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Entry: 5HYN
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HEADER    TRANSFERASE                             01-FEB-16   5HYN              
TITLE     STRUCTURE OF HUMAN POLYCOMB REPRESSIVE COMPLEX 2 (PRC2) WITH ONCOGENIC
TITLE    2 HISTONE H3K27M PEPTIDE                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE EZH2;                   
COMPND   3 CHAIN: A, F, K, Q;                                                   
COMPND   4 SYNONYM: ENX-1,ENHANCER OF ZESTE HOMOLOG 2,LYSINE N-METHYLTRANSFERASE
COMPND   5 6;                                                                   
COMPND   6 EC: 2.1.1.43;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: POLYCOMB PROTEIN EED;                                      
COMPND  10 CHAIN: B, G, L, R;                                                   
COMPND  11 SYNONYM: HEED,WD PROTEIN ASSOCIATING WITH INTEGRIN CYTOPLASMIC TAILS 
COMPND  12 1,WAIT-1;                                                            
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MOL_ID: 3;                                                           
COMPND  15 MOLECULE: POLYCOMB PROTEIN SUZ12;                                    
COMPND  16 CHAIN: C, H, M, S;                                                   
COMPND  17 SYNONYM: CHROMATIN PRECIPITATED E2F TARGET 9 PROTEIN,CHET 9 PROTEIN, 
COMPND  18 JOINED TO JAZF1 PROTEIN,SUPPRESSOR OF ZESTE 12 PROTEIN HOMOLOG;      
COMPND  19 ENGINEERED: YES;                                                     
COMPND  20 MOL_ID: 4;                                                           
COMPND  21 MOLECULE: H3K27M;                                                    
COMPND  22 CHAIN: D, I, O, T;                                                   
COMPND  23 ENGINEERED: YES;                                                     
COMPND  24 MOL_ID: 5;                                                           
COMPND  25 MOLECULE: JARID2 K116ME3;                                            
COMPND  26 CHAIN: E, J, P, U;                                                   
COMPND  27 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: EZH2, KMT6;                                                    
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: EED;                                                           
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  17 ORGANISM_COMMON: HUMAN;                                              
SOURCE  18 ORGANISM_TAXID: 9606;                                                
SOURCE  19 GENE: SUZ12, CHET9, JJAZ1, KIAA0160;                                 
SOURCE  20 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  21 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  22 MOL_ID: 4;                                                           
SOURCE  23 SYNTHETIC: YES;                                                      
SOURCE  24 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  25 ORGANISM_TAXID: 9606;                                                
SOURCE  26 MOL_ID: 5;                                                           
SOURCE  27 SYNTHETIC: YES;                                                      
SOURCE  28 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  29 ORGANISM_TAXID: 9606                                                 
KEYWDS    CHROMATIN MODIFICATION COMPLEX, TRANSFERASE                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.ZHANG,N.JUSTIN,J.R.WILSON,S.J.GAMBLIN                               
REVDAT   1   11-MAY-16 5HYN    0                                                
JRNL        AUTH   N.JUSTIN,Y.ZHANG,C.TARRICONE,S.R.MARTIN,S.CHEN,E.UNDERWOOD,  
JRNL        AUTH 2 V.DE MARCO,L.F.HAIRE,P.A.WALKER,D.REINBERG,J.R.WILSON,       
JRNL        AUTH 3 S.J.GAMBLIN                                                  
JRNL        TITL   STRUCTURAL BASIS OF ONCOGENIC HISTONE H3K27M INHIBITION OF   
JRNL        TITL 2 HUMAN POLYCOMB REPRESSIVE COMPLEX 2.                         
JRNL        REF    NAT COMMUN                    V.   7 11316 2016              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   27121947                                                     
JRNL        DOI    10.1038/NCOMMS11316                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.95 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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 95.01                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 130834                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.222                           
REMARK   3   R VALUE            (WORKING SET) : 0.219                           
REMARK   3   FREE R VALUE                     : 0.273                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.950                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6476                            
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 95.0625 -  9.1637    0.98     4355   255  0.2106 0.2265        
REMARK   3     2  9.1637 -  7.2743    1.00     4258   225  0.1941 0.2287        
REMARK   3     3  7.2743 -  6.3550    1.00     4240   207  0.2164 0.2620        
REMARK   3     4  6.3550 -  5.7741    1.00     4194   238  0.2021 0.2514        
REMARK   3     5  5.7741 -  5.3602    1.00     4207   200  0.1898 0.2659        
REMARK   3     6  5.3602 -  5.0442    1.00     4167   218  0.1800 0.2310        
REMARK   3     7  5.0442 -  4.7916    1.00     4142   236  0.1692 0.2105        
REMARK   3     8  4.7916 -  4.5830    1.00     4171   197  0.1651 0.2355        
REMARK   3     9  4.5830 -  4.4066    1.00     4148   219  0.1730 0.2280        
REMARK   3    10  4.4066 -  4.2546    1.00     4122   234  0.1789 0.2412        
REMARK   3    11  4.2546 -  4.1215    1.00     4158   209  0.1908 0.2626        
REMARK   3    12  4.1215 -  4.0037    1.00     4131   202  0.2036 0.2554        
REMARK   3    13  4.0037 -  3.8983    1.00     4148   218  0.1989 0.2728        
REMARK   3    14  3.8983 -  3.8032    1.00     4141   214  0.2136 0.2737        
REMARK   3    15  3.8032 -  3.7167    1.00     4122   188  0.2170 0.2878        
REMARK   3    16  3.7167 -  3.6376    1.00     4112   230  0.2237 0.2765        
REMARK   3    17  3.6376 -  3.5649    1.00     4136   203  0.2317 0.2826        
REMARK   3    18  3.5649 -  3.4976    1.00     4111   202  0.2444 0.3099        
REMARK   3    19  3.4976 -  3.4351    1.00     4167   184  0.2493 0.3019        
REMARK   3    20  3.4351 -  3.3769    1.00     4092   220  0.2578 0.3214        
REMARK   3    21  3.3769 -  3.3224    1.00     4148   214  0.2814 0.3393        
REMARK   3    22  3.3224 -  3.2713    1.00     4084   239  0.2954 0.3763        
REMARK   3    23  3.2713 -  3.2232    1.00     4136   193  0.3000 0.3842        
REMARK   3    24  3.2232 -  3.1778    1.00     4091   217  0.3023 0.3664        
REMARK   3    25  3.1778 -  3.1348    1.00     4087   218  0.2997 0.3833        
REMARK   3    26  3.1348 -  3.0941    1.00     4119   209  0.3200 0.3920        
REMARK   3    27  3.0941 -  3.0554    1.00     4061   237  0.3247 0.3910        
REMARK   3    28  3.0554 -  3.0186    1.00     4128   212  0.3310 0.4356        
REMARK   3    29  3.0186 -  2.9835    1.00     4082   214  0.3551 0.3936        
REMARK   3    30  2.9835 -  2.9500    1.00     4100   224  0.3671 0.4325        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.500            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.320           
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      :  0.013          35790                                  
REMARK   3   ANGLE     :  1.523          48294                                  
REMARK   3   CHIRALITY :  0.074           5135                                  
REMARK   3   PLANARITY :  0.010           6253                                  
REMARK   3   DIHEDRAL  : 15.895          21664                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 20                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 10:246)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  70.3478 -71.2168  15.2517              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2763 T22:   0.4705                                     
REMARK   3      T33:   0.4275 T12:  -0.0381                                     
REMARK   3      T13:   0.0261 T23:   0.0031                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3331 L22:   0.3036                                     
REMARK   3      L33:   0.3375 L12:  -0.2535                                     
REMARK   3      L13:   0.1007 L23:   0.4874                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0387 S12:  -0.2570 S13:   0.0947                       
REMARK   3      S21:  -0.1479 S22:  -0.0095 S23:  -0.0177                       
REMARK   3      S31:   0.1086 S32:  -0.1322 S33:  -0.0000                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 262:476)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  44.0800 -70.4740 -34.0922              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3829 T22:   0.4782                                     
REMARK   3      T33:   0.4423 T12:   0.0151                                     
REMARK   3      T13:  -0.0097 T23:   0.0488                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0791 L22:   0.4132                                     
REMARK   3      L33:   0.1293 L12:  -0.0265                                     
REMARK   3      L13:  -0.0339 L23:  -0.2367                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0173 S12:   0.2166 S13:   0.0464                       
REMARK   3      S21:  -0.0291 S22:   0.0046 S23:   0.0146                       
REMARK   3      S31:   0.0946 S32:   0.1213 S33:   0.0000                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 522:750)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  73.5960 -96.7503 -15.4972              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3120 T22:   0.2972                                     
REMARK   3      T33:   0.3223 T12:   0.0204                                     
REMARK   3      T13:  -0.0065 T23:  -0.0052                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.0684 L22:   0.1997                                     
REMARK   3      L33:   0.4720 L12:  -0.0350                                     
REMARK   3      L13:   0.0378 L23:   0.2312                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0106 S12:   0.0585 S13:  -0.0279                       
REMARK   3      S21:   0.0584 S22:   0.0746 S23:  -0.0251                       
REMARK   3      S31:   0.0525 S32:   0.0429 S33:  -0.0000                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 77:438)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  64.0640 -81.5144  26.2770              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4031 T22:   0.6590                                     
REMARK   3      T33:   0.3801 T12:  -0.0625                                     
REMARK   3      T13:   0.0059 T23:  -0.0311                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3559 L22:   0.4841                                     
REMARK   3      L33:   0.7821 L12:  -0.0733                                     
REMARK   3      L13:   0.4910 L23:   0.1960                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0375 S12:  -0.2648 S13:   0.1106                       
REMARK   3      S21:   0.1199 S22:  -0.1091 S23:   0.0199                       
REMARK   3      S31:   0.1115 S32:  -0.2972 S33:   0.0000                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: (CHAIN C AND RESID 589:684)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  47.7266 -82.1232 -18.1243              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3294 T22:   0.5138                                     
REMARK   3      T33:   0.3898 T12:  -0.0198                                     
REMARK   3      T13:   0.0059 T23:   0.0390                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1143 L22:   0.2384                                     
REMARK   3      L33:   0.0665 L12:  -0.1615                                     
REMARK   3      L13:   0.0046 L23:  -0.1905                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0085 S12:  -0.2725 S13:  -0.0798                       
REMARK   3      S21:   0.0538 S22:   0.0880 S23:  -0.0105                       
REMARK   3      S31:   0.0488 S32:  -0.3470 S33:  -0.0000                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: (CHAIN F AND RESID 10:246)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.3164 -70.5034 -24.8669              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3041 T22:   0.6300                                     
REMARK   3      T33:   0.4264 T12:  -0.0906                                     
REMARK   3      T13:  -0.0320 T23:  -0.0414                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6339 L22:   0.6990                                     
REMARK   3      L33:   0.4823 L12:  -0.1201                                     
REMARK   3      L13:   0.3939 L23:  -0.3119                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0972 S12:   0.2774 S13:   0.2025                       
REMARK   3      S21:   0.2813 S22:  -0.0606 S23:   0.0625                       
REMARK   3      S31:   0.0705 S32:   0.1093 S33:  -0.0000                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: (CHAIN F AND RESID 262:476)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  19.3443 -68.7045  25.0938              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3813 T22:   0.6566                                     
REMARK   3      T33:   0.4083 T12:  -0.1155                                     
REMARK   3      T13:  -0.0471 T23:  -0.0825                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.0029 L22:   0.1428                                     
REMARK   3      L33:   0.2191 L12:   0.1882                                     
REMARK   3      L13:  -0.1053 L23:   0.0999                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0961 S12:   0.0672 S13:  -0.0213                       
REMARK   3      S21:   0.0434 S22:   0.1432 S23:   0.0210                       
REMARK   3      S31:  -0.1492 S32:   0.1356 S33:  -0.0000                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: (CHAIN F AND RESID 522:750)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.9053 -96.2046   5.7928              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2728 T22:   0.2692                                     
REMARK   3      T33:   0.3087 T12:  -0.0302                                     
REMARK   3      T13:   0.0275 T23:  -0.0090                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0003 L22:   0.6344                                     
REMARK   3      L33:   0.5321 L12:  -0.2014                                     
REMARK   3      L13:  -0.0727 L23:   0.0626                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0155 S12:  -0.0769 S13:  -0.0363                       
REMARK   3      S21:  -0.0640 S22:  -0.0073 S23:  -0.0036                       
REMARK   3      S31:   0.0376 S32:   0.0712 S33:   0.0000                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: (CHAIN G AND RESID 77:438)                             
REMARK   3    ORIGIN FOR THE GROUP (A):   0.5978 -79.0863 -35.5123              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2776 T22:   0.7512                                     
REMARK   3      T33:   0.3632 T12:  -0.0370                                     
REMARK   3      T13:  -0.0216 T23:   0.0204                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4932 L22:   0.5540                                     
REMARK   3      L33:   0.6473 L12:  -0.2833                                     
REMARK   3      L13:   0.2824 L23:  -0.2042                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0259 S12:   0.4820 S13:   0.0851                       
REMARK   3      S21:   0.0266 S22:  -0.1323 S23:  -0.0204                       
REMARK   3      S31:   0.0514 S32:   0.3985 S33:  -0.0000                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: (CHAIN H AND RESID 589:684)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  16.8405 -80.1452   8.9425              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3926 T22:   0.9148                                     
REMARK   3      T33:   0.4563 T12:  -0.0707                                     
REMARK   3      T13:   0.0128 T23:   0.0080                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1206 L22:   0.1636                                     
REMARK   3      L33:   0.1389 L12:   0.1009                                     
REMARK   3      L13:  -0.0654 L23:   0.2188                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0068 S12:   0.2160 S13:  -0.0116                       
REMARK   3      S21:  -0.1080 S22:  -0.0134 S23:   0.0468                       
REMARK   3      S31:   0.0245 S32:   0.7123 S33:   0.0000                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: (CHAIN K AND RESID 10:246)                             
REMARK   3    ORIGIN FOR THE GROUP (A): 103.3211 -56.3825 -61.4357              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3143 T22:   0.1126                                     
REMARK   3      T33:   0.2699 T12:  -0.1485                                     
REMARK   3      T13:  -0.0512 T23:  -0.0317                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4759 L22:   0.6064                                     
REMARK   3      L33:  -0.0389 L12:   0.3297                                     
REMARK   3      L13:   0.1049 L23:   0.4801                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2159 S12:   0.0478 S13:  -0.1239                       
REMARK   3      S21:  -0.1250 S22:  -0.0792 S23:  -0.0144                       
REMARK   3      S31:  -0.0409 S32:   0.5922 S33:  -0.0000                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: (CHAIN K AND RESID 262:476)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  96.0527 -32.3160-111.5367              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7117 T22:   0.5389                                     
REMARK   3      T33:   0.6433 T12:  -0.1240                                     
REMARK   3      T13:  -0.0340 T23:   0.2160                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0288 L22:  -0.0014                                     
REMARK   3      L33:   0.1995 L12:   0.0587                                     
REMARK   3      L13:  -0.1836 L23:  -0.0109                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1781 S12:   0.2507 S13:  -0.0123                       
REMARK   3      S21:  -0.1263 S22:  -0.1030 S23:   0.2165                       
REMARK   3      S31:   0.0740 S32:   0.5577 S33:   0.0000                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: (CHAIN K AND RESID 522:750)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  79.8932 -67.1571 -92.3491              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2975 T22:   0.2459                                     
REMARK   3      T33:   0.3271 T12:   0.0463                                     
REMARK   3      T13:  -0.0485 T23:  -0.0244                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3907 L22:   0.3448                                     
REMARK   3      L33:   0.6324 L12:   0.6403                                     
REMARK   3      L13:  -0.1052 L23:   0.2341                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1123 S12:  -0.0283 S13:   0.0935                       
REMARK   3      S21:  -0.0067 S22:  -0.0678 S23:   0.0103                       
REMARK   3      S31:   0.0526 S32:   0.0206 S33:   0.0000                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: (CHAIN L AND RESID 77:438)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  92.7342 -53.0488 -50.7854              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3617 T22:   0.2062                                     
REMARK   3      T33:   0.3978 T12:  -0.0719                                     
REMARK   3      T13:  -0.0413 T23:  -0.0651                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5717 L22:   0.4818                                     
REMARK   3      L33:   0.3581 L12:   0.0524                                     
REMARK   3      L13:   0.5419 L23:  -0.1795                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0768 S12:  -0.2841 S13:   0.0282                       
REMARK   3      S21:  -0.0680 S22:  -0.0546 S23:   0.0382                       
REMARK   3      S31:  -0.0860 S32:   0.1652 S33:  -0.0000                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: (CHAIN M AND RESID 589:684)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  86.1284 -38.5920 -95.2085              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5597 T22:   0.3886                                     
REMARK   3      T33:   0.5834 T12:  -0.0173                                     
REMARK   3      T13:   0.0248 T23:   0.0487                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0028 L22:   0.1571                                     
REMARK   3      L33:   0.0949 L12:  -0.0371                                     
REMARK   3      L13:  -0.0778 L23:   0.0731                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1588 S12:   0.1754 S13:  -0.0020                       
REMARK   3      S21:   0.1583 S22:  -0.1610 S23:   0.0255                       
REMARK   3      S31:  -0.1437 S32:   0.1283 S33:  -0.0000                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: (CHAIN Q AND RESID 10:246)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  27.1678 -28.5682 -51.9793              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3090 T22:   0.3006                                     
REMARK   3      T33:   0.2833 T12:  -0.0118                                     
REMARK   3      T13:   0.0249 T23:   0.0510                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5066 L22:   0.9457                                     
REMARK   3      L33:   0.0067 L12:   0.1596                                     
REMARK   3      L13:  -0.0115 L23:   0.0478                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0129 S12:   0.0680 S13:   0.0253                       
REMARK   3      S21:   0.0030 S22:   0.0138 S23:   0.2409                       
REMARK   3      S31:  -0.1422 S32:  -0.1488 S33:  -0.0000                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: (CHAIN Q AND RESID 262:476)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  34.8717 -52.9628-101.5491              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7278 T22:  -0.9873                                     
REMARK   3      T33:  -2.3292 T12:  -0.9657                                     
REMARK   3      T13:  -0.7044 T23:  -1.9923                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.0197 L22:  -0.0665                                     
REMARK   3      L33:   0.0937 L12:  -0.0440                                     
REMARK   3      L13:   0.0856 L23:   0.0348                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6082 S12:   2.1333 S13:   2.2425                       
REMARK   3      S21:  -0.2974 S22:  -0.3036 S23:  -0.1678                       
REMARK   3      S31:  -0.0196 S32:  -0.6997 S33:   0.0000                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: (CHAIN Q AND RESID 522:750)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  51.3675 -17.8945 -82.0975              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3221 T22:   0.3697                                     
REMARK   3      T33:   0.3095 T12:  -0.0423                                     
REMARK   3      T13:  -0.0077 T23:   0.0398                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0360 L22:   0.2755                                     
REMARK   3      L33:   0.4996 L12:   0.1270                                     
REMARK   3      L13:  -0.4311 L23:  -0.4314                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0821 S12:   0.0690 S13:  -0.0104                       
REMARK   3      S21:  -0.0297 S22:   0.0166 S23:  -0.0147                       
REMARK   3      S31:  -0.1315 S32:  -0.1211 S33:   0.0000                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: (CHAIN R AND RESID 77:438)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  36.8466 -31.9049 -41.3466              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3445 T22:   0.1498                                     
REMARK   3      T33:   0.3106 T12:  -0.0496                                     
