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Database: PDB
Entry: 3MO0
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Original site: 3MO0 
HEADER    TRANSFERASE                             22-APR-10   3MO0              
TITLE     HUMAN G9A-LIKE (GLP, ALSO KNOWN AS EHMT1) IN COMPLEX WITH INHIBITOR   
TITLE    2 E11                                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE, H3 LYSINE-9 SPECIFIC 5;
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: C-TERMINAL SET DOMAIN;                                     
COMPND   5 SYNONYM: HISTONE H3-K9 METHYLTRANSFERASE 5, H3-K9-HMTASE 5,          
COMPND   6 EUCHROMATIC HISTONE-LYSINE N-METHYLTRANSFERASE 1, EU-HMTASE1, G9A-   
COMPND   7 LIKE PROTEIN 1, GLP1, LYSINE N-METHYLTRANSFERASE 1D;                 
COMPND   8 EC: 2.1.1.43;                                                        
COMPND   9 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: EHMT1, EUHMTASE1, KIAA1876, KMT1D;                             
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    EPIGENETICS, HISTONE LYSINE METHYLATION, ENZYMATIC INHIBITION, LYSINE 
KEYWDS   2 MIMICS, TRANSFERASE                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.CHANG,J.R.HORTON,X.CHENG                                            
REVDAT   1   30-JUN-10 3MO0    0                                                
JRNL        AUTH   Y.CHANG,T.GANESH,J.R.HORTON,A.SPANNHOFF,J.LIU,A.SUN,         
JRNL        AUTH 2 X.ZHANG,M.T.BEDFORD,Y.SHINKAI,J.P.SNYDER,X.CHENG             
JRNL        TITL   ADDING A LYSINE MIMIC IN THE DESIGN OF POTENT INHIBITORS OF  
JRNL        TITL 2 HISTONE LYSINE METHYLTRANSFERASES.                           
JRNL        REF    J.MOL.BIOL.                   V. 400     1 2010              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   20434463                                                     
JRNL        DOI    10.1016/J.JMB.2010.04.048                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.78 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.2                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.78                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.55                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 237296.890                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 85.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 13837                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.225                           
REMARK   3   FREE R VALUE                     : 0.306                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 688                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.012                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.78                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.88                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 72.70                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1084                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3330                       
REMARK   3   BIN FREE R VALUE                    : 0.4990                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 3.90                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 44                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.075                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3833                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 175                                     
REMARK   3   SOLVENT ATOMS            : 44                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 40.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 55.70                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 10.37000                                             
REMARK   3    B22 (A**2) : -1.88000                                             
REMARK   3    B33 (A**2) : -8.49000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.37                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.35                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 34.60                           
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.53                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.45                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.30                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.60                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.91                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.640 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.970 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.860 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.980 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.35                                                 
REMARK   3   BSOL        : 44.88                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NONE                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  3  : WATER.PARAM                                    
