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Database: PDB
Entry: 3F9Y
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HEADER    TRANSFERASE                             14-NOV-08   3F9Y              
TITLE     STRUCTURAL INSIGHTS INTO LYSINE MULTIPLE METHYLATION BY SET DOMAIN    
TITLE    2 METHYLTRANSFERASES, SET8-Y334F / H4-LYS20ME1 / ADOHCY                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE SETD8;                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: SET DOMAIN: UNP RESIDUES 232-393;                          
COMPND   5 SYNONYM: H4-K20-HMTASE SETD8, SET DOMAIN-CONTAINING PROTEIN 8, PR/SET
COMPND   6 DOMAIN-CONTAINING PROTEIN 07, PR/SET07, PR-SET7, LYSINE N-           
COMPND   7 METHYLTRANSFERASE 5A;                                                
COMPND   8 EC: 2.1.1.43;                                                        
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MUTATION: YES;                                                       
COMPND  11 MOL_ID: 2;                                                           
COMPND  12 MOLECULE: HISTONE H4;                                                
COMPND  13 CHAIN: E, F;                                                         
COMPND  14 FRAGMENT: UNP RESIDUES 16-25;                                        
COMPND  15 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_TAXID: 9606;                                                
SOURCE   4 GENE: SETD8, KMT5A, PRSET7, SET07, SET8;                             
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PARALLEL;                                  
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PHIS2;                                    
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 OTHER_DETAILS: SYNTHETIC PEPTIDE CORRESPONDING TO RESIDUES 16-25 OF  
SOURCE  14 HUMAN HISTONE H4                                                     
KEYWDS    METHYLTRANSFERASE, HISTONE, SET, LYSINE, CELL CYCLE, CELL DIVISION,   
KEYWDS   2 CHROMATIN REGULATOR, CHROMOSOMAL PROTEIN, MITOSIS, NUCLEUS,          
KEYWDS   3 REPRESSOR, S-ADENOSYL-L-METHIONINE, TRANSCRIPTION, TRANSCRIPTION     
KEYWDS   4 REGULATION, DNA-BINDING, METHYLATION, NUCLEOSOME CORE, TRANSFERASE   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.-F.COUTURE,L.M.A.DIRK,J.S.BRUNZELLE,R.L.HOUTZ,R.C.TRIEVEL           
REVDAT   7   24-JAN-18 3F9Y    1       AUTHOR                                   
REVDAT   6   09-APR-14 3F9Y    1       REMARK                                   
REVDAT   5   13-JUL-11 3F9Y    1       VERSN                                    
REVDAT   4   09-JUN-09 3F9Y    1       REVDAT                                   
REVDAT   3   24-FEB-09 3F9Y    1       VERSN                                    
REVDAT   2   13-JAN-09 3F9Y    1       JRNL                                     
REVDAT   1   25-NOV-08 3F9Y    0                                                
JRNL        AUTH   J.F.COUTURE,L.M.DIRK,J.S.BRUNZELLE,R.L.HOUTZ,R.C.TRIEVEL     
JRNL        TITL   STRUCTURAL ORIGINS FOR THE PRODUCT SPECIFICITY OF SET DOMAIN 
JRNL        TITL 2 PROTEIN METHYLTRANSFERASES.                                  
