GenomeNet

Database: PDB
Entry: 4H12
LinkDB: 4H12
Original site: 4H12 
HEADER    TRANSFERASE                             10-SEP-12   4H12              
TITLE     THE CRYSTAL STRUCTURE OF METHYLTRANSFERASE DOMAIN OF HUMAN SET DOMAIN-
TITLE    2 CONTAINING PROTEIN 2 IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE SETD2;                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: METHYLTRANSFERASE 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,        
COMPND   8 P231HBP;                                                             
COMPND   9 EC: 2.1.1.43;                                                        
COMPND  10 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: SETD2, HIF1, HYPB, KIAA1732, KMT3A, SET2, HSPC069;             
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21-V2R-PRARE2;                           
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28-LIC                                 
KEYWDS    METHYLTRANSFERASE, SET DOMAIN-CONTAINING PROTEIN 2, S-ADENOSYL-L-     
KEYWDS   2 HOMOCYSTEINE, STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM,   
KEYWDS   3 SGC, ACTIVATOR, CHROMATIN REGULATOR, DNA-BINDING, METHYLATION,       
KEYWDS   4 NUCLEUS, PHOSPHOPROTEIN, TRANSCRIPTION, TRANSCRIPTION REGULATION,    
KEYWDS   5 TRANSFERASE                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.F.AMAYA,A.DONG,H.ZENG,F.MACKENZIE,M.BUNNAGE,J.WEIGELT,C.BOUNTRA,    
AUTHOR   2 C.H.ARROWSMITH,A.M.EDWARDS,J.MIN,H.WU,STRUCTURAL GENOMICS CONSORTIUM 
AUTHOR   3 (SGC)                                                                
REVDAT   3   14-NOV-12 4H12    1       JRNL                                     
REVDAT   2   24-OCT-12 4H12    1       JRNL                                     
REVDAT   1   03-OCT-12 4H12    0                                                
SPRSDE     03-OCT-12 4H12      3H6L                                             
JRNL        AUTH   W.ZHENG,G.IBANEZ,H.WU,G.BLUM,H.ZENG,A.DONG,F.LI,T.HAJIAN,    
JRNL        AUTH 2 A.ALLALI-HASSANI,M.F.AMAYA,A.SIARHEYEVA,W.YU,P.J.BROWN,      
JRNL        AUTH 3 M.SCHAPIRA,M.VEDADI,J.MIN,M.LUO                              
JRNL        TITL   SINEFUNGIN DERIVATIVES AS INHIBITORS AND STRUCTURE PROBES OF 
JRNL        TITL 2 PROTEIN LYSINE METHYLTRANSFERASE SETD2.                      
JRNL        REF    J.AM.CHEM.SOC.                V. 134 18004 2012              
JRNL        REFN                   ISSN 0002-7863                               
JRNL        PMID   23043551                                                     
JRNL        DOI    10.1021/JA307060P                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.06 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0027                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.06                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.36                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 18905                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.210                           
REMARK   3   R VALUE            (WORKING SET) : 0.207                           
REMARK   3   FREE R VALUE                     : 0.249                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1011                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.06                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.11                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1342                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.72                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3320                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 71                           
REMARK   3   BIN FREE R VALUE                    : 0.3420                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1778                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 30                                      
REMARK   3   SOLVENT ATOMS            : 124                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 39.61                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 5.62000                                              
REMARK   3    B22 (A**2) : -4.55000                                             
REMARK   3    B33 (A**2) : -1.07000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.182         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.168         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.126         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.679        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.949                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.923                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1853 ; 0.009 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2506 ; 1.251 ; 1.954       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   233 ; 5.630 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    87 ;34.318 ;24.023       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   288 ;12.749 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    11 ;19.050 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   264 ; 0.085 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1434 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A  1447        A  1691                          