REMARK   3      T13:  -0.0042 T23:   0.0123                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4850 L22:   0.4038                                     
REMARK   3      L33:   0.6453 L12:   0.0071                                     
REMARK   3      L13:  -0.1579 L23:   0.2521                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0013 S12:  -0.2316 S13:  -0.0205                       
REMARK   3      S21:  -0.0619 S22:   0.0501 S23:  -0.0488                       
REMARK   3      S31:   0.0392 S32:  -0.3057 S33:  -0.0000                       
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    SELECTION: (CHAIN S AND RESID 589:684)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  44.3777 -46.8397 -85.2903              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7563 T22:   0.1308                                     
REMARK   3      T33:   0.4845 T12:  -0.3990                                     
REMARK   3      T13:   0.0746 T23:  -0.0592                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0873 L22:   0.0849                                     
REMARK   3      L33:   0.0401 L12:   0.0639                                     
REMARK   3      L13:   0.0748 L23:   0.0657                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2085 S12:  -0.2212 S13:   0.1449                       
REMARK   3      S21:  -0.0989 S22:  -0.1476 S23:  -0.0856                       
REMARK   3      S31:   0.4307 S32:  -0.2314 S33:  -0.0000                       
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 5HYN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-FEB-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000217934.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-OCT-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5-6.8                            
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I03                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9763                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XIA2                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 132394                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.940                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 104.430                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 5.600                              
REMARK 200  R MERGE                    (I) : 0.16500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.94                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.02                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.60700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.33                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.82                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG3350, 400MM AMMONIAN CITRATE      
REMARK 280  PH6.5, VAPOR DIFFUSION, SITTING 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       65.82000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      137.27500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       85.75500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      137.27500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       65.82000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       85.75500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8                                  
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: PENTAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E                         
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 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, G, H, I, J                         
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: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: K, L, M, O, P                         
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: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: Q, R, S, T, U                         
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: 5                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 16660 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 50120 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -106.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
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: 6                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 16980 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 48710 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -107.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 7                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 16530 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 48620 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -74.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: K, L, M, O                            
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: 8                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 16660 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 48680 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -107.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: Q, R, S, T                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 465     GLN A     3                                                      
REMARK 465     THR A     4                                                      
REMARK 465     GLY A     5                                                      
REMARK 465     LYS A     6                                                      
REMARK 465     LYS A     7                                                      
REMARK 465     SER A     8                                                      
REMARK 465     GLU A     9                                                      
REMARK 465     ASP A   183                                                      
REMARK 465     ASP A   184                                                      
REMARK 465     ASP A   185                                                      
REMARK 465     ASP A   186                                                      
REMARK 465     ASP A   187                                                      
REMARK 465     ASP A   188                                                      
REMARK 465     ASP A   189                                                      
REMARK 465     GLY A   190                                                      
REMARK 465     ASP A   191                                                      
REMARK 465     ASP A   192                                                      
REMARK 465     PRO A   193                                                      
REMARK 465     GLU A   194                                                      
REMARK 465     GLU A   195                                                      
REMARK 465     ARG A   196                                                      
REMARK 465     GLU A   197                                                      
REMARK 465     GLU A   198                                                      
REMARK 465     LYS A   199                                                      
REMARK 465     GLN A   200                                                      
REMARK 465     LYS A   201                                                      
REMARK 465     ASP A   202                                                      
REMARK 465     LEU A   203                                                      
REMARK 465     GLU A   204                                                      
REMARK 465     ASP A   205                                                      
REMARK 465     HIS A   206                                                      
REMARK 465     ARG A   207                                                      
REMARK 465     ASP A   208                                                      
REMARK 465     ASP A   209                                                      
REMARK 465     LYS A   210                                                      
REMARK 465     LYS A   217                                                      
REMARK 465     PHE A   218                                                      
REMARK 465     PRO A   219                                                      
REMARK 465     GLN A   250                                                      
REMARK 465     GLN A   251                                                      
REMARK 465     LEU A   252                                                      
REMARK 465     PRO A   253                                                      
REMARK 465     GLY A   254                                                      
REMARK 465     ALA A   255                                                      
REMARK 465     LEU A   256                                                      
REMARK 465     PRO A   346                                                      
REMARK 465     PRO A   347                                                      
REMARK 465     LYS A   348                                                      
REMARK 465     ARG A   349                                                      
REMARK 465     PRO A   350                                                      
REMARK 465     GLY A   351                                                      
REMARK 465     GLY A   352                                                      
REMARK 465     ARG A   353                                                      
REMARK 465     ARG A   354                                                      
REMARK 465     ARG A   355                                                      
REMARK 465     GLY A   356                                                      
REMARK 465     ARG A   357                                                      
REMARK 465     LEU A   358                                                      
REMARK 465     PRO A   359                                                      
REMARK 465     ASN A   360                                                      
REMARK 465     ASN A   361                                                      
REMARK 465     SER A   362                                                      
REMARK 465     SER A   363                                                      
REMARK 465     ARG A   364                                                      
REMARK 465     PRO A   365                                                      
REMARK 465     SER A   366                                                      
REMARK 465     THR A   367                                                      
REMARK 465     PRO A   368                                                      
REMARK 465     THR A   369                                                      
REMARK 465     ILE A   370                                                      
REMARK 465     ASN A   371                                                      
REMARK 465     VAL A   372                                                      
REMARK 465     LEU A   373                                                      
REMARK 465     GLU A   374                                                      
REMARK 465     SER A   375                                                      
REMARK 465     LYS A   376                                                      
REMARK 465     ASP A   377                                                      
REMARK 465     THR A   378                                                      
REMARK 465     ASP A   379                                                      
REMARK 465     SER A   380                                                      
REMARK 465     ASP A   381                                                      
REMARK 465     ARG A   382                                                      
REMARK 465     GLU A   383                                                      
REMARK 465     ALA A   384                                                      
REMARK 465     GLY A   385                                                      
REMARK 465     THR A   386                                                      
REMARK 465     GLU A   387                                                      
REMARK 465     THR A   388                                                      
REMARK 465     GLY A   389                                                      
REMARK 465     GLY A   390                                                      
REMARK 465     GLU A   391                                                      
REMARK 465     ASN A   392                                                      
REMARK 465     ASN A   393                                                      
REMARK 465     ASP A   394                                                      
REMARK 465     LYS A   395                                                      
REMARK 465     GLU A   396                                                      
REMARK 465     GLU A   397                                                      
REMARK 465     GLU A   398                                                      
REMARK 465     GLU A   399                                                      
REMARK 465     LYS A   400                                                      
REMARK 465     LYS A   401                                                      
REMARK 465     ASP A   402                                                      
REMARK 465     GLU A   403                                                      
REMARK 465     THR A   404                                                      
REMARK 465     SER A   405                                                      
REMARK 465     SER A   406                                                      
REMARK 465     SER A   407                                                      
REMARK 465     SER A   408                                                      
REMARK 465     GLU A   409                                                      
REMARK 465     ALA A   410                                                      
REMARK 465     ASN A   411                                                      
REMARK 465     SER A   412                                                      
REMARK 465     ARG A   413                                                      
REMARK 465     CYS A   414                                                      
REMARK 465     GLN A   415                                                      
REMARK 465     THR A   416                                                      
REMARK 465     PRO A   417                                                      
REMARK 465     ILE A   418                                                      
REMARK 465     LYS A   419                                                      
REMARK 465     MET A   420                                                      
REMARK 465     LYS A   421                                                      
REMARK 465     ALA A   480                                                      
REMARK 465     PRO A   481                                                      
REMARK 465     ALA A   482                                                      
REMARK 465     GLU A   483                                                      
REMARK 465     ASP A   484                                                      
REMARK 465     VAL A   485                                                      
REMARK 465     ASP A   486                                                      
REMARK 465     THR A   487                                                      
REMARK 465     PRO A   488                                                      
REMARK 465     PRO A   489                                                      
REMARK 465     ARG A   490                                                      
REMARK 465     LYS A   491                                                      
REMARK 465     LYS A   492                                                      
REMARK 465     LYS A   493                                                      
REMARK 465     ARG A   494                                                      
REMARK 465     LYS A   495                                                      
REMARK 465     HIS A   496                                                      
REMARK 465     ARG A   497                                                      
REMARK 465     LEU A   498                                                      
REMARK 465     TRP A   499                                                      
REMARK 465     ALA A   500                                                      
REMARK 465     ALA A   501                                                      
REMARK 465     HIS A   502                                                      
REMARK 465     CYS A   503                                                      
REMARK 465     ARG A   504                                                      
REMARK 465     LYS A   505                                                      
REMARK 465     ILE A   506                                                      
REMARK 465     GLN A   507                                                      
REMARK 465     LEU A   508                                                      
REMARK 465     LYS A   509                                                      
REMARK 465     LYS A   510                                                      
REMARK 465     ASP A   511                                                      
REMARK 465     GLY A   512                                                      
REMARK 465     SER A   513                                                      
REMARK 465     SER A   514                                                      
REMARK 465     ASN A   515                                                      
REMARK 465     ARG A   741                                                      
REMARK 465     GLU A   742                                                      
REMARK 465     MET A   743                                                      
REMARK 465     GLU A   744                                                      
REMARK 465     ILE A   745                                                      
REMARK 465     PRO A   746                                                      
REMARK 465     GLY B    75                                                      
REMARK 465     SER B    76                                                      
REMARK 465     GLY C   557                                                      
REMARK 465     SER C   558                                                      
REMARK 465     SER C   559                                                      
REMARK 465     GLY C   560                                                      
REMARK 465     ALA D    21                                                      
REMARK 465     ALA D    31                                                      
REMARK 465     THR D    32                                                      
REMARK 465     GLY D    33                                                      
REMARK 465     GLN E    12                                                      
REMARK 465     MET F     1                                                      
REMARK 465     GLY F     2                                                      
REMARK 465     GLN F     3                                                      
REMARK 465     THR F     4                                                      
REMARK 465     GLY F     5                                                      
REMARK 465     LYS F     6                                                      
REMARK 465     LYS F     7                                                      
REMARK 465     SER F     8                                                      
REMARK 465     GLU F     9                                                      
REMARK 465     ASN F   182                                                      
REMARK 465     ASP F   183                                                      
REMARK 465     ASP F   184                                                      
REMARK 465     ASP F   185                                                      
REMARK 465     ASP F   186                                                      
REMARK 465     ASP F   187                                                      
REMARK 465     ASP F   188                                                      
REMARK 465     ASP F   189                                                      
REMARK 465     GLY F   190                                                      
REMARK 465     ASP F   191                                                      
REMARK 465     ASP F   192                                                      
REMARK 465     PRO F   193                                                      
REMARK 465     GLU F   194                                                      
REMARK 465     GLU F   195                                                      
REMARK 465     ARG F   196                                                      
REMARK 465     GLU F   197                                                      
REMARK 465     GLU F   198                                                      
REMARK 465     LYS F   199                                                      
REMARK 465     GLN F   200                                                      
REMARK 465     LYS F   201                                                      
REMARK 465     ASP F   202                                                      
REMARK 465     LEU F   203                                                      
REMARK 465     GLU F   204                                                      
REMARK 465     ASP F   205                                                      
REMARK 465     HIS F   206                                                      
REMARK 465     ARG F   207                                                      
REMARK 465     ASP F   208                                                      
REMARK 465     ASP F   209                                                      
REMARK 465     LYS F   210                                                      
REMARK 465     GLU F   211                                                      
REMARK 465     SER F   212                                                      
REMARK 465     ARG F   213                                                      
REMARK 465     PRO F   214                                                      
REMARK 465     PRO F   215                                                      
REMARK 465     ARG F   216                                                      
REMARK 465     LYS F   217                                                      
REMARK 465     PHE F   218                                                      
REMARK 465     GLU F   249                                                      
REMARK 465     GLN F   250                                                      
REMARK 465     GLN F   251                                                      
REMARK 465     LEU F   252                                                      
REMARK 465     PRO F   253                                                      
REMARK 465     GLY F   254                                                      
REMARK 465     ALA F   255                                                      
REMARK 465     LEU F   256                                                      
REMARK 465     PRO F   257                                                      
REMARK 465     PRO F   258                                                      
REMARK 465     PRO F   346                                                      
REMARK 465     PRO F   347                                                      
REMARK 465     LYS F   348                                                      
REMARK 465     ARG F   349                                                      
REMARK 465     PRO F   350                                                      
REMARK 465     GLY F   351                                                      
REMARK 465     GLY F   352                                                      
REMARK 465     ARG F   353                                                      
REMARK 465     ARG F   354                                                      
REMARK 465     ARG F   355                                                      
REMARK 465     GLY F   356                                                      
REMARK 465     ARG F   357                                                      
REMARK 465     LEU F   358                                                      
REMARK 465     PRO F   359                                                      
REMARK 465     ASN F   360                                                      
REMARK 465     ASN F   361                                                      
REMARK 465     SER F   362                                                      
REMARK 465     SER F   363                                                      
