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Database: PDB
Entry: 3OPE
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Original site: 3OPE 
HEADER    TRANSFERASE                             31-AUG-10   3OPE              
TITLE     STRUCTURAL BASIS OF AUTO-INHIBITORY MECHANISM OF HISTONE              
TITLE    2 METHYLTRANSFERASE                                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROBABLE HISTONE-LYSINE N-METHYLTRANSFERASE ASH1L;         
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: SET DOMAIN (UNP RESIDUES 2074-2293);                       
COMPND   5 SYNONYM: ABSENT SMALL AND HOMEOTIC DISKS PROTEIN 1 HOMOLOG, ASH1-LIKE
COMPND   6 PROTEIN, HUASH1, LYSINE N-METHYLTRANSFERASE 2H;                      
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: ASH1L, KIAA1420, KMT2H;                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A(MODIFIED)                          
KEYWDS    SET, METHYLTRANSFERASE, NUCLEUS, TRANSFERASE                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.AN,J.SONG                                                           
REVDAT   2   14-AUG-13 3OPE    1       JRNL   VERSN                             
REVDAT   1   12-JAN-11 3OPE    0                                                
JRNL        AUTH   S.AN,K.J.YEO,Y.H.JEON,J.SONG                                 
JRNL        TITL   CRYSTAL STRUCTURE OF THE HUMAN HISTONE METHYLTRANSFERASE     
JRNL        TITL 2 ASH1L CATALYTIC DOMAIN AND ITS IMPLICATIONS FOR THE          
JRNL        TITL 3 REGULATORY MECHANISM                                         
JRNL        REF    J.BIOL.CHEM.                  V. 286  8369 2011              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   21239497                                                     
JRNL        DOI    10.1074/JBC.M110.203380                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : -3.000                         
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 18803                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.235                           
REMARK   3   FREE R VALUE                     : 0.299                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 963                             
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           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
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            : 3304                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 60                                      
REMARK   3   SOLVENT ATOMS            : 27                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
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  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: THE FILE CONTAINS FRIEDEL PAIRS.          
REMARK   4                                                                      
REMARK   4 3OPE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-SEP-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB061406.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 110                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PAL/PLS                            
REMARK 200  BEAMLINE                       : 4A                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.2827                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19766                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.09700                            
REMARK 200  R SYM                      (I) : 0.09700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 46.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.62000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: THE FILE CONTAINS FRIEDEL PAIRS.                             
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.16                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: BISTRISPROFANE, PEG, PH 7.5, VAPOR       
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 291K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      155.86933            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       77.93467            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       77.93467            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      155.86933            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A  2067                                                      
REMARK 465     GLY A  2281                                                      
REMARK 465     LYS A  2282                                                      
REMARK 465     SER A  2283                                                      
REMARK 465     GLN A  2284                                                      
REMARK 465     ARG A  2285                                                      
REMARK 465     VAL A  2286                                                      
REMARK 465     ASN A  2287                                                      