REMARK   3    RESIDUE RANGE :   A  1801        A  1805                          
REMARK   3    RESIDUE RANGE :   A  1901        A  2024                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.8258  16.0767  14.4687              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0179 T22:   0.0471                                     
REMARK   3      T33:   0.0178 T12:  -0.0196                                     
REMARK   3      T13:  -0.0034 T23:   0.0068                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3620 L22:   3.0820                                     
REMARK   3      L33:   0.9939 L12:  -1.2652                                     
REMARK   3      L13:  -0.4221 L23:   0.4505                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0397 S12:  -0.0916 S13:  -0.0266                       
REMARK   3      S21:   0.1361 S22:   0.0065 S23:   0.0011                       
REMARK   3      S31:   0.0736 S32:  -0.0018 S33:   0.0332                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT                                                           
REMARK   4                                                                      
REMARK   4 4H12 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-SEP-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB074884.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-MAR-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97935                            
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21811                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.991                              
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     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY                : 6.900                              
REMARK 200  R MERGE                    (I) : 0.10100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.99                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.03                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.75300                            
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: PDB ENTRY 2R3A                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.78                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1 UL PROTEIN (1:10 MOLAR RATIO OF        
REMARK 280  SETD2:ADOMET) + 1 UL RESERVOIR SOLUTION (30% PEG2000 MME, 0.1 M     
REMARK 280  POTASSIUM THIOCYANATE), VAPOR DIFFUSION, HANGING DROP,              
REMARK 280  TEMPERATURE 298K                                                    
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       26.14650            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       39.04650            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       38.33150            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       39.04650            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       26.14650            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       38.33150            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     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     ARG A  1485                                                      
REMARK 465     LYS A  1486                                                      
REMARK 465     LYS A  1487                                                      
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     GLU A  1692                                                      
REMARK 465     ASN A  1693                                                      
REMARK 465     ARG A  1694                                                      
REMARK 465     VAL A  1695                                                      
REMARK 465     SER A  1696                                                      
REMARK 465     ILE A  1697                                                      
REMARK 465     ARG A  1698                                                      
REMARK 465     ALA A  1699                                                      
REMARK 465     ALA A  1700                                                      
REMARK 465     GLY A  1701                                                      
REMARK 465     GLY A  1702                                                      
REMARK 465     LYS A  1703                                                      
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 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     VAL A1450    CG1  CG2                                            
REMARK 470     ARG A1455    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLN A1458    CG   CD   OE1  NE2                                  
REMARK 470     ARG A1459    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A1462    CG   CD   OE1  OE2                                  