REMARK 465     ARG F   364                                                      
REMARK 465     PRO F   365                                                      
REMARK 465     SER F   366                                                      
REMARK 465     THR F   367                                                      
REMARK 465     PRO F   368                                                      
REMARK 465     THR F   369                                                      
REMARK 465     ILE F   370                                                      
REMARK 465     ASN F   371                                                      
REMARK 465     VAL F   372                                                      
REMARK 465     LEU F   373                                                      
REMARK 465     GLU F   374                                                      
REMARK 465     SER F   375                                                      
REMARK 465     LYS F   376                                                      
REMARK 465     ASP F   377                                                      
REMARK 465     THR F   378                                                      
REMARK 465     ASP F   379                                                      
REMARK 465     SER F   380                                                      
REMARK 465     ASP F   381                                                      
REMARK 465     ARG F   382                                                      
REMARK 465     GLU F   383                                                      
REMARK 465     ALA F   384                                                      
REMARK 465     GLY F   385                                                      
REMARK 465     THR F   386                                                      
REMARK 465     GLU F   387                                                      
REMARK 465     THR F   388                                                      
REMARK 465     GLY F   389                                                      
REMARK 465     GLY F   390                                                      
REMARK 465     GLU F   391                                                      
REMARK 465     ASN F   392                                                      
REMARK 465     ASN F   393                                                      
REMARK 465     ASP F   394                                                      
REMARK 465     LYS F   395                                                      
REMARK 465     GLU F   396                                                      
REMARK 465     GLU F   397                                                      
REMARK 465     GLU F   398                                                      
REMARK 465     GLU F   399                                                      
REMARK 465     LYS F   400                                                      
REMARK 465     LYS F   401                                                      
REMARK 465     ASP F   402                                                      
REMARK 465     GLU F   403                                                      
REMARK 465     THR F   404                                                      
REMARK 465     SER F   405                                                      
REMARK 465     SER F   406                                                      
REMARK 465     SER F   407                                                      
REMARK 465     SER F   408                                                      
REMARK 465     GLU F   409                                                      
REMARK 465     ALA F   410                                                      
REMARK 465     ASN F   411                                                      
REMARK 465     SER F   412                                                      
REMARK 465     ARG F   413                                                      
REMARK 465     CYS F   414                                                      
REMARK 465     GLN F   415                                                      
REMARK 465     THR F   416                                                      
REMARK 465     PRO F   417                                                      
REMARK 465     ILE F   418                                                      
REMARK 465     LYS F   419                                                      
REMARK 465     MET F   420                                                      
REMARK 465     LYS F   421                                                      
REMARK 465     PRO F   422                                                      
REMARK 465     ASN F   423                                                      
REMARK 465     PRO F   479                                                      
REMARK 465     ALA F   480                                                      
REMARK 465     PRO F   481                                                      
REMARK 465     ALA F   482                                                      
REMARK 465     GLU F   483                                                      
REMARK 465     ASP F   484                                                      
REMARK 465     VAL F   485                                                      
REMARK 465     ASP F   486                                                      
REMARK 465     THR F   487                                                      
REMARK 465     PRO F   488                                                      
REMARK 465     PRO F   489                                                      
REMARK 465     ARG F   490                                                      
REMARK 465     LYS F   491                                                      
REMARK 465     LYS F   492                                                      
REMARK 465     LYS F   493                                                      
REMARK 465     ARG F   494                                                      
REMARK 465     LYS F   495                                                      
REMARK 465     HIS F   496                                                      
REMARK 465     ARG F   497                                                      
REMARK 465     LEU F   498                                                      
REMARK 465     TRP F   499                                                      
REMARK 465     ALA F   500                                                      
REMARK 465     ALA F   501                                                      
REMARK 465     HIS F   502                                                      
REMARK 465     CYS F   503                                                      
REMARK 465     ARG F   504                                                      
REMARK 465     LYS F   505                                                      
REMARK 465     ILE F   506                                                      
REMARK 465     GLN F   507                                                      
REMARK 465     LEU F   508                                                      
REMARK 465     LYS F   509                                                      
REMARK 465     LYS F   510                                                      
REMARK 465     ASP F   511                                                      
REMARK 465     GLY F   512                                                      
REMARK 465     SER F   513                                                      
REMARK 465     SER F   514                                                      
REMARK 465     ASN F   515                                                      
REMARK 465     GLU F   740                                                      
REMARK 465     ARG F   741                                                      
REMARK 465     GLU F   742                                                      
REMARK 465     MET F   743                                                      
REMARK 465     GLU F   744                                                      
REMARK 465     ILE F   745                                                      
REMARK 465     PRO F   746                                                      
REMARK 465     GLY G    75                                                      
REMARK 465     SER G    76                                                      
REMARK 465     GLY H   557                                                      
REMARK 465     SER H   558                                                      
REMARK 465     SER H   559                                                      
REMARK 465     GLY H   560                                                      
REMARK 465     HIS H   561                                                      
REMARK 465     ALA I    21                                                      
REMARK 465     ALA I    31                                                      
REMARK 465     THR I    32                                                      
REMARK 465     GLY I    33                                                      
REMARK 465     ARG J     1                                                      
REMARK 465     GLN J    12                                                      
REMARK 465     MET K     1                                                      
REMARK 465     GLY K     2                                                      
REMARK 465     GLN K     3                                                      
REMARK 465     THR K     4                                                      
REMARK 465     GLY K     5                                                      
REMARK 465     LYS K     6                                                      
REMARK 465     LYS K     7                                                      
REMARK 465     SER K     8                                                      
REMARK 465     GLU K     9                                                      
REMARK 465     ASN K   182                                                      
REMARK 465     ASP K   183                                                      
REMARK 465     ASP K   184                                                      
REMARK 465     ASP K   185                                                      
REMARK 465     ASP K   186                                                      
REMARK 465     ASP K   187                                                      
REMARK 465     ASP K   188                                                      
REMARK 465     ASP K   189                                                      
REMARK 465     GLY K   190                                                      
REMARK 465     ASP K   191                                                      
REMARK 465     ASP K   192                                                      
REMARK 465     PRO K   193                                                      
REMARK 465     GLU K   194                                                      
REMARK 465     GLU K   195                                                      
REMARK 465     ARG K   196                                                      
REMARK 465     GLU K   197                                                      
REMARK 465     GLU K   198                                                      
REMARK 465     LYS K   199                                                      
REMARK 465     GLN K   200                                                      
REMARK 465     LYS K   201                                                      
REMARK 465     ASP K   202                                                      
REMARK 465     LEU K   203                                                      
REMARK 465     GLU K   204                                                      
REMARK 465     ASP K   205                                                      
REMARK 465     HIS K   206                                                      
REMARK 465     ARG K   207                                                      
REMARK 465     ASP K   208                                                      
REMARK 465     ASP K   209                                                      
REMARK 465     LYS K   210                                                      
REMARK 465     GLU K   211                                                      
REMARK 465     SER K   212                                                      
REMARK 465     ARG K   213                                                      
REMARK 465     PRO K   214                                                      
REMARK 465     PRO K   215                                                      
REMARK 465     ARG K   216                                                      
REMARK 465     LYS K   217                                                      
REMARK 465     PHE K   218                                                      
REMARK 465     THR K   248                                                      
REMARK 465     GLU K   249                                                      
REMARK 465     GLN K   250                                                      
REMARK 465     GLN K   251                                                      
REMARK 465     LEU K   252                                                      
REMARK 465     PRO K   253                                                      
REMARK 465     GLY K   254                                                      
REMARK 465     ALA K   255                                                      
REMARK 465     LEU K   256                                                      
REMARK 465     PRO K   257                                                      
REMARK 465     PRO K   258                                                      
REMARK 465     GLU K   259                                                      
REMARK 465     PRO K   346                                                      
REMARK 465     PRO K   347                                                      
REMARK 465     LYS K   348                                                      
REMARK 465     ARG K   349                                                      
REMARK 465     PRO K   350                                                      
REMARK 465     GLY K   351                                                      
REMARK 465     GLY K   352                                                      
REMARK 465     ARG K   353                                                      
REMARK 465     ARG K   354                                                      
REMARK 465     ARG K   355                                                      
REMARK 465     GLY K   356                                                      
REMARK 465     ARG K   357                                                      
REMARK 465     LEU K   358                                                      
REMARK 465     PRO K   359                                                      
REMARK 465     ASN K   360                                                      
REMARK 465     ASN K   361                                                      
REMARK 465     SER K   362                                                      
REMARK 465     SER K   363                                                      
REMARK 465     ARG K   364                                                      
REMARK 465     PRO K   365                                                      
REMARK 465     SER K   366                                                      
REMARK 465     THR K   367                                                      
REMARK 465     PRO K   368                                                      
REMARK 465     THR K   369                                                      
REMARK 465     ILE K   370                                                      
REMARK 465     ASN K   371                                                      
REMARK 465     VAL K   372                                                      
REMARK 465     LEU K   373                                                      
REMARK 465     GLU K   374                                                      
REMARK 465     SER K   375                                                      
REMARK 465     LYS K   376                                                      
REMARK 465     ASP K   377                                                      
REMARK 465     THR K   378                                                      
REMARK 465     ASP K   379                                                      
REMARK 465     SER K   380                                                      
REMARK 465     ASP K   381                                                      
REMARK 465     ARG K   382                                                      
REMARK 465     GLU K   383                                                      
REMARK 465     ALA K   384                                                      
REMARK 465     GLY K   385                                                      
REMARK 465     THR K   386                                                      
REMARK 465     GLU K   387                                                      
REMARK 465     THR K   388                                                      
REMARK 465     GLY K   389                                                      
REMARK 465     GLY K   390                                                      
REMARK 465     GLU K   391                                                      
REMARK 465     ASN K   392                                                      
REMARK 465     ASN K   393                                                      
REMARK 465     ASP K   394                                                      
REMARK 465     LYS K   395                                                      
REMARK 465     GLU K   396                                                      
REMARK 465     GLU K   397                                                      
REMARK 465     GLU K   398                                                      
REMARK 465     GLU K   399                                                      
REMARK 465     LYS K   400                                                      
REMARK 465     LYS K   401                                                      
REMARK 465     ASP K   402                                                      
REMARK 465     GLU K   403                                                      
REMARK 465     THR K   404                                                      
REMARK 465     SER K   405                                                      
REMARK 465     SER K   406                                                      
REMARK 465     SER K   407                                                      
REMARK 465     SER K   408                                                      
REMARK 465     GLU K   409                                                      
REMARK 465     ALA K   410                                                      
REMARK 465     ASN K   411                                                      
REMARK 465     SER K   412                                                      
REMARK 465     ARG K   413                                                      
REMARK 465     CYS K   414                                                      
REMARK 465     GLN K   415                                                      
REMARK 465     THR K   416                                                      
REMARK 465     PRO K   417                                                      
REMARK 465     ILE K   418                                                      
REMARK 465     LYS K   419                                                      
REMARK 465     MET K   420                                                      
REMARK 465     LYS K   421                                                      
REMARK 465     PRO K   422                                                      
REMARK 465     ALA K   480                                                      
REMARK 465     PRO K   481                                                      
REMARK 465     ALA K   482                                                      
REMARK 465     GLU K   483                                                      
REMARK 465     ASP K   484                                                      
REMARK 465     VAL K   485                                                      
REMARK 465     ASP K   486                                                      
REMARK 465     THR K   487                                                      
REMARK 465     PRO K   488                                                      
REMARK 465     PRO K   489                                                      
REMARK 465     ARG K   490                                                      
REMARK 465     LYS K   491                                                      
REMARK 465     LYS K   492                                                      
REMARK 465     LYS K   493                                                      
REMARK 465     ARG K   494                                                      
REMARK 465     LYS K   495                                                      
REMARK 465     HIS K   496                                                      
REMARK 465     ARG K   497                                                      
REMARK 465     LEU K   498                                                      
REMARK 465     TRP K   499                                                      
REMARK 465     ALA K   500                                                      
REMARK 465     ALA K   501                                                      
REMARK 465     HIS K   502                                                      
REMARK 465     CYS K   503                                                      
REMARK 465     ARG K   504                                                      
REMARK 465     LYS K   505                                                      
REMARK 465     ILE K   506                                                      
REMARK 465     GLN K   507                                                      
REMARK 465     LEU K   508                                                      
REMARK 465     LYS K   509                                                      
REMARK 465     LYS K   510                                                      
REMARK 465     ASP K   511                                                      
REMARK 465     GLY K   512                                                      
REMARK 465     SER K   513                                                      
REMARK 465     SER K   514                                                      
REMARK 465     ALA K   733                                                      
REMARK 465     LEU K   734                                                      
REMARK 465     LYS K   735                                                      
REMARK 465     TYR K   736                                                      
REMARK 465     VAL K   737                                                      
REMARK 465     GLY K   738                                                      
REMARK 465     ILE K   739                                                      
REMARK 465     GLU K   740                                                      
REMARK 465     ARG K   741                                                      
REMARK 465     GLU K   742                                                      
REMARK 465     MET K   743                                                      
REMARK 465     GLU K   744                                                      
REMARK 465     ILE K   745                                                      
REMARK 465     PRO K   746                                                      
REMARK 465     GLY L    75                                                      
REMARK 465     SER L    76                                                      
REMARK 465     GLY M   557                                                      
REMARK 465     SER M   558                                                      
REMARK 465     SER M   559                                                      
REMARK 465     GLY M   560                                                      
REMARK 465     ALA O    21                                                      
REMARK 465     ALA O    31                                                      
REMARK 465     THR O    32                                                      
REMARK 465     GLY O    33                                                      
REMARK 465     ARG P     1                                                      
REMARK 465     LEU P     2                                                      
