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Database: PDB
Entry: 5VSD
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HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       11-MAY-17   5VSD              
TITLE     STRUCTURE OF HUMAN GLP SET-DOMAIN (EHMT1) IN COMPLEX WITH INHIBITOR 13
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE EHMT1;                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: GLP CATALYTIC SET-DOMAIN RESIDUES 1006-1266;               
COMPND   5 SYNONYM: EUCHROMATIC HISTONE-LYSINE N-METHYLTRANSFERASE 1,EU-HMTASE1,
COMPND   6 G9A-LIKE PROTEIN 1,GLP1,HISTONE H3-K9 METHYLTRANSFERASE 5,H3-K9-     
COMPND   7 HMTASE 5,LYSINE N-METHYLTRANSFERASE 1D;                              
COMPND   8 EC: 2.1.1.-,2.1.1.43;                                                
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: EHMT1, EUHMTASE1, GLP, KIAA1876, KMT1D;                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) CODON PLUS RIL;                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A-LIC                                
KEYWDS    PROTEIN-SMALL MOLECULE INHIBITOR COMPLEX, TRANSFERASE-TRANSFERASE     
KEYWDS   2 INHIBITOR COMPLEX                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.BABAULT,Y.XIONG,J.LIU,J.JIN                                         
REVDAT   2   02-AUG-17 5VSD    1       JRNL                                     
REVDAT   1   12-JUL-17 5VSD    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.    1.85 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) : 1.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.91                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 62809                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.194                           
REMARK   3   R VALUE            (WORKING SET) : 0.192                           
REMARK   3   FREE R VALUE                     : 0.235                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.160                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3238                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 19.9068 -  5.2306    1.00     2809   172  0.1571 0.1682        
REMARK   3     2  5.2306 -  4.1641    0.93     2529   120  0.1235 0.1627        
REMARK   3     3  4.1641 -  3.6414    0.93     2487   148  0.1439 0.1565        
REMARK   3     4  3.6414 -  3.3101    0.94     2516   120  0.1577 0.2045        
REMARK   3     5  3.3101 -  3.0738    0.93     2497   126  0.1753 0.2197        
REMARK   3     6  3.0738 -  2.8931    0.96     2559   123  0.1726 0.1976        
REMARK   3     7  2.8931 -  2.7486    0.98     2566   148  0.1752 0.2175        
REMARK   3     8  2.7486 -  2.6293    0.99     2607   153  0.1840 0.2342        
REMARK   3     9  2.6293 -  2.5283    1.00     2654   142  0.1906 0.2779        
REMARK   3    10  2.5283 -  2.4412    1.00     2596   144  0.2129 0.2714        
REMARK   3    11  2.4412 -  2.3650    1.00     2616   146  0.2579 0.3394        
REMARK   3    12  2.3650 -  2.2975    1.00     2626   141  0.2575 0.3090        
REMARK   3    13  2.2975 -  2.2371    1.00     2615   135  0.2552 0.3303        
REMARK   3    14  2.2371 -  2.1826    0.99     2588   138  0.2688 0.3098        
REMARK   3    15  2.1826 -  2.1330    1.00     2624   137  0.2847 0.3407        
REMARK   3    16  2.1330 -  2.0877    0.99     2585   164  0.2767 0.3346        
REMARK   3    17  2.0877 -  2.0459    1.00     2562   150  0.2705 0.3243        
REMARK   3    18  2.0459 -  2.0074    0.99     2577   163  0.2665 0.2749        
REMARK   3    19  2.0074 -  1.9715    1.00     2571   136  0.2512 0.3511        
REMARK   3    20  1.9715 -  1.9382    0.99     2626   152  0.2447 0.3233        
REMARK   3    21  1.9382 -  1.9069    0.99     2595   122  0.2406 0.2757        
REMARK   3    22  1.9069 -  1.8776    0.99     2575   137  0.2774 0.3108        
REMARK   3    23  1.8776 -  1.8500    0.99     2591   121  0.2941 0.3566        
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)     : 0.250            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.750           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 24.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.28                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.007           4398                                  
REMARK   3   ANGLE     :  1.154           5951                                  
REMARK   3   CHIRALITY :  0.073            612                                  
REMARK   3   PLANARITY :  0.006            779                                  
REMARK   3   DIHEDRAL  : 13.720           2635                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 13                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1006 THROUGH 1042 )               
REMARK   3    ORIGIN FOR THE GROUP (A):   4.4004 -12.6153  -1.2694              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3295 T22:   0.3223                                     
