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Database: PDB
Entry: 5VSC
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HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       11-MAY-17   5VSC              
TITLE     STRUCTURE OF HUMAN G9A SET-DOMAIN (EHMT2) IN COMPLEX WITH INHIBITOR 13
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE EHMT2;                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: G9A CATALYTIC SET-DOMAIN RESIDUES 916-1190;                
COMPND   5 SYNONYM: EUCHROMATIC HISTONE-LYSINE N-METHYLTRANSFERASE 2,HLA-B-     
COMPND   6 ASSOCIATED TRANSCRIPT 8,HISTONE H3-K9 METHYLTRANSFERASE 3,H3-K9-     
COMPND   7 HMTASE 3,LYSINE N-METHYLTRANSFERASE 1C,PROTEIN G9A;                  
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: EHMT2, BAT8, C6ORF30, G9A, KMT1C, NG36;                        
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 5VSC    1       JRNL                                     
REVDAT   1   12-JUL-17 5VSC    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.    1.40 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) : 1.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.05                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 119498                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.166                           
REMARK   3   R VALUE            (WORKING SET) : 0.165                           
REMARK   3   FREE R VALUE                     : 0.182                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.980                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5954                            
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 39.0631 -  4.3482    0.94     3790   230  0.1441 0.1420        
REMARK   3     2  4.3482 -  3.4520    0.99     4003   179  0.1435 0.1423        
REMARK   3     3  3.4520 -  3.0158    1.00     3997   191  0.1660 0.2090        
REMARK   3     4  3.0158 -  2.7401    1.00     3990   183  0.1695 0.1952        
REMARK   3     5  2.7401 -  2.5438    0.99     3922   194  0.1727 0.1815        
REMARK   3     6  2.5438 -  2.3938    0.93     3743   196  0.1737 0.2021        
REMARK   3     7  2.3938 -  2.2739    0.99     3850   234  0.1753 0.2027        
REMARK   3     8  2.2739 -  2.1750    0.99     3924   185  0.1702 0.1934        
REMARK   3     9  2.1750 -  2.0912    0.98     3904   198  0.1723 0.1814        
REMARK   3    10  2.0912 -  2.0191    0.99     3870   219  0.1694 0.1804        
REMARK   3    11  2.0191 -  1.9560    0.99     3939   195  0.1685 0.1934        
REMARK   3    12  1.9560 -  1.9000    0.98     3913   194  0.1691 0.2055        
REMARK   3    13  1.9000 -  1.8500    0.99     3916   196  0.1682 0.1999        
REMARK   3    14  1.8500 -  1.8049    0.98     3877   218  0.1676 0.1907        
REMARK   3    15  1.8049 -  1.7639    0.94     3664   207  0.1611 0.1967        
REMARK   3    16  1.7639 -  1.7263    0.97     3853   228  0.1642 0.1858        
REMARK   3    17  1.7263 -  1.6918    0.98     3829   216  0.1641 0.1761        
REMARK   3    18  1.6918 -  1.6599    0.98     3841   206  0.1689 0.1652        
REMARK   3    19  1.6599 -  1.6302    0.98     3880   221  0.1695 0.1829        
REMARK   3    20  1.6302 -  1.6026    0.98     3851   204  0.1694 0.2007        
REMARK   3    21  1.6026 -  1.5767    0.98     3809   233  0.1715 0.1787        
REMARK   3    22  1.5767 -  1.5525    0.98     3867   191  0.1698 0.1942        
REMARK   3    23  1.5525 -  1.5296    0.97     3809   199  0.1738 0.2003        
REMARK   3    24  1.5296 -  1.5081    0.97     3850   196  0.1836 0.2166        
REMARK   3    25  1.5081 -  1.4877    0.96     3778   192  0.1961 0.2234        
REMARK   3    26  1.4877 -  1.4684    0.95     3768   184  0.1995 0.2110        
REMARK   3    27  1.4684 -  1.4500    0.94     3673   195  0.2115 0.2277        
REMARK   3    28  1.4500 -  1.4326    0.89     3515   182  0.2243 0.2528        
REMARK   3    29  1.4326 -  1.4159    0.78     3110   142  0.2403 0.2677        
REMARK   3    30  1.4159 -  1.4000    0.71     2809   146  0.2644 0.2812        
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)     : 0.130            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.610           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 17.95                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.87                          
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      :  0.006           4563                                  
REMARK   3   ANGLE     :  1.056           6172                                  
REMARK   3   CHIRALITY :  0.091            655                                  
REMARK   3   PLANARITY :  0.005            800                                  
REMARK   3   DIHEDRAL  : 16.080           1712                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 19                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1002 THROUGH 1021 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  14.7175   3.3613 -12.9060              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2041 T22:   0.2352                                     
REMARK   3      T33:   0.1551 T12:   0.0010                                     
REMARK   3      T13:  -0.0463 T23:   0.0274                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.4076 L22:   2.8503                                     
REMARK   3      L33:   7.2945 L12:  -0.9930                                     
