GenomeNet

Database: PDB
Entry: 3MO2
LinkDB: 3MO2
Original site: 3MO2 
HEADER    TRANSFERASE                             22-APR-10   3MO2              
TITLE     HUMAN G9A-LIKE (GLP, ALSO KNOWN AS EHMT1) IN COMPLEX WITH INHIBITOR   
TITLE    2 E67                                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE, H3 LYSINE-9 SPECIFIC 5;
COMPND   3 CHAIN: A, B, C, D;                                                   
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 3MO2    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.    2.49 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 : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.49                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 31.83                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 451338.010                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 91.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 41772                          
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) : 0.192                           
REMARK   3   FREE R VALUE                     : 0.248                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2107                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.005                           
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) : 2.49                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.58                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 84.60                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3640                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2660                       
REMARK   3   BIN FREE R VALUE                    : 0.3080                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.10                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 195                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.022                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8094                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 228                                     
REMARK   3   SOLVENT ATOMS            : 397                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 27.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.60                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.39000                                             
REMARK   3    B22 (A**2) : -5.43000                                             
REMARK   3    B33 (A**2) : 8.82000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 10.25000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.28                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.24                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 35.00                           
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.37                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.33                            
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) : 24.00                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.83                            
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) : 1.390 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.400 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.980 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.950 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.35                                                 
REMARK   3   BSOL        : 39.84                                                
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  : E67_MOD.PAR                                    
REMARK   3  PARAMETER FILE  5  : SAH_XPLOR.PAR                                  
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : E67_MOD.TOP                                    
REMARK   3  TOPOLOGY FILE  5   : SAH_XPLOR.TOP                                  
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED                   
REMARK   4                                                                      
REMARK   4 3MO2 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 RCSB058786.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-OCT-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 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   : 43245                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.490                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 31.830                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.4                               
REMARK 200  DATA REDUNDANCY                : 4.300                              
REMARK 200  R MERGE                    (I) : 0.09500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.49                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.58                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.38400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.600                              
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   (%): 51.51                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES PH 7.5, 14% POLYETHYLENE     
REMARK 280  GLYCOL 4000, 9% ISOPROPANOL, AND 12% DIMETHYL SULFOXIDE, VAPOR      
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 289K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       81.50000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6                                        
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: 4 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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
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: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
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: 5                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2150 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24030 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 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 350                                                                      
