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Database: PDB
Entry: 5VSF
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HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       11-MAY-17   5VSF              
TITLE     STRUCTURE OF HUMAN GLP SET-DOMAIN (EHMT1) IN COMPLEX WITH INHIBITOR 17
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE EHMT1;                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: GLP CATALYTIC SET-DOMAIN RESIDUES 1006-1266;               
COMPND   5 SYNONYM: EUCHROMATIC HISTONE-LYSINE N-METHYLTRANSFERASE 1,EU-HMTASE1,
COMPND   6 G9A-LIKE PROTEIN 1,GLP1,HISTONE H3-K9 METHYLTRANSFERASE 5,H3-K9-     
COMPND   7 HMTASE 5,LYSINE N-METHYLTRANSFERASE 1D;                              
COMPND   8 EC: 2.1.1.-,2.1.1.43;                                                
COMPND   9 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: EHMT1, EUHMTASE1, GLP, KIAA1876, KMT1D;                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) CODON PLUS RIL;                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A-LIC                                
KEYWDS    PROTEIN-SMALL MOLECULE INHIBITOR COMPLEX, TRANSFERASE-TRANSFERASE     
KEYWDS   2 INHIBITOR COMPLEX                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.BABAULT,Y.XIONG,J.LIU,J.JIN                                         
REVDAT   2   02-AUG-17 5VSF    1       JRNL                                     
REVDAT   1   12-JUL-17 5VSF    0                                                
JRNL        AUTH   Y.XIONG,F.LI,N.BABAULT,H.WU,A.DONG,H.ZENG,X.CHEN,            
JRNL        AUTH 2 C.H.ARROWSMITH,P.J.BROWN,J.LIU,M.VEDADI,J.JIN                
JRNL        TITL   STRUCTURE-ACTIVITY RELATIONSHIP STUDIES OF G9A-LIKE PROTEIN  
JRNL        TITL 2 (GLP) INHIBITORS.                                            
JRNL        REF    BIOORG. MED. CHEM.            V.  25  4414 2017              
JRNL        REFN                   ESSN 1464-3391                               
JRNL        PMID   28662962                                                     
JRNL        DOI    10.1016/J.BMC.2017.06.021                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.11.1_2575                                   
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) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.96                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 78148                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.162                           
REMARK   3   R VALUE            (WORKING SET) : 0.161                           
REMARK   3   FREE R VALUE                     : 0.185                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.840                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3779                            
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 19.9631 -  5.0730    0.98     3039   138  0.1373 0.1558        
REMARK   3     2  5.0730 -  4.0375    1.00     2976   132  0.1187 0.1292        
REMARK   3     3  4.0375 -  3.5304    1.00     2892   163  0.1453 0.1598        
REMARK   3     4  3.5304 -  3.2090    1.00     2905   142  0.1568 0.1656        
REMARK   3     5  3.2090 -  2.9798    0.99     2867   144  0.1681 0.1764        
REMARK   3     6  2.9798 -  2.8046    0.95     2761   130  0.1623 0.1898        
REMARK   3     7  2.8046 -  2.6645    0.94     2663   159  0.1653 0.1776        
REMARK   3     8  2.6645 -  2.5488    0.92     2646   120  0.1652 0.1842        
REMARK   3     9  2.5488 -  2.4508    0.91     2626   134  0.1735 0.2011        
REMARK   3    10  2.4508 -  2.3664    0.92     2631   131  0.1720 0.2303        
REMARK   3    11  2.3664 -  2.2925    0.92     2628   136  0.1715 0.1874        
REMARK   3    12  2.2925 -  2.2271    0.93     2638   149  0.1787 0.2516        
REMARK   3    13  2.2271 -  2.1685    0.93     2680   132  0.1668 0.2067        
REMARK   3    14  2.1685 -  2.1157    0.94     2690   142  0.1630 0.1872        
REMARK   3    15  2.1157 -  2.0676    0.96     2696   160  0.1610 0.2132        
REMARK   3    16  2.0676 -  2.0237    0.96     2761   136  0.1639 0.1999        
REMARK   3    17  2.0237 -  1.9832    0.96     2722   156  0.1671 0.1927        
REMARK   3    18  1.9832 -  1.9458    0.97     2748   117  0.1702 0.2227        
REMARK   3    19  1.9458 -  1.9111    0.96     2723   148  0.2043 0.2379        
REMARK   3    20  1.9111 -  1.8787    0.97     2781   150  0.2032 0.2486        
REMARK   3    21  1.8787 -  1.8485    0.97     2719   149  0.1760 0.2151        
REMARK   3    22  1.8485 -  1.8200    0.97     2764   141  0.1741 0.1948        
REMARK   3    23  1.8200 -  1.7933    0.97     2768   137  0.1699 0.2126        
REMARK   3    24  1.7933 -  1.7680    0.97     2756   133  0.1870 0.2113        
REMARK   3    25  1.7680 -  1.7442    0.97     2756   131  0.1864 0.1987        
REMARK   3    26  1.7442 -  1.7215    0.97     2790   131  0.2094 0.2560        
REMARK   3    27  1.7215 -  1.7000    0.97     2743   138  0.2279 0.2561        
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)     : 0.160            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.720           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 18.27                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.52                          
