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Database: PDB
Entry: 4MI0
LinkDB: 4MI0
Original site: 4MI0 
HEADER    TRANSFERASE                             30-AUG-13   4MI0              
TITLE     HUMAN ENHANCER OF ZESTE (DROSOPHILA) HOMOLOG 2(EZH2)                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE EZH2;                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 520-746;                                      
COMPND   5 SYNONYM: ENX-1, ENHANCER OF ZESTE HOMOLOG 2, LYSINE N-               
COMPND   6 METHYLTRANSFERASE 6;                                                 
COMPND   7 EC: 2.1.1.43;                                                        
COMPND   8 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: EZH2, KMT6;                                                    
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  11 EXPRESSION_SYSTEM_VECTOR: PFBOH-LIC-C-HIS                            
KEYWDS    EZH2, GENE REGULATION, CHROMATIN MODIFICATION, HISTONE                
KEYWDS   2 METHYLTRANSFERASE, TRANSCRIPTION, GENE SILENCING, POLYCOMB           
KEYWDS   3 REPRESSIVE COMPLEX 2, STRUCTURAL GENOMICS, STRUCTURAL GENOMICS       
KEYWDS   4 CONSORTIUM, SGC, TRANSFERASE                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.DONG,H.ZENG,H.HE,A.WERNIMONT,C.BOUNTRA,C.H.ARROWSMITH,A.M.EDWARDS,  
AUTHOR   2 P.J.BROWN,H.WU,STRUCTURAL GENOMICS CONSORTIUM (SGC)                  
REVDAT   3   15-NOV-17 4MI0    1       REMARK                                   
REVDAT   2   18-MAR-15 4MI0    1       JRNL                                     
REVDAT   1   25-SEP-13 4MI0    0                                                
JRNL        AUTH   H.WU,H.ZENG,A.DONG,F.LI,H.HE,G.SENISTERRA,A.SEITOVA,S.DUAN,  
JRNL        AUTH 2 P.J.BROWN,M.VEDADI,C.H.ARROWSMITH,M.SCHAPIRA                 
JRNL        TITL   STRUCTURE OF THE CATALYTIC DOMAIN OF EZH2 REVEALS            
JRNL        TITL 2 CONFORMATIONAL PLASTICITY IN COFACTOR AND SUBSTRATE BINDING  
JRNL        TITL 3 SITES AND EXPLAINS ONCOGENIC MUTATIONS.                      
JRNL        REF    PLOS ONE                      V.   8 83737 2013              
JRNL        REFN                   ESSN 1932-6203                               
JRNL        PMID   24367611                                                     
JRNL        DOI    10.1371/JOURNAL.PONE.0083737                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 32.06                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 13414                          
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)  : 0.200                          
REMARK   3   R VALUE            (WORKING SET)  : 0.198                          
REMARK   3   FREE R VALUE                      : 0.239                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 4.880                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 654                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 7                        
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.00                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.16                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 98.08                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2674                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2046                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2538                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2023                   
REMARK   3   BIN FREE R VALUE                        : 0.2474                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.09                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 136                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1584                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 10                                      
REMARK   3   SOLVENT ATOMS            : 64                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 25.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 36.18                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -11.48040                                            
REMARK   3    B22 (A**2) : 6.51810                                              
REMARK   3    B33 (A**2) : 4.96230                                              
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) : 0.234               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.195               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.928                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.917                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : NULL   ; NULL   ; NULL                
REMARK   3    BOND ANGLES               : NULL   ; NULL   ; NULL                
REMARK   3    TORSION ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    TRIGONAL CARBON PLANES    : NULL   ; NULL   ; NULL                
REMARK   3    GENERAL PLANES            : NULL   ; NULL   ; NULL                
REMARK   3    ISOTROPIC THERMAL FACTORS : NULL   ; NULL   ; NULL                
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : NULL   ; NULL   ; NULL                
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : NULL   ; NULL   ; NULL                
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : NULL                     
