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Database: PDB
Entry: 4WXX
LinkDB: 4WXX
Original site: 4WXX 
HEADER    TRANSFERASE                             14-NOV-14   4WXX              
TITLE     THE CRYSTAL STRUCTURE OF HUMAN DNMT1(351-1600)                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DNA (CYTOSINE-5)-METHYLTRANSFERASE 1;                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: DNMT1, CXXC-TYPE ZINC FINGER PROTEIN 9, DNA                 
COMPND   5 METHYLTRANSFERASE HSAI, MCMT;                                        
COMPND   6 EC: 2.1.1.37;                                                        
COMPND   7 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                                         
KEYWDS    DNMT1, DNA METHYTRANSFERASE1, DNA METHYLATION, TRANSFERASE            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Z.M.ZHANG,J.SONG                                                      
REVDAT   3   05-AUG-15 4WXX    1       JRNL                                     
REVDAT   2   22-JUL-15 4WXX    1       TITLE                                    
REVDAT   1   15-JUL-15 4WXX    0                                                
JRNL        AUTH   Z.M.ZHANG,S.LIU,K.LIN,Y.LUO,J.J.PERRY,Y.WANG,J.SONG          
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN DNA METHYLTRANSFERASE 1.          
JRNL        REF    J.MOL.BIOL.                   V. 427  2520 2015              
JRNL        REFN                   ESSN 1089-8638                               
JRNL        PMID   26070743                                                     
JRNL        DOI    10.1016/J.JMB.2015.06.001                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.62 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.9_1692)                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.62                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.22                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 122708                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.207                           
REMARK   3   R VALUE            (WORKING SET) : 0.205                           
REMARK   3   FREE R VALUE                     : 0.245                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.970                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6102                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 48.2228 -  8.1351    0.96     3852   186  0.1750 0.1946        
REMARK   3     2  8.1351 -  6.4620    0.97     3917   163  0.1873 0.2232        
REMARK   3     3  6.4620 -  5.6466    0.98     3865   216  0.1988 0.2266        
REMARK   3     4  5.6466 -  5.1310    0.98     3884   187  0.1936 0.2250        
REMARK   3     5  5.1310 -  4.7636    0.98     3862   221  0.1757 0.2051        
REMARK   3     6  4.7636 -  4.4829    0.98     3879   218  0.1632 0.1843        
REMARK   3     7  4.4829 -  4.2586    0.98     3929   185  0.1681 0.1838        
REMARK   3     8  4.2586 -  4.0733    0.98     3871   197  0.1781 0.2347        
REMARK   3     9  4.0733 -  3.9165    0.99     3912   190  0.1899 0.2511        
REMARK   3    10  3.9165 -  3.7815    0.99     3859   222  0.1971 0.2416        
REMARK   3    11  3.7815 -  3.6633    0.99     3944   171  0.1981 0.2449        
REMARK   3    12  3.6633 -  3.5586    0.99     3838   213  0.2059 0.2326        
REMARK   3    13  3.5586 -  3.4649    0.99     3900   218  0.2127 0.2591        
REMARK   3    14  3.4649 -  3.3804    0.99     3875   219  0.2171 0.2866        
REMARK   3    15  3.3804 -  3.3036    0.99     3931   214  0.2237 0.2651        
REMARK   3    16  3.3036 -  3.2333    0.99     3897   186  0.2482 0.2912        
REMARK   3    17  3.2333 -  3.1686    0.99     3941   179  0.2357 0.2953        
REMARK   3    18  3.1686 -  3.1088    0.99     3885   200  0.2285 0.2716        
REMARK   3    19  3.1088 -  3.0533    0.99     3917   205  0.2355 0.2532        
REMARK   3    20  3.0533 -  3.0016    0.99     3870   221  0.2315 0.3111        
REMARK   3    21  3.0016 -  2.9532    0.99     3871   241  0.2366 0.2873        
REMARK   3    22  2.9532 -  2.9077    0.99     3963   162  0.2428 0.2974        
REMARK   3    23  2.9077 -  2.8650    0.99     3886   231  0.2345 0.2669        
REMARK   3    24  2.8650 -  2.8246    0.99     3908   219  0.2437 0.3414        
REMARK   3    25  2.8246 -  2.7865    0.99     3892   199  0.2447 0.2816        
REMARK   3    26  2.7865 -  2.7503    0.99     3937   175  0.2510 0.2889        
REMARK   3    27  2.7503 -  2.7159    0.99     3866   210  0.2529 0.3028        
REMARK   3    28  2.7159 -  2.6832    0.99     3921   215  0.2666 0.2884        
REMARK   3    29  2.6832 -  2.6520    0.99     3878   228  0.2682 0.3046        
REMARK   3    30  2.6520 -  2.6222    0.93     3656   211  0.3062 0.3669        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.350            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.020           
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.003          18840                                  
REMARK   3   ANGLE     :  0.792          25518                                  
REMARK   3   CHIRALITY :  0.030           2735                                  
REMARK   3   PLANARITY :  0.004           3339                                  
REMARK   3   DIHEDRAL  : 14.452           7000                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4WXX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-NOV-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000204707.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-AUG-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9774                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 122755                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.620                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.220                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY                : 5.200                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
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   (%): 67.13                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.74                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 45% PEG200, 50 MM CACL2, 0.1 MM MES,     
REMARK 280  PH 6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y,X,Z+3/4                                              
REMARK 290       4555   Y,-X,Z+1/4                                              
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      110.76800            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      166.15200            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       55.38400            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A   350                                                      
REMARK 465     LEU A   386                                                      
REMARK 465     SER A   387                                                      
REMARK 465     ILE A   388                                                      
REMARK 465     PHE A   389                                                      
REMARK 465     ASP A   390                                                      
REMARK 465     ALA A   391                                                      
REMARK 465     ASN A   392                                                      
REMARK 465     GLU A   393                                                      
REMARK 465     SER A   394                                                      
REMARK 465     GLY A   395                                                      
REMARK 465     PHE A   396                                                      
REMARK 465     GLU A   397                                                      
REMARK 465     SER A   398                                                      
REMARK 465     TYR A   399                                                      
REMARK 465     GLU A   400                                                      
REMARK 465     THR A   603                                                      
REMARK 465     ILE A   604                                                      
REMARK 465     ARG A   605                                                      
REMARK 465     HIS A   606                                                      
REMARK 465     SER A   607                                                      
REMARK 465     THR A   608                                                      
REMARK 465     ARG A   609                                                      
REMARK 465     GLU A   610                                                      
REMARK 465     LYS A   611                                                      
REMARK 465     ASP A   612                                                      
REMARK 465     ARG A   613                                                      
REMARK 465     GLY A   614                                                      
REMARK 465     PRO A   615                                                      
REMARK 465     ASP A   639                                                      
REMARK 465     ASP A   640                                                      
REMARK 465     ARG A   641                                                      
REMARK 465     GLU A   642                                                      
REMARK 465     ASP A   643                                                      
REMARK 465     LYS A   644                                                      
REMARK 465     GLU A   645                                                      
REMARK 465     ASN A   646                                                      
REMARK 465     ALA A   647                                                      
REMARK 465     PHE A   648                                                      
REMARK 465     GLY A   742                                                      
REMARK 465     LYS A   951                                                      
REMARK 465     LEU A   952                                                      
REMARK 465     SER A   953                                                      
REMARK 465     SER A   954                                                      
REMARK 465     PRO A   955                                                      
REMARK 465     VAL A   956                                                      
REMARK 465     LYS A   957                                                      
REMARK 465     ARG A   958                                                      
REMARK 465     PRO A   959                                                      
REMARK 465     SER A   977                                                      
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   984                                                      
REMARK 465     PRO A  1106                                                      
REMARK 465     GLY A  1107                                                      
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     SER B   350                                                      
REMARK 465     PHE B   389                                                      
REMARK 465     ASP B   390                                                      
REMARK 465     ALA B   391                                                      
REMARK 465     ASN B   392                                                      
REMARK 465     GLU B   393                                                      
REMARK 465     SER B   394                                                      
REMARK 465     GLY B   395                                                      
REMARK 465     PHE B   396                                                      
REMARK 465     GLU B   397                                                      
REMARK 465     SER B   398                                                      
REMARK 465     TYR B   399                                                      
REMARK 465     THR B   603                                                      
REMARK 465     ILE B   604                                                      
REMARK 465     ARG B   605                                                      
REMARK 465     HIS B   606                                                      
REMARK 465     SER B   607                                                      
REMARK 465     THR B   608                                                      
REMARK 465     ARG B   609                                                      
REMARK 465     GLU B   610                                                      
REMARK 465     LYS B   611                                                      
REMARK 465     ASP B   612                                                      
REMARK 465     ARG B   613                                                      
REMARK 465     GLY B   614                                                      
REMARK 465     ASP B   639                                                      
REMARK 465     ASP B   640                                                      
REMARK 465     ARG B   641                                                      
REMARK 465     GLU B   642                                                      
REMARK 465     ASP B   643                                                      
REMARK 465     LYS B   644                                                      
REMARK 465     GLU B   645                                                      
REMARK 465     ASN B   646                                                      
REMARK 465     ALA B   647                                                      
REMARK 465     PHE B   648                                                      
REMARK 465     LEU B   952                                                      
REMARK 465     SER B   953                                                      
REMARK 465     SER B   954                                                      
REMARK 465     PRO B   955                                                      
REMARK 465     VAL B   956                                                      
REMARK 465     LYS B   957                                                      
REMARK 465     ARG B   958                                                      
REMARK 465     PRO B   959                                                      
REMARK 465     ASP B   978                                                      
REMARK 465     TYR B   979                                                      
REMARK 465     ILE B   980                                                      
REMARK 465     LYS B   981                                                      
