GenomeNet

Database: PDB
Entry: 5TUZ
LinkDB: 5TUZ
Original site: 5TUZ 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       07-NOV-16   5TUZ              
TITLE     STRUCTURE OF HUMAN GLP SET-DOMAIN (EHMT1) IN COMPLEX WITH INHIBITOR   
TITLE    2 MS0124                                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE EHMT1;                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 1006-1266;                                    
COMPND   5 SYNONYM: EUCHROMATIC HISTONE-LYSINE N-METHYLTRANSFERASE 1,EU-HMTASE1,
COMPND   6 G9A-LIKE PROTEIN 1,GLP1,HISTONE H3-K9 METHYLTRANSFERASE 5,H3-K9-     
COMPND   7 HMTASE 5,LYSINE N-METHYLTRANSFERASE 1D;                              
COMPND   8 EC: 2.1.1.-,2.1.1.43;                                                
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: EHMT1, EUHMTASE1, GLP, KIAA1876, KMT1D;                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) CODON PLUS RIL;                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A-LIC                                
KEYWDS    METHYL TRANSFERASE, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.BABAULT,Y.XIONG,J.LIU,J.JIN                                         
REVDAT   3   27-SEP-17 5TUZ    1       REMARK                                   
REVDAT   2   22-MAR-17 5TUZ    1       JRNL                                     
REVDAT   1   22-FEB-17 5TUZ    0                                                
JRNL        AUTH   Y.XIONG,F.LI,N.BABAULT,A.DONG,H.ZENG,H.WU,X.CHEN,            
JRNL        AUTH 2 C.H.ARROWSMITH,P.J.BROWN,J.LIU,M.VEDADI,J.JIN                
JRNL        TITL   DISCOVERY OF POTENT AND SELECTIVE INHIBITORS FOR G9A-LIKE    
JRNL        TITL 2 PROTEIN (GLP) LYSINE METHYLTRANSFERASE.                      
JRNL        REF    J. MED. CHEM.                 V.  60  1876 2017              
JRNL        REFN                   ISSN 1520-4804                               
JRNL        PMID   28135087                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.6B01645                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.95 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
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) : 1.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 59.02                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 54238                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.163                           
REMARK   3   R VALUE            (WORKING SET) : 0.161                           
REMARK   3   FREE R VALUE                     : 0.201                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.110                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2772                            
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 59.0481 -  5.2919    0.99     2747   147  0.1328 0.1727        
REMARK   3     2  5.2919 -  4.2007    1.00     2669   130  0.1238 0.1631        
REMARK   3     3  4.2007 -  3.6698    1.00     2618   145  0.1425 0.1712        
REMARK   3     4  3.6698 -  3.3343    1.00     2601   141  0.1632 0.1978        
REMARK   3     5  3.3343 -  3.0953    1.00     2585   141  0.1800 0.1990        
REMARK   3     6  3.0953 -  2.9129    1.00     2597   140  0.1733 0.2184        
REMARK   3     7  2.9129 -  2.7670    1.00     2570   133  0.1706 0.2038        
REMARK   3     8  2.7670 -  2.6465    1.00     2571   122  0.1698 0.2113        
REMARK   3     9  2.6465 -  2.5446    1.00     2574   147  0.1591 0.1822        
REMARK   3    10  2.5446 -  2.4568    1.00     2557   135  0.1658 0.2107        
REMARK   3    11  2.4568 -  2.3800    1.00     2526   153  0.1723 0.2261        
REMARK   3    12  2.3800 -  2.3120    1.00     2555   145  0.1631 0.2386        
REMARK   3    13  2.3120 -  2.2511    1.00     2557   133  0.1690 0.2045        
REMARK   3    14  2.2511 -  2.1962    1.00     2536   147  0.1688 0.2107        
REMARK   3    15  2.1962 -  2.1463    1.00     2491   159  0.1691 0.2138        
REMARK   3    16  2.1463 -  2.1006    1.00     2569   136  0.1732 0.2006        
REMARK   3    17  2.1006 -  2.0586    1.00     2523   147  0.1797 0.2242        
REMARK   3    18  2.0586 -  2.0197    1.00     2534   123  0.1916 0.2370        
REMARK   3    19  2.0197 -  1.9836    1.00     2542   129  0.1977 0.2829        
REMARK   3    20  1.9836 -  1.9500    1.00     2544   119  0.2255 0.2592        
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)     : 0.180            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.190           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.34                          
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      :  0.008           4432                                  
REMARK   3   ANGLE     :  1.085           5956                                  
REMARK   3   CHIRALITY :  0.052            613                                  
REMARK   3   PLANARITY :  0.005            781                                  
REMARK   3   DIHEDRAL  : 14.084           1666                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 20                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1006 THROUGH 1023 )               
REMARK   3    ORIGIN FOR THE GROUP (A):   7.5314 -15.2089   0.1852              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2274 T22:   0.3308                                     
REMARK   3      T33:   0.1708 T12:  -0.1361                                     
REMARK   3      T13:  -0.0183 T23:   0.0016                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7568 L22:   4.6142                                     
REMARK   3      L33:   4.1727 L12:   0.0553                                     
