GenomeNet

Database: PDB
Entry: 3PTA
LinkDB: 3PTA
Original site: 3PTA 
HEADER    TRANSFERASE/DNA                         02-DEC-10   3PTA              
TITLE     CRYSTAL STRUCTURE OF HUMAN DNMT1(646-1600) IN COMPLEX WITH DNA        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DNA (CYTOSINE-5)-METHYLTRANSFERASE 1;                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 646-1600;                                     
COMPND   5 SYNONYM: DNMT1, CXXC-TYPE ZINC FINGER PROTEIN 9, DNA                 
COMPND   6 METHYLTRANSFERASE HSAI, DNA MTASE HSAI, M.HSAI, MCMT;                
COMPND   7 EC: 2.1.1.37;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: DNA (5'-                                                   
COMPND  11 D(*TP*CP*CP*CP*GP*TP*GP*AP*GP*CP*CP*TP*CP*CP*GP*CP*AP*GP*G)-3');     
COMPND  12 CHAIN: B;                                                            
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MOL_ID: 3;                                                           
COMPND  15 MOLECULE: DNA (5'-                                                   
COMPND  16 D(*CP*CP*TP*GP*CP*GP*GP*AP*GP*GP*CP*TP*CP*AP*CP*GP*GP*GP*A)-3');     
COMPND  17 CHAIN: C;                                                            
COMPND  18 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: DNMT1, AIM, CXXC9, DNMT;                                       
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: C41(DE3);                                  
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 SYNTHETIC: YES;                                                      
SOURCE  11 MOL_ID: 3;                                                           
SOURCE  12 SYNTHETIC: YES                                                       
KEYWDS    DNMT1, MAINTENANCE DNA METHYLATION, TRANSFERASE-DNA COMPLEX           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.SONG,D.J.PATEL                                                      
REVDAT   2   30-MAR-11 3PTA    1       JRNL   SOURCE                            
REVDAT   1   29-DEC-10 3PTA    0                                                
JRNL        AUTH   J.SONG,O.RECHKOBLIT,T.H.BESTOR,D.J.PATEL                     
JRNL        TITL   STRUCTURE OF DNMT1-DNA COMPLEX REVEALS A ROLE FOR            
JRNL        TITL 2 AUTOINHIBITION IN MAINTENANCE DNA METHYLATION.               
JRNL        REF    SCIENCE                       V. 331  1036 2011              
JRNL        REFN                   ISSN 0036-8075                               
JRNL        PMID   21163962                                                     
JRNL        DOI    10.1126/SCIENCE.1195380                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
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 : MLF                                             
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 18554                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.257                           
REMARK   3   FREE R VALUE                     : 0.291                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 954                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7186                                    
REMARK   3   NUCLEIC ACID ATOMS       : 773                                     
REMARK   3   HETEROGEN ATOMS          : 30                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.02                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3PTA COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-DEC-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB062789.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-MAR-09                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.2827                             
REMARK 200  MONOCHROMATOR                  : SI MIRRORS                         
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19075                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -0.500                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 7.200                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.10100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.73                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.40                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.50800                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.800                              
