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Database: PDB
Entry: 1MT6
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HEADER    TRANSFERASE                             20-SEP-02   1MT6              
TITLE     STRUCTURE OF HISTONE H3 K4-SPECIFIC METHYLTRANSFERASE                 
TITLE    2 SET7/9 WITH ADOHCY                                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SET9;                                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: HISTONE H3 LYSINE 4 SPECIFIC METHYLTRANSFERASE,             
COMPND   5 SET7/9;                                                              
COMPND   6 EC: 2.1.1.43;                                                        
COMPND   7 ENGINEERED: YES                                                      
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 BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PGEX                                      
KEYWDS    SET DOMAIN, HISTONE LYSINE METHYLTRANSFERASE, ADOHCY, KNOT            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.A.JACOBS,J.M.HARP,S.DEVARAKONDA,Y.KIM,F.RASTINEJAD,                 
AUTHOR   2 S.KHORASANIZADEH                                                     
REVDAT   2   24-FEB-09 1MT6    1       VERSN                                    
REVDAT   1   06-NOV-02 1MT6    0                                                
JRNL        AUTH   S.A.JACOBS,J.M.HARP,S.DEVARAKONDA,Y.KIM,                     
JRNL        AUTH 2 F.RASTINEJAD,S.KHORASANIZADEH                                
JRNL        TITL   THE ACTIVE SITE OF THE SET DOMAIN IS CONSTRUCTED             
JRNL        TITL 2 ON A KNOT                                                    
JRNL        REF    NAT.STRUCT.BIOL.              V.   9   833 2002              
JRNL        REFN                   ISSN 1072-8368                               
JRNL        PMID   12389038                                                     
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.64                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 132634.400                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 93.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 21464                          
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 SET) : 0.226                           
REMARK   3   FREE R VALUE                     : 0.263                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2132                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.006                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.34                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 78.80                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2655                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3700                       
REMARK   3   BIN FREE R VALUE                    : 0.3560                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.80                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 323                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.020                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2187                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 26                                      
REMARK   3   SOLVENT ATOMS            : 171                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 20.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 52.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -13.83000                                            
REMARK   3    B22 (A**2) : -14.94000                                            
REMARK   3    B33 (A**2) : 28.78000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.30                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.52                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.35                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.42                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.040                           
REMARK   3   BOND ANGLES            (DEGREES) : 3.20                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 28.10                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 2.46                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 2.860 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 3.900 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 4.720 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 5.980 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.33                                                 
REMARK   3   BSOL        : 59.63                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : SAH.PARAM                                      
REMARK   3  PARAMETER FILE  3  : WATER.PARAM                                    
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : SAH.TOP                                        
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1MT6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-OCT-02.                  
REMARK 100 THE RCSB ID CODE IS RCSB017164.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-AUG-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 17-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97780                            
REMARK 200  MONOCHROMATOR                  : SINGLE CRYSTAL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21496                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.0                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.28                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 77.1                               
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: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65.52                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.57                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, SODIUM CITRATE,                
REMARK 280  ISOPROPANOL, DTT, PH 5.6, VAPOR DIFFUSION, HANGING DROP,            
REMARK 280  TEMPERATURE 283K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2                                     
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        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
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        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       35.17350            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       38.01900            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       83.14200            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       35.17350            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       38.01900            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       83.14200            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       35.17350            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       38.01900            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       83.14200            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       35.17350            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       38.01900            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       83.14200            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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 A 450  LIES ON A SPECIAL POSITION.                          
