQUITINATING ENZYME OTUB1, OTU DOMAIN-        
COMPND   8 CONTAINING UBIQUITIN ALDEHYDE-BINDING PROTEIN 1, OTUBAIN-1, HOTU1,   
COMPND   9 UBIQUITIN-SPECIFIC-PROCESSING PROTEASE OTUB1;                        
COMPND  10 EC: 6.3.2.19, 3.4.19.12;                                             
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MOL_ID: 2;                                                           
COMPND  13 MOLECULE: POLYUBIQUITIN-C;                                           
COMPND  14 CHAIN: D, E, F, G, H, I, M, N, O, P, Q, R;                           
COMPND  15 SYNONYM: UBIQUITIN;                                                  
COMPND  16 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: E2, HSPC263, OTB1, OTU1, OTUB1, UBC4, UBC5B, UBCH4, UBCH5B,    
SOURCE   6 UBE2D2;                                                              
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 GENE: UBC;                                                           
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    INHIBITION, HYDROLASE-LIGASE COMPLEX                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.C.JUANG,M.SANCHES,F.SICHERI                                         
REVDAT   4   15-NOV-17 4DDG    1       REMARK                                   
REVDAT   3   02-AUG-17 4DDG    1       SOURCE                                   
REVDAT   2   23-MAY-12 4DDG    1       ATOM   HELIX  REMARK SHEET               
REVDAT   1   22-FEB-12 4DDG    0                                                
JRNL        AUTH   Y.C.JUANG,M.C.LANDRY,M.SANCHES,V.VITTAL,C.C.LEUNG,           
JRNL        AUTH 2 D.F.CECCARELLI,A.R.MATEO,J.N.PRUNEDA,D.Y.MAO,R.K.SZILARD,    
JRNL        AUTH 3 S.ORLICKY,M.MUNRO,P.S.BRZOVIC,R.E.KLEVIT,F.SICHERI,          
JRNL        AUTH 4 D.DUROCHER                                                   
JRNL        TITL   OTUB1 CO-OPTS LYS48-LINKED UBIQUITIN RECOGNITION TO SUPPRESS 
JRNL        TITL 2 E2 ENZYME FUNCTION.                                          
JRNL        REF    MOL.CELL                      V.  45   384 2012              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   22325355                                                     
JRNL        DOI    10.1016/J.MOLCEL.2012.01.011                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7.1_743)                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MLHL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.12                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.990                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 60385                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.236                           
REMARK   3   R VALUE            (WORKING SET) : 0.233                           
REMARK   3   FREE R VALUE                     : 0.280                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.060                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3053                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 49.1268 -  9.2236    0.95     2612   129  0.1772 0.1684        
REMARK   3     2  9.2236 -  7.3289    1.00     2659   133  0.1738 0.1991        
REMARK   3     3  7.3289 -  6.4047    1.00     2607   171  0.2021 0.2688        
REMARK   3     4  6.4047 -  5.8202    1.00     2627   147  0.2507 0.3206        
REMARK   3     5  5.8202 -  5.4036    1.00     2654   140  0.2416 0.2714        
REMARK   3     6  5.4036 -  5.0853    1.00     2610   138  0.2183 0.2733        
REMARK   3     7  5.0853 -  4.8309    1.00     2598   145  0.2116 0.2576        
REMARK   3     8  4.8309 -  4.6207    1.00     2591   141  0.1986 0.2747        
REMARK   3     9  4.6207 -  4.4430    1.00     2641   125  0.2075 0.2526        
REMARK   3    10  4.4430 -  4.2898    1.00     2635   130  0.2122 0.2698        
REMARK   3    11  4.2898 -  4.1557    1.00     2564   138  0.2261 0.3140        
REMARK   3    12  4.1557 -  4.0370    1.00     2619   135  0.2450 0.2774        
REMARK   3    13  4.0370 -  3.9307    1.00     2607   154  0.2465 0.3017        
REMARK   3    14  3.9307 -  3.8349    0.99     2564   141  0.2818 0.3376        
REMARK   3    15  3.8349 -  3.7477    1.00     2588   143  0.2748 0.3567        
REMARK   3    16  3.7477 -  3.6680    1.00     2621   145  0.2930 0.3455        
REMARK   3    17  3.6680 -  3.5946    1.00     2610   126  0.3216 0.4092        
REMARK   3    18  3.5946 -  3.5268    1.00     2582   139  0.3247 0.3750        
REMARK   3    19  3.5268 -  3.4639    1.00     2601   124  0.3282 0.4114        
REMARK   3    20  3.4639 -  3.4052    0.99     2597   128  0.3697 0.4129        
REMARK   3    21  3.4052 -  3.3502    1.00     2578   145  0.3718 0.4259        
REMARK   3    22  3.3502 -  3.2987    0.99     2567   136  0.3765 0.3961        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.10                                          
REMARK   3   SHRINKAGE RADIUS   : 0.86                                          
REMARK   3   K_SOL              : 0.31                                          
REMARK   3   B_SOL              : 110.3                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.400            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 33.260           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -4.77940                                             
REMARK   3    B22 (A**2) : 3.13020                                              
REMARK   3    B33 (A**2) : 1.64920                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -2.56620                                             
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      :  0.004          27126                                  
REMARK   3   ANGLE     :  0.938          36660                                  
REMARK   3   CHIRALITY :  0.070           4032                                  
REMARK   3   PLANARITY :  0.005           4782                                  
REMARK   3   DIHEDRAL  : 16.511          10326                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 24                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ -1:147)                          
REMARK   3    ORIGIN FOR THE GROUP (A): -58.9105 -14.4602   9.1567              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9419 T22:   1.6336                                     
REMARK   3      T33:   0.4728 T12:   0.1492                                     
REMARK   3      T13:   0.1658 T23:   0.0061                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0807 L22:   4.9080                                     
REMARK   3      L33:   3.3389 L12:  -0.5462                                     
REMARK   3      L13:   0.3255 L23:   0.9439                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4190 S12:  -0.8663 S13:  -0.2664                       
REMARK   3      S21:   0.5422 S22:   0.5825 S23:  -0.4760                       
REMARK   3      S31:   0.4796 S32:   1.8712 S33:  -0.2026                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 1025:1271)                       
REMARK   3    ORIGIN FOR THE GROUP (A): -22.9339   9.8754  17.1484              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.9324 T22:   1.0264                                     
REMARK   3      T33:   1.8534 T12:   0.3414                                     
REMARK   3      T13:  -1.6001 T23:  -0.2334                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4574 L22:   0.6582                                     
REMARK   3      L33:   0.2849 L12:  -0.3889                                     
REMARK   3      L13:   0.2519 L23:  -0.4136                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.0755 S12:  -0.8252 S13:   1.4552                       
REMARK   3      S21:   1.0662 S22:  -0.0036 S23:  -0.6423                       
REMARK   3      S31:  -1.5783 S32:  -0.1924 S33:  -0.4898                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESSEQ -1:147)                          
REMARK   3    ORIGIN FOR THE GROUP (A): -36.0794  -9.0058  -9.4012              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1894 T22:   0.3064                                     
REMARK   3      T33:   0.2552 T12:  -0.0208                                     
REMARK   3      T13:  -0.0578 T23:   0.0251                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0780 L22:   5.1069                                     
REMARK   3      L33:   4.0853 L12:  -0.5796                                     
REMARK   3      L13:   0.4705 L23:   0.1521                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2898 S12:  -0.1099 S13:   0.2845                       
REMARK   3      S21:   0.5541 S22:  -0.2047 S23:  -0.2387                       
REMARK   3      S31:   0.1862 S32:   0.1770 S33:   0.5010                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESSEQ 1025:1271)                       
REMARK   3    ORIGIN FOR THE GROUP (A): -54.3319  13.8772 -42.3539              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4201 T22:   0.4143                                     
REMARK   3      T33:   0.7802 T12:   0.1292                                     
REMARK   3      T13:   0.1367 T23:   0.3035                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3740 L22:   1.5529                                     
REMARK   3      L33:   3.3143 L12:   0.0549                                     
REMARK   3      L13:  -0.3174 L23:  -0.5322                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0598 S12:   0.2840 S13:   0.8090                       
REMARK   3      S21:   0.3717 S22:   0.4770 S23:   0.5065                       
REMARK   3      S31:  -0.9640 S32:  -0.5032 S33:  -0.2843                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESSEQ -1:147)                          
REMARK   3    ORIGIN FOR THE GROUP (A): -70.4904  41.0497  20.0663              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4495 T22:   0.3232                                     
REMARK   3      T33:   0.1768 T12:  -0.0327                                     
REMARK   3      T13:   0.4084 T23:   0.3431                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3648 L22:   3.1954                                     
REMARK   3      L33:   3.8301 L12:  -0.0770                                     
REMARK   3      L13:  -0.9824 L23:   0.3238                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2069 S12:  -0.2358 S13:  -0.2104                       
REMARK   3      S21:  -0.2764 S22:   0.0882 S23:   0.0213                       
REMARK   3      S31:   0.3718 S32:   0.2477 S33:  -0.0352                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESSEQ 1025:1271)                       
REMARK   3    ORIGIN FOR THE GROUP (A): -45.2023  55.8861 -10.6272              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3769 T22:   0.3228                                     
REMARK   3      T33:   0.0702 T12:   0.0108                                     
REMARK   3      T13:   0.1025 T23:   0.0232                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4590 L22:   2.1460                                     
REMARK   3      L33:   3.1508 L12:   0.6662                                     
REMARK   3      L13:   0.2895 L23:  -0.3961                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4352 S12:   0.3382 S13:  -0.5676                       
REMARK   3      S21:  -0.0313 S22:   0.1473 S23:  -0.1456                       
REMARK   3      S31:  -0.1264 S32:   0.0008 S33:   0.2978                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'D' AND (RESSEQ 1:76)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.9547  -6.9973  21.3419              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1241 T22:   1.5070                                     
REMARK   3      T33:   2.3957 T12:   0.0984                                     
REMARK   3      T13:  -0.4724 T23:   0.8255                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9494 L22:   2.0690                                     
REMARK   3      L33:   3.7310 L12:  -1.1823                                     
REMARK   3      L13:   0.6937 L23:   0.7830                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.1612 S12:  -0.0634 S13:   0.9771                       
REMARK   3      S21:   0.2854 S22:  -0.8336 S23:  -1.6717                       
REMARK   3      S31:  -1.2501 S32:   1.0278 S33:   1.1179                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'E' AND (RESSEQ 1:76)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -56.1234  -3.5318 -63.2212              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2464 T22:   0.7711                                     
REMARK   3      T33:   0.5682 T12:   0.0024                                     
REMARK   3      T13:   0.1207 T23:   0.1695                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1383 L22:   2.7618                                     
REMARK   3      L33:   3.9570 L12:   0.6512                                     
REMARK   3      L13:   1.7296 L23:  -0.1012                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1268 S12:   0.4125 S13:  -0.9753                       
REMARK   3      S21:  -0.3865 S22:  -0.1439 S23:  -0.6125                       
REMARK   3      S31:   0.5277 S32:   1.4668 S33:   0.3010                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'F' AND (RESSEQ 1:76)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -31.1846  35.1420 -21.2524              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0833 T22:   1.5423                                     
REMARK   3      T33:   1.3303 T12:   0.2070                                     
REMARK   3      T13:   0.4293 T23:  -0.4930                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1608 L22:   2.1124                                     
REMARK   3      L33:   3.7189 L12:   0.1223                                     
REMARK   3      L13:  -0.5518 L23:   1.9358                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0978 S12:   0.9546 S13:  -1.1516                       
REMARK   3      S21:  -0.2420 S22:  -0.0184 S23:  -0.9743                       
REMARK   3      S31:   1.1829 S32:   1.0309 S33:   0.2848                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'G' AND (RESSEQ 1:76)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -31.3618 -12.9096  26.6998              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1977 T22:   2.4350                                     
REMARK   3      T33:   1.0369 T12:   0.7024                                     
REMARK   3      T13:  -0.0969 T23:  -0.1644                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4597 L22:   2.2868                                     
REMARK   3      L33:   0.1409 L12:   1.2149                                     
REMARK   3      L13:  -0.6522 L23:  -0.0546                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.7744 S12:  -1.9095 S13:  -0.5916                       
REMARK   3      S21:   1.0345 S22:   0.2460 S23:  -0.2977                       
REMARK   3      S31:  -0.7385 S32:  -1.5042 S33:   0.0758                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'H' AND (RESSEQ 1:76)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -98.1222  47.7609  41.5723              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1259 T22:   0.7978                                     
REMARK   3      T33:   0.3539 T12:   0.0235                                     
REMARK   3      T13:  -0.1548 T23:  -0.0938                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6924 L22:   3.6849                                     
REMARK   3      L33:   4.8960 L12:   0.4790                                     
REMARK   3      L13:   0.4395 L23:  -0.1495                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1682 S12:  -0.4019 S13:   0.3535                       
REMARK   3      S21:  -0.0156 S22:  -0.2645 S23:   0.0404                       
REMARK   3      S31:   0.7237 S32:  -0.3778 S33:  -0.0191                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'I' AND (RESSEQ 1:76)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -92.0553 -15.4750  -6.5831              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3589 T22:   0.5334                                     
REMARK   3      T33:   0.9240 T12:  -0.2197                                     
REMARK   3      T13:   0.2470 T23:  -0.1681                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.2007 L22:   2.5706                                     
REMARK   3      L33:   2.9649 L12:   0.4020                                     
REMARK   3      L13:  -2.0017 L23:   0.9270                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5086 S12:  -0.1912 S13:  -1.7469                       
REMARK   3      S21:  -0.0422 S22:  -0.2682 S23:   0.5953                       
REMARK   3      S31:   0.8081 S32:  -0.2966 S33:   0.4323                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'J' AND (RESSEQ -1:147)                          
REMARK   3    ORIGIN FOR THE GROUP (A):   9.8367 -13.3747 -80.2532              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4471 T22:   1.3932                                     
REMARK   3      T33:   1.1017 T12:   0.1171                                     
REMARK   3      T13:   0.0701 T23:   0.2691                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5900 L22:   3.8721                                     
REMARK   3      L33:   2.1568 L12:   0.9315                                     
REMARK   3      L13:   0.7416 L23:  -0.3553                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0085 S12:   0.0968 S13:  -0.1019                       
REMARK   3      S21:  -0.0482 S22:  -0.2311 S23:   0.0552                       
REMARK   3      S31:   0.0100 S32:  -0.5721 S33:   0.1969                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'K' AND (RESSEQ -1:147)                          
REMARK   3    ORIGIN FOR THE GROUP (A): -13.0959  -8.5163 -61.5791              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4178 T22:   0.6658                                     
REMARK   3      T33:   0.5706 T12:   0.0522                                     
REMARK   3      T13:  -0.1560 T23:   0.0719                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5507 L22:   4.7121                                     
REMARK   3      L33:   3.7965 L12:   0.2475                                     
REMARK   3      L13:   0.9859 L23:  -0.2889                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3027 S12:  -0.1047 S13:   0.4058                       
REMARK   3      S21:  -0.1071 S22:  -0.0958 S23:  -0.4224                       
REMARK   3      S31:  -0.7795 S32:   0.0552 S33:   0.3695                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN 'J' AND (RESSEQ 1025:1271)                       
REMARK   3    ORIGIN FOR THE GROUP (A): -26.9404  10.6581 -87.4801              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7401 T22:   0.4566                                     
REMARK   3      T33:   0.5977 T12:  -0.1225                                     
REMARK   3      T13:  -0.3361 T23:   0.1184                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2311 L22:   4.1969                                     
REMARK   3      L33:   3.0654 L12:  -0.6458                                     
REMARK   3      L13:  -0.6011 L23:   0.0221                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1486 S12:   0.1742 S13:   0.4181                       
REMARK   3      S21:  -0.3245 S22:  -0.0793 S23:  -0.2555                       
REMARK   3      S31:  -0.7100 S32:   0.4860 S33:   0.2204                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN 'K' AND (RESSEQ 1025:1271)                       
REMARK   3    ORIGIN FOR THE GROUP (A):   4.8728  13.3960 -27.3988              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2054 T22:   1.3101                                     
REMARK   3      T33:   1.9997 T12:   0.0083                                     
REMARK   3      T13:  -0.8520 T23:  -0.7413                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1821 L22:   1.1696                                     
REMARK   3      L33:   2.0293 L12:   0.6002                                     
REMARK   3      L13:   0.3648 L23:  -0.3797                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4755 S12:  -0.5348 S13:   1.2691                       
REMARK   3      S21:   0.2594 S22:  -0.0378 S23:  -0.7963                       
REMARK   3      S31:  -0.5607 S32:   0.8415 S33:  -2.2680                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN 'L' AND (RESSEQ -1:147)                          
REMARK   3    ORIGIN FOR THE GROUP (A):  21.5250  41.5020 -93.1211              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4329 T22:   1.3269                                     
REMARK   3      T33:   1.2664 T12:  -0.1012                                     
REMARK   3      T13:   0.0871 T23:  -0.4034                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9624 L22:   3.4864                                     
REMARK   3      L33:   3.6670 L12:   0.3984                                     
REMARK   3      L13:  -1.2620 L23:  -1.5030                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0964 S12:   0.2017 S13:   0.4343                       
REMARK   3      S21:  -0.4078 S22:  -0.0979 S23:   0.1691                       
REMARK   3      S31:   0.1852 S32:  -0.5454 S33:   0.0982                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: CHAIN 'L' AND (RESSEQ 1025:1271)                       
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.0500  56.3017 -61.9920              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3013 T22:   0.4407                                     
REMARK   3      T33:   0.1486 T12:  -0.0186                                     
REMARK   3      T13:   0.0032 T23:  -0.1350                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9861 L22:   2.9704                                     
REMARK   3      L33:   2.4779 L12:  -0.4222                                     
REMARK   3      L13:   0.2713 L23:   0.1775                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4380 S12:  -0.3978 S13:  -0.3993                       
REMARK   3      S21:   0.2289 S22:   0.3170 S23:  -0.3195                       
REMARK   3      S31:  -0.3312 S32:   0.2766 S33:   0.0830                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: CHAIN 'M' AND (RESSEQ 1:76)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -47.1965  -7.0626 -92.1962              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1272 T22:   0.7074                                     
REMARK   3      T33:   0.8545 T12:  -0.1738                                     
REMARK   3      T13:  -0.1982 T23:  -0.2381                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.4789 L22:   1.6485                                     
REMARK   3      L33:   3.2077 L12:   0.6505                                     
REMARK   3      L13:  -0.6803 L23:  -1.0844                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.8028 S12:  -0.5462 S13:   0.1312                       
REMARK   3      S21:   0.1359 S22:  -0.1253 S23:   0.4774                       
REMARK   3      S31:   0.5436 S32:  -0.5721 S33:   0.8372                       
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    SELECTION: CHAIN 'N' AND (RESSEQ 1:76)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   6.9972  -4.6255  -7.2317              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4776 T22:   1.6826                                     
REMARK   3      T33:   1.5323 T12:   0.1036                                     
REMARK   3      T13:  -0.3664 T23:  -0.4340                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8357 L22:   0.9924                                     
REMARK   3      L33:   2.3652 L12:   0.4300                                     
REMARK   3      L13:   0.4348 L23:  -0.2124                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1334 S12:  -0.4520 S13:  -0.8932                       
REMARK   3      S21:   0.0405 S22:  -0.5350 S23:   0.2396                       
REMARK   3      S31:  -0.0706 S32:  -1.2376 S33:  -0.2957                       
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    SELECTION: CHAIN 'O' AND (RESSEQ 1:76)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -18.0514  35.1583 -52.1277              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0656 T22:   1.4918                                     
REMARK   3      T33:   1.3305 T12:  -0.0351                                     
REMARK   3      T13:   0.4237 T23:   0.4972                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9495 L22:   3.0763                                     
REMARK   3      L33:   4.2498 L12:   0.0930                                     
REMARK   3      L13:  -0.0782 L23:  -1.2824                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0980 S12:  -1.6565 S13:  -1.4953                       
REMARK   3      S21:   0.5155 S22:  -0.1893 S23:   0.7928                       
REMARK   3      S31:   1.4231 S32:  -0.4887 S33:   0.1002                       
REMARK   3   TLS GROUP : 22                                                     
REMARK   3    SELECTION: CHAIN 'P' AND (RESSEQ 1:76)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -17.7606 -11.2334 -97.5855              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6757 T22:   0.8090                                     
REMARK   3      T33:   0.8103 T12:   0.0025                                     
REMARK   3      T13:   0.0015 T23:   0.2399                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7753 L22:   3.2471                                     
REMARK   3      L33:   2.7322 L12:  -0.6057                                     
REMARK   3      L13:   1.2368 L23:   0.0320                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3415 S12:  -0.5625 S13:  -1.1439                       
REMARK   3      S21:  -0.5090 S22:  -0.1719 S23:  -0.1326                       
REMARK   3      S31:   0.0438 S32:   1.1875 S33:  -0.0963                       
REMARK   3   TLS GROUP : 23                                                     
REMARK   3    SELECTION: CHAIN 'Q' AND (RESSEQ 1:76)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  49.3083  47.2202-114.8069              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3084 T22:   0.9125                                     
REMARK   3      T33:   0.7586 T12:  -0.3418                                     
REMARK   3      T13:  -0.3720 T23:   0.3104                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0545 L22:   2.0616                                     
REMARK   3      L33:   4.5475 L12:  -0.5268                                     
REMARK   3      L13:   0.7334 L23:   0.7660                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1528 S12:   0.7491 S13:   0.7884                       
REMARK   3      S21:  -0.1670 S22:   0.1941 S23:   0.2822                       
REMARK   3      S31:   0.4024 S32:  -0.4081 S33:   0.0718                       
REMARK   3   TLS GROUP : 24                                                     
REMARK   3    SELECTION: CHAIN 'R' AND (RESSEQ 1:76)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  42.9515 -14.7086 -64.1468              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5016 T22:   0.5736                                     
REMARK   3      T33:   0.9028 T12:   0.0060                                     
REMARK   3      T13:   0.1770 T23:   0.0414                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8175 L22:   4.0405                                     
REMARK   3      L33:   3.2463 L12:   0.7614                                     
REMARK   3      L13:  -1.8775 L23:  -0.8993                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6080 S12:   0.1884 S13:  -1.8303                       
REMARK   3      S21:   0.1067 S22:   0.0333 S23:  -0.3532                       
REMARK   3      S31:   0.4703 S32:  -0.2867 S33:   0.4716                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 4                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN 'G'                                   
REMARK   3     SELECTION          : CHAIN 'H'                                   
REMARK   3     ATOM PAIRS NUMBER  : 601                                         
REMARK   3     RMSD               : 0.001                                       
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: CHAIN 'G'                                   
REMARK   3     SELECTION          : CHAIN 'I'                                   
REMARK   3     ATOM PAIRS NUMBER  : 601                                         
REMARK   3     RMSD               : 0.001                                       
REMARK   3    NCS OPERATOR : 3                                                  
REMARK   3     REFERENCE SELECTION: CHAIN 'G'                                   
REMARK   3     SELECTION          : CHAIN 'Q'                                   
REMARK   3     ATOM PAIRS NUMBER  : 601                                         
REMARK   3     RMSD               : 0.001                                       
REMARK   3    NCS OPERATOR : 4                                                  
REMARK   3     REFERENCE SELECTION: CHAIN 'G'                                   
REMARK   3     SELECTION          : CHAIN 'P'                                   
REMARK   3     ATOM PAIRS NUMBER  : 601                                         
REMARK   3     RMSD               : 0.001                                       
REMARK   3    NCS OPERATOR : 5                                                  
REMARK   3     REFERENCE SELECTION: CHAIN 'G'                                   
REMARK   3     SELECTION          : CHAIN 'R'                                   
REMARK   3     ATOM PAIRS NUMBER  : 601                                         
REMARK   3     RMSD               : 0.001                                       
REMARK   3   NCS GROUP : 2                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN 'A' AND (RESSEQ 1:150 ) AND (NOT      
REMARK   3                          ELEMENT H) AND (NOT ELEMENT D)              
REMARK   3     SELECTION          : CHAIN 'B' AND (RESSEQ 1:150 ) AND (NOT      
REMARK   3                          ELEMENT H) AND (NOT ELEMENT D)              
REMARK   3     ATOM PAIRS NUMBER  : 1191                                        
REMARK   3     RMSD               : 0.003                                       
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: CHAIN 'A' AND (RESSEQ 1:150 ) AND (NOT      
REMARK   3                          ELEMENT H) AND (NOT ELEMENT D)              
REMARK   3     SELECTION          : CHAIN 'C' AND (RESSEQ 1:150 ) AND (NOT      
REMARK   3                          ELEMENT H) AND (NOT ELEMENT D)              
REMARK   3     ATOM PAIRS NUMBER  : 1191                                        
REMARK   3     RMSD               : 0.003                                       
REMARK   3    NCS OPERATOR : 3                                                  
REMARK   3     REFERENCE SELECTION: CHAIN 'A' AND (RESSEQ 1:150 ) AND (NOT      
REMARK   3                          ELEMENT H) AND (NOT ELEMENT D)              
REMARK   3     SELECTION          : CHAIN 'J' AND (RESSEQ 1:150 ) AND (NOT      
REMARK   3                          ELEMENT H) AND (NOT ELEMENT D)              
REMARK   3     ATOM PAIRS NUMBER  : 1191                                        
REMARK   3     RMSD               : 0.002                                       
REMARK   3    NCS OPERATOR : 4                                                  
REMARK   3     REFERENCE SELECTION: CHAIN 'A' AND (RESSEQ 1:150 ) AND (NOT      
REMARK   3                          ELEMENT H) AND (NOT ELEMENT D)              
REMARK   3     SELECTION          : CHAIN 'K' AND (RESSEQ 1:150 ) AND (NOT      
REMARK   3                          ELEMENT H) AND (NOT ELEMENT D)              
REMARK   3     ATOM PAIRS NUMBER  : 1191                                        
REMARK   3     RMSD               : 0.002                                       
REMARK   3    NCS OPERATOR : 5                                                  
REMARK   3     REFERENCE SELECTION: CHAIN 'A' AND (RESSEQ 1:150 ) AND (NOT      
REMARK   3                          ELEMENT H) AND (NOT ELEMENT D)              
REMARK   3     SELECTION          : CHAIN 'L' AND (RESSEQ 1:150 ) AND (NOT      
REMARK   3                          ELEMENT H) AND (NOT ELEMENT D)              
REMARK   3     ATOM PAIRS NUMBER  : 1191                                        
REMARK   3     RMSD               : 0.003                                       
REMARK   3   NCS GROUP : 3                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN 'A' AND (RESSEQ 1025:1271 ) AND       
REMARK   3                          (NOT ELEMENT H) AND (NOT ELEMENT D)         
REMARK   3     SELECTION          : CHAIN 'B' AND (RESSEQ 1025:1271 ) AND       
REMARK   3                          (NOT ELEMENT H) AND (NOT ELEMENT D)         
REMARK   3     ATOM PAIRS NUMBER  : 2026                                        
REMARK   3     RMSD               : 0.002                                       
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: CHAIN 'A' AND (RESSEQ 1025:1271 ) AND       
REMARK   3                          (NOT ELEMENT H) AND (NOT ELEMENT D)         
REMARK   3     SELECTION          : CHAIN 'C' AND (RESSEQ 1025:1271 ) AND       
REMARK   3                          (NOT ELEMENT H) AND (NOT ELEMENT D)         
REMARK   3     ATOM PAIRS NUMBER  : 2026                                        
REMARK   3     RMSD               : 0.002                                       
REMARK   3    NCS OPERATOR : 3                                                  
REMARK   3     REFERENCE SELECTION: CHAIN 'A' AND (RESSEQ 1025:1271 ) AND       
REMARK   3                          (NOT ELEMENT H) AND (NOT ELEMENT D)         
REMARK   3     SELECTION          : CHAIN 'J' AND (RESSEQ 1025:1271 ) AND       
REMARK   3                          (NOT ELEMENT H) AND (NOT ELEMENT D)         
REMARK   3     ATOM PAIRS NUMBER  : 2026                                        
REMARK   3     RMSD               : 0.001                                       
REMARK   3    NCS OPERATOR : 4                                                  
REMARK   3     REFERENCE SELECTION: CHAIN 'A' AND (RESSEQ 1025:1271 ) AND       
REMARK   3                          (NOT ELEMENT H) AND (NOT ELEMENT D)         
REMARK   3     SELECTION          : CHAIN 'K' AND (RESSEQ 1025:1271 ) AND       
REMARK   3                          (NOT ELEMENT H) AND (NOT ELEMENT D)         
REMARK   3     ATOM PAIRS NUMBER  : 2026                                        
REMARK   3     RMSD               : 0.002                                       
REMARK   3    NCS OPERATOR : 5                                                  
REMARK   3     REFERENCE SELECTION: CHAIN 'A' AND (RESSEQ 1025:1271 ) AND       
REMARK   3                          (NOT ELEMENT H) AND (NOT ELEMENT D)         
REMARK   3     SELECTION          : CHAIN 'L' AND (RESSEQ 1025:1271 ) AND       
REMARK   3                          (NOT ELEMENT H) AND (NOT ELEMENT D)         
REMARK   3     ATOM PAIRS NUMBER  : 2026                                        
REMARK   3     RMSD               : 0.002                                       
REMARK   3   NCS GROUP : 4                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN 'D'                                   
REMARK   3     SELECTION          : CHAIN 'E'                                   
REMARK   3     ATOM PAIRS NUMBER  : 601                                         
REMARK   3     RMSD               : 0.001                                       
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: CHAIN 'D'                                   
REMARK   3     SELECTION          : CHAIN 'F'                                   
REMARK   3     ATOM PAIRS NUMBER  : 601                                         
REMARK   3     RMSD               : 0.001                                       
REMARK   3    NCS OPERATOR : 3                                                  
REMARK   3     REFERENCE SELECTION: CHAIN 'D'                                   
REMARK   3     SELECTION          : CHAIN 'N'                                   
REMARK   3     ATOM PAIRS NUMBER  : 601                                         
REMARK   3     RMSD               : 0.001                                       
REMARK   3    NCS OPERATOR : 4                                                  
REMARK   3     REFERENCE SELECTION: CHAIN 'D'                                   
REMARK   3     SELECTION          : CHAIN 'M'                                   
REMARK   3     ATOM PAIRS NUMBER  : 601                                         
REMARK   3     RMSD               : 0.001                                       
REMARK   3    NCS OPERATOR : 5                                                  
REMARK   3     REFERENCE SELECTION: CHAIN 'D'                                   
REMARK   3     SELECTION          : CHAIN 'O'                                   
REMARK   3     ATOM PAIRS NUMBER  : 601                                         
REMARK   3     RMSD               : 0.001                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4DDG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JAN-12.                  
REMARK 100 THE DEPOSITION ID IS D_1000070190.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-DEC-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 198.25                             
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CLSI                               
REMARK 200  BEAMLINE                       : 08ID-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97949                            
REMARK 200  MONOCHROMATOR                  : ACCEL/BRUKER DOUBLE CRYSTAL        
REMARK 200                                   MONOCHROMATOR (DCM)                
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX-300                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 60387                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.299                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.290                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.50                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2ESK AND 2ZFY                              
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.28                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG1500, 0.1 M SPG, PH 7.5, VAPOR    
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 293K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       52.46400            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: THE BIOLOGICAL COMPLEX DEFINED BY THE AUTHOR CONSISTS OF:    
REMARK 300 COMPLEX 1: CHAIN H, CHAIN E, RESIDUES 1 TO 147 OF CHAIN C,           
REMARK 300            AND RESIDUES 1025-1271 OF CHAIN B;                        
REMARK 300 COMPLEX 2: CHAIN G, CHAIN D, RESIDUES 1 TO 147 OF CHAIN B,           
REMARK 300            AND RESIDUES 1025-1271 OF CHAIN A;                        
REMARK 300 COMPLEX 3: CHAIN I, CHAIN F, RESIDUES 1 TO 147 OF CHAIN A,           
REMARK 300            AND RESIDUES 1025-1271 OF CHAIN  C;                       
REMARK 300 COMPLEX 4: CHAIN Q, CHAIN N, RESIDUES 1 TO 147 OF CHAIN L,           
REMARK 300            AND RESIDUES 1025-1271 OF CHAIN K;                        
REMARK 300 COMPLEX 5: CHAIN P, CHAIN M, RESIDUES 1 TO 147 OF CHAIN K,           
REMARK 300            AND RESIDUES 1025-1271 OF CHAIN J;                        
REMARK 300 COMPLEX 6: CHAIN R, CHAIN O, RESIDUES 1 TO 147 OF CHAIN J,           
REMARK 300            AND RESIDUES 1025-1271 OF CHAIN  L                        
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: NONAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 13330 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 63270 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -69.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I             
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: NONAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 13140 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 63600 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -66.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: J, K, L, M, N, O, P, Q, R             
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 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OG   SER L    85     O    GLY Q    76              1.85            
REMARK 500   OG   SER C    85     O    GLY H    76              1.93            
REMARK 500   NZ   LYS A  1188     OE1  GLN N    31              2.05            
REMARK 500   OE1  GLU B  1195     NH2  ARG E    42              2.16            
REMARK 500   OE1  GLU K  1195     NH2  ARG N    42              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A1250   C   -  N   -  CA  ANGL. DEV. =  -9.1 DEGREES          
REMARK 500    PRO C1250   C   -  N   -  CA  ANGL. DEV. =  -9.1 DEGREES          
REMARK 500    PRO J1250   C   -  N   -  CA  ANGL. DEV. =  -9.0 DEGREES          
REMARK 500    PRO K1250   C   -  N   -  CA  ANGL. DEV. =  -9.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    HIS A  75      138.76   -176.39                                   
REMARK 500    ARG A  90      -85.09   -123.27                                   
REMARK 500    PRO A 113     -175.96    -67.54                                   
REMARK 500    THR A 129      -69.25    -96.91                                   
REMARK 500    TYR A1026      -37.50    -38.74                                   
REMARK 500    GLU A1150      -70.15    -57.32                                   
REMARK 500    GLN A1206      -61.18    -94.80                                   
REMARK 500    VAL A1208      -59.79   -128.69                                   
REMARK 500    CYS A1212       -3.90     70.26                                   
REMARK 500    ASP A1237      -82.11   -128.44                                   
REMARK 500    HIS B  75      138.82   -176.36                                   
REMARK 500    ARG B  90      -85.11   -123.20                                   
REMARK 500    PRO B 113     -175.95    -67.65                                   
REMARK 500    THR B 129      -69.23    -96.96                                   
REMARK 500    SER B 150      -78.49    -86.41                                   
REMARK 500    ALA B1025      -58.29    -25.91                                   
REMARK 500    GLU B1150      -70.12    -57.34                                   
REMARK 500    GLN B1206      -61.07    -94.84                                   
REMARK 500    VAL B1208      -59.80   -128.62                                   
REMARK 500    CYS B1212       -3.94     70.27                                   
REMARK 500    ASP B1237      -82.18   -128.45                                   
REMARK 500    HIS C  75      138.78   -176.41                                   
REMARK 500    ARG C  90      -85.15   -123.22                                   
REMARK 500    PRO C 113     -175.98    -67.51                                   
REMARK 500    THR C 129      -69.25    -96.93                                   
REMARK 500    GLU C1150      -70.12    -57.27                                   
REMARK 500    GLN C1206      -61.10    -94.86                                   
REMARK 500    VAL C1208      -59.82   -128.70                                   
REMARK 500    CYS C1212       -3.88     70.27                                   
REMARK 500    ASP C1237      -82.22   -128.38                                   
REMARK 500    ARG D  72      -72.95    -55.92                                   
REMARK 500    ARG E  72      -72.91    -55.85                                   
REMARK 500    ARG F  72      -73.05    -55.82                                   
REMARK 500    HIS J  75      138.69   -176.39                                   
REMARK 500    ARG J  90      -85.09   -123.25                                   
REMARK 500    PRO J 113     -175.93    -67.64                                   
REMARK 500    THR J 129      -69.22    -96.95                                   
REMARK 500    SER J 150      -86.18    -85.10                                   
REMARK 500    ALA J1025      -57.21    -18.89                                   
REMARK 500    GLU J1150      -70.04    -57.33                                   
REMARK 500    GLN J1206      -61.10    -94.84                                   
REMARK 500    VAL J1208      -59.74   -128.69                                   
REMARK 500    CYS J1212       -3.91     70.34                                   
REMARK 500    ASP J1237      -82.11   -128.36                                   
REMARK 500    HIS K  75      138.75   -176.42                                   
REMARK 500    ARG K  90      -85.10   -123.26                                   
REMARK 500    PRO K 113     -175.96    -67.71                                   
REMARK 500    THR K 129      -69.27    -96.89                                   
REMARK 500    SER K 150      -83.90    -85.31                                   
REMARK 500    ALA K1025      -57.58    -20.84                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      68 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 PHE A 1249     PRO A 1250                  115.25                    
REMARK 500 PHE B 1249     PRO B 1250                  115.29                    
REMARK 500 PHE C 1249     PRO C 1250                  115.28                    
REMARK 500 PHE J 1249     PRO J 1250                  115.25                    
REMARK 500 PHE K 1249     PRO K 1250                  115.28                    
REMARK 500 PHE L 1249     PRO L 1250                  115.25                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4DDI   RELATED DB: PDB                                   
DBREF  4DDG A    1   147  UNP    P62837   UB2D2_HUMAN      1    147             
DBREF  4DDG A 1025  1271  UNP    Q96FW1   OTUB1_HUMAN     25    271             
DBREF  4DDG B    1   147  UNP    P62837   UB2D2_HUMAN      1    147             
DBREF  4DDG B 1025  1271  UNP    Q96FW1   OTUB1_HUMAN     25    271             
DBREF  4DDG C    1   147  UNP    P62837   UB2D2_HUMAN      1    147             
DBREF  4DDG C 1025  1271  UNP    Q96FW1   OTUB1_HUMAN     25    271             
DBREF  4DDG D    1    76  UNP    P0CG48   UBC_HUMAN        1     76             
DBREF  4DDG E    1    76  UNP    P0CG48   UBC_HUMAN        1     76             
DBREF  4DDG F    1    76  UNP    P0CG48   UBC_HUMAN        1     76             
DBREF  4DDG G    1    76  UNP    P0CG48   UBC_HUMAN        1     76             
DBREF  4DDG H    1    76  UNP    P0CG48   UBC_HUMAN        1     76             
DBREF  4DDG I    1    76  UNP    P0CG48   UBC_HUMAN        1     76             
DBREF  4DDG J    1   147  UNP    P62837   UB2D2_HUMAN      1    147             
DBREF  4DDG J 1025  1271  UNP    Q96FW1   OTUB1_HUMAN     25    271             
DBREF  4DDG K    1   147  UNP    P62837   UB2D2_HUMAN      1    147             
DBREF  4DDG K 1025  1271  UNP    Q96FW1   OTUB1_HUMAN     25    271             
DBREF  4DDG L    1   147  UNP    P62837   UB2D2_HUMAN      1    147             
DBREF  4DDG L 1025  1271  UNP    Q96FW1   OTUB1_HUMAN     25    271             
DBREF  4DDG M    1    76  UNP    P0CG48   UBC_HUMAN        1     76             
DBREF  4DDG N    1    76  UNP    P0CG48   UBC_HUMAN        1     76             
DBREF  4DDG O    1    76  UNP    P0CG48   UBC_HUMAN        1     76             
DBREF  4DDG P    1    76  UNP    P0CG48   UBC_HUMAN        1     76             
DBREF  4DDG Q    1    76  UNP    P0CG48   UBC_HUMAN        1     76             
DBREF  4DDG R    1    76  UNP    P0CG48   UBC_HUMAN        1     76             
SEQADV 4DDG GLY A   -1  UNP  P62837              EXPRESSION TAG                 
SEQADV 4DDG ALA A    0  UNP  P62837              EXPRESSION TAG                 
SEQADV 4DDG SER A   85  UNP  P62837    CYS    85 CONFLICT                       
SEQADV 4DDG GLY A  148  UNP  Q96FW1              LINKER                         
SEQADV 4DDG GLY A  149  UNP  Q96FW1              LINKER                         
SEQADV 4DDG SER A  150  UNP  Q96FW1              LINKER                         
SEQADV 4DDG SER A 1091  UNP  Q96FW1    CYS    91 CONFLICT                       
SEQADV 4DDG GLY B   -1  UNP  P62837              EXPRESSION TAG                 
SEQADV 4DDG ALA B    0  UNP  P62837              EXPRESSION TAG                 
SEQADV 4DDG SER B   85  UNP  P62837    CYS    85 CONFLICT                       
SEQADV 4DDG GLY B  148  UNP  Q96FW1              LINKER                         
SEQADV 4DDG GLY B  149  UNP  Q96FW1              LINKER                         
SEQADV 4DDG SER B  150  UNP  Q96FW1              LINKER                         
SEQADV 4DDG SER B 1091  UNP  Q96FW1    CYS    91 CONFLICT                       
SEQADV 4DDG GLY C   -1  UNP  P62837              EXPRESSION TAG                 
SEQADV 4DDG ALA C    0  UNP  P62837              EXPRESSION TAG                 
SEQADV 4DDG SER C   85  UNP  P62837    CYS    85 CONFLICT                       
SEQADV 4DDG GLY C  148  UNP  Q96FW1              LINKER                         
SEQADV 4DDG GLY C  149  UNP  Q96FW1              LINKER                         
SEQADV 4DDG SER C  150  UNP  Q96FW1              LINKER                         
SEQADV 4DDG SER C 1091  UNP  Q96FW1    CYS    91 CONFLICT                       
SEQADV 4DDG GLY J   -1  UNP  P62837              EXPRESSION TAG                 
SEQADV 4DDG ALA J    0  UNP  P62837              EXPRESSION TAG                 
SEQADV 4DDG SER J   85  UNP  P62837    CYS    85 CONFLICT                       
SEQADV 4DDG GLY J  148  UNP  Q96FW1              LINKER                         
SEQADV 4DDG GLY J  149  UNP  Q96FW1              LINKER                         
SEQADV 4DDG SER J  150  UNP  Q96FW1              LINKER                         
SEQADV 4DDG SER J 1091  UNP  Q96FW1    CYS    91 CONFLICT                       
SEQADV 4DDG GLY K   -1  UNP  P62837              EXPRESSION TAG                 
SEQADV 4DDG ALA K    0  UNP  P62837              EXPRESSION TAG                 