REMARK 465     GLY B   982                                                      
REMARK 465     SER B   983                                                      
REMARK 465     ASN B   984                                                      
REMARK 465     PRO B  1106                                                      
REMARK 465     GLY B  1107                                                      
REMARK 465     ASN B  1108                                                      
REMARK 465     LYS B  1109                                                      
REMARK 465     GLY B  1110                                                      
REMARK 465     LYS B  1111                                                      
REMARK 465     GLY B  1112                                                      
REMARK 465     LYS B  1113                                                      
REMARK 465     GLY B  1114                                                      
REMARK 465     LYS B  1115                                                      
REMARK 465     GLY B  1116                                                      
REMARK 465     LYS B  1117                                                      
REMARK 465     GLY B  1118                                                      
REMARK 465     LYS B  1119                                                      
REMARK 465     PRO B  1120                                                      
REMARK 465     LYS B  1121                                                      
REMARK 465     SER B  1122                                                      
REMARK 465     GLN B  1123                                                      
REMARK 465     ALA B  1124                                                      
REMARK 465     CYS B  1125                                                      
REMARK 465     GLU B  1126                                                      
REMARK 465     PRO B  1127                                                      
REMARK 465     SER B  1128                                                      
REMARK 465     GLU B  1129                                                      
REMARK 465     PRO B  1130                                                      
REMARK 465     GLU B  1131                                                      
REMARK 465     ILE B  1132                                                      
REMARK 465     GLU B  1133                                                      
REMARK 465     ILE B  1134                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ILE A 354    CG1  CG2  CD1                                       
REMARK 470     GLN A 355    O                                                   
REMARK 470     ASP A 361    CG   OD1  OD2                                       
REMARK 470     ASP A 362    CG   OD1  OD2                                       
REMARK 470     LYS A 366    CG   CD   CE   NZ                                   
REMARK 470     GLN A 369    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 377    CG   CD   OE1  OE2                                  
REMARK 470     MET A 380    CE                                                  
REMARK 470     GLU A 384    CD   OE1  OE2                                       
REMARK 470     LYS A 385    CG   CD   CE   NZ                                   
REMARK 470     SER A 448    OG                                                  
REMARK 470     LYS A 456    CD   CE   NZ                                        
REMARK 470     ASP A 569    OD1  OD2                                            
REMARK 470     ASP A 571    CG   OD1  OD2                                       
REMARK 470     GLU A 572    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 596    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 598    CG   CD   OE1  NE2                                  
REMARK 470     ARG A 600    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG A 601    NE   CZ   NH1  NH2                                  
REMARK 470     GLN A 602    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 649    CE   NZ                                             
REMARK 470     ARG A 651    NE   CZ   NH1  NH2                                  
REMARK 470     LYS A 666    CG   CD   CE   NZ                                   
REMARK 470     LYS A 668    CG   CD   CE   NZ                                   
REMARK 470     LYS A 671    CE   NZ                                             
REMARK 470     VAL A 674    CG1  CG2                                            
REMARK 470     LYS A 675    CG   CD   CE   NZ                                   
REMARK 470     PHE A 676    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLN A 687    CB   CG   CD   OE1  NE2                             
REMARK 470     ASP A 707    CG   OD1  OD2                                       
REMARK 470     ASN A 708    CG   OD1  ND2                                       
REMARK 470     GLU A 711    CD   OE1  OE2                                       
REMARK 470     HIS A 719    CA                                                  
REMARK 470     LYS A 743    CD   CE   NZ                                        
REMARK 470     LYS A 744    CG   CD   CE   NZ                                   
REMARK 470     SER A 771    OG                                                  
REMARK 470     GLU A 852    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 855    CG   CD1  CD2                                       
REMARK 470     GLU A 856    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 858    OD1  OD2                                            
REMARK 470     ASP A 859    CG   OD1  OD2                                       
REMARK 470     LYS A 861    CD   CE   NZ                                        
REMARK 470     GLU A 901    CD   OE1  OE2                                       
REMARK 470     GLU A 906    CD   OE1  OE2                                       
REMARK 470     ASP A 918    CG   OD1  OD2                                       
REMARK 470     SER A1005    OG                                                  
REMARK 470     ARG A1506    CZ   NH1  NH2                                       
REMARK 470     ILE B 354    CG1  CG2  CD1                                       
REMARK 470     ASP B 361    CG   OD1  OD2                                       
REMARK 470     LYS B 366    CD   CE   NZ                                        
REMARK 470     ASP B 373    OD1  OD2                                            
REMARK 470     VAL B 375    CG1  CG2                                            
REMARK 470     GLU B 377    CG   CD   OE1  OE2                                  
REMARK 470     MET B 380    SD   CE                                             
REMARK 470     ASN B 383    CG   OD1  ND2                                       
REMARK 470     GLU B 384    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 385    CD   CE   NZ                                        
REMARK 470     GLU B 400    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 428    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 456    CE   NZ                                             
REMARK 470     VAL B 561    O                                                   
REMARK 470     ASP B 565    OD1  OD2                                            
REMARK 470     GLU B 566    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 571    OD1  OD2                                            
REMARK 470     GLU B 572    CD   OE1  OE2                                       
REMARK 470     ARG B 596    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B 598    CG   CD   OE1  NE2                                  
REMARK 470     ARG B 601    NE   CZ   NH1  NH2                                  
REMARK 470     GLN B 602    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 622    CD   CE   NZ                                        
REMARK 470     GLU B 637    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 638    CG   CD   CE   NZ                                   
REMARK 470     LYS B 649    CD   CE   NZ                                        
REMARK 470     ARG B 651    NE   CZ   NH1  NH2                                  
REMARK 470     LYS B 666    CG   CD   CE   NZ                                   
REMARK 470     LYS B 668    CG   CD   CE   NZ                                   
REMARK 470     LYS B 671    CE   NZ                                             
REMARK 470     VAL B 674    CG1  CG2                                            
REMARK 470     LYS B 675    CG   CD   CE   NZ                                   
REMARK 470     PHE B 676    CD1  CD2  CE1  CE2  CZ                              
REMARK 470     LYS B 683    CG   CD   CE   NZ                                   
REMARK 470     GLN B 684    CG   CD   OE1  NE2                                  
REMARK 470     GLN B 687    CB   CG   CD   OE1  NE2                             
REMARK 470     ARG B 690    CD   NE   CZ   NH1  NH2                             
REMARK 470     ASP B 707    CG   OD1  OD2                                       
REMARK 470     ASN B 708    CG   OD1  ND2                                       
REMARK 470     GLU B 711    CD   OE1  OE2                                       
REMARK 470     THR B 740    OG1  CG2                                            
REMARK 470     ASP B 741    CG   OD1  OD2                                       
REMARK 470     LYS B 743    CD   CE   NZ                                        
REMARK 470     LYS B 744    CG   CD   CE   NZ                                   
REMARK 470     LYS B 749    CD   CE   NZ                                        
REMARK 470     GLU B 852    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 855    CG   CD1  CD2                                       
REMARK 470     GLU B 856    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 858    CG   OD1  OD2                                       
REMARK 470     ASP B 859    CG   OD1  OD2                                       
REMARK 470     LYS B 861    CD   CE   NZ                                        
REMARK 470     LYS B 951    CD   CE   NZ                                        
REMARK 470     ARG B 960    NE   CZ   NH1  NH2                                  
REMARK 470     LYS B 961    CE   NZ                                             
REMARK 470     SER B1005    OG                                                  
REMARK 470     ARG B1008    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR B1012    OG1  CG2                                            
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    LEU A 449   CA  -  CB  -  CG  ANGL. DEV. =  18.9 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    GLN A 355      -83.55    -86.21                                   
REMARK 500    ASP A 362      167.40     65.93                                   
REMARK 500    ASP A 373     -136.16   -138.39                                   
REMARK 500    GLU A 377      -40.11    113.16                                   
REMARK 500    PRO A 378       56.01    -56.58                                   
REMARK 500    LEU A 381      -71.03    -53.54                                   
REMARK 500    LEU A 449      -10.22     84.49                                   
REMARK 500    ASN A 457       45.87     19.90                                   
REMARK 500    ASN A 462      -81.72    -91.98                                   
REMARK 500    PHE A 483      -67.59    -96.01                                   
REMARK 500    MET A 489     -102.87   -120.95                                   
REMARK 500    ASN A 541       31.64    -87.32                                   
REMARK 500    SER A 570     -156.81   -153.74                                   
REMARK 500    ARG A 595      146.71     58.33                                   
REMARK 500    ARG A 596       86.78   -168.89                                   
REMARK 500    ARG A 600       66.37     68.33                                   
REMARK 500    ARG A 601     -171.39     59.23                                   
REMARK 500    PHE A 632      -75.98    -56.42                                   
REMARK 500    ALA A 633      -34.88    -39.79                                   
REMARK 500    ARG A 650      151.00     76.37                                   
REMARK 500    PHE A 676       89.42     57.98                                   
REMARK 500    GLU A 688       31.06    -99.23                                   
REMARK 500    ARG A 689       14.92   -146.64                                   
REMARK 500    PRO A 713     -158.89    -75.22                                   
REMARK 500    ASN A 727       64.90   -108.63                                   
REMARK 500    LYS A 744       21.52     49.10                                   
REMARK 500    ALA A 754      -11.53     79.86                                   
REMARK 500    ASP A 769      127.58     83.40                                   
REMARK 500    SER A 770      -68.78   -120.04                                   
REMARK 500    ASP A 818       49.18    -77.20                                   
REMARK 500    ASP A 858       84.25     54.75                                   
REMARK 500    GLN A 866      -21.40   -148.64                                   
REMARK 500    LYS A 891      -18.93   -144.42                                   
REMARK 500    LEU A 911      -79.66   -103.48                                   
REMARK 500    LEU A 914      -51.57   -125.32                                   
REMARK 500    LYS A 961      166.12    -34.61                                   
REMARK 500    SER A1030     -153.82     62.68                                   
REMARK 500    PHE A1229       30.82   -146.18                                   
REMARK 500    SER A1230       33.07    -97.84                                   
REMARK 500    MET A1371       15.41   -149.60                                   
REMARK 500    ALA A1403       54.09   -117.03                                   
REMARK 500    TYR A1405      -70.95    -66.47                                   
REMARK 500    ASP A1435     -154.80   -147.65                                   
REMARK 500    HIS A1507       49.26   -140.76                                   
REMARK 500    GLN B 355      -68.87    -92.21                                   
REMARK 500    PRO B 363     -138.70    -81.20                                   
REMARK 500    PRO B 372     -151.73    -99.28                                   
REMARK 500    ASP B 373      124.38    131.10                                   
REMARK 500    ALA B 374      129.13     65.39                                   
REMARK 500    VAL B 375     -167.38    -75.12                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      83 RAMACHANDRAN OUTLIERS.                        