REMARK   3      L13:  -2.7004 L23:   1.4801                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1246 S12:   0.6845 S13:   0.1397                       
REMARK   3      S21:  -0.4315 S22:  -0.0776 S23:   0.0732                       
REMARK   3      S31:   0.0417 S32:  -0.2449 S33:  -0.0381                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1022 THROUGH 1079 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  28.1640  -1.7654  -6.8746              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1697 T22:   0.1112                                     
REMARK   3      T33:   0.1391 T12:  -0.0233                                     
REMARK   3      T13:  -0.0145 T23:  -0.0077                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3902 L22:   0.8187                                     
REMARK   3      L33:   0.9362 L12:  -0.3802                                     
REMARK   3      L13:  -0.4682 L23:   0.2165                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0445 S12:   0.0953 S13:  -0.0391                       
REMARK   3      S21:  -0.0509 S22:  -0.0222 S23:  -0.0035                       
REMARK   3      S31:  -0.0140 S32:  -0.0628 S33:   0.0076                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1080 THROUGH 1096 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  35.0411  14.3639  -8.2619              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2851 T22:   0.1385                                     
REMARK   3      T33:   0.2106 T12:  -0.0153                                     
REMARK   3      T13:   0.0546 T23:   0.0308                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7172 L22:   6.1770                                     
REMARK   3      L33:   4.8152 L12:  -0.0420                                     
REMARK   3      L13:  -1.7963 L23:   1.8872                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1494 S12:   0.1412 S13:   0.3390                       
REMARK   3      S21:  -0.2279 S22:   0.0575 S23:  -0.2422                       
REMARK   3      S31:  -0.6163 S32:  -0.0303 S33:  -0.1930                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1097 THROUGH 1140 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  28.4380   5.9228  -8.1206              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1775 T22:   0.1003                                     
REMARK   3      T33:   0.1437 T12:  -0.0239                                     
REMARK   3      T13:  -0.0002 T23:   0.0167                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7589 L22:   0.9981                                     
REMARK   3      L33:   0.7729 L12:  -0.6341                                     
REMARK   3      L13:  -0.4824 L23:   0.2639                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0378 S12:   0.1192 S13:   0.1713                       
REMARK   3      S21:  -0.0812 S22:   0.0237 S23:  -0.0567                       
REMARK   3      S31:  -0.1143 S32:  -0.0566 S33:  -0.0656                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1141 THROUGH 1155 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  31.9511  -4.9513 -17.9816              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2498 T22:   0.1878                                     
REMARK   3      T33:   0.1408 T12:  -0.0111                                     
REMARK   3      T13:   0.0081 T23:  -0.0298                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3819 L22:   2.1610                                     
REMARK   3      L33:   1.2421 L12:  -0.5349                                     
REMARK   3      L13:  -0.0334 L23:  -1.2196                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0770 S12:   0.3953 S13:  -0.2339                       
REMARK   3      S21:  -0.5314 S22:  -0.0244 S23:  -0.0105                       
REMARK   3      S31:   0.1450 S32:  -0.0675 S33:  -0.0248                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1156 THROUGH 1190 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  42.8479   8.3722 -25.8837              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3366 T22:   0.3398                                     
REMARK   3      T33:   0.2688 T12:  -0.0005                                     
REMARK   3      T13:   0.1033 T23:   0.0586                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4364 L22:   2.4407                                     
REMARK   3      L33:   5.6377 L12:   0.5069                                     
REMARK   3      L13:  -1.7940 L23:  -1.3019                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1933 S12:   0.7474 S13:   0.3044                       
REMARK   3      S21:  -0.5786 S22:   0.0796 S23:  -0.1620                       
REMARK   3      S31:  -0.2035 S32:  -0.1060 S33:  -0.2185                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 918 THROUGH 935 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   3.6622  -8.7809  12.1033              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2224 T22:   0.2627                                     
REMARK   3      T33:   0.3406 T12:  -0.0389                                     
REMARK   3      T13:  -0.0270 T23:   0.0080                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3327 L22:   3.7061                                     
REMARK   3      L33:   6.2517 L12:   2.2335                                     
