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Database: PDB
Entry: 3FPD
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HEADER    TRANSFERASE                             05-JAN-09   3FPD              
TITLE     G9A-LIKE PROTEIN LYSINE METHYLTRANSFERASE INHIBITION BY BIX-          
TITLE    2 01294                                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE, H3 LYSINE-9            
COMPND   3 SPECIFIC 5;                                                          
COMPND   4 CHAIN: A, B;                                                         
COMPND   5 FRAGMENT: UNP RESIDUES 975-1235, SET DOMAIN;                         
COMPND   6 SYNONYM: HISTONE H3-K9 METHYLTRANSFERASE 5, H3-K9-HMTASE 5,          
COMPND   7 EUCHROMATIC HISTONE-LYSINE N-METHYLTRANSFERASE 1, EU-                
COMPND   8 HMTASE1, G9A-LIKE PROTEIN 1, GLP1, LYSINE N-                         
COMPND   9 METHYLTRANSFERASE 1D;                                                
COMPND  10 EC: 2.1.1.43;                                                        
COMPND  11 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;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PXC681                                    
KEYWDS    EPIGENETICS, HISTONE LYSINE METHYLATION, CATALYTIC SET                
KEYWDS   2 DOMAIN, INHIBITION BY BIX-01294, ALTERNATIVE SPLICING, ANK           
KEYWDS   3 REPEAT, CHROMATIN REGULATOR, METAL-BINDING,                          
KEYWDS   4 METHYLTRANSFERASE, NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, S-         
KEYWDS   5 ADENOSYL-L-METHIONINE, TRANSFERASE, ZINC                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.CHANG,X.ZHANG,J.R.HORTON,X.CHENG                                    
REVDAT   2   24-MAR-09 3FPD    1       JRNL                                     
REVDAT   1   17-FEB-09 3FPD    0                                                
JRNL        AUTH   Y.CHANG,X.ZHANG,J.R.HORTON,A.K.UPADHYAY,                     
JRNL        AUTH 2 A.SPANNHOFF,J.LIU,J.P.SNYDER,M.T.BEDFORD,X.CHENG             
JRNL        TITL   STRUCTURAL BASIS FOR G9A-LIKE PROTEIN LYSINE                 
JRNL        TITL 2 METHYLTRANSFERASE INHIBITION BY BIX-01294.                   
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  16   312 2009              
JRNL        REFN                   ISSN 1545-9993                               
JRNL        PMID   19219047                                                     
JRNL        DOI    10.1038/NSMB.1560                                            
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 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) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.26                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 270243.590                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 86.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 24680                          
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) : 0.221                           
REMARK   3   FREE R VALUE                     : 0.262                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1201                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.008                           
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) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.49                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 42.90                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1183                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3980                       
REMARK   3   BIN FREE R VALUE                    : 0.4020                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.20                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 52                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.056                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4174                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 132                                     
REMARK   3   SOLVENT ATOMS            : 119                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 32.30                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 39.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 13.35000                                             
REMARK   3    B22 (A**2) : -13.97000                                            
REMARK   3    B33 (A**2) : 0.62000                                              
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) : 0.32                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.34                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 30.30                           