REMARK 350 BIOMOLECULE: 6                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2080 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23280 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
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     ARG A   977                                                      
REMARK 465     ASN A  1148                                                      
REMARK 465     LYS A  1149                                                      
REMARK 465     ASP A  1150                                                      
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     ASP B  1150                                                      
REMARK 465     GLY B  1151                                                      
REMARK 465     ASN C   951                                                      
REMARK 465     SER C   952                                                      
REMARK 465     GLN C   953                                                      
REMARK 465     VAL C   954                                                      
REMARK 465     TRP C   955                                                      
REMARK 465     SER C   956                                                      
REMARK 465     ALA C   957                                                      
REMARK 465     LEU C   958                                                      
REMARK 465     GLN C   959                                                      
REMARK 465     MET C   960                                                      
REMARK 465     SER C   961                                                      
REMARK 465     LYS C   962                                                      
REMARK 465     ALA C   963                                                      
REMARK 465     LEU C   964                                                      
REMARK 465     GLN C   965                                                      
REMARK 465     ASP C   966                                                      
REMARK 465     SER C   967                                                      
REMARK 465     ALA C   968                                                      
REMARK 465     PRO C   969                                                      
REMARK 465     ASP C   970                                                      
REMARK 465     ARG C   971                                                      
REMARK 465     PRO C   972                                                      
REMARK 465     SER C   973                                                      
REMARK 465     PRO C   974                                                      
REMARK 465     ASN C  1148                                                      
REMARK 465     LYS C  1149                                                      
REMARK 465     ASP C  1150                                                      
REMARK 465     ASN D   951                                                      
REMARK 465     SER D   952                                                      
REMARK 465     GLN D   953                                                      
REMARK 465     VAL D   954                                                      
REMARK 465     TRP D   955                                                      
REMARK 465     SER D   956                                                      
REMARK 465     ALA D   957                                                      
REMARK 465     LEU D   958                                                      
REMARK 465     GLN D   959                                                      
REMARK 465     MET D   960                                                      
REMARK 465     SER D   961                                                      
REMARK 465     LYS D   962                                                      
REMARK 465     ALA D   963                                                      
REMARK 465     LEU D   964                                                      
REMARK 465     GLN D   965                                                      
REMARK 465     ASP D   966                                                      
REMARK 465     SER D   967                                                      
REMARK 465     ALA D   968                                                      
REMARK 465     PRO D   969                                                      
REMARK 465     ASP D   970                                                      
REMARK 465     ARG D   971                                                      
REMARK 465     PRO D   972                                                      
REMARK 465     SER D   973                                                      
REMARK 465     PRO D   974                                                      
REMARK 465     VAL D   975                                                      
REMARK 465     ASN D  1148                                                      
REMARK 465     LYS D  1149                                                      
REMARK 465     ASP D  1150                                                      
REMARK 465     GLY D  1151                                                      
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     ILE A 978    CG1  CG2  CD1                                       
REMARK 470     LYS A1055    CG   CD   CE   NZ                                   
REMARK 470     ARG A1103    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     MET A1105    CG   SD   CE                                        
REMARK 470     GLU A1138    CG   CD   OE1  OE2                                  
REMARK 470     GLU A1152    CG   CD   OE1  OE2                                  
REMARK 470     GLU A1173    CG   CD   OE1  OE2                                  
REMARK 470     GLU A1213    CG   CD   OE1  OE2                                  
REMARK 470     LEU A1222    CG   CD1  CD2                                       
REMARK 470     SER A1224    OG                                                  
