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Database: PDB
Entry: 5WVO
LinkDB: 5WVO
Original site: 5WVO 
HEADER    SIGNALING PROTEIN/TRANSFERASE           28-DEC-16   5WVO              
TITLE     CRYSTAL STRUCTURE OF DNMT1 RFTS DOMAIN IN COMPLEX WITH K18/K23 MONO-  
TITLE    2 UBIQUITYLATED HISTONE H3                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UBIQUITIN;                                                 
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES;                                                       
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: DNA (CYTOSINE-5)-METHYLTRANSFERASE 1;                      
COMPND   8 CHAIN: C;                                                            
COMPND   9 FRAGMENT: RFTS DOMAIN, UNP RESIDUES 351-600;                         
COMPND  10 SYNONYM: DNMT1,CXXC-TYPE ZINC FINGER PROTEIN 9,DNA METHYLTRANSFERASE 
COMPND  11 HSAI,M.HSAI,MCMT;                                                    
COMPND  12 EC: 2.1.1.37;                                                        
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MOL_ID: 3;                                                           
COMPND  15 MOLECULE: HISTONE H3.1;                                              
COMPND  16 CHAIN: D;                                                            
COMPND  17 FRAGMENT: UNP RESIDUES 2-37;                                         
COMPND  18 SYNONYM: HISTONE H3/A,HISTONE H3/B,HISTONE H3/C,HISTONE H3/D,HISTONE 
COMPND  19 H3/F,HISTONE H3/H,HISTONE H3/I,HISTONE H3/J,HISTONE H3/K,HISTONE     
COMPND  20 H3/L;                                                                
COMPND  21 ENGINEERED: YES;                                                     
COMPND  22 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: RPS27A, UBA80, UBCEP1;                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI-PICHIA PASTORIS SHUTTLE VECTOR   
SOURCE   7 PPPT4;                                                               
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 1182041;                                    
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PET22B;                                   
SOURCE  12 MOL_ID: 2;                                                           
SOURCE  13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  14 ORGANISM_COMMON: HUMAN;                                              
SOURCE  15 ORGANISM_TAXID: 9606;                                                
SOURCE  16 GENE: DNMT1, AIM, CXXC9, DNMT;                                       
SOURCE  17 EXPRESSION_SYSTEM: ESCHERICHIA COLI-PICHIA PASTORIS SHUTTLE VECTOR   
SOURCE  18 PPPT4;                                                               
SOURCE  19 EXPRESSION_SYSTEM_TAXID: 1182041;                                    
SOURCE  20 EXPRESSION_SYSTEM_STRAIN: ROSETTA2 (DE3);                            
SOURCE  21 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  22 EXPRESSION_SYSTEM_PLASMID: MODIFIED PGEX4T VECTOR;                   
SOURCE  23 MOL_ID: 3;                                                           
SOURCE  24 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  25 ORGANISM_COMMON: HUMAN;                                              
SOURCE  26 ORGANISM_TAXID: 9606;                                                
SOURCE  27 GENE: HIST1H3A, H3FA, HIST1H3B, H3FL, HIST1H3C, H3FC, HIST1H3D,      
SOURCE  28 H3FB, HIST1H3E, H3FD, HIST1H3F, H3FI, HIST1H3G, H3FH, HIST1H3H,      
SOURCE  29 H3FK, HIST1H3I, H3FF, HIST1H3J, H3FJ;                                
SOURCE  30 EXPRESSION_SYSTEM: ESCHERICHIA COLI-PICHIA PASTORIS SHUTTLE VECTOR   
SOURCE  31 PPPT4;                                                               
SOURCE  32 EXPRESSION_SYSTEM_TAXID: 1182041;                                    