REMARK   3  PARAMETER FILE  4  : SAH.PARAM                                      
REMARK   3  PARAMETER FILE  5  : E11.PARAM                                      
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  4   : SAH.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : BIX.TOP                                        
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED                   
REMARK   4                                                                      
REMARK   4 3MO0 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-APR-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB058784.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-DEC-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.99999                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 14906                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.780                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 34.550                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.2                               
REMARK 200  DATA REDUNDANCY                : 3.100                              
REMARK 200  R MERGE                    (I) : 0.09000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.78                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.88                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.56800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 3FPD                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES, 18   20% (V/V)              
REMARK 280  POLYETHYLENE GLYCOL 4000 AND 7 10% (V/V) ISOPROPANOL, PH 7.5,       
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 289K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 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       23.65000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       69.10000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       47.25000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       69.10000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       23.65000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       47.25000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: 2 COMPLEXES PER ASYMMETRIC UNIT                              
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 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 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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2650 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23210 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -87.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ASN A   951                                                      
REMARK 465     SER A   952                                                      
REMARK 465     GLN A   953                                                      
REMARK 465     VAL A   954                                                      
REMARK 465     TRP A   955                                                      
REMARK 465     SER A   956                                                      
REMARK 465     ALA A   957                                                      
REMARK 465     LEU A   958                                                      
REMARK 465     GLN A   959                                                      
REMARK 465     MET A   960                                                      
REMARK 465     SER A   961                                                      
REMARK 465     LYS A   962                                                      
REMARK 465     ALA A   963                                                      
REMARK 465     LEU A   964                                                      
REMARK 465     GLN A   965                                                      
REMARK 465     ASP A   966                                                      
REMARK 465     SER A   967                                                      
REMARK 465     ALA A   968                                                      
REMARK 465     PRO A   969                                                      
REMARK 465     ASP A   970                                                      
REMARK 465     ARG A   971                                                      
REMARK 465     PRO A   972                                                      
REMARK 465     SER A   973                                                      
REMARK 465     PRO A   974                                                      
REMARK 465     VAL A   975                                                      
REMARK 465     GLU A   976                                                      
REMARK 465     PRO A  1018                                                      
REMARK 465     MET A  1019                                                      
REMARK 465     ASN A  1020                                                      
REMARK 465     ILE A  1021                                                      
REMARK 465     ASP A  1022                                                      
