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Database: PDB
Entry: 5LSY
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HEADER    TRANSFERASE                             05-SEP-16   5LSY              
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 FRAGMENT: UNP RESIDUES 1433-1711;                                    
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                                                      
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 BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: CODON PLUS RIL                            
KEYWDS    LYSINE METHYLTRANSFERASE SETD2 SET DOMAIN, SETD2#1, TRANSFERASE       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.TISI,P.PATHURI,T.HEIGHTMAN                                          
REVDAT   2   21-DEC-16 5LSY    1       JRNL                                     
REVDAT   1   12-OCT-16 5LSY    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.    1.62 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) : 1.62                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.89                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 31691                          
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) : 0.183                           
REMARK   3   R VALUE            (WORKING SET) : 0.181                           
REMARK   3   FREE R VALUE                     : 0.215                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1659                            
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) : 1.62                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.66                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1375                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 54.08                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3280                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 70                           
REMARK   3   BIN FREE R VALUE                    : 0.3250                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1964                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 37                                      
REMARK   3   SOLVENT ATOMS            : 405                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.26                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.02000                                             
REMARK   3    B22 (A**2) : 0.06000                                              
REMARK   3    B33 (A**2) : -0.05000                                             
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): 0.103         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.101         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.073         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.856         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.951                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.937                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2090 ; 0.011 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  1932 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2821 ; 1.483 ; 1.949       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4464 ; 0.939 ; 2.975       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   257 ; 6.023 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   107 ;33.478 ;23.832       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   382 ;13.146 ;15.314       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;16.593 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   291 ; 0.092 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2393 ; 0.000 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   508 ; 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):  1002 ; 1.256 ; 2.002       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1000 ; 1.193 ; 1.992       
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):  1088 ; 1.780 ; 2.381       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1088 ; 1.780 ; 2.381       
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):   764 ; 4.691 ; 4.793       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):   765 ; 4.687 ; 4.791       
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  1434        A  1803                          
REMARK   3    ORIGIN FOR THE GROUP (A):   8.8508  23.4739  30.9312              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0222 T22:   0.0262                                     
REMARK   3      T33:   0.0020 T12:  -0.0074                                     
REMARK   3      T13:   0.0031 T23:   0.0021                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9038 L22:   1.5540                                     
REMARK   3      L33:   0.7917 L12:  -0.8318                                     
REMARK   3      L13:   0.1058 L23:  -0.0705                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0256 S12:   0.1886 S13:   0.0430                       
REMARK   3      S21:  -0.0292 S22:  -0.0144 S23:  -0.0413                       
REMARK   3      S31:  -0.1283 S32:   0.0626 S33:  -0.0112                       
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 5LSY 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_1200001309.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-JUN-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               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.976                              