REMARK   3    BOND ANGLES                  (DEGREES) : NULL                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : NULL                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : NULL                     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4MI0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-SEP-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000081934.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-APR-13; 28-MAY-13               
REMARK 200  TEMPERATURE           (KELVIN) : 100; 100                           
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : APS; CLSI                          
REMARK 200  BEAMLINE                       : 19-ID; 08ID-1                      
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97904; 1.28295                   
REMARK 200  MONOCHROMATOR                  : NULL; NULL                         
REMARK 200  OPTICS                         : NULL; NULL                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; CCD                           
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R; RAYONIX         
REMARK 200                                   MX300HE                            
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-3000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13445                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY                : 4.600                              
REMARK 200  R MERGE                    (I) : 0.08400                            
REMARK 200  R SYM                      (I) : 0.08400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.03                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.53900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: ARPWARP 7.3.0                                         
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 32.24                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.82                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 0.2M LITHIUM SULFATE,      
REMARK 280  0.1M HEPES PH7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       22.50500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       37.27100            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       28.89800            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       37.27100            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       22.50500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       28.89800            
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 300 REMARK: THE AUTHOR STATES THAT THE BIOLOGICAL UNIT OF THIS PROTEIN   
REMARK 300 IS UNKNOWN.                                                          
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 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     TYR A   658                                                      
REMARK 465     ASP A   659                                                      
REMARK 465     GLN A   730                                                      
REMARK 465     ALA A   731                                                      
REMARK 465     ASP A   732                                                      
REMARK 465     ALA A   733                                                      
REMARK 465     LEU A   734                                                      
REMARK 465     LYS A   735                                                      
REMARK 465     TYR A   736                                                      
REMARK 465     VAL A   737                                                      
REMARK 465     GLY A   738                                                      
REMARK 465     ILE A   739                                                      
REMARK 465     GLU A   740                                                      
REMARK 465     ARG A   741                                                      
REMARK 465     GLU A   742                                                      
REMARK 465     MET A   743                                                      
REMARK 465     GLU A   744                                                      
REMARK 465     ILE A   745                                                      
REMARK 465     PRO A   746                                                      
REMARK 465     HIS A   747                                                      
REMARK 465     HIS A   748                                                      
REMARK 465     HIS A   749                                                      
REMARK 465     HIS A   750                                                      
REMARK 465     HIS A   751                                                      
REMARK 465     HIS A   752                                                      
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     TYR A 520    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ARG A 527    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 545    CG   CD   CE   NZ                                   
REMARK 470     PHE A 546    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLN A 554    CD   OE1  NE2                                       
REMARK 470     LYS A 563    CD   CE   NZ                                        
REMARK 470     GLN A 565    OE1  NE2                                            
REMARK 470     LYS A 569    CG   CD   CE   NZ                                   