REMARK 465     ARG A  1023                                                      
REMARK 465     ASN A  1024                                                      
REMARK 465     SER A  1235                                                      
REMARK 465     ASN B   951                                                      
REMARK 465     SER B   952                                                      
REMARK 465     GLN B   953                                                      
REMARK 465     VAL B   954                                                      
REMARK 465     TRP B   955                                                      
REMARK 465     SER B   956                                                      
REMARK 465     ALA B   957                                                      
REMARK 465     LEU B   958                                                      
REMARK 465     GLN B   959                                                      
REMARK 465     MET B   960                                                      
REMARK 465     SER B   961                                                      
REMARK 465     LYS B   962                                                      
REMARK 465     ALA B   963                                                      
REMARK 465     LEU B   964                                                      
REMARK 465     GLN B   965                                                      
REMARK 465     ASP B   966                                                      
REMARK 465     SER B   967                                                      
REMARK 465     ALA B   968                                                      
REMARK 465     PRO B   969                                                      
REMARK 465     ASP B   970                                                      
REMARK 465     ARG B   971                                                      
REMARK 465     PRO B   972                                                      
REMARK 465     SER B   973                                                      
REMARK 465     PRO B   974                                                      
REMARK 465     VAL B   975                                                      
REMARK 465     GLU B   976                                                      
REMARK 465     ARG B   977                                                      
REMARK 465     TRP B  1052                                                      
REMARK 465     TYR B  1053                                                      
REMARK 465     ASP B  1054                                                      
REMARK 465     LYS B  1055                                                      
REMARK 465     ASP B  1056                                                      
REMARK 465     GLY B  1057                                                      
REMARK 465     ARG B  1058                                                      
REMARK 465     LEU B  1059                                                      
REMARK 465     LEU B  1060                                                      
REMARK 465     PRO B  1061                                                      
REMARK 465     GLU B  1062                                                      
REMARK 465     PHE B  1063                                                      
REMARK 465     ASN B  1064                                                      
REMARK 465     MET B  1065                                                      
REMARK 465     ALA B  1066                                                      
REMARK 465     GLU B  1067                                                      
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     VAL A 979    CG1  CG2                                            
REMARK 470     GLN A1012    CG   CD   OE1  NE2                                  
REMARK 470     THR A1016    OG1  CG2                                            
REMARK 470     SER A1017    OG                                                  
REMARK 470     ILE A1025    CG1  CG2  CD1                                       
REMARK 470     THR A1026    OG1  CG2                                            
REMARK 470     LEU A1028    CG   CD1  CD2                                       
REMARK 470     GLN A1029    CG   CD   OE1  NE2                                  
REMARK 470     LYS A1055    CG   CD   CE   NZ                                   
REMARK 470     ARG A1103    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A1149    CG   CD   CE   NZ                                   
REMARK 470     ASP A1150    CG   OD1  OD2                                       
REMARK 470     GLU A1173    CG   CD   OE1  OE2                                  
REMARK 470     LYS A1231    CG   CD   CE   NZ                                   
REMARK 470     THR B1016    OG1  CG2                                            
REMARK 470     SER B1017    OG                                                  
REMARK 470     MET B1019    CG   SD   CE                                        
REMARK 470     ASN B1020    CG   OD1  ND2                                       
