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Entry: 5JLB
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HEADER    TRANSFERASE                             26-APR-16   5JLB              
TITLE     CRYSTAL STRUCTURE OF SETD2 BOUND TO HISTONE H3.3 K36I PEPTIDE         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE SETD2;                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: CATALYTIC DOMAIN, UNP RESIDUES 1434-1711;                  
COMPND   5 SYNONYM: HIF-1,HUNTINGTIN YEAST PARTNER B,HUNTINGTIN-INTERACTING     
COMPND   6 PROTEIN 1,HIP-1,HUNTINGTIN-INTERACTING PROTEIN B,LYSINE N-           
COMPND   7 METHYLTRANSFERASE 3A,SET DOMAIN-CONTAINING PROTEIN 2,HSET2,P231HBP;  
COMPND   8 EC: 2.1.1.43;                                                        
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: HISTONE H3.3;                                              
COMPND  12 CHAIN: B;                                                            
COMPND  13 FRAGMENT: H3 PEPTIDE, UNP RESIDUES 30-43;                            
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: SETD2;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28B;                                   
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  14 ORGANISM_COMMON: HUMAN;                                              
SOURCE  15 ORGANISM_TAXID: 9606;                                                
SOURCE  16 OTHER_DETAILS: CHEMICALLY SYNTHESIZED                                
KEYWDS    SET DOMAIN, TRANSFERASE                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.LI,S.YANG                                                           
REVDAT   2   30-AUG-17 5JLB    1       JRNL   REMARK                            
REVDAT   1   02-NOV-16 5JLB    0                                                
JRNL        AUTH   S.YANG,X.ZHENG,C.LU,G.M.LI,C.D.ALLIS,H.LI                    
JRNL        TITL   MOLECULAR BASIS FOR ONCOHISTONE H3 RECOGNITION BY SETD2      
JRNL        TITL 2 METHYLTRANSFERASE                                            
JRNL        REF    GENES DEV.                    V.  30  1611 2016              
JRNL        REFN                   ISSN 0890-9369                               
JRNL        PMID   27474439                                                     
JRNL        DOI    10.1101/GAD.284323.116                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.10_2155                                     
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) : 1.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.52                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 58391                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.166                           
REMARK   3   R VALUE            (WORKING SET) : 0.164                           
REMARK   3   FREE R VALUE                     : 0.190                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.870                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2842                            
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 34.5248 -  4.0680    1.00     2978   157  0.1588 0.2138        
REMARK   3     2  4.0680 -  3.2297    1.00     2845   162  0.1480 0.1670        
REMARK   3     3  3.2297 -  2.8216    1.00     2860   111  0.1661 0.1648        
REMARK   3     4  2.8216 -  2.5637    1.00     2812   130  0.1739 0.2041        
REMARK   3     5  2.5637 -  2.3800    1.00     2843   119  0.1763 0.2071        
REMARK   3     6  2.3800 -  2.2397    1.00     2788   125  0.1699 0.1917        
REMARK   3     7  2.2397 -  2.1276    1.00     2775   139  0.1623 0.1904        
REMARK   3     8  2.1276 -  2.0350    1.00     2753   157  0.1597 0.1786        
REMARK   3     9  2.0350 -  1.9566    1.00     2781   123  0.1575 0.1812        
REMARK   3    10  1.9566 -  1.8891    1.00     2769   137  0.1605 0.1759        
REMARK   3    11  1.8891 -  1.8301    1.00     2754   155  0.1590 0.1885        
REMARK   3    12  1.8301 -  1.7778    1.00     2742   161  0.1611 0.2009        
REMARK   3    13  1.7778 -  1.7310    1.00     2741   141  0.1666 0.1876        
REMARK   3    14  1.7310 -  1.6887    1.00     2749   146  0.1647 0.1922        
REMARK   3    15  1.6887 -  1.6503    1.00     2745   163  0.1659 0.1938        
REMARK   3    16  1.6503 -  1.6152    1.00     2737   152  0.1760 0.1760        
REMARK   3    17  1.6152 -  1.5829    1.00     2730   143  0.1829 0.1961        
REMARK   3    18  1.5829 -  1.5530    1.00     2742   141  0.1989 0.1968        
REMARK   3    19  1.5530 -  1.5253    1.00     2769   127  0.2049 0.2509        
REMARK   3    20  1.5253 -  1.4994    0.96     2636   153  0.2343 0.2660        
