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Database: PDB
Entry: 4IJ8
LinkDB: 4IJ8
Original site: 4IJ8 
HEADER    TRANSFERASE                             21-DEC-12   4IJ8              
TITLE     CRYSTAL STRUCTURE OF THE COMPLEX OF SETD8 WITH SAM                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: N-LYSINE METHYLTRANSFERASE SETD8;                          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: H4-K20-HMTASE SETD8, HISTONE-LYSINE N-METHYLTRANSFERASE     
COMPND   5 SETD8, LYSINE N-METHYLTRANSFERASE 5A, PR/SET DOMAIN-CONTAINING       
COMPND   6 PROTEIN 07, PR-SET7, PR/SET07, SET DOMAIN-CONTAINING PROTEIN 8;      
COMPND   7 EC: 2.1.1.-, 2.1.1.43;                                               
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES;                                                       
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: HELICAL PEPTIDE;                                           
COMPND  12 CHAIN: I;                                                            
COMPND  13 FRAGMENT: SEE REMARK 999;                                            
COMPND  14 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: SETD8, KMT5A, PRSET7, SET07, SET8;                             
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21-V2R-PRARE2;                           
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PHIS2;                                    
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: UNIDENTIFIED;                                   
SOURCE  12 ORGANISM_TAXID: 32644;                                               
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    STRUCTURAL GENOMICS CONSORTIUM, SGC, N-LYSINE METHYLTRANSFERASE,      
KEYWDS   2 TRANSFERASE                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.YU,W.TEMPEL,Y.LI,M.EL BAKKOURI,M.SHAPIRA,C.BOUNTRA,C.H.ARROWSMITH,  
AUTHOR   2 A.M.EDWARDS,P.J.BROWN,STRUCTURAL GENOMICS CONSORTIUM (SGC)           
REVDAT   2   02-APR-14 4IJ8    1       SOURCE                                   
REVDAT   1   16-JAN-13 4IJ8    0                                                
JRNL        AUTH   W.YU,W.TEMPEL,Y.LI,M.EL BAKKOURI,M.SHAPIRA,C.BOUNTRA,        
JRNL        AUTH 2 C.H.ARROWSMITH,A.M.EDWARDS,P.J.BROWN,                        
JRNL        AUTH 3 STRUCTURAL GENOMICS CONSORTIUM (SGC)                         
JRNL        TITL   CRYSTAL STRUCTURE OF THE COMPLEX OF SETD8 WITH SAM           
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0032                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.96                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 29561                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : THIN SHELLS (SFTOOLS)           
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.177                           
REMARK   3   R VALUE            (WORKING SET) : 0.176                           
REMARK   3   FREE R VALUE                     : 0.199                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1516                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2116                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.95                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2220                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 2                            
REMARK   3   BIN FREE R VALUE                    : 0.3210                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2440                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 76                                      
REMARK   3   SOLVENT ATOMS            : 130                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 37.76                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.14000                                             
REMARK   3    B22 (A**2) : -0.14000                                             
REMARK   3    B33 (A**2) : 0.44000                                              
REMARK   3    B12 (A**2) : -0.14000                                             
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): 0.140         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.125         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.090         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.332         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.952                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2575 ; 0.015 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  2342 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3497 ; 1.481 ; 1.990       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5383 ; 0.720 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   331 ; 6.144 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   112 ;30.140 ;24.107       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   418 ;11.840 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    15 ;18.086 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   391 ; 0.086 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2945 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   583 ; 0.001 ; 0.020       