REMARK   3      T33:   0.2506 T12:  -0.1811                                     
REMARK   3      T13:  -0.0328 T23:   0.0085                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5591 L22:   1.9551                                     
REMARK   3      L33:   5.9324 L12:  -0.2590                                     
REMARK   3      L13:  -0.6324 L23:  -1.1211                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1759 S12:   0.3108 S13:   0.2660                       
REMARK   3      S21:  -0.3480 S22:   0.1169 S23:  -0.0863                       
REMARK   3      S31:  -0.4937 S32:   0.6288 S33:   0.0521                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1043 THROUGH 1089 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.4904 -35.0497  17.2189              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1555 T22:   0.2347                                     
REMARK   3      T33:   0.2778 T12:  -0.0000                                     
REMARK   3      T13:  -0.0312 T23:   0.0161                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6195 L22:   2.3092                                     
REMARK   3      L33:   1.2371 L12:  -0.1881                                     
REMARK   3      L13:  -0.0332 L23:  -0.4627                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0430 S12:  -0.0484 S13:  -0.1257                       
REMARK   3      S21:  -0.0902 S22:  -0.0358 S23:   0.2582                       
REMARK   3      S31:   0.1263 S32:  -0.0543 S33:   0.0248                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1090 THROUGH 1137 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.2463 -31.3043   6.2805              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1415 T22:   0.1652                                     
REMARK   3      T33:   0.1824 T12:  -0.0167                                     
REMARK   3      T13:  -0.0255 T23:  -0.0173                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9737 L22:   2.1385                                     
REMARK   3      L33:   2.6044 L12:   0.1671                                     
REMARK   3      L13:   0.1198 L23:  -0.9665                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0188 S12:   0.1154 S13:  -0.0469                       
REMARK   3      S21:  -0.1858 S22:  -0.0137 S23:   0.0525                       
REMARK   3      S31:   0.0004 S32:   0.2215 S33:   0.0270                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1138 THROUGH 1167 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.4430 -20.8111   2.5706              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1490 T22:   0.2061                                     
REMARK   3      T33:   0.1620 T12:   0.0051                                     
REMARK   3      T13:  -0.0500 T23:  -0.0006                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6731 L22:   3.0111                                     
REMARK   3      L33:   2.7597 L12:   0.1422                                     
REMARK   3      L13:  -0.0913 L23:   0.8961                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0626 S12:   0.0796 S13:   0.0525                       
REMARK   3      S21:  -0.1090 S22:  -0.0299 S23:   0.0116                       
REMARK   3      S31:  -0.2309 S32:  -0.0698 S33:   0.1067                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1168 THROUGH 1184 )               
REMARK   3    ORIGIN FOR THE GROUP (A): -17.8581 -14.4740   5.7020              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2008 T22:   0.2691                                     
REMARK   3      T33:   0.2175 T12:   0.0805                                     
REMARK   3      T13:  -0.0738 T23:  -0.0186                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.8039 L22:   7.8274                                     
REMARK   3      L33:   5.5100 L12:  -1.7005                                     
REMARK   3      L13:   0.0687 L23:   1.6632                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0385 S12:  -0.0638 S13:   0.1251                       
REMARK   3      S21:   0.1352 S22:   0.0557 S23:   0.4479                       
REMARK   3      S31:  -0.5926 S32:  -0.7630 S33:  -0.0611                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1185 THROUGH 1266 )               
REMARK   3    ORIGIN FOR THE GROUP (A): -12.7930 -22.0170  -1.1434              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1846 T22:   0.1822                                     
REMARK   3      T33:   0.2109 T12:   0.0060                                     
REMARK   3      T13:  -0.0401 T23:   0.0024                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6880 L22:   0.6373                                     
REMARK   3      L33:   3.0814 L12:   0.2018                                     
REMARK   3      L13:   0.5463 L23:   0.3398                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0861 S12:   0.0742 S13:   0.0295                       