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   : 182683                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.620                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.893                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.9                               
REMARK 200  DATA REDUNDANCY                : 5.300                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.6000                            
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: 3OOI                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.18                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.06                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES, PH7.3, 0.1MKSCN, 25          
REMARK 280  -30%MPEG2000, VAPOR DIFFUSION, 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       29.49150            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       38.65400            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       30.75200            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       38.65400            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       29.49150            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       30.75200            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 250 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 15140 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL                        
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     GLU A  1484                                                      
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     SER A  1505                                                      
REMARK 465     LYS A  1506                                                      
REMARK 465     ASP A  1507                                                      
REMARK 465     GLU A  1508                                                      
REMARK 465     ARG A  1509                                                      
REMARK 465     ALA A  1510                                                      
REMARK 465     GLN A  1511                                                      
REMARK 465     GLY A  1512                                                      
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 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   NH1  ARG A  1546     O    HOH A  1902              2.11            
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    VAL A1445      -63.25    -97.04                                   
REMARK 500    VAL A1576      -64.89    -90.38                                   
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 A2295        DISTANCE =  5.84 ANGSTROMS                       
REMARK 525    HOH A2296        DISTANCE =  5.86 ANGSTROMS                       
REMARK 525    HOH A2297        DISTANCE =  5.88 ANGSTROMS                       
REMARK 525    HOH A2298        DISTANCE =  5.98 ANGSTROMS                       
REMARK 525    HOH A2299        DISTANCE =  6.33 ANGSTROMS                       
REMARK 525    HOH A2300        DISTANCE =  6.43 ANGSTROMS                       
REMARK 525    HOH A2301        DISTANCE =  6.46 ANGSTROMS                       
REMARK 525    HOH A2302        DISTANCE =  6.69 ANGSTROMS                       
REMARK 525    HOH A2303        DISTANCE =  6.78 ANGSTROMS                       
REMARK 525    HOH A2304        DISTANCE =  6.87 ANGSTROMS                       
REMARK 525    HOH A2305        DISTANCE =  7.08 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 A1801  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1499   SG                                                     
REMARK 620 2 CYS A1501   SG  107.0                                              
REMARK 620 3 CYS A1516   SG  109.9 103.2                                        
REMARK 620 4 CYS A1520   SG  116.2 107.2 112.3                                  
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 A1516   SG                                                     
REMARK 620 2 CYS A1529   SG  115.0                                              
REMARK 620 3 CYS A1533   SG   94.7 117.6                                        
REMARK 620 4 CYS A1539   SG  113.4 104.0 112.6                                  
REMARK 620 5 SCN A1804   S    95.0  59.4  64.7 151.5                            
REMARK 620 N                    1     2     3     4                             
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 A1631   SG                                                     
REMARK 620 2 CYS A1678   SG  111.1                                              
REMARK 620 3 CYS A1680   SG  108.8 107.9                                        
REMARK 620 4 CYS A1685   SG  110.2 109.7 109.0                                  
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 SCN A 1804                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 76M A 1805                
DBREF  5LSY A 1433  1711  UNP    Q9BYW2   SETD2_HUMAN   1433   1711             
SEQADV 5LSY MET A 1417  UNP  Q9BYW2              INITIATING METHIONINE          
SEQADV 5LSY HIS A 1418  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5LSY HIS A 1419  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5LSY HIS A 1420  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5LSY HIS A 1421  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5LSY HIS A 1422  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5LSY HIS A 1423  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5LSY SER A 1424  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5LSY SER A 1425  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5LSY GLY A 1426  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5LSY ARG A 1427  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5LSY GLU A 1428  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5LSY ASN A 1429  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5LSY LEU A 1430  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5LSY TYR A 1431  UNP  Q9BYW2              EXPRESSION TAG                 