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 A  77   CG    GLU A  77   CD      0.099                       
REMARK 500    TRP A 120   CB    TRP A 120   CG     -0.140                       
REMARK 500    TYR A 123   CZ    TYR A 123   CE2     0.082                       
REMARK 500    ILE A 144   CA    ILE A 144   CB      0.161                       
REMARK 500    TYR A 148   CZ    TYR A 148   CE2    -0.106                       
REMARK 500    TYR A 148   CE2   TYR A 148   CD2     0.101                       
REMARK 500    TYR A 156   CE2   TYR A 156   CD2     0.139                       
REMARK 500    GLU A 163   CD    GLU A 163   OE1     0.074                       
REMARK 500    MET A 164   CG    MET A 164   SD      0.157                       
REMARK 500    PHE A 193   CE1   PHE A 193   CZ      0.188                       
REMARK 500    GLU A 214   CG    GLU A 214   CD      0.103                       
REMARK 500    GLU A 214   CD    GLU A 214   OE2     0.071                       
REMARK 500    ARG A 215   CB    ARG A 215   CG     -0.218                       
REMARK 500    ARG A 215   NE    ARG A 215   CZ      0.079                       
REMARK 500    ARG A 215   CZ    ARG A 215   NH1     0.121                       
REMARK 500    ARG A 215   CZ    ARG A 215   NH2     0.105                       
REMARK 500    VAL A 216   CA    VAL A 216   CB      0.180                       
REMARK 500    GLU A 220   CG    GLU A 220   CD      0.163                       
REMARK 500    GLU A 228   CG    GLU A 228   CD      0.105                       
REMARK 500    LEU A 230   CG    LEU A 230   CD1     0.229                       
REMARK 500    PHE A 244   CD1   PHE A 244   CE1     0.134                       
REMARK 500    GLU A 254   CG    GLU A 254   CD      0.101                       
REMARK 500    VAL A 274   CA    VAL A 274   CB     -0.146                       
REMARK 500    GLU A 279   C     GLU A 279   O       0.252                       
REMARK 500    TYR A 287   CD1   TYR A 287   CE1     0.103                       
REMARK 500    ASN A 296   C     ASN A 296   O       0.146                       
REMARK 500    SER A 298   CB    SER A 298   OG      0.096                       
REMARK 500    TYR A 305   CD1   TYR A 305   CE1     0.123                       
REMARK 500    TYR A 305   CE2   TYR A 305   CD2     0.107                       
REMARK 500    PHE A 308   CE1   PHE A 308   CZ      0.119                       
REMARK 500    ARG A 312   CB    ARG A 312   CG      0.170                       
REMARK 500    GLU A 326   CD    GLU A 326   OE1     0.074                       
REMARK 500    THR A 332   C     THR A 332   O       0.144                       
REMARK 500    VAL A 333   CB    VAL A 333   CG1     0.140                       
REMARK 500    VAL A 333   C     VAL A 333   O       0.124                       
REMARK 500    TYR A 337   CE2   TYR A 337   CD2     0.140                       
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    LEU A  59   CA  -  CB  -  CG  ANGL. DEV. =  19.1 DEGREES          
REMARK 500    MET A 164   CG  -  SD  -  CE  ANGL. DEV. = -10.4 DEGREES          
REMARK 500    MET A 185   CG  -  SD  -  CE  ANGL. DEV. = -12.3 DEGREES          
REMARK 500    ASP A 194   CB  -  CG  -  OD1 ANGL. DEV. =   7.9 DEGREES          
REMARK 500    SER A 224   CA  -  C   -  N   ANGL. DEV. =  13.6 DEGREES          
REMARK 500    SER A 225   C   -  N   -  CA  ANGL. DEV. = -16.7 DEGREES          
REMARK 500    MET A 242   CG  -  SD  -  CE  ANGL. DEV. = -11.9 DEGREES          
REMARK 500    GLU A 279   CA  -  C   -  O   ANGL. DEV. = -18.5 DEGREES          
REMARK 500    CYS A 303   CA  -  CB  -  SG  ANGL. DEV. =   6.7 DEGREES          
REMARK 500    ASP A 306   CB  -  CG  -  OD2 ANGL. DEV. =   7.0 DEGREES          
REMARK 500    ARG A 312   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.6 DEGREES          
REMARK 500    ARG A 312   NE  -  CZ  -  NH2 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG A 323   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.2 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    TYR A  62      -79.35   -120.93                                   
