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Database: PDB
Entry: 5VSE
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HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       11-MAY-17   5VSE              
TITLE     STRUCTURE OF HUMAN G9A SET-DOMAIN (EHMT2) IN COMPLEX WITH INHIBITOR   
TITLE    2 17: N~2~-CYCLOPENTYL-6,7-DIMETHOXY-N~2~-METHYL-N~4~-(1-              
TITLE    3 METHYLPIPERIDIN-4-YL)QUINAZOLINE-2,4-DIAMINE                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE EHMT2;                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: G9A CATALYTIC SET-DOMAIN (913-1193);                       
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 5VSE    1       JRNL                                     
REVDAT   1   19-JUL-17 5VSE    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.    1.60 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) : 1.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.88                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 82711                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.169                           
REMARK   3   R VALUE            (WORKING SET) : 0.168                           
REMARK   3   FREE R VALUE                     : 0.191                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.980                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4118                            
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 45.9008 -  4.9138    0.98     2733   168  0.1464 0.1559        
REMARK   3     2  4.9138 -  3.9009    0.99     2747   149  0.1250 0.1428        
REMARK   3     3  3.9009 -  3.4079    1.00     2777   129  0.1511 0.1674        
REMARK   3     4  3.4079 -  3.0964    1.00     2771   111  0.1707 0.1829        
REMARK   3     5  3.0964 -  2.8745    0.99     2747   146  0.1769 0.2099        
REMARK   3     6  2.8745 -  2.7051    0.98     2652   159  0.1791 0.2041        
REMARK   3     7  2.7051 -  2.5696    0.97     2683   130  0.1805 0.2111        
REMARK   3     8  2.5696 -  2.4578    0.98     2677   139  0.1841 0.2124        
REMARK   3     9  2.4578 -  2.3631    0.99     2778   108  0.1825 0.2462        
REMARK   3    10  2.3631 -  2.2816    0.99     2728   134  0.1814 0.2226        
REMARK   3    11  2.2816 -  2.2103    0.99     2754   118  0.1738 0.1981        
REMARK   3    12  2.2103 -  2.1471    1.00     2737   115  0.1763 0.2211        
REMARK   3    13  2.1471 -  2.0906    1.00     2721   150  0.1812 0.2066        
REMARK   3    14  2.0906 -  2.0396    1.00     2757   132  0.1744 0.2122        
REMARK   3    15  2.0396 -  1.9932    1.00     2759   129  0.1745 0.2011        
REMARK   3    16  1.9932 -  1.9508    1.00     2709   140  0.1752 0.1851        
REMARK   3    17  1.9508 -  1.9118    0.98     2672   131  0.1750 0.2207        
REMARK   3    18  1.9118 -  1.8757    0.97     2705   122  0.1759 0.2394        
REMARK   3    19  1.8757 -  1.8422    0.98     2661   165  0.1839 0.1938        
REMARK   3    20  1.8422 -  1.8109    0.98     2637   161  0.1853 0.2288        
REMARK   3    21  1.8109 -  1.7817    0.99     2678   195  0.1821 0.2189        
REMARK   3    22  1.7817 -  1.7543    0.99     2658   163  0.1866 0.2138        
REMARK   3    23  1.7543 -  1.7285    0.99     2667   175  0.2037 0.2412        
REMARK   3    24  1.7285 -  1.7042    0.99     2698   158  0.2119 0.2116        
REMARK   3    25  1.7042 -  1.6811    0.99     2709   131  0.2277 0.2596        
REMARK   3    26  1.6811 -  1.6593    0.99     2664   145  0.2404 0.2684        
REMARK   3    27  1.6593 -  1.6386    0.99     2712   141  0.2516 0.2759        
REMARK   3    28  1.6386 -  1.6188    0.99     2667   134  0.2571 0.2852        
REMARK   3    29  1.6188 -  1.6000    0.99     2735   140  0.2830 0.2803        
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)     : 0.170            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.240           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 24.78                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.66                          
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           4565                                  
REMARK   3   ANGLE     :  1.104           6177                                  
REMARK   3   CHIRALITY :  0.065            656                                  
REMARK   3   PLANARITY :  0.006            800                                  
REMARK   3   DIHEDRAL  : 14.749           2743                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 18                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1022 THROUGH 1079 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  28.1475  -1.7915  -6.7506              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2227 T22:   0.1622                                     
