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Database: PDB
Entry: 3M55
LinkDB: 3M55
Original site: 3M55 
HEADER    TRANSFERASE                             12-MAR-10   3M55              
TITLE     SET7/9 Y305F IN COMPLEX WITH TAF10-K189ME1 PEPTIDE AND ADOHCY         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE SETD7;                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 110-366;                                      
COMPND   5 SYNONYM: HISTONE H3-K4 METHYLTRANSFERASE SETD7, H3-K4-HMTASE SETD7,  
COMPND   6 SET DOMAIN-CONTAINING PROTEIN 7, SET7/9, LYSINE N-METHYLTRANSFERASE  
COMPND   7 7;                                                                   
COMPND   8 EC: 2.1.1.43;                                                        
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MUTATION: YES;                                                       
COMPND  11 MOL_ID: 2;                                                           
COMPND  12 MOLECULE: TAF10 PEPTIDE;                                             
COMPND  13 CHAIN: B;                                                            
COMPND  14 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 STRAIN: 9606;                                                        
SOURCE   6 GENE: KIAA1717, KMT7, SET7, SET9, SETD7;                             
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)ROSETTA2;                         
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PHIS2;                                    
SOURCE  12 MOL_ID: 2;                                                           
SOURCE  13 SYNTHETIC: YES;                                                      
SOURCE  14 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  15 ORGANISM_COMMON: HUMAN;                                              
SOURCE  16 ORGANISM_TAXID: 9606                                                 
KEYWDS    TERNARY COMPLEX, SET DOMAIN, METHYLTRANSFERASE, S-ADENOSYL-L-         
KEYWDS   2 HOMOCYSTEINE, TAF10 PEPTIDE, N-MONOMETHYLLYSINE, CHROMATIN           
KEYWDS   3 REGULATOR, CHROMOSOMAL PROTEIN, NUCLEUS, S-ADENOSYL-L-METHIONINE,    
KEYWDS   4 TRANSCRIPTION, TRANSCRIPTION REGULATION, TRANSFERASE                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.A.DEL RIZZO,J.-F.COUTURE,M.S.ROIKO,B.S.STRUNK,J.S.BRUNZELLE,        
AUTHOR   2 L.M.DIRK,R.L.HOUTZ,R.C.TRIEVEL                                       
REVDAT   3   08-NOV-17 3M55    1       REMARK                                   
REVDAT   2   14-NOV-12 3M55    1       JRNL   VERSN                             
REVDAT   1   28-JUL-10 3M55    0                                                
JRNL        AUTH   P.A.DEL RIZZO,J.F.COUTURE,L.M.DIRK,B.S.STRUNK,M.S.ROIKO,     
JRNL        AUTH 2 J.S.BRUNZELLE,R.L.HOUTZ,R.C.TRIEVEL                          
JRNL        TITL   SET7/9 CATALYTIC MUTANTS REVEAL THE ROLE OF ACTIVE SITE      
JRNL        TITL 2 WATER MOLECULES IN LYSINE MULTIPLE METHYLATION.              
JRNL        REF    J.BIOL.CHEM.                  V. 285 31849 2010              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   20675860                                                     
JRNL        DOI    10.1074/JBC.M110.114587                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.55 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.19                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 56216                          
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) : 0.192                           
REMARK   3   R VALUE            (WORKING SET) : 0.191                           
REMARK   3   FREE R VALUE                     : 0.217                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2853                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.55                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.59                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3403                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 87.09                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3460                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 186                          
REMARK   3   BIN FREE R VALUE                    : 0.3690                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1935                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 26                                      
REMARK   3   SOLVENT ATOMS            : 324                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.63                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.09000                                              
REMARK   3    B22 (A**2) : 0.09000                                              
REMARK   3    B33 (A**2) : -0.13000                                             
REMARK   3    B12 (A**2) : 0.04000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.070         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.072         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.045         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.227         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.965                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.956                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2108 ; 0.012 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2900 ; 1.391 ; 1.972       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   281 ; 5.911 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    94 ;37.282 ;24.787       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   317 ;10.053 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     7 ; 7.783 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   321 ; 0.093 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1642 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1311 ; 0.995 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2131 ; 1.752 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   797 ; 2.247 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   753 ; 3.582 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES: REFINED INDIVIDUALLY                            