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):  1303 ; 1.645 ; 2.224       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1302 ; 1.645 ; 2.223       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1624 ; 2.380 ; 3.323       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
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):  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  : 2                                          
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   233        A   393                          
REMARK   3    ORIGIN FOR THE GROUP (A): -11.2089  34.0938   4.9505              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0592 T22:   0.0553                                     
REMARK   3      T33:   0.1252 T12:  -0.0157                                     
REMARK   3      T13:   0.0447 T23:   0.0108                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3918 L22:   1.4072                                     
REMARK   3      L33:   1.7877 L12:   0.0310                                     
REMARK   3      L13:  -0.1607 L23:   0.4080                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0796 S12:   0.0487 S13:   0.0541                       
REMARK   3      S21:  -0.0558 S22:   0.0252 S23:  -0.3596                       
REMARK   3      S31:   0.0240 S32:   0.2652 S33:   0.0544                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   244        B   393                          
REMARK   3    ORIGIN FOR THE GROUP (A): -37.9893  20.1746   3.5645              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1112 T22:   0.0561                                     
REMARK   3      T33:   0.1106 T12:  -0.0592                                     
REMARK   3      T13:   0.0349 T23:  -0.0603                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8454 L22:   2.2859                                     
REMARK   3      L33:   1.7569 L12:  -0.2796                                     
REMARK   3      L13:  -0.1013 L23:  -0.1508                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0104 S12:   0.1036 S13:  -0.4324                       
REMARK   3      S21:  -0.1415 S22:  -0.1416 S23:   0.2694                       
REMARK   3      S31:   0.3434 S32:  -0.1925 S33:   0.1520                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS:                                           
REMARK   3  HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS                   
REMARK   3  U VALUES      : WITH TLS ADDED                                      
REMARK   3  ARP/WARP, COOT, AND THE MOLPROBITY SERVER WERE ALSO USED DURING     
REMARK   3  REFINEMENT.                                                         
REMARK   4                                                                      
REMARK   4 4IJ8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JAN-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB076820.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-JAN-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CLSI                               
REMARK 200  BEAMLINE                       : 08ID-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97949                            
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI(111)             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX-300                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 29619                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 87.849                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 21.600                             
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.11200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 22.00                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.94200                            
REMARK 200  R SYM FOR SHELL            (I) : 0.94200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.800                              
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   (%): 54.94                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.2 M SODIUM CITRATE, 0.1 M HEPES, 10-   
REMARK 280  FOLD EXCESS SAM, PH 7.5, VAPOR DIFFUSION, TEMPERATURE 291K          
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
REMARK 290       7555   Y,X,-Z+1/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+2/3                                          
REMARK 290      10555   -Y,-X,-Z+5/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/6                                            
