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Database: PDB
Entry: 5LT8
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HEADER    TRANSFERASE                             06-SEP-16   5LT8              
TITLE     STRUCTURE OF THE EPIGENETIC ONCOGENE MMSET AND INHIBITION BY N-ALKYL  
TITLE    2 SINEFUNGIN DERIVATIVES                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE SETD2;                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: HIF-1,HUNTINGTIN YEAST PARTNER B,HUNTINGTIN-INTERACTING     
COMPND   5 PROTEIN 1,HIP-1,HUNTINGTIN-INTERACTING PROTEIN B,LYSINE N-           
COMPND   6 METHYLTRANSFERASE 3A,SET DOMAIN-CONTAINING PROTEIN 2,HSET2,P231HBP;  
COMPND   7 EC: 2.1.1.43;                                                        
COMPND   8 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: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VARIANT:  CODON PLUS RIL                           
KEYWDS    LYSINE METHYLTRANSFERASE SETD2 SET DOMAIN, TRANSFERASE                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.TISI,P.PATHURI,T.HEIGHTMAN                                          
REVDAT   2   21-DEC-16 5LT8    1       JRNL                                     
REVDAT   1   05-OCT-16 5LT8    0                                                
JRNL        AUTH   D.TISI,E.CHIARPARIN,E.TAMANINI,P.PATHURI,J.E.COYLE,A.HOLD,   
JRNL        AUTH 2 F.P.HOLDING,N.AMIN,A.C.MARTIN,S.J.RICH,V.BERDINI,J.YON,      
JRNL        AUTH 3 P.ACKLAM,R.BURKE,L.DROUIN,J.E.HARMER,F.JEGANATHAN,           
JRNL        AUTH 4 R.L.VAN MONTFORT,Y.NEWBATT,M.TORTORICI,M.WESTLAKE,A.WOOD,    
JRNL        AUTH 5 S.HOELDER,T.D.HEIGHTMAN                                      
JRNL        TITL   STRUCTURE OF THE EPIGENETIC ONCOGENE MMSET AND INHIBITION BY 
JRNL        TITL 2 N-ALKYL SINEFUNGIN DERIVATIVES.                              
JRNL        REF    ACS CHEM. BIOL.               V.  11  3093 2016              
JRNL        REFN                   ESSN 1554-8937                               
JRNL        PMID   27571355                                                     
JRNL        DOI    10.1021/ACSCHEMBIO.6B00308                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.57 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0131                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.57                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.33                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 34914                          
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) : 0.176                           
REMARK   3   R VALUE            (WORKING SET) : 0.174                           
REMARK   3   FREE R VALUE                     : 0.216                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1817                            
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) : 1.57                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.61                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2561                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.30                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3230                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 117                          
REMARK   3   BIN FREE R VALUE                    : 0.3270                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1814                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 30                                      
REMARK   3   SOLVENT ATOMS            : 293                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.77                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.47000                                             
REMARK   3    B22 (A**2) : -0.30000                                             
REMARK   3    B33 (A**2) : 0.77000                                              
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): 0.080         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.086         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.067         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.675         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.969                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.952                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1918 ; 0.011 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  1766 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2588 ; 1.540 ; 1.949       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4082 ; 0.944 ; 2.985       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   236 ; 5.444 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    99 ;34.824 ;24.141       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   354 ;13.524 ;15.212       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    15 ;16.877 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   269 ; 0.096 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2189 ; 0.000 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   461 ; 0.000 ; 0.021       
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):   917 ; 2.190 ; 4.072       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   916 ; 2.163 ; 4.057       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1001 ; 3.126 ; 4.860       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1002 ; 3.124 ; 4.860       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):   705 ; 7.309 ; 9.681       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):   695 ; 7.359 ; 9.690       
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 : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A  1446        A  1716                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.3455  18.1859  23.7540              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0114 T22:   0.0210                                     
REMARK   3      T33:   0.0171 T12:   0.0034                                     
REMARK   3      T13:  -0.0018 T23:  -0.0107                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6174 L22:   1.8282                                     
REMARK   3      L33:   1.6928 L12:   0.2872                                     
REMARK   3      L13:  -0.2085 L23:  -0.7871                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0139 S12:   0.1415 S13:   0.0062                       
REMARK   3      S21:  -0.1427 S22:  -0.0225 S23:   0.0060                       
REMARK   3      S31:   0.0681 S32:  -0.0290 S33:   0.0364                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
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 ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 5LT8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-SEP-16.                  
