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Database: PDB
Entry: 1O9S
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HEADER    TRANSFERASE                             18-DEC-02   1O9S              
TITLE     CRYSTAL STRUCTURE OF A TERNARY COMPLEX OF THE HUMAN HISTONE           
TITLE    2 METHYLTRANSFERASE SET7/9                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE, H3 LYSINE-4            
COMPND   3  SPECIFIC;                                                           
COMPND   4 CHAIN: A, B;                                                         
COMPND   5 FRAGMENT: N-DOMAIN, SET-DOMAIN, RESIDUES 108-366;                    
COMPND   6 SYNONYM: HISTONE H3-K4 METHYLTRANSFERASE, H3-K4-HMTASE;              
COMPND   7 EC: 2.1.1.43;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: GENE FRAGMENT FOR HISTONE H3;                              
COMPND  11 CHAIN: K, L;                                                         
COMPND  12 FRAGMENT: RESIDUES 2-11                                              
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 SYNTHETIC: YES;                                                      
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606                                                 
KEYWDS    METHYLATION, HISTONE H3, METHYLTRANSFERASE, TRANSFERASE               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.XIAO,C.JING,J.R.WILSON,P.A.WALKER,N.VASISHT,G.KELLY,                
AUTHOR   2 S.HOWELL,I.A.TAYLOR,G.M.BLACKBURN,S.J.GAMBLIN                        
REVDAT   3   24-FEB-09 1O9S    1       VERSN                                    
REVDAT   2   11-SEP-03 1O9S    1       JRNL                                     
REVDAT   1   06-FEB-03 1O9S    0                                                
JRNL        AUTH   B.XIAO,C.JING,J.R.WILSON,P.A.WALKER,N.VASISHT,               
JRNL        AUTH 2 G.KELLY,S.HOWELL,I.A.TAYLOR,G.M.BLACKBURN,                   
JRNL        AUTH 3 S.J.GAMBLIN                                                  
JRNL        TITL   STRUCTURE AND CATALYTIC MECHANISM OF THE HUMAN               
JRNL        TITL 2 HISTONE METHYLTRANSFERASE SET7/9                             
JRNL        REF    NATURE                        V. 421   652 2003              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   12540855                                                     
JRNL        DOI    10.1038/NATURE01378                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.75 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20                             
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 89.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 54441                          
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) : 0.206                           
REMARK   3   R VALUE            (WORKING SET) : 0.205                           
REMARK   3   FREE R VALUE                     : 0.222                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 2440                            
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4035                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 70                                      
REMARK   3   SOLVENT ATOMS            : 660                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL          
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : NULL  ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : NULL  ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1O9S COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-DEC-02.                  
REMARK 100 THE PDBE ID CODE IS EBI-11905.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.80                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU                             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 54703                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.750                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 89.9                               
REMARK 200  DATA REDUNDANCY                : 22.000                             
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 47.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1H3I                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): NULL                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       37.71900            
REMARK 290   SMTRY3   2  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 300                                                                      
REMARK 300 DETAILS:THE DIMER IN THIS ENTRY IS FORMED BY THE                     
REMARK 300  COMPLEXOF CHAIN A WITH A PEPTIDE CHAIN K AND                        
REMARK 300 CHAIN B WITHPEPTIDE CHAIN L. CHAINS A AND B                          
REMARK 300 ARE MONOMERIC IN THEPHYSIOLOGICAL STATE.                             