REMARK   3      S21:  -0.1831 S22:   0.0665 S23:   0.1148                       
REMARK   3      S31:  -0.2629 S32:  -0.1334 S33:   0.0127                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1006 THROUGH 1023 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  11.7351 -38.1615  28.3478              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1867 T22:   0.1907                                     
REMARK   3      T33:   0.2744 T12:   0.0266                                     
REMARK   3      T13:  -0.0067 T23:   0.0039                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1247 L22:   7.4292                                     
REMARK   3      L33:   7.6138 L12:  -2.8292                                     
REMARK   3      L13:   2.1060 L23:  -3.3498                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0734 S12:  -0.0655 S13:  -0.4719                       
REMARK   3      S21:   0.2326 S22:  -0.0201 S23:  -0.2889                       
REMARK   3      S31:   0.4059 S32:   0.1631 S33:   0.0630                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1024 THROUGH 1058 )               
REMARK   3    ORIGIN FOR THE GROUP (A):   1.1851 -28.0942  31.9724              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1748 T22:   0.2161                                     
REMARK   3      T33:   0.2584 T12:  -0.0073                                     
REMARK   3      T13:   0.0024 T23:   0.0249                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0804 L22:   1.2754                                     
REMARK   3      L33:   0.8688 L12:  -0.4085                                     
REMARK   3      L13:   0.5151 L23:  -0.3323                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0491 S12:  -0.1034 S13:  -0.1895                       
REMARK   3      S21:  -0.0013 S22:  -0.0157 S23:   0.0641                       
REMARK   3      S31:   0.1218 S32:  -0.0319 S33:  -0.0631                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1059 THROUGH 1127 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  13.1133  -9.1599  21.8956              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1725 T22:   0.1811                                     
REMARK   3      T33:   0.2014 T12:  -0.0342                                     
REMARK   3      T13:   0.0104 T23:   0.0041                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3747 L22:   2.3936                                     
REMARK   3      L33:   2.6137 L12:  -0.0976                                     
REMARK   3      L13:  -0.1259 L23:  -0.2658                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0383 S12:   0.0281 S13:   0.1987                       
REMARK   3      S21:  -0.1206 S22:   0.0208 S23:  -0.1437                       
REMARK   3      S31:  -0.2451 S32:   0.2061 S33:   0.0188                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1128 THROUGH 1150 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  18.5130 -31.6033  37.2785              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1258 T22:   0.2554                                     
REMARK   3      T33:   0.2636 T12:   0.0318                                     
REMARK   3      T13:  -0.0452 T23:   0.0642                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8956 L22:   4.9257                                     
REMARK   3      L33:   1.1362 L12:   1.8837                                     
REMARK   3      L13:  -1.1712 L23:  -0.4580                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0160 S12:  -0.3650 S13:  -0.2997                       
REMARK   3      S21:   0.2168 S22:  -0.1973 S23:  -0.4202                       
REMARK   3      S31:   0.1574 S32:   0.3417 S33:   0.2409                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1151 THROUGH 1184 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.8033 -20.9002  40.0412              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2161 T22:   0.2409                                     
REMARK   3      T33:   0.2210 T12:   0.0269                                     
REMARK   3      T13:   0.0138 T23:   0.0120                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.6336 L22:   2.3262                                     
REMARK   3      L33:   5.1862 L12:  -0.8038                                     
REMARK   3      L13:  -2.3414 L23:   0.5455                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0451 S12:  -0.5826 S13:   0.1187                       
REMARK   3      S21:   0.3251 S22:   0.0699 S23:   0.3785                       
REMARK   3      S31:  -0.2213 S32:  -0.4454 S33:  -0.0073                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1185 THROUGH 1243 )               
REMARK   3    ORIGIN FOR THE GROUP (A):   9.6567 -20.5322  36.3697              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1322 T22:   0.1998                                     
REMARK   3      T33:   0.1739 T12:   0.0060                                     