REMARK   3      L13:  -1.2313 L23:  -3.9934                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2081 S12:   0.4611 S13:   0.0858                       
REMARK   3      S21:  -0.4000 S22:   0.2104 S23:  -0.2155                       
REMARK   3      S31:   0.2932 S32:   0.5873 S33:   0.0185                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1024 THROUGH 1042 )               
REMARK   3    ORIGIN FOR THE GROUP (A):   1.1580  -9.3089  -2.8871              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4781 T22:   0.2946                                     
REMARK   3      T33:   0.2370 T12:  -0.1908                                     
REMARK   3      T13:  -0.0688 T23:   0.0552                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9504 L22:   0.0742                                     
REMARK   3      L33:   2.8398 L12:   0.2633                                     
REMARK   3      L13:  -1.6416 L23:  -0.4232                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1081 S12:   0.2509 S13:   0.3057                       
REMARK   3      S21:  -0.4373 S22:   0.2240 S23:   0.1198                       
REMARK   3      S31:  -0.6129 S32:   0.3546 S33:  -0.1002                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1043 THROUGH 1073 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.7975 -30.9377  21.2168              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1000 T22:   0.1675                                     
REMARK   3      T33:   0.1938 T12:   0.0014                                     
REMARK   3      T13:  -0.0287 T23:   0.0033                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2924 L22:   2.0780                                     
REMARK   3      L33:   1.2718 L12:   0.7968                                     
REMARK   3      L13:  -0.1051 L23:  -0.5944                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0496 S12:  -0.0670 S13:  -0.0228                       
REMARK   3      S21:   0.0333 S22:   0.0076 S23:   0.2347                       
REMARK   3      S31:   0.0257 S32:  -0.1314 S33:  -0.0555                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1074 THROUGH 1109 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.4320 -38.6986   9.6554              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1482 T22:   0.0947                                     
REMARK   3      T33:   0.2234 T12:  -0.0073                                     
REMARK   3      T13:  -0.0546 T23:  -0.0063                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9758 L22:   2.0634                                     
REMARK   3      L33:   5.3490 L12:  -0.0353                                     
REMARK   3      L13:   1.9515 L23:   0.3294                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1973 S12:   0.0773 S13:  -0.2193                       
REMARK   3      S21:  -0.1747 S22:  -0.0364 S23:   0.2275                       
REMARK   3      S31:   0.3865 S32:  -0.1852 S33:  -0.1066                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1110 THROUGH 1137 )               
REMARK   3    ORIGIN FOR THE GROUP (A):   0.1598 -27.1856   4.2129              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1643 T22:   0.1656                                     
REMARK   3      T33:   0.1174 T12:  -0.0516                                     
REMARK   3      T13:  -0.0088 T23:  -0.0130                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7928 L22:   4.7823                                     
REMARK   3      L33:   5.4272 L12:  -0.1778                                     
REMARK   3      L13:   0.4709 L23:  -4.0744                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0298 S12:   0.1829 S13:  -0.0805                       
REMARK   3      S21:  -0.3022 S22:  -0.0998 S23:  -0.1244                       
REMARK   3      S31:  -0.0622 S32:   0.4000 S33:   0.1347                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1138 THROUGH 1167 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.4403 -20.4516   2.5119              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1302 T22:   0.1269                                     
REMARK   3      T33:   0.1262 T12:  -0.0039                                     
REMARK   3      T13:  -0.0599 T23:  -0.0152                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1051 L22:   2.7750                                     
REMARK   3      L33:   1.9041 L12:  -0.2230                                     
REMARK   3      L13:   0.6673 L23:  -0.3394                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1189 S12:  -0.0368 S13:   0.0608                       
REMARK   3      S21:  -0.2501 S22:   0.0266 S23:   0.1498                       
REMARK   3      S31:  -0.2371 S32:  -0.0156 S33:   0.0640                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1168 THROUGH 1184 )               
REMARK   3    ORIGIN FOR THE GROUP (A): -18.4510 -14.9683   6.4261              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2662 T22:   0.2659                                     
REMARK   3      T33:   0.2475 T12:   0.0726                                     
REMARK   3      T13:  -0.1142 T23:  -0.0536                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.7844 L22:   3.8634                                     
REMARK   3      L33:   5.9120 L12:  -3.3362                                     
REMARK   3      L13:   0.0535 L23:   1.8102                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0856 S12:  -0.0578 S13:  -0.0945                       