REMARK 465     GLY A  2288                                                      
REMARK 465     GLY B  2067                                                      
REMARK 465     GLY B  2085                                                      
REMARK 465     TYR B  2086                                                      
REMARK 465     GLU B  2087                                                      
REMARK 465     ALA B  2088                                                      
REMARK 465     THR B  2089                                                      
REMARK 465     THR B  2090                                                      
REMARK 465     CYS B  2091                                                      
REMARK 465     ASN B  2092                                                      
REMARK 465     CYS B  2093                                                      
REMARK 465     LYS B  2094                                                      
REMARK 465     LYS B  2095                                                      
REMARK 465     PRO B  2096                                                      
REMARK 465     ASP B  2097                                                      
REMARK 465     ASP B  2098                                                      
REMARK 465     ASP B  2099                                                      
REMARK 465     THR B  2100                                                      
REMARK 465     ARG B  2101                                                      
REMARK 465     LYS B  2102                                                      
REMARK 465     GLY B  2103                                                      
REMARK 465     GLY B  2280                                                      
REMARK 465     GLY B  2281                                                      
REMARK 465     LYS B  2282                                                      
REMARK 465     SER B  2283                                                      
REMARK 465     GLN B  2284                                                      
REMARK 465     ARG B  2285                                                      
REMARK 465     VAL B  2286                                                      
REMARK 465     ASN B  2287                                                      
REMARK 465     GLY B  2288                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO B2246   C   -  N   -  CA  ANGL. DEV. =  11.9 DEGREES          
REMARK 500    CYS B2275   CA  -  CB  -  SG  ANGL. DEV. =  10.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    VAL A2078      -84.26    -75.82                                   
REMARK 500    PRO A2082       39.59    -82.72                                   
REMARK 500    LEU A2083      109.10    -56.00                                   
REMARK 500    GLU A2087       87.52    -69.34                                   
REMARK 500    CYS A2091       -8.05    -53.01                                   
REMARK 500    ASN A2092      -29.92     52.24                                   
REMARK 500    PRO A2096     -141.66    -54.32                                   
REMARK 500    ASP A2097      -24.18   -159.45                                   
REMARK 500    VAL A2105     -162.21    -51.05                                   
REMARK 500    ASP A2107     -112.69   -120.41                                   
REMARK 500    CYS A2108       96.77     51.68                                   
REMARK 500    LEU A2109      -36.99    -24.66                                   
REMARK 500    ASN A2120       30.02    -71.34                                   
REMARK 500    THR A2121      -22.70   -167.79                                   
REMARK 500    GLU A2126      -25.63    -34.35                                   
REMARK 500    GLN A2127       77.91   -106.74                                   
REMARK 500    CYS A2128     -158.95   -118.46                                   
REMARK 500    CYS A2129        9.59   -163.82                                   
REMARK 500    ARG A2135       12.95    -58.27                                   
REMARK 500    HIS A2136       53.94     39.75                                   
REMARK 500    CYS A2141      -38.08   -142.69                                   
REMARK 500    LEU A2142      139.25    -37.97                                   
REMARK 500    GLU A2148     -100.22      5.20                                   
REMARK 500    PRO A2159      171.68    -58.40                                   
REMARK 500    ILE A2167      151.87    179.49                                   
REMARK 500    GLN A2186      -40.71   -140.61                                   
REMARK 500    TYR A2187       33.56    -85.87                                   
REMARK 500    HIS A2188      -84.02    -48.38                                   
REMARK 500    TYR A2194       79.67   -104.61                                   