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      :  0.007           4434                                  
REMARK   3   ANGLE     :  1.096           6002                                  
REMARK   3   CHIRALITY :  0.063            617                                  
REMARK   3   PLANARITY :  0.006            786                                  
REMARK   3   DIHEDRAL  : 13.581           2662                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 14                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1006 THROUGH 1042 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.5323 -12.5594   1.3464              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2667 T22:   0.2763                                     
REMARK   3      T33:   0.2074 T12:   0.1608                                     
REMARK   3      T13:  -0.0267 T23:  -0.0225                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3089 L22:   1.7634                                     
REMARK   3      L33:   6.3247 L12:   0.4409                                     
REMARK   3      L13:  -0.2743 L23:   0.8491                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1460 S12:  -0.3847 S13:   0.2536                       
REMARK   3      S21:   0.3319 S22:   0.0671 S23:   0.0549                       
REMARK   3      S31:  -0.3969 S32:  -0.5171 S33:   0.0907                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1043 THROUGH 1093 )               
REMARK   3    ORIGIN FOR THE GROUP (A):   8.3856 -35.2930 -16.0674              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1064 T22:   0.1787                                     
REMARK   3      T33:   0.2070 T12:   0.0047                                     
REMARK   3      T13:  -0.0424 T23:  -0.0091                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4888 L22:   2.8281                                     
REMARK   3      L33:   1.6564 L12:   0.2824                                     
REMARK   3      L13:  -0.0997 L23:  -0.0980                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0219 S12:  -0.0021 S13:  -0.1131                       
REMARK   3      S21:   0.0698 S22:  -0.0437 S23:  -0.2660                       
REMARK   3      S31:   0.1364 S32:   0.0693 S33:   0.0421                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1094 THROUGH 1127 )               
REMARK   3    ORIGIN FOR THE GROUP (A):   4.2939 -34.7229 -11.9813              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1265 T22:   0.1279                                     
REMARK   3      T33:   0.1839 T12:  -0.0018                                     
REMARK   3      T13:  -0.0204 T23:   0.0080                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0058 L22:   2.0322                                     
REMARK   3      L33:   3.8172 L12:   0.2180                                     
REMARK   3      L13:   0.9202 L23:   0.8881                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1062 S12:  -0.0255 S13:  -0.1516                       
REMARK   3      S21:   0.0374 S22:  -0.0597 S23:   0.0227                       
REMARK   3      S31:   0.0778 S32:  -0.1024 S33:  -0.0478                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1128 THROUGH 1150 )               
REMARK   3    ORIGIN FOR THE GROUP (A):   0.6663 -21.0647   8.0736              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2318 T22:   0.2717                                     
REMARK   3      T33:   0.1198 T12:   0.0625                                     
REMARK   3      T13:  -0.0040 T23:  -0.0011                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5995 L22:   4.5633                                     
REMARK   3      L33:   2.7283 L12:  -0.9025                                     
REMARK   3      L13:   0.3848 L23:   1.0797                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1521 S12:  -0.4139 S13:   0.0741                       
REMARK   3      S21:   0.6300 S22:   0.0092 S23:   0.0835                       
REMARK   3      S31:  -0.2212 S32:  -0.4713 S33:   0.1897                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1151 THROUGH 1184 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  16.4193 -16.4244  -8.2020              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1911 T22:   0.1912                                     
REMARK   3      T33:   0.2089 T12:  -0.0345                                     
REMARK   3      T13:  -0.0555 T23:  -0.0020                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8575 L22:   3.9060                                     
REMARK   3      L33:   3.9353 L12:   2.5392                                     
REMARK   3      L13:  -0.5995 L23:  -1.5725                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1259 S12:   0.2138 S13:  -0.1163                       
REMARK   3      S21:   0.1220 S22:  -0.0298 S23:  -0.5801                       
REMARK   3      S31:  -0.3719 S32:   0.5330 S33:   0.1149                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1185 THROUGH 1243 )               
REMARK   3    ORIGIN FOR THE GROUP (A):   9.8619 -23.4404  -2.4283              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1145 T22:   0.1366                                     