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63.58                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.38                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 6% PEG 20,000, 0.1M MES, PH 6.5, VAPOR   
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 292K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       81.40000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       43.95000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       81.40000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       43.95000            
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3330 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 47810 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 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     SER A   645                                                      
REMARK 465     ASN A   646                                                      
REMARK 465     GLU A   852                                                      
REMARK 465     SER A   853                                                      
REMARK 465     LEU A   854                                                      
REMARK 465     LEU A   855                                                      
REMARK 465     GLU A   856                                                      
REMARK 465     GLY A   857                                                      
REMARK 465     ASP A   858                                                      
REMARK 465     ASP A   859                                                      
REMARK 465     VAL A   956                                                      
REMARK 465     LYS A   957                                                      
REMARK 465     ARG A   958                                                      
REMARK 465     PRO A   959                                                      
REMARK 465     ARG A   960                                                      
REMARK 465     ASP A   978                                                      
REMARK 465     TYR A   979                                                      
REMARK 465     ILE A   980                                                      
REMARK 465     LYS A   981                                                      
REMARK 465     GLY A   982                                                      
REMARK 465     SER A   983                                                      
REMARK 465     ASN A  1108                                                      
REMARK 465     LYS A  1109                                                      
REMARK 465     GLY A  1110                                                      
REMARK 465     LYS A  1111                                                      
REMARK 465     GLY A  1112                                                      
REMARK 465     LYS A  1113                                                      
REMARK 465     GLY A  1114                                                      
REMARK 465     LYS A  1115                                                      
REMARK 465     GLY A  1116                                                      
REMARK 465     LYS A  1117                                                      
REMARK 465     GLY A  1118                                                      
REMARK 465     LYS A  1119                                                      
REMARK 465     PRO A  1120                                                      
REMARK 465     LYS A  1121                                                      
REMARK 465     SER A  1122                                                      
REMARK 465     GLN A  1123                                                      
REMARK 465     ALA A  1124                                                      
REMARK 465     CYS A  1125                                                      
REMARK 465     GLU A  1126                                                      
REMARK 465     PRO A  1127                                                      
REMARK 465     SER A  1128                                                      
REMARK 465     GLU A  1129                                                      
REMARK 465     PRO A  1130                                                      
REMARK 465     GLU A  1131                                                      
REMARK 465     ILE A  1132                                                      
REMARK 465     GLU A  1133                                                      