REMARK 470     ASP B1022    CG   OD1  OD2                                       
REMARK 470     ARG B1023    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN B1024    CG   OD1  ND2                                       
REMARK 470     ILE B1025    CG1  CG2  CD1                                       
REMARK 470     LEU B1028    CG   CD1  CD2                                       
REMARK 470     SER B1048    OG                                                  
REMARK 470     MET B1049    CG   SD   CE                                        
REMARK 470     ARG B1050    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     CYS B1051    SG                                                  
REMARK 470     ARG B1103    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B1138    CG   CD   OE1  OE2                                  
REMARK 470     LYS B1149    CG   CD   CE   NZ                                   
REMARK 470     ASP B1150    CG   OD1  OD2                                       
REMARK 470     GLU B1152    CG   CD   OE1  OE2                                  
REMARK 470     TYR B1154    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASP B1187    CG   OD1  OD2                                       
REMARK 470     LEU B1188    CG   CD1  CD2                                       
REMARK 470     ARG B1189    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE B1190    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG B1214    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B1219    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OD2  ASP A  1131     CAU  E11 A  2001              1.96            
REMARK 500   O    ASP A  1131     CAU  E11 A  2001              1.99            
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    ILE A 978      119.64     77.39                                   
REMARK 500    VAL A 979      -63.74    -97.78                                   
REMARK 500    ASP A 999     -161.81   -164.14                                   
REMARK 500    PRO A1004      152.82    -49.19                                   
REMARK 500    SER A1005       13.13   -160.16                                   
REMARK 500    THR A1016      -81.74    -86.35                                   
REMARK 500    GLN A1029       59.46    149.49                                   
REMARK 500    ASP A1035     -157.10    -98.31                                   
REMARK 500    MET A1049      -38.68     87.82                                   
REMARK 500    ARG A1050      149.58    177.92                                   
REMARK 500    ASN A1075     -158.12   -123.13                                   
REMARK 500    ASP A1104      -11.95   -142.98                                   
REMARK 500    VAL A1121      -61.90    -94.54                                   
REMARK 500    ASP A1140       19.27   -143.14                                   
REMARK 500    LYS A1149       33.98    -59.84                                   
REMARK 500    VAL A1164      -35.07    -34.52                                   
REMARK 500    MET A1183      -75.31   -110.47                                   
REMARK 500    HIS A1185       36.60     71.44                                   
REMARK 500    PHE A1190       67.79   -114.00                                   
REMARK 500    ARG A1199      176.12    175.56                                   
REMARK 500    ALA A1203      126.75    -35.58                                   
REMARK 500    TRP A1216       -5.09    -57.11                                   
REMARK 500    PRO A1230       55.06    -61.08                                   
REMARK 500    LYS A1231        4.85    171.04                                   
REMARK 500    CYS A1232      163.97    -47.03                                   
REMARK 500    ARG A1233       30.92   -150.69                                   
REMARK 500    VAL B 979      101.33     60.71                                   
REMARK 500    ASP B 982      105.05    173.35                                   
REMARK 500    VAL B 998      -82.59   -144.78                                   
REMARK 500    ASP B 999     -152.47    -90.58                                   
REMARK 500    CYS B1003      115.25    -38.40                                   
REMARK 500    PRO B1004      142.50    -32.11                                   
REMARK 500    SER B1005       30.53   -151.82                                   
REMARK 500    ASN B1013      171.07    -51.32                                   
REMARK 500    THR B1016      -94.61     67.93                                   
REMARK 500    SER B1017      -24.14   -146.57                                   
REMARK 500    PRO B1018       15.69    -60.30                                   
REMARK 500    MET B1019     -146.50     67.91                                   
REMARK 500    ASN B1020      149.49    174.90                                   
REMARK 500    ARG B1023     -114.76    -66.08                                   
REMARK 500    HIS B1027       27.50    -74.55                                   
REMARK 500    ASP B1035     -145.43   -127.34                                   