REMARK   4                                                                      
REMARK   4 3M55 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-MAR-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000058120.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-APR-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.3                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-G                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9786                             
REMARK 200  MONOCHROMATOR                  : C(111)                             
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-2000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 56257                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.550                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY                : 10.20                              
REMARK 200  R MERGE                    (I) : 0.05300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.61                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.38800                            
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: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2F69                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.32                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.18                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.95 M SODIUM CITRATE, 0.1 M IMIDAZOLE   
REMARK 280  PH 8.3, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -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       63.78200            
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       31.89100            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  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        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       31.89100            
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       63.78200            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1520 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11720 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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   106                                                      
REMARK 465     ALA A   107                                                      
REMARK 465     MET A   108                                                      
REMARK 465     GLY 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     PRO A   342                                                      
REMARK 465     GLY A   343                                                      
REMARK 465     LYS A   344                                                      
REMARK 465     SER A   345                                                      
REMARK 465     GLY A   346                                                      
REMARK 465     GLN A   365                                                      
REMARK 465     LYS A   366                                                      
REMARK 465     TYR B   193                                                      
REMARK 465     THR B   194                                                      
REMARK 465     LEU B   195                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     HIS A 116    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU A 135    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 152    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 220    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 272    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 351    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 358    CG   CD   CE   NZ                                   
REMARK 470     GLN A 364    CG   CD   OE1  NE2                                  
REMARK 470     ARG B 191    CZ   NH1  NH2                                       
REMARK 470     LYS B 192    CG   CD   CE   NZ                                   
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      -44.38   -140.27                                   
REMARK 500    ASN A 188       51.78   -141.64                                   
REMARK 500    ASN A 188       59.17   -145.56                                   
REMARK 500    ASP A 194       58.57   -154.96                                   
REMARK 500    THR A 197     -167.18   -118.20                                   
REMARK 500    SER A 202      148.25   -174.52                                   
REMARK 500    CYS A 288       17.68   -142.23                                   
REMARK 500    LYS B 187       54.56    -94.34                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH A 1                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2F69   RELATED DB: PDB                                   
REMARK 900 TERNARY COMPLEX OF SET7/9 BOUND TO ADOHCY AND A TAF10 PEPTIDE        
REMARK 900 RELATED ID: 3M54   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3M53   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3M56   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3M57   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3M58   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3M59   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3M5A   RELATED DB: PDB                                   