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 A1705  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 353   SG                                                     
REMARK 620 2 CYS A 356   SG  112.9                                              
REMARK 620 3 CYS A 414   SG  122.1 108.9                                        
REMARK 620 4 HIS A 418   ND1 105.7 105.8  99.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1704  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 653   SG                                                     
REMARK 620 2 CYS A 656   SG  103.9                                              
REMARK 620 3 CYS A 659   SG  119.3 102.1                                        
REMARK 620 4 CYS A 691   SG  105.1 123.8 104.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1703  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 664   SG                                                     
REMARK 620 2 CYS A 667   SG  100.5                                              
REMARK 620 3 CYS A 670   SG  131.0 117.0                                        
REMARK 620 4 CYS A 686   SG   92.3 119.5  95.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1702  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 793   NE2                                                    
REMARK 620 2 CYS A 820   SG  102.6                                              
REMARK 620 3 CYS A 893   SG  114.3 125.2                                        
REMARK 620 4 CYS A 896   SG   96.7 101.3 112.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1701  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1476   SG                                                     
REMARK 620 2 CYS A1478   SG  111.0                                              
REMARK 620 3 CYS A1485   SG  117.4 105.1                                        
REMARK 620 4 HIS A1502   NE2 110.0 101.0 111.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1705  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 353   SG                                                     
REMARK 620 2 CYS B 356   SG  102.4                                              
REMARK 620 3 CYS B 414   SG   93.5 118.6                                        
REMARK 620 4 HIS B 418   ND1 104.7 100.4 132.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1704  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 653   SG                                                     
REMARK 620 2 CYS B 656   SG  107.9                                              
REMARK 620 3 CYS B 659   SG  118.2 106.7                                        
REMARK 620 4 CYS B 691   SG  104.9 122.6  97.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1703  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 664   SG                                                     
REMARK 620 2 CYS B 667   SG  101.2                                              
REMARK 620 3 CYS B 670   SG  119.7 114.1                                        
REMARK 620 4 CYS B 686   SG   99.3 125.5  97.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1702  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 793   NE2                                                    
REMARK 620 2 CYS B 820   SG  105.9                                              
REMARK 620 3 CYS B 893   SG  107.9 125.1                                        
REMARK 620 4 CYS B 896   SG   97.4 100.3 116.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1701  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B1476   SG                                                     
REMARK 620 2 CYS B1478   SG  106.7                                              
REMARK 620 3 CYS B1485   SG  116.7 107.3                                        
REMARK 620 4 HIS B1502   NE2 111.3 102.7 111.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1704                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1705                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAH A 1706                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1704                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1705                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAH B 1706                
DBREF  4WXX A  351  1600  UNP    P26358   DNMT1_HUMAN     15   1264             
DBREF  4WXX B  351  1600  UNP    P26358   DNMT1_HUMAN     15   1264             
SEQADV 4WXX SER A  350  UNP  P26358              EXPRESSION TAG                 
SEQADV 4WXX LEU A 1601  UNP  P26358              EXPRESSION TAG                 
SEQADV 4WXX THR A 1602  UNP  P26358              EXPRESSION TAG                 
SEQADV 4WXX ARG A 1603  UNP  P26358              EXPRESSION TAG                 
SEQADV 4WXX VAL A 1604  UNP  P26358              EXPRESSION TAG                 
SEQADV 4WXX TRP A 1605  UNP  P26358              EXPRESSION TAG                 
SEQADV 4WXX SER B  350  UNP  P26358              EXPRESSION TAG                 
SEQADV 4WXX LEU B 1601  UNP  P26358              EXPRESSION TAG                 
SEQADV 4WXX THR B 1602  UNP  P26358              EXPRESSION TAG                 
SEQADV 4WXX ARG B 1603  UNP  P26358              EXPRESSION TAG                 
SEQADV 4WXX VAL B 1604  UNP  P26358              EXPRESSION TAG                 
SEQADV 4WXX TRP B 1605  UNP  P26358              EXPRESSION TAG                 
SEQRES   1 A 1256  SER PRO LYS CYS ILE GLN CYS GLY GLN TYR LEU ASP ASP          
SEQRES   2 A 1256  PRO ASP LEU LYS TYR GLY GLN HIS PRO PRO ASP ALA VAL          
SEQRES   3 A 1256  ASP GLU PRO GLN MET LEU THR ASN GLU LYS LEU SER ILE          
SEQRES   4 A 1256  PHE ASP ALA ASN GLU SER GLY PHE GLU SER TYR GLU ALA          
SEQRES   5 A 1256  LEU PRO GLN HIS LYS LEU THR CYS PHE SER VAL TYR CYS          
SEQRES   6 A 1256  LYS HIS GLY HIS LEU CYS PRO ILE ASP THR GLY LEU ILE          
SEQRES   7 A 1256  GLU LYS ASN ILE GLU LEU PHE PHE SER GLY SER ALA LYS          
SEQRES   8 A 1256  PRO ILE TYR ASP ASP ASP PRO SER LEU GLU GLY GLY VAL          
SEQRES   9 A 1256  ASN GLY LYS ASN LEU GLY PRO ILE ASN GLU TRP TRP ILE          
SEQRES  10 A 1256  THR GLY PHE ASP GLY GLY GLU LYS ALA LEU ILE GLY PHE          
SEQRES  11 A 1256  SER THR SER PHE ALA GLU TYR ILE LEU MET ASP PRO SER          
SEQRES  12 A 1256  PRO GLU TYR ALA PRO ILE PHE GLY LEU MET GLN GLU LYS          
SEQRES  13 A 1256  ILE TYR ILE SER LYS ILE VAL VAL GLU PHE LEU GLN SER          
SEQRES  14 A 1256  ASN SER ASP SER THR TYR GLU ASP LEU ILE ASN LYS ILE          
SEQRES  15 A 1256  GLU THR THR VAL PRO PRO SER GLY LEU ASN LEU ASN ARG          
SEQRES  16 A 1256  PHE THR GLU ASP SER LEU LEU ARG HIS ALA GLN PHE VAL          
SEQRES  17 A 1256  VAL GLU GLN VAL GLU SER TYR ASP GLU ALA GLY ASP SER          
SEQRES  18 A 1256  ASP GLU GLN PRO ILE PHE LEU THR PRO CYS MET ARG ASP          
SEQRES  19 A 1256  LEU ILE LYS LEU ALA GLY VAL THR LEU GLY GLN ARG ARG          
SEQRES  20 A 1256  ALA GLN ALA ARG ARG GLN THR ILE ARG HIS SER THR ARG          
SEQRES  21 A 1256  GLU LYS ASP ARG GLY PRO THR LYS ALA THR THR THR LYS          
SEQRES  22 A 1256  LEU VAL TYR GLN ILE PHE ASP THR PHE PHE ALA GLU GLN          
SEQRES  23 A 1256  ILE GLU LYS ASP ASP ARG GLU ASP LYS GLU ASN ALA PHE          
SEQRES  24 A 1256  LYS ARG ARG ARG CYS GLY VAL CYS GLU VAL CYS GLN GLN          
SEQRES  25 A 1256  PRO GLU CYS GLY LYS CYS LYS ALA CYS LYS ASP MET VAL          