REMARK 470     ARG A1226    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 976    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 977    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 981    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE B1034    CG1  CG2  CD1                                       
REMARK 470     GLU B1067    CG   CD   OE1  OE2                                  
REMARK 470     ARG B1103    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B1138    CG   CD   OE1  OE2                                  
REMARK 470     ASN B1148    CG   OD1  ND2                                       
REMARK 470     LYS B1149    CG   CD   CE   NZ                                   
REMARK 470     GLU B1213    CG   CD   OE1  OE2                                  
REMARK 470     SER B1235    OG                                                  
REMARK 470     VAL C 975    CG1  CG2                                            
REMARK 470     GLU C 976    CG   CD   OE1  OE2                                  
REMARK 470     ILE C 978    CG1  CG2  CD1                                       
REMARK 470     ARG C 981    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C1094    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C1103    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP C1104    CG   OD1  OD2                                       
REMARK 470     GLU C1138    CG   CD   OE1  OE2                                  
REMARK 470     ASP C1147    CG   OD1  OD2                                       
REMARK 470     LYS C1221    CG   CD   CE   NZ                                   
REMARK 470     LYS C1231    CG   CD   CE   NZ                                   
REMARK 470     GLU D 976    CG   CD   OE1  OE2                                  
REMARK 470     ARG D 977    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL D 979    CG1  CG2                                            
REMARK 470     ARG D 981    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER D1040    OG                                                  
REMARK 470     ARG D1050    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D1055    CG   CD   CE   NZ                                   
REMARK 470     GLU D1067    CG   CD   OE1  OE2                                  
REMARK 470     ARG D1094    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG D1103    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP D1104    CG   OD1  OD2                                       
REMARK 470     GLU D1138    CG   CD   OE1  OE2                                  
REMARK 470     GLU D1139    CG   CD   OE1  OE2                                  
REMARK 470     GLU D1152    CG   CD   OE1  OE2                                  
REMARK 470     GLU D1173    CG   CD   OE1  OE2                                  
REMARK 470     GLU D1213    CG   CD   OE1  OE2                                  
REMARK 470     LYS D1221    CG   CD   CE   NZ                                   
REMARK 470     ARG D1226    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D1231    CG   CD   CE   NZ                                   
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 D1174   C   -  N   -  CA  ANGL. DEV. =   9.2 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    SER A 980      124.26   -179.84                                   
REMARK 500    VAL A 998      -94.87   -107.14                                   
REMARK 500    ASP A 999     -158.20    -88.46                                   
REMARK 500    PRO A1002     -178.34    -68.68                                   
REMARK 500    SER A1005       15.56   -148.83                                   
REMARK 500    ASN A1006       38.70    -97.11                                   
REMARK 500    SER A1017     -179.78   -176.61                                   
REMARK 500    ASP A1035     -155.91   -105.90                                   
REMARK 500    CYS A1042      116.02    -38.95                                   
REMARK 500    MET A1049      -46.33     85.02                                   
REMARK 500    ASN A1086       46.76    -89.03                                   
REMARK 500    VAL A1088      -59.78   -130.39                                   
REMARK 500    ASP A1104        5.89    -62.56                                   
REMARK 500    VAL A1121      -65.88    -97.57                                   
REMARK 500    MET A1183      -92.15   -132.29                                   
REMARK 500    ARG A1199      176.86    177.10                                   
REMARK 500    PHE A1223      167.62    178.20                                   
REMARK 500    SER B 980      129.23    171.75                                   
REMARK 500    ASP B 982      106.47   -172.62                                   
REMARK 500    PRO B 991      155.44    -49.81                                   
REMARK 500    ALA B 997       29.60   -142.53                                   
REMARK 500    ASP B 999     -154.43   -172.79                                   
REMARK 500    GLU B1001      115.86    -12.49                                   
REMARK 500    SER B1005       19.18   -154.81                                   
REMARK 500    ASN B1020       42.18    -64.55                                   
REMARK 500    ASP B1035     -153.71   -102.42                                   
REMARK 500    MET B1049      -48.20     87.39                                   
REMARK 500    ASN B1086       47.34    -81.14                                   
REMARK 500    VAL B1088      -66.02   -131.98                                   
REMARK 500    ASN B1163     -169.72   -118.91                                   
REMARK 500    MET B1183      -89.33   -129.65                                   
REMARK 500    LEU B1188      -13.43    -48.91                                   
REMARK 500    LEU B1222      -21.75   -149.07                                   
REMARK 500    HIS B1234       25.65   -141.43                                   
REMARK 500    SER C 980      130.18   -175.19                                   
REMARK 500    ASP C 982      100.35   -169.90                                   
REMARK 500    ALA C 997       20.83   -155.33                                   