SEQADV 4DDG SER K   85  UNP  P62837    CYS    85 CONFLICT                       
SEQADV 4DDG GLY K  148  UNP  Q96FW1              LINKER                         
SEQADV 4DDG GLY K  149  UNP  Q96FW1              LINKER                         
SEQADV 4DDG SER K  150  UNP  Q96FW1              LINKER                         
SEQADV 4DDG SER K 1091  UNP  Q96FW1    CYS    91 CONFLICT                       
SEQADV 4DDG GLY L   -1  UNP  P62837              EXPRESSION TAG                 
SEQADV 4DDG ALA L    0  UNP  P62837              EXPRESSION TAG                 
SEQADV 4DDG SER L   85  UNP  P62837    CYS    85 CONFLICT                       
SEQADV 4DDG GLY L  148  UNP  Q96FW1              LINKER                         
SEQADV 4DDG GLY L  149  UNP  Q96FW1              LINKER                         
SEQADV 4DDG SER L  150  UNP  Q96FW1              LINKER                         
SEQADV 4DDG SER L 1091  UNP  Q96FW1    CYS    91 CONFLICT                       
SEQRES   1 A  399  GLY ALA MET ALA LEU LYS ARG ILE HIS LYS GLU LEU ASN          
SEQRES   2 A  399  ASP LEU ALA ARG ASP PRO PRO ALA GLN CYS SER ALA GLY          
SEQRES   3 A  399  PRO VAL GLY ASP ASP MET PHE HIS TRP GLN ALA THR ILE          
SEQRES   4 A  399  MET GLY PRO ASN ASP SER PRO TYR GLN GLY GLY VAL PHE          
SEQRES   5 A  399  PHE LEU THR ILE HIS PHE PRO THR ASP TYR PRO PHE LYS          
SEQRES   6 A  399  PRO PRO LYS VAL ALA PHE THR THR ARG ILE TYR HIS PRO          
SEQRES   7 A  399  ASN ILE ASN SER ASN GLY SER ILE SER LEU ASP ILE LEU          
SEQRES   8 A  399  ARG SER GLN TRP SER PRO ALA LEU THR ILE SER LYS VAL          
SEQRES   9 A  399  LEU LEU SER ILE CYS SER LEU LEU CYS ASP PRO ASN PRO          
SEQRES  10 A  399  ASP ASP PRO LEU VAL PRO GLU ILE ALA ARG ILE TYR LYS          
SEQRES  11 A  399  THR ASP ARG GLU LYS TYR ASN ARG ILE ALA ARG GLU TRP          
SEQRES  12 A  399  THR GLN LYS TYR ALA MET GLY GLY SER ALA TYR ASP GLU          
SEQRES  13 A  399  ALA ILE MET ALA GLN GLN ASP ARG ILE GLN GLN GLU ILE          
SEQRES  14 A  399  ALA VAL GLN ASN PRO LEU VAL SER GLU ARG LEU GLU LEU          
SEQRES  15 A  399  SER VAL LEU TYR LYS GLU TYR ALA GLU ASP ASP ASN ILE          
SEQRES  16 A  399  TYR GLN GLN LYS ILE LYS ASP LEU HIS LYS LYS TYR SER          
SEQRES  17 A  399  TYR ILE ARG LYS THR ARG PRO ASP GLY ASN SER PHE TYR          
SEQRES  18 A  399  ARG ALA PHE GLY PHE SER HIS LEU GLU ALA LEU LEU ASP          
SEQRES  19 A  399  ASP SER LYS GLU LEU GLN ARG PHE LYS ALA VAL SER ALA          
SEQRES  20 A  399  LYS SER LYS GLU ASP LEU VAL SER GLN GLY PHE THR GLU          
SEQRES  21 A  399  PHE THR ILE GLU ASP PHE HIS ASN THR PHE MET ASP LEU          
SEQRES  22 A  399  ILE GLU GLN VAL GLU LYS GLN THR SER VAL ALA ASP LEU          
SEQRES  23 A  399  LEU ALA SER PHE ASN ASP GLN SER THR SER ASP TYR LEU          
SEQRES  24 A  399  VAL VAL TYR LEU ARG LEU LEU THR SER GLY TYR LEU GLN          
SEQRES  25 A  399  ARG GLU SER LYS PHE PHE GLU HIS PHE ILE GLU GLY GLY          
SEQRES  26 A  399  ARG THR VAL LYS GLU PHE CYS GLN GLN GLU VAL GLU PRO          
SEQRES  27 A  399  MET CYS LYS GLU SER ASP HIS ILE HIS ILE ILE ALA LEU          
SEQRES  28 A  399  ALA GLN ALA LEU SER VAL SER ILE GLN VAL GLU TYR MET          
SEQRES  29 A  399  ASP ARG GLY GLU GLY GLY THR THR ASN PRO HIS ILE PHE          
SEQRES  30 A  399  PRO GLU GLY SER GLU PRO LYS VAL TYR LEU LEU TYR ARG          
SEQRES  31 A  399  PRO GLY HIS TYR ASP ILE LEU TYR LYS                          
SEQRES   1 B  399  GLY ALA MET ALA LEU LYS ARG ILE HIS LYS GLU LEU ASN          
SEQRES   2 B  399  ASP LEU ALA ARG ASP PRO PRO ALA GLN CYS SER ALA GLY          
SEQRES   3 B  399  PRO VAL GLY ASP ASP MET PHE HIS TRP GLN ALA THR ILE          
SEQRES   4 B  399  MET GLY PRO ASN ASP SER PRO TYR GLN GLY GLY VAL PHE          
SEQRES   5 B  399  PHE LEU THR ILE HIS PHE PRO THR ASP TYR PRO PHE LYS          
SEQRES   6 B  399  PRO PRO LYS VAL ALA PHE THR THR ARG ILE TYR HIS PRO          
SEQRES   7 B  399  ASN ILE ASN SER ASN GLY SER ILE SER LEU ASP ILE LEU          
SEQRES   8 B  399  ARG SER GLN TRP SER PRO ALA LEU THR ILE SER LYS VAL          
SEQRES   9 B  399  LEU LEU SER ILE CYS SER LEU LEU CYS ASP PRO ASN PRO          
SEQRES  10 B  399  ASP ASP PRO LEU VAL PRO GLU ILE ALA ARG ILE TYR LYS          
SEQRES  11 B  399  THR ASP ARG GLU LYS TYR ASN ARG ILE ALA ARG GLU TRP          
SEQRES  12 B  399  THR GLN LYS TYR ALA MET GLY GLY SER ALA TYR ASP GLU          
SEQRES  13 B  399  ALA ILE MET ALA GLN GLN ASP ARG ILE GLN GLN GLU ILE          
SEQRES  14 B  399  ALA VAL GLN ASN PRO LEU VAL SER GLU ARG LEU GLU LEU          
SEQRES  15 B  399  SER VAL LEU TYR LYS GLU TYR ALA GLU ASP ASP ASN ILE          
SEQRES  16 B  399  TYR GLN GLN LYS ILE LYS ASP LEU HIS LYS LYS TYR SER          
SEQRES  17 B  399  TYR ILE ARG LYS THR ARG PRO ASP GLY ASN SER PHE TYR          
SEQRES  18 B  399  ARG ALA PHE GLY PHE SER HIS LEU GLU ALA LEU LEU ASP          
SEQRES  19 B  399  ASP SER LYS GLU LEU GLN ARG PHE LYS ALA VAL SER ALA          
SEQRES  20 B  399  LYS SER LYS GLU ASP LEU VAL SER GLN GLY PHE THR GLU          
SEQRES  21 B  399  PHE THR ILE GLU ASP PHE HIS ASN THR PHE MET ASP LEU          
SEQRES  22 B  399  ILE GLU GLN VAL GLU LYS GLN THR SER VAL ALA ASP LEU          
SEQRES  23 B  399  LEU ALA SER PHE ASN ASP GLN SER THR SER ASP TYR LEU          
SEQRES  24 B  399  VAL VAL TYR LEU ARG LEU LEU THR SER GLY TYR LEU GLN          
SEQRES  25 B  399  ARG GLU SER LYS PHE PHE GLU HIS PHE ILE GLU GLY GLY          
SEQRES  26 B  399  ARG THR VAL LYS GLU PHE CYS GLN GLN GLU VAL GLU PRO          
SEQRES  27 B  399  MET CYS LYS GLU SER ASP HIS ILE HIS ILE ILE ALA LEU          
SEQRES  28 B  399  ALA GLN ALA LEU SER VAL SER ILE GLN VAL GLU TYR MET          
SEQRES  29 B  399  ASP ARG GLY GLU GLY GLY THR THR ASN PRO HIS ILE PHE          
SEQRES  30 B  399  PRO GLU GLY SER GLU PRO LYS VAL TYR LEU LEU TYR ARG          
SEQRES  31 B  399  PRO GLY HIS TYR ASP ILE LEU TYR LYS                          
SEQRES   1 C  399  GLY ALA MET ALA LEU LYS ARG ILE HIS LYS GLU LEU ASN          
SEQRES   2 C  399  ASP LEU ALA ARG ASP PRO PRO ALA GLN CYS SER ALA GLY          
SEQRES   3 C  399  PRO VAL GLY ASP ASP MET PHE HIS TRP GLN ALA THR ILE          
SEQRES   4 C  399  MET GLY PRO ASN ASP SER PRO TYR GLN GLY GLY VAL PHE          
SEQRES   5 C  399  PHE LEU THR ILE HIS PHE PRO THR ASP TYR PRO PHE LYS          
SEQRES   6 C  399  PRO PRO LYS VAL ALA PHE THR THR ARG ILE TYR HIS PRO          
SEQRES   7 C  399  ASN ILE ASN SER ASN GLY SER ILE SER LEU ASP ILE LEU          
SEQRES   8 C  399  ARG SER GLN TRP SER PRO ALA LEU THR ILE SER LYS VAL          
SEQRES   9 C  399  LEU LEU SER ILE CYS SER LEU LEU CYS ASP PRO ASN PRO          
SEQRES  10 C  399  ASP ASP PRO LEU VAL PRO GLU ILE ALA ARG ILE TYR LYS          
SEQRES  11 C  399  THR ASP ARG GLU LYS TYR ASN ARG ILE ALA ARG GLU TRP          
SEQRES  12 C  399  THR GLN LYS TYR ALA MET GLY GLY SER ALA TYR ASP GLU          
SEQRES  13 C  399  ALA ILE MET ALA GLN GLN ASP ARG ILE GLN GLN GLU ILE          
SEQRES  14 C  399  ALA VAL GLN ASN PRO LEU VAL SER GLU ARG LEU GLU LEU          
SEQRES  15 C  399  SER VAL LEU TYR LYS GLU TYR ALA GLU ASP ASP ASN ILE          
SEQRES  16 C  399  TYR GLN GLN LYS ILE LYS ASP LEU HIS LYS LYS TYR SER          
SEQRES  17 C  399  TYR ILE ARG LYS THR ARG PRO ASP GLY ASN SER PHE TYR          
SEQRES  18 C  399  ARG ALA PHE GLY PHE SER HIS LEU GLU ALA LEU LEU ASP          
SEQRES  19 C  399  ASP SER LYS GLU LEU GLN ARG PHE LYS ALA VAL SER ALA          
SEQRES  20 C  399  LYS SER LYS GLU ASP LEU VAL SER GLN GLY PHE THR GLU          
SEQRES  21 C  399  PHE THR ILE GLU ASP PHE HIS ASN THR PHE MET ASP LEU          
SEQRES  22 C  399  ILE GLU GLN VAL GLU LYS GLN THR SER VAL ALA ASP LEU          
SEQRES  23 C  399  LEU ALA SER PHE ASN ASP GLN SER THR SER ASP TYR LEU          
SEQRES  24 C  399  VAL VAL TYR LEU ARG LEU LEU THR SER GLY TYR LEU GLN          
SEQRES  25 C  399  ARG GLU SER LYS PHE PHE GLU HIS PHE ILE GLU GLY GLY          
SEQRES  26 C  399  ARG THR VAL LYS GLU PHE CYS GLN GLN GLU VAL GLU PRO          
SEQRES  27 C  399  MET CYS LYS GLU SER ASP HIS ILE HIS ILE ILE ALA LEU          
SEQRES  28 C  399  ALA GLN ALA LEU SER VAL SER ILE GLN VAL GLU TYR MET          
SEQRES  29 C  399  ASP ARG GLY GLU GLY GLY THR THR ASN PRO HIS ILE PHE          
SEQRES  30 C  399  PRO GLU GLY SER GLU PRO LYS VAL TYR LEU LEU TYR ARG          
SEQRES  31 C  399  PRO GLY HIS TYR ASP ILE LEU TYR LYS                          
SEQRES   1 D   76  MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE          
SEQRES   2 D   76  THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL          
SEQRES   3 D   76  LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP          
SEQRES   4 D   76  GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP          
SEQRES   5 D   76  GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER          
SEQRES   6 D   76  THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY                  
SEQRES   1 E   76  MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE          
SEQRES   2 E   76  THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL          
SEQRES   3 E   76  LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP          
SEQRES   4 E   76  GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP          
SEQRES   5 E   76  GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER          
SEQRES   6 E   76  THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY                  
SEQRES   1 F   76  MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE          
SEQRES   2 F   76  THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL          
SEQRES   3 F   76  LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP          
SEQRES   4 F   76  GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP          
SEQRES   5 F   76  GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER          
SEQRES   6 F   76  THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY                  
SEQRES   1 G   76  MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE          
SEQRES   2 G   76  THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL          
SEQRES   3 G   76  LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP          
SEQRES   4 G   76  GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP          
SEQRES   5 G   76  GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER          
SEQRES   6 G   76  THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY                  
SEQRES   1 H   76  MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE          
SEQRES   2 H   76  THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL          
SEQRES   3 H   76  LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP          
SEQRES   4 H   76  GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP          
SEQRES   5 H   76  GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER          
SEQRES   6 H   76  THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY                  
SEQRES   1 I   76  MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE          
SEQRES   2 I   76  THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL          
SEQRES   3 I   76  LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP          
SEQRES   4 I   76  GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP          
SEQRES   5 I   76  GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER          
SEQRES   6 I   76  THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY                  
SEQRES   1 J  399  GLY ALA MET ALA LEU LYS ARG ILE HIS LYS GLU LEU ASN          
SEQRES   2 J  399  ASP LEU ALA ARG ASP PRO PRO ALA GLN CYS SER ALA GLY          
SEQRES   3 J  399  PRO VAL GLY ASP ASP MET PHE HIS TRP GLN ALA THR ILE          
SEQRES   4 J  399  MET GLY PRO ASN ASP SER PRO TYR GLN GLY GLY VAL PHE          
SEQRES   5 J  399  PHE LEU THR ILE HIS PHE PRO THR ASP TYR PRO PHE LYS          
SEQRES   6 J  399  PRO PRO LYS VAL ALA PHE THR THR ARG ILE TYR HIS PRO          
SEQRES   7 J  399  ASN ILE ASN SER ASN GLY SER ILE SER LEU ASP ILE LEU          
SEQRES   8 J  399  ARG SER GLN TRP SER PRO ALA LEU THR ILE SER LYS VAL          
SEQRES   9 J  399  LEU LEU SER ILE CYS SER LEU LEU CYS ASP PRO ASN PRO          
SEQRES  10 J  399  ASP ASP PRO LEU VAL PRO GLU ILE ALA ARG ILE TYR LYS          
SEQRES  11 J  399  THR ASP ARG GLU LYS TYR ASN ARG ILE ALA ARG GLU TRP          
SEQRES  12 J  399  THR GLN LYS TYR ALA MET GLY GLY SER ALA TYR ASP GLU          
SEQRES  13 J  399  ALA ILE MET ALA GLN GLN ASP ARG ILE GLN GLN GLU ILE          
SEQRES  14 J  399  ALA VAL GLN ASN PRO LEU VAL SER GLU ARG LEU GLU LEU          
SEQRES  15 J  399  SER VAL LEU TYR LYS GLU TYR ALA GLU ASP ASP ASN ILE          
SEQRES  16 J  399  TYR GLN GLN LYS ILE LYS ASP LEU HIS LYS LYS TYR SER          
SEQRES  17 J  399  TYR ILE ARG LYS THR ARG PRO ASP GLY ASN SER PHE TYR          
SEQRES  18 J  399  ARG ALA PHE GLY PHE SER HIS LEU GLU ALA LEU LEU ASP          
SEQRES  19 J  399  ASP SER LYS GLU LEU GLN ARG PHE LYS ALA VAL SER ALA          
SEQRES  20 J  399  LYS SER LYS GLU ASP LEU VAL SER GLN GLY PHE THR GLU          
SEQRES  21 J  399  PHE THR ILE GLU ASP PHE HIS ASN THR PHE MET ASP LEU          
SEQRES  22 J  399  ILE GLU GLN VAL GLU LYS GLN THR SER VAL ALA ASP LEU          
SEQRES  23 J  399  LEU ALA SER PHE ASN ASP GLN SER THR SER ASP TYR LEU          
SEQRES  24 J  399  VAL VAL TYR LEU ARG LEU LEU THR SER GLY TYR LEU GLN          
SEQRES  25 J  399  ARG GLU SER LYS PHE PHE GLU HIS PHE ILE GLU GLY GLY          
SEQRES  26 J  399  ARG THR VAL LYS GLU PHE CYS GLN GLN GLU VAL GLU PRO          
SEQRES  27 J  399  MET CYS LYS GLU SER ASP HIS ILE HIS ILE ILE ALA LEU          
SEQRES  28 J  399  ALA GLN ALA LEU SER VAL SER ILE GLN VAL GLU TYR MET          
SEQRES  29 J  399  ASP ARG GLY GLU GLY GLY THR THR ASN PRO HIS ILE PHE          
SEQRES  30 J  399  PRO GLU GLY SER GLU PRO LYS VAL TYR LEU LEU TYR ARG          
SEQRES  31 J  399  PRO GLY HIS TYR ASP ILE LEU TYR LYS                          
SEQRES   1 K  399  GLY ALA MET ALA LEU LYS ARG ILE HIS LYS GLU LEU ASN          
SEQRES   2 K  399  ASP LEU ALA ARG ASP PRO PRO ALA GLN CYS SER ALA GLY          
SEQRES   3 K  399  PRO VAL GLY ASP ASP MET PHE HIS TRP GLN ALA THR ILE          
SEQRES   4 K  399  MET GLY PRO ASN ASP SER PRO TYR GLN GLY GLY VAL PHE          
SEQRES   5 K  399  PHE LEU THR ILE HIS PHE PRO THR ASP TYR PRO PHE LYS          
SEQRES   6 K  399  PRO PRO LYS VAL ALA PHE THR THR ARG ILE TYR HIS PRO          
SEQRES   7 K  399  ASN ILE ASN SER ASN GLY SER ILE SER LEU ASP ILE LEU          
SEQRES   8 K  399  ARG SER GLN TRP SER PRO ALA LEU THR ILE SER LYS VAL          
SEQRES   9 K  399  LEU LEU SER ILE CYS SER LEU LEU CYS ASP PRO ASN PRO          
SEQRES  10 K  399  ASP ASP PRO LEU VAL PRO GLU ILE ALA ARG ILE TYR LYS          
SEQRES  11 K  399  THR ASP ARG GLU LYS TYR ASN ARG ILE ALA ARG GLU TRP          
SEQRES  12 K  399  THR GLN LYS TYR ALA MET GLY GLY SER ALA TYR ASP GLU          
SEQRES  13 K  399  ALA ILE MET ALA GLN GLN ASP ARG ILE GLN GLN GLU ILE          
SEQRES  14 K  399  ALA VAL GLN ASN PRO LEU VAL SER GLU ARG LEU GLU LEU          
SEQRES  15 K  399  SER VAL LEU TYR LYS GLU TYR ALA GLU ASP ASP ASN ILE          
SEQRES  16 K  399  TYR GLN GLN LYS ILE LYS ASP LEU HIS LYS LYS TYR SER          
SEQRES  17 K  399  TYR ILE ARG LYS THR ARG PRO ASP GLY ASN SER PHE TYR          
SEQRES  18 K  399  ARG ALA PHE GLY PHE SER HIS LEU GLU ALA LEU LEU ASP          
SEQRES  19 K  399  ASP SER LYS GLU LEU GLN ARG PHE LYS ALA VAL SER ALA          
SEQRES  20 K  399  LYS SER LYS GLU ASP LEU VAL SER GLN GLY PHE THR GLU          
SEQRES  21 K  399  PHE THR ILE GLU ASP PHE HIS ASN THR PHE MET ASP LEU          
SEQRES  22 K  399  ILE GLU GLN VAL GLU LYS GLN THR SER VAL ALA ASP LEU          
SEQRES  23 K  399  LEU ALA SER PHE ASN ASP GLN SER THR SER ASP TYR LEU          
SEQRES  24 K  399  VAL VAL TYR LEU ARG LEU LEU THR SER GLY TYR LEU GLN          
SEQRES  25 K  399  ARG GLU SER LYS PHE PHE GLU HIS PHE ILE GLU GLY GLY          
SEQRES  26 K  399  ARG THR VAL LYS GLU PHE CYS GLN GLN GLU VAL GLU PRO          
SEQRES  27 K  399  MET CYS LYS GLU SER ASP HIS ILE HIS ILE ILE ALA LEU          
SEQRES  28 K  399  ALA GLN ALA LEU SER VAL SER ILE GLN VAL GLU TYR MET          
SEQRES  29 K  399  ASP ARG GLY GLU GLY GLY THR THR ASN PRO HIS ILE PHE          
SEQRES  30 K  399  PRO GLU GLY SER GLU PRO LYS VAL TYR LEU LEU TYR ARG          
SEQRES  31 K  399  PRO GLY HIS TYR ASP ILE LEU TYR LYS                          
SEQRES   1 L  399  GLY ALA MET ALA LEU LYS ARG ILE HIS LYS GLU LEU ASN          
SEQRES   2 L  399  ASP LEU ALA ARG ASP PRO PRO ALA GLN CYS SER ALA GLY          
SEQRES   3 L  399  PRO VAL GLY ASP ASP MET PHE HIS TRP GLN ALA THR ILE          
SEQRES   4 L  399  MET GLY PRO ASN ASP SER PRO TYR GLN GLY GLY VAL PHE          
SEQRES   5 L  399  PHE LEU THR ILE HIS PHE PRO THR ASP TYR PRO PHE LYS          
SEQRES   6 L  399  PRO PRO LYS VAL ALA PHE THR THR ARG ILE TYR HIS PRO          
SEQRES   7 L  399  ASN ILE ASN SER ASN GLY SER ILE SER LEU ASP ILE LEU          
SEQRES   8 L  399  ARG SER GLN TRP SER PRO ALA LEU THR ILE SER LYS VAL          
SEQRES   9 L  399  LEU LEU SER ILE CYS SER LEU LEU CYS ASP PRO ASN PRO          
SEQRES  10 L  399  ASP ASP PRO LEU VAL PRO GLU ILE ALA ARG ILE TYR LYS          
SEQRES  11 L  399  THR ASP ARG GLU LYS TYR ASN ARG ILE ALA ARG GLU TRP          
SEQRES  12 L  399  THR GLN LYS TYR ALA MET GLY GLY SER ALA TYR ASP GLU          
SEQRES  13 L  399  ALA ILE MET ALA GLN GLN ASP ARG ILE GLN GLN GLU ILE          
SEQRES  14 L  399  ALA VAL GLN ASN PRO LEU VAL SER GLU ARG LEU GLU LEU          
SEQRES  15 L  399  SER VAL LEU TYR LYS GLU TYR ALA GLU ASP ASP ASN ILE          
SEQRES  16 L  399  TYR GLN GLN LYS ILE LYS ASP LEU HIS LYS LYS TYR SER          
SEQRES  17 L  399  TYR ILE ARG LYS THR ARG PRO ASP GLY ASN SER PHE TYR          
SEQRES  18 L  399  ARG ALA PHE GLY PHE SER HIS LEU GLU ALA LEU LEU ASP          
SEQRES  19 L  399  ASP SER LYS GLU LEU GLN ARG PHE LYS ALA VAL SER ALA          
SEQRES  20 L  399  LYS SER LYS GLU ASP LEU VAL SER GLN GLY PHE THR GLU          
SEQRES  21 L  399  PHE THR ILE GLU ASP PHE HIS ASN THR PHE MET ASP LEU          
SEQRES  22 L  399  ILE GLU GLN VAL GLU LYS GLN THR SER VAL ALA ASP LEU          
SEQRES  23 L  399  LEU ALA SER PHE ASN ASP GLN SER THR SER ASP TYR LEU          
SEQRES  24 L  399  VAL VAL TYR LEU ARG LEU LEU THR SER GLY TYR LEU GLN          
SEQRES  25 L  399  ARG GLU SER LYS PHE PHE GLU HIS PHE ILE GLU GLY GLY          
SEQRES  26 L  399  ARG THR VAL LYS GLU PHE CYS GLN GLN GLU VAL GLU PRO          
SEQRES  27 L  399  MET CYS LYS GLU SER ASP HIS ILE HIS ILE ILE ALA LEU          
SEQRES  28 L  399  ALA GLN ALA LEU SER VAL SER ILE GLN VAL GLU TYR MET          
SEQRES  29 L  399  ASP ARG GLY GLU GLY GLY THR THR ASN PRO HIS ILE PHE          
SEQRES  30 L  399  PRO GLU GLY SER GLU PRO LYS VAL TYR LEU LEU TYR ARG          
SEQRES  31 L  399  PRO GLY HIS TYR ASP ILE LEU TYR LYS                          
SEQRES   1 M   76  MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE          
SEQRES   2 M   76  THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL          
SEQRES   3 M   76  LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP          
SEQRES   4 M   76  GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP          
SEQRES   5 M   76  GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER          
SEQRES   6 M   76  THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY                  
SEQRES   1 N   76  MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE          
SEQRES   2 N   76  THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL          
SEQRES   3 N   76  LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP          
SEQRES   4 N   76  GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP          
SEQRES   5 N   76  GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER          
SEQRES   6 N   76  THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY                  
SEQRES   1 O   76  MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE          
SEQRES   2 O   76  THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL          
SEQRES   3 O   76  LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP          
SEQRES   4 O   76  GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP          
SEQRES   5 O   76  GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER          
SEQRES   6 O   76  THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY                  
SEQRES   1 P   76  MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE          
SEQRES   2 P   76  THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL          
SEQRES   3 P   76  LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP          
SEQRES   4 P   76  GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP          
SEQRES   5 P   76  GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER          
SEQRES   6 P   76  THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY                  
SEQRES   1 Q   76  MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE          
SEQRES   2 Q   76  THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL          
SEQRES   3 Q   76  LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP          
SEQRES   4 Q   76  GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP          
SEQRES   5 Q   76  GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER          
SEQRES   6 Q   76  THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY                  
SEQRES   1 R   76  MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE          
SEQRES   2 R   76  THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL          
SEQRES   3 R   76  LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP          
SEQRES   4 R   76  GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP          
SEQRES   5 R   76  GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER          
SEQRES   6 R   76  THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY                  
HELIX    1   1 GLY A   -1  ASP A   16  1                                  18    
HELIX    2   2 LEU A   86  ARG A   90  5                                   5    
HELIX    3   3 THR A   98  ASP A  112  1                                  15    
HELIX    4   4 VAL A  120  ASP A  130  1                                  11    
HELIX    5   5 ASP A  130  ALA A  146  1                                  17    
HELIX    6   6 SER A  150  ASN A 1045  1                                  22    
HELIX    7   7 VAL A 1056  TYR A 1061  1                                   6    
HELIX    8   8 ASP A 1065  TYR A 1079  1                                  15    
HELIX    9   9 ASN A 1090  LEU A 1104  1                                  15    
HELIX   10  10 ASP A 1107  GLN A 1128  1                                  22    
HELIX   11  11 THR A 1131  LYS A 1151  1                                  21    
HELIX   12  12 SER A 1154  ASN A 1163  1                                  10    
HELIX   13  13 ASP A 1164  GLU A 1186  1                                  23    
HELIX   14  14 GLU A 1186  GLU A 1191  1                                   6    
HELIX   15  15 HIS A 1192  ILE A 1194  5                                   3    
HELIX   16  16 THR A 1199  VAL A 1208  1                                  10    
HELIX   17  17 ASP A 1216  SER A 1228  1                                  13    
HELIX   18  18 ALA B    0  ASP B   16  1                                  17    
HELIX   19  19 LEU B   86  ARG B   90  5                                   5    
HELIX   20  20 THR B   98  ASP B  112  1                                  15    
HELIX   21  21 VAL B  120  ASP B  130  1                                  11    
HELIX   22  22 ASP B  130  ALA B  146  1                                  17    
HELIX   23  23 SER B  150  ASN B 1045  1                                  22    
HELIX   24  24 VAL B 1056  TYR B 1061  1                                   6    
HELIX   25  25 ASP B 1065  TYR B 1079  1                                  15    
HELIX   26  26 ASN B 1090  LEU B 1104  1                                  15    
HELIX   27  27 ASP B 1107  GLN B 1128  1                                  22    
HELIX   28  28 THR B 1131  LYS B 1151  1                                  21    
HELIX   29  29 SER B 1154  ASN B 1163  1                                  10    
HELIX   30  30 ASP B 1164  GLU B 1186  1                                  23    
HELIX   31  31 GLU B 1186  GLU B 1191  1                                   6    
HELIX   32  32 HIS B 1192  ILE B 1194  5                                   3    
HELIX   33  33 THR B 1199  VAL B 1208  1                                  10    
HELIX   34  34 ASP B 1216  SER B 1228  1                                  13    
HELIX   35  35 ALA C    0  ASP C   16  1                                  17    
HELIX   36  36 LEU C   86  ARG C   90  5                                   5    
HELIX   37  37 THR C   98  ASP C  112  1                                  15    
HELIX   38  38 VAL C  120  ASP C  130  1                                  11    
HELIX   39  39 ASP C  130  ALA C  146  1                                  17    
HELIX   40  40 SER C  150  ASN C 1045  1                                  22    
HELIX   41  41 VAL C 1056  TYR C 1061  1                                   6    
HELIX   42  42 ASP C 1065  TYR C 1079  1                                  15    
HELIX   43  43 ASN C 1090  LEU C 1104  1                                  15    
HELIX   44  44 ASP C 1107  GLN C 1128  1                                  22    
HELIX   45  45 THR C 1131  LYS C 1151  1                                  21    
HELIX   46  46 SER C 1154  ASN C 1163  1                                  10    
HELIX   47  47 ASP C 1164  GLU C 1186  1                                  23    
HELIX   48  48 GLU C 1186  GLU C 1191  1                                   6    
HELIX   49  49 HIS C 1192  ILE C 1194  5                                   3    
HELIX   50  50 THR C 1199  VAL C 1208  1                                  10    
HELIX   51  51 ASP C 1216  SER C 1228  1                                  13    
HELIX   52  52 THR D   22  GLY D   35  1                                  14    
HELIX   53  53 PRO D   37  ASP D   39  5                                   3    
HELIX   54  54 THR E   22  GLY E   35  1                                  14    
HELIX   55  55 PRO E   37  ASP E   39  5                                   3    
HELIX   56  56 THR F   22  GLY F   35  1                                  14    
HELIX   57  57 PRO F   37  ASP F   39  5                                   3    
HELIX   58  58 THR G   22  GLY G   35  1                                  14    
HELIX   59  59 PRO G   37  ASP G   39  5                                   3    
HELIX   60  60 THR G   55  ASN G   60  5                                   6    
HELIX   61  61 THR H   22  GLY H   35  1                                  14    
HELIX   62  62 PRO H   37  ASP H   39  5                                   3    
HELIX   63  63 THR H   55  ASN H   60  5                                   6    
HELIX   64  64 THR I   22  GLY I   35  1                                  14    
HELIX   65  65 PRO I   37  ASP I   39  5                                   3    
HELIX   66  66 THR I   55  ASN I   60  5                                   6    
HELIX   67  67 ALA J    0  ASP J   16  1                                  17    
HELIX   68  68 LEU J   86  ARG J   90  5                                   5    
HELIX   69  69 THR J   98  ASP J  112  1                                  15    
HELIX   70  70 VAL J  120  ASP J  130  1                                  11    
HELIX   71  71 ASP J  130  ALA J  146  1                                  17    
HELIX   72  72 SER J  150  ASN J 1045  1                                  22    
HELIX   73  73 VAL J 1056  TYR J 1061  1                                   6    
HELIX   74  74 ASP J 1065  TYR J 1079  1                                  15    
HELIX   75  75 ASN J 1090  LEU J 1104  1                                  15    
HELIX   76  76 ASP J 1107  GLN J 1128  1                                  22    
HELIX   77  77 THR J 1131  LYS J 1151  1                                  21    
HELIX   78  78 SER J 1154  ASN J 1163  1                                  10    
HELIX   79  79 ASP J 1164  GLU J 1186  1                                  23    
HELIX   80  80 GLU J 1186  GLU J 1191  1                                   6    
HELIX   81  81 HIS J 1192  ILE J 1194  5                                   3    
HELIX   82  82 THR J 1199  VAL J 1208  1                                  10    
HELIX   83  83 ASP J 1216  SER J 1228  1                                  13    
HELIX   84  84 ALA K    0  ASP K   16  1                                  17    
HELIX   85  85 LEU K   86  ARG K   90  5                                   5    
HELIX   86  86 THR K   98  ASP K  112  1                                  15    
HELIX   87  87 VAL K  120  ASP K  130  1                                  11    
HELIX   88  88 ASP K  130  ALA K  146  1                                  17    
HELIX   89  89 SER K  150  ASN K 1045  1                                  22    
HELIX   90  90 VAL K 1056  TYR K 1061  1                                   6    
HELIX   91  91 ASP K 1065  TYR K 1079  1                                  15    
HELIX   92  92 ASN K 1090  LEU K 1104  1                                  15    
HELIX   93  93 ASP K 1107  GLN K 1128  1                                  22    
HELIX   94  94 THR K 1131  LYS K 1151  1                                  21    
HELIX   95  95 SER K 1154  ASN K 1163  1                                  10    
HELIX   96  96 ASP K 1164  GLU K 1186  1                                  23    
HELIX   97  97 GLU K 1186  GLU K 1191  1                                   6    
HELIX   98  98 HIS K 1192  ILE K 1194  5                                   3    
HELIX   99  99 THR K 1199  VAL K 1208  1                                  10    
HELIX  100 100 ASP K 1216  SER K 1228  1                                  13    
HELIX  101 101 ALA L    0  ASP L   16  1                                  17    
HELIX  102 102 LEU L   86  ARG L   90  5                                   5    
HELIX  103 103 THR L   98  ASP L  112  1                                  15    
HELIX  104 104 VAL L  120  ASP L  130  1                                  11    
HELIX  105 105 ASP L  130  ALA L  146  1                                  17    
HELIX  106 106 ALA L 1025  ASN L 1045  1                                  21    
HELIX  107 107 VAL L 1056  TYR L 1061  1                                   6    
HELIX  108 108 ASP L 1065  TYR L 1079  1                                  15    
HELIX  109 109 ASN L 1090  LEU L 1104  1                                  15    
HELIX  110 110 ASP L 1107  GLN L 1128  1                                  22    
HELIX  111 111 THR L 1131  LYS L 1151  1                                  21    
HELIX  112 112 SER L 1154  ASN L 1163  1                                  10    
HELIX  113 113 ASP L 1164  GLU L 1186  1                                  23    
HELIX  114 114 GLU L 1186  GLU L 1191  1                                   6    
HELIX  115 115 HIS L 1192  ILE L 1194  5                                   3    
HELIX  116 116 THR L 1199  VAL L 1208  1                                  10    
HELIX  117 117 ASP L 1216  SER L 1228  1                                  13    
HELIX  118 118 THR M   22  GLY M   35  1                                  14    
HELIX  119 119 PRO M   37  ASP M   39  5                                   3    
HELIX  120 120 THR N   22  GLY N   35  1                                  14    
HELIX  121 121 PRO N   37  ASP N   39  5                                   3    
HELIX  122 122 THR O   22  GLY O   35  1                                  14    
HELIX  123 123 PRO O   37  ASP O   39  5                                   3    
HELIX  124 124 THR P   22  GLY P   35  1                                  14    
HELIX  125 125 PRO P   37  ASP P   39  5                                   3    
HELIX  126 126 THR P   55  ASN P   60  5                                   6    
HELIX  127 127 THR Q   22  GLY Q   35  1                                  14    
HELIX  128 128 PRO Q   37  ASP Q   39  5                                   3    
HELIX  129 129 THR Q   55  ASN Q   60  5                                   6    
HELIX  130 130 THR R   22  GLY R   35  1                                  14    
HELIX  131 131 PRO R   37  ASP R   39  5                                   3    
HELIX  132 132 THR R   55  ASN R   60  5                                   6    
SHEET    1   A 4 CYS A  21  VAL A  26  0                                        
SHEET    2   A 4 ASP A  29  MET A  38 -1  O  THR A  36   N  SER A  22           
SHEET    3   A 4 VAL A  49  HIS A  55 -1  O  PHE A  50   N  ILE A  37           
SHEET    4   A 4 LYS A  66  PHE A  69 -1  O  LYS A  66   N  HIS A  55           
SHEET    1   B 6 LEU A1052  GLU A1053  0                                        
SHEET    2   B 6 TYR A1081  ARG A1083 -1  O  ILE A1082   N  LEU A1052           
SHEET    3   B 6 HIS A1265  TYR A1270 -1  O  ILE A1268   N  ARG A1083           
SHEET    4   B 6 TYR A1258  ARG A1262 -1  N  ARG A1262   O  HIS A1265           
SHEET    5   B 6 GLN A1232  TYR A1235  1  N  GLU A1234   O  LEU A1259           
SHEET    6   B 6 PRO A1246  ILE A1248 -1  O  HIS A1247   N  VAL A1233           
SHEET    1   C 4 CYS B  21  VAL B  26  0                                        
SHEET    2   C 4 ASP B  29  MET B  38 -1  O  THR B  36   N  SER B  22           
SHEET    3   C 4 VAL B  49  HIS B  55 -1  O  PHE B  50   N  ILE B  37           
SHEET    4   C 4 LYS B  66  PHE B  69 -1  O  LYS B  66   N  HIS B  55           
SHEET    1   D 6 LEU B1052  GLU B1053  0                                        
SHEET    2   D 6 TYR B1081  ARG B1083 -1  O  ILE B1082   N  LEU B1052           
SHEET    3   D 6 HIS B1265  TYR B1270 -1  O  ILE B1268   N  ARG B1083           
SHEET    4   D 6 TYR B1258  ARG B1262 -1  N  ARG B1262   O  HIS B1265           
SHEET    5   D 6 GLN B1232  TYR B1235  1  N  GLU B1234   O  LEU B1259           
SHEET    6   D 6 PRO B1246  ILE B1248 -1  O  HIS B1247   N  VAL B1233           
SHEET    1   E 4 CYS C  21  VAL C  26  0                                        
SHEET    2   E 4 ASP C  29  MET C  38 -1  O  THR C  36   N  SER C  22           
SHEET    3   E 4 VAL C  49  HIS C  55 -1  O  PHE C  50   N  ILE C  37           
SHEET    4   E 4 LYS C  66  PHE C  69 -1  O  LYS C  66   N  HIS C  55           
SHEET    1   F 6 LEU C1052  GLU C1053  0                                        
SHEET    2   F 6 TYR C1081  ARG C1083 -1  O  ILE C1082   N  LEU C1052           
SHEET    3   F 6 HIS C1265  TYR C1270 -1  O  ILE C1268   N  ARG C1083           
SHEET    4   F 6 TYR C1258  ARG C1262 -1  N  ARG C1262   O  HIS C1265           
SHEET    5   F 6 GLN C1232  TYR C1235  1  N  GLU C1234   O  LEU C1259           
SHEET    6   F 6 PRO C1246  ILE C1248 -1  O  HIS C1247   N  VAL C1233           
SHEET    1   G 5 THR D  12  GLU D  16  0                                        
SHEET    2   G 5 GLN D   2  THR D   7 -1  N  VAL D   5   O  ILE D  13           
SHEET    3   G 5 THR D  66  LEU D  71  1  O  LEU D  67   N  PHE D   4           
SHEET    4   G 5 GLN D  41  PHE D  45 -1  N  ARG D  42   O  VAL D  70           
SHEET    5   G 5 LYS D  48  GLN D  49 -1  O  LYS D  48   N  PHE D  45           
SHEET    1   H 5 THR E  12  GLU E  16  0                                        
SHEET    2   H 5 GLN E   2  THR E   7 -1  N  VAL E   5   O  ILE E  13           
SHEET    3   H 5 THR E  66  LEU E  71  1  O  LEU E  67   N  PHE E   4           
SHEET    4   H 5 GLN E  41  PHE E  45 -1  N  ARG E  42   O  VAL E  70           
SHEET    5   H 5 LYS E  48  GLN E  49 -1  O  LYS E  48   N  PHE E  45           
SHEET    1   I 5 THR F  12  GLU F  16  0                                        
SHEET    2   I 5 GLN F   2  THR F   7 -1  N  VAL F   5   O  ILE F  13           
SHEET    3   I 5 THR F  66  LEU F  71  1  O  LEU F  67   N  PHE F   4           
SHEET    4   I 5 GLN F  41  PHE F  45 -1  N  ARG F  42   O  VAL F  70           
SHEET    5   I 5 LYS F  48  GLN F  49 -1  O  LYS F  48   N  PHE F  45           
SHEET    1   J 5 THR G  12  GLU G  16  0                                        
SHEET    2   J 5 GLN G   2  LYS G   6 -1  N  VAL G   5   O  ILE G  13           
SHEET    3   J 5 THR G  66  LEU G  71  1  O  LEU G  67   N  PHE G   4           
SHEET    4   J 5 GLN G  41  PHE G  45 -1  N  ARG G  42   O  VAL G  70           
SHEET    5   J 5 LYS G  48  GLN G  49 -1  O  LYS G  48   N  PHE G  45           
SHEET    1   K 5 THR H  12  GLU H  16  0                                        
SHEET    2   K 5 GLN H   2  LYS H   6 -1  N  VAL H   5   O  ILE H  13           
SHEET    3   K 5 THR H  66  LEU H  71  1  O  LEU H  67   N  PHE H   4           
SHEET    4   K 5 GLN H  41  PHE H  45 -1  N  ARG H  42   O  VAL H  70           
SHEET    5   K 5 LYS H  48  GLN H  49 -1  O  LYS H  48   N  PHE H  45           
SHEET    1   L 5 THR I  12  GLU I  16  0                                        
SHEET    2   L 5 GLN I   2  LYS I   6 -1  N  VAL I   5   O  ILE I  13           
SHEET    3   L 5 THR I  66  LEU I  71  1  O  LEU I  67   N  PHE I   4           
SHEET    4   L 5 GLN I  41  PHE I  45 -1  N  ARG I  42   O  VAL I  70           
SHEET    5   L 5 LYS I  48  GLN I  49 -1  O  LYS I  48   N  PHE I  45           
SHEET    1   M 4 CYS J  21  VAL J  26  0                                        
SHEET    2   M 4 ASP J  29  MET J  38 -1  O  THR J  36   N  SER J  22           
SHEET    3   M 4 VAL J  49  HIS J  55 -1  O  PHE J  50   N  ILE J  37           
SHEET    4   M 4 LYS J  66  PHE J  69 -1  O  LYS J  66   N  HIS J  55           
SHEET    1   N 6 LEU J1052  GLU J1053  0                                        
SHEET    2   N 6 TYR J1081  ARG J1083 -1  O  ILE J1082   N  LEU J1052           
SHEET    3   N 6 HIS J1265  TYR J1270 -1  O  ILE J1268   N  ARG J1083           
SHEET    4   N 6 TYR J1258  ARG J1262 -1  N  ARG J1262   O  HIS J1265           
SHEET    5   N 6 GLN J1232  TYR J1235  1  N  GLU J1234   O  LEU J1259           
SHEET    6   N 6 PRO J1246  ILE J1248 -1  O  HIS J1247   N  VAL J1233           
SHEET    1   O 4 CYS K  21  VAL K  26  0                                        
SHEET    2   O 4 ASP K  29  MET K  38 -1  O  THR K  36   N  SER K  22           
SHEET    3   O 4 VAL K  49  HIS K  55 -1  O  PHE K  50   N  ILE K  37           
SHEET    4   O 4 LYS K  66  PHE K  69 -1  O  LYS K  66   N  HIS K  55           
SHEET    1   P 6 LEU K1052  GLU K1053  0                                        
SHEET    2   P 6 TYR K1081  ARG K1083 -1  O  ILE K1082   N  LEU K1052           
SHEET    3   P 6 HIS K1265  TYR K1270 -1  O  ILE K1268   N  ARG K1083           
SHEET    4   P 6 TYR K1258  ARG K1262 -1  N  ARG K1262   O  HIS K1265           
SHEET    5   P 6 GLN K1232  TYR K1235  1  N  GLU K1234   O  LEU K1259           
SHEET    6   P 6 PRO K1246  ILE K1248 -1  O  HIS K1247   N  VAL K1233           
SHEET    1   Q 4 CYS L  21  VAL L  26  0                                        
SHEET    2   Q 4 ASP L  29  MET L  38 -1  O  THR L  36   N  SER L  22           
SHEET    3   Q 4 VAL L  49  HIS L  55 -1  O  PHE L  50   N  ILE L  37           
SHEET    4   Q 4 LYS L  66  PHE L  69 -1  O  LYS L  66   N  HIS L  55           
SHEET    1   R 6 LEU L1052  GLU L1053  0                                        
SHEET    2   R 6 TYR L1081  ARG L1083 -1  O  ILE L1082   N  LEU L1052           
SHEET    3   R 6 HIS L1265  TYR L1270 -1  O  ILE L1268   N  ARG L1083           
SHEET    4   R 6 TYR L1258  ARG L1262 -1  N  ARG L1262   O  HIS L1265           
SHEET    5   R 6 GLN L1232  TYR L1235  1  N  GLU L1234   O  LEU L1259           
SHEET    6   R 6 PRO L1246  ILE L1248 -1  O  HIS L1247   N  VAL L1233           
SHEET    1   S 5 THR M  12  GLU M  16  0                                        
SHEET    2   S 5 GLN M   2  THR M   7 -1  N  VAL M   5   O  ILE M  13           
SHEET    3   S 5 THR M  66  LEU M  71  1  O  LEU M  67   N  PHE M   4           
SHEET    4   S 5 GLN M  41  PHE M  45 -1  N  ARG M  42   O  VAL M  70           
SHEET    5   S 5 LYS M  48  GLN M  49 -1  O  LYS M  48   N  PHE M  45           
SHEET    1   T 5 THR N  12  GLU N  16  0                                        
SHEET    2   T 5 GLN N   2  THR N   7 -1  N  VAL N   5   O  ILE N  13           
SHEET    3   T 5 THR N  66  LEU N  71  1  O  LEU N  67   N  PHE N   4           
SHEET    4   T 5 GLN N  41  PHE N  45 -1  N  ARG N  42   O  VAL N  70           
SHEET    5   T 5 LYS N  48  GLN N  49 -1  O  LYS N  48   N  PHE N  45           
SHEET    1   U 5 THR O  12  GLU O  16  0                                        
SHEET    2   U 5 GLN O   2  THR O   7 -1  N  VAL O   5   O  ILE O  13           
SHEET    3   U 5 THR O  66  LEU O  71  1  O  LEU O  67   N  PHE O   4           
SHEET    4   U 5 GLN O  41  PHE O  45 -1  N  ARG O  42   O  VAL O  70           
SHEET    5   U 5 LYS O  48  GLN O  49 -1  O  LYS O  48   N  PHE O  45           
SHEET    1   V 5 THR P  12  GLU P  16  0                                        
SHEET    2   V 5 GLN P   2  LYS P   6 -1  N  VAL P   5   O  ILE P  13           
SHEET    3   V 5 THR P  66  LEU P  71  1  O  LEU P  67   N  PHE P   4           
SHEET    4   V 5 GLN P  41  PHE P  45 -1  N  ARG P  42   O  VAL P  70           
SHEET    5   V 5 LYS P  48  GLN P  49 -1  O  LYS P  48   N  PHE P  45           
SHEET    1   W 5 THR Q  12  GLU Q  16  0                                        
SHEET    2   W 5 GLN Q   2  LYS Q   6 -1  N  VAL Q   5   O  ILE Q  13           
SHEET    3   W 5 THR Q  66  LEU Q  71  1  O  LEU Q  67   N  PHE Q   4           
SHEET    4   W 5 GLN Q  41  PHE Q  45 -1  N  ARG Q  42   O  VAL Q  70           
SHEET    5   W 5 LYS Q  48  GLN Q  49 -1  O  LYS Q  48   N  PHE Q  45           
SHEET    1   X 5 THR R  12  GLU R  16  0                                        
SHEET    2   X 5 GLN R   2  LYS R   6 -1  N  VAL R   5   O  ILE R  13           
SHEET    3   X 5 THR R  66  LEU R  71  1  O  LEU R  67   N  PHE R   4           
SHEET    4   X 5 GLN R  41  PHE R  45 -1  N  ARG R  42   O  VAL R  70           
SHEET    5   X 5 LYS R  48  GLN R  49 -1  O  LYS R  48   N  PHE R  45           
SSBOND   1 CYS A   21    CYS A  107                          1555   1555  2.04  
SSBOND   2 CYS B   21    CYS B  107                          1555   1555  2.04  
SSBOND   3 CYS C   21    CYS C  107                          1555   1555  2.04  
SSBOND   4 CYS J   21    CYS J  107                          1555   1555  2.04  
SSBOND   5 CYS K   21    CYS K  107                          1555   1555  2.04  
SSBOND   6 CYS L   21    CYS L  107                          1555   1555  2.04  
CISPEP   1 TYR A   60    PRO A   61          0        -7.60                     
CISPEP   2 TYR B   60    PRO B   61          0        -7.60                     
CISPEP   3 TYR C   60    PRO C   61          0        -7.59                     
CISPEP   4 TYR J   60    PRO J   61          0        -7.69                     
CISPEP   5 TYR K   60    PRO K   61          0        -7.62                     
CISPEP   6 TYR L   60    PRO L   61          0        -7.60                     
CRYST1  134.566  104.928  148.479  90.00 104.19  90.00 P 1 21 1     24          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.007431  0.000000  0.001879        0.00000                         
SCALE2      0.000000  0.009530  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006947        0.00000                         
ATOM     10  N   MET A   1       3.991 -63.855  28.189  1.00166.74           N  
ANISOU   10  N   MET A   1    22393  21339  19622  -5805    242  -1636       N  
ATOM     11  CA  MET A   1       4.561 -63.863  26.845  1.00166.40           C  
ANISOU   11  CA  MET A   1    22187  21570  19469  -5440    288  -1897       C  
ATOM     12  C   MET A   1       4.590 -65.284  26.305  1.00146.71           C  
ANISOU   12  C   MET A   1    19489  19655  16600  -5162    452  -1814       C  
ATOM     13  O   MET A   1       4.486 -65.499  25.097  1.00135.55           O  
ANISOU   13  O   MET A   1    17875  18657  14972  -4958    492  -2029       O  
ATOM     14  CB  MET A   1       5.975 -63.279  26.837  1.00169.21           C  
ANISOU   14  CB  MET A   1    22717  21506  20068  -5135    258  -1902       C  
ATOM     15  CG  MET A   1       6.234 -62.244  27.913  1.00142.20           C  
ANISOU   15  CG  MET A   1    19563  17415  17051  -5337     89  -1808       C  
ATOM     16  SD  MET A   1       6.289 -63.009  29.542  1.00245.91           S  
ANISOU   16  SD  MET A   1    32911  30341  30183  -5476     62  -1351       S  
ATOM     17  CE  MET A   1       7.409 -64.372  29.228  1.00179.33           C  
ANISOU   17  CE  MET A   1    24381  22226  21529  -5002    236  -1212       C  
ATOM     18  N   ALA A   2       4.738 -66.247  27.212  1.00141.63           N  
ANISOU   18  N   ALA A   2    18918  19023  15872  -5139    533  -1506       N  
ATOM     19  CA  ALA A   2       4.669 -67.659  26.861  1.00136.49           C  
ANISOU   19  CA  ALA A   2    18088  18877  14894  -4896    685  -1410       C  
ATOM     20  C   ALA A   2       3.309 -67.979  26.246  1.00106.45           C  
ANISOU   20  C   ALA A   2    13978  15599  10871  -5077    710  -1582       C  
ATOM     21  O   ALA A   2       3.227 -68.593  25.181  1.00 98.93           O  
ANISOU   21  O   ALA A   2    12800  15110   9677  -4810    758  -1709       O  
ATOM     22  CB  ALA A   2       4.923 -68.520  28.088  1.00105.01           C  
ANISOU   22  CB  ALA A   2    14256  14765  10877  -4905    748  -1088       C  
ATOM     23  N   LEU A   3       2.246 -67.547  26.920  1.00129.59           N  
ANISOU   23  N   LEU A   3    16895  18446  13897  -5535    671  -1581       N  
ATOM     24  CA  LEU A   3       0.889 -67.768  26.430  1.00133.68           C  
ANISOU   24  CA  LEU A   3    17082  19433  14279  -5773    692  -1759       C  
ATOM     25  C   LEU A   3       0.680 -67.095  25.078  1.00119.79           C  
ANISOU   25  C   LEU A   3    15135  17871  12507  -5703    565  -2134       C  
ATOM     26  O   LEU A   3       0.190 -67.724  24.133  1.00141.49           O  
ANISOU   26  O   LEU A   3    17577  21165  15016  -5546    574  -2296       O  
ATOM     27  CB  LEU A   3      -0.144 -67.250  27.432  1.00135.00           C  
ANISOU   27  CB  LEU A   3    17299  19384  14609  -6329    691  -1680       C  
ATOM     28  CG  LEU A   3      -1.610 -67.465  27.035  1.00132.46           C  
ANISOU   28  CG  LEU A   3    16592  19530  14206  -6643    736  -1860       C  
ATOM     29  CD1 LEU A   3      -2.148 -68.778  27.599  1.00112.60           C  
ANISOU   29  CD1 LEU A   3    13913  17409  11462  -6651    952  -1658       C  
ATOM     30  CD2 LEU A   3      -2.478 -66.285  27.455  1.00148.58           C  
ANISOU   30  CD2 LEU A   3    18687  21231  16535  -7201    651  -1943       C  
ATOM     31  N   LYS A   4       1.053 -65.818  24.996  1.00106.70           N  
ANISOU   31  N   LYS A   4    13668  15769  11103  -5801    432  -2283       N  
ATOM     32  CA  LYS A   4       0.927 -65.072  23.746  1.00138.95           C  
ANISOU   32  CA  LYS A   4    17628  19998  15170  -5728    303  -2673       C  
ATOM     33  C   LYS A   4       1.600 -65.832  22.604  1.00134.43           C  
ANISOU   33  C   LYS A   4    16945  19861  14270  -5205    359  -2735       C  
ATOM     34  O   LYS A   4       1.016 -66.016  21.524  1.00115.29           O  
ANISOU   34  O   LYS A   4    14266  17919  11620  -5120    290  -2990       O  
ATOM     35  CB  LYS A   4       1.528 -63.668  23.879  1.00133.62           C  
ANISOU   35  CB  LYS A   4    17224  18727  14817  -5800    185  -2805       C  
ATOM     36  CG  LYS A   4       1.600 -62.912  22.557  1.00157.36           C  
ANISOU   36  CG  LYS A   4    20151  21873  17767  -5648     73  -3231       C  
ATOM     37  CD  LYS A   4       2.223 -61.529  22.709  1.00163.28           C  
ANISOU   37  CD  LYS A   4    21162  22020  18859  -5689    -24  -3386       C  
ATOM     38  CE  LYS A   4       1.244 -60.535  23.310  1.00176.64           C  
ANISOU   38  CE  LYS A   4    22899  23329  20886  -6217   -175  -3504       C  
ATOM     39  NZ  LYS A   4       1.790 -59.147  23.292  1.00172.53           N  
ANISOU   39  NZ  LYS A   4    22610  22238  20705  -6218   -294  -3724       N  
ATOM     40  N   ARG A   5       2.820 -66.295  22.869  1.00106.31           N  
ANISOU   40  N   ARG A   5    13580  16124  10688  -4864    477  -2488       N  
ATOM     41  CA  ARG A   5       3.592 -67.056  21.895  1.00103.75           C  
ANISOU   41  CA  ARG A   5    13208  16136  10077  -4368    567  -2469       C  
ATOM     42  C   ARG A   5       2.866 -68.324  21.462  1.00 82.13           C  
ANISOU   42  C   ARG A   5    10188  14000   7019  -4244    609  -2425       C  
ATOM     43  O   ARG A   5       2.790 -68.622  20.271  1.00125.39           O  
ANISOU   43  O   ARG A   5    15515  19907  12220  -3971    572  -2586       O  
ATOM     44  CB  ARG A   5       4.970 -67.407  22.459  1.00118.03           C  
ANISOU   44  CB  ARG A   5    15258  17598  11989  -4096    701  -2175       C  
ATOM     45  CG  ARG A   5       5.675 -68.542  21.733  1.00 92.23           C  
ANISOU   45  CG  ARG A   5    11943  14664   8437  -3629    841  -2037       C  
ATOM     46  CD  ARG A   5       6.431 -68.079  20.503  1.00 81.24           C  
ANISOU   46  CD  ARG A   5    10598  13354   6915  -3310    873  -2210       C  
ATOM     47  NE  ARG A   5       7.288 -69.145  19.993  1.00 75.81           N  
ANISOU   47  NE  ARG A   5     9934  12859   6010  -2879   1038  -1994       N  
ATOM     48  CZ  ARG A   5       8.488 -68.950  19.460  1.00104.71           C  
ANISOU   48  CZ  ARG A   5    13740  16372   9672  -2583   1174  -1951       C  
ATOM     49  NH1 ARG A   5       9.193 -69.985  19.025  1.00 83.66           N  
ANISOU   49  NH1 ARG A   5    11099  13868   6820  -2223   1332  -1724       N  
ATOM     50  NH2 ARG A   5       8.983 -67.720  19.366  1.00106.23           N  
ANISOU   50  NH2 ARG A   5    14051  16244  10070  -2648   1166  -2136       N  
ATOM     51  N   ILE A   6       2.335 -69.064  22.431  1.00110.97           N  
ANISOU   51  N   ILE A   6    13776  17686  10700  -4428    684  -2211       N  
ATOM     52  CA  ILE A   6       1.566 -70.268  22.128  1.00 96.76           C  
ANISOU   52  CA  ILE A   6    11676  16445   8644  -4324    734  -2185       C  
ATOM     53  C   ILE A   6       0.408 -69.948  21.178  1.00108.00           C  
ANISOU   53  C   ILE A   6    12767  18306   9961  -4472    579  -2530       C  
ATOM     54  O   ILE A   6       0.166 -70.677  20.204  1.00113.01           O  
ANISOU   54  O   ILE A   6    13169  19449  10322  -4174    539  -2622       O  
ATOM     55  CB  ILE A   6       1.054 -70.955  23.414  1.00 79.89           C  