REMARK   3      L13:  -4.1505 L23:  -1.5308                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2163 S12:   0.3024 S13:  -0.4845                       
REMARK   3      S21:  -0.2031 S22:   0.1433 S23:   0.4311                       
REMARK   3      S31:   0.4581 S32:  -0.7592 S33:   0.1381                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 936 THROUGH 954 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.9120  -2.5765  15.5933              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1424 T22:   0.2384                                     
REMARK   3      T33:   0.2318 T12:  -0.0004                                     
REMARK   3      T13:  -0.0065 T23:   0.0499                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.5942 L22:   3.5430                                     
REMARK   3      L33:   3.5906 L12:   3.5522                                     
REMARK   3      L13:  -4.5191 L23:  -2.4482                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1301 S12:   0.3247 S13:  -0.1112                       
REMARK   3      S21:   0.0251 S22:   0.2883 S23:   0.4487                       
REMARK   3      S31:   0.0117 S32:  -0.4416 S33:  -0.1882                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 955 THROUGH 1001 )                
REMARK   3    ORIGIN FOR THE GROUP (A):  30.2794   2.9563  18.9847              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2072 T22:   0.2445                                     
REMARK   3      T33:   0.1755 T12:   0.0103                                     
REMARK   3      T13:  -0.0070 T23:   0.0295                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6969 L22:   1.1005                                     
REMARK   3      L33:   0.3624 L12:  -0.1384                                     
REMARK   3      L13:  -0.6358 L23:   0.0717                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1613 S12:  -0.4814 S13:  -0.1770                       
REMARK   3      S21:   0.2480 S22:   0.1176 S23:  -0.0904                       
REMARK   3      S31:  -0.0440 S32:   0.1650 S33:   0.0392                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1002 THROUGH 1021 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  27.1475   0.1962  27.1126              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2594 T22:   0.4136                                     
REMARK   3      T33:   0.1505 T12:   0.0291                                     
REMARK   3      T13:  -0.0027 T23:   0.0493                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0998 L22:   3.0363                                     
REMARK   3      L33:   4.6903 L12:   0.4569                                     
REMARK   3      L13:  -1.5198 L23:  -0.7500                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0072 S12:  -0.8577 S13:   0.1153                       
REMARK   3      S21:   0.6363 S22:   0.0776 S23:   0.0549                       
REMARK   3      S31:  -0.0399 S32:   0.1341 S33:   0.0222                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1022 THROUGH 1079 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  13.5349  -2.4980  20.6817              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1665 T22:   0.1632                                     
REMARK   3      T33:   0.1887 T12:   0.0100                                     
REMARK   3      T13:   0.0090 T23:   0.0633                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2644 L22:   0.6733                                     
REMARK   3      L33:   0.9583 L12:   0.0836                                     
REMARK   3      L13:  -0.2629 L23:  -0.2218                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0059 S12:  -0.1750 S13:  -0.2795                       
REMARK   3      S21:   0.0643 S22:   0.0349 S23:   0.1163                       
REMARK   3      S31:  -0.0146 S32:  -0.0021 S33:  -0.0129                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1080 THROUGH 1110 )               
REMARK   3    ORIGIN FOR THE GROUP (A):   7.6394  10.4785  21.0432              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1791 T22:   0.1583                                     
REMARK   3      T33:   0.1765 T12:   0.0482                                     
REMARK   3      T13:   0.0483 T23:   0.0520                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4004 L22:   5.2312                                     
REMARK   3      L33:   5.0082 L12:  -0.3305                                     
REMARK   3      L13:  -0.3594 L23:   0.0055                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0355 S12:  -0.1648 S13:   0.4248                       
REMARK   3      S21:   0.2676 S22:   0.1790 S23:   0.1763                       
REMARK   3      S31:  -0.5509 S32:  -0.2111 S33:  -0.1052                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1111 THROUGH 1140 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  17.5413   3.6347  25.0516              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1702 T22:   0.2054                                     
REMARK   3      T33:   0.1380 T12:   0.0188                                     
REMARK   3      T13:  -0.0023 T23:   0.0432                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4830 L22:   1.6304                                     
REMARK   3      L33:   1.4444 L12:   1.6802                                     
REMARK   3      L13:  -1.9464 L23:  -1.3324                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0202 S12:  -0.3703 S13:  -0.1073                       