REMARK   3      S21:  -0.3731 S22:  -0.1618 S23:   0.7385                       
REMARK   3      S31:  -0.6471 S32:  -0.8324 S33:  -0.0644                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1185 THROUGH 1228 )               
REMARK   3    ORIGIN FOR THE GROUP (A): -10.9208 -22.2168   5.6379              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1378 T22:   0.1190                                     
REMARK   3      T33:   0.1571 T12:   0.0143                                     
REMARK   3      T13:  -0.0490 T23:  -0.0148                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5223 L22:   0.9777                                     
REMARK   3      L33:   2.5747 L12:  -0.0059                                     
REMARK   3      L13:  -0.0106 L23:  -0.1346                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0137 S12:   0.0253 S13:  -0.0380                       
REMARK   3      S21:  -0.1542 S22:  -0.0028 S23:   0.1447                       
REMARK   3      S31:  -0.1948 S32:  -0.0680 S33:   0.0165                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1229 THROUGH 1243 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.7783 -26.6989  -7.6236              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2257 T22:   0.1838                                     
REMARK   3      T33:   0.1000 T12:  -0.0066                                     
REMARK   3      T13:  -0.0301 T23:  -0.0226                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0775 L22:   2.2398                                     
REMARK   3      L33:   1.3010 L12:   0.6477                                     
REMARK   3      L13:   1.2201 L23:  -1.0173                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0250 S12:   0.5092 S13:  -0.0071                       
REMARK   3      S21:  -0.4030 S22:   0.0021 S23:  -0.0248                       
REMARK   3      S31:   0.0677 S32:   0.0412 S33:   0.0596                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1244 THROUGH 1266 )               
REMARK   3    ORIGIN FOR THE GROUP (A): -20.0299 -17.7096 -10.2927              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3547 T22:   0.2490                                     
REMARK   3      T33:   0.2596 T12:   0.0787                                     
REMARK   3      T13:  -0.1632 T23:  -0.0336                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8521 L22:   4.6916                                     
REMARK   3      L33:   3.6459 L12:  -2.9928                                     
REMARK   3      L13:  -1.1774 L23:   1.9211                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1186 S12:  -0.0854 S13:   0.1402                       
REMARK   3      S21:  -0.4340 S22:  -0.1905 S23:   0.2795                       
REMARK   3      S31:  -0.9738 S32:  -0.4570 S33:   0.2653                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1006 THROUGH 1023 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  11.7971 -37.9847  28.2724              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2242 T22:   0.1377                                     
REMARK   3      T33:   0.2722 T12:   0.0048                                     
REMARK   3      T13:  -0.0168 T23:  -0.0099                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.0666 L22:   2.6423                                     
REMARK   3      L33:   7.0739 L12:  -3.3245                                     
REMARK   3      L13:   2.8789 L23:  -3.4621                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0263 S12:   0.0151 S13:  -0.4518                       
REMARK   3      S21:   0.2221 S22:   0.0021 S23:  -0.0326                       
REMARK   3      S31:   0.5435 S32:   0.1229 S33:   0.0383                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1024 THROUGH 1042 )               
REMARK   3    ORIGIN FOR THE GROUP (A):   8.3066 -38.9195  36.6886              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2360 T22:   0.1576                                     
REMARK   3      T33:   0.2699 T12:  -0.0161                                     
REMARK   3      T13:  -0.0177 T23:   0.0484                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3416 L22:   2.6979                                     
REMARK   3      L33:   1.1639 L12:  -2.3246                                     
REMARK   3      L13:   1.3395 L23:  -0.4629                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0850 S12:  -0.3342 S13:  -0.5642                       
REMARK   3      S21:   0.1488 S22:   0.0038 S23:  -0.0197                       
REMARK   3      S31:   0.3902 S32:  -0.0701 S33:  -0.1083                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1043 THROUGH 1058 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.7497 -15.4302  26.6126              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1503 T22:   0.1627                                     
REMARK   3      T33:   0.2296 T12:   0.0038                                     
REMARK   3      T13:  -0.0008 T23:  -0.0269                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5423 L22:   4.1267                                     
REMARK   3      L33:   5.0493 L12:  -1.3184                                     
REMARK   3      L13:   1.5159 L23:  -4.5817                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0227 S12:  -0.0967 S13:   0.0203                       
REMARK   3      S21:   0.3308 S22:  -0.0044 S23:   0.4141                       