SEQRES  26 A 1256  LYS PHE GLY GLY SER GLY ARG SER LYS GLN ALA CYS GLN          
SEQRES  27 A 1256  GLU ARG ARG CYS PRO ASN MET ALA MET LYS GLU ALA ASP          
SEQRES  28 A 1256  ASP ASP GLU GLU VAL ASP ASP ASN ILE PRO GLU MET PRO          
SEQRES  29 A 1256  SER PRO LYS LYS MET HIS GLN GLY LYS LYS LYS LYS GLN          
SEQRES  30 A 1256  ASN LYS ASN ARG ILE SER TRP VAL GLY GLU ALA VAL LYS          
SEQRES  31 A 1256  THR ASP GLY LYS LYS SER TYR TYR LYS LYS VAL CYS ILE          
SEQRES  32 A 1256  ASP ALA GLU THR LEU GLU VAL GLY ASP CYS VAL SER VAL          
SEQRES  33 A 1256  ILE PRO ASP ASP SER SER LYS PRO LEU TYR LEU ALA ARG          
SEQRES  34 A 1256  VAL THR ALA LEU TRP GLU ASP SER SER ASN GLY GLN MET          
SEQRES  35 A 1256  PHE HIS ALA HIS TRP PHE CYS ALA GLY THR ASP THR VAL          
SEQRES  36 A 1256  LEU GLY ALA THR SER ASP PRO LEU GLU LEU PHE LEU VAL          
SEQRES  37 A 1256  ASP GLU CYS GLU ASP MET GLN LEU SER TYR ILE HIS SER          
SEQRES  38 A 1256  LYS VAL LYS VAL ILE TYR LYS ALA PRO SER GLU ASN TRP          
SEQRES  39 A 1256  ALA MET GLU GLY GLY MET ASP PRO GLU SER LEU LEU GLU          
SEQRES  40 A 1256  GLY ASP ASP GLY LYS THR TYR PHE TYR GLN LEU TRP TYR          
SEQRES  41 A 1256  ASP GLN ASP TYR ALA ARG PHE GLU SER PRO PRO LYS THR          
SEQRES  42 A 1256  GLN PRO THR GLU ASP ASN LYS PHE LYS PHE CYS VAL SER          
SEQRES  43 A 1256  CYS ALA ARG LEU ALA GLU MET ARG GLN LYS GLU ILE PRO          
SEQRES  44 A 1256  ARG VAL LEU GLU GLN LEU GLU ASP LEU ASP SER ARG VAL          
SEQRES  45 A 1256  LEU TYR TYR SER ALA THR LYS ASN GLY ILE LEU TYR ARG          
SEQRES  46 A 1256  VAL GLY ASP GLY VAL TYR LEU PRO PRO GLU ALA PHE THR          
SEQRES  47 A 1256  PHE ASN ILE LYS LEU SER SER PRO VAL LYS ARG PRO ARG          
SEQRES  48 A 1256  LYS GLU PRO VAL ASP GLU ASP LEU TYR PRO GLU HIS TYR          
SEQRES  49 A 1256  ARG LYS TYR SER ASP TYR ILE LYS GLY SER ASN LEU ASP          
SEQRES  50 A 1256  ALA PRO GLU PRO TYR ARG ILE GLY ARG ILE LYS GLU ILE          
SEQRES  51 A 1256  PHE CYS PRO LYS LYS SER ASN GLY ARG PRO ASN GLU THR          
SEQRES  52 A 1256  ASP ILE LYS ILE ARG VAL ASN LYS PHE TYR ARG PRO GLU          
SEQRES  53 A 1256  ASN THR HIS LYS SER THR PRO ALA SER TYR HIS ALA ASP          
SEQRES  54 A 1256  ILE ASN LEU LEU TYR TRP SER ASP GLU GLU ALA VAL VAL          
SEQRES  55 A 1256  ASP PHE LYS ALA VAL GLN GLY ARG CYS THR VAL GLU TYR          
SEQRES  56 A 1256  GLY GLU ASP LEU PRO GLU CYS VAL GLN VAL TYR SER MET          
SEQRES  57 A 1256  GLY GLY PRO ASN ARG PHE TYR PHE LEU GLU ALA TYR ASN          
SEQRES  58 A 1256  ALA LYS SER LYS SER PHE GLU ASP PRO PRO ASN HIS ALA          
SEQRES  59 A 1256  ARG SER PRO GLY ASN LYS GLY LYS GLY LYS GLY LYS GLY          
SEQRES  60 A 1256  LYS GLY LYS PRO LYS SER GLN ALA CYS GLU PRO SER GLU          
SEQRES  61 A 1256  PRO GLU ILE GLU ILE LYS LEU PRO LYS LEU ARG THR LEU          
SEQRES  62 A 1256  ASP VAL PHE SER GLY CYS GLY GLY LEU SER GLU GLY PHE          
SEQRES  63 A 1256  HIS GLN ALA GLY ILE SER ASP THR LEU TRP ALA ILE GLU          
SEQRES  64 A 1256  MET TRP ASP PRO ALA ALA GLN ALA PHE ARG LEU ASN ASN          
SEQRES  65 A 1256  PRO GLY SER THR VAL PHE THR GLU ASP CYS ASN ILE LEU          
SEQRES  66 A 1256  LEU LYS LEU VAL MET ALA GLY GLU THR THR ASN SER ARG          
SEQRES  67 A 1256  GLY GLN ARG LEU PRO GLN LYS GLY ASP VAL GLU MET LEU          
SEQRES  68 A 1256  CYS GLY GLY PRO PRO CYS GLN GLY PHE SER GLY MET ASN          
SEQRES  69 A 1256  ARG PHE ASN SER ARG THR TYR SER LYS PHE LYS ASN SER          
SEQRES  70 A 1256  LEU VAL VAL SER PHE LEU SER TYR CYS ASP TYR TYR ARG          
SEQRES  71 A 1256  PRO ARG PHE PHE LEU LEU GLU ASN VAL ARG ASN PHE VAL          
SEQRES  72 A 1256  SER PHE LYS ARG SER MET VAL LEU LYS LEU THR LEU ARG          
SEQRES  73 A 1256  CYS LEU VAL ARG MET GLY TYR GLN CYS THR PHE GLY VAL          
SEQRES  74 A 1256  LEU GLN ALA GLY GLN TYR GLY VAL ALA GLN THR ARG ARG          
SEQRES  75 A 1256  ARG ALA ILE ILE LEU ALA ALA ALA PRO GLY GLU LYS LEU          
SEQRES  76 A 1256  PRO LEU PHE PRO GLU PRO LEU HIS VAL PHE ALA PRO ARG          
SEQRES  77 A 1256  ALA CYS GLN LEU SER VAL VAL VAL ASP ASP LYS LYS PHE          
SEQRES  78 A 1256  VAL SER ASN ILE THR ARG LEU SER SER GLY PRO PHE ARG          
SEQRES  79 A 1256  THR ILE THR VAL ARG ASP THR MET SER ASP LEU PRO GLU          
SEQRES  80 A 1256  VAL ARG ASN GLY ALA SER ALA LEU GLU ILE SER TYR ASN          
SEQRES  81 A 1256  GLY GLU PRO GLN SER TRP PHE GLN ARG GLN LEU ARG GLY          
SEQRES  82 A 1256  ALA GLN TYR GLN PRO ILE LEU ARG ASP HIS ILE CYS LYS          
SEQRES  83 A 1256  ASP MET SER ALA LEU VAL ALA ALA ARG MET ARG HIS ILE          
SEQRES  84 A 1256  PRO LEU ALA PRO GLY SER ASP TRP ARG ASP LEU PRO ASN          
SEQRES  85 A 1256  ILE GLU VAL ARG LEU SER ASP GLY THR MET ALA ARG LYS          
SEQRES  86 A 1256  LEU ARG TYR THR HIS HIS ASP ARG LYS ASN GLY ARG SER          
SEQRES  87 A 1256  SER SER GLY ALA LEU ARG GLY VAL CYS SER CYS VAL GLU          
SEQRES  88 A 1256  ALA GLY LYS ALA CYS ASP PRO ALA ALA ARG GLN PHE ASN          
SEQRES  89 A 1256  THR LEU ILE PRO TRP CYS LEU PRO HIS THR GLY ASN ARG          
SEQRES  90 A 1256  HIS ASN HIS TRP ALA GLY LEU TYR GLY ARG LEU GLU TRP          
SEQRES  91 A 1256  ASP GLY PHE PHE SER THR THR VAL THR ASN PRO GLU PRO          
SEQRES  92 A 1256  MET GLY LYS GLN GLY ARG VAL LEU HIS PRO GLU GLN HIS          
SEQRES  93 A 1256  ARG VAL VAL SER VAL ARG GLU CYS ALA ARG SER GLN GLY          
SEQRES  94 A 1256  PHE PRO ASP THR TYR ARG LEU PHE GLY ASN ILE LEU ASP          
SEQRES  95 A 1256  LYS HIS ARG GLN VAL GLY ASN ALA VAL PRO PRO PRO LEU          
SEQRES  96 A 1256  ALA LYS ALA ILE GLY LEU GLU ILE LYS LEU CYS MET LEU          
SEQRES  97 A 1256  ALA LYS ALA LEU THR ARG VAL TRP                              
SEQRES   1 B 1256  SER PRO LYS CYS ILE GLN CYS GLY GLN TYR LEU ASP ASP          
SEQRES   2 B 1256  PRO ASP LEU LYS TYR GLY GLN HIS PRO PRO ASP ALA VAL          
SEQRES   3 B 1256  ASP GLU PRO GLN MET LEU THR ASN GLU LYS LEU SER ILE          
SEQRES   4 B 1256  PHE ASP ALA ASN GLU SER GLY PHE GLU SER TYR GLU ALA          
SEQRES   5 B 1256  LEU PRO GLN HIS LYS LEU THR CYS PHE SER VAL TYR CYS          
SEQRES   6 B 1256  LYS HIS GLY HIS LEU CYS PRO ILE ASP THR GLY LEU ILE          
SEQRES   7 B 1256  GLU LYS ASN ILE GLU LEU PHE PHE SER GLY SER ALA LYS          
SEQRES   8 B 1256  PRO ILE TYR ASP ASP ASP PRO SER LEU GLU GLY GLY VAL          
SEQRES   9 B 1256  ASN GLY LYS ASN LEU GLY PRO ILE ASN GLU TRP TRP ILE          
SEQRES  10 B 1256  THR GLY PHE ASP GLY GLY GLU LYS ALA LEU ILE GLY PHE          
SEQRES  11 B 1256  SER THR SER PHE ALA GLU TYR ILE LEU MET ASP PRO SER          
SEQRES  12 B 1256  PRO GLU TYR ALA PRO ILE PHE GLY LEU MET GLN GLU LYS          
SEQRES  13 B 1256  ILE TYR ILE SER LYS ILE VAL VAL GLU PHE LEU GLN SER          
SEQRES  14 B 1256  ASN SER ASP SER THR TYR GLU ASP LEU ILE ASN LYS ILE          
SEQRES  15 B 1256  GLU THR THR VAL PRO PRO SER GLY LEU ASN LEU ASN ARG          
SEQRES  16 B 1256  PHE THR GLU ASP SER LEU LEU ARG HIS ALA GLN PHE VAL          
SEQRES  17 B 1256  VAL GLU GLN VAL GLU SER TYR ASP GLU ALA GLY ASP SER          
SEQRES  18 B 1256  ASP GLU GLN PRO ILE PHE LEU THR PRO CYS MET ARG ASP          
SEQRES  19 B 1256  LEU ILE LYS LEU ALA GLY VAL THR LEU GLY GLN ARG ARG          
SEQRES  20 B 1256  ALA GLN ALA ARG ARG GLN THR ILE ARG HIS SER THR ARG          