REMARK   3      S21:   0.2091 S22:  -0.0377 S23:  -0.0204                       
REMARK   3      S31:  -0.0846 S32:   0.0815 S33:   0.0245                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1141 THROUGH 1162 )               
REMARK   3    ORIGIN FOR THE GROUP (A):   7.4026  -0.0425  32.4087              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1993 T22:   0.3430                                     
REMARK   3      T33:   0.1831 T12:   0.0236                                     
REMARK   3      T13:   0.0572 T23:   0.1103                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5094 L22:   4.2779                                     
REMARK   3      L33:   2.7005 L12:  -1.3354                                     
REMARK   3      L13:  -0.6275 L23:   0.4945                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1018 S12:  -0.6040 S13:  -0.2592                       
REMARK   3      S21:   0.4569 S22:   0.1583 S23:   0.1667                       
REMARK   3      S31:   0.0038 S32:   0.0177 S33:  -0.0462                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1163 THROUGH 1190 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.0894   5.8513  42.9845              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3599 T22:   0.5202                                     
REMARK   3      T33:   0.2880 T12:   0.0167                                     
REMARK   3      T13:   0.1035 T23:   0.0735                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9609 L22:   3.2929                                     
REMARK   3      L33:   7.2683 L12:  -0.8592                                     
REMARK   3      L13:  -2.0903 L23:   2.1162                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1736 S12:  -0.5015 S13:   0.2068                       
REMARK   3      S21:   0.3857 S22:  -0.0857 S23:  -0.0790                       
REMARK   3      S31:  -0.1576 S32:   0.3392 S33:  -0.1429                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 916 THROUGH 936 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  39.2164 -10.9631  -0.6417              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1959 T22:   0.1147                                     
REMARK   3      T33:   0.2147 T12:  -0.0098                                     
REMARK   3      T13:  -0.0080 T23:   0.0055                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.6568 L22:   2.2198                                     
REMARK   3      L33:   4.8806 L12:  -2.1108                                     
REMARK   3      L13:  -4.4660 L23:   1.3922                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1865 S12:  -0.2360 S13:  -0.3557                       
REMARK   3      S21:   0.0688 S22:   0.0880 S23:  -0.1998                       
REMARK   3      S31:   0.2375 S32:   0.3389 S33:   0.1296                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 937 THROUGH 954 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  43.7676  -4.0034  -1.7763              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1833 T22:   0.1615                                     
REMARK   3      T33:   0.2177 T12:  -0.0154                                     
REMARK   3      T13:  -0.0286 T23:  -0.0247                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.8675 L22:   8.0494                                     
REMARK   3      L33:   3.6024 L12:  -6.8985                                     
REMARK   3      L13:  -4.5878 L23:   5.2535                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1770 S12:  -0.3865 S13:   0.3464                       
REMARK   3      S21:   0.1282 S22:   0.4678 S23:  -0.6327                       
REMARK   3      S31:   0.0156 S32:   0.4530 S33:  -0.3589                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 955 THROUGH 970 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  21.6294  14.3001   4.1303              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2220 T22:   0.1536                                     
REMARK   3      T33:   0.2039 T12:  -0.0027                                     
REMARK   3      T13:  -0.0020 T23:   0.0321                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.5607 L22:   0.9820                                     
REMARK   3      L33:   0.1536 L12:  -2.6529                                     
REMARK   3      L13:  -0.9664 L23:   0.3024                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0011 S12:   0.0972 S13:   0.2654                       
REMARK   3      S21:  -0.0004 S22:   0.0250 S23:  -0.0382                       
REMARK   3      S31:  -0.0291 S32:  -0.0072 S33:  -0.0167                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 971 THROUGH 1001 )                
REMARK   3    ORIGIN FOR THE GROUP (A):   6.8642   0.7817  -9.0129              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2011 T22:   0.2790                                     
REMARK   3      T33:   0.2025 T12:  -0.0403                                     
REMARK   3      T13:  -0.0487 T23:  -0.0187                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2666 L22:   2.8737                                     
REMARK   3      L33:   3.6157 L12:  -1.3845                                     
REMARK   3      L13:  -1.6672 L23:   2.5328                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0621 S12:   0.5226 S13:  -0.3196                       