REMARK 350                                                                      
REMARK 350 GENERATING THE BIOMOLECULE                                           
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: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, K                                  
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 BIOMOLECULE:  2                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, L                                  
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   108                                                      
REMARK 465     GLN A   109                                                      
REMARK 465     TYR A   110                                                      
REMARK 465     LYS A   111                                                      
REMARK 465     ASP A   112                                                      
REMARK 465     ASN A   113                                                      
REMARK 465     ILE A   114                                                      
REMARK 465     ARG A   115                                                      
REMARK 465     HIS A   116                                                      
REMARK 465     GLY B   108                                                      
REMARK 465     GLN B   109                                                      
REMARK 465     TYR B   110                                                      
REMARK 465     LYS B   111                                                      
REMARK 465     ASP B   112                                                      
REMARK 465     ASN B   113                                                      
REMARK 465     ILE B   114                                                      
REMARK 465     ARG B   115                                                      
REMARK 465     HIS B   116                                                      
REMARK 465     ALA L     7                                                      
REMARK 465     ARG L     8                                                      
REMARK 465     LYS L     9                                                      
REMARK 465     TYR L    10                                                      
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   OE1  GLU A   183  -  O    HOH A  2067              2.08            
REMARK 500   NZ   LYS B   317  -  OG1  THR L     6              2.13            
REMARK 500   O3'  SAH B  1367  -  O    HOH B  2327              2.17            
REMARK 500   O    HOH A  2069  -  O    HOH A  2073              2.18            
REMARK 500   O    HOH B  2122  -  O    HOH B  2174              2.16            
REMARK 500   O    HOH B  2128  -  O    HOH B  2178              2.05            
REMARK 500   O    HOH B  2138  -  O    HOH B  2194              2.16            
REMARK 500   O    HOH B  2139  -  O    HOH B  2194              2.06            
REMARK 500   O    HOH B  2206  -  O    HOH B  2282              1.99            
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                                                                      
REMARK 500   SD   MET B   185     NE2  GLN B   365     1555      2.18           
REMARK 500   NE2  GLN B   365     SD   MET B   185     1545      2.18           
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    GLU B 356   CD A  GLU B 356   OE1A    0.211                       
REMARK 500    THR K   3   C     MLZ K   4   N       0.150                       
REMARK 500    MLZ K   4   C     GLN K   5   N       0.197                       
REMARK 500    THR L   3   C     MLZ L   4   N       0.264                       
REMARK 500    MLZ L   4   C     GLN L   5   N       0.433                       
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    ASP A 256   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ASP A 306   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    GLY A 343   N   -  CA  -  C   ANGL. DEV. = -16.9 DEGREES          
REMARK 500    SER A 345   CB  -  CA  -  C   ANGL. DEV. = -11.6 DEGREES          
REMARK 500    SER A 345   N   -  CA  -  C   ANGL. DEV. =  26.7 DEGREES          
REMARK 500    SER A 345   N   -  CA  -  CB  ANGL. DEV. = -14.4 DEGREES          
REMARK 500    VAL B 118   N   -  CA  -  CB  ANGL. DEV. = -15.7 DEGREES          