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)     : 0.120            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.800           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 17.87                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.45                          
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      :  0.005           2187                                  
REMARK   3   ANGLE     :  0.914           2924                                  
REMARK   3   CHIRALITY :  0.085            295                                  
REMARK   3   PLANARITY :  0.004            382                                  
REMARK   3   DIHEDRAL  : 24.301            843                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 8                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1447 THROUGH 1485 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.2886  -0.4617   4.8632              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2402 T22:   0.3294                                     
REMARK   3      T33:   0.2272 T12:   0.0627                                     
REMARK   3      T13:  -0.0495 T23:   0.0126                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6855 L22:   0.5170                                     
REMARK   3      L33:   1.7530 L12:   0.2805                                     
REMARK   3      L13:  -0.4331 L23:  -0.3923                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0157 S12:  -0.2625 S13:  -0.1054                       
REMARK   3      S21:   0.2130 S22:   0.0135 S23:  -0.1532                       
REMARK   3      S31:   0.2619 S32:   0.5200 S33:  -0.0039                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1486 THROUGH 1511 )               
REMARK   3    ORIGIN FOR THE GROUP (A): -33.2448   5.2391  23.7909              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2365 T22:   0.4388                                     
REMARK   3      T33:   0.3828 T12:   0.0503                                     
REMARK   3      T13:   0.0661 T23:   0.0712                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5108 L22:   0.2107                                     
REMARK   3      L33:   1.1495 L12:  -0.2415                                     
REMARK   3      L13:   0.3651 L23:   0.1951                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0226 S12:  -0.5209 S13:  -0.1613                       
REMARK   3      S21:   0.1030 S22:  -0.0887 S23:  -0.1719                       
REMARK   3      S31:  -0.2471 S32:  -0.1213 S33:  -0.0841                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1512 THROUGH 1551 )               
REMARK   3    ORIGIN FOR THE GROUP (A): -28.6019   4.7872  16.9402              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1813 T22:   0.2010                                     
REMARK   3      T33:   0.1729 T12:   0.0301                                     
REMARK   3      T13:   0.0029 T23:   0.0143                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6097 L22:   0.9726                                     
REMARK   3      L33:   0.9057 L12:   0.1934                                     
REMARK   3      L13:   0.2101 L23:  -0.2128                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0184 S12:  -0.1119 S13:  -0.0346                       
REMARK   3      S21:   0.0740 S22:   0.0039 S23:   0.0545                       
REMARK   3      S31:   0.0881 S32:  -0.1928 S33:   0.0005                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1552 THROUGH 1574 )               
REMARK   3    ORIGIN FOR THE GROUP (A): -18.5968  -6.5149  -2.9909              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2375 T22:   0.1606                                     
REMARK   3      T33:   0.2119 T12:  -0.0216                                     
REMARK   3      T13:   0.0323 T23:   0.0090                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2990 L22:   0.0481                                     
REMARK   3      L33:   0.5586 L12:  -0.1448                                     
REMARK   3      L13:   0.2049 L23:   0.0654                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0934 S12:   0.1208 S13:  -0.1517                       
REMARK   3      S21:  -0.0487 S22:   0.0612 S23:   0.0699                       
REMARK   3      S31:   0.4876 S32:  -0.1926 S33:   0.0065                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1575 THROUGH 1616 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.8512  14.1609  -2.3152              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1669 T22:   0.1400                                     