REMARK   3      S31:  -0.3134 S32:  -0.0471 S33:  -0.0948                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1059 THROUGH 1127 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  13.1561  -8.9847  21.8109              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1195 T22:   0.1251                                     
REMARK   3      T33:   0.1353 T12:  -0.0361                                     
REMARK   3      T13:   0.0020 T23:   0.0035                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9892 L22:   2.4299                                     
REMARK   3      L33:   2.1992 L12:  -0.0471                                     
REMARK   3      L13:   0.3067 L23:  -0.4493                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0801 S12:   0.0736 S13:   0.1427                       
REMARK   3      S21:  -0.1332 S22:   0.0519 S23:  -0.1114                       
REMARK   3      S31:  -0.1435 S32:   0.1622 S33:   0.0255                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1128 THROUGH 1150 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  18.6781 -31.4815  37.0766              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1148 T22:   0.1628                                     
REMARK   3      T33:   0.2387 T12:   0.0285                                     
REMARK   3      T13:  -0.0632 T23:   0.0435                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4886 L22:   5.4281                                     
REMARK   3      L33:   1.7431 L12:   2.0638                                     
REMARK   3      L13:  -1.4617 L23:  -0.7731                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0110 S12:  -0.2540 S13:  -0.3230                       
REMARK   3      S21:   0.2964 S22:  -0.1823 S23:  -0.5736                       
REMARK   3      S31:   0.2094 S32:   0.3204 S33:   0.2098                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1151 THROUGH 1167 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.2915 -21.0856  37.2626              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1322 T22:   0.1578                                     
REMARK   3      T33:   0.1435 T12:   0.0079                                     
REMARK   3      T13:   0.0148 T23:   0.0066                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.8009 L22:   2.4022                                     
REMARK   3      L33:   3.0428 L12:   0.2374                                     
REMARK   3      L13:  -1.9954 L23:  -0.0447                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0180 S12:  -0.3726 S13:  -0.0175                       
REMARK   3      S21:   0.2911 S22:  -0.0299 S23:   0.2981                       
REMARK   3      S31:  -0.0415 S32:  -0.2343 S33:   0.0480                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1168 THROUGH 1198 )               
REMARK   3    ORIGIN FOR THE GROUP (A):   0.2723 -23.8946  40.1497              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1303 T22:   0.2146                                     
REMARK   3      T33:   0.1305 T12:  -0.0361                                     
REMARK   3      T13:   0.0085 T23:   0.0386                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3078 L22:   5.2744                                     
REMARK   3      L33:   5.2483 L12:   0.0330                                     
REMARK   3      L13:  -1.4035 L23:   0.9554                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0340 S12:  -0.5754 S13:  -0.1866                       
REMARK   3      S21:   0.4433 S22:  -0.0032 S23:   0.2707                       
REMARK   3      S31:  -0.0057 S32:  -0.2620 S33:   0.0149                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1199 THROUGH 1212 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  14.8633 -19.1306  40.3156              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0955 T22:   0.1607                                     
REMARK   3      T33:   0.1380 T12:  -0.0171                                     
REMARK   3      T13:  -0.0229 T23:  -0.0094                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8026 L22:   3.9082                                     
REMARK   3      L33:   6.6406 L12:  -0.6758                                     
REMARK   3      L13:   1.2049 L23:  -2.9807                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0402 S12:  -0.3175 S13:   0.0337                       
REMARK   3      S21:   0.3920 S22:  -0.0298 S23:  -0.3107                       
REMARK   3      S31:  -0.0888 S32:   0.2149 S33:   0.0879                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1213 THROUGH 1243 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  11.4017 -17.9087  34.0518              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0793 T22:   0.0933                                     
REMARK   3      T33:   0.1194 T12:  -0.0113                                     
REMARK   3      T13:  -0.0158 T23:   0.0039                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6441 L22:   1.7679                                     
REMARK   3      L33:   2.0061 L12:   0.2926                                     
REMARK   3      L13:   0.1275 L23:  -0.0924                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0346 S12:  -0.1330 S13:  -0.1168                       
REMARK   3      S21:   0.2000 S22:   0.0165 S23:  -0.1295                       
REMARK   3      S31:  -0.0680 S32:   0.0765 S33:   0.0138                       
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1244 THROUGH 1266 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  12.2853 -22.0596  53.1193              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3422 T22:   0.4505                                     