REMARK 500    ASP C 999     -156.42   -133.44                                   
REMARK 500    GLU C1001      122.85    -21.12                                   
REMARK 500    SER C1005       13.04   -155.74                                   
REMARK 500    ASN C1006       33.24    -87.76                                   
REMARK 500    ASP C1035     -150.88    -99.68                                   
REMARK 500    MET C1049      -44.46     90.79                                   
REMARK 500    CYS C1080      170.81    -56.89                                   
REMARK 500    VAL C1088      -66.85   -131.28                                   
REMARK 500    ARG C1094       21.73   -140.59                                   
REMARK 500    GLU C1138      -70.08    -59.13                                   
REMARK 500    ASN C1163     -169.58   -112.68                                   
REMARK 500    GLU C1173       64.86   -119.18                                   
REMARK 500    MET C1183      -93.47   -131.97                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      73 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 352        DISTANCE =  5.04 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 D   5  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH D 295   O                                                      
REMARK 620 2 CYS D1044   SG  161.6                                              
REMARK 620 3 CYS D1078   SG   96.7  97.2                                        
REMARK 620 4 CYS D1074   SG   73.2 107.4 126.9                                  
REMARK 620 5 CYS D1031   SG   59.7 106.1  99.3 117.0                            
REMARK 620 N                    1     2     3     4                             
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 B1080   SG                                                     
REMARK 620 2 CYS B1037   SG  101.2                                              
REMARK 620 3 CYS B1074   SG  110.8 115.0                                        
REMARK 620 4 CYS B1084   SG  114.1 113.0 103.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D   6  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH D 295   O                                                      
REMARK 620 2 CYS D1074   SG   71.4                                              
REMARK 620 3 CYS D1084   SG  172.2 110.3                                        
REMARK 620 4 CYS D1080   SG   62.1 120.8 111.7                                  
REMARK 620 5 CYS D1037   SG   85.6 105.8 101.0 105.0                            
REMARK 620 N                    1     2     3     4                             
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 B1042   SG                                                     
REMARK 620 2 CYS B1031   SG  124.4                                              
REMARK 620 3 CYS B1037   SG  120.9  99.8                                        
REMARK 620 4 CYS B1033   SG  110.1  99.2  97.4                                  
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  112.0                                              
REMARK 620 3 CYS B1172   SG  114.2 112.8                                        
REMARK 620 4 CYS B1232   SG   96.6 122.9  97.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D   7  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D1031   SG                                                     
REMARK 620 2 CYS D1037   SG  125.4                                              
REMARK 620 3 CYS D1042   SG  106.5 117.8                                        
REMARK 620 4 CYS D1033   SG   99.2 102.8  99.8                                  
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 B1074   SG                                                     
REMARK 620 2 CYS B1044   SG  102.0                                              
REMARK 620 3 CYS B1078   SG  119.3  95.8                                        
REMARK 620 4 CYS B1031   SG  111.3 124.6 104.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D   8  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D1225   SG                                                     
REMARK 620 2 CYS D1172   SG  110.9                                              
REMARK 620 3 CYS D1227   SG  108.8 123.5                                        
REMARK 620 4 CYS D1232   SG   94.9  94.3 120.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C   2  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C1080   SG                                                     
REMARK 620 2 CYS C1037   SG  114.9                                              
REMARK 620 3 CYS C1074   SG  110.7 111.0                                        
REMARK 620 4 CYS C1084   SG  108.9 106.4 104.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 340  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1044   SG                                                     
REMARK 620 2 CYS A1031   SG  117.4                                              
REMARK 620 3 CYS A1078   SG   94.7 102.3                                        
REMARK 620 4 CYS A1074   SG  108.1 112.4 121.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 341  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1037   SG                                                     
REMARK 620 2 CYS A1080   SG  106.4                                              
REMARK 620 3 CYS A1074   SG  114.2 114.8                                        
REMARK 620 4 CYS A1084   SG  106.9 112.3 102.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C   1  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C1074   SG                                                     
REMARK 620 2 CYS C1078   SG  125.2                                              
REMARK 620 3 CYS C1044   SG  106.2  94.9                                        
REMARK 620 4 CYS C1031   SG  108.9  99.4 123.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 342  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1042   SG                                                     
REMARK 620 2 CYS A1031   SG  117.6                                              