ANISOU   55  CB  ILE A   6     9524  14258   6574  -4568    859  -1946       C  
ATOM     56  CG1 ILE A   6       2.233 -71.456  24.248  1.00 85.61           C  
ANISOU   56  CG1 ILE A   6    10555  14620   7352  -4353    977  -1631       C  
ATOM     57  CG2 ILE A   6       0.121 -72.113  23.085  1.00104.31           C  
ANISOU   57  CG2 ILE A   6    12247  17946   9438  -4484    918  -1977       C  
ATOM     58  CD1 ILE A   6       1.827 -72.167  25.519  1.00124.58           C  
ANISOU   58  CD1 ILE A   6    15528  19512  12294  -4549   1099  -1405       C  
ATOM     59  N   HIS A   7      -0.285 -68.842  21.443  1.00128.31           N  
ANISOU   59  N   HIS A   7    15326  20661  12765  -4922    469  -2725       N  
ATOM     60  CA  HIS A   7      -1.354 -68.397  20.552  1.00106.31           C  
ANISOU   60  CA  HIS A   7    12230  18232   9932  -5105    288  -3099       C  
ATOM     61  C   HIS A   7      -0.839 -68.120  19.140  1.00129.93           C  
ANISOU   61  C   HIS A   7    15232  21449  12688  -4720    151  -3351       C  
ATOM     62  O   HIS A   7      -1.477 -68.506  18.152  1.00126.56           O  
ANISOU   62  O   HIS A   7    14507  21556  12025  -4587     18  -3568       O  
ATOM     63  CB  HIS A   7      -2.070 -67.168  21.116  1.00148.90           C  
ANISOU   63  CB  HIS A   7    17661  23249  15666  -5669    196  -3261       C  
ATOM     64  CG  HIS A   7      -3.161 -67.500  22.087  1.00156.44           C  
ANISOU   64  CG  HIS A   7    18431  24247  16762  -6119    295  -3133       C  
ATOM     65  ND1 HIS A   7      -3.226 -66.952  23.350  1.00165.80           N  
ANISOU   65  ND1 HIS A   7    19864  24910  18222  -6512    377  -2924       N  
ATOM     66  CD2 HIS A   7      -4.237 -68.316  21.977  1.00120.82           C  
ANISOU   66  CD2 HIS A   7    13509  20248  12150  -6237    340  -3180       C  
ATOM     67  CE1 HIS A   7      -4.289 -67.420  23.978  1.00147.94           C  
ANISOU   67  CE1 HIS A   7    17375  22841  15995  -6866    496  -2833       C  
ATOM     68  NE2 HIS A   7      -4.919 -68.250  23.166  1.00154.80           N  
ANISOU   68  NE2 HIS A   7    17820  24340  16657  -6710    486  -2999       N  
ATOM     69  N   LYS A   8       0.314 -67.462  19.045  1.00131.02           N  
ANISOU   69  N   LYS A   8    15707  21195  12878  -4531    183  -3323       N  
ATOM     70  CA  LYS A   8       0.915 -67.206  17.735  1.00123.43           C  
ANISOU   70  CA  LYS A   8    14808  20439  11652  -4145    108  -3531       C  
ATOM     71  C   LYS A   8       1.213 -68.509  16.990  1.00101.13           C  
ANISOU   71  C   LYS A   8    11875  18111   8438  -3660    170  -3371       C  
ATOM     72  O   LYS A   8       0.937 -68.628  15.790  1.00150.02           O  
ANISOU   72  O   LYS A   8    17928  24758  14316  -3430     26  -3591       O  
ATOM     73  CB  LYS A   8       2.193 -66.370  17.866  1.00 88.80           C  
ANISOU   73  CB  LYS A   8    10788  15537   7415  -4010    200  -3490       C  
ATOM     74  CG  LYS A   8       1.996 -65.003  18.514  1.00153.25           C  
ANISOU   74  CG  LYS A   8    19088  23164  15975  -4425    113  -3665       C  
ATOM     75  CD  LYS A   8       3.306 -64.221  18.562  1.00131.99           C  
ANISOU   75  CD  LYS A   8    16713  20000  13438  -4227    205  -3648       C  
ATOM     76  CE  LYS A   8       3.668 -63.639  17.201  1.00157.96           C  
ANISOU   76  CE  LYS A   8    20041  23501  16477  -3946    157  -3994       C  
ATOM     77  NZ  LYS A   8       3.024 -62.316  16.956  1.00141.69           N  
ANISOU   77  NZ  LYS A   8    17981  21256  14598  -4250    -43  -4434       N  
ATOM     78  N   GLU A   9       1.763 -69.487  17.704  1.00120.54           N  
ANISOU   78  N   GLU A   9    14413  20470  10917  -3500    363  -2991       N  
ATOM     79  CA  GLU A   9       2.105 -70.771  17.097  1.00122.34           C  
ANISOU   79  CA  GLU A   9    14571  21086  10825  -3033    434  -2801       C  
ATOM     80  C   GLU A   9       0.854 -71.483  16.598  1.00106.31           C  
ANISOU   80  C   GLU A   9    12137  19648   8606  -3038    287  -2946       C  
ATOM     81  O   GLU A   9       0.862 -72.082  15.520  1.00147.94           O  
ANISOU   81  O   GLU A   9    17307  25359  13546  -2652    200  -2987       O  
ATOM     82  CB  GLU A   9       2.881 -71.669  18.071  1.00 82.21           C  
ANISOU   82  CB  GLU A   9     9648  15733   5854  -2904    657  -2397       C  
ATOM     83  CG  GLU A   9       4.240 -71.120  18.496  1.00143.62           C  
ANISOU   83  CG  GLU A   9    17786  22959  13825  -2829    794  -2238       C  
ATOM     84  CD  GLU A   9       5.308 -72.197  18.619  1.00131.05           C  
ANISOU   84  CD  GLU A   9    16339  21287  12167  -2447    982  -1895       C  
ATOM     85  OE1 GLU A   9       5.149 -73.267  17.996  1.00115.82           O  
ANISOU   85  OE1 GLU A   9    14280  19759   9967  -2134    996  -1810       O  
ATOM     86  OE2 GLU A   9       6.308 -71.973  19.339  1.00 93.09           O  
ANISOU   86  OE2 GLU A   9    11767  16002   7601  -2455   1101  -1719       O  
ATOM     87  N   LEU A  10      -0.219 -71.412  17.378  1.00 91.75           N  
ANISOU   87  N   LEU A  10    10062  17819   6980  -3474    259  -3016       N  
ATOM     88  CA  LEU A  10      -1.475 -72.029  16.967  1.00101.45           C  
ANISOU   88  CA  LEU A  10    10841  19608   8097  -3527    129  -3185       C  
ATOM     89  C   LEU A  10      -2.033 -71.340  15.724  1.00123.25           C  
ANISOU   89  C   LEU A  10    13428  22704  10698  -3522   -159  -3596       C  
ATOM     90  O   LEU A  10      -2.591 -71.992  14.834  1.00120.02           O  
ANISOU   90  O   LEU A  10    12717  22844  10038  -3277   -322  -3725       O  
ATOM     91  CB  LEU A  10      -2.491 -71.998  18.106  1.00108.72           C  
ANISOU   91  CB  LEU A  10    11555  20443   9310  -4048    208  -3173       C  
ATOM     92  CG  LEU A  10      -3.789 -72.760  17.840  1.00 99.03           C  
ANISOU   92  CG  LEU A  10     9806  19796   8024  -4118    135  -3321       C  
ATOM     93  CD1 LEU A  10      -3.492 -74.188  17.406  1.00 98.32           C  
ANISOU   93  CD1 LEU A  10     9604  20089   7662  -3572    189  -3139       C  
ATOM     94  CD2 LEU A  10      -4.677 -72.743  19.073  1.00135.23           C  
ANISOU   94  CD2 LEU A  10    14234  24255  12894  -4646    297  -3253       C  
ATOM     95  N   ASN A  11      -1.870 -70.020  15.664  1.00157.86           N  
ANISOU   95  N   ASN A  11    18004  26749  15227  -3775   -240  -3816       N  
ATOM     96  CA  ASN A  11      -2.237 -69.260  14.473  1.00133.41           C  
ANISOU   96  CA  ASN A  11    14819  23911  11957  -3747   -518  -4238       C  
ATOM     97  C   ASN A  11      -1.477 -69.735  13.236  1.00123.82           C  
ANISOU   97  C   ASN A  11    13734  23032  10281  -3146   -574  -4215       C  
ATOM     98  O   ASN A  11      -2.074 -69.960  12.183  1.00141.20           O  
ANISOU   98  O   ASN A  11    15697  25757  12196  -2968   -825  -4458       O  
ATOM     99  CB  ASN A  11      -2.010 -67.762  14.695  1.00154.21           C  
ANISOU   99  CB  ASN A  11    17707  26040  14844  -4074   -557  -4462       C  
ATOM    100  CG  ASN A  11      -3.048 -67.144  15.611  1.00170.72           C  
ANISOU  100  CG  ASN A  11    19627  27884  17355  -4704   -594  -4583       C  
ATOM    101  OD1 ASN A  11      -4.221 -67.513  15.574  1.00175.93           O  
ANISOU  101  OD1 ASN A  11    19881  28903  18060  -4938   -702  -4718       O  
ATOM    102  ND2 ASN A  11      -2.620 -66.195  16.439  1.00162.91           N  
ANISOU  102  ND2 ASN A  11    18939  26270  16690  -4981   -502  -4526       N  
ATOM    103  N   ASP A  12      -0.161 -69.889  13.370  1.00164.41           N  
ANISOU  103  N   ASP A  12    19249  27868  15352  -2840   -346  -3912       N  
ATOM    104  CA  ASP A  12       0.665 -70.367  12.259  1.00175.54           C  
ANISOU  104  CA  ASP A  12    20832  29542  16324  -2278   -337  -3817       C  
ATOM    105  C   ASP A  12       0.283 -71.778  11.819  1.00148.28           C  
ANISOU  105  C   ASP A  12    17134  26600  12606  -1927   -399  -3646       C  
ATOM    106  O   ASP A  12       0.203 -72.061  10.623  1.00140.81           O  
ANISOU  106  O   ASP A  12    16144  26032  11324  -1554   -574  -3718       O  
ATOM    107  CB  ASP A  12       2.154 -70.318  12.619  1.00209.11           C  
ANISOU  107  CB  ASP A  12    25496  33327  20630  -2068    -35  -3494       C  
ATOM    108  CG  ASP A  12       3.028 -71.012  11.584  1.00195.91           C  
ANISOU  108  CG  ASP A  12    24006  31906  18524  -1497     42  -3299       C  
ATOM    109  OD1 ASP A  12       3.209 -70.455  10.482  1.00142.12           O  
ANISOU  109  OD1 ASP A  12    17309  25194  11496  -1286    -63  -3466       O  
ATOM    110  OD2 ASP A  12       3.546 -72.113  11.879  1.00196.27           O  
ANISOU  110  OD2 ASP A  12    24099  31924  18551  -1243    215  -2918       O  
ATOM    111  N   LEU A  13       0.054 -72.662  12.786  1.00159.88           N  
ANISOU  111  N   LEU A  13    18457  27997  14291  -2014   -251  -3384       N  
ATOM    112  CA  LEU A  13      -0.288 -74.046  12.482  1.00132.55           C  
ANISOU  112  CA  LEU A  13    14755  24970  10637  -1668   -286  -3218       C  
ATOM    113  C   LEU A  13      -1.659 -74.131  11.825  1.00125.93           C  
ANISOU  113  C   LEU A  13    13447  24702   9699  -1751   -608  -3566       C  
ATOM    114  O   LEU A  13      -1.917 -75.028  11.023  1.00142.57           O  
ANISOU  114  O   LEU A  13    15367  27280  11523  -1350   -761  -3542       O  
ATOM    115  CB  LEU A  13      -0.249 -74.903  13.750  1.00105.73           C  
ANISOU  115  CB  LEU A  13    11315  21347   7513  -1770    -38  -2908       C  
ATOM    116  CG  LEU A  13      -0.390 -76.415  13.557  1.00124.91           C  
ANISOU  116  CG  LEU A  13    13555  24125   9781  -1357    -15  -2696       C  
ATOM    117  CD1 LEU A  13       0.695 -76.950  12.630  1.00137.87           C  
ANISOU  117  CD1 LEU A  13    15491  25803  11089   -781     12  -2466       C  
ATOM    118  CD2 LEU A  13      -0.345 -77.122  14.898  1.00106.90           C  
ANISOU  118  CD2 LEU A  13    11265  21576   7774  -1505    242  -2445       C  
ATOM    119  N   ALA A  14      -2.534 -73.189  12.168  1.00144.53           N  
ANISOU  119  N   ALA A  14    15607  26996  12311  -2272   -723  -3888       N  
ATOM    120  CA  ALA A  14      -3.864 -73.134  11.572  1.00153.39           C  
ANISOU  120  CA  ALA A  14    16247  28626  13406  -2426  -1043  -4269       C  
ATOM    121  C   ALA A  14      -3.832 -72.517  10.171  1.00134.15           C  
ANISOU  121  C   ALA A  14    13886  26402  10684  -2175  -1338  -4548       C  
ATOM    122  O   ALA A  14      -4.679 -72.823   9.331  1.00130.61           O  
ANISOU  122  O   ALA A  14    13096  26387  10143  -2026  -1615  -4742       O  
ATOM    123  CB  ALA A  14      -4.817 -72.364  12.474  1.00171.47           C  
ANISOU  123  CB  ALA A  14    18309  30708  16135  -3103  -1029  -4480       C  
ATOM    124  N   ARG A  15      -2.850 -71.651   9.930  1.00164.11           N  
ANISOU  124  N   ARG A  15    18138  29797  14419  -2098  -1246  -4522       N  
ATOM    125  CA  ARG A  15      -2.694 -70.996   8.632  1.00147.90           C  
ANISOU  125  CA  ARG A  15    16245  27805  12145  -1832  -1453  -4722       C  
ATOM    126  C   ARG A  15      -2.456 -72.000   7.500  1.00164.20           C  
ANISOU  126  C   ARG A  15    18322  30249  13819  -1209  -1565  -4528       C  
ATOM    127  O   ARG A  15      -3.175 -72.004   6.501  1.00144.36           O  
ANISOU  127  O   ARG A  15    15603  28095  11152  -1059  -1878  -4758       O  
ATOM    128  CB  ARG A  15      -1.555 -69.974   8.680  1.00168.51           C  
ANISOU  128  CB  ARG A  15    19350  29917  14758  -1839  -1266  -4698       C  
ATOM    129  CG  ARG A  15      -1.042 -69.541   7.316  1.00191.65           C  
ANISOU  129  CG  ARG A  15    22551  32915  17351  -1435  -1382  -4784       C  
ATOM    130  CD  ARG A  15      -0.114 -68.338   7.419  1.00189.23           C  
ANISOU  130  CD  ARG A  15    22652  32140  17106  -1530  -1209  -4875       C  
ATOM    131  NE  ARG A  15      -0.774 -67.107   6.991  1.00233.90           N  
ANISOU  131  NE  ARG A  15    28265  37748  22860  -1794  -1449  -5354       N  
ATOM    132  CZ  ARG A  15      -1.454 -66.299   7.799  1.00226.44           C  
ANISOU  132  CZ  ARG A  15    27165  36550  22320  -2328  -1507  -5622       C  
ATOM    133  NH1 ARG A  15      -2.021 -65.200   7.317  1.00204.67           N  
ANISOU  133  NH1 ARG A  15    24393  33711  19662  -2523  -1730  -6044       N  
ATOM    134  NH2 ARG A  15      -1.568 -66.590   9.089  1.00211.56           N  
ANISOU  134  NH2 ARG A  15    25168  34465  20749  -2672  -1340  -5454       N  
ATOM    135  N   ASP A  16      -1.447 -72.846   7.670  1.00214.77           N  
ANISOU  135  N   ASP A  16    24981  36534  20088   -852  -1315  -4095       N  
ATOM    136  CA  ASP A  16      -1.136 -73.881   6.692  1.00215.62           C  
ANISOU  136  CA  ASP A  16    25146  36917  19863   -262  -1389  -3841       C  
ATOM    137  C   ASP A  16      -1.287 -75.250   7.326  1.00197.17           C  
ANISOU  137  C   ASP A  16    22585  34750  17582   -117  -1285  -3559       C  
ATOM    138  O   ASP A  16      -0.303 -75.842   7.770  1.00177.38           O  
ANISOU  138  O   ASP A  16    20355  31957  15086     81   -998  -3170       O  
ATOM    139  CB  ASP A  16       0.286 -73.717   6.162  1.00237.73           C  
ANISOU  139  CB  ASP A  16    28490  39378  22460     84  -1171  -3548       C  
ATOM    140  CG  ASP A  16       0.358 -72.787   4.974  1.00246.97           C  
ANISOU  140  CG  ASP A  16    29860  40599  23378    195  -1354  -3795       C  
ATOM    141  OD1 ASP A  16      -0.595 -72.788   4.166  1.00229.96           O  
ANISOU  141  OD1 ASP A  16    27450  38848  21078    258  -1704  -4065       O  
ATOM    142  OD2 ASP A  16       1.364 -72.058   4.846  1.00237.14           O  
ANISOU  142  OD2 ASP A  16    29022  38999  22082    222  -1144  -3732       O  
ATOM    143  N   PRO A  17      -2.526 -75.756   7.376  1.00169.00           N  
ANISOU  143  N   PRO A  17    18499  31640  14073   -217  -1514  -3769       N  
ATOM    144  CA  PRO A  17      -2.752 -77.004   8.104  1.00156.15           C  
ANISOU  144  CA  PRO A  17    16621  30198  12512   -120  -1398  -3556       C  
ATOM    145  C   PRO A  17      -2.110 -78.201   7.416  1.00178.09           C  
ANISOU  145  C   PRO A  17    19562  33080  15026    535  -1384  -3186       C  
ATOM    146  O   PRO A  17      -2.328 -78.412   6.222  1.00161.01           O  
ANISOU  146  O   PRO A  17    17356  31205  12615    903  -1655  -3238       O  
ATOM    147  CB  PRO A  17      -4.277 -77.144   8.098  1.00156.65           C  
ANISOU  147  CB  PRO A  17    16052  30771  12699   -365  -1680  -3927       C  
ATOM    148  CG  PRO A  17      -4.761 -76.297   6.944  1.00164.49           C  
ANISOU  148  CG  PRO A  17    16998  31904  13598   -356  -2012  -4259       C  
ATOM    149  CD  PRO A  17      -3.636 -75.420   6.468  1.00146.35           C  
ANISOU  149  CD  PRO A  17    15284  29181  11142   -247  -1906  -4161       C  
ATOM    150  N   PRO A  18      -1.316 -78.978   8.166  1.00210.59           N  
ANISOU  150  N   PRO A  18    23883  36923  19210    676  -1074  -2810       N  
ATOM    151  CA  PRO A  18      -0.845 -80.279   7.684  1.00178.10           C  
ANISOU  151  CA  PRO A  18    19859  32899  14912   1265  -1056  -2460       C  
ATOM    152  C   PRO A  18      -1.995 -81.275   7.710  1.00190.62           C  
ANISOU  152  C   PRO A  18    20890  35069  16469   1406  -1273  -2602       C  
ATOM    153  O   PRO A  18      -2.734 -81.324   8.695  1.00178.60           O  
ANISOU  153  O   PRO A  18    19018  33646  15196   1024  -1198  -2769       O  
ATOM    154  CB  PRO A  18       0.225 -80.670   8.711  1.00159.97           C  
ANISOU  154  CB  PRO A  18    17898  30077  12807   1241   -648  -2091       C  
ATOM    155  CG  PRO A  18       0.571 -79.392   9.432  1.00157.86           C  
ANISOU  155  CG  PRO A  18    17830  29391  12758    723   -474  -2213       C  
ATOM    156  CD  PRO A  18      -0.699 -78.612   9.451  1.00182.65           C  
ANISOU  156  CD  PRO A  18    20568  32894  15935    306   -724  -2678       C  
ATOM    157  N   ALA A  19      -2.150 -82.056   6.647  1.00208.98           N  
ANISOU  157  N   ALA A  19    23132  37718  18553   1940  -1521  -2523       N  
ATOM    158  CA  ALA A  19      -3.215 -83.043   6.599  1.00189.75           C  
ANISOU  158  CA  ALA A  19    20137  35850  16109   2142  -1755  -2662       C  
ATOM    159  C   ALA A  19      -2.826 -84.271   7.406  1.00188.80           C  
ANISOU  159  C   ALA A  19    20039  35587  16109   2379  -1484  -2341       C  
ATOM    160  O   ALA A  19      -3.665 -84.887   8.061  1.00166.49           O  
ANISOU  160  O   ALA A  19    16755  32922  13581   2272  -1442  -2451       O  
ATOM    161  CB  ALA A  19      -3.525 -83.425   5.164  1.00184.04           C  
ANISOU  161  CB  ALA A  19    19332  35466  15129   2649  -2133  -2688       C  
ATOM    162  N   GLN A  20      -1.547 -84.622   7.353  1.00184.85           N  
ANISOU  162  N   GLN A  20    20078  34682  15473   2683  -1256  -1932       N  
ATOM    163  CA  GLN A  20      -1.068 -85.814   8.037  1.00165.30           C  
ANISOU  163  CA  GLN A  20    17689  31920  13195   2936   -986  -1602       C  
ATOM    164  C   GLN A  20      -0.857 -85.627   9.543  1.00141.33           C  
ANISOU  164  C   GLN A  20    14705  28418  10577   2445   -594  -1571       C  
ATOM    165  O   GLN A  20      -1.317 -86.449  10.333  1.00136.13           O  
ANISOU  165  O   GLN A  20    13774  27770  10178   2435   -465  -1571       O  
ATOM    166  CB  GLN A  20       0.207 -86.338   7.374  1.00193.50           C  
ANISOU  166  CB  GLN A  20    21803  35217  16503   3450   -901  -1167       C  
ATOM    167  CG  GLN A  20       0.513 -87.787   7.706  1.00222.12           C  
ANISOU  167  CG  GLN A  20    25448  38687  20261   3874   -763   -864       C  
ATOM    168  CD  GLN A  20       1.570 -88.379   6.800  1.00227.10           C  
ANISOU  168  CD  GLN A  20    26552  39133  20604   4436   -763   -445       C  
ATOM    169  OE1 GLN A  20       2.717 -88.566   7.204  1.00220.30           O  
ANISOU  169  OE1 GLN A  20    26120  37704  19878   4445   -439   -118       O  
ATOM    170  NE2 GLN A  20       1.186 -88.681   5.564  1.00205.02           N  
ANISOU  170  NE2 GLN A  20    23666  36687  17544   4861  -1112   -445       N  
ATOM    171  N   CYS A  21      -0.174 -84.556   9.944  1.00153.91           N  
ANISOU  171  N   CYS A  21    16647  29607  12223   2058   -411  -1552       N  
ATOM    172  CA  CYS A  21       0.046 -84.313  11.374  1.00134.71           C  
ANISOU  172  CA  CYS A  21    14296  26724  10165   1598    -82  -1514       C  
ATOM    173  C   CYS A  21      -0.325 -82.912  11.863  1.00119.20           C  
ANISOU  173  C   CYS A  21    12291  24650   8351    972    -72  -1786       C  
ATOM    174  O   CYS A  21       0.341 -81.929  11.548  1.00123.28           O  
ANISOU  174  O   CYS A  21    13132  24940   8767    853    -64  -1788       O  
ATOM    175  CB  CYS A  21       1.483 -84.661  11.790  1.00110.20           C  
ANISOU  175  CB  CYS A  21    11707  23046   7119   1764    216  -1124       C  
ATOM    176  SG  CYS A  21       2.798 -84.181  10.642  1.00253.69           S  
ANISOU  176  SG  CYS A  21    30408  40931  25053   2059    208   -872       S  
ATOM    177  N   SER A  22      -1.373 -82.852  12.679  1.00150.16           N  
ANISOU  177  N   SER A  22    15819  28704  12531    574    -45  -2003       N  
ATOM    178  CA  SER A  22      -1.843 -81.603  13.257  1.00127.30           C  
ANISOU  178  CA  SER A  22    12863  25676   9830    -48    -28  -2245       C  
ATOM    179  C   SER A  22      -1.942 -81.757  14.765  1.00136.66           C  
ANISOU  179  C   SER A  22    14049  26532  11342   -427    275  -2153       C  
ATOM    180  O   SER A  22      -1.999 -82.868  15.286  1.00141.09           O  
ANISOU  180  O   SER A  22    14513  27123  11972   -230    426  -2008       O  
ATOM    181  CB  SER A  22      -3.218 -81.242  12.698  1.00126.86           C  
ANISOU  181  CB  SER A  22    12285  26156   9760   -240   -324  -2639       C  
ATOM    182  OG  SER A  22      -4.206 -82.127  13.201  1.00130.08           O  
ANISOU  182  OG  SER A  22    12213  26869  10343   -274   -276  -2712       O  
ATOM    183  N   ALA A  23      -1.968 -80.628  15.462  1.00116.33           N  
ANISOU  183  N   ALA A  23    11603  23640   8958   -957    355  -2243       N  
ATOM    184  CA  ALA A  23      -2.077 -80.634  16.912  1.00 94.45           C  
ANISOU  184  CA  ALA A  23     8881  20546   6460  -1351    619  -2150       C  
ATOM    185  C   ALA A  23      -2.852 -79.413  17.370  1.00106.45           C  
ANISOU  185  C   ALA A  23    10279  21993   8175  -1976    581  -2385       C  
ATOM    186  O   ALA A  23      -3.035 -78.458  16.613  1.00115.20           O  
ANISOU  186  O   ALA A  23    11362  23179   9229  -2096    366  -2607       O  
ATOM    187  CB  ALA A  23      -0.704 -80.661  17.548  1.00114.52           C  
ANISOU  187  CB  ALA A  23    11943  22513   9058  -1258    824  -1840       C  
ATOM    188  N   GLY A  24      -3.315 -79.445  18.613  1.00 97.61           N  
ANISOU  188  N   GLY A  24     9101  20714   7271  -2373    790  -2338       N  
ATOM    189  CA  GLY A  24      -4.122 -78.360  19.132  1.00125.40           C  
ANISOU  189  CA  GLY A  24    12507  24139  11000  -2990    780  -2522       C  
ATOM    190  C   GLY A  24      -4.426 -78.547  20.597  1.00 95.16           C  
ANISOU  190  C   GLY A  24     8722  20083   7351  -3363   1062  -2372       C  
ATOM    191  O   GLY A  24      -4.284 -79.649  21.124  1.00143.04           O  
ANISOU  191  O   GLY A  24    14780  26208  13363  -3135   1249  -2202       O  
ATOM    192  N   PRO A  25      -4.862 -77.469  21.257  1.00 95.68           N  
ANISOU  192  N   PRO A  25     8852  19882   7620  -3933   1090  -2437       N  
ATOM    193  CA  PRO A  25      -5.128 -77.441  22.698  1.00120.62           C  
ANISOU  193  CA  PRO A  25    12137  22770  10924  -4344   1349  -2267       C  
ATOM    194  C   PRO A  25      -6.244 -78.386  23.120  1.00106.36           C  
ANISOU  194  C   PRO A  25     9887  21411   9116  -4445   1545  -2312       C  
ATOM    195  O   PRO A  25      -7.192 -78.621  22.368  1.00104.18           O  
ANISOU  195  O   PRO A  25     9101  21638   8846  -4434   1444  -2559       O  
ATOM    196  CB  PRO A  25      -5.545 -75.988  22.945  1.00121.24           C  
ANISOU  196  CB  PRO A  25    12297  22550  11220  -4913   1262  -2387       C  
ATOM    197  CG  PRO A  25      -6.040 -75.509  21.627  1.00139.85           C  
ANISOU  197  CG  PRO A  25    14338  25239  13561  -4869    982  -2721       C  
ATOM    198  CD  PRO A  25      -5.164 -76.178  20.619  1.00112.53           C  
ANISOU  198  CD  PRO A  25    10953  21957   9847  -4219    858  -2691       C  
ATOM    199  N   VAL A  26      -6.126 -78.910  24.334  1.00109.06           N  
ANISOU  199  N   VAL A  26    10417  21571   9448  -4542   1822  -2089       N  
ATOM    200  CA  VAL A  26      -7.147 -79.774  24.891  1.00100.42           C  
ANISOU  200  CA  VAL A  26     8943  20867   8344  -4666   2076  -2121       C  
ATOM    201  C   VAL A  26      -8.123 -78.915  25.672  1.00103.34           C  
ANISOU  201  C   VAL A  26     9226  21147   8892  -5365   2213  -2151       C  
ATOM    202  O   VAL A  26      -7.785 -78.369  26.729  1.00121.37           O  
ANISOU  202  O   VAL A  26    11940  22964  11212  -5679   2334  -1936       O  
ATOM    203  CB  VAL A  26      -6.537 -80.802  25.852  1.00 98.11           C  
ANISOU  203  CB  VAL A  26     8931  20433   7913  -4417   2327  -1880       C  
ATOM    204  CG1 VAL A  26      -7.631 -81.625  26.511  1.00122.69           C  
ANISOU  204  CG1 VAL A  26    11667  23947  11003  -4579   2637  -1930       C  
ATOM    205  CG2 VAL A  26      -5.549 -81.694  25.115  1.00135.99           C  
ANISOU  205  CG2 VAL A  26    13833  25267  12570  -3738   2208  -1828       C  
ATOM    206  N   GLY A  27      -9.332 -78.796  25.135  1.00108.08           N  
ANISOU  206  N   GLY A  27     9266  22184   9615  -5609   2179  -2412       N  
ATOM    207  CA  GLY A  27     -10.371 -78.023  25.781  1.00129.89           C  
ANISOU  207  CA  GLY A  27    11878  24893  12582  -6301   2326  -2453       C  
ATOM    208  C   GLY A  27      -9.909 -76.616  26.089  1.00139.03           C  
ANISOU  208  C   GLY A  27    13508  25440  13877  -6670   2186  -2364       C  
ATOM    209  O   GLY A  27      -9.469 -75.877  25.208  1.00108.70           O  
ANISOU  209  O   GLY A  27     9753  21458  10089  -6558   1872  -2511       O  
ATOM    210  N   ASP A  28      -9.993 -76.265  27.365  1.00161.82           N  
ANISOU  210  N   ASP A  28    16756  27918  16810  -7044   2399  -2114       N  
ATOM    211  CA  ASP A  28      -9.626 -74.942  27.838  1.00153.68           C  
ANISOU  211  CA  ASP A  28    16195  26259  15937  -7402   2283  -1995       C  
ATOM    212  C   ASP A  28      -8.118 -74.717  27.829  1.00150.47           C  
ANISOU  212  C   ASP A  28    16296  25440  15434  -7064   2128  -1841       C  
ATOM    213  O   ASP A  28      -7.658 -73.603  27.583  1.00124.06           O  
ANISOU  213  O   ASP A  28    13212  21684  12243  -7173   1904  -1882       O  
ATOM    214  CB  ASP A  28     -10.152 -74.744  29.262  1.00195.99           C  
ANISOU  214  CB  ASP A  28    21896  31222  21348  -7706   2490  -1727       C  
ATOM    215  CG  ASP A  28     -10.313 -73.286  29.630  1.00225.16           C  
ANISOU  215  CG  ASP A  28    25920  34341  25290  -8125   2358  -1666       C  
ATOM    216  OD1 ASP A  28     -10.888 -72.530  28.817  1.00217.59           O  
ANISOU  216  OD1 ASP A  28    24700  33426  24547  -8318   2186  -1919       O  
ATOM    217  OD2 ASP A  28      -9.865 -72.895  30.728  1.00229.18           O  
ANISOU  217  OD2 ASP A  28    26955  34338  25784  -8220   2403  -1371       O  
ATOM    218  N   ASP A  29      -7.347 -75.773  28.084  1.00201.04           N  
ANISOU  218  N   ASP A  29    22862  31909  21616  -6597   2229  -1681       N  
ATOM    219  CA  ASP A  29      -5.932 -75.591  28.420  1.00163.64           C  
ANISOU  219  CA  ASP A  29    18679  26670  16828  -6312   2123  -1474       C  
ATOM    220  C   ASP A  29      -5.051 -75.252  27.222  1.00134.62           C  
ANISOU  220  C   ASP A  29    15050  22927  13172  -5911   1838  -1616       C  
ATOM    221  O   ASP A  29      -4.989 -76.000  26.248  1.00190.19           O  
ANISOU  221  O   ASP A  29    21810  30370  20083  -5493   1777  -1753       O  
ATOM    222  CB  ASP A  29      -5.384 -76.817  29.159  1.00157.28           C  
ANISOU  222  CB  ASP A  29    18050  25908  15802  -5981   2322  -1265       C  
ATOM    223  CG  ASP A  29      -4.072 -76.529  29.867  1.00175.48           C  
ANISOU  223  CG  ASP A  29    20941  27631  18103  -5846   2241  -1024       C  
ATOM    224  OD1 ASP A  29      -3.688 -75.344  29.952  1.00160.27           O  
ANISOU  224  OD1 ASP A  29    19284  25255  16356  -6059   2067   -990       O  
ATOM    225  OD2 ASP A  29      -3.432 -77.485  30.353  1.00194.82           O  
ANISOU  225  OD2 ASP A  29    23568  30063  20393  -5526   2341   -886       O  
ATOM    226  N   MET A  30      -4.365 -74.118  27.313  1.00 90.76           N  
ANISOU  226  N   MET A  30     9860  16853   7770  -6031   1672  -1576       N  
ATOM    227  CA  MET A  30      -3.480 -73.662  26.249  1.00109.21           C  
ANISOU  227  CA  MET A  30    12289  19083  10123  -5687   1440  -1705       C  
ATOM    228  C   MET A  30      -2.127 -74.364  26.262  1.00112.82           C  
ANISOU  228  C   MET A  30    13029  19384  10454  -5170   1458  -1518       C  
ATOM    229  O   MET A  30      -1.479 -74.493  25.224  1.00100.86           O  
ANISOU  229  O   MET A  30    11487  17976   8859  -4769   1344  -1608       O  
ATOM    230  CB  MET A  30      -3.277 -72.148  26.337  1.00125.38           C  
ANISOU  230  CB  MET A  30    14594  20628  12415  -6007   1274  -1766       C  
ATOM    231  CG  MET A  30      -4.286 -71.354  25.539  1.00152.68           C  
ANISOU  231  CG  MET A  30    17730  24285  15998  -6313   1130  -2092       C  
ATOM    232  SD  MET A  30      -4.271 -71.846  23.804  1.00136.32           S  
ANISOU  232  SD  MET A  30    15286  22793  13715  -5830    956  -2401       S  
ATOM    233  CE  MET A  30      -5.973 -72.367  23.591  1.00159.46           C  
ANISOU  233  CE  MET A  30    17595  26340  16653  -6136   1009  -2610       C  
ATOM    234  N   PHE A  31      -1.703 -74.810  27.438  1.00 95.14           N  
ANISOU  234  N   PHE A  31    11071  16886   8193  -5190   1601  -1259       N  
ATOM    235  CA  PHE A  31      -0.381 -75.402  27.593  1.00 78.88           C  
ANISOU  235  CA  PHE A  31     9302  14595   6074  -4761   1607  -1082       C  
ATOM    236  C   PHE A  31      -0.403 -76.913  27.417  1.00 84.85           C  
ANISOU  236  C   PHE A  31     9870  15751   6616  -4375   1748  -1047       C  
ATOM    237  O   PHE A  31       0.640 -77.564  27.448  1.00121.53           O  
ANISOU  237  O   PHE A  31    14715  20245  11217  -3996   1762   -917       O  
ATOM    238  CB  PHE A  31       0.209 -75.043  28.957  1.00112.02           C  
ANISOU  238  CB  PHE A  31    13933  18257  10373  -4958   1627   -843       C  
ATOM    239  CG  PHE A  31       0.531 -73.586  29.112  1.00106.12           C  
ANISOU  239  CG  PHE A  31    13428  17022   9872  -5223   1456   -853       C  
ATOM    240  CD1 PHE A  31      -0.477 -72.655  29.282  1.00100.99           C  
ANISOU  240  CD1 PHE A  31    12699  16328   9344  -5703   1425   -942       C  
ATOM    241  CD2 PHE A  31       1.843 -73.149  29.088  1.00123.71           C  
ANISOU  241  CD2 PHE A  31    15946  18818  12241  -4993   1333   -782       C  
ATOM    242  CE1 PHE A  31      -0.188 -71.315  29.430  1.00117.72           C  
ANISOU  242  CE1 PHE A  31    15051  17962  11714  -5927   1257   -963       C  
ATOM    243  CE2 PHE A  31       2.143 -71.808  29.233  1.00120.44           C  
ANISOU  243  CE2 PHE A  31    15735  17949  12079  -5206   1176   -812       C  
ATOM    244  CZ  PHE A  31       1.125 -70.889  29.403  1.00 99.39           C  
ANISOU  244  CZ  PHE A  31    13014  15224   9526  -5662   1129   -904       C  
ATOM    245  N   HIS A  32      -1.598 -77.466  27.234  1.00100.01           N  
ANISOU  245  N   HIS A  32    11393  18169   8438  -4475   1853  -1173       N  
ATOM    246  CA  HIS A  32      -1.752 -78.896  27.003  1.00 82.45           C  
ANISOU  246  CA  HIS A  32     8936  16357   6035  -4093   1981  -1179       C  
ATOM    247  C   HIS A  32      -2.381 -79.120  25.633  1.00 85.16           C  
ANISOU  247  C   HIS A  32     8825  17215   6317  -3887   1870  -1414       C  
ATOM    248  O   HIS A  32      -3.542 -78.778  25.410  1.00117.97           O  
ANISOU  248  O   HIS A  32    12622  21682  10518  -4197   1861  -1598       O  
ATOM    249  CB  HIS A  32      -2.604 -79.527  28.108  1.00128.44           C  
ANISOU  249  CB  HIS A  32    14667  22351  11782  -4342   2233  -1121       C  
ATOM    250  CG  HIS A  32      -2.729 -81.019  28.011  1.00104.77           C  
ANISOU  250  CG  HIS A  32    11463  19689   8654  -3915   2359  -1137       C  
ATOM    251  ND1 HIS A  32      -2.106 -81.762  27.034  1.00149.68           N  
ANISOU  251  ND1 HIS A  32    17069  25532  14269  -3377   2270  -1169       N  
ATOM    252  CD2 HIS A  32      -3.409 -81.902  28.781  1.00106.20           C  
ANISOU  252  CD2 HIS A  32    11534  19988   8828  -3902   2526  -1120       C  
ATOM    253  CE1 HIS A  32      -2.399 -83.041  27.200  1.00149.12           C  
ANISOU  253  CE1 HIS A  32    16835  25657  14165  -3063   2375  -1175       C  
ATOM    254  NE2 HIS A  32      -3.187 -83.152  28.254  1.00110.04           N  
ANISOU  254  NE2 HIS A  32    11859  20701   9250  -3370   2538  -1162       N  
ATOM    255  N   TRP A  33      -1.602 -79.689  24.718  1.00102.19           N  
ANISOU  255  N   TRP A  33    11005  19449   8375  -3368   1775  -1400       N  
ATOM    256  CA  TRP A  33      -2.073 -79.982  23.370  1.00 99.91           C  
ANISOU  256  CA  TRP A  33    10336  19645   7980  -3089   1629  -1595       C  
ATOM    257  C   TRP A  33      -2.068 -81.473  23.098  1.00108.31           C  
ANISOU  257  C   TRP A  33    11215  21037   8900  -2601   1711  -1551       C  
ATOM    258  O   TRP A  33      -1.299 -82.225  23.692  1.00120.57           O  
ANISOU  258  O   TRP A  33    13030  22352  10430  -2369   1842  -1359       O  
ATOM    259  CB  TRP A  33      -1.198 -79.306  22.313  1.00 84.17           C  
ANISOU  259  CB  TRP A  33     8535  17495   5952  -2859   1423  -1620       C  
ATOM    260  CG  TRP A  33      -1.320 -77.817  22.235  1.00 96.59           C  
ANISOU  260  CG  TRP A  33    10205  18834   7660  -3265   1293  -1753       C  
ATOM    261  CD1 TRP A  33      -1.754 -76.973  23.215  1.00110.40           C  
ANISOU  261  CD1 TRP A  33    12046  20303   9598  -3796   1348  -1754       C  
ATOM    262  CD2 TRP A  33      -1.001 -76.995  21.108  1.00 84.84           C  
ANISOU  262  CD2 TRP A  33     8755  17358   6123  -3159   1087  -1909       C  
ATOM    263  NE1 TRP A  33      -1.720 -75.674  22.769  1.00113.90           N  
ANISOU  263  NE1 TRP A  33    12571  20554  10151  -4021   1178  -1912       N  
ATOM    264  CE2 TRP A  33      -1.261 -75.661  21.479  1.00 97.87           C  
ANISOU  264  CE2 TRP A  33    10506  18711   7969  -3636   1022  -2027       C  
ATOM    265  CE3 TRP A  33      -0.520 -77.257  19.822  1.00 85.24           C  
ANISOU  265  CE3 TRP A  33     8788  17638   5964  -2698    956  -1956       C  
ATOM    266  CZ2 TRP A  33      -1.056 -74.594  20.610  1.00117.01           C  
ANISOU  266  CZ2 TRP A  33    12997  21066  10397  -3659    834  -2229       C  
ATOM    267  CZ3 TRP A  33      -0.315 -76.196  18.963  1.00 86.07           C  
ANISOU  267  CZ3 TRP A  33     8973  17700   6028  -2727    780  -2139       C  
ATOM    268  CH2 TRP A  33      -0.583 -74.881  19.359  1.00108.18           C  
ANISOU  268  CH2 TRP A  33    11857  20207   9038  -3202    722  -2293       C  
ATOM    269  N   GLN A  34      -2.932 -81.888  22.182  1.00101.53           N  
ANISOU  269  N   GLN A  34     9898  20715   7963  -2436   1609  -1747       N  
ATOM    270  CA  GLN A  34      -2.931 -83.254  21.695  1.00 91.19           C  
ANISOU  270  CA  GLN A  34     8387  19732   6528  -1903   1628  -1726       C  
ATOM    271  C   GLN A  34      -2.622 -83.239  20.208  1.00 93.21           C  
ANISOU  271  C   GLN A  34     8577  20198   6642  -1487   1361  -1785       C  
ATOM    272  O   GLN A  34      -3.238 -82.499  19.441  1.00 94.47           O  
ANISOU  272  O   GLN A  34     8500  20614   6780  -1641   1156  -1998       O  
ATOM    273  CB  GLN A  34      -4.279 -83.926  21.946  1.00 95.35           C  
ANISOU  273  CB  GLN A  34     8384  20761   7084  -2009   1744  -1903       C  
ATOM    274  CG  GLN A  34      -4.263 -85.424  21.693  1.00129.83           C  
ANISOU  274  CG  GLN A  34    12565  25403  11361  -1452   1805  -1874       C  
ATOM    275  CD  GLN A  34      -5.651 -86.023  21.608  1.00157.57           C  
ANISOU  275  CD  GLN A  34    15446  29506  14918  -1489   1866  -2110       C  
ATOM    276  OE1 GLN A  34      -6.580 -85.402  21.086  1.00173.80           O  
ANISOU  276  OE1 GLN A  34    17109  31890  17035  -1754   1722  -2331       O  
ATOM    277  NE2 GLN A  34      -5.803 -87.238  22.124  1.00154.87           N  
ANISOU  277  NE2 GLN A  34    14984  29297  14564  -1224   2080  -2085       N  
ATOM    278  N   ALA A  35      -1.655 -84.054  19.806  1.00108.56           N  
ANISOU  278  N   ALA A  35    10751  22017   8478   -966   1360  -1593       N  
ATOM    279  CA  ALA A  35      -1.280 -84.158  18.405  1.00 91.75           C  
ANISOU  279  CA  ALA A  35     8621  20075   6163   -522   1131  -1589       C  
ATOM    280  C   ALA A  35      -1.849 -85.429  17.801  1.00 95.27           C  
ANISOU  280  C   ALA A  35     8701  20988   6508    -52   1060  -1635       C  
ATOM    281  O   ALA A  35      -1.770 -86.502  18.393  1.00111.63           O  
ANISOU  281  O   ALA A  35    10760  23019   8636    158   1235  -1533       O  
ATOM    282  CB  ALA A  35       0.228 -84.138  18.260  1.00100.76           C  
ANISOU  282  CB  ALA A  35    10283  20738   7262   -261   1180  -1316       C  
ATOM    283  N   THR A  36      -2.435 -85.299  16.620  1.00130.82           N  
ANISOU  283  N   THR A  36    12903  25938  10866    127    785  -1809       N  
ATOM    284  CA  THR A  36      -2.887 -86.467  15.884  1.00127.01           C  
ANISOU  284  CA  THR A  36    12086  25893  10277    648    653  -1841       C  
ATOM    285  C   THR A  36      -2.010 -86.613  14.656  1.00112.01           C  
ANISOU  285  C   THR A  36    10474  23964   8121   1163    450  -1667       C  
ATOM    286  O   THR A  36      -2.114 -85.819  13.721  1.00151.28           O  
ANISOU  286  O   THR A  36    15438  29122  12920   1141    203  -1788       O  
ATOM    287  CB  THR A  36      -4.348 -86.313  15.435  1.00125.81           C  
ANISOU  287  CB  THR A  36    11302  26345  10154    493    450  -2189       C  
ATOM    288  OG1 THR A  36      -5.202 -86.253  16.586  1.00157.40           O  
ANISOU  288  OG1 THR A  36    15020  30390  14393      9    689  -2326       O  
ATOM    289  CG2 THR A  36      -4.760 -87.488  14.566  1.00118.55           C  
ANISOU  289  CG2 THR A  36    10032  25883   9127   1094    257  -2224       C  
ATOM    290  N   ILE A  37      -1.146 -87.622  14.653  1.00101.72           N  
ANISOU  290  N   ILE A  37     9443  22421   6786   1622    558  -1386       N  
ATOM    291  CA  ILE A  37      -0.300 -87.860  13.491  1.00106.56           C  
ANISOU  291  CA  ILE A  37    10352  22991   7146   2127    401  -1169       C  
ATOM    292  C   ILE A  37      -0.601 -89.206  12.827  1.00106.52           C  
ANISOU  292  C   ILE A  37    10121  23300   7050   2746    257  -1105       C  
ATOM    293  O   ILE A  37      -0.681 -90.247  13.482  1.00106.58           O  
ANISOU  293  O   ILE A  37    10035  23231   7230   2920    419  -1049       O  
ATOM    294  CB  ILE A  37       1.217 -87.668  13.796  1.00 98.11           C  
ANISOU  294  CB  ILE A  37     9890  21288   6101   2142    620   -845       C  
ATOM    295  CG1 ILE A  37       1.907 -88.983  14.157  1.00104.59           C  
ANISOU  295  CG1 ILE A  37    10899  21815   7024   2543    792   -577       C  
ATOM    296  CG2 ILE A  37       1.418 -86.630  14.892  1.00 94.09           C  
ANISOU  296  CG2 ILE A  37     9535  20416   5800   1532    811   -914       C  
ATOM    297  CD1 ILE A  37       3.398 -88.834  14.366  1.00148.74           C  
ANISOU  297  CD1 ILE A  37    17044  26800  12671   2565    988   -267       C  
ATOM    298  N   MET A  38      -0.809 -89.155  11.517  1.00121.88           N  
ANISOU  298  N   MET A  38    11981  25613   8716   3087    -67  -1133       N  
ATOM    299  CA  MET A  38      -1.196 -90.331  10.757  1.00121.92           C  
ANISOU  299  CA  MET A  38    11742  25965   8618   3698   -282  -1090       C  
ATOM    300  C   MET A  38       0.030 -91.089  10.284  1.00121.42           C  
ANISOU  300  C   MET A  38    12183  25531   8422   4225   -221   -670       C  
ATOM    301  O   MET A  38       1.028 -90.485   9.883  1.00122.66           O  
ANISOU  301  O   MET A  38    12815  25387   8404   4205   -169   -454       O  
ATOM    302  CB  MET A  38      -2.043 -89.929   9.548  1.00126.90           C  
ANISOU  302  CB  MET A  38    12036  27191   8990   3833   -713  -1324       C  
ATOM    303  CG  MET A  38      -3.424 -90.557   9.526  1.00131.60           C  
ANISOU  303  CG  MET A  38    11927  28344   9730   3932   -902  -1631       C  
ATOM    304  SD  MET A  38      -4.599 -89.695  10.584  1.00132.25           S  
ANISOU  304  SD  MET A  38    11508  28608  10131   3132   -758  -2051       S  
ATOM    305  CE  MET A  38      -4.977 -88.266   9.571  1.00145.33           C  
ANISOU  305  CE  MET A  38    13111  30567  11541   2852  -1135  -2315       C  
ATOM    306  N   GLY A  39      -0.043 -92.413  10.341  1.00134.88           N  
ANISOU  306  N   GLY A  39    13777  27241  10232   4692   -209   -558       N  
ATOM    307  CA  GLY A  39       1.011 -93.238   9.787  1.00135.53           C  
ANISOU  307  CA  GLY A  39    14302  26990  10205   5235   -189   -156       C  
ATOM    308  C   GLY A  39       1.138 -92.934   8.311  1.00144.82           C  
ANISOU  308  C   GLY A  39    15620  28444  10963   5582   -520    -36       C  
ATOM    309  O   GLY A  39       0.171 -93.067   7.557  1.00143.94           O  
ANISOU  309  O   GLY A  39    15103  28891  10695   5813   -877   -237       O  
ATOM    310  N   PRO A  40       2.338 -92.518   7.889  1.00136.71           N  
ANISOU  310  N   PRO A  40    15163  27036   9743   5618   -404    285       N  
ATOM    311  CA  PRO A  40       2.590 -92.150   6.495  1.00141.02           C  
ANISOU  311  CA  PRO A  40    15940  27815   9825   5926   -668    430       C  
ATOM    312  C   PRO A  40       2.455 -93.371   5.605  1.00145.68           C  
ANISOU  312  C   PRO A  40    16507  28593  10252   6651   -929    648       C  
ATOM    313  O   PRO A  40       2.821 -94.464   6.028  1.00145.55           O  
ANISOU  313  O   PRO A  40    16577  28248  10479   6937   -775    859       O  
ATOM    314  CB  PRO A  40       4.051 -91.688   6.518  1.00158.74           C  
ANISOU  314  CB  PRO A  40    18817  29491  12007   5810   -350    781       C  
ATOM    315  CG  PRO A  40       4.356 -91.407   7.958  1.00130.97           C  
ANISOU  315  CG  PRO A  40    15306  25535   8922   5286      9    691       C  
ATOM    316  CD  PRO A  40       3.542 -92.383   8.722  1.00131.58           C  
ANISOU  316  CD  PRO A  40    14969  25719   9307   5367     -3    525       C  
ATOM    317  N   ASN A  41       1.926 -93.198   4.401  1.00133.06           N  
ANISOU  317  N   ASN A  41    14797  27508   8254   6958  -1342    583       N  
ATOM    318  CA  ASN A  41       1.902 -94.300   3.453  1.00138.75           C  
ANISOU  318  CA  ASN A  41    15569  28342   8807   7669  -1609    836       C  
ATOM    319  C   ASN A  41       3.330 -94.631   3.043  1.00139.94           C  
ANISOU  319  C   ASN A  41    16414  27845   8911   7888  -1340   1361       C  
ATOM    320  O   ASN A  41       4.223 -93.790   3.163  1.00154.60           O  
ANISOU  320  O   ASN A  41    18658  29302  10779   7498  -1041   1473       O  
ATOM    321  CB  ASN A  41       1.028 -93.968   2.244  1.00144.63           C  
ANISOU  321  CB  ASN A  41    16053  29561   9339   7803  -2041    594       C  
ATOM    322  CG  ASN A  41      -0.432 -93.795   2.616  1.00169.68           C  
ANISOU  322  CG  ASN A  41    18470  33364  12635   7613  -2318     74       C  
ATOM    323  OD1 ASN A  41      -0.753 -93.221   3.657  1.00165.44           O  
ANISOU  323  OD1 ASN A  41    17680  32897  12282   7097  -2146   -190       O  
ATOM    324  ND2 ASN A  41      -1.324 -94.310   1.778  1.00166.22           N  
ANISOU  324  ND2 ASN A  41    17668  33338  12152   7992  -2720    -82       N  
ATOM    325  N   ASP A  42       3.535 -95.859   2.577  1.00161.98           N  
ANISOU  325  N   ASP A  42    19333  30508  11703   8493  -1438   1669       N  
ATOM    326  CA  ASP A  42       4.867 -96.417   2.347  1.00161.91           C  
ANISOU  326  CA  ASP A  42    19944  29846  11728   8722  -1157   2189       C  
ATOM    327  C   ASP A  42       5.661 -96.534   3.643  1.00155.85           C  
ANISOU  327  C   ASP A  42    19372  28601  11242   8466   -737   2330       C  
ATOM    328  O   ASP A  42       6.891 -96.589   3.617  1.00154.38           O  
ANISOU  328  O   ASP A  42    19701  27819  11138   8420   -418   2699       O  
ATOM    329  CB  ASP A  42       5.667 -95.596   1.327  1.00192.40           C  
ANISOU  329  CB  ASP A  42    24275  33479  15351   8562  -1066   2378       C  
ATOM    330  CG  ASP A  42       5.092 -95.676  -0.070  1.00240.64           C  
ANISOU  330  CG  ASP A  42    30338  39959  21137   8909  -1468   2342       C  
ATOM    331  OD1 ASP A  42       4.421 -96.682  -0.381  1.00259.42           O  
ANISOU  331  OD1 ASP A  42    32473  42570  23522   9396  -1765   2338       O  
ATOM    332  OD2 ASP A  42       5.320 -94.736  -0.862  1.00237.74           O  
ANISOU  332  OD2 ASP A  42    30178  39634  20518   8700  -1492   2309       O  
ATOM    333  N   SER A  43       4.960 -96.553   4.772  1.00143.52           N  
ANISOU  333  N   SER A  43    17360  27130  10042   8142   -663   1952       N  
ATOM    334  CA  SER A  43       5.570 -96.978   6.024  1.00128.47           C  
ANISOU  334  CA  SER A  43    15566  24635   8611   7897   -267   1997       C  
ATOM    335  C   SER A  43       5.054 -98.360   6.391  1.00131.14           C  
ANISOU  335  C   SER A  43    15624  24951   9251   8318   -342   1942       C  
ATOM    336  O   SER A  43       4.153 -98.884   5.735  1.00140.15           O  
ANISOU  336  O   SER A  43    16422  26565  10263   8750   -697   1834       O  
ATOM    337  CB  SER A  43       5.244 -95.990   7.146  1.00122.97           C  
ANISOU  337  CB  SER A  43    14626  23964   8133   7182    -70   1615       C  
ATOM    338  OG  SER A  43       5.862 -94.737   6.916  1.00172.20           O  
ANISOU  338  OG  SER A  43    21155  30113  14160   6796     45   1670       O  
ATOM    339  N   PRO A  44       5.621 -98.959   7.448  1.00128.11           N  
ANISOU  339  N   PRO A  44    15376  24022   9278   8207    -20   1994       N  
ATOM    340  CA  PRO A  44       4.942-100.059   8.134  1.00129.65           C  
ANISOU  340  CA  PRO A  44    15202  24249   9809   8439    -30   1774       C  
ATOM    341  C   PRO A  44       3.789 -99.498   8.955  1.00127.59           C  
ANISOU  341  C   PRO A  44    14371  24447   9660   7978    -25   1261       C  
ATOM    342  O   PRO A  44       2.812-100.193   9.239  1.00149.38           O  
ANISOU  342  O   PRO A  44    16650  27526  12580   8175   -123    984       O  
ATOM    343  CB  PRO A  44       6.029-100.615   9.054  1.00126.50           C  
ANISOU  343  CB  PRO A  44    15196  23096   9772   8344    335   1964       C  
ATOM    344  CG  PRO A  44       7.311-100.212   8.411  1.00125.74           C  
ANISOU  344  CG  PRO A  44    15693  22575   9507   8337    449   2418       C  
ATOM    345  CD  PRO A  44       7.037 -98.861   7.839  1.00124.59           C  
ANISOU  345  CD  PRO A  44    15486  22867   8984   8009    335   2324       C  
ATOM    346  N   TYR A  45       3.918 -98.224   9.314  1.00123.19           N  
ANISOU  346  N   TYR A  45    13871  23910   9024   7365    102   1144       N  
ATOM    347  CA  TYR A  45       2.980 -97.559  10.206  1.00120.73           C  
ANISOU  347  CA  TYR A  45    13113  23919   8838   6827    168    709       C  
ATOM    348  C   TYR A  45       1.753 -97.092   9.444  1.00125.95           C  
ANISOU  348  C   TYR A  45    13274  25310   9270   6852   -183    429       C  
ATOM    349  O   TYR A  45       0.840 -96.503  10.023  1.00123.31           O  
ANISOU  349  O   TYR A  45    12518  25308   9026   6411   -165     63       O  
ATOM    350  CB  TYR A  45       3.654 -96.361  10.875  1.00114.94           C  
ANISOU  350  CB  TYR A  45    12671  22866   8136   6180    420    715       C  
ATOM    351  CG  TYR A  45       4.995 -96.686  11.485  1.00111.64           C  
ANISOU  351  CG  TYR A  45    12769  21720   7928   6140    726   1011       C  
ATOM    352  CD1 TYR A  45       5.093 -97.136  12.795  1.00109.01           C  
ANISOU  352  CD1 TYR A  45    12418  21068   7931   5931    974    887       C  
ATOM    353  CD2 TYR A  45       6.166 -96.541  10.751  1.00149.62           C  
ANISOU  353  CD2 TYR A  45    18082  26168  12599   6304    769   1405       C  
ATOM    354  CE1 TYR A  45       6.322 -97.435  13.354  1.00114.15           C  
ANISOU  354  CE1 TYR A  45    13520  21053   8799   5887   1215   1126       C  
ATOM    355  CE2 TYR A  45       7.396 -96.838  11.303  1.00126.57           C  
ANISOU  355  CE2 TYR A  45    15593  22575   9921   6243   1048   1662       C  
ATOM    356  CZ  TYR A  45       7.468 -97.284  12.603  1.00106.34           C  
ANISOU  356  CZ  TYR A  45    12986  19700   7717   6034   1250   1510       C  
ATOM    357  OH  TYR A  45       8.692 -97.580  13.156  1.00104.09           O  
ANISOU  357  OH  TYR A  45    13110  18744   7694   5965   1491   1735       O  
ATOM    358  N   GLN A  46       1.749 -97.349   8.140  1.00128.96           N  
ANISOU  358  N   GLN A  46    13718  25926   9353   7363   -510    610       N  
ATOM    359  CA  GLN A  46       0.640 -96.972   7.275  1.00133.26           C  
ANISOU  359  CA  GLN A  46    13807  27170   9658   7461   -916    351       C  
ATOM    360  C   GLN A  46      -0.680 -97.503   7.811  1.00135.75           C  
ANISOU  360  C   GLN A  46    13410  27924  10243   7463   -989    -56       C  
ATOM    361  O   GLN A  46      -0.787 -98.672   8.186  1.00137.52           O  
ANISOU  361  O   GLN A  46    13504  28033  10715   7827   -909    -37       O  
ATOM    362  CB  GLN A  46       0.881 -97.494   5.859  1.00143.54           C  
ANISOU  362  CB  GLN A  46    15314  28611  10613   8143  -1272    652       C  
ATOM    363  CG  GLN A  46      -0.336 -97.462   4.956  1.00144.57           C  
ANISOU  363  CG  GLN A  46    14908  29480  10540   8403  -1765    375       C  
ATOM    364  CD  GLN A  46      -0.053 -98.051   3.593  1.00158.58           C  
ANISOU  364  CD  GLN A  46    16939  31364  11952   9123  -2137    709       C  
ATOM    365  OE1 GLN A  46       1.063 -97.953   3.082  1.00184.66           O  
ANISOU  365  OE1 GLN A  46    20883  34282  14997   9270  -2042   1137       O  
ATOM    366  NE2 GLN A  46      -1.061 -98.675   2.995  1.00156.47           N  
ANISOU  366  NE2 GLN A  46    16167  31621  11664   9581  -2560    525       N  
ATOM    367  N   GLY A  47      -1.679 -96.630   7.860  1.00136.10           N  
ANISOU  367  N   GLY A  47    12992  28458  10260   7037  -1118   -437       N  
ATOM    368  CA  GLY A  47      -3.014 -97.016   8.277  1.00139.13           C  
ANISOU  368  CA  GLY A  47    12642  29328  10894   6990  -1184   -843       C  
ATOM    369  C   GLY A  47      -3.259 -96.770   9.748  1.00134.86           C  
ANISOU  369  C   GLY A  47    11953  28613  10674   6389   -758  -1054       C  
ATOM    370  O   GLY A  47      -4.394 -96.815  10.217  1.00136.86           O  
ANISOU  370  O   GLY A  47    11599  29276  11126   6172   -735  -1414       O  
ATOM    371  N   GLY A  48      -2.183 -96.503  10.479  1.00133.77           N  
ANISOU  371  N   GLY A  48    12372  27870  10583   6114   -420   -824       N  
ATOM    372  CA  GLY A  48      -2.279 -96.295  11.909  1.00131.82           C  
