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Database: PDB
Entry: 4NM6
LinkDB: 4NM6
Original site: 4NM6 
HEADER    OXIDOREDUCTASE/DNA                      14-NOV-13   4NM6              
TITLE     CRYSTAL STRUCTURE OF TET2-DNA COMPLEX                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: METHYLCYTOSINE DIOXYGENASE TET2;                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: SEE REMARK 999;                                            
COMPND   5 EC: 1.14.11.-;                                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: 5'-D(*AP*CP*CP*AP*CP*(5CM)P*GP*GP*TP*GP*GP*T)-3';          
COMPND   9 CHAIN: B, C;                                                         
COMPND  10 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: TET2, KIAA1546, NBLA00191;                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES                                                       
KEYWDS    DNA HYDROXYLATION, OXIDOREDUCTASE-DNA COMPLEX                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.HU,Z.LI,J.CHENG,Q.RAO,W.GONG,M.LIU,P.WANG,Y.XU                      
REVDAT   3   26-JUL-17 4NM6    1       SOURCE                                   
REVDAT   2   15-JAN-14 4NM6    1       JRNL                                     
REVDAT   1   18-DEC-13 4NM6    0                                                
JRNL        AUTH   L.HU,Z.LI,J.CHENG,Q.RAO,W.GONG,M.LIU,Y.G.SHI,J.ZHU,P.WANG,   
JRNL        AUTH 2 Y.XU                                                         
JRNL        TITL   CRYSTAL STRUCTURE OF TET2-DNA COMPLEX: INSIGHT INTO          
JRNL        TITL 2 TET-MEDIATED 5MC OXIDATION.                                  
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V. 155  1545 2013              
JRNL        REFN                   ISSN 0092-8674                               
JRNL        PMID   24315485                                                     
JRNL        DOI    10.1016/J.CELL.2013.11.020                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.03 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8_1069)                     
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) : 2.03                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.81                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 34834                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.204                           
REMARK   3   R VALUE            (WORKING SET) : 0.202                           
REMARK   3   FREE R VALUE                     : 0.243                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.970                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1731                            
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 41.8137 -  4.6372    0.91     2857   137  0.1930 0.2220        
REMARK   3     2  4.6372 -  3.6814    0.95     2801   164  0.1818 0.2041        
REMARK   3     3  3.6814 -  3.2162    0.96     2822   159  0.2028 0.2606        
REMARK   3     4  3.2162 -  2.9223    0.95     2799   154  0.2147 0.2572        
REMARK   3     5  2.9223 -  2.7128    0.96     2809   158  0.2261 0.2748        
REMARK   3     6  2.7128 -  2.5529    0.96     2799   162  0.2279 0.2677        
REMARK   3     7  2.5529 -  2.4251    0.95     2766   123  0.2083 0.2784        
REMARK   3     8  2.4251 -  2.3195    0.95     2799   123  0.2164 0.2668        
REMARK   3     9  2.3195 -  2.2302    0.93     2712   129  0.2203 0.2527        
REMARK   3    10  2.2302 -  2.1533    0.93     2710   133  0.2152 0.2826        
REMARK   3    11  2.1533 -  2.0860    0.92     2624   156  0.2119 0.2914        
REMARK   3    12  2.0860 -  2.0260    0.90     2605   133  0.2149 0.2766        
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)     : 0.230            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.230           
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      :  0.008           3761                                  
REMARK   3   ANGLE     :  1.294           5159                                  
REMARK   3   CHIRALITY :  0.087            559                                  
REMARK   3   PLANARITY :  0.005            598                                  
REMARK   3   DIHEDRAL  : 20.344           1450                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.9709   0.5435 -34.3880              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4230 T22:   0.4315                                     
REMARK   3      T33:   0.4500 T12:  -0.0042                                     
REMARK   3      T13:  -0.1287 T23:   0.0384                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9659 L22:   1.6766                                     
REMARK   3      L33:   1.9267 L12:   0.0231                                     
REMARK   3      L13:   0.3465 L23:   0.3348                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0016 S12:  -0.1304 S13:  -0.1602                       
REMARK   3      S21:   0.0434 S22:  -0.0890 S23:   0.0845                       
REMARK   3      S31:  -0.1744 S32:  -0.1692 S33:  -0.0118                       
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 4NM6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-NOV-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000083376.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-AUG-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.3                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9792, 1.2818                     
REMARK 200  MONOCHROMATOR                  : SAGITALLY FOCUSED SI(111)          
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 34839                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.020                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.8                               
REMARK 200  DATA REDUNDANCY                : 4.800                              
REMARK 200  R MERGE                    (I) : 0.06600                            
REMARK 200  R SYM                      (I) : 0.06600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.8600                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.02                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.09                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.48800                            
REMARK 200  R SYM FOR SHELL            (I) : 0.48800                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.33                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 23% PEG2000 MME, 0.1 M MES, PH 6.3,      
REMARK 280  VAPOR DIFFUSION, HANGING 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      131.48100            
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      131.48100            