REMARK 465     GLN P    12                                                      
REMARK 465     MET Q     1                                                      
REMARK 465     GLY Q     2                                                      
REMARK 465     GLN Q     3                                                      
REMARK 465     THR Q     4                                                      
REMARK 465     GLY Q     5                                                      
REMARK 465     LYS Q     6                                                      
REMARK 465     LYS Q     7                                                      
REMARK 465     SER Q     8                                                      
REMARK 465     GLU Q     9                                                      
REMARK 465     LYS Q    10                                                      
REMARK 465     GLY Q    11                                                      
REMARK 465     TYR Q   181                                                      
REMARK 465     ASN Q   182                                                      
REMARK 465     ASP Q   183                                                      
REMARK 465     ASP Q   184                                                      
REMARK 465     ASP Q   185                                                      
REMARK 465     ASP Q   186                                                      
REMARK 465     ASP Q   187                                                      
REMARK 465     ASP Q   188                                                      
REMARK 465     ASP Q   189                                                      
REMARK 465     GLY Q   190                                                      
REMARK 465     ASP Q   191                                                      
REMARK 465     ASP Q   192                                                      
REMARK 465     PRO Q   193                                                      
REMARK 465     GLU Q   194                                                      
REMARK 465     GLU Q   195                                                      
REMARK 465     ARG Q   196                                                      
REMARK 465     GLU Q   197                                                      
REMARK 465     GLU Q   198                                                      
REMARK 465     LYS Q   199                                                      
REMARK 465     GLN Q   200                                                      
REMARK 465     LYS Q   201                                                      
REMARK 465     ASP Q   202                                                      
REMARK 465     LEU Q   203                                                      
REMARK 465     GLU Q   204                                                      
REMARK 465     ASP Q   205                                                      
REMARK 465     HIS Q   206                                                      
REMARK 465     ARG Q   207                                                      
REMARK 465     ASP Q   208                                                      
REMARK 465     ASP Q   209                                                      
REMARK 465     LYS Q   210                                                      
REMARK 465     GLU Q   211                                                      
REMARK 465     SER Q   212                                                      
REMARK 465     ARG Q   213                                                      
REMARK 465     PRO Q   214                                                      
REMARK 465     PRO Q   215                                                      
REMARK 465     ARG Q   216                                                      
REMARK 465     LYS Q   217                                                      
REMARK 465     PHE Q   218                                                      
REMARK 465     GLU Q   249                                                      
REMARK 465     GLN Q   250                                                      
REMARK 465     GLN Q   251                                                      
REMARK 465     LEU Q   252                                                      
REMARK 465     PRO Q   253                                                      
REMARK 465     GLY Q   254                                                      
REMARK 465     ALA Q   255                                                      
REMARK 465     LEU Q   256                                                      
REMARK 465     PRO Q   257                                                      
REMARK 465     PRO Q   258                                                      
REMARK 465     PRO Q   346                                                      
REMARK 465     PRO Q   347                                                      
REMARK 465     LYS Q   348                                                      
REMARK 465     ARG Q   349                                                      
REMARK 465     PRO Q   350                                                      
REMARK 465     GLY Q   351                                                      
REMARK 465     GLY Q   352                                                      
REMARK 465     ARG Q   353                                                      
REMARK 465     ARG Q   354                                                      
REMARK 465     ARG Q   355                                                      
REMARK 465     GLY Q   356                                                      
REMARK 465     ARG Q   357                                                      
REMARK 465     LEU Q   358                                                      
REMARK 465     PRO Q   359                                                      
REMARK 465     ASN Q   360                                                      
REMARK 465     ASN Q   361                                                      
REMARK 465     SER Q   362                                                      
REMARK 465     SER Q   363                                                      
REMARK 465     ARG Q   364                                                      
REMARK 465     PRO Q   365                                                      
REMARK 465     SER Q   366                                                      
REMARK 465     THR Q   367                                                      
REMARK 465     PRO Q   368                                                      
REMARK 465     THR Q   369                                                      
REMARK 465     ILE Q   370                                                      
REMARK 465     ASN Q   371                                                      
REMARK 465     VAL Q   372                                                      
REMARK 465     LEU Q   373                                                      
REMARK 465     GLU Q   374                                                      
REMARK 465     SER Q   375                                                      
REMARK 465     LYS Q   376                                                      
REMARK 465     ASP Q   377                                                      
REMARK 465     THR Q   378                                                      
REMARK 465     ASP Q   379                                                      
REMARK 465     SER Q   380                                                      
REMARK 465     ASP Q   381                                                      
REMARK 465     ARG Q   382                                                      
REMARK 465     GLU Q   383                                                      
REMARK 465     ALA Q   384                                                      
REMARK 465     GLY Q   385                                                      
REMARK 465     THR Q   386                                                      
REMARK 465     GLU Q   387                                                      
REMARK 465     THR Q   388                                                      
REMARK 465     GLY Q   389                                                      
REMARK 465     GLY Q   390                                                      
REMARK 465     GLU Q   391                                                      
REMARK 465     ASN Q   392                                                      
REMARK 465     ASN Q   393                                                      
REMARK 465     ASP Q   394                                                      
REMARK 465     LYS Q   395                                                      
REMARK 465     GLU Q   396                                                      
REMARK 465     GLU Q   397                                                      
REMARK 465     GLU Q   398                                                      
REMARK 465     GLU Q   399                                                      
REMARK 465     LYS Q   400                                                      
REMARK 465     LYS Q   401                                                      
REMARK 465     ASP Q   402                                                      
REMARK 465     GLU Q   403                                                      
REMARK 465     THR Q   404                                                      
REMARK 465     SER Q   405                                                      
REMARK 465     SER Q   406                                                      
REMARK 465     SER Q   407                                                      
REMARK 465     SER Q   408                                                      
REMARK 465     GLU Q   409                                                      
REMARK 465     ALA Q   410                                                      
REMARK 465     ASN Q   411                                                      
REMARK 465     SER Q   412                                                      
REMARK 465     ARG Q   413                                                      
REMARK 465     CYS Q   414                                                      
REMARK 465     GLN Q   415                                                      
REMARK 465     THR Q   416                                                      
REMARK 465     PRO Q   417                                                      
REMARK 465     ILE Q   418                                                      
REMARK 465     LYS Q   419                                                      
REMARK 465     MET Q   420                                                      
REMARK 465     LYS Q   421                                                      
REMARK 465     PRO Q   422                                                      
REMARK 465     ASN Q   423                                                      
REMARK 465     ILE Q   424                                                      
REMARK 465     PRO Q   479                                                      
REMARK 465     ALA Q   480                                                      
REMARK 465     PRO Q   481                                                      
REMARK 465     ALA Q   482                                                      
REMARK 465     GLU Q   483                                                      
REMARK 465     ASP Q   484                                                      
REMARK 465     VAL Q   485                                                      
REMARK 465     ASP Q   486                                                      
REMARK 465     THR Q   487                                                      
REMARK 465     PRO Q   488                                                      
REMARK 465     PRO Q   489                                                      
REMARK 465     ARG Q   490                                                      
REMARK 465     LYS Q   491                                                      
REMARK 465     LYS Q   492                                                      
REMARK 465     LYS Q   493                                                      
REMARK 465     ARG Q   494                                                      
REMARK 465     LYS Q   495                                                      
REMARK 465     HIS Q   496                                                      
REMARK 465     ARG Q   497                                                      
REMARK 465     LEU Q   498                                                      
REMARK 465     TRP Q   499                                                      
REMARK 465     ALA Q   500                                                      
REMARK 465     ALA Q   501                                                      
REMARK 465     HIS Q   502                                                      
REMARK 465     CYS Q   503                                                      
REMARK 465     ARG Q   504                                                      
REMARK 465     LYS Q   505                                                      
REMARK 465     ILE Q   506                                                      
REMARK 465     GLN Q   507                                                      
REMARK 465     LEU Q   508                                                      
REMARK 465     LYS Q   509                                                      
REMARK 465     LYS Q   510                                                      
REMARK 465     ASP Q   511                                                      
REMARK 465     GLY Q   512                                                      
REMARK 465     SER Q   513                                                      
REMARK 465     SER Q   514                                                      
REMARK 465     GLU Q   740                                                      
REMARK 465     ARG Q   741                                                      
REMARK 465     GLU Q   742                                                      
REMARK 465     MET Q   743                                                      
REMARK 465     GLU Q   744                                                      
REMARK 465     ILE Q   745                                                      
REMARK 465     PRO Q   746                                                      
REMARK 465     GLY R    75                                                      
REMARK 465     SER R    76                                                      
REMARK 465     GLY S   557                                                      
REMARK 465     SER S   558                                                      
REMARK 465     SER S   559                                                      
REMARK 465     GLY S   560                                                      
REMARK 465     ALA T    21                                                      
REMARK 465     ALA T    31                                                      
REMARK 465     THR T    32                                                      
REMARK 465     GLY T    33                                                      
REMARK 465     ARG U     1                                                      
REMARK 465     GLN U    12                                                      
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   OH   TYR F    23     O    PHE F   165              1.87            
REMARK 500   OE2  GLU F   436     OG1  THR F   460              1.92            
REMARK 500   OD1  ASP Q   652     NH2  ARG T    26              1.93            
REMARK 500   OH   TYR Q    23     O    PHE Q   165              1.99            
REMARK 500   ND1  HIS R   305     OE1  GLU R   325              2.05            
REMARK 500   OE2  GLU L   131     NH2  ARG L   133              2.05            
REMARK 500   O    ILE G   274     OG   SER G   277              2.06            
REMARK 500   NH2  ARG F   161     OD2  ASP F   233              2.07            
REMARK 500   OD1  ASN F   688     N    SAH F  1009              2.07            
REMARK 500   OE2  GLU K    22     OH   TYR K   181              2.10            
REMARK 500   OG1  THR K   462     OE1  GLN K   465              2.11            
REMARK 500   OD1  ASP Q   142     OG1  THR Q   144              2.12            
REMARK 500   OD2  ASP Q   136     N    M3L U     7              2.13            
REMARK 500   NZ   LYS K   611     OE2  GLU M   586              2.13            
REMARK 500   OH   TYR A    23     O    PHE A   165              2.13            
REMARK 500   NZ   LYS G    79     OE2  GLU G   392              2.16            
REMARK 500   NZ   LYS B   197     O    ALA B   242              2.17            
REMARK 500   OG1  THR A   339     OD2  ASP A   449              2.17            
REMARK 500   OE2  GLU K   436     OG1  THR K   460              2.17            
REMARK 500   O    TRP Q   624     N    SAH Q  1009              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OG1  THR A   568     NH1  ARG Q   561     3644     2.11            
REMARK 500   NH1  ARG F   561     OG1  THR K   568     2545     2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    PHE A  32   CE1   PHE A  32   CZ      0.153                       
REMARK 500    ARG A  33   NE    ARG A  33   CZ     -0.160                       
REMARK 500    GLU A 249   CG    GLU A 249   CD      0.110                       
REMARK 500    GLU A 249   CD    GLU A 249   OE1     0.087                       
REMARK 500    TYR F 181   CB    TYR F 181   CG     -0.156                       
REMARK 500    TYR F 181   CD1   TYR F 181   CE1    -0.097                       
REMARK 500    CYS F 320   CB    CYS F 320   SG     -0.122                       
REMARK 500    PRO G 396   CD    PRO G 396   N       0.105                       
REMARK 500    GLY K  11   CA    GLY K  11   C      -0.099                       
REMARK 500    VAL M 581   CB    VAL M 581   CG2     0.136                       
REMARK 500    SER M 583   CB    SER M 583   OG      0.089                       
REMARK 500    PHE Q 224   CB    PHE Q 224   CG     -0.125                       
REMARK 500    TYR Q 661   CZ    TYR Q 661   CE2     0.086                       
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    ARG A  33   CA  -  CB  -  CG  ANGL. DEV. = -13.2 DEGREES          
REMARK 500    LEU A 315   CA  -  CB  -  CG  ANGL. DEV. =  14.8 DEGREES          
REMARK 500    CYS A 566   CA  -  CB  -  SG  ANGL. DEV. =   9.7 DEGREES          
REMARK 500    ARG C 575   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    LEU F  71   CA  -  CB  -  CG  ANGL. DEV. =  16.1 DEGREES          
REMARK 500    LEU F  98   CB  -  CG  -  CD2 ANGL. DEV. = -10.5 DEGREES          
REMARK 500    ARG F 161   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    TYR F 181   CA  -  CB  -  CG  ANGL. DEV. = -14.8 DEGREES          
REMARK 500    LEU F 240   CB  -  CG  -  CD2 ANGL. DEV. = -10.2 DEGREES          
REMARK 500    CYS F 562   CA  -  CB  -  SG  ANGL. DEV. =   7.7 DEGREES          
REMARK 500    ASP G 212   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    CYS G 324   CA  -  CB  -  SG  ANGL. DEV. = -15.7 DEGREES          
REMARK 500    ARG J   6   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.6 DEGREES          
REMARK 500    PRO K  12   C   -  N   -  CA  ANGL. DEV. =   9.9 DEGREES          
REMARK 500    VAL K  68   CG1 -  CB  -  CG2 ANGL. DEV. = -10.3 DEGREES          
REMARK 500    LYS K 222   CD  -  CE  -  NZ  ANGL. DEV. = -14.6 DEGREES          
REMARK 500    GLY K 321   N   -  CA  -  C   ANGL. DEV. = -17.4 DEGREES          
REMARK 500    CYS K 562   CA  -  CB  -  SG  ANGL. DEV. =   8.1 DEGREES          
REMARK 500    MET L 180   CB  -  CG  -  SD  ANGL. DEV. = -20.5 DEGREES          
REMARK 500    ASP M 582   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ASP M 582   CB  -  CG  -  OD2 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    ARG O  26   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ARG Q  33   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    ILE Q  70   CG1 -  CB  -  CG2 ANGL. DEV. = -22.4 DEGREES          
REMARK 500    MET Q 134   CA  -  CB  -  CG  ANGL. DEV. = -11.5 DEGREES          
REMARK 500    MET Q 134   N   -  CA  -  C   ANGL. DEV. =  17.1 DEGREES          
REMARK 500    GLY Q 135   N   -  CA  -  C   ANGL. DEV. = -15.3 DEGREES          
REMARK 500    LEU Q 443   CB  -  CG  -  CD1 ANGL. DEV. = -22.8 DEGREES          
REMARK 500    CYS R 324   CA  -  CB  -  SG  ANGL. DEV. = -14.2 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    VAL A  68       20.66    102.45                                   
REMARK 500    ASP A  90       -1.23     79.15                                   
REMARK 500    ASP A 265       45.44    -84.66                                   
REMARK 500    ALA A 331      -75.94    -80.17                                   
REMARK 500    TYR A 448       76.69     52.00                                   
REMARK 500    ASP A 531     -163.14   -121.63                                   
REMARK 500    GLN A 540       31.08     74.65                                   
REMARK 500    ALA A 564     -126.98   -134.66                                   
REMARK 500    CYS A 566       57.82     38.98                                   
REMARK 500    SER A 610       46.96    -85.42                                   
REMARK 500    MET A 662       -2.08     84.55                                   
REMARK 500    ASP A 732       59.40   -117.37                                   
REMARK 500    ALA A 733       55.89   -141.06                                   
REMARK 500    LYS A 735       -0.58     87.70                                   
REMARK 500    TYR A 736       30.13   -151.07                                   
REMARK 500    SER B 118     -132.89     49.86                                   
REMARK 500    HIS B 213       13.92     81.66                                   
REMARK 500    PHE B 229       72.53   -105.90                                   
REMARK 500    HIS B 258        4.43     81.31                                   
REMARK 500    ASN B 307     -167.88   -162.29                                   
REMARK 500    CYS B 324       33.65    -75.49                                   
REMARK 500    TYR B 365       37.68     72.65                                   
REMARK 500    ASP B 395      164.20     67.59                                   
REMARK 500    HIS B 397       68.86     33.03                                   
REMARK 500    LYS B 398     -111.56     41.10                                   
REMARK 500    ASP C 605       47.99     70.06                                   
REMARK 500    ARG F  78        5.28     87.89                                   
REMARK 500    ASP F  90       -8.19     94.71                                   
REMARK 500    GLU F 137       61.60     39.04                                   
REMARK 500    LEU F 139     -171.94     89.41                                   
REMARK 500    THR F 144       -5.58     71.52                                   
REMARK 500    LYS F 222       11.10     80.67                                   
REMARK 500    CYS F 260     -113.65     61.41                                   
REMARK 500    ALA F 331      -74.36   -102.41                                   
REMARK 500    ASN F 429       19.45     80.88                                   
REMARK 500    TYR F 447       73.37   -113.68                                   
REMARK 500    ASP F 449     -122.33     58.53                                   
REMARK 500    ALA F 564     -121.99   -143.20                                   
REMARK 500    ILE F 638      -60.16    -98.16                                   
REMARK 500    MET F 662        4.27     88.11                                   
REMARK 500    ARG F 727       31.11     72.46                                   
REMARK 500    LYS F 735     -110.84     35.97                                   
REMARK 500    SER G 118     -130.01     52.23                                   
REMARK 500    SER G 159       18.41     59.76                                   
REMARK 500    ARG G 169        2.15    -69.15                                   
REMARK 500    HIS G 213       10.70     80.14                                   
REMARK 500    ASP G 257        5.14    -67.91                                   
REMARK 500    CYS G 324       42.40    -76.99                                   
REMARK 500    SER G 422       21.33    -79.66                                   
REMARK 500    GLU H 580     -156.09     61.04                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      95 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 ASN A  102     ALA A  103                  146.38                    
REMARK 500 MET A  134     GLY A  135                 -145.91                    