REMARK 500    TYR A  63      134.62    127.39                                   
REMARK 500    ASP A  66      174.71    133.62                                   
REMARK 500    ALA A  67      -97.65    -64.53                                   
REMARK 500    GLN A  69     -145.15   -162.14                                   
REMARK 500    LEU A  82      109.90   -170.76                                   
REMARK 500    ASP A  88       34.84     75.22                                   
REMARK 500    THR A 100      -13.43    -47.50                                   
REMARK 500    ARG A 152      -40.70   -141.40                                   
REMARK 500    GLU A 166      113.21   -161.27                                   
REMARK 500    SER A 174      139.18   -179.43                                   
REMARK 500    GLU A 176       98.95     -9.35                                   
REMARK 500    GLU A 177     -117.91     86.66                                   
REMARK 500    SER A 189      109.70    -53.46                                   
REMARK 500    ASP A 194       46.60   -149.66                                   
REMARK 500    THR A 197     -164.06   -120.07                                   
REMARK 500    ASN A 204       75.80   -153.55                                   
REMARK 500    SER A 224      -89.19    -32.77                                   
REMARK 500    ASN A 239       39.18     70.71                                   
REMARK 500    PRO A 278     -134.38    -81.68                                   
REMARK 500    GLU A 279     -123.11     16.59                                   
REMARK 500    CYS A 288       18.44   -147.95                                   
REMARK 500    HIS A 293        3.13    -68.90                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR A 148         0.06    SIDE_CHAIN                              
REMARK 500    TYR A 305         0.09    SIDE_CHAIN                              
REMARK 500    TYR A 337         0.07    SIDE_CHAIN                              
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    ARG A 215        -11.00                                           
REMARK 500    PRO A 278        -10.47                                           
REMARK 500    GLU A 279        -10.12                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 472        DISTANCE =  5.05 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH A 1                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1MUF   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HISTONE H3 K4-SPECIFIC METHYLTRANSFERASE SET7/9         
DBREF  1MT6 A   58   337  UNP    Q8WTS6   SET7_HUMAN      58    337             
SEQRES   1 A  280  THR LEU GLU GLY TYR TYR VAL ASP ASP ALA LEU GLN GLY          
SEQRES   2 A  280  GLN GLY VAL TYR THR TYR GLU ASP GLY GLY VAL LEU GLN          
SEQRES   3 A  280  GLY THR TYR VAL ASP GLY GLU LEU ASN GLY PRO ALA GLN          
SEQRES   4 A  280  GLU TYR ASP THR ASP GLY ARG LEU ILE PHE LYS GLY GLN          
SEQRES   5 A  280  TYR LYS ASP ASN ILE ARG HIS GLY VAL CYS TRP ILE TYR          
SEQRES   6 A  280  TYR PRO ASP GLY GLY SER LEU VAL GLY GLU VAL ASN GLU          
SEQRES   7 A  280  ASP GLY GLU MET THR GLY GLU LYS ILE ALA TYR VAL TYR          
SEQRES   8 A  280  PRO ASP GLU ARG THR ALA LEU TYR GLY LYS PHE ILE ASP          
SEQRES   9 A  280  GLY GLU MET ILE GLU GLY LYS LEU ALA THR LEU MET SER          
SEQRES  10 A  280  THR GLU GLU GLY ARG PRO HIS PHE GLU LEU MET PRO GLY          
SEQRES  11 A  280  ASN SER VAL TYR HIS PHE ASP LYS SER THR SER SER CYS          
SEQRES  12 A  280  ILE SER THR ASN ALA LEU LEU PRO ASP PRO TYR GLU SER          
SEQRES  13 A  280  GLU ARG VAL TYR VAL ALA GLU SER LEU ILE SER SER ALA          
SEQRES  14 A  280  GLY GLU GLY LEU PHE SER LYS VAL ALA VAL GLY PRO ASN          
SEQRES  15 A  280  THR VAL MET SER PHE TYR ASN GLY VAL ARG ILE THR HIS          
SEQRES  16 A  280  GLN GLU VAL ASP SER ARG ASP TRP ALA LEU ASN GLY ASN          
SEQRES  17 A  280  THR LEU SER LEU ASP GLU GLU THR VAL ILE ASP VAL PRO          