REMARK 465     ILE A  1134                                                      
REMARK 465     GLU A  1480                                                      
REMARK 465     ALA A  1481                                                      
REMARK 465     GLY A  1482                                                      
REMARK 465     LYS A  1483                                                      
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 A1407   C   -  N   -  CA  ANGL. DEV. =  12.0 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    VAL A 655      -70.40   -111.92                                   
REMARK 500    CYS A 656      153.57    -35.68                                   
REMARK 500    CYS A 664      -88.78    -44.02                                   
REMARK 500    LYS A 668      -71.06    -49.69                                   
REMARK 500    ARG A 681        1.22    -69.75                                   
REMARK 500    LYS A 683       78.65     56.17                                   
REMARK 500    ARG A 690       98.74    -54.08                                   
REMARK 500    ASP A 700     -151.96   -105.19                                   
REMARK 500    GLU A 703       92.88     -6.19                                   
REMARK 500    ASN A 708     -168.65    -73.35                                   
REMARK 500    GLU A 711      115.90    -35.87                                   
REMARK 500    MET A 712      142.55   -175.58                                   
REMARK 500    PRO A 715     -110.06    -66.54                                   
REMARK 500    LYS A 717      -25.17    -33.42                                   
REMARK 500    GLN A 720     -170.20     69.23                                   
REMARK 500    LYS A 722       77.73     51.26                                   
REMARK 500    ASP A 741     -121.12    -87.74                                   
REMARK 500    LYS A 749     -168.70   -127.02                                   
REMARK 500    ALA A 754      -25.69     81.21                                   
REMARK 500    PRO A 767     -161.97    -65.38                                   
REMARK 500    SER A 770        6.98    -65.47                                   
REMARK 500    SER A 787      -31.09   -156.49                                   
REMARK 500    ASP A 818       48.65    -75.94                                   
REMARK 500    LEU A 825      -45.84    -15.84                                   
REMARK 500    SER A 826       -9.57    -54.31                                   
REMARK 500    ASN A 842       66.95   -105.03                                   
REMARK 500    ALA A 844       20.46    -58.06                                   
REMARK 500    LYS A 861      -17.07   -140.80                                   
REMARK 500    GLN A 866      -15.49   -148.91                                   
REMARK 500    THR A 885     -160.00   -115.20                                   
REMARK 500    ASN A 888        0.51   -167.83                                   
REMARK 500    LYS A 891       29.85   -140.60                                   
REMARK 500    SER A 895      -72.32    -52.87                                   
REMARK 500    GLU A 906      -70.28    -69.65                                   
REMARK 500    LEU A 911     -129.50   -120.84                                   
REMARK 500    LEU A 914      -42.31   -131.23                                   
REMARK 500    ASN A 929       34.95     35.15                                   
REMARK 500    LYS A 951      104.05    -38.88                                   
REMARK 500    LEU A 952      116.72    -39.27                                   
REMARK 500    GLU A 962      156.41    -48.80                                   
REMARK 500    ASP A 965       97.93    -50.54                                   
REMARK 500    TYR A 969       76.28   -113.61                                   
REMARK 500    PRO A 970      -74.97    -51.67                                   
REMARK 500    GLU A 971        3.88    -61.88                                   
REMARK 500    TYR A 976      -73.11    -64.41                                   
REMARK 500    PRO A 990      177.36    -59.63                                   
REMARK 500    PRO A1002     -177.54    -57.13                                   
REMARK 500    SER A1005      115.86    -24.92                                   
REMARK 500    ASN A1006      -38.69    122.00                                   