REMARK   3      S21:  -0.2311 S22:  -0.2651 S23:   0.3237                       
REMARK   3      S31:   0.1099 S32:  -0.6017 S33:   0.1965                       
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                                     
REMARK   3     SELECTION          : (CHAIN B AND (RESID 918 THROUGH 1090 OR     
REMARK   3                          RESID 1095 THROUGH 1190))                   
REMARK   3     ATOM PAIRS NUMBER  : 2616                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5VSC 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_1000227936.                                   
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                             : 7.5                                
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   : 119728                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 73.050                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.9                               
REMARK 200  DATA REDUNDANCY                : 6.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.48                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 84.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.40800                            
REMARK 200  R SYM FOR SHELL            (I) : 0.40800                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.800                              
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: 3K5K                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.72                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20 % PEG3350, 10% GLYCEROL, 0.2 M        
REMARK 280  SODIUM BROMIDE, PH 7.5, VAPOR DIFFUSION, TEMPERATURE 290K           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       39.21500            
REMARK 290   SMTRY3   2  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: 2240 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25660 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 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     ILE A   916                                                      
REMARK 465     ARG A   917                                                      
REMARK 465     ASN A  1091                                                      
REMARK 465     LYS A  1092                                                      
REMARK 465     ASP A  1093                                                      
REMARK 465     GLY A  1094                                                      
REMARK 465     ASN B  1091                                                      
REMARK 465     LYS B  1092                                                      
REMARK 465     ASP B  1093                                                      
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  1672     O    HOH B  1818              2.10            
REMARK 500   OE1  GLU B   958     O    HOH B  1601              2.16            
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    LYS B 998   CB  -  CA  -  C   ANGL. DEV. = -13.3 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 A 949       35.74    -88.54                                   
REMARK 500    ASP A 978     -151.73   -103.51                                   
REMARK 500    ILE A 992      -58.05     74.69                                   
REMARK 500    ARG A1030       36.89   -145.10                                   
REMARK 500    ILE A1064      -62.51   -103.55                                   
REMARK 500    ASN A1106     -161.83   -108.48                                   
REMARK 500    ASP A1116       75.25   -116.94                                   
REMARK 500    MET A1126      -92.88   -128.82                                   
REMARK 500    ASP B 925      105.50   -162.54                                   
REMARK 500    ASP B 949       34.57    -88.43                                   
REMARK 500    ASP B 978     -151.33   -108.62                                   
REMARK 500    ILE B 992      -57.68     72.84                                   
REMARK 500    ASN B1029       50.71   -114.45                                   
REMARK 500    ARG B1030       37.23   -145.14                                   
REMARK 500    ILE B1064      -63.20   -103.64                                   
REMARK 500    ASN B1106     -162.10   -107.71                                   
REMARK 500    ASP B1116       76.83   -117.16                                   
REMARK 500    MET B1126      -92.42   -129.36                                   
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 A1503  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 974   SG                                                     
REMARK 620 2 CYS A 976   SG  108.2                                              
REMARK 620 3 CYS A 980   SG  104.3 105.1                                        
REMARK 620 4 CYS A 985   SG  110.3 110.2 118.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1502  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 974   SG                                                     
REMARK 620 2 CYS A 987   SG  114.1                                              
REMARK 620 3 CYS A1017   SG  109.6 110.1                                        
REMARK 620 4 CYS A1021   SG  106.7  98.6 117.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 980   SG                                                     
REMARK 620 2 CYS A1017   SG  111.1                                              