REMARK   3      T33:   0.1624 T12:   0.0037                                     
REMARK   3      T13:  -0.0346 T23:   0.0112                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5268 L22:   0.8553                                     
REMARK   3      L33:   3.0234 L12:  -0.0396                                     
REMARK   3      L13:   0.1576 L23:   0.1308                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0444 S12:  -0.0397 S13:  -0.0094                       
REMARK   3      S21:   0.1113 S22:   0.0233 S23:  -0.0714                       
REMARK   3      S31:  -0.1728 S32:  -0.0208 S33:   0.0214                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1244 THROUGH 1266 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  19.8947 -17.8069  10.4092              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2874 T22:   0.2473                                     
REMARK   3      T33:   0.2252 T12:  -0.0653                                     
REMARK   3      T13:  -0.1192 T23:   0.0180                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8652 L22:   4.9214                                     
REMARK   3      L33:   5.8753 L12:   2.5566                                     
REMARK   3      L13:  -2.0639 L23:  -3.5660                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0098 S12:  -0.0155 S13:   0.0712                       
REMARK   3      S21:   0.5081 S22:  -0.2326 S23:  -0.3353                       
REMARK   3      S31:  -0.7630 S32:   0.5164 S33:   0.2502                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1006 THROUGH 1023 )               
REMARK   3    ORIGIN FOR THE GROUP (A): -11.7811 -38.0872 -28.2870              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1585 T22:   0.1118                                     
REMARK   3      T33:   0.2106 T12:   0.0135                                     
REMARK   3      T13:  -0.0162 T23:   0.0263                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.6935 L22:   8.6344                                     
REMARK   3      L33:   8.5231 L12:   4.1997                                     
REMARK   3      L13:   3.4272 L23:   4.6700                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0078 S12:  -0.0076 S13:  -0.4919                       
REMARK   3      S21:  -0.2203 S22:   0.0285 S23:   0.1306                       
REMARK   3      S31:   0.4241 S32:  -0.0052 S33:  -0.0429                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1024 THROUGH 1073 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.0491 -20.4737 -27.0071              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1166 T22:   0.1249                                     
REMARK   3      T33:   0.0912 T12:   0.0075                                     
REMARK   3      T13:  -0.0133 T23:   0.0281                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1984 L22:   2.2294                                     
REMARK   3      L33:   1.1358 L12:   0.1142                                     
REMARK   3      L13:   0.3678 L23:   0.5986                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0102 S12:   0.0315 S13:  -0.0741                       
REMARK   3      S21:  -0.0368 S22:   0.0445 S23:  -0.0920                       
REMARK   3      S31:   0.0126 S32:   0.0613 S33:  -0.0520                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1074 THROUGH 1127 )               
REMARK   3    ORIGIN FOR THE GROUP (A): -13.8864 -10.7240 -23.5118              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1194 T22:   0.1531                                     
REMARK   3      T33:   0.1571 T12:   0.0287                                     
REMARK   3      T13:   0.0024 T23:   0.0054                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5097 L22:   2.5503                                     
REMARK   3      L33:   2.5598 L12:   0.3467                                     
REMARK   3      L13:   0.1423 L23:   0.7054                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0687 S12:   0.0086 S13:   0.0915                       
REMARK   3      S21:   0.0342 S22:   0.0623 S23:   0.1424                       
REMARK   3      S31:  -0.1366 S32:  -0.1688 S33:  -0.0011                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1128 THROUGH 1167 )               
REMARK   3    ORIGIN FOR THE GROUP (A): -10.7660 -27.1661 -37.2341              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1405 T22:   0.1483                                     
REMARK   3      T33:   0.1235 T12:   0.0090                                     
REMARK   3      T13:  -0.0316 T23:  -0.0079                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1609 L22:   2.0663                                     
REMARK   3      L33:   1.3006 L12:  -0.0423                                     
REMARK   3      L13:  -0.0998 L23:   0.2754                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0210 S12:   0.2190 S13:  -0.1498                       
REMARK   3      S21:  -0.1987 S22:  -0.0192 S23:   0.1662                       
REMARK   3      S31:   0.0658 S32:  -0.0036 S33:   0.0105                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1168 THROUGH 1194 )               