REMARK 500    ASN A1010      112.21   -177.12                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      92 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR A1405         0.09    SIDE CHAIN                              
REMARK 500     DC C  21         0.07    SIDE CHAIN                              
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   1  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A1502   NE2                                                    
REMARK 620 2 CYS A1476   SG  125.7                                              
REMARK 620 3 CYS A1478   SG   91.8  92.7                                        
REMARK 620 4 CYS A1485   SG  108.4 124.0  99.6                                  
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 A 656   SG                                                     
REMARK 620 2 CYS A 653   SG   95.1                                              
REMARK 620 3 CYS A 691   SG  129.0 112.3                                        
REMARK 620 4 CYS A 659   SG   96.4 131.2  96.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A   5  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 667   SG                                                     
REMARK 620 2 CYS A 686   SG  137.9                                              
REMARK 620 N                    1                                               
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 HIS A 793   NE2                                                    
REMARK 620 2 CYS A 896   SG  105.4                                              
REMARK 620 3 CYS A 820   SG   96.7 116.9                                        
REMARK 620 4 CYS A 893   SG  128.9  95.2 114.9                                  
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 1601                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 2                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 3                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 5                    
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3PT6   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3PT9   RELATED DB: PDB                                   
DBREF  3PTA A  646  1600  UNP    P26358   DNMT1_HUMAN    646   1600             
DBREF  3PTA B    1    19  PDB    3PTA     3PTA             1     19             
DBREF  3PTA C   20    38  PDB    3PTA     3PTA            20     38             
SEQADV 3PTA SER A  645  UNP  P26358              EXPRESSION TAG                 
SEQRES   1 A  956  SER ASN ALA PHE LYS ARG ARG ARG CYS GLY VAL CYS GLU          
SEQRES   2 A  956  VAL CYS GLN GLN PRO GLU CYS GLY LYS CYS LYS ALA CYS          
SEQRES   3 A  956  LYS ASP MET VAL LYS PHE GLY GLY SER GLY ARG SER LYS          
SEQRES   4 A  956  GLN ALA CYS GLN GLU ARG ARG CYS PRO ASN MET ALA MET          
SEQRES   5 A  956  LYS GLU ALA ASP ASP ASP GLU GLU VAL ASP ASP ASN ILE          
SEQRES   6 A  956  PRO GLU MET PRO SER PRO LYS LYS MET HIS GLN GLY LYS          
SEQRES   7 A  956  LYS LYS LYS GLN ASN LYS ASN ARG ILE SER TRP VAL GLY          
SEQRES   8 A  956  GLU ALA VAL LYS THR ASP GLY LYS LYS SER TYR TYR LYS          
SEQRES   9 A  956  LYS VAL CYS ILE ASP ALA GLU THR LEU GLU VAL GLY ASP          
SEQRES  10 A  956  CYS VAL SER VAL ILE PRO ASP ASP SER SER LYS PRO LEU          
SEQRES  11 A  956  TYR LEU ALA ARG VAL THR ALA LEU TRP GLU ASP SER SER          
SEQRES  12 A  956  ASN GLY GLN MET PHE HIS ALA HIS TRP PHE CYS ALA GLY          
SEQRES  13 A  956  THR ASP THR VAL LEU GLY ALA THR SER ASP PRO LEU GLU          
SEQRES  14 A  956  LEU PHE LEU VAL ASP GLU CYS GLU ASP MET GLN LEU SER          
SEQRES  15 A  956  TYR ILE HIS SER LYS VAL LYS VAL ILE TYR LYS ALA PRO          
SEQRES  16 A  956  SER GLU ASN TRP ALA MET GLU GLY GLY MET ASP PRO GLU          
SEQRES  17 A  956  SER LEU LEU GLU GLY ASP ASP GLY LYS THR TYR PHE TYR          
SEQRES  18 A  956  GLN LEU TRP TYR ASP GLN ASP TYR ALA ARG PHE GLU SER          
SEQRES  19 A  956  PRO PRO LYS THR GLN PRO THR GLU ASP ASN LYS PHE LYS          
SEQRES  20 A  956  PHE CYS VAL SER CYS ALA ARG LEU ALA GLU MET ARG GLN          
SEQRES  21 A  956  LYS GLU ILE PRO ARG VAL LEU GLU GLN LEU GLU ASP LEU          
SEQRES  22 A  956  ASP SER ARG VAL LEU TYR TYR SER ALA THR LYS ASN GLY          
SEQRES  23 A  956  ILE LEU TYR ARG VAL GLY ASP GLY VAL TYR LEU PRO PRO          
SEQRES  24 A  956  GLU ALA PHE THR PHE ASN ILE LYS LEU SER SER PRO VAL          
