GenomeNet

Database: PDB
Entry: 4MI5
LinkDB: 4MI5
Original site: 4MI5 
HEADER    TRANSFERASE                             30-AUG-13   4MI5              
TITLE     CRYSTAL STRUCTURE OF THE EZH2 SET DOMAIN                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE EZH2;                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: SET DOMAIN (UNP RESIDUES 521-746);                         
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_TAXID: 7108                                        
KEYWDS    TRANSFERASE                                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.ANTONYSAMY,B.CONDON,Z.DRUZINA,J.BONANNO,T.GHEYI,I.MACEWAN,A.ZHANG,  
AUTHOR   2 S.ASHOK,M.RUSSELL,J.G.LUZ                                            
REVDAT   1   08-JAN-14 4MI5    0                                                
JRNL        AUTH   S.ANTONYSAMY,B.CONDON,Z.DRUZINA,J.B.BONANNO,T.GHEYI,F.ZHANG, 
JRNL        AUTH 2 I.MACEWAN,A.ZHANG,S.ASHOK,L.RODGERS,M.RUSSELL,J.GATELY LUZ   
JRNL        TITL   STRUCTURAL CONTEXT OF DISEASE-ASSOCIATED MUTATIONS AND       
JRNL        TITL 2 PUTATIVE MECHANISM OF AUTOINHIBITION REVEALED BY X-RAY       
JRNL        TITL 3 CRYSTALLOGRAPHIC ANALYSIS OF THE EZH2-SET DOMAIN.            
JRNL        REF    PLOS ONE                      V.   8 84147 2013              
JRNL        REFN                   ESSN 1932-6203                               
JRNL        PMID   24367637                                                     
JRNL        DOI    10.1371/JOURNAL.PONE.0084147                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0029                                      
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) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.02                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 12456                          
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) : 0.199                           
REMARK   3   R VALUE            (WORKING SET) : 0.196                           
REMARK   3   FREE R VALUE                     : 0.257                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 681                             
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) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 848                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 90.64                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2180                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 62                           
REMARK   3   BIN FREE R VALUE                    : 0.2920                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1600                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 11                                      
REMARK   3   SOLVENT ATOMS            : 159                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.37                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.30000                                             
REMARK   3    B22 (A**2) : 0.26000                                              
REMARK   3    B33 (A**2) : 0.05000                                              
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 OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.234         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.201         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.124         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.363         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.945                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.905                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1643 ; 0.005 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2218 ; 0.978 ; 1.944       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   208 ; 5.538 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    81 ;34.207 ;24.074       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   268 ;12.784 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    12 ; 9.087 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   233 ; 0.069 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1282 ; 0.003 ; 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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
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: NULL                                      
REMARK   4                                                                      
REMARK   4 4MI5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-SEP-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB081939.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-APR-08                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 31-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.2821                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13157                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.6                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 34.98                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.89                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM MES PH 6.5, 30% PEG MME 5K,        
REMARK 280  200MM AMMONIUM SULFATE, VAPOR DIFFUSION, SITTING DROP,              
REMARK 280  TEMPERATURE 294K                                                    
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       22.56700            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       37.75050            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       28.83700            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       37.75050            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       22.56700            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       28.83700            
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: MONOMERIC                         
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     HIS A   598                                                      