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       46.93300            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       93.86600            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       70.39950            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      117.33250            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       23.46650            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       46.93300            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000       93.86600            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      117.33250            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       70.39950            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       23.46650            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1830 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15380 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I                                     
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH B 631  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 658  LIES ON A SPECIAL POSITION.                          
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     ALA A   229                                                      
REMARK 465     MET A   230                                                      
REMARK 465     GLY A   231                                                      
REMARK 465     SER A   232                                                      
REMARK 465     ALA B   229                                                      
REMARK 465     MET B   230                                                      
REMARK 465     GLY B   231                                                      
REMARK 465     SER B   232                                                      
REMARK 465     ARG B   233                                                      
REMARK 465     LYS B   234                                                      
REMARK 465     SER B   235                                                      
REMARK 465     LYS B   236                                                      
REMARK 465     ALA B   237                                                      
REMARK 465     GLU B   238                                                      
REMARK 465     LEU B   239                                                      
REMARK 465     GLN B   240                                                      
REMARK 465     SER B   241                                                      
REMARK 465     GLU B   242                                                      
REMARK 465     GLU B   243                                                      
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     ARG A 233    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 234    CE   NZ                                             
REMARK 470     GLU A 238    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 239    CG   CD1  CD2                                       
REMARK 470     GLN A 240    CG   CD   OE1  NE2                                  
REMARK 470     SER A 241    OG                                                  
REMARK 470     GLU A 242    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 243    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 245    CG   CD   CE   NZ                                   
REMARK 470     ARG A 246    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE A 247    CD1                                                 
REMARK 470     GLU A 249    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 255    CG   CD   CE   NZ                                   
REMARK 470     GLU A 257    CD   OE1  OE2                                       
REMARK 470     ARG A 279    NE   CZ   NH1  NH2                                  
REMARK 470     LYS A 297    CD   CE   NZ                                        
REMARK 470     LYS A 382    CD   CE   NZ                                        
REMARK 470     ARG B 244    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 245    CG   CD   CE   NZ                                   
REMARK 470     ARG B 246    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE B 247    CD1                                                 
REMARK 470     GLU B 249    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 260    NZ                                                  
REMARK 470     ARG B 279    NH1  NH2                                            
REMARK 470     LYS B 297    CG   CD   CE   NZ                                   
REMARK 470     ARG B 329    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS B 349    CD   CE   NZ                                        
REMARK 470     ASP B 354    CG   OD1  OD2                                       
REMARK 470     LYS B 382    NZ                                                  
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    MET A   313    UNK   UNX A   502              2.16            
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 B 299   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 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 283      -61.79   -102.36                                   