REMARK 500    ASP B 194   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASP B 306   CB  -  CG  -  OD2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    GLU B 356   OE1 -  CD  -  OE2 ANGL. DEV. = -12.8 DEGREES          
REMARK 500    THR K   3   CA  -  C   -  N   ANGL. DEV. = -19.0 DEGREES          
REMARK 500    THR K   3   O   -  C   -  N   ANGL. DEV. =  16.6 DEGREES          
REMARK 500    MLZ K   4   C   -  N   -  CA  ANGL. DEV. = -18.7 DEGREES          
REMARK 500    MLZ L   4   CA  -  C   -  N   ANGL. DEV. = -16.6 DEGREES          
REMARK 500    MLZ L   4   O   -  C   -  N   ANGL. DEV. =  11.4 DEGREES          
REMARK 500    GLN L   5   C   -  N   -  CA  ANGL. DEV. = -20.3 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 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    ARG A 152      -53.35   -144.42                                   
REMARK 500    CYS A 200      108.91   -162.20                                   
REMARK 500    TYR A 245       76.08   -113.71                                   
REMARK 500    CYS A 288       16.79   -141.50                                   
REMARK 500    ILE A 316     -156.74   -139.25                                   
REMARK 500    GLN A 365      116.28     80.80                                   
REMARK 500    VAL B 118      120.95    -37.98                                   
REMARK 500    ARG B 152      -51.30   -133.78                                   
REMARK 500    ASP B 194       60.64   -150.17                                   
REMARK 500    THR B 197     -168.93   -115.23                                   
REMARK 500    CYS B 288       16.99   -144.55                                   
REMARK 500    ILE B 316     -155.92   -131.74                                   
REMARK 500    PRO B 341     -122.56    -62.53                                   
REMARK 500    LYS B 344       18.12    178.93                                   
REMARK 500    ARG K   2       49.48    -68.81                                   
REMARK 500    GLN K   5       29.47     42.59                                   
REMARK 500    ARG L   2       23.50    -43.19                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER                       
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    MLZ K   4        -12.64                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     SAH A 1367                                                       
REMARK 610     SAH B 1367                                                       
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN               
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,          
REMARK 700 TWO SHEETS ARE DEFINED.                                              
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH A1367                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH B1367                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1H3I   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE HISTONE                                    
REMARK 900  METHYLTRANSFERASE SET7/9                                            
DBREF  1O9S A  108   366  UNP    Q8WTS6   SET7_HUMAN     108    366             
DBREF  1O9S B  108   366  UNP    Q8WTS6   SET7_HUMAN     108    366             
DBREF  1O9S K    1    10  UNP    Q16776   Q16776           2     11             
DBREF  1O9S L    1    10  UNP    Q16776   Q16776           2     11             
SEQADV 1O9S TYR K   10  UNP  Q16776    SER    11 CONFLICT                       
SEQADV 1O9S TYR L   10  UNP  Q16776    SER    11 CONFLICT                       
SEQRES   1 A  259  GLY GLN TYR LYS ASP ASN ILE ARG HIS GLY VAL CYS TRP          
SEQRES   2 A  259  ILE TYR TYR PRO ASP GLY GLY SER LEU VAL GLY GLU VAL          
SEQRES   3 A  259  ASN GLU ASP GLY GLU MET THR GLY GLU LYS ILE ALA TYR          
SEQRES   4 A  259  VAL TYR PRO ASP GLU ARG THR ALA LEU TYR GLY LYS PHE          
SEQRES   5 A  259  ILE ASP GLY GLU MET ILE GLU GLY LYS LEU ALA THR LEU          
SEQRES   6 A  259  MET SER THR GLU GLU GLY ARG PRO HIS PHE GLU LEU MET          
SEQRES   7 A  259  PRO GLY ASN SER VAL TYR HIS PHE ASP LYS SER THR SER          
SEQRES   8 A  259  SER CYS ILE SER THR ASN ALA LEU LEU PRO ASP PRO TYR          
SEQRES   9 A  259  GLU SER GLU ARG VAL TYR VAL ALA GLU SER LEU ILE SER          