REMARK   3      T33:   0.1796 T12:  -0.0205                                     
REMARK   3      T13:  -0.0054 T23:  -0.0248                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8587 L22:   0.9155                                     
REMARK   3      L33:   0.9034 L12:   0.5542                                     
REMARK   3      L13:  -0.3698 L23:  -0.7035                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0101 S12:  -0.1438 S13:   0.0629                       
REMARK   3      S21:   0.1798 S22:   0.0084 S23:  -0.0343                       
REMARK   3      S31:  -0.1802 S32:   0.0939 S33:  -0.0001                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1617 THROUGH 1662 )               
REMARK   3    ORIGIN FOR THE GROUP (A): -21.0438   3.7980   0.3910              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1491 T22:   0.1372                                     
REMARK   3      T33:   0.1639 T12:   0.0092                                     
REMARK   3      T13:  -0.0143 T23:  -0.0074                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6714 L22:   0.5673                                     
REMARK   3      L33:   1.5106 L12:  -0.0708                                     
REMARK   3      L13:  -0.6671 L23:  -0.5731                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0387 S12:   0.0217 S13:  -0.0749                       
REMARK   3      S21:   0.0135 S22:   0.0450 S23:   0.0161                       
REMARK   3      S31:   0.0181 S32:  -0.0873 S33:  -0.0000                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1663 THROUGH 1703 )               
REMARK   3    ORIGIN FOR THE GROUP (A): -17.9455  11.2549 -15.0039              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2106 T22:   0.2008                                     
REMARK   3      T33:   0.1870 T12:   0.0104                                     
REMARK   3      T13:  -0.0136 T23:   0.0109                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9750 L22:   0.5702                                     
REMARK   3      L33:   0.7990 L12:  -0.0056                                     
REMARK   3      L13:  -0.1481 L23:   0.3830                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0576 S12:   0.2897 S13:   0.1514                       
REMARK   3      S21:  -0.2877 S22:   0.0477 S23:   0.0149                       
REMARK   3      S31:  -0.1891 S32:  -0.1851 S33:  -0.0008                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 29 THROUGH 42 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -20.7013  12.1100  -8.3557              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2112 T22:   0.2091                                     
REMARK   3      T33:   0.1858 T12:   0.0193                                     
REMARK   3      T13:  -0.0110 T23:  -0.0181                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1451 L22:   0.3993                                     
REMARK   3      L33:   0.4291 L12:  -0.1044                                     
REMARK   3      L13:   0.2054 L23:   0.1235                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1278 S12:   0.2805 S13:  -0.1444                       
REMARK   3      S21:  -0.2459 S22:  -0.1110 S23:   0.0323                       
REMARK   3      S31:  -0.3329 S32:  -0.2642 S33:   0.0124                       
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 5JLB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-MAY-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000220821.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-JUN-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9790                             
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL, SI(111)            
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 58483                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 9.300                              
REMARK 200  R MERGE                    (I) : 0.07800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.53                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.75400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 4H12                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.07                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M KSCN, 0.1 M BIS-TRIS PROPANE,      
REMARK 280  20% PEG3350, PH 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE     
REMARK 280  277K                                                                
