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Database: PDB
Entry: 1MUF
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HEADER    TRANSFERASE                             23-SEP-02   1MUF              
TITLE     STRUCTURE OF HISTONE H3 K4-SPECIFIC METHYLTRANSFERASE SET7/9          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SET9;                                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: HISTONE H3 LYSINE 4 SPECIFIC METHYLTRANSFERASE, SET7/9;     
COMPND   5 EC: 2.1.1.43;                                                        
COMPND   6 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, KNOT, TRANSFERASE       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.A.JACOBS,J.M.HARP,S.DEVARAKONDA,Y.KIM,F.RASTINEJAD,S.KHORASANIZADEH 
REVDAT   3   16-NOV-11 1MUF    1       VERSN  HETATM                            
REVDAT   2   24-FEB-09 1MUF    1       VERSN                                    
REVDAT   1   06-NOV-02 1MUF    0                                                
JRNL        AUTH   S.A.JACOBS,J.M.HARP,S.DEVARAKONDA,Y.KIM,F.RASTINEJAD,        
JRNL        AUTH 2 S.KHORASANIZADEH                                             
JRNL        TITL   THE ACTIVE SITE OF THE SET DOMAIN IS CONSTRUCTED ON A KNOT   
JRNL        REF    NAT.STRUCT.BIOL.              V.   9   833 2002              
JRNL        REFN                   ISSN 1072-8368                               
JRNL        PMID   12389038                                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.26 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) : 2.26                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.22                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1918515.970                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 16789                          
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) : 0.229                           
REMARK   3   FREE R VALUE                     : 0.249                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 848                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.008                           
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) : 2.26                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.34                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 52.00                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1473                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2710                       
REMARK   3   BIN FREE R VALUE                    : 0.3040                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.70                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 73                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.035                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2015                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 141                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 27.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.10000                                              
REMARK   3    B22 (A**2) : 2.10000                                              
REMARK   3    B33 (A**2) : -4.20000                                             
REMARK   3    B12 (A**2) : 2.87000                                              
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) : 0.28                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.21                            
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) : 0.33                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.26                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.011                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.80                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 27.80                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.13                            
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) : 1.580 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.620 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.660 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.930 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.35                                                 
REMARK   3   BSOL        : 49.78                                                
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  : WATER.PARAM                                    
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1MUF COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-OCT-02.                  
REMARK 100 THE RCSB ID CODE IS RCSB017189.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-AUG-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.95372,0.9791,0.97921             
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI 111              
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : SBC-2                              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16789                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.260                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.220                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
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) : 2.26                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.34                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 52.0                               
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: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SOLVE/RESOLVE                                         
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.29                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.95                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3000, CACL2, DTT, PH 7.0, VAPOR      
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 283K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 64 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                                                 
REMARK 290       5555   Y,-X+Y,Z+1/3                                            
REMARK 290       6555   X-Y,X,Z+2/3                                             
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+1/3                                            
REMARK 290      11555   -X+Y,Y,-Z                                               
REMARK 290      12555   X,X-Y,-Z+2/3                                            
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       32.01667            
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       64.03333            
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  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       32.01667            
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       64.03333            
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       32.01667            
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       64.03333            
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       32.01667            
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        0.00000            
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       64.03333            
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 454  LIES ON A SPECIAL POSITION.                          