REMARK 465     TRP A   599                                                      
REMARK 465     ASP A   600                                                      
REMARK 465     SER A   601                                                      
REMARK 465     LYS A   602                                                      
REMARK 465     ASN A   603                                                      
REMARK 465     ASP A   737                                                      
REMARK 465     ALA A   738                                                      
REMARK 465     LEU A   739                                                      
REMARK 465     LYS A   740                                                      
REMARK 465     TYR A   741                                                      
REMARK 465     VAL A   742                                                      
REMARK 465     GLY A   743                                                      
REMARK 465     ILE A   744                                                      
REMARK 465     GLU A   745                                                      
REMARK 465     ARG A   746                                                      
REMARK 465     GLU A   747                                                      
REMARK 465     MET A   748                                                      
REMARK 465     GLU A   749                                                      
REMARK 465     ILE A   750                                                      
REMARK 465     PRO A   751                                                      
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     GLN A 559    CG   CD   OE1  NE2                                  
REMARK 470     ASP A 597    CG   OD1  OD2                                       
REMARK 470     VAL A 604    CG1  CG2                                            
REMARK 470     LYS A 616    CE   NZ                                             
REMARK 470     ASP A 625    CG   OD1  OD2                                       
REMARK 470     LYS A 661    CG   CD   CE   NZ                                   
REMARK 470     ASP A 664    CG   OD1  OD2                                       
REMARK 470     LYS A 665    CG   CD   CE   NZ                                   
REMARK 470     MET A 667    CG   SD   CE                                        
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    GLN A 570      -64.89     73.56                                   
REMARK 500    ALA A 596       59.74    -97.79                                   
REMARK 500    VAL A 626      -78.31    -73.37                                   
REMARK 500    ALA A 627      143.38   -172.12                                   
REMARK 500    ASN A 675     -158.13   -145.01                                   
REMARK 500    TYR A 733       89.56   -171.13                                   
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 806  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 539   SG                                                     
REMARK 620 2 CYS A 528   SG  115.6                                              
REMARK 620 3 HIS A 530   NE2 110.9 106.7                                        
REMARK 620 4 CYS A 535   SG  115.1 106.8 100.4                                  
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 590   SG                                                     
REMARK 620 2 CYS A 578   SG  101.8                                              
REMARK 620 3 CYS A 585   SG  113.6 115.2                                        
REMARK 620 4 CYS A 565   SG  111.2 112.6 102.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 807  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 554   SG                                                     
REMARK 620 2 CYS A 558   SG  113.2                                              
REMARK 620 3 CYS A 535   SG  107.3 103.6                                        
REMARK 620 4 CYS A 548   SG  111.7 114.2 106.0                                  
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 576   SG                                                     
REMARK 620 2 CYS A 571   SG  114.2                                              
REMARK 620 3 CYS A 565   SG  115.3 108.2                                        
REMARK 620 4 CYS A 567   SG  105.1 110.0 103.4                                  
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 593   SG                                                     
REMARK 620 2 CYS A 606   SG  114.6                                              
REMARK 620 3 CYS A 571   SG  107.1 115.6                                        
REMARK 620 4 CYS A 585   SG  116.2 100.7 102.2                                  
REMARK 620 N                    1     2     3                                   
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 CYS A 541   SG                                                     
REMARK 620 2 CYS A 552   SG  102.1                                              
REMARK 620 3 CYS A 548   SG  110.3 118.9                                        
REMARK 620 4 CYS A 528   SG  109.4 107.1 108.7                                  
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 SO4 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                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 807                  
DBREF  4MI5 A  526   751  UNP    Q15910   EZH2_HUMAN     521    746             
SEQADV 4MI5 GLY A  523  UNP  Q15910              EXPRESSION TAG                 
SEQADV 4MI5 SER A  524  UNP  Q15910              EXPRESSION TAG                 
SEQADV 4MI5 LEU A  525  UNP  Q15910              EXPRESSION TAG                 
SEQRES   1 A  229  GLY SER LEU GLN PRO CYS ASP HIS PRO ARG GLN PRO CYS          
SEQRES   2 A  229  ASP SER SER CYS PRO CYS VAL ILE ALA GLN ASN PHE CYS          
SEQRES   3 A  229  GLU LYS PHE CYS GLN CYS SER SER GLU CYS GLN ASN ARG          