SEQRES  10 A  259  SER ALA GLY GLU GLY LEU PHE SER LYS VAL ALA VAL GLY          
SEQRES  11 A  259  PRO ASN THR VAL MET SER PHE TYR ASN GLY VAL ARG ILE          
SEQRES  12 A  259  THR HIS GLN GLU VAL ASP SER ARG ASP TRP ALA LEU ASN          
SEQRES  13 A  259  GLY ASN THR LEU SER LEU ASP GLU GLU THR VAL ILE ASP          
SEQRES  14 A  259  VAL PRO GLU PRO TYR ASN HIS VAL SER LYS TYR CYS ALA          
SEQRES  15 A  259  SER LEU GLY HIS LYS ALA ASN HIS SER PHE THR PRO ASN          
SEQRES  16 A  259  CYS ILE TYR ASP MET PHE VAL HIS PRO ARG PHE GLY PRO          
SEQRES  17 A  259  ILE LYS CYS ILE ARG THR LEU ARG ALA VAL GLU ALA ASP          
SEQRES  18 A  259  GLU GLU LEU THR VAL ALA TYR GLY TYR ASP HIS SER PRO          
SEQRES  19 A  259  PRO GLY LYS SER GLY PRO GLU ALA PRO GLU TRP TYR GLN          
SEQRES  20 A  259  VAL GLU LEU LYS ALA PHE GLN ALA THR GLN GLN LYS              
SEQRES   1 B  259  GLY GLN TYR LYS ASP ASN ILE ARG HIS GLY VAL CYS TRP          
SEQRES   2 B  259  ILE TYR TYR PRO ASP GLY GLY SER LEU VAL GLY GLU VAL          
SEQRES   3 B  259  ASN GLU ASP GLY GLU MET THR GLY GLU LYS ILE ALA TYR          
SEQRES   4 B  259  VAL TYR PRO ASP GLU ARG THR ALA LEU TYR GLY LYS PHE          
SEQRES   5 B  259  ILE ASP GLY GLU MET ILE GLU GLY LYS LEU ALA THR LEU          
SEQRES   6 B  259  MET SER THR GLU GLU GLY ARG PRO HIS PHE GLU LEU MET          
SEQRES   7 B  259  PRO GLY ASN SER VAL TYR HIS PHE ASP LYS SER THR SER          
SEQRES   8 B  259  SER CYS ILE SER THR ASN ALA LEU LEU PRO ASP PRO TYR          
SEQRES   9 B  259  GLU SER GLU ARG VAL TYR VAL ALA GLU SER LEU ILE SER          
SEQRES  10 B  259  SER ALA GLY GLU GLY LEU PHE SER LYS VAL ALA VAL GLY          
SEQRES  11 B  259  PRO ASN THR VAL MET SER PHE TYR ASN GLY VAL ARG ILE          
SEQRES  12 B  259  THR HIS GLN GLU VAL ASP SER ARG ASP TRP ALA LEU ASN          
SEQRES  13 B  259  GLY ASN THR LEU SER LEU ASP GLU GLU THR VAL ILE ASP          
SEQRES  14 B  259  VAL PRO GLU PRO TYR ASN HIS VAL SER LYS TYR CYS ALA          
SEQRES  15 B  259  SER LEU GLY HIS LYS ALA ASN HIS SER PHE THR PRO ASN          
SEQRES  16 B  259  CYS ILE TYR ASP MET PHE VAL HIS PRO ARG PHE GLY PRO          
SEQRES  17 B  259  ILE LYS CYS ILE ARG THR LEU ARG ALA VAL GLU ALA ASP          
SEQRES  18 B  259  GLU GLU LEU THR VAL ALA TYR GLY TYR ASP HIS SER PRO          
SEQRES  19 B  259  PRO GLY LYS SER GLY PRO GLU ALA PRO GLU TRP TYR GLN          
SEQRES  20 B  259  VAL GLU LEU LYS ALA PHE GLN ALA THR GLN GLN LYS              
SEQRES   1 K   10  ALA ARG THR MLZ GLN THR ALA ARG LYS TYR                      
SEQRES   1 L   10  ALA ARG THR MLZ GLN THR ALA ARG LYS TYR                      
MODRES 1O9S MLZ K    4  LYS  N-METHYL-LYSINE                                    
MODRES 1O9S MLZ L    4  LYS  N-METHYL-LYSINE                                    
HET    MLZ  K   4      10                                                       
HET    MLZ  L   4      10                                                       
HET    SAH  A1367      25                                                       
HET    SAH  B1367      25                                                       
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   *660(H2 O1)                                                   
HELIX    1   1 ASP A  209  ARG A  215  1                                   7    
HELIX    2   2 THR A  251  SER A  257  1                                   7    
HELIX    3   3 ASP A  259  ASN A  263  5                                   5    
HELIX    4   4 LEU A  291  ALA A  295  5                                   5    
HELIX    5   5 PRO A  350  ALA A  362  1                                  13    
HELIX    6   6 ASP B  209  ARG B  215  1                                   7    
HELIX    7   7 HIS B  252  SER B  257  1                                   6    
HELIX    8   8 LEU B  291  ALA B  295  5                                   5    
HELIX    9   9 PRO B  350  THR B  363  1                                  14    
SHEET    1  AA 6 VAL A 118  TYR A 122  0                                        
SHEET    2  AA 6 SER A 128  GLU A 132 -1  O  LEU A 129   N  ILE A 121           
SHEET    3  AA 6 GLY A 141  VAL A 147 -1  O  ALA A 145   N  VAL A 130           
SHEET    4  AA 6 THR A 153  ILE A 160 -1  O  LEU A 155   N  TYR A 146           
SHEET    5  AA 6 GLU A 163  GLU A 176 -1  O  GLU A 163   N  ILE A 160           