REMARK 500    CYS A2195      141.59   -177.30                                   
REMARK 500    LEU A2198      -72.71   -106.17                                   
REMARK 500    ASP A2199      143.27   -173.24                                   
REMARK 500    ASN A2211     -165.79   -115.71                                   
REMARK 500    HIS A2258      -59.05   -121.50                                   
REMARK 500    PHE A2260      174.56    -54.62                                   
REMARK 500    GLU A2263        4.55    -66.48                                   
REMARK 500    GLU A2273      -71.57    -41.92                                   
REMARK 500    VAL B2078      -79.34    -79.09                                   
REMARK 500    ASP B2106      -63.87   -132.55                                   
REMARK 500    CYS B2108      107.29   -167.66                                   
REMARK 500    LEU B2109       -8.54    -47.06                                   
REMARK 500    PHE B2114       55.92     71.39                                   
REMARK 500    THR B2121      -16.07    -43.59                                   
REMARK 500    ASN B2130       68.49   -105.30                                   
REMARK 500    GLN B2131       27.81   -160.53                                   
REMARK 500    ARG B2135       26.94    -76.84                                   
REMARK 500    HIS B2136       35.08     28.58                                   
REMARK 500    GLU B2137       53.82    -69.77                                   
REMARK 500    TRP B2138     -160.13    -71.53                                   
REMARK 500    LYS B2150       44.19   -157.10                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      70 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B  18        DISTANCE =  5.20 ANGSTROMS                       
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 B   5  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B2122   SG                                                     
REMARK 620 2 CYS B2128   SG   52.5                                              
REMARK 620 3 CYS B2117   SG  109.9  84.5                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B   3  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B2220   SG                                                     
REMARK 620 2 CYS B2268   SG   44.8                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A   4  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A2104   SG                                                     
REMARK 620 2 CYS A2093   SG   50.3                                              
REMARK 620 3 CYS A2091   SG  113.3 125.8                                        
REMARK 620 4 CYS A2108   SG   43.9  44.6 157.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A   2  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A2122   SG                                                     
REMARK 620 2 CYS A2117   SG  125.7                                              
REMARK 620 3 CYS A2128   SG   94.2 133.9                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A   1  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A2220   SG                                                     
REMARK 620 2 CYS A2268   SG  115.6                                              
REMARK 620 3 CYS A2275   SG  104.9 111.2                                        
REMARK 620 4 CYS A2270   SG   92.7 105.5 126.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B   6  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B2108   SG                                                     
REMARK 620 2 CYS B2104   SG  126.3                                              
REMARK 620 N                    1                                               
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 1                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 2                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 4                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAM A 7                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 3                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 5                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 6                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAM B 8                   
DBREF  3OPE A 2069  2288  UNP    Q9NR48   ASH1L_HUMAN   2074   2293             
DBREF  3OPE B 2069  2288  UNP    Q9NR48   ASH1L_HUMAN   2074   2293             
SEQADV 3OPE GLY A 2067  UNP  Q9NR48              EXPRESSION TAG                 
SEQADV 3OPE SER A 2068  UNP  Q9NR48              EXPRESSION TAG                 
SEQADV 3OPE GLY B 2067  UNP  Q9NR48              EXPRESSION TAG                 
SEQADV 3OPE SER B 2068  UNP  Q9NR48              EXPRESSION TAG                 
SEQRES   1 A  222  GLY SER TYR LYS LYS ILE ARG SER ASN VAL TYR VAL ASP          
SEQRES   2 A  222  VAL LYS PRO LEU SER GLY TYR GLU ALA THR THR CYS ASN          