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 105 20659 2008              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   19088188                                                     
JRNL        DOI    10.1073/PNAS.0806712105                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 23.68                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 53407                          
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) : 0.195                           
REMARK   3   R VALUE            (WORKING SET) : 0.194                           
REMARK   3   FREE R VALUE                     : 0.220                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2811                            
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) : 1.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.54                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3860                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3340                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 203                          
REMARK   3   BIN FREE R VALUE                    : 0.4150                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2680                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 52                                      
REMARK   3   SOLVENT ATOMS            : 227                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.44                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.25000                                             
REMARK   3    B22 (A**2) : 0.21000                                              
REMARK   3    B33 (A**2) : 0.12000                                              
REMARK   3    B12 (A**2) : -0.05000                                             
REMARK   3    B13 (A**2) : 0.10000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.079         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.079         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.055         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.931         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.969                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.959                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2801 ; 0.019 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3758 ; 1.895 ; 1.994       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   330 ; 6.543 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   137 ;29.569 ;23.431       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   520 ;14.017 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    25 ;17.717 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   402 ; 0.123 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2091 ; 0.009 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1246 ; 0.217 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1884 ; 0.308 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   213 ; 0.159 ; 0.200       
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):    45 ; 0.235 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    24 ; 0.205 ; 0.200       
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):  1721 ; 1.216 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2652 ; 1.862 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1241 ; 2.794 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1106 ; 4.082 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   194        A   352                          
REMARK   3    RESIDUE RANGE :   E    16        E    22                          
REMARK   3    ORIGIN FOR THE GROUP (A): -19.5400 -16.2540  18.1240              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0332 T22:  -0.1537                                     
REMARK   3      T33:  -0.1487 T12:   0.0351                                     
REMARK   3      T13:  -0.0135 T23:   0.0267                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7562 L22:   2.3936                                     
REMARK   3      L33:   4.1035 L12:   0.5272                                     
REMARK   3      L13:   0.6024 L23:  -0.2968                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1429 S12:  -0.1435 S13:  -0.2696                       
REMARK   3      S21:   0.1600 S22:  -0.0695 S23:  -0.1678                       
REMARK   3      S31:   0.3398 S32:   0.1593 S33:  -0.0734                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   193        B   352                          
REMARK   3    RESIDUE RANGE :   F    16        F    23                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.6980  -0.4140  -0.1110              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0296 T22:  -0.1552                                     
REMARK   3      T33:  -0.1686 T12:   0.0012                                     
REMARK   3      T13:  -0.0104 T23:   0.0125                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0643 L22:   2.2281                                     