SEQRES  18 A  280  GLU PRO TYR ASN HIS VAL SER LYS TYR CYS ALA SER LEU          
SEQRES  19 A  280  GLY HIS LYS ALA ASN HIS SER PHE THR PRO ASN CYS ILE          
SEQRES  20 A  280  TYR ASP MET PHE VAL HIS PRO ARG PHE GLY PRO ILE LYS          
SEQRES  21 A  280  CYS ILE ARG THR LEU ARG ALA VAL GLU ALA ASP GLU GLU          
SEQRES  22 A  280  LEU THR VAL ALA TYR GLY TYR                                  
HET    SAH  A   1      26                                                       
HETNAM     SAH S-ADENOSYL-L-HOMOCYSTEINE                                        
FORMUL   2  SAH    C14 H20 N6 O5 S                                              
FORMUL   3  HOH   *171(H2 O)                                                    
HELIX    1   1 ASP A  209  ARG A  215  1                                   7    
HELIX    2   2 HIS A  252  ARG A  258  1                                   7    
HELIX    3   3 ASP A  259  ASN A  263  5                                   5    
HELIX    4   4 LEU A  291  ALA A  295  5                                   5    
SHEET    1   A10 VAL A  73  THR A  75  0                                        
SHEET    2   A10 VAL A  81  GLN A  83 -1  O  LEU A  82   N  TYR A  74           
SHEET    3   A10 GLY A  93  TYR A  98 -1  O  GLN A  96   N  GLN A  83           
SHEET    4   A10 LEU A 104  LYS A 111 -1  O  TYR A 110   N  GLY A  93           
SHEET    5   A10 VAL A 118  TYR A 122 -1  O  TRP A 120   N  LYS A 107           
SHEET    6   A10 SER A 128  GLU A 132 -1  O  GLY A 131   N  CYS A 119           
SHEET    7   A10 GLY A 141  VAL A 147 -1  O  VAL A 147   N  SER A 128           
SHEET    8   A10 THR A 153  ILE A 160 -1  O  LEU A 155   N  TYR A 146           
SHEET    9   A10 GLU A 163  SER A 174 -1  O  LYS A 168   N  TYR A 156           
SHEET   10   A10 HIS A 181  LEU A 184 -1  O  HIS A 181   N  SER A 174           
SHEET    1   B 8 ILE A 114  ARG A 115  0                                        
SHEET    2   B 8 LEU A 104  LYS A 111 -1  N  LYS A 111   O  ILE A 114           
SHEET    3   B 8 VAL A 118  TYR A 122 -1  O  TRP A 120   N  LYS A 107           
SHEET    4   B 8 SER A 128  GLU A 132 -1  O  GLY A 131   N  CYS A 119           
SHEET    5   B 8 GLY A 141  VAL A 147 -1  O  VAL A 147   N  SER A 128           
SHEET    6   B 8 THR A 153  ILE A 160 -1  O  LEU A 155   N  TYR A 146           
SHEET    7   B 8 GLU A 163  SER A 174 -1  O  LYS A 168   N  TYR A 156           
SHEET    8   B 8 VAL A 190  TYR A 191 -1  O  TYR A 191   N  GLY A 167           
SHEET    1   C 2 TYR A  86  VAL A  87  0                                        
SHEET    2   C 2 GLU A  90  LEU A  91 -1  O  GLU A  90   N  VAL A  87           
SHEET    1   D 4 VAL A 216  GLU A 220  0                                        
SHEET    2   D 4 GLU A 228  SER A 232 -1  O  GLY A 229   N  ALA A 219           
SHEET    3   D 4 GLU A 330  VAL A 333 -1  O  LEU A 331   N  LEU A 230           
SHEET    4   D 4 ASN A 296  HIS A 297  1  N  ASN A 296   O  VAL A 333           
SHEET    1   E 3 VAL A 241  TYR A 245  0                                        
SHEET    2   E 3 GLY A 314  THR A 321 -1  O  LYS A 317   N  TYR A 245           
SHEET    3   E 3 CYS A 303  HIS A 310 -1  N  PHE A 308   O  ILE A 316           
SHEET    1   F 3 VAL A 248  THR A 251  0                                        
SHEET    2   F 3 THR A 273  ASP A 276 -1  O  VAL A 274   N  ILE A 250           
SHEET    3   F 3 LEU A 267  SER A 268 -1  N  LEU A 267   O  ILE A 275           
SITE     1 AC1 13 ALA A 226  GLU A 228  ASN A 265  HIS A 293                    
SITE     2 AC1 13 LYS A 294  ALA A 295  ASN A 296  HIS A 297                    
SITE     3 AC1 13 TYR A 335  HOH A 416  HOH A 447  HOH A 478                    
SITE     4 AC1 13 HOH A 493                                                     
CRYST1   70.347   76.038  166.284  90.00  90.00  90.00 I 2 2 2       8          
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      0.014215  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013151  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006014        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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