SEQRES   3 A  222  CYS LYS LYS PRO ASP ASP ASP THR ARG LYS GLY CYS VAL          
SEQRES   4 A  222  ASP ASP CYS LEU ASN ARG MET ILE PHE ALA GLU CYS SER          
SEQRES   5 A  222  PRO ASN THR CYS PRO CYS GLY GLU GLN CYS CYS ASN GLN          
SEQRES   6 A  222  ARG ILE GLN ARG HIS GLU TRP VAL GLN CYS LEU GLU ARG          
SEQRES   7 A  222  PHE ARG ALA GLU GLU LYS GLY TRP GLY ILE ARG THR LYS          
SEQRES   8 A  222  GLU PRO LEU LYS ALA GLY GLN PHE ILE ILE GLU TYR LEU          
SEQRES   9 A  222  GLY GLU VAL VAL SER GLU GLN GLU PHE ARG ASN ARG MET          
SEQRES  10 A  222  ILE GLU GLN TYR HIS ASN HIS SER ASP HIS TYR CYS LEU          
SEQRES  11 A  222  ASN LEU ASP SER GLY MET VAL ILE ASP SER TYR ARG MET          
SEQRES  12 A  222  GLY ASN GLU ALA ARG PHE ILE ASN HIS SER CYS ASP PRO          
SEQRES  13 A  222  ASN CYS GLU MET GLN LYS TRP SER VAL ASN GLY VAL TYR          
SEQRES  14 A  222  ARG ILE GLY LEU TYR ALA LEU LYS ASP MET PRO ALA GLY          
SEQRES  15 A  222  THR GLU LEU THR TYR ASP TYR ASN PHE HIS SER PHE ASN          
SEQRES  16 A  222  VAL GLU LYS GLN GLN LEU CYS LYS CYS GLY PHE GLU LYS          
SEQRES  17 A  222  CYS ARG GLY ILE ILE GLY GLY LYS SER GLN ARG VAL ASN          
SEQRES  18 A  222  GLY                                                          
SEQRES   1 B  222  GLY SER TYR LYS LYS ILE ARG SER ASN VAL TYR VAL ASP          
SEQRES   2 B  222  VAL LYS PRO LEU SER GLY TYR GLU ALA THR THR CYS ASN          
SEQRES   3 B  222  CYS LYS LYS PRO ASP ASP ASP THR ARG LYS GLY CYS VAL          
SEQRES   4 B  222  ASP ASP CYS LEU ASN ARG MET ILE PHE ALA GLU CYS SER          
SEQRES   5 B  222  PRO ASN THR CYS PRO CYS GLY GLU GLN CYS CYS ASN GLN          
SEQRES   6 B  222  ARG ILE GLN ARG HIS GLU TRP VAL GLN CYS LEU GLU ARG          
SEQRES   7 B  222  PHE ARG ALA GLU GLU LYS GLY TRP GLY ILE ARG THR LYS          
SEQRES   8 B  222  GLU PRO LEU LYS ALA GLY GLN PHE ILE ILE GLU TYR LEU          
SEQRES   9 B  222  GLY GLU VAL VAL SER GLU GLN GLU PHE ARG ASN ARG MET          
SEQRES  10 B  222  ILE GLU GLN TYR HIS ASN HIS SER ASP HIS TYR CYS LEU          
SEQRES  11 B  222  ASN LEU ASP SER GLY MET VAL ILE ASP SER TYR ARG MET          
SEQRES  12 B  222  GLY ASN GLU ALA ARG PHE ILE ASN HIS SER CYS ASP PRO          
SEQRES  13 B  222  ASN CYS GLU MET GLN LYS TRP SER VAL ASN GLY VAL TYR          
SEQRES  14 B  222  ARG ILE GLY LEU TYR ALA LEU LYS ASP MET PRO ALA GLY          
SEQRES  15 B  222  THR GLU LEU THR TYR ASP TYR ASN PHE HIS SER PHE ASN          
SEQRES  16 B  222  VAL GLU LYS GLN GLN LEU CYS LYS CYS GLY PHE GLU LYS          
SEQRES  17 B  222  CYS ARG GLY ILE ILE GLY GLY LYS SER GLN ARG VAL ASN          
SEQRES  18 B  222  GLY                                                          
HET     ZN  A   1       1                                                       
HET     ZN  A   2       1                                                       
HET     ZN  A   4       1                                                       
HET    SAM  A   7      27                                                       
HET     ZN  B   3       1                                                       
HET     ZN  B   5       1                                                       
HET     ZN  B   6       1                                                       
HET    SAM  B   8      27                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     SAM S-ADENOSYLMETHIONINE                                             
FORMUL   3   ZN    6(ZN 2+)                                                     
FORMUL   6  SAM    2(C15 H22 N6 O5 S)                                           
FORMUL  11  HOH   *27(H2 O)                                                     
HELIX    1   1 ASN A 2110  PHE A 2114  5                                   5    
HELIX    2   2 SER A 2175  GLN A 2186  1                                  12    
HELIX    3   3 ASN A 2211  ILE A 2216  5                                   6    
HELIX    4   4 CYS B 2124  CYS B 2128  5                                   5    
HELIX    5   5 SER B 2175  GLN B 2186  1                                  12    
HELIX    6   6 ASN B 2211  ILE B 2216  5                                   6    
HELIX    7   7 ASP B 2254  SER B 2259  1                                   6    
SHEET    1   A 2 LYS A2070  LYS A2071  0                                        
SHEET    2   A 2 MET A2209  GLY A2210  1  O  GLY A2210   N  LYS A2070           
SHEET    1   B 4 VAL A2076  TYR A2077  0                                        
SHEET    2   B 4 GLU A2172  VAL A2174  1  O  VAL A2173   N  VAL A2076           
SHEET    3   B 4 MET A2202  ASP A2205 -1  O  ASP A2205   N  GLU A2172           
SHEET    4   B 4 CYS A2195  ASP A2199 -1  N  LEU A2196   O  ILE A2204           
SHEET    1   C 2 GLU A2143  ARG A2146  0                                        
SHEET    2   C 2 TRP A2152  ARG A2155 -1  O  ARG A2155   N  GLU A2143           
SHEET    1   D 3 PHE A2165  GLU A2168  0                                        