REMARK 500    MET B1043       -1.98    -58.96                                   
REMARK 500    MET B1049       38.51   -145.21                                   
REMARK 500    PRO B1069      174.93    -28.61                                   
REMARK 500    LEU B1070      164.61    -35.08                                   
REMARK 500    CYS B1122      158.07    178.56                                   
REMARK 500    ILE B1129     -165.12   -110.64                                   
REMARK 500    LEU B1146      -67.27    -97.84                                   
REMARK 500    ASP B1147       67.45     81.77                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      59 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  41        DISTANCE =  7.29 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 A   2  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1074   SG                                                     
REMARK 620 2 CYS A1080   SG  103.5                                              
REMARK 620 3 CYS A1037   SG  110.7 114.2                                        
REMARK 620 4 CYS A1084   SG  106.0 111.8 110.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A  10  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A1076   NE2                                                    
REMARK 620 2 HIS A1185   NE2 101.7                                              
REMARK 620 3 CYS B1014   SG  100.8 131.9                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B   9  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B1076   NE2                                                    
REMARK 620 2 CYS A1014   SG  117.6                                              
REMARK 620 3 HIS B1027   NE2  90.4 118.1                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B   7  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B1031   SG                                                     
REMARK 620 2 CYS B1042   SG  127.8                                              
REMARK 620 3 CYS B1037   SG  114.8 104.5                                        
REMARK 620 4 CYS B1033   SG  102.1 106.0  96.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B   8  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B1225   SG                                                     
REMARK 620 2 CYS B1227   SG  115.3                                              
REMARK 620 3 CYS B1172   SG  117.4 117.3                                        
REMARK 620 4 CYS B1232   SG   83.8 114.9 102.2                                  
REMARK 620 N                    1     2     3                                   
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 B1078   SG                                                     
REMARK 620 2 CYS B1031   SG  108.3                                              
REMARK 620 3 CYS B1044   SG   97.0 109.0                                        
REMARK 620 4 CYS B1074   SG  124.5 102.5 115.1                                  
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 B1074   SG                                                     
REMARK 620 2 CYS B1080   SG  108.2                                              
REMARK 620 3 CYS B1084   SG   99.0 118.5                                        
REMARK 620 4 CYS B1037   SG  103.0 115.0 110.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1236  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1031   SG                                                     
REMARK 620 2 CYS A1078   SG  101.7                                              
REMARK 620 3 CYS A1074   SG  105.0 126.2                                        
REMARK 620 4 CYS A1044   SG  114.3  93.8 115.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A   3  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1031   SG                                                     
REMARK 620 2 CYS A1037   SG  115.4                                              
REMARK 620 3 CYS A1042   SG  115.4 106.3                                        
REMARK 620 4 CYS A1033   SG  112.7 102.2 103.3                                  
REMARK 620 N                    1     2     3                                   
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 A1225   SG                                                     
REMARK 620 2 CYS A1172   SG  102.9                                              
REMARK 620 3 CYS A1232   SG   82.1  88.1                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH A 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE E11 A 2001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1236                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 2                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 3                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 4                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 10                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE E11 A 2002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 2                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH B 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE E11 B 2003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 5                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 6                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 7                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 8                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 9                    