REMARK   3      T33:   0.1458 T12:   0.0092                                     
REMARK   3      T13:  -0.0661 T23:   0.0370                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.9487 L22:   2.1237                                     
REMARK   3      L33:   3.0615 L12:   0.7931                                     
REMARK   3      L13:  -0.8865 L23:   0.2375                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0904 S12:  -1.4513 S13:  -0.1854                       
REMARK   3      S21:   0.6184 S22:  -0.1678 S23:  -0.1636                       
REMARK   3      S31:  -0.0801 S32:  -0.0525 S33:   0.0812                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5TUZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-NOV-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000224865.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-APR-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 9.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-C                            
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                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 54301                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.950                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 74.940                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 6.800                              
REMARK 200  R MERGE                    (I) : 0.14600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.06                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.65500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 3HNA                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.51                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.04                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 20,000, 2% (V/V) 1,4-DIOXANE,    
REMARK 280  0.1 M BICINE (PH 9.0), VAPOR DIFFUSION, TEMPERATURE 290K            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       37.47000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       51.18000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       47.89000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       51.18000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       37.47000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       47.89000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2510 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23920 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 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     LYS A  1180                                                      
REMARK 465     ASP A  1181                                                      
REMARK 465     ASN B  1179                                                      
REMARK 465     LYS B  1180                                                      
REMARK 465     ASP B  1181                                                      
REMARK 465     GLY B  1182                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A1013      102.44   -166.89                                   
REMARK 500    THR A1047      -87.74   -101.36                                   
REMARK 500    ASP A1066     -148.01   -119.65                                   
REMARK 500    MET A1080      -56.92     80.88                                   
REMARK 500    GLU A1098       67.47   -154.63                                   
REMARK 500    ASN A1117       46.97    -95.04                                   
REMARK 500    VAL A1119      -60.99   -139.11                                   
REMARK 500    ASN A1194     -160.26   -105.84                                   
REMARK 500    MET A1214      -90.99   -131.07                                   
REMARK 500    ASP B1013      107.55   -171.13                                   
REMARK 500    ASP B1030     -159.35   -148.03                                   
REMARK 500    ASN B1037       31.12    -91.92                                   
REMARK 500    THR B1047      -87.47   -104.21                                   
REMARK 500    ASP B1066     -149.65   -109.48                                   
REMARK 500    MET B1080      -47.51     77.29                                   
REMARK 500    GLU B1098       77.67   -151.47                                   
REMARK 500    ASN B1117       46.86    -94.00                                   
REMARK 500    VAL B1119      -59.37   -137.82                                   
REMARK 500    ASN B1194     -162.08   -107.12                                   
REMARK 500    MET B1214      -94.68   -130.39                                   
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 A3004  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1062   SG                                                     
REMARK 620 2 CYS A1064   SG  107.6                                              
REMARK 620 3 CYS A1068   SG  106.3 105.3                                        
REMARK 620 4 CYS A1073   SG  111.6 106.7 118.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A3002  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1062   SG                                                     
REMARK 620 2 CYS A1075   SG  114.1                                              
REMARK 620 3 CYS A1105   SG  106.4 111.9                                        
REMARK 620 4 CYS A1109   SG  108.8  97.0 118.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A3003  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1068   SG                                                     