SEQRES  25 A  956  LYS ARG PRO ARG LYS GLU PRO VAL ASP GLU ASP LEU TYR          
SEQRES  26 A  956  PRO GLU HIS TYR ARG LYS TYR SER ASP TYR ILE LYS GLY          
SEQRES  27 A  956  SER ASN LEU ASP ALA PRO GLU PRO TYR ARG ILE GLY ARG          
SEQRES  28 A  956  ILE LYS GLU ILE PHE CYS PRO LYS LYS SER ASN GLY ARG          
SEQRES  29 A  956  PRO ASN GLU THR ASP ILE LYS ILE ARG VAL ASN LYS PHE          
SEQRES  30 A  956  TYR ARG PRO GLU ASN THR HIS LYS SER THR PRO ALA SER          
SEQRES  31 A  956  TYR HIS ALA ASP ILE ASN LEU LEU TYR TRP SER ASP GLU          
SEQRES  32 A  956  GLU ALA VAL VAL ASP PHE LYS ALA VAL GLN GLY ARG CYS          
SEQRES  33 A  956  THR VAL GLU TYR GLY GLU ASP LEU PRO GLU CYS VAL GLN          
SEQRES  34 A  956  VAL TYR SER MET GLY GLY PRO ASN ARG PHE TYR PHE LEU          
SEQRES  35 A  956  GLU ALA TYR ASN ALA LYS SER LYS SER PHE GLU ASP PRO          
SEQRES  36 A  956  PRO ASN HIS ALA ARG SER PRO GLY ASN LYS GLY LYS GLY          
SEQRES  37 A  956  LYS GLY LYS GLY LYS GLY LYS PRO LYS SER GLN ALA CYS          
SEQRES  38 A  956  GLU PRO SER GLU PRO GLU ILE GLU ILE LYS LEU PRO LYS          
SEQRES  39 A  956  LEU ARG THR LEU ASP VAL PHE SER GLY CYS GLY GLY LEU          
SEQRES  40 A  956  SER GLU GLY PHE HIS GLN ALA GLY ILE SER ASP THR LEU          
SEQRES  41 A  956  TRP ALA ILE GLU MET TRP ASP PRO ALA ALA GLN ALA PHE          
SEQRES  42 A  956  ARG LEU ASN ASN PRO GLY SER THR VAL PHE THR GLU ASP          
SEQRES  43 A  956  CYS ASN ILE LEU LEU LYS LEU VAL MET ALA GLY GLU THR          
SEQRES  44 A  956  THR ASN SER ARG GLY GLN ARG LEU PRO GLN LYS GLY ASP          
SEQRES  45 A  956  VAL GLU MET LEU CYS GLY GLY PRO PRO CYS GLN GLY PHE          
SEQRES  46 A  956  SER GLY MET ASN ARG PHE ASN SER ARG THR TYR SER LYS          
SEQRES  47 A  956  PHE LYS ASN SER LEU VAL VAL SER PHE LEU SER TYR CYS          
SEQRES  48 A  956  ASP TYR TYR ARG PRO ARG PHE PHE LEU LEU GLU ASN VAL          
SEQRES  49 A  956  ARG ASN PHE VAL SER PHE LYS ARG SER MET VAL LEU LYS          
SEQRES  50 A  956  LEU THR LEU ARG CYS LEU VAL ARG MET GLY TYR GLN CYS          
SEQRES  51 A  956  THR PHE GLY VAL LEU GLN ALA GLY GLN TYR GLY VAL ALA          
SEQRES  52 A  956  GLN THR ARG ARG ARG ALA ILE ILE LEU ALA ALA ALA PRO          
SEQRES  53 A  956  GLY GLU LYS LEU PRO LEU PHE PRO GLU PRO LEU HIS VAL          
SEQRES  54 A  956  PHE ALA PRO ARG ALA CYS GLN LEU SER VAL VAL VAL ASP          
SEQRES  55 A  956  ASP LYS LYS PHE VAL SER ASN ILE THR ARG LEU SER SER          
SEQRES  56 A  956  GLY PRO PHE ARG THR ILE THR VAL ARG ASP THR MET SER          
SEQRES  57 A  956  ASP LEU PRO GLU VAL ARG ASN GLY ALA SER ALA LEU GLU          
SEQRES  58 A  956  ILE SER TYR ASN GLY GLU PRO GLN SER TRP PHE GLN ARG          
SEQRES  59 A  956  GLN LEU ARG GLY ALA GLN TYR GLN PRO ILE LEU ARG ASP          
SEQRES  60 A  956  HIS ILE CYS LYS ASP MET SER ALA LEU VAL ALA ALA ARG          
SEQRES  61 A  956  MET ARG HIS ILE PRO LEU ALA PRO GLY SER ASP TRP ARG          
SEQRES  62 A  956  ASP LEU PRO ASN ILE GLU VAL ARG LEU SER ASP GLY THR          
SEQRES  63 A  956  MET ALA ARG LYS LEU ARG TYR THR HIS HIS ASP ARG LYS          
SEQRES  64 A  956  ASN GLY ARG SER SER SER GLY ALA LEU ARG GLY VAL CYS          
SEQRES  65 A  956  SER CYS VAL GLU ALA GLY LYS ALA CYS ASP PRO ALA ALA          
SEQRES  66 A  956  ARG GLN PHE ASN THR LEU ILE PRO TRP CYS LEU PRO HIS          
SEQRES  67 A  956  THR GLY ASN ARG HIS ASN HIS TRP ALA GLY LEU TYR GLY          
SEQRES  68 A  956  ARG LEU GLU TRP ASP GLY PHE PHE SER THR THR VAL THR          
SEQRES  69 A  956  ASN PRO GLU PRO MET GLY LYS GLN GLY ARG VAL LEU HIS          
SEQRES  70 A  956  PRO GLU GLN HIS ARG VAL VAL SER VAL ARG GLU CYS ALA          
SEQRES  71 A  956  ARG SER GLN GLY PHE PRO ASP THR TYR ARG LEU PHE GLY          
SEQRES  72 A  956  ASN ILE LEU ASP LYS HIS ARG GLN VAL GLY ASN ALA VAL          
SEQRES  73 A  956  PRO PRO PRO LEU ALA LYS ALA ILE GLY LEU GLU ILE LYS          
SEQRES  74 A  956  LEU CYS MET LEU ALA LYS ALA                                  
SEQRES   1 B   19   DT  DC  DC  DC  DG  DT  DG  DA  DG  DC  DC  DT  DC          
SEQRES   2 B   19   DC  DG  DC  DA  DG  DG                                      
SEQRES   1 C   19   DC  DC  DT  DG  DC  DG  DG  DA  DG  DG  DC  DT  DC          
SEQRES   2 C   19   DA  DC  DG  DG  DG  DA                                      
HET    SAH  A1601      26                                                       
HET     ZN  A   1       1                                                       