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3FPD   RELATED DB: PDB                                   
REMARK 900 GLP-BIX COMPLEX STRUCTURE                                            
REMARK 900 RELATED ID: 3MO2   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3MO5   RELATED DB: PDB                                   
DBREF  3MO0 A  951  1235  UNP    Q9H9B1   EHMT1_HUMAN    951   1235             
DBREF  3MO0 B  951  1235  UNP    Q9H9B1   EHMT1_HUMAN    951   1235             
SEQRES   1 A  285  ASN SER GLN VAL TRP SER ALA LEU GLN MET SER LYS ALA          
SEQRES   2 A  285  LEU GLN ASP SER ALA PRO ASP ARG PRO SER PRO VAL GLU          
SEQRES   3 A  285  ARG ILE VAL SER ARG ASP ILE ALA ARG GLY TYR GLU ARG          
SEQRES   4 A  285  ILE PRO ILE PRO CYS VAL ASN ALA VAL ASP SER GLU PRO          
SEQRES   5 A  285  CYS PRO SER ASN TYR LYS TYR VAL SER GLN ASN CYS VAL          
SEQRES   6 A  285  THR SER PRO MET ASN ILE ASP ARG ASN ILE THR HIS LEU          
SEQRES   7 A  285  GLN TYR CYS VAL CYS ILE ASP ASP CYS SER SER SER ASN          
SEQRES   8 A  285  CYS MET CYS GLY GLN LEU SER MET ARG CYS TRP TYR ASP          
SEQRES   9 A  285  LYS ASP GLY ARG LEU LEU PRO GLU PHE ASN MET ALA GLU          
SEQRES  10 A  285  PRO PRO LEU ILE PHE GLU CYS ASN HIS ALA CYS SER CYS          
SEQRES  11 A  285  TRP ARG ASN CYS ARG ASN ARG VAL VAL GLN ASN GLY LEU          
SEQRES  12 A  285  ARG ALA ARG LEU GLN LEU TYR ARG THR ARG ASP MET GLY          
SEQRES  13 A  285  TRP GLY VAL ARG SER LEU GLN ASP ILE PRO PRO GLY THR          
SEQRES  14 A  285  PHE VAL CYS GLU TYR VAL GLY GLU LEU ILE SER ASP SER          
SEQRES  15 A  285  GLU ALA ASP VAL ARG GLU GLU ASP SER TYR LEU PHE ASP          
SEQRES  16 A  285  LEU ASP ASN LYS ASP GLY GLU VAL TYR CYS ILE ASP ALA          
SEQRES  17 A  285  ARG PHE TYR GLY ASN VAL SER ARG PHE ILE ASN HIS HIS          
SEQRES  18 A  285  CYS GLU PRO ASN LEU VAL PRO VAL ARG VAL PHE MET ALA          
SEQRES  19 A  285  HIS GLN ASP LEU ARG PHE PRO ARG ILE ALA PHE PHE SER          
SEQRES  20 A  285  THR ARG LEU ILE GLU ALA GLY GLU GLN LEU GLY PHE ASP          
SEQRES  21 A  285  TYR GLY GLU ARG PHE TRP ASP ILE LYS GLY LYS LEU PHE          
SEQRES  22 A  285  SER CYS ARG CYS GLY SER PRO LYS CYS ARG HIS SER              
SEQRES   1 B  285  ASN SER GLN VAL TRP SER ALA LEU GLN MET SER LYS ALA          
SEQRES   2 B  285  LEU GLN ASP SER ALA PRO ASP ARG PRO SER PRO VAL GLU          
SEQRES   3 B  285  ARG ILE VAL SER ARG ASP ILE ALA ARG GLY TYR GLU ARG          
SEQRES   4 B  285  ILE PRO ILE PRO CYS VAL ASN ALA VAL ASP SER GLU PRO          
SEQRES   5 B  285  CYS PRO SER ASN TYR LYS TYR VAL SER GLN ASN CYS VAL          
SEQRES   6 B  285  THR SER PRO MET ASN ILE ASP ARG ASN ILE THR HIS LEU          
SEQRES   7 B  285  GLN TYR CYS VAL CYS ILE ASP ASP CYS SER SER SER ASN          
SEQRES   8 B  285  CYS MET CYS GLY GLN LEU SER MET ARG CYS TRP TYR ASP          
SEQRES   9 B  285  LYS ASP GLY ARG LEU LEU PRO GLU PHE ASN MET ALA GLU          
SEQRES  10 B  285  PRO PRO LEU ILE PHE GLU CYS ASN HIS ALA CYS SER CYS          
SEQRES  11 B  285  TRP ARG ASN CYS ARG ASN ARG VAL VAL GLN ASN GLY LEU          
SEQRES  12 B  285  ARG ALA ARG LEU GLN LEU TYR ARG THR ARG ASP MET GLY          
SEQRES  13 B  285  TRP GLY VAL ARG SER LEU GLN ASP ILE PRO PRO GLY THR          
SEQRES  14 B  285  PHE VAL CYS GLU TYR VAL GLY GLU LEU ILE SER ASP SER          
SEQRES  15 B  285  GLU ALA ASP VAL ARG GLU GLU ASP SER TYR LEU PHE ASP          
SEQRES  16 B  285  LEU ASP ASN LYS ASP GLY GLU VAL TYR CYS ILE ASP ALA          
SEQRES  17 B  285  ARG PHE TYR GLY ASN VAL SER ARG PHE ILE ASN HIS HIS          
SEQRES  18 B  285  CYS GLU PRO ASN LEU VAL PRO VAL ARG VAL PHE MET ALA          
SEQRES  19 B  285  HIS GLN ASP LEU ARG PHE PRO ARG ILE ALA PHE PHE SER          
SEQRES  20 B  285  THR ARG LEU ILE GLU ALA GLY GLU GLN LEU GLY PHE ASP          
SEQRES  21 B  285  TYR GLY GLU ARG PHE TRP ASP ILE LYS GLY LYS LEU PHE          
SEQRES  22 B  285  SER CYS ARG CYS GLY SER PRO LYS CYS ARG HIS SER              
HET    SAH  A 101      26                                                       
HET    E11  A2001      35                                                       
HET     ZN  A1236       1                                                       
HET     ZN  A   2       1                                                       
HET     ZN  A   3       1                                                       
HET     ZN  A   4       1                                                       
HET     ZN  A  10       1                                                       
HET    E11  A2002      35                                                       
HET    EDO  B   1       4                                                       