ANISOU  372  CA  GLY A  48    12085  27400  10599   5575    -26   -974       C  
ATOM    373  C   GLY A  48      -2.501 -94.840  12.260  1.00126.47           C  
ANISOU  373  C   GLY A  48    11400  26777   9875   4859     32  -1137       C  
ATOM    374  O   GLY A  48      -2.198 -93.949  11.468  1.00126.01           O  
ANISOU  374  O   GLY A  48    11545  26756   9579   4771   -167  -1069       O  
ATOM    375  N   VAL A  49      -3.040 -94.604  13.452  1.00120.14           N  
ANISOU  375  N   VAL A  49    10378  25977   9291   4356    309  -1353       N  
ATOM    376  CA  VAL A  49      -3.227 -93.247  13.946  1.00117.02           C  
ANISOU  376  CA  VAL A  49    10012  25549   8900   3651    397  -1487       C  
ATOM    377  C   VAL A  49      -2.577 -93.105  15.315  1.00114.17           C  
ANISOU  377  C   VAL A  49    10021  24658   8700   3262    787  -1383       C  
ATOM    378  O   VAL A  49      -2.943 -93.794  16.268  1.00123.08           O  
ANISOU  378  O   VAL A  49    10983  25781  10003   3218   1031  -1478       O  
ATOM    379  CB  VAL A  49      -4.710 -92.865  14.040  1.00120.47           C  
ANISOU  379  CB  VAL A  49     9770  26564   9437   3308    316  -1878       C  
ATOM    380  CG1 VAL A  49      -4.857 -91.473  14.631  1.00117.33           C  
ANISOU  380  CG1 VAL A  49     9457  26046   9077   2563    426  -1990       C  
ATOM    381  CG2 VAL A  49      -5.357 -92.936  12.669  1.00125.76           C  
ANISOU  381  CG2 VAL A  49    10055  27774   9952   3676   -128  -2015       C  
ATOM    382  N   PHE A  50      -1.608 -92.200  15.401  1.00111.97           N  
ANISOU  382  N   PHE A  50    10243  23947   8352   2994    836  -1199       N  
ATOM    383  CA  PHE A  50      -0.796 -92.061  16.597  1.00103.03           C  
ANISOU  383  CA  PHE A  50     9524  22260   7361   2691   1145  -1062       C  
ATOM    384  C   PHE A  50      -1.060 -90.743  17.311  1.00106.48           C  
ANISOU  384  C   PHE A  50     9983  22621   7853   1993   1236  -1190       C  
ATOM    385  O   PHE A  50      -1.046 -89.674  16.694  1.00 99.91           O  
ANISOU  385  O   PHE A  50     9196  21850   6916   1784   1068  -1229       O  
ATOM    386  CB  PHE A  50       0.684 -92.188  16.241  1.00100.38           C  
ANISOU  386  CB  PHE A  50     9768  21401   6970   2972   1160   -716       C  
ATOM    387  CG  PHE A  50       1.041 -93.510  15.622  1.00103.08           C  
ANISOU  387  CG  PHE A  50    10164  21715   7288   3646   1093   -543       C  
ATOM    388  CD1 PHE A  50       0.933 -93.703  14.255  1.00106.64           C  
ANISOU  388  CD1 PHE A  50    10530  22461   7527   4092    806   -467       C  
ATOM    389  CD2 PHE A  50       1.480 -94.560  16.409  1.00119.02           C  
ANISOU  389  CD2 PHE A  50    12334  23400   9488   3844   1300   -459       C  
ATOM    390  CE1 PHE A  50       1.258 -94.918  13.689  1.00109.53           C  
ANISOU  390  CE1 PHE A  50    10969  22767   7878   4726    730   -279       C  
ATOM    391  CE2 PHE A  50       1.808 -95.776  15.847  1.00109.24           C  
ANISOU  391  CE2 PHE A  50    11157  22087   8260   4469   1234   -302       C  
ATOM    392  CZ  PHE A  50       1.697 -95.955  14.485  1.00113.61           C  
ANISOU  392  CZ  PHE A  50    11634  22916   8618   4913    950   -196       C  
ATOM    393  N   PHE A  51      -1.307 -90.828  18.615  1.00 98.89           N  
ANISOU  393  N   PHE A  51     9009  21518   7046   1647   1500  -1259       N  
ATOM    394  CA  PHE A  51      -1.580 -89.647  19.421  1.00 96.70           C  
ANISOU  394  CA  PHE A  51     8780  21124   6836    987   1601  -1350       C  
ATOM    395  C   PHE A  51      -0.362 -89.223  20.218  1.00103.89           C  
ANISOU  395  C   PHE A  51    10262  21398   7813    793   1745  -1130       C  
ATOM    396  O   PHE A  51       0.400 -90.055  20.709  1.00107.90           O  
ANISOU  396  O   PHE A  51    11040  21584   8375   1042   1878   -976       O  
ATOM    397  CB  PHE A  51      -2.748 -89.889  20.371  1.00 98.89           C  
ANISOU  397  CB  PHE A  51     8667  21693   7215    668   1803  -1563       C  
ATOM    398  CG  PHE A  51      -4.056 -90.116  19.676  1.00114.15           C  
ANISOU  398  CG  PHE A  51     9958  24270   9144    744   1669  -1824       C  
ATOM    399  CD1 PHE A  51      -4.559 -89.172  18.798  1.00125.48           C  
ANISOU  399  CD1 PHE A  51    11171  25975  10533    558   1408  -1966       C  
ATOM    400  CD2 PHE A  51      -4.789 -91.265  19.912  1.00126.43           C  
ANISOU  400  CD2 PHE A  51    11112  26166  10759   1001   1798  -1956       C  
ATOM    401  CE1 PHE A  51      -5.763 -89.376  18.160  1.00110.54           C  
ANISOU  401  CE1 PHE A  51     8656  24679   8664    618   1250  -2230       C  
ATOM    402  CE2 PHE A  51      -5.994 -91.472  19.279  1.00112.58           C  
ANISOU  402  CE2 PHE A  51     8716  25016   9043   1074   1665  -2213       C  
ATOM    403  CZ  PHE A  51      -6.480 -90.527  18.402  1.00115.34           C  
ANISOU  403  CZ  PHE A  51     8837  25631   9358    875   1379  -2348       C  
ATOM    404  N   LEU A  52      -0.184 -87.914  20.340  1.00112.19           N  
ANISOU  404  N   LEU A  52    11481  22262   8883    352   1700  -1136       N  
ATOM    405  CA  LEU A  52       0.888 -87.352  21.140  1.00 93.04           C  
ANISOU  405  CA  LEU A  52     9545  19251   6555    118   1810   -959       C  
ATOM    406  C   LEU A  52       0.283 -86.388  22.147  1.00 86.71           C  
ANISOU  406  C   LEU A  52     8715  18387   5844   -505   1897  -1070       C  
ATOM    407  O   LEU A  52      -0.788 -85.823  21.920  1.00 92.75           O  
ANISOU  407  O   LEU A  52     9135  19509   6598   -788   1831  -1267       O  
ATOM    408  CB  LEU A  52       1.897 -86.609  20.258  1.00 86.91           C  
ANISOU  408  CB  LEU A  52     9069  18221   5731    227   1669   -822       C  
ATOM    409  CG  LEU A  52       2.903 -87.366  19.384  1.00 83.51           C  
ANISOU  409  CG  LEU A  52     8855  17652   5223    784   1627   -606       C  
ATOM    410  CD1 LEU A  52       2.233 -88.171  18.287  1.00108.61           C  
ANISOU  410  CD1 LEU A  52    11703  21333   8230   1233   1473   -670       C  
ATOM    411  CD2 LEU A  52       3.892 -86.389  18.771  1.00113.57           C  
ANISOU  411  CD2 LEU A  52    12984  21171   8997    745   1567   -481       C  
ATOM    412  N   THR A  53       0.964 -86.222  23.270  1.00 94.86           N  
ANISOU  412  N   THR A  53    10121  18903   7017   -713   2013   -932       N  
ATOM    413  CA  THR A  53       0.633 -85.166  24.208  1.00101.51           C  
ANISOU  413  CA  THR A  53    11061  19547   7962  -1281   2053   -966       C  
ATOM    414  C   THR A  53       1.790 -84.181  24.235  1.00 90.31           C  
ANISOU  414  C   THR A  53    10052  17629   6631  -1395   1972   -829       C  
ATOM    415  O   THR A  53       2.969 -84.569  24.154  1.00 93.52           O  
ANISOU  415  O   THR A  53    10753  17691   7090  -1097   1972   -661       O  
ATOM    416  CB  THR A  53       0.331 -85.700  25.624  1.00 93.08           C  
ANISOU  416  CB  THR A  53    10086  18298   6982  -1459   2229   -933       C  
ATOM    417  OG1 THR A  53       1.322 -86.666  25.996  1.00120.71           O  
ANISOU  417  OG1 THR A  53    13876  21468  10519  -1100   2284   -790       O  
ATOM    418  CG2 THR A  53      -1.047 -86.355  25.671  1.00 98.71           C  
ANISOU  418  CG2 THR A  53    10331  19540   7634  -1491   2341  -1114       C  
ATOM    419  N   ILE A  54       1.434 -82.906  24.327  1.00 81.88           N  
ANISOU  419  N   ILE A  54     8978  16550   5583  -1837   1919   -916       N  
ATOM    420  CA  ILE A  54       2.378 -81.807  24.268  1.00 87.58           C  
ANISOU  420  CA  ILE A  54    10026  16828   6423  -1966   1822   -837       C  
ATOM    421  C   ILE A  54       2.144 -80.882  25.453  1.00106.58           C  
ANISOU  421  C   ILE A  54    12599  18932   8965  -2489   1852   -826       C  
ATOM    422  O   ILE A  54       1.073 -80.297  25.585  1.00109.64           O  
ANISOU  422  O   ILE A  54    12777  19523   9360  -2860   1842   -963       O  
ATOM    423  CB  ILE A  54       2.178 -80.997  22.977  1.00 75.90           C  
ANISOU  423  CB  ILE A  54     8393  15559   4886  -1936   1650   -983       C  
ATOM    424  CG1 ILE A  54       2.437 -81.876  21.755  1.00 78.35           C  
ANISOU  424  CG1 ILE A  54     8583  16165   5021  -1396   1595   -961       C  
ATOM    425  CG2 ILE A  54       3.070 -79.767  22.964  1.00 87.97           C  
ANISOU  425  CG2 ILE A  54    10235  16637   6553  -2097   1577   -942       C  
ATOM    426  CD1 ILE A  54       1.979 -81.257  20.460  1.00 93.98           C  
ANISOU  426  CD1 ILE A  54    10357  18489   6864  -1342   1405  -1143       C  
ATOM    427  N   HIS A  55       3.142 -80.759  26.317  1.00 86.24           N  
ANISOU  427  N   HIS A  55    10398  15860   6508  -2522   1876   -657       N  
ATOM    428  CA  HIS A  55       3.051 -79.845  27.447  1.00116.11           C  
ANISOU  428  CA  HIS A  55    14398  19301  10416  -2977   1864   -610       C  
ATOM    429  C   HIS A  55       4.059 -78.715  27.310  1.00102.32           C  
ANISOU  429  C   HIS A  55    12919  17090   8868  -3034   1725   -561       C  
ATOM    430  O   HIS A  55       5.274 -78.929  27.365  1.00116.80           O  
ANISOU  430  O   HIS A  55    14982  18597  10800  -2787   1712   -436       O  
ATOM    431  CB  HIS A  55       3.222 -80.587  28.775  1.00115.23           C  
ANISOU  431  CB  HIS A  55    14498  19011  10274  -3015   1979   -476       C  
ATOM    432  CG  HIS A  55       2.037 -81.418  29.152  1.00103.44           C  
ANISOU  432  CG  HIS A  55    12748  17866   8690  -3044   2102   -545       C  
ATOM    433  ND1 HIS A  55       1.910 -82.742  28.791  1.00 77.26           N  
ANISOU  433  ND1 HIS A  55     9244  14806   5304  -2633   2177   -581       N  
ATOM    434  CD2 HIS A  55       0.916 -81.108  29.846  1.00123.55           C  
ANISOU  434  CD2 HIS A  55    15188  20548  11207  -3442   2183   -586       C  
ATOM    435  CE1 HIS A  55       0.766 -83.214  29.253  1.00130.43           C  
ANISOU  435  CE1 HIS A  55    15751  21833  11974  -2767   2303   -660       C  
ATOM    436  NE2 HIS A  55       0.143 -82.243  29.896  1.00154.84           N  
ANISOU  436  NE2 HIS A  55    18885  24859  15088  -3262   2317   -658       N  
ATOM    437  N   PHE A  56       3.536 -77.510  27.104  1.00 88.37           N  
ANISOU  437  N   PHE A  56    11097  15295   7186  -3361   1629   -679       N  
ATOM    438  CA  PHE A  56       4.358 -76.318  27.012  1.00 87.71           C  
ANISOU  438  CA  PHE A  56    11239  14776   7312  -3444   1503   -675       C  
ATOM    439  C   PHE A  56       4.772 -75.882  28.404  1.00 93.81           C  
ANISOU  439  C   PHE A  56    12333  15057   8253  -3699   1471   -519       C  
ATOM    440  O   PHE A  56       3.918 -75.669  29.267  1.00113.37           O  
ANISOU  440  O   PHE A  56    14831  17537  10708  -4060   1492   -495       O  
ATOM    441  CB  PHE A  56       3.581 -75.184  26.341  1.00105.48           C  
ANISOU  441  CB  PHE A  56    13325  17151   9603  -3708   1397   -889       C  
ATOM    442  CG  PHE A  56       3.277 -75.430  24.893  1.00 96.18           C  
ANISOU  442  CG  PHE A  56    11865  16430   8250  -3445   1365  -1066       C  
ATOM    443  CD1 PHE A  56       4.202 -75.107  23.915  1.00 95.21           C  
ANISOU  443  CD1 PHE A  56    11828  16226   8121  -3145   1314  -1100       C  
ATOM    444  CD2 PHE A  56       2.064 -75.972  24.507  1.00114.20           C  
ANISOU  444  CD2 PHE A  56    13791  19234  10368  -3494   1384  -1200       C  
ATOM    445  CE1 PHE A  56       3.926 -75.326  22.580  1.00 91.18           C  
ANISOU  445  CE1 PHE A  56    11100  16146   7397  -2887   1264  -1247       C  
ATOM    446  CE2 PHE A  56       1.781 -76.191  23.170  1.00 99.49           C  
ANISOU  446  CE2 PHE A  56    11671  17799   8331  -3229   1304  -1366       C  
ATOM    447  CZ  PHE A  56       2.714 -75.868  22.208  1.00110.13           C  
ANISOU  447  CZ  PHE A  56    13154  19060   9629  -2921   1234  -1382       C  
ATOM    448  N   PRO A  57       6.086 -75.756  28.630  1.00 72.16           N  
ANISOU  448  N   PRO A  57     9841  11895   5683  -3514   1418   -404       N  
ATOM    449  CA  PRO A  57       6.600 -75.264  29.910  1.00111.69           C  
ANISOU  449  CA  PRO A  57    15159  16405  10874  -3718   1325   -265       C  
ATOM    450  C   PRO A  57       6.081 -73.860  30.189  1.00109.46           C  
ANISOU  450  C   PRO A  57    14943  15899  10746  -4113   1202   -327       C  
ATOM    451  O   PRO A  57       5.887 -73.087  29.252  1.00 87.41           O  
ANISOU  451  O   PRO A  57    12012  13183   8017  -4139   1159   -495       O  
ATOM    452  CB  PRO A  57       8.110 -75.214  29.678  1.00134.59           C  
ANISOU  452  CB  PRO A  57    18202  18950  13986  -3417   1277   -201       C  
ATOM    453  CG  PRO A  57       8.359 -76.207  28.603  1.00120.03           C  
ANISOU  453  CG  PRO A  57    16178  17440  11989  -3031   1407   -224       C  
ATOM    454  CD  PRO A  57       7.167 -76.127  27.703  1.00 97.04           C  
ANISOU  454  CD  PRO A  57    12987  15020   8865  -3096   1446   -388       C  
ATOM    455  N   THR A  58       5.863 -73.550  31.463  1.00129.04           N  
ANISOU  455  N   THR A  58    17655  18099  13276  -4407   1137   -194       N  
ATOM    456  CA  THR A  58       5.403 -72.228  31.874  1.00107.06           C  
ANISOU  456  CA  THR A  58    14991  15021  10667  -4790   1008   -209       C  
ATOM    457  C   THR A  58       6.287 -71.093  31.343  1.00126.05           C  
ANISOU  457  C   THR A  58    17461  17049  13382  -4698    855   -305       C  
ATOM    458  O   THR A  58       5.808 -69.984  31.108  1.00133.46           O  
ANISOU  458  O   THR A  58    18385  17859  14465  -4939    769   -426       O  
ATOM    459  CB  THR A  58       5.291 -72.135  33.410  1.00144.92           C  
ANISOU  459  CB  THR A  58    20107  19500  15456  -5052    940     11       C  
ATOM    460  OG1 THR A  58       5.284 -70.755  33.806  1.00185.17           O  
ANISOU  460  OG1 THR A  58    25395  24147  20813  -5326    755     33       O  
ATOM    461  CG2 THR A  58       6.460 -72.838  34.071  1.00139.95           C  
ANISOU  461  CG2 THR A  58    19689  18641  14844  -4770    881    153       C  
ATOM    462  N   ASP A  59       7.573 -71.380  31.160  1.00136.42           N  
ANISOU  462  N   ASP A  59    18838  18180  14815  -4352    836   -265       N  
ATOM    463  CA  ASP A  59       8.476 -70.448  30.507  1.00104.73           C  
ANISOU  463  CA  ASP A  59    14829  13885  11076  -4205    758   -379       C  
ATOM    464  C   ASP A  59       8.739 -70.895  29.072  1.00122.22           C  
ANISOU  464  C   ASP A  59    16810  16470  13156  -3883    905   -517       C  
ATOM    465  O   ASP A  59       9.404 -71.897  28.825  1.00150.83           O  
ANISOU  465  O   ASP A  59    20401  20213  16694  -3578   1012   -429       O  
ATOM    466  CB  ASP A  59       9.789 -70.328  31.276  1.00131.58           C  
ANISOU  466  CB  ASP A  59    18443  16797  14755  -4062    641   -242       C  
ATOM    467  CG  ASP A  59      10.385 -71.679  31.644  1.00173.80           C  
ANISOU  467  CG  ASP A  59    23821  22233  19982  -3824    719    -94       C  
ATOM    468  OD1 ASP A  59       9.619 -72.658  31.693  1.00206.94           O  
ANISOU  468  OD1 ASP A  59    27946  26810  23872  -3840    839    -59       O  
ATOM    469  OD2 ASP A  59      11.613 -71.754  31.874  1.00159.33           O  
ANISOU  469  OD2 ASP A  59    22068  20084  18385  -3623    661    -32       O  
ATOM    470  N   TYR A  60       8.182 -70.162  28.123  1.00124.75           N  
ANISOU  470  N   TYR A  60    16985  16971  13445  -3954    900   -734       N  
ATOM    471  CA  TYR A  60       8.250 -70.543  26.724  1.00 84.11           C  
ANISOU  471  CA  TYR A  60    11634  12229   8095  -3667   1015   -870       C  
ATOM    472  C   TYR A  60       8.498 -69.256  25.924  1.00111.58           C  
ANISOU  472  C   TYR A  60    15107  15566  11722  -3672    956  -1102       C  
ATOM    473  O   TYR A  60       8.142 -68.179  26.391  1.00174.68           O  
ANISOU  473  O   TYR A  60    23184  23262  19923  -3963    823  -1194       O  
ATOM    474  CB  TYR A  60       6.937 -71.242  26.358  1.00 84.40           C  
ANISOU  474  CB  TYR A  60    11443  12807   7820  -3760   1064   -938       C  
ATOM    475  CG  TYR A  60       6.938 -71.899  25.001  1.00 96.10           C  
ANISOU  475  CG  TYR A  60    12720  14758   9037  -3421   1152  -1034       C  
ATOM    476  CD1 TYR A  60       7.471 -73.171  24.814  1.00 92.49           C  
ANISOU  476  CD1 TYR A  60    12242  14470   8430  -3075   1275   -870       C  
ATOM    477  CD2 TYR A  60       6.421 -71.239  23.899  1.00139.65           C  
ANISOU  477  CD2 TYR A  60    18084  20531  14448  -3436   1093  -1290       C  
ATOM    478  CE1 TYR A  60       7.483 -73.762  23.563  1.00104.24           C  
ANISOU  478  CE1 TYR A  60    13576  16363   9666  -2745   1338   -924       C  
ATOM    479  CE2 TYR A  60       6.429 -71.816  22.655  1.00 87.86           C  
ANISOU  479  CE2 TYR A  60    11369  14405   7609  -3108   1142  -1364       C  
ATOM    480  CZ  TYR A  60       6.958 -73.074  22.485  1.00 74.38           C  
ANISOU  480  CZ  TYR A  60     9656  12853   5751  -2758   1265  -1164       C  
ATOM    481  OH  TYR A  60       6.959 -73.637  21.233  1.00 92.52           O  
ANISOU  481  OH  TYR A  60    11828  15565   7760  -2416   1295  -1209       O  
ATOM    482  N   PRO A  61       9.162 -69.339  24.758  1.00 86.26           N  
ANISOU  482  N   PRO A  61    11829  12533   8414  -3342   1061  -1191       N  
ATOM    483  CA  PRO A  61       9.870 -70.436  24.085  1.00 90.40           C  
ANISOU  483  CA  PRO A  61    12304  13296   8747  -2951   1227  -1062       C  
ATOM    484  C   PRO A  61      11.149 -70.922  24.792  1.00101.30           C  
ANISOU  484  C   PRO A  61    13831  14302  10358  -2785   1298   -825       C  
ATOM    485  O   PRO A  61      11.701 -71.916  24.336  1.00138.59           O  
ANISOU  485  O   PRO A  61    18525  19181  14950  -2490   1439   -693       O  
ATOM    486  CB  PRO A  61      10.203 -69.854  22.722  1.00110.51           C  
ANISOU  486  CB  PRO A  61    14799  16012  11179  -2743   1292  -1259       C  
ATOM    487  CG  PRO A  61      10.211 -68.388  22.901  1.00137.37           C  
ANISOU  487  CG  PRO A  61    18274  19074  14845  -2964   1182  -1467       C  
ATOM    488  CD  PRO A  61       9.146 -68.116  23.933  1.00135.31           C  
ANISOU  488  CD  PRO A  61    18023  18699  14692  -3371   1013  -1470       C  
ATOM    489  N   PHE A  62      11.634 -70.231  25.822  1.00101.60           N  
ANISOU  489  N   PHE A  62    14015  13847  10743  -2956   1189   -779       N  
ATOM    490  CA  PHE A  62      12.972 -70.502  26.369  1.00 83.93           C  
ANISOU  490  CA  PHE A  62    11880  11227   8782  -2789   1226   -610       C  
ATOM    491  C   PHE A  62      13.306 -71.962  26.669  1.00101.99           C  
ANISOU  491  C   PHE A  62    14178  13619  10955  -2609   1314   -397       C  
ATOM    492  O   PHE A  62      14.470 -72.363  26.567  1.00114.12           O  
ANISOU  492  O   PHE A  62    15736  14968  12657  -2384   1415   -289       O  
ATOM    493  CB  PHE A  62      13.209 -69.708  27.650  1.00 91.10           C  
ANISOU  493  CB  PHE A  62    12942  11627  10045  -3023   1023   -573       C  
ATOM    494  CG  PHE A  62      12.987 -68.245  27.492  1.00 98.75           C  
ANISOU  494  CG  PHE A  62    13927  12388  11205  -3189    917   -776       C  
ATOM    495  CD1 PHE A  62      13.338 -67.600  26.313  1.00 74.50           C  
ANISOU  495  CD1 PHE A  62    10760   9409   8138  -3026   1038   -976       C  
ATOM    496  CD2 PHE A  62      12.422 -67.512  28.509  1.00177.10           C  
ANISOU  496  CD2 PHE A  62    23985  22015  21292  -3500    700   -769       C  
ATOM    497  CE1 PHE A  62      13.124 -66.250  26.176  1.00109.84           C  
ANISOU  497  CE1 PHE A  62    15258  13675  12800  -3167    937  -1201       C  
ATOM    498  CE2 PHE A  62      12.203 -66.168  28.381  1.00197.76           C  
ANISOU  498  CE2 PHE A  62    26631  24393  24116  -3648    591   -960       C  
ATOM    499  CZ  PHE A  62      12.559 -65.530  27.206  1.00191.23           C  
ANISOU  499  CZ  PHE A  62    25691  23653  23315  -3476    706  -1197       C  
ATOM    500  N   LYS A  63      12.307 -72.754  27.051  1.00 95.55           N  
ANISOU  500  N   LYS A  63    13339  13085   9882  -2712   1287   -347       N  
ATOM    501  CA  LYS A  63      12.489 -74.190  27.202  1.00 77.93           C  
ANISOU  501  CA  LYS A  63    11103  11003   7505  -2510   1382   -190       C  
ATOM    502  C   LYS A  63      11.632 -74.915  26.173  1.00 87.44           C  
ANISOU  502  C   LYS A  63    12127  12760   8335  -2361   1492   -244       C  
ATOM    503  O   LYS A  63      10.560 -74.440  25.806  1.00131.60           O  
ANISOU  503  O   LYS A  63    17602  18640  13762  -2530   1444   -395       O  
ATOM    504  CB  LYS A  63      12.069 -74.640  28.610  1.00 97.89           C  
ANISOU  504  CB  LYS A  63    13756  13404  10032  -2716   1268    -93       C  
ATOM    505  CG  LYS A  63      13.071 -74.373  29.704  1.00107.98           C  
ANISOU  505  CG  LYS A  63    15226  14158  11643  -2767   1133      6       C  
ATOM    506  CD  LYS A  63      12.455 -74.737  31.044  1.00135.28           C  
ANISOU  506  CD  LYS A  63    18841  17561  14999  -2989   1010     88       C  
ATOM    507  CE  LYS A  63      13.497 -74.822  32.127  1.00151.01           C  
ANISOU  507  CE  LYS A  63    21027  19090  17259  -2968    852    193       C  
ATOM    508  NZ  LYS A  63      14.230 -73.542  32.266  1.00180.26           N  
ANISOU  508  NZ  LYS A  63    24778  22372  21342  -3039    700    159       N  
ATOM    509  N   PRO A  64      12.106 -76.079  25.711  1.00 85.64           N  
ANISOU  509  N   PRO A  64    11872  12670   7997  -2041   1623   -124       N  
ATOM    510  CA  PRO A  64      11.390 -76.845  24.687  1.00 83.52           C  
ANISOU  510  CA  PRO A  64    11434  12915   7385  -1833   1704   -156       C  
ATOM    511  C   PRO A  64      10.127 -77.482  25.246  1.00 93.76           C  
ANISOU  511  C   PRO A  64    12618  14520   8485  -1977   1660   -196       C  
ATOM    512  O   PRO A  64      10.075 -77.778  26.440  1.00118.41           O  
ANISOU  512  O   PRO A  64    15847  17446  11698  -2135   1626   -128       O  
ATOM    513  CB  PRO A  64      12.392 -77.931  24.301  1.00 73.15           C  
ANISOU  513  CB  PRO A  64    10179  11526   6088  -1464   1844     28       C  
ATOM    514  CG  PRO A  64      13.239 -78.109  25.507  1.00 97.86           C  
ANISOU  514  CG  PRO A  64    13474  14180   9527  -1548   1812    139       C  
ATOM    515  CD  PRO A  64      13.339 -76.760  26.154  1.00111.94           C  
ANISOU  515  CD  PRO A  64    15329  15656  11547  -1859   1682     48       C  
ATOM    516  N   PRO A  65       9.113 -77.687  24.394  1.00 89.11           N  
ANISOU  516  N   PRO A  65    11808  14425   7623  -1922   1661   -315       N  
ATOM    517  CA  PRO A  65       7.891 -78.380  24.819  1.00 92.75           C  
ANISOU  517  CA  PRO A  65    12099  15235   7909  -2033   1659   -366       C  
ATOM    518  C   PRO A  65       8.174 -79.846  25.125  1.00 95.21           C  
ANISOU  518  C   PRO A  65    12432  15586   8156  -1747   1760   -225       C  
ATOM    519  O   PRO A  65       9.064 -80.443  24.514  1.00 95.37           O  
ANISOU  519  O   PRO A  65    12520  15530   8187  -1397   1824   -109       O  
ATOM    520  CB  PRO A  65       6.974 -78.257  23.599  1.00102.40           C  
ANISOU  520  CB  PRO A  65    13048  16965   8893  -1960   1617   -538       C  
ATOM    521  CG  PRO A  65       7.896 -78.033  22.445  1.00 65.75           C  
ANISOU  521  CG  PRO A  65     8482  12287   4213  -1652   1635   -507       C  
ATOM    522  CD  PRO A  65       9.041 -77.241  22.993  1.00 67.27           C  
ANISOU  522  CD  PRO A  65     8931  11932   4697  -1759   1656   -427       C  
ATOM    523  N   LYS A  66       7.439 -80.413  26.076  1.00 86.87           N  
ANISOU  523  N   LYS A  66    11336  14632   7039  -1900   1788   -235       N  
ATOM    524  CA  LYS A  66       7.589 -81.828  26.392  1.00 92.14           C  
ANISOU  524  CA  LYS A  66    12014  15360   7635  -1625   1885   -151       C  
ATOM    525  C   LYS A  66       6.598 -82.615  25.555  1.00 84.31           C  
ANISOU  525  C   LYS A  66    10704  14926   6406  -1411   1929   -247       C  
ATOM    526  O   LYS A  66       5.391 -82.434  25.679  1.00104.85           O  
ANISOU  526  O   LYS A  66    13075  17868   8895  -1640   1928   -385       O  
ATOM    527  CB  LYS A  66       7.361 -82.090  27.885  1.00108.96           C  
ANISOU  527  CB  LYS A  66    14289  17320   9791  -1866   1907   -126       C  
ATOM    528  CG  LYS A  66       8.534 -81.700  28.780  1.00 97.32           C  
ANISOU  528  CG  LYS A  66    13145  15274   8557  -1956   1832    -10       C  
ATOM    529  CD  LYS A  66       8.235 -80.443  29.583  1.00141.77           C  
ANISOU  529  CD  LYS A  66    18894  20695  14278  -2394   1723    -27       C  
ATOM    530  CE  LYS A  66       7.112 -80.681  30.583  1.00177.47           C  
ANISOU  530  CE  LYS A  66    23405  25413  18612  -2673   1775    -57       C  
ATOM    531  NZ  LYS A  66       6.796 -79.458  31.375  1.00146.77           N  
ANISOU  531  NZ  LYS A  66    19668  21289  14808  -3106   1667    -34       N  
ATOM    532  N   VAL A  67       7.105 -83.481  24.686  1.00 87.13           N  
ANISOU  532  N   VAL A  67    11036  15366   6705   -972   1963   -169       N  
ATOM    533  CA  VAL A  67       6.244 -84.178  23.742  1.00 95.08           C  
ANISOU  533  CA  VAL A  67    11735  16895   7495   -708   1958   -254       C  
ATOM    534  C   VAL A  67       6.408 -85.687  23.845  1.00 87.25           C  
ANISOU  534  C   VAL A  67    10735  15946   6470   -321   2048   -177       C  
ATOM    535  O   VAL A  67       7.530 -86.193  23.853  1.00 68.88           O  
ANISOU  535  O   VAL A  67     8650  13260   4260    -80   2091    -13       O  
ATOM    536  CB  VAL A  67       6.555 -83.756  22.300  1.00 69.94           C  
ANISOU  536  CB  VAL A  67     8511  13850   4212   -480   1875   -240       C  
ATOM    537  CG1 VAL A  67       5.576 -84.402  21.345  1.00 84.63           C  
ANISOU  537  CG1 VAL A  67    10038  16271   5845   -217   1808   -344       C  
ATOM    538  CG2 VAL A  67       6.507 -82.244  22.168  1.00106.32           C  
ANISOU  538  CG2 VAL A  67    13156  18368   8871   -832   1789   -344       C  
ATOM    539  N   ALA A  68       5.292 -86.408  23.916  1.00 83.07           N  
ANISOU  539  N   ALA A  68     9916  15816   5829   -259   2074   -306       N  
ATOM    540  CA  ALA A  68       5.379 -87.866  23.999  1.00 73.87           C  
ANISOU  540  CA  ALA A  68     8722  14722   4624    137   2167   -269       C  
ATOM    541  C   ALA A  68       4.211 -88.623  23.358  1.00103.75           C  
ANISOU  541  C   ALA A  68    12092  19069   8260    378   2151   -413       C  
ATOM    542  O   ALA A  68       3.071 -88.170  23.395  1.00103.65           O  
ANISOU  542  O   ALA A  68    11778  19403   8201    112   2121   -585       O  
ATOM    543  CB  ALA A  68       5.566 -88.300  25.446  1.00 99.50           C  
ANISOU  543  CB  ALA A  68    12160  17688   7957    -25   2284   -273       C  
ATOM    544  N   PHE A  69       4.511 -89.780  22.776  1.00 78.98           N  
ANISOU  544  N   PHE A  69     8932  15992   5083    886   2162   -339       N  
ATOM    545  CA  PHE A  69       3.485 -90.643  22.208  1.00 82.76           C  
ANISOU  545  CA  PHE A  69     9010  16989   5446   1192   2137   -474       C  
ATOM    546  C   PHE A  69       2.664 -91.315  23.304  1.00 84.27           C  
ANISOU  546  C   PHE A  69     9018  17349   5650   1076   2308   -646       C  
ATOM    547  O   PHE A  69       3.219 -91.987  24.173  1.00 83.37           O  
ANISOU  547  O   PHE A  69     9150  16912   5616   1147   2435   -602       O  
ATOM    548  CB  PHE A  69       4.123 -91.742  21.356  1.00 96.67           C  
ANISOU  548  CB  PHE A  69    10856  18668   7204   1797   2089   -317       C  
ATOM    549  CG  PHE A  69       4.557 -91.289  19.991  1.00 84.58           C  
ANISOU  549  CG  PHE A  69     9387  17187   5562   2010   1922   -172       C  
ATOM    550  CD1 PHE A  69       5.772 -90.655  19.811  1.00 88.02           C  
ANISOU  550  CD1 PHE A  69    10208  17176   6058   1938   1935     35       C  
ATOM    551  CD2 PHE A  69       3.762 -91.524  18.885  1.00 88.12           C  
ANISOU  551  CD2 PHE A  69     9504  18141   5837   2300   1754   -249       C  
ATOM    552  CE1 PHE A  69       6.176 -90.245  18.554  1.00 92.19           C  
ANISOU  552  CE1 PHE A  69    10816  17771   6440   2139   1819    170       C  
ATOM    553  CE2 PHE A  69       4.164 -91.117  17.625  1.00108.69           C  
ANISOU  553  CE2 PHE A  69    12205  20812   8280   2512   1592   -114       C  
ATOM    554  CZ  PHE A  69       5.372 -90.478  17.461  1.00 86.16           C  
ANISOU  554  CZ  PHE A  69     9765  17519   5454   2429   1643    100       C  
ATOM    555  N   THR A  70       1.346 -91.136  23.261  1.00 86.93           N  
ANISOU  555  N   THR A  70     8927  18174   5928    889   2309   -852       N  
ATOM    556  CA  THR A  70       0.447 -91.919  24.107  1.00 95.92           C  
ANISOU  556  CA  THR A  70     9832  19508   7105    847   2476  -1018       C  
ATOM    557  C   THR A  70       0.183 -93.295  23.493  1.00 92.95           C  
ANISOU  557  C   THR A  70     9177  19469   6669   1450   2500  -1093       C  
ATOM    558  O   THR A  70       0.027 -94.287  24.204  1.00124.35           O  
ANISOU  558  O   THR A  70    13144  23403  10702   1606   2659  -1172       O  
ATOM    559  CB  THR A  70      -0.883 -91.190  24.386  1.00 91.49           C  
ANISOU  559  CB  THR A  70     8903  19310   6549    371   2505  -1202       C  
ATOM    560  OG1 THR A  70      -1.073 -90.143  23.425  1.00 91.28           O  
ANISOU  560  OG1 THR A  70     8725  19510   6448    221   2324  -1228       O  
ATOM    561  CG2 THR A  70      -0.876 -90.584  25.782  1.00133.35           C  
ANISOU  561  CG2 THR A  70    14497  24225  11943   -148   2629  -1161       C  
ATOM    562  N   THR A  71       0.141 -93.341  22.165  1.00 94.48           N  
ANISOU  562  N   THR A  71     9189  19902   6807   1791   2290  -1059       N  
ATOM    563  CA  THR A  71      -0.030 -94.590  21.425  1.00112.48           C  
ANISOU  563  CA  THR A  71    11250  22399   9090   2413   2221  -1080       C  
ATOM    564  C   THR A  71       1.288 -95.364  21.374  1.00104.32           C  
ANISOU  564  C   THR A  71    10679  20827   8131   2820   2228   -845       C  
ATOM    565  O   THR A  71       2.329 -94.791  21.058  1.00 93.48           O  
ANISOU  565  O   THR A  71     9692  19061   6764   2769   2150   -620       O  
ATOM    566  CB  THR A  71      -0.501 -94.306  19.978  1.00100.58           C  
ANISOU  566  CB  THR A  71     9431  21304   7480   2638   1934  -1098       C  
ATOM    567  OG1 THR A  71      -1.704 -93.524  20.004  1.00132.53           O  
ANISOU  567  OG1 THR A  71    13038  25821  11498   2219   1907  -1336       O  
ATOM    568  CG2 THR A  71      -0.759 -95.601  19.224  1.00116.39           C  
ANISOU  568  CG2 THR A  71    11183  23548   9490   3304   1829  -1118       C  
ATOM    569  N   ARG A  72       1.256 -96.656  21.688  1.00 98.80           N  
ANISOU  569  N   ARG A  72     9935  20094   7509   3214   2335   -906       N  
ATOM    570  CA  ARG A  72       2.475 -97.457  21.630  1.00 97.92           C  
ANISOU  570  CA  ARG A  72    10251  19444   7510   3601   2337   -697       C  
ATOM    571  C   ARG A  72       2.919 -97.613  20.182  1.00 99.29           C  
ANISOU  571  C   ARG A  72    10474  19612   7641   4050   2105   -472       C  
ATOM    572  O   ARG A  72       2.090 -97.725  19.279  1.00132.83           O  
ANISOU  572  O   ARG A  72    14335  24349  11786   4287   1941   -551       O  
ATOM    573  CB  ARG A  72       2.286 -98.825  22.288  1.00100.66           C  
ANISOU  573  CB  ARG A  72    10536  19750   7960   3940   2497   -852       C  
ATOM    574  CG  ARG A  72       3.512 -99.294  23.073  1.00141.98           C  
ANISOU  574  CG  ARG A  72    16290  24318  13338   3974   2602   -736       C  
ATOM    575  CD  ARG A  72       3.564-100.809  23.222  1.00147.12           C  
ANISOU  575  CD  ARG A  72    16934  24850  14116   4512   2674   -836       C  
ATOM    576  NE  ARG A  72       2.467-101.336  24.028  1.00176.10           N  
ANISOU  576  NE  ARG A  72    20258  28919  17732   4481   2868  -1174       N  
ATOM    577  CZ  ARG A  72       2.543-101.561  25.335  1.00193.59           C  
ANISOU  577  CZ  ARG A  72    22654  30961  19939   4252   3079  -1340       C  
ATOM    578  NH1 ARG A  72       3.670-101.302  25.987  1.00211.90           N  
ANISOU  578  NH1 ARG A  72    25480  32704  22326   4039   3081  -1209       N  
ATOM    579  NH2 ARG A  72       1.494-102.043  25.992  1.00137.34           N  
ANISOU  579  NH2 ARG A  72    15198  24251  12733   4240   3290  -1643       N  
ATOM    580  N   ILE A  73       4.230 -97.607  19.960  1.00 97.07           N  
ANISOU  580  N   ILE A  73    10666  18784   7433   4155   2090   -189       N  
ATOM    581  CA  ILE A  73       4.765 -97.671  18.604  1.00101.82           C  
ANISOU  581  CA  ILE A  73    11397  19336   7955   4543   1905     79       C  
ATOM    582  C   ILE A  73       6.114 -98.389  18.564  1.00 97.89           C  
ANISOU  582  C   ILE A  73    11371  18193   7631   4836   1970    361       C  
ATOM    583  O   ILE A  73       6.928 -98.260  19.479  1.00114.40           O  
ANISOU  583  O   ILE A  73    13773  19804   9890   4565   2120    397       O  
ATOM    584  CB  ILE A  73       4.883 -96.255  17.985  1.00 96.24           C  
ANISOU  584  CB  ILE A  73    10740  18751   7075   4199   1795    165       C  
ATOM    585  CG1 ILE A  73       5.321 -96.330  16.525  1.00 98.42           C  
ANISOU  585  CG1 ILE A  73    11142  19063   7189   4620   1608    428       C  
ATOM    586  CG2 ILE A  73       5.837 -95.386  18.788  1.00 91.49           C  
ANISOU  586  CG2 ILE A  73    10515  17659   6587   3723   1939    256       C  
ATOM    587  CD1 ILE A  73       5.401 -94.980  15.855  1.00 96.92           C  
ANISOU  587  CD1 ILE A  73    11002  19031   6794   4327   1502    474       C  
ATOM    588  N   TYR A  74       6.339 -99.158  17.506  1.00101.27           N  
ANISOU  588  N   TYR A  74    11849  18602   8029   5389   1842    563       N  
ATOM    589  CA  TYR A  74       7.589 -99.888  17.346  1.00101.59           C  
ANISOU  589  CA  TYR A  74    12329  18016   8252   5687   1904    861       C  
ATOM    590  C   TYR A  74       8.537 -99.062  16.499  1.00100.05           C  
ANISOU  590  C   TYR A  74    12458  17603   7953   5596   1874   1198       C  
ATOM    591  O   TYR A  74       8.264 -98.800  15.328  1.00112.59           O  
ANISOU  591  O   TYR A  74    13969  19519   9289   5816   1706   1328       O  
ATOM    592  CB  TYR A  74       7.327-101.236  16.678  1.00106.83           C  
ANISOU  592  CB  TYR A  74    12902  18732   8957   6363   1793    924       C  
ATOM    593  CG  TYR A  74       8.486-102.205  16.746  1.00115.91           C  
ANISOU  593  CG  TYR A  74    14478  19192  10372   6671   1883   1170       C  
ATOM    594  CD1 TYR A  74       8.702-102.977  17.882  1.00114.03           C  
ANISOU  594  CD1 TYR A  74    14324  18595  10406   6652   2036    983       C  
ATOM    595  CD2 TYR A  74       9.347-102.367  15.669  1.00128.30           C  
ANISOU  595  CD2 TYR A  74    16374  20463  11911   6979   1817   1584       C  
ATOM    596  CE1 TYR A  74       9.752-103.873  17.946  1.00117.12           C  
ANISOU  596  CE1 TYR A  74    15098  18326  11076   6918   2101   1180       C  
ATOM    597  CE2 TYR A  74      10.401-103.259  15.724  1.00115.98           C  
ANISOU  597  CE2 TYR A  74    15200  18237  10631   7234   1910   1821       C  
ATOM    598  CZ  TYR A  74      10.599-104.008  16.865  1.00110.35           C  
ANISOU  598  CZ  TYR A  74    14546  17154  10229   7197   2042   1605       C  
ATOM    599  OH  TYR A  74      11.643-104.899  16.928  1.00127.08           O  
ANISOU  599  OH  TYR A  74    17043  18581  12661   7433   2119   1812       O  
ATOM    600  N   HIS A  75       9.662 -98.677  17.085  1.00 96.68           N  
ANISOU  600  N   HIS A  75    12390  16627   7717   5287   2037   1330       N  
ATOM    601  CA  HIS A  75      10.556 -97.714  16.461  1.00 94.85           C  
ANISOU  601  CA  HIS A  75    12429  16202   7407   5097   2070   1599       C  
ATOM    602  C   HIS A  75      11.790 -97.548  17.330  1.00 91.69           C  
ANISOU  602  C   HIS A  75    12367  15147   7325   4791   2261   1695       C  
ATOM    603  O   HIS A  75      11.681 -97.484  18.553  1.00131.46           O  
ANISOU  603  O   HIS A  75    17358  20063  12530   4479   2325   1458       O  
ATOM    604  CB  HIS A  75       9.844 -96.366  16.340  1.00 92.86           C  
ANISOU  604  CB  HIS A  75    11945  16428   6908   4701   1992   1419       C  
ATOM    605  CG  HIS A  75      10.567 -95.372  15.489  1.00 96.29           C  
ANISOU  605  CG  HIS A  75    12604  16792   7189   4585   2005   1652       C  
ATOM    606  ND1 HIS A  75      11.709 -94.723  15.906  1.00100.76           N  
ANISOU  606  ND1 HIS A  75    13467  16871   7945   4260   2180   1786       N  
ATOM    607  CD2 HIS A  75      10.302 -94.905  14.246  1.00117.36           C  
ANISOU  607  CD2 HIS A  75    15236  19835   9522   4758   1866   1754       C  
ATOM    608  CE1 HIS A  75      12.121 -93.907  14.955  1.00121.72           C  
ANISOU  608  CE1 HIS A  75    16255  19602  10392   4241   2185   1962       C  
ATOM    609  NE2 HIS A  75      11.285 -93.997  13.937  1.00 95.25           N  
ANISOU  609  NE2 HIS A  75    12726  16770   6696   4539   1992   1946       N  
ATOM    610  N   PRO A  76      12.970 -97.471  16.700  1.00 92.00           N  
ANISOU  610  N   PRO A  76    12743  14769   7445   4872   2351   2044       N  
ATOM    611  CA  PRO A  76      14.250 -97.394  17.415  1.00 90.42           C  
ANISOU  611  CA  PRO A  76    12843  13910   7603   4616   2526   2157       C  
ATOM    612  C   PRO A  76      14.437 -96.104  18.211  1.00 90.51           C  
ANISOU  612  C   PRO A  76    12826  13893   7673   4039   2578   1995       C  
ATOM    613  O   PRO A  76      15.196 -96.086  19.181  1.00120.82           O  
ANISOU  613  O   PRO A  76    16811  17267  11830   3781   2664   1952       O  
ATOM    614  CB  PRO A  76      15.283 -97.471  16.286  1.00103.48           C  
ANISOU  614  CB  PRO A  76    14799  15266   9254   4845   2622   2590       C  
ATOM    615  CG  PRO A  76      14.553 -97.010  15.073  1.00 93.83           C  
ANISOU  615  CG  PRO A  76    13447  14623   7582   5045   2492   2662       C  
ATOM    616  CD  PRO A  76      13.161 -97.525  15.242  1.00 95.19           C  
ANISOU  616  CD  PRO A  76    13263  15306   7601   5239   2295   2364       C  
ATOM    617  N   ASN A  77      13.780 -95.034  17.789  1.00 93.53           N  
ANISOU  617  N   ASN A  77    13028  14746   7764   3850   2504   1902       N  
ATOM    618  CA  ASN A  77      13.909 -93.744  18.460  1.00 81.49           C  
ANISOU  618  CA  ASN A  77    11477  13193   6291   3328   2534   1754       C  
ATOM    619  C   ASN A  77      12.788 -93.392  19.438  1.00 78.88           C  
ANISOU  619  C   ASN A  77    10880  13196   5895   3028   2442   1398       C  
ATOM    620  O   ASN A  77      12.774 -92.301  20.003  1.00109.51           O  
ANISOU  620  O   ASN A  77    14736  17069   9803   2601   2441   1276       O  
ATOM    621  CB  ASN A  77      14.104 -92.636  17.433  1.00 93.21           C  
ANISOU  621  CB  ASN A  77    12993  14873   7548   3250   2546   1882       C  
ATOM    622  CG  ASN A  77      15.328 -92.862  16.579  1.00110.15           C  
ANISOU  622  CG  ASN A  77    15439  16649   9764   3472   2700   2256       C  
ATOM    623  OD1 ASN A  77      15.224 -93.104  15.376  1.00 85.26           O  
ANISOU  623  OD1 ASN A  77    12339  13724   6333   3818   2673   2455       O  
ATOM    624  ND2 ASN A  77      16.501 -92.800  17.199  1.00138.73           N  
ANISOU  624  ND2 ASN A  77    19258  19696  13758   3271   2861   2362       N  
ATOM    625  N   ILE A  78      11.838 -94.303  19.623  1.00 82.79           N  
ANISOU  625  N   ILE A  78    11172  13982   6305   3256   2376   1240       N  
ATOM    626  CA  ILE A  78      10.748 -94.077  20.568  1.00 79.95           C  
ANISOU  626  CA  ILE A  78    10556  13945   5877   2976   2337    920       C  
ATOM    627  C   ILE A  78      10.553 -95.290  21.473  1.00 81.17           C  
ANISOU  627  C   ILE A  78    10703  13968   6169   3137   2388    782       C  
ATOM    628  O   ILE A  78      10.211 -96.372  20.996  1.00140.82           O  
ANISOU  628  O   ILE A  78    18161  21654  13688   3580   2366    792       O  
ATOM    629  CB  ILE A  78       9.417 -93.804  19.834  1.00 90.07           C  
ANISOU  629  CB  ILE A  78    11469  15903   6851   3047   2213    774       C  
ATOM    630  CG1 ILE A  78       9.627 -92.883  18.630  1.00 82.07           C  
ANISOU  630  CG1 ILE A  78    10488  15047   5648   3053   2135    921       C  
ATOM    631  CG2 ILE A  78       8.397 -93.214  20.786  1.00108.58           C  
ANISOU  631  CG2 ILE A  78    13569  18542   9143   2622   2212    480       C  
ATOM    632  CD1 ILE A  78       8.405 -92.752  17.751  1.00 84.83           C  
ANISOU  632  CD1 ILE A  78    10486  16045   5700   3198   1964    784       C  
ATOM    633  N   ASN A  79      10.769 -95.116  22.776  1.00 85.95           N  
ANISOU  633  N   ASN A  79    11419  14317   6922   2799   2445    642       N  
ATOM    634  CA  ASN A  79      10.574 -96.210  23.731  1.00 84.90           C  
ANISOU  634  CA  ASN A  79    11306  14072   6881   2924   2501    467       C  
ATOM    635  C   ASN A  79       9.099 -96.473  24.005  1.00107.54           C  
ANISOU  635  C   ASN A  79    13814  17521   9525   2933   2515    200       C  
ATOM    636  O   ASN A  79       8.265 -95.595  23.798  1.00137.67           O  
ANISOU  636  O   ASN A  79    17390  21763  13157   2683   2478    122       O  
ATOM    637  CB  ASN A  79      11.318 -95.941  25.044  1.00 91.25           C  
ANISOU  637  CB  ASN A  79    12374  14417   7881   2569   2531    401       C  
ATOM    638  CG  ASN A  79      10.939 -94.612  25.677  1.00102.97           C  
ANISOU  638  CG  ASN A  79    13808  16054   9260   2046   2502    309       C  
ATOM    639  OD1 ASN A  79      10.007 -93.942  25.235  1.00126.24           O  
ANISOU  639  OD1 ASN A  79    16504  19467  11996   1921   2478    254       O  
ATOM    640  ND2 ASN A  79      11.665 -94.227  26.723  1.00133.43           N  
ANISOU  640  ND2 ASN A  79    17908  19502  13286   1742   2482    288       N  
ATOM    641  N   SER A  80       8.780 -97.676  24.475  1.00150.75           N  
ANISOU  641  N   SER A  80    19239  23005  15034   3213   2580     43       N  
ATOM    642  CA  SER A  80       7.398 -98.015  24.812  1.00156.36           C  
ANISOU  642  CA  SER A  80    19585  24267  15559   3229   2643   -230       C  
ATOM    643  C   SER A  80       6.907 -97.183  26.003  1.00139.78           C  
ANISOU  643  C   SER A  80    17472  22288  13350   2677   2721   -399       C  
ATOM    644  O   SER A  80       5.719 -97.188  26.334  1.00153.33           O  
ANISOU  644  O   SER A  80    18877  24484  14899   2560   2807   -607       O  
ATOM    645  CB  SER A  80       7.250 -99.511  25.084  1.00139.45           C  
ANISOU  645  CB  SER A  80    17416  22073  13497   3678   2720   -377       C  
ATOM    646  OG  SER A  80       8.267 -99.970  25.957  1.00203.83           O  
ANISOU  646  OG  SER A  80    25959  29645  21844   3652   2762   -379       O  
ATOM    647  N   ASN A  81       7.835 -96.472  26.634  1.00 81.87           N  
ANISOU  647  N   ASN A  81    10475  14507   6125   2341   2691   -298       N  
ATOM    648  CA  ASN A  81       7.508 -95.462  27.623  1.00105.38           C  
ANISOU  648  CA  ASN A  81    13496  17539   9004   1803   2714   -383       C  
ATOM    649  C   ASN A  81       6.858 -94.247  26.951  1.00 85.93           C  
ANISOU  649  C   ASN A  81    10796  15434   6420   1529   2652   -338       C  
ATOM    650  O   ASN A  81       6.072 -93.527  27.570  1.00111.59           O  
ANISOU  650  O   ASN A  81    13933  18925   9540   1129   2694   -448       O  
ATOM    651  CB  ASN A  81       8.773 -95.047  28.382  1.00183.19           C  
ANISOU  651  CB  ASN A  81    23766  26788  19050   1577   2649   -278       C  
ATOM    652  CG  ASN A  81       8.474 -94.235  29.629  1.00181.58           C  
ANISOU  652  CG  ASN A  81    23671  26580  18740   1080   2656   -374       C  
ATOM    653  OD1 ASN A  81       7.399 -94.358  30.223  1.00129.33           O  
ANISOU  653  OD1 ASN A  81    16893  20342  11905    945   2768   -545       O  
ATOM    654  ND2 ASN A  81       9.430 -93.404  30.039  1.00144.79           N  
ANISOU  654  ND2 ASN A  81    19285  21489  14242    811   2542   -255       N  
ATOM    655  N   GLY A  82       7.186 -94.029  25.679  1.00 94.82           N  
ANISOU  655  N   GLY A  82    11864  16585   7580   1745   2553   -177       N  
ATOM    656  CA  GLY A  82       6.557 -92.981  24.894  1.00 83.37           C  
ANISOU  656  CA  GLY A  82    10180  15498   6001   1554   2470   -171       C  
ATOM    657  C   GLY A  82       7.425 -91.777  24.558  1.00 96.21           C  
ANISOU  657  C   GLY A  82    12026  16821   7709   1314   2384     -3       C  
ATOM    658  O   GLY A  82       7.011 -90.900  23.795  1.00 83.48           O  
ANISOU  658  O   GLY A  82    10254  15474   5991   1192   2302     -7       O  
ATOM    659  N   SER A  83       8.625 -91.734  25.128  1.00119.64           N  
ANISOU  659  N   SER A  83    15343  19236  10879   1249   2399    119       N  
ATOM    660  CA  SER A  83       9.538 -90.607  24.958  1.00 80.35           C  
ANISOU  660  CA  SER A  83    10569  13929   6032   1015   2343    260       C  
ATOM    661  C   SER A  83      10.177 -90.572  23.569  1.00 89.63           C  
ANISOU  661  C   SER A  83    11776  15068   7210   1318   2323    456       C  
ATOM    662  O   SER A  83      10.678 -91.587  23.084  1.00 83.53           O  
ANISOU  662  O   SER A  83    11083  14158   6495   1715   2360    584       O  
ATOM    663  CB  SER A  83      10.627 -90.660  26.032  1.00 96.46           C  
ANISOU  663  CB  SER A  83    12933  15397   8322    870   2354    312       C  
ATOM    664  OG  SER A  83      10.067 -90.926  27.306  1.00127.32           O  
ANISOU  664  OG  SER A  83    16860  19346  12171    670   2375    143       O  
ATOM    665  N   ILE A  84      10.167 -89.398  22.937  1.00106.75           N  
ANISOU  665  N   ILE A  84    13905  17348   9309   1133   2270    481       N  
ATOM    666  CA  ILE A  84      10.745 -89.226  21.603  1.00 80.79           C  
ANISOU  666  CA  ILE A  84    10673  14066   5958   1392   2266    663       C  
ATOM    667  C   ILE A  84      12.198 -88.765  21.698  1.00 70.93           C  
ANISOU  667  C   ILE A  84     9719  12267   4964   1306   2344    847       C  
ATOM    668  O   ILE A  84      12.515 -87.842  22.447  1.00 94.77           O  
ANISOU  668  O   ILE A  84    12817  15054   8139    939   2332    786       O  
ATOM    669  CB  ILE A  84       9.940 -88.216  20.772  1.00 71.63           C  
ANISOU  669  CB  ILE A  84     9307  13353   4555   1267   2167    556       C  
ATOM    670  CG1 ILE A  84       8.459 -88.600  20.763  1.00103.55           C  
ANISOU  670  CG1 ILE A  84    12998  17944   8400   1290   2087    344       C  
ATOM    671  CG2 ILE A  84      10.489 -88.131  19.358  1.00 81.27           C  
ANISOU  671  CG2 ILE A  84    10612  14633   5634   1579   2164    739       C  
ATOM    672  CD1 ILE A  84       7.541 -87.498  20.277  1.00100.11           C  
ANISOU  672  CD1 ILE A  84    12332  17914   7790   1035   1969    165       C  
ATOM    673  N   SER A  85      13.078 -89.413  20.940  1.00 88.10           N  
ANISOU  673  N   SER A  85    12047  14227   7199   1647   2426   1080       N  
ATOM    674  CA  SER A  85      14.520 -89.247  21.132  1.00 70.48           C  
ANISOU  674  CA  SER A  85    10070  11430   5278   1587   2538   1261       C  
ATOM    675  C   SER A  85      15.261 -88.269  20.217  1.00 95.29           C  
ANISOU  675  C   SER A  85    13302  14500   8405   1547   2625   1409       C  
ATOM    676  O   SER A  85      16.488 -88.174  20.289  1.00135.37           O  
ANISOU  676  O   SER A  85    18554  19119  13761   1513   2753   1572       O  
ATOM    677  CB  SER A  85      15.222 -90.601  21.113  1.00141.02           C  
ANISOU  677  CB  SER A  85    19160  20030  14392   1919   2618   1435       C  
ATOM    678  OG  SER A  85      16.505 -90.475  21.699  1.00 69.35           O  
ANISOU  678  OG  SER A  85    10281  10375   5695   1760   2702   1534       O  
ATOM    679  N   LEU A  86      14.543 -87.565  19.350  1.00 86.32           N  
ANISOU  679  N   LEU A  86    12036  13813   6950   1555   2565   1339       N  
ATOM    680  CA  LEU A  86      15.176 -86.530  18.534  1.00136.74           C  
ANISOU  680  CA  LEU A  86    18509  20165  13281   1497   2655   1425       C  
ATOM    681  C   LEU A  86      15.547 -85.335  19.414  1.00108.11           C  
ANISOU  681  C   LEU A  86    14894  16269   9913   1065   2654   1282       C  
ATOM    682  O   LEU A  86      14.806 -84.982  20.333  1.00114.26           O  
ANISOU  682  O   LEU A  86    15559  17126  10729    790   2520   1068       O  
ATOM    683  CB  LEU A  86      14.275 -86.108  17.370  1.00 99.46           C  
ANISOU  683  CB  LEU A  86    13659  16008   8125   1633   2556   1348       C  
ATOM    684  CG  LEU A  86      12.958 -85.389  17.669  1.00 88.53           C  
ANISOU  684  CG  LEU A  86    12023  15035   6581   1368   2365   1029       C  
ATOM    685  CD1 LEU A  86      13.125 -83.881  17.586  1.00143.21           C  
ANISOU  685  CD1 LEU A  86    18966  21926  13521   1053   2367    892       C  
ATOM    686  CD2 LEU A  86      11.880 -85.855  16.712  1.00127.91           C  
ANISOU  686  CD2 LEU A  86    16817  20552  11230   1634   2199    959       C  
ATOM    687  N   ASP A  87      16.689 -84.712  19.133  1.00 84.22           N  
ANISOU  687  N   ASP A  87    12002  12925   7071   1013   2811   1407       N  
ATOM    688  CA  ASP A  87      17.272 -83.744  20.068  1.00145.12           C  
ANISOU  688  CA  ASP A  87    19733  20275  15132    654   2809   1301       C  
ATOM    689  C   ASP A  87      16.939 -82.258  19.869  1.00 90.30           C  