REMARK 620 2 CYS A1105   SG  110.8                                              
REMARK 620 3 CYS A1111   SG  105.2 108.8                                        
REMARK 620 4 CYS A1115   SG  112.7 106.7 112.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A3005  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1203   SG                                                     
REMARK 620 2 CYS A1256   SG  117.8                                              
REMARK 620 3 CYS A1258   SG  108.8 103.8                                        
REMARK 620 4 CYS A1263   SG  103.5 106.4 117.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B3004  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B1062   SG                                                     
REMARK 620 2 CYS B1064   SG  107.6                                              
REMARK 620 3 CYS B1068   SG  106.8 107.9                                        
REMARK 620 4 CYS B1073   SG  113.4 104.4 116.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B3002  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B1062   SG                                                     
REMARK 620 2 CYS B1075   SG  117.1                                              
REMARK 620 3 CYS B1105   SG  108.9 110.3                                        
REMARK 620 4 CYS B1109   SG  104.8  97.0 118.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B3003  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B1068   SG                                                     
REMARK 620 2 CYS B1105   SG  111.0                                              
REMARK 620 3 CYS B1111   SG  106.2 106.3                                        
REMARK 620 4 CYS B1115   SG  113.1 105.6 114.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B3005  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B1203   SG                                                     
REMARK 620 2 CYS B1256   SG  115.2                                              
REMARK 620 3 CYS B1258   SG  107.6 106.1                                        
REMARK 620 4 CYS B1263   SG  105.6 108.2 114.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAM A 3001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 3002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 3003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 3004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 3005                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 7L6 A 3006                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 3007                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAM B 3001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 3002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 3003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 3004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 3005                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 7L6 B 3006                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 3007                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5TUY   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN G9A SET-DOMAIN (EHMT2) IN COMPLEX WITH INHIBITOR  
REMARK 900 MS0124                                                               
DBREF  5TUZ A 1006  1266  UNP    Q9H9B1   EHMT1_HUMAN   1006   1266             
DBREF  5TUZ B 1006  1266  UNP    Q9H9B1   EHMT1_HUMAN   1006   1266             
SEQRES   1 A  261  VAL GLU ARG ILE VAL SER ARG ASP ILE ALA ARG GLY TYR          
SEQRES   2 A  261  GLU ARG ILE PRO ILE PRO CYS VAL ASN ALA VAL ASP SER          
SEQRES   3 A  261  GLU PRO CYS PRO SER ASN TYR LYS TYR VAL SER GLN ASN          
SEQRES   4 A  261  CYS VAL THR SER PRO MET ASN ILE ASP ARG ASN ILE THR          
SEQRES   5 A  261  HIS LEU GLN TYR CYS VAL CYS ILE ASP ASP CYS SER SER          
SEQRES   6 A  261  SER ASN CYS MET CYS GLY GLN LEU SER MET ARG CYS TRP          
SEQRES   7 A  261  TYR ASP LYS ASP GLY ARG LEU LEU PRO GLU PHE ASN MET          
SEQRES   8 A  261  ALA GLU PRO PRO LEU ILE PHE GLU CYS ASN HIS ALA CYS          
SEQRES   9 A  261  SER CYS TRP ARG ASN CYS ARG ASN ARG VAL VAL GLN ASN          
SEQRES  10 A  261  GLY LEU ARG ALA ARG LEU GLN LEU TYR ARG THR ARG ASP          
SEQRES  11 A  261  MET GLY TRP GLY VAL ARG SER LEU GLN ASP ILE PRO PRO          
SEQRES  12 A  261  GLY THR PHE VAL CYS GLU TYR VAL GLY GLU LEU ILE SER          
SEQRES  13 A  261  ASP SER GLU ALA ASP VAL ARG GLU GLU ASP SER TYR LEU          
SEQRES  14 A  261  PHE ASP LEU ASP ASN LYS ASP GLY GLU VAL TYR CYS ILE          
SEQRES  15 A  261  ASP ALA ARG PHE TYR GLY ASN VAL SER ARG PHE ILE ASN          
SEQRES  16 A  261  HIS HIS CYS GLU PRO ASN LEU VAL PRO VAL ARG VAL PHE          
SEQRES  17 A  261  MET ALA HIS GLN ASP LEU ARG PHE PRO ARG ILE ALA PHE          
SEQRES  18 A  261  PHE SER THR ARG LEU ILE GLU ALA GLY GLU GLN LEU GLY          
SEQRES  19 A  261  PHE ASP TYR GLY GLU ARG PHE TRP ASP ILE LYS GLY LYS          
SEQRES  20 A  261  LEU PHE SER CYS ARG CYS GLY SER PRO LYS CYS ARG HIS          
SEQRES  21 A  261  SER                                                          
SEQRES   1 B  261  VAL GLU ARG ILE VAL SER ARG ASP ILE ALA ARG GLY TYR          
SEQRES   2 B  261  GLU ARG ILE PRO ILE PRO CYS VAL ASN ALA VAL ASP SER          
SEQRES   3 B  261  GLU PRO CYS PRO SER ASN TYR LYS TYR VAL SER GLN ASN          
SEQRES   4 B  261  CYS VAL THR SER PRO MET ASN ILE ASP ARG ASN ILE THR          
SEQRES   5 B  261  HIS LEU GLN TYR CYS VAL CYS ILE ASP ASP CYS SER SER          
SEQRES   6 B  261  SER ASN CYS MET CYS GLY GLN LEU SER MET ARG CYS TRP          
SEQRES   7 B  261  TYR ASP LYS ASP GLY ARG LEU LEU PRO GLU PHE ASN MET          