REMARK 500    LEU A 319     -125.56     52.28                                   
REMARK 500    LEU B 319     -121.76     55.70                                   
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 SAM A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAM B 501                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE MODEL INCLUDES A DISJOINT APPARENT ALPHA-HELIX THAT COULD NOT    
REMARK 999 BE ASSIGNED TO A SPECIFIC SECTION OF THE AMINO ACID SEQUENCE OF THE  
REMARK 999 TARGET PROTEIN.                                                      
DBREF  4IJ8 A  232   393  UNP    Q9NQR1   SETD8_HUMAN    232    393             
DBREF  4IJ8 B  232   393  UNP    Q9NQR1   SETD8_HUMAN    232    393             
DBREF  4IJ8 I    4    13  PDB    4IJ8     4IJ8             4     13             
SEQADV 4IJ8 ALA A  229  UNP  Q9NQR1              EXPRESSION TAG                 
SEQADV 4IJ8 MET A  230  UNP  Q9NQR1              EXPRESSION TAG                 
SEQADV 4IJ8 GLY A  231  UNP  Q9NQR1              EXPRESSION TAG                 
SEQADV 4IJ8 SER A  343  UNP  Q9NQR1    CYS   343 ENGINEERED MUTATION            
SEQADV 4IJ8 ALA B  229  UNP  Q9NQR1              EXPRESSION TAG                 
SEQADV 4IJ8 MET B  230  UNP  Q9NQR1              EXPRESSION TAG                 
SEQADV 4IJ8 GLY B  231  UNP  Q9NQR1              EXPRESSION TAG                 
SEQADV 4IJ8 SER B  343  UNP  Q9NQR1    CYS   343 ENGINEERED MUTATION            
SEQRES   1 A  165  ALA MET GLY SER ARG LYS SER LYS ALA GLU LEU GLN SER          
SEQRES   2 A  165  GLU GLU ARG LYS ARG ILE ASP GLU LEU ILE GLU SER GLY          
SEQRES   3 A  165  LYS GLU GLU GLY MET LYS ILE ASP LEU ILE ASP GLY LYS          
SEQRES   4 A  165  GLY ARG GLY VAL ILE ALA THR LYS GLN PHE SER ARG GLY          
SEQRES   5 A  165  ASP PHE VAL VAL GLU TYR HIS GLY ASP LEU ILE GLU ILE          
SEQRES   6 A  165  THR ASP ALA LYS LYS ARG GLU ALA LEU TYR ALA GLN ASP          
SEQRES   7 A  165  PRO SER THR GLY CYS TYR MET TYR TYR PHE GLN TYR LEU          
SEQRES   8 A  165  SER LYS THR TYR CYS VAL ASP ALA THR ARG GLU THR ASN          
SEQRES   9 A  165  ARG LEU GLY ARG LEU ILE ASN HIS SER LYS SER GLY ASN          
SEQRES  10 A  165  CYS GLN THR LYS LEU HIS ASP ILE ASP GLY VAL PRO HIS          
SEQRES  11 A  165  LEU ILE LEU ILE ALA SER ARG ASP ILE ALA ALA GLY GLU          
SEQRES  12 A  165  GLU LEU LEU TYR ASP TYR GLY ASP ARG SER LYS ALA SER          
SEQRES  13 A  165  ILE GLU ALA HIS PRO TRP LEU LYS HIS                          
SEQRES   1 B  165  ALA MET GLY SER ARG LYS SER LYS ALA GLU LEU GLN SER          
SEQRES   2 B  165  GLU GLU ARG LYS ARG ILE ASP GLU LEU ILE GLU SER GLY          
SEQRES   3 B  165  LYS GLU GLU GLY MET LYS ILE ASP LEU ILE ASP GLY LYS          
SEQRES   4 B  165  GLY ARG GLY VAL ILE ALA THR LYS GLN PHE SER ARG GLY          
SEQRES   5 B  165  ASP PHE VAL VAL GLU TYR HIS GLY ASP LEU ILE GLU ILE          
SEQRES   6 B  165  THR ASP ALA LYS LYS ARG GLU ALA LEU TYR ALA GLN ASP          
SEQRES   7 B  165  PRO SER THR GLY CYS TYR MET TYR TYR PHE GLN TYR LEU          
SEQRES   8 B  165  SER LYS THR TYR CYS VAL ASP ALA THR ARG GLU THR ASN          
SEQRES   9 B  165  ARG LEU GLY ARG LEU ILE ASN HIS SER LYS SER GLY ASN          
SEQRES  10 B  165  CYS GLN THR LYS LEU HIS ASP ILE ASP GLY VAL PRO HIS          
SEQRES  11 B  165  LEU ILE LEU ILE ALA SER ARG ASP ILE ALA ALA GLY GLU          
SEQRES  12 B  165  GLU LEU LEU TYR ASP TYR GLY ASP ARG SER LYS ALA SER          
SEQRES  13 B  165  ILE GLU ALA HIS PRO TRP LEU LYS HIS                          
SEQRES   1 I   10  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK                      
HET    SAM  A 501      27                                                       
HET    UNX  A 502       1                                                       
HET    UNX  A 503       1                                                       
HET    UNX  A 504       1                                                       
HET    UNX  A 505       1                                                       
HET    UNX  A 506       1                                                       
HET    UNX  A 507       1                                                       
HET    UNX  A 508       1                                                       
HET    UNX  A 509       1                                                       
HET    UNX  A 510       1                                                       
HET    UNX  A 511       1                                                       
HET    UNX  A 512       1                                                       
HET    UNX  A 513       1                                                       
HET    UNX  A 514       1                                                       
HET    SAM  B 501      27                                                       