REMARK 470     ASP A 583    CG   OD1  OD2                                       
REMARK 470     LYS A 597    CG   CD   CE   NZ                                   
REMARK 470     VAL A 621    CG1  CG2                                            
REMARK 470     LYS A 629    CD   CE   NZ                                        
REMARK 470     LYS A 634    NZ                                                  
REMARK 470     ARG A 653    CD   NE   CZ   NH1  NH2                             
REMARK 470     VAL A 657    CG1  CG2                                            
REMARK 470     LYS A 660    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    ASP A 531     -153.47   -105.04                                   
REMARK 500    ALA A 564     -174.12   -179.05                                   
REMARK 500    GLN A 565      -68.65     70.89                                   
REMARK 500    VAL A 621      -78.80    -93.90                                   
REMARK 500    TYR A 728      139.40   -176.72                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 805  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 525   NE2                                                    
REMARK 620 2 CYS A 523   SG  102.2                                              
REMARK 620 3 CYS A 534   SG  112.7 115.1                                        
REMARK 620 4 CYS A 530   SG  108.8 107.2 110.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 801  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 566   SG                                                     
REMARK 620 2 CYS A 601   SG  112.9                                              
REMARK 620 3 CYS A 580   SG  108.1  98.6                                        
REMARK 620 4 CYS A 588   SG  109.6 109.6 117.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 804  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 549   SG                                                     
REMARK 620 2 CYS A 553   SG  115.7                                              
REMARK 620 3 CYS A 530   SG  111.5 101.2                                        
REMARK 620 4 CYS A 543   SG  110.2 114.5 102.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 802  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 585   SG                                                     
REMARK 620 2 CYS A 573   SG  100.3                                              
REMARK 620 3 CYS A 560   SG  113.3 113.1                                        
REMARK 620 4 CYS A 580   SG  110.3 117.2 103.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 803  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 571   SG                                                     
REMARK 620 2 CYS A 562   SG  108.6                                              
REMARK 620 3 CYS A 560   SG  115.6 103.5                                        
REMARK 620 4 CYS A 566   SG  113.3 109.3 106.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 806  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 547   SG                                                     
REMARK 620 2 CYS A 536   SG  102.0                                              
REMARK 620 3 CYS A 543   SG  114.7 112.5                                        
REMARK 620 4 CYS A 523   SG  105.8 113.8 108.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 801                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 802                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 803                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 804                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 805                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 806                  
DBREF  4MI0 A  520   746  UNP    Q15910   EZH2_HUMAN     520    746             
SEQADV 4MI0 HIS A  747  UNP  Q15910              EXPRESSION TAG                 
SEQADV 4MI0 HIS A  748  UNP  Q15910              EXPRESSION TAG                 
SEQADV 4MI0 HIS A  749  UNP  Q15910              EXPRESSION TAG                 
SEQADV 4MI0 HIS A  750  UNP  Q15910              EXPRESSION TAG                 
SEQADV 4MI0 HIS A  751  UNP  Q15910              EXPRESSION TAG                 
SEQADV 4MI0 HIS A  752  UNP  Q15910              EXPRESSION TAG                 
SEQRES   1 A  233  TYR GLN PRO CYS ASP HIS PRO ARG GLN PRO CYS ASP SER          
SEQRES   2 A  233  SER CYS PRO CYS VAL ILE ALA GLN ASN PHE CYS GLU LYS          
SEQRES   3 A  233  PHE CYS GLN CYS SER SER GLU CYS GLN ASN ARG PHE PRO          
SEQRES   4 A  233  GLY CYS ARG CYS LYS ALA GLN CYS ASN THR LYS GLN CYS          
SEQRES   5 A  233  PRO CYS TYR LEU ALA VAL ARG GLU CYS ASP PRO ASP LEU          
SEQRES   6 A  233  CYS LEU THR CYS GLY ALA ALA ASP HIS TRP ASP SER LYS          
SEQRES   7 A  233  ASN VAL SER CYS LYS ASN CYS SER ILE GLN ARG GLY SER          
SEQRES   8 A  233  LYS LYS HIS LEU LEU LEU ALA PRO SER ASP VAL ALA GLY          
SEQRES   9 A  233  TRP GLY ILE PHE ILE LYS ASP PRO VAL GLN LYS ASN GLU          
SEQRES  10 A  233  PHE ILE SER GLU TYR CYS GLY GLU ILE ILE SER GLN ASP          
SEQRES  11 A  233  GLU ALA ASP ARG ARG GLY LYS VAL TYR ASP LYS TYR MET          
SEQRES  12 A  233  CYS SER PHE LEU PHE ASN LEU ASN ASN ASP PHE VAL VAL          
SEQRES  13 A  233  ASP ALA THR ARG LYS GLY ASN LYS ILE ARG PHE ALA ASN          
SEQRES  14 A  233  HIS SER VAL ASN PRO ASN CYS TYR ALA LYS VAL MET MET          