REMARK 500 ALA F  564     GLN F  565                 -144.66                    
REMARK 500 GLU G  392     VAL G  393                 -149.66                    
REMARK 500 ASP G  395     PRO G  396                  -31.82                    
REMARK 500 GLU H  608     GLY H  609                  148.33                    
REMARK 500 GLN K  730     ALA K  731                  138.87                    
REMARK 500 VAL L  393     GLU L  394                 -141.14                    
REMARK 500 PRO L  396     HIS L  397                 -141.08                    
REMARK 500 SER Q   76     LEU Q   77                 -142.75                    
REMARK 500 ASN Q  102     ALA Q  103                  146.89                    
REMARK 500 THR Q  311     GLU Q  312                  141.69                    
REMARK 500 HIS Q  327     LEU Q  328                  147.00                    
REMARK 500 PRO R  396     HIS R  397                 -144.52                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    ARG L 355        -10.48                                           
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 A1001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 286   SG                                                     
REMARK 620 2 CYS A 289   SG  112.1                                              
REMARK 620 3 CYS A 294   SG   98.7 121.4                                        
REMARK 620 4 HIS A 297   ND1 105.2 100.5 118.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1002  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 320   SG                                                     
REMARK 620 2 CYS A 324   SG  120.8                                              
REMARK 620 3 CYS A 452   SG  108.5 111.4                                        
REMARK 620 4 CYS A 463   SG  110.0  89.4 116.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1004  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 523   SG                                                     
REMARK 620 2 HIS A 525   NE2 111.0                                              
REMARK 620 3 CYS A 530   SG  112.6 116.2                                        
REMARK 620 4 CYS A 534   SG   99.5  97.4 118.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1005  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 523   SG                                                     
REMARK 620 2 CYS A 536   SG  101.6                                              
REMARK 620 3 CYS A 543   SG  108.6 109.0                                        
REMARK 620 4 CYS A 547   SG  104.7 108.0 122.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1003  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 530   SG                                                     
REMARK 620 2 CYS A 543   SG  100.9                                              
REMARK 620 3 CYS A 549   SG  104.5 116.1                                        
REMARK 620 4 CYS A 553   SG  105.4 119.2 108.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1008  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 560   SG                                                     
REMARK 620 2 CYS A 562   SG  103.9                                              
REMARK 620 3 CYS A 566   SG  122.8 107.2                                        
REMARK 620 4 CYS A 571   SG  111.8  95.0 111.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1007  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 560   SG                                                     
REMARK 620 2 CYS A 573   SG  117.9                                              
REMARK 620 3 CYS A 580   SG  105.4 111.4                                        
REMARK 620 4 CYS A 585   SG  120.5  95.6 105.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1006  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 566   SG                                                     
REMARK 620 2 CYS A 580   SG  111.4                                              
REMARK 620 3 CYS A 588   SG  125.1 121.2                                        
REMARK 620 4 CYS A 601   SG   95.3 100.6  89.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN F1001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS F 286   SG                                                     
REMARK 620 2 CYS F 289   SG  111.8                                              
REMARK 620 3 CYS F 294   SG   94.0 109.6                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN F1002  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS F 320   SG                                                     
REMARK 620 2 CYS F 324   SG  126.3                                              
REMARK 620 3 CYS F 452   SG   89.0 103.8                                        
REMARK 620 4 CYS F 463   SG  123.3  98.0 115.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN F1005  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS F 523   SG                                                     
REMARK 620 2 CYS F 536   SG   99.9                                              
REMARK 620 3 CYS F 543   SG  108.9 108.9                                        
REMARK 620 4 CYS F 547   SG  102.2 113.3 121.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN F1004  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS F 523   SG                                                     
REMARK 620 2 HIS F 525   NE2 112.3                                              
REMARK 620 3 CYS F 530   SG  114.9 121.3                                        
REMARK 620 4 CYS F 534   SG  102.2  92.1 109.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN F1003  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS F 530   SG                                                     
REMARK 620 2 CYS F 543   SG   88.8                                              
REMARK 620 3 CYS F 549   SG  109.4 111.2                                        
REMARK 620 4 CYS F 553   SG  114.7 108.4 120.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN F1008  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS F 560   SG                                                     
REMARK 620 2 CYS F 562   SG  119.9                                              
REMARK 620 3 CYS F 566   SG  107.0  98.2                                        
REMARK 620 4 CYS F 571   SG  119.4 104.7 104.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN F1007  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS F 560   SG                                                     
REMARK 620 2 CYS F 573   SG  129.8                                              
REMARK 620 3 CYS F 580   SG  114.2 113.3                                        
REMARK 620 4 CYS F 585   SG  103.4  86.1  97.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN F1006  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS F 566   SG                                                     
REMARK 620 2 CYS F 580   SG  108.6                                              
REMARK 620 3 CYS F 588   SG  106.9 111.1                                        
REMARK 620 4 CYS F 601   SG  122.9 113.0  92.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN K1001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS K 286   SG                                                     
REMARK 620 2 CYS K 289   SG   94.7                                              
REMARK 620 3 CYS K 294   SG   97.5  96.9                                        
REMARK 620 4 HIS K 297   ND1 126.2 122.3 113.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN K1002  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS K 320   SG                                                     
REMARK 620 2 CYS K 452   SG  115.2                                              
REMARK 620 3 CYS K 463   SG  128.5 115.7                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN K1004  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS K 523   SG                                                     
REMARK 620 2 HIS K 525   NE2 113.1                                              
REMARK 620 3 CYS K 530   SG  114.6 106.8                                        
REMARK 620 4 CYS K 534   SG  107.7 102.0 112.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN K1005  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS K 523   SG                                                     
REMARK 620 2 CYS K 536   SG  114.1                                              
REMARK 620 3 CYS K 543   SG  104.5 109.6                                        
REMARK 620 4 CYS K 547   SG   97.3 115.4 115.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN K1003  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS K 530   SG                                                     
REMARK 620 2 CYS K 543   SG   99.1                                              
REMARK 620 3 CYS K 549   SG   99.1 111.1                                        
REMARK 620 4 CYS K 553   SG  109.8 116.8 117.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN K1008  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS K 560   SG                                                     
REMARK 620 2 CYS K 562   SG  122.1                                              
REMARK 620 3 CYS K 566   SG  108.6 106.3                                        
REMARK 620 4 CYS K 571   SG  124.0  94.8  97.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN K1007  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS K 560   SG                                                     
REMARK 620 2 CYS K 573   SG  123.2                                              
REMARK 620 3 CYS K 580   SG  100.4 120.4                                        
REMARK 620 4 CYS K 585   SG  102.5 102.5 105.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN K1006  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS K 566   SG                                                     
REMARK 620 2 CYS K 580   SG   95.9                                              
REMARK 620 3 CYS K 588   SG  115.3 114.7                                        
REMARK 620 4 CYS K 601   SG  115.3 108.8 106.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN Q1001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS Q 286   SG                                                     
REMARK 620 2 CYS Q 289   SG  100.3                                              
REMARK 620 3 CYS Q 294   SG  112.8 114.7                                        
REMARK 620 4 HIS Q 297   ND1 115.5 111.1 102.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN Q1002  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS Q 320   SG                                                     
REMARK 620 2 CYS Q 452   SG  110.3                                              
REMARK 620 3 CYS Q 463   SG  122.7  92.7                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN Q1004  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS Q 523   SG                                                     
REMARK 620 2 HIS Q 525   NE2 113.0                                              
REMARK 620 3 CYS Q 530   SG  108.2 110.2                                        
REMARK 620 4 CYS Q 534   SG  109.5 106.1 109.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN Q1005  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS Q 523   SG                                                     
REMARK 620 2 CYS Q 536   SG  105.1                                              
REMARK 620 3 CYS Q 543   SG  107.9 102.2                                        
REMARK 620 4 CYS Q 547   SG  104.5 119.2 117.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN Q1003  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS Q 530   SG                                                     
REMARK 620 2 CYS Q 543   SG   93.9                                              
REMARK 620 3 CYS Q 549   SG  112.5 119.8                                        
REMARK 620 4 CYS Q 553   SG  108.6 111.2 109.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN Q1007  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS Q 560   SG                                                     
REMARK 620 2 CYS Q 573   SG  139.5                                              
REMARK 620 3 CYS Q 580   SG   93.5 125.1                                        
REMARK 620 4 CYS Q 585   SG  102.3  90.9  89.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN Q1008  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS Q 560   SG                                                     
REMARK 620 2 CYS Q 562   SG  102.1                                              
REMARK 620 3 CYS Q 566   SG  117.7 114.7                                        
REMARK 620 4 CYS Q 571   SG  118.0  92.6 108.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN Q1006  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS Q 566   SG                                                     
REMARK 620 2 CYS Q 580   SG  100.5                                              
REMARK 620 3 CYS Q 588   SG  132.1 104.9                                        
REMARK 620 4 CYS Q 601   SG  113.5 103.8  98.9                                  
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 1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1005                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1006                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1007                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1008                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAH A 1009                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN F 1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN F 1002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN F 1003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN F 1004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN F 1005                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN F 1006                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN F 1007                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN F 1008                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAH F 1009                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN K 1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN K 1002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN K 1003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN K 1004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN K 1005                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN K 1006                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN K 1007                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN K 1008                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAH K 1009                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN Q 1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN Q 1002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN Q 1003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN Q 1004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN Q 1005                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN Q 1006                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN Q 1007                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN Q 1008                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAH Q 1009                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ARG J 6 and M3L J 7    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide M3L J 7 and PHE J 8    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ARG P 6 and M3L P 7    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide M3L P 7 and PHE P 8    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ARG U 6 and M3L U 7    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide M3L U 7 and PHE U 8    
DBREF  5HYN A    1   746  UNP    Q15910   EZH2_HUMAN       1    746             
DBREF  5HYN B   77   441  UNP    O75530   EED_HUMAN       77    441             
DBREF  5HYN C  558   685  UNP    Q15022   SUZ12_HUMAN    558    685             
DBREF  5HYN D   21    33  PDB    5HYN     5HYN            21     33             
DBREF  5HYN E    1    12  PDB    5HYN     5HYN             1     12             
DBREF  5HYN F    1   746  UNP    Q15910   EZH2_HUMAN       1    746             
DBREF  5HYN G   77   441  UNP    O75530   EED_HUMAN       77    441             
DBREF  5HYN H  558   685  UNP    Q15022   SUZ12_HUMAN    558    685             
DBREF  5HYN I   21    33  PDB    5HYN     5HYN            21     33             
DBREF  5HYN J    1    12  PDB    5HYN     5HYN             1     12             
DBREF  5HYN K    1   746  UNP    Q15910   EZH2_HUMAN       1    746             
DBREF  5HYN L   77   441  UNP    O75530   EED_HUMAN       77    441             
DBREF  5HYN M  558   685  UNP    Q15022   SUZ12_HUMAN    558    685             
DBREF  5HYN O   21    33  PDB    5HYN     5HYN            21     33             
DBREF  5HYN P    1    12  PDB    5HYN     5HYN             1     12             
DBREF  5HYN Q    1   746  UNP    Q15910   EZH2_HUMAN       1    746             
DBREF  5HYN R   77   441  UNP    O75530   EED_HUMAN       77    441             
DBREF  5HYN S  558   685  UNP    Q15022   SUZ12_HUMAN    558    685             
DBREF  5HYN T   21    33  PDB    5HYN     5HYN            21     33             
DBREF  5HYN U    1    12  PDB    5HYN     5HYN             1     12             
SEQADV 5HYN GLY B   75  UNP  O75530              EXPRESSION TAG                 
SEQADV 5HYN SER B   76  UNP  O75530              EXPRESSION TAG                 
SEQADV 5HYN GLY C  557  UNP  Q15022              EXPRESSION TAG                 
SEQADV 5HYN GLY G   75  UNP  O75530              EXPRESSION TAG                 
SEQADV 5HYN SER G   76  UNP  O75530              EXPRESSION TAG                 
SEQADV 5HYN GLY H  557  UNP  Q15022              EXPRESSION TAG                 
SEQADV 5HYN GLY L   75  UNP  O75530              EXPRESSION TAG                 
SEQADV 5HYN SER L   76  UNP  O75530              EXPRESSION TAG                 
SEQADV 5HYN GLY M  557  UNP  Q15022              EXPRESSION TAG                 
SEQADV 5HYN GLY R   75  UNP  O75530              EXPRESSION TAG                 
SEQADV 5HYN SER R   76  UNP  O75530              EXPRESSION TAG                 
SEQADV 5HYN GLY S  557  UNP  Q15022              EXPRESSION TAG                 
SEQRES   1 A  746  MET GLY GLN THR GLY LYS LYS SER GLU LYS GLY PRO VAL          
SEQRES   2 A  746  CYS TRP ARG LYS ARG VAL LYS SER GLU TYR MET ARG LEU          
SEQRES   3 A  746  ARG GLN LEU LYS ARG PHE ARG ARG ALA ASP GLU VAL LYS          
SEQRES   4 A  746  SER MET PHE SER SER ASN ARG GLN LYS ILE LEU GLU ARG          
SEQRES   5 A  746  THR GLU ILE LEU ASN GLN GLU TRP LYS GLN ARG ARG ILE          
SEQRES   6 A  746  GLN PRO VAL HIS ILE LEU THR SER VAL SER SER LEU ARG          
SEQRES   7 A  746  GLY THR ARG GLU CYS SER VAL THR SER ASP LEU ASP PHE          
SEQRES   8 A  746  PRO THR GLN VAL ILE PRO LEU LYS THR LEU ASN ALA VAL          
SEQRES   9 A  746  ALA SER VAL PRO ILE MET TYR SER TRP SER PRO LEU GLN          
SEQRES  10 A  746  GLN ASN PHE MET VAL GLU ASP GLU THR VAL LEU HIS ASN          
SEQRES  11 A  746  ILE PRO TYR MET GLY ASP GLU VAL LEU ASP GLN ASP GLY          
SEQRES  12 A  746  THR PHE ILE GLU GLU LEU ILE LYS ASN TYR ASP GLY LYS          
SEQRES  13 A  746  VAL HIS GLY ASP ARG GLU CYS GLY PHE ILE ASN ASP GLU          
SEQRES  14 A  746  ILE PHE VAL GLU LEU VAL ASN ALA LEU GLY GLN TYR ASN          
SEQRES  15 A  746  ASP ASP ASP ASP ASP ASP ASP GLY ASP ASP PRO GLU GLU          
SEQRES  16 A  746  ARG GLU GLU LYS GLN LYS ASP LEU GLU ASP HIS ARG ASP          
SEQRES  17 A  746  ASP LYS GLU SER ARG PRO PRO ARG LYS PHE PRO SER ASP          
SEQRES  18 A  746  LYS ILE PHE GLU ALA ILE SER SER MET PHE PRO ASP LYS          
SEQRES  19 A  746  GLY THR ALA GLU GLU LEU LYS GLU LYS TYR LYS GLU LEU          
SEQRES  20 A  746  THR GLU GLN GLN LEU PRO GLY ALA LEU PRO PRO GLU CYS          
SEQRES  21 A  746  THR PRO ASN ILE ASP GLY PRO ASN ALA LYS SER VAL GLN          
SEQRES  22 A  746  ARG GLU GLN SER LEU HIS SER PHE HIS THR LEU PHE CYS          
SEQRES  23 A  746  ARG ARG CYS PHE LYS TYR ASP CYS PHE LEU HIS PRO PHE          
SEQRES  24 A  746  HIS ALA THR PRO ASN THR TYR LYS ARG LYS ASN THR GLU          
SEQRES  25 A  746  THR ALA LEU ASP ASN LYS PRO CYS GLY PRO GLN CYS TYR          
SEQRES  26 A  746  GLN HIS LEU GLU GLY ALA LYS GLU PHE ALA ALA ALA LEU          
SEQRES  27 A  746  THR ALA GLU ARG ILE LYS THR PRO PRO LYS ARG PRO GLY          
SEQRES  28 A  746  GLY ARG ARG ARG GLY ARG LEU PRO ASN ASN SER SER ARG          
SEQRES  29 A  746  PRO SER THR PRO THR ILE ASN VAL LEU GLU SER LYS ASP          
SEQRES  30 A  746  THR ASP SER ASP ARG GLU ALA GLY THR GLU THR GLY GLY          
SEQRES  31 A  746  GLU ASN ASN ASP LYS GLU GLU GLU GLU LYS LYS ASP GLU          
SEQRES  32 A  746  THR SER SER SER SER GLU ALA ASN SER ARG CYS GLN THR          
SEQRES  33 A  746  PRO ILE LYS MET LYS PRO ASN ILE GLU PRO PRO GLU ASN          
SEQRES  34 A  746  VAL GLU TRP SER GLY ALA GLU ALA SER MET PHE ARG VAL          
SEQRES  35 A  746  LEU ILE GLY THR TYR TYR ASP ASN PHE CYS ALA ILE ALA          
SEQRES  36 A  746  ARG LEU ILE GLY THR LYS THR CYS ARG GLN VAL TYR GLU          
SEQRES  37 A  746  PHE ARG VAL LYS GLU SER SER ILE ILE ALA PRO ALA PRO          
SEQRES  38 A  746  ALA GLU ASP VAL ASP THR PRO PRO ARG LYS LYS LYS ARG          
SEQRES  39 A  746  LYS HIS ARG LEU TRP ALA ALA HIS CYS ARG LYS ILE GLN          
SEQRES  40 A  746  LEU LYS LYS ASP GLY SER SER ASN HIS VAL TYR ASN TYR          
SEQRES  41 A  746  GLN PRO CYS ASP HIS PRO ARG GLN PRO CYS ASP SER SER          
SEQRES  42 A  746  CYS PRO CYS VAL ILE ALA GLN ASN PHE CYS GLU LYS PHE          
SEQRES  43 A  746  CYS GLN CYS SER SER GLU CYS GLN ASN ARG PHE PRO GLY          
SEQRES  44 A  746  CYS ARG CYS LYS ALA GLN CYS ASN THR LYS GLN CYS PRO          
SEQRES  45 A  746  CYS TYR LEU ALA VAL ARG GLU CYS ASP PRO ASP LEU CYS          
SEQRES  46 A  746  LEU THR CYS GLY ALA ALA ASP HIS TRP ASP SER LYS ASN          
SEQRES  47 A  746  VAL SER CYS LYS ASN CYS SER ILE GLN ARG GLY SER LYS          
SEQRES  48 A  746  LYS HIS LEU LEU LEU ALA PRO SER ASP VAL ALA GLY TRP          
SEQRES  49 A  746  GLY ILE PHE ILE LYS ASP PRO VAL GLN LYS ASN GLU PHE          
SEQRES  50 A  746  ILE SER GLU TYR CYS GLY GLU ILE ILE SER GLN ASP GLU          
SEQRES  51 A  746  ALA ASP ARG ARG GLY LYS VAL TYR ASP LYS TYR MET CYS          
SEQRES  52 A  746  SER PHE LEU PHE ASN LEU ASN ASN ASP PHE VAL VAL ASP          
SEQRES  53 A  746  ALA THR ARG LYS GLY ASN LYS ILE ARG PHE ALA ASN HIS          
SEQRES  54 A  746  SER VAL ASN PRO ASN CYS TYR ALA LYS VAL MET MET VAL          
SEQRES  55 A  746  ASN GLY ASP HIS ARG ILE GLY ILE PHE ALA LYS ARG ALA          
SEQRES  56 A  746  ILE GLN THR GLY GLU GLU LEU PHE PHE ASP TYR ARG TYR          
SEQRES  57 A  746  SER GLN ALA ASP ALA LEU LYS TYR VAL GLY ILE GLU ARG          
SEQRES  58 A  746  GLU MET GLU ILE PRO                                          
SEQRES   1 B  367  GLY SER LYS CYS LYS TYR SER PHE LYS CYS VAL ASN SER          
SEQRES   2 B  367  LEU LYS GLU ASP HIS ASN GLN PRO LEU PHE GLY VAL GLN          
SEQRES   3 B  367  PHE ASN TRP HIS SER LYS GLU GLY ASP PRO LEU VAL PHE          
SEQRES   4 B  367  ALA THR VAL GLY SER ASN ARG VAL THR LEU TYR GLU CYS          
SEQRES   5 B  367  HIS SER GLN GLY GLU ILE ARG LEU LEU GLN SER TYR VAL          
SEQRES   6 B  367  ASP ALA ASP ALA ASP GLU ASN PHE TYR THR CYS ALA TRP          
SEQRES   7 B  367  THR TYR ASP SER ASN THR SER HIS PRO LEU LEU ALA VAL          
SEQRES   8 B  367  ALA GLY SER ARG GLY ILE ILE ARG ILE ILE ASN PRO ILE          
SEQRES   9 B  367  THR MET GLN CYS ILE LYS HIS TYR VAL GLY HIS GLY ASN          
SEQRES  10 B  367  ALA ILE ASN GLU LEU LYS PHE HIS PRO ARG ASP PRO ASN          
SEQRES  11 B  367  LEU LEU LEU SER VAL SER LYS ASP HIS ALA LEU ARG LEU          
SEQRES  12 B  367  TRP ASN ILE GLN THR ASP THR LEU VAL ALA ILE PHE GLY          
SEQRES  13 B  367  GLY VAL GLU GLY HIS ARG ASP GLU VAL LEU SER ALA ASP          
SEQRES  14 B  367  TYR ASP LEU LEU GLY GLU LYS ILE MET SER CYS GLY MET          
SEQRES  15 B  367  ASP HIS SER LEU LYS LEU TRP ARG ILE ASN SER LYS ARG          
SEQRES  16 B  367  MET MET ASN ALA ILE LYS GLU SER TYR ASP TYR ASN PRO          
SEQRES  17 B  367  ASN LYS THR ASN ARG PRO PHE ILE SER GLN LYS ILE HIS          
SEQRES  18 B  367  PHE PRO ASP PHE SER THR ARG ASP ILE HIS ARG ASN TYR          
SEQRES  19 B  367  VAL ASP CYS VAL ARG TRP LEU GLY ASP LEU ILE LEU SER          
SEQRES  20 B  367  LYS SER CYS GLU ASN ALA ILE VAL CYS TRP LYS PRO GLY          
SEQRES  21 B  367  LYS MET GLU ASP ASP ILE ASP LYS ILE LYS PRO SER GLU          
SEQRES  22 B  367  SER ASN VAL THR ILE LEU GLY ARG PHE ASP TYR SER GLN          
SEQRES  23 B  367  CYS ASP ILE TRP TYR MET ARG PHE SER MET ASP PHE TRP          
SEQRES  24 B  367  GLN LYS MET LEU ALA LEU GLY ASN GLN VAL GLY LYS LEU          
SEQRES  25 B  367  TYR VAL TRP ASP LEU GLU VAL GLU ASP PRO HIS LYS ALA          