REMARK   3      L33:   1.8998 L12:  -0.5651                                     
REMARK   3      L13:  -0.6343 L23:   0.5594                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0344 S12:   0.0200 S13:   0.1125                       
REMARK   3      S21:   0.1019 S22:  -0.0103 S23:   0.1314                       
REMARK   3      S31:  -0.0722 S32:   0.0136 S33:   0.0447                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B   186                          
REMARK   3    RESIDUE RANGE :   B   353        B   393                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.5520  -7.6317   8.5359              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0956 T22:  -0.0524                                     
REMARK   3      T33:  -0.0340 T12:   0.0279                                     
REMARK   3      T13:  -0.0176 T23:   0.0028                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3504 L22:   0.2550                                     
REMARK   3      L33:   0.8537 L12:   0.5185                                     
REMARK   3      L13:  -0.8040 L23:  -0.3120                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0267 S12:  -0.0369 S13:  -0.0245                       
REMARK   3      S21:   0.0126 S22:   0.0009 S23:   0.0064                       
REMARK   3      S31:   0.0179 S32:   0.0431 S33:   0.0258                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
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 3F9Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-NOV-08.                  
REMARK 100 THE DEPOSITION ID IS D_1000050331.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-FEB-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 200                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : SI(220) SAGITAL FOCUSING           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 55907                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : 7.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 22.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.60                     
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) : 0.52800                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 8.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1ZKK                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.64                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PENTAERYTHRITOL ETHOXYLATE, 50MM     
REMARK 280  AMMONIUM SULFATE, 50MM BIS-TRIS, PH 6.5, VAPOR DIFFUSION,           
REMARK 280  HANGING DROP, TEMPERATURE 298K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1550 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9240 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.5 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E                                  
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1570 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9620 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.1 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, F                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A   187                                                      
REMARK 465     ALA A   188                                                      
REMARK 465     MET A   189                                                      
REMARK 465     GLY A   190                                                      
REMARK 465     SER A   191                                                      
REMARK 465     ARG A   192                                                      
REMARK 465     LYS A   193                                                      
REMARK 465     GLY B   187                                                      
REMARK 465     ALA B   188                                                      
REMARK 465     MET B   189                                                      
REMARK 465     GLY B   190                                                      
REMARK 465     SER B   191                                                      
REMARK 465     ARG B   192                                                      
REMARK 465     ALA E    15                                                      
REMARK 465     ARG E    23                                                      
REMARK 465     ASP E    24                                                      
REMARK 465     ALA F    15                                                      
REMARK 465     ASP F    24                                                      
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 F  16    CG   CD   CE   NZ                                   
REMARK 470     ARG F  23    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH B   111     O    HOH B   378              2.13            
REMARK 500   OH   TYR A   277     OD2  ASP A   311              2.14            
REMARK 500   OE1  GLN B   235     O    HOH B   112              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH B   121     O    HOH B   127     1556     2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    SER A 194   CB    SER A 194   OG      0.082                       