REMARK 470     LYS A1465    CG   CD   CE   NZ                                   
REMARK 470     GLN A1466    CG   CD   OE1  NE2                                  
REMARK 470     LYS A1468    CG   CD   CE   NZ                                   
REMARK 470     GLU A1478    CG   CD   OE1  OE2                                  
REMARK 470     GLU A1484    CG   CD   OE1  OE2                                  
REMARK 470     MET A1497    CG   SD   CE                                        
REMARK 470     GLN A1498    CG   CD   OE1  NE2                                  
REMARK 470     GLU A1500    CG   CD   OE1  OE2                                  
REMARK 470     LEU A1504    CD1  CD2                                            
REMARK 470     LYS A1506    CG   CD   CE   NZ                                   
REMARK 470     ARG A1509    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A1513    CD   OE1  OE2                                       
REMARK 470     GLU A1518    CG   CD   OE1  OE2                                  
REMARK 470     ARG A1532    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU A1558    CD   OE1  OE2                                       
REMARK 470     LYS A1568    CG   CD   CE   NZ                                   
REMARK 470     LYS A1600    CE   NZ                                             
REMARK 470     ILE A1602    CD1                                                 
REMARK 470     LYS A1610    CE   NZ                                             
REMARK 470     LYS A1673    CG   CD   CE   NZ                                   
REMARK 470     GLU A1674    CG   CD   OE1  OE2                                  
REMARK 470     ASN A1684    CG   OD1  ND2                                       
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       40.51   -105.07                                   
REMARK 500    VAL A1576      -65.84    -92.80                                   
REMARK 500    ASN A1622     -167.41   -127.77                                   
REMARK 500    PHE A1668       -8.32     73.57                                   
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 A1801  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1499   SG                                                     
REMARK 620 2 CYS A1501   SG  107.5                                              
REMARK 620 3 CYS A1516   SG  108.9 104.3                                        
REMARK 620 4 CYS A1520   SG  113.8 107.7 114.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1803  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1678   SG                                                     
REMARK 620 2 CYS A1680   SG  108.6                                              
REMARK 620 3 CYS A1631   SG  116.7 107.2                                        
REMARK 620 4 CYS A1685   SG  107.3 108.6 108.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1802  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1533   SG                                                     
REMARK 620 2 CYS A1539   SG  114.1                                              
REMARK 620 3 CYS A1516   SG   94.1 113.0                                        
REMARK 620 4 CYS A1529   SG  116.2 102.7 117.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1803                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH A 1804                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1805                 
DBREF  4H12 A 1434  1711  UNP    Q9BYW2   SETD2_HUMAN   1434   1711             
SEQRES   1 A  278  GLY GLU THR SER VAL PRO PRO GLY SER ALA LEU VAL GLY          
SEQRES   2 A  278  PRO SER CYS VAL MET ASP ASP PHE ARG ASP PRO GLN ARG          
SEQRES   3 A  278  TRP LYS GLU CYS ALA LYS GLN GLY LYS MET PRO CYS TYR          
SEQRES   4 A  278  PHE ASP LEU ILE GLU GLU ASN VAL TYR LEU THR GLU ARG          
SEQRES   5 A  278  LYS LYS ASN LYS SER HIS ARG ASP ILE LYS ARG MET GLN          
SEQRES   6 A  278  CYS GLU CYS THR PRO LEU SER LYS ASP GLU ARG ALA GLN          
SEQRES   7 A  278  GLY GLU ILE ALA CYS GLY GLU ASP CYS LEU ASN ARG LEU          
SEQRES   8 A  278  LEU MET ILE GLU CYS SER SER ARG CYS PRO ASN GLY ASP          
SEQRES   9 A  278  TYR CYS SER ASN ARG ARG PHE GLN ARG LYS GLN HIS ALA          
SEQRES  10 A  278  ASP VAL GLU VAL ILE LEU THR GLU LYS LYS GLY TRP GLY          
SEQRES  11 A  278  LEU ARG ALA ALA LYS ASP LEU PRO SER ASN THR PHE VAL          
SEQRES  12 A  278  LEU GLU TYR CYS GLY GLU VAL LEU ASP HIS LYS GLU PHE          
SEQRES  13 A  278  LYS ALA ARG VAL LYS GLU TYR ALA ARG ASN LYS ASN ILE          
SEQRES  14 A  278  HIS TYR TYR PHE MET ALA LEU LYS ASN ASP GLU ILE ILE          
SEQRES  15 A  278  ASP ALA THR GLN LYS GLY ASN CYS SER ARG PHE MET ASN          
SEQRES  16 A  278  HIS SER CYS GLU PRO ASN CYS GLU THR GLN LYS TRP THR          
SEQRES  17 A  278  VAL ASN GLY GLN LEU ARG VAL GLY PHE PHE THR THR LYS          
SEQRES  18 A  278  LEU VAL PRO SER GLY SER GLU LEU THR PHE ASP TYR GLN          
SEQRES  19 A  278  PHE GLN ARG TYR GLY LYS GLU ALA GLN LYS CYS PHE CYS          