SEQRES  26 B  367  LYS CYS THR THR LEU THR HIS HIS LYS CYS GLY ALA ALA          
SEQRES  27 B  367  ILE ARG GLN THR SER PHE SER ARG ASP SER SER ILE LEU          
SEQRES  28 B  367  ILE ALA VAL CYS ASP ASP ALA SER ILE TRP ARG TRP ASP          
SEQRES  29 B  367  ARG LEU ARG                                                  
SEQRES   1 C  129  GLY SER SER GLY HIS ASN ARG LEU TYR PHE HIS SER ASP          
SEQRES   2 C  129  THR CYS LEU PRO LEU ARG PRO GLN GLU MET GLU VAL ASP          
SEQRES   3 C  129  SER GLU ASP GLU LYS ASP PRO GLU TRP LEU ARG GLU LYS          
SEQRES   4 C  129  THR ILE THR GLN ILE GLU GLU PHE SER ASP VAL ASN GLU          
SEQRES   5 C  129  GLY GLU LYS GLU VAL MET LYS LEU TRP ASN LEU HIS VAL          
SEQRES   6 C  129  MET LYS HIS GLY PHE ILE ALA ASP ASN GLN MET ASN HIS          
SEQRES   7 C  129  ALA CYS MET LEU PHE VAL GLU ASN TYR GLY GLN LYS ILE          
SEQRES   8 C  129  ILE LYS LYS ASN LEU CYS ARG ASN PHE MET LEU HIS LEU          
SEQRES   9 C  129  VAL SER MET HIS ASP PHE ASN LEU ILE SER ILE MET SER          
SEQRES  10 C  129  ILE ASP LYS ALA VAL THR LYS LEU ARG GLU MET GLN              
SEQRES   1 D   13  ALA THR LYS ALA ALA ARG MET SER ALA PRO ALA THR GLY          
SEQRES   1 E   12  ARG LEU GLN ALA GLN ARG M3L PHE ALA GLN SER GLN              
SEQRES   1 F  746  MET GLY GLN THR GLY LYS LYS SER GLU LYS GLY PRO VAL          
SEQRES   2 F  746  CYS TRP ARG LYS ARG VAL LYS SER GLU TYR MET ARG LEU          
SEQRES   3 F  746  ARG GLN LEU LYS ARG PHE ARG ARG ALA ASP GLU VAL LYS          
SEQRES   4 F  746  SER MET PHE SER SER ASN ARG GLN LYS ILE LEU GLU ARG          
SEQRES   5 F  746  THR GLU ILE LEU ASN GLN GLU TRP LYS GLN ARG ARG ILE          
SEQRES   6 F  746  GLN PRO VAL HIS ILE LEU THR SER VAL SER SER LEU ARG          
SEQRES   7 F  746  GLY THR ARG GLU CYS SER VAL THR SER ASP LEU ASP PHE          
SEQRES   8 F  746  PRO THR GLN VAL ILE PRO LEU LYS THR LEU ASN ALA VAL          
SEQRES   9 F  746  ALA SER VAL PRO ILE MET TYR SER TRP SER PRO LEU GLN          
SEQRES  10 F  746  GLN ASN PHE MET VAL GLU ASP GLU THR VAL LEU HIS ASN          
SEQRES  11 F  746  ILE PRO TYR MET GLY ASP GLU VAL LEU ASP GLN ASP GLY          
SEQRES  12 F  746  THR PHE ILE GLU GLU LEU ILE LYS ASN TYR ASP GLY LYS          
SEQRES  13 F  746  VAL HIS GLY ASP ARG GLU CYS GLY PHE ILE ASN ASP GLU          
SEQRES  14 F  746  ILE PHE VAL GLU LEU VAL ASN ALA LEU GLY GLN TYR ASN          
SEQRES  15 F  746  ASP ASP ASP ASP ASP ASP ASP GLY ASP ASP PRO GLU GLU          
SEQRES  16 F  746  ARG GLU GLU LYS GLN LYS ASP LEU GLU ASP HIS ARG ASP          
SEQRES  17 F  746  ASP LYS GLU SER ARG PRO PRO ARG LYS PHE PRO SER ASP          
SEQRES  18 F  746  LYS ILE PHE GLU ALA ILE SER SER MET PHE PRO ASP LYS          
SEQRES  19 F  746  GLY THR ALA GLU GLU LEU LYS GLU LYS TYR LYS GLU LEU          
SEQRES  20 F  746  THR GLU GLN GLN LEU PRO GLY ALA LEU PRO PRO GLU CYS          
SEQRES  21 F  746  THR PRO ASN ILE ASP GLY PRO ASN ALA LYS SER VAL GLN          
SEQRES  22 F  746  ARG GLU GLN SER LEU HIS SER PHE HIS THR LEU PHE CYS          
SEQRES  23 F  746  ARG ARG CYS PHE LYS TYR ASP CYS PHE LEU HIS PRO PHE          
SEQRES  24 F  746  HIS ALA THR PRO ASN THR TYR LYS ARG LYS ASN THR GLU          
SEQRES  25 F  746  THR ALA LEU ASP ASN LYS PRO CYS GLY PRO GLN CYS TYR          
SEQRES  26 F  746  GLN HIS LEU GLU GLY ALA LYS GLU PHE ALA ALA ALA LEU          
SEQRES  27 F  746  THR ALA GLU ARG ILE LYS THR PRO PRO LYS ARG PRO GLY          
SEQRES  28 F  746  GLY ARG ARG ARG GLY ARG LEU PRO ASN ASN SER SER ARG          
SEQRES  29 F  746  PRO SER THR PRO THR ILE ASN VAL LEU GLU SER LYS ASP          
SEQRES  30 F  746  THR ASP SER ASP ARG GLU ALA GLY THR GLU THR GLY GLY          
SEQRES  31 F  746  GLU ASN ASN ASP LYS GLU GLU GLU GLU LYS LYS ASP GLU          
SEQRES  32 F  746  THR SER SER SER SER GLU ALA ASN SER ARG CYS GLN THR          
SEQRES  33 F  746  PRO ILE LYS MET LYS PRO ASN ILE GLU PRO PRO GLU ASN          
SEQRES  34 F  746  VAL GLU TRP SER GLY ALA GLU ALA SER MET PHE ARG VAL          
SEQRES  35 F  746  LEU ILE GLY THR TYR TYR ASP ASN PHE CYS ALA ILE ALA          
SEQRES  36 F  746  ARG LEU ILE GLY THR LYS THR CYS ARG GLN VAL TYR GLU          
SEQRES  37 F  746  PHE ARG VAL LYS GLU SER SER ILE ILE ALA PRO ALA PRO          
SEQRES  38 F  746  ALA GLU ASP VAL ASP THR PRO PRO ARG LYS LYS LYS ARG          
SEQRES  39 F  746  LYS HIS ARG LEU TRP ALA ALA HIS CYS ARG LYS ILE GLN          
SEQRES  40 F  746  LEU LYS LYS ASP GLY SER SER ASN HIS VAL TYR ASN TYR          
SEQRES  41 F  746  GLN PRO CYS ASP HIS PRO ARG GLN PRO CYS ASP SER SER          
SEQRES  42 F  746  CYS PRO CYS VAL ILE ALA GLN ASN PHE CYS GLU LYS PHE          
SEQRES  43 F  746  CYS GLN CYS SER SER GLU CYS GLN ASN ARG PHE PRO GLY          
SEQRES  44 F  746  CYS ARG CYS LYS ALA GLN CYS ASN THR LYS GLN CYS PRO          
SEQRES  45 F  746  CYS TYR LEU ALA VAL ARG GLU CYS ASP PRO ASP LEU CYS          
SEQRES  46 F  746  LEU THR CYS GLY ALA ALA ASP HIS TRP ASP SER LYS ASN          
SEQRES  47 F  746  VAL SER CYS LYS ASN CYS SER ILE GLN ARG GLY SER LYS          
SEQRES  48 F  746  LYS HIS LEU LEU LEU ALA PRO SER ASP VAL ALA GLY TRP          
SEQRES  49 F  746  GLY ILE PHE ILE LYS ASP PRO VAL GLN LYS ASN GLU PHE          
SEQRES  50 F  746  ILE SER GLU TYR CYS GLY GLU ILE ILE SER GLN ASP GLU          
SEQRES  51 F  746  ALA ASP ARG ARG GLY LYS VAL TYR ASP LYS TYR MET CYS          
SEQRES  52 F  746  SER PHE LEU PHE ASN LEU ASN ASN ASP PHE VAL VAL ASP          
SEQRES  53 F  746  ALA THR ARG LYS GLY ASN LYS ILE ARG PHE ALA ASN HIS          
SEQRES  54 F  746  SER VAL ASN PRO ASN CYS TYR ALA LYS VAL MET MET VAL          
SEQRES  55 F  746  ASN GLY ASP HIS ARG ILE GLY ILE PHE ALA LYS ARG ALA          
SEQRES  56 F  746  ILE GLN THR GLY GLU GLU LEU PHE PHE ASP TYR ARG TYR          
SEQRES  57 F  746  SER GLN ALA ASP ALA LEU LYS TYR VAL GLY ILE GLU ARG          
SEQRES  58 F  746  GLU MET GLU ILE PRO                                          
SEQRES   1 G  367  GLY SER LYS CYS LYS TYR SER PHE LYS CYS VAL ASN SER          
SEQRES   2 G  367  LEU LYS GLU ASP HIS ASN GLN PRO LEU PHE GLY VAL GLN          
SEQRES   3 G  367  PHE ASN TRP HIS SER LYS GLU GLY ASP PRO LEU VAL PHE          
SEQRES   4 G  367  ALA THR VAL GLY SER ASN ARG VAL THR LEU TYR GLU CYS          
SEQRES   5 G  367  HIS SER GLN GLY GLU ILE ARG LEU LEU GLN SER TYR VAL          
SEQRES   6 G  367  ASP ALA ASP ALA ASP GLU ASN PHE TYR THR CYS ALA TRP          
SEQRES   7 G  367  THR TYR ASP SER ASN THR SER HIS PRO LEU LEU ALA VAL          
SEQRES   8 G  367  ALA GLY SER ARG GLY ILE ILE ARG ILE ILE ASN PRO ILE          
SEQRES   9 G  367  THR MET GLN CYS ILE LYS HIS TYR VAL GLY HIS GLY ASN          
SEQRES  10 G  367  ALA ILE ASN GLU LEU LYS PHE HIS PRO ARG ASP PRO ASN          
SEQRES  11 G  367  LEU LEU LEU SER VAL SER LYS ASP HIS ALA LEU ARG LEU          
SEQRES  12 G  367  TRP ASN ILE GLN THR ASP THR LEU VAL ALA ILE PHE GLY          
SEQRES  13 G  367  GLY VAL GLU GLY HIS ARG ASP GLU VAL LEU SER ALA ASP          
SEQRES  14 G  367  TYR ASP LEU LEU GLY GLU LYS ILE MET SER CYS GLY MET          
SEQRES  15 G  367  ASP HIS SER LEU LYS LEU TRP ARG ILE ASN SER LYS ARG          
SEQRES  16 G  367  MET MET ASN ALA ILE LYS GLU SER TYR ASP TYR ASN PRO          
SEQRES  17 G  367  ASN LYS THR ASN ARG PRO PHE ILE SER GLN LYS ILE HIS          
SEQRES  18 G  367  PHE PRO ASP PHE SER THR ARG ASP ILE HIS ARG ASN TYR          
SEQRES  19 G  367  VAL ASP CYS VAL ARG TRP LEU GLY ASP LEU ILE LEU SER          
SEQRES  20 G  367  LYS SER CYS GLU ASN ALA ILE VAL CYS TRP LYS PRO GLY          
SEQRES  21 G  367  LYS MET GLU ASP ASP ILE ASP LYS ILE LYS PRO SER GLU          
SEQRES  22 G  367  SER ASN VAL THR ILE LEU GLY ARG PHE ASP TYR SER GLN          
SEQRES  23 G  367  CYS ASP ILE TRP TYR MET ARG PHE SER MET ASP PHE TRP          
SEQRES  24 G  367  GLN LYS MET LEU ALA LEU GLY ASN GLN VAL GLY LYS LEU          
SEQRES  25 G  367  TYR VAL TRP ASP LEU GLU VAL GLU ASP PRO HIS LYS ALA          
SEQRES  26 G  367  LYS CYS THR THR LEU THR HIS HIS LYS CYS GLY ALA ALA          
SEQRES  27 G  367  ILE ARG GLN THR SER PHE SER ARG ASP SER SER ILE LEU          
SEQRES  28 G  367  ILE ALA VAL CYS ASP ASP ALA SER ILE TRP ARG TRP ASP          
SEQRES  29 G  367  ARG LEU ARG                                                  
SEQRES   1 H  129  GLY SER SER GLY HIS ASN ARG LEU TYR PHE HIS SER ASP          
SEQRES   2 H  129  THR CYS LEU PRO LEU ARG PRO GLN GLU MET GLU VAL ASP          
SEQRES   3 H  129  SER GLU ASP GLU LYS ASP PRO GLU TRP LEU ARG GLU LYS          
SEQRES   4 H  129  THR ILE THR GLN ILE GLU GLU PHE SER ASP VAL ASN GLU          
SEQRES   5 H  129  GLY GLU LYS GLU VAL MET LYS LEU TRP ASN LEU HIS VAL          
SEQRES   6 H  129  MET LYS HIS GLY PHE ILE ALA ASP ASN GLN MET ASN HIS          
SEQRES   7 H  129  ALA CYS MET LEU PHE VAL GLU ASN TYR GLY GLN LYS ILE          
SEQRES   8 H  129  ILE LYS LYS ASN LEU CYS ARG ASN PHE MET LEU HIS LEU          
SEQRES   9 H  129  VAL SER MET HIS ASP PHE ASN LEU ILE SER ILE MET SER          
SEQRES  10 H  129  ILE ASP LYS ALA VAL THR LYS LEU ARG GLU MET GLN              
SEQRES   1 I   13  ALA THR LYS ALA ALA ARG MET SER ALA PRO ALA THR GLY          
SEQRES   1 J   12  ARG LEU GLN ALA GLN ARG M3L PHE ALA GLN SER GLN              
SEQRES   1 K  746  MET GLY GLN THR GLY LYS LYS SER GLU LYS GLY PRO VAL          
SEQRES   2 K  746  CYS TRP ARG LYS ARG VAL LYS SER GLU TYR MET ARG LEU          
SEQRES   3 K  746  ARG GLN LEU LYS ARG PHE ARG ARG ALA ASP GLU VAL LYS          
SEQRES   4 K  746  SER MET PHE SER SER ASN ARG GLN LYS ILE LEU GLU ARG          
SEQRES   5 K  746  THR GLU ILE LEU ASN GLN GLU TRP LYS GLN ARG ARG ILE          
SEQRES   6 K  746  GLN PRO VAL HIS ILE LEU THR SER VAL SER SER LEU ARG          
SEQRES   7 K  746  GLY THR ARG GLU CYS SER VAL THR SER ASP LEU ASP PHE          
SEQRES   8 K  746  PRO THR GLN VAL ILE PRO LEU LYS THR LEU ASN ALA VAL          
SEQRES   9 K  746  ALA SER VAL PRO ILE MET TYR SER TRP SER PRO LEU GLN          
SEQRES  10 K  746  GLN ASN PHE MET VAL GLU ASP GLU THR VAL LEU HIS ASN          
SEQRES  11 K  746  ILE PRO TYR MET GLY ASP GLU VAL LEU ASP GLN ASP GLY          
SEQRES  12 K  746  THR PHE ILE GLU GLU LEU ILE LYS ASN TYR ASP GLY LYS          
SEQRES  13 K  746  VAL HIS GLY ASP ARG GLU CYS GLY PHE ILE ASN ASP GLU          
SEQRES  14 K  746  ILE PHE VAL GLU LEU VAL ASN ALA LEU GLY GLN TYR ASN          
SEQRES  15 K  746  ASP ASP ASP ASP ASP ASP ASP GLY ASP ASP PRO GLU GLU          
SEQRES  16 K  746  ARG GLU GLU LYS GLN LYS ASP LEU GLU ASP HIS ARG ASP          
SEQRES  17 K  746  ASP LYS GLU SER ARG PRO PRO ARG LYS PHE PRO SER ASP          
SEQRES  18 K  746  LYS ILE PHE GLU ALA ILE SER SER MET PHE PRO ASP LYS          
SEQRES  19 K  746  GLY THR ALA GLU GLU LEU LYS GLU LYS TYR LYS GLU LEU          
SEQRES  20 K  746  THR GLU GLN GLN LEU PRO GLY ALA LEU PRO PRO GLU CYS          
SEQRES  21 K  746  THR PRO ASN ILE ASP GLY PRO ASN ALA LYS SER VAL GLN          
SEQRES  22 K  746  ARG GLU GLN SER LEU HIS SER PHE HIS THR LEU PHE CYS          
SEQRES  23 K  746  ARG ARG CYS PHE LYS TYR ASP CYS PHE LEU HIS PRO PHE          
SEQRES  24 K  746  HIS ALA THR PRO ASN THR TYR LYS ARG LYS ASN THR GLU          
SEQRES  25 K  746  THR ALA LEU ASP ASN LYS PRO CYS GLY PRO GLN CYS TYR          
SEQRES  26 K  746  GLN HIS LEU GLU GLY ALA LYS GLU PHE ALA ALA ALA LEU          
SEQRES  27 K  746  THR ALA GLU ARG ILE LYS THR PRO PRO LYS ARG PRO GLY          
SEQRES  28 K  746  GLY ARG ARG ARG GLY ARG LEU PRO ASN ASN SER SER ARG          
SEQRES  29 K  746  PRO SER THR PRO THR ILE ASN VAL LEU GLU SER LYS ASP          
SEQRES  30 K  746  THR ASP SER ASP ARG GLU ALA GLY THR GLU THR GLY GLY          
SEQRES  31 K  746  GLU ASN ASN ASP LYS GLU GLU GLU GLU LYS LYS ASP GLU          
SEQRES  32 K  746  THR SER SER SER SER GLU ALA ASN SER ARG CYS GLN THR          
SEQRES  33 K  746  PRO ILE LYS MET LYS PRO ASN ILE GLU PRO PRO GLU ASN          
SEQRES  34 K  746  VAL GLU TRP SER GLY ALA GLU ALA SER MET PHE ARG VAL          
SEQRES  35 K  746  LEU ILE GLY THR TYR TYR ASP ASN PHE CYS ALA ILE ALA          
SEQRES  36 K  746  ARG LEU ILE GLY THR LYS THR CYS ARG GLN VAL TYR GLU          
SEQRES  37 K  746  PHE ARG VAL LYS GLU SER SER ILE ILE ALA PRO ALA PRO          
SEQRES  38 K  746  ALA GLU ASP VAL ASP THR PRO PRO ARG LYS LYS LYS ARG          
SEQRES  39 K  746  LYS HIS ARG LEU TRP ALA ALA HIS CYS ARG LYS ILE GLN          
SEQRES  40 K  746  LEU LYS LYS ASP GLY SER SER ASN HIS VAL TYR ASN TYR          
SEQRES  41 K  746  GLN PRO CYS ASP HIS PRO ARG GLN PRO CYS ASP SER SER          
SEQRES  42 K  746  CYS PRO CYS VAL ILE ALA GLN ASN PHE CYS GLU LYS PHE          
SEQRES  43 K  746  CYS GLN CYS SER SER GLU CYS GLN ASN ARG PHE PRO GLY          
SEQRES  44 K  746  CYS ARG CYS LYS ALA GLN CYS ASN THR LYS GLN CYS PRO          
SEQRES  45 K  746  CYS TYR LEU ALA VAL ARG GLU CYS ASP PRO ASP LEU CYS          
SEQRES  46 K  746  LEU THR CYS GLY ALA ALA ASP HIS TRP ASP SER LYS ASN          
SEQRES  47 K  746  VAL SER CYS LYS ASN CYS SER ILE GLN ARG GLY SER LYS          
SEQRES  48 K  746  LYS HIS LEU LEU LEU ALA PRO SER ASP VAL ALA GLY TRP          
SEQRES  49 K  746  GLY ILE PHE ILE LYS ASP PRO VAL GLN LYS ASN GLU PHE          
SEQRES  50 K  746  ILE SER GLU TYR CYS GLY GLU ILE ILE SER GLN ASP GLU          
SEQRES  51 K  746  ALA ASP ARG ARG GLY LYS VAL TYR ASP LYS TYR MET CYS          
SEQRES  52 K  746  SER PHE LEU PHE ASN LEU ASN ASN ASP PHE VAL VAL ASP          
SEQRES  53 K  746  ALA THR ARG LYS GLY ASN LYS ILE ARG PHE ALA ASN HIS          
SEQRES  54 K  746  SER VAL ASN PRO ASN CYS TYR ALA LYS VAL MET MET VAL          
SEQRES  55 K  746  ASN GLY ASP HIS ARG ILE GLY ILE PHE ALA LYS ARG ALA          
SEQRES  56 K  746  ILE GLN THR GLY GLU GLU LEU PHE PHE ASP TYR ARG TYR          
SEQRES  57 K  746  SER GLN ALA ASP ALA LEU LYS TYR VAL GLY ILE GLU ARG          
SEQRES  58 K  746  GLU MET GLU ILE PRO                                          
SEQRES   1 L  367  GLY SER LYS CYS LYS TYR SER PHE LYS CYS VAL ASN SER          
SEQRES   2 L  367  LEU LYS GLU ASP HIS ASN GLN PRO LEU PHE GLY VAL GLN          
SEQRES   3 L  367  PHE ASN TRP HIS SER LYS GLU GLY ASP PRO LEU VAL PHE          
SEQRES   4 L  367  ALA THR VAL GLY SER ASN ARG VAL THR LEU TYR GLU CYS          
SEQRES   5 L  367  HIS SER GLN GLY GLU ILE ARG LEU LEU GLN SER TYR VAL          
SEQRES   6 L  367  ASP ALA ASP ALA ASP GLU ASN PHE TYR THR CYS ALA TRP          
SEQRES   7 L  367  THR TYR ASP SER ASN THR SER HIS PRO LEU LEU ALA VAL          
SEQRES   8 L  367  ALA GLY SER ARG GLY ILE ILE ARG ILE ILE ASN PRO ILE          
SEQRES   9 L  367  THR MET GLN CYS ILE LYS HIS TYR VAL GLY HIS GLY ASN          
SEQRES  10 L  367  ALA ILE ASN GLU LEU LYS PHE HIS PRO ARG ASP PRO ASN          
SEQRES  11 L  367  LEU LEU LEU SER VAL SER LYS ASP HIS ALA LEU ARG LEU          
SEQRES  12 L  367  TRP ASN ILE GLN THR ASP THR LEU VAL ALA ILE PHE GLY          
SEQRES  13 L  367  GLY VAL GLU GLY HIS ARG ASP GLU VAL LEU SER ALA ASP          
SEQRES  14 L  367  TYR ASP LEU LEU GLY GLU LYS ILE MET SER CYS GLY MET          
SEQRES  15 L  367  ASP HIS SER LEU LYS LEU TRP ARG ILE ASN SER LYS ARG          
SEQRES  16 L  367  MET MET ASN ALA ILE LYS GLU SER TYR ASP TYR ASN PRO          
SEQRES  17 L  367  ASN LYS THR ASN ARG PRO PHE ILE SER GLN LYS ILE HIS          
SEQRES  18 L  367  PHE PRO ASP PHE SER THR ARG ASP ILE HIS ARG ASN TYR          
SEQRES  19 L  367  VAL ASP CYS VAL ARG TRP LEU GLY ASP LEU ILE LEU SER          
SEQRES  20 L  367  LYS SER CYS GLU ASN ALA ILE VAL CYS TRP LYS PRO GLY          
SEQRES  21 L  367  LYS MET GLU ASP ASP ILE ASP LYS ILE LYS PRO SER GLU          
SEQRES  22 L  367  SER ASN VAL THR ILE LEU GLY ARG PHE ASP TYR SER GLN          
SEQRES  23 L  367  CYS ASP ILE TRP TYR MET ARG PHE SER MET ASP PHE TRP          
SEQRES  24 L  367  GLN LYS MET LEU ALA LEU GLY ASN GLN VAL GLY LYS LEU          
SEQRES  25 L  367  TYR VAL TRP ASP LEU GLU VAL GLU ASP PRO HIS LYS ALA          
SEQRES  26 L  367  LYS CYS THR THR LEU THR HIS HIS LYS CYS GLY ALA ALA          
SEQRES  27 L  367  ILE ARG GLN THR SER PHE SER ARG ASP SER SER ILE LEU          
SEQRES  28 L  367  ILE ALA VAL CYS ASP ASP ALA SER ILE TRP ARG TRP ASP          
SEQRES  29 L  367  ARG LEU ARG                                                  
SEQRES   1 M  129  GLY SER SER GLY HIS ASN ARG LEU TYR PHE HIS SER ASP          
SEQRES   2 M  129  THR CYS LEU PRO LEU ARG PRO GLN GLU MET GLU VAL ASP          
SEQRES   3 M  129  SER GLU ASP GLU LYS ASP PRO GLU TRP LEU ARG GLU LYS          
SEQRES   4 M  129  THR ILE THR GLN ILE GLU GLU PHE SER ASP VAL ASN GLU          
SEQRES   5 M  129  GLY GLU LYS GLU VAL MET LYS LEU TRP ASN LEU HIS VAL          
SEQRES   6 M  129  MET LYS HIS GLY PHE ILE ALA ASP ASN GLN MET ASN HIS          
SEQRES   7 M  129  ALA CYS MET LEU PHE VAL GLU ASN TYR GLY GLN LYS ILE          
SEQRES   8 M  129  ILE LYS LYS ASN LEU CYS ARG ASN PHE MET LEU HIS LEU          
SEQRES   9 M  129  VAL SER MET HIS ASP PHE ASN LEU ILE SER ILE MET SER          
SEQRES  10 M  129  ILE ASP LYS ALA VAL THR LYS LEU ARG GLU MET GLN              
SEQRES   1 O   13  ALA THR LYS ALA ALA ARG MET SER ALA PRO ALA THR GLY          
SEQRES   1 P   12  ARG LEU GLN ALA GLN ARG M3L PHE ALA GLN SER GLN              
SEQRES   1 Q  746  MET GLY GLN THR GLY LYS LYS SER GLU LYS GLY PRO VAL          
SEQRES   2 Q  746  CYS TRP ARG LYS ARG VAL LYS SER GLU TYR MET ARG LEU          
SEQRES   3 Q  746  ARG GLN LEU LYS ARG PHE ARG ARG ALA ASP GLU VAL LYS          
SEQRES   4 Q  746  SER MET PHE SER SER ASN ARG GLN LYS ILE LEU GLU ARG          
SEQRES   5 Q  746  THR GLU ILE LEU ASN GLN GLU TRP LYS GLN ARG ARG ILE          
SEQRES   6 Q  746  GLN PRO VAL HIS ILE LEU THR SER VAL SER SER LEU ARG          
SEQRES   7 Q  746  GLY THR ARG GLU CYS SER VAL THR SER ASP LEU ASP PHE          
SEQRES   8 Q  746  PRO THR GLN VAL ILE PRO LEU LYS THR LEU ASN ALA VAL          
SEQRES   9 Q  746  ALA SER VAL PRO ILE MET TYR SER TRP SER PRO LEU GLN          
SEQRES  10 Q  746  GLN ASN PHE MET VAL GLU ASP GLU THR VAL LEU HIS ASN          
SEQRES  11 Q  746  ILE PRO TYR MET GLY ASP GLU VAL LEU ASP GLN ASP GLY          
SEQRES  12 Q  746  THR PHE ILE GLU GLU LEU ILE LYS ASN TYR ASP GLY LYS          
SEQRES  13 Q  746  VAL HIS GLY ASP ARG GLU CYS GLY PHE ILE ASN ASP GLU          
SEQRES  14 Q  746  ILE PHE VAL GLU LEU VAL ASN ALA LEU GLY GLN TYR ASN          
SEQRES  15 Q  746  ASP ASP ASP ASP ASP ASP ASP GLY ASP ASP PRO GLU GLU          
SEQRES  16 Q  746  ARG GLU GLU LYS GLN LYS ASP LEU GLU ASP HIS ARG ASP          
SEQRES  17 Q  746  ASP LYS GLU SER ARG PRO PRO ARG LYS PHE PRO SER ASP          
SEQRES  18 Q  746  LYS ILE PHE GLU ALA ILE SER SER MET PHE PRO ASP LYS          
SEQRES  19 Q  746  GLY THR ALA GLU GLU LEU LYS GLU LYS TYR LYS GLU LEU          
SEQRES  20 Q  746  THR GLU GLN GLN LEU PRO GLY ALA LEU PRO PRO GLU CYS          
SEQRES  21 Q  746  THR PRO ASN ILE ASP GLY PRO ASN ALA LYS SER VAL GLN          
SEQRES  22 Q  746  ARG GLU GLN SER LEU HIS SER PHE HIS THR LEU PHE CYS          
SEQRES  23 Q  746  ARG ARG CYS PHE LYS TYR ASP CYS PHE LEU HIS PRO PHE          
SEQRES  24 Q  746  HIS ALA THR PRO ASN THR TYR LYS ARG LYS ASN THR GLU          
SEQRES  25 Q  746  THR ALA LEU ASP ASN LYS PRO CYS GLY PRO GLN CYS TYR          
SEQRES  26 Q  746  GLN HIS LEU GLU GLY ALA LYS GLU PHE ALA ALA ALA LEU          
SEQRES  27 Q  746  THR ALA GLU ARG ILE LYS THR PRO PRO LYS ARG PRO GLY          
SEQRES  28 Q  746  GLY ARG ARG ARG GLY ARG LEU PRO ASN ASN SER SER ARG          
SEQRES  29 Q  746  PRO SER THR PRO THR ILE ASN VAL LEU GLU SER LYS ASP          
SEQRES  30 Q  746  THR ASP SER ASP ARG GLU ALA GLY THR GLU THR GLY GLY          
SEQRES  31 Q  746  GLU ASN ASN ASP LYS GLU GLU GLU GLU LYS LYS ASP GLU          
SEQRES  32 Q  746  THR SER SER SER SER GLU ALA ASN SER ARG CYS GLN THR          
SEQRES  33 Q  746  PRO ILE LYS MET LYS PRO ASN ILE GLU PRO PRO GLU ASN          
SEQRES  34 Q  746  VAL GLU TRP SER GLY ALA GLU ALA SER MET PHE ARG VAL          
SEQRES  35 Q  746  LEU ILE GLY THR TYR TYR ASP ASN PHE CYS ALA ILE ALA          
SEQRES  36 Q  746  ARG LEU ILE GLY THR LYS THR CYS ARG GLN VAL TYR GLU          
SEQRES  37 Q  746  PHE ARG VAL LYS GLU SER SER ILE ILE ALA PRO ALA PRO          
SEQRES  38 Q  746  ALA GLU ASP VAL ASP THR PRO PRO ARG LYS LYS LYS ARG          
SEQRES  39 Q  746  LYS HIS ARG LEU TRP ALA ALA HIS CYS ARG LYS ILE GLN          
SEQRES  40 Q  746  LEU LYS LYS ASP GLY SER SER ASN HIS VAL TYR ASN TYR          
SEQRES  41 Q  746  GLN PRO CYS ASP HIS PRO ARG GLN PRO CYS ASP SER SER          
SEQRES  42 Q  746  CYS PRO CYS VAL ILE ALA GLN ASN PHE CYS GLU LYS PHE          
SEQRES  43 Q  746  CYS GLN CYS SER SER GLU CYS GLN ASN ARG PHE PRO GLY          
SEQRES  44 Q  746  CYS ARG CYS LYS ALA GLN CYS ASN THR LYS GLN CYS PRO          
SEQRES  45 Q  746  CYS TYR LEU ALA VAL ARG GLU CYS ASP PRO ASP LEU CYS          
SEQRES  46 Q  746  LEU THR CYS GLY ALA ALA ASP HIS TRP ASP SER LYS ASN          
SEQRES  47 Q  746  VAL SER CYS LYS ASN CYS SER ILE GLN ARG GLY SER LYS          
SEQRES  48 Q  746  LYS HIS LEU LEU LEU ALA PRO SER ASP VAL ALA GLY TRP          
SEQRES  49 Q  746  GLY ILE PHE ILE LYS ASP PRO VAL GLN LYS ASN GLU PHE          
SEQRES  50 Q  746  ILE SER GLU TYR CYS GLY GLU ILE ILE SER GLN ASP GLU          
SEQRES  51 Q  746  ALA ASP ARG ARG GLY LYS VAL TYR ASP LYS TYR MET CYS          
SEQRES  52 Q  746  SER PHE LEU PHE ASN LEU ASN ASN ASP PHE VAL VAL ASP          
SEQRES  53 Q  746  ALA THR ARG LYS GLY ASN LYS ILE ARG PHE ALA ASN HIS          
SEQRES  54 Q  746  SER VAL ASN PRO ASN CYS TYR ALA LYS VAL MET MET VAL          
SEQRES  55 Q  746  ASN GLY ASP HIS ARG ILE GLY ILE PHE ALA LYS ARG ALA          
SEQRES  56 Q  746  ILE GLN THR GLY GLU GLU LEU PHE PHE ASP TYR ARG TYR          
SEQRES  57 Q  746  SER GLN ALA ASP ALA LEU LYS TYR VAL GLY ILE GLU ARG          
SEQRES  58 Q  746  GLU MET GLU ILE PRO                                          
SEQRES   1 R  367  GLY SER LYS CYS LYS TYR SER PHE LYS CYS VAL ASN SER          
SEQRES   2 R  367  LEU LYS GLU ASP HIS ASN GLN PRO LEU PHE GLY VAL GLN          
SEQRES   3 R  367  PHE ASN TRP HIS SER LYS GLU GLY ASP PRO LEU VAL PHE          
SEQRES   4 R  367  ALA THR VAL GLY SER ASN ARG VAL THR LEU TYR GLU CYS          
SEQRES   5 R  367  HIS SER GLN GLY GLU ILE ARG LEU LEU GLN SER TYR VAL          
SEQRES   6 R  367  ASP ALA ASP ALA ASP GLU ASN PHE TYR THR CYS ALA TRP          
SEQRES   7 R  367  THR TYR ASP SER ASN THR SER HIS PRO LEU LEU ALA VAL          
SEQRES   8 R  367  ALA GLY SER ARG GLY ILE ILE ARG ILE ILE ASN PRO ILE          
SEQRES   9 R  367  THR MET GLN CYS ILE LYS HIS TYR VAL GLY HIS GLY ASN          
SEQRES  10 R  367  ALA ILE ASN GLU LEU LYS PHE HIS PRO ARG ASP PRO ASN          
SEQRES  11 R  367  LEU LEU LEU SER VAL SER LYS ASP HIS ALA LEU ARG LEU          
SEQRES  12 R  367  TRP ASN ILE GLN THR ASP THR LEU VAL ALA ILE PHE GLY          
SEQRES  13 R  367  GLY VAL GLU GLY HIS ARG ASP GLU VAL LEU SER ALA ASP          
SEQRES  14 R  367  TYR ASP LEU LEU GLY GLU LYS ILE MET SER CYS GLY MET          
SEQRES  15 R  367  ASP HIS SER LEU LYS LEU TRP ARG ILE ASN SER LYS ARG          
SEQRES  16 R  367  MET MET ASN ALA ILE LYS GLU SER TYR ASP TYR ASN PRO          
SEQRES  17 R  367  ASN LYS THR ASN ARG PRO PHE ILE SER GLN LYS ILE HIS          
SEQRES  18 R  367  PHE PRO ASP PHE SER THR ARG ASP ILE HIS ARG ASN TYR          
SEQRES  19 R  367  VAL ASP CYS VAL ARG TRP LEU GLY ASP LEU ILE LEU SER          
SEQRES  20 R  367  LYS SER CYS GLU ASN ALA ILE VAL CYS TRP LYS PRO GLY          
SEQRES  21 R  367  LYS MET GLU ASP ASP ILE ASP LYS ILE LYS PRO SER GLU          
SEQRES  22 R  367  SER ASN VAL THR ILE LEU GLY ARG PHE ASP TYR SER GLN          
SEQRES  23 R  367  CYS ASP ILE TRP TYR MET ARG PHE SER MET ASP PHE TRP          
SEQRES  24 R  367  GLN LYS MET LEU ALA LEU GLY ASN GLN VAL GLY LYS LEU          
SEQRES  25 R  367  TYR VAL TRP ASP LEU GLU VAL GLU ASP PRO HIS LYS ALA          
SEQRES  26 R  367  LYS CYS THR THR LEU THR HIS HIS LYS CYS GLY ALA ALA          
SEQRES  27 R  367  ILE ARG GLN THR SER PHE SER ARG ASP SER SER ILE LEU          
SEQRES  28 R  367  ILE ALA VAL CYS ASP ASP ALA SER ILE TRP ARG TRP ASP          
SEQRES  29 R  367  ARG LEU ARG                                                  
SEQRES   1 S  129  GLY SER SER GLY HIS ASN ARG LEU TYR PHE HIS SER ASP          
SEQRES   2 S  129  THR CYS LEU PRO LEU ARG PRO GLN GLU MET GLU VAL ASP          
SEQRES   3 S  129  SER GLU ASP GLU LYS ASP PRO GLU TRP LEU ARG GLU LYS          
SEQRES   4 S  129  THR ILE THR GLN ILE GLU GLU PHE SER ASP VAL ASN GLU          
SEQRES   5 S  129  GLY GLU LYS GLU VAL MET LYS LEU TRP ASN LEU HIS VAL          
SEQRES   6 S  129  MET LYS HIS GLY PHE ILE ALA ASP ASN GLN MET ASN HIS          
SEQRES   7 S  129  ALA CYS MET LEU PHE VAL GLU ASN TYR GLY GLN LYS ILE          
SEQRES   8 S  129  ILE LYS LYS ASN LEU CYS ARG ASN PHE MET LEU HIS LEU          
SEQRES   9 S  129  VAL SER MET HIS ASP PHE ASN LEU ILE SER ILE MET SER          
SEQRES  10 S  129  ILE ASP LYS ALA VAL THR LYS LEU ARG GLU MET GLN              
SEQRES   1 T   13  ALA THR LYS ALA ALA ARG MET SER ALA PRO ALA THR GLY          