SHEET    6  AA 6 VAL A 190  TYR A 191 -1  O  TYR A 191   N  GLY A 167           
SHEET    1  AB 6 VAL A 118  TYR A 122  0                                        
SHEET    2  AB 6 SER A 128  GLU A 132 -1  O  LEU A 129   N  ILE A 121           
SHEET    3  AB 6 GLY A 141  VAL A 147 -1  O  ALA A 145   N  VAL A 130           
SHEET    4  AB 6 THR A 153  ILE A 160 -1  O  LEU A 155   N  TYR A 146           
SHEET    5  AB 6 GLU A 163  GLU A 176 -1  O  GLU A 163   N  ILE A 160           
SHEET    6  AB 6 ARG A 179  LEU A 184 -1  O  ARG A 179   N  GLU A 176           
SHEET    1  AC 4 VAL A 216  GLU A 220  0                                        
SHEET    2  AC 4 GLU A 228  SER A 232 -1  O  GLY A 229   N  ALA A 219           
SHEET    3  AC 4 GLU A 330  VAL A 333 -1  N  LEU A 331   O  LEU A 230           
SHEET    4  AC 4 ASN A 296  HIS A 297  1  O  ASN A 296   N  VAL A 333           
SHEET    1  AD 3 VAL A 241  TYR A 245  0                                        
SHEET    2  AD 3 GLY A 314  THR A 321 -1  O  LYS A 317   N  TYR A 245           
SHEET    3  AD 3 CYS A 303  HIS A 310 -1  O  ILE A 304   N  ARG A 320           
SHEET    1  AE 3 VAL A 248  ILE A 250  0                                        
SHEET    2  AE 3 VAL A 274  ASP A 276 -1  O  VAL A 274   N  ILE A 250           
SHEET    3  AE 3 LEU A 267  SER A 268 -1  O  LEU A 267   N  ILE A 275           
SHEET    1  BA 6 VAL B 118  TYR B 122  0                                        
SHEET    2  BA 6 SER B 128  GLU B 132 -1  O  LEU B 129   N  ILE B 121           
SHEET    3  BA 6 GLY B 141  VAL B 147 -1  O  ALA B 145   N  VAL B 130           
SHEET    4  BA 6 THR B 153  ILE B 160 -1  O  LEU B 155   N  TYR B 146           
SHEET    5  BA 6 GLU B 163  GLU B 176 -1  O  GLU B 163   N  ILE B 160           
SHEET    6  BA 6 ARG B 179  LEU B 184 -1  O  ARG B 179   N  GLU B 176           
SHEET    1  BB 4 VAL B 216  GLU B 220  0                                        
SHEET    2  BB 4 GLU B 228  SER B 232 -1  O  GLY B 229   N  ALA B 219           
SHEET    3  BB 4 GLU B 330  VAL B 333 -1  N  LEU B 331   O  LEU B 230           
SHEET    4  BB 4 ASN B 296  HIS B 297  1  O  ASN B 296   N  VAL B 333           
SHEET    1  BC 3 VAL B 241  TYR B 245  0                                        
SHEET    2  BC 3 GLY B 314  THR B 321 -1  O  LYS B 317   N  TYR B 245           
SHEET    3  BC 3 CYS B 303  HIS B 310 -1  O  ILE B 304   N  ARG B 320           
SHEET    1  BD 3 VAL B 248  THR B 251  0                                        
SHEET    2  BD 3 THR B 273  ASP B 276 -1  O  VAL B 274   N  ILE B 250           
SHEET    3  BD 3 LEU B 267  SER B 268 -1  O  LEU B 267   N  ILE B 275           
LINK         C   THR K   3                 N   MLZ K   4     1555   1555  1.48  
LINK         C   MLZ K   4                 N   GLN K   5     1555   1555  1.52  
LINK         C   THR L   3                 N   MLZ L   4     1555   1555  1.59  
LINK         C   MLZ L   4                 N   GLN L   5     1555   1555  1.76  
CISPEP   1 GLU A  279    PRO A  280          0        -6.68                     
CISPEP   2 GLU B  279    PRO B  280          0         0.18                     
SITE     1 AC1 17 ALA A 226  GLU A 228  ASN A 265  HIS A 293                    
SITE     2 AC1 17 LYS A 294  ASN A 296  HIS A 297  TYR A 335                    
SITE     3 AC1 17 TRP A 352  GLU A 356  HOH A2302  HOH A2303                    
SITE     4 AC1 17 HOH A2307  HOH A2308  HOH A2309  HOH A2310                    
SITE     5 AC1 17 MLZ K   4                                                     
SITE     1 AC2 17 ALA B 226  GLU B 228  ASN B 265  HIS B 293                    
SITE     2 AC2 17 LYS B 294  ASN B 296  HIS B 297  TYR B 335                    
SITE     3 AC2 17 TRP B 352  GLU B 356  HOH B2322  HOH B2324                    
SITE     4 AC2 17 HOH B2325  HOH B2326  HOH B2327  HOH B2328                    
SITE     5 AC2 17 MLZ L   4                                                     
CRYST1   52.690   75.438   69.099  90.00  94.16  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.018979  0.000000  0.001380        0.00000                         
SCALE2      0.000000  0.013256  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014510        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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