REMARK 620 3 CYS A1037   SG  119.2 105.8                                        
REMARK 620 4 CYS A1033   SG  101.5 106.8 104.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 343  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1227   SG                                                     
REMARK 620 2 CYS A1225   SG   99.6                                              
REMARK 620 3 CYS A1172   SG  112.3 134.6                                        
REMARK 620 4 CYS A1232   SG  118.2  97.8  94.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C   3  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C1031   SG                                                     
REMARK 620 2 CYS C1042   SG  116.1                                              
REMARK 620 3 CYS C1037   SG  107.4 114.8                                        
REMARK 620 4 CYS C1033   SG  105.4 104.3 108.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C   4  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C1225   SG                                                     
REMARK 620 2 CYS C1227   SG  108.0                                              
REMARK 620 3 CYS C1232   SG   97.0 118.0                                        
REMARK 620 4 CYS C1172   SG  119.4 114.1  99.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 340                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 341                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 342                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 343                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE E67 A 1                   
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 ZN B 7                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 8                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE E67 B 2                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 1                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 2                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 3                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 4                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH C 103                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE E67 C 1236                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 5                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 6                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 7                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 8                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH D 104                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE E67 D 4                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3FPD   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3MO0   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3MO5   RELATED DB: PDB                                   
DBREF  3MO2 A  951  1235  UNP    Q9H9B1   EHMT1_HUMAN    951   1235             
DBREF  3MO2 B  951  1235  UNP    Q9H9B1   EHMT1_HUMAN    951   1235             
DBREF  3MO2 C  951  1235  UNP    Q9H9B1   EHMT1_HUMAN    951   1235             
DBREF  3MO2 D  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              
SEQRES   1 C  285  ASN SER GLN VAL TRP SER ALA LEU GLN MET SER LYS ALA          
SEQRES   2 C  285  LEU GLN ASP SER ALA PRO ASP ARG PRO SER PRO VAL GLU          
SEQRES   3 C  285  ARG ILE VAL SER ARG ASP ILE ALA ARG GLY TYR GLU ARG          
SEQRES   4 C  285  ILE PRO ILE PRO CYS VAL ASN ALA VAL ASP SER GLU PRO          
SEQRES   5 C  285  CYS PRO SER ASN TYR LYS TYR VAL SER GLN ASN CYS VAL          
SEQRES   6 C  285  THR SER PRO MET ASN ILE ASP ARG ASN ILE THR HIS LEU          
SEQRES   7 C  285  GLN TYR CYS VAL CYS ILE ASP ASP CYS SER SER SER ASN          
SEQRES   8 C  285  CYS MET CYS GLY GLN LEU SER MET ARG CYS TRP TYR ASP          
SEQRES   9 C  285  LYS ASP GLY ARG LEU LEU PRO GLU PHE ASN MET ALA GLU          
SEQRES  10 C  285  PRO PRO LEU ILE PHE GLU CYS ASN HIS ALA CYS SER CYS          
SEQRES  11 C  285  TRP ARG ASN CYS ARG ASN ARG VAL VAL GLN ASN GLY LEU          
SEQRES  12 C  285  ARG ALA ARG LEU GLN LEU TYR ARG THR ARG ASP MET GLY          
SEQRES  13 C  285  TRP GLY VAL ARG SER LEU GLN ASP ILE PRO PRO GLY THR          
SEQRES  14 C  285  PHE VAL CYS GLU TYR VAL GLY GLU LEU ILE SER ASP SER          
SEQRES  15 C  285  GLU ALA ASP VAL ARG GLU GLU ASP SER TYR LEU PHE ASP          
SEQRES  16 C  285  LEU ASP ASN LYS ASP GLY GLU VAL TYR CYS ILE ASP ALA          
SEQRES  17 C  285  ARG PHE TYR GLY ASN VAL SER ARG PHE ILE ASN HIS HIS          
SEQRES  18 C  285  CYS GLU PRO ASN LEU VAL PRO VAL ARG VAL PHE MET ALA          
SEQRES  19 C  285  HIS GLN ASP LEU ARG PHE PRO ARG ILE ALA PHE PHE SER          
SEQRES  20 C  285  THR ARG LEU ILE GLU ALA GLY GLU GLN LEU GLY PHE ASP          
SEQRES  21 C  285  TYR GLY GLU ARG PHE TRP ASP ILE LYS GLY LYS LEU PHE          
SEQRES  22 C  285  SER CYS ARG CYS GLY SER PRO LYS CYS ARG HIS SER              
SEQRES   1 D  285  ASN SER GLN VAL TRP SER ALA LEU GLN MET SER LYS ALA          
SEQRES   2 D  285  LEU GLN ASP SER ALA PRO ASP ARG PRO SER PRO VAL GLU          
SEQRES   3 D  285  ARG ILE VAL SER ARG ASP ILE ALA ARG GLY TYR GLU ARG          
SEQRES   4 D  285  ILE PRO ILE PRO CYS VAL ASN ALA VAL ASP SER GLU PRO          
SEQRES   5 D  285  CYS PRO SER ASN TYR LYS TYR VAL SER GLN ASN CYS VAL          
SEQRES   6 D  285  THR SER PRO MET ASN ILE ASP ARG ASN ILE THR HIS LEU          
SEQRES   7 D  285  GLN TYR CYS VAL CYS ILE ASP ASP CYS SER SER SER ASN          
SEQRES   8 D  285  CYS MET CYS GLY GLN LEU SER MET ARG CYS TRP TYR ASP          
SEQRES   9 D  285  LYS ASP GLY ARG LEU LEU PRO GLU PHE ASN MET ALA GLU          
SEQRES  10 D  285  PRO PRO LEU ILE PHE GLU CYS ASN HIS ALA CYS SER CYS          
SEQRES  11 D  285  TRP ARG ASN CYS ARG ASN ARG VAL VAL GLN ASN GLY LEU          
SEQRES  12 D  285  ARG ALA ARG LEU GLN LEU TYR ARG THR ARG ASP MET GLY          
SEQRES  13 D  285  TRP GLY VAL ARG SER LEU GLN ASP ILE PRO PRO GLY THR          
SEQRES  14 D  285  PHE VAL CYS GLU TYR VAL GLY GLU LEU ILE SER ASP SER          