SEQRES  15 A  233  VAL ASN GLY ASP HIS ARG ILE GLY ILE PHE ALA LYS ARG          
SEQRES  16 A  233  ALA ILE GLN THR GLY GLU GLU LEU PHE PHE ASP TYR ARG          
SEQRES  17 A  233  TYR SER GLN ALA ASP ALA LEU LYS TYR VAL GLY ILE GLU          
SEQRES  18 A  233  ARG GLU MET GLU ILE PRO HIS HIS HIS HIS HIS HIS              
HET     ZN  A 801       1                                                       
HET     ZN  A 802       1                                                       
HET     ZN  A 803       1                                                       
HET     ZN  A 804       1                                                       
HET     ZN  A 805       1                                                       
HET     ZN  A 806       1                                                       
HET    UNX  A 807       1                                                       
HET    UNX  A 808       1                                                       
HET    UNX  A 809       1                                                       
HET    UNX  A 810       1                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     UNX UNKNOWN ATOM OR ION                                              
FORMUL   2   ZN    6(ZN 2+)                                                     
FORMUL   8  UNX    4(X)                                                         
FORMUL  12  HOH   *64(H2 O)                                                     
HELIX    1   1 CYS A  534  ALA A  539  1                                   6    
HELIX    2   2 CYS A  571  ALA A  576  1                                   6    
HELIX    3   3 CYS A  604  GLY A  609  1                                   6    
HELIX    4   4 GLN A  648  VAL A  657  1                                  10    
HELIX    5   5 ASN A  682  ALA A  687  5                                   6    
SHEET    1   A 2 LEU A 614  PRO A 618  0                                        
SHEET    2   A 2 TRP A 624  ILE A 628 -1  O  GLY A 625   N  ALA A 617           
SHEET    1   B 3 PHE A 637  GLU A 640  0                                        
SHEET    2   B 3 ASP A 705  ALA A 712 -1  O  ILE A 710   N  ILE A 638           
SHEET    3   B 3 CYS A 695  VAL A 702 -1  N  MET A 700   O  ARG A 707           
SHEET    1   C 3 GLU A 644  SER A 647  0                                        
SHEET    2   C 3 PHE A 673  ASP A 676 -1  O  ASP A 676   N  GLU A 644           
SHEET    3   C 3 LEU A 666  ASN A 668 -1  N  PHE A 667   O  VAL A 675           
SHEET    1   D 2 ASN A 688  HIS A 689  0                                        
SHEET    2   D 2 PHE A 723  PHE A 724  1  O  PHE A 724   N  ASN A 688           
LINK         NE2 HIS A 525                ZN    ZN A 805     1555   1555  1.97  
LINK         SG  CYS A 566                ZN    ZN A 801     1555   1555  2.19  
LINK         SG  CYS A 549                ZN    ZN A 804     1555   1555  2.20  
LINK         SG  CYS A 585                ZN    ZN A 802     1555   1555  2.26  
LINK         SG  CYS A 571                ZN    ZN A 803     1555   1555  2.27  
LINK         SG  CYS A 523                ZN    ZN A 805     1555   1555  2.28  
LINK         SG  CYS A 573                ZN    ZN A 802     1555   1555  2.29  
LINK         SG  CYS A 534                ZN    ZN A 805     1555   1555  2.30  
LINK         SG  CYS A 553                ZN    ZN A 804     1555   1555  2.31  
LINK         SG  CYS A 547                ZN    ZN A 806     1555   1555  2.31  
LINK         SG  CYS A 562                ZN    ZN A 803     1555   1555  2.32  
LINK         SG  CYS A 530                ZN    ZN A 805     1555   1555  2.34  
LINK         SG  CYS A 530                ZN    ZN A 804     1555   1555  2.34  
LINK         SG  CYS A 601                ZN    ZN A 801     1555   1555  2.35  
LINK         SG  CYS A 560                ZN    ZN A 803     1555   1555  2.35  
LINK         SG  CYS A 536                ZN    ZN A 806     1555   1555  2.36  
LINK         SG  CYS A 580                ZN    ZN A 801     1555   1555  2.38  
LINK         SG  CYS A 543                ZN    ZN A 806     1555   1555  2.39  
LINK         SG  CYS A 588                ZN    ZN A 801     1555   1555  2.39  
LINK         SG  CYS A 543                ZN    ZN A 804     1555   1555  2.40  
LINK         SG  CYS A 523                ZN    ZN A 806     1555   1555  2.42  
LINK         SG  CYS A 560                ZN    ZN A 802     1555   1555  2.45  
LINK         SG  CYS A 580                ZN    ZN A 802     1555   1555  2.48  
LINK         SG  CYS A 566                ZN    ZN A 803     1555   1555  2.54  
SITE     1 AC1  4 CYS A 566  CYS A 580  CYS A 588  CYS A 601                    
SITE     1 AC2  4 CYS A 560  CYS A 573  CYS A 580  CYS A 585                    
SITE     1 AC3  4 CYS A 560  CYS A 562  CYS A 566  CYS A 571                    
SITE     1 AC4  4 CYS A 530  CYS A 543  CYS A 549  CYS A 553                    
SITE     1 AC5  4 CYS A 523  HIS A 525  CYS A 530  CYS A 534                    
SITE     1 AC6  4 CYS A 523  CYS A 536  CYS A 543  CYS A 547                    
CRYST1   45.010   57.796   74.542  90.00  90.00  90.00 P 21 21 21    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      0.022217  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.017302  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013415        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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