REMARK 100 THE DEPOSITION ID IS D_1200001314.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-JUL-13                          
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               : DIAMOND                            
REMARK 200  BEAMLINE                       : I03                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 S 6M              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 268230                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.510                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.330                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 5.900                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
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: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: REFMAC                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 34.28                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.87                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES, PH7.3, 0.1MKSCN, 25          
REMARK 280  -30%MPEG2000, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K       
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       21.61800            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       38.42350            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       38.41800            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       38.42350            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       21.61800            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       38.41800            
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     MET A  1417                                                      
REMARK 465     HIS A  1418                                                      
REMARK 465     HIS A  1419                                                      
REMARK 465     HIS A  1420                                                      
REMARK 465     HIS A  1421                                                      
REMARK 465     HIS A  1422                                                      
REMARK 465     HIS A  1423                                                      
REMARK 465     SER A  1424                                                      
REMARK 465     SER A  1425                                                      
REMARK 465     GLY A  1426                                                      
REMARK 465     ARG A  1427                                                      
REMARK 465     GLU A  1428                                                      
REMARK 465     ASN A  1429                                                      
REMARK 465     LEU A  1430                                                      
REMARK 465     TYR A  1431                                                      
REMARK 465     PHE A  1432                                                      
REMARK 465     GLN 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     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     MET A  1497                                                      
REMARK 465     PHE A  1668                                                      
REMARK 465     GLN A  1669                                                      
REMARK 465     ARG A  1670                                                      
REMARK 465     TYR A  1671                                                      
REMARK 465     GLY A  1672                                                      
REMARK 465     LYS A  1673                                                      
REMARK 465     GLU A  1674                                                      
REMARK 465     GLY A  1691                                                      
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     LYS A1486    CG   CD   CE   NZ                                   
REMARK 470     ILE A1514    CD1                                                 
REMARK 470     ILE A1602    CD1                                                 
REMARK 470     GLN A1667    CG   CD   OE1  NE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A1598   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG A1647   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG A1647   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A1541       40.66   -106.84                                   
REMARK 500    VAL A1576      -65.93    -95.34                                   
REMARK 500    TYR A1605       42.06   -143.85                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A2192        DISTANCE =  5.82 ANGSTROMS                       
REMARK 525    HOH A2193        DISTANCE =  6.31 ANGSTROMS                       
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 A1802  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1499   SG                                                     
REMARK 620 2 CYS A1501   SG  106.9                                              
REMARK 620 3 CYS A1516   SG  105.4 107.8                                        
REMARK 620 4 CYS A1520   SG  115.6 110.5 110.2                                  
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 A1516   SG                                                     
REMARK 620 2 CYS A1529   SG  116.9                                              
REMARK 620 3 CYS A1533   SG   96.4 117.2                                        
REMARK 620 4 CYS A1539   SG  111.3 103.6 111.8                                  
REMARK 620 N                    1     2     3                                   
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 A1631   SG                                                     
REMARK 620 2 CYS A1678   SG  114.0                                              
REMARK 620 3 CYS A1680   SG  108.0 106.0                                        
REMARK 620 4 CYS A1685   SG  109.9 106.7 112.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 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 SFG A 1804                
DBREF  5LT8 A 1433  1711  UNP    Q9BYW2   SETD2_HUMAN   1433   1711             
SEQADV 5LT8 MET A 1417  UNP  Q9BYW2              INITIATING METHIONINE          