REMARK   3    ORIGIN FOR THE GROUP (A):   1.1861 -22.5196 -40.6410              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1572 T22:   0.2112                                     
REMARK   3      T33:   0.1340 T12:   0.0024                                     
REMARK   3      T13:   0.0177 T23:  -0.0277                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.5562 L22:   3.3029                                     
REMARK   3      L33:   5.5750 L12:   0.2649                                     
REMARK   3      L13:  -0.7202 L23:  -0.7435                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0232 S12:   0.5726 S13:  -0.0234                       
REMARK   3      S21:  -0.4192 S22:  -0.0080 S23:  -0.2112                       
REMARK   3      S31:  -0.0938 S32:   0.2557 S33:   0.0021                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1195 THROUGH 1243 )               
REMARK   3    ORIGIN FOR THE GROUP (A): -12.1199 -19.3389 -36.1129              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0984 T22:   0.1375                                     
REMARK   3      T33:   0.1368 T12:   0.0058                                     
REMARK   3      T13:  -0.0169 T23:   0.0065                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3320 L22:   1.6556                                     
REMARK   3      L33:   1.8287 L12:   0.3303                                     
REMARK   3      L13:   0.2779 L23:   0.5073                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0147 S12:   0.1620 S13:  -0.0353                       
REMARK   3      S21:  -0.1445 S22:   0.0226 S23:   0.1300                       
REMARK   3      S31:  -0.0290 S32:  -0.0675 S33:  -0.0010                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1244 THROUGH 1266 )               
REMARK   3    ORIGIN FOR THE GROUP (A): -12.2748 -22.1723 -53.2031              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2803 T22:   0.3783                                     
REMARK   3      T33:   0.1547 T12:   0.0056                                     
REMARK   3      T13:  -0.0520 T23:  -0.0271                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.0013 L22:   2.6858                                     
REMARK   3      L33:   4.2422 L12:   0.2968                                     
REMARK   3      L13:  -0.7205 L23:  -0.4765                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0623 S12:   1.1289 S13:   0.1047                       
REMARK   3      S21:  -0.4790 S22:  -0.0610 S23:   0.1406                       
REMARK   3      S31:  -0.1229 S32:   0.0306 S33:   0.0265                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 1                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: (CHAIN A AND (RESID 1006 THROUGH 1178 OR    
REMARK   3                          RESID 1182 THROUGH 1266))                   
REMARK   3     SELECTION          : CHAIN B                                     
REMARK   3     ATOM PAIRS NUMBER  : 2524                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5VSF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-MAY-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000227939.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-MAR-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 9.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-E                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9792                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : SCALA 3.3.22                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 78227                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.960                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.1                               
REMARK 200  DATA REDUNDANCY                : 6.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.79                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.62800                            
REMARK 200  R SYM FOR SHELL            (I) : 0.62800                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 3HNA                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.49                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.04                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10 % PEG 20K, 1.4% V/V 1,4-DIOXANE,      
REMARK 280  10% GLYCEROL, 0 0.1 M BICINE, PH 9.0, VAPOR DIFFUSION,              
REMARK 280  TEMPERATURE 290K                                                    
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       37.42550            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       51.05050            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       48.04400            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       51.05050            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       37.42550            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       48.04400            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2890 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24080 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ASN B  1179                                                      
REMARK 465     LYS B  1180                                                      