SEQRES  15 D  285  GLU ALA ASP VAL ARG GLU GLU ASP SER TYR LEU PHE ASP          
SEQRES  16 D  285  LEU ASP ASN LYS ASP GLY GLU VAL TYR CYS ILE ASP ALA          
SEQRES  17 D  285  ARG PHE TYR GLY ASN VAL SER ARG PHE ILE ASN HIS HIS          
SEQRES  18 D  285  CYS GLU PRO ASN LEU VAL PRO VAL ARG VAL PHE MET ALA          
SEQRES  19 D  285  HIS GLN ASP LEU ARG PHE PRO ARG ILE ALA PHE PHE SER          
SEQRES  20 D  285  THR ARG LEU ILE GLU ALA GLY GLU GLN LEU GLY PHE ASP          
SEQRES  21 D  285  TYR GLY GLU ARG PHE TRP ASP ILE LYS GLY LYS LEU PHE          
SEQRES  22 D  285  SER CYS ARG CYS GLY SER PRO LYS CYS ARG HIS SER              
HET     ZN  A 340       1                                                       
HET     ZN  A 341       1                                                       
HET     ZN  A 342       1                                                       
HET     ZN  A 343       1                                                       
HET    E67  A   1      40                                                       
HET     ZN  B   5       1                                                       
HET     ZN  B   6       1                                                       
HET     ZN  B   7       1                                                       
HET     ZN  B   8       1                                                       
HET    E67  B   2      40                                                       
HET     ZN  C   1       1                                                       
HET     ZN  C   2       1                                                       
HET     ZN  C   3       1                                                       
HET     ZN  C   4       1                                                       
HET    SAH  C 103      26                                                       
HET    E67  C1236      40                                                       
HET     ZN  D   5       1                                                       
HET     ZN  D   6       1                                                       
HET     ZN  D   7       1                                                       
HET     ZN  D   8       1                                                       
HET    SAH  D 104      26                                                       
HET    E67  D   4      40                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     E67 7-[(5-AMINOPENTYL)OXY]-N~4~-(1-BENZYLPIPERIDIN-4-YL)-            
HETNAM   2 E67  N~2~-[3-(DIMETHYLAMINO)PROPYL]-6-METHOXYQUINAZOLINE-2,          
HETNAM   3 E67  4-DIAMINE                                                       
HETNAM     SAH S-ADENOSYL-L-HOMOCYSTEINE                                        
FORMUL   5   ZN    16(ZN 2+)                                                    
FORMUL   9  E67    4(C31 H47 N7 O2)                                             
FORMUL  19  SAH    2(C14 H20 N6 O5 S)                                           
FORMUL  27  HOH   *397(H2 O)                                                    
HELIX    1   1 ASN A 1024  LEU A 1028  5                                   5    
HELIX    2   2 CYS A 1042  SER A 1048  1                                   7    
HELIX    3   3 VAL A 1088  GLY A 1092  5                                   5    
HELIX    4   4 ASP A 1131  VAL A 1136  1                                   6    
HELIX    5   5 VAL A 1164  ILE A 1168  5                                   5    
HELIX    6   6 GLY A 1212  GLY A 1220  1                                   9    
HELIX    7   7 ASN B 1024  LEU B 1028  5                                   5    
HELIX    8   8 CYS B 1042  SER B 1048  1                                   7    
HELIX    9   9 VAL B 1088  GLY B 1092  5                                   5    
HELIX   10  10 ASP B 1131  ASP B 1135  1                                   5    
HELIX   11  11 VAL B 1164  ILE B 1168  5                                   5    
HELIX   12  12 GLY B 1212  GLY B 1220  1                                   9    
HELIX   13  13 ASN C 1024  LEU C 1028  5                                   5    
HELIX   14  14 CYS C 1042  SER C 1048  1                                   7    
HELIX   15  15 VAL C 1088  GLY C 1092  5                                   5    
HELIX   16  16 ASP C 1131  VAL C 1136  1                                   6    
HELIX   17  17 VAL C 1164  ILE C 1168  5                                   5    
HELIX   18  18 GLY C 1212  GLY C 1220  1                                   9    
HELIX   19  19 ASN D 1024  LEU D 1028  5                                   5    
HELIX   20  20 CYS D 1042  SER D 1048  1                                   7    
HELIX   21  21 VAL D 1088  GLY D 1092  5                                   5    
HELIX   22  22 ASP D 1131  ASP D 1135  1                                   5    
HELIX   23  23 VAL D 1164  ILE D 1168  5                                   5    
HELIX   24  24 GLY D 1212  GLY D 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 3 LYS A1008  TYR A1009  0                                        
SHEET    2   B 3 TYR A1154  GLY A1162  1  O  PHE A1160   N  LYS A1008           
SHEET    3   B 3 GLY A1126  SER A1130 -1  N  GLU A1127   O  ASP A1157           
SHEET    1   C 3 LYS A1008  TYR A1009  0                                        
SHEET    2   C 3 TYR A1154  GLY A1162  1  O  PHE A1160   N  LYS A1008           
SHEET    3   C 3 LEU A1143  ASP A1145 -1  N  PHE A1144   O  ILE A1156           
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  ARG A1192   N  VAL A1181           
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 4 ARG B 977  SER B 980  0                                        
SHEET    2   F 4 CYS B 994  ASN B 996 -1  O  CYS B 994   N  SER B 980           
SHEET    3   F 4 LEU B1097  ARG B1101  1  O  LEU B1099   N  VAL B 995           
SHEET    4   F 4 TRP B1107  SER B1111 -1  O  GLY B1108   N  TYR B1100           
SHEET    1   G 4 LYS B1008  TYR B1009  0                                        
SHEET    2   G 4 TYR B1154  GLY B1162  1  O  PHE B1160   N  LYS B1008           