SOURCE  33 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  34 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  35 EXPRESSION_SYSTEM_PLASMID: MODIFIED PGEX4T                           
KEYWDS    DNA METHYLATION, UBIQUITINATION, SIGNALING PROTEIN-TRANSFERASE        
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.ISHIYAMA,A.NISHIYAMA,M.NAKANISHI,K.ARITA                            
REVDAT   1   15-NOV-17 5WVO    0                                                
JRNL        AUTH   S.ISHIYAMA,A.NISHIYAMA,Y.SAEKI,K.MORITSUGU,D.MORIMOTO,       
JRNL        AUTH 2 L.YAMAGUCHI,N.ARAI,R.MATSUMURA,T.KAWAKAMI,Y.MISHIMA,H.HOJO,  
JRNL        AUTH 3 S.SHIMAMURA,F.ISHIKAWA,S.TAJIMA,K.TANAKA,M.ARIYOSHI,         
JRNL        AUTH 4 M.SHIRAKAWA,M.IKEGUCHI,A.KIDERA,I.SUETAKE,K.ARITA,           
JRNL        AUTH 5 M.NAKANISHI                                                  
JRNL        TITL   STRUCTURE OF THE DNMT1 READER MODULE COMPLEXED WITH A UNIQUE 
JRNL        TITL 2 TWO-MONO-UBIQUITIN MARK ON HISTONE H3 REVEALS THE BASIS FOR  
JRNL        TITL 3 DNA METHYLATION MAINTENANCE                                  
JRNL        REF    MOL. CELL                     V.  68   350 2017              
JRNL        REFN                   ISSN 1097-4164                               
JRNL        PMID   29053958                                                     
JRNL        DOI    10.1016/J.MOLCEL.2017.09.037                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10.1_2155: ???)                            
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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.18                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 35890                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.198                           
REMARK   3   R VALUE            (WORKING SET) : 0.196                           
REMARK   3   FREE R VALUE                     : 0.239                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.170                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1855                            
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 34.1860 -  4.6918    0.99     2773   153  0.1741 0.1889        
REMARK   3     2  4.6918 -  3.7255    1.00     2692   124  0.1525 0.1874        
REMARK   3     3  3.7255 -  3.2550    1.00     2642   141  0.1821 0.2276        
REMARK   3     4  3.2550 -  2.9575    1.00     2641   131  0.2099 0.2481        
REMARK   3     5  2.9575 -  2.7457    1.00     2634   151  0.2165 0.2823        
REMARK   3     6  2.7457 -  2.5838    1.00     2612   147  0.2198 0.2452        
REMARK   3     7  2.5838 -  2.4545    1.00     2597   137  0.2130 0.3036        
REMARK   3     8  2.4545 -  2.3477    1.00     2585   172  0.2200 0.2814        
REMARK   3     9  2.3477 -  2.2573    1.00     2606   143  0.2163 0.2199        
REMARK   3    10  2.2573 -  2.1794    1.00     2598   136  0.2260 0.2982        
REMARK   3    11  2.1794 -  2.1113    1.00     2598   128  0.2312 0.2896        
REMARK   3    12  2.1113 -  2.0509    1.00     2580   154  0.2450 0.3164        
REMARK   3    13  2.0509 -  1.9969    0.96     2477   138  0.2456 0.2723        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
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)     : 0.220            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.850           
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      :  0.019           3237                                  
REMARK   3   ANGLE     :  0.934           4378                                  
REMARK   3   CHIRALITY :  0.063            496                                  
REMARK   3   PLANARITY :  0.006            576                                  
REMARK   3   DIHEDRAL  : 17.912           1980                                  
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 5WVO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-JAN-17.                  