REMARK   3      T33:   0.1832 T12:  -0.0316                                     
REMARK   3      T13:  -0.0207 T23:  -0.0085                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2430 L22:   1.2316                                     
REMARK   3      L33:   1.4011 L12:  -0.4095                                     
REMARK   3      L13:  -0.5525 L23:   0.3359                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0559 S12:   0.1175 S13:  -0.0715                       
REMARK   3      S21:  -0.0989 S22:  -0.0094 S23:  -0.0772                       
REMARK   3      S31:  -0.0052 S32:  -0.0878 S33:  -0.0213                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1080 THROUGH 1110 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  35.6810  10.3536  -5.6088              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2808 T22:   0.1743                                     
REMARK   3      T33:   0.3288 T12:  -0.0430                                     
REMARK   3      T13:   0.0361 T23:  -0.0196                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8451 L22:   3.3143                                     
REMARK   3      L33:   3.4045 L12:  -0.6063                                     
REMARK   3      L13:  -1.4301 L23:   0.6292                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1929 S12:   0.1069 S13:   0.4470                       
REMARK   3      S21:  -0.2288 S22:   0.0888 S23:  -0.4841                       
REMARK   3      S31:  -0.4322 S32:   0.0991 S33:  -0.2175                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1111 THROUGH 1155 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  27.1228   2.0209 -12.7902              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2509 T22:   0.2066                                     
REMARK   3      T33:   0.1711 T12:  -0.0376                                     
REMARK   3      T13:  -0.0111 T23:   0.0064                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6374 L22:   1.4652                                     
REMARK   3      L33:   1.6462 L12:  -0.6537                                     
REMARK   3      L13:  -0.8647 L23:   0.1225                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0834 S12:   0.3603 S13:  -0.0487                       
REMARK   3      S21:  -0.2768 S22:  -0.0243 S23:  -0.0176                       
REMARK   3      S31:  -0.0227 S32:  -0.1363 S33:  -0.0483                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1156 THROUGH 1190 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  42.9260   8.3177 -25.7243              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4509 T22:   0.4725                                     
REMARK   3      T33:   0.3837 T12:  -0.0220                                     
REMARK   3      T13:   0.1638 T23:   0.0555                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7301 L22:   2.2294                                     
REMARK   3      L33:   5.5585 L12:   0.1373                                     
REMARK   3      L13:  -1.5043 L23:  -1.0423                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1594 S12:   0.9093 S13:   0.3256                       
REMARK   3      S21:  -0.5760 S22:   0.0619 S23:  -0.2559                       
REMARK   3      S31:  -0.2187 S32:   0.0024 S33:  -0.2164                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 919 THROUGH 938 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   3.6845  -8.6999  12.3376              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2616 T22:   0.3325                                     
REMARK   3      T33:   0.4207 T12:  -0.0443                                     
REMARK   3      T13:  -0.0213 T23:  -0.0005                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.6879 L22:   2.9266                                     
REMARK   3      L33:   5.7690 L12:   0.5953                                     
REMARK   3      L13:  -2.7373 L23:  -0.8641                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1945 S12:   0.4312 S13:  -0.6529                       
REMARK   3      S21:  -0.2187 S22:   0.2322 S23:   0.3843                       
REMARK   3      S31:   0.2891 S32:  -0.6376 S33:  -0.0396                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 939 THROUGH 958 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   1.3099   0.8586  14.6359              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1702 T22:   0.2907                                     
REMARK   3      T33:   0.2744 T12:   0.0009                                     
REMARK   3      T13:  -0.0134 T23:   0.0676                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.5749 L22:   4.8510                                     