REMARK   3      T13:  -0.0082 T23:  -0.0023                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0849 L22:   1.9241                                     
REMARK   3      L33:   1.6487 L12:  -0.1444                                     
REMARK   3      L13:   0.0608 L23:  -0.5792                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0475 S12:  -0.2671 S13:  -0.1080                       
REMARK   3      S21:   0.1692 S22:   0.0734 S23:  -0.0564                       
REMARK   3      S31:  -0.0281 S32:  -0.0005 S33:  -0.0185                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1244 THROUGH 1266 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  12.1409 -22.2274  53.2352              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3721 T22:   0.5561                                     
REMARK   3      T33:   0.2292 T12:  -0.0180                                     
REMARK   3      T13:  -0.0664 T23:   0.0364                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3278 L22:   3.0088                                     
REMARK   3      L33:   3.0823 L12:   0.5861                                     
REMARK   3      L13:  -0.5802 L23:  -0.4407                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1280 S12:  -1.5067 S13:  -0.1147                       
REMARK   3      S21:   0.7128 S22:  -0.1351 S23:  -0.0734                       
REMARK   3      S31:  -0.0611 S32:  -0.1532 S33:   0.0152                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 1                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : (CHAIN B AND (RESID 1006 THROUGH 1178 OR    
REMARK   3                          RESID 1183 THROUGH 1266))                   
REMARK   3     ATOM PAIRS NUMBER  : 2501                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5VSD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-MAY-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000227937.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-MAR-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 9.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-E                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9792                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : SCALA 3.3.22                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 62905                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.850                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.910                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.2                               
REMARK 200  DATA REDUNDANCY                : 10.80                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.09700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 11.00                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.52000                            
REMARK 200  R SYM FOR SHELL            (I) : 0.52000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 5TUZ                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.86                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.06                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 7 % PEG 20K, 1.4% V/V 1,4-DIOXANE, 10%   
REMARK 280  GLYCEROL, 0.07 M BICINE, PH 9.0, VAPOR DIFFUSION, TEMPERATURE       
REMARK 280  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       37.43200            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       51.23900            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       48.29700            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       51.23900            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       37.43200            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       48.29700            
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: 2910 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24010 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ASN A  1179                                                      
REMARK 465     LYS A  1180                                                      
REMARK 465     ASP A  1181                                                      
REMARK 465     GLY A  1182                                                      
REMARK 465     ASN B  1179                                                      
REMARK 465     LYS B  1180                                                      
REMARK 465     ASP B  1181                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     GLN B 1043   CD                                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A  3326     O    HOH A  3335              2.07            
REMARK 500   O    HOH A  3313     O    HOH A  3336              2.13            
REMARK 500   O    HOH B  3256     O    HOH B  3295              2.15            
REMARK 500   O    HOH B  3171     O    HOH B  3277              2.18            