SEQRES   1 U   12  ARG LEU GLN ALA GLN ARG M3L PHE ALA GLN SER GLN              
HET    M3L  E   7      12                                                       
HET    M3L  J   7      12                                                       
HET    M3L  P   7      12                                                       
HET    M3L  U   7      12                                                       
HET     ZN  A1001       1                                                       
HET     ZN  A1002       1                                                       
HET     ZN  A1003       1                                                       
HET     ZN  A1004       1                                                       
HET     ZN  A1005       1                                                       
HET     ZN  A1006       1                                                       
HET     ZN  A1007       1                                                       
HET     ZN  A1008       1                                                       
HET    SAH  A1009      26                                                       
HET     ZN  F1001       1                                                       
HET     ZN  F1002       1                                                       
HET     ZN  F1003       1                                                       
HET     ZN  F1004       1                                                       
HET     ZN  F1005       1                                                       
HET     ZN  F1006       1                                                       
HET     ZN  F1007       1                                                       
HET     ZN  F1008       1                                                       
HET    SAH  F1009      26                                                       
HET     ZN  K1001       1                                                       
HET     ZN  K1002       1                                                       
HET     ZN  K1003       1                                                       
HET     ZN  K1004       1                                                       
HET     ZN  K1005       1                                                       
HET     ZN  K1006       1                                                       
HET     ZN  K1007       1                                                       
HET     ZN  K1008       1                                                       
HET    SAH  K1009      26                                                       
HET     ZN  Q1001       1                                                       
HET     ZN  Q1002       1                                                       
HET     ZN  Q1003       1                                                       
HET     ZN  Q1004       1                                                       
HET     ZN  Q1005       1                                                       
HET     ZN  Q1006       1                                                       
HET     ZN  Q1007       1                                                       
HET     ZN  Q1008       1                                                       
HET    SAH  Q1009      26                                                       
HETNAM     M3L N-TRIMETHYLLYSINE                                                
HETNAM      ZN ZINC ION                                                         
HETNAM     SAH S-ADENOSYL-L-HOMOCYSTEINE                                        
FORMUL   5  M3L    4(C9 H21 N2 O2 1+)                                           
FORMUL  21   ZN    32(ZN 2+)                                                    
FORMUL  29  SAH    4(C14 H20 N6 O5 S)                                           
HELIX    1 AA1 GLY A   11  ARG A   63  1                                  53    
HELIX    2 AA2 MET A  134  LEU A  139  1                                   6    
HELIX    3 AA3 GLY A  143  TYR A  153  1                                  11    
HELIX    4 AA4 ASN A  167  ASN A  182  1                                  16    
HELIX    5 AA5 ASP A  221  PHE A  231  1                                  11    
HELIX    6 AA6 THR A  236  GLU A  249  1                                  14    
HELIX    7 AA7 GLN A  273  PHE A  285  1                                  13    
HELIX    8 AA8 ALA A  331  LYS A  344  1                                  14    
HELIX    9 AA9 SER A  433  TYR A  448  1                                  16    
HELIX   10 AB1 ASN A  450  GLY A  459  1                                  10    
HELIX   11 AB2 THR A  462  SER A  475  1                                  14    
HELIX   12 AB3 CYS A  534  ALA A  539  1                                   6    
HELIX   13 AB4 CYS A  571  ALA A  576  1                                   6    
HELIX   14 AB5 GLN A  648  TYR A  661  1                                  14    
HELIX   15 AB6 LYS A  683  ALA A  687  5                                   5    
HELIX   16 AB7 SER B  267  TYR B  280  1                                  14    
HELIX   17 AB8 ASP B  339  ILE B  343  5                                   5    
HELIX   18 AB9 PRO C  589  GLU C  602  1                                  14    
HELIX   19 AC1 GLY C  609  GLY C  625  1                                  17    
HELIX   20 AC2 ASN C  630  LYS C  650  1                                  21    
HELIX   21 AC3 LEU C  652  PHE C  666  1                                  15    
HELIX   22 AC4 ILE C  671  MET C  684  1                                  14    
HELIX   23 AC5 GLY F   11  ARG F   63  1                                  53    
HELIX   24 AC6 THR F  144  TYR F  153  1                                  10    
HELIX   25 AC7 ASN F  167  TYR F  181  1                                  15    
HELIX   26 AC8 LYS F  222  PHE F  231  1                                  10    
HELIX   27 AC9 THR F  236  THR F  248  1                                  13    
HELIX   28 AD1 GLN F  273  LEU F  278  1                                   6    
HELIX   29 AD2 LEU F  278  PHE F  285  1                                   8    
HELIX   30 AD3 ALA F  331  ILE F  343  1                                  13    
HELIX   31 AD4 SER F  433  TYR F  447  1                                  15    
HELIX   32 AD5 ASN F  450  GLY F  459  1                                  10    
HELIX   33 AD6 THR F  462  SER F  475  1                                  14    
HELIX   34 AD7 CYS F  534  ALA F  539  1                                   6    
HELIX   35 AD8 CYS F  571  ALA F  576  1                                   6    
HELIX   36 AD9 CYS F  604  GLY F  609  1                                   6    
HELIX   37 AE1 GLN F  648  MET F  662  1                                  15    
HELIX   38 AE2 LYS F  683  ALA F  687  5                                   5    
HELIX   39 AE3 SER G  128  GLY G  130  5                                   3    
HELIX   40 AE4 SER G  267  TYR G  280  1                                  14    
HELIX   41 AE5 ASP G  339  ILE G  343  5                                   5    
HELIX   42 AE6 ARG H  575  MET H  579  5                                   5    
HELIX   43 AE7 PRO H  589  GLU H  602  1                                  14    
HELIX   44 AE8 ASN H  607  GLY H  625  1                                  19    
HELIX   45 AE9 ASN H  630  LYS H  650  1                                  21    
HELIX   46 AF1 LEU H  652  PHE H  666  1                                  15    
HELIX   47 AF2 ILE H  671  MET H  684  1                                  14    
HELIX   48 AF3 VAL K   13  ARG K   63  1                                  51    
HELIX   49 AF4 THR K  144  TYR K  153  1                                  10    
HELIX   50 AF5 ASN K  167  GLN K  180  1                                  14    
HELIX   51 AF6 SER K  220  PHE K  231  1                                  12    
HELIX   52 AF7 THR K  236  LEU K  247  1                                  12    
HELIX   53 AF8 GLN K  273  LEU K  278  1                                   6    
HELIX   54 AF9 LEU K  278  PHE K  285  1                                   8    
HELIX   55 AG1 LYS K  332  LYS K  344  1                                  13    
HELIX   56 AG2 SER K  433  TYR K  447  1                                  15    
HELIX   57 AG3 ASN K  450  GLY K  459  1                                  10    
HELIX   58 AG4 THR K  462  ILE K  476  1                                  15    
HELIX   59 AG5 CYS K  534  GLN K  540  1                                   7    
HELIX   60 AG6 CYS K  571  ALA K  576  1                                   6    
HELIX   61 AG7 CYS K  604  GLY K  609  1                                   6    
HELIX   62 AG8 GLN K  648  MET K  662  1                                  15    
HELIX   63 AG9 LYS K  683  ALA K  687  5                                   5    
HELIX   64 AH1 SER L  267  TYR L  280  1                                  14    
HELIX   65 AH2 ASP L  339  ILE L  343  5                                   5    
HELIX   66 AH3 PRO M  589  GLU M  601  1                                  13    
HELIX   67 AH4 ASN M  607  GLY M  625  1                                  19    
HELIX   68 AH5 ASN M  630  LYS M  650  1                                  21    
HELIX   69 AH6 LEU M  652  PHE M  666  1                                  15    
HELIX   70 AH7 SER M  670  GLN M  685  1                                  16    
HELIX   71 AH8 VAL Q   13  ARG Q   63  1                                  51    
HELIX   72 AH9 ASP Q  142  TYR Q  153  1                                  12    
HELIX   73 AI1 ASN Q  167  GLN Q  180  1                                  14    
HELIX   74 AI2 LYS Q  222  SER Q  229  1                                   8    
HELIX   75 AI3 PHE Q  231  GLY Q  235  5                                   5    
HELIX   76 AI4 THR Q  236  THR Q  248  1                                  13    
HELIX   77 AI5 GLN Q  273  LEU Q  278  1                                   6    
HELIX   78 AI6 LEU Q  278  PHE Q  285  1                                   8    
HELIX   79 AI7 ALA Q  331  LYS Q  344  1                                  14    
HELIX   80 AI8 GLY Q  434  TYR Q  447  1                                  14    
HELIX   81 AI9 ASN Q  450  GLY Q  459  1                                  10    
HELIX   82 AJ1 THR Q  462  ILE Q  476  1                                  15    
HELIX   83 AJ2 CYS Q  534  GLN Q  540  1                                   7    
HELIX   84 AJ3 CYS Q  571  ALA Q  576  1                                   6    
HELIX   85 AJ4 CYS Q  604  GLY Q  609  1                                   6    
HELIX   86 AJ5 GLN Q  648  MET Q  662  1                                  15    
HELIX   87 AJ6 LYS Q  683  ALA Q  687  5                                   5    
HELIX   88 AJ7 SER R  128  GLY R  130  5                                   3    
HELIX   89 AJ8 SER R  267  TYR R  280  1                                  14    
HELIX   90 AJ9 ASP R  339  ILE R  343  5                                   5    
HELIX   91 AK1 ARG S  575  MET S  579  5                                   5    
HELIX   92 AK2 PRO S  589  PHE S  603  1                                  15    
HELIX   93 AK3 ASN S  607  GLY S  625  1                                  19    
HELIX   94 AK4 ASN S  630  LYS S  650  1                                  21    
HELIX   95 AK5 LEU S  652  PHE S  666  1                                  15    
HELIX   96 AK6 SER S  670  MET S  684  1                                  15    
SHEET    1 AA1 6 GLN A  94  PRO A  97  0                                        
SHEET    2 AA1 6 GLU A  82  SER A  87 -1  N  CYS A  83   O  ILE A  96           
SHEET    3 AA1 6 PHE B  82  GLU B  90 -1  O  LYS B  89   N  THR A  86           
SHEET    4 AA1 6 SER B 433  ARG B 439 -1  O  ILE B 434   N  LEU B  88           
SHEET    5 AA1 6 ILE B 424  CYS B 429 -1  N  LEU B 425   O  TRP B 437           
SHEET    6 AA1 6 ILE B 413  PHE B 418 -1  N  SER B 417   O  ILE B 426           
SHEET    1 AA2 5 LYS A  99  LEU A 101  0                                        
SHEET    2 AA2 5 GLU B 131  ASP B 140  1  O  VAL B 139   N  LEU A 101           
SHEET    3 AA2 5 ARG B 120  HIS B 127 -1  N  LEU B 123   O  GLN B 136           
SHEET    4 AA2 5 VAL B 112  GLY B 117 -1  N  PHE B 113   O  TYR B 124           
SHEET    5 AA2 5 LEU B  96  PHE B 101 -1  N  GLN B 100   O  ALA B 114           
SHEET    1 AA3 4 SER A 114  PRO A 115  0                                        
SHEET    2 AA3 4 PHE A 673  GLY A 681  1  O  ARG A 679   N  SER A 114           
SHEET    3 AA3 4 GLY A 643  SER A 647 -1  N  GLU A 644   O  ASP A 676           
SHEET    4 AA3 4 PHE A 120  MET A 121  1  N  PHE A 120   O  ILE A 645           
SHEET    1 AA4 3 SER A 114  PRO A 115  0                                        
SHEET    2 AA4 3 PHE A 673  GLY A 681  1  O  ARG A 679   N  SER A 114           
SHEET    3 AA4 3 LEU A 666  ASN A 668 -1  N  PHE A 667   O  VAL A 675           
SHEET    1 AA5 2 LEU A 614  PRO A 618  0                                        
SHEET    2 AA5 2 TRP A 624  ILE A 628 -1  O  PHE A 627   N  LEU A 615           
SHEET    1 AA6 3 PHE A 637  GLU A 640  0                                        
SHEET    2 AA6 3 ASP A 705  ALA A 712 -1  O  ILE A 710   N  SER A 639           
SHEET    3 AA6 3 CYS A 695  VAL A 702 -1  N  VAL A 702   O  ASP A 705           
SHEET    1 AA7 2 ASN A 688  HIS A 689  0                                        
SHEET    2 AA7 2 PHE A 723  PHE A 724  1  O  PHE A 724   N  ASN A 688           
SHEET    1 AA8 4 PHE B 147  TYR B 154  0                                        
SHEET    2 AA8 4 PRO B 161  GLY B 167 -1  O  LEU B 162   N  THR B 153           
SHEET    3 AA8 4 ILE B 172  ASN B 176 -1  O  ILE B 175   N  LEU B 163           
SHEET    4 AA8 4 GLN B 181  TYR B 186 -1  O  LYS B 184   N  ILE B 174           
SHEET    1 AA9 5 ILE B 193  PHE B 198  0                                        
SHEET    2 AA9 5 LEU B 205  SER B 210 -1  O  LEU B 207   N  LYS B 197           
SHEET    3 AA9 5 LEU B 215  ASN B 219 -1  O  ARG B 216   N  SER B 208           
SHEET    4 AA9 5 THR B 224  ILE B 228 -1  O  THR B 224   N  ASN B 219           
SHEET    5 AA9 5 GLN B 292  LYS B 293  1  O  GLN B 292   N  VAL B 226           
SHEET    1 AB1 4 VAL B 239  TYR B 244  0                                        
SHEET    2 AB1 4 LYS B 250  GLY B 255 -1  O  CYS B 254   N  SER B 241           
SHEET    3 AB1 4 LEU B 260  ARG B 264 -1  O  TRP B 263   N  ILE B 251           
SHEET    4 AB1 4 PHE B 299  THR B 301 -1  O  PHE B 299   N  LEU B 262           
SHEET    1 AB2 4 VAL B 309  LEU B 315  0                                        
SHEET    2 AB2 4 LEU B 318  SER B 323 -1  O  LEU B 320   N  ARG B 313           
SHEET    3 AB2 4 ALA B 327  PRO B 333 -1  O  TRP B 331   N  ILE B 319           
SHEET    4 AB2 4 VAL B 350  ASP B 357 -1  O  GLY B 354   N  CYS B 330           
SHEET    1 AB3 4 PHE B 368  MET B 370  0                                        
SHEET    2 AB3 4 MET B 376  GLY B 380 -1  O  ALA B 378   N  SER B 369           
SHEET    3 AB3 4 LEU B 386  ASP B 390 -1  O  TRP B 389   N  LEU B 377           
SHEET    4 AB3 4 THR B 402  LEU B 404 -1  O  THR B 402   N  VAL B 388           
SHEET    1 AB4 6 GLN F  94  PRO F  97  0                                        
SHEET    2 AB4 6 GLU F  82  SER F  87 -1  N  CYS F  83   O  ILE F  96           
SHEET    3 AB4 6 PHE G  82  GLU G  90 -1  O  LYS G  89   N  THR F  86           
SHEET    4 AB4 6 SER G 433  ARG G 439 -1  O  ILE G 434   N  LEU G  88           
SHEET    5 AB4 6 ILE G 424  CYS G 429 -1  N  ALA G 427   O  TRP G 435           
SHEET    6 AB4 6 ILE G 413  PHE G 418 -1  N  SER G 417   O  ILE G 426           
SHEET    1 AB5 5 LYS F  99  LEU F 101  0                                        
SHEET    2 AB5 5 ILE G 132  ASP G 140  1  O  VAL G 139   N  LEU F 101           
SHEET    3 AB5 5 ARG G 120  CYS G 126 -1  N  LEU G 123   O  GLN G 136           
SHEET    4 AB5 5 LEU G 111  GLY G 117 -1  N  LEU G 111   O  CYS G 126           
SHEET    5 AB5 5 LEU G  96  PHE G 101 -1  N  GLN G 100   O  ALA G 114           
SHEET    1 AB6 4 SER F 114  PRO F 115  0                                        
SHEET    2 AB6 4 PHE F 673  GLY F 681  1  O  GLY F 681   N  SER F 114           
SHEET    3 AB6 4 GLY F 643  SER F 647 -1  N  GLU F 644   O  ASP F 676           
SHEET    4 AB6 4 PHE F 120  MET F 121  1  N  PHE F 120   O  ILE F 645           
SHEET    1 AB7 3 SER F 114  PRO F 115  0                                        
SHEET    2 AB7 3 PHE F 673  GLY F 681  1  O  GLY F 681   N  SER F 114           
SHEET    3 AB7 3 LEU F 666  ASN F 668 -1  N  PHE F 667   O  VAL F 675           
SHEET    1 AB8 2 LEU F 614  PRO F 618  0                                        
SHEET    2 AB8 2 TRP F 624  ILE F 628 -1  O  PHE F 627   N  LEU F 615           
SHEET    1 AB9 3 PHE F 637  GLU F 640  0                                        
SHEET    2 AB9 3 ASP F 705  ALA F 712 -1  O  ILE F 710   N  ILE F 638           
SHEET    3 AB9 3 CYS F 695  VAL F 702 -1  N  VAL F 702   O  ASP F 705           
SHEET    1 AC1 2 ASN F 688  HIS F 689  0                                        
SHEET    2 AC1 2 PHE F 723  PHE F 724  1  O  PHE F 724   N  ASN F 688           
SHEET    1 AC2 4 PHE G 147  TYR G 154  0                                        
SHEET    2 AC2 4 PRO G 161  GLY G 167 -1  O  LEU G 162   N  THR G 153           
SHEET    3 AC2 4 ILE G 172  ASN G 176 -1  O  ILE G 175   N  LEU G 163           
SHEET    4 AC2 4 GLN G 181  TYR G 186 -1  O  GLN G 181   N  ASN G 176           
SHEET    1 AC3 5 ILE G 193  PHE G 198  0                                        
SHEET    2 AC3 5 LEU G 205  SER G 210 -1  O  LEU G 207   N  LYS G 197           
SHEET    3 AC3 5 LEU G 215  ASN G 219 -1  O  ARG G 216   N  SER G 208           
SHEET    4 AC3 5 THR G 224  PHE G 229 -1  O  PHE G 229   N  LEU G 215           
SHEET    5 AC3 5 GLN G 292  ILE G 294  1  O  GLN G 292   N  VAL G 226           
SHEET    1 AC4 4 VAL G 239  TYR G 244  0                                        
SHEET    2 AC4 4 LYS G 250  GLY G 255 -1  O  CYS G 254   N  SER G 241           
SHEET    3 AC4 4 LEU G 260  ARG G 264 -1  O  TRP G 263   N  ILE G 251           
SHEET    4 AC4 4 PHE G 299  THR G 301 -1  O  THR G 301   N  LEU G 260           
SHEET    1 AC5 4 VAL G 309  LEU G 315  0                                        
SHEET    2 AC5 4 LEU G 318  SER G 323 -1  O  LEU G 320   N  ARG G 313           
SHEET    3 AC5 4 ALA G 327  PRO G 333 -1  O  TRP G 331   N  ILE G 319           
SHEET    4 AC5 4 VAL G 350  ASP G 357 -1  O  PHE G 356   N  ILE G 328           
SHEET    1 AC6 4 PHE G 368  MET G 370  0                                        
SHEET    2 AC6 4 MET G 376  GLY G 380 -1  O  ALA G 378   N  SER G 369           
SHEET    3 AC6 4 LEU G 386  ASP G 390 -1  O  TRP G 389   N  LEU G 377           
SHEET    4 AC6 4 CYS G 401  LEU G 404 -1  O  THR G 402   N  VAL G 388           
SHEET    1 AC7 6 THR K  93  PRO K  97  0                                        
SHEET    2 AC7 6 GLU K  82  SER K  87 -1  N  CYS K  83   O  ILE K  96           
SHEET    3 AC7 6 PHE L  82  GLU L  90 -1  O  LYS L  89   N  THR K  86           
SHEET    4 AC7 6 SER L 433  ARG L 439 -1  O  ARG L 436   N  ASN L  86           
SHEET    5 AC7 6 ILE L 424  CYS L 429 -1  N  ALA L 427   O  TRP L 435           
SHEET    6 AC7 6 ILE L 413  PHE L 418 -1  N  SER L 417   O  ILE L 426           
SHEET    1 AC8 5 LYS K  99  LEU K 101  0                                        
SHEET    2 AC8 5 GLU L 131  ASP L 140  1  O  VAL L 139   N  LEU K 101           
SHEET    3 AC8 5 ARG L 120  HIS L 127 -1  N  GLU L 125   O  ARG L 133           
SHEET    4 AC8 5 LEU L 111  GLY L 117 -1  N  LEU L 111   O  CYS L 126           
SHEET    5 AC8 5 LEU L  96  PHE L 101 -1  N  GLN L 100   O  ALA L 114           
SHEET    1 AC9 4 SER K 114  PRO K 115  0                                        
SHEET    2 AC9 4 PHE K 673  GLY K 681  1  O  GLY K 681   N  SER K 114           
SHEET    3 AC9 4 GLY K 643  SER K 647 -1  N  GLU K 644   O  ASP K 676           
SHEET    4 AC9 4 PHE K 120  MET K 121  1  N  PHE K 120   O  ILE K 645           
SHEET    1 AD1 3 SER K 114  PRO K 115  0                                        
SHEET    2 AD1 3 PHE K 673  GLY K 681  1  O  GLY K 681   N  SER K 114           
SHEET    3 AD1 3 LEU K 666  ASN K 668 -1  N  PHE K 667   O  VAL K 675           
SHEET    1 AD2 2 LEU K 614  PRO K 618  0                                        
SHEET    2 AD2 2 TRP K 624  ILE K 628 -1  O  PHE K 627   N  LEU K 615           
SHEET    1 AD3 3 PHE K 637  GLU K 640  0                                        
SHEET    2 AD3 3 ASP K 705  ALA K 712 -1  O  ILE K 710   N  ILE K 638           
SHEET    3 AD3 3 CYS K 695  VAL K 702 -1  N  VAL K 702   O  ASP K 705           
SHEET    1 AD4 2 ASN K 688  HIS K 689  0                                        
SHEET    2 AD4 2 PHE K 723  PHE K 724  1  O  PHE K 724   N  ASN K 688           
SHEET    1 AD5 4 PHE L 147  ASP L 155  0                                        
SHEET    2 AD5 4 HIS L 160  GLY L 167 -1  O  LEU L 162   N  THR L 153           
SHEET    3 AD5 4 ILE L 172  ASN L 176 -1  O  ILE L 175   N  LEU L 163           
SHEET    4 AD5 4 GLN L 181  TYR L 186 -1  O  LYS L 184   N  ILE L 174           
SHEET    1 AD6 5 ILE L 193  PHE L 198  0                                        
SHEET    2 AD6 5 LEU L 205  SER L 210 -1  O  LEU L 207   N  LYS L 197           
SHEET    3 AD6 5 LEU L 215  ASN L 219 -1  O  TRP L 218   N  LEU L 206           
SHEET    4 AD6 5 THR L 224  PHE L 229 -1  O  PHE L 229   N  LEU L 215           
SHEET    5 AD6 5 GLN L 292  ILE L 294  1  O  ILE L 294   N  ILE L 228           
SHEET    1 AD7 4 VAL L 239  TYR L 244  0                                        
SHEET    2 AD7 4 LYS L 250  GLY L 255 -1  O  CYS L 254   N  SER L 241           
SHEET    3 AD7 4 LEU L 260  ARG L 264 -1  O  TRP L 263   N  ILE L 251           
SHEET    4 AD7 4 PHE L 299  THR L 301 -1  O  PHE L 299   N  LEU L 262           
SHEET    1 AD8 4 VAL L 309  LEU L 315  0                                        
SHEET    2 AD8 4 LEU L 318  SER L 323 -1  O  LEU L 318   N  LEU L 315           
SHEET    3 AD8 4 ALA L 327  PRO L 333 -1  O  VAL L 329   N  SER L 321           
SHEET    4 AD8 4 VAL L 350  ASP L 357 -1  O  PHE L 356   N  ILE L 328           
SHEET    1 AD9 4 PHE L 368  MET L 370  0                                        
SHEET    2 AD9 4 MET L 376  GLY L 380 -1  O  ALA L 378   N  SER L 369           
SHEET    3 AD9 4 LEU L 386  ASP L 390 -1  O  TRP L 389   N  LEU L 377           
SHEET    4 AD9 4 CYS L 401  LEU L 404 -1  O  THR L 402   N  VAL L 388           
SHEET    1 AE1 6 GLN Q  94  PRO Q  97  0                                        
SHEET    2 AE1 6 GLU Q  82  SER Q  87 -1  N  CYS Q  83   O  ILE Q  96           
SHEET    3 AE1 6 SER R  81  GLU R  90 -1  O  LYS R  89   N  THR Q  86           
SHEET    4 AE1 6 SER R 433  LEU R 440 -1  O  ILE R 434   N  LEU R  88           
SHEET    5 AE1 6 ILE R 424  CYS R 429 -1  N  ALA R 427   O  TRP R 435           
SHEET    6 AE1 6 ILE R 413  PHE R 418 -1  N  SER R 417   O  ILE R 426           
SHEET    1 AE2 5 LYS Q  99  LEU Q 101  0                                        
SHEET    2 AE2 5 ILE R 132  ASP R 140  1  O  VAL R 139   N  LEU Q 101           
SHEET    3 AE2 5 ARG R 120  CYS R 126 -1  N  GLU R 125   O  ARG R 133           
SHEET    4 AE2 5 LEU R 111  GLY R 117 -1  N  LEU R 111   O  CYS R 126           
SHEET    5 AE2 5 LEU R  96  PHE R 101 -1  N  GLN R 100   O  ALA R 114           
SHEET    1 AE3 4 SER Q 114  PRO Q 115  0                                        
SHEET    2 AE3 4 PHE Q 673  GLY Q 681  1  O  GLY Q 681   N  SER Q 114           
SHEET    3 AE3 4 GLY Q 643  SER Q 647 -1  N  GLU Q 644   O  ASP Q 676           
SHEET    4 AE3 4 PHE Q 120  MET Q 121  1  N  PHE Q 120   O  ILE Q 645           
SHEET    1 AE4 3 SER Q 114  PRO Q 115  0                                        
SHEET    2 AE4 3 PHE Q 673  GLY Q 681  1  O  GLY Q 681   N  SER Q 114           
SHEET    3 AE4 3 LEU Q 666  ASN Q 668 -1  N  PHE Q 667   O  VAL Q 675           
SHEET    1 AE5 2 LEU Q 614  PRO Q 618  0                                        
SHEET    2 AE5 2 TRP Q 624  ILE Q 628 -1  O  PHE Q 627   N  LEU Q 615           
SHEET    1 AE6 3 PHE Q 637  GLU Q 640  0                                        
SHEET    2 AE6 3 ASP Q 705  ALA Q 712 -1  O  ILE Q 710   N  ILE Q 638           
SHEET    3 AE6 3 CYS Q 695  VAL Q 702 -1  N  VAL Q 702   O  ASP Q 705           
SHEET    1 AE7 2 ASN Q 688  HIS Q 689  0                                        
SHEET    2 AE7 2 PHE Q 723  PHE Q 724  1  O  PHE Q 724   N  ASN Q 688           
SHEET    1 AE8 4 PHE R 147  TYR R 154  0                                        
SHEET    2 AE8 4 PRO R 161  GLY R 167 -1  O  LEU R 162   N  THR R 153           
SHEET    3 AE8 4 ILE R 172  ASN R 176 -1  O  ILE R 175   N  LEU R 163           
SHEET    4 AE8 4 GLN R 181  TYR R 186 -1  O  LYS R 184   N  ILE R 174           
SHEET    1 AE9 5 ILE R 193  PHE R 198  0                                        
SHEET    2 AE9 5 LEU R 205  SER R 210 -1  O  LEU R 207   N  LYS R 197           
SHEET    3 AE9 5 LEU R 215  ASN R 219 -1  O  TRP R 218   N  LEU R 206           