DBREF  3M55 A  110   366  UNP    Q8WTS6   SETD7_HUMAN    110    366             
DBREF  3M55 B  185   195  PDB    3M55     3M55           185    195             
SEQADV 3M55 GLY A  106  UNP  Q8WTS6              EXPRESSION TAG                 
SEQADV 3M55 ALA A  107  UNP  Q8WTS6              EXPRESSION TAG                 
SEQADV 3M55 MET A  108  UNP  Q8WTS6              EXPRESSION TAG                 
SEQADV 3M55 GLY A  109  UNP  Q8WTS6              EXPRESSION TAG                 
SEQADV 3M55 PHE A  305  UNP  Q8WTS6    TYR   305 ENGINEERED                     
SEQRES   1 A  261  GLY ALA MET GLY TYR LYS ASP ASN ILE ARG HIS GLY VAL          
SEQRES   2 A  261  CYS TRP ILE TYR TYR PRO ASP GLY GLY SER LEU VAL GLY          
SEQRES   3 A  261  GLU VAL ASN GLU ASP GLY GLU MET THR GLY GLU LYS ILE          
SEQRES   4 A  261  ALA TYR VAL TYR PRO ASP GLU ARG THR ALA LEU TYR GLY          
SEQRES   5 A  261  LYS PHE ILE ASP GLY GLU MET ILE GLU GLY LYS LEU ALA          
SEQRES   6 A  261  THR LEU MET SER THR GLU GLU GLY ARG PRO HIS PHE GLU          
SEQRES   7 A  261  LEU MET PRO GLY ASN SER VAL TYR HIS PHE ASP LYS SER          
SEQRES   8 A  261  THR SER SER CYS ILE SER THR ASN ALA LEU LEU PRO ASP          
SEQRES   9 A  261  PRO TYR GLU SER GLU ARG VAL TYR VAL ALA GLU SER LEU          
SEQRES  10 A  261  ILE SER SER ALA GLY GLU GLY LEU PHE SER LYS VAL ALA          
SEQRES  11 A  261  VAL GLY PRO ASN THR VAL MET SER PHE TYR ASN GLY VAL          
SEQRES  12 A  261  ARG ILE THR HIS GLN GLU VAL ASP SER ARG ASP TRP ALA          
SEQRES  13 A  261  LEU ASN GLY ASN THR LEU SER LEU ASP GLU GLU THR VAL          
SEQRES  14 A  261  ILE ASP VAL PRO GLU PRO TYR ASN HIS VAL SER LYS TYR          
SEQRES  15 A  261  CYS ALA SER LEU GLY HIS LYS ALA ASN HIS SER PHE THR          
SEQRES  16 A  261  PRO ASN CYS ILE PHE ASP MET PHE VAL HIS PRO ARG PHE          
SEQRES  17 A  261  GLY PRO ILE LYS CYS ILE ARG THR LEU ARG ALA VAL GLU          
SEQRES  18 A  261  ALA ASP GLU GLU LEU THR VAL ALA TYR GLY TYR ASP HIS          
SEQRES  19 A  261  SER PRO PRO GLY LYS SER GLY PRO GLU ALA PRO GLU TRP          
SEQRES  20 A  261  TYR GLN VAL GLU LEU LYS ALA PHE GLN ALA THR GLN GLN          
SEQRES  21 A  261  LYS                                                          
SEQRES   1 B   11  ACE SER LYS SER MLZ ASP ARG LYS TYR THR LEU                  
MODRES 3M55 MLZ B  189  LYS  N-METHYL-LYSINE                                    
HET    ACE  B 185       3                                                       
HET    MLZ  B 189      10                                                       
HET    SAH  A   1      26                                                       
HETNAM     ACE ACETYL GROUP                                                     
HETNAM     MLZ N-METHYL-LYSINE                                                  
HETNAM     SAH S-ADENOSYL-L-HOMOCYSTEINE                                        
FORMUL   2  ACE    C2 H4 O                                                      
FORMUL   2  MLZ    C7 H16 N2 O2                                                 
FORMUL   3  SAH    C14 H20 N6 O5 S                                              
FORMUL   4  HOH   *324(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    
HELIX    5   5 PRO A  350  GLN A  364  1                                  15    
SHEET    1   A 6 VAL A 118  TYR A 122  0                                        
SHEET    2   A 6 SER A 128  GLU A 132 -1  O  LEU A 129   N  ILE A 121           
SHEET    3   A 6 GLY A 141  VAL A 147 -1  O  VAL A 147   N  SER A 128           
SHEET    4   A 6 THR A 153  ILE A 160 -1  O  GLY A 157   N  ILE A 144           
SHEET    5   A 6 GLU A 163  GLU A 176 -1  O  LYS A 168   N  TYR A 156           
SHEET    6   A 6 ARG A 179  LEU A 184 -1  O  HIS A 181   N  SER A 174           
SHEET    1   B 6 VAL A 118  TYR A 122  0                                        
SHEET    2   B 6 SER A 128  GLU A 132 -1  O  LEU A 129   N  ILE A 121           
SHEET    3   B 6 GLY A 141  VAL A 147 -1  O  VAL A 147   N  SER A 128           
SHEET    4   B 6 THR A 153  ILE A 160 -1  O  GLY A 157   N  ILE A 144           
SHEET    5   B 6 GLU A 163  GLU A 176 -1  O  LYS A 168   N  TYR A 156           
SHEET    6   B 6 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  ILE A 319   N  MET A 242           
SHEET    3   D 3 CYS A 303  HIS A 310 -1  N  PHE A 308   O  ILE A 316           
SHEET    1   E 3 VAL A 248  ILE A 250  0                                        
SHEET    2   E 3 VAL A 274  ASP A 276 -1  O  VAL A 274   N  ILE A 250           
SHEET    3   E 3 LEU A 267  SER A 268 -1  N  LEU A 267   O  ILE A 275           
LINK         C   SER B 188                 N   MLZ B 189     1555   1555  1.33  
LINK         C   MLZ B 189                 N   ASP B 190     1555   1555  1.34  
LINK         C   ACE B 185                 N   SER B 186     1555   1555  1.33  
CISPEP   1 GLU A  279    PRO A  280          0         4.61                     
SITE     1 AC1 18 HOH A  25  ALA A 226  GLU A 228  GLY A 264                    
SITE     2 AC1 18 ASN A 265  HIS A 293  LYS A 294  ASN A 296                    
SITE     3 AC1 18 HIS A 297  TYR A 335  TRP A 352  GLU A 356                    
SITE     4 AC1 18 HOH A 476  HOH A 478  HOH A 479  HOH A 484                    
SITE     5 AC1 18 HOH A 515  MLZ B 189                                          
CRYST1   83.524   83.524   95.673  90.00  90.00 120.00 P 32 2 1      6          
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      0.011973  0.006912  0.000000        0.00000                         
SCALE2      0.000000  0.013825  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010452        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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