HET     ZN  A   2       1                                                       
HET     ZN  A   3       1                                                       
HET     ZN  A   5       1                                                       
HETNAM     SAH S-ADENOSYL-L-HOMOCYSTEINE                                        
HETNAM      ZN ZINC ION                                                         
FORMUL   4  SAH    C14 H20 N6 O5 S                                              
FORMUL   5   ZN    4(ZN 2+)                                                     
HELIX    1   1 CYS A  656  GLN A  661  1                                   6    
HELIX    2   2 CYS A  667  ASP A  672  1                                   6    
HELIX    3   3 MET A  673  GLY A  677  5                                   5    
HELIX    4   4 THR A  801  THR A  803  5                                   3    
HELIX    5   5 CYS A  893  ILE A  907  1                                  15    
HELIX    6   6 TYR A  969  LYS A  975  5                                   7    
HELIX    7   7 ARG A 1023  THR A 1027  5                                   5    
HELIX    8   8 SER A 1030  HIS A 1036  5                                   7    
HELIX    9   9 LYS A 1054  VAL A 1056  5                                   3    
HELIX   10  10 CYS A 1071  GLY A 1078  1                                   8    
HELIX   11  11 PRO A 1100  ARG A 1104  5                                   5    
HELIX   12  12 GLY A 1149  GLY A 1159  1                                  11    
HELIX   13  13 TRP A 1170  ASN A 1181  1                                  12    
HELIX   14  14 ASP A 1190  MET A 1199  1                                  10    
HELIX   15  15 ASN A 1236  LYS A 1244  1                                   9    
HELIX   16  16 VAL A 1248  CYS A 1255  1                                   8    
HELIX   17  17 ASN A 1270  ARG A 1276  5                                   7    
HELIX   18  18 SER A 1277  MET A 1290  1                                  14    
HELIX   19  19 GLY A 1302  GLY A 1305  5                                   4    
HELIX   20  20 ALA A 1335  CYS A 1339  5                                   5    
HELIX   21  21 THR A 1366  MET A 1371  1                                   6    
HELIX   22  22 SER A 1394  ARG A 1401  1                                   8    
HELIX   23  23 SER A 1418  HIS A 1427  1                                  10    
HELIX   24  24 ASP A 1435  LEU A 1439  5                                   5    
HELIX   25  25 ASP A 1486  ARG A 1490  5                                   5    
HELIX   26  26 TRP A 1498  ASN A 1505  1                                   8    
HELIX   27  27 ARG A 1506  ALA A 1511  5                                   6    
HELIX   28  28 SER A 1549  GLN A 1557  1                                   9    
HELIX   29  29 ASN A 1568  ALA A 1579  1                                  12    
HELIX   30  30 PRO A 1581  LEU A 1597  1                                  17    
SHEET    1   A 3 ILE A 731  VAL A 734  0                                        
SHEET    2   A 3 LYS A 749  ILE A 752 -1  O  CYS A 751   N  SER A 732           
SHEET    3   A 3 GLU A 755  GLU A 758 -1  O  GLU A 755   N  ILE A 752           
SHEET    1   B 7 ILE A 828  VAL A 832  0                                        
SHEET    2   B 7 CYS A 762  VAL A 765 -1  N  SER A 764   O  HIS A 829           
SHEET    3   B 7 TYR A 775  GLU A 784 -1  O  TYR A 775   N  VAL A 765           
SHEET    4   B 7 GLN A 790  ALA A 799 -1  O  HIS A 793   N  THR A 780           
SHEET    5   B 7 GLU A 813  GLN A 824 -1  O  PHE A 815   N  CYS A 798           
SHEET    6   B 7 PHE A 864  ASP A 870  1  O  TYR A 869   N  LEU A 816           
SHEET    7   B 7 ILE A 835  TYR A 836  1  N  ILE A 835   O  TYR A 865           
SHEET    1   C 7 ILE A 828  VAL A 832  0                                        
SHEET    2   C 7 CYS A 762  VAL A 765 -1  N  SER A 764   O  HIS A 829           
SHEET    3   C 7 TYR A 775  GLU A 784 -1  O  TYR A 775   N  VAL A 765           
SHEET    4   C 7 GLN A 790  ALA A 799 -1  O  HIS A 793   N  THR A 780           
SHEET    5   C 7 GLU A 813  GLN A 824 -1  O  PHE A 815   N  CYS A 798           
SHEET    6   C 7 PHE A 864  ASP A 870  1  O  TYR A 869   N  LEU A 816           
SHEET    7   C 7 ARG A 875  GLU A 877 -1  O  GLU A 877   N  TRP A 868           
SHEET    1   D 3 ARG A 909  VAL A 910  0                                        