REMARK 620 3 CYS A1023   SG  104.6 107.5                                        
REMARK 620 4 CYS A1027   SG  112.6 106.6 114.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1504  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1115   SG                                                     
REMARK 620 2 CYS A1168   SG  112.6                                              
REMARK 620 3 CYS A1170   SG  111.0 107.3                                        
REMARK 620 4 CYS A1175   SG  105.9 107.6 112.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1503  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 974   SG                                                     
REMARK 620 2 CYS B 976   SG  109.0                                              
REMARK 620 3 CYS B 980   SG  105.3 105.4                                        
REMARK 620 4 CYS B 985   SG  111.0 109.0 116.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1502  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 974   SG                                                     
REMARK 620 2 CYS B 987   SG  113.6                                              
REMARK 620 3 CYS B1017   SG  108.6 113.0                                        
REMARK 620 4 CYS B1021   SG  104.9  97.9 118.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 980   SG                                                     
REMARK 620 2 CYS B1017   SG  110.4                                              
REMARK 620 3 CYS B1023   SG  105.3 108.2                                        
REMARK 620 4 CYS B1027   SG  113.2 105.9 113.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1504  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B1115   SG                                                     
REMARK 620 2 CYS B1168   SG  113.1                                              
REMARK 620 3 CYS B1170   SG  110.3 106.4                                        
REMARK 620 4 CYS B1175   SG  105.0 109.6 112.6                                  
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 1501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAM A 1505                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 9HJ A 1506                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAM B 1505                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 9HJ B 1506                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5VSF   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VSD   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VSE   RELATED DB: PDB                                   
DBREF  5VSC A  916  1190  UNP    Q96KQ7   EHMT2_HUMAN    916   1190             
DBREF  5VSC B  916  1190  UNP    Q96KQ7   EHMT2_HUMAN    916   1190             
SEQRES   1 A  275  ILE ARG THR GLU LYS ILE ILE CYS ARG ASP VAL ALA ARG          
SEQRES   2 A  275  GLY TYR GLU ASN VAL PRO ILE PRO CYS VAL ASN GLY VAL          
SEQRES   3 A  275  ASP GLY GLU PRO CYS PRO GLU ASP TYR LYS TYR ILE SER          
SEQRES   4 A  275  GLU ASN CYS GLU THR SER THR MET ASN ILE ASP ARG ASN          
SEQRES   5 A  275  ILE THR HIS LEU GLN HIS CYS THR CYS VAL ASP ASP CYS          
SEQRES   6 A  275  SER SER SER ASN CYS LEU CYS GLY GLN LEU SER ILE ARG          
SEQRES   7 A  275  CYS TRP TYR ASP LYS ASP GLY ARG LEU LEU GLN GLU PHE          
SEQRES   8 A  275  ASN LYS ILE GLU PRO PRO LEU ILE PHE GLU CYS ASN GLN          
SEQRES   9 A  275  ALA CYS SER CYS TRP ARG ASN CYS LYS ASN ARG VAL VAL          
SEQRES  10 A  275  GLN SER GLY ILE LYS VAL ARG LEU GLN LEU TYR ARG THR          
SEQRES  11 A  275  ALA LYS MET GLY TRP GLY VAL ARG ALA LEU GLN THR ILE          
SEQRES  12 A  275  PRO GLN GLY THR PHE ILE CYS GLU TYR VAL GLY GLU LEU          
SEQRES  13 A  275  ILE SER ASP ALA GLU ALA ASP VAL ARG GLU ASP ASP SER          
SEQRES  14 A  275  TYR LEU PHE ASP LEU ASP ASN LYS ASP GLY GLU VAL TYR          
SEQRES  15 A  275  CYS ILE ASP ALA ARG TYR TYR GLY ASN ILE SER ARG PHE          
SEQRES  16 A  275  ILE ASN HIS LEU CYS ASP PRO ASN ILE ILE PRO VAL ARG          
SEQRES  17 A  275  VAL PHE MET LEU HIS GLN ASP LEU ARG PHE PRO ARG ILE          
SEQRES  18 A  275  ALA PHE PHE SER SER ARG ASP ILE ARG THR GLY GLU GLU          
SEQRES  19 A  275  LEU GLY PHE ASP TYR GLY ASP ARG PHE TRP ASP ILE LYS          
SEQRES  20 A  275  SER LYS TYR PHE THR CYS GLN CYS GLY SER GLU LYS CYS          
SEQRES  21 A  275  LYS HIS SER ALA GLU ALA ILE ALA LEU GLU GLN SER ARG          
SEQRES  22 A  275  LEU ALA                                                      
SEQRES   1 B  275  ILE ARG THR GLU LYS ILE ILE CYS ARG ASP VAL ALA ARG          
SEQRES   2 B  275  GLY TYR GLU ASN VAL PRO ILE PRO CYS VAL ASN GLY VAL          
SEQRES   3 B  275  ASP GLY GLU PRO CYS PRO GLU ASP TYR LYS TYR ILE SER          
SEQRES   4 B  275  GLU ASN CYS GLU THR SER THR MET ASN ILE ASP ARG ASN          
SEQRES   5 B  275  ILE THR HIS LEU GLN HIS CYS THR CYS VAL ASP ASP CYS          
SEQRES   6 B  275  SER SER SER ASN CYS LEU CYS GLY GLN LEU SER ILE ARG          
SEQRES   7 B  275  CYS TRP TYR ASP LYS ASP GLY ARG LEU LEU GLN GLU PHE          
SEQRES   8 B  275  ASN LYS ILE GLU PRO PRO LEU ILE PHE GLU CYS ASN GLN          
SEQRES   9 B  275  ALA CYS SER CYS TRP ARG ASN CYS LYS ASN ARG VAL VAL          
SEQRES  10 B  275  GLN SER GLY ILE LYS VAL ARG LEU GLN LEU TYR ARG THR          
SEQRES  11 B  275  ALA LYS MET GLY TRP GLY VAL ARG ALA LEU GLN THR ILE          
SEQRES  12 B  275  PRO GLN GLY THR PHE ILE CYS GLU TYR VAL GLY GLU LEU          