HET    EDO  B   2       4                                                       
HET    SAH  B 102      26                                                       
HET    E11  B2003      35                                                       
HET     ZN  B   5       1                                                       
HET     ZN  B   6       1                                                       
HET     ZN  B   7       1                                                       
HET     ZN  B   8       1                                                       
HET     ZN  B   9       1                                                       
HETNAM     SAH S-ADENOSYL-L-HOMOCYSTEINE                                        
HETNAM     E11 N~4~-(1-BENZYLPIPERIDIN-4-YL)-N~2~-[3-(DIMETHYLAMINO)            
HETNAM   2 E11  PROPYL]-6,7-DIMETHOXYQUINAZOLINE-2,4-DIAMINE                    
HETNAM      ZN ZINC ION                                                         
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3  SAH    2(C14 H20 N6 O5 S)                                           
FORMUL   4  E11    3(C27 H38 N6 O2)                                             
FORMUL   5   ZN    10(ZN 2+)                                                    
FORMUL  11  EDO    2(C2 H6 O2)                                                  
FORMUL  20  HOH   *44(H2 O)                                                     
HELIX    1   1 CYS A 1042  SER A 1048  1                                   7    
HELIX    2   2 VAL A 1088  GLY A 1092  5                                   5    
HELIX    3   3 ASP A 1131  ASP A 1135  1                                   5    
HELIX    4   4 VAL A 1164  ILE A 1168  5                                   5    
HELIX    5   5 GLY A 1212  LYS A 1219  1                                   8    
HELIX    6   6 ARG B 1023  HIS B 1027  5                                   5    
HELIX    7   7 GLN B 1046  ARG B 1050  5                                   5    
HELIX    8   8 VAL B 1088  GLY B 1092  5                                   5    
HELIX    9   9 ASP B 1131  ASP B 1135  1                                   5    
HELIX   10  10 ASN B 1163  ILE B 1168  5                                   6    
HELIX   11  11 GLY B 1212  GLY B 1220  1                                   9    
SHEET    1   A 3 CYS A 994  VAL A 995  0                                        
SHEET    2   A 3 LEU A1097  ARG A1101  1  O  LEU A1099   N  VAL A 995           
SHEET    3   A 3 TRP A1107  SER A1111 -1  O  GLY A1108   N  TYR A1100           
SHEET    1   B 4 LYS A1008  TYR A1009  0                                        
SHEET    2   B 4 VAL A1153  GLY A1162  1  O  GLY A1162   N  LYS A1008           
SHEET    3   B 4 GLY A1126  SER A1130 -1  N  GLU A1127   O  ASP A1157           
SHEET    4   B 4 CYS A1014  VAL A1015  1  N  CYS A1014   O  LEU A1128           
SHEET    1   C 3 LYS A1008  TYR A1009  0                                        
SHEET    2   C 3 VAL A1153  GLY A1162  1  O  GLY A1162   N  LYS A1008           
SHEET    3   C 3 LEU A1143  ASP A1147 -1  N  LEU A1146   O  TYR A1154           
SHEET    1   D 4 ILE A1071  PHE A1072  0                                        
SHEET    2   D 4 LEU A1176  PHE A1182  1  O  PHE A1182   N  ILE A1071           
SHEET    3   D 4 ARG A1192  SER A1197 -1  O  PHE A1196   N  VAL A1177           
SHEET    4   D 4 PHE A1120  GLU A1123 -1  N  CYS A1122   O  PHE A1195           
SHEET    1   E 2 ASN A1169  HIS A1170  0                                        
SHEET    2   E 2 GLY A1208  PHE A1209  1  O  PHE A1209   N  ASN A1169           
SHEET    1   F 3 CYS B 994  VAL B 995  0                                        
SHEET    2   F 3 LEU B1097  ARG B1101  1  O  LEU B1099   N  VAL B 995           
SHEET    3   F 3 TRP B1107  SER B1111 -1  O  GLY B1108   N  TYR B1100           
SHEET    1   G 2 LYS B1008  TYR B1009  0                                        
SHEET    2   G 2 TYR B1161  GLY B1162  1  O  GLY B1162   N  LYS B1008           
SHEET    1   H 3 PHE B1120  GLU B1123  0                                        
SHEET    2   H 3 ARG B1192  SER B1197 -1  O  PHE B1195   N  CYS B1122           
SHEET    3   H 3 LEU B1176  VAL B1181 -1  N  VAL B1179   O  ALA B1194           
SHEET    1   I 2 GLU B1127  SER B1130  0                                        
SHEET    2   I 2 TYR B1154  ASP B1157 -1  O  ASP B1157   N  GLU B1127           
SSBOND   1 CYS A  994    CYS A 1003                          1555   1555  2.05  
SSBOND   2 CYS B  994    CYS B 1003                          1555   1555  2.04  
LINK         SG  CYS A1074                ZN    ZN A   2     1555   1555  2.13  
LINK         NE2 HIS A1076                ZN    ZN A  10     1555   1555  2.17  
LINK         NE2 HIS B1076                ZN    ZN B   9     1555   1555  2.18  
LINK         SG  CYS A1080                ZN    ZN A   2     1555   1555  2.20  
LINK         SG  CYS B1031                ZN    ZN B   7     1555   1555  2.23  
LINK         SG  CYS A1014                ZN    ZN B   9     1555   1555  2.25  
LINK         SG  CYS B1225                ZN    ZN B   8     1555   1555  2.26  