SEQRES   8 B  261  ALA GLU PRO PRO LEU ILE PHE GLU CYS ASN HIS ALA CYS          
SEQRES   9 B  261  SER CYS TRP ARG ASN CYS ARG ASN ARG VAL VAL GLN ASN          
SEQRES  10 B  261  GLY LEU ARG ALA ARG LEU GLN LEU TYR ARG THR ARG ASP          
SEQRES  11 B  261  MET GLY TRP GLY VAL ARG SER LEU GLN ASP ILE PRO PRO          
SEQRES  12 B  261  GLY THR PHE VAL CYS GLU TYR VAL GLY GLU LEU ILE SER          
SEQRES  13 B  261  ASP SER GLU ALA ASP VAL ARG GLU GLU ASP SER TYR LEU          
SEQRES  14 B  261  PHE ASP LEU ASP ASN LYS ASP GLY GLU VAL TYR CYS ILE          
SEQRES  15 B  261  ASP ALA ARG PHE TYR GLY ASN VAL SER ARG PHE ILE ASN          
SEQRES  16 B  261  HIS HIS CYS GLU PRO ASN LEU VAL PRO VAL ARG VAL PHE          
SEQRES  17 B  261  MET ALA HIS GLN ASP LEU ARG PHE PRO ARG ILE ALA PHE          
SEQRES  18 B  261  PHE SER THR ARG LEU ILE GLU ALA GLY GLU GLN LEU GLY          
SEQRES  19 B  261  PHE ASP TYR GLY GLU ARG PHE TRP ASP ILE LYS GLY LYS          
SEQRES  20 B  261  LEU PHE SER CYS ARG CYS GLY SER PRO LYS CYS ARG HIS          
SEQRES  21 B  261  SER                                                          
HET    SAM  A3001      27                                                       
HET     ZN  A3002       1                                                       
HET     ZN  A3003       1                                                       
HET     ZN  A3004       1                                                       
HET     ZN  A3005       1                                                       
HET    7L6  A3006      28                                                       
HET    EDO  A3007       4                                                       
HET    SAM  B3001      27                                                       
HET     ZN  B3002       1                                                       
HET     ZN  B3003       1                                                       
HET     ZN  B3004       1                                                       
HET     ZN  B3005       1                                                       
HET    7L6  B3006      28                                                       
HET    EDO  B3007       4                                                       
HETNAM     SAM S-ADENOSYLMETHIONINE                                             
HETNAM      ZN ZINC ION                                                         
HETNAM     7L6 6,7-DIMETHOXY-N-(1-METHYLPIPERIDIN-4-YL)-2-(MORPHOLIN-           
HETNAM   2 7L6  4-YL)QUINAZOLIN-4-AMINE                                         
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3  SAM    2(C15 H22 N6 O5 S)                                           
FORMUL   4   ZN    8(ZN 2+)                                                     
FORMUL   8  7L6    2(C20 H29 N5 O3)                                             
FORMUL   9  EDO    2(C2 H6 O2)                                                  
FORMUL  17  HOH   *340(H2 O)                                                    
HELIX    1 AA1 ASN A 1055  LEU A 1059  5                                   5    
HELIX    2 AA2 CYS A 1073  SER A 1079  1                                   7    
HELIX    3 AA3 VAL A 1119  GLY A 1123  5                                   5    
HELIX    4 AA4 ASP A 1162  ASP A 1166  1                                   5    
HELIX    5 AA5 VAL A 1195  ILE A 1199  5                                   5    
HELIX    6 AA6 GLY A 1243  GLY A 1251  1                                   9    
HELIX    7 AA7 ASN B 1055  LEU B 1059  5                                   5    
HELIX    8 AA8 CYS B 1073  SER B 1079  1                                   7    
HELIX    9 AA9 VAL B 1119  GLY B 1123  5                                   5    
HELIX   10 AB1 ASP B 1162  ASP B 1166  1                                   5    
HELIX   11 AB2 VAL B 1195  ILE B 1199  5                                   5    
HELIX   12 AB3 GLY B 1243  GLY B 1251  1                                   9    
SHEET    1 AA1 4 ARG A1008  SER A1011  0                                        
SHEET    2 AA1 4 CYS A1025  ASN A1027 -1  O  CYS A1025   N  SER A1011           
SHEET    3 AA1 4 LEU A1128  ARG A1132  1  O  LEU A1130   N  VAL A1026           
SHEET    4 AA1 4 TRP A1138  SER A1142 -1  O  GLY A1139   N  TYR A1131           
SHEET    1 AA2 3 LYS A1039  TYR A1040  0                                        
SHEET    2 AA2 3 TYR A1185  GLY A1193  1  O  PHE A1191   N  LYS A1039           
SHEET    3 AA2 3 GLY A1157  SER A1161 -1  N  ILE A1160   O  CYS A1186           
SHEET    1 AA3 3 LYS A1039  TYR A1040  0                                        
SHEET    2 AA3 3 TYR A1185  GLY A1193  1  O  PHE A1191   N  LYS A1039           
SHEET    3 AA3 3 LEU A1174  LEU A1177 -1  N  LEU A1177   O  TYR A1185           
SHEET    1 AA4 4 ILE A1102  PHE A1103  0                                        
SHEET    2 AA4 4 LEU A1207  PHE A1213  1  O  PHE A1213   N  ILE A1102           
SHEET    3 AA4 4 ARG A1223  SER A1228 -1  O  ALA A1225   N  VAL A1210           
SHEET    4 AA4 4 PHE A1151  TYR A1155 -1  N  CYS A1153   O  PHE A1226           
SHEET    1 AA5 2 ASN A1200  HIS A1201  0                                        
SHEET    2 AA5 2 GLY A1239  PHE A1240  1  O  PHE A1240   N  ASN A1200           
SHEET    1 AA6 4 ARG B1008  SER B1011  0                                        
SHEET    2 AA6 4 CYS B1025  ASN B1027 -1  O  CYS B1025   N  VAL B1010           
SHEET    3 AA6 4 LEU B1128  ARG B1132  1  O  LEU B1130   N  VAL B1026           
SHEET    4 AA6 4 TRP B1138  SER B1142 -1  O  GLY B1139   N  TYR B1131           
SHEET    1 AA7 3 LYS B1039  TYR B1040  0                                        
SHEET    2 AA7 3 TYR B1185  GLY B1193  1  O  PHE B1191   N  LYS B1039           