REMARK   3      L33:   3.3388 L12:   3.8592                                     
REMARK   3      L13:  -2.9554 L23:  -2.3938                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0492 S12:   0.4753 S13:  -0.0502                       
REMARK   3      S21:  -0.0138 S22:   0.2729 S23:   0.3829                       
REMARK   3      S31:   0.0350 S32:  -0.4749 S33:  -0.2104                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 959 THROUGH 985 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  32.1581   6.3713  15.5273              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2505 T22:   0.2938                                     
REMARK   3      T33:   0.2359 T12:  -0.0290                                     
REMARK   3      T13:  -0.0023 T23:  -0.0020                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8952 L22:   2.0705                                     
REMARK   3      L33:   1.0268 L12:  -0.6093                                     
REMARK   3      L13:  -0.4954 L23:   0.0219                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1853 S12:  -0.3907 S13:   0.0727                       
REMARK   3      S21:   0.1944 S22:   0.1937 S23:  -0.2155                       
REMARK   3      S31:  -0.1297 S32:   0.1807 S33:  -0.0063                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 986 THROUGH 1005 )                
REMARK   3    ORIGIN FOR THE GROUP (A):  30.2988  -4.4392  27.7425              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4910 T22:   0.7630                                     
REMARK   3      T33:   0.4581 T12:   0.0634                                     
REMARK   3      T13:  -0.0649 T23:   0.1025                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.7660 L22:   4.0440                                     
REMARK   3      L33:   5.7516 L12:   1.3578                                     
REMARK   3      L13:  -1.1933 L23:   0.2212                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1121 S12:  -1.2139 S13:  -0.4817                       
REMARK   3      S21:   1.0232 S22:  -0.0849 S23:  -0.7320                       
REMARK   3      S31:  -0.3474 S32:   1.0858 S33:   0.1521                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1006 THROUGH 1025 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  28.9194   0.6857  22.3489              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2737 T22:   0.3765                                     
REMARK   3      T33:   0.2170 T12:  -0.0144                                     
REMARK   3      T13:  -0.0212 T23:   0.0371                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3688 L22:   3.3960                                     
REMARK   3      L33:   4.9775 L12:  -0.5797                                     
REMARK   3      L13:  -1.8789 L23:   0.5362                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0677 S12:  -0.5220 S13:  -0.0136                       
REMARK   3      S21:   0.5762 S22:  -0.0115 S23:  -0.0658                       
REMARK   3      S31:   0.0842 S32:   0.0503 S33:   0.0909                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1026 THROUGH 1062 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  11.6647  -7.9606  22.1710              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2300 T22:   0.2300                                     
REMARK   3      T33:   0.3210 T12:  -0.0028                                     
REMARK   3      T13:   0.0099 T23:   0.0861                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6401 L22:   1.1059                                     
REMARK   3      L33:   1.0625 L12:   0.4937                                     
REMARK   3      L13:  -0.6068 L23:  -0.3315                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0770 S12:  -0.0547 S13:  -0.5763                       
REMARK   3      S21:   0.0980 S22:   0.0726 S23:   0.1294                       
REMARK   3      S31:   0.0979 S32:  -0.0734 S33:   0.0347                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1063 THROUGH 1096 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  10.3412  12.3453  22.1894              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2847 T22:   0.2593                                     
REMARK   3      T33:   0.2545 T12:   0.0174                                     
REMARK   3      T13:   0.0449 T23:   0.0241                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5810 L22:   7.2334                                     
REMARK   3      L33:   3.6692 L12:  -0.9250                                     
REMARK   3      L13:  -1.3982 L23:  -0.2369                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0831 S12:  -0.3750 S13:   0.4268                       
REMARK   3      S21:   0.4148 S22:   0.2286 S23:   0.0193                       