REMARK 465     ASP B  1181                                                      
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   O    HOH B  3221     O    HOH B  3304              2.14            
REMARK 500   O    HOH A  3118     O    HOH A  3141              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    LYS B1086   CD    LYS B1086   CE      0.240                       
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    GLN A1144   CB  -  CA  -  C   ANGL. DEV. = -12.2 DEGREES          
REMARK 500    ARG B1008   CA  -  CB  -  CG  ANGL. DEV. =  17.5 DEGREES          
REMARK 500    ARG B1008   CB  -  CG  -  CD  ANGL. DEV. = -20.1 DEGREES          
REMARK 500    ARG B1008   CG  -  CD  -  NE  ANGL. DEV. = -14.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A1013      103.61   -166.59                                   
REMARK 500    SER A1036       10.28   -141.32                                   
REMARK 500    THR A1047      -86.37   -100.58                                   
REMARK 500    ASP A1066     -148.51   -121.04                                   
REMARK 500    MET A1080      -55.07     82.92                                   
REMARK 500    ASN A1117       45.40    -92.22                                   
REMARK 500    VAL A1119      -61.25   -135.18                                   
REMARK 500    ASP A1135       17.28   -144.85                                   
REMARK 500    ASN A1194     -159.92   -107.62                                   
REMARK 500    MET A1214      -92.65   -131.65                                   
REMARK 500    ASP B1013      105.86   -166.47                                   
REMARK 500    SER B1036       10.45   -140.29                                   
REMARK 500    THR B1047      -85.57   -101.16                                   
REMARK 500    ASP B1066     -150.67   -116.51                                   
REMARK 500    MET B1080      -49.93     79.96                                   
REMARK 500    ASN B1117       46.70    -92.42                                   
REMARK 500    VAL B1119      -61.04   -137.65                                   
REMARK 500    ASP B1135       16.65   -144.13                                   
REMARK 500    ASN B1194     -160.03   -107.35                                   
REMARK 500    MET B1214      -92.30   -132.00                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B3345        DISTANCE =  6.30 ANGSTROMS                       
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 A3004  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1062   SG                                                     
REMARK 620 2 CYS A1064   SG  107.2                                              
REMARK 620 3 CYS A1068   SG  105.6 107.2                                        
REMARK 620 4 CYS A1073   SG  111.9 108.0 116.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A3002  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1062   SG                                                     
REMARK 620 2 CYS A1075   SG  112.9                                              
REMARK 620 3 CYS A1105   SG  107.2 111.7                                        
REMARK 620 4 CYS A1109   SG  107.7  99.7 117.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A3003  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1068   SG                                                     
REMARK 620 2 CYS A1105   SG  111.0                                              
REMARK 620 3 CYS A1111   SG  106.7 109.4                                        
REMARK 620 4 CYS A1115   SG  112.6 103.9 113.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A3005  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1203   SG                                                     
REMARK 620 2 CYS A1256   SG  115.6                                              
REMARK 620 3 CYS A1258   SG  108.9 104.8                                        
REMARK 620 4 CYS A1263   SG  105.4 106.7 115.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B3002  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B1062   SG                                                     
REMARK 620 2 CYS B1075   SG  116.1                                              
REMARK 620 3 CYS B1105   SG  107.7 111.6                                        
REMARK 620 4 CYS B1109   SG  105.5  97.4 118.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B3004  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B1062   SG                                                     
REMARK 620 2 CYS B1064   SG  107.4                                              
REMARK 620 3 CYS B1068   SG  106.0 105.9                                        
REMARK 620 4 CYS B1073   SG  110.4 107.8 118.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B3003  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B1068   SG                                                     
REMARK 620 2 CYS B1105   SG  112.0                                              
REMARK 620 3 CYS B1111   SG  105.5 108.8                                        
REMARK 620 4 CYS B1115   SG  111.7 105.0 114.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B3005  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B1203   SG                                                     
