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Database: PDB
Entry: 3OS5
LinkDB: 3OS5
Original site: 3OS5 
HEADER    TRANSFERASE                             08-SEP-10   3OS5              
TITLE     SET7/9-DNMT1 K142ME1 COMPLEX                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE SETD7;                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: HISTONE H3-K4 METHYLTRANSFERASE SETD7, H3-K4-HMTASE SETD7,  
COMPND   5 SET DOMAIN-CONTAINING PROTEIN 7, SET7/9, LYSINE N-METHYLTRANSFERASE  
COMPND   6 7;                                                                   
COMPND   7 EC: 2.1.1.43;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: DNMT1;                                                     
COMPND  11 CHAIN: B;                                                            
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: SETD7, KIAA1717, KMT7, SET7, SET9;                             
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PXC408;                                   
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 SYNTHETIC: YES                                                       
KEYWDS    EPIGENETIC MODIFICATION, SET DOMAIN, PROTEIN LYSINE                   
KEYWDS   2 METHYLTRANSFERASE, DNMT1, LYSINE MONO-METHYLATION, K142, TRANSFERASE 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.-O.ESTEVE,Y.CHANG,M.SAMARANAYAKE,A.K.UPADHYAY,J.R.HORTON,           
AUTHOR   2 G.R.FEEHERY,X.CHENG,S.PRADHAN                                        
REVDAT   2   19-JAN-11 3OS5    1       JRNL                                     
REVDAT   1   15-DEC-10 3OS5    0                                                
JRNL        AUTH   P.O.ESTEVE,Y.CHANG,M.SAMARANAYAKE,A.K.UPADHYAY,J.R.HORTON,   
JRNL        AUTH 2 G.R.FEEHERY,X.CHENG,S.PRADHAN                                
JRNL        TITL   A METHYLATION AND PHOSPHORYLATION SWITCH BETWEEN AN ADJACENT 
JRNL        TITL 2 LYSINE AND SERINE DETERMINES HUMAN DNMT1 STABILITY.          
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  18    42 2011              
JRNL        REFN                   ISSN 1545-9993                               
JRNL        PMID   21151116                                                     
JRNL        DOI    10.1038/NSMB.1939                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.69 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.2                                              
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) : 1.69                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 31.68                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 801382.480                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 95.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 28645                          
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) : 0.211                           
REMARK   3   FREE R VALUE                     : 0.238                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1421                            
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           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.69                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.75                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 82.10                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2301                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2650                       
REMARK   3   BIN FREE R VALUE                    : 0.3090                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.50                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 135                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.027                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1959                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 58                                      
REMARK   3   SOLVENT ATOMS            : 117                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 19.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 4.13000                                              
REMARK   3    B22 (A**2) : -0.10000                                             
REMARK   3    B33 (A**2) : -4.03000                                             
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) : 0.20                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.13                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 35.00                           
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.23                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.18                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.40                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.00                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.99                            
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) : 1.310 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.160 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 3.220 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 4.170 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.40                                                 
REMARK   3   BSOL        : 53.76                                                
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  : ION.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   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3OS5 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-SEP-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB061504.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-AUG-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-BM                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 30160                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.690                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 31.680                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 6.200                              
REMARK 200  R MERGE                    (I) : 0.06800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 21.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.69                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.75                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.60400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR                          
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 3CBM                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.19                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 40% PEG3350, 100 MM TRIS, PH 7.5,        
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 289K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 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+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       50.67950            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       19.26750            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       50.67950            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       19.26750            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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: 2330 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12560 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 3.0 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 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 378  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     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     GLN A   365                                                      
REMARK 465     LYS A   366                                                      
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 176    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 183    CG   CD   OE1  OE2                                  