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       30.29650            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       38.63200            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       38.42200            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       38.63200            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       30.29650            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       38.42200            
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: 3270 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13730 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 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     SER A  1433                                                      
REMARK 465     GLY A  1434                                                      
REMARK 465     GLU A  1435                                                      
REMARK 465     THR A  1436                                                      
REMARK 465     SER A  1437                                                      
REMARK 465     VAL A  1438                                                      
REMARK 465     PRO A  1439                                                      
REMARK 465     PRO A  1440                                                      
REMARK 465     GLY A  1441                                                      
REMARK 465     SER A  1442                                                      
REMARK 465     ALA A  1443                                                      
REMARK 465     LEU A  1444                                                      
REMARK 465     VAL A  1445                                                      
REMARK 465     GLY A  1446                                                      
REMARK 465     ASN A  1488                                                      
REMARK 465     LYS A  1489                                                      
REMARK 465     SER A  1490                                                      
REMARK 465     HIS A  1491                                                      
REMARK 465     ARG A  1492                                                      
REMARK 465     ASP A  1493                                                      
REMARK 465     ILE A  1494                                                      
REMARK 465     LYS A  1495                                                      
REMARK 465     ARG A  1496                                                      
REMARK 465     MET A  1704                                                      
REMARK 465     LYS A  1705                                                      
REMARK 465     LYS A  1706                                                      
REMARK 465     GLU A  1707                                                      
REMARK 465     ARG A  1708                                                      
REMARK 465     SER A  1709                                                      
REMARK 465     ARG A  1710                                                      
REMARK 465     LYS A  1711                                                      
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  2113     O    HOH A  2167              2.14            
REMARK 500   O    HOH A  1917     O    HOH A  2110              2.15            
REMARK 500   O    HOH A  2088     O    HOH A  2127              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A  2009     O    HOH A  2141     2455     2.09            
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    ASN A1541       40.52   -108.86                                   
REMARK 500    LYS A1559       14.96   -147.45                                   
REMARK 500    VAL A1576      -70.67    -92.68                                   
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 A1807  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1499   SG                                                     
REMARK 620 2 CYS A1501   SG  105.6                                              
REMARK 620 3 CYS A1516   SG  107.3 107.1                                        
REMARK 620 4 CYS A1520   SG  117.4 107.9 111.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1808  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1516   SG                                                     
REMARK 620 2 CYS A1529   SG  114.8                                              
REMARK 620 3 CYS A1533   SG   98.8 119.7                                        
REMARK 620 4 CYS A1539   SG  111.2  99.8 113.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1809  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1631   SG                                                     