SEQADV 5LSY 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    SCN  A1804       3                                                       
HET    76M  A1805      63                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     SCN THIOCYANATE ION                                                  
HETNAM     76M [(2~{S},5~{R})-1-[(2~{R},3~{S},4~{R},5~{R})-5-(6-                
HETNAM   2 76M  AMINOPURIN-9-YL)-3,4-BIS(OXIDANYL)OXOLAN-2-YL]-5-               
HETNAM   3 76M  AZANIUMYL-6-OXIDANYL-6-OXIDANYLIDENE-HEXAN-2-YL]-(2-            
HETNAM   4 76M  METHYLPROPYL)AZANIUM                                            
FORMUL   2   ZN    3(ZN 2+)                                                     
FORMUL   5  SCN    C N S 1-                                                     
FORMUL   6  76M    C19 H33 N7 O5 2+                                             
FORMUL   7  HOH   *405(H2 O)                                                    
HELIX    1 AA1 VAL A 1450  ARG A 1455  5                                   6    
HELIX    2 AA2 ASP A 1456  GLN A 1466  1                                  11    
HELIX    3 AA3 CYS A 1520  LEU A 1525  1                                   6    
HELIX    4 AA4 ASN A 1535  CYS A 1539  5                                   5    
HELIX    5 AA5 ARG A 1542  LYS A 1547  1                                   6    
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 TYR A 1666  TYR A 1671  1                                   6    
SHEET    1 AA1 2 ASP A1474  LEU A1475  0                                        
SHEET    2 AA1 2 LYS A1620  GLY A1621  1  O  GLY A1621   N  ASP A1474           
SHEET    1 AA2 4 VAL A1480  TYR A1481  0                                        
SHEET    2 AA2 4 GLU A1582  LEU A1584  1  O  VAL A1583   N  VAL A1480           
SHEET    3 AA2 4 GLU A1613  ASP A1616 -1  O  ILE A1614   N  LEU A1584           
SHEET    4 AA2 4 PHE A1606  LYS A1610 -1  N  MET A1607   O  ILE A1615           
SHEET    1 AA3 4 VAL A1552  LEU A1556  0                                        
SHEET    2 AA3 4 TRP A1562  ALA A1566 -1  O  ARG A1565   N  GLU A1553           
SHEET    3 AA3 4 GLU A1661  PHE A1664 -1  O  LEU A1662   N  LEU A1564           
SHEET    4 AA3 4 ASN A1628  HIS A1629  1  N  ASN A1628   O  PHE A1664           
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  GLU A1636   O  PHE A1651           
SHEET    1 AA5 2 ALA A1675  LYS A1677  0                                        
SHEET    2 AA5 2 TYR A1688  GLY A1690 -1  O  LEU A1689   N  GLN A1676           
SSBOND   1 CYS A 1449    CYS A 1463                          1555   1555  2.08  
LINK         SG  CYS A1499                ZN    ZN A1801     1555   1555  2.22  
LINK         SG  CYS A1501                ZN    ZN A1801     1555   1555  2.39  
LINK         SG  CYS A1516                ZN    ZN A1802     1555   1555  2.39  
LINK         SG  CYS A1516                ZN    ZN A1801     1555   1555  2.47  
LINK         SG  CYS A1520                ZN    ZN A1801     1555   1555  2.36  
LINK         SG  CYS A1529                ZN    ZN A1802     1555   1555  2.32  
LINK         SG  CYS A1533                ZN    ZN A1802     1555   1555  2.36  
LINK         SG  CYS A1539                ZN    ZN A1802     1555   1555  2.24  
LINK         SG  CYS A1631                ZN    ZN A1803     1555   1555  2.35  
LINK         SG  CYS A1678                ZN    ZN A1803     1555   1555  2.34  
LINK         SG  CYS A1680                ZN    ZN A1803     1555   1555  2.35  
LINK         SG  CYS A1685                ZN    ZN A1803     1555   1555  2.34  
LINK        ZN    ZN A1802                 S   SCN A1804     1555   1555  2.54  
SITE     1 AC1  5 CYS A1499  CYS A1501  CYS A1516  CYS A1520                    
SITE     2 AC1  5 SCN A1804                                                     
SITE     1 AC2  5 CYS A1516  CYS A1529  CYS A1533  CYS A1539                    
SITE     2 AC2  5 SCN A1804                                                     
SITE     1 AC3  4 CYS A1631  CYS A1678  CYS A1680  CYS A1685                    
SITE     1 AC4 11 MET A1497  GLN A1498  CYS A1499  CYS A1516                    
SITE     2 AC4 11 ASN A1522  CYS A1529  CYS A1533  PRO A1534                    
SITE     3 AC4 11  ZN A1801   ZN A1802  HOH A1904                               
SITE     1 AC5 26 GLY A1434  LYS A1560  GLY A1561  TRP A1562                    
SITE     2 AC5 26 TYR A1579  ILE A1602  HIS A1603  TYR A1604                    
SITE     3 AC5 26 TYR A1605  SER A1624  ARG A1625  PHE A1626                    
SITE     4 AC5 26 MET A1627  ASN A1628  HIS A1629  TYR A1666                    
SITE     5 AC5 26 GLN A1669  GLN A1676  LYS A1677  CYS A1678                    
SITE     6 AC5 26 PHE A1679  CYS A1680  HOH A1961  HOH A1981                    
SITE     7 AC5 26 HOH A1995  HOH A2053                                          
CRYST1   58.983   61.504   77.308  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      0.016954  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.016259  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012935        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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