LINK         SG  CYS B1042                ZN    ZN B   7     1555   1555  2.27  
LINK         NE2 HIS B1027                ZN    ZN B   9     1555   1555  2.28  
LINK         SG  CYS B1078                ZN    ZN B   5     1555   1555  2.28  
LINK         SG  CYS B1074                ZN    ZN B   6     1555   1555  2.30  
LINK         SG  CYS A1037                ZN    ZN A   2     1555   1555  2.31  
LINK         SG  CYS B1080                ZN    ZN B   6     1555   1555  2.32  
LINK         SG  CYS B1227                ZN    ZN B   8     1555   1555  2.33  
LINK         SG  CYS A1031                ZN    ZN A1236     1555   1555  2.33  
LINK         SG  CYS B1037                ZN    ZN B   7     1555   1555  2.38  
LINK         SG  CYS A1031                ZN    ZN A   3     1555   1555  2.39  
LINK         SG  CYS A1084                ZN    ZN A   2     1555   1555  2.39  
LINK         SG  CYS A1037                ZN    ZN A   3     1555   1555  2.39  
LINK         SG  CYS A1078                ZN    ZN A1236     1555   1555  2.40  
LINK         SG  CYS A1042                ZN    ZN A   3     1555   1555  2.41  
LINK         SG  CYS B1031                ZN    ZN B   5     1555   1555  2.42  
LINK         NE2 HIS A1185                ZN    ZN A  10     1555   1555  2.42  
LINK         SG  CYS B1084                ZN    ZN B   6     1555   1555  2.42  
LINK         SG  CYS A1074                ZN    ZN A1236     1555   1555  2.45  
LINK         SG  CYS B1044                ZN    ZN B   5     1555   1555  2.46  
LINK         SG  CYS B1033                ZN    ZN B   7     1555   1555  2.47  
LINK         SG  CYS B1172                ZN    ZN B   8     1555   1555  2.56  
LINK         SG  CYS B1037                ZN    ZN B   6     1555   1555  2.61  
LINK         SG  CYS A1044                ZN    ZN A1236     1555   1555  2.61  
LINK         SG  CYS B1074                ZN    ZN B   5     1555   1555  2.61  
LINK         SG  CYS A1033                ZN    ZN A   3     1555   1555  2.62  
LINK         SG  CYS A1225                ZN    ZN A   4     1555   1555  2.64  
LINK         SG  CYS A1172                ZN    ZN A   4     1555   1555  2.65  
LINK         SG  CYS A1232                ZN    ZN A   4     1555   1555  2.75  
LINK         SG  CYS B1232                ZN    ZN B   8     1555   1555  2.75  
LINK         SG  CYS B1014                ZN    ZN A  10     1555   1555  2.81  
SITE     1 AC1 11 MET A1105  GLY A1106  TRP A1107  SER A1141                    
SITE     2 AC1 11 TYR A1142  ARG A1166  ASN A1169  HIS A1170                    
SITE     3 AC1 11 TYR A1211  PHE A1223  ARG A1226                               
SITE     1 AC2 11 ASN A1083  ASP A1131  ALA A1134  ASP A1135                    
SITE     2 AC2 11 GLU A1138  ASP A1140  LEU A1143  ASP A1145                    
SITE     3 AC2 11 ARG A1214  PHE A1215  ILE A1218                               
SITE     1 AC3  5  ZN A   3  CYS A1031  CYS A1044  CYS A1074                    
SITE     2 AC3  5 CYS A1078                                                     
SITE     1 AC4  5  ZN A   3  CYS A1037  CYS A1074  CYS A1080                    
SITE     2 AC4  5 CYS A1084                                                     
SITE     1 AC5  6  ZN A   2  CYS A1031  CYS A1033  CYS A1037                    
SITE     2 AC5  6 CYS A1042   ZN A1236                                          
SITE     1 AC6  4 CYS A1172  CYS A1225  CYS A1227  CYS A1232                    
SITE     1 AC7  4 HIS A1027  HIS A1076  HIS A1185  CYS B1014                    
SITE     1 AC8 10 ASP A1131  ALA A1134  ARG A1137  GLU A1138                    
SITE     2 AC8 10 ASP A1140  LEU A1143  ASP A1145  ARG A1214                    
SITE     3 AC8 10 PHE A1215  ILE A1218                                          
SITE     1 AC9  6 SER A1132  ASP A1135  VAL A1136  GLY B 986                    
SITE     2 AC9  6 GLU B 988  PRO B 991                                          
SITE     1 BC1  4 ILE B 983  ARG B 985  TYR B1007  TYR B1009                    
SITE     1 BC2 12 MET B1105  GLY B1106  TRP B1107  SER B1141                    
SITE     2 BC2 12 TYR B1142  ARG B1166  ASN B1169  HIS B1170                    
SITE     3 BC2 12 TYR B1211  PHE B1223  ARG B1226  CYS B1227                    
SITE     1 BC3  8 ALA B1134  ASP B1135  ARG B1137  ASP B1140                    
SITE     2 BC3  8 LEU B1143  ASP B1145  PHE B1215  ILE B1218                    
SITE     1 BC4  4 CYS B1031  CYS B1044  CYS B1074  CYS B1078                    
SITE     1 BC5  4 CYS B1037  CYS B1074  CYS B1080  CYS B1084                    
SITE     1 BC6  4 CYS B1031  CYS B1033  CYS B1037  CYS B1042                    
SITE     1 BC7  4 CYS B1172  CYS B1225  CYS B1227  CYS B1232                    
SITE     1 BC8  4 CYS A1014  HIS B1027  HIS B1076  HIS B1185                    
CRYST1   47.300   94.500  138.200  90.00  90.00  90.00 P 21 21 21    8          
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      0.021142  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010582  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007236        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system