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.39                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.35                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.30                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.40                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.82                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.320 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.270 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.940 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.900 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.40                                                 
REMARK   3   BSOL        : 38.02                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  3  : WATER.PARAM                                    
REMARK   3  PARAMETER FILE  4  : 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   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3FPD COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-JAN-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB050875.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-AUG-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-BM                              
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 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26244                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.260                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.7                               
REMARK 200  DATA REDUNDANCY                : 4.400                              
REMARK 200  R MERGE                    (I) : 0.09700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.51                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.43000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
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: PDB ENTRY 2IGQ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.19                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.01                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES PH 7.5, 18-20 %              
REMARK 280  POLYETHYLENE GLYCOL 4000 AND 7-10 % ISOPROPANOL, IN THE             
REMARK 280  ABSENCE OR PRESENCE OF DMSO (6-36%), VAPOR DIFFUSION,               
REMARK 280  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       37.65000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       50.85000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       47.60000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       50.85000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       37.65000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       47.60000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2130 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24410 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 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     VAL B   975                                                      
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     LYS A1055    CG   CD   CE   NZ                                   
REMARK 470     ARG A1103    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A1138    CG   CD   OE1  OE2                                  
REMARK 470     ASP A1147    CG   OD1  OD2                                       
REMARK 470     ASN A1148    CG   OD1  ND2                                       
REMARK 470     LYS A1149    CG   CD   CE   NZ                                   
REMARK 470     GLU A1152    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 976    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 977    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     LYS B1221    CG   CD   CE   NZ                                   
REMARK 470     ARG B1226    CG   CD   NE   CZ   NH1  NH2                        
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      136.79   -178.05                                   
REMARK 500    ASP A 982      108.33    179.77                                   
REMARK 500    ALA A 997       30.10   -152.59                                   
REMARK 500    ASP A 999     -157.16   -140.47                                   
REMARK 500    SER A1005        6.00   -150.79                                   
REMARK 500    ASN A1006       45.92    -87.37                                   
REMARK 500    THR A1016      -81.06   -108.12                                   
REMARK 500    ASN A1020       46.65    -81.14                                   
REMARK 500    ASN A1024      105.32    -59.14                                   
REMARK 500    ASP A1035     -152.06   -113.33                                   