REMARK   3      S31:  -0.6296 S32:  -0.0855 S33:  -0.2828                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1097 THROUGH 1140 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  14.0024   5.0286  22.8451              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2297 T22:   0.2463                                     
REMARK   3      T33:   0.2154 T12:   0.0189                                     
REMARK   3      T13:   0.0127 T23:   0.0485                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5142 L22:   1.1533                                     
REMARK   3      L33:   1.5091 L12:   0.7474                                     
REMARK   3      L13:  -1.1127 L23:  -0.3761                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0134 S12:  -0.2766 S13:   0.0893                       
REMARK   3      S21:   0.1239 S22:   0.0504 S23:   0.0417                       
REMARK   3      S31:  -0.0762 S32:  -0.0210 S33:  -0.0691                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1141 THROUGH 1162 )               
REMARK   3    ORIGIN FOR THE GROUP (A):   7.2374   0.1471  32.3775              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2792 T22:   0.4266                                     
REMARK   3      T33:   0.2567 T12:   0.0051                                     
REMARK   3      T13:   0.0880 T23:   0.1187                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3738 L22:   3.2612                                     
REMARK   3      L33:   2.9713 L12:  -1.5731                                     
REMARK   3      L13:  -0.6792 L23:   0.4056                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0936 S12:  -0.7246 S13:  -0.3681                       
REMARK   3      S21:   0.5567 S22:   0.1559 S23:   0.3086                       
REMARK   3      S31:  -0.0658 S32:   0.0403 S33:  -0.0655                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1163 THROUGH 1190 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.2931   6.0064  42.9530              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4875 T22:   0.6402                                     
REMARK   3      T33:   0.4166 T12:   0.0227                                     
REMARK   3      T13:   0.1858 T23:   0.0749                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7020 L22:   1.8922                                     
REMARK   3      L33:   4.5905 L12:  -0.2391                                     
REMARK   3      L13:   0.8427 L23:   1.0931                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2208 S12:  -0.3109 S13:   0.3038                       
REMARK   3      S21:   0.3650 S22:  -0.0959 S23:   0.1756                       
REMARK   3      S31:  -0.1871 S32:   0.0925 S33:  -0.1216                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 916 THROUGH 935 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  39.1480 -10.8896  -0.3449              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2608 T22:   0.1934                                     
REMARK   3      T33:   0.3091 T12:  -0.0338                                     
REMARK   3      T13:  -0.0148 T23:  -0.0307                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1868 L22:   5.1419                                     
REMARK   3      L33:   5.4367 L12:  -3.3043                                     
REMARK   3      L13:  -3.4602 L23:   2.4015                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2006 S12:  -0.3944 S13:   0.0876                       
REMARK   3      S21:   0.1327 S22:   0.2741 S23:  -0.5705                       
REMARK   3      S31:   0.3626 S32:   0.4744 S33:   0.0230                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 936 THROUGH 954 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  43.4422  -4.3445  -1.6487              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2802 T22:   0.2624                                     
REMARK   3      T33:   0.3805 T12:  -0.0172                                     
REMARK   3      T13:  -0.0442 T23:  -0.0601                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6322 L22:   3.6282                                     
REMARK   3      L33:   2.3213 L12:  -3.1897                                     
REMARK   3      L13:  -2.9908 L23:   2.2347                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2715 S12:  -0.2986 S13:   0.1897                       
REMARK   3      S21:   0.1571 S22:   0.4017 S23:  -0.6614                       
REMARK   3      S31:   0.0810 S32:   0.4606 S33:  -0.1718                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 955 THROUGH 985 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  12.8915   8.6646  -0.0692              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2430 T22:   0.2756                                     