REMARK 100 THE DEPOSITION ID IS D_1300002411.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-NOV-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 93                                 
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-5A                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 2M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 35892                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.997                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 34.181                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 6.400                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.03                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.70600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 1UBQ, 3EPZ                                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.43                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.89                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM BIS-TRIS (PH 6.0), 200MM LITHIUM   
REMARK 280  SULFATE MONOHYDRATE, 20% PEG 10000, VAPOR DIFFUSION, HANGING        
REMARK 280  DROP, TEMPERATURE 277K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
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   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       38.45200            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       38.45200            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       34.18100            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       99.38950            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       34.18100            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       99.38950            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       38.45200            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       34.18100            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       99.38950            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       38.45200            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       34.18100            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       99.38950            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6780 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18150 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     PRO C   351                                                      
REMARK 465     LYS C   352                                                      
REMARK 465     GLN C   358                                                      
REMARK 465     TYR C   359                                                      
REMARK 465     LEU C   360                                                      
REMARK 465     ASP C   361                                                      
REMARK 465     ASP C   362                                                      
REMARK 465     PRO C   363                                                      
REMARK 465     ASP C   364                                                      
REMARK 465     LEU C   592                                                      
REMARK 465     GLY C   593                                                      
REMARK 465     GLN C   594                                                      
REMARK 465     ARG C   595                                                      
REMARK 465     ARG C   596                                                      
REMARK 465     ALA C   597                                                      
REMARK 465     GLN C   598                                                      
REMARK 465     ALA C   599                                                      
REMARK 465     ARG C   600                                                      
REMARK 465     ALA D     1                                                      
REMARK 465     ALA D    21                                                      
REMARK 465     THR D    22                                                      
REMARK 465     CYS D    23                                                      
REMARK 465     ALA D    24                                                      
REMARK 465     ALA D    25                                                      
REMARK 465     ARG D    26                                                      
REMARK 465     LYS D    27                                                      
REMARK 465     SER D    28                                                      
REMARK 465     ALA D    29                                                      
REMARK 465     PRO D    30                                                      
REMARK 465     ALA D    31                                                      
REMARK 465     THR D    32                                                      