REMARK 620 2 CYS A1678   SG  114.7                                              
REMARK 620 3 CYS A1680   SG  106.7 105.8                                        
REMARK 620 4 CYS A1685   SG  111.0 108.0 110.5                                  
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 SAH A 1801                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SCN A 1802                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SCN A 1803                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SCN A 1804                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1805                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1806                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1807                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1808                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1809                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5JJY   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5JLE   RELATED DB: PDB                                   
DBREF  5JLB A 1434  1711  UNP    Q9BYW2   SETD2_HUMAN   1434   1711             
DBREF  5JLB B   29    42  UNP    P84243   H33_HUMAN       30     43             
SEQADV 5JLB SER A 1433  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5JLB ILE B   36  UNP  P84243    LYS    37 ENGINEERED MUTATION            
SEQRES   1 A  279  SER GLY GLU THR SER VAL PRO PRO GLY SER ALA LEU VAL          
SEQRES   2 A  279  GLY PRO SER CYS VAL MET ASP ASP PHE ARG ASP PRO GLN          
SEQRES   3 A  279  ARG TRP LYS GLU CYS ALA LYS GLN GLY LYS MET PRO CYS          
SEQRES   4 A  279  TYR PHE ASP LEU ILE GLU GLU ASN VAL TYR LEU THR GLU          
SEQRES   5 A  279  ARG LYS LYS ASN LYS SER HIS ARG ASP ILE LYS ARG MET          
SEQRES   6 A  279  GLN CYS GLU CYS THR PRO LEU SER LYS ASP GLU ARG ALA          
SEQRES   7 A  279  GLN GLY GLU ILE ALA CYS GLY GLU ASP CYS LEU ASN ARG          
SEQRES   8 A  279  LEU LEU MET ILE GLU CYS SER SER ARG CYS PRO ASN GLY          
SEQRES   9 A  279  ASP TYR CYS SER ASN ARG ARG PHE GLN ARG LYS GLN HIS          
SEQRES  10 A  279  ALA ASP VAL GLU VAL ILE LEU THR GLU LYS LYS GLY TRP          
SEQRES  11 A  279  GLY LEU ARG ALA ALA LYS ASP LEU PRO SER ASN THR PHE          
SEQRES  12 A  279  VAL LEU GLU TYR CYS GLY GLU VAL LEU ASP HIS LYS GLU          
SEQRES  13 A  279  PHE LYS ALA ARG VAL LYS GLU TYR ALA ARG ASN LYS ASN          
SEQRES  14 A  279  ILE HIS TYR TYR PHE MET ALA LEU LYS ASN ASP GLU ILE          
SEQRES  15 A  279  ILE ASP ALA THR GLN LYS GLY ASN CYS SER ARG PHE MET          
SEQRES  16 A  279  ASN HIS SER CYS GLU PRO ASN CYS GLU THR GLN LYS TRP          
SEQRES  17 A  279  THR VAL ASN GLY GLN LEU ARG VAL GLY PHE PHE THR THR          
SEQRES  18 A  279  LYS LEU VAL PRO SER GLY SER GLU LEU THR PHE ASP TYR          
SEQRES  19 A  279  GLN PHE GLN ARG TYR GLY LYS GLU ALA GLN LYS CYS PHE          
SEQRES  20 A  279  CYS GLY SER ALA ASN CYS ARG GLY TYR LEU GLY GLY GLU          
SEQRES  21 A  279  ASN ARG VAL SER ILE ARG ALA ALA GLY GLY LYS MET LYS          
SEQRES  22 A  279  LYS GLU ARG SER ARG LYS                                      
SEQRES   1 B   14  ALA PRO SER THR GLY GLY VAL ILE LYS PRO HIS ARG TYR          
SEQRES   2 B   14  ARG                                                          
HET    SAH  A1801      26                                                       
HET    SCN  A1802       3                                                       
HET    SCN  A1803       3                                                       
HET    SCN  A1804       3                                                       
HET    GOL  A1805       6                                                       
HET    GOL  A1806       6                                                       
HET     ZN  A1807       1                                                       
HET     ZN  A1808       1                                                       
HET     ZN  A1809       1                                                       
HETNAM     SAH S-ADENOSYL-L-HOMOCYSTEINE                                        
HETNAM     SCN THIOCYANATE ION                                                  
HETNAM     GOL GLYCEROL                                                         
HETNAM      ZN ZINC ION                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  SAH    C14 H20 N6 O5 S                                              
FORMUL   4  SCN    3(C N S 1-)                                                  
FORMUL   7  GOL    2(C3 H8 O3)                                                  
FORMUL   9   ZN    3(ZN 2+)                                                     