REMARK 500    TYR B 273   CZ    TYR B 273   CE2     0.078                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 339   NE  -  CZ  -  NH1 ANGL. DEV. =   4.7 DEGREES          
REMARK 500    ARG A 339   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.4 DEGREES          
REMARK 500    ARG B 324   NE  -  CZ  -  NH2 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ARG B 339   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.7 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    VAL A 242      -60.46    -99.63                                   
REMARK 500    VAL B 242      -61.42   -105.96                                   
REMARK 500    LEU B 278     -121.35     55.97                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH A 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH B 801                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1ZKK   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HSET8 IN TERNARY COMPLEX WITH H4 PEPTIDE (16-   
REMARK 900 24) AND ADOHCY                                                       
REMARK 900 RELATED ID: 3F9W   RELATED DB: PDB                                   
REMARK 900 STRUCTURAL INSIGHTS INTO LYSINE MULTIPLE METHYLATION BY SET DOMAIN   
REMARK 900 METHYLTRANSFERASES, SET8-Y334F / H4-LYS20 / ADOHCY                   
REMARK 900 RELATED ID: 3F9X   RELATED DB: PDB                                   
REMARK 900 STRUCTURAL INSIGHTS INTO LYSINE MULTIPLE METHYLATION BY SET DOMAIN   
REMARK 900 METHYLTRANSFERASES, SET8-Y334F / H4-LYS20ME2 / ADOHCY                
REMARK 900 RELATED ID: 3F9Z   RELATED DB: PDB                                   
REMARK 900 STRUCTURAL INSIGHTS INTO LYSINE MULTIPLE METHYLATION BY SET DOMAIN   
REMARK 900 METHYLTRANSFERASES, SET8-Y245F / H4-LYS20 / ADOHCY                   
DBREF  3F9Y A  191   352  UNP    Q9NQR1   SETD8_HUMAN    232    393             
DBREF  3F9Y B  191   352  UNP    Q9NQR1   SETD8_HUMAN    232    393             
DBREF  3F9Y E   15    24  UNP    P62805   H4_HUMAN        16     25             
DBREF  3F9Y F   15    24  UNP    P62805   H4_HUMAN        16     25             
SEQADV 3F9Y GLY A  187  UNP  Q9NQR1              EXPRESSION TAG                 
SEQADV 3F9Y ALA A  188  UNP  Q9NQR1              EXPRESSION TAG                 
SEQADV 3F9Y MET A  189  UNP  Q9NQR1              EXPRESSION TAG                 
SEQADV 3F9Y GLY A  190  UNP  Q9NQR1              EXPRESSION TAG                 
SEQADV 3F9Y PHE A  334  UNP  Q9NQR1    TYR   375 ENGINEERED                     
SEQADV 3F9Y GLY B  187  UNP  Q9NQR1              EXPRESSION TAG                 
SEQADV 3F9Y ALA B  188  UNP  Q9NQR1              EXPRESSION TAG                 
SEQADV 3F9Y MET B  189  UNP  Q9NQR1              EXPRESSION TAG                 
SEQADV 3F9Y GLY B  190  UNP  Q9NQR1              EXPRESSION TAG                 
SEQADV 3F9Y PHE B  334  UNP  Q9NQR1    TYR   375 ENGINEERED                     
SEQRES   1 A  166  GLY ALA MET GLY SER ARG LYS SER LYS ALA GLU LEU GLN          
SEQRES   2 A  166  SER GLU GLU ARG LYS ARG ILE ASP GLU LEU ILE GLU SER          
SEQRES   3 A  166  GLY LYS GLU GLU GLY MET LYS ILE ASP LEU ILE ASP GLY          
SEQRES   4 A  166  LYS GLY ARG GLY VAL ILE ALA THR LYS GLN PHE SER ARG          
SEQRES   5 A  166  GLY ASP PHE VAL VAL GLU TYR HIS GLY ASP LEU ILE GLU          
SEQRES   6 A  166  ILE THR ASP ALA LYS LYS ARG GLU ALA LEU TYR ALA GLN          
SEQRES   7 A  166  ASP PRO SER THR GLY CYS TYR MET TYR TYR PHE GLN TYR          
SEQRES   8 A  166  LEU SER LYS THR TYR CYS VAL ASP ALA THR ARG GLU THR          
SEQRES   9 A  166  ASN ARG LEU GLY ARG LEU ILE ASN HIS SER LYS CYS GLY          
SEQRES  10 A  166  ASN CYS GLN THR LYS LEU HIS ASP ILE ASP GLY VAL PRO          
SEQRES  11 A  166  HIS LEU ILE LEU ILE ALA SER ARG ASP ILE ALA ALA GLY          
SEQRES  12 A  166  GLU GLU LEU LEU PHE ASP TYR GLY ASP ARG SER LYS ALA          
SEQRES  13 A  166  SER ILE GLU ALA HIS PRO TRP LEU LYS HIS                      
SEQRES   1 B  166  GLY ALA MET GLY SER ARG LYS SER LYS ALA GLU LEU GLN          
SEQRES   2 B  166  SER GLU GLU ARG LYS ARG ILE ASP GLU LEU ILE GLU SER          
SEQRES   3 B  166  GLY LYS GLU GLU GLY MET LYS ILE ASP LEU ILE ASP GLY          
SEQRES   4 B  166  LYS GLY ARG GLY VAL ILE ALA THR LYS GLN PHE SER ARG          
SEQRES   5 B  166  GLY ASP PHE VAL VAL GLU TYR HIS GLY ASP LEU ILE GLU          
SEQRES   6 B  166  ILE THR ASP ALA LYS LYS ARG GLU ALA LEU TYR ALA GLN          
SEQRES   7 B  166  ASP PRO SER THR GLY CYS TYR MET TYR TYR PHE GLN TYR          
SEQRES   8 B  166  LEU SER LYS THR TYR CYS VAL ASP ALA THR ARG GLU THR          
SEQRES   9 B  166  ASN ARG LEU GLY ARG LEU ILE ASN HIS SER LYS CYS GLY          
SEQRES  10 B  166  ASN CYS GLN THR LYS LEU HIS ASP ILE ASP GLY VAL PRO          
SEQRES  11 B  166  HIS LEU ILE LEU ILE ALA SER ARG ASP ILE ALA ALA GLY          
SEQRES  12 B  166  GLU GLU LEU LEU PHE ASP TYR GLY ASP ARG SER LYS ALA          
SEQRES  13 B  166  SER ILE GLU ALA HIS PRO TRP LEU LYS HIS                      