ANISOU  689  C   ASP A  87    12715  13493   8103    410   2759   1107       C  
ATOM    690  O   ASP A  87      17.493 -81.407  20.565  1.00115.64           O  
ANISOU  690  O   ASP A  87    15942  16377  11621    150   2755   1031       O  
ATOM    691  CB  ASP A  87      18.784 -83.954  20.223  1.00144.27           C  
ANISOU  691  CB  ASP A  87    19767  19630  15417    682   2999   1505       C  
ATOM    692  CG  ASP A  87      19.465 -84.271  18.914  1.00159.86           C  
ANISOU  692  CG  ASP A  87    21852  21631  17257    982   3232   1766       C  
ATOM    693  OD1 ASP A  87      18.862 -84.006  17.851  1.00162.21           O  
ANISOU  693  OD1 ASP A  87    22132  22362  17139   1140   3234   1762       O  
ATOM    694  OD2 ASP A  87      20.606 -84.779  18.949  1.00173.34           O  
ANISOU  694  OD2 ASP A  87    23671  22922  19270   1052   3410   1978       O  
ATOM    695  N   ILE A  88      16.053 -81.934  18.932  1.00 85.66           N  
ANISOU  695  N   ILE A  88    12041  13387   7120    501   2699   1010       N  
ATOM    696  CA  ILE A  88      15.521 -80.571  18.880  1.00107.62           C  
ANISOU  696  CA  ILE A  88    14737  16325   9828    239   2602    763       C  
ATOM    697  C   ILE A  88      14.542 -80.393  20.042  1.00 82.14           C  
ANISOU  697  C   ILE A  88    11391  13132   6686    -71   2398    565       C  
ATOM    698  O   ILE A  88      14.123 -79.280  20.363  1.00 66.67           O  
ANISOU  698  O   ILE A  88     9379  11175   4776   -361   2297    367       O  
ATOM    699  CB  ILE A  88      14.826 -80.243  17.537  1.00 81.89           C  
ANISOU  699  CB  ILE A  88    11419  13579   6117    409   2565    677       C  
ATOM    700  CG1 ILE A  88      13.303 -80.353  17.662  1.00 93.53           C  
ANISOU  700  CG1 ILE A  88    12684  15492   7363    314   2329    461       C  
ATOM    701  CG2 ILE A  88      15.363 -81.137  16.422  1.00 97.94           C  
ANISOU  701  CG2 ILE A  88    13572  15721   7919    828   2716    946       C  
ATOM    702  CD1 ILE A  88      12.555 -79.947  16.420  1.00103.95           C  
ANISOU  702  CD1 ILE A  88    13913  17309   8273    443   2226    319       C  
ATOM    703  N   LEU A  89      14.188 -81.512  20.667  1.00 75.14           N  
ANISOU  703  N   LEU A  89    10478  12260   5812     -2   2354    624       N  
ATOM    704  CA  LEU A  89      13.359 -81.504  21.861  1.00 67.19           C  
ANISOU  704  CA  LEU A  89     9395  11261   4873   -283   2211    479       C  
ATOM    705  C   LEU A  89      14.184 -81.437  23.145  1.00101.41           C  
ANISOU  705  C   LEU A  89    13874  15073   9584   -475   2203    530       C  
ATOM    706  O   LEU A  89      13.619 -81.268  24.229  1.00 76.23           O  
ANISOU  706  O   LEU A  89    10678  11834   6451   -739   2085    428       O  
ATOM    707  CB  LEU A  89      12.466 -82.748  21.903  1.00 67.88           C  
ANISOU  707  CB  LEU A  89     9362  11677   4752   -102   2178    478       C  
ATOM    708  CG  LEU A  89      11.213 -82.751  21.030  1.00 67.58           C  
ANISOU  708  CG  LEU A  89     9094  12222   4363    -20   2093    341       C  
ATOM    709  CD1 LEU A  89      10.477 -84.076  21.166  1.00 81.99           C  
ANISOU  709  CD1 LEU A  89    10780  14317   6055    195   2081    346       C  
ATOM    710  CD2 LEU A  89      10.303 -81.595  21.402  1.00 95.90           C  
ANISOU  710  CD2 LEU A  89    12555  15954   7928   -422   1973    110       C  
ATOM    711  N   ARG A  90      15.506 -81.589  23.043  1.00 82.23           N  
ANISOU  711  N   ARG A  90    11575  12258   7410   -348   2324    690       N  
ATOM    712  CA  ARG A  90      16.324 -81.517  24.251  1.00 95.20           C  
ANISOU  712  CA  ARG A  90    13329  13406   9435   -524   2274    715       C  
ATOM    713  C   ARG A  90      17.436 -80.464  24.233  1.00111.50           C  
ANISOU  713  C   ARG A  90    15439  15095  11830   -637   2326    731       C  
ATOM    714  O   ARG A  90      17.237 -79.339  24.691  1.00108.93           O  
ANISOU  714  O   ARG A  90    15096  14688  11606   -895   2211    594       O  
ATOM    715  CB  ARG A  90      16.957 -82.888  24.507  1.00 77.44           C  
ANISOU  715  CB  ARG A  90    11170  10944   7311   -300   2342    865       C  
ATOM    716  CG  ARG A  90      16.032 -84.062  24.230  1.00117.45           C  
ANISOU  716  CG  ARG A  90    16177  16381  12066    -74   2345    868       C  
ATOM    717  CD  ARG A  90      16.782 -85.257  23.648  1.00105.78           C  
ANISOU  717  CD  ARG A  90    14781  14758  10652    281   2486   1067       C  
ATOM    718  NE  ARG A  90      17.356 -86.125  24.675  1.00 94.07           N  
ANISOU  718  NE  ARG A  90    13414  12889   9439    283   2452   1085       N  
ATOM    719  CZ  ARG A  90      18.600 -86.019  25.130  1.00135.99           C  
ANISOU  719  CZ  ARG A  90    18831  17694  15144    202   2477   1159       C  
ATOM    720  NH1 ARG A  90      19.408 -85.081  24.653  1.00153.30           N  
ANISOU  720  NH1 ARG A  90    21015  19713  17520    117   2570   1233       N  
ATOM    721  NH2 ARG A  90      19.036 -86.855  26.063  1.00108.47           N  
ANISOU  721  NH2 ARG A  90    15449  13885  11881    207   2410   1137       N  
ATOM    722  N   SER A  91      18.592 -80.817  23.676  1.00 90.25           N  
ANISOU  722  N   SER A  91    12795  12174   9320   -441   2512    899       N  
ATOM    723  CA  SER A  91      19.754 -79.928  23.746  1.00 84.66           C  
ANISOU  723  CA  SER A  91    12093  11082   8991   -541   2593    913       C  
ATOM    724  C   SER A  91      19.856 -78.901  22.627  1.00 78.14           C  
ANISOU  724  C   SER A  91    11218  10437   8035   -502   2745    869       C  
ATOM    725  O   SER A  91      20.464 -77.842  22.792  1.00 87.93           O  
ANISOU  725  O   SER A  91    12423  11439   9548   -641   2767    785       O  
ATOM    726  CB  SER A  91      21.050 -80.746  23.838  1.00 94.98           C  
ANISOU  726  CB  SER A  91    13456  11991  10641   -409   2738   1103       C  
ATOM    727  OG  SER A  91      21.075 -81.783  22.874  1.00100.90           O  
ANISOU  727  OG  SER A  91    14256  12919  11163   -110   2918   1289       O  
ATOM    728  N   GLN A  92      19.245 -79.217  21.493  1.00 87.54           N  
ANISOU  728  N   GLN A  92    12405  12057   8798   -294   2834    907       N  
ATOM    729  CA  GLN A  92      19.389 -78.407  20.287  1.00 84.69           C  
ANISOU  729  CA  GLN A  92    12037  11907   8235   -198   2998    876       C  
ATOM    730  C   GLN A  92      18.250 -77.411  20.088  1.00 98.89           C  
ANISOU  730  C   GLN A  92    13760  14045   9770   -352   2829    611       C  
ATOM    731  O   GLN A  92      18.145 -76.774  19.038  1.00109.27           O  
ANISOU  731  O   GLN A  92    15075  15614  10830   -261   2921    533       O  
ATOM    732  CB  GLN A  92      19.628 -79.285  19.051  1.00 95.37           C  
ANISOU  732  CB  GLN A  92    13469  13483   9285    149   3207   1104       C  
ATOM    733  CG  GLN A  92      20.988 -79.993  19.088  1.00 88.11           C  
ANISOU  733  CG  GLN A  92    12633  12146   8697    268   3441   1373       C  
ATOM    734  CD  GLN A  92      21.362 -80.660  17.775  1.00129.20           C  
ANISOU  734  CD  GLN A  92    17959  17519  13613    599   3691   1637       C  
ATOM    735  OE1 GLN A  92      21.214 -80.078  16.698  1.00129.44           O  
ANISOU  735  OE1 GLN A  92    18025  17860  13295    712   3803   1620       O  
ATOM    736  NE2 GLN A  92      21.864 -81.888  17.859  1.00144.36           N  
ANISOU  736  NE2 GLN A  92    19963  19218  15668    762   3773   1884       N  
ATOM    737  N   TRP A  93      17.394 -77.286  21.093  1.00 60.89           N  
ANISOU  737  N   TRP A  93     8895   9233   5009   -591   2587    470       N  
ATOM    738  CA  TRP A  93      16.226 -76.431  20.965  1.00 61.25           C  
ANISOU  738  CA  TRP A  93     8860   9578   4835   -772   2421    226       C  
ATOM    739  C   TRP A  93      16.583 -74.948  21.010  1.00 75.81           C  
ANISOU  739  C   TRP A  93    10705  11205   6893   -957   2413     46       C  
ATOM    740  O   TRP A  93      17.124 -74.454  21.997  1.00 93.71           O  
ANISOU  740  O   TRP A  93    12999  13053   9555  -1139   2348     32       O  
ATOM    741  CB  TRP A  93      15.240 -76.751  22.084  1.00105.55           C  
ANISOU  741  CB  TRP A  93    14426  15221  10457   -998   2205    162       C  
ATOM    742  CG  TRP A  93      14.161 -75.738  22.244  1.00 80.85           C  
ANISOU  742  CG  TRP A  93    11221  12258   7239  -1279   2034    -77       C  
ATOM    743  CD1 TRP A  93      14.153 -74.672  23.096  1.00 96.07           C  
ANISOU  743  CD1 TRP A  93    13189  13875   9440  -1580   1908   -194       C  
ATOM    744  CD2 TRP A  93      12.921 -75.694  21.535  1.00 80.84           C  
ANISOU  744  CD2 TRP A  93    11087  12750   6877  -1291   1954   -230       C  
ATOM    745  NE1 TRP A  93      12.986 -73.965  22.959  1.00 95.78           N  
ANISOU  745  NE1 TRP A  93    13069  14083   9241  -1795   1774   -400       N  
ATOM    746  CE2 TRP A  93      12.210 -74.575  22.007  1.00 77.28           C  
ANISOU  746  CE2 TRP A  93    10601  12244   6516  -1634   1799   -440       C  
ATOM    747  CE3 TRP A  93      12.341 -76.494  20.548  1.00 89.03           C  
ANISOU  747  CE3 TRP A  93    12022  14261   7543  -1039   1979   -213       C  
ATOM    748  CZ2 TRP A  93      10.949 -74.234  21.524  1.00 97.14           C  
ANISOU  748  CZ2 TRP A  93    12968  15158   8783  -1763   1682   -646       C  
ATOM    749  CZ3 TRP A  93      11.093 -76.156  20.069  1.00 93.50           C  
ANISOU  749  CZ3 TRP A  93    12424  15249   7853  -1145   1841   -427       C  
ATOM    750  CH2 TRP A  93      10.409 -75.035  20.556  1.00 95.16           C  
ANISOU  750  CH2 TRP A  93    12586  15391   8179  -1519   1701   -647       C  
ATOM    751  N   SER A  94      16.277 -74.251  19.920  1.00 75.68           N  
ANISOU  751  N   SER A  94    10665  11480   6609   -887   2463   -105       N  
ATOM    752  CA  SER A  94      16.313 -72.792  19.879  1.00 66.49           C  
ANISOU  752  CA  SER A  94     9492  10185   5587  -1061   2425   -350       C  
ATOM    753  C   SER A  94      14.934 -72.212  20.193  1.00106.40           C  
ANISOU  753  C   SER A  94    14477  15429  10522  -1329   2164   -588       C  
ATOM    754  O   SER A  94      13.914 -72.832  19.894  1.00 94.92           O  
ANISOU  754  O   SER A  94    12948  14372   8745  -1310   2070   -607       O  
ATOM    755  CB  SER A  94      16.794 -72.304  18.509  1.00117.89           C  
ANISOU  755  CB  SER A  94    16037  16893  11862   -836   2640   -415       C  
ATOM    756  OG  SER A  94      16.468 -70.935  18.314  1.00119.59           O  
ANISOU  756  OG  SER A  94    16234  17102  12103   -990   2562   -727       O  
ATOM    757  N   PRO A  95      14.897 -71.014  20.794  1.00 88.15           N  
ANISOU  757  N   PRO A  95    12176  12818   8496  -1582   2048   -772       N  
ATOM    758  CA  PRO A  95      13.640 -70.302  21.052  1.00 77.85           C  
ANISOU  758  CA  PRO A  95    10821  11630   7127  -1872   1820  -1004       C  
ATOM    759  C   PRO A  95      12.949 -69.857  19.764  1.00 92.16           C  
ANISOU  759  C   PRO A  95    12569  13882   8567  -1798   1811  -1248       C  
ATOM    760  O   PRO A  95      11.779 -69.474  19.790  1.00 89.04           O  
ANISOU  760  O   PRO A  95    12093  13676   8063  -2022   1624  -1445       O  
ATOM    761  CB  PRO A  95      14.093 -69.078  21.852  1.00 82.10           C  
ANISOU  761  CB  PRO A  95    11425  11663   8104  -2081   1734  -1116       C  
ATOM    762  CG  PRO A  95      15.383 -69.484  22.463  1.00 83.65           C  
ANISOU  762  CG  PRO A  95    11676  11482   8626  -1959   1846   -891       C  
ATOM    763  CD  PRO A  95      16.041 -70.350  21.437  1.00105.67           C  
ANISOU  763  CD  PRO A  95    14448  14520  11180  -1626   2104   -747       C  
ATOM    764  N   ALA A  96      13.676 -69.890  18.655  1.00 88.57           N  
ANISOU  764  N   ALA A  96    12155  13580   7917  -1497   2010  -1239       N  
ATOM    765  CA  ALA A  96      13.139 -69.446  17.377  1.00 75.01           C  
ANISOU  765  CA  ALA A  96    10413  12284   5804  -1388   1993  -1481       C  
ATOM    766  C   ALA A  96      12.389 -70.564  16.652  1.00101.06           C  
ANISOU  766  C   ALA A  96    13632  16116   8651  -1202   1940  -1393       C  
ATOM    767  O   ALA A  96      11.787 -70.339  15.604  1.00123.92           O  
ANISOU  767  O   ALA A  96    16487  19424  11171  -1106   1862  -1594       O  
ATOM    768  CB  ALA A  96      14.256 -68.909  16.502  1.00 97.58           C  
ANISOU  768  CB  ALA A  96    13380  15081   8615  -1143   2247  -1517       C  
ATOM    769  N   LEU A  97      12.436 -71.767  17.215  1.00 94.72           N  
ANISOU  769  N   LEU A  97    12802  15300   7889  -1136   1965  -1110       N  
ATOM    770  CA  LEU A  97      11.773 -72.920  16.615  1.00100.12           C  
ANISOU  770  CA  LEU A  97    13393  16450   8198   -925   1914  -1007       C  
ATOM    771  C   LEU A  97      10.275 -72.940  16.898  1.00104.64           C  
ANISOU  771  C   LEU A  97    13760  17317   8680  -1170   1661  -1203       C  
ATOM    772  O   LEU A  97       9.809 -72.398  17.900  1.00106.23           O  
ANISOU  772  O   LEU A  97    13919  17283   9160  -1527   1555  -1303       O  
ATOM    773  CB  LEU A  97      12.409 -74.223  17.102  1.00101.20           C  
ANISOU  773  CB  LEU A  97    13580  16435   8437   -741   2048   -654       C  
ATOM    774  CG  LEU A  97      13.898 -74.406  16.802  1.00 99.61           C  
ANISOU  774  CG  LEU A  97    13553  15947   8349   -501   2322   -419       C  
ATOM    775  CD1 LEU A  97      14.365 -75.798  17.221  1.00 83.53           C  
ANISOU  775  CD1 LEU A  97    11552  13785   6400   -324   2415    -97       C  
ATOM    776  CD2 LEU A  97      14.180 -74.153  15.329  1.00104.32           C  
ANISOU  776  CD2 LEU A  97    14231  16849   8555   -220   2444   -450       C  
ATOM    777  N   THR A  98       9.528 -73.587  16.011  1.00102.11           N  
ANISOU  777  N   THR A  98    13309  17512   7977   -973   1565  -1245       N  
ATOM    778  CA  THR A  98       8.081 -73.660  16.133  1.00118.56           C  
ANISOU  778  CA  THR A  98    15137  19938   9971  -1187   1337  -1448       C  
ATOM    779  C   THR A  98       7.662 -75.089  16.459  1.00108.16           C  
ANISOU  779  C   THR A  98    13682  18828   8587  -1042   1341  -1242       C  
ATOM    780  O   THR A  98       8.366 -76.038  16.120  1.00 97.81           O  
ANISOU  780  O   THR A  98    12469  17529   7164   -684   1469   -985       O  
ATOM    781  CB  THR A  98       7.384 -73.211  14.828  1.00112.24           C  
ANISOU  781  CB  THR A  98    14229  19620   8798  -1087   1163  -1737       C  
ATOM    782  OG1 THR A  98       6.852 -74.350  14.144  1.00143.55           O  
ANISOU  782  OG1 THR A  98    18038  24069  12438   -786   1078  -1652       O  
ATOM    783  CG2 THR A  98       8.366 -72.498  13.915  1.00139.75           C  
ANISOU  783  CG2 THR A  98    17947  23027  12123   -872   1282  -1781       C  
ATOM    784  N   ILE A  99       6.523 -75.236  17.127  1.00105.06           N  
ANISOU  784  N   ILE A  99    13062  18578   8276  -1323   1218  -1356       N  
ATOM    785  CA  ILE A  99       5.975 -76.555  17.434  1.00104.07           C  
ANISOU  785  CA  ILE A  99    12761  18698   8083  -1193   1226  -1220       C  
ATOM    786  C   ILE A  99       5.637 -77.317  16.145  1.00104.27           C  
ANISOU  786  C   ILE A  99    12640  19246   7731   -782   1132  -1233       C  
ATOM    787  O   ILE A  99       5.593 -78.548  16.129  1.00102.23           O  
ANISOU  787  O   ILE A  99    12309  19144   7391   -499   1172  -1056       O  
ATOM    788  CB  ILE A  99       4.740 -76.446  18.371  1.00 89.31           C  
ANISOU  788  CB  ILE A  99    10653  16915   6365  -1614   1145  -1367       C  
ATOM    789  CG1 ILE A  99       4.825 -77.459  19.517  1.00118.64           C  
ANISOU  789  CG1 ILE A  99    14390  20466  10222  -1624   1283  -1145       C  
ATOM    790  CG2 ILE A  99       3.438 -76.591  17.594  1.00114.40           C  
ANISOU  790  CG2 ILE A  99    13468  20672   9325  -1619    961  -1612       C  
ATOM    791  CD1 ILE A  99       4.492 -78.878  19.118  1.00111.39           C  
ANISOU  791  CD1 ILE A  99    13286  19930   9106  -1257   1303  -1054       C  
ATOM    792  N   SER A 100       5.417 -76.577  15.059  1.00105.15           N  
ANISOU  792  N   SER A 100    12726  19617   7609   -728    990  -1449       N  
ATOM    793  CA  SER A 100       5.174 -77.189  13.758  1.00101.36           C  
ANISOU  793  CA  SER A 100    12157  19557   6799   -309    851  -1441       C  
ATOM    794  C   SER A 100       6.441 -77.892  13.270  1.00105.50           C  
ANISOU  794  C   SER A 100    12981  19807   7299    131   1019  -1079       C  
ATOM    795  O   SER A 100       6.387 -79.032  12.798  1.00149.95           O  
ANISOU  795  O   SER A 100    18560  25608  12804    493    986   -896       O  
ATOM    796  CB  SER A 100       4.706 -76.139  12.742  1.00119.18           C  
ANISOU  796  CB  SER A 100    14362  22077   8843   -368    641  -1768       C  
ATOM    797  OG  SER A 100       4.303 -76.741  11.524  1.00132.80           O  
ANISOU  797  OG  SER A 100    15971  24215  10272     16    447  -1775       O  
ATOM    798  N   LYS A 101       7.578 -77.210  13.402  1.00116.14           N  
ANISOU  798  N   LYS A 101    14626  20734   8767     83   1209   -985       N  
ATOM    799  CA  LYS A 101       8.871 -77.788  13.045  1.00110.60           C  
ANISOU  799  CA  LYS A 101    14211  19726   8085    418   1419   -643       C  
ATOM    800  C   LYS A 101       9.108 -79.092  13.795  1.00 89.97           C  
ANISOU  800  C   LYS A 101    11588  16951   5646    544   1523   -371       C  
ATOM    801  O   LYS A 101       9.560 -80.075  13.210  1.00111.57           O  
ANISOU  801  O   LYS A 101    14421  19678   8291    909   1572   -123       O  
ATOM    802  CB  LYS A 101      10.014 -76.809  13.331  1.00108.14           C  
ANISOU  802  CB  LYS A 101    14148  19003   7936    273   1642   -621       C  
ATOM    803  CG  LYS A 101      10.144 -75.667  12.329  1.00161.65           C  
ANISOU  803  CG  LYS A 101    21028  25887  14503    289   1612   -833       C  
ATOM    804  CD  LYS A 101      11.571 -75.122  12.312  1.00166.29           C  
ANISOU  804  CD  LYS A 101    21886  26088  15208    331   1916   -697       C  
ATOM    805  CE  LYS A 101      11.705 -73.910  11.403  1.00182.92           C  
ANISOU  805  CE  LYS A 101    24099  28293  17109    333   1919   -950       C  
ATOM    806  NZ  LYS A 101      11.241 -74.192  10.018  1.00168.35           N  
ANISOU  806  NZ  LYS A 101    22283  26803  14878    617   1749   -972       N  
ATOM    807  N   VAL A 102       8.793 -79.090  15.086  1.00 81.17           N  
ANISOU  807  N   VAL A 102    10369  15704   4767    233   1552   -426       N  
ATOM    808  CA  VAL A 102       8.890 -80.286  15.915  1.00 86.47           C  
ANISOU  808  CA  VAL A 102    11019  16241   5595    319   1635   -230       C  
ATOM    809  C   VAL A 102       7.990 -81.384  15.364  1.00 91.43           C  
ANISOU  809  C   VAL A 102    11419  17299   6021    606   1491   -229       C  
ATOM    810  O   VAL A 102       8.403 -82.542  15.222  1.00 78.65           O  
ANISOU  810  O   VAL A 102     9869  15618   4395    943   1560      3       O  
ATOM    811  CB  VAL A 102       8.461 -79.997  17.367  1.00 72.82           C  
ANISOU  811  CB  VAL A 102     9202  14373   4094   -106   1653   -340       C  
ATOM    812  CG1 VAL A 102       8.613 -81.242  18.225  1.00 91.78           C  
ANISOU  812  CG1 VAL A 102    11614  16626   6634      3   1747   -157       C  
ATOM    813  CG2 VAL A 102       9.265 -78.847  17.945  1.00 73.90           C  
ANISOU  813  CG2 VAL A 102     9537  14057   4484   -397   1737   -362       C  
ATOM    814  N   LEU A 103       6.754 -81.003  15.051  1.00 82.73           N  
ANISOU  814  N   LEU A 103    10026  16654   4754    472   1289   -504       N  
ATOM    815  CA  LEU A 103       5.767 -81.951  14.552  1.00 83.10           C  
ANISOU  815  CA  LEU A 103     9774  17202   4597    725   1132   -561       C  
ATOM    816  C   LEU A 103       6.236 -82.666  13.290  1.00 93.32           C  
ANISOU  816  C   LEU A 103    11189  18613   5655   1248   1077   -360       C  
ATOM    817  O   LEU A 103       6.279 -83.895  13.257  1.00113.18           O  
ANISOU  817  O   LEU A 103    13672  21195   8138   1585   1103   -180       O  
ATOM    818  CB  LEU A 103       4.425 -81.262  14.318  1.00 96.70           C  
ANISOU  818  CB  LEU A 103    11146  19422   6175    462    915   -925       C  
ATOM    819  CG  LEU A 103       3.280 -81.802  15.174  1.00101.11           C  
ANISOU  819  CG  LEU A 103    11338  20265   6816    256    904  -1070       C  
ATOM    820  CD1 LEU A 103       3.736 -81.985  16.616  1.00 82.33           C  
ANISOU  820  CD1 LEU A 103     9118  17412   4751      9   1136   -925       C  
ATOM    821  CD2 LEU A 103       2.081 -80.873  15.102  1.00131.15           C  
ANISOU  821  CD2 LEU A 103    14825  24375  10629   -143    719  -1428       C  
ATOM    822  N   LEU A 104       6.598 -81.914  12.255  1.00108.51           N  
ANISOU  822  N   LEU A 104    13270  20555   7403   1329   1008   -385       N  
ATOM    823  CA  LEU A 104       7.072 -82.569  11.035  1.00 98.95           C  
ANISOU  823  CA  LEU A 104    12217  19435   5945   1812    965   -162       C  
ATOM    824  C   LEU A 104       8.477 -83.149  11.192  1.00 88.51           C  
ANISOU  824  C   LEU A 104    11251  17600   4779   1995   1236    214       C  
ATOM    825  O   LEU A 104       8.935 -83.916  10.347  1.00136.43           O  
ANISOU  825  O   LEU A 104    17467  23687  10681   2400   1242    464       O  
ATOM    826  CB  LEU A 104       6.957 -81.677   9.789  1.00116.95           C  
ANISOU  826  CB  LEU A 104    14560  21938   7936   1869    801   -310       C  
ATOM    827  CG  LEU A 104       7.180 -80.170   9.867  1.00130.57           C  
ANISOU  827  CG  LEU A 104    16401  23489   9722   1500    846   -533       C  
ATOM    828  CD1 LEU A 104       8.211 -79.737   8.839  1.00138.62           C  
ANISOU  828  CD1 LEU A 104    17777  24323  10570   1695    955   -386       C  
ATOM    829  CD2 LEU A 104       5.859 -79.459   9.630  1.00118.18           C  
ANISOU  829  CD2 LEU A 104    14505  22385   8014   1285    556   -946       C  
ATOM    830  N   SER A 105       9.152 -82.796  12.280  1.00 88.78           N  
ANISOU  830  N   SER A 105    11414  17185   5134   1696   1449    254       N  
ATOM    831  CA  SER A 105      10.418 -83.434  12.603  1.00 96.45           C  
ANISOU  831  CA  SER A 105    12658  17685   6303   1833   1699    580       C  
ATOM    832  C   SER A 105      10.134 -84.869  13.033  1.00 93.68           C  
ANISOU  832  C   SER A 105    12203  17397   5992   2088   1692    719       C  
ATOM    833  O   SER A 105      10.845 -85.798  12.645  1.00101.42           O  
ANISOU  833  O   SER A 105    13364  18217   6955   2435   1792   1013       O  
ATOM    834  CB  SER A 105      11.151 -82.672  13.708  1.00 82.01           C  
ANISOU  834  CB  SER A 105    10952  15407   4801   1455   1892    554       C  
ATOM    835  OG  SER A 105      12.528 -83.001  13.728  1.00172.01           O  
ANISOU  835  OG  SER A 105    22620  26369  16367   1574   2135    845       O  
ATOM    836  N   ILE A 106       9.076 -85.042  13.824  1.00 92.24           N  
ANISOU  836  N   ILE A 106    11731  17460   5857   1918   1590    503       N  
ATOM    837  CA  ILE A 106       8.633 -86.372  14.250  1.00 84.28           C  
ANISOU  837  CA  ILE A 106    10576  16594   4854   2166   1587    566       C  
ATOM    838  C   ILE A 106       8.017 -87.159  13.088  1.00 87.60           C  
ANISOU  838  C   ILE A 106    10849  17497   4940   2645   1399    610       C  
ATOM    839  O   ILE A 106       8.331 -88.341  12.886  1.00115.86           O  
ANISOU  839  O   ILE A 106    14513  21043   8467   3067   1448    840       O  
ATOM    840  CB  ILE A 106       7.610 -86.279  15.405  1.00 86.52           C  
ANISOU  840  CB  ILE A 106    10567  17045   5262   1822   1557    300       C  
ATOM    841  CG1 ILE A 106       8.200 -85.504  16.584  1.00 77.91           C  
ANISOU  841  CG1 ILE A 106     9645  15485   4471   1374   1707    275       C  
ATOM    842  CG2 ILE A 106       7.178 -87.662  15.857  1.00 82.93           C  
ANISOU  842  CG2 ILE A 106     9957  16744   4808   2095   1592    336       C  
ATOM    843  CD1 ILE A 106       7.175 -85.109  17.622  1.00 76.95           C  
ANISOU  843  CD1 ILE A 106     9282  15514   4442    960   1668     20       C  
ATOM    844  N   CYS A 107       7.141 -86.499  12.332  1.00 89.95           N  
ANISOU  844  N   CYS A 107    10931  18246   5001   2597   1170    383       N  
ATOM    845  CA  CYS A 107       6.527 -87.099  11.147  1.00 96.77           C  
ANISOU  845  CA  CYS A 107    11643  19612   5514   3050    932    395       C  
ATOM    846  C   CYS A 107       7.609 -87.586  10.185  1.00111.15           C  
ANISOU  846  C   CYS A 107    13840  21184   7209   3469    997    767       C  
ATOM    847  O   CYS A 107       7.464 -88.636   9.556  1.00113.02           O  
ANISOU  847  O   CYS A 107    14061  21635   7245   3963    892    939       O  
ATOM    848  CB  CYS A 107       5.603 -86.108  10.429  1.00116.97           C  
ANISOU  848  CB  CYS A 107    13966  22625   7853   2885    666     79       C  
ATOM    849  SG  CYS A 107       4.091 -85.611  11.312  1.00167.52           S  
ANISOU  849  SG  CYS A 107    19851  29465  14336   2423    547   -375       S  
ATOM    850  N   SER A 108       8.687 -86.812  10.074  1.00101.10           N  
ANISOU  850  N   SER A 108    12897  19463   6052   3272   1177    893       N  
ATOM    851  CA  SER A 108       9.838 -87.214   9.272  1.00116.46           C  
ANISOU  851  CA  SER A 108    15216  21107   7927   3585   1314   1263       C  
ATOM    852  C   SER A 108      10.565 -88.384   9.925  1.00 95.07           C  
ANISOU  852  C   SER A 108    12663  18023   5434   3790   1526   1562       C  
ATOM    853  O   SER A 108      11.037 -89.296   9.244  1.00109.53           O  
ANISOU  853  O   SER A 108    14690  19784   7143   4227   1554   1878       O  
ATOM    854  CB  SER A 108      10.804 -86.042   9.086  1.00131.18           C  
ANISOU  854  CB  SER A 108    17345  22617   9882   3283   1492   1280       C  
ATOM    855  OG  SER A 108      12.018 -86.464   8.491  1.00129.06           O  
ANISOU  855  OG  SER A 108    17422  22007   9608   3521   1696   1651       O  
ATOM    856  N   LEU A 109      10.650 -88.354  11.252  1.00105.04           N  
ANISOU  856  N   LEU A 109    13862  19033   7017   3478   1669   1461       N  
ATOM    857  CA  LEU A 109      11.306 -89.420  12.001  1.00105.82           C  
ANISOU  857  CA  LEU A 109    14106  18764   7337   3639   1868   1691       C  
ATOM    858  C   LEU A 109      10.605 -90.765  11.804  1.00107.22           C  
ANISOU  858  C   LEU A 109    14143  19261   7334   4128   1747   1757       C  
ATOM    859  O   LEU A 109      11.220 -91.821  11.968  1.00103.50           O  
ANISOU  859  O   LEU A 109    13846  18428   7053   4393   1857   1999       O  
ATOM    860  CB  LEU A 109      11.377 -89.065  13.488  1.00 85.54           C  
ANISOU  860  CB  LEU A 109    11471  15924   5107   3197   1997   1513       C  
ATOM    861  CG  LEU A 109      12.184 -90.011  14.378  1.00 84.09           C  
ANISOU  861  CG  LEU A 109    11463  15247   5241   3271   2195   1699       C  
ATOM    862  CD1 LEU A 109      13.608 -90.140  13.859  1.00 92.02           C  
ANISOU  862  CD1 LEU A 109    12836  15799   6327   3423   2413   2067       C  
ATOM    863  CD2 LEU A 109      12.174 -89.532  15.818  1.00 97.76           C  
ANISOU  863  CD2 LEU A 109    13123  16725   7296   2798   2254   1482       C  
ATOM    864  N   LEU A 110       9.324 -90.733  11.449  1.00109.72           N  
ANISOU  864  N   LEU A 110    14107  20155   7426   4203   1480   1500       N  
ATOM    865  CA  LEU A 110       8.614 -91.981  11.169  1.00 98.58           C  
ANISOU  865  CA  LEU A 110    12490  18996   5969   4655   1306   1512       C  
ATOM    866  C   LEU A 110       9.051 -92.670   9.874  1.00105.98           C  
ANISOU  866  C   LEU A 110    13671  19971   6626   5230   1216   1865       C  
ATOM    867  O   LEU A 110       9.396 -93.851   9.888  1.00127.29           O  
ANISOU  867  O   LEU A 110    16488  22408   9467   5602   1259   2090       O  
ATOM    868  CB  LEU A 110       7.098 -91.774  11.183  1.00104.18           C  
ANISOU  868  CB  LEU A 110    12695  20323   6565   4562   1047   1122       C  
ATOM    869  CG  LEU A 110       6.467 -91.591  12.565  1.00 96.95           C  
ANISOU  869  CG  LEU A 110    11500  19384   5955   4108   1142    813       C  
ATOM    870  CD1 LEU A 110       4.993 -91.933  12.516  1.00 99.92           C  
ANISOU  870  CD1 LEU A 110    11349  20343   6272   4180    924    503       C  
ATOM    871  CD2 LEU A 110       7.182 -92.434  13.611  1.00110.44           C  
ANISOU  871  CD2 LEU A 110    13398  20555   8008   4120   1382    948       C  
ATOM    872  N   CYS A 111       9.035 -91.941   8.757  1.00139.87           N  
ANISOU  872  N   CYS A 111    18057  24564  10522   5305   1084   1909       N  
ATOM    873  CA  CYS A 111       9.405 -92.519   7.464  1.00126.89           C  
ANISOU  873  CA  CYS A 111    16655  22933   8626   5814    972   2238       C  
ATOM    874  C   CYS A 111      10.881 -92.879   7.438  1.00141.07           C  
ANISOU  874  C   CYS A 111    18926  24060  10614   5880   1292   2665       C  
ATOM    875  O   CYS A 111      11.290 -93.842   6.789  1.00145.44           O  
ANISOU  875  O   CYS A 111    19712  24471  11078   6354   1283   3017       O  
ATOM    876  CB  CYS A 111       9.121 -91.547   6.317  1.00123.11           C  
ANISOU  876  CB  CYS A 111    16156  22747   7872   5734    765   2111       C  
ATOM    877  SG  CYS A 111       7.512 -90.741   6.351  1.00175.93           S  
ANISOU  877  SG  CYS A 111    22298  30143  14405   5484    418   1561       S  
ATOM    878  N   ASP A 112      11.681 -92.087   8.143  1.00135.97           N  
ANISOU  878  N   ASP A 112    18412  22991  10260   5394   1565   2629       N  
ATOM    879  CA  ASP A 112      13.127 -92.253   8.121  1.00146.33           C  
ANISOU  879  CA  ASP A 112    20127  23679  11792   5375   1882   2992       C  
ATOM    880  C   ASP A 112      13.705 -92.242   9.529  1.00131.03           C  
ANISOU  880  C   ASP A 112    18219  21296  10272   5035   2143   2952       C  
ATOM    881  O   ASP A 112      14.087 -91.189  10.039  1.00121.24           O  
ANISOU  881  O   ASP A 112    16962  19874   9231   4557   2262   2784       O  
ATOM    882  CB  ASP A 112      13.771 -91.151   7.284  1.00174.31           C  
ANISOU  882  CB  ASP A 112    23847  27135  15249   5143   1960   3019       C  
ATOM    883  CG  ASP A 112      15.197 -91.473   6.899  1.00206.91           C  
ANISOU  883  CG  ASP A 112    28372  30721  19522   5228   2264   3435       C  
ATOM    884  OD1 ASP A 112      16.109 -91.200   7.708  1.00194.71           O  
ANISOU  884  OD1 ASP A 112    26927  28712  18343   4911   2543   3482       O  
ATOM    885  OD2 ASP A 112      15.403 -92.000   5.786  1.00228.49           O  
ANISOU  885  OD2 ASP A 112    31308  33493  22014   5603   2219   3713       O  
ATOM    886  N   PRO A 113      13.772 -93.421  10.163  1.00124.56           N  
ANISOU  886  N   PRO A 113    17427  20247   9655   5267   2196   3069       N  
ATOM    887  CA  PRO A 113      14.297 -93.565  11.526  1.00 96.54           C  
ANISOU  887  CA  PRO A 113    13876  16193   6614   4930   2379   2969       C  
ATOM    888  C   PRO A 113      15.793 -93.284  11.614  1.00 96.35           C  
ANISOU  888  C   PRO A 113    14197  15575   6838   4752   2698   3258       C  
ATOM    889  O   PRO A 113      16.418 -92.913  10.620  1.00129.48           O  
ANISOU  889  O   PRO A 113    18623  19751  10822   4851   2810   3524       O  
ATOM    890  CB  PRO A 113      14.008 -95.031  11.861  1.00102.21           C  
ANISOU  890  CB  PRO A 113    14539  16764   7531   5288   2297   3001       C  
ATOM    891  CG  PRO A 113      13.892 -95.702  10.553  1.00127.28           C  
ANISOU  891  CG  PRO A 113    17842  20134  10384   5840   2170   3295       C  
ATOM    892  CD  PRO A 113      13.286 -94.703   9.626  1.00156.02           C  
ANISOU  892  CD  PRO A 113    21380  24362  13539   5817   2008   3207       C  
ATOM    893  N   ASN A 114      16.358 -93.474  12.801  1.00113.63           N  
ANISOU  893  N   ASN A 114    16400  17277   9497   4479   2831   3182       N  
ATOM    894  CA  ASN A 114      17.716 -93.023  13.075  1.00106.94           C  
ANISOU  894  CA  ASN A 114    15784  15888   8959   4209   3115   3365       C  
ATOM    895  C   ASN A 114      18.524 -93.994  13.940  1.00131.95           C  
ANISOU  895  C   ASN A 114    19079  18418  12639   4201   3233   3462       C  
ATOM    896  O   ASN A 114      18.738 -93.741  15.125  1.00156.27           O  
ANISOU  896  O   ASN A 114    22072  21239  16063   3848   3250   3238       O  
ATOM    897  CB  ASN A 114      17.649 -91.658  13.756  1.00108.35           C  
ANISOU  897  CB  ASN A 114    15809  16152   9208   3705   3132   3069       C  
ATOM    898  CG  ASN A 114      18.887 -90.831  13.525  1.00154.15           C  
ANISOU  898  CG  ASN A 114    21802  21620  15149   3488   3410   3255       C  
ATOM    899  OD1 ASN A 114      19.986 -91.367  13.378  1.00161.66           O  
ANISOU  899  OD1 ASN A 114    22978  22095  16350   3574   3632   3565       O  
ATOM    900  ND2 ASN A 114      18.718 -89.514  13.485  1.00163.32           N  
ANISOU  900  ND2 ASN A 114    22833  22985  16237   3167   3367   3019       N  
ATOM    901  N   PRO A 115      18.984 -95.108  13.353  1.00119.69           N  
ANISOU  901  N   PRO A 115    17747  16591  11139   4593   3297   3793       N  
ATOM    902  CA  PRO A 115      19.740 -96.142  14.071  1.00116.98           C  
ANISOU  902  CA  PRO A 115    17543  15613  11290   4628   3390   3883       C  
ATOM    903  C   PRO A 115      21.143 -95.703  14.476  1.00145.43           C  
ANISOU  903  C   PRO A 115    21309  18632  15314   4278   3662   4027       C  
ATOM    904  O   PRO A 115      21.966 -96.547  14.826  1.00129.32           O  
ANISOU  904  O   PRO A 115    19433  16013  13691   4322   3770   4176       O  
ATOM    905  CB  PRO A 115      19.806 -97.306  13.089  1.00108.52           C  
ANISOU  905  CB  PRO A 115    16682  14448  10101   5167   3379   4239       C  
ATOM    906  CG  PRO A 115      18.884 -96.943  11.967  1.00136.80           C  
ANISOU  906  CG  PRO A 115    20185  18699  13095   5436   3215   4277       C  
ATOM    907  CD  PRO A 115      18.837 -95.458  11.930  1.00122.90           C  
ANISOU  907  CD  PRO A 115    18314  17250  11132   5041   3269   4117       C  
ATOM    908  N   ASP A 116      21.426 -94.414  14.351  1.00180.13           N  
ANISOU  908  N   ASP A 116    25655  23170  19615   3958   3774   3986       N  
ATOM    909  CA  ASP A 116      22.710 -93.856  14.740  1.00234.08           C  
ANISOU  909  CA  ASP A 116    32573  29507  26861   3608   4030   4081       C  
ATOM    910  C   ASP A 116      22.759 -93.719  16.254  1.00217.07           C  
ANISOU  910  C   ASP A 116    30252  27100  25125   3251   3914   3726       C  
ATOM    911  O   ASP A 116      23.599 -94.323  16.923  1.00198.11           O  
ANISOU  911  O   ASP A 116    27933  24134  23206   3161   3983   3767       O  
ATOM    912  CB  ASP A 116      22.914 -92.491  14.078  1.00266.51           C  
ANISOU  912  CB  ASP A 116    36662  33897  30703   3423   4181   4116       C  
ATOM    913  CG  ASP A 116      24.291 -91.916  14.337  1.00270.80           C  
ANISOU  913  CG  ASP A 116    37266  33946  31678   3101   4486   4239       C  
ATOM    914  OD1 ASP A 116      25.272 -92.687  14.316  1.00282.61           O  
ANISOU  914  OD1 ASP A 116    38930  34908  33540   3154   4679   4517       O  
ATOM    915  OD2 ASP A 116      24.395 -90.690  14.561  1.00237.75           O  
ANISOU  915  OD2 ASP A 116    32945  29893  27498   2795   4532   4051       O  
ATOM    916  N   ASP A 117      21.843 -92.911  16.777  1.00183.24           N  
ANISOU  916  N   ASP A 117    25744  23235  20643   3045   3726   3380       N  
ATOM    917  CA  ASP A 117      21.736 -92.652  18.204  1.00143.50           C  
ANISOU  917  CA  ASP A 117    20570  18048  15907   2705   3586   3042       C  
ATOM    918  C   ASP A 117      20.387 -93.183  18.669  1.00166.47           C  
ANISOU  918  C   ASP A 117    23330  21348  18571   2834   3335   2773       C  
ATOM    919  O   ASP A 117      19.424 -92.426  18.799  1.00210.22           O  
ANISOU  919  O   ASP A 117    28687  27356  23831   2692   3202   2544       O  
ATOM    920  CB  ASP A 117      21.825 -91.148  18.458  1.00199.12           C  
ANISOU  920  CB  ASP A 117    27489  25226  22941   2323   3603   2882       C  
ATOM    921  CG  ASP A 117      22.756 -90.801  19.602  1.00213.03           C  
ANISOU  921  CG  ASP A 117    29235  26481  25225   1966   3622   2770       C  
ATOM    922  OD1 ASP A 117      23.654 -91.613  19.908  1.00207.56           O  
ANISOU  922  OD1 ASP A 117    28658  25278  24928   2002   3704   2897       O  
ATOM    923  OD2 ASP A 117      22.585 -89.718  20.198  1.00219.28           O  
ANISOU  923  OD2 ASP A 117    29897  27372  26047   1653   3535   2549       O  
ATOM    924  N   PRO A 118      20.309 -94.503  18.886  1.00113.93           N  
ANISOU  924  N   PRO A 118    16750  14501  12040   3109   3287   2798       N  
ATOM    925  CA  PRO A 118      19.069 -95.216  19.202  1.00 96.94           C  
ANISOU  925  CA  PRO A 118    14451  12712   9669   3313   3097   2568       C  
ATOM    926  C   PRO A 118      18.609 -95.027  20.634  1.00 91.09           C  
ANISOU  926  C   PRO A 118    13583  11984   9041   3002   2968   2200       C  
ATOM    927  O   PRO A 118      19.425 -95.053  21.554  1.00121.20           O  
ANISOU  927  O   PRO A 118    17499  15326  13226   2772   2987   2139       O  
ATOM    928  CB  PRO A 118      19.447 -96.688  18.988  1.00124.60           C  
ANISOU  928  CB  PRO A 118    18124  15855  13362   3708   3131   2740       C  
ATOM    929  CG  PRO A 118      20.905 -96.701  18.574  1.00137.37           C  
ANISOU  929  CG  PRO A 118    19988  16898  15308   3666   3346   3080       C  
ATOM    930  CD  PRO A 118      21.473 -95.391  18.985  1.00117.37           C  
ANISOU  930  CD  PRO A 118    17400  14291  12903   3204   3421   3013       C  
ATOM    931  N   LEU A 119      17.306 -94.857  20.818  1.00 93.17           N  
ANISOU  931  N   LEU A 119    13626  12789   8984   2994   2835   1959       N  
ATOM    932  CA  LEU A 119      16.710 -94.875  22.146  1.00 94.66           C  
ANISOU  932  CA  LEU A 119    13715  13041   9211   2756   2731   1630       C  
ATOM    933  C   LEU A 119      16.450 -96.306  22.606  1.00 96.61           C  
ANISOU  933  C   LEU A 119    13994  13173   9542   3057   2704   1521       C  
ATOM    934  O   LEU A 119      16.494 -96.612  23.797  1.00124.05           O  
ANISOU  934  O   LEU A 119    17517  16447  13171   2900   2662   1304       O  
ATOM    935  CB  LEU A 119      15.408 -94.085  22.142  1.00 87.82           C  
ANISOU  935  CB  LEU A 119    12589  12794   7984   2594   2638   1428       C  
ATOM    936  CG  LEU A 119      14.783 -93.874  23.513  1.00 73.09           C  
ANISOU  936  CG  LEU A 119    10642  11014   6117   2276   2564   1126       C  
ATOM    937  CD1 LEU A 119      15.778 -93.181  24.426  1.00107.42           C  
ANISOU  937  CD1 LEU A 119    15165  14887  10762   1903   2556   1119       C  
ATOM    938  CD2 LEU A 119      13.511 -93.061  23.377  1.00 89.68           C  
ANISOU  938  CD2 LEU A 119    12480  13706   7890   2097   2498    965       C  
ATOM    939  N   VAL A 120      16.172 -97.177  21.644  1.00111.59           N  
ANISOU  939  N   VAL A 120    15873  15202  11324   3510   2716   1665       N  
ATOM    940  CA  VAL A 120      15.868 -98.574  21.922  1.00105.39           C  
ANISOU  940  CA  VAL A 120    15100  14327  10618   3868   2692   1559       C  
ATOM    941  C   VAL A 120      16.835 -99.458  21.151  1.00134.28           C  
ANISOU  941  C   VAL A 120    19002  17507  14513   4226   2764   1875       C  
ATOM    942  O   VAL A 120      16.594 -99.780  19.984  1.00118.67           O  
ANISOU  942  O   VAL A 120    17008  15725  12356   4594   2758   2096       O  
ATOM    943  CB  VAL A 120      14.431 -98.935  21.518  1.00103.28           C  
ANISOU  943  CB  VAL A 120    14536  14701  10005   4143   2612   1404       C  
ATOM    944  CG1 VAL A 120      14.112-100.365  21.925  1.00109.91           C  
ANISOU  944  CG1 VAL A 120    15368  15439  10954   4513   2603   1244       C  
ATOM    945  CG2 VAL A 120      13.445 -97.968  22.150  1.00101.14           C  
ANISOU  945  CG2 VAL A 120    14015  14914   9499   3754   2566   1134       C  
ATOM    946  N   PRO A 121      17.945 -99.834  21.801  1.00112.92           N  
ANISOU  946  N   PRO A 121    16529  14159  12215   4109   2822   1903       N  
ATOM    947  CA  PRO A 121      19.067-100.564  21.198  1.00109.86           C  
ANISOU  947  CA  PRO A 121    16404  13193  12146   4341   2922   2222       C  
ATOM    948  C   PRO A 121      18.636-101.795  20.401  1.00123.53           C  
ANISOU  948  C   PRO A 121    18166  14971  13800   4914   2895   2345       C  
ATOM    949  O   PRO A 121      19.155-102.020  19.305  1.00147.92           O  
ANISOU  949  O   PRO A 121    21414  17888  16903   5163   2971   2725       O  
ATOM    950  CB  PRO A 121      19.890-100.993  22.416  1.00120.93           C  
ANISOU  950  CB  PRO A 121    17960  14003  13987   4128   2913   2038       C  
ATOM    951  CG  PRO A 121      19.590 -99.966  23.446  1.00118.71           C  
ANISOU  951  CG  PRO A 121    17547  13946  13614   3668   2838   1758       C  
ATOM    952  CD  PRO A 121      18.147 -99.608  23.241  1.00107.88           C  
ANISOU  952  CD  PRO A 121    15915  13312  11765   3734   2774   1605       C  
ATOM    953  N   GLU A 122      17.698-102.569  20.936  1.00129.99           N  
ANISOU  953  N   GLU A 122    18837  16023  14529   5131   2794   2034       N  
ATOM    954  CA  GLU A 122      17.280-103.803  20.279  1.00125.35           C  
ANISOU  954  CA  GLU A 122    18258  15449  13922   5709   2749   2108       C  
ATOM    955  C   GLU A 122      16.584-103.547  18.946  1.00110.50           C  
ANISOU  955  C   GLU A 122    16231  14098  11655   6006   2689   2337       C  
ATOM    956  O   GLU A 122      16.950-104.141  17.931  1.00125.62           O  
ANISOU  956  O   GLU A 122    18317  15813  13598   6398   2694   2679       O  
ATOM    957  CB  GLU A 122      16.389-104.645  21.198  1.00123.31           C  
ANISOU  957  CB  GLU A 122    17835  15365  13653   5871   2678   1676       C  
ATOM    958  CG  GLU A 122      15.822-105.907  20.548  1.00152.00           C  
ANISOU  958  CG  GLU A 122    21414  19068  17270   6505   2615   1698       C  
ATOM    959  CD  GLU A 122      16.844-107.026  20.397  1.00187.29           C  
ANISOU  959  CD  GLU A 122    26225  22772  22162   6804   2651   1885       C  
ATOM    960  OE1 GLU A 122      16.443-108.139  19.994  1.00198.88           O  
ANISOU  960  OE1 GLU A 122    27678  24209  23678   7339   2589   1875       O  
ATOM    961  OE2 GLU A 122      18.042-106.805  20.678  1.00168.24           O  
ANISOU  961  OE2 GLU A 122    24083  19778  20065   6510   2735   2035       O  
ATOM    962  N   ILE A 123      15.587-102.666  18.952  1.00143.57           N  
ANISOU  962  N   ILE A 123    20118  18947  15484   5816   2620   2152       N  
ATOM    963  CA  ILE A 123      14.869-102.309  17.730  1.00102.15           C  
ANISOU  963  CA  ILE A 123    14705  14255   9852   6054   2522   2312       C  
ATOM    964  C   ILE A 123      15.844-101.731  16.713  1.00102.40           C  
ANISOU  964  C   ILE A 123    15004  14061   9842   6021   2608   2753       C  
ATOM    965  O   ILE A 123      15.736-101.989  15.515  1.00114.19           O  
ANISOU  965  O   ILE A 123    16556  15708  11121   6409   2545   3038       O  
ATOM    966  CB  ILE A 123      13.732-101.293  17.992  1.00 99.36           C  
ANISOU  966  CB  ILE A 123    13988  14593   9171   5745   2443   2017       C  
ATOM    967  CG1 ILE A 123      12.665-101.899  18.905  1.00107.04           C  
ANISOU  967  CG1 ILE A 123    14671  15858  10140   5799   2398   1601       C  
ATOM    968  CG2 ILE A 123      13.086-100.859  16.688  1.00117.97           C  
ANISOU  968  CG2 ILE A 123    16187  17495  11143   5965   2314   2169       C  
ATOM    969  CD1 ILE A 123      11.478-100.982  19.140  1.00115.17           C  
ANISOU  969  CD1 ILE A 123    15326  17560  10872   5497   2339   1326       C  
ATOM    970  N   ALA A 124      16.802-100.955  17.205  1.00115.19           N  
ANISOU  970  N   ALA A 124    16785  15320  11661   5567   2753   2809       N  
ATOM    971  CA  ALA A 124      17.839-100.401  16.346  1.00125.02           C  
ANISOU  971  CA  ALA A 124    18284  16306  12912   5496   2899   3214       C  
ATOM    972  C   ALA A 124      18.604-101.524  15.663  1.00120.21           C  
ANISOU  972  C   ALA A 124    17978  15191  12504   5914   2972   3590       C  
ATOM    973  O   ALA A 124      18.859-101.468  14.460  1.00130.46           O  
ANISOU  973  O   ALA A 124    19440  16543  13587   6155   3014   3970       O  
ATOM    974  CB  ALA A 124      18.786 -99.542  17.148  1.00133.48           C  
ANISOU  974  CB  ALA A 124    19440  17008  14270   4959   3046   3166       C  
ATOM    975  N   ARG A 125      18.958-102.543  16.439  1.00146.16           N  
ANISOU  975  N   ARG A 125    21363  17978  16194   5999   2982   3481       N  
ATOM    976  CA  ARG A 125      19.701-103.680  15.913  1.00133.79           C  
ANISOU  976  CA  ARG A 125    20099  15839  14896   6377   3048   3815       C  
ATOM    977  C   ARG A 125      18.889-104.403  14.846  1.00138.20           C  
ANISOU  977  C   ARG A 125    20629  16740  15140   6981   2892   3980       C  
ATOM    978  O   ARG A 125      19.410-104.734  13.780  1.00142.05           O  
ANISOU  978  O   ARG A 125    21383  17012  15578   7277   2949   4434       O  
ATOM    979  CB  ARG A 125      20.070-104.648  17.040  1.00137.30           C  
ANISOU  979  CB  ARG A 125    20618  15725  15824   6362   3044   3566       C  
ATOM    980  CG  ARG A 125      21.085-105.712  16.641  1.00138.94           C  
ANISOU  980  CG  ARG A 125    21178  15183  16432   6634   3144   3907       C  
ATOM    981  CD  ARG A 125      21.288-106.721  17.759  1.00147.30           C  
ANISOU  981  CD  ARG A 125    22288  15741  17937   6661   3095   3581       C  
ATOM    982  NE  ARG A 125      20.084-107.510  17.999  1.00176.72           N  
ANISOU  982  NE  ARG A 125    25812  19842  21491   7060   2914   3251       N  
ATOM    983  CZ  ARG A 125      19.853-108.702  17.458  1.00202.35           C  
ANISOU  983  CZ  ARG A 125    29157  22913  24814   7627   2839   3362       C  
ATOM    984  NH1 ARG A 125      20.747-109.248  16.646  1.00205.71           N  
ANISOU  984  NH1 ARG A 125    29919  22769  25474   7852   2924   3824       N  
ATOM    985  NH2 ARG A 125      18.728-109.347  17.731  1.00196.91           N  
ANISOU  985  NH2 ARG A 125    28227  22608  23980   7973   2689   3016       N  
ATOM    986  N   ILE A 126      17.613-104.634  15.140  1.00181.99           N  
ANISOU  986  N   ILE A 126    25846  22826  20477   7159   2697   3616       N  
ATOM    987  CA  ILE A 126      16.715-105.321  14.214  1.00131.89           C  
ANISOU  987  CA  ILE A 126    19389  16868  13856   7746   2501   3699       C  
ATOM    988  C   ILE A 126      16.596-104.558  12.897  1.00132.99           C  
ANISOU  988  C   ILE A 126    19567  17425  13538   7842   2451   4034       C  
ATOM    989  O   ILE A 126      16.732-105.138  11.824  1.00139.69           O  
ANISOU  989  O   ILE A 126    20617  18198  14263   8309   2384   4409       O  
ATOM    990  CB  ILE A 126      15.304-105.511  14.821  1.00131.18           C  
ANISOU  990  CB  ILE A 126    18852  17370  13621   7834   2329   3200       C  
ATOM    991  CG1 ILE A 126      15.382-106.237  16.171  1.00130.34           C  
ANISOU  991  CG1 ILE A 126    18725  16898  13901   7735   2393   2834       C  
ATOM    992  CG2 ILE A 126      14.398-106.254  13.851  1.00136.20           C  
ANISOU  992  CG2 ILE A 126    19327  18398  14023   8467   2105   3272       C  
ATOM    993  CD1 ILE A 126      15.973-107.628  16.102  1.00134.93           C  
ANISOU  993  CD1 ILE A 126    19580  16832  14857   8176   2404   2975       C  
ATOM    994  N   TYR A 127      16.353-103.256  12.990  1.00117.31           N  
ANISOU  994  N   TYR A 127    17413  15865  11295   7405   2475   3894       N  
ATOM    995  CA  TYR A 127      16.196-102.407  11.814  1.00118.15           C  
ANISOU  995  CA  TYR A 127    17545  16413  10934   7449   2423   4134       C  
ATOM    996  C   TYR A 127      17.474-102.351  10.988  1.00146.02           C  
ANISOU  996  C   TYR A 127    21529  19464  14489   7492   2633   4673       C  
ATOM    997  O   TYR A 127      17.438-102.396   9.754  1.00132.97           O  
ANISOU  997  O   TYR A 127    20039  18007  12478   7842   2562   5018       O  
ATOM    998  CB  TYR A 127      15.798-100.993  12.240  1.00113.16           C  
ANISOU  998  CB  TYR A 127    16666  16223  10107   6914   2438   3836       C  
ATOM    999  CG  TYR A 127      15.680-100.011  11.096  1.00113.89           C  
ANISOU  999  CG  TYR A 127    16795  16759   9720   6908   2393   4022       C  
ATOM   1000  CD1 TYR A 127      16.771 -99.259  10.682  1.00119.79           C  
ANISOU 1000  CD1 TYR A 127    17845  17231  10438   6668   2631   4325       C  
ATOM   1001  CD2 TYR A 127      14.475 -99.829  10.436  1.00121.17           C  
ANISOU 1001  CD2 TYR A 127    17434  18385  10220   7142   2116   3868       C  
ATOM   1002  CE1 TYR A 127      16.669 -98.358   9.639  1.00131.52           C  
ANISOU 1002  CE1 TYR A 127    19387  19134  11452   6676   2605   4467       C  
ATOM   1003  CE2 TYR A 127      14.360 -98.931   9.392  1.00152.25           C  
ANISOU 1003  CE2 TYR A 127    21420  22733  13696   7143   2049   4001       C  
ATOM   1004  CZ  TYR A 127      15.460 -98.198   8.997  1.00136.43           C  
ANISOU 1004  CZ  TYR A 127    19755  20447  11635   6916   2300   4298       C  
ATOM   1005  OH  TYR A 127      15.352 -97.302   7.961  1.00117.33           O  
ANISOU 1005  OH  TYR A 127    17408  18449   8724   6929   2248   4403       O  
ATOM   1006  N   LYS A 128      18.601-102.237  11.679  1.00169.96           N  