REMARK 470     ASN A 188    CG   OD1                                            
REMARK 470     GLU A 271    CG   CD   OE1  OE2                                  
REMARK 470     SER A 340    OG                                                  
REMARK 470     LYS A 344    CG   CD   CE   NZ                                   
REMARK 470     SER A 345    OG                                                  
REMARK 470     GLU A 351    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 358    CG   CD   CE   NZ                                   
REMARK 470     THR A 363    OG1  CG2                                            
REMARK 470     GLN A 364    CG   CD   OE1  NE2                                  
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      -49.48   -138.44                                   
REMARK 500    ASP A 194       51.69   -146.24                                   
REMARK 500    THR A 197     -169.55   -124.70                                   
REMARK 500    ASP A 270     -162.04   -162.30                                   
REMARK 500    CYS A 288       17.49   -142.78                                   
REMARK 500    LYS A 344      118.81   -172.18                                   
REMARK 500    PRO B 138      -57.15   -121.18                                   
REMARK 500    SER B 143      117.32     88.77                                   
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 BME A 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 391                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 392                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 393                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 394                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 395                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH A 1501                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3CBM   RELATED DB: PDB                                   
REMARK 900 SET7/9-ER PEPTIDE COMPLEX STRUCTURE                                  
REMARK 900 RELATED ID: 3CBO   RELATED DB: PDB                                   
REMARK 900 SET7/9-ER PEPTIDE COMPLEX STRUCTURE                                  
REMARK 900 RELATED ID: 3CBP   RELATED DB: PDB                                   
REMARK 900 SET7/9-ER PEPTIDE COMPLEX STRUCTURE                                  
DBREF  3OS5 A  111   366  UNP    Q8WTS6   SETD7_HUMAN    111    366             
DBREF  3OS5 B  137   144  PDB    3OS5     3OS5           137    144             
SEQRES   1 A  256  LYS ASP ASN ILE ARG HIS GLY VAL CYS TRP ILE TYR TYR          
SEQRES   2 A  256  PRO ASP GLY GLY SER LEU VAL GLY GLU VAL ASN GLU ASP          
SEQRES   3 A  256  GLY GLU MET THR GLY GLU LYS ILE ALA TYR VAL TYR PRO          
SEQRES   4 A  256  ASP GLU ARG THR ALA LEU TYR GLY LYS PHE ILE ASP GLY          
SEQRES   5 A  256  GLU MET ILE GLU GLY LYS LEU ALA THR LEU MET SER THR          
SEQRES   6 A  256  GLU GLU GLY ARG PRO HIS PHE GLU LEU MET PRO GLY ASN          
SEQRES   7 A  256  SER VAL TYR HIS PHE ASP LYS SER THR SER SER CYS ILE          
SEQRES   8 A  256  SER THR ASN ALA LEU LEU PRO ASP PRO TYR GLU SER GLU          
SEQRES   9 A  256  ARG VAL TYR VAL ALA GLU SER LEU ILE SER SER ALA GLY          
SEQRES  10 A  256  GLU GLY LEU PHE SER LYS VAL ALA VAL GLY PRO ASN THR          
SEQRES  11 A  256  VAL MET SER PHE TYR ASN GLY VAL ARG ILE THR HIS GLN          
SEQRES  12 A  256  GLU VAL ASP SER ARG ASP TRP ALA LEU ASN GLY ASN THR          
SEQRES  13 A  256  LEU SER LEU ASP GLU GLU THR VAL ILE ASP VAL PRO GLU          
SEQRES  14 A  256  PRO TYR ASN HIS VAL SER LYS TYR CYS ALA SER LEU GLY          
SEQRES  15 A  256  HIS LYS ALA ASN HIS SER PHE THR PRO ASN CYS ILE TYR          
SEQRES  16 A  256  ASP MET PHE VAL HIS PRO ARG PHE GLY PRO ILE LYS CYS          
SEQRES  17 A  256  ILE ARG THR LEU ARG ALA VAL GLU ALA ASP GLU GLU LEU          
SEQRES  18 A  256  THR VAL ALA TYR GLY TYR ASP HIS SER PRO PRO GLY LYS          
SEQRES  19 A  256  SER GLY PRO GLU ALA PRO GLU TRP TYR GLN VAL GLU LEU          
SEQRES  20 A  256  LYS ALA PHE GLN ALA THR GLN GLN LYS                          
SEQRES   1 B    8  THR PRO ARG ARG SER MLZ SER ALA                              
MODRES 3OS5 MLZ B  142  LYS  N-METHYL-LYSINE                                    
HET    MLZ  B 142      10                                                       
HET    BME  A 500       4                                                       
HET    EDO  A 391       4                                                       
HET    EDO  A 392       4                                                       
HET    EDO  A 393       4                                                       
HET    EDO  A 394       4                                                       
HET    EDO  A 395       8                                                       
HET    UNL  A 400       8                                                       
HET    SAH  A1501      26                                                       
HETNAM     MLZ N-METHYL-LYSINE                                                  
HETNAM     BME BETA-MERCAPTOETHANOL                                             
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     UNL UNKNOWN LIGAND                                                   
HETNAM     SAH S-ADENOSYL-L-HOMOCYSTEINE                                        
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   2  MLZ    C7 H16 N2 O2                                                 
FORMUL   3  BME    C2 H6 O S                                                    
FORMUL   4  EDO    5(C2 H6 O2)                                                  
FORMUL  10  SAH    C14 H20 N6 O5 S                                              
FORMUL  11  HOH   *117(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 CYS A 119  TYR A 122  0                                        
SHEET    2   A 6 SER A 128  GLY A 131 -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 CYS A 119  TYR A 122  0                                        
SHEET    2   B 6 SER A 128  GLY A 131 -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  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 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 141                 N   MLZ B 142     1555   1555  1.33  
LINK         C   MLZ B 142                 N   SER B 143     1555   1555  1.34  
CISPEP   1 GLU A  279    PRO A  280          0         0.09                     
SITE     1 AC1  5 ASP A 194  LYS A 195  CYS A 200  SER A 202                    
SITE     2 AC1  5 GLU A 272                                                     
SITE     1 AC2  6 HOH A  15  HOH A  50  THR A 300  PRO A 301                    
SITE     2 AC2  6 ASN A 302  ARG A 323                                          
SITE     1 AC3  4 TYR A 217  GLU A 220  PHE A 231  HOH A 381                    
SITE     1 AC4  6 HOH A  74  GLU A 228  ASN A 282  HIS A 283                    
SITE     2 AC4  6 LYS A 294  SAH A1501                                          
SITE     1 AC5  2 TRP A 120  TYR A 122                                          
SITE     1 AC6  3 GLU A 163  ASP A 256  PRO B 138                               
SITE     1 AC7 16 HOH A  14  HOH A  36  HOH A  52  HOH A  74                    
SITE     2 AC7 16 ALA A 226  GLU A 228  ASN A 265  HIS A 293                    
SITE     3 AC7 16 LYS A 294  ASN A 296  HIS A 297  TYR A 335                    
SITE     4 AC7 16 TRP A 352  GLU A 356  EDO A 393  MLZ B 142                    
CRYST1  101.359   38.535   66.541  90.00  90.00  90.00 P 21 21 2     4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.009866  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.025950  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015028        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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