REMARK 500   OG   SER A  1079     O    HOH A  3101              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG B1081   NE  -  CZ  -  NH2 ANGL. DEV. =   3.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A1013      106.54   -163.94                                   
REMARK 500    SER A1036       14.66   -141.06                                   
REMARK 500    THR A1047      -83.84   -101.91                                   
REMARK 500    ASP A1066     -149.39   -115.48                                   
REMARK 500    MET A1080      -38.07     70.67                                   
REMARK 500    ASN A1117       47.49    -89.11                                   
REMARK 500    VAL A1119      -60.86   -134.67                                   
REMARK 500    ASN A1194     -161.15   -106.58                                   
REMARK 500    MET A1214      -93.11   -134.74                                   
REMARK 500    ASP B1013      107.41   -163.98                                   
REMARK 500    SER B1036       13.68   -140.02                                   
REMARK 500    THR B1047      -83.58   -101.42                                   
REMARK 500    ASP B1066     -150.67   -111.66                                   
REMARK 500    MET B1080      -45.92     74.38                                   
REMARK 500    ASN B1117       46.91    -90.09                                   
REMARK 500    VAL B1119      -62.20   -135.73                                   
REMARK 500    ASN B1194     -160.55   -106.62                                   
REMARK 500    MET B1214      -94.89   -135.61                                   
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  106.8                                              
REMARK 620 3 CYS A1068   SG  106.6 107.2                                        
REMARK 620 4 CYS A1073   SG  112.1 106.8 116.7                                  
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  114.8                                              
REMARK 620 3 CYS A1105   SG  106.1 112.1                                        
REMARK 620 4 CYS A1109   SG  107.1  97.0 119.9                                  
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  108.2                                              
REMARK 620 3 CYS A1111   SG  107.7 106.7                                        
REMARK 620 4 CYS A1115   SG  113.1 103.9 116.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A3005  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1203   SG                                                     
REMARK 620 2 CYS A1256   SG  115.2                                              
REMARK 620 3 CYS A1258   SG  107.8 103.6                                        
REMARK 620 4 CYS A1263   SG  107.8 105.9 116.9                                  
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  105.4                                              
REMARK 620 3 CYS B1068   SG  106.2 105.0                                        
REMARK 620 4 CYS B1073   SG  109.3 109.2 120.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B3002  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B1062   SG                                                     
REMARK 620 2 CYS B1075   SG  116.9                                              
REMARK 620 3 CYS B1105   SG  107.4 110.1                                        
REMARK 620 4 CYS B1109   SG  106.5  97.3 118.9                                  
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  114.6                                              
REMARK 620 3 CYS B1111   SG  103.9 112.5                                        
REMARK 620 4 CYS B1115   SG  108.1 105.1 112.7                                  
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  112.5                                              
REMARK 620 3 CYS B1258   SG  109.8 108.1                                        
REMARK 620 4 CYS B1263   SG  103.9 108.2 114.4                                  
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 9HJ A 3006                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DIO A 3007                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 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 9HJ B 3006                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 3007                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 3008                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5VSF   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VSC   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5VSE   RELATED DB: PDB                                   
DBREF  5VSD A 1006  1266  UNP    Q9H9B1   EHMT1_HUMAN   1006   1266             
DBREF  5VSD 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    9HJ  A3006      27                                                       
HET    DIO  A3007       6                                                       
HET    SAM  B3001      27                                                       
HET     ZN  B3002       1                                                       