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 179   N   -  CA  -  C   ANGL. DEV. =  16.9 DEGREES          
REMARK 500    ASP A 259   N   -  CA  -  C   ANGL. DEV. =  20.2 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    ARG A 152      -54.67   -131.07                                   
REMARK 500    GLU A 177     -130.91     63.52                                   
REMARK 500    ASP A 194       58.49   -148.41                                   
REMARK 500    THR A 197     -169.59   -124.29                                   
REMARK 500    SER A 202      147.92   -175.18                                   
REMARK 500    SER A 257     -113.68    -77.78                                   
REMARK 500    ARG A 258      175.54    -48.74                                   
REMARK 500    TRP A 260      -54.54     -5.57                                   
REMARK 500    PRO A 278     -151.49    -96.14                                   
REMARK 500    GLU A 279     -118.28     36.44                                   
REMARK 500    CYS A 288       22.35   -140.14                                   
REMARK 500    ILE A 316     -159.28   -138.99                                   
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 465        DISTANCE =  5.49 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1MT6   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF THE HISTONE H3 K4-SPECIFIC METHYLTRANSFERASE            
REMARK 900 SET7/9 WITH ADOHCY                                                   
DBREF  1MUF A   81   337  UNP    Q8WTS6   SET7_HUMAN      81    337             
SEQADV 1MUF MSE A  139  UNP  Q8WTS6    MET   139 MODIFIED RESIDUE               
SEQADV 1MUF MSE A  164  UNP  Q8WTS6    MET   164 MODIFIED RESIDUE               
SEQADV 1MUF MSE A  173  UNP  Q8WTS6    MET   173 MODIFIED RESIDUE               
SEQADV 1MUF MSE A  185  UNP  Q8WTS6    MET   185 MODIFIED RESIDUE               
SEQADV 1MUF MSE A  242  UNP  Q8WTS6    MET   242 MODIFIED RESIDUE               
SEQADV 1MUF MSE A  307  UNP  Q8WTS6    MET   307 MODIFIED RESIDUE               
SEQRES   1 A  257  VAL LEU GLN GLY THR TYR VAL ASP GLY GLU LEU ASN GLY          
SEQRES   2 A  257  PRO ALA GLN GLU TYR ASP THR ASP GLY ARG LEU ILE PHE          
SEQRES   3 A  257  LYS GLY GLN TYR LYS ASP ASN ILE ARG HIS GLY VAL CYS          
SEQRES   4 A  257  TRP ILE TYR TYR PRO ASP GLY GLY SER LEU VAL GLY GLU          
SEQRES   5 A  257  VAL ASN GLU ASP GLY GLU MSE THR GLY GLU LYS ILE ALA          
SEQRES   6 A  257  TYR VAL TYR PRO ASP GLU ARG THR ALA LEU TYR GLY LYS          
SEQRES   7 A  257  PHE ILE ASP GLY GLU MSE ILE GLU GLY LYS LEU ALA THR          
SEQRES   8 A  257  LEU MSE SER THR GLU GLU GLY ARG PRO HIS PHE GLU LEU          
SEQRES   9 A  257  MSE PRO GLY ASN SER VAL TYR HIS PHE ASP LYS SER THR          
SEQRES  10 A  257  SER SER CYS ILE SER THR ASN ALA LEU LEU PRO ASP PRO          
SEQRES  11 A  257  TYR GLU SER GLU ARG VAL TYR VAL ALA GLU SER LEU ILE          
SEQRES  12 A  257  SER SER ALA GLY GLU GLY LEU PHE SER LYS VAL ALA VAL          
SEQRES  13 A  257  GLY PRO ASN THR VAL MSE SER PHE TYR ASN GLY VAL ARG          
SEQRES  14 A  257  ILE THR HIS GLN GLU VAL ASP SER ARG ASP TRP ALA LEU          
SEQRES  15 A  257  ASN GLY ASN THR LEU SER LEU ASP GLU GLU THR VAL ILE          
SEQRES  16 A  257  ASP VAL PRO GLU PRO TYR ASN HIS VAL SER LYS TYR CYS          
SEQRES  17 A  257  ALA SER LEU GLY HIS LYS ALA ASN HIS SER PHE THR PRO          
SEQRES  18 A  257  ASN CYS ILE TYR ASP MSE PHE VAL HIS PRO ARG PHE GLY          
SEQRES  19 A  257  PRO ILE LYS CYS ILE ARG THR LEU ARG ALA VAL GLU ALA          
SEQRES  20 A  257  ASP GLU GLU LEU THR VAL ALA TYR GLY TYR                      
MODRES 1MUF MSE A  139  MET  SELENOMETHIONINE                                   
MODRES 1MUF MSE A  164  MET  SELENOMETHIONINE                                   
MODRES 1MUF MSE A  173  MET  SELENOMETHIONINE                                   
MODRES 1MUF MSE A  185  MET  SELENOMETHIONINE                                   
MODRES 1MUF MSE A  242  MET  SELENOMETHIONINE                                   
MODRES 1MUF MSE A  307  MET  SELENOMETHIONINE                                   
HET    MSE  A 139       8                                                       
HET    MSE  A 164       8                                                       