SHEET    3 AA7 3 GLY B1157  SER B1161 -1  N  GLU B1158   O  ASP B1188           
SHEET    1 AA8 3 LYS B1039  TYR B1040  0                                        
SHEET    2 AA8 3 TYR B1185  GLY B1193  1  O  PHE B1191   N  LYS B1039           
SHEET    3 AA8 3 LEU B1174  LEU B1177 -1  N  LEU B1177   O  TYR B1185           
SHEET    1 AA9 4 ILE B1102  PHE B1103  0                                        
SHEET    2 AA9 4 LEU B1207  PHE B1213  1  O  PHE B1213   N  ILE B1102           
SHEET    3 AA9 4 ARG B1223  SER B1228 -1  O  ALA B1225   N  VAL B1210           
SHEET    4 AA9 4 PHE B1151  TYR B1155 -1  N  CYS B1153   O  PHE B1226           
SHEET    1 AB1 2 ASN B1200  HIS B1201  0                                        
SHEET    2 AB1 2 GLY B1239  PHE B1240  1  O  PHE B1240   N  ASN B1200           
LINK         SG  CYS A1062                ZN    ZN A3004     1555   1555  2.35  
LINK         SG  CYS A1062                ZN    ZN A3002     1555   1555  2.41  
LINK         SG  CYS A1064                ZN    ZN A3004     1555   1555  2.36  
LINK         SG  CYS A1068                ZN    ZN A3004     1555   1555  2.32  
LINK         SG  CYS A1068                ZN    ZN A3003     1555   1555  2.38  
LINK         SG  CYS A1073                ZN    ZN A3004     1555   1555  2.33  
LINK         SG  CYS A1075                ZN    ZN A3002     1555   1555  2.35  
LINK         SG  CYS A1105                ZN    ZN A3002     1555   1555  2.31  
LINK         SG  CYS A1105                ZN    ZN A3003     1555   1555  2.33  
LINK         SG  CYS A1109                ZN    ZN A3002     1555   1555  2.32  
LINK         SG  CYS A1111                ZN    ZN A3003     1555   1555  2.29  
LINK         SG  CYS A1115                ZN    ZN A3003     1555   1555  2.31  
LINK         SG  CYS A1203                ZN    ZN A3005     1555   1555  2.34  
LINK         SG  CYS A1256                ZN    ZN A3005     1555   1555  2.28  
LINK         SG  CYS A1258                ZN    ZN A3005     1555   1555  2.31  
LINK         SG  CYS A1263                ZN    ZN A3005     1555   1555  2.38  
LINK         SG  CYS B1062                ZN    ZN B3004     1555   1555  2.36  
LINK         SG  CYS B1062                ZN    ZN B3002     1555   1555  2.43  
LINK         SG  CYS B1064                ZN    ZN B3004     1555   1555  2.37  
LINK         SG  CYS B1068                ZN    ZN B3003     1555   1555  2.30  
LINK         SG  CYS B1068                ZN    ZN B3004     1555   1555  2.32  
LINK         SG  CYS B1073                ZN    ZN B3004     1555   1555  2.35  
LINK         SG  CYS B1075                ZN    ZN B3002     1555   1555  2.30  
LINK         SG  CYS B1105                ZN    ZN B3003     1555   1555  2.39  
LINK         SG  CYS B1105                ZN    ZN B3002     1555   1555  2.36  
LINK         SG  CYS B1109                ZN    ZN B3002     1555   1555  2.35  
LINK         SG  CYS B1111                ZN    ZN B3003     1555   1555  2.32  
LINK         SG  CYS B1115                ZN    ZN B3003     1555   1555  2.32  
LINK         SG  CYS B1203                ZN    ZN B3005     1555   1555  2.39  
LINK         SG  CYS B1256                ZN    ZN B3005     1555   1555  2.27  
LINK         SG  CYS B1258                ZN    ZN B3005     1555   1555  2.33  
LINK         SG  CYS B1263                ZN    ZN B3005     1555   1555  2.40  
SITE     1 AC1 16 MET A1136  GLY A1137  TRP A1138  SER A1172                    
SITE     2 AC1 16 TYR A1173  ARG A1197  ASN A1200  HIS A1201                    
SITE     3 AC1 16 TYR A1242  PHE A1246  CYS A1256  ARG A1257                    
SITE     4 AC1 16 HOH A3110  HOH A3191  HOH A3201  HOH A3209                    
SITE     1 AC2  4 CYS A1062  CYS A1075  CYS A1105  CYS A1109                    
SITE     1 AC3  4 CYS A1068  CYS A1105  CYS A1111  CYS A1115                    
SITE     1 AC4  4 CYS A1062  CYS A1064  CYS A1068  CYS A1073                    
SITE     1 AC5  4 CYS A1203  CYS A1256  CYS A1258  CYS A1263                    
SITE     1 AC6 11 ASP A1162  ALA A1165  ASP A1166  ARG A1168                    
SITE     2 AC6 11 ASP A1171  LEU A1174  ASP A1176  CYS A1186                    
SITE     3 AC6 11 ARG A1245  PHE A1246  ILE A1249                               
SITE     1 AC7  6 CYS A1064  ILE A1065  ASP A1066  ASN A1072                    
SITE     2 AC7  6 LEU B1078  PHE B1103                                          
SITE     1 AC8 16 MET B1136  GLY B1137  TRP B1138  SER B1172                    
SITE     2 AC8 16 TYR B1173  ARG B1197  ASN B1200  HIS B1201                    
SITE     3 AC8 16 TYR B1242  PHE B1246  CYS B1256  ARG B1257                    
SITE     4 AC8 16 HOH B3164  HOH B3167  HOH B3172  HOH B3179                    
SITE     1 AC9  4 CYS B1062  CYS B1075  CYS B1105  CYS B1109                    
SITE     1 AD1  4 CYS B1068  CYS B1105  CYS B1111  CYS B1115                    
SITE     1 AD2  4 CYS B1062  CYS B1064  CYS B1068  CYS B1073                    
SITE     1 AD3  4 CYS B1203  CYS B1256  CYS B1258  CYS B1263                    
SITE     1 AD4 12 ASP B1162  ALA B1165  ASP B1166  ARG B1168                    
SITE     2 AD4 12 ASP B1171  LEU B1174  ASP B1176  CYS B1186                    
SITE     3 AD4 12 ARG B1245  PHE B1246  ILE B1249  LYS B1250                    
SITE     1 AD5  2 ARG A1054  ARG B1054                                          
CRYST1   74.940   95.780  102.360  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013344  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010441  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009769        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system