ANISOU 1006  N   LYS A 128    24758  21879  17940   7125   2892   4742       N  
ATOM   1007  CA  LYS A 128      19.891-102.097  11.020  1.00169.49           C  
ANISOU 1007  CA  LYS A 128    25094  21336  17968   7069   3158   5234       C  
ATOM   1008  C   LYS A 128      20.313-103.396  10.334  1.00172.56           C  
ANISOU 1008  C   LYS A 128    25806  21268  18489   7589   3161   5651       C  
ATOM   1009  O   LYS A 128      20.965-103.368   9.291  1.00171.09           O  
ANISOU 1009  O   LYS A 128    25916  20939  18152   7701   3294   6094       O  
ATOM   1010  CB  LYS A 128      20.952-101.643  12.025  1.00157.87           C  
ANISOU 1010  CB  LYS A 128    23679  19327  16977   6520   3413   5148       C  
ATOM   1011  CG  LYS A 128      22.183-101.024  11.392  1.00172.66           C  
ANISOU 1011  CG  LYS A 128    25840  20879  18884   6307   3733   5571       C  
ATOM   1012  CD  LYS A 128      22.723 -99.887  12.244  1.00184.69           C  
ANISOU 1012  CD  LYS A 128    27222  22320  20632   5697   3895   5334       C  
ATOM   1013  CE  LYS A 128      23.845 -99.151  11.530  1.00196.82           C  
ANISOU 1013  CE  LYS A 128    28985  23648  22152   5495   4236   5722       C  
ATOM   1014  NZ  LYS A 128      24.212 -97.889  12.229  1.00184.75           N  
ANISOU 1014  NZ  LYS A 128    27266  22162  20769   4949   4357   5463       N  
ATOM   1015  N   THR A 129      19.925-104.530  10.915  1.00169.43           N  
ANISOU 1015  N   THR A 129    25333  20657  18388   7864   3012   5452       N  
ATOM   1016  CA  THR A 129      20.297-105.830  10.355  1.00144.85           C  
ANISOU 1016  CA  THR A 129    22525  17047  15466   8377   2993   5814       C  
ATOM   1017  C   THR A 129      19.204-106.444   9.474  1.00141.80           C  
ANISOU 1017  C   THR A 129    22024  17156  14697   8985   2674   5842       C  
ATOM   1018  O   THR A 129      19.367-106.539   8.258  1.00146.21           O  
ANISOU 1018  O   THR A 129    22742  17816  14993   9132   2635   6138       O  
ATOM   1019  CB  THR A 129      20.730-106.831  11.452  1.00140.49           C  
ANISOU 1019  CB  THR A 129    22018  15820  15543   8344   3038   5603       C  
ATOM   1020  OG1 THR A 129      19.614-107.149  12.292  1.00135.73           O  
ANISOU 1020  OG1 THR A 129    21038  15594  14940   8431   2817   5053       O  
ATOM   1021  CG2 THR A 129      21.853-106.245  12.302  1.00164.76           C  
ANISOU 1021  CG2 THR A 129    25178  18396  19026   7727   3310   5552       C  
ATOM   1022  N   ASP A 130      18.096-106.859  10.087  1.00173.75           N  
ANISOU 1022  N   ASP A 130    25704  21558  18754   9180   2440   5394       N  
ATOM   1023  CA  ASP A 130      17.006-107.500   9.351  1.00167.58           C  
ANISOU 1023  CA  ASP A 130    24747  21249  17678   9796   2117   5379       C  
ATOM   1024  C   ASP A 130      15.774-106.598   9.243  1.00155.73           C  
ANISOU 1024  C   ASP A 130    22789  20666  15715   9686   1911   5025       C  
ATOM   1025  O   ASP A 130      15.024-106.434  10.207  1.00151.96           O  
ANISOU 1025  O   ASP A 130    21919  20488  15330   9459   1866   4515       O  
ATOM   1026  CB  ASP A 130      16.627-108.820  10.029  1.00160.40           C  
ANISOU 1026  CB  ASP A 130    23722  20049  17173  10157   2009   5109       C  
ATOM   1027  CG  ASP A 130      15.469-109.522   9.345  1.00175.74           C  
ANISOU 1027  CG  ASP A 130    25410  22482  18880  10783   1669   5028       C  
ATOM   1028  OD1 ASP A 130      15.257-109.296   8.136  1.00195.15           O  
ANISOU 1028  OD1 ASP A 130    27917  25292  20938  10943   1513   5282       O  
ATOM   1029  OD2 ASP A 130      14.778-110.312  10.022  1.00173.42           O  
ANISOU 1029  OD2 ASP A 130    24841  22234  18817  11041   1563   4646       O  
ATOM   1030  N   ARG A 131      15.541-106.064   8.047  1.00158.00           N  
ANISOU 1030  N   ARG A 131    23139  21395  15499   9869   1778   5300       N  
ATOM   1031  CA  ARG A 131      14.475-105.089   7.821  1.00136.01           C  
ANISOU 1031  CA  ARG A 131    19956  19453  12267   9723   1580   4993       C  
ATOM   1032  C   ARG A 131      13.112-105.762   7.697  1.00146.59           C  
ANISOU 1032  C   ARG A 131    20859  21327  13510  10190   1225   4686       C  
ATOM   1033  O   ARG A 131      12.088-105.177   8.047  1.00138.67           O  
ANISOU 1033  O   ARG A 131    19392  20941  12355   9982   1094   4249       O  
ATOM   1034  CB  ARG A 131      14.770-104.258   6.570  1.00137.77           C  
ANISOU 1034  CB  ARG A 131    20429  19948  11968   9750   1559   5373       C  
ATOM   1035  CG  ARG A 131      13.847-103.068   6.376  1.00135.20           C  
ANISOU 1035  CG  ARG A 131    19742  20419  11208   9490   1390   5043       C  
ATOM   1036  CD  ARG A 131      14.142-101.972   7.386  1.00128.45           C  
ANISOU 1036  CD  ARG A 131    18771  19513  10519   8766   1646   4745       C  
ATOM   1037  NE  ARG A 131      15.447-101.350   7.169  1.00139.53           N  
ANISOU 1037  NE  ARG A 131    20600  20478  11936   8464   1975   5103       N  
ATOM   1038  CZ  ARG A 131      15.648-100.276   6.411  1.00144.68           C  
ANISOU 1038  CZ  ARG A 131    21378  21428  12167   8297   2026   5236       C  
ATOM   1039  NH1 ARG A 131      16.870 -99.777   6.275  1.00130.40           N  
ANISOU 1039  NH1 ARG A 131    19859  19158  10527   7933   2363   5441       N  
ATOM   1040  NH2 ARG A 131      14.629 -99.697   5.789  1.00128.01           N  
ANISOU 1040  NH2 ARG A 131    18994  20023   9620   8364   1737   5001       N  
ATOM   1041  N   GLU A 132      13.112-106.983   7.173  1.00191.71           N  
ANISOU 1041  N   GLU A 132    26720  26789  19333  10822   1074   4926       N  
ATOM   1042  CA  GLU A 132      11.916-107.811   7.094  1.00195.41           C  
ANISOU 1042  CA  GLU A 132    26770  27666  19809  11336    752   4643       C  
ATOM   1043  C   GLU A 132      11.207-107.847   8.439  1.00191.44           C  
ANISOU 1043  C   GLU A 132    25800  27338  19601  11025    831   4033       C  
ATOM   1044  O   GLU A 132      10.063-107.405   8.565  1.00190.46           O  
ANISOU 1044  O   GLU A 132    25169  27911  19286  10938    666   3639       O  
ATOM   1045  CB  GLU A 132      12.296-109.233   6.678  1.00208.66           C  
ANISOU 1045  CB  GLU A 132    28711  28783  21786  11782    699   4859       C  
ATOM   1046  CG  GLU A 132      11.169-110.250   6.790  1.00227.69           C  
ANISOU 1046  CG  GLU A 132    30689  31478  24343  12261    425   4505       C  
ATOM   1047  CD  GLU A 132      10.268-110.264   5.574  1.00237.80           C  
ANISOU 1047  CD  GLU A 132    31747  33377  25228  12604     41   4522       C  
ATOM   1048  OE1 GLU A 132       9.673-109.214   5.255  1.00244.74           O  
ANISOU 1048  OE1 GLU A 132    32373  34925  25694  12448    -90   4413       O  
ATOM   1049  OE2 GLU A 132      10.161-111.328   4.930  1.00244.06           O  
ANISOU 1049  OE2 GLU A 132    32621  33973  26137  13022   -148   4634       O  
ATOM   1050  N   LYS A 133      11.906-108.382   9.437  1.00142.73           N  
ANISOU 1050  N   LYS A 133    19814  20522  13892  10853   1086   3961       N  
ATOM   1051  CA  LYS A 133      11.366-108.525  10.782  1.00139.48           C  
ANISOU 1051  CA  LYS A 133    19051  20189  13756  10577   1194   3413       C  
ATOM   1052  C   LYS A 133      10.891-107.187  11.334  1.00133.69           C  
ANISOU 1052  C   LYS A 133    18022  19972  12802   9929   1267   3096       C  
ATOM   1053  O   LYS A 133       9.853-107.118  11.985  1.00132.54           O  
ANISOU 1053  O   LYS A 133    17411  20301  12649   9815   1224   2637       O  
ATOM   1054  CB  LYS A 133      12.412-109.134  11.721  1.00138.20           C  
ANISOU 1054  CB  LYS A 133    19234  19196  14080  10418   1457   3428       C  
ATOM   1055  CG  LYS A 133      11.830-109.750  12.989  1.00142.81           C  
ANISOU 1055  CG  LYS A 133    19519  19788  14954  10377   1521   2889       C  
ATOM   1056  CD  LYS A 133      12.747-109.549  14.194  1.00132.90           C  
ANISOU 1056  CD  LYS A 133    18508  17969  14020   9840   1793   2762       C  
ATOM   1057  CE  LYS A 133      14.113-110.190  13.993  1.00164.48           C  
ANISOU 1057  CE  LYS A 133    23048  21076  18373   9965   1907   3160       C  
ATOM   1058  NZ  LYS A 133      14.059-111.677  14.016  1.00178.59           N  
ANISOU 1058  NZ  LYS A 133    24912  22461  20485  10561   1831   3111       N  
ATOM   1059  N   TYR A 134      11.648-106.127  11.066  1.00130.40           N  
ANISOU 1059  N   TYR A 134    17875  19453  12218   9508   1393   3346       N  
ATOM   1060  CA  TYR A 134      11.284-104.798  11.549  1.00125.11           C  
ANISOU 1060  CA  TYR A 134    16972  19206  11359   8893   1458   3074       C  
ATOM   1061  C   TYR A 134       9.948-104.346  10.982  1.00126.50           C  
ANISOU 1061  C   TYR A 134    16677  20225  11160   9000   1187   2843       C  
ATOM   1062  O   TYR A 134       9.054-103.950  11.726  1.00124.10           O  
ANISOU 1062  O   TYR A 134    15958  20337  10857   8697   1185   2413       O  
ATOM   1063  CB  TYR A 134      12.361-103.764  11.207  1.00129.37           C  
ANISOU 1063  CB  TYR A 134    17887  19486  11783   8501   1631   3400       C  
ATOM   1064  CG  TYR A 134      11.944-102.335  11.498  1.00117.59           C  
ANISOU 1064  CG  TYR A 134    16165  18453  10061   7935   1653   3147       C  
ATOM   1065  CD1 TYR A 134      12.013-101.819  12.789  1.00126.97           C  
ANISOU 1065  CD1 TYR A 134    17249  19515  11477   7390   1824   2835       C  
ATOM   1066  CD2 TYR A 134      11.484-101.501  10.485  1.00118.56           C  
ANISOU 1066  CD2 TYR A 134    16195  19119   9735   7957   1485   3216       C  
ATOM   1067  CE1 TYR A 134      11.635-100.516  13.061  1.00108.69           C  
ANISOU 1067  CE1 TYR A 134    14746  17573   8977   6884   1835   2620       C  
ATOM   1068  CE2 TYR A 134      11.104-100.198  10.748  1.00114.65           C  
ANISOU 1068  CE2 TYR A 134    15501  19000   9060   7444   1498   2967       C  
ATOM   1069  CZ  TYR A 134      11.183 -99.712  12.037  1.00115.99           C  
ANISOU 1069  CZ  TYR A 134    15573  19005   9492   6910   1678   2681       C  
ATOM   1070  OH  TYR A 134      10.807 -98.416  12.306  1.00114.18           O  
ANISOU 1070  OH  TYR A 134    15166  19108   9109   6411   1684   2450       O  
ATOM   1071  N   ASN A 135       9.827-104.398   9.661  1.00130.72           N  
ANISOU 1071  N   ASN A 135    17288  21004  11373   9420    956   3137       N  
ATOM   1072  CA  ASN A 135       8.599-104.001   8.989  1.00132.87           C  
ANISOU 1072  CA  ASN A 135    17122  22075  11290   9564    644   2930       C  
ATOM   1073  C   ASN A 135       7.412-104.833   9.455  1.00135.35           C  
ANISOU 1073  C   ASN A 135    16902  22742  11781   9843    500   2523       C  
ATOM   1074  O   ASN A 135       6.341-104.295   9.741  1.00134.28           O  
ANISOU 1074  O   ASN A 135    16269  23203  11547   9601    410   2126       O  
ATOM   1075  CB  ASN A 135       8.761-104.098   7.470  1.00137.96           C  
ANISOU 1075  CB  ASN A 135    18002  22861  11556  10057    387   3348       C  
ATOM   1076  CG  ASN A 135       9.592-102.962   6.897  1.00135.77           C  
ANISOU 1076  CG  ASN A 135    18113  22509  10963   9719    508   3644       C  
ATOM   1077  OD1 ASN A 135      10.114-102.125   7.630  1.00130.41           O  
ANISOU 1077  OD1 ASN A 135    17526  21626  10398   9131    784   3551       O  
ATOM   1078  ND2 ASN A 135       9.725-102.937   5.575  1.00157.88           N  
ANISOU 1078  ND2 ASN A 135    21151  25482  13356  10110    301   4002       N  
ATOM   1079  N   ARG A 136       7.612-106.145   9.546  1.00156.68           N  
ANISOU 1079  N   ARG A 136    19706  25057  14770  10343    498   2612       N  
ATOM   1080  CA  ARG A 136       6.554-107.051   9.990  1.00155.52           C  
ANISOU 1080  CA  ARG A 136    19062  25202  14825  10671    396   2223       C  
ATOM   1081  C   ARG A 136       6.073-106.726  11.404  1.00151.03           C  
ANISOU 1081  C   ARG A 136    18177  24760  14449  10128    646   1739       C  
ATOM   1082  O   ARG A 136       4.874-106.533  11.636  1.00151.64           O  
ANISOU 1082  O   ARG A 136    17692  25463  14462  10045    562   1346       O  
ATOM   1083  CB  ARG A 136       7.023-108.505   9.904  1.00163.11           C  
ANISOU 1083  CB  ARG A 136    20267  25605  16100  11289    386   2412       C  
ATOM   1084  CG  ARG A 136       6.126-109.493  10.632  1.00162.64           C  
ANISOU 1084  CG  ARG A 136    19752  25708  16336  11573    388   1966       C  
ATOM   1085  CD  ARG A 136       6.406-110.920  10.195  1.00168.77           C  
ANISOU 1085  CD  ARG A 136    20717  26043  17364  12332    264   2168       C  
ATOM   1086  NE  ARG A 136       7.836-111.198  10.111  1.00173.28           N  
ANISOU 1086  NE  ARG A 136    21978  25764  18097  12334    424   2619       N  
ATOM   1087  CZ  ARG A 136       8.597-111.529  11.149  1.00176.65           C  
ANISOU 1087  CZ  ARG A 136    22675  25567  18876  12072    723   2533       C  
ATOM   1088  NH1 ARG A 136       8.062-111.621  12.361  1.00163.06           N  
ANISOU 1088  NH1 ARG A 136    20632  23992  17332  11802    897   2020       N  
ATOM   1089  NH2 ARG A 136       9.890-111.763  10.975  1.00165.53           N  
ANISOU 1089  NH2 ARG A 136    21863  23394  17637  12070    848   2958       N  
ATOM   1090  N   ILE A 137       7.014-106.661  12.339  1.00133.34           N  
ANISOU 1090  N   ILE A 137    16299  21925  12440   9755    949   1776       N  
ATOM   1091  CA  ILE A 137       6.693-106.354  13.729  1.00131.45           C  
ANISOU 1091  CA  ILE A 137    15857  21736  12351   9237   1188   1364       C  
ATOM   1092  C   ILE A 137       6.001-105.005  13.843  1.00126.66           C  
ANISOU 1092  C   ILE A 137    14943  21707  11476   8681   1172   1162       C  
ATOM   1093  O   ILE A 137       4.974-104.884  14.507  1.00125.41           O  
ANISOU 1093  O   ILE A 137    14329  21998  11323   8479   1215    762       O  
ATOM   1094  CB  ILE A 137       7.952-106.329  14.615  1.00125.33           C  
ANISOU 1094  CB  ILE A 137    15574  20215  11831   8892   1462   1480       C  
ATOM   1095  CG1 ILE A 137       8.554-107.727  14.739  1.00128.91           C  
ANISOU 1095  CG1 ILE A 137    16296  20061  12623   9384   1503   1581       C  
ATOM   1096  CG2 ILE A 137       7.609-105.814  15.998  1.00121.02           C  
ANISOU 1096  CG2 ILE A 137    14851  19778  11352   8315   1669   1084       C  
ATOM   1097  CD1 ILE A 137       9.835-107.750  15.539  1.00125.76           C  
ANISOU 1097  CD1 ILE A 137    16372  18900  12508   9061   1735   1693       C  
ATOM   1098  N   ALA A 138       6.568-103.999  13.189  1.00123.47           N  
ANISOU 1098  N   ALA A 138    14796  21275  10844   8436   1125   1440       N  
ATOM   1099  CA  ALA A 138       6.024-102.646  13.229  1.00120.27           C  
ANISOU 1099  CA  ALA A 138    14158  21342  10195   7904   1098   1267       C  
ATOM   1100  C   ALA A 138       4.594-102.619  12.712  1.00123.81           C  
ANISOU 1100  C   ALA A 138    14017  22563  10463   8085    844    992       C  
ATOM   1101  O   ALA A 138       3.735-101.924  13.257  1.00128.49           O  
ANISOU 1101  O   ALA A 138    14228  23579  11013   7653    881    656       O  
ATOM   1102  CB  ALA A 138       6.895-101.701  12.431  1.00118.45           C  
ANISOU 1102  CB  ALA A 138    14315  20952   9738   7733   1073   1618       C  
ATOM   1103  N   ARG A 139       4.343-103.391  11.657  1.00131.52           N  
ANISOU 1103  N   ARG A 139    14914  23705  11351   8724    578   1140       N  
ATOM   1104  CA  ARG A 139       2.998-103.500  11.114  1.00135.78           C  
ANISOU 1104  CA  ARG A 139    14853  24971  11764   8970    294    871       C  
ATOM   1105  C   ARG A 139       2.066-104.148  12.123  1.00136.80           C  
ANISOU 1105  C   ARG A 139    14492  25323  12164   8953    434    439       C  
ATOM   1106  O   ARG A 139       0.923-103.724  12.272  1.00137.59           O  
ANISOU 1106  O   ARG A 139    14041  26023  12215   8730    372     90       O  
ATOM   1107  CB  ARG A 139       2.991-104.278   9.796  1.00141.90           C  
ANISOU 1107  CB  ARG A 139    15677  25835  12404   9719    -50   1141       C  
ATOM   1108  CG  ARG A 139       2.849-103.395   8.566  1.00143.33           C  
ANISOU 1108  CG  ARG A 139    15881  26420  12159   9735   -362   1297       C  
ATOM   1109  CD  ARG A 139       2.714-104.222   7.298  1.00150.16           C  
ANISOU 1109  CD  ARG A 139    16762  27428  12863  10513   -745   1546       C  
ATOM   1110  NE  ARG A 139       3.891-105.051   7.052  1.00151.38           N  
ANISOU 1110  NE  ARG A 139    17518  26883  13115  10909   -643   2013       N  
ATOM   1111  CZ  ARG A 139       4.949-104.654   6.353  1.00162.49           C  
ANISOU 1111  CZ  ARG A 139    19516  27946  14275  10910   -615   2476       C  
ATOM   1112  NH1 ARG A 139       5.977-105.476   6.180  1.00179.85           N  
ANISOU 1112  NH1 ARG A 139    22232  29487  16617  11254   -499   2897       N  
ATOM   1113  NH2 ARG A 139       4.982-103.436   5.826  1.00148.98           N  
ANISOU 1113  NH2 ARG A 139    17881  26542  12183  10562   -686   2509       N  
ATOM   1114  N   GLU A 140       2.550-105.174  12.818  1.00134.85           N  
ANISOU 1114  N   GLU A 140    14442  24591  12205   9176    636    450       N  
ATOM   1115  CA  GLU A 140       1.728-105.829  13.832  1.00136.09           C  
ANISOU 1115  CA  GLU A 140    14177  24938  12594   9171    818     29       C  
ATOM   1116  C   GLU A 140       1.379-104.882  14.977  1.00131.26           C  
ANISOU 1116  C   GLU A 140    13426  24482  11964   8410   1087   -252       C  
ATOM   1117  O   GLU A 140       0.237-104.848  15.440  1.00135.20           O  
ANISOU 1117  O   GLU A 140    13380  25500  12489   8255   1151   -625       O  
ATOM   1118  CB  GLU A 140       2.406-107.098  14.350  1.00137.56           C  
ANISOU 1118  CB  GLU A 140    14667  24521  13080   9565    978     84       C  
ATOM   1119  CG  GLU A 140       2.181-108.302  13.453  1.00183.86           C  
ANISOU 1119  CG  GLU A 140    20408  30409  19043  10393    723    177       C  
ATOM   1120  CD  GLU A 140       3.341-109.274  13.472  1.00218.75           C  
ANISOU 1120  CD  GLU A 140    25392  34030  23694  10781    792    468       C  
ATOM   1121  OE1 GLU A 140       3.518-110.005  12.477  1.00246.55           O  
ANISOU 1121  OE1 GLU A 140    29021  37421  27234  11419    541    735       O  
ATOM   1122  OE2 GLU A 140       4.078-109.309  14.481  1.00203.52           O  
ANISOU 1122  OE2 GLU A 140    23803  31592  21935  10449   1081    432       O  
ATOM   1123  N   TRP A 141       2.367-104.109  15.419  1.00125.88           N  
ANISOU 1123  N   TRP A 141    13233  23347  11247   7940   1244    -60       N  
ATOM   1124  CA  TRP A 141       2.176-103.151  16.501  1.00126.98           C  
ANISOU 1124  CA  TRP A 141    13331  23553  11364   7220   1473   -268       C  
ATOM   1125  C   TRP A 141       1.198-102.064  16.089  1.00121.13           C  
ANISOU 1125  C   TRP A 141    12169  23445  10412   6873   1332   -424       C  
ATOM   1126  O   TRP A 141       0.403-101.584  16.898  1.00120.04           O  
ANISOU 1126  O   TRP A 141    11713  23617  10282   6418   1486   -718       O  
ATOM   1127  CB  TRP A 141       3.506-102.512  16.910  1.00116.94           C  
ANISOU 1127  CB  TRP A 141    12664  21653  10114   6844   1611     -3       C  
ATOM   1128  CG  TRP A 141       4.285-103.295  17.922  1.00114.83           C  
ANISOU 1128  CG  TRP A 141    12738  20796  10097   6878   1837    -12       C  
ATOM   1129  CD1 TRP A 141       4.449-104.649  17.966  1.00122.26           C  
ANISOU 1129  CD1 TRP A 141    13734  21483  11237   7415   1856    -29       C  
ATOM   1130  CD2 TRP A 141       5.000-102.767  19.047  1.00110.12           C  
ANISOU 1130  CD2 TRP A 141    12475  19780   9584   6357   2048    -28       C  
ATOM   1131  NE1 TRP A 141       5.229-104.995  19.045  1.00116.25           N  
ANISOU 1131  NE1 TRP A 141    13326  20169  10673   7247   2069    -72       N  
ATOM   1132  CE2 TRP A 141       5.578-103.857  19.722  1.00111.17           C  
ANISOU 1132  CE2 TRP A 141    12854  19428   9956   6603   2178    -68       C  
ATOM   1133  CE3 TRP A 141       5.209-101.475  19.544  1.00117.79           C  
ANISOU 1133  CE3 TRP A 141    13563  20729  10465   5724   2118    -21       C  
ATOM   1134  CZ2 TRP A 141       6.352-103.697  20.869  1.00121.42           C  
ANISOU 1134  CZ2 TRP A 141    14501  20248  11385   6229   2354   -109       C  
ATOM   1135  CZ3 TRP A 141       5.978-101.319  20.681  1.00147.00           C  
ANISOU 1135  CZ3 TRP A 141    17603  23947  14302   5372   2293    -40       C  
ATOM   1136  CH2 TRP A 141       6.539-102.425  21.332  1.00125.94           C  
ANISOU 1136  CH2 TRP A 141    15168  20828  11854   5622   2400    -87       C  
ATOM   1137  N   THR A 142       1.273-101.673  14.823  1.00122.60           N  
ANISOU 1137  N   THR A 142    12375  23808  10400   7079   1039   -222       N  
ATOM   1138  CA  THR A 142       0.335-100.701  14.290  1.00123.35           C  
ANISOU 1138  CA  THR A 142    12061  24508  10298   6809    846   -394       C  
ATOM   1139  C   THR A 142      -1.066-101.296  14.342  1.00128.18           C  
ANISOU 1139  C   THR A 142    11971  25728  11004   7002    779   -760       C  
ATOM   1140  O   THR A 142      -1.995-100.671  14.849  1.00127.81           O  
ANISOU 1140  O   THR A 142    11511  26085  10967   6539    863  -1060       O  
ATOM   1141  CB  THR A 142       0.698-100.303  12.849  1.00124.95           C  
ANISOU 1141  CB  THR A 142    12444  24798  10233   7086    514   -118       C  
ATOM   1142  OG1 THR A 142       2.051 -99.832  12.811  1.00120.93           O  
ANISOU 1142  OG1 THR A 142    12577  23709   9663   6931    631    230       O  
ATOM   1143  CG2 THR A 142      -0.227 -99.211  12.344  1.00125.63           C  
ANISOU 1143  CG2 THR A 142    12139  25481  10116   6757    301   -336       C  
ATOM   1144  N   GLN A 143      -1.190-102.523  13.837  1.00133.00           N  
ANISOU 1144  N   GLN A 143    12450  26373  11710   7688    643   -728       N  
ATOM   1145  CA  GLN A 143      -2.448-103.268  13.824  1.00138.43           C  
ANISOU 1145  CA  GLN A 143    12450  27612  12535   7987    576  -1072       C  
ATOM   1146  C   GLN A 143      -3.083-103.372  15.203  1.00137.41           C  
ANISOU 1146  C   GLN A 143    12026  27595  12587   7582    964  -1421       C  
ATOM   1147  O   GLN A 143      -4.308-103.336  15.338  1.00140.56           O  
ANISOU 1147  O   GLN A 143    11778  28579  13050   7466    977  -1761       O  
ATOM   1148  CB  GLN A 143      -2.216-104.677  13.279  1.00169.76           C  
ANISOU 1148  CB  GLN A 143    16457  31409  16634   8813    430   -947       C  
ATOM   1149  CG  GLN A 143      -2.374-104.811  11.776  1.00167.33           C  
ANISOU 1149  CG  GLN A 143    16045  31379  16153   9357    -44   -767       C  
ATOM   1150  CD  GLN A 143      -3.785-105.203  11.378  1.00199.60           C  
ANISOU 1150  CD  GLN A 143    19320  36194  20326   9644   -275  -1125       C  
ATOM   1151  OE1 GLN A 143      -4.622-105.501  12.230  1.00189.98           O  
ANISOU 1151  OE1 GLN A 143    17610  35249  19326   9482    -35  -1500       O  
ATOM   1152  NE2 GLN A 143      -4.054-105.204  10.077  1.00209.06           N  
ANISOU 1152  NE2 GLN A 143    20367  37720  21346  10076   -742  -1015       N  
ATOM   1153  N   LYS A 144      -2.248-103.514  16.225  1.00136.61           N  
ANISOU 1153  N   LYS A 144    12400  26938  12567   7368   1280  -1338       N  
ATOM   1154  CA  LYS A 144      -2.746-103.652  17.586  1.00132.61           C  
ANISOU 1154  CA  LYS A 144    11714  26496  12177   7001   1661  -1640       C  
ATOM   1155  C   LYS A 144      -3.085-102.304  18.212  1.00128.67           C  
ANISOU 1155  C   LYS A 144    11170  26159  11558   6195   1804  -1731       C  
ATOM   1156  O   LYS A 144      -4.249-101.998  18.470  1.00130.81           O  
ANISOU 1156  O   LYS A 144    10891  26968  11842   5909   1886  -2021       O  
ATOM   1157  CB  LYS A 144      -1.738-104.410  18.459  1.00130.60           C  
ANISOU 1157  CB  LYS A 144    11989  25584  12047   7125   1908  -1548       C  
ATOM   1158  CG  LYS A 144      -1.537-105.861  18.037  1.00175.71           C  
ANISOU 1158  CG  LYS A 144    17704  31119  17938   7913   1821  -1527       C  
ATOM   1159  CD  LYS A 144      -0.568-106.596  18.951  1.00169.00           C  
ANISOU 1159  CD  LYS A 144    17370  29605  17237   7997   2060  -1485       C  
ATOM   1160  CE  LYS A 144      -0.506-108.073  18.589  1.00192.29           C  
ANISOU 1160  CE  LYS A 144    20271  32388  20400   8783   1987  -1521       C  
ATOM   1161  NZ  LYS A 144       0.467-108.826  19.430  1.00183.61           N  
ANISOU 1161  NZ  LYS A 144    19688  30605  19471   8884   2191  -1504       N  
ATOM   1162  N   TYR A 145      -2.059-101.496  18.444  1.00123.25           N  
ANISOU 1162  N   TYR A 145    11056  24992  10781   5832   1835  -1479       N  
ATOM   1163  CA  TYR A 145      -2.209-100.284  19.242  1.00121.23           C  
ANISOU 1163  CA  TYR A 145    10866  24749  10447   5077   2003  -1543       C  
ATOM   1164  C   TYR A 145      -2.773 -99.053  18.520  1.00118.91           C  
ANISOU 1164  C   TYR A 145    10322  24840  10019   4722   1785  -1568       C  
ATOM   1165  O   TYR A 145      -3.554 -98.298  19.098  1.00118.46           O  
ANISOU 1165  O   TYR A 145     9996  25060   9953   4176   1914  -1763       O  
ATOM   1166  CB  TYR A 145      -0.885 -99.973  19.939  1.00113.92           C  
ANISOU 1166  CB  TYR A 145    10628  23130   9526   4838   2139  -1305       C  
ATOM   1167  CG  TYR A 145      -0.268-101.215  20.546  1.00114.68           C  
ANISOU 1167  CG  TYR A 145    10991  22814   9768   5218   2303  -1295       C  
ATOM   1168  CD1 TYR A 145      -0.792-101.779  21.700  1.00138.79           C  
ANISOU 1168  CD1 TYR A 145    13898  25957  12880   5116   2594  -1566       C  
ATOM   1169  CD2 TYR A 145       0.822-101.834  19.951  1.00133.52           C  
ANISOU 1169  CD2 TYR A 145    13781  24721  12230   5682   2174  -1023       C  
ATOM   1170  CE1 TYR A 145      -0.240-102.920  22.254  1.00117.70           C  
ANISOU 1170  CE1 TYR A 145    11478  22906  10336   5475   2730  -1601       C  
ATOM   1171  CE2 TYR A 145       1.380-102.973  20.494  1.00145.27           C  
ANISOU 1171  CE2 TYR A 145    15512  25798  13884   6023   2308  -1038       C  
ATOM   1172  CZ  TYR A 145       0.847-103.511  21.644  1.00128.88           C  
ANISOU 1172  CZ  TYR A 145    13286  23820  11863   5925   2573  -1345       C  
ATOM   1173  OH  TYR A 145       1.406-104.644  22.182  1.00131.83           O  
ANISOU 1173  OH  TYR A 145    13916  23776  12396   6273   2693  -1399       O  
ATOM   1174  N   ALA A 146      -2.384 -98.853  17.265  1.00136.13           N  
ANISOU 1174  N   ALA A 146    12607  27031  12086   5027   1457  -1373       N  
ATOM   1175  CA  ALA A 146      -2.749 -97.630  16.546  1.00135.65           C  
ANISOU 1175  CA  ALA A 146    12407  27266  11869   4699   1228  -1396       C  
ATOM   1176  C   ALA A 146      -4.077 -97.687  15.791  1.00141.06           C  
ANISOU 1176  C   ALA A 146    12391  28661  12544   4835    987  -1669       C  
ATOM   1177  O   ALA A 146      -4.570 -96.658  15.335  1.00157.35           O  
ANISOU 1177  O   ALA A 146    14259  31019  14507   4491    811  -1774       O  
ATOM   1178  CB  ALA A 146      -1.630 -97.227  15.595  1.00133.63           C  
ANISOU 1178  CB  ALA A 146    12657  26675  11443   4895   1013  -1059       C  
ATOM   1179  N   MET A 147      -4.641 -98.880  15.639  1.00137.78           N  
ANISOU 1179  N   MET A 147    11587  28512  12251   5345    962  -1801       N  
ATOM   1180  CA  MET A 147      -5.842 -99.050  14.817  1.00135.06           C  
ANISOU 1180  CA  MET A 147    10545  28844  11929   5569    682  -2055       C  
ATOM   1181  C   MET A 147      -7.179 -99.103  15.564  1.00138.04           C  
ANISOU 1181  C   MET A 147    10236  29713  12499   5231    903  -2450       C  
ATOM   1182  O   MET A 147      -8.221 -99.337  14.952  1.00143.45           O  
ANISOU 1182  O   MET A 147    10266  30974  13264   5421    690  -2696       O  
ATOM   1183  CB  MET A 147      -5.680-100.241  13.871  1.00139.58           C  
ANISOU 1183  CB  MET A 147    11057  29469  12508   6416    409  -1944       C  
ATOM   1184  CG  MET A 147      -4.440-100.124  12.999  1.00137.53           C  
ANISOU 1184  CG  MET A 147    11450  28775  12030   6730    184  -1530       C  
ATOM   1185  SD  MET A 147      -4.756-100.249  11.237  1.00143.27           S  
ANISOU 1185  SD  MET A 147    11960  29939  12536   7334   -407  -1454       S  
ATOM   1186  CE  MET A 147      -5.142-101.989  11.080  1.00182.28           C  
ANISOU 1186  CE  MET A 147    16555  34989  17712   8165   -478  -1513       C  
TER    3227      LYS A1271                                                      
CONECT  176  849                                                                
CONECT  849  176                                                                
CONECT 3403 4076                                                                
CONECT 4076 3403                                                                
CONECT 6630 7303                                                                
CONECT 7303 6630                                                                
CONECT1346914142                                                                
CONECT1414213469                                                                
CONECT1669617369                                                                
CONECT1736916696                                                                
CONECT1992320596                                                                
CONECT2059619923                                                                
MASTER      838    0    0  132  120    0    0    626568   18   12  258          
END                                                                             


A second structure was input as follows:


HEADER    LIGASE                                  17-DEC-15   5FER              
TITLE     COMPLEX OF TRIM25 RING WITH UBCH5-UB                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: E3 UBIQUITIN/ISG15 LIGASE TRIM25;                          
COMPND   3 CHAIN: A, D;                                                         
COMPND   4 SYNONYM: ESTROGEN-RESPONSIVE FINGER PROTEIN,RING FINGER PROTEIN 147, 
COMPND   5 RING-TYPE E3 UBIQUITIN TRANSFERASE,TRIPARTITE MOTIF-CONTAINING       
COMPND   6 PROTEIN 25,UBIQUITIN/ISG15-CONJUGATING ENZYME TRIM25,ZINC FINGER     
COMPND   7 PROTEIN 147;                                                         
COMPND   8 EC: 6.3.2.-,2.3.2.27;                                                
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: UBIQUITIN-CONJUGATING ENZYME E2 D1;                        
COMPND  12 CHAIN: B, E;                                                         
COMPND  13 SYNONYM: (E3-INDEPENDENT) E2 UBIQUITIN-CONJUGATING ENZYME D1,E2      
COMPND  14 UBIQUITIN-CONJUGATING ENZYME D1,STIMULATOR OF FE TRANSPORT,SFT,UBC4/5
COMPND  15 HOMOLOG,UBCH5,UBIQUITIN CARRIER PROTEIN D1,UBIQUITIN-CONJUGATING     
COMPND  16 ENZYME E2(17)KB 1,UBIQUITIN-CONJUGATING ENZYME E2-17 KDA 1,UBIQUITIN-
COMPND  17 PROTEIN LIGASE D1;                                                   
COMPND  18 EC: 2.3.2.23,2.3.2.24;                                               
COMPND  19 ENGINEERED: YES;                                                     
COMPND  20 MOL_ID: 3;                                                           
COMPND  21 MOLECULE: UBIQUITIN-40S RIBOSOMAL PROTEIN S27A;                      
COMPND  22 CHAIN: C, F;                                                         
COMPND  23 SYNONYM: UBIQUITIN CARBOXYL EXTENSION PROTEIN 80                     
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: TRIM25, EFP, RNF147, ZNF147;                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: UBE2D1, SFT, UBC5A, UBCH5, UBCH5A;                             
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE  17 ORGANISM_COMMON: BOVINE;                                             
SOURCE  18 ORGANISM_TAXID: 9913                                                 
KEYWDS    E3 LIGASE, UBIQUITIN, LIGASE                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.RITTINGER,M.G.KOLIOPOULOS,D.ESPOSITO                                
REVDAT   4   20-FEB-19 5FER    1       REMARK LINK                              
REVDAT   3   13-SEP-17 5FER    1       REMARK                                   
REVDAT   2   15-JUN-16 5FER    1       JRNL                                     
REVDAT   1   18-MAY-16 5FER    0                                                
JRNL        AUTH   M.G.KOLIOPOULOS,D.ESPOSITO,E.CHRISTODOULOU,I.A.TAYLOR,       
JRNL        AUTH 2 K.RITTINGER                                                  
JRNL        TITL   FUNCTIONAL ROLE OF TRIM E3 LIGASE OLIGOMERIZATION AND        
JRNL        TITL 2 REGULATION OF CATALYTIC ACTIVITY.                            
JRNL        REF    EMBO J.                       V.  35  1204 2016              
JRNL        REFN                   ESSN 1460-2075                               
JRNL        PMID   27154206                                                     
JRNL        DOI    10.15252/EMBJ.201593741                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.34 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10.1_2155: ???)                            
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.34                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.30                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 30000                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.229                           
REMARK   3   R VALUE            (WORKING SET) : 0.227                           
REMARK   3   FREE R VALUE                     : 0.273                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.890                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1468                            
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 30.2978 -  5.0345    1.00     3046   161  0.1790 0.2272        
REMARK   3     2  5.0345 -  3.9989    1.00     2915   151  0.1770 0.2143        
REMARK   3     3  3.9989 -  3.4943    1.00     2883   147  0.2091 0.2672        
REMARK   3     4  3.4943 -  3.1752    1.00     2869   145  0.2459 0.3070        
REMARK   3     5  3.1752 -  2.9478    0.99     2821   163  0.2688 0.3163        
REMARK   3     6  2.9478 -  2.7741    0.99     2807   131  0.2911 0.3022        
REMARK   3     7  2.7741 -  2.6353    0.99     2811   136  0.3087 0.3684        
REMARK   3     8  2.6353 -  2.5206    0.99     2789   167  0.3365 0.4033        
REMARK   3     9  2.5206 -  2.4236    0.99     2786   134  0.3428 0.3737        
REMARK   3    10  2.4236 -  2.3400    0.99     2805   133  0.3685 0.3674        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.400            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.820           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.002           4879                                  
REMARK   3   ANGLE     :  0.539           6630                                  
REMARK   3   CHIRALITY :  0.041            740                                  
REMARK   3   PLANARITY :  0.006            862                                  
REMARK   3   DIHEDRAL  : 12.639           2990                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
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 5FER COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-DEC-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000216462.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-MAY-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.2829                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : PSI PILATUS 6M                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XIA2                               
REMARK 200  DATA SCALING SOFTWARE          : XIA2                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 30000                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.340                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.280                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 12.80                              
REMARK 200  R MERGE                    (I) : 0.13900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 13.7500                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.34                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.42                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.91800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: AUTOSOL                                               
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.80                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 20000 AND 100 MM TRIS PH 8.5,    
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       30.24000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       80.21500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       35.85000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       80.21500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       30.24000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       35.85000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5630 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 30820 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F                      
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    -2                                                      
REMARK 465     PRO A    -1                                                      
REMARK 465     GLY A     0                                                      
REMARK 465     ASP A    80                                                      
REMARK 465     LEU A    81                                                      
REMARK 465     ALA A    82                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     PRO B    -1                                                      
REMARK 465     GLY B     0                                                      
REMARK 465     ALA B   146                                                      
REMARK 465     MET B   147                                                      
REMARK 465     GLY D    -2                                                      
REMARK 465     PRO D    -1                                                      
REMARK 465     GLY D     0                                                      
REMARK 465     MET D     1                                                      
REMARK 465     ALA D     2                                                      
REMARK 465     GLY E    -2                                                      
REMARK 465     PRO E    -1                                                      
REMARK 465     GLY E     0                                                      
REMARK 465     MET E   147                                                      
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   NZ   LYS B    85     O    GLY C    76              1.27            
REMARK 500   NZ   LYS E    85     O    GLY F    76              1.41            
REMARK 500   CE   LYS E    85     O    GLY F    76              1.56            
REMARK 500   OH   TYR E   134     O    HOH E   201              2.02            
REMARK 500   O    TYR E    74     O    HOH E   201              2.03            
REMARK 500   OH   TYR E    45     O    HOH E   201              2.05            
REMARK 500   CE   LYS B    85     O    GLY C    76              2.15            
REMARK 500   OD2  ASP B    87     O    HOH B   201              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLU A   3       21.08    -76.50                                   
REMARK 500    SER A  46     -136.50     61.70                                   
REMARK 500    PRO B  17       77.30     21.11                                   
REMARK 500    ARG B  90     -108.86   -137.17                                   
REMARK 500    ASP B 130       81.07   -158.87                                   
REMARK 500    VAL C  17     -169.68   -129.61                                   
REMARK 500    GLN C  62     -169.60   -114.67                                   
REMARK 500    SER D  46     -149.58     58.75                                   
REMARK 500    ARG E  90      -98.16   -139.33                                   
REMARK 500    ASP E 130       82.69   -159.18                                   
REMARK 500    VAL F  17     -168.17   -129.30                                   
REMARK 500    GLN F  62     -155.09   -115.57                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 101  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  13   SG                                                     
REMARK 620 2 CYS A  16   SG   99.7                                              
REMARK 620 3 CYS A  33   SG  107.8  97.5                                        
REMARK 620 4 CYS A  36   SG  120.3 105.6 120.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 102  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  28   SG                                                     
REMARK 620 2 HIS A  30   ND1 114.7                                              
REMARK 620 3 CYS A  50   SG  101.4 112.4                                        
REMARK 620 4 CYS A  53   SG  109.4 108.1 110.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 102  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D  13   SG                                                     
REMARK 620 2 CYS D  16   SG  112.6                                              
REMARK 620 3 CYS D  33   SG  103.2 106.2                                        
REMARK 620 4 CYS D  36   SG  113.7 108.9 111.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 101  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D  28   SG                                                     
REMARK 620 2 HIS D  30   ND1 112.5                                              
REMARK 620 3 CYS D  50   SG  102.7 109.8                                        
REMARK 620 4 CYS D  53   SG  110.2 109.1 112.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 101                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 102                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 101                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 102                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide GLY F 76 and LYS E     
REMARK 800  85                                                                  
DBREF  5FER A    1    82  UNP    Q14258   TRI25_HUMAN      1     82             
DBREF  5FER B    1   147  UNP    P51668   UB2D1_HUMAN      1    147             
DBREF  5FER C    1    76  UNP    P62992   RS27A_BOVIN      1     76             
DBREF  5FER D    1    82  UNP    Q14258   TRI25_HUMAN      1     82             
DBREF  5FER E    1   147  UNP    P51668   UB2D1_HUMAN      1    147             
DBREF  5FER F    1    76  UNP    P62992   RS27A_BOVIN      1     76             
SEQADV 5FER GLY A   -2  UNP  Q14258              EXPRESSION TAG                 
SEQADV 5FER PRO A   -1  UNP  Q14258              EXPRESSION TAG                 
SEQADV 5FER GLY A    0  UNP  Q14258              EXPRESSION TAG                 
SEQADV 5FER GLY B   -2  UNP  P51668              EXPRESSION TAG                 
SEQADV 5FER PRO B   -1  UNP  P51668              EXPRESSION TAG                 
SEQADV 5FER GLY B    0  UNP  P51668              EXPRESSION TAG                 
SEQADV 5FER ARG B   22  UNP  P51668    SER    22 ENGINEERED MUTATION            
SEQADV 5FER LYS B   85  UNP  P51668    CYS    85 ENGINEERED MUTATION            
SEQADV 5FER GLY D   -2  UNP  Q14258              EXPRESSION TAG                 
SEQADV 5FER PRO D   -1  UNP  Q14258              EXPRESSION TAG                 
SEQADV 5FER GLY D    0  UNP  Q14258              EXPRESSION TAG                 
SEQADV 5FER GLY E   -2  UNP  P51668              EXPRESSION TAG                 
SEQADV 5FER PRO E   -1  UNP  P51668              EXPRESSION TAG                 
SEQADV 5FER GLY E    0  UNP  P51668              EXPRESSION TAG                 
SEQADV 5FER ARG E   22  UNP  P51668    SER    22 ENGINEERED MUTATION            
SEQADV 5FER LYS E   85  UNP  P51668    CYS    85 ENGINEERED MUTATION            
SEQRES   1 A   85  GLY PRO GLY MET ALA GLU LEU CYS PRO LEU ALA GLU GLU          
SEQRES   2 A   85  LEU SER CYS SER ILE CYS LEU GLU PRO PHE LYS GLU PRO          
SEQRES   3 A   85  VAL THR THR PRO CYS GLY HIS ASN PHE CYS GLY SER CYS          
SEQRES   4 A   85  LEU ASN GLU THR TRP ALA VAL GLN GLY SER PRO TYR LEU          
SEQRES   5 A   85  CYS PRO GLN CYS ARG ALA VAL TYR GLN ALA ARG PRO GLN          
SEQRES   6 A   85  LEU HIS LYS ASN THR VAL LEU CYS ASN VAL VAL GLU GLN          
SEQRES   7 A   85  PHE LEU GLN ALA ASP LEU ALA                                  
SEQRES   1 B  150  GLY PRO GLY MET ALA LEU LYS ARG ILE GLN LYS GLU LEU          
SEQRES   2 B  150  SER ASP LEU GLN ARG ASP PRO PRO ALA HIS CYS ARG ALA          
SEQRES   3 B  150  GLY PRO VAL GLY ASP ASP LEU PHE HIS TRP GLN ALA THR          
SEQRES   4 B  150  ILE MET GLY PRO PRO ASP SER ALA TYR GLN GLY GLY VAL          
SEQRES   5 B  150  PHE PHE LEU THR VAL HIS PHE PRO THR ASP TYR PRO PHE          
SEQRES   6 B  150  LYS PRO PRO LYS ILE ALA PHE THR THR LYS ILE TYR HIS          
SEQRES   7 B  150  PRO ASN ILE ASN SER ASN GLY SER ILE LYS LEU ASP ILE          
SEQRES   8 B  150  LEU ARG SER GLN TRP SER PRO ALA LEU THR VAL SER LYS          
SEQRES   9 B  150  VAL LEU LEU SER ILE CYS SER LEU LEU CYS ASP PRO ASN          
SEQRES  10 B  150  PRO ASP ASP PRO LEU VAL PRO ASP ILE ALA GLN ILE TYR          
SEQRES  11 B  150  LYS SER ASP LYS GLU LYS TYR ASN ARG HIS ALA ARG GLU          
SEQRES  12 B  150  TRP THR GLN LYS TYR ALA MET                                  
SEQRES   1 C   76  MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE          
SEQRES   2 C   76  THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL          
SEQRES   3 C   76  LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP          
SEQRES   4 C   76  GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP          
SEQRES   5 C   76  GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER          
SEQRES   6 C   76  THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY                  
SEQRES   1 D   85  GLY PRO GLY MET ALA GLU LEU CYS PRO LEU ALA GLU GLU          
SEQRES   2 D   85  LEU SER CYS SER ILE CYS LEU GLU PRO PHE LYS GLU PRO          
SEQRES   3 D   85  VAL THR THR PRO CYS GLY HIS ASN PHE CYS GLY SER CYS          
SEQRES   4 D   85  LEU ASN GLU THR TRP ALA VAL GLN GLY SER PRO TYR LEU          
SEQRES   5 D   85  CYS PRO GLN CYS ARG ALA VAL TYR GLN ALA ARG PRO GLN          
SEQRES   6 D   85  LEU HIS LYS ASN THR VAL LEU CYS ASN VAL VAL GLU GLN          
SEQRES   7 D   85  PHE LEU GLN ALA ASP LEU ALA                                  
SEQRES   1 E  150  GLY PRO GLY MET ALA LEU LYS ARG ILE GLN LYS GLU LEU          
SEQRES   2 E  150  SER ASP LEU GLN ARG ASP PRO PRO ALA HIS CYS ARG ALA          
SEQRES   3 E  150  GLY PRO VAL GLY ASP ASP LEU PHE HIS TRP GLN ALA THR          
SEQRES   4 E  150  ILE MET GLY PRO PRO ASP SER ALA TYR GLN GLY GLY VAL          
SEQRES   5 E  150  PHE PHE LEU THR VAL HIS PHE PRO THR ASP TYR PRO PHE          
SEQRES   6 E  150  LYS PRO PRO LYS ILE ALA PHE THR THR LYS ILE TYR HIS          
SEQRES   7 E  150  PRO ASN ILE ASN SER ASN GLY SER ILE LYS LEU ASP ILE          
SEQRES   8 E  150  LEU ARG SER GLN TRP SER PRO ALA LEU THR VAL SER LYS          
SEQRES   9 E  150  VAL LEU LEU SER ILE CYS SER LEU LEU CYS ASP PRO ASN          
SEQRES  10 E  150  PRO ASP ASP PRO LEU VAL PRO ASP ILE ALA GLN ILE TYR          
SEQRES  11 E  150  LYS SER ASP LYS GLU LYS TYR ASN ARG HIS ALA ARG GLU          
SEQRES  12 E  150  TRP THR GLN LYS TYR ALA MET                                  
SEQRES   1 F   76  MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE          
SEQRES   2 F   76  THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL          
SEQRES   3 F   76  LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP          
SEQRES   4 F   76  GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP          
SEQRES   5 F   76  GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER          
SEQRES   6 F   76  THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY                  
HET     ZN  A 101       1                                                       
HET     ZN  A 102       1                                                       
HET     ZN  D 101       1                                                       
HET     ZN  D 102       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL   7   ZN    4(ZN 2+)                                                     
FORMUL  11  HOH   *68(H2 O)                                                     
HELIX    1 AA1 PRO A    6  LEU A   11  1                                   6    
HELIX    2 AA2 GLY A   34  GLN A   44  1                                  11    
HELIX    3 AA3 ASN A   66  ALA A   79  1                                  14    
HELIX    4 AA4 ALA B    2  ASP B   16  1                                  15    
HELIX    5 AA5 LEU B   86  ARG B   90  5                                   5    
HELIX    6 AA6 THR B   98  CYS B  111  1                                  14    
HELIX    7 AA7 VAL B  120  ASP B  130  1                                  11    
HELIX    8 AA8 ASP B  130  TYR B  145  1                                  16    
HELIX    9 AA9 THR C   22  GLY C   35  1                                  14    
HELIX   10 AB1 PRO C   37  ASP C   39  5                                   3    
HELIX   11 AB2 LEU C   56  ASN C   60  5                                   5    
HELIX   12 AB3 LEU D    4  LEU D   11  1                                   8    
HELIX   13 AB4 GLY D   34  VAL D   43  1                                  10    
HELIX   14 AB5 ASN D   66  ALA D   82  1                                  17    
HELIX   15 AB6 ALA E    2  ASP E   16  1                                  15    
HELIX   16 AB7 LEU E   86  ARG E   90  5                                   5    
HELIX   17 AB8 THR E   98  CYS E  111  1                                  14    
HELIX   18 AB9 VAL E  120  ASP E  130  1                                  11    
HELIX   19 AC1 ASP E  130  TYR E  145  1                                  16    