REMARK   3      T33:   0.2405 T12:   0.0027                                     
REMARK   3      T13:  -0.0086 T23:   0.0480                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6827 L22:   2.0410                                     
REMARK   3      L33:   1.8203 L12:  -0.2871                                     
REMARK   3      L13:  -0.7568 L23:   0.3046                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0265 S12:   0.2594 S13:   0.0117                       
REMARK   3      S21:  -0.0675 S22:  -0.0047 S23:   0.1212                       
REMARK   3      S31:   0.0138 S32:  -0.3502 S33:  -0.0357                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 986 THROUGH 1021 )                
REMARK   3    ORIGIN FOR THE GROUP (A):  12.7718   1.5962 -12.6795              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3008 T22:   0.4589                                     
REMARK   3      T33:   0.2575 T12:  -0.0131                                     
REMARK   3      T13:  -0.0714 T23:   0.0139                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5884 L22:   2.3028                                     
REMARK   3      L33:   4.4982 L12:  -0.8233                                     
REMARK   3      L13:  -1.8411 L23:   0.8463                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1662 S12:   0.8461 S13:  -0.0392                       
REMARK   3      S21:  -0.4407 S22:  -0.1918 S23:   0.2396                       
REMARK   3      S31:  -0.0141 S32:  -0.7130 S33:   0.0370                       
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 919 THROUGH 1090 OR     
REMARK   3                          RESID 1095 THROUGH 1190))                   
REMARK   3     SELECTION          : (CHAIN B AND RESID 919 THROUGH 1190)        
REMARK   3     ATOM PAIRS NUMBER  : 2608                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5VSE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-MAY-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000227938.                                   
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                             : 6.5                                
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   : 82905                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 72.589                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.04800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.46900                            
REMARK 200  R SYM FOR SHELL            (I) : 0.46900                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.600                              
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: 5TUY                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.64                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20 % PEG3350, 10% GLYCEROL, 0.2 M        
REMARK 280  SODIUM FLUORIDE, BIS-TRIS PROPANE PH6.5, VAPOR DIFFUSION,           
REMARK 280  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       39.34550            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2290 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25640 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     THR A   916                                                      
REMARK 465     ARG A   917                                                      
REMARK 465     THR A   918                                                      
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 465     GLY B  1094                                                      
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    ILE A 922   CG1 -  CB  -  CG2 ANGL. DEV. = -15.3 DEGREES          
REMARK 500    LYS A1176   CB  -  CG  -  CD  ANGL. DEV. = -18.1 DEGREES          
REMARK 500    LYS A1176   CD  -  CE  -  NZ  ANGL. DEV. =  13.9 DEGREES          
REMARK 500    LEU A1189   CA  -  CB  -  CG  ANGL. DEV. =  16.6 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    GLU A 948       13.82   -143.86                                   
REMARK 500    ASP A 949       35.95    -97.53                                   
REMARK 500    ASP A 978     -151.21   -103.49                                   
REMARK 500    ILE A 992      -54.57     71.51                                   
REMARK 500    ARG A1030       36.84   -142.52                                   
REMARK 500    ILE A1064      -63.67   -102.94                                   
REMARK 500    ASP A1090      156.59     65.23                                   
REMARK 500    ASN A1106     -160.83   -109.23                                   
REMARK 500    ASP A1116       74.73   -115.23                                   
REMARK 500    MET A1126      -91.23   -127.87                                   