HET    UNX  B 502       1                                                       
HET    UNX  B 503       1                                                       
HET    UNX  B 504       1                                                       
HET    UNX  B 505       1                                                       
HET    UNX  B 506       1                                                       
HET    UNX  B 507       1                                                       
HET    UNX  B 508       1                                                       
HET    UNX  B 509       1                                                       
HET    UNX  B 510       1                                                       
HETNAM     SAM S-ADENOSYLMETHIONINE                                             
HETNAM     UNX UNKNOWN ATOM OR ION                                              
FORMUL   4  SAM    2(C15 H22 N6 O5 S)                                           
FORMUL   5  UNX    22(X)                                                        
FORMUL  28  HOH   *130(H2 O)                                                    
HELIX    1   1 SER A  235  GLY A  254  1                                  20    
HELIX    2   2 ASP A  295  GLN A  305  1                                  11    
HELIX    3   3 GLN A  305  GLY A  310  1                                   6    
HELIX    4   4 LEU A  334  ILE A  338  5                                   5    
HELIX    5   5 SER A  381  HIS A  388  1                                   8    
HELIX    6   6 PRO A  389  HIS A  393  5                                   5    
HELIX    7   7 LYS B  245  GLY B  254  1                                  10    
HELIX    8   8 ASP B  295  GLN B  305  1                                  11    
HELIX    9   9 GLN B  305  GLY B  310  1                                   6    
HELIX   10  10 LEU B  334  ILE B  338  5                                   5    
HELIX   11  11 SER B  381  HIS B  388  1                                   8    
HELIX   12  12 PRO B  389  HIS B  393  5                                   5    
HELIX   13  13 UNK I    5  UNK I   12  1                                   8    
SHEET    1   A 2 MET A 259  ILE A 264  0                                        
SHEET    2   A 2 GLY A 268  ALA A 273 -1  O  GLY A 268   N  ILE A 264           
SHEET    1   B 3 PHE A 282  GLU A 285  0                                        
SHEET    2   B 3 VAL A 356  ALA A 363 -1  O  LEU A 361   N  VAL A 283           
SHEET    3   B 3 CYS A 346  ILE A 353 -1  N  LYS A 349   O  ILE A 360           
SHEET    1   C 3 ASP A 289  ILE A 293  0                                        
SHEET    2   C 3 LYS A 321  ASP A 326 -1  O  ASP A 326   N  ASP A 289           
SHEET    3   C 3 MET A 313  TYR A 318 -1  N  PHE A 316   O  TYR A 323           
SHEET    1   D 2 ASN A 339  HIS A 340  0                                        
SHEET    2   D 2 LEU A 374  TYR A 375  1  O  TYR A 375   N  ASN A 339           
SHEET    1   E 2 MET B 259  ILE B 264  0                                        
SHEET    2   E 2 GLY B 268  ALA B 273 -1  O  GLY B 268   N  ILE B 264           
SHEET    1   F 3 PHE B 282  GLU B 285  0                                        
SHEET    2   F 3 VAL B 356  ALA B 363 -1  O  LEU B 361   N  VAL B 284           
SHEET    3   F 3 CYS B 346  ILE B 353 -1  N  HIS B 351   O  HIS B 358           
SHEET    1   G 3 ASP B 289  ILE B 293  0                                        
SHEET    2   G 3 LYS B 321  ASP B 326 -1  O  CYS B 324   N  ILE B 291           
SHEET    3   G 3 MET B 313  TYR B 318 -1  N  PHE B 316   O  TYR B 323           
SHEET    1   H 2 ASN B 339  HIS B 340  0                                        
SHEET    2   H 2 LEU B 374  TYR B 375  1  O  TYR B 375   N  ASN B 339           
SITE     1 AC1 17 GLY A 266  LYS A 267  ARG A 269  CYS A 311                    
SITE     2 AC1 17 TYR A 312  ARG A 336  LEU A 337  ILE A 338                    
SITE     3 AC1 17 ASN A 339  HIS A 340  TYR A 377  TRP A 390                    
SITE     4 AC1 17 HOH A 609  HOH A 613  HOH A 615  HOH A 618                    
SITE     5 AC1 17 ALA B 387                                                     
SITE     1 AC2 17 ALA A 387  HOH A 601  HOH A 613  GLY B 266                    
SITE     2 AC2 17 LYS B 267  ARG B 269  CYS B 311  TYR B 312                    
SITE     3 AC2 17 ARG B 336  LEU B 337  ILE B 338  ASN B 339                    
SITE     4 AC2 17 HIS B 340  TYR B 377  TRP B 390  HOH B 611                    
SITE     5 AC2 17 HOH B 621                                                     
CRYST1  101.439  101.439  140.799  90.00  90.00 120.00 P 61 2 2     24          
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      0.009858  0.005692  0.000000        0.00000                         
SCALE2      0.000000  0.011383  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007102        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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