HELIX   20 AC2 THR F   22  GLY F   35  1                                  14    
HELIX   21 AC3 PRO F   37  ASP F   39  5                                   3    
SHEET    1 AA1 2 PRO A  23  THR A  25  0                                        
SHEET    2 AA1 2 ASN A  31  CYS A  33 -1  O  PHE A  32   N  VAL A  24           
SHEET    1 AA2 2 TYR A  48  LEU A  49  0                                        
SHEET    2 AA2 2 VAL A  56  TYR A  57 -1  O  TYR A  57   N  TYR A  48           
SHEET    1 AA3 4 CYS B  21  GLY B  24  0                                        
SHEET    2 AA3 4 HIS B  32  MET B  38 -1  O  THR B  36   N  ARG B  22           
SHEET    3 AA3 4 VAL B  49  HIS B  55 -1  O  VAL B  54   N  TRP B  33           
SHEET    4 AA3 4 LYS B  66  PHE B  69 -1  O  LYS B  66   N  HIS B  55           
SHEET    1 AA4 5 THR C  12  GLU C  16  0                                        
SHEET    2 AA4 5 GLN C   2  LYS C   6 -1  N  ILE C   3   O  LEU C  15           
SHEET    3 AA4 5 THR C  66  LEU C  71  1  O  LEU C  67   N  PHE C   4           
SHEET    4 AA4 5 GLN C  41  PHE C  45 -1  N  ILE C  44   O  HIS C  68           
SHEET    5 AA4 5 LYS C  48  GLN C  49 -1  O  LYS C  48   N  PHE C  45           
SHEET    1 AA5 2 PRO D  23  THR D  25  0                                        
SHEET    2 AA5 2 ASN D  31  CYS D  33 -1  O  PHE D  32   N  VAL D  24           
SHEET    1 AA6 2 TYR D  48  LEU D  49  0                                        
SHEET    2 AA6 2 VAL D  56  TYR D  57 -1  O  TYR D  57   N  TYR D  48           
SHEET    1 AA7 4 CYS E  21  PRO E  25  0                                        
SHEET    2 AA7 4 HIS E  32  MET E  38 -1  O  GLN E  34   N  GLY E  24           
SHEET    3 AA7 4 VAL E  49  HIS E  55 -1  O  VAL E  54   N  TRP E  33           
SHEET    4 AA7 4 LYS E  66  PHE E  69 -1  O  ALA E  68   N  THR E  53           
SHEET    1 AA8 5 THR F  12  GLU F  16  0                                        
SHEET    2 AA8 5 GLN F   2  LYS F   6 -1  N  ILE F   3   O  LEU F  15           
SHEET    3 AA8 5 THR F  66  LEU F  71  1  O  LEU F  67   N  LYS F   6           
SHEET    4 AA8 5 GLN F  41  PHE F  45 -1  N  ILE F  44   O  HIS F  68           
SHEET    5 AA8 5 LYS F  48  GLN F  49 -1  O  LYS F  48   N  PHE F  45           
LINK         SG  CYS A  13                ZN  L ZN A 101     1555   1555  2.48  
LINK         SG  CYS A  16                ZN  L ZN A 101     1555   1555  2.33  
LINK         SG  CYS A  28                ZN  L ZN A 102     1555   1555  2.27  
LINK         ND1 HIS A  30                ZN  L ZN A 102     1555   1555  2.07  
LINK         SG  CYS A  33                ZN  L ZN A 101     1555   1555  2.35  
LINK         SG  CYS A  36                ZN  L ZN A 101     1555   1555  2.35  
LINK         SG  CYS A  50                ZN  L ZN A 102     1555   1555  2.35  
LINK         SG  CYS A  53                ZN  L ZN A 102     1555   1555  2.33  
LINK         SG  CYS D  13                ZN  L ZN D 102     1555   1555  2.41  
LINK         SG  CYS D  16                ZN  L ZN D 102     1555   1555  2.33  
LINK         SG  CYS D  28                ZN  L ZN D 101     1555   1555  2.28  
LINK         ND1 HIS D  30                ZN  L ZN D 101     1555   1555  2.06  
LINK         SG  CYS D  33                ZN  L ZN D 102     1555   1555  2.31  
LINK         SG  CYS D  36                ZN  L ZN D 102     1555   1555  2.34  
LINK         SG  CYS D  50                ZN  L ZN D 101     1555   1555  2.38  
LINK         SG  CYS D  53                ZN  L ZN D 101     1555   1555  2.27  
CISPEP   1 TYR B   60    PRO B   61          0         3.01                     
CISPEP   2 TYR E   60    PRO E   61          0         1.00                     
SITE     1 AC1  5 CYS A  13  CYS A  16  LYS A  21  CYS A  33                    
SITE     2 AC1  5 CYS A  36                                                     
SITE     1 AC2  4 CYS A  28  HIS A  30  CYS A  50  CYS A  53                    
SITE     1 AC3  4 CYS D  28  HIS D  30  CYS D  50  CYS D  53                    
SITE     1 AC4  4 CYS D  13  CYS D  16  CYS D  33  CYS D  36                    
SITE     1 AC5 13 HIS E  75  ASN E  77  ILE E  78  ILE E  84                    
SITE     2 AC5 13 LEU E  86  ASP E 117  PRO E 118  LEU E 119                    
SITE     3 AC5 13 VAL E 120  ILE E 123  TYR E 134  ARG F  74                    
SITE     4 AC5 13 GLY F  75                                                     
CRYST1   60.480   71.700  160.430  90.00  90.00  90.00 P 21 21 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      0.016534  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013947  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006233        0.00000                         
ATOM   2992  N   MET E   1       7.237 -64.918  27.585  1.00 58.60           N  
ATOM   2993  CA  MET E   1       5.950 -65.249  28.182  1.00 74.77           C  
ATOM   2994  C   MET E   1       5.206 -66.254  27.299  1.00 66.04           C  
ATOM   2995  O   MET E   1       5.283 -66.192  26.073  1.00 58.79           O  
ATOM   2996  CB  MET E   1       5.123 -63.980  28.397  1.00 73.76           C  
ATOM   2997  CG  MET E   1       4.107 -64.071  29.523  1.00 75.41           C  
ATOM   2998  SD  MET E   1       4.299 -62.718  30.698  1.00 83.33           S  
ATOM   2999  CE  MET E   1       4.342 -61.315  29.586  1.00 75.54           C  
ATOM   3000  N   ALA E   2       4.473 -67.168  27.940  1.00 60.02           N  
ATOM   3001  CA  ALA E   2       4.046 -68.389  27.266  1.00 56.04           C  
ATOM   3002  C   ALA E   2       2.879 -68.161  26.309  1.00 58.57           C  
ATOM   3003  O   ALA E   2       2.850 -68.749  25.222  1.00 56.07           O  
ATOM   3004  CB  ALA E   2       3.672 -69.450  28.301  1.00 51.18           C  
ATOM   3005  N   LEU E   3       1.909 -67.327  26.693  1.00 57.90           N  
ATOM   3006  CA  LEU E   3       0.659 -67.256  25.939  1.00 57.36           C  
ATOM   3007  C   LEU E   3       0.882 -66.761  24.514  1.00 58.12           C  
ATOM   3008  O   LEU E   3       0.238 -67.247  23.575  1.00 56.57           O  
ATOM   3009  CB  LEU E   3      -0.344 -66.363  26.668  1.00 61.48           C  
ATOM   3010  CG  LEU E   3      -1.703 -66.178  25.983  1.00 59.18           C  
ATOM   3011  CD1 LEU E   3      -2.383 -67.520  25.749  1.00 57.16           C  
ATOM   3012  CD2 LEU E   3      -2.599 -65.249  26.790  1.00 62.38           C  
ATOM   3013  N   LYS E   4       1.793 -65.799  24.329  1.00 53.95           N  
ATOM   3014  CA  LYS E   4       2.024 -65.242  22.997  1.00 56.54           C  
ATOM   3015  C   LYS E   4       2.574 -66.298  22.045  1.00 54.40           C  
ATOM   3016  O   LYS E   4       2.135 -66.394  20.892  1.00 52.56           O  
ATOM   3017  CB  LYS E   4       2.979 -64.051  23.075  1.00 57.10           C  
ATOM   3018  CG  LYS E   4       2.329 -62.723  23.468  1.00 62.75           C  
ATOM   3019  CD  LYS E   4       1.837 -62.746  24.907  1.00 78.09           C  
ATOM   3020  CE  LYS E   4       2.950 -63.175  25.847  1.00 69.13           C  
ATOM   3021  NZ  LYS E   4       2.444 -63.911  27.040  1.00 59.76           N1+
ATOM   3022  N   ARG E   5       3.542 -67.093  22.511  1.00 51.06           N  
ATOM   3023  CA  ARG E   5       4.080 -68.171  21.691  1.00 51.69           C  
ATOM   3024  C   ARG E   5       2.996 -69.175  21.319  1.00 51.05           C  
ATOM   3025  O   ARG E   5       2.947 -69.655  20.179  1.00 50.20           O  
ATOM   3026  CB  ARG E   5       5.228 -68.859  22.431  1.00 50.33           C  
ATOM   3027  CG  ARG E   5       5.612 -70.232  21.904  1.00 52.39           C  
ATOM   3028  CD  ARG E   5       6.304 -70.164  20.558  1.00 45.66           C  
ATOM   3029  NE  ARG E   5       6.678 -71.499  20.092  1.00 56.36           N  
ATOM   3030  CZ  ARG E   5       7.878 -72.041  20.270  1.00 48.06           C  
ATOM   3031  NH1 ARG E   5       8.832 -71.363  20.893  1.00 44.57           N1+
ATOM   3032  NH2 ARG E   5       8.125 -73.261  19.814  1.00 56.90           N  
ATOM   3033  N   ILE E   6       2.102 -69.488  22.261  1.00 52.55           N  
ATOM   3034  CA  ILE E   6       1.010 -70.412  21.983  1.00 49.20           C  
ATOM   3035  C   ILE E   6       0.063 -69.825  20.942  1.00 52.37           C  
ATOM   3036  O   ILE E   6      -0.416 -70.532  20.047  1.00 51.20           O  
ATOM   3037  CB  ILE E   6       0.274 -70.770  23.288  1.00 53.70           C  
ATOM   3038  CG1 ILE E   6       1.223 -71.470  24.259  1.00 52.72           C  
ATOM   3039  CG2 ILE E   6      -0.936 -71.642  23.005  1.00 49.99           C  
ATOM   3040  CD1 ILE E   6       0.609 -71.761  25.606  1.00 56.39           C  
ATOM   3041  N   GLN E   7      -0.219 -68.524  21.044  1.00 58.04           N  
ATOM   3042  CA  GLN E   7      -1.124 -67.877  20.099  1.00 55.60           C  
ATOM   3043  C   GLN E   7      -0.574 -67.933  18.680  1.00 47.84           C  
ATOM   3044  O   GLN E   7      -1.301 -68.254  17.731  1.00 48.86           O  
ATOM   3045  CB  GLN E   7      -1.372 -66.427  20.520  1.00 53.80           C  
ATOM   3046  CG  GLN E   7      -2.176 -66.265  21.803  1.00 61.95           C  
ATOM   3047  CD  GLN E   7      -2.084 -64.863  22.380  1.00 69.13           C  
ATOM   3048  OE1 GLN E   7      -1.225 -64.070  21.985  1.00 71.69           O  
ATOM   3049  NE2 GLN E   7      -2.966 -64.548  23.322  1.00 68.31           N  
ATOM   3050  N   LYS E   8       0.714 -67.622  18.515  1.00 44.50           N  
ATOM   3051  CA  LYS E   8       1.289 -67.594  17.175  1.00 46.50           C  
ATOM   3052  C   LYS E   8       1.378 -68.993  16.577  1.00 56.58           C  
ATOM   3053  O   LYS E   8       1.138 -69.172  15.377  1.00 56.54           O  
ATOM   3054  CB  LYS E   8       2.663 -66.928  17.199  1.00 51.71           C  
ATOM   3055  CG  LYS E   8       3.192 -66.629  15.812  1.00 56.29           C  
ATOM   3056  CD  LYS E   8       4.297 -65.597  15.841  1.00 61.70           C  
ATOM   3057  CE  LYS E   8       4.433 -64.930  14.480  1.00 68.42           C  
ATOM   3058  NZ  LYS E   8       4.517 -65.935  13.383  1.00 71.84           N1+
ATOM   3059  N   GLU E   9       1.721 -69.992  17.395  1.00 55.07           N  
ATOM   3060  CA  GLU E   9       1.711 -71.368  16.904  1.00 51.67           C  
ATOM   3061  C   GLU E   9       0.325 -71.760  16.408  1.00 54.03           C  
ATOM   3062  O   GLU E   9       0.189 -72.409  15.365  1.00 54.35           O  
ATOM   3063  CB  GLU E   9       2.174 -72.333  17.994  1.00 48.04           C  
ATOM   3064  CG  GLU E   9       3.652 -72.268  18.332  1.00 51.96           C  
ATOM   3065  CD  GLU E   9       4.111 -73.475  19.130  1.00 55.46           C  
ATOM   3066  OE1 GLU E   9       3.680 -74.601  18.802  1.00 51.70           O  
ATOM   3067  OE2 GLU E   9       4.888 -73.302  20.093  1.00 53.51           O1-
ATOM   3068  N   LEU E  10      -0.717 -71.366  17.142  1.00 51.88           N  
ATOM   3069  CA  LEU E  10      -2.076 -71.717  16.741  1.00 57.12           C  
ATOM   3070  C   LEU E  10      -2.481 -70.995  15.462  1.00 54.96           C  
ATOM   3071  O   LEU E  10      -3.104 -71.596  14.577  1.00 52.89           O  
ATOM   3072  CB  LEU E  10      -3.052 -71.395  17.872  1.00 56.35           C  
ATOM   3073  CG  LEU E  10      -4.523 -71.711  17.593  1.00 60.01           C  
ATOM   3074  CD1 LEU E  10      -4.718 -73.199  17.331  1.00 58.21           C  
ATOM   3075  CD2 LEU E  10      -5.392 -71.247  18.751  1.00 55.99           C  
ATOM   3076  N   SER E  11      -2.134 -69.709  15.341  1.00 55.52           N  
ATOM   3077  CA  SER E  11      -2.518 -68.949  14.154  1.00 61.35           C  
ATOM   3078  C   SER E  11      -1.815 -69.475  12.909  1.00 62.76           C  
ATOM   3079  O   SER E  11      -2.429 -69.583  11.843  1.00 62.55           O  
ATOM   3080  CB  SER E  11      -2.212 -67.466  14.357  1.00 63.77           C  
ATOM   3081  OG  SER E  11      -0.815 -67.219  14.285  1.00 72.73           O  
ATOM   3082  N   ASP E  12      -0.527 -69.806  13.025  1.00 63.90           N  
ATOM   3083  CA  ASP E  12       0.168 -70.440  11.908  1.00 67.92           C  
ATOM   3084  C   ASP E  12      -0.383 -71.833  11.640  1.00 65.54           C  
ATOM   3085  O   ASP E  12      -0.391 -72.287  10.488  1.00 57.65           O  
ATOM   3086  CB  ASP E  12       1.672 -70.506  12.187  1.00 69.11           C  
ATOM   3087  CG  ASP E  12       2.277 -69.140  12.462  1.00 78.22           C  
ATOM   3088  OD1 ASP E  12       1.657 -68.118  12.092  1.00 83.14           O  
ATOM   3089  OD2 ASP E  12       3.381 -69.088  13.047  1.00 76.22           O1-
ATOM   3090  N   LEU E  13      -0.852 -72.523  12.682  1.00 60.85           N  
ATOM   3091  CA  LEU E  13      -1.453 -73.837  12.498  1.00 58.62           C  
ATOM   3092  C   LEU E  13      -2.808 -73.738  11.818  1.00 67.98           C  
ATOM   3093  O   LEU E  13      -3.201 -74.644  11.078  1.00 74.87           O  
ATOM   3094  CB  LEU E  13      -1.578 -74.537  13.854  1.00 61.23           C  
ATOM   3095  CG  LEU E  13      -1.688 -76.058  13.884  1.00 63.89           C  
ATOM   3096  CD1 LEU E  13      -0.475 -76.695  13.236  1.00 58.91           C  
ATOM   3097  CD2 LEU E  13      -1.834 -76.524  15.319  1.00 68.90           C  
ATOM   3098  N   GLN E  14      -3.540 -72.648  12.057  1.00 63.71           N  
ATOM   3099  CA  GLN E  14      -4.821 -72.436  11.396  1.00 62.77           C  
ATOM   3100  C   GLN E  14      -4.643 -71.908   9.978  1.00 67.55           C  
ATOM   3101  O   GLN E  14      -5.419 -72.254   9.084  1.00 73.25           O  
ATOM   3102  CB  GLN E  14      -5.683 -71.476  12.215  1.00 55.13           C  
ATOM   3103  CG  GLN E  14      -6.154 -72.042  13.546  1.00 51.85           C  
ATOM   3104  CD  GLN E  14      -6.677 -70.969  14.482  1.00 58.76           C  
ATOM   3105  OE1 GLN E  14      -6.479 -69.775  14.248  1.00 65.65           O  
ATOM   3106  NE2 GLN E  14      -7.347 -71.389  15.549  1.00 53.92           N  
ATOM   3107  N   ARG E  15      -3.626 -71.067   9.760  1.00 69.59           N  
ATOM   3108  CA  ARG E  15      -3.381 -70.537   8.421  1.00 69.83           C  
ATOM   3109  C   ARG E  15      -2.972 -71.641   7.456  1.00 75.18           C  
ATOM   3110  O   ARG E  15      -3.297 -71.581   6.266  1.00 77.98           O  
ATOM   3111  CB  ARG E  15      -2.305 -69.452   8.474  1.00 66.83           C  
ATOM   3112  CG  ARG E  15      -2.045 -68.775   7.137  1.00 77.12           C  
ATOM   3113  CD  ARG E  15      -3.305 -68.105   6.608  1.00 87.57           C  
ATOM   3114  NE  ARG E  15      -3.195 -67.761   5.193  1.00 89.47           N  
ATOM   3115  CZ  ARG E  15      -2.704 -66.617   4.731  1.00 88.88           C  
ATOM   3116  NH1 ARG E  15      -2.643 -66.397   3.424  1.00 86.36           N1+
ATOM   3117  NH2 ARG E  15      -2.267 -65.691   5.574  1.00 83.09           N  
ATOM   3118  N   ASP E  16      -2.266 -72.652   7.945  1.00 82.61           N  
ATOM   3119  CA  ASP E  16      -1.868 -73.789   7.130  1.00 85.16           C  
ATOM   3120  C   ASP E  16      -2.028 -75.081   7.920  1.00 86.44           C  
ATOM   3121  O   ASP E  16      -1.313 -75.299   8.907  1.00 84.18           O  
ATOM   3122  CB  ASP E  16      -0.428 -73.638   6.651  1.00 83.61           C  
ATOM   3123  CG  ASP E  16       0.111 -74.913   6.031  1.00 90.72           C  
ATOM   3124  OD1 ASP E  16       0.621 -75.772   6.784  1.00 94.96           O1-
ATOM   3125  OD2 ASP E  16       0.019 -75.058   4.793  1.00 95.91           O  
ATOM   3126  N   PRO E  17      -2.947 -75.956   7.525  1.00 88.75           N  
ATOM   3127  CA  PRO E  17      -3.117 -77.221   8.236  1.00 83.45           C  
ATOM   3128  C   PRO E  17      -2.127 -78.259   7.743  1.00 82.84           C  
ATOM   3129  O   PRO E  17      -2.150 -78.640   6.564  1.00 80.14           O  
ATOM   3130  CB  PRO E  17      -4.567 -77.623   7.904  1.00 86.31           C  
ATOM   3131  CG  PRO E  17      -5.079 -76.580   6.912  1.00 86.93           C  
ATOM   3132  CD  PRO E  17      -3.890 -75.831   6.410  1.00 80.67           C  
ATOM   3133  N   PRO E  18      -1.234 -78.731   8.608  1.00 79.58           N  
ATOM   3134  CA  PRO E  18      -0.301 -79.784   8.196  1.00 71.51           C  
ATOM   3135  C   PRO E  18      -1.029 -81.099   7.963  1.00 72.70           C  
ATOM   3136  O   PRO E  18      -2.026 -81.412   8.618  1.00 74.98           O  
ATOM   3137  CB  PRO E  18       0.668 -79.882   9.380  1.00 69.36           C  
ATOM   3138  CG  PRO E  18      -0.115 -79.392  10.548  1.00 68.67           C  
ATOM   3139  CD  PRO E  18      -1.026 -78.322  10.009  1.00 71.78           C  
ATOM   3140  N   ALA E  19      -0.510 -81.873   7.008  1.00 64.73           N  
ATOM   3141  CA  ALA E  19      -1.167 -83.116   6.616  1.00 66.64           C  
ATOM   3142  C   ALA E  19      -1.102 -84.184   7.699  1.00 70.93           C  
ATOM   3143  O   ALA E  19      -1.928 -85.102   7.692  1.00 72.52           O  
ATOM   3144  CB  ALA E  19      -0.548 -83.649   5.324  1.00 71.27           C  
ATOM   3145  N   HIS E  20      -0.153 -84.083   8.628  1.00 73.57           N  
ATOM   3146  CA  HIS E  20       0.099 -85.153   9.580  1.00 71.67           C  
ATOM   3147  C   HIS E  20      -0.722 -85.046  10.860  1.00 69.78           C  
ATOM   3148  O   HIS E  20      -0.718 -85.994  11.655  1.00 66.09           O  
ATOM   3149  CB  HIS E  20       1.589 -85.197   9.941  1.00 65.75           C  
ATOM   3150  CG  HIS E  20       2.092 -83.945  10.590  1.00 67.86           C  
ATOM   3151  ND1 HIS E  20       2.696 -82.930   9.881  1.00 65.41           N  
ATOM   3152  CD2 HIS E  20       2.091 -83.549  11.887  1.00 61.01           C  
ATOM   3153  CE1 HIS E  20       3.042 -81.960  10.709  1.00 65.77           C  
ATOM   3154  NE2 HIS E  20       2.686 -82.312  11.933  1.00 61.26           N  
ATOM   3155  N   CYS E  21      -1.426 -83.939  11.086  1.00 66.83           N  
ATOM   3156  CA  CYS E  21      -2.136 -83.773  12.348  1.00 63.65           C  
ATOM   3157  C   CYS E  21      -3.191 -82.682  12.206  1.00 67.44           C  
ATOM   3158  O   CYS E  21      -3.321 -82.038  11.161  1.00 66.48           O  
ATOM   3159  CB  CYS E  21      -1.168 -83.445  13.486  1.00 65.11           C  
ATOM   3160  SG  CYS E  21      -0.469 -81.779  13.404  1.00 75.27           S  
ATOM   3161  N   ARG E  22      -3.957 -82.500  13.281  1.00 62.53           N  
ATOM   3162  CA  ARG E  22      -4.882 -81.384  13.446  1.00 61.50           C  
ATOM   3163  C   ARG E  22      -4.954 -81.090  14.933  1.00 58.42           C  
ATOM   3164  O   ARG E  22      -5.276 -81.982  15.723  1.00 68.13           O  
ATOM   3165  CB  ARG E  22      -6.271 -81.712  12.895  1.00 69.68           C  
ATOM   3166  CG  ARG E  22      -7.371 -80.822  13.474  1.00 75.48           C  
ATOM   3167  CD  ARG E  22      -8.651 -81.606  13.724  1.00 80.93           C  
ATOM   3168  NE  ARG E  22      -9.500 -80.964  14.726  1.00 84.63           N  
ATOM   3169  CZ  ARG E  22      -9.444 -81.219  16.032  1.00 85.23           C  
ATOM   3170  NH1 ARG E  22      -8.575 -82.104  16.503  1.00 74.57           N1+
ATOM   3171  NH2 ARG E  22     -10.254 -80.585  16.871  1.00 78.76           N  
ATOM   3172  N   ALA E  23      -4.649 -79.856  15.321  1.00 62.18           N  
ATOM   3173  CA  ALA E  23      -4.591 -79.495  16.728  1.00 66.48           C  
ATOM   3174  C   ALA E  23      -5.340 -78.191  16.962  1.00 66.14           C  
ATOM   3175  O   ALA E  23      -5.539 -77.387  16.049  1.00 70.81           O  
ATOM   3176  CB  ALA E  23      -3.143 -79.365  17.217  1.00 62.53           C  
ATOM   3177  N   GLY E  24      -5.746 -77.996  18.213  1.00 62.49           N  
ATOM   3178  CA  GLY E  24      -6.456 -76.808  18.621  1.00 62.69           C  
ATOM   3179  C   GLY E  24      -6.855 -76.880  20.080  1.00 63.39           C  
ATOM   3180  O   GLY E  24      -6.876 -77.958  20.686  1.00 69.73           O  
ATOM   3181  N   PRO E  25      -7.173 -75.737  20.677  1.00 65.69           N  
ATOM   3182  CA  PRO E  25      -7.562 -75.722  22.092  1.00 67.46           C  
ATOM   3183  C   PRO E  25      -8.889 -76.430  22.308  1.00 69.26           C  
ATOM   3184  O   PRO E  25      -9.646 -76.714  21.373  1.00 68.45           O  
ATOM   3185  CB  PRO E  25      -7.659 -74.229  22.421  1.00 64.26           C  
ATOM   3186  CG  PRO E  25      -7.925 -73.574  21.107  1.00 61.80           C  
ATOM   3187  CD  PRO E  25      -7.186 -74.388  20.083  1.00 61.29           C  
ATOM   3188  N   VAL E  26      -9.168 -76.723  23.576  1.00 68.34           N  
ATOM   3189  CA  VAL E  26     -10.407 -77.400  23.946  1.00 75.20           C  
ATOM   3190  C   VAL E  26     -11.540 -76.406  24.152  1.00 78.41           C  
ATOM   3191  O   VAL E  26     -12.625 -76.556  23.583  1.00 74.44           O  
ATOM   3192  CB  VAL E  26     -10.184 -78.273  25.202  1.00 77.36           C  
ATOM   3193  CG1 VAL E  26      -9.553 -79.603  24.819  1.00 66.55           C  
ATOM   3194  CG2 VAL E  26      -9.315 -77.547  26.221  1.00 69.10           C  
ATOM   3195  N   GLY E  27     -11.310 -75.372  24.957  1.00 78.23           N  
ATOM   3196  CA  GLY E  27     -12.312 -74.351  25.184  1.00 75.78           C  
ATOM   3197  C   GLY E  27     -11.739 -72.955  25.098  1.00 79.59           C  
ATOM   3198  O   GLY E  27     -11.240 -72.543  24.044  1.00 79.00           O  
ATOM   3199  N   ASP E  28     -11.804 -72.212  26.199  1.00 85.56           N  
ATOM   3200  CA  ASP E  28     -11.244 -70.871  26.247  1.00 84.72           C  
ATOM   3201  C   ASP E  28      -9.772 -70.858  26.623  1.00 85.46           C  
ATOM   3202  O   ASP E  28      -9.073 -69.889  26.308  1.00 87.21           O  
ATOM   3203  CB  ASP E  28     -12.024 -70.010  27.245  1.00 90.55           C  
ATOM   3204  CG  ASP E  28     -13.519 -70.053  27.010  1.00 99.65           C  
ATOM   3205  OD1 ASP E  28     -13.936 -70.158  25.837  1.00100.59           O  
ATOM   3206  OD2 ASP E  28     -14.276 -69.986  28.003  1.00104.94           O1-
ATOM   3207  N   ASP E  29      -9.283 -71.906  27.281  1.00 80.83           N  
ATOM   3208  CA  ASP E  29      -7.903 -71.969  27.746  1.00 75.68           C  
ATOM   3209  C   ASP E  29      -7.031 -72.508  26.618  1.00 75.98           C  
ATOM   3210  O   ASP E  29      -7.158 -73.674  26.227  1.00 75.82           O  
ATOM   3211  CB  ASP E  29      -7.798 -72.848  28.990  1.00 79.04           C  
ATOM   3212  CG  ASP E  29      -6.515 -72.609  29.764  1.00 81.46           C  
ATOM   3213  OD1 ASP E  29      -5.608 -71.934  29.234  1.00 80.34           O  
ATOM   3214  OD2 ASP E  29      -6.415 -73.107  30.906  1.00 81.66           O1-
ATOM   3215  N   LEU E  30      -6.147 -71.660  26.093  1.00 75.69           N  
ATOM   3216  CA  LEU E  30      -5.210 -72.084  25.060  1.00 75.25           C  
ATOM   3217  C   LEU E  30      -4.029 -72.864  25.622  1.00 67.65           C  
ATOM   3218  O   LEU E  30      -3.211 -73.361  24.841  1.00 63.87           O  
ATOM   3219  CB  LEU E  30      -4.705 -70.872  24.268  1.00 67.43           C  
ATOM   3220  CG  LEU E  30      -5.725 -70.171  23.364  1.00 67.17           C  
ATOM   3221  CD1 LEU E  30      -6.490 -69.092  24.120  1.00 73.10           C  
ATOM   3222  CD2 LEU E  30      -5.048 -69.601  22.123  1.00 63.19           C  
ATOM   3223  N   PHE E  31      -3.920 -72.981  26.945  1.00 62.29           N  
ATOM   3224  CA  PHE E  31      -2.897 -73.819  27.556  1.00 67.57           C  
ATOM   3225  C   PHE E  31      -3.263 -75.297  27.546  1.00 62.94           C  
ATOM   3226  O   PHE E  31      -2.423 -76.126  27.912  1.00 60.25           O  
ATOM   3227  CB  PHE E  31      -2.624 -73.360  28.990  1.00 65.34           C  
ATOM   3228  CG  PHE E  31      -1.817 -72.094  29.082  1.00 68.23           C  
ATOM   3229  CD1 PHE E  31      -2.437 -70.856  29.012  1.00 70.17           C  
ATOM   3230  CD2 PHE E  31      -0.441 -72.143  29.233  1.00 62.47           C  
ATOM   3231  CE1 PHE E  31      -1.695 -69.688  29.096  1.00 63.75           C  
ATOM   3232  CE2 PHE E  31       0.304 -70.981  29.319  1.00 61.30           C  
ATOM   3233  CZ  PHE E  31      -0.324 -69.750  29.250  1.00 65.74           C  
ATOM   3234  N   HIS E  32      -4.489 -75.640  27.152  1.00 66.62           N  
ATOM   3235  CA  HIS E  32      -4.924 -77.028  27.032  1.00 65.49           C  
ATOM   3236  C   HIS E  32      -5.459 -77.234  25.622  1.00 60.88           C  
ATOM   3237  O   HIS E  32      -6.408 -76.556  25.214  1.00 63.32           O  
ATOM   3238  CB  HIS E  32      -5.993 -77.374  28.069  1.00 64.44           C  
ATOM   3239  CG  HIS E  32      -5.552 -77.174  29.487  1.00 71.42           C  
ATOM   3240  ND1 HIS E  32      -5.522 -75.936  30.092  1.00 78.71           N  
ATOM   3241  CD2 HIS E  32      -5.117 -78.058  30.416  1.00 72.80           C  
ATOM   3242  CE1 HIS E  32      -5.089 -76.066  31.333  1.00 79.35           C  
ATOM   3243  NE2 HIS E  32      -4.836 -77.341  31.556  1.00 85.04           N  
ATOM   3244  N   TRP E  33      -4.852 -78.159  24.886  1.00 58.20           N  
ATOM   3245  CA  TRP E  33      -5.230 -78.437  23.512  1.00 56.17           C  
ATOM   3246  C   TRP E  33      -5.637 -79.896  23.357  1.00 60.18           C  
ATOM   3247  O   TRP E  33      -5.342 -80.745  24.203  1.00 61.39           O  
ATOM   3248  CB  TRP E  33      -4.087 -78.142  22.530  1.00 60.73           C  
ATOM   3249  CG  TRP E  33      -3.767 -76.694  22.340  1.00 55.52           C  
ATOM   3250  CD1 TRP E  33      -4.109 -75.658  23.156  1.00 58.38           C  
ATOM   3251  CD2 TRP E  33      -3.037 -76.119  21.249  1.00 55.12           C  
ATOM   3252  NE1 TRP E  33      -3.633 -74.474  22.644  1.00 54.78           N  
ATOM   3253  CE2 TRP E  33      -2.975 -74.731  21.473  1.00 58.57           C  
ATOM   3254  CE3 TRP E  33      -2.433 -76.647  20.102  1.00 53.26           C  
ATOM   3255  CZ2 TRP E  33      -2.326 -73.862  20.596  1.00 59.22           C  
ATOM   3256  CZ3 TRP E  33      -1.793 -75.785  19.234  1.00 61.17           C  
ATOM   3257  CH2 TRP E  33      -1.743 -74.408  19.485  1.00 61.96           C  
ATOM   3258  N   GLN E  34      -6.313 -80.172  22.249  1.00 61.59           N  
ATOM   3259  CA  GLN E  34      -6.611 -81.524  21.804  1.00 63.38           C  
ATOM   3260  C   GLN E  34      -6.083 -81.687  20.387  1.00 63.39           C  
ATOM   3261  O   GLN E  34      -6.421 -80.895  19.500  1.00 71.56           O  
ATOM   3262  CB  GLN E  34      -8.111 -81.814  21.842  1.00 70.23           C  
ATOM   3263  CG  GLN E  34      -8.508 -83.059  21.066  1.00 67.28           C  
ATOM   3264  CD  GLN E  34     -10.005 -83.287  21.043  1.00 70.26           C  
ATOM   3265  OE1 GLN E  34     -10.700 -83.019  22.025  1.00 72.49           O  
ATOM   3266  NE2 GLN E  34     -10.514 -83.774  19.918  1.00 72.84           N  
ATOM   3267  N   ALA E  35      -5.255 -82.703  20.180  1.00 61.00           N  
ATOM   3268  CA  ALA E  35      -4.656 -82.962  18.882  1.00 58.56           C  
ATOM   3269  C   ALA E  35      -5.082 -84.336  18.384  1.00 59.80           C  
ATOM   3270  O   ALA E  35      -5.480 -85.207  19.160  1.00 66.11           O  
ATOM   3271  CB  ALA E  35      -3.128 -82.877  18.948  1.00 60.23           C  
ATOM   3272  N   THR E  36      -4.989 -84.519  17.070  1.00 56.76           N  
ATOM   3273  CA  THR E  36      -5.275 -85.799  16.439  1.00 62.08           C  
ATOM   3274  C   THR E  36      -4.267 -86.028  15.322  1.00 66.50           C  
ATOM   3275  O   THR E  36      -4.103 -85.173  14.447  1.00 72.04           O  
ATOM   3276  CB  THR E  36      -6.711 -85.856  15.889  1.00 66.83           C  
ATOM   3277  OG1 THR E  36      -6.833 -86.948  14.970  1.00 71.61           O  
ATOM   3278  CG2 THR E  36      -7.082 -84.561  15.186  1.00 67.29           C  
ATOM   3279  N   ILE E  37      -3.586 -87.171  15.364  1.00 62.03           N  
ATOM   3280  CA  ILE E  37      -2.569 -87.507  14.379  1.00 64.36           C  
ATOM   3281  C   ILE E  37      -3.010 -88.754  13.629  1.00 63.63           C  
ATOM   3282  O   ILE E  37      -3.751 -89.591  14.156  1.00 69.02           O  
ATOM   3283  CB  ILE E  37      -1.181 -87.720  15.021  1.00 64.03           C  
ATOM   3284  CG1 ILE E  37      -1.194 -88.937  15.944  1.00 62.58           C  
ATOM   3285  CG2 ILE E  37      -0.752 -86.477  15.789  1.00 58.66           C  
ATOM   3286  CD1 ILE E  37       0.141 -89.229  16.592  1.00 59.13           C  
ATOM   3287  N   MET E  38      -2.551 -88.871  12.389  1.00 64.67           N  
ATOM   3288  CA  MET E  38      -2.851 -90.022  11.554  1.00 61.58           C  
ATOM   3289  C   MET E  38      -1.678 -90.989  11.566  1.00 68.69           C  
ATOM   3290  O   MET E  38      -0.514 -90.571  11.591  1.00 72.97           O  
ATOM   3291  CB  MET E  38      -3.166 -89.593  10.121  1.00 71.47           C  
ATOM   3292  CG  MET E  38      -4.401 -88.721   9.992  1.00 77.38           C  
ATOM   3293  SD  MET E  38      -5.467 -89.244   8.635  1.00 94.07           S  
ATOM   3294  CE  MET E  38      -5.889 -90.906   9.158  1.00 64.82           C  
ATOM   3295  N   GLY E  39      -1.990 -92.280  11.553  1.00 64.87           N  
ATOM   3296  CA  GLY E  39      -0.974 -93.302  11.529  1.00 60.43           C  
ATOM   3297  C   GLY E  39      -0.184 -93.282  10.240  1.00 64.28           C  
ATOM   3298  O   GLY E  39      -0.666 -92.835   9.195  1.00 70.59           O  
ATOM   3299  N   PRO E  40       1.059 -93.754  10.295  1.00 67.13           N  
ATOM   3300  CA  PRO E  40       1.867 -93.828   9.084  1.00 62.13           C  
ATOM   3301  C   PRO E  40       1.188 -94.692   8.038  1.00 64.24           C  
ATOM   3302  O   PRO E  40       0.393 -95.590   8.370  1.00 67.28           O  
ATOM   3303  CB  PRO E  40       3.179 -94.454   9.574  1.00 64.89           C  
ATOM   3304  CG  PRO E  40       3.256 -94.044  11.010  1.00 64.52           C  
ATOM   3305  CD  PRO E  40       1.838 -94.080  11.506  1.00 62.41           C  
ATOM   3306  N   PRO E  41       1.482 -94.460   6.756  1.00 74.48           N  
ATOM   3307  CA  PRO E  41       0.678 -95.073   5.688  1.00 74.64           C  
ATOM   3308  C   PRO E  41       0.962 -96.551   5.452  1.00 74.65           C  
ATOM   3309  O   PRO E  41       0.082 -97.278   4.988  1.00 87.45           O  
ATOM   3310  CB  PRO E  41       1.050 -94.237   4.457  1.00 69.33           C  
ATOM   3311  CG  PRO E  41       2.447 -93.798   4.731  1.00 79.73           C  
ATOM   3312  CD  PRO E  41       2.522 -93.568   6.220  1.00 77.53           C  
ATOM   3313  N   ASP E  42       2.175 -97.002   5.736  1.00 70.62           N  
ATOM   3314  CA  ASP E  42       2.590 -98.380   5.477  1.00 75.81           C  
ATOM   3315  C   ASP E  42       3.098 -98.991   6.778  1.00 75.27           C  
ATOM   3316  O   ASP E  42       4.304 -99.191   6.951  1.00 73.12           O  
ATOM   3317  CB  ASP E  42       3.663 -98.435   4.374  1.00 75.49           C  
ATOM   3318  CG  ASP E  42       3.107 -98.144   2.993  1.00 85.74           C  
ATOM   3319  OD1 ASP E  42       2.027 -97.526   2.897  1.00 87.04           O  
ATOM   3320  OD2 ASP E  42       3.758 -98.532   1.998  1.00 88.40           O1-
ATOM   3321  N   SER E  43       2.184 -99.302   7.690  1.00 70.96           N  
ATOM   3322  CA  SER E  43       2.571 -99.808   9.001  1.00 72.15           C  
ATOM   3323  C   SER E  43       1.384-100.536   9.621  1.00 68.62           C  
ATOM   3324  O   SER E  43       0.387-100.827   8.953  1.00 72.44           O  
ATOM   3325  CB  SER E  43       3.059 -98.672   9.902  1.00 62.35           C  
ATOM   3326  OG  SER E  43       2.015 -97.754  10.174  1.00 62.44           O  
ATOM   3327  N   ALA E  44       1.499-100.832  10.914  1.00 67.56           N  
ATOM   3328  CA  ALA E  44       0.404-101.423  11.666  1.00 63.00           C  
ATOM   3329  C   ALA E  44      -0.628-100.393  12.099  1.00 64.64           C  
ATOM   3330  O   ALA E  44      -1.686-100.777  12.614  1.00 63.70           O  
ATOM   3331  CB  ALA E  44       0.952-102.155  12.892  1.00 62.02           C  
ATOM   3332  N   TYR E  45      -0.356 -99.103  11.897  1.00 61.97           N  
ATOM   3333  CA  TYR E  45      -1.252 -98.026  12.303  1.00 59.53           C  
ATOM   3334  C   TYR E  45      -1.908 -97.343  11.107  1.00 60.93           C  
ATOM   3335  O   TYR E  45      -2.288 -96.173  11.191  1.00 62.05           O  
ATOM   3336  CB  TYR E  45      -0.500 -97.000  13.148  1.00 61.16           C  
ATOM   3337  CG  TYR E  45       0.352 -97.608  14.233  1.00 61.72           C  
ATOM   3338  CD1 TYR E  45      -0.177 -97.862  15.491  1.00 60.21           C  
ATOM   3339  CD2 TYR E  45       1.684 -97.925  14.001  1.00 56.06           C  
ATOM   3340  CE1 TYR E  45       0.595 -98.417  16.485  1.00 57.45           C  
ATOM   3341  CE2 TYR E  45       2.462 -98.476  14.989  1.00 53.92           C  
ATOM   3342  CZ  TYR E  45       1.914 -98.721  16.226  1.00 54.42           C  
ATOM   3343  OH  TYR E  45       2.691 -99.270  17.208  1.00 50.89           O  
ATOM   3344  N   GLN E  46      -2.039 -98.061   9.992  1.00 65.38           N  
ATOM   3345  CA  GLN E  46      -2.655 -97.500   8.797  1.00 64.12           C  
ATOM   3346  C   GLN E  46      -4.083 -97.055   9.076  1.00 66.26           C  
ATOM   3347  O   GLN E  46      -4.829 -97.704   9.818  1.00 73.58           O  
ATOM   3348  CB  GLN E  46      -2.657 -98.516   7.659  1.00 66.50           C  
ATOM   3349  CG  GLN E  46      -1.286 -98.944   7.202  1.00 69.92           C  
ATOM   3350  CD  GLN E  46      -1.336 -99.994   6.105  1.00 76.44           C  
ATOM   3351  OE1 GLN E  46      -2.369-100.188   5.465  1.00 83.42           O  
ATOM   3352  NE2 GLN E  46      -0.217-100.677   5.886  1.00 76.98           N  
ATOM   3353  N   GLY E  47      -4.459 -95.937   8.472  1.00 63.36           N  
ATOM   3354  CA  GLY E  47      -5.779 -95.375   8.650  1.00 60.37           C  
ATOM   3355  C   GLY E  47      -6.178 -95.030  10.070  1.00 74.74           C  
ATOM   3356  O   GLY E  47      -7.316 -94.579  10.273  1.00 73.50           O  
ATOM   3357  N   GLY E  48      -5.320 -95.217  11.067  1.00 66.89           N  
ATOM   3358  CA  GLY E  48      -5.711 -94.918  12.431  1.00 56.48           C  
ATOM   3359  C   GLY E  48      -5.753 -93.427  12.702  1.00 61.61           C  
ATOM   3360  O   GLY E  48      -5.007 -92.637  12.125  1.00 64.60           O  
ATOM   3361  N   VAL E  49      -6.657 -93.040  13.593  1.00 57.82           N  
ATOM   3362  CA  VAL E  49      -6.832 -91.657  14.015  1.00 59.49           C  
ATOM   3363  C   VAL E  49      -6.663 -91.647  15.522  1.00 62.51           C  
ATOM   3364  O   VAL E  49      -7.520 -92.161  16.253  1.00 70.90           O  
ATOM   3365  CB  VAL E  49      -8.197 -91.102  13.601  1.00 65.71           C  
ATOM   3366  CG1 VAL E  49      -8.386 -89.712  14.155  1.00 59.99           C  
ATOM   3367  CG2 VAL E  49      -8.328 -91.108  12.082  1.00 57.89           C  
ATOM   3368  N   PHE E  50      -5.559 -91.080  15.990  1.00 61.62           N  
ATOM   3369  CA  PHE E  50      -5.174 -91.130  17.395  1.00 59.43           C  
ATOM   3370  C   PHE E  50      -5.318 -89.741  17.999  1.00 57.40           C  
ATOM   3371  O   PHE E  50      -4.725 -88.781  17.498  1.00 63.83           O  
ATOM   3372  CB  PHE E  50      -3.741 -91.643  17.547  1.00 59.52           C  
ATOM   3373  CG  PHE E  50      -3.507 -92.980  16.905  1.00 53.79           C  
ATOM   3374  CD1 PHE E  50      -3.138 -93.071  15.570  1.00 49.46           C  
ATOM   3375  CD2 PHE E  50      -3.654 -94.150  17.636  1.00 52.26           C  
ATOM   3376  CE1 PHE E  50      -2.924 -94.306  14.977  1.00 58.03           C  
ATOM   3377  CE2 PHE E  50      -3.440 -95.386  17.051  1.00 49.93           C  
ATOM   3378  CZ  PHE E  50      -3.074 -95.465  15.720  1.00 54.15           C  
ATOM   3379  N   PHE E  51      -6.098 -89.643  19.065  1.00 51.49           N  
ATOM   3380  CA  PHE E  51      -6.292 -88.389  19.780  1.00 54.88           C  
ATOM   3381  C   PHE E  51      -5.232 -88.237  20.864  1.00 59.89           C  
ATOM   3382  O   PHE E  51      -4.782 -89.220  21.461  1.00 63.23           O  
ATOM   3383  CB  PHE E  51      -7.687 -88.330  20.406  1.00 59.06           C  
ATOM   3384  CG  PHE E  51      -8.810 -88.229  19.405  1.00 64.81           C  
ATOM   3385  CD1 PHE E  51      -9.153 -89.315  18.612  1.00 60.16           C  
ATOM   3386  CD2 PHE E  51      -9.535 -87.054  19.273  1.00 67.25           C  
ATOM   3387  CE1 PHE E  51     -10.186 -89.224  17.696  1.00 59.53           C  
ATOM   3388  CE2 PHE E  51     -10.569 -86.959  18.364  1.00 62.33           C  
ATOM   3389  CZ  PHE E  51     -10.896 -88.045  17.573  1.00 66.06           C  
ATOM   3390  N   LEU E  52      -4.829 -86.991  21.113  1.00 59.11           N  
ATOM   3391  CA  LEU E  52      -3.839 -86.689  22.137  1.00 50.28           C  
ATOM   3392  C   LEU E  52      -4.258 -85.440  22.896  1.00 57.64           C  
ATOM   3393  O   LEU E  52      -5.076 -84.646  22.429  1.00 64.39           O  
ATOM   3394  CB  LEU E  52      -2.437 -86.486  21.543  1.00 53.28           C  
ATOM   3395  CG  LEU E  52      -1.765 -87.668  20.839  1.00 55.15           C  
ATOM   3396  CD1 LEU E  52      -2.110 -87.698  19.358  1.00 54.67           C  
ATOM   3397  CD2 LEU E  52      -0.259 -87.622  21.043  1.00 54.49           C  
ATOM   3398  N   THR E  53      -3.673 -85.274  24.080  1.00 57.10           N  
ATOM   3399  CA  THR E  53      -3.894 -84.110  24.924  1.00 56.90           C  
ATOM   3400  C   THR E  53      -2.588 -83.336  25.050  1.00 58.66           C  
ATOM   3401  O   THR E  53      -1.535 -83.928  25.313  1.00 66.28           O  
ATOM   3402  CB  THR E  53      -4.396 -84.517  26.312  1.00 61.69           C  
ATOM   3403  OG1 THR E  53      -5.659 -85.180  26.188  1.00 74.43           O  
ATOM   3404  CG2 THR E  53      -4.557 -83.297  27.211  1.00 49.04           C  
ATOM   3405  N   VAL E  54      -2.656 -82.021  24.855  1.00 57.45           N  
ATOM   3406  CA  VAL E  54      -1.497 -81.145  24.953  1.00 52.48           C  
ATOM   3407  C   VAL E  54      -1.749 -80.155  26.078  1.00 52.73           C  
ATOM   3408  O   VAL E  54      -2.739 -79.416  26.050  1.00 59.93           O  
ATOM   3409  CB  VAL E  54      -1.221 -80.412  23.629  1.00 49.16           C  
ATOM   3410  CG1 VAL E  54       0.036 -79.573  23.745  1.00 45.94           C  
ATOM   3411  CG2 VAL E  54      -1.102 -81.409  22.485  1.00 43.58           C  
ATOM   3412  N   HIS E  55      -0.858 -80.141  27.063  1.00 53.18           N  
ATOM   3413  CA  HIS E  55      -0.959 -79.254  28.217  1.00 59.35           C  
ATOM   3414  C   HIS E  55       0.315 -78.422  28.288  1.00 59.79           C  
ATOM   3415  O   HIS E  55       1.393 -78.954  28.575  1.00 56.44           O  
ATOM   3416  CB  HIS E  55      -1.173 -80.052  29.503  1.00 58.62           C  
ATOM   3417  CG  HIS E  55      -1.242 -79.206  30.734  1.00 63.43           C  
ATOM   3418  ND1 HIS E  55      -1.573 -77.867  30.704  1.00 72.92           N  
ATOM   3419  CD2 HIS E  55      -1.019 -79.506  32.038  1.00 67.81           C  
ATOM   3420  CE1 HIS E  55      -1.554 -77.382  31.931  1.00 70.50           C  
ATOM   3421  NE2 HIS E  55      -1.222 -78.355  32.759  1.00 75.45           N  
ATOM   3422  N   PHE E  56       0.189 -77.129  28.029  1.00 57.22           N  
ATOM   3423  CA  PHE E  56       1.347 -76.245  28.040  1.00 49.97           C  
ATOM   3424  C   PHE E  56       1.628 -75.765  29.459  1.00 53.47           C  
ATOM   3425  O   PHE E  56       0.705 -75.317  30.146  1.00 62.91           O  
ATOM   3426  CB  PHE E  56       1.118 -75.043  27.132  1.00 53.60           C  
ATOM   3427  CG  PHE E  56       0.902 -75.398  25.694  1.00 51.05           C  
ATOM   3428  CD1 PHE E  56       1.976 -75.493  24.824  1.00 51.73           C  
ATOM   3429  CD2 PHE E  56      -0.374 -75.617  25.202  1.00 55.83           C  
ATOM   3430  CE1 PHE E  56       1.783 -75.810  23.497  1.00 47.14           C  
ATOM   3431  CE2 PHE E  56      -0.572 -75.937  23.872  1.00 53.81           C  
ATOM   3432  CZ  PHE E  56       0.505 -76.032  23.020  1.00 46.43           C  
ATOM   3433  N   PRO E  57       2.870 -75.839  29.922  1.00 56.05           N  
ATOM   3434  CA  PRO E  57       3.209 -75.244  31.219  1.00 56.06           C  
ATOM   3435  C   PRO E  57       3.227 -73.725  31.137  1.00 59.84           C  
ATOM   3436  O   PRO E  57       3.141 -73.123  30.064  1.00 57.10           O  
ATOM   3437  CB  PRO E  57       4.601 -75.806  31.516  1.00 52.91           C  
ATOM   3438  CG  PRO E  57       5.170 -76.116  30.168  1.00 51.70           C  
ATOM   3439  CD  PRO E  57       4.011 -76.546  29.317  1.00 49.20           C  
ATOM   3440  N   THR E  58       3.342 -73.099  32.310  1.00 57.60           N  
ATOM   3441  CA  THR E  58       3.363 -71.642  32.367  1.00 62.55           C  
ATOM   3442  C   THR E  58       4.664 -71.056  31.837  1.00 56.84           C  
ATOM   3443  O   THR E  58       4.684 -69.890  31.428  1.00 58.54           O  
ATOM   3444  CB  THR E  58       3.131 -71.166  33.803  1.00 63.06           C  
ATOM   3445  OG1 THR E  58       4.197 -71.636  34.642  1.00 65.94           O  
ATOM   3446  CG2 THR E  58       1.802 -71.693  34.333  1.00 63.03           C  
ATOM   3447  N   ASP E  59       5.750 -71.832  31.831  1.00 57.51           N  
ATOM   3448  CA  ASP E  59       7.043 -71.372  31.347  1.00 54.37           C  
ATOM   3449  C   ASP E  59       7.358 -71.885  29.946  1.00 53.41           C  
ATOM   3450  O   ASP E  59       8.531 -71.989  29.573  1.00 54.02           O  
ATOM   3451  CB  ASP E  59       8.145 -71.774  32.327  1.00 51.43           C  
ATOM   3452  CG  ASP E  59       7.934 -73.163  32.906  1.00 59.44           C  
ATOM   3453  OD1 ASP E  59       7.219 -73.971  32.278  1.00 67.61           O  
ATOM   3454  OD2 ASP E  59       8.488 -73.447  33.989  1.00 61.92           O1-
ATOM   3455  N   TYR E  60       6.334 -72.216  29.163  1.00 50.90           N  
ATOM   3456  CA  TYR E  60       6.495 -72.594  27.764  1.00 49.79           C  
ATOM   3457  C   TYR E  60       7.047 -71.395  26.988  1.00 50.20           C  
ATOM   3458  O   TYR E  60       6.691 -70.257  27.287  1.00 55.39           O  
ATOM   3459  CB  TYR E  60       5.151 -73.061  27.195  1.00 46.73           C  
ATOM   3460  CG  TYR E  60       5.194 -73.614  25.789  1.00 43.47           C  
ATOM   3461  CD1 TYR E  60       5.623 -74.912  25.546  1.00 45.49           C  
ATOM   3462  CD2 TYR E  60       4.786 -72.844  24.708  1.00 48.32           C  
ATOM   3463  CE1 TYR E  60       5.659 -75.426  24.261  1.00 44.04           C  
ATOM   3464  CE2 TYR E  60       4.814 -73.348  23.420  1.00 47.56           C  
ATOM   3465  CZ  TYR E  60       5.252 -74.639  23.202  1.00 43.61           C  
ATOM   3466  OH  TYR E  60       5.284 -75.140  21.921  1.00 47.43           O  
ATOM   3467  N   PRO E  61       7.922 -71.634  25.993  1.00 51.37           N  
ATOM   3468  CA  PRO E  61       8.439 -72.919  25.508  1.00 47.30           C  
ATOM   3469  C   PRO E  61       9.770 -73.331  26.128  1.00 46.52           C  
ATOM   3470  O   PRO E  61      10.437 -74.221  25.594  1.00 42.04           O  
ATOM   3471  CB  PRO E  61       8.609 -72.656  24.014  1.00 45.62           C  
ATOM   3472  CG  PRO E  61       9.043 -71.228  23.968  1.00 49.40           C  
ATOM   3473  CD  PRO E  61       8.365 -70.523  25.132  1.00 47.15           C  
ATOM   3474  N   PHE E  62      10.156 -72.699  27.235  1.00 39.82           N  
ATOM   3475  CA  PHE E  62      11.408 -73.061  27.884  1.00 38.70           C  
ATOM   3476  C   PHE E  62      11.308 -74.389  28.626  1.00 46.76           C  
ATOM   3477  O   PHE E  62      12.341 -74.998  28.926  1.00 46.23           O  
ATOM   3478  CB  PHE E  62      11.846 -71.936  28.822  1.00 46.30           C  
ATOM   3479  CG  PHE E  62      11.870 -70.586  28.157  1.00 47.38           C  
ATOM   3480  CD1 PHE E  62      12.908 -70.235  27.312  1.00 43.19           C  
ATOM   3481  CD2 PHE E  62      10.840 -69.681  28.360  1.00 45.74           C  
ATOM   3482  CE1 PHE E  62      12.921 -69.002  26.686  1.00 46.27           C  
ATOM   3483  CE2 PHE E  62      10.852 -68.443  27.740  1.00 48.33           C  
ATOM   3484  CZ  PHE E  62      11.895 -68.107  26.903  1.00 45.45           C  
ATOM   3485  N   LYS E  63      10.094 -74.851  28.921  1.00 51.63           N  
ATOM   3486  CA  LYS E  63       9.844 -76.191  29.410  1.00 46.88           C  
ATOM   3487  C   LYS E  63       8.913 -76.906  28.442  1.00 48.36           C  
ATOM   3488  O   LYS E  63       8.010 -76.280  27.880  1.00 43.98           O  
ATOM   3489  CB  LYS E  63       9.218 -76.169  30.817  1.00 52.35           C  
ATOM   3490  CG  LYS E  63      10.138 -75.624  31.900  1.00 55.38           C  
ATOM   3491  CD  LYS E  63      11.358 -76.513  32.089  1.00 62.00           C  
ATOM   3492  CE  LYS E  63      12.263 -75.974  33.185  1.00 64.90           C  
ATOM   3493  NZ  LYS E  63      13.468 -76.822  33.388  1.00 67.42           N1+
ATOM   3494  N   PRO E  64       9.103 -78.206  28.221  1.00 48.55           N  
ATOM   3495  CA  PRO E  64       8.325 -78.915  27.192  1.00 49.06           C  
ATOM   3496  C   PRO E  64       6.867 -79.052  27.584  1.00 51.61           C  
ATOM   3497  O   PRO E  64       6.525 -79.043  28.780  1.00 54.66           O  
ATOM   3498  CB  PRO E  64       9.008 -80.294  27.124  1.00 47.58           C  
ATOM   3499  CG  PRO E  64       9.595 -80.464  28.477  1.00 49.09           C  
ATOM   3500  CD  PRO E  64      10.021 -79.102  28.941  1.00 47.77           C  
ATOM   3501  N   PRO E  65       5.977 -79.192  26.609  1.00 52.41           N  
ATOM   3502  CA  PRO E  65       4.568 -79.433  26.916  1.00 49.46           C  
ATOM   3503  C   PRO E  65       4.315 -80.897  27.234  1.00 58.08           C  
ATOM   3504  O   PRO E  65       4.963 -81.799  26.701  1.00 54.19           O  
ATOM   3505  CB  PRO E  65       3.855 -79.021  25.627  1.00 53.06           C  
ATOM   3506  CG  PRO E  65       4.856 -79.326  24.556  1.00 45.12           C  
ATOM   3507  CD  PRO E  65       6.209 -79.040  25.162  1.00 48.10           C  
ATOM   3508  N   LYS E  66       3.354 -81.119  28.125  1.00 56.39           N  
ATOM   3509  CA  LYS E  66       2.964 -82.468  28.510  1.00 46.33           C  
ATOM   3510  C   LYS E  66       1.981 -83.011  27.485  1.00 51.83           C  
ATOM   3511  O   LYS E  66       0.879 -82.477  27.322  1.00 54.33           O  
ATOM   3512  CB  LYS E  66       2.354 -82.464  29.909  1.00 58.42           C  
ATOM   3513  CG  LYS E  66       1.919 -83.828  30.414  1.00 54.83           C  
ATOM   3514  CD  LYS E  66       1.193 -83.703  31.747  1.00 68.13           C  
ATOM   3515  CE  LYS E  66       0.374 -84.943  32.059  1.00 80.59           C  
ATOM   3516  NZ  LYS E  66      -0.575 -84.710  33.186  1.00 79.02           N1+
ATOM   3517  N   ILE E  67       2.382 -84.069  26.784  1.00 54.99           N  
ATOM   3518  CA  ILE E  67       1.602 -84.649  25.699  1.00 44.88           C  
ATOM   3519  C   ILE E  67       1.370 -86.123  26.003  1.00 57.22           C  
ATOM   3520  O   ILE E  67       2.320 -86.857  26.293  1.00 63.48           O  
ATOM   3521  CB  ILE E  67       2.316 -84.481  24.346  1.00 49.52           C  
ATOM   3522  CG1 ILE E  67       2.540 -82.996  24.050  1.00 54.27           C  
ATOM   3523  CG2 ILE E  67       1.522 -85.152  23.233  1.00 49.24           C  
ATOM   3524  CD1 ILE E  67       3.275 -82.736  22.763  1.00 47.77           C  
ATOM   3525  N   ALA E  68       0.112 -86.547  25.926  1.00 59.14           N  
ATOM   3526  CA  ALA E  68      -0.261 -87.922  26.218  1.00 52.51           C  
ATOM   3527  C   ALA E  68      -1.393 -88.362  25.304  1.00 51.54           C  
ATOM   3528  O   ALA E  68      -2.287 -87.574  24.986  1.00 56.05           O  
ATOM   3529  CB  ALA E  68      -0.685 -88.088  27.685  1.00 50.51           C  
ATOM   3530  N   PHE E  69      -1.346 -89.624  24.882  1.00 57.42           N  
ATOM   3531  CA  PHE E  69      -2.424 -90.196  24.089  1.00 53.33           C  
ATOM   3532  C   PHE E  69      -3.682 -90.364  24.933  1.00 65.05           C  
ATOM   3533  O   PHE E  69      -3.619 -90.731  26.108  1.00 57.56           O  
ATOM   3534  CB  PHE E  69      -2.014 -91.556  23.526  1.00 55.62           C  
ATOM   3535  CG  PHE E  69      -1.128 -91.483  22.319  1.00 58.73           C  
ATOM   3536  CD1 PHE E  69       0.231 -91.252  22.449  1.00 57.92           C  
ATOM   3537  CD2 PHE E  69      -1.652 -91.675  21.051  1.00 49.98           C  
ATOM   3538  CE1 PHE E  69       1.047 -91.196  21.331  1.00 49.60           C  
ATOM   3539  CE2 PHE E  69      -0.842 -91.619  19.931  1.00 53.71           C  
ATOM   3540  CZ  PHE E  69       0.509 -91.381  20.074  1.00 47.45           C  
ATOM   3541  N   THR E  70      -4.831 -90.086  24.320  1.00 67.61           N  
ATOM   3542  CA  THR E  70      -6.118 -90.499  24.874  1.00 56.25           C  
ATOM   3543  C   THR E  70      -6.684 -91.722  24.171  1.00 62.89           C  
ATOM   3544  O   THR E  70      -7.367 -92.528  24.806  1.00 67.26           O  
ATOM   3545  CB  THR E  70      -7.133 -89.353  24.800  1.00 55.41           C  
ATOM   3546  OG1 THR E  70      -7.212 -88.865  23.455  1.00 63.83           O  
ATOM   3547  CG2 THR E  70      -6.724 -88.220  25.723  1.00 45.76           C  
ATOM   3548  N   THR E  71      -6.410 -91.874  22.878  1.00 59.96           N  
ATOM   3549  CA  THR E  71      -6.697 -93.120  22.187  1.00 58.32           C  
ATOM   3550  C   THR E  71      -5.719 -94.196  22.647  1.00 66.12           C  
ATOM   3551  O   THR E  71      -4.535 -93.923  22.873  1.00 67.63           O  
ATOM   3552  CB  THR E  71      -6.593 -92.925  20.673  1.00 61.11           C  
ATOM   3553  OG1 THR E  71      -7.441 -91.844  20.270  1.00 66.28           O  
ATOM   3554  CG2 THR E  71      -7.002 -94.190  19.930  1.00 58.03           C  
ATOM   3555  N   LYS E  72      -6.216 -95.420  22.794  1.00 71.76           N  
ATOM   3556  CA  LYS E  72      -5.376 -96.533  23.211  1.00 67.37           C  
ATOM   3557  C   LYS E  72      -4.546 -97.006  22.026  1.00 59.32           C  
ATOM   3558  O   LYS E  72      -5.062 -97.147  20.912  1.00 67.59           O  
ATOM   3559  CB  LYS E  72      -6.227 -97.678  23.766  1.00 72.94           C  
ATOM   3560  CG  LYS E  72      -7.160 -97.274  24.908  1.00 72.83           C  
ATOM   3561  CD  LYS E  72      -8.506 -96.787  24.385  1.00 75.50           C  
ATOM   3562  CE  LYS E  72      -9.201 -95.865  25.374  1.00 81.92           C  
ATOM   3563  NZ  LYS E  72     -10.402 -95.228  24.763  1.00 69.07           N1+
ATOM   3564  N   ILE E  73      -3.258 -97.232  22.259  1.00 59.67           N  
ATOM   3565  CA  ILE E  73      -2.319 -97.568  21.194  1.00 55.88           C  
ATOM   3566  C   ILE E  73      -1.353 -98.625  21.708  1.00 55.09           C  
ATOM   3567  O   ILE E  73      -0.946 -98.596  22.874  1.00 61.68           O  