REMARK 500    LEU A1189      -52.45    -26.83                                   
REMARK 500    ASP B 949       35.52    -95.14                                   
REMARK 500    ASP B 978     -151.47   -107.51                                   
REMARK 500    ILE B 992      -55.59     71.01                                   
REMARK 500    ASN B1029       50.43   -114.86                                   
REMARK 500    ARG B1030       37.26   -143.12                                   
REMARK 500    ILE B1064      -64.52   -102.13                                   
REMARK 500    LEU B1089       79.16   -103.01                                   
REMARK 500    ASN B1106     -161.48   -108.83                                   
REMARK 500    ASP B1116       76.14   -114.38                                   
REMARK 500    MET B1126      -91.47   -129.19                                   
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  105.6                                              
REMARK 620 3 CYS A 980   SG  105.2 105.7                                        
REMARK 620 4 CYS A 985   SG  112.7 110.7 116.3                                  
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  113.5                                              
REMARK 620 3 CYS A1017   SG  111.0 110.7                                        
REMARK 620 4 CYS A1021   SG  106.2  97.0 117.8                                  
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  113.0                                              
REMARK 620 3 CYS A1023   SG  103.9 105.4                                        
REMARK 620 4 CYS A1027   SG  112.7 107.7 114.0                                  
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  110.8                                              
REMARK 620 3 CYS A1170   SG  108.8 109.4                                        
REMARK 620 4 CYS A1175   SG  109.9 108.7 109.1                                  
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  107.9                                              
REMARK 620 3 CYS B 980   SG  107.9 105.1                                        
REMARK 620 4 CYS B 985   SG  110.1 107.9 117.4                                  
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  111.1                                              
REMARK 620 3 CYS B1017   SG  111.5 113.8                                        
REMARK 620 4 CYS B1021   SG  102.8  98.9 117.7                                  
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  109.4                                              
REMARK 620 3 CYS B1023   SG  104.1 110.5                                        
REMARK 620 4 CYS B1027   SG  115.0 104.7 113.2                                  
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  113.9                                              
REMARK 620 3 CYS B1170   SG  111.2 106.4                                        
REMARK 620 4 CYS B1175   SG  104.8 109.4 111.2                                  
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 9HG 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 9HG B 1506                
DBREF  5VSE A  917  1190  UNP    Q96KQ7   EHMT2_HUMAN    883   1156             
DBREF  5VSE B  917  1190  UNP    Q96KQ7   EHMT2_HUMAN    883   1156             
SEQADV 5VSE THR A  916  UNP  Q96KQ7              EXPRESSION TAG                 
SEQADV 5VSE THR B  916  UNP  Q96KQ7              EXPRESSION TAG                 
SEQRES   1 A  275  THR 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  THR 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    9HG  A1506      29                                                       
HET     ZN  B1501       1                                                       
HET     ZN  B1502       1                                                       
HET     ZN  B1503       1                                                       
HET     ZN  B1504       1                                                       
HET    SAM  B1505      27                                                       
HET    9HG  B1506      29                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     SAM S-ADENOSYLMETHIONINE                                             
HETNAM     9HG N~2~-CYCLOPENTYL-6,7-DIMETHOXY-N~2~-METHYL-N~4~-(1-              
HETNAM   2 9HG  METHYLPIPERIDIN-4-YL)QUINAZOLINE-2,4-DIAMINE                    
FORMUL   3   ZN    8(ZN 2+)                                                     
FORMUL   7  SAM    2(C15 H22 N6 O5 S)                                           
FORMUL   8  9HG    2(C22 H33 N5 O2)                                             
FORMUL  15  HOH   *338(H2 O)                                                    
HELIX    1 AA1 ASN A  967  LEU A  971  5                                   5    