REMARK 620 2 CYS B1256   SG  114.4                                              
REMARK 620 3 CYS B1258   SG  108.9 105.9                                        
REMARK 620 4 CYS B1263   SG  105.7 106.2 116.1                                  
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 SAM A 3001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 3002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 3003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 3004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 3005                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 9HG A 3006                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DIO A 3007                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 3008                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAM B 3001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 3002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 3003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 3004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 3005                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 9HG B 3006                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 3007                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5VSC   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VSD   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VSE   RELATED DB: PDB                                   
DBREF  5VSF A 1006  1266  UNP    Q9H9B1   EHMT1_HUMAN   1006   1266             
DBREF  5VSF B 1006  1266  UNP    Q9H9B1   EHMT1_HUMAN   1006   1266             
SEQRES   1 A  261  VAL GLU ARG ILE VAL SER ARG ASP ILE ALA ARG GLY TYR          
SEQRES   2 A  261  GLU ARG ILE PRO ILE PRO CYS VAL ASN ALA VAL ASP SER          
SEQRES   3 A  261  GLU PRO CYS PRO SER ASN TYR LYS TYR VAL SER GLN ASN          
SEQRES   4 A  261  CYS VAL THR SER PRO MET ASN ILE ASP ARG ASN ILE THR          
SEQRES   5 A  261  HIS LEU GLN TYR CYS VAL CYS ILE ASP ASP CYS SER SER          
SEQRES   6 A  261  SER ASN CYS MET CYS GLY GLN LEU SER MET ARG CYS TRP          
SEQRES   7 A  261  TYR ASP LYS ASP GLY ARG LEU LEU PRO GLU PHE ASN MET          
SEQRES   8 A  261  ALA GLU PRO PRO LEU ILE PHE GLU CYS ASN HIS ALA CYS          
SEQRES   9 A  261  SER CYS TRP ARG ASN CYS ARG ASN ARG VAL VAL GLN ASN          
SEQRES  10 A  261  GLY LEU ARG ALA ARG LEU GLN LEU TYR ARG THR ARG ASP          
SEQRES  11 A  261  MET GLY TRP GLY VAL ARG SER LEU GLN ASP ILE PRO PRO          
SEQRES  12 A  261  GLY THR PHE VAL CYS GLU TYR VAL GLY GLU LEU ILE SER          
SEQRES  13 A  261  ASP SER GLU ALA ASP VAL ARG GLU GLU ASP SER TYR LEU          
SEQRES  14 A  261  PHE ASP LEU ASP ASN LYS ASP GLY GLU VAL TYR CYS ILE          
SEQRES  15 A  261  ASP ALA ARG PHE TYR GLY ASN VAL SER ARG PHE ILE ASN          
SEQRES  16 A  261  HIS HIS CYS GLU PRO ASN LEU VAL PRO VAL ARG VAL PHE          
SEQRES  17 A  261  MET ALA HIS GLN ASP LEU ARG PHE PRO ARG ILE ALA PHE          
SEQRES  18 A  261  PHE SER THR ARG LEU ILE GLU ALA GLY GLU GLN LEU GLY          
SEQRES  19 A  261  PHE ASP TYR GLY GLU ARG PHE TRP ASP ILE LYS GLY LYS          
SEQRES  20 A  261  LEU PHE SER CYS ARG CYS GLY SER PRO LYS CYS ARG HIS          
SEQRES  21 A  261  SER                                                          
SEQRES   1 B  261  VAL GLU ARG ILE VAL SER ARG ASP ILE ALA ARG GLY TYR          
SEQRES   2 B  261  GLU ARG ILE PRO ILE PRO CYS VAL ASN ALA VAL ASP SER          
SEQRES   3 B  261  GLU PRO CYS PRO SER ASN TYR LYS TYR VAL SER GLN ASN          
SEQRES   4 B  261  CYS VAL THR SER PRO MET ASN ILE ASP ARG ASN ILE THR          
SEQRES   5 B  261  HIS LEU GLN TYR CYS VAL CYS ILE ASP ASP CYS SER SER          
SEQRES   6 B  261  SER ASN CYS MET CYS GLY GLN LEU SER MET ARG CYS TRP          
SEQRES   7 B  261  TYR ASP LYS ASP GLY ARG LEU LEU PRO GLU PHE ASN MET          
SEQRES   8 B  261  ALA GLU PRO PRO LEU ILE PHE GLU CYS ASN HIS ALA CYS          
SEQRES   9 B  261  SER CYS TRP ARG ASN CYS ARG ASN ARG VAL VAL GLN ASN          
SEQRES  10 B  261  GLY LEU ARG ALA ARG LEU GLN LEU TYR ARG THR ARG ASP          
SEQRES  11 B  261  MET GLY TRP GLY VAL ARG SER LEU GLN ASP ILE PRO PRO          
SEQRES  12 B  261  GLY THR PHE VAL CYS GLU TYR VAL GLY GLU LEU ILE SER          
SEQRES  13 B  261  ASP SER GLU ALA ASP VAL ARG GLU GLU ASP SER TYR LEU          
SEQRES  14 B  261  PHE ASP LEU ASP ASN LYS ASP GLY GLU VAL TYR CYS ILE          
SEQRES  15 B  261  ASP ALA ARG PHE TYR GLY ASN VAL SER ARG PHE ILE ASN          
SEQRES  16 B  261  HIS HIS CYS GLU PRO ASN LEU VAL PRO VAL ARG VAL PHE          
SEQRES  17 B  261  MET ALA HIS GLN ASP LEU ARG PHE PRO ARG ILE ALA PHE          
SEQRES  18 B  261  PHE SER THR ARG LEU ILE GLU ALA GLY GLU GLN LEU GLY          
SEQRES  19 B  261  PHE ASP TYR GLY GLU ARG PHE TRP ASP ILE LYS GLY LYS          
SEQRES  20 B  261  LEU PHE SER CYS ARG CYS GLY SER PRO LYS CYS ARG HIS          
SEQRES  21 B  261  SER                                                          
HET    SAM  A3001      27                                                       
HET     ZN  A3002       1                                                       
HET     ZN  A3003       1                                                       
HET     ZN  A3004       1                                                       
HET     ZN  A3005       1                                                       