REMARK 500    MET A1049      -36.92     81.60                                   
REMARK 500    ARG A1050      157.37    175.82                                   
REMARK 500    GLU A1062       29.66    -77.34                                   
REMARK 500    GLU A1067       71.12   -154.91                                   
REMARK 500    ASN A1086       45.47    -83.24                                   
REMARK 500    VAL A1088      -60.56   -137.77                                   
REMARK 500    LEU A1146       55.33   -112.99                                   
REMARK 500    LYS A1149        5.48    -65.94                                   
REMARK 500    GLU A1152       92.59    -66.49                                   
REMARK 500    ASN A1163     -162.43   -101.75                                   
REMARK 500    MET A1183      -98.77   -126.55                                   
REMARK 500    PHE A1190       63.05   -117.02                                   
REMARK 500    CYS A1232      147.59    -39.26                                   
REMARK 500    HIS A1234       24.34   -142.78                                   
REMARK 500    ASP B 982      101.96   -172.63                                   
REMARK 500    PRO B 993      171.73    -56.40                                   
REMARK 500    VAL B 998      -94.53   -108.11                                   
REMARK 500    SER B1005       15.67   -159.79                                   
REMARK 500    THR B1016      -79.38   -105.22                                   
REMARK 500    ASP B1035     -150.56   -122.48                                   
REMARK 500    MET B1049      -45.55     77.43                                   
REMARK 500    GLU B1067       69.28   -159.25                                   
REMARK 500    ASN B1086       49.34    -86.96                                   
REMARK 500    VAL B1088      -62.86   -137.73                                   
REMARK 500    ASN B1148       66.13    150.40                                   
REMARK 500    LYS B1149      144.84    -33.82                                   
REMARK 500    ASP B1150       17.14    170.96                                   
REMARK 500    ASN B1163     -169.93   -113.73                                   
REMARK 500    MET B1183      -89.36   -132.38                                   
REMARK 500    ALA B1203      126.62    -39.81                                   
REMARK 500    ILE B1218      -72.49    -83.95                                   
REMARK 500    LYS B1219       -5.89    -59.57                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A   3  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1031   SG                                                     
REMARK 620 2 CYS A1033   SG  104.0                                              
REMARK 620 3 CYS A1037   SG  113.8 105.5                                        
REMARK 620 4 CYS A1042   SG  112.9 103.2 115.8                                  
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 A1044   SG  117.0                                              
REMARK 620 3 CYS A1074   SG  112.1 111.5                                        
REMARK 620 4 CYS A1078   SG  101.5  94.4 119.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A   2  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1037   SG                                                     
REMARK 620 2 CYS A1074   SG  112.9                                              
REMARK 620 3 CYS A1080   SG  118.0 103.4                                        
REMARK 620 4 CYS A1084   SG  107.3 100.9 112.9                                  
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 A1172   SG                                                     
REMARK 620 2 CYS A1225   SG  118.0                                              
REMARK 620 3 CYS A1227   SG  108.4 114.9                                        
REMARK 620 4 CYS A1232   SG   90.1 102.6 120.9                                  
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 B1031   SG                                                     
REMARK 620 2 CYS B1044   SG  115.3                                              
REMARK 620 3 CYS B1074   SG  114.1 109.8                                        
REMARK 620 4 CYS B1078   SG  103.1  87.0 125.0                                  
REMARK 620 N                    1     2     3                                   
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 B1033   SG  107.8                                              
REMARK 620 3 CYS B1037   SG  105.0 103.6                                        
REMARK 620 4 CYS B1042   SG  117.1 105.8 116.4                                  