HET     ZN  B3003       1                                                       
HET     ZN  B3004       1                                                       
HET     ZN  B3005       1                                                       
HET    9HJ  B3006      27                                                       
HET    GOL  B3007       6                                                       
HET    GOL  B3008       6                                                       
HETNAM     SAM S-ADENOSYLMETHIONINE                                             
HETNAM      ZN ZINC ION                                                         
HETNAM     9HJ 6,7-DIMETHOXY-N~2~-METHYL-N~4~-(1-METHYLPIPERIDIN-4-             
HETNAM   2 9HJ  YL)-N~2~-PROPYLQUINAZOLINE-2,4-DIAMINE                          
HETNAM     DIO 1,4-DIETHYLENE DIOXIDE                                           
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  SAM    2(C15 H22 N6 O5 S)                                           
FORMUL   4   ZN    8(ZN 2+)                                                     
FORMUL   8  9HJ    2(C20 H31 N5 O2)                                             
FORMUL   9  DIO    C4 H8 O2                                                     
FORMUL  16  GOL    2(C3 H8 O3)                                                  
FORMUL  18  HOH   *529(H2 O)                                                    
HELIX    1 AA1 ASN A 1055  LEU A 1059  5                                   5    
HELIX    2 AA2 CYS A 1073  LEU A 1078  1                                   6    
HELIX    3 AA3 VAL A 1119  GLY A 1123  5                                   5    
HELIX    4 AA4 ASP A 1162  ASP A 1166  1                                   5    
HELIX    5 AA5 VAL A 1195  ILE A 1199  5                                   5    
HELIX    6 AA6 GLY A 1243  GLY A 1251  1                                   9    
HELIX    7 AA7 ASN B 1055  LEU B 1059  5                                   5    
HELIX    8 AA8 CYS B 1073  SER B 1079  1                                   7    
HELIX    9 AA9 VAL B 1119  GLY B 1123  5                                   5    
HELIX   10 AB1 ASP B 1162  ASP B 1166  1                                   5    
HELIX   11 AB2 VAL B 1195  ILE B 1199  5                                   5    
HELIX   12 AB3 GLY B 1243  GLY B 1251  1                                   9    
SHEET    1 AA1 4 ARG A1008  SER A1011  0                                        
SHEET    2 AA1 4 CYS A1025  ASN A1027 -1  O  CYS A1025   N  SER A1011           
SHEET    3 AA1 4 LEU A1128  ARG A1132  1  O  LEU A1130   N  VAL A1026           
SHEET    4 AA1 4 TRP A1138  SER A1142 -1  O  GLY A1139   N  TYR A1131           
SHEET    1 AA2 3 LYS A1039  TYR A1040  0                                        
SHEET    2 AA2 3 TYR A1185  GLY A1193  1  O  PHE A1191   N  LYS A1039           
SHEET    3 AA2 3 GLY A1157  SER A1161 -1  N  GLU A1158   O  ASP A1188           
SHEET    1 AA3 3 LYS A1039  TYR A1040  0                                        
SHEET    2 AA3 3 TYR A1185  GLY A1193  1  O  PHE A1191   N  LYS A1039           
SHEET    3 AA3 3 LEU A1174  ASP A1176 -1  N  PHE A1175   O  ILE A1187           
SHEET    1 AA4 4 ILE A1102  PHE A1103  0                                        
SHEET    2 AA4 4 LEU A1207  PHE A1213  1  O  PHE A1213   N  ILE A1102           
SHEET    3 AA4 4 ARG A1223  SER A1228 -1  O  ALA A1225   N  VAL A1210           
SHEET    4 AA4 4 PHE A1151  TYR A1155 -1  N  CYS A1153   O  PHE A1226           
SHEET    1 AA5 2 ASN A1200  HIS A1201  0                                        
SHEET    2 AA5 2 GLY A1239  PHE A1240  1  O  PHE A1240   N  ASN A1200           
SHEET    1 AA6 4 ARG B1008  SER B1011  0                                        
SHEET    2 AA6 4 CYS B1025  ASN B1027 -1  O  CYS B1025   N  SER B1011           
SHEET    3 AA6 4 LEU B1128  ARG B1132  1  O  LEU B1130   N  VAL B1026           
SHEET    4 AA6 4 TRP B1138  SER B1142 -1  O  GLY B1139   N  TYR B1131           
SHEET    1 AA7 3 LYS B1039  TYR B1040  0                                        
SHEET    2 AA7 3 TYR B1185  GLY B1193  1  O  PHE B1191   N  LYS B1039           
SHEET    3 AA7 3 GLY B1157  SER B1161 -1  N  GLU B1158   O  ASP B1188           
SHEET    1 AA8 3 LYS B1039  TYR B1040  0                                        
SHEET    2 AA8 3 TYR B1185  GLY B1193  1  O  PHE B1191   N  LYS B1039           
SHEET    3 AA8 3 LEU B1174  LEU B1177 -1  N  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  VAL B1152   O  PHE B1226           
SHEET    1 AB1 2 ASN B1200  HIS B1201  0                                        
SHEET    2 AB1 2 GLY B1239  PHE B1240  1  O  PHE B1240   N  ASN B1200           
LINK         SG  CYS A1062                ZN    ZN A3004     1555   1555  2.37  
LINK         SG  CYS A1062                ZN    ZN A3002     1555   1555  2.40  
LINK         SG  CYS A1064                ZN    ZN A3004     1555   1555  2.37  
LINK         SG  CYS A1068                ZN    ZN A3003     1555   1555  2.39  