FORMUL  12  HOH   *330(H2 O)                                                    
HELIX    1 AA1 ASP A 1452  ARG A 1455  5                                   4    
HELIX    2 AA2 ASP A 1456  GLN A 1466  1                                  11    
HELIX    3 AA3 SER A 1505  GLY A 1512  1                                   8    
HELIX    4 AA4 CYS A 1520  LEU A 1525  1                                   6    
HELIX    5 AA5 ASN A 1535  CYS A 1539  5                                   5    
HELIX    6 AA6 ASP A 1585  ASN A 1599  1                                  15    
HELIX    7 AA7 ASN A 1622  MET A 1627  5                                   6    
HELIX    8 AA8 SER A 1696  GLY A 1701  1                                   6    
SHEET    1 AA1 5 SER A1448  VAL A1450  0                                        
SHEET    2 AA1 5 VAL A1552  LEU A1556 -1  O  VAL A1554   N  CYS A1449           
SHEET    3 AA1 5 TRP A1562  ALA A1566 -1  O  GLY A1563   N  ILE A1555           
SHEET    4 AA1 5 GLU A1661  PHE A1664 -1  O  LEU A1662   N  LEU A1564           
SHEET    5 AA1 5 ASN A1628  HIS A1629  1  N  ASN A1628   O  PHE A1664           
SHEET    1 AA2 2 ASP A1474  LEU A1475  0                                        
SHEET    2 AA2 2 LYS A1620  GLY A1621  1  O  GLY A1621   N  ASP A1474           
SHEET    1 AA3 6 VAL A1480  TYR A1481  0                                        
SHEET    2 AA3 6 GLU A1582  LEU A1584  1  O  VAL A1583   N  VAL A1480           
SHEET    3 AA3 6 GLU A1613  ASP A1616 -1  O  ILE A1614   N  LEU A1584           
SHEET    4 AA3 6 PHE A1606  LYS A1610 -1  N  MET A1607   O  ILE A1615           
SHEET    5 AA3 6 GLY B  34  ILE B  36  1  O  ILE B  36   N  PHE A1606           
SHEET    6 AA3 6 GLN A1669  ARG A1670 -1  N  GLN A1669   O  VAL B  35           
SHEET    1 AA4 3 PHE A1575  GLU A1578  0                                        
SHEET    2 AA4 3 GLN A1645  THR A1652 -1  O  PHE A1650   N  VAL A1576           
SHEET    3 AA4 3 CYS A1635  VAL A1642 -1  N  VAL A1642   O  GLN A1645           
LINK         SG  CYS A1499                ZN    ZN A1807     1555   1555  2.30  
LINK         SG  CYS A1501                ZN    ZN A1807     1555   1555  2.41  
LINK         SG  CYS A1516                ZN    ZN A1807     1555   1555  2.38  
LINK         SG  CYS A1516                ZN    ZN A1808     1555   1555  2.38  
LINK         SG  CYS A1520                ZN    ZN A1807     1555   1555  2.28  
LINK         SG  CYS A1529                ZN    ZN A1808     1555   1555  2.40  
LINK         SG  CYS A1533                ZN    ZN A1808     1555   1555  2.23  
LINK         SG  CYS A1539                ZN    ZN A1808     1555   1555  2.31  
LINK         SG  CYS A1631                ZN    ZN A1809     1555   1555  2.41  
LINK         SG  CYS A1678                ZN    ZN A1809     1555   1555  2.30  
LINK         SG  CYS A1680                ZN    ZN A1809     1555   1555  2.38  
LINK         SG  CYS A1685                ZN    ZN A1809     1555   1555  2.27  
SITE     1 AC1 18 LYS A1560  GLY A1561  TRP A1562  ILE A1602                    
SITE     2 AC1 18 HIS A1603  TYR A1604  TYR A1605  ARG A1625                    
SITE     3 AC1 18 PHE A1626  ASN A1628  HIS A1629  TYR A1666                    
SITE     4 AC1 18 LYS A1677  CYS A1678  PHE A1679  HOH A1935                    
SITE     5 AC1 18 HOH A1961  HOH A1966                                          
SITE     1 AC2  7 HIS A1629  PHE A1668  ARG A1686  GLY A1690                    
SITE     2 AC2  7 GLY A1691  HOH A1994  HOH A2096                               
SITE     1 AC3  1 LYS A1590                                                     
SITE     1 AC4  5 THR A1637  LYS A1639  HOH A2058  HIS B  39                    
SITE     2 AC4  5 ARG B  40                                                     
SITE     1 AC5  6 GLU A1477  LYS A1547  LYS A1677  CYS A1678                    
SITE     2 AC5  6 GLY A1687  HOH A1950                                          
SITE     1 AC6  6 ARG A1509  ASP A1537  CYS A1539  GLN A1548                    
SITE     2 AC6  6 HOH A1927  HOH A2112                                          
SITE     1 AC7  4 CYS A1499  CYS A1501  CYS A1516  CYS A1520                    
SITE     1 AC8  4 CYS A1516  CYS A1529  CYS A1533  CYS A1539                    
SITE     1 AC9  4 CYS A1631  CYS A1678  CYS A1680  CYS A1685                    
CRYST1   60.593   76.844   77.264  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.016504  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013013  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012943        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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