HET    9HG  A3006      29                                                       
HET    DIO  A3007       6                                                       
HET    GOL  A3008       6                                                       
HET    SAM  B3001      27                                                       
HET     ZN  B3002       1                                                       
HET     ZN  B3003       1                                                       
HET     ZN  B3004       1                                                       
HET     ZN  B3005       1                                                       
HET    9HG  B3006      29                                                       
HET    GOL  B3007       6                                                       
HETNAM     SAM S-ADENOSYLMETHIONINE                                             
HETNAM      ZN ZINC ION                                                         
HETNAM     9HG N~2~-CYCLOPENTYL-6,7-DIMETHOXY-N~2~-METHYL-N~4~-(1-              
HETNAM   2 9HG  METHYLPIPERIDIN-4-YL)QUINAZOLINE-2,4-DIAMINE                    
HETNAM     DIO 1,4-DIETHYLENE DIOXIDE                                           
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  SAM    2(C15 H22 N6 O5 S)                                           
FORMUL   4   ZN    8(ZN 2+)                                                     
FORMUL   8  9HG    2(C22 H33 N5 O2)                                             
FORMUL   9  DIO    C4 H8 O2                                                     
FORMUL  10  GOL    2(C3 H8 O3)                                                  
FORMUL  18  HOH   *492(H2 O)                                                    
HELIX    1 AA1 ASN A 1055  LEU A 1059  5                                   5    
HELIX    2 AA2 CYS A 1073  SER A 1079  1                                   7    
HELIX    3 AA3 VAL A 1119  GLY A 1123  5                                   5    
HELIX    4 AA4 ASP A 1162  ASP A 1166  1                                   5    
HELIX    5 AA5 VAL A 1195  ILE A 1199  5                                   5    
HELIX    6 AA6 GLY A 1243  GLY A 1251  1                                   9    
HELIX    7 AA7 ASN B 1055  LEU B 1059  5                                   5    
HELIX    8 AA8 CYS B 1073  SER B 1079  1                                   7    
HELIX    9 AA9 VAL B 1119  GLY B 1123  5                                   5    
HELIX   10 AB1 ASP B 1162  ASP B 1166  1                                   5    
HELIX   11 AB2 VAL B 1195  ILE B 1199  5                                   5    
HELIX   12 AB3 GLY B 1243  GLY B 1251  1                                   9    
SHEET    1 AA1 4 ARG A1008  SER A1011  0                                        
SHEET    2 AA1 4 CYS A1025  ASN A1027 -1  O  CYS A1025   N  SER A1011           
SHEET    3 AA1 4 LEU A1128  ARG A1132  1  O  LEU A1130   N  VAL A1026           
SHEET    4 AA1 4 TRP A1138  SER A1142 -1  O  GLY A1139   N  TYR A1131           
SHEET    1 AA2 3 LYS A1039  TYR A1040  0                                        
SHEET    2 AA2 3 TYR A1185  GLY A1193  1  O  PHE A1191   N  LYS A1039           
SHEET    3 AA2 3 GLY A1157  SER A1161 -1  N  GLU A1158   O  ASP A1188           
SHEET    1 AA3 3 LYS A1039  TYR A1040  0                                        
SHEET    2 AA3 3 TYR A1185  GLY A1193  1  O  PHE A1191   N  LYS A1039           
SHEET    3 AA3 3 LEU A1174  ASP A1176 -1  N  PHE A1175   O  ILE A1187           
SHEET    1 AA4 4 ILE A1102  PHE A1103  0                                        
SHEET    2 AA4 4 LEU A1207  PHE A1213  1  O  PHE A1213   N  ILE A1102           
SHEET    3 AA4 4 ARG A1223  SER A1228 -1  O  ALA A1225   N  VAL A1210           
SHEET    4 AA4 4 PHE A1151  TYR A1155 -1  N  CYS A1153   O  PHE A1226           
SHEET    1 AA5 2 ASN A1200  HIS A1201  0                                        
SHEET    2 AA5 2 GLY A1239  PHE A1240  1  O  PHE A1240   N  ASN A1200           
SHEET    1 AA6 4 ARG B1008  SER B1011  0                                        
SHEET    2 AA6 4 CYS B1025  ASN B1027 -1  O  CYS B1025   N  SER B1011           
SHEET    3 AA6 4 LEU B1128  ARG B1132  1  O  LEU B1130   N  VAL B1026           
SHEET    4 AA6 4 TRP B1138  SER B1142 -1  O  GLY B1139   N  TYR B1131           
SHEET    1 AA7 3 LYS B1039  TYR B1040  0                                        
SHEET    2 AA7 3 TYR B1185  GLY B1193  1  O  PHE B1191   N  LYS B1039           
SHEET    3 AA7 3 GLY B1157  SER B1161 -1  N  GLU B1158   O  ASP B1188           
SHEET    1 AA8 3 LYS B1039  TYR B1040  0                                        
SHEET    2 AA8 3 TYR B1185  GLY B1193  1  O  PHE B1191   N  LYS B1039           
SHEET    3 AA8 3 LEU B1174  LEU B1177 -1  N  PHE B1175   O  ILE B1187           
SHEET    1 AA9 4 ILE B1102  PHE B1103  0                                        
SHEET    2 AA9 4 LEU B1207  PHE B1213  1  O  PHE B1213   N  ILE B1102           
SHEET    3 AA9 4 ARG B1223  SER B1228 -1  O  ALA B1225   N  VAL B1210           
SHEET    4 AA9 4 PHE B1151  TYR B1155 -1  N  VAL B1152   O  PHE B1226           
SHEET    1 AB1 2 ASN B1200  HIS B1201  0                                        
SHEET    2 AB1 2 GLY B1239  PHE B1240  1  O  PHE B1240   N  ASN B1200           
LINK         SG  CYS A1062                ZN    ZN A3004     1555   1555  2.37  