SHEET    3   G 4 GLY B1126  SER B1130 -1  N  GLU B1127   O  ASP B1157           
SHEET    4   G 4 CYS B1014  VAL B1015  1  N  CYS B1014   O  LEU B1128           
SHEET    1   H 3 LYS B1008  TYR B1009  0                                        
SHEET    2   H 3 TYR B1154  GLY B1162  1  O  PHE B1160   N  LYS B1008           
SHEET    3   H 3 LEU B1143  ASP B1145 -1  N  PHE B1144   O  ILE B1156           
SHEET    1   I 4 ILE B1071  PHE B1072  0                                        
SHEET    2   I 4 LEU B1176  PHE B1182  1  O  ARG B1180   N  ILE B1071           
SHEET    3   I 4 ARG B1192  SER B1197 -1  O  ARG B1192   N  VAL B1181           
SHEET    4   I 4 PHE B1120  TYR B1124 -1  N  CYS B1122   O  PHE B1195           
SHEET    1   J 2 ASN B1169  HIS B1170  0                                        
SHEET    2   J 2 GLY B1208  PHE B1209  1  O  PHE B1209   N  ASN B1169           
SHEET    1   K 2 ARG C 977  SER C 980  0                                        
SHEET    2   K 2 CYS C 994  ASN C 996 -1  O  ASN C 996   N  ARG C 977           
SHEET    1   L 3 LYS C1008  TYR C1009  0                                        
SHEET    2   L 3 TYR C1154  GLY C1162  1  O  PHE C1160   N  LYS C1008           
SHEET    3   L 3 GLY C1126  SER C1130 -1  N  GLU C1127   O  ASP C1157           
SHEET    1   M 4 ILE C1071  PHE C1072  0                                        
SHEET    2   M 4 LEU C1176  PHE C1182  1  O  ARG C1180   N  ILE C1071           
SHEET    3   M 4 ARG C1192  SER C1197 -1  O  ARG C1192   N  VAL C1181           
SHEET    4   M 4 PHE C1120  TYR C1124 -1  N  VAL C1121   O  PHE C1195           
SHEET    1   N 2 LEU C1097  ARG C1101  0                                        
SHEET    2   N 2 TRP C1107  SER C1111 -1  O  GLY C1108   N  TYR C1100           
SHEET    1   O 2 ASN C1169  HIS C1170  0                                        
SHEET    2   O 2 GLY C1208  PHE C1209  1  O  PHE C1209   N  ASN C1169           
SHEET    1   P 3 CYS D 994  VAL D 995  0                                        
SHEET    2   P 3 LEU D1097  ARG D1101  1  O  LEU D1099   N  VAL D 995           
SHEET    3   P 3 TRP D1107  SER D1111 -1  O  GLY D1108   N  TYR D1100           
SHEET    1   Q 3 LYS D1008  TYR D1009  0                                        
SHEET    2   Q 3 TYR D1154  GLY D1162  1  O  PHE D1160   N  LYS D1008           
SHEET    3   Q 3 GLY D1126  SER D1130 -1  N  GLU D1127   O  ASP D1157           
SHEET    1   R 4 ILE D1071  PHE D1072  0                                        
SHEET    2   R 4 LEU D1176  PHE D1182  1  O  ARG D1180   N  ILE D1071           
SHEET    3   R 4 ARG D1192  SER D1197 -1  O  ARG D1192   N  VAL D1181           
SHEET    4   R 4 PHE D1120  GLU D1123 -1  N  VAL D1121   O  PHE D1195           
SHEET    1   S 2 ASN D1169  HIS D1170  0                                        
SHEET    2   S 2 GLY D1208  PHE D1209  1  O  PHE D1209   N  ASN D1169           
LINK        ZN    ZN D   5                 O   HOH D 295     1555   1555  2.11  
LINK         SG  CYS B1080                ZN    ZN B   6     1555   1555  2.26  
LINK        ZN    ZN D   6                 O   HOH D 295     1555   1555  2.28  
LINK         SG  CYS B1042                ZN    ZN B   7     1555   1555  2.30  
LINK         SG  CYS D1074                ZN    ZN D   6     1555   1555  2.34  
LINK         SG  CYS B1225                ZN    ZN B   8     1555   1555  2.35  
LINK         SG  CYS D1044                ZN    ZN D   5     1555   1555  2.35  
LINK         SG  CYS D1084                ZN    ZN D   6     1555   1555  2.35  
LINK         SG  CYS D1078                ZN    ZN D   5     1555   1555  2.36  
LINK         SG  CYS D1031                ZN    ZN D   7     1555   1555  2.36  
LINK         SG  CYS D1074                ZN    ZN D   5     1555   1555  2.39  
LINK         SG  CYS B1227                ZN    ZN B   8     1555   1555  2.40  
LINK         SG  CYS B1074                ZN    ZN B   5     1555   1555  2.40  
LINK         SG  CYS B1044                ZN    ZN B   5     1555   1555  2.41  
LINK         SG  CYS B1031                ZN    ZN B   7     1555   1555  2.41  
LINK         SG  CYS B1037                ZN    ZN B   6     1555   1555  2.41  
LINK         SG  CYS B1074                ZN    ZN B   6     1555   1555  2.41  
LINK         SG  CYS B1084                ZN    ZN B   6     1555   1555  2.42  
LINK         SG  CYS B1078                ZN    ZN B   5     1555   1555  2.45  
LINK         SG  CYS D1037                ZN    ZN D   7     1555   1555  2.45  
LINK         SG  CYS D1080                ZN    ZN D   6     1555   1555  2.47  
LINK         SG  CYS B1172                ZN    ZN B   8     1555   1555  2.48  
LINK         SG  CYS B1031                ZN    ZN B   5     1555   1555  2.48  
LINK         SG  CYS B1037                ZN    ZN B   7     1555   1555  2.48  
LINK         SG  CYS B1033                ZN    ZN B   7     1555   1555  2.49  
LINK         SG  CYS D1042                ZN    ZN D   7     1555   1555  2.53  
LINK         SG  CYS D1033                ZN    ZN D   7     1555   1555  2.54  
LINK         SG  CYS D1225                ZN    ZN D   8     1555   1555  2.54  
LINK         SG  CYS D1037                ZN    ZN D   6     1555   1555  2.58  
LINK         SG  CYS D1172                ZN    ZN D   8     1555   1555  2.59  
LINK         SG  CYS D1227                ZN    ZN D   8     1555   1555  2.60  
LINK         SG  CYS D1232                ZN    ZN D   8     1555   1555  2.65  
LINK         SG  CYS B1232                ZN    ZN B   8     1555   1555  2.69  
LINK         SG  CYS D1031                ZN    ZN D   5     1555   1555  2.72  
LINK         SG  CYS C1080                ZN    ZN C   2     1555   1555  2.20  
LINK         SG  CYS A1044                ZN    ZN A 340     1555   1555  2.25  
LINK         SG  CYS A1037                ZN    ZN A 341     1555   1555  2.27  
LINK         SG  CYS A1080                ZN    ZN A 341     1555   1555  2.28  
LINK         SG  CYS A1074                ZN    ZN A 341     1555   1555  2.30  
LINK         SG  CYS C1074                ZN    ZN C   1     1555   1555  2.32  
LINK         SG  CYS A1042                ZN    ZN A 342     1555   1555  2.32  