SHEET    2   D 3 SER A 925  LYS A 928 -1  O  THR A 927   N  ARG A 909           
SHEET    3   D 3 ILE A 931  ARG A 934 -1  O  ILE A 931   N  LYS A 928           
SHEET    1   E 7 GLN A 913  LEU A 917  0                                        
SHEET    2   E 7 ARG A 920  TYR A 923 -1  O  LEU A 922   N  LEU A 914           
SHEET    3   E 7 ARG A 992  PRO A1002 -1  O  ILE A 999   N  TYR A 923           
SHEET    4   E 7 GLY A 938  LEU A 941 -1  N  LEU A 941   O  ARG A 992           
SHEET    5   E 7 ARG A1059  TYR A1064 -1  O  CYS A1060   N  GLY A 938           
SHEET    6   E 7 ARG A1082  ASN A1090  1  O  PHE A1083   N  THR A1061           
SHEET    7   E 7 SER A1095  GLU A1097 -1  O  SER A1095   N  ASN A1090           
SHEET    1   F 7 GLN A 913  LEU A 917  0                                        
SHEET    2   F 7 ARG A 920  TYR A 923 -1  O  LEU A 922   N  LEU A 914           
SHEET    3   F 7 ARG A 992  PRO A1002 -1  O  ILE A 999   N  TYR A 923           
SHEET    4   F 7 LYS A1015  TYR A1022 -1  O  ARG A1017   N  LYS A 997           
SHEET    5   F 7 LEU A1041  ASP A1052 -1  O  TYR A1043   N  TYR A1022           
SHEET    6   F 7 ARG A1082  ASN A1090  1  O  TYR A1089   N  TRP A1044           
SHEET    7   F 7 SER A1095  GLU A1097 -1  O  SER A1095   N  ASN A1090           
SHEET    1   G 7 THR A1185  PHE A1187  0                                        
SHEET    2   G 7 SER A1161  ILE A1167  1  N  ALA A1166   O  PHE A1187           
SHEET    3   G 7 LEU A1139  VAL A1144  1  N  THR A1141   O  LEU A1164           
SHEET    4   G 7 MET A1219  GLY A1222  1  O  MET A1219   N  LEU A1142           
SHEET    5   G 7 PHE A1262  VAL A1268  1  O  PHE A1262   N  LEU A1220           
SHEET    6   G 7 ARG A1311  ALA A1318 -1  O  ALA A1313   N  ASN A1267           
SHEET    7   G 7 GLN A1293  GLN A1300 -1  N  GLN A1293   O  ALA A1318           
SHEET    1   H 2 VAL A1343  VAL A1344  0                                        
SHEET    2   H 2 LYS A1349  PHE A1350 -1  O  PHE A1350   N  VAL A1343           
SHEET    1   I 2 GLU A1385  ILE A1386  0                                        
SHEET    2   I 2 LEU A1409  ARG A1410 -1  O  LEU A1409   N  ILE A1386           
SHEET    1   J 2 VAL A1444  ARG A1445  0                                        
SHEET    2   J 2 MET A1451  ALA A1452 -1  O  ALA A1452   N  VAL A1444           
LINK         NE2 HIS A1502                ZN    ZN A   1     1555   1555  2.24  
LINK         SG  CYS A 656                ZN    ZN A   2     1555   1555  2.29  
LINK         SG  CYS A 667                ZN    ZN A   5     1555   1555  2.29  
LINK         NE2 HIS A 793                ZN    ZN A   3     1555   1555  2.31  
LINK         SG  CYS A 896                ZN    ZN A   3     1555   1555  2.32  
LINK         SG  CYS A 653                ZN    ZN A   2     1555   1555  2.33  
LINK         SG  CYS A1476                ZN    ZN A   1     1555   1555  2.39  
LINK         SG  CYS A 820                ZN    ZN A   3     1555   1555  2.39  
LINK         SG  CYS A 691                ZN    ZN A   2     1555   1555  2.41  
LINK         SG  CYS A 659                ZN    ZN A   2     1555   1555  2.44  
LINK         SG  CYS A 893                ZN    ZN A   3     1555   1555  2.44  
LINK         SG  CYS A1478                ZN    ZN A   1     1555   1555  2.52  
LINK         SG  CYS A 686                ZN    ZN A   5     1555   1555  2.66  
LINK         SG  CYS A1485                ZN    ZN A   1     1555   1555  2.88  
SITE     1 AC1 16 PHE A1145  SER A1146  GLY A1147  GLY A1150                    
SITE     2 AC1 16 LEU A1151  GLU A1168  MET A1169  TRP A1170                    
SITE     3 AC1 16 GLU A1189  CYS A1191  PRO A1225  LEU A1247                    
SITE     4 AC1 16 GLU A1266  ASN A1578  ALA A1579  VAL A1580                    
SITE     1 AC2  4 CYS A1476  CYS A1478  CYS A1485  HIS A1502                    
SITE     1 AC3  4 CYS A 653  CYS A 656  CYS A 659  CYS A 691                    
SITE     1 AC4  4 HIS A 793  CYS A 820  CYS A 893  CYS A 896                    
SITE     1 AC5  5 CYS A 664  CYS A 667  CYS A 670  CYS A 686                    
SITE     2 AC5  5 GLN A 687                                                     
CRYST1  162.800   87.900  113.900  90.00  97.20  90.00 C 1 2 1       4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.006143  0.000000  0.000776        0.00000                         
SCALE2      0.000000  0.011377  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008849        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system