SHEET    2   D 3 VAL A2234  ALA A2241 -1  O  LEU A2239   N  ILE A2166           
SHEET    3   D 3 CYS A2224  VAL A2231 -1  N  GLN A2227   O  GLY A2238           
SHEET    1   E 2 ASN A2217  HIS A2218  0                                        
SHEET    2   E 2 THR A2252  TYR A2253  1  O  TYR A2253   N  ASN A2217           
SHEET    1   F 2 LYS B2070  LYS B2071  0                                        
SHEET    2   F 2 MET B2209  GLY B2210  1  O  GLY B2210   N  LYS B2070           
SHEET    1   G 3 VAL B2076  TYR B2077  0                                        
SHEET    2   G 3 GLU B2172  VAL B2174  1  O  VAL B2173   N  VAL B2076           
SHEET    3   G 3 VAL B2203  ASP B2205 -1  O  ASP B2205   N  GLU B2172           
SHEET    1   H 4 LEU B2142  ARG B2146  0                                        
SHEET    2   H 4 TRP B2152  THR B2156 -1  O  ARG B2155   N  GLU B2143           
SHEET    3   H 4 GLU B2250  TYR B2253 -1  O  LEU B2251   N  ILE B2154           
SHEET    4   H 4 ASN B2217  HIS B2218  1  N  ASN B2217   O  TYR B2253           
SHEET    1   I 3 PHE B2165  GLU B2168  0                                        
SHEET    2   I 3 VAL B2234  ALA B2241 -1  O  LEU B2239   N  ILE B2167           
SHEET    3   I 3 CYS B2224  VAL B2231 -1  N  VAL B2231   O  VAL B2234           
SSBOND   1 CYS A 2093    CYS A 2108                          1555   1555  2.06  
SSBOND   2 CYS A 2093    CYS A 2104                          1555   1555  2.06  
SSBOND   3 CYS A 2104    CYS A 2108                          1555   1555  1.99  
SSBOND   4 CYS B 2122    CYS B 2128                          1555   1555  2.04  
SSBOND   5 CYS B 2220    CYS B 2270                          1555   1555  1.96  
SSBOND   6 CYS B 2220    CYS B 2268                          1555   1555  2.08  
SSBOND   7 CYS B 2268    CYS B 2275                          1555   1555  2.05  
SSBOND   8 CYS B 2268    CYS B 2270                          1555   1555  2.08  
LINK         SG  CYS B2122                ZN    ZN B   5     1555   1555  2.13  
LINK         SG  CYS B2220                ZN    ZN B   3     1555   1555  2.20  
LINK         SG  CYS A2104                ZN    ZN A   4     1555   1555  2.34  
LINK         SG  CYS A2122                ZN    ZN A   2     1555   1555  2.34  
LINK         SG  CYS A2220                ZN    ZN A   1     1555   1555  2.41  
LINK         SG  CYS B2128                ZN    ZN B   5     1555   1555  2.44  
LINK         SG  CYS A2093                ZN    ZN A   4     1555   1555  2.49  
LINK         SG  CYS A2268                ZN    ZN A   1     1555   1555  2.52  
LINK         SG  CYS A2117                ZN    ZN A   2     1555   1555  2.55  
LINK         SG  CYS B2108                ZN    ZN B   6     1555   1555  2.61  
LINK         SG  CYS A2275                ZN    ZN A   1     1555   1555  2.63  
LINK         SG  CYS A2128                ZN    ZN A   2     1555   1555  2.67  
LINK         SG  CYS A2270                ZN    ZN A   1     1555   1555  2.73  
LINK         SG  CYS B2117                ZN    ZN B   5     1555   1555  2.75  
LINK         SG  CYS A2091                ZN    ZN A   4     1555   1555  2.77  
LINK         SG  CYS B2104                ZN    ZN B   6     1555   1555  2.78  
LINK         SG  CYS A2108                ZN    ZN A   4     1555   1555  2.85  
LINK         SG  CYS B2268                ZN    ZN B   3     1555   1555  2.95  
SITE     1 AC1  4 CYS A2220  CYS A2268  CYS A2270  CYS A2275                    
SITE     1 AC2  5 CYS A2091  CYS A2104  CYS A2117  CYS A2122                    
SITE     2 AC2  5 CYS A2128                                                     
SITE     1 AC3  4 CYS A2091  CYS A2093  CYS A2104  CYS A2108                    
SITE     1 AC4 13 LYS A2150  GLY A2151  TRP A2152  ASP A2192                    
SITE     2 AC4 13 HIS A2193  TYR A2194  ARG A2214  ASN A2217                    
SITE     3 AC4 13 HIS A2218  GLN A2266  LEU A2267  CYS A2268                    
SITE     4 AC4 13 LYS A2269                                                     
SITE     1 AC5  4 CYS B2220  CYS B2268  CYS B2275  GLY B2277                    
SITE     1 AC6  4  ZN B   6  CYS B2117  CYS B2122  CYS B2128                    
SITE     1 AC7  3  ZN B   5  CYS B2104  CYS B2108                               
SITE     1 AC8 15 LYS B2150  GLY B2151  TRP B2152  ASP B2192                    
SITE     2 AC8 15 HIS B2193  TYR B2194  ARG B2214  PHE B2215                    
SITE     3 AC8 15 ASN B2217  HIS B2218  TYR B2255  GLN B2266                    
SITE     4 AC8 15 LEU B2267  LYS B2269  ILE B2279                               
CRYST1   59.530   59.530  233.804  90.00  90.00 120.00 P 32 2 1     12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.016798  0.009698  0.000000        0.00000                         
SCALE2      0.000000  0.019397  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004277        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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