SEQRES  21 B 1256  GLU LYS ASP ARG GLY PRO THR LYS ALA THR THR THR LYS          
SEQRES  22 B 1256  LEU VAL TYR GLN ILE PHE ASP THR PHE PHE ALA GLU GLN          
SEQRES  23 B 1256  ILE GLU LYS ASP ASP ARG GLU ASP LYS GLU ASN ALA PHE          
SEQRES  24 B 1256  LYS ARG ARG ARG CYS GLY VAL CYS GLU VAL CYS GLN GLN          
SEQRES  25 B 1256  PRO GLU CYS GLY LYS CYS LYS ALA CYS LYS ASP MET VAL          
SEQRES  26 B 1256  LYS PHE GLY GLY SER GLY ARG SER LYS GLN ALA CYS GLN          
SEQRES  27 B 1256  GLU ARG ARG CYS PRO ASN MET ALA MET LYS GLU ALA ASP          
SEQRES  28 B 1256  ASP ASP GLU GLU VAL ASP ASP ASN ILE PRO GLU MET PRO          
SEQRES  29 B 1256  SER PRO LYS LYS MET HIS GLN GLY LYS LYS LYS LYS GLN          
SEQRES  30 B 1256  ASN LYS ASN ARG ILE SER TRP VAL GLY GLU ALA VAL LYS          
SEQRES  31 B 1256  THR ASP GLY LYS LYS SER TYR TYR LYS LYS VAL CYS ILE          
SEQRES  32 B 1256  ASP ALA GLU THR LEU GLU VAL GLY ASP CYS VAL SER VAL          
SEQRES  33 B 1256  ILE PRO ASP ASP SER SER LYS PRO LEU TYR LEU ALA ARG          
SEQRES  34 B 1256  VAL THR ALA LEU TRP GLU ASP SER SER ASN GLY GLN MET          
SEQRES  35 B 1256  PHE HIS ALA HIS TRP PHE CYS ALA GLY THR ASP THR VAL          
SEQRES  36 B 1256  LEU GLY ALA THR SER ASP PRO LEU GLU LEU PHE LEU VAL          
SEQRES  37 B 1256  ASP GLU CYS GLU ASP MET GLN LEU SER TYR ILE HIS SER          
SEQRES  38 B 1256  LYS VAL LYS VAL ILE TYR LYS ALA PRO SER GLU ASN TRP          
SEQRES  39 B 1256  ALA MET GLU GLY GLY MET ASP PRO GLU SER LEU LEU GLU          
SEQRES  40 B 1256  GLY ASP ASP GLY LYS THR TYR PHE TYR GLN LEU TRP TYR          
SEQRES  41 B 1256  ASP GLN ASP TYR ALA ARG PHE GLU SER PRO PRO LYS THR          
SEQRES  42 B 1256  GLN PRO THR GLU ASP ASN LYS PHE LYS PHE CYS VAL SER          
SEQRES  43 B 1256  CYS ALA ARG LEU ALA GLU MET ARG GLN LYS GLU ILE PRO          
SEQRES  44 B 1256  ARG VAL LEU GLU GLN LEU GLU ASP LEU ASP SER ARG VAL          
SEQRES  45 B 1256  LEU TYR TYR SER ALA THR LYS ASN GLY ILE LEU TYR ARG          
SEQRES  46 B 1256  VAL GLY ASP GLY VAL TYR LEU PRO PRO GLU ALA PHE THR          
SEQRES  47 B 1256  PHE ASN ILE LYS LEU SER SER PRO VAL LYS ARG PRO ARG          
SEQRES  48 B 1256  LYS GLU PRO VAL ASP GLU ASP LEU TYR PRO GLU HIS TYR          
SEQRES  49 B 1256  ARG LYS TYR SER ASP TYR ILE LYS GLY SER ASN LEU ASP          
SEQRES  50 B 1256  ALA PRO GLU PRO TYR ARG ILE GLY ARG ILE LYS GLU ILE          
SEQRES  51 B 1256  PHE CYS PRO LYS LYS SER ASN GLY ARG PRO ASN GLU THR          
SEQRES  52 B 1256  ASP ILE LYS ILE ARG VAL ASN LYS PHE TYR ARG PRO GLU          
SEQRES  53 B 1256  ASN THR HIS LYS SER THR PRO ALA SER TYR HIS ALA ASP          
SEQRES  54 B 1256  ILE ASN LEU LEU TYR TRP SER ASP GLU GLU ALA VAL VAL          
SEQRES  55 B 1256  ASP PHE LYS ALA VAL GLN GLY ARG CYS THR VAL GLU TYR          
SEQRES  56 B 1256  GLY GLU ASP LEU PRO GLU CYS VAL GLN VAL TYR SER MET          
SEQRES  57 B 1256  GLY GLY PRO ASN ARG PHE TYR PHE LEU GLU ALA TYR ASN          
SEQRES  58 B 1256  ALA LYS SER LYS SER PHE GLU ASP PRO PRO ASN HIS ALA          
SEQRES  59 B 1256  ARG SER PRO GLY ASN LYS GLY LYS GLY LYS GLY LYS GLY          
SEQRES  60 B 1256  LYS GLY LYS PRO LYS SER GLN ALA CYS GLU PRO SER GLU          
SEQRES  61 B 1256  PRO GLU ILE GLU ILE LYS LEU PRO LYS LEU ARG THR LEU          
SEQRES  62 B 1256  ASP VAL PHE SER GLY CYS GLY GLY LEU SER GLU GLY PHE          
SEQRES  63 B 1256  HIS GLN ALA GLY ILE SER ASP THR LEU TRP ALA ILE GLU          
SEQRES  64 B 1256  MET TRP ASP PRO ALA ALA GLN ALA PHE ARG LEU ASN ASN          
SEQRES  65 B 1256  PRO GLY SER THR VAL PHE THR GLU ASP CYS ASN ILE LEU          
SEQRES  66 B 1256  LEU LYS LEU VAL MET ALA GLY GLU THR THR ASN SER ARG          
SEQRES  67 B 1256  GLY GLN ARG LEU PRO GLN LYS GLY ASP VAL GLU MET LEU          
SEQRES  68 B 1256  CYS GLY GLY PRO PRO CYS GLN GLY PHE SER GLY MET ASN          
SEQRES  69 B 1256  ARG PHE ASN SER ARG THR TYR SER LYS PHE LYS ASN SER          
SEQRES  70 B 1256  LEU VAL VAL SER PHE LEU SER TYR CYS ASP TYR TYR ARG          
SEQRES  71 B 1256  PRO ARG PHE PHE LEU LEU GLU ASN VAL ARG ASN PHE VAL          
SEQRES  72 B 1256  SER PHE LYS ARG SER MET VAL LEU LYS LEU THR LEU ARG          
SEQRES  73 B 1256  CYS LEU VAL ARG MET GLY TYR GLN CYS THR PHE GLY VAL          
SEQRES  74 B 1256  LEU GLN ALA GLY GLN TYR GLY VAL ALA GLN THR ARG ARG          
SEQRES  75 B 1256  ARG ALA ILE ILE LEU ALA ALA ALA PRO GLY GLU LYS LEU          
SEQRES  76 B 1256  PRO LEU PHE PRO GLU PRO LEU HIS VAL PHE ALA PRO ARG          
SEQRES  77 B 1256  ALA CYS GLN LEU SER VAL VAL VAL ASP ASP LYS LYS PHE          
SEQRES  78 B 1256  VAL SER ASN ILE THR ARG LEU SER SER GLY PRO PHE ARG          
SEQRES  79 B 1256  THR ILE THR VAL ARG ASP THR MET SER ASP LEU PRO GLU          
SEQRES  80 B 1256  VAL ARG ASN GLY ALA SER ALA LEU GLU ILE SER TYR ASN          
SEQRES  81 B 1256  GLY GLU PRO GLN SER TRP PHE GLN ARG GLN LEU ARG GLY          
SEQRES  82 B 1256  ALA GLN TYR GLN PRO ILE LEU ARG ASP HIS ILE CYS LYS          
SEQRES  83 B 1256  ASP MET SER ALA LEU VAL ALA ALA ARG MET ARG HIS ILE          
SEQRES  84 B 1256  PRO LEU ALA PRO GLY SER ASP TRP ARG ASP LEU PRO ASN          
SEQRES  85 B 1256  ILE GLU VAL ARG LEU SER ASP GLY THR MET ALA ARG LYS          
SEQRES  86 B 1256  LEU ARG TYR THR HIS HIS ASP ARG LYS ASN GLY ARG SER          
SEQRES  87 B 1256  SER SER GLY ALA LEU ARG GLY VAL CYS SER CYS VAL GLU          
SEQRES  88 B 1256  ALA GLY LYS ALA CYS ASP PRO ALA ALA ARG GLN PHE ASN          
SEQRES  89 B 1256  THR LEU ILE PRO TRP CYS LEU PRO HIS THR GLY ASN ARG          
SEQRES  90 B 1256  HIS ASN HIS TRP ALA GLY LEU TYR GLY ARG LEU GLU TRP          
SEQRES  91 B 1256  ASP GLY PHE PHE SER THR THR VAL THR ASN PRO GLU PRO          
SEQRES  92 B 1256  MET GLY LYS GLN GLY ARG VAL LEU HIS PRO GLU GLN HIS          
SEQRES  93 B 1256  ARG VAL VAL SER VAL ARG GLU CYS ALA ARG SER GLN GLY          
SEQRES  94 B 1256  PHE PRO ASP THR TYR ARG LEU PHE GLY ASN ILE LEU ASP          
SEQRES  95 B 1256  LYS HIS ARG GLN VAL GLY ASN ALA VAL PRO PRO PRO LEU          
SEQRES  96 B 1256  ALA LYS ALA ILE GLY LEU GLU ILE LYS LEU CYS MET LEU          
SEQRES  97 B 1256  ALA LYS ALA LEU THR ARG VAL TRP                              
HET     ZN  A1701       1                                                       
HET     ZN  A1702       1                                                       
HET     ZN  A1703       1                                                       
HET     ZN  A1704       1                                                       
HET     ZN  A1705       1                                                       
HET    SAH  A1706      26                                                       
HET     ZN  B1701       1                                                       
HET     ZN  B1702       1                                                       
HET     ZN  B1703       1                                                       
HET     ZN  B1704       1                                                       
HET     ZN  B1705       1                                                       
HET    SAH  B1706      26                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     SAH S-ADENOSYL-L-HOMOCYSTEINE                                        
FORMUL   3   ZN    10(ZN 2+)                                                    
FORMUL   8  SAH    2(C14 H20 N6 O5 S)                                           