REMARK 465     GLY D    33                                                      
REMARK 465     GLY D    34                                                      
REMARK 465     VAL D    35                                                      
REMARK 465     LYS D    36                                                      
REMARK 465     TRP D    37                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A  63    CD   CE   NZ                                        
REMARK 470     ILE C 354    CG1  CD1                                            
REMARK 470     LYS C 366    CD   CE   NZ                                        
REMARK 470     TYR C 367    CD1  CD2  CE1  CE2  CZ   OH                         
REMARK 470     LYS C 415    CD   CE   NZ                                        
REMARK 470     SER C 520    OG                                                  
REMARK 470     ASP C 521    CG   OD1  OD2                                       
REMARK 470     SER C 522    OG                                                  
REMARK 470     GLN C 573    CG   CD   OE1  NE2                                  
REMARK 470     LEU D  20    CG   CD1  CD2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH C   852     O    HOH C   883              2.00            
REMARK 500   OD2  ASP C   548     NH1  ARG C   552              2.12            
REMARK 500   O    HOH A   127     O    HOH A   153              2.13            
REMARK 500   NH1  ARG A    54     O    HOH A   101              2.17            
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 C 355      -62.82   -106.18                                   
REMARK 500    CYS C 356      -88.98    -48.03                                   
REMARK 500    LYS C 415       -6.20    -49.26                                   
REMARK 500    HIS C 416       49.41   -152.56                                   
REMARK 500    MET C 489     -107.71   -109.17                                   
REMARK 500    ASN C 519       60.90   -150.84                                   
REMARK 500    SER C 570       26.37    -65.85                                   
REMARK 500    ASP C 571       17.25   -141.16                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 HIS C  416     GLY C  417                  148.15                    
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 C 701  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 353   SG                                                     
REMARK 620 2 CYS C 414   SG  104.3                                              
REMARK 620 3 HIS C 418   ND1 115.6  83.4                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 701                  
DBREF  5WVO A    1    76  UNP    P62979   RS27A_HUMAN      1     76             
DBREF  5WVO B    1    76  UNP    P62979   RS27A_HUMAN      1     76             
DBREF  5WVO C  351   600  UNP    P26358   DNMT1_HUMAN    351    600             
DBREF  5WVO D    1    36  UNP    P68431   H31_HUMAN        2     37             
SEQADV 5WVO CYS A   76  UNP  P62979    GLY    76 ENGINEERED MUTATION            
SEQADV 5WVO CYS B   76  UNP  P62979    GLY    76 ENGINEERED MUTATION            
SEQADV 5WVO CYS D   18  UNP  P68431    LYS    19 ENGINEERED MUTATION            
SEQADV 5WVO CYS D   23  UNP  P68431    LYS    24 ENGINEERED MUTATION            
SEQADV 5WVO TRP D   37  UNP  P68431              EXPRESSION TAG                 
SEQRES   1 A   76  MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE          
SEQRES   2 A   76  THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL          
SEQRES   3 A   76  LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP          
SEQRES   4 A   76  GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP          
SEQRES   5 A   76  GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER          
SEQRES   6 A   76  THR LEU HIS LEU VAL LEU ARG LEU ARG GLY CYS                  
SEQRES   1 B   76  MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE          
SEQRES   2 B   76  THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL          
SEQRES   3 B   76  LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP          
SEQRES   4 B   76  GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP          
SEQRES   5 B   76  GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER          
SEQRES   6 B   76  THR LEU HIS LEU VAL LEU ARG LEU ARG GLY CYS                  
SEQRES   1 C  250  PRO LYS CYS ILE GLN CYS GLY GLN TYR LEU ASP ASP PRO          
SEQRES   2 C  250  ASP LEU LYS TYR GLY GLN HIS PRO PRO ASP ALA VAL ASP          
SEQRES   3 C  250  GLU PRO GLN MET LEU THR ASN GLU LYS LEU SER ILE PHE          
SEQRES   4 C  250  ASP ALA ASN GLU SER GLY PHE GLU SER TYR GLU ALA LEU          
SEQRES   5 C  250  PRO GLN HIS LYS LEU THR CYS PHE SER VAL TYR CYS LYS          