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 B1037   SG                                                     
REMARK 620 2 CYS B1074   SG  110.1                                              
REMARK 620 3 CYS B1080   SG  103.1 113.4                                        
REMARK 620 4 CYS B1084   SG  107.3 104.2 118.5                                  
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 B1172   SG                                                     
REMARK 620 2 CYS B1225   SG  117.0                                              
REMARK 620 3 CYS B1227   SG  113.5 105.4                                        
REMARK 620 4 CYS B1232   SG   99.8 102.8 118.3                                  
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 SAH A 101                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE Q4A A 1                   
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A1236                  
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 2                    
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 3                    
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 4                    
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH B 102                 
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE Q4A B 2                   
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 5                    
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 6                    
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 7                    
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 8                    
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2RFI   RELATED DB: PDB                                   
REMARK 900 GLP IN COMPLEX WITH A H3 PEPTIDE SUBSTRATE                           
DBREF  3FPD A  975  1235  UNP    Q9H9B1   EHMT1_HUMAN    975   1235             
DBREF  3FPD B  975  1235  UNP    Q9H9B1   EHMT1_HUMAN    975   1235             
SEQRES   1 A  261  VAL GLU ARG ILE VAL SER ARG ASP ILE ALA ARG GLY TYR          
SEQRES   2 A  261  GLU ARG ILE PRO ILE PRO CYS VAL ASN ALA VAL ASP SER          
SEQRES   3 A  261  GLU PRO CYS PRO SER ASN TYR LYS TYR VAL SER GLN ASN          
SEQRES   4 A  261  CYS VAL THR SER PRO MET ASN ILE ASP ARG ASN ILE THR          
SEQRES   5 A  261  HIS LEU GLN TYR CYS VAL CYS ILE ASP ASP CYS SER SER          
SEQRES   6 A  261  SER ASN CYS MET CYS GLY GLN LEU SER MET ARG CYS TRP          
SEQRES   7 A  261  TYR ASP LYS ASP GLY ARG LEU LEU PRO GLU PHE ASN MET          
SEQRES   8 A  261  ALA GLU PRO PRO LEU ILE PHE GLU CYS ASN HIS ALA CYS          
SEQRES   9 A  261  SER CYS TRP ARG ASN CYS ARG ASN ARG VAL VAL GLN ASN          
SEQRES  10 A  261  GLY LEU ARG ALA ARG LEU GLN LEU TYR ARG THR ARG ASP          
SEQRES  11 A  261  MET GLY TRP GLY VAL ARG SER LEU GLN ASP ILE PRO PRO          
SEQRES  12 A  261  GLY THR PHE VAL CYS GLU TYR VAL GLY GLU LEU ILE SER          
SEQRES  13 A  261  ASP SER GLU ALA ASP VAL ARG GLU GLU ASP SER TYR LEU          
SEQRES  14 A  261  PHE ASP LEU ASP ASN LYS ASP GLY GLU VAL TYR CYS ILE          
SEQRES  15 A  261  ASP ALA ARG PHE TYR GLY ASN VAL SER ARG PHE ILE ASN          
SEQRES  16 A  261  HIS HIS CYS GLU PRO ASN LEU VAL PRO VAL ARG VAL PHE          
SEQRES  17 A  261  MET ALA HIS GLN ASP LEU ARG PHE PRO ARG ILE ALA PHE          
SEQRES  18 A  261  PHE SER THR ARG LEU ILE GLU ALA GLY GLU GLN LEU GLY          
SEQRES  19 A  261  PHE ASP TYR GLY GLU ARG PHE TRP ASP ILE LYS GLY LYS          
SEQRES  20 A  261  LEU PHE SER CYS ARG CYS GLY SER PRO LYS CYS ARG HIS          
SEQRES  21 A  261  SER                                                          
SEQRES   1 B  261  VAL GLU ARG ILE VAL SER ARG ASP ILE ALA ARG GLY TYR          
SEQRES   2 B  261  GLU ARG ILE PRO ILE PRO CYS VAL ASN ALA VAL ASP SER          
SEQRES   3 B  261  GLU PRO CYS PRO SER ASN TYR LYS TYR VAL SER GLN ASN          
SEQRES   4 B  261  CYS VAL THR SER PRO MET ASN ILE ASP ARG ASN ILE THR          
SEQRES   5 B  261  HIS LEU GLN TYR CYS VAL CYS ILE ASP ASP CYS SER SER          
SEQRES   6 B  261  SER ASN CYS MET CYS GLY GLN LEU SER MET ARG CYS TRP          
SEQRES   7 B  261  TYR ASP LYS ASP GLY ARG LEU LEU PRO GLU PHE ASN MET          
SEQRES   8 B  261  ALA GLU PRO PRO LEU ILE PHE GLU CYS ASN HIS ALA CYS          
SEQRES   9 B  261  SER CYS TRP ARG ASN CYS ARG ASN ARG VAL VAL GLN ASN          
SEQRES  10 B  261  GLY LEU ARG ALA ARG LEU GLN LEU TYR ARG THR ARG ASP          
SEQRES  11 B  261  MET GLY TRP GLY VAL ARG SER LEU GLN ASP ILE PRO PRO          
SEQRES  12 B  261  GLY THR PHE VAL CYS GLU TYR VAL GLY GLU LEU ILE SER          
SEQRES  13 B  261  ASP SER GLU ALA ASP VAL ARG GLU GLU ASP SER TYR LEU          