LINK         SG  CYS A1068                ZN    ZN A3004     1555   1555  2.19  
LINK         SG  CYS A1073                ZN    ZN A3004     1555   1555  2.42  
LINK         SG  CYS A1075                ZN    ZN A3002     1555   1555  2.38  
LINK         SG  CYS A1105                ZN    ZN A3003     1555   1555  2.32  
LINK         SG  CYS A1105                ZN    ZN A3002     1555   1555  2.39  
LINK         SG  CYS A1109                ZN    ZN A3002     1555   1555  2.33  
LINK         SG  CYS A1111                ZN    ZN A3003     1555   1555  2.28  
LINK         SG  CYS A1115                ZN    ZN A3003     1555   1555  2.32  
LINK         SG  CYS A1203                ZN    ZN A3005     1555   1555  2.31  
LINK         SG  CYS A1256                ZN    ZN A3005     1555   1555  2.40  
LINK         SG  CYS A1258                ZN    ZN A3005     1555   1555  2.35  
LINK         SG  CYS A1263                ZN    ZN A3005     1555   1555  2.37  
LINK         SG  CYS B1062                ZN    ZN B3004     1555   1555  2.39  
LINK         SG  CYS B1062                ZN    ZN B3002     1555   1555  2.36  
LINK         SG  CYS B1064                ZN    ZN B3004     1555   1555  2.36  
LINK         SG  CYS B1068                ZN    ZN B3003     1555   1555  2.33  
LINK         SG  CYS B1068                ZN    ZN B3004     1555   1555  2.33  
LINK         SG  CYS B1073                ZN    ZN B3004     1555   1555  2.33  
LINK         SG  CYS B1075                ZN    ZN B3002     1555   1555  2.36  
LINK         SG  CYS B1105                ZN    ZN B3003     1555   1555  2.28  
LINK         SG  CYS B1105                ZN    ZN B3002     1555   1555  2.42  
LINK         SG  CYS B1109                ZN    ZN B3002     1555   1555  2.36  
LINK         SG  CYS B1111                ZN    ZN B3003     1555   1555  2.29  
LINK         SG  CYS B1115                ZN    ZN B3003     1555   1555  2.38  
LINK         SG  CYS B1203                ZN    ZN B3005     1555   1555  2.47  
LINK         SG  CYS B1256                ZN    ZN B3005     1555   1555  2.31  
LINK         SG  CYS B1258                ZN    ZN B3005     1555   1555  2.34  
LINK         SG  CYS B1263                ZN    ZN B3005     1555   1555  2.38  
SITE     1 AC1 19 MET A1136  GLY A1137  TRP A1138  SER A1172                    
SITE     2 AC1 19 TYR A1173  ARG A1197  PHE A1198  ASN A1200                    
SITE     3 AC1 19 HIS A1201  TYR A1242  PHE A1246  CYS A1256                    
SITE     4 AC1 19 ARG A1257  HOH A3125  HOH A3177  HOH A3202                    
SITE     5 AC1 19 HOH A3226  HOH A3261  HOH A3287                               
SITE     1 AC2  4 CYS A1062  CYS A1075  CYS A1105  CYS A1109                    
SITE     1 AC3  4 CYS A1068  CYS A1105  CYS A1111  CYS A1115                    
SITE     1 AC4  4 CYS A1062  CYS A1064  CYS A1068  CYS A1073                    
SITE     1 AC5  4 CYS A1203  CYS A1256  CYS A1258  CYS A1263                    
SITE     1 AC6 12 ASP A1162  ALA A1165  ASP A1166  ARG A1168                    
SITE     2 AC6 12 ASP A1171  LEU A1174  ASP A1176  CYS A1186                    
SITE     3 AC6 12 ARG A1245  PHE A1246  ILE A1249  LYS A1250                    
SITE     1 AC7  6 CYS A1064  ILE A1065  ASP A1066  ASN A1072                    
SITE     2 AC7  6 LEU B1078  PHE B1103                                          
SITE     1 AC8 17 MET B1136  GLY B1137  TRP B1138  SER B1172                    
SITE     2 AC8 17 TYR B1173  ARG B1197  PHE B1198  ASN B1200                    
SITE     3 AC8 17 HIS B1201  TYR B1242  CYS B1256  ARG B1257                    
SITE     4 AC8 17 HOH B3216  HOH B3222  HOH B3249  HOH B3263                    
SITE     5 AC8 17 HOH B3285                                                     
SITE     1 AC9  4 CYS B1062  CYS B1075  CYS B1105  CYS B1109                    
SITE     1 AD1  5 CYS B1068  CYS B1105  CYS B1111  CYS B1115                    
SITE     2 AD1  5  ZN B3004                                                     
SITE     1 AD2  5 CYS B1062  CYS B1064  CYS B1068  CYS B1073                    
SITE     2 AD2  5  ZN B3003                                                     
SITE     1 AD3  4 CYS B1203  CYS B1256  CYS B1258  CYS B1263                    
SITE     1 AD4 10 ALA B1165  ASP B1166  ARG B1168  ASP B1171                    
SITE     2 AD4 10 LEU B1174  ASP B1176  ARG B1245  PHE B1246                    
SITE     3 AD4 10 ILE B1249  LYS B1250                                          
SITE     1 AD5  3 HOH A3159  HOH A3260  ARG B1054                               
SITE     1 AD6  8 ASN B1044  LEU B1159  LEU B1177  HIS B1216                    
SITE     2 AD6  8 PHE B1221  PRO B1222  ARG B1223  HOH B3254                    
CRYST1   74.864   96.594  102.478  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      0.013358  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010353  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009758        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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