SEQADV 5LT8 HIS A 1418  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5LT8 HIS A 1419  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5LT8 HIS A 1420  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5LT8 HIS A 1421  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5LT8 HIS A 1422  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5LT8 HIS A 1423  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5LT8 SER A 1424  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5LT8 SER A 1425  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5LT8 GLY A 1426  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5LT8 ARG A 1427  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5LT8 GLU A 1428  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5LT8 ASN A 1429  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5LT8 LEU A 1430  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5LT8 TYR A 1431  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5LT8 PHE A 1432  UNP  Q9BYW2              EXPRESSION TAG                 
SEQRES   1 A  295  MET HIS HIS HIS HIS HIS HIS SER SER GLY ARG GLU ASN          
SEQRES   2 A  295  LEU TYR PHE GLN GLY GLU THR SER VAL PRO PRO GLY SER          
SEQRES   3 A  295  ALA LEU VAL GLY PRO SER CYS VAL MET ASP ASP PHE ARG          
SEQRES   4 A  295  ASP PRO GLN ARG TRP LYS GLU CYS ALA LYS GLN GLY LYS          
SEQRES   5 A  295  MET PRO CYS TYR PHE ASP LEU ILE GLU GLU ASN VAL TYR          
SEQRES   6 A  295  LEU THR GLU ARG LYS LYS ASN LYS SER HIS ARG ASP ILE          
SEQRES   7 A  295  LYS ARG MET GLN CYS GLU CYS THR PRO LEU SER LYS ASP          
SEQRES   8 A  295  GLU ARG ALA GLN GLY GLU ILE ALA CYS GLY GLU ASP CYS          
SEQRES   9 A  295  LEU ASN ARG LEU LEU MET ILE GLU CYS SER SER ARG CYS          
SEQRES  10 A  295  PRO ASN GLY ASP TYR CYS SER ASN ARG ARG PHE GLN ARG          
SEQRES  11 A  295  LYS GLN HIS ALA ASP VAL GLU VAL ILE LEU THR GLU LYS          
SEQRES  12 A  295  LYS GLY TRP GLY LEU ARG ALA ALA LYS ASP LEU PRO SER          
SEQRES  13 A  295  ASN THR PHE VAL LEU GLU TYR CYS GLY GLU VAL LEU ASP          
SEQRES  14 A  295  HIS LYS GLU PHE LYS ALA ARG VAL LYS GLU TYR ALA ARG          
SEQRES  15 A  295  ASN LYS ASN ILE HIS TYR TYR PHE MET ALA LEU LYS ASN          
SEQRES  16 A  295  ASP GLU ILE ILE ASP ALA THR GLN LYS GLY ASN CYS SER          
SEQRES  17 A  295  ARG PHE MET ASN HIS SER CYS GLU PRO ASN CYS GLU THR          
SEQRES  18 A  295  GLN LYS TRP THR VAL ASN GLY GLN LEU ARG VAL GLY PHE          
SEQRES  19 A  295  PHE THR THR LYS LEU VAL PRO SER GLY SER GLU LEU THR          
SEQRES  20 A  295  PHE ASP TYR GLN PHE GLN ARG TYR GLY LYS GLU ALA GLN          
SEQRES  21 A  295  LYS CYS PHE CYS GLY SER ALA ASN CYS ARG GLY TYR LEU          
SEQRES  22 A  295  GLY GLY GLU ASN ARG VAL SER ILE ARG ALA ALA GLY GLY          
SEQRES  23 A  295  LYS MET LYS LYS GLU ARG SER ARG LYS                          
HET     ZN  A1801       1                                                       
HET     ZN  A1802       1                                                       
HET     ZN  A1803       1                                                       
HET    SFG  A1804      51                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     SFG SINEFUNGIN                                                       
HETSYN     SFG ADENOSYL-ORNITHINE                                               
FORMUL   2   ZN    3(ZN 2+)                                                     
FORMUL   5  SFG    C15 H23 N7 O5                                                
FORMUL   6  HOH   *293(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 CYS A 1623  MET A 1627  5                                   5    
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 4 ASP A1474  LEU A1475  0                                        
SHEET    2 AA2 4 GLU A1613  GLY A1621  1  O  GLN A1619   N  ASP A1474           
SHEET    3 AA2 4 GLY A1581  LEU A1584 -1  N  LEU A1584   O  ILE A1614           
SHEET    4 AA2 4 VAL A1480  TYR A1481  1  N  VAL A1480   O  VAL A1583           
SHEET    1 AA3 3 ASP A1474  LEU A1475  0                                        
SHEET    2 AA3 3 GLU A1613  GLY A1621  1  O  GLN A1619   N  ASP A1474           
SHEET    3 AA3 3 PHE A1606  LYS A1610 -1  N  MET A1607   O  ILE A1615           
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 A1802     1555   1555  2.33  
LINK         SG  CYS A1501                ZN    ZN A1802     1555   1555  2.33  
LINK         SG  CYS A1516                ZN    ZN A1803     1555   1555  2.33  
LINK         SG  CYS A1516                ZN    ZN A1802     1555   1555  2.41  
LINK         SG  CYS A1520                ZN    ZN A1802     1555   1555  2.30  
LINK         SG  CYS A1529                ZN    ZN A1803     1555   1555  2.34  
LINK         SG  CYS A1533                ZN    ZN A1803     1555   1555  2.28  
LINK         SG  CYS A1539                ZN    ZN A1803     1555   1555  2.28  
LINK         SG  CYS A1631                ZN    ZN A1801     1555   1555  2.42  
LINK         SG  CYS A1678                ZN    ZN A1801     1555   1555  2.30  
LINK         SG  CYS A1680                ZN    ZN A1801     1555   1555  2.38  
LINK         SG  CYS A1685                ZN    ZN A1801     1555   1555  2.35  
SITE     1 AC1  4 CYS A1631  CYS A1678  CYS A1680  CYS A1685                    
SITE     1 AC2  4 CYS A1499  CYS A1501  CYS A1516  CYS A1520                    
SITE     1 AC3  4 CYS A1516  CYS A1529  CYS A1533  CYS A1539                    
SITE     1 AC4 21 LYS A1560  GLY A1561  TRP A1562  ILE A1602                    
SITE     2 AC4 21 HIS A1603  TYR A1604  TYR A1605  ARG A1625                    
SITE     3 AC4 21 PHE A1626  ASN A1628  HIS A1629  TYR A1666                    
SITE     4 AC4 21 GLN A1676  LYS A1677  CYS A1678  PHE A1679                    
SITE     5 AC4 21 LEU A1689  HOH A1974  HOH A1975  HOH A2044                    
SITE     6 AC4 21 HOH A2097                                                     
CRYST1   43.236   76.836   76.847  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      0.023129  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013015  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013013        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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