LINK         SG  CYS A1062                ZN    ZN A3002     1555   1555  2.37  
LINK         SG  CYS A1064                ZN    ZN A3004     1555   1555  2.32  
LINK         SG  CYS A1068                ZN    ZN A3003     1555   1555  2.34  
LINK         SG  CYS A1068                ZN    ZN A3004     1555   1555  2.33  
LINK         SG  CYS A1073                ZN    ZN A3004     1555   1555  2.34  
LINK         SG  CYS A1075                ZN    ZN A3002     1555   1555  2.33  
LINK         SG  CYS A1105                ZN    ZN A3003     1555   1555  2.37  
LINK         SG  CYS A1105                ZN    ZN A3002     1555   1555  2.41  
LINK         SG  CYS A1109                ZN    ZN A3002     1555   1555  2.30  
LINK         SG  CYS A1111                ZN    ZN A3003     1555   1555  2.32  
LINK         SG  CYS A1115                ZN    ZN A3003     1555   1555  2.33  
LINK         SG  CYS A1203                ZN    ZN A3005     1555   1555  2.36  
LINK         SG  CYS A1256                ZN    ZN A3005     1555   1555  2.34  
LINK         SG  CYS A1258                ZN    ZN A3005     1555   1555  2.33  
LINK         SG  CYS A1263                ZN    ZN A3005     1555   1555  2.30  
LINK         SG  CYS B1062                ZN    ZN B3002     1555   1555  2.38  
LINK         SG  CYS B1062                ZN    ZN B3004     1555   1555  2.36  
LINK         SG  CYS B1064                ZN    ZN B3004     1555   1555  2.33  
LINK         SG  CYS B1068                ZN    ZN B3003     1555   1555  2.35  
LINK         SG  CYS B1068                ZN    ZN B3004     1555   1555  2.36  
LINK         SG  CYS B1073                ZN    ZN B3004     1555   1555  2.31  
LINK         SG  CYS B1075                ZN    ZN B3002     1555   1555  2.36  
LINK         SG  CYS B1105                ZN    ZN B3002     1555   1555  2.39  
LINK         SG  CYS B1105                ZN    ZN B3003     1555   1555  2.34  
LINK         SG  CYS B1109                ZN    ZN B3002     1555   1555  2.34  
LINK         SG  CYS B1111                ZN    ZN B3003     1555   1555  2.32  
LINK         SG  CYS B1115                ZN    ZN B3003     1555   1555  2.32  
LINK         SG  CYS B1203                ZN    ZN B3005     1555   1555  2.40  
LINK         SG  CYS B1256                ZN    ZN B3005     1555   1555  2.33  
LINK         SG  CYS B1258                ZN    ZN B3005     1555   1555  2.34  
LINK         SG  CYS B1263                ZN    ZN B3005     1555   1555  2.31  
SITE     1 AC1 19 MET A1136  TRP A1138  SER A1172  TYR A1173                    
SITE     2 AC1 19 ARG A1197  PHE A1198  ASN A1200  HIS A1201                    
SITE     3 AC1 19 TYR A1242  PHE A1246  PHE A1254  CYS A1256                    
SITE     4 AC1 19 ARG A1257  HOH A3107  HOH A3119  HOH A3199                    
SITE     5 AC1 19 HOH A3206  HOH A3215  HOH A3271                               
SITE     1 AC2  4 CYS A1062  CYS A1075  CYS A1105  CYS A1109                    
SITE     1 AC3  4 CYS A1068  CYS A1105  CYS A1111  CYS A1115                    
SITE     1 AC4  4 CYS A1062  CYS A1064  CYS A1068  CYS A1073                    
SITE     1 AC5  4 CYS A1203  CYS A1256  CYS A1258  CYS A1263                    
SITE     1 AC6 12 ASP A1162  ALA A1165  ASP A1166  ARG A1168                    
SITE     2 AC6 12 ASP A1171  LEU A1174  ASP A1176  CYS A1186                    
SITE     3 AC6 12 ARG A1245  PHE A1246  ILE A1249  LYS A1250                    
SITE     1 AC7  8 CYS A1064  ILE A1065  ASP A1066  SER A1070                    
SITE     2 AC7  8 ASN A1072  LEU B1078  LEU B1101  PHE B1103                    
SITE     1 AC8  5 ARG A1054  HOH A3118  HOH A3141  HOH A3282                    
SITE     2 AC8  5 ARG B1054                                                     
SITE     1 AC9 18 MET B1136  TRP B1138  SER B1172  TYR B1173                    
SITE     2 AC9 18 ARG B1197  PHE B1198  ASN B1200  HIS B1201                    
SITE     3 AC9 18 TYR B1242  PHE B1246  CYS B1256  ARG B1257                    
SITE     4 AC9 18 HOH B3117  HOH B3122  HOH B3156  HOH B3162                    
SITE     5 AC9 18 HOH B3182  HOH B3258                                          
SITE     1 AD1  4 CYS B1062  CYS B1075  CYS B1105  CYS B1109                    
SITE     1 AD2  4 CYS B1068  CYS B1105  CYS B1111  CYS B1115                    
SITE     1 AD3  4 CYS B1062  CYS B1064  CYS B1068  CYS B1073                    
SITE     1 AD4  4 CYS B1203  CYS B1256  CYS B1258  CYS B1263                    
SITE     1 AD5 13 ASP B1162  ALA B1165  ASP B1166  ARG B1168                    
SITE     2 AD5 13 ASP B1171  LEU B1174  ASP B1176  VAL B1184                    
SITE     3 AD5 13 ARG B1245  PHE B1246  ILE B1249  LYS B1250                    
SITE     4 AD5 13 HOH B3204                                                     
SITE     1 AD6  5 ARG A1054  ILE B1052  ARG B1054  HOH B3269                    
SITE     2 AD6  5 HOH B3271                                                     
CRYST1   74.851   96.088  102.101  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013360  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010407  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009794        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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