SEQRES  13 B  275  ILE SER ASP ALA GLU ALA ASP VAL ARG GLU ASP ASP SER          
SEQRES  14 B  275  TYR LEU PHE ASP LEU ASP ASN LYS ASP GLY GLU VAL TYR          
SEQRES  15 B  275  CYS ILE ASP ALA ARG TYR TYR GLY ASN ILE SER ARG PHE          
SEQRES  16 B  275  ILE ASN HIS LEU CYS ASP PRO ASN ILE ILE PRO VAL ARG          
SEQRES  17 B  275  VAL PHE MET LEU HIS GLN ASP LEU ARG PHE PRO ARG ILE          
SEQRES  18 B  275  ALA PHE PHE SER SER ARG ASP ILE ARG THR GLY GLU GLU          
SEQRES  19 B  275  LEU GLY PHE ASP TYR GLY ASP ARG PHE TRP ASP ILE LYS          
SEQRES  20 B  275  SER LYS TYR PHE THR CYS GLN CYS GLY SER GLU LYS CYS          
SEQRES  21 B  275  LYS HIS SER ALA GLU ALA ILE ALA LEU GLU GLN SER ARG          
SEQRES  22 B  275  LEU ALA                                                      
HET     ZN  A1501       1                                                       
HET     ZN  A1502       1                                                       
HET     ZN  A1503       1                                                       
HET     ZN  A1504       1                                                       
HET    SAM  A1505      27                                                       
HET    9HJ  A1506      27                                                       
HET     ZN  B1501       1                                                       
HET     ZN  B1502       1                                                       
HET     ZN  B1503       1                                                       
HET     ZN  B1504       1                                                       
HET    SAM  B1505      27                                                       
HET    9HJ  B1506      27                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     SAM S-ADENOSYLMETHIONINE                                             
HETNAM     9HJ 6,7-DIMETHOXY-N~2~-METHYL-N~4~-(1-METHYLPIPERIDIN-4-             
HETNAM   2 9HJ  YL)-N~2~-PROPYLQUINAZOLINE-2,4-DIAMINE                          
FORMUL   3   ZN    8(ZN 2+)                                                     
FORMUL   7  SAM    2(C15 H22 N6 O5 S)                                           
FORMUL   8  9HJ    2(C20 H31 N5 O2)                                             
FORMUL  15  HOH   *415(H2 O)                                                    
HELIX    1 AA1 ASN A  967  LEU A  971  5                                   5    
HELIX    2 AA2 CYS A  985  LEU A  990  1                                   6    
HELIX    3 AA3 VAL A 1031  GLY A 1035  5                                   5    
HELIX    4 AA4 ASP A 1074  ASP A 1078  1                                   5    
HELIX    5 AA5 ILE A 1107  ILE A 1111  5                                   5    
HELIX    6 AA6 GLY A 1155  SER A 1163  1                                   9    
HELIX    7 AA7 SER A 1178  ALA A 1190  1                                  13    
HELIX    8 AA8 ASN B  967  LEU B  971  5                                   5    
HELIX    9 AA9 CYS B  985  LEU B  990  1                                   6    
HELIX   10 AB1 VAL B 1031  GLY B 1035  5                                   5    
HELIX   11 AB2 ASP B 1074  ASP B 1078  1                                   5    
HELIX   12 AB3 ILE B 1107  ILE B 1111  5                                   5    
HELIX   13 AB4 GLY B 1155  SER B 1163  1                                   9    
HELIX   14 AB5 SER B 1178  ALA B 1190  1                                  13    
SHEET    1 AA1 4 LYS A 920  CYS A 923  0                                        
SHEET    2 AA1 4 CYS A 937  ASN A 939 -1  O  CYS A 937   N  CYS A 923           
SHEET    3 AA1 4 LEU A1040  ARG A1044  1  O  LEU A1042   N  VAL A 938           
SHEET    4 AA1 4 TRP A1050  ALA A1054 -1  O  GLY A1051   N  TYR A1043           
SHEET    1 AA2 4 LYS A 951  TYR A 952  0                                        
SHEET    2 AA2 4 TYR A1097  GLY A1105  1  O  TYR A1103   N  LYS A 951           
SHEET    3 AA2 4 GLY A1069  SER A1073 -1  N  GLU A1070   O  ASP A1100           
SHEET    4 AA2 4 CYS A 957  GLU A 958  1  N  CYS A 957   O  LEU A1071           
SHEET    1 AA3 3 LYS A 951  TYR A 952  0                                        
SHEET    2 AA3 3 TYR A1097  GLY A1105  1  O  TYR A1103   N  LYS A 951           
SHEET    3 AA3 3 LEU A1086  LEU A1089 -1  N  LEU A1089   O  TYR A1097           
SHEET    1 AA4 4 ILE A1014  PHE A1015  0                                        
SHEET    2 AA4 4 ILE A1119  PHE A1125  1  O  ARG A1123   N  ILE A1014           
SHEET    3 AA4 4 ARG A1135  SER A1140 -1  O  ALA A1137   N  VAL A1122           
SHEET    4 AA4 4 PHE A1063  TYR A1067 -1  N  ILE A1064   O  PHE A1138           
SHEET    1 AA5 2 ASN A1112  HIS A1113  0                                        
SHEET    2 AA5 2 GLY A1151  PHE A1152  1  O  PHE A1152   N  ASN A1112           
SHEET    1 AA6 4 LYS B 920  CYS B 923  0                                        
SHEET    2 AA6 4 CYS B 937  ASN B 939 -1  O  CYS B 937   N  CYS B 923           
SHEET    3 AA6 4 LEU B1040  ARG B1044  1  O  LEU B1042   N  VAL B 938           
SHEET    4 AA6 4 TRP B1050  ALA B1054 -1  O  GLY B1051   N  TYR B1043           
SHEET    1 AA7 4 LYS B 951  TYR B 952  0                                        
SHEET    2 AA7 4 TYR B1097  GLY B1105  1  O  TYR B1103   N  LYS B 951           
SHEET    3 AA7 4 GLY B1069  SER B1073 -1  N  GLU B1070   O  ASP B1100           
SHEET    4 AA7 4 CYS B 957  GLU B 958  1  N  CYS B 957   O  LEU B1071           
SHEET    1 AA8 3 LYS B 951  TYR B 952  0                                        