SEQRES  14 B  261  PHE ASP LEU ASP ASN LYS ASP GLY GLU VAL TYR CYS ILE          
SEQRES  15 B  261  ASP ALA ARG PHE TYR GLY ASN VAL SER ARG PHE ILE ASN          
SEQRES  16 B  261  HIS HIS CYS GLU PRO ASN LEU VAL PRO VAL ARG VAL PHE          
SEQRES  17 B  261  MET ALA HIS GLN ASP LEU ARG PHE PRO ARG ILE ALA PHE          
SEQRES  18 B  261  PHE SER THR ARG LEU ILE GLU ALA GLY GLU GLN LEU GLY          
SEQRES  19 B  261  PHE ASP TYR GLY GLU ARG PHE TRP ASP ILE LYS GLY LYS          
SEQRES  20 B  261  LEU PHE SER CYS ARG CYS GLY SER PRO LYS CYS ARG HIS          
SEQRES  21 B  261  SER                                                          
HET    SAH  A 101      26                                                       
HET    Q4A  A   1      36                                                       
HET     ZN  A1236       1                                                       
HET     ZN  A   2       1                                                       
HET     ZN  A   3       1                                                       
HET     ZN  A   4       1                                                       
HET    SAH  B 102      26                                                       
HET    Q4A  B   2      36                                                       
HET     ZN  B   5       1                                                       
HET     ZN  B   6       1                                                       
HET     ZN  B   7       1                                                       
HET     ZN  B   8       1                                                       
HETNAM     SAH S-ADENOSYL-L-HOMOCYSTEINE                                        
HETNAM     Q4A N-(1-BENZYLPIPERIDIN-4-YL)-6,7-DIMETHOXY-2-(4-METHYL-            
HETNAM   2 Q4A  1,4-DIAZEPAN-1-YL)QUINAZOLIN-4-AMINE                            
HETNAM      ZN ZINC ION                                                         
FORMUL   3  SAH    2(C14 H20 N6 O5 S)                                           
FORMUL   4  Q4A    2(C28 H38 N6 O2)                                             
FORMUL   5   ZN    8(ZN 2+)                                                     
FORMUL  15  HOH   *119(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  GLY A 1220  1                                   9    
HELIX    6   6 ASN B 1024  LEU B 1028  5                                   5    
HELIX    7   7 CYS B 1042  SER B 1048  1                                   7    
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 VAL B 1164  ILE B 1168  5                                   5    
HELIX   11  11 TYR B 1211  GLY B 1220  1                                  10    
SHEET    1   A 4 ARG A 977  SER A 980  0                                        
SHEET    2   A 4 CYS A 994  ASN A 996 -1  O  ASN A 996   N  ARG A 977           
SHEET    3   A 4 LEU A1097  ARG A1101  1  O  LEU A1099   N  VAL A 995           
SHEET    4   A 4 TRP A1107  SER A1111 -1  O  GLY A1108   N  TYR A1100           
SHEET    1   B 4 LYS A1008  TYR A1009  0                                        
SHEET    2   B 4 TYR A1154  GLY A1162  1  O  PHE A1160   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 TYR A1154  GLY A1162  1  O  PHE A1160   N  LYS A1008           
SHEET    3   C 3 LEU A1143  LEU A1146 -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  ARG A1180   N  ILE A1071           
SHEET    3   D 4 ARG A1192  SER A1197 -1  O  ALA A1194   N  VAL A1179           
SHEET    4   D 4 PHE A1120  TYR A1124 -1  N  CYS A1122   O  PHE A1195           
SHEET    1   E 4 ARG B 977  SER B 980  0                                        
SHEET    2   E 4 CYS B 994  ASN B 996 -1  O  ASN B 996   N  ARG B 977           
SHEET    3   E 4 LEU B1097  ARG B1101  1  O  LEU B1099   N  VAL B 995           
SHEET    4   E 4 TRP B1107  SER B1111 -1  O  GLY B1108   N  TYR B1100           
SHEET    1   F 3 LYS B1008  TYR B1009  0                                        
SHEET    2   F 3 TYR B1154  GLY B1162  1  O  PHE B1160   N  LYS B1008           
SHEET    3   F 3 GLY B1126  SER B1130 -1  N  GLU B1127   O  ASP B1157           
SHEET    1   G 3 LYS B1008  TYR B1009  0                                        
SHEET    2   G 3 TYR B1154  GLY B1162  1  O  PHE B1160   N  LYS B1008           
SHEET    3   G 3 LEU B1143  LEU B1146 -1  N  LEU B1146   O  TYR B1154           
SHEET    1   H 4 ILE B1071  PHE B1072  0                                        
SHEET    2   H 4 LEU B1176  PHE B1182  1  O  ARG B1180   N  ILE B1071           
SHEET    3   H 4 ARG B1192  SER B1197 -1  O  ALA B1194   N  VAL B1179           
SHEET    4   H 4 PHE B1120  GLU B1123 -1  N  CYS B1122   O  PHE B1195           
SHEET    1   I 2 ASN B1169  HIS B1170  0                                        