FORMUL  15  HOH   *637(H2 O)                                                    
HELIX    1 AA1 TYR A  495  ASN A  519  1                                  25    
HELIX    2 AA2 THR A  523  THR A  534  1                                  12    
HELIX    3 AA3 THR A  546  HIS A  553  1                                   8    
HELIX    4 AA4 HIS A  553  GLY A  568  1                                  16    
HELIX    5 AA5 PRO A  574  LEU A  577  5                                   4    
HELIX    6 AA6 THR A  578  ALA A  588  1                                  11    
HELIX    7 AA7 THR A  621  GLN A  635  1                                  15    
HELIX    8 AA8 CYS A  667  ASP A  672  1                                   6    
HELIX    9 AA9 CYS A  691  GLU A  704  1                                  14    
HELIX   10 AB1 THR A  801  THR A  803  5                                   3    
HELIX   11 AB2 LEU A  805  SER A  809  5                                   5    
HELIX   12 AB3 ASN A  842  GLU A  846  5                                   5    
HELIX   13 AB4 CYS A  893  GLU A  906  1                                  14    
HELIX   14 AB5 GLU A  971  TYR A  976  5                                   6    
HELIX   15 AB6 SER A 1030  TYR A 1035  5                                   6    
HELIX   16 AB7 LYS A 1054  VAL A 1056  5                                   3    
HELIX   17 AB8 CYS A 1071  MET A 1077  1                                   7    
HELIX   18 AB9 PRO A 1100  ARG A 1104  5                                   5    
HELIX   19 AC1 GLY A 1149  ALA A 1158  1                                  10    
HELIX   20 AC2 TRP A 1170  ASN A 1181  1                                  12    
HELIX   21 AC3 ASP A 1190  MET A 1199  1                                  10    
HELIX   22 AC4 ASN A 1236  ASN A 1245  1                                  10    
HELIX   23 AC5 SER A 1246  ARG A 1259  1                                  14    
HELIX   24 AC6 ASN A 1270  VAL A 1272  5                                   3    
HELIX   25 AC7 SER A 1273  GLY A 1291  1                                  19    
HELIX   26 AC8 GLY A 1302  GLY A 1305  5                                   4    
HELIX   27 AC9 ALA A 1335  CYS A 1339  5                                   5    
HELIX   28 AD1 THR A 1366  SER A 1372  1                                   7    
HELIX   29 AD2 SER A 1394  GLY A 1402  1                                   9    
HELIX   30 AD3 SER A 1418  HIS A 1427  1                                  10    
HELIX   31 AD4 ASP A 1435  LEU A 1439  5                                   5    
HELIX   32 AD5 CYS A 1476  GLU A 1480  5                                   5    
HELIX   33 AD6 TRP A 1498  GLY A 1504  1                                   7    
HELIX   34 AD7 ASN A 1505  ALA A 1511  5                                   7    
HELIX   35 AD8 SER A 1549  GLN A 1557  1                                   9    
HELIX   36 AD9 ASN A 1568  ALA A 1579  1                                  12    
HELIX   37 AE1 PRO A 1581  THR A 1602  1                                  22    
HELIX   38 AE2 THR B  382  SER B  387  1                                   6    
HELIX   39 AE3 TYR B  495  ASN B  519  1                                  25    
HELIX   40 AE4 THR B  523  THR B  533  1                                  11    
HELIX   41 AE5 THR B  546  HIS B  553  1                                   8    
HELIX   42 AE6 HIS B  553  GLY B  568  1                                  16    
HELIX   43 AE7 PRO B  574  LEU B  577  5                                   4    
HELIX   44 AE8 THR B  578  ALA B  588  1                                  11    
HELIX   45 AE9 THR B  621  GLU B  634  1                                  14    
HELIX   46 AF1 CYS B  667  ASP B  672  1                                   6    
HELIX   47 AF2 CYS B  691  GLU B  703  1                                  13    
HELIX   48 AF3 THR B  801  THR B  803  5                                   3    
HELIX   49 AF4 LEU B  805  SER B  809  5                                   5    
HELIX   50 AF5 SER B  826  ILE B  828  5                                   3    
HELIX   51 AF6 ASN B  842  GLU B  846  5                                   5    
HELIX   52 AF7 CYS B  893  GLU B  906  1                                  14    
HELIX   53 AF8 GLU B  971  TYR B  976  5                                   6    
HELIX   54 AF9 SER B 1030  SER B 1034  5                                   5    
HELIX   55 AG1 LYS B 1054  VAL B 1056  5                                   3    
HELIX   56 AG2 GLU B 1066  LEU B 1068  5                                   3    
HELIX   57 AG3 CYS B 1071  GLY B 1078  1                                   8    
HELIX   58 AG4 PRO B 1100  ARG B 1104  5                                   5    
HELIX   59 AG5 GLY B 1149  ALA B 1158  1                                  10    
HELIX   60 AG6 TRP B 1170  ASN B 1181  1                                  12    
HELIX   61 AG7 ASP B 1190  MET B 1199  1                                  10    
HELIX   62 AG8 ASN B 1236  ASN B 1245  1                                  10    
HELIX   63 AG9 SER B 1246  ARG B 1259  1                                  14    
HELIX   64 AH1 ASN B 1270  VAL B 1272  5                                   3    
HELIX   65 AH2 SER B 1273  GLY B 1291  1                                  19    
HELIX   66 AH3 GLY B 1302  GLY B 1305  5                                   4    
HELIX   67 AH4 ALA B 1335  CYS B 1339  5                                   5    
HELIX   68 AH5 THR B 1366  SER B 1372  1                                   7    
HELIX   69 AH6 SER B 1394  GLY B 1402  1                                   9    
HELIX   70 AH7 SER B 1418  HIS B 1427  1                                  10    
HELIX   71 AH8 ASP B 1435  LEU B 1439  5                                   5    
HELIX   72 AH9 CYS B 1476  GLU B 1480  5                                   5    
HELIX   73 AI1 TRP B 1498  GLY B 1504  1                                   7    
HELIX   74 AI2 ASN B 1505  ALA B 1511  5                                   7    
HELIX   75 AI3 SER B 1549  GLN B 1557  1                                   9    
HELIX   76 AI4 ASN B 1568  ALA B 1579  1                                  12    
HELIX   77 AI5 PRO B 1581  THR B 1602  1                                  22    
SHEET    1 AA1 7 ALA A 374  VAL A 375  0                                        
SHEET    2 AA1 7 VAL A 453  LEU A 458  1  O  ASN A 454   N  ALA A 374           
SHEET    3 AA1 7 PHE A 434  LYS A 440 -1  N  GLY A 437   O  GLY A 455           
SHEET    4 AA1 7 GLN A 404  TYR A 413 -1  N  TYR A 413   O  PHE A 434           
SHEET    5 AA1 7 GLU A 485  LEU A 488  1  O  ILE A 487   N  HIS A 405           
SHEET    6 AA1 7 ALA A 475  SER A 480 -1  N  PHE A 479   O  TYR A 486           
SHEET    7 AA1 7 TRP A 464  PHE A 469 -1  N  THR A 467   O  LEU A 476           
SHEET    1 AA2 3 SER A 732  VAL A 734  0                                        
SHEET    2 AA2 3 VAL A 750  ILE A 752 -1  O  ILE A 752   N  SER A 732           
SHEET    3 AA2 3 THR A 756  GLU A 758 -1  O  LEU A 757   N  CYS A 751           
SHEET    1 AA3 7 LYS A 739  THR A 740  0                                        
SHEET    2 AA3 7 TYR A 746  LYS A 748 -1  O  TYR A 747   N  LYS A 739           
SHEET    3 AA3 7 TYR A 775  GLU A 784 -1  O  LEU A 782   N  LYS A 748           
SHEET    4 AA3 7 GLN A 790  ALA A 799 -1  O  PHE A 797   N  LEU A 776           