SEQRES   4 A  229  PHE PRO GLY CYS ARG CYS LYS ALA GLN CYS ASN THR LYS          
SEQRES   5 A  229  GLN CYS PRO CYS TYR LEU ALA VAL ARG GLU CYS ASP PRO          
SEQRES   6 A  229  ASP LEU CYS LEU THR CYS GLY ALA ALA ASP HIS TRP ASP          
SEQRES   7 A  229  SER LYS ASN VAL SER CYS LYS ASN CYS SER ILE GLN ARG          
SEQRES   8 A  229  GLY SER LYS LYS HIS LEU LEU LEU ALA PRO SER ASP VAL          
SEQRES   9 A  229  ALA GLY TRP GLY ILE PHE ILE LYS ASP PRO VAL GLN LYS          
SEQRES  10 A  229  ASN GLU PHE ILE SER GLU TYR CYS GLY GLU ILE ILE SER          
SEQRES  11 A  229  GLN ASP GLU ALA ASP ARG ARG GLY LYS VAL TYR ASP LYS          
SEQRES  12 A  229  TYR MET CYS SER PHE LEU PHE ASN LEU ASN ASN ASP PHE          
SEQRES  13 A  229  VAL VAL ASP ALA THR ARG LYS GLY ASN LYS ILE ARG PHE          
SEQRES  14 A  229  ALA ASN HIS SER VAL ASN PRO ASN CYS TYR ALA LYS VAL          
SEQRES  15 A  229  MET MET VAL ASN GLY ASP HIS ARG ILE GLY ILE PHE ALA          
SEQRES  16 A  229  LYS ARG ALA ILE GLN THR GLY GLU GLU LEU PHE PHE ASP          
SEQRES  17 A  229  TYR ARG TYR SER GLN ALA ASP ALA LEU LYS TYR VAL GLY          
SEQRES  18 A  229  ILE GLU ARG GLU MET GLU ILE PRO                              
HET    SO4  A 801       5                                                       
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     ZN  A 807       1                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM      ZN ZINC ION                                                         
FORMUL   2  SO4    O4 S 2-                                                      
FORMUL   3   ZN    6(ZN 2+)                                                     
FORMUL   9  HOH   *159(H2 O)                                                    
HELIX    1   1 CYS A  539  ALA A  544  1                                   6    
HELIX    2   2 CYS A  576  ALA A  581  1                                   6    
HELIX    3   3 CYS A  609  GLY A  614  1                                   6    
HELIX    4   4 GLN A  653  VAL A  662  1                                  10    
HELIX    5   5 ASN A  687  ALA A  692  5                                   6    
SHEET    1   A 2 LEU A 619  PRO A 623  0                                        
SHEET    2   A 2 TRP A 629  ILE A 633 -1  O  PHE A 632   N  LEU A 620           
SHEET    1   B 3 PHE A 642  GLU A 645  0                                        
SHEET    2   B 3 ASP A 710  ALA A 717 -1  O  ILE A 715   N  ILE A 643           
SHEET    3   B 3 CYS A 700  VAL A 707 -1  N  VAL A 707   O  ASP A 710           
SHEET    1   C 3 GLU A 649  SER A 652  0                                        
SHEET    2   C 3 PHE A 678  ASP A 681 -1  O  VAL A 679   N  ILE A 651           
SHEET    3   C 3 LEU A 671  ASN A 673 -1  N  PHE A 672   O  VAL A 680           
SHEET    1   D 2 ASN A 693  HIS A 694  0                                        
SHEET    2   D 2 PHE A 728  PHE A 729  1  O  PHE A 729   N  ASN A 693           
LINK         SG  CYS A 539                ZN    ZN A 806     1555   1555  2.22  
LINK         SG  CYS A 590                ZN    ZN A 802     1555   1555  2.24  
LINK         SG  CYS A 554                ZN    ZN A 807     1555   1555  2.25  
LINK         SG  CYS A 528                ZN    ZN A 806     1555   1555  2.26  
LINK         NE2 HIS A 530                ZN    ZN A 806     1555   1555  2.26  
LINK         SG  CYS A 558                ZN    ZN A 807     1555   1555  2.28  
LINK         SG  CYS A 576                ZN    ZN A 803     1555   1555  2.28  
LINK         SG  CYS A 593                ZN    ZN A 804     1555   1555  2.30  
LINK         SG  CYS A 571                ZN    ZN A 803     1555   1555  2.30  
LINK         SG  CYS A 535                ZN    ZN A 807     1555   1555  2.31  
LINK         SG  CYS A 578                ZN    ZN A 802     1555   1555  2.31  
LINK         SG  CYS A 606                ZN    ZN A 804     1555   1555  2.32  
LINK         SG  CYS A 541                ZN    ZN A 805     1555   1555  2.35  
LINK         SG  CYS A 535                ZN    ZN A 806     1555   1555  2.35  
LINK         SG  CYS A 552                ZN    ZN A 805     1555   1555  2.37  
LINK         SG  CYS A 548                ZN    ZN A 805     1555   1555  2.37  
LINK         SG  CYS A 585                ZN    ZN A 802     1555   1555  2.40  
LINK         SG  CYS A 565                ZN    ZN A 803     1555   1555  2.41  
LINK         SG  CYS A 567                ZN    ZN A 803     1555   1555  2.41  
LINK         SG  CYS A 571                ZN    ZN A 804     1555   1555  2.41  
LINK         SG  CYS A 548                ZN    ZN A 807     1555   1555  2.42  
LINK         SG  CYS A 585                ZN    ZN A 804     1555   1555  2.44  
LINK         SG  CYS A 528                ZN    ZN A 805     1555   1555  2.46  
LINK         SG  CYS A 565                ZN    ZN A 802     1555   1555  2.48  
SITE     1 AC1  5 LYS A 568  ASN A 687  LYS A 688  HOH A 930                    
SITE     2 AC1  5 HOH A1032                                                     
SITE     1 AC2  4 CYS A 565  CYS A 578  CYS A 585  CYS A 590                    
SITE     1 AC3  4 CYS A 565  CYS A 567  CYS A 571  CYS A 576                    
SITE     1 AC4  4 CYS A 571  CYS A 585  CYS A 593  CYS A 606                    
SITE     1 AC5  5 CYS A 528  CYS A 541  CYS A 548  CYS A 552                    
SITE     2 AC5  5  ZN A 806                                                     
SITE     1 AC6  5 CYS A 528  HIS A 530  CYS A 535  CYS A 539                    
SITE     2 AC6  5  ZN A 805                                                     
SITE     1 AC7  4 CYS A 535  CYS A 548  CYS A 554  CYS A 558                    
CRYST1   45.134   57.674   75.501  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      0.022156  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.017339  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013245        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system