SHEET    4 AE9 5 THR R 224  PHE R 229 -1  O  PHE R 229   N  LEU R 215           
SHEET    5 AE9 5 GLN R 292  ILE R 294  1  O  ILE R 294   N  ILE R 228           
SHEET    1 AF1 4 VAL R 239  TYR R 244  0                                        
SHEET    2 AF1 4 LYS R 250  GLY R 255 -1  O  CYS R 254   N  LEU R 240           
SHEET    3 AF1 4 LEU R 260  ARG R 264 -1  O  TRP R 263   N  ILE R 251           
SHEET    4 AF1 4 PHE R 299  THR R 301 -1  O  THR R 301   N  LEU R 260           
SHEET    1 AF2 4 CYS R 311  LEU R 315  0                                        
SHEET    2 AF2 4 LEU R 318  LYS R 322 -1  O  LEU R 320   N  ARG R 313           
SHEET    3 AF2 4 ALA R 327  PRO R 333 -1  O  VAL R 329   N  SER R 321           
SHEET    4 AF2 4 VAL R 350  ASP R 357 -1  O  GLY R 354   N  CYS R 330           
SHEET    1 AF3 4 PHE R 368  MET R 370  0                                        
SHEET    2 AF3 4 MET R 376  GLY R 380 -1  O  ALA R 378   N  SER R 369           
SHEET    3 AF3 4 LEU R 386  ASP R 390 -1  O  TRP R 389   N  LEU R 377           
SHEET    4 AF3 4 THR R 402  LEU R 404 -1  O  THR R 402   N  VAL R 388           
LINK         SG  CYS A 286                ZN    ZN A1001     1555   1555  2.26  
LINK         SG  CYS A 289                ZN    ZN A1001     1555   1555  2.14  
LINK         SG  CYS A 294                ZN    ZN A1001     1555   1555  2.15  
LINK         ND1 HIS A 297                ZN    ZN A1001     1555   1555  1.98  
LINK         SG  CYS A 320                ZN    ZN A1002     1555   1555  2.51  
LINK         SG  CYS A 324                ZN    ZN A1002     1555   1555  2.92  
LINK         SG  CYS A 452                ZN    ZN A1002     1555   1555  2.26  
LINK         SG  CYS A 463                ZN    ZN A1002     1555   1555  2.15  
LINK         SG  CYS A 523                ZN    ZN A1004     1555   1555  2.37  
LINK         SG  CYS A 523                ZN    ZN A1005     1555   1555  2.24  
LINK         NE2 HIS A 525                ZN    ZN A1004     1555   1555  2.02  
LINK         SG  CYS A 530                ZN    ZN A1003     1555   1555  2.18  
LINK         SG  CYS A 530                ZN    ZN A1004     1555   1555  2.18  
LINK         SG  CYS A 534                ZN    ZN A1004     1555   1555  2.09  
LINK         SG  CYS A 536                ZN    ZN A1005     1555   1555  2.27  
LINK         SG  CYS A 543                ZN    ZN A1003     1555   1555  2.45  
LINK         SG  CYS A 543                ZN    ZN A1005     1555   1555  2.04  
LINK         SG  CYS A 547                ZN    ZN A1005     1555   1555  2.36  
LINK         SG  CYS A 549                ZN    ZN A1003     1555   1555  2.57  
LINK         SG  CYS A 553                ZN    ZN A1003     1555   1555  2.34  
LINK         SG  CYS A 560                ZN    ZN A1008     1555   1555  1.99  
LINK         SG  CYS A 560                ZN    ZN A1007     1555   1555  2.24  
LINK         SG  CYS A 562                ZN    ZN A1008     1555   1555  2.39  
LINK         SG  CYS A 566                ZN    ZN A1008     1555   1555  2.72  
LINK         SG  CYS A 566                ZN    ZN A1006     1555   1555  2.25  
LINK         SG  CYS A 571                ZN    ZN A1008     1555   1555  2.22  
LINK         SG  CYS A 573                ZN    ZN A1007     1555   1555  2.33  
LINK         SG  CYS A 580                ZN    ZN A1007     1555   1555  2.61  
LINK         SG  CYS A 580                ZN    ZN A1006     1555   1555  2.13  
LINK         SG  CYS A 585                ZN    ZN A1007     1555   1555  2.24  
LINK         SG  CYS A 588                ZN    ZN A1006     1555   1555  2.29  
LINK         SG  CYS A 601                ZN    ZN A1006     1555   1555  2.27  
LINK         C   ARG E   6                 N   M3L E   7     1555   1555  1.33  
LINK         C   M3L E   7                 N   PHE E   8     1555   1555  1.34  
LINK         SG  CYS F 286                ZN    ZN F1001     1555   1555  2.17  
LINK         SG  CYS F 289                ZN    ZN F1001     1555   1555  2.07  
LINK         SG  CYS F 294                ZN    ZN F1001     1555   1555  2.30  
LINK         SG  CYS F 320                ZN    ZN F1002     1555   1555  2.71  
LINK         SG  CYS F 324                ZN    ZN F1002     1555   1555  2.68  
LINK         SG  CYS F 452                ZN    ZN F1002     1555   1555  2.60  
LINK         SG  CYS F 463                ZN    ZN F1002     1555   1555  2.19  
LINK         SG  CYS F 523                ZN    ZN F1005     1555   1555  2.39  
LINK         SG  CYS F 523                ZN    ZN F1004     1555   1555  2.26  
LINK         NE2 HIS F 525                ZN    ZN F1004     1555   1555  2.18  
LINK         SG  CYS F 530                ZN    ZN F1003     1555   1555  2.16  
LINK         SG  CYS F 530                ZN    ZN F1004     1555   1555  2.11  
LINK         SG  CYS F 534                ZN    ZN F1004     1555   1555  2.09  
LINK         SG  CYS F 536                ZN    ZN F1005     1555   1555  2.47  
LINK         SG  CYS F 543                ZN    ZN F1005     1555   1555  2.20  
LINK         SG  CYS F 543                ZN    ZN F1003     1555   1555  2.72  
LINK         SG  CYS F 547                ZN    ZN F1005     1555   1555  2.23  
LINK         SG  CYS F 549                ZN    ZN F1003     1555   1555  2.11  
LINK         SG  CYS F 553                ZN    ZN F1003     1555   1555  2.39  
LINK         SG  CYS F 560                ZN    ZN F1008     1555   1555  2.31  
LINK         SG  CYS F 560                ZN    ZN F1007     1555   1555  2.11  
LINK         SG  CYS F 562                ZN    ZN F1008     1555   1555  2.24  
LINK         SG  CYS F 566                ZN    ZN F1006     1555   1555  2.34  
LINK         SG  CYS F 566                ZN    ZN F1008     1555   1555  2.32  
LINK         SG  CYS F 571                ZN    ZN F1008     1555   1555  2.29  
LINK         SG  CYS F 573                ZN    ZN F1007     1555   1555  2.29  
LINK         SG  CYS F 580                ZN    ZN F1006     1555   1555  2.30  
LINK         SG  CYS F 580                ZN    ZN F1007     1555   1555  2.19  
LINK         SG  CYS F 585                ZN    ZN F1007     1555   1555  2.43  
LINK         SG  CYS F 588                ZN    ZN F1006     1555   1555  2.36  
LINK         SG  CYS F 601                ZN    ZN F1006     1555   1555  2.23  
LINK         C   ARG J   6                 N   M3L J   7     1555   1555  1.33  
LINK         C   M3L J   7                 N   PHE J   8     1555   1555  1.32  
LINK         SG  CYS K 286                ZN    ZN K1001     1555   1555  2.39  
LINK         SG  CYS K 289                ZN    ZN K1001     1555   1555  2.28  
LINK         SG  CYS K 294                ZN    ZN K1001     1555   1555  2.40  
LINK         ND1 HIS K 297                ZN    ZN K1001     1555   1555  2.00  
LINK         SG  CYS K 320                ZN    ZN K1002     1555   1555  2.14  
LINK         SG  CYS K 452                ZN    ZN K1002     1555   1555  2.45  
LINK         SG  CYS K 463                ZN    ZN K1002     1555   1555  2.43  
LINK         SG  CYS K 523                ZN    ZN K1004     1555   1555  2.25  
LINK         SG  CYS K 523                ZN    ZN K1005     1555   1555  2.39  
LINK         NE2 HIS K 525                ZN    ZN K1004     1555   1555  2.28  
LINK         SG  CYS K 530                ZN    ZN K1003     1555   1555  2.41  
LINK         SG  CYS K 530                ZN    ZN K1004     1555   1555  2.25  
LINK         SG  CYS K 534                ZN    ZN K1004     1555   1555  2.08  
LINK         SG  CYS K 536                ZN    ZN K1005     1555   1555  2.16  
LINK         SG  CYS K 543                ZN    ZN K1003     1555   1555  2.50  
LINK         SG  CYS K 543                ZN    ZN K1005     1555   1555  2.24  
LINK         SG  CYS K 547                ZN    ZN K1005     1555   1555  2.39  
LINK         SG  CYS K 549                ZN    ZN K1003     1555   1555  2.20  
LINK         SG  CYS K 553                ZN    ZN K1003     1555   1555  2.31  
LINK         SG  CYS K 560                ZN    ZN K1008     1555   1555  2.18  
LINK         SG  CYS K 560                ZN    ZN K1007     1555   1555  2.30  
LINK         SG  CYS K 562                ZN    ZN K1008     1555   1555  2.28  
LINK         SG  CYS K 566                ZN    ZN K1008     1555   1555  2.40  
LINK         SG  CYS K 566                ZN    ZN K1006     1555   1555  2.42  
LINK         SG  CYS K 571                ZN    ZN K1008     1555   1555  2.22  
LINK         SG  CYS K 573                ZN    ZN K1007     1555   1555  2.30  
LINK         SG  CYS K 580                ZN    ZN K1006     1555   1555  2.33  
LINK         SG  CYS K 580                ZN    ZN K1007     1555   1555  2.30  
LINK         SG  CYS K 585                ZN    ZN K1007     1555   1555  2.14  
LINK         SG  CYS K 588                ZN    ZN K1006     1555   1555  2.05  
LINK         SG  CYS K 601                ZN    ZN K1006     1555   1555  2.16  
LINK         C   ARG P   6                 N   M3L P   7     1555   1555  1.34  
LINK         C   M3L P   7                 N   PHE P   8     1555   1555  1.33  
LINK         SG  CYS Q 286                ZN    ZN Q1001     1555   1555  2.39  
LINK         SG  CYS Q 289                ZN    ZN Q1001     1555   1555  2.07  
LINK         SG  CYS Q 294                ZN    ZN Q1001     1555   1555  2.33  
LINK         ND1 HIS Q 297                ZN    ZN Q1001     1555   1555  1.93  
LINK         SG  CYS Q 320                ZN    ZN Q1002     1555   1555  2.47  
LINK         SG  CYS Q 452                ZN    ZN Q1002     1555   1555  2.74  
LINK         SG  CYS Q 463                ZN    ZN Q1002     1555   1555  2.29  
LINK         SG  CYS Q 523                ZN    ZN Q1004     1555   1555  2.48  
LINK         SG  CYS Q 523                ZN    ZN Q1005     1555   1555  2.28  
LINK         NE2 HIS Q 525                ZN    ZN Q1004     1555   1555  2.50  
LINK         SG  CYS Q 530                ZN    ZN Q1003     1555   1555  2.31  
LINK         SG  CYS Q 530                ZN    ZN Q1004     1555   1555  2.23  
LINK         SG  CYS Q 534                ZN    ZN Q1004     1555   1555  2.02  
LINK         SG  CYS Q 536                ZN    ZN Q1005     1555   1555  2.26  
LINK         SG  CYS Q 543                ZN    ZN Q1003     1555   1555  2.45  
LINK         SG  CYS Q 543                ZN    ZN Q1005     1555   1555  2.32  
LINK         SG  CYS Q 547                ZN    ZN Q1005     1555   1555  2.38  
LINK         SG  CYS Q 549                ZN    ZN Q1003     1555   1555  2.17  
LINK         SG  CYS Q 553                ZN    ZN Q1003     1555   1555  2.45  
LINK         SG  CYS Q 560                ZN    ZN Q1007     1555   1555  2.52  
LINK         SG  CYS Q 560                ZN    ZN Q1008     1555   1555  2.20  
LINK         SG  CYS Q 562                ZN    ZN Q1008     1555   1555  2.20  
LINK         SG  CYS Q 566                ZN    ZN Q1008     1555   1555  2.26  
LINK         SG  CYS Q 566                ZN    ZN Q1006     1555   1555  2.20  
LINK         SG  CYS Q 571                ZN    ZN Q1008     1555   1555  2.25  
LINK         SG  CYS Q 573                ZN    ZN Q1007     1555   1555  2.28  
LINK         SG  CYS Q 580                ZN    ZN Q1007     1555   1555  2.41  
LINK         SG  CYS Q 580                ZN    ZN Q1006     1555   1555  2.31  
LINK         SG  CYS Q 585                ZN    ZN Q1007     1555   1555  2.47  
LINK         SG  CYS Q 588                ZN    ZN Q1006     1555   1555  2.09  
LINK         SG  CYS Q 601                ZN    ZN Q1006     1555   1555  2.27  
LINK         C   ARG U   6                 N   M3L U   7     1555   1555  1.33  
LINK         C   M3L U   7                 N   PHE U   8     1555   1555  1.34  
CISPEP   1 SER A   73    VAL A   74          0         0.44                     
CISPEP   2 GLN A  141    ASP A  142          0         2.82                     
CISPEP   3 HIS A  158    GLY A  159          0       -11.03                     
CISPEP   4 SER A  212    ARG A  213          0        -1.60                     
CISPEP   5 PRO A  214    PRO A  215          0        -7.24                     
CISPEP   6 GLY A  235    THR A  236          0         7.96                     
CISPEP   7 PRO A  258    GLU A  259          0         0.51                     
CISPEP   8 THR A  302    PRO A  303          0         1.25                     
CISPEP   9 THR A  311    GLU A  312          0         8.88                     
CISPEP  10 GLU A  312    THR A  313          0         4.75                     
CISPEP  11 LYS A  318    PRO A  319          0        -3.35                     
CISPEP  12 CYS A  320    GLY A  321          0        -7.96                     
CISPEP  13 GLY A  321    PRO A  322          0        -1.15                     
CISPEP  14 GLN A  326    HIS A  327          0        -5.72                     
CISPEP  15 SER A  729    GLN A  730          0       -16.02                     
CISPEP  16 ASP A  732    ALA A  733          0         7.38                     
CISPEP  17 LEU A  734    LYS A  735          0       -10.41                     
CISPEP  18 VAL A  737    GLY A  738          0        -2.42                     
CISPEP  19 LYS B   79    TYR B   80          0         5.03                     
CISPEP  20 SER B  128    GLN B  129          0        -7.73                     
CISPEP  21 PRO B  396    HIS B  397          0        20.23                     
CISPEP  22 HIS B  397    LYS B  398          0        -0.27                     
CISPEP  23 ALA B  399    LYS B  400          0        -1.99                     
CISPEP  24 HIS C  561    ASN C  562          0       -21.21                     
CISPEP  25 MET C  579    GLU C  580          0       -16.57                     
CISPEP  26 VAL C  581    ASP C  582          0        -8.77                     
CISPEP  27 GLU C  586    LYS C  587          0        -6.29                     
CISPEP  28 GLU C  608    GLY C  609          0        12.81                     
CISPEP  29 SER F   73    VAL F   74          0        -8.79                     
CISPEP  30 GLU F  137    VAL F  138          0        -3.19                     
CISPEP  31 ASP F  140    GLN F  141          0         0.73                     
CISPEP  32 HIS F  158    GLY F  159          0        -8.14                     
CISPEP  33 GLY F  235    THR F  236          0        11.10                     
CISPEP  34 THR F  302    PRO F  303          0         5.27                     
CISPEP  35 LEU F  315    ASP F  316          0         0.33                     
CISPEP  36 LYS F  318    PRO F  319          0        -2.30                     
CISPEP  37 CYS F  320    GLY F  321          0       -15.33                     
CISPEP  38 GLN F  326    HIS F  327          0       -12.53                     
CISPEP  39 ASP F  592    HIS F  593          0        14.48                     
CISPEP  40 SER F  729    GLN F  730          0       -21.22                     
CISPEP  41 ASP F  732    ALA F  733          0       -13.04                     
CISPEP  42 ALA G  399    LYS G  400          0        -3.35                     
CISPEP  43 MET H  579    GLU H  580          0        -0.64                     
CISPEP  44 GLU H  580    VAL H  581          0        -2.38                     
CISPEP  45 GLU H  584    ASP H  585          0        -0.17                     
CISPEP  46 THR I   22    LYS I   23          0        -2.88                     
CISPEP  47 PRO K   67    VAL K   68          0        -1.28                     
CISPEP  48 THR K   72    SER K   73          0         9.62                     
CISPEP  49 PHE K   91    PRO K   92          0         0.80                     
CISPEP  50 ASP K  140    GLN K  141          0       -12.76                     
CISPEP  51 HIS K  158    GLY K  159          0        -8.44                     
CISPEP  52 THR K  302    PRO K  303          0         1.75                     
CISPEP  53 ALA K  314    LEU K  315          0        -5.09                     
CISPEP  54 PRO K  319    CYS K  320          0        -8.81                     
CISPEP  55 GLY K  321    PRO K  322          0       -12.30                     
CISPEP  56 GLN K  326    HIS K  327          0       -13.93                     
CISPEP  57 ASP K  592    HIS K  593          0        -6.28                     
CISPEP  58 SER K  729    GLN K  730          0       -15.85                     
CISPEP  59 LYS L   79    TYR L   80          0        -2.43                     
CISPEP  60 GLU L  392    VAL L  393          0        -5.87                     
CISPEP  61 ASP L  395    PRO L  396          0       -17.32                     
CISPEP  62 ALA L  399    LYS L  400          0         3.98                     
CISPEP  63 ASP M  585    GLU M  586          0         0.70                     
CISPEP  64 GLU M  586    LYS M  587          0       -11.61                     
CISPEP  65 LEU Q   71    THR Q   72          0         1.02                     
CISPEP  66 VAL Q   74    SER Q   75          0        -2.57                     
CISPEP  67 MET Q  134    GLY Q  135          0        12.03                     
CISPEP  68 VAL Q  138    LEU Q  139          0        -9.86                     
CISPEP  69 LEU Q  139    ASP Q  140          0        -2.44                     
CISPEP  70 ASP Q  140    GLN Q  141          0        -7.28                     
CISPEP  71 CYS Q  163    GLY Q  164          0         9.72                     
CISPEP  72 CYS Q  260    THR Q  261          0        22.56                     
CISPEP  73 ILE Q  264    ASP Q  265          0        26.25                     
CISPEP  74 THR Q  302    PRO Q  303          0         1.13                     
CISPEP  75 LYS Q  318    PRO Q  319          0         2.25                     
CISPEP  76 CYS Q  320    GLY Q  321          0       -10.19                     
CISPEP  77 GLY Q  321    PRO Q  322          0        -4.12                     
CISPEP  78 SER Q  729    GLN Q  730          0        -7.21                     
CISPEP  79 ASP Q  732    ALA Q  733          0        -7.90                     
CISPEP  80 GLU R  392    VAL R  393          0        -1.11                     
CISPEP  81 ASP R  395    PRO R  396          0        -8.06                     
CISPEP  82 ALA R  399    LYS R  400          0        -5.58                     
CISPEP  83 HIS S  561    ASN S  562          0         5.09                     
CISPEP  84 VAL S  581    ASP S  582          0        -1.85                     
CISPEP  85 LYS S  587    ASP S  588          0        -5.86                     
SITE     1 AC1  4 CYS A 286  CYS A 289  CYS A 294  HIS A 297                    
SITE     1 AC2  4 CYS A 320  CYS A 324  CYS A 452  CYS A 463                    
SITE     1 AC3  4 CYS A 530  CYS A 543  CYS A 549  CYS A 553                    
SITE     1 AC4  4 CYS A 523  HIS A 525  CYS A 530  CYS A 534                    
SITE     1 AC5  4 CYS A 523  CYS A 536  CYS A 543  CYS A 547                    
SITE     1 AC6  7 CYS A 560  CYS A 566  CYS A 580  CYS A 588                    
SITE     2 AC6  7 CYS A 601   ZN A1007   ZN A1008                               
SITE     1 AC7  6 CYS A 560  CYS A 573  CYS A 580  CYS A 585                    
SITE     2 AC7  6  ZN A1006   ZN A1008                                          
SITE     1 AC8  6 CYS A 560  CYS A 562  CYS A 566  CYS A 571                    
SITE     2 AC8  6  ZN A1006   ZN A1007                                          
SITE     1 AC9 15 VAL A 621  ALA A 622  GLY A 623  TRP A 624                    
SITE     2 AC9 15 MET A 662  CYS A 663  SER A 664  PHE A 665                    
SITE     3 AC9 15 PHE A 686  ALA A 687  ASN A 688  HIS A 689                    
SITE     4 AC9 15 TYR A 726  LEU A 734  TYR A 736                               
SITE     1 AD1  4 CYS F 286  CYS F 289  CYS F 294  HIS F 297                    
SITE     1 AD2  4 CYS F 320  CYS F 324  CYS F 452  CYS F 463                    
SITE     1 AD3  4 CYS F 530  CYS F 543  CYS F 549  CYS F 553                    
SITE     1 AD4  4 CYS F 523  HIS F 525  CYS F 530  CYS F 534                    
SITE     1 AD5  4 CYS F 523  CYS F 536  CYS F 543  CYS F 547                    
SITE     1 AD6  4 CYS F 566  CYS F 580  CYS F 588  CYS F 601                    
SITE     1 AD7  5 CYS F 560  CYS F 573  CYS F 580  CYS F 585                    
SITE     2 AD7  5  ZN F1008                                                     
SITE     1 AD8  5 CYS F 560  CYS F 562  CYS F 566  CYS F 571                    
SITE     2 AD8  5  ZN F1007                                                     
SITE     1 AD9 15 VAL F 621  ALA F 622  GLY F 623  TRP F 624                    
SITE     2 AD9 15 MET F 662  CYS F 663  SER F 664  PHE F 665                    
SITE     3 AD9 15 PHE F 686  ASN F 688  HIS F 689  TYR F 726                    
SITE     4 AD9 15 ALA F 733  LEU F 734  TYR F 736                               
SITE     1 AE1  4 CYS K 286  CYS K 289  CYS K 294  HIS K 297                    
SITE     1 AE2  4 CYS K 320  CYS K 324  CYS K 452  CYS K 463                    
SITE     1 AE3  4 CYS K 530  CYS K 543  CYS K 549  CYS K 553                    
SITE     1 AE4  4 CYS K 523  HIS K 525  CYS K 530  CYS K 534                    
SITE     1 AE5  4 CYS K 523  CYS K 536  CYS K 543  CYS K 547                    
SITE     1 AE6  4 CYS K 566  CYS K 580  CYS K 588  CYS K 601                    
SITE     1 AE7  5 CYS K 560  CYS K 573  CYS K 580  CYS K 585                    
SITE     2 AE7  5  ZN K1008                                                     
SITE     1 AE8  5 CYS K 560  CYS K 562  CYS K 566  CYS K 571                    
SITE     2 AE8  5  ZN K1007                                                     
SITE     1 AE9 13 VAL K 621  ALA K 622  GLY K 623  TRP K 624                    
SITE     2 AE9 13 MET K 662  CYS K 663  SER K 664  PHE K 665                    
SITE     3 AE9 13 ARG K 685  PHE K 686  ASN K 688  HIS K 689                    
SITE     4 AE9 13 TYR K 726                                                     
SITE     1 AF1  4 CYS Q 286  CYS Q 289  CYS Q 294  HIS Q 297                    
SITE     1 AF2  4 CYS Q 320  GLN Q 323  CYS Q 452  CYS Q 463                    
SITE     1 AF3  4 CYS Q 530  CYS Q 543  CYS Q 549  CYS Q 553                    
SITE     1 AF4  4 CYS Q 523  HIS Q 525  CYS Q 530  CYS Q 534                    
SITE     1 AF5  4 CYS Q 523  CYS Q 536  CYS Q 543  CYS Q 547                    
SITE     1 AF6  5 CYS Q 566  CYS Q 580  CYS Q 588  CYS Q 601                    
SITE     2 AF6  5  ZN Q1008                                                     
SITE     1 AF7  5 CYS Q 560  CYS Q 573  CYS Q 580  CYS Q 585                    
SITE     2 AF7  5  ZN Q1008                                                     
SITE     1 AF8  6 CYS Q 560  CYS Q 562  CYS Q 566  CYS Q 571                    
SITE     2 AF8  6  ZN Q1006   ZN Q1007                                          
SITE     1 AF9 15 VAL Q 621  ALA Q 622  GLY Q 623  TRP Q 624                    
SITE     2 AF9 15 MET Q 662  CYS Q 663  SER Q 664  PHE Q 665                    
SITE     3 AF9 15 PHE Q 686  ASN Q 688  HIS Q 689  TYR Q 726                    
SITE     4 AF9 15 ALA Q 733  LEU Q 734  LYS Q 735                               
SITE     1 AG1 11 ASP F 136  GLU F 137  ASP F 140  TYR G 148                    
SITE     2 AG1 11 ILE G 363  TRP G 364  TYR G 365  ARG G 414                    
SITE     3 AG1 11 GLN J   5  PHE J   8  GLN J  10                               
SITE     1 AG2  9 ASP F 136  GLU F 137  TYR G 148  ILE G 363                    
SITE     2 AG2  9 TRP G 364  TYR G 365  ARG G 414  ARG J   6                    
SITE     3 AG2  9 ALA J   9                                                     
SITE     1 AG3 12 TYR K 133  ASP K 136  ASP K 140  TYR L 148                    
SITE     2 AG3 12 ILE L 363  TRP L 364  ARG L 414  GLN P   3                    
SITE     3 AG3 12 ALA P   4  GLN P   5  PHE P   8  GLN P  10                    
SITE     1 AG4 10 TYR K 133  ASP K 136  GLU K 137  TYR L 148                    
SITE     2 AG4 10 ILE L 363  TRP L 364  ARG L 414  ARG P   6                    
SITE     3 AG4 10 ALA P   9  GLN P  10                                          
SITE     1 AG5 11 TYR Q 133  ASP Q 136  TYR R 148  ILE R 363                    
SITE     2 AG5 11 TRP R 364  TYR R 365  ARG R 414  ALA U   4                    
SITE     3 AG5 11 GLN U   5  PHE U   8  GLN U  10                               
SITE     1 AG6 11 TYR Q 133  ASP Q 136  PHE R  97  TYR R 148                    
SITE     2 AG6 11 ILE R 363  TRP R 364  TYR R 365  ARG R 414                    
SITE     3 AG6 11 ASP R 430  ARG U   6  ALA U   9                               
CRYST1  131.640  171.510  274.550  90.00  90.00  90.00 P 21 21 21   16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.007596  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005831  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003642        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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