SEQRES  20 A  278  GLY SER ALA ASN CYS ARG GLY TYR LEU GLY GLY GLU ASN          
SEQRES  21 A  278  ARG VAL SER ILE ARG ALA ALA GLY GLY LYS MET LYS LYS          
SEQRES  22 A  278  GLU ARG SER ARG LYS                                          
HET     ZN  A1801       1                                                       
HET     ZN  A1802       1                                                       
HET     ZN  A1803       1                                                       
HET    SAH  A1804      26                                                       
HET     CL  A1805       1                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     SAH S-ADENOSYL-L-HOMOCYSTEINE                                        
HETNAM      CL CHLORIDE ION                                                     
FORMUL   2   ZN    3(ZN 2+)                                                     
FORMUL   5  SAH    C14 H20 N6 O5 S                                              
FORMUL   6   CL    CL 1-                                                        
FORMUL   7  HOH   *124(H2 O)                                                    
HELIX    1   1 ASP A 1452  ARG A 1455  5                                   4    
HELIX    2   2 ASP A 1456  GLN A 1466  1                                  11    
HELIX    3   3 SER A 1505  GLY A 1512  1                                   8    
HELIX    4   4 ASN A 1522  MET A 1526  5                                   5    
HELIX    5   5 ASN A 1535  CYS A 1539  5                                   5    
HELIX    6   6 ASP A 1585  ASN A 1599  1                                  15    
HELIX    7   7 ASN A 1622  MET A 1627  5                                   6    
SHEET    1   A 5 SER A1448  VAL A1450  0                                        
SHEET    2   A 5 VAL A1552  LEU A1556 -1  O  VAL A1554   N  CYS A1449           
SHEET    3   A 5 TRP A1562  ALA A1566 -1  O  ARG A1565   N  GLU A1553           
SHEET    4   A 5 GLU A1661  PHE A1664 -1  O  LEU A1662   N  LEU A1564           
SHEET    5   A 5 ASN A1628  HIS A1629  1  N  ASN A1628   O  PHE A1664           
SHEET    1   B 2 ASP A1474  LEU A1475  0                                        
SHEET    2   B 2 LYS A1620  GLY A1621  1  O  GLY A1621   N  ASP A1474           
SHEET    1   C 5 VAL A1480  TYR A1481  0                                        
SHEET    2   C 5 GLU A1582  LEU A1584  1  O  VAL A1583   N  VAL A1480           
SHEET    3   C 5 GLU A1613  ASP A1616 -1  O  ILE A1614   N  LEU A1584           
SHEET    4   C 5 PHE A1606  LYS A1610 -1  N  MET A1607   O  ILE A1615           
SHEET    5   C 5 ARG A1670  TYR A1671 -1  O  TYR A1671   N  PHE A1606           
SHEET    1   D 3 PHE A1575  GLU A1578  0                                        
SHEET    2   D 3 GLN A1645  THR A1652 -1  O  PHE A1650   N  VAL A1576           
SHEET    3   D 3 CYS A1635  VAL A1642 -1  N  VAL A1642   O  GLN A1645           
SHEET    1   E 2 GLN A1676  LYS A1677  0                                        
SHEET    2   E 2 TYR A1688  LEU A1689 -1  O  LEU A1689   N  GLN A1676           
LINK         SG  CYS A1499                ZN    ZN A1801     1555   1555  2.22  
LINK         SG  CYS A1678                ZN    ZN A1803     1555   1555  2.23  
LINK         SG  CYS A1533                ZN    ZN A1802     1555   1555  2.24  
LINK         SG  CYS A1501                ZN    ZN A1801     1555   1555  2.27  
LINK         SG  CYS A1539                ZN    ZN A1802     1555   1555  2.29  
LINK         SG  CYS A1516                ZN    ZN A1802     1555   1555  2.35  
LINK         SG  CYS A1529                ZN    ZN A1802     1555   1555  2.35  
LINK         SG  CYS A1680                ZN    ZN A1803     1555   1555  2.36  
LINK         SG  CYS A1516                ZN    ZN A1801     1555   1555  2.39  
LINK         SG  CYS A1520                ZN    ZN A1801     1555   1555  2.40  
LINK         SG  CYS A1631                ZN    ZN A1803     1555   1555  2.43  
LINK         SG  CYS A1685                ZN    ZN A1803     1555   1555  2.43  
SITE     1 AC1  4 CYS A1499  CYS A1501  CYS A1516  CYS A1520                    
SITE     1 AC2  4 CYS A1516  CYS A1529  CYS A1533  CYS A1539                    
SITE     1 AC3  4 CYS A1631  CYS A1678  CYS A1680  CYS A1685                    
SITE     1 AC4 22 LYS A1560  GLY A1561  TRP A1562  ILE A1602                    
SITE     2 AC4 22 HIS A1603  TYR A1604  TYR A1605  ARG A1625                    
SITE     3 AC4 22 PHE A1626  ASN A1628  HIS A1629  TYR A1666                    
SITE     4 AC4 22 ARG A1670  GLN A1676  LYS A1677  CYS A1678                    
SITE     5 AC4 22 PHE A1679  LEU A1689  HOH A1914  HOH A1922                    
SITE     6 AC4 22 HOH A1963  HOH A1982                                          
SITE     1 AC5  3 GLU A1558  LYS A1559  LYS A1560                               
CRYST1   52.293   76.663   78.093  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      0.019123  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013044  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012805        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system