ATOM   3568  CB  ILE E  73      -1.578 -96.314  20.687  1.00 58.14           C  
ATOM   3569  CG1 ILE E  73      -0.686 -96.648  19.489  1.00 55.15           C  
ATOM   3570  CG2 ILE E  73      -0.776 -95.669  21.808  1.00 56.22           C  
ATOM   3571  CD1 ILE E  73      -0.048 -95.430  18.865  1.00 47.66           C  
ATOM   3572  N   TYR E  74      -1.008 -99.573  20.840  1.00 51.69           N  
ATOM   3573  CA  TYR E  74      -0.111-100.675  21.185  1.00 51.05           C  
ATOM   3574  C   TYR E  74       1.300-100.245  20.815  1.00 54.47           C  
ATOM   3575  O   TYR E  74       1.664-100.237  19.638  1.00 54.50           O  
ATOM   3576  CB  TYR E  74      -0.533-101.943  20.451  1.00 55.58           C  
ATOM   3577  CG  TYR E  74       0.120-103.212  20.949  1.00 54.48           C  
ATOM   3578  CD1 TYR E  74      -0.399-103.897  22.046  1.00 55.15           C  
ATOM   3579  CD2 TYR E  74       1.236-103.739  20.316  1.00 52.89           C  
ATOM   3580  CE1 TYR E  74       0.188-105.060  22.503  1.00 55.88           C  
ATOM   3581  CE2 TYR E  74       1.830-104.906  20.767  1.00 55.09           C  
ATOM   3582  CZ  TYR E  74       1.301-105.561  21.867  1.00 55.34           C  
ATOM   3583  OH  TYR E  74       1.874-106.723  22.332  1.00 55.16           O  
ATOM   3584  N   HIS E  75       2.108 -99.872  21.813  1.00 45.97           N  
ATOM   3585  CA  HIS E  75       3.457 -99.389  21.540  1.00 48.65           C  
ATOM   3586  C   HIS E  75       4.349 -99.604  22.753  1.00 49.90           C  
ATOM   3587  O   HIS E  75       3.892 -99.406  23.886  1.00 52.07           O  
ATOM   3588  CB  HIS E  75       3.450 -97.904  21.159  1.00 49.97           C  
ATOM   3589  CG  HIS E  75       4.712 -97.443  20.500  1.00 45.86           C  
ATOM   3590  ND1 HIS E  75       5.749 -96.863  21.196  1.00 49.83           N  
ATOM   3591  CD2 HIS E  75       5.100 -97.481  19.204  1.00 47.95           C  
ATOM   3592  CE1 HIS E  75       6.724 -96.561  20.356  1.00 50.33           C  
ATOM   3593  NE2 HIS E  75       6.355 -96.925  19.140  1.00 53.92           N  
ATOM   3594  N   PRO E  76       5.613-100.000  22.555  1.00 48.90           N  
ATOM   3595  CA  PRO E  76       6.497-100.248  23.707  1.00 47.00           C  
ATOM   3596  C   PRO E  76       6.817 -99.009  24.523  1.00 49.71           C  
ATOM   3597  O   PRO E  76       7.211 -99.137  25.686  1.00 50.54           O  
ATOM   3598  CB  PRO E  76       7.771-100.821  23.061  1.00 47.16           C  
ATOM   3599  CG  PRO E  76       7.362-101.249  21.675  1.00 51.52           C  
ATOM   3600  CD  PRO E  76       6.272-100.306  21.273  1.00 46.27           C  
ATOM   3601  N   ASN E  77       6.675 -97.818  23.946  1.00 48.69           N  
ATOM   3602  CA  ASN E  77       7.037 -96.579  24.621  1.00 42.37           C  
ATOM   3603  C   ASN E  77       5.819 -95.759  25.036  1.00 47.32           C  
ATOM   3604  O   ASN E  77       5.975 -94.612  25.465  1.00 47.59           O  
ATOM   3605  CB  ASN E  77       7.958 -95.752  23.721  1.00 46.00           C  
ATOM   3606  CG  ASN E  77       9.186 -96.527  23.278  1.00 48.31           C  
ATOM   3607  OD1 ASN E  77       9.371 -96.802  22.092  1.00 49.09           O  
ATOM   3608  ND2 ASN E  77      10.035 -96.880  24.234  1.00 49.75           N  
ATOM   3609  N   ILE E  78       4.615 -96.312  24.907  1.00 50.58           N  
ATOM   3610  CA  ILE E  78       3.376 -95.646  25.302  1.00 53.49           C  
ATOM   3611  C   ILE E  78       2.585 -96.614  26.174  1.00 48.11           C  
ATOM   3612  O   ILE E  78       2.208 -97.695  25.709  1.00 50.50           O  
ATOM   3613  CB  ILE E  78       2.537 -95.211  24.088  1.00 51.57           C  
ATOM   3614  CG1 ILE E  78       3.413 -94.498  23.056  1.00 49.88           C  
ATOM   3615  CG2 ILE E  78       1.395 -94.309  24.523  1.00 51.04           C  
ATOM   3616  CD1 ILE E  78       2.757 -94.339  21.710  1.00 43.19           C  
ATOM   3617  N   ASN E  79       2.328 -96.227  27.423  1.00 49.37           N  
ATOM   3618  CA  ASN E  79       1.682 -97.129  28.360  1.00 53.70           C  
ATOM   3619  C   ASN E  79       0.161 -97.044  28.228  1.00 53.99           C  
ATOM   3620  O   ASN E  79      -0.382 -96.332  27.382  1.00 62.01           O  
ATOM   3621  CB  ASN E  79       2.140 -96.849  29.792  1.00 47.38           C  
ATOM   3622  CG  ASN E  79       1.854 -95.429  30.240  1.00 52.09           C  
ATOM   3623  OD1 ASN E  79       1.029 -94.730  29.653  1.00 57.87           O  
ATOM   3624  ND2 ASN E  79       2.532 -95.002  31.297  1.00 52.06           N  
ATOM   3625  N   SER E  80      -0.542 -97.793  29.087  1.00 52.17           N  
ATOM   3626  CA  SER E  80      -1.998 -97.839  29.037  1.00 51.29           C  
ATOM   3627  C   SER E  80      -2.638 -96.508  29.409  1.00 55.57           C  
ATOM   3628  O   SER E  80      -3.775 -96.248  29.001  1.00 55.93           O  
ATOM   3629  CB  SER E  80      -2.519 -98.946  29.957  1.00 54.42           C  
ATOM   3630  OG  SER E  80      -2.087 -98.738  31.290  1.00 65.10           O  
ATOM   3631  N   ASN E  81      -1.947 -95.671  30.175  1.00 57.31           N  
ATOM   3632  CA  ASN E  81      -2.451 -94.342  30.508  1.00 55.65           C  
ATOM   3633  C   ASN E  81      -2.196 -93.322  29.406  1.00 56.52           C  
ATOM   3634  O   ASN E  81      -2.560 -92.153  29.574  1.00 54.94           O  
ATOM   3635  CB  ASN E  81      -1.825 -93.854  31.817  1.00 55.27           C  
ATOM   3636  CG  ASN E  81      -2.235 -94.697  33.009  1.00 66.62           C  
ATOM   3637  OD1 ASN E  81      -1.660 -95.752  33.267  1.00 70.51           O  
ATOM   3638  ND2 ASN E  81      -3.236 -94.225  33.746  1.00 61.73           N  
ATOM   3639  N   GLY E  82      -1.591 -93.730  28.293  1.00 53.12           N  
ATOM   3640  CA  GLY E  82      -1.274 -92.821  27.212  1.00 57.45           C  
ATOM   3641  C   GLY E  82       0.002 -92.026  27.387  1.00 59.23           C  
ATOM   3642  O   GLY E  82       0.335 -91.226  26.502  1.00 56.30           O  
ATOM   3643  N   SER E  83       0.726 -92.213  28.492  1.00 47.70           N  
ATOM   3644  CA  SER E  83       1.967 -91.487  28.705  1.00 44.76           C  
ATOM   3645  C   SER E  83       3.003 -91.886  27.665  1.00 47.70           C  
ATOM   3646  O   SER E  83       3.134 -93.062  27.313  1.00 48.41           O  
ATOM   3647  CB  SER E  83       2.503 -91.754  30.113  1.00 51.93           C  
ATOM   3648  OG  SER E  83       1.605 -91.290  31.104  1.00 56.78           O  
ATOM   3649  N   ILE E  84       3.743 -90.895  27.169  1.00 52.08           N  
ATOM   3650  CA  ILE E  84       4.763 -91.089  26.144  1.00 47.62           C  
ATOM   3651  C   ILE E  84       6.121 -90.847  26.784  1.00 50.21           C  
ATOM   3652  O   ILE E  84       6.411 -89.733  27.240  1.00 56.30           O  
ATOM   3653  CB  ILE E  84       4.559 -90.145  24.953  1.00 51.54           C  
ATOM   3654  CG1 ILE E  84       3.096 -90.142  24.510  1.00 50.94           C  
ATOM   3655  CG2 ILE E  84       5.481 -90.533  23.801  1.00 44.31           C  
ATOM   3656  CD1 ILE E  84       2.774 -89.041  23.522  1.00 51.61           C  
ATOM   3657  N   LYS E  85       6.958 -91.880  26.813  1.00 43.52           N  
ATOM   3658  CA  LYS E  85       8.321 -91.739  27.319  1.00 53.63           C  
ATOM   3659  C   LYS E  85       9.224 -91.450  26.128  1.00 50.34           C  
ATOM   3660  O   LYS E  85       9.640 -92.362  25.407  1.00 44.17           O  
ATOM   3661  CB  LYS E  85       8.754 -92.982  28.088  1.00 48.00           C  
ATOM   3662  CG  LYS E  85       9.839 -92.704  29.122  1.00 49.12           C  
ATOM   3663  CD  LYS E  85      10.012 -93.861  30.098  1.00 48.90           C  
ATOM   3664  CE  LYS E  85      10.594 -95.084  29.419  1.00 45.48           C  
ATOM   3665  NZ  LYS E  85      11.878 -94.776  28.730  1.00 53.37           N1+
ATOM   3666  N   LEU E  86       9.515 -90.169  25.911  1.00 52.33           N  
ATOM   3667  CA  LEU E  86      10.241 -89.696  24.741  1.00 47.64           C  
ATOM   3668  C   LEU E  86      11.200 -88.599  25.175  1.00 49.33           C  
ATOM   3669  O   LEU E  86      10.835 -87.729  25.971  1.00 50.20           O  
ATOM   3670  CB  LEU E  86       9.267 -89.182  23.670  1.00 40.57           C  
ATOM   3671  CG  LEU E  86       9.826 -88.666  22.346  1.00 48.15           C  
ATOM   3672  CD1 LEU E  86      10.646 -89.736  21.648  1.00 50.12           C  
ATOM   3673  CD2 LEU E  86       8.681 -88.205  21.460  1.00 42.77           C  
ATOM   3674  N   ASP E  87      12.423 -88.634  24.635  1.00 42.39           N  
ATOM   3675  CA  ASP E  87      13.484 -87.772  25.155  1.00 49.76           C  
ATOM   3676  C   ASP E  87      13.223 -86.299  24.857  1.00 47.08           C  
ATOM   3677  O   ASP E  87      13.518 -85.433  25.690  1.00 47.25           O  
ATOM   3678  CB  ASP E  87      14.842 -88.202  24.585  1.00 49.24           C  
ATOM   3679  CG  ASP E  87      14.915 -88.072  23.076  1.00 50.23           C  
ATOM   3680  OD1 ASP E  87      13.855 -88.105  22.413  1.00 50.72           O  
ATOM   3681  OD2 ASP E  87      16.039 -87.936  22.549  1.00 63.79           O1-
ATOM   3682  N   ILE E  88      12.671 -85.985  23.680  1.00 42.08           N  
ATOM   3683  CA  ILE E  88      12.398 -84.595  23.336  1.00 44.49           C  
ATOM   3684  C   ILE E  88      11.295 -83.985  24.185  1.00 47.23           C  
ATOM   3685  O   ILE E  88      11.097 -82.766  24.141  1.00 51.44           O  
ATOM   3686  CB  ILE E  88      12.026 -84.445  21.849  1.00 46.12           C  
ATOM   3687  CG1 ILE E  88      10.734 -85.201  21.542  1.00 49.73           C  
ATOM   3688  CG2 ILE E  88      13.168 -84.923  20.960  1.00 48.45           C  
ATOM   3689  CD1 ILE E  88      10.260 -85.044  20.118  1.00 47.18           C  
ATOM   3690  N   LEU E  89      10.575 -84.795  24.957  1.00 47.58           N  
ATOM   3691  CA  LEU E  89       9.580 -84.293  25.892  1.00 49.38           C  
ATOM   3692  C   LEU E  89      10.140 -84.094  27.294  1.00 52.18           C  
ATOM   3693  O   LEU E  89       9.389 -83.729  28.203  1.00 54.63           O  
ATOM   3694  CB  LEU E  89       8.379 -85.245  25.948  1.00 47.88           C  
ATOM   3695  CG  LEU E  89       7.606 -85.402  24.636  1.00 53.42           C  
ATOM   3696  CD1 LEU E  89       6.544 -86.484  24.757  1.00 53.17           C  
ATOM   3697  CD2 LEU E  89       6.982 -84.078  24.226  1.00 50.81           C  
ATOM   3698  N   ARG E  90      11.438 -84.324  27.490  1.00 57.66           N  
ATOM   3699  CA  ARG E  90      12.060 -84.130  28.796  1.00 54.20           C  
ATOM   3700  C   ARG E  90      13.434 -83.487  28.666  1.00 51.55           C  
ATOM   3701  O   ARG E  90      13.548 -82.264  28.529  1.00 59.63           O  
ATOM   3702  CB  ARG E  90      12.183 -85.462  29.542  1.00 63.86           C  
ATOM   3703  CG  ARG E  90      10.864 -86.077  29.982  1.00 73.72           C  
ATOM   3704  CD  ARG E  90      10.502 -87.273  29.119  1.00 67.65           C  
ATOM   3705  NE  ARG E  90      11.602 -88.231  29.027  1.00 71.36           N  
ATOM   3706  CZ  ARG E  90      11.875 -89.147  29.951  1.00 74.82           C  
ATOM   3707  NH1 ARG E  90      11.127 -89.236  31.043  1.00 68.87           N1+
ATOM   3708  NH2 ARG E  90      12.895 -89.977  29.782  1.00 74.25           N  
ATOM   3709  N   SER E  91      14.485 -84.310  28.708  1.00 52.47           N  
ATOM   3710  CA  SER E  91      15.841 -83.779  28.757  1.00 53.92           C  
ATOM   3711  C   SER E  91      16.273 -83.211  27.410  1.00 46.56           C  
ATOM   3712  O   SER E  91      16.998 -82.213  27.359  1.00 54.89           O  
ATOM   3713  CB  SER E  91      16.812 -84.867  29.215  1.00 52.18           C  
ATOM   3714  OG  SER E  91      16.734 -86.002  28.371  1.00 55.53           O  
ATOM   3715  N   GLN E  92      15.843 -83.832  26.314  1.00 47.00           N  
ATOM   3716  CA  GLN E  92      16.228 -83.398  24.976  1.00 49.90           C  
ATOM   3717  C   GLN E  92      15.261 -82.381  24.385  1.00 45.05           C  
ATOM   3718  O   GLN E  92      15.196 -82.239  23.157  1.00 45.58           O  
ATOM   3719  CB  GLN E  92      16.361 -84.609  24.050  1.00 46.48           C  
ATOM   3720  CG  GLN E  92      17.488 -85.545  24.441  1.00 52.37           C  
ATOM   3721  CD  GLN E  92      18.843 -84.866  24.402  1.00 56.20           C  
ATOM   3722  OE1 GLN E  92      19.397 -84.611  23.332  1.00 48.73           O  
ATOM   3723  NE2 GLN E  92      19.388 -84.569  25.578  1.00 50.10           N  
ATOM   3724  N   TRP E  93      14.510 -81.669  25.223  1.00 51.99           N  
ATOM   3725  CA  TRP E  93      13.591 -80.656  24.730  1.00 43.20           C  
ATOM   3726  C   TRP E  93      14.352 -79.437  24.222  1.00 38.76           C  
ATOM   3727  O   TRP E  93      15.386 -79.052  24.774  1.00 39.87           O  
ATOM   3728  CB  TRP E  93      12.618 -80.244  25.835  1.00 47.42           C  
ATOM   3729  CG  TRP E  93      11.863 -78.986  25.532  1.00 41.57           C  
ATOM   3730  CD1 TRP E  93      12.053 -77.764  26.106  1.00 45.33           C  
ATOM   3731  CD2 TRP E  93      10.809 -78.824  24.576  1.00 40.43           C  
ATOM   3732  NE1 TRP E  93      11.177 -76.850  25.571  1.00 42.94           N  
ATOM   3733  CE2 TRP E  93      10.402 -77.474  24.630  1.00 39.13           C  
ATOM   3734  CE3 TRP E  93      10.164 -79.685  23.685  1.00 40.94           C  
ATOM   3735  CZ2 TRP E  93       9.384 -76.967  23.827  1.00 41.95           C  
ATOM   3736  CZ3 TRP E  93       9.155 -79.178  22.887  1.00 43.65           C  
ATOM   3737  CH2 TRP E  93       8.774 -77.836  22.964  1.00 41.52           C  
ATOM   3738  N   SER E  94      13.834 -78.829  23.155  1.00 45.16           N  
ATOM   3739  CA  SER E  94      14.389 -77.600  22.614  1.00 45.60           C  
ATOM   3740  C   SER E  94      13.281 -76.556  22.513  1.00 39.57           C  
ATOM   3741  O   SER E  94      12.189 -76.862  22.007  1.00 44.15           O  
ATOM   3742  CB  SER E  94      15.026 -77.831  21.239  1.00 42.10           C  
ATOM   3743  OG  SER E  94      15.345 -76.596  20.622  1.00 39.39           O  
ATOM   3744  N   PRO E  95      13.516 -75.325  22.975  1.00 39.03           N  
ATOM   3745  CA  PRO E  95      12.480 -74.287  22.830  1.00 39.97           C  
ATOM   3746  C   PRO E  95      12.182 -73.932  21.383  1.00 42.92           C  
ATOM   3747  O   PRO E  95      11.126 -73.349  21.112  1.00 46.38           O  
ATOM   3748  CB  PRO E  95      13.071 -73.093  23.593  1.00 38.82           C  
ATOM   3749  CG  PRO E  95      14.538 -73.341  23.622  1.00 41.75           C  
ATOM   3750  CD  PRO E  95      14.701 -74.831  23.692  1.00 41.44           C  
ATOM   3751  N   ALA E  96      13.068 -74.269  20.444  1.00 33.78           N  
ATOM   3752  CA  ALA E  96      12.799 -74.038  19.030  1.00 38.15           C  
ATOM   3753  C   ALA E  96      11.824 -75.053  18.446  1.00 43.23           C  
ATOM   3754  O   ALA E  96      11.382 -74.876  17.306  1.00 45.71           O  
ATOM   3755  CB  ALA E  96      14.099 -74.055  18.229  1.00 40.48           C  
ATOM   3756  N   LEU E  97      11.483 -76.099  19.190  1.00 42.81           N  
ATOM   3757  CA  LEU E  97      10.489 -77.058  18.731  1.00 39.11           C  
ATOM   3758  C   LEU E  97       9.088 -76.471  18.864  1.00 49.50           C  
ATOM   3759  O   LEU E  97       8.763 -75.812  19.857  1.00 45.98           O  
ATOM   3760  CB  LEU E  97      10.592 -78.359  19.531  1.00 40.76           C  
ATOM   3761  CG  LEU E  97      11.680 -79.356  19.129  1.00 48.92           C  
ATOM   3762  CD1 LEU E  97      11.790 -80.478  20.154  1.00 37.44           C  
ATOM   3763  CD2 LEU E  97      11.404 -79.924  17.742  1.00 40.30           C  
ATOM   3764  N   THR E  98       8.262 -76.710  17.852  1.00 46.50           N  
ATOM   3765  CA  THR E  98       6.867 -76.306  17.864  1.00 46.33           C  
ATOM   3766  C   THR E  98       5.982 -77.534  18.016  1.00 56.10           C  
ATOM   3767  O   THR E  98       6.422 -78.671  17.815  1.00 49.32           O  
ATOM   3768  CB  THR E  98       6.494 -75.548  16.584  1.00 50.73           C  
ATOM   3769  OG1 THR E  98       6.706 -76.392  15.446  1.00 50.39           O  
ATOM   3770  CG2 THR E  98       7.343 -74.291  16.441  1.00 47.37           C  
ATOM   3771  N   VAL E  99       4.722 -77.289  18.382  1.00 46.29           N  
ATOM   3772  CA  VAL E  99       3.779 -78.384  18.597  1.00 48.73           C  
ATOM   3773  C   VAL E  99       3.604 -79.197  17.322  1.00 46.07           C  
ATOM   3774  O   VAL E  99       3.491 -80.427  17.365  1.00 50.58           O  
ATOM   3775  CB  VAL E  99       2.436 -77.834  19.113  1.00 50.03           C  
ATOM   3776  CG1 VAL E  99       1.401 -78.947  19.208  1.00 47.09           C  
ATOM   3777  CG2 VAL E  99       2.634 -77.177  20.461  1.00 49.51           C  
ATOM   3778  N   SER E 100       3.587 -78.528  16.167  1.00 48.18           N  
ATOM   3779  CA  SER E 100       3.503 -79.247  14.903  1.00 50.62           C  
ATOM   3780  C   SER E 100       4.707 -80.157  14.708  1.00 46.17           C  
ATOM   3781  O   SER E 100       4.565 -81.293  14.240  1.00 50.32           O  
ATOM   3782  CB  SER E 100       3.383 -78.260  13.739  1.00 58.58           C  
ATOM   3783  OG  SER E 100       3.296 -78.940  12.499  1.00 58.98           O  
ATOM   3784  N   LYS E 101       5.901 -79.683  15.078  1.00 49.16           N  
ATOM   3785  CA  LYS E 101       7.099 -80.506  14.937  1.00 47.41           C  
ATOM   3786  C   LYS E 101       7.089 -81.670  15.919  1.00 44.30           C  
ATOM   3787  O   LYS E 101       7.501 -82.784  15.572  1.00 40.49           O  
ATOM   3788  CB  LYS E 101       8.351 -79.651  15.131  1.00 37.72           C  
ATOM   3789  CG  LYS E 101       8.631 -78.700  13.988  1.00 44.99           C  
ATOM   3790  CD  LYS E 101       8.897 -79.460  12.701  1.00 43.89           C  
ATOM   3791  CE  LYS E 101       9.322 -78.521  11.585  1.00 52.67           C  
ATOM   3792  NZ  LYS E 101       9.679 -79.262  10.345  1.00 46.67           N1+
ATOM   3793  N   VAL E 102       6.617 -81.434  17.144  1.00 47.32           N  
ATOM   3794  CA  VAL E 102       6.572 -82.501  18.139  1.00 43.20           C  
ATOM   3795  C   VAL E 102       5.572 -83.575  17.730  1.00 44.29           C  
ATOM   3796  O   VAL E 102       5.865 -84.773  17.814  1.00 52.62           O  
ATOM   3797  CB  VAL E 102       6.247 -81.924  19.529  1.00 49.69           C  
ATOM   3798  CG1 VAL E 102       6.133 -83.043  20.551  1.00 44.03           C  
ATOM   3799  CG2 VAL E 102       7.311 -80.926  19.946  1.00 47.30           C  
ATOM   3800  N   LEU E 103       4.380 -83.172  17.283  1.00 50.62           N  
ATOM   3801  CA  LEU E 103       3.379 -84.150  16.858  1.00 47.09           C  
ATOM   3802  C   LEU E 103       3.880 -84.967  15.676  1.00 46.02           C  
ATOM   3803  O   LEU E 103       3.609 -86.172  15.584  1.00 46.13           O  
ATOM   3804  CB  LEU E 103       2.072 -83.444  16.501  1.00 46.87           C  
ATOM   3805  CG  LEU E 103       1.289 -82.840  17.668  1.00 56.60           C  
ATOM   3806  CD1 LEU E 103       0.021 -82.162  17.169  1.00 59.88           C  
ATOM   3807  CD2 LEU E 103       0.962 -83.915  18.692  1.00 52.52           C  
ATOM   3808  N   LEU E 104       4.611 -84.332  14.763  1.00 45.96           N  
ATOM   3809  CA  LEU E 104       5.203 -85.070  13.656  1.00 47.63           C  
ATOM   3810  C   LEU E 104       6.327 -85.972  14.142  1.00 44.91           C  
ATOM   3811  O   LEU E 104       6.519 -87.071  13.606  1.00 47.81           O  
ATOM   3812  CB  LEU E 104       5.709 -84.101  12.592  1.00 48.47           C  
ATOM   3813  CG  LEU E 104       6.351 -84.719  11.352  1.00 46.15           C  
ATOM   3814  CD1 LEU E 104       5.384 -85.659  10.657  1.00 43.45           C  
ATOM   3815  CD2 LEU E 104       6.797 -83.613  10.417  1.00 54.08           C  
ATOM   3816  N   SER E 105       7.073 -85.530  15.156  1.00 47.99           N  
ATOM   3817  CA  SER E 105       8.087 -86.385  15.764  1.00 40.58           C  
ATOM   3818  C   SER E 105       7.452 -87.615  16.403  1.00 45.35           C  
ATOM   3819  O   SER E 105       7.984 -88.724  16.298  1.00 46.21           O  
ATOM   3820  CB  SER E 105       8.888 -85.593  16.793  1.00 44.09           C  
ATOM   3821  OG  SER E 105       9.565 -84.507  16.183  1.00 48.29           O  
ATOM   3822  N   ILE E 106       6.312 -87.433  17.073  1.00 44.78           N  
ATOM   3823  CA  ILE E 106       5.609 -88.562  17.682  1.00 41.56           C  
ATOM   3824  C   ILE E 106       5.112 -89.520  16.615  1.00 47.77           C  
ATOM   3825  O   ILE E 106       5.074 -90.738  16.830  1.00 49.05           O  
ATOM   3826  CB  ILE E 106       4.460 -88.052  18.577  1.00 40.97           C  
ATOM   3827  CG1 ILE E 106       5.019 -87.193  19.714  1.00 46.17           C  
ATOM   3828  CG2 ILE E 106       3.664 -89.212  19.153  1.00 40.28           C  
ATOM   3829  CD1 ILE E 106       3.960 -86.621  20.624  1.00 44.68           C  
ATOM   3830  N   CYS E 107       4.738 -89.000  15.443  1.00 46.40           N  
ATOM   3831  CA ACYS E 107       4.298 -89.870  14.358  0.52 47.95           C  
ATOM   3832  CA BCYS E 107       4.295 -89.869  14.360  0.48 48.16           C  
ATOM   3833  C   CYS E 107       5.401 -90.831  13.936  1.00 41.54           C  
ATOM   3834  O   CYS E 107       5.156 -92.028  13.748  1.00 44.22           O  
ATOM   3835  CB ACYS E 107       3.827 -89.035  13.167  0.52 50.38           C  
ATOM   3836  CB BCYS E 107       3.824 -89.029  13.173  0.48 49.84           C  
ATOM   3837  SG ACYS E 107       2.300 -88.107  13.450  0.52 48.77           S  
ATOM   3838  SG BCYS E 107       3.052 -89.974  11.844  0.48 51.32           S  
ATOM   3839  N   SER E 108       6.632 -90.323  13.790  1.00 46.58           N  
ATOM   3840  CA  SER E 108       7.749 -91.173  13.391  1.00 46.14           C  
ATOM   3841  C   SER E 108       8.159 -92.144  14.490  1.00 54.88           C  
ATOM   3842  O   SER E 108       8.861 -93.122  14.207  1.00 40.90           O  
ATOM   3843  CB  SER E 108       8.947 -90.316  12.989  1.00 47.53           C  
ATOM   3844  OG  SER E 108       9.440 -89.585  14.097  1.00 45.47           O  
ATOM   3845  N   LEU E 109       7.747 -91.890  15.735  1.00 54.79           N  
ATOM   3846  CA  LEU E 109       8.053 -92.810  16.823  1.00 47.79           C  
ATOM   3847  C   LEU E 109       7.285 -94.118  16.683  1.00 51.62           C  
ATOM   3848  O   LEU E 109       7.751 -95.163  17.152  1.00 52.16           O  
ATOM   3849  CB  LEU E 109       7.749 -92.147  18.166  1.00 45.98           C  
ATOM   3850  CG  LEU E 109       7.918 -92.965  19.446  1.00 53.44           C  
ATOM   3851  CD1 LEU E 109       9.357 -93.426  19.607  1.00 43.19           C  
ATOM   3852  CD2 LEU E 109       7.463 -92.165  20.661  1.00 48.04           C  
ATOM   3853  N   LEU E 110       6.122 -94.084  16.027  1.00 54.50           N  
ATOM   3854  CA  LEU E 110       5.271 -95.269  15.952  1.00 50.93           C  
ATOM   3855  C   LEU E 110       5.963 -96.409  15.216  1.00 49.15           C  
ATOM   3856  O   LEU E 110       5.884 -97.568  15.640  1.00 58.57           O  
ATOM   3857  CB  LEU E 110       3.948 -94.920  15.276  1.00 51.01           C  
ATOM   3858  CG  LEU E 110       3.183 -93.754  15.904  1.00 49.98           C  
ATOM   3859  CD1 LEU E 110       1.842 -93.557  15.215  1.00 56.62           C  
ATOM   3860  CD2 LEU E 110       2.996 -93.980  17.394  1.00 50.93           C  
ATOM   3861  N   CYS E 111       6.651 -96.105  14.117  1.00 52.42           N  
ATOM   3862  CA  CYS E 111       7.344 -97.117  13.332  1.00 52.84           C  
ATOM   3863  C   CYS E 111       8.819 -97.232  13.691  1.00 54.34           C  
ATOM   3864  O   CYS E 111       9.551 -97.973  13.026  1.00 58.08           O  
ATOM   3865  CB  CYS E 111       7.194 -96.820  11.842  1.00 60.10           C  
ATOM   3866  SG  CYS E 111       5.486 -96.733  11.314  1.00 70.42           S  
ATOM   3867  N   ASP E 112       9.271 -96.519  14.716  1.00 55.12           N  
ATOM   3868  CA  ASP E 112      10.653 -96.599  15.184  1.00 53.27           C  
ATOM   3869  C   ASP E 112      10.651 -96.567  16.706  1.00 56.37           C  
ATOM   3870  O   ASP E 112      11.047 -95.574  17.326  1.00 56.23           O  
ATOM   3871  CB  ASP E 112      11.495 -95.464  14.599  1.00 54.17           C  
ATOM   3872  CG  ASP E 112      12.953 -95.545  15.001  1.00 62.83           C  
ATOM   3873  OD1 ASP E 112      13.451 -96.673  15.209  1.00 63.35           O  
ATOM   3874  OD2 ASP E 112      13.596 -94.479  15.111  1.00 57.61           O1-
ATOM   3875  N   PRO E 113      10.201 -97.641  17.344  1.00 53.34           N  
ATOM   3876  CA  PRO E 113      10.208 -97.694  18.807  1.00 52.77           C  
ATOM   3877  C   PRO E 113      11.576 -98.091  19.339  1.00 53.09           C  
ATOM   3878  O   PRO E 113      12.460 -98.539  18.606  1.00 57.06           O  
ATOM   3879  CB  PRO E 113       9.157 -98.763  19.118  1.00 50.34           C  
ATOM   3880  CG  PRO E 113       9.261 -99.700  17.959  1.00 54.91           C  
ATOM   3881  CD  PRO E 113       9.618 -98.862  16.754  1.00 47.94           C  
ATOM   3882  N   ASN E 114      11.739 -97.913  20.649  1.00 56.97           N  
ATOM   3883  CA  ASN E 114      12.956 -98.312  21.349  1.00 51.77           C  
ATOM   3884  C   ASN E 114      12.612 -99.450  22.298  1.00 59.97           C  
ATOM   3885  O   ASN E 114      12.299 -99.215  23.475  1.00 60.85           O  
ATOM   3886  CB  ASN E 114      13.567 -97.132  22.109  1.00 53.09           C  
ATOM   3887  CG  ASN E 114      14.895 -97.480  22.753  1.00 60.80           C  
ATOM   3888  OD1 ASN E 114      15.487 -98.519  22.466  1.00 59.45           O  
ATOM   3889  ND2 ASN E 114      15.375 -96.599  23.627  1.00 59.63           N  
ATOM   3890  N   PRO E 115      12.647-100.705  21.840  1.00 62.96           N  
ATOM   3891  CA  PRO E 115      12.300-101.829  22.721  1.00 61.94           C  
ATOM   3892  C   PRO E 115      13.365-102.172  23.747  1.00 59.08           C  
ATOM   3893  O   PRO E 115      13.107-103.009  24.622  1.00 64.55           O  
ATOM   3894  CB  PRO E 115      12.101-102.987  21.734  1.00 62.68           C  
ATOM   3895  CG  PRO E 115      13.021-102.652  20.605  1.00 56.82           C  
ATOM   3896  CD  PRO E 115      13.005-101.152  20.483  1.00 57.14           C  
ATOM   3897  N   ASP E 116      14.552-101.562  23.665  1.00 62.48           N  
ATOM   3898  CA  ASP E 116      15.622-101.883  24.603  1.00 63.24           C  
ATOM   3899  C   ASP E 116      15.479-101.138  25.925  1.00 63.59           C  
ATOM   3900  O   ASP E 116      15.887-101.661  26.968  1.00 62.90           O  
ATOM   3901  CB  ASP E 116      16.978-101.575  23.961  1.00 63.44           C  
ATOM   3902  CG  ASP E 116      17.184-102.320  22.658  1.00 72.81           C  
ATOM   3903  OD1 ASP E 116      16.755-103.489  22.569  1.00 79.51           O  
ATOM   3904  OD2 ASP E 116      17.766-101.732  21.719  1.00 76.05           O1-
ATOM   3905  N   ASP E 117      14.915 -99.930  25.904  1.00 65.61           N  
ATOM   3906  CA  ASP E 117      14.567 -99.179  27.112  1.00 65.46           C  
ATOM   3907  C   ASP E 117      13.084 -98.844  27.021  1.00 59.56           C  
ATOM   3908  O   ASP E 117      12.710 -97.734  26.616  1.00 59.74           O  
ATOM   3909  CB  ASP E 117      15.416 -97.916  27.262  1.00 55.41           C  
ATOM   3910  CG  ASP E 117      15.056 -97.117  28.503  1.00 70.19           C  
ATOM   3911  OD1 ASP E 117      14.604 -97.727  29.495  1.00 65.52           O  
ATOM   3912  OD2 ASP E 117      15.220 -95.878  28.479  1.00 79.28           O1-
ATOM   3913  N   PRO E 118      12.207 -99.783  27.382  1.00 58.08           N  
ATOM   3914  CA  PRO E 118      10.778 -99.597  27.103  1.00 56.54           C  
ATOM   3915  C   PRO E 118       9.984 -99.029  28.266  1.00 51.76           C  
ATOM   3916  O   PRO E 118      10.429 -99.054  29.417  1.00 53.32           O  
ATOM   3917  CB  PRO E 118      10.322-101.020  26.772  1.00 58.48           C  
ATOM   3918  CG  PRO E 118      11.173-101.873  27.667  1.00 52.45           C  
ATOM   3919  CD  PRO E 118      12.502-101.153  27.837  1.00 52.42           C  
ATOM   3920  N   LEU E 119       8.790 -98.523  27.962  1.00 55.45           N  
ATOM   3921  CA  LEU E 119       7.824 -98.141  28.983  1.00 51.09           C  
ATOM   3922  C   LEU E 119       6.873 -99.282  29.322  1.00 53.87           C  
ATOM   3923  O   LEU E 119       6.439 -99.397  30.473  1.00 54.05           O  
ATOM   3924  CB  LEU E 119       7.033 -96.914  28.524  1.00 47.23           C  
ATOM   3925  CG  LEU E 119       6.032 -96.308  29.512  1.00 52.12           C  
ATOM   3926  CD1 LEU E 119       6.710 -95.970  30.829  1.00 39.64           C  
ATOM   3927  CD2 LEU E 119       5.377 -95.073  28.913  1.00 53.99           C  
ATOM   3928  N   VAL E 120       6.548-100.124  28.346  1.00 51.91           N  
ATOM   3929  CA  VAL E 120       5.757-101.330  28.551  1.00 52.39           C  
ATOM   3930  C   VAL E 120       6.655-102.528  28.247  1.00 53.66           C  
ATOM   3931  O   VAL E 120       6.927-102.811  27.070  1.00 54.75           O  
ATOM   3932  CB  VAL E 120       4.500-101.342  27.670  1.00 55.97           C  
ATOM   3933  CG1 VAL E 120       3.576-102.476  28.095  1.00 46.65           C  
ATOM   3934  CG2 VAL E 120       3.790-100.001  27.742  1.00 49.36           C  
ATOM   3935  N   PRO E 121       7.134-103.255  29.261  1.00 53.44           N  
ATOM   3936  CA  PRO E 121       8.123-104.308  28.987  1.00 57.34           C  
ATOM   3937  C   PRO E 121       7.575-105.471  28.178  1.00 55.91           C  
ATOM   3938  O   PRO E 121       8.270-105.980  27.292  1.00 55.06           O  
ATOM   3939  CB  PRO E 121       8.559-104.751  30.395  1.00 59.99           C  
ATOM   3940  CG  PRO E 121       8.150-103.631  31.304  1.00 56.01           C  
ATOM   3941  CD  PRO E 121       6.906-103.069  30.702  1.00 55.40           C  
ATOM   3942  N   ASP E 122       6.344-105.913  28.459  1.00 54.72           N  
ATOM   3943  CA  ASP E 122       5.814-107.087  27.770  1.00 60.34           C  
ATOM   3944  C   ASP E 122       5.553-106.807  26.295  1.00 55.67           C  
ATOM   3945  O   ASP E 122       5.701-107.707  25.463  1.00 56.44           O  
ATOM   3946  CB  ASP E 122       4.540-107.575  28.457  1.00 56.79           C  
ATOM   3947  CG  ASP E 122       3.462-106.511  28.510  1.00 68.60           C  
ATOM   3948  OD1 ASP E 122       3.544-105.627  29.392  1.00 76.79           O  
ATOM   3949  OD2 ASP E 122       2.534-106.559  27.683  1.00 69.92           O1-
ATOM   3950  N   ILE E 123       5.166-105.576  25.951  1.00 59.05           N  
ATOM   3951  CA  ILE E 123       4.992-105.223  24.546  1.00 53.37           C  
ATOM   3952  C   ILE E 123       6.339-105.186  23.833  1.00 55.69           C  
ATOM   3953  O   ILE E 123       6.468-105.653  22.696  1.00 55.04           O  
ATOM   3954  CB  ILE E 123       4.240-103.882  24.416  1.00 54.41           C  
ATOM   3955  CG1 ILE E 123       2.792-104.037  24.881  1.00 52.26           C  
ATOM   3956  CG2 ILE E 123       4.289-103.368  22.990  1.00 46.99           C  
ATOM   3957  CD1 ILE E 123       1.979-102.776  24.762  1.00 50.55           C  
ATOM   3958  N   ALA E 124       7.363-104.645  24.497  1.00 58.20           N  
ATOM   3959  CA  ALA E 124       8.699-104.635  23.911  1.00 55.71           C  
ATOM   3960  C   ALA E 124       9.258-106.042  23.757  1.00 56.18           C  
ATOM   3961  O   ALA E 124       9.997-106.314  22.805  1.00 59.83           O  
ATOM   3962  CB  ALA E 124       9.641-103.790  24.765  1.00 53.49           C  
ATOM   3963  N   GLN E 125       8.925-106.945  24.682  1.00 58.87           N  
ATOM   3964  CA  GLN E 125       9.400-108.322  24.579  1.00 60.34           C  
ATOM   3965  C   GLN E 125       8.830-109.008  23.344  1.00 53.42           C  
ATOM   3966  O   GLN E 125       9.546-109.726  22.638  1.00 57.53           O  
ATOM   3967  CB  GLN E 125       9.039-109.096  25.848  1.00 57.74           C  
ATOM   3968  CG  GLN E 125       9.309-110.586  25.770  1.00 59.72           C  
ATOM   3969  CD  GLN E 125      10.763-110.907  25.499  1.00 58.94           C  
ATOM   3970  OE1 GLN E 125      11.656-110.136  25.850  1.00 64.27           O  
ATOM   3971  NE2 GLN E 125      11.008-112.051  24.869  1.00 69.92           N  
ATOM   3972  N   ILE E 126       7.542-108.794  23.064  1.00 53.96           N  
ATOM   3973  CA  ILE E 126       6.935-109.353  21.860  1.00 61.39           C  
ATOM   3974  C   ILE E 126       7.574-108.751  20.613  1.00 62.45           C  
ATOM   3975  O   ILE E 126       7.784-109.443  19.609  1.00 60.48           O  
ATOM   3976  CB  ILE E 126       5.409-109.139  21.877  1.00 57.35           C  
ATOM   3977  CG1 ILE E 126       4.770-109.964  22.997  1.00 54.81           C  
ATOM   3978  CG2 ILE E 126       4.789-109.495  20.534  1.00 55.25           C  
ATOM   3979  CD1 ILE E 126       3.257-109.882  23.031  1.00 57.51           C  
ATOM   3980  N   TYR E 127       7.906-107.456  20.664  1.00 61.67           N  
ATOM   3981  CA  TYR E 127       8.532-106.790  19.525  1.00 59.76           C  
ATOM   3982  C   TYR E 127       9.876-107.411  19.168  1.00 58.84           C  
ATOM   3983  O   TYR E 127      10.241-107.463  17.988  1.00 60.73           O  
ATOM   3984  CB  TYR E 127       8.701-105.298  19.826  1.00 58.52           C  
ATOM   3985  CG  TYR E 127       9.259-104.475  18.684  1.00 62.02           C  
ATOM   3986  CD1 TYR E 127      10.629-104.286  18.534  1.00 62.23           C  
ATOM   3987  CD2 TYR E 127       8.415-103.877  17.759  1.00 61.20           C  
ATOM   3988  CE1 TYR E 127      11.140-103.533  17.494  1.00 62.46           C  
ATOM   3989  CE2 TYR E 127       8.916-103.123  16.714  1.00 58.46           C  
ATOM   3990  CZ  TYR E 127      10.279-102.952  16.586  1.00 63.73           C  
ATOM   3991  OH  TYR E 127      10.778-102.200  15.546  1.00 67.02           O  
ATOM   3992  N   LYS E 128      10.623-107.890  20.166  1.00 57.07           N  
ATOM   3993  CA  LYS E 128      11.959-108.425  19.941  1.00 63.93           C  
ATOM   3994  C   LYS E 128      11.952-109.900  19.546  1.00 63.51           C  
ATOM   3995  O   LYS E 128      12.780-110.324  18.731  1.00 65.92           O  
ATOM   3996  CB  LYS E 128      12.817-108.233  21.196  1.00 60.25           C  
ATOM   3997  CG  LYS E 128      13.027-106.781  21.584  1.00 57.83           C  
ATOM   3998  CD  LYS E 128      13.757-106.665  22.910  1.00 69.90           C  
ATOM   3999  CE  LYS E 128      15.102-107.371  22.866  1.00 78.97           C  
ATOM   4000  NZ  LYS E 128      16.010-106.781  21.843  1.00 77.96           N1+
ATOM   4001  N   SER E 129      11.041-110.694  20.109  1.00 57.48           N  
ATOM   4002  CA  SER E 129      11.020-112.132  19.863  1.00 61.96           C  
ATOM   4003  C   SER E 129      10.043-112.553  18.773  1.00 63.96           C  
ATOM   4004  O   SER E 129      10.179-113.660  18.244  1.00 66.77           O  
ATOM   4005  CB  SER E 129      10.676-112.884  21.156  1.00 66.88           C  
ATOM   4006  OG  SER E 129       9.451-112.430  21.702  1.00 69.46           O  
ATOM   4007  N   ASP E 130       9.073-111.711  18.428  1.00 66.90           N  
ATOM   4008  CA  ASP E 130       8.122-112.041  17.375  1.00 66.68           C  
ATOM   4009  C   ASP E 130       7.470-110.775  16.829  1.00 64.01           C  
ATOM   4010  O   ASP E 130       6.365-110.410  17.237  1.00 63.26           O  
ATOM   4011  CB  ASP E 130       7.058-113.009  17.902  1.00 63.64           C  
ATOM   4012  CG  ASP E 130       6.249-113.650  16.793  1.00 70.52           C  
ATOM   4013  OD1 ASP E 130       6.673-113.569  15.619  1.00 75.66           O  
ATOM   4014  OD2 ASP E 130       5.195-114.249  17.095  1.00 77.87           O1-
ATOM   4015  N   LYS E 131       8.157-110.095  15.902  1.00 59.92           N  
ATOM   4016  CA  LYS E 131       7.655-108.823  15.396  1.00 64.55           C  
ATOM   4017  C   LYS E 131       6.376-109.000  14.589  1.00 66.80           C  
ATOM   4018  O   LYS E 131       5.552-108.079  14.529  1.00 63.24           O  
ATOM   4019  CB  LYS E 131       8.732-108.129  14.558  1.00 57.76           C  
ATOM   4020  CG  LYS E 131       8.449-106.663  14.282  1.00 64.02           C  
ATOM   4021  CD  LYS E 131       9.612-105.995  13.574  1.00 65.67           C  
ATOM   4022  CE  LYS E 131       9.358-104.513  13.363  1.00 64.96           C  
ATOM   4023  NZ  LYS E 131      10.488-103.860  12.641  1.00 68.60           N1+
ATOM   4024  N   GLU E 132       6.186-110.170  13.975  1.00 64.91           N  
ATOM   4025  CA  GLU E 132       4.952-110.435  13.242  1.00 63.80           C  
ATOM   4026  C   GLU E 132       3.758-110.447  14.188  1.00 63.22           C  
ATOM   4027  O   GLU E 132       2.713-109.850  13.902  1.00 62.48           O  
ATOM   4028  CB  GLU E 132       5.063-111.760  12.491  1.00 68.43           C  
ATOM   4029  CG  GLU E 132       6.419-111.981  11.846  1.00 78.89           C  
ATOM   4030  CD  GLU E 132       6.809-110.850  10.914  1.00 84.64           C  
ATOM   4031  OE1 GLU E 132       6.109-110.649   9.900  1.00 89.44           O  
ATOM   4032  OE2 GLU E 132       7.809-110.159  11.202  1.00 89.17           O1-
ATOM   4033  N   LYS E 133       3.896-111.134  15.324  1.00 60.40           N  
ATOM   4034  CA  LYS E 133       2.856-111.099  16.344  1.00 62.95           C  
ATOM   4035  C   LYS E 133       2.663-109.686  16.884  1.00 62.95           C  
ATOM   4036  O   LYS E 133       1.539-109.291  17.211  1.00 61.70           O  
ATOM   4037  CB  LYS E 133       3.206-112.066  17.473  1.00 65.07           C  
ATOM   4038  CG  LYS E 133       2.133-112.228  18.537  1.00 67.10           C  
ATOM   4039  CD  LYS E 133       2.477-113.375  19.477  1.00 69.90           C  
ATOM   4040  CE  LYS E 133       1.401-113.570  20.535  1.00 72.18           C  
ATOM   4041  NZ  LYS E 133       1.334-112.418  21.479  1.00 68.53           N1+
ATOM   4042  N   TYR E 134       3.750-108.917  16.975  1.00 65.33           N  
ATOM   4043  CA  TYR E 134       3.647-107.522  17.398  1.00 59.56           C  
ATOM   4044  C   TYR E 134       2.847-106.707  16.391  1.00 59.36           C  
ATOM   4045  O   TYR E 134       1.977-105.914  16.772  1.00 61.18           O  
ATOM   4046  CB  TYR E 134       5.047-106.934  17.577  1.00 59.29           C  
ATOM   4047  CG  TYR E 134       5.090-105.441  17.826  1.00 56.88           C  
ATOM   4048  CD1 TYR E 134       5.039-104.929  19.118  1.00 61.62           C  
ATOM   4049  CD2 TYR E 134       5.201-104.546  16.767  1.00 60.72           C  
ATOM   4050  CE1 TYR E 134       5.087-103.568  19.345  1.00 59.36           C  
ATOM   4051  CE2 TYR E 134       5.244-103.190  16.985  1.00 57.11           C  
ATOM   4052  CZ  TYR E 134       5.195-102.708  18.273  1.00 61.30           C  
ATOM   4053  OH  TYR E 134       5.248-101.352  18.480  1.00 54.86           O  
ATOM   4054  N   ASN E 135       3.133-106.887  15.098  1.00 57.57           N  
ATOM   4055  CA  ASN E 135       2.431-106.127  14.071  1.00 59.65           C  
ATOM   4056  C   ASN E 135       0.939-106.417  14.086  1.00 60.51           C  
ATOM   4057  O   ASN E 135       0.119-105.496  13.988  1.00 59.49           O  
ATOM   4058  CB  ASN E 135       3.025-106.425  12.695  1.00 57.92           C  
ATOM   4059  CG  ASN E 135       4.369-105.767  12.485  1.00 60.69           C  
ATOM   4060  OD1 ASN E 135       4.614-104.667  12.980  1.00 60.42           O  
ATOM   4061  ND2 ASN E 135       5.256-106.437  11.756  1.00 65.40           N  
ATOM   4062  N   ARG E 136       0.565-107.691  14.213  1.00 60.19           N  
ATOM   4063  CA  ARG E 136      -0.854-108.040  14.223  1.00 55.19           C  
ATOM   4064  C   ARG E 136      -1.547-107.480  15.458  1.00 56.63           C  
ATOM   4065  O   ARG E 136      -2.700-107.035  15.381  1.00 60.05           O  
ATOM   4066  CB  ARG E 136      -1.025-109.554  14.148  1.00 62.09           C  
ATOM   4067  CG  ARG E 136      -0.352-110.188  12.944  1.00 63.90           C  
ATOM   4068  CD  ARG E 136      -0.942-111.553  12.644  1.00 68.52           C  
ATOM   4069  NE  ARG E 136      -1.002-112.397  13.830  1.00 59.95           N  
ATOM   4070  CZ  ARG E 136      -0.019-113.209  14.220  1.00 70.06           C  
ATOM   4071  NH1 ARG E 136       1.103-113.282  13.520  1.00 67.95           N1+
ATOM   4072  NH2 ARG E 136      -0.163-113.944  15.317  1.00 74.06           N  
ATOM   4073  N   HIS E 137      -0.868-107.494  16.607  1.00 56.92           N  
ATOM   4074  CA  HIS E 137      -1.445-106.904  17.809  1.00 65.58           C  
ATOM   4075  C   HIS E 137      -1.659-105.405  17.634  1.00 60.43           C  
ATOM   4076  O   HIS E 137      -2.693-104.865  18.044  1.00 65.51           O  
ATOM   4077  CB  HIS E 137      -0.551-107.179  19.021  1.00 66.39           C  
ATOM   4078  CG  HIS E 137      -0.720-108.548  19.598  1.00 69.26           C  
ATOM   4079  ND1 HIS E 137      -1.825-109.335  19.349  1.00 70.13           N  
ATOM   4080  CD2 HIS E 137       0.076-109.273  20.423  1.00 61.80           C  
ATOM   4081  CE1 HIS E 137      -1.699-110.483  19.991  1.00 72.89           C  
ATOM   4082  NE2 HIS E 137      -0.557-110.469  20.651  1.00 68.16           N  
ATOM   4083  N   ALA E 138      -0.691-104.719  17.019  1.00 59.25           N  
ATOM   4084  CA  ALA E 138      -0.846-103.288  16.785  1.00 61.34           C  
ATOM   4085  C   ALA E 138      -1.876-103.017  15.695  1.00 60.57           C  
ATOM   4086  O   ALA E 138      -2.646-102.055  15.795  1.00 61.41           O  
ATOM   4087  CB  ALA E 138       0.504-102.665  16.428  1.00 54.31           C  
ATOM   4088  N   ARG E 139      -1.907-103.851  14.652  1.00 61.78           N  
ATOM   4089  CA  ARG E 139      -2.948-103.727  13.633  1.00 57.08           C  
ATOM   4090  C   ARG E 139      -4.332-103.928  14.235  1.00 63.94           C  
ATOM   4091  O   ARG E 139      -5.272-103.192  13.910  1.00 68.28           O  
ATOM   4092  CB  ARG E 139      -2.719-104.730  12.499  1.00 61.79           C  
ATOM   4093  CG  ARG E 139      -1.547-104.409  11.592  1.00 67.18           C  
ATOM   4094  CD  ARG E 139      -1.499-105.331  10.382  1.00 63.76           C  
ATOM   4095  NE  ARG E 139      -2.629-105.106   9.486  1.00 81.79           N  
ATOM   4096  CZ  ARG E 139      -2.639-104.208   8.510  1.00 88.06           C  
ATOM   4097  NH1 ARG E 139      -1.575-103.441   8.296  1.00 72.09           N1+
ATOM   4098  NH2 ARG E 139      -3.712-104.069   7.743  1.00 83.58           N  
ATOM   4099  N   GLU E 140      -4.475-104.920  15.116  1.00 65.37           N  
ATOM   4100  CA  GLU E 140      -5.764-105.168  15.747  1.00 60.61           C  
ATOM   4101  C   GLU E 140      -6.176-104.002  16.640  1.00 66.78           C  
ATOM   4102  O   GLU E 140      -7.348-103.600  16.639  1.00 66.95           O  
ATOM   4103  CB  GLU E 140      -5.709-106.469  16.546  1.00 65.85           C  
ATOM   4104  CG  GLU E 140      -6.890-106.678  17.482  1.00 77.40           C  
ATOM   4105  CD  GLU E 140      -6.720-107.892  18.375  1.00 84.68           C  
ATOM   4106  OE1 GLU E 140      -7.412-108.903  18.146  1.00 89.86           O  
ATOM   4107  OE2 GLU E 140      -5.882-107.835  19.305  1.00 78.44           O1-
ATOM   4108  N   TRP E 141      -5.233-103.445  17.403  1.00 65.91           N  
ATOM   4109  CA  TRP E 141      -5.571-102.345  18.304  1.00 62.08           C  
ATOM   4110  C   TRP E 141      -5.975-101.092  17.539  1.00 67.29           C  
ATOM   4111  O   TRP E 141      -6.774-100.293  18.038  1.00 66.66           O  
ATOM   4112  CB  TRP E 141      -4.402-102.039  19.235  1.00 63.11           C  
ATOM   4113  CG  TRP E 141      -4.338-102.940  20.432  1.00 66.88           C  
ATOM   4114  CD1 TRP E 141      -4.602-104.277  20.468  1.00 67.04           C  
ATOM   4115  CD2 TRP E 141      -4.009-102.557  21.774  1.00 61.28           C  
ATOM   4116  NE1 TRP E 141      -4.447-104.754  21.744  1.00 64.20           N  
ATOM   4117  CE2 TRP E 141      -4.084-103.720  22.568  1.00 64.33           C  
ATOM   4118  CE3 TRP E 141      -3.652-101.348  22.382  1.00 61.08           C  
ATOM   4119  CZ2 TRP E 141      -3.815-103.711  23.935  1.00 65.36           C  
ATOM   4120  CZ3 TRP E 141      -3.385-101.342  23.739  1.00 64.23           C  
ATOM   4121  CH2 TRP E 141      -3.470-102.515  24.500  1.00 68.69           C  
ATOM   4122  N   THR E 142      -5.436-100.897  16.330  1.00 70.41           N  
ATOM   4123  CA  THR E 142      -5.817 -99.729  15.543  1.00 72.27           C  
ATOM   4124  C   THR E 142      -7.239 -99.857  15.017  1.00 70.62           C  
ATOM   4125  O   THR E 142      -7.977 -98.865  14.959  1.00 71.01           O  
ATOM   4126  CB  THR E 142      -4.831 -99.525  14.395  1.00 70.44           C  
ATOM   4127  OG1 THR E 142      -4.686-100.748  13.664  1.00 78.32           O  
ATOM   4128  CG2 THR E 142      -3.476 -99.103  14.931  1.00 57.45           C  
ATOM   4129  N   GLN E 143      -7.649-101.069  14.627  1.00 72.83           N  
ATOM   4130  CA  GLN E 143      -9.032-101.271  14.203  1.00 69.40           C  
ATOM   4131  C   GLN E 143     -10.008-101.057  15.353  1.00 76.53           C  
ATOM   4132  O   GLN E 143     -11.118-100.555  15.138  1.00 79.83           O  
ATOM   4133  CB  GLN E 143      -9.201-102.670  13.610  1.00 65.21           C  
ATOM   4134  CG  GLN E 143     -10.643-103.030  13.270  1.00 83.20           C  
ATOM   4135  CD  GLN E 143     -10.777-104.412  12.670  1.00 84.47           C  
ATOM   4136  OE1 GLN E 143      -9.838-104.941  12.078  1.00 90.18           O  
ATOM   4137  NE2 GLN E 143     -11.957-105.010  12.820  1.00 80.79           N  
ATOM   4138  N   LYS E 144      -9.608-101.412  16.575  1.00 73.05           N  
ATOM   4139  CA  LYS E 144     -10.497-101.334  17.725  1.00 67.56           C  
ATOM   4140  C   LYS E 144     -10.380-100.023  18.491  1.00 70.79           C  
ATOM   4141  O   LYS E 144     -11.341 -99.637  19.167  1.00 68.97           O  
ATOM   4142  CB  LYS E 144     -10.221-102.498  18.687  1.00 71.57           C  
ATOM   4143  CG  LYS E 144     -10.905-103.818  18.325  1.00 81.02           C  
ATOM   4144  CD  LYS E 144     -10.382-104.406  17.018  1.00 78.93           C  
ATOM   4145  CE  LYS E 144     -10.918-105.806  16.778  1.00 82.03           C  
ATOM   4146  NZ  LYS E 144     -10.377-106.782  17.761  1.00 75.33           N1+
ATOM   4147  N   TYR E 145      -9.239 -99.334  18.396  1.00 66.93           N  
ATOM   4148  CA  TYR E 145      -8.948 -98.155  19.216  1.00 68.50           C  
ATOM   4149  C   TYR E 145      -9.083 -98.459  20.706  1.00 75.57           C  
ATOM   4150  O   TYR E 145      -9.462 -97.590  21.494  1.00 81.77           O  
ATOM   4151  CB  TYR E 145      -9.839 -96.964  18.838  1.00 65.52           C  
ATOM   4152  CG  TYR E 145      -9.518 -96.339  17.503  1.00 73.34           C  
ATOM   4153  CD1 TYR E 145      -8.267 -96.488  16.925  1.00 71.63           C  
ATOM   4154  CD2 TYR E 145     -10.474 -95.596  16.820  1.00 80.05           C  
ATOM   4155  CE1 TYR E 145      -7.973 -95.914  15.704  1.00 75.22           C  
ATOM   4156  CE2 TYR E 145     -10.193 -95.022  15.596  1.00 70.46           C  
ATOM   4157  CZ  TYR E 145      -8.940 -95.184  15.044  1.00 68.80           C  
ATOM   4158  OH  TYR E 145      -8.655 -94.611  13.827  1.00 73.35           O  
ATOM   4159  N   ALA E 146      -8.775 -99.691  21.102  1.00 69.28           N  
ATOM   4160  CA  ALA E 146      -8.915-100.111  22.490  1.00 68.22           C  
ATOM   4161  C   ALA E 146      -8.075-101.352  22.772  1.00 70.06           C  
ATOM   4162  O   ALA E 146      -8.514-102.259  23.479  1.00 75.19           O  
ATOM   4163  CB  ALA E 146     -10.377-100.375  22.823  1.00 69.43           C  
TER    4164      ALA E 146                                                      
HETATM 4816  O   HOH E 201       3.419-100.523  18.661  1.00 30.00           O  
HETATM 4817  O   HOH E 202       2.765 -88.328  27.990  1.00 30.00           O  
HETATM 4818  O   HOH E 203       6.479 -83.061  28.246  1.00 52.50           O  
HETATM 4819  O   HOH E 204       7.478 -79.874   9.264  1.00 51.75           O  
HETATM 4820  O   HOH E 205       9.309 -93.791  11.799  1.00 46.79           O  
HETATM 4821  O   HOH E 206       1.006 -99.736  24.114  1.00 51.54           O  
HETATM 4822  O   HOH E 207      13.521-102.125  15.185  1.00 63.54           O  
HETATM 4823  O   HOH E 208      -2.308 -99.510  18.383  1.00 53.32           O  
HETATM 4824  O   HOH E 209      13.719 -96.221  31.708  1.00 50.96           O  
HETATM 4825  O   HOH E 210       2.818 -75.539  16.166  1.00 50.02           O  
HETATM 4826  O   HOH E 211      16.372 -76.804  26.372  1.00 47.81           O  
HETATM 4827  O   HOH E 212       6.817 -65.471  23.683  1.00 41.72           O  
HETATM 4828  O   HOH E 213       4.599 -87.163  28.885  1.00 30.00           O  
HETATM 4829  O   HOH E 214       6.827 -62.862  31.419  1.00 71.61           O  
CONECT   94 4767                                                                
CONECT  114 4767                                                                
CONECT  208 4768                                                                
CONECT  219 4768                                                                
CONECT  247 4767                                                                
CONECT  263 4767                                                                
CONECT  373 4768                                                                
CONECT  395 4768                                                                
CONECT 2456 4770                                                                
CONECT 2476 4770                                                                
CONECT 2570 4769                                                                
CONECT 2581 4769                                                                
CONECT 2609 4770                                                                
CONECT 2625 4770                                                                
CONECT 2735 4769                                                                
CONECT 2757 4769                                                                
CONECT 4767   94  114  247  263                                                 
CONECT 4768  208  219  373  395                                                 
CONECT 4769 2570 2581 2735 2757                                                 
CONECT 4770 2456 2476 2609 2625                                                 
MASTER      336    0    4   21   26    0    9    6 4829    6   20   50          
END                                                                             



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