SHEET    5 AA3 7 GLU A 813  GLN A 824 -1  O  GLU A 821   N  ALA A 794           
SHEET    6 AA3 7 TYR A 863  ASP A 870  1  O  PHE A 864   N  LEU A 814           
SHEET    7 AA3 7 VAL A 834  TYR A 836  1  N  ILE A 835   O  TYR A 863           
SHEET    1 AA4 7 ILE A 828  VAL A 832  0                                        
SHEET    2 AA4 7 CYS A 762  VAL A 765 -1  N  CYS A 762   O  VAL A 832           
SHEET    3 AA4 7 TYR A 775  GLU A 784 -1  O  TYR A 775   N  VAL A 765           
SHEET    4 AA4 7 GLN A 790  ALA A 799 -1  O  PHE A 797   N  LEU A 776           
SHEET    5 AA4 7 GLU A 813  GLN A 824 -1  O  GLU A 821   N  ALA A 794           
SHEET    6 AA4 7 TYR A 863  ASP A 870  1  O  PHE A 864   N  LEU A 814           
SHEET    7 AA4 7 ARG A 875  GLU A 877 -1  O  GLU A 877   N  TRP A 868           
SHEET    1 AA5 3 ARG A 909  VAL A 910  0                                        
SHEET    2 AA5 3 SER A 925  LYS A 928 -1  O  THR A 927   N  ARG A 909           
SHEET    3 AA5 3 ILE A 931  ARG A 934 -1  O  TYR A 933   N  ALA A 926           
SHEET    1 AA6 7 GLN A 913  ASP A 916  0                                        
SHEET    2 AA6 7 ARG A 920  TYR A 923 -1  O  LEU A 922   N  GLU A 915           
SHEET    3 AA6 7 ARG A 992  PRO A1002 -1  O  ILE A 999   N  TYR A 923           
SHEET    4 AA6 7 GLY A 938  LEU A 941 -1  N  LEU A 941   O  ARG A 992           
SHEET    5 AA6 7 GLY A1058  TYR A1064 -1  O  GLY A1058   N  TYR A 940           
SHEET    6 AA6 7 ARG A1082  ASN A1090  1  O  PHE A1083   N  THR A1061           
SHEET    7 AA6 7 SER A1095  GLU A1097 -1  O  GLU A1097   N  ALA A1088           
SHEET    1 AA7 7 GLN A 913  ASP A 916  0                                        
SHEET    2 AA7 7 ARG A 920  TYR A 923 -1  O  LEU A 922   N  GLU A 915           
SHEET    3 AA7 7 ARG A 992  PRO A1002 -1  O  ILE A 999   N  TYR A 923           
SHEET    4 AA7 7 LYS A1015  TYR A1022 -1  O  LYS A1015   N  PHE A1000           
SHEET    5 AA7 7 LEU A1041  ASP A1052 -1  O  ALA A1049   N  VAL A1018           
SHEET    6 AA7 7 ARG A1082  ASN A1090  1  O  TYR A1089   N  TRP A1044           
SHEET    7 AA7 7 SER A1095  GLU A1097 -1  O  GLU A1097   N  ALA A1088           
SHEET    1 AA8 7 THR A1185  PHE A1187  0                                        
SHEET    2 AA8 7 SER A1161  ILE A1167  1  N  ALA A1166   O  PHE A1187           
SHEET    3 AA8 7 LEU A1139  VAL A1144  1  N  LEU A1139   O  ASP A1162           
SHEET    4 AA8 7 MET A1219  GLY A1222  1  O  MET A1219   N  LEU A1142           
SHEET    5 AA8 7 PHE A1262  VAL A1268  1  O  PHE A1262   N  LEU A1220           
SHEET    6 AA8 7 ARG A1311  ALA A1318 -1  O  ALA A1317   N  PHE A1263           
SHEET    7 AA8 7 GLN A1293  GLN A1300 -1  N  GLY A1297   O  ILE A1314           
SHEET    1 AA9 2 VAL A1343  VAL A1345  0                                        
SHEET    2 AA9 2 LYS A1348  PHE A1350 -1  O  PHE A1350   N  VAL A1343           
SHEET    1 AB1 2 GLU A1385  ILE A1386  0                                        
SHEET    2 AB1 2 LEU A1409  ARG A1410 -1  O  LEU A1409   N  ILE A1386           
SHEET    1 AB2 2 VAL A1444  ARG A1445  0                                        
SHEET    2 AB2 2 MET A1451  ALA A1452 -1  O  ALA A1452   N  VAL A1444           
SHEET    1 AB3 6 VAL B 453  LEU B 458  0                                        
SHEET    2 AB3 6 PHE B 434  PRO B 441 -1  N  PHE B 435   O  LEU B 458           
SHEET    3 AB3 6 GLN B 404  TYR B 413 -1  N  TYR B 413   O  PHE B 434           
SHEET    4 AB3 6 GLU B 485  LEU B 488  1  O  ILE B 487   N  HIS B 405           
SHEET    5 AB3 6 ALA B 475  SER B 480 -1  N  PHE B 479   O  TYR B 486           
SHEET    6 AB3 6 GLU B 463  PHE B 469 -1  N  THR B 467   O  LEU B 476           
SHEET    1 AB4 3 SER B 732  VAL B 734  0                                        
SHEET    2 AB4 3 VAL B 750  ILE B 752 -1  O  ILE B 752   N  SER B 732           
SHEET    3 AB4 3 THR B 756  GLU B 758 -1  O  LEU B 757   N  CYS B 751           
SHEET    1 AB5 7 LYS B 739  THR B 740  0                                        
SHEET    2 AB5 7 TYR B 746  LYS B 748 -1  O  TYR B 747   N  LYS B 739           
SHEET    3 AB5 7 LEU B 782  GLU B 784 -1  O  LEU B 782   N  LYS B 748           
SHEET    4 AB5 7 GLN B 790  ALA B 799 -1  O  MET B 791   N  TRP B 783           
SHEET    5 AB5 7 GLU B 813  GLN B 824 -1  O  MET B 823   N  PHE B 792           
SHEET    6 AB5 7 TYR B 863  ASP B 870  1  O  PHE B 864   N  LEU B 814           
SHEET    7 AB5 7 VAL B 834  TYR B 836  1  N  ILE B 835   O  TYR B 863           
SHEET    1 AB6 7 SER B 830  VAL B 832  0                                        
SHEET    2 AB6 7 CYS B 762  VAL B 765 -1  N  SER B 764   O  SER B 830           
SHEET    3 AB6 7 TYR B 775  VAL B 779 -1  O  TYR B 775   N  VAL B 765           
SHEET    4 AB6 7 GLN B 790  ALA B 799 -1  O  PHE B 797   N  LEU B 776           
SHEET    5 AB6 7 GLU B 813  GLN B 824 -1  O  MET B 823   N  PHE B 792           
SHEET    6 AB6 7 TYR B 863  ASP B 870  1  O  PHE B 864   N  LEU B 814           
SHEET    7 AB6 7 ARG B 875  GLU B 877 -1  O  GLU B 877   N  TRP B 868           
SHEET    1 AB7 3 ARG B 909  VAL B 910  0                                        
SHEET    2 AB7 3 SER B 925  LYS B 928 -1  O  THR B 927   N  ARG B 909           
SHEET    3 AB7 3 ILE B 931  ARG B 934 -1  O  TYR B 933   N  ALA B 926           
SHEET    1 AB8 7 GLN B 913  ASP B 916  0                                        
SHEET    2 AB8 7 ARG B 920  TYR B 923 -1  O  LEU B 922   N  LEU B 914           
SHEET    3 AB8 7 ARG B 992  PRO B1002 -1  O  ILE B 999   N  TYR B 923           
SHEET    4 AB8 7 GLY B 938  LEU B 941 -1  N  LEU B 941   O  ARG B 992           
SHEET    5 AB8 7 GLY B1058  TYR B1064 -1  O  GLY B1058   N  TYR B 940           
SHEET    6 AB8 7 ARG B1082  ASN B1090  1  O  PHE B1083   N  THR B1061           
SHEET    7 AB8 7 SER B1095  GLU B1097 -1  O  GLU B1097   N  ALA B1088           
SHEET    1 AB9 7 GLN B 913  ASP B 916  0                                        
SHEET    2 AB9 7 ARG B 920  TYR B 923 -1  O  LEU B 922   N  LEU B 914           
SHEET    3 AB9 7 ARG B 992  PRO B1002 -1  O  ILE B 999   N  TYR B 923           
SHEET    4 AB9 7 LYS B1015  TYR B1022 -1  O  LYS B1015   N  PHE B1000           
SHEET    5 AB9 7 LEU B1041  ASP B1052 -1  O  ALA B1049   N  VAL B1018           
SHEET    6 AB9 7 ARG B1082  ASN B1090  1  O  TYR B1089   N  TRP B1044           
SHEET    7 AB9 7 SER B1095  GLU B1097 -1  O  GLU B1097   N  ALA B1088           
SHEET    1 AC1 7 THR B1185  PHE B1187  0                                        
SHEET    2 AC1 7 SER B1161  ILE B1167  1  N  LEU B1164   O  THR B1185           
SHEET    3 AC1 7 LEU B1139  VAL B1144  1  N  ASP B1143   O  TRP B1165           
SHEET    4 AC1 7 MET B1219  GLY B1222  1  O  MET B1219   N  LEU B1142           
SHEET    5 AC1 7 PHE B1262  VAL B1268  1  O  LEU B1264   N  LEU B1220           
SHEET    6 AC1 7 ARG B1311  ALA B1318 -1  O  ILE B1315   N  LEU B1265           
SHEET    7 AC1 7 GLN B1293  GLN B1300 -1  N  GLY B1297   O  ILE B1314           
SHEET    1 AC2 2 VAL B1343  VAL B1345  0                                        
SHEET    2 AC2 2 LYS B1348  PHE B1350 -1  O  PHE B1350   N  VAL B1343           
SHEET    1 AC3 2 GLU B1385  ILE B1386  0                                        
SHEET    2 AC3 2 LEU B1409  ARG B1410 -1  O  LEU B1409   N  ILE B1386           
SHEET    1 AC4 2 VAL B1444  ARG B1445  0                                        
SHEET    2 AC4 2 MET B1451  ALA B1452 -1  O  ALA B1452   N  VAL B1444           