SHEET    2   I 2 GLY B1208  PHE B1209  1  O  PHE B1209   N  ASN B1169           
LINK         SG  CYS A1031                ZN    ZN A   3     1555   1555  2.45  
LINK         SG  CYS A1031                ZN    ZN A1236     1555   1555  2.45  
LINK         SG  CYS A1033                ZN    ZN A   3     1555   1555  2.50  
LINK         SG  CYS A1037                ZN    ZN A   3     1555   1555  2.40  
LINK         SG  CYS A1037                ZN    ZN A   2     1555   1555  2.33  
LINK         SG  CYS A1042                ZN    ZN A   3     1555   1555  2.52  
LINK         SG  CYS A1044                ZN    ZN A1236     1555   1555  2.46  
LINK         SG  CYS A1074                ZN    ZN A   2     1555   1555  2.31  
LINK         SG  CYS A1074                ZN    ZN A1236     1555   1555  2.38  
LINK         SG  CYS A1078                ZN    ZN A1236     1555   1555  2.48  
LINK         SG  CYS A1080                ZN    ZN A   2     1555   1555  2.40  
LINK         SG  CYS A1084                ZN    ZN A   2     1555   1555  2.35  
LINK         SG  CYS A1172                ZN    ZN A   4     1555   1555  2.67  
LINK         SG  CYS A1225                ZN    ZN A   4     1555   1555  2.44  
LINK         SG  CYS A1227                ZN    ZN A   4     1555   1555  2.70  
LINK         SG  CYS A1232                ZN    ZN A   4     1555   1555  2.71  
LINK         SG  CYS B1031                ZN    ZN B   5     1555   1555  2.38  
LINK         SG  CYS B1031                ZN    ZN B   7     1555   1555  2.36  
LINK         SG  CYS B1033                ZN    ZN B   7     1555   1555  2.48  
LINK         SG  CYS B1037                ZN    ZN B   6     1555   1555  2.43  
LINK         SG  CYS B1037                ZN    ZN B   7     1555   1555  2.47  
LINK         SG  CYS B1042                ZN    ZN B   7     1555   1555  2.40  
LINK         SG  CYS B1044                ZN    ZN B   5     1555   1555  2.46  
LINK         SG  CYS B1074                ZN    ZN B   6     1555   1555  2.38  
LINK         SG  CYS B1074                ZN    ZN B   5     1555   1555  2.36  
LINK         SG  CYS B1078                ZN    ZN B   5     1555   1555  2.41  
LINK         SG  CYS B1080                ZN    ZN B   6     1555   1555  2.27  
LINK         SG  CYS B1084                ZN    ZN B   6     1555   1555  2.36  
LINK         SG  CYS B1172                ZN    ZN B   8     1555   1555  2.33  
LINK         SG  CYS B1225                ZN    ZN B   8     1555   1555  2.42  
LINK         SG  CYS B1227                ZN    ZN B   8     1555   1555  2.39  
LINK         SG  CYS B1232                ZN    ZN B   8     1555   1555  2.65  
SITE     1 AC1 10 MET A1105  TRP A1107  SER A1141  TYR A1142                    
SITE     2 AC1 10 ARG A1166  ASN A1169  HIS A1170  TYR A1211                    
SITE     3 AC1 10 CYS A1225  ARG A1226                                          
SITE     1 AC2 10 ASP A1131  ALA A1134  ASP A1135  ARG A1137                    
SITE     2 AC2 10 ASP A1140  LEU A1143  ASP A1145  CYS A1155                    
SITE     3 AC2 10 ARG A1214  PHE A1215                                          
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 13 MET B1105  GLY B1106  TRP B1107  SER B1141                    
SITE     2 AC7 13 TYR B1142  ARG B1166  ASN B1169  HIS B1170                    
SITE     3 AC7 13 TYR B1211  PHE B1215  PHE B1223  CYS B1225                    
SITE     4 AC7 13 ARG B1226                                                     
SITE     1 AC8 13 ASP B1131  ALA B1134  ASP B1135  VAL B1136                    
SITE     2 AC8 13 ARG B1137  GLU B1138  ASP B1140  LEU B1143                    
SITE     3 AC8 13 ASP B1145  CYS B1155  ARG B1214  PHE B1215                    
SITE     4 AC8 13 LYS B1219                                                     
SITE     1 AC9  6  ZN B   6   ZN B   7  CYS B1031  CYS B1044                    
SITE     2 AC9  6 CYS B1074  CYS B1078                                          
SITE     1 BC1  5  ZN B   5  CYS B1037  CYS B1074  CYS B1080                    
SITE     2 BC1  5 CYS B1084                                                     
SITE     1 BC2  5  ZN B   5  CYS B1031  CYS B1033  CYS B1037                    
SITE     2 BC2  5 CYS B1042                                                     
SITE     1 BC3  4 CYS B1172  CYS B1225  CYS B1227  CYS B1232                    
CRYST1   75.300   95.200  101.700  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      0.013280  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010504  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009833        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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