SEQRES   1 E   10  ALA LYS ARG HIS ARG MLZ VAL LEU ARG ASP                      
SEQRES   1 F   10  ALA LYS ARG HIS ARG MLZ VAL LEU ARG ASP                      
MODRES 3F9Y MLZ E   20  LYS  N-METHYL-LYSINE                                    
MODRES 3F9Y MLZ F   20  LYS  N-METHYL-LYSINE                                    
HET    MLZ  E  20      10                                                       
HET    MLZ  F  20      10                                                       
HET    SAH  A 801      26                                                       
HET    SAH  B 801      26                                                       
HETNAM     MLZ N-METHYL-LYSINE                                                  
HETNAM     SAH S-ADENOSYL-L-HOMOCYSTEINE                                        
FORMUL   3  MLZ    2(C7 H16 N2 O2)                                              
FORMUL   5  SAH    2(C14 H20 N6 O5 S)                                           
FORMUL   7  HOH   *227(H2 O)                                                    
HELIX    1   1 SER A  194  GLY A  213  1                                  20    
HELIX    2   2 ILE A  252  ALA A  263  1                                  12    
HELIX    3   3 LEU A  293  ILE A  297  5                                   5    
HELIX    4   4 SER A  340  HIS A  347  1                                   8    
HELIX    5   5 PRO A  348  HIS A  352  5                                   5    
HELIX    6   6 SER B  194  GLY B  213  1                                  20    
HELIX    7   7 ILE B  252  ALA B  263  1                                  12    
HELIX    8   8 LEU B  293  ILE B  297  5                                   5    
HELIX    9   9 SER B  340  HIS B  347  1                                   8    
HELIX   10  10 PRO B  348  HIS B  352  5                                   5    
SHEET    1   A 2 MET A 218  ILE A 223  0                                        
SHEET    2   A 2 GLY A 227  ALA A 232 -1  O  GLY A 227   N  ILE A 223           
SHEET    1   B 3 PHE A 241  TYR A 245  0                                        
SHEET    2   B 3 VAL A 315  ALA A 322 -1  O  LEU A 320   N  VAL A 243           
SHEET    3   B 3 CYS A 305  ILE A 312 -1  N  HIS A 310   O  HIS A 317           
SHEET    1   C 4 ASP A 248  GLU A 251  0                                        
SHEET    2   C 4 LYS A 280  ASP A 285 -1  O  ASP A 285   N  ASP A 248           
SHEET    3   C 4 MET A 272  TYR A 277 -1  N  TYR A 277   O  LYS A 280           
SHEET    4   C 4 MLZ E  20  VAL E  21  1  O  MLZ E  20   N  TYR A 274           
SHEET    1   D 2 ASN A 298  HIS A 299  0                                        
SHEET    2   D 2 LEU A 333  PHE A 334  1  O  PHE A 334   N  ASN A 298           
SHEET    1   E 2 MET B 218  ILE B 223  0                                        
SHEET    2   E 2 GLY B 227  ALA B 232 -1  O  ILE B 231   N  LYS B 219           
SHEET    1   F 3 PHE B 241  TYR B 245  0                                        
SHEET    2   F 3 VAL B 315  ALA B 322 -1  O  LEU B 320   N  VAL B 243           
SHEET    3   F 3 CYS B 305  ILE B 312 -1  N  HIS B 310   O  HIS B 317           
SHEET    1   G 4 ASP B 248  GLU B 251  0                                        
SHEET    2   G 4 LYS B 280  ASP B 285 -1  O  CYS B 283   N  ILE B 250           
SHEET    3   G 4 MET B 272  TYR B 277 -1  N  PHE B 275   O  TYR B 282           
SHEET    4   G 4 MLZ F  20  VAL F  21  1  O  MLZ F  20   N  TYR B 274           
SHEET    1   H 2 ASN B 298  HIS B 299  0                                        
SHEET    2   H 2 LEU B 333  PHE B 334  1  O  PHE B 334   N  ASN B 298           
LINK         C   ARG E  19                 N   MLZ E  20     1555   1555  1.34  
LINK         C   MLZ E  20                 N   VAL E  21     1555   1555  1.31  
LINK         C   ARG F  19                 N   MLZ F  20     1555   1555  1.35  
LINK         C   MLZ F  20                 N   VAL F  21     1555   1555  1.31  
SITE     1 AC1 17 GLY A 225  LYS A 226  ARG A 228  TYR A 271                    
SITE     2 AC1 17 ARG A 295  LEU A 296  ASN A 298  HIS A 299                    
SITE     3 AC1 17 TYR A 336  TRP A 349  HOH B  25  HOH B  40                    
SITE     4 AC1 17 HOH B  50  HOH B  51  HOH B 140  HIS E  18                    
SITE     5 AC1 17 MLZ E  20                                                     
SITE     1 AC2 15 HOH B  62  HOH B  87  HOH B 153  GLY B 225                    
SITE     2 AC2 15 LYS B 226  GLY B 227  ARG B 228  TYR B 271                    
SITE     3 AC2 15 LEU B 296  ASN B 298  HIS B 299  TYR B 336                    
SITE     4 AC2 15 TRP B 349  HIS F  18  MLZ F  20                               
CRYST1   44.400   45.000   52.400  91.40 115.30  89.80 P 1           2          
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      0.022523 -0.000079  0.010648        0.00000                         
SCALE2      0.000000  0.022222  0.000564        0.00000                         
SCALE3      0.000000  0.000000  0.021115        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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