SHEET    2 AA8 3 TYR B1097  GLY B1105  1  O  TYR B1103   N  LYS B 951           
SHEET    3 AA8 3 LEU B1086  LEU B1089 -1  N  LEU B1089   O  TYR B1097           
SHEET    1 AA9 4 ILE B1014  PHE B1015  0                                        
SHEET    2 AA9 4 ILE B1119  PHE B1125  1  O  ARG B1123   N  ILE B1014           
SHEET    3 AA9 4 ARG B1135  SER B1140 -1  O  ALA B1137   N  VAL B1122           
SHEET    4 AA9 4 PHE B1063  TYR B1067 -1  N  ILE B1064   O  PHE B1138           
SHEET    1 AB1 2 ASN B1112  HIS B1113  0                                        
SHEET    2 AB1 2 GLY B1151  PHE B1152  1  O  PHE B1152   N  ASN B1112           
LINK         SG  CYS A 974                ZN    ZN A1503     1555   1555  2.39  
LINK         SG  CYS A 974                ZN    ZN A1502     1555   1555  2.33  
LINK         SG  CYS A 976                ZN    ZN A1503     1555   1555  2.30  
LINK         SG  CYS A 980                ZN    ZN A1501     1555   1555  2.31  
LINK         SG  CYS A 980                ZN    ZN A1503     1555   1555  2.45  
LINK         SG  CYS A 985                ZN    ZN A1503     1555   1555  2.33  
LINK         SG  CYS A 987                ZN    ZN A1502     1555   1555  2.37  
LINK         SG  CYS A1017                ZN    ZN A1501     1555   1555  2.43  
LINK         SG  CYS A1017                ZN    ZN A1502     1555   1555  2.32  
LINK         SG  CYS A1021                ZN    ZN A1502     1555   1555  2.32  
LINK         SG  CYS A1023                ZN    ZN A1501     1555   1555  2.30  
LINK         SG  CYS A1027                ZN    ZN A1501     1555   1555  2.28  
LINK         SG  CYS A1115                ZN    ZN A1504     1555   1555  2.45  
LINK         SG  CYS A1168                ZN    ZN A1504     1555   1555  2.30  
LINK         SG  CYS A1170                ZN    ZN A1504     1555   1555  2.35  
LINK         SG  CYS A1175                ZN    ZN A1504     1555   1555  2.19  
LINK         SG  CYS B 974                ZN    ZN B1503     1555   1555  2.38  
LINK         SG  CYS B 974                ZN    ZN B1502     1555   1555  2.33  
LINK         SG  CYS B 976                ZN    ZN B1503     1555   1555  2.24  
LINK         SG  CYS B 980                ZN    ZN B1501     1555   1555  2.31  
LINK         SG  CYS B 980                ZN    ZN B1503     1555   1555  2.40  
LINK         SG  CYS B 985                ZN    ZN B1503     1555   1555  2.32  
LINK         SG  CYS B 987                ZN    ZN B1502     1555   1555  2.35  
LINK         SG  CYS B1017                ZN    ZN B1501     1555   1555  2.35  
LINK         SG  CYS B1017                ZN    ZN B1502     1555   1555  2.38  
LINK         SG  CYS B1021                ZN    ZN B1502     1555   1555  2.32  
LINK         SG  CYS B1023                ZN    ZN B1501     1555   1555  2.31  
LINK         SG  CYS B1027                ZN    ZN B1501     1555   1555  2.38  
LINK         SG  CYS B1115                ZN    ZN B1504     1555   1555  2.42  
LINK         SG  CYS B1168                ZN    ZN B1504     1555   1555  2.29  
LINK         SG  CYS B1170                ZN    ZN B1504     1555   1555  2.36  
LINK         SG  CYS B1175                ZN    ZN B1504     1555   1555  2.22  
SITE     1 AC1  4 CYS A 980  CYS A1017  CYS A1023  CYS A1027                    
SITE     1 AC2  4 CYS A 974  CYS A 987  CYS A1017  CYS A1021                    
SITE     1 AC3  4 CYS A 974  CYS A 976  CYS A 980  CYS A 985                    
SITE     1 AC4  4 CYS A1115  CYS A1168  CYS A1170  CYS A1175                    
SITE     1 AC5 18 MET A1048  TRP A1050  SER A1084  TYR A1085                    
SITE     2 AC5 18 ARG A1109  PHE A1110  ASN A1112  HIS A1113                    
SITE     3 AC5 18 TYR A1154  PHE A1166  THR A1167  CYS A1168                    
SITE     4 AC5 18 GLN A1169  HOH A1627  HOH A1634  HOH A1696                    
SITE     5 AC5 18 HOH A1723  HOH A1731                                          
SITE     1 AC6 10 ALA A1077  ASP A1078  ARG A1080  ASP A1083                    
SITE     2 AC6 10 LEU A1086  ASP A1088  CYS A1098  ARG A1157                    
SITE     3 AC6 10 PHE A1158  ILE A1161                                          
SITE     1 AC7  4 CYS B 980  CYS B1017  CYS B1023  CYS B1027                    
SITE     1 AC8  4 CYS B 974  CYS B 987  CYS B1017  CYS B1021                    
SITE     1 AC9  4 CYS B 974  CYS B 976  CYS B 980  CYS B 985                    
SITE     1 AD1  4 CYS B1115  CYS B1168  CYS B1170  CYS B1175                    
SITE     1 AD2 20 MET B1048  TRP B1050  SER B1084  TYR B1085                    
SITE     2 AD2 20 ARG B1109  PHE B1110  ASN B1112  HIS B1113                    
SITE     3 AD2 20 TYR B1154  PHE B1158  PHE B1166  THR B1167                    
SITE     4 AD2 20 CYS B1168  GLN B1169  HOH B1634  HOH B1659                    
SITE     5 AD2 20 HOH B1667  HOH B1722  HOH B1737  HOH B1771                    
SITE     1 AD3 12 ASP B1074  ALA B1077  ASP B1078  ARG B1080                    
SITE     2 AD3 12 ASP B1083  LEU B1086  ASP B1088  VAL B1096                    
SITE     3 AD3 12 TYR B1097  CYS B1098  ARG B1157  PHE B1158                    
CRYST1   56.440   78.430   73.060  90.00  90.96  90.00 P 1 21 1      4          
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      0.017718  0.000000  0.000297        0.00000                         
SCALE2      0.000000  0.012750  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013689        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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