SEQRES   6 C  250  HIS GLY HIS LEU CYS PRO ILE ASP THR GLY LEU ILE GLU          
SEQRES   7 C  250  LYS ASN ILE GLU LEU PHE PHE SER GLY SER ALA LYS PRO          
SEQRES   8 C  250  ILE TYR ASP ASP ASP PRO SER LEU GLU GLY GLY VAL ASN          
SEQRES   9 C  250  GLY LYS ASN LEU GLY PRO ILE ASN GLU TRP TRP ILE THR          
SEQRES  10 C  250  GLY PHE ASP GLY GLY GLU LYS ALA LEU ILE GLY PHE SER          
SEQRES  11 C  250  THR SER PHE ALA GLU TYR ILE LEU MET ASP PRO SER PRO          
SEQRES  12 C  250  GLU TYR ALA PRO ILE PHE GLY LEU MET GLN GLU LYS ILE          
SEQRES  13 C  250  TYR ILE SER LYS ILE VAL VAL GLU PHE LEU GLN SER ASN          
SEQRES  14 C  250  SER ASP SER THR TYR GLU ASP LEU ILE ASN LYS ILE GLU          
SEQRES  15 C  250  THR THR VAL PRO PRO SER GLY LEU ASN LEU ASN ARG PHE          
SEQRES  16 C  250  THR GLU ASP SER LEU LEU ARG HIS ALA GLN PHE VAL VAL          
SEQRES  17 C  250  GLU GLN VAL GLU SER TYR ASP GLU ALA GLY ASP SER ASP          
SEQRES  18 C  250  GLU GLN PRO ILE PHE LEU THR PRO CYS MET ARG ASP LEU          
SEQRES  19 C  250  ILE LYS LEU ALA GLY VAL THR LEU GLY GLN ARG ARG ALA          
SEQRES  20 C  250  GLN ALA ARG                                                  
SEQRES   1 D   37  ALA ARG THR LYS GLN THR ALA ARG LYS SER THR GLY GLY          
SEQRES   2 D   37  LYS ALA PRO ARG CYS GLN LEU ALA THR CYS ALA ALA ARG          
SEQRES   3 D   37  LYS SER ALA PRO ALA THR GLY GLY VAL LYS TRP                  
HET     ZN  C 701       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL   5   ZN    ZN 2+                                                        
FORMUL   6  HOH   *197(H2 O)                                                    
HELIX    1 AA1 THR A   22  GLY A   35  1                                  14    
HELIX    2 AA2 PRO A   37  ASP A   39  5                                   3    
HELIX    3 AA3 THR A   55  ASN A   60  1                                   6    
HELIX    4 AA4 THR B   22  GLY B   35  1                                  14    
HELIX    5 AA5 PRO B   37  ASP B   39  5                                   3    
HELIX    6 AA6 ASP C  376  THR C  382  1                                   7    
HELIX    7 AA7 ASN C  383  SER C  387  5                                   5    
HELIX    8 AA8 TYR C  495  ASN C  519  1                                  25    
HELIX    9 AA9 THR C  523  THR C  534  1                                  12    
HELIX   10 AB1 THR C  546  ARG C  552  1                                   7    
HELIX   11 AB2 HIS C  553  ALA C  567  1                                  15    
HELIX   12 AB3 THR C  578  GLY C  589  1                                  12    
SHEET    1 AA1 5 THR A  12  GLU A  16  0                                        
SHEET    2 AA1 5 GLN A   2  THR A   7 -1  N  VAL A   5   O  ILE A  13           
SHEET    3 AA1 5 THR A  66  LEU A  71  1  O  LEU A  67   N  LYS A   6           
SHEET    4 AA1 5 GLN A  41  PHE A  45 -1  N  ARG A  42   O  VAL A  70           
SHEET    5 AA1 5 LYS A  48  GLN A  49 -1  O  LYS A  48   N  PHE A  45           
SHEET    1 AA2 5 THR B  12  GLU B  16  0                                        
SHEET    2 AA2 5 GLN B   2  THR B   7 -1  N  VAL B   5   O  ILE B  13           
SHEET    3 AA2 5 THR B  66  LEU B  71  1  O  LEU B  67   N  PHE B   4           
SHEET    4 AA2 5 GLN B  41  PHE B  45 -1  N  ARG B  42   O  VAL B  70           
SHEET    5 AA2 5 LYS B  48  GLN B  49 -1  O  LYS B  48   N  PHE B  45           
SHEET    1 AA3 7 VAL C 453  LEU C 458  0                                        
SHEET    2 AA3 7 LEU C 433  LYS C 440 -1  N  GLY C 437   O  GLY C 455           
SHEET    3 AA3 7 GLN C 404  CYS C 414 -1  N  THR C 408   O  SER C 438           
SHEET    4 AA3 7 GLU C 485  LEU C 488  1  O  ILE C 487   N  HIS C 405           
SHEET    5 AA3 7 LEU C 476  SER C 480 -1  N  ILE C 477   O  LEU C 488           
SHEET    6 AA3 7 GLU C 463  THR C 467 -1  N  GLU C 463   O  SER C 480           
SHEET    7 AA3 7 LYS D   9  LYS D  14 -1  O  SER D  10   N  ILE C 466           
SSBOND   1 CYS B   76    CYS D   18                          1555   1555  2.05  
LINK         SG  CYS C 353                ZN    ZN C 701     1555   1555  2.62  
LINK         SG  CYS C 414                ZN    ZN C 701     1555   1555  2.68  
LINK         ND1 HIS C 418                ZN    ZN C 701     1555   1555  2.39  
CISPEP   1 GLY C  459    PRO C  460          0         9.22                     
SITE     1 AC1  4 CYS C 353  CYS C 356  CYS C 414  HIS C 418                    
CRYST1   68.362  198.779   76.904  90.00  90.00  90.00 C 2 2 21     16          
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      0.014628  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005031  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013003        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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