LINK         SG  CYS C1037                ZN    ZN C   2     1555   1555  2.33  
LINK         SG  CYS A1227                ZN    ZN A 343     1555   1555  2.35  
LINK         SG  CYS C1031                ZN    ZN C   3     1555   1555  2.37  
LINK         SG  CYS A1031                ZN    ZN A 342     1555   1555  2.37  
LINK         SG  CYS C1078                ZN    ZN C   1     1555   1555  2.37  
LINK         SG  CYS C1225                ZN    ZN C   4     1555   1555  2.38  
LINK         SG  CYS C1042                ZN    ZN C   3     1555   1555  2.39  
LINK         SG  CYS C1074                ZN    ZN C   2     1555   1555  2.40  
LINK         SG  CYS A1225                ZN    ZN A 343     1555   1555  2.40  
LINK         SG  CYS C1227                ZN    ZN C   4     1555   1555  2.41  
LINK         SG  CYS A1037                ZN    ZN A 342     1555   1555  2.41  
LINK         SG  CYS A1031                ZN    ZN A 340     1555   1555  2.41  
LINK         SG  CYS A1084                ZN    ZN A 341     1555   1555  2.41  
LINK         SG  CYS C1037                ZN    ZN C   3     1555   1555  2.44  
LINK         SG  CYS A1078                ZN    ZN A 340     1555   1555  2.44  
LINK         SG  CYS A1074                ZN    ZN A 340     1555   1555  2.45  
LINK         SG  CYS C1044                ZN    ZN C   1     1555   1555  2.46  
LINK         SG  CYS A1033                ZN    ZN A 342     1555   1555  2.46  
LINK         SG  CYS C1084                ZN    ZN C   2     1555   1555  2.46  
LINK         SG  CYS C1033                ZN    ZN C   3     1555   1555  2.50  
LINK         SG  CYS C1232                ZN    ZN C   4     1555   1555  2.51  
LINK         SG  CYS C1031                ZN    ZN C   1     1555   1555  2.53  
LINK         SG  CYS C1172                ZN    ZN C   4     1555   1555  2.55  
LINK         SG  CYS A1172                ZN    ZN A 343     1555   1555  2.62  
LINK         SG  CYS A1232                ZN    ZN A 343     1555   1555  2.79  
SITE     1 AC1  6  ZN A 341   ZN A 342  CYS A1031  CYS A1044                    
SITE     2 AC1  6 CYS A1074  CYS A1078                                          
SITE     1 AC2  6  ZN A 340   ZN A 342  CYS A1037  CYS A1074                    
SITE     2 AC2  6 CYS A1080  CYS A1084                                          
SITE     1 AC3  6  ZN A 340   ZN A 341  CYS A1031  CYS A1033                    
SITE     2 AC3  6 CYS A1037  CYS A1042                                          
SITE     1 AC4  4 CYS A1172  CYS A1225  CYS A1227  CYS A1232                    
SITE     1 AC5 13 HOH A 164  ASP A1131  ALA A1134  ASP A1135                    
SITE     2 AC5 13 ARG A1137  GLU A1138  ASP A1140  SER A1141                    
SITE     3 AC5 13 LEU A1143  ASP A1145  TYR A1211  ARG A1214                    
SITE     4 AC5 13 PHE A1215                                                     
SITE     1 AC6  5  ZN B   7  CYS B1031  CYS B1044  CYS B1074                    
SITE     2 AC6  5 CYS B1078                                                     
SITE     1 AC7  4 CYS B1037  CYS B1074  CYS B1080  CYS B1084                    
SITE     1 AC8  5  ZN B   5  CYS B1031  CYS B1033  CYS B1037                    
SITE     2 AC8  5 CYS B1042                                                     
SITE     1 AC9  4 CYS B1172  CYS B1225  CYS B1227  CYS B1232                    
SITE     1 BC1 11 ASP B1131  ASP B1135  ARG B1137  ASP B1140                    
SITE     2 BC1 11 SER B1141  LEU B1143  ASP B1145  TYR B1211                    
SITE     3 BC1 11 ARG B1214  PHE B1215  ARG D1189                               
SITE     1 BC2  5  ZN C   2  CYS C1031  CYS C1044  CYS C1074                    
SITE     2 BC2  5 CYS C1078                                                     
SITE     1 BC3  6  ZN C   1   ZN C   3  CYS C1037  CYS C1074                    
SITE     2 BC3  6 CYS C1080  CYS C1084                                          
SITE     1 BC4  5  ZN C   2  CYS C1031  CYS C1033  CYS C1037                    
SITE     2 BC4  5 CYS C1042                                                     
SITE     1 BC5  4 CYS C1172  CYS C1225  CYS C1227  CYS C1232                    
SITE     1 BC6 11 MET C1105  TRP C1107  SER C1141  TYR C1142                    
SITE     2 BC6 11 ARG C1166  PHE C1167  ASN C1169  HIS C1170                    
SITE     3 BC6 11 TYR C1211  CYS C1225  ARG C1226                               
SITE     1 BC7 12 ARG A1189  ASP C1131  ASP C1135  ARG C1137                    
SITE     2 BC7 12 ASP C1140  SER C1141  LEU C1143  ASP C1145                    
SITE     3 BC7 12 TYR C1211  ARG C1214  PHE C1215  LYS C1219                    
SITE     1 BC8  7  ZN D   6   ZN D   7  HOH D 295  CYS D1031                    
SITE     2 BC8  7 CYS D1044  CYS D1074  CYS D1078                               
SITE     1 BC9  6  ZN D   5  HOH D 295  CYS D1037  CYS D1074                    
SITE     2 BC9  6 CYS D1080  CYS D1084                                          
SITE     1 CC1  6  ZN D   5  HOH D 295  CYS D1031  CYS D1033                    
SITE     2 CC1  6 CYS D1037  CYS D1042                                          
SITE     1 CC2  4 CYS D1172  CYS D1225  CYS D1227  CYS D1232                    
SITE     1 CC3 14 MET D1105  GLY D1106  TRP D1107  SER D1141                    
SITE     2 CC3 14 TYR D1142  ARG D1166  ASN D1169  HIS D1170                    
SITE     3 CC3 14 TYR D1211  PHE D1215  PHE D1223  SER D1224                    
SITE     4 CC3 14 CYS D1225  ARG D1226                                          
SITE     1 CC4 12 ASP D1131  ASP D1135  VAL D1136  ARG D1137                    
SITE     2 CC4 12 ASP D1140  SER D1141  LEU D1143  ASP D1145                    
SITE     3 CC4 12 TYR D1211  ARG D1214  PHE D1215  LYS D1219                    
CRYST1   59.700  163.000   69.300  90.00  98.90  90.00 P 1 21 1      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      0.016750  0.000000  0.002623        0.00000                         
SCALE2      0.000000  0.006135  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014606        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system