HELIX    2 AA2 CYS A  985  SER A  991  1                                   7    
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  LEU A 1189  1                                  12    
HELIX    8 AA8 ASN B  967  LEU B  971  5                                   5    
HELIX    9 AA9 CYS B  985  SER B  991  1                                   7    
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 ILE A 921  CYS A 923  0                                        
SHEET    2 AA1 4 CYS A 937  VAL A 938 -1  O  CYS A 937   N  ILE A 922           
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  ASP A1088 -1  N  PHE A1087   O  ILE A1099           
SHEET    1 AA4 4 ILE A1014  PHE A1015  0                                        
SHEET    2 AA4 4 ILE A1119  PHE A1125  1  O  PHE A1125   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  2.35  
LINK         SG  CYS A 974                ZN    ZN A1502     1555   1555  2.41  
LINK         SG  CYS A 976                ZN    ZN A1503     1555   1555  2.25  
LINK         SG  CYS A 980                ZN    ZN A1501     1555   1555  2.33  
LINK         SG  CYS A 980                ZN    ZN A1503     1555   1555  2.45  
LINK         SG  CYS A 985                ZN    ZN A1503     1555   1555  2.40  
LINK         SG  CYS A 987                ZN    ZN A1502     1555   1555  2.30  
LINK         SG  CYS A1017                ZN    ZN A1501     1555   1555  2.42  
LINK         SG  CYS A1017                ZN    ZN A1502     1555   1555  2.26  
LINK         SG  CYS A1021                ZN    ZN A1502     1555   1555  2.33  
LINK         SG  CYS A1023                ZN    ZN A1501     1555   1555  2.35  
LINK         SG  CYS A1027                ZN    ZN A1501     1555   1555  2.32  
LINK         SG  CYS A1115                ZN    ZN A1504     1555   1555  2.46  
LINK         SG  CYS A1168                ZN    ZN A1504     1555   1555  2.30  
LINK         SG  CYS A1170                ZN    ZN A1504     1555   1555  2.27  
LINK         SG  CYS A1175                ZN    ZN A1504     1555   1555  2.18  
LINK         SG  CYS B 974                ZN    ZN B1503     1555   1555  2.46  
LINK         SG  CYS B 974                ZN    ZN B1502     1555   1555  2.29  
LINK         SG  CYS B 976                ZN    ZN B1503     1555   1555  2.28  
LINK         SG  CYS B 980                ZN    ZN B1501     1555   1555  2.38  
LINK         SG  CYS B 980                ZN    ZN B1503     1555   1555  2.29  
LINK         SG  CYS B 985                ZN    ZN B1503     1555   1555  2.33  
LINK         SG  CYS B 987                ZN    ZN B1502     1555   1555  2.34  
LINK         SG  CYS B1017                ZN    ZN B1501     1555   1555  2.31  
LINK         SG  CYS B1017                ZN    ZN B1502     1555   1555  2.46  
LINK         SG  CYS B1021                ZN    ZN B1502     1555   1555  2.31  
LINK         SG  CYS B1023                ZN    ZN B1501     1555   1555  2.31  
LINK         SG  CYS B1027                ZN    ZN B1501     1555   1555  2.34  
LINK         SG  CYS B1115                ZN    ZN B1504     1555   1555  2.42  
LINK         SG  CYS B1168                ZN    ZN B1504     1555   1555  2.28  
LINK         SG  CYS B1170                ZN    ZN B1504     1555   1555  2.36  
LINK         SG  CYS B1175                ZN    ZN B1504     1555   1555  2.24  
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 A1158  PHE A1166  THR A1167                    
SITE     4 AC5 18 CYS A1168  GLN A1169  HOH A1640  HOH A1651                    
SITE     5 AC5 18 HOH A1706  HOH A1712                                          
SITE     1 AC6 11 ASP A1074  ALA A1077  ASP A1078  ARG A1080                    
SITE     2 AC6 11 ASP A1083  LEU A1086  ASP A1088  VAL A1096                    
SITE     3 AC6 11 CYS A1098  ARG A1157  PHE A1158                               
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 19 MET B1048  TRP B1050  SER B1084  TYR B1085                    
SITE     2 AD2 19 ARG B1109  PHE B1110  ASN B1112  HIS B1113                    
SITE     3 AD2 19 TYR B1154  PHE B1158  PHE B1166  THR B1167                    
SITE     4 AD2 19 CYS B1168  GLN B1169  HOH B1633  HOH B1651                    
SITE     5 AD2 19 HOH B1689  HOH B1740  HOH B1745                               
SITE     1 AD3  9 ALA B1077  ASP B1078  ARG B1080  ASP B1083                    
SITE     2 AD3  9 LEU B1086  ASP B1088  VAL B1096  ARG B1157                    
SITE     3 AD3  9 PHE B1158                                                     
CRYST1   56.491   78.691   72.610  90.00  91.35  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      0.017702  0.000000  0.000417        0.00000                         
SCALE2      0.000000  0.012708  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013776        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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