LINK         SG  CYS A 353                ZN    ZN A1705     1555   1555  2.45  
LINK         SG  CYS A 356                ZN    ZN A1705     1555   1555  2.42  
LINK         SG  CYS A 414                ZN    ZN A1705     1555   1555  2.43  
LINK         ND1 HIS A 418                ZN    ZN A1705     1555   1555  2.18  
LINK         SG  CYS A 653                ZN    ZN A1704     1555   1555  2.29  
LINK         SG  CYS A 656                ZN    ZN A1704     1555   1555  2.33  
LINK         SG  CYS A 659                ZN    ZN A1704     1555   1555  2.39  
LINK         SG  CYS A 664                ZN    ZN A1703     1555   1555  2.39  
LINK         SG  CYS A 667                ZN    ZN A1703     1555   1555  2.40  
LINK         SG  CYS A 670                ZN    ZN A1703     1555   1555  2.42  
LINK         SG  CYS A 686                ZN    ZN A1703     1555   1555  2.59  
LINK         SG  CYS A 691                ZN    ZN A1704     1555   1555  2.39  
LINK         NE2 HIS A 793                ZN    ZN A1702     1555   1555  2.17  
LINK         SG  CYS A 820                ZN    ZN A1702     1555   1555  2.39  
LINK         SG  CYS A 893                ZN    ZN A1702     1555   1555  2.35  
LINK         SG  CYS A 896                ZN    ZN A1702     1555   1555  2.42  
LINK         SG  CYS A1476                ZN    ZN A1701     1555   1555  2.41  
LINK         SG  CYS A1478                ZN    ZN A1701     1555   1555  2.33  
LINK         SG  CYS A1485                ZN    ZN A1701     1555   1555  2.42  
LINK         NE2 HIS A1502                ZN    ZN A1701     1555   1555  2.12  
LINK         SG  CYS B 353                ZN    ZN B1705     1555   1555  2.52  
LINK         SG  CYS B 356                ZN    ZN B1705     1555   1555  2.40  
LINK         SG  CYS B 414                ZN    ZN B1705     1555   1555  2.63  
LINK         ND1 HIS B 418                ZN    ZN B1705     1555   1555  2.19  
LINK         SG  CYS B 653                ZN    ZN B1704     1555   1555  2.27  
LINK         SG  CYS B 656                ZN    ZN B1704     1555   1555  2.32  
LINK         SG  CYS B 659                ZN    ZN B1704     1555   1555  2.40  
LINK         SG  CYS B 664                ZN    ZN B1703     1555   1555  2.37  
LINK         SG  CYS B 667                ZN    ZN B1703     1555   1555  2.40  
LINK         SG  CYS B 670                ZN    ZN B1703     1555   1555  2.40  
LINK         SG  CYS B 686                ZN    ZN B1703     1555   1555  2.43  
LINK         SG  CYS B 691                ZN    ZN B1704     1555   1555  2.45  
LINK         NE2 HIS B 793                ZN    ZN B1702     1555   1555  2.20  
LINK         SG  CYS B 820                ZN    ZN B1702     1555   1555  2.36  
LINK         SG  CYS B 893                ZN    ZN B1702     1555   1555  2.30  
LINK         SG  CYS B 896                ZN    ZN B1702     1555   1555  2.39  
LINK         SG  CYS B1476                ZN    ZN B1701     1555   1555  2.41  
LINK         SG  CYS B1478                ZN    ZN B1701     1555   1555  2.43  
LINK         SG  CYS B1485                ZN    ZN B1701     1555   1555  2.39  
LINK         NE2 HIS B1502                ZN    ZN B1701     1555   1555  2.15  
CISPEP   1 ASP A  362    PRO A  363          0        -4.06                     
CISPEP   2 PRO A  371    PRO A  372          0        -7.34                     
CISPEP   3 GLU A  450    GLY A  451          0         1.66                     
CISPEP   4 GLY A  459    PRO A  460          0         3.17                     
CISPEP   5 GLY A  471    GLY A  472          0         0.08                     
CISPEP   6 GLY A  472    GLU A  473          0        -1.29                     
CISPEP   7 PHE A  676    GLY A  677          0         0.36                     
CISPEP   8 ASP A  706    ASP A  707          0        -1.12                     
CISPEP   9 GLU A  711    MET A  712          0         7.28                     
CISPEP  10 GLU A  856    GLY A  857          0         2.59                     
CISPEP  11 ASP A  859    GLY A  860          0        -2.70                     
CISPEP  12 LEU B  360    ASP B  361          0        -8.06                     
CISPEP  13 PRO B  371    PRO B  372          0        23.30                     
CISPEP  14 PRO B  378    GLN B  379          0        -7.20                     
CISPEP  15 GLY B  459    PRO B  460          0         3.19                     
CISPEP  16 GLY B  471    GLY B  472          0        -0.37                     
CISPEP  17 GLY B  472    GLU B  473          0        -1.23                     
CISPEP  18 PHE B  676    GLY B  677          0        -0.29                     
CISPEP  19 SER B  679    GLY B  680          0        -4.05                     
CISPEP  20 ASP B  706    ASP B  707          0        -0.84                     
CISPEP  21 GLU B  711    MET B  712          0         2.03                     
CISPEP  22 GLU B  856    GLY B  857          0        -1.28                     
CISPEP  23 ASP B  859    GLY B  860          0         4.71                     
SITE     1 AC1  4 CYS A1476  CYS A1478  CYS A1485  HIS A1502                    
SITE     1 AC2  4 HIS A 793  CYS A 820  CYS A 893  CYS A 896                    
SITE     1 AC3  5 CYS A 664  GLY A 665  CYS A 667  CYS A 670                    
SITE     2 AC3  5 CYS A 686                                                     
SITE     1 AC4  5 CYS A 653  GLY A 654  CYS A 656  CYS A 659                    
SITE     2 AC4  5 CYS A 691                                                     
SITE     1 AC5  4 CYS A 353  CYS A 356  CYS A 414  HIS A 418                    
SITE     1 AC6 19 PHE A1145  SER A1146  GLY A1147  CYS A1148                    
SITE     2 AC6 19 GLY A1150  LEU A1151  GLU A1168  MET A1169                    
SITE     3 AC6 19 TRP A1170  GLU A1189  ASP A1190  CYS A1191                    
SITE     4 AC6 19 GLY A1223  LEU A1247  ASN A1578  ALA A1579                    
SITE     5 AC6 19 VAL A1580  HOH A1918  HOH A2051                               
SITE     1 AC7  4 CYS B1476  CYS B1478  CYS B1485  HIS B1502                    
SITE     1 AC8  4 HIS B 793  CYS B 820  CYS B 893  CYS B 896                    
SITE     1 AC9  6 CYS B 664  GLY B 665  CYS B 667  CYS B 670                    
SITE     2 AC9  6 CYS B 686  GLN B 687                                          
SITE     1 AD1  5 CYS B 653  GLY B 654  CYS B 656  CYS B 659                    
SITE     2 AD1  5 CYS B 691                                                     
SITE     1 AD2  4 CYS B 353  CYS B 356  CYS B 414  HIS B 418                    
SITE     1 AD3 17 PHE B1145  SER B1146  GLY B1147  GLY B1150                    
SITE     2 AD3 17 LEU B1151  GLU B1168  MET B1169  TRP B1170                    
SITE     3 AD3 17 GLU B1189  ASP B1190  CYS B1191  GLY B1223                    
SITE     4 AD3 17 LEU B1247  ASN B1578  ALA B1579  VAL B1580                    
SITE     5 AD3 17 HOH B1974                                                     
CRYST1  138.568  138.568  221.536  90.00  90.00  90.00 P 43          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      0.007217  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007217  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004514        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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