HET    MSE  A 173       8                                                       
HET    MSE  A 185       8                                                       
HET    MSE  A 242       8                                                       
HET    MSE  A 307       8                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
FORMUL   1  MSE    6(C5 H11 N O2 SE)                                            
FORMUL   2  HOH   *141(H2 O)                                                    
HELIX    1   1 ASP A  209  GLU A  214  1                                   6    
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    
SHEET    1   A 9 LEU A  82  TYR A  86  0                                        
SHEET    2   A 9 LEU A  91  TYR A  98 -1  O  GLN A  96   N  GLN A  83           
SHEET    3   A 9 LEU A 104  LYS A 111 -1  O  ILE A 105   N  GLU A  97           
SHEET    4   A 9 ILE A 114  TYR A 122 -1  O  TRP A 120   N  LYS A 107           
SHEET    5   A 9 SER A 128  GLU A 132 -1  O  LEU A 129   N  ILE A 121           
SHEET    6   A 9 GLY A 141  VAL A 147 -1  O  VAL A 147   N  SER A 128           
SHEET    7   A 9 THR A 153  ILE A 160 -1  O  GLY A 157   N  ILE A 144           
SHEET    8   A 9 GLU A 163  SER A 174 -1  O  LYS A 168   N  TYR A 156           
SHEET    9   A 9 HIS A 181  LEU A 184 -1  O  GLU A 183   N  THR A 171           
SHEET    1   B 9 LEU A  82  TYR A  86  0                                        
SHEET    2   B 9 LEU A  91  TYR A  98 -1  O  GLN A  96   N  GLN A  83           
SHEET    3   B 9 LEU A 104  LYS A 111 -1  O  ILE A 105   N  GLU A  97           
SHEET    4   B 9 ILE A 114  TYR A 122 -1  O  TRP A 120   N  LYS A 107           
SHEET    5   B 9 SER A 128  GLU A 132 -1  O  LEU A 129   N  ILE A 121           
SHEET    6   B 9 GLY A 141  VAL A 147 -1  O  VAL A 147   N  SER A 128           
SHEET    7   B 9 THR A 153  ILE A 160 -1  O  GLY A 157   N  ILE A 144           
SHEET    8   B 9 GLU A 163  SER A 174 -1  O  LYS A 168   N  TYR A 156           
SHEET    9   B 9 VAL A 190  TYR A 191 -1  O  TYR A 191   N  GLY A 167           
SHEET    1   C 4 VAL A 216  GLU A 220  0                                        
SHEET    2   C 4 GLU A 228  SER A 232 -1  O  GLY A 229   N  ALA A 219           
SHEET    3   C 4 GLU A 330  VAL A 333 -1  O  LEU A 331   N  LEU A 230           
SHEET    4   C 4 ASN A 296  HIS A 297  1  N  ASN A 296   O  VAL A 333           
SHEET    1   D 3 VAL A 241  TYR A 245  0                                        
SHEET    2   D 3 GLY A 314  THR A 321 -1  O  LYS A 317   N  TYR A 245           
SHEET    3   D 3 CYS A 303  HIS A 310 -1  N  ASP A 306   O  CYS A 318           
SHEET    1   E 3 VAL A 248  ILE A 250  0                                        
SHEET    2   E 3 THR A 273  ASP A 276 -1  O  VAL A 274   N  ILE A 250           
SHEET    3   E 3 THR A 266  ASP A 270 -1  N  LEU A 267   O  ILE A 275           
LINK         C   GLU A 138                 N   MSE A 139     1555   1555  1.34  
LINK         C   MSE A 139                 N   THR A 140     1555   1555  1.33  
LINK         C   GLU A 163                 N   MSE A 164     1555   1555  1.33  
LINK         C   MSE A 164                 N   ILE A 165     1555   1555  1.34  
LINK         C   LEU A 172                 N   MSE A 173     1555   1555  1.33  
LINK         C   MSE A 173                 N   SER A 174     1555   1555  1.33  
LINK         C   LEU A 184                 N   MSE A 185     1555   1555  1.32  
LINK         C   MSE A 185                 N   PRO A 186     1555   1555  1.33  
LINK         C   VAL A 241                 N   MSE A 242     1555   1555  1.32  
LINK         C   MSE A 242                 N   SER A 243     1555   1555  1.33  
LINK         C   ASP A 306                 N   MSE A 307     1555   1555  1.33  
LINK         C   MSE A 307                 N   PHE A 308     1555   1555  1.33  
CRYST1  110.973  110.973   96.050  90.00  90.00 120.00 P 64 2 2     12          
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      0.009011  0.005203  0.000000        0.00000                         
SCALE2      0.000000  0.010405  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010411        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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