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       24.14800            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       44.09300            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       24.14800            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       44.09300            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      131.48100            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       24.14800            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       44.09300            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      131.48100            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       24.14800            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       44.09300            
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4910 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20740 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A  1126                                                      
REMARK 465     GLY A  1127                                                      
REMARK 465     SER A  1128                                                      
REMARK 465     ASP A  1129                                                      
REMARK 465     PHE A  1130                                                      
REMARK 465     PRO A  1131                                                      
REMARK 465     VAL A  1136                                                      
REMARK 465     GLU A  1137                                                      
REMARK 465     GLN A  1138                                                      
REMARK 465     ILE A  1139                                                      
REMARK 465     ILE A  1140                                                      
REMARK 465     GLU A  1141                                                      
REMARK 465     LYS A  1142                                                      
REMARK 465     ASP A  1143                                                      
REMARK 465     CYS A  1812                                                      
REMARK 465     ARG A  1813                                                      
REMARK 465     GLN A  1814                                                      
REMARK 465     ARG A  1815                                                      
REMARK 465     LYS A  1816                                                      
REMARK 465     LEU A  1817                                                      
REMARK 465     GLU A  1818                                                      
REMARK 465     ALA A  1819                                                      
REMARK 465     LYS A  1820                                                      
REMARK 465     LYS A  1821                                                      
REMARK 465     ALA A  1822                                                      
REMARK 465     ALA A  1823                                                      
REMARK 465     ALA A  1824                                                      
REMARK 465     GLU A  1825                                                      
REMARK 465     LYS A  1826                                                      
REMARK 465     LEU A  1827                                                      
REMARK 465     SER A  1828                                                      
REMARK 465     GLY A  1829                                                      
REMARK 465     GLY A  1830                                                      
REMARK 465     GLY A  1831                                                      
REMARK 465     GLY A  1832                                                      
REMARK 465     SER A  1833                                                      
REMARK 465     GLY A  1834                                                      
REMARK 465     GLY A  1835                                                      
REMARK 465     GLY A  1836                                                      
REMARK 465     GLY A  1837                                                      
REMARK 465     SER A  1838                                                      
REMARK 465     GLY A  1839                                                      
REMARK 465     GLY A  1840                                                      
REMARK 465     GLY A  1841                                                      
REMARK 465     ALA A  1925                                                      
REMARK 465     ARG A  1926                                                      
REMARK 465     GLU A  1927                                                      
REMARK 465     LYS A  1928                                                      
REMARK 465     GLU A  1929                                                      
REMARK 465     GLU A  1930                                                      
REMARK 465     GLU A  1931                                                      
REMARK 465     CYS A  1932                                                      
REMARK 465     GLU A  1933                                                      
REMARK 465     LYS A  1934                                                      
REMARK 465     TYR A  1935                                                      
REMARK 465     GLY A  1936                                                      
REMARK 465      DT B    12                                                      
REMARK 465      DA C     1                                                      
REMARK 465      DC C     2                                                      
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   O2    DC B     2     N2    DG C    11              2.14            
REMARK 500   O    HOH A  2198     O    HOH A  2202              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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 A1229   CA  -  CB  -  CG  ANGL. DEV. =  15.2 DEGREES          
REMARK 500     DC B   2   O4' -  C1' -  N1  ANGL. DEV. =   2.7 DEGREES          
REMARK 500     DA B   4   O4' -  C1' -  N9  ANGL. DEV. =   2.1 DEGREES          
REMARK 500     DG B   7   O4' -  C1' -  N9  ANGL. DEV. =  -5.2 DEGREES          
REMARK 500     DG B  10   O4' -  C1' -  N9  ANGL. DEV. =   3.9 DEGREES          
REMARK 500     DC C   3   O4' -  C1' -  N1  ANGL. DEV. =   4.3 DEGREES          
REMARK 500     DA C   4   O4' -  C1' -  N9  ANGL. DEV. =   3.2 DEGREES          
REMARK 500     DC C   5   O4' -  C1' -  N1  ANGL. DEV. =   2.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A1190        0.72    -63.12                                   
REMARK 500    GLU A1234       72.28   -100.32                                   
REMARK 500    ILE A1305       87.55     49.98                                   
REMARK 500    ASP A1315      100.57    -36.52                                   
REMARK 500    GLU A1411       99.83     48.91                                   
REMARK 500    SER A1448       49.39    115.12                                   
REMARK 500    LYS A1462       93.58     59.41                                   
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 A2002  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1135   SG                                                     
REMARK 620 2 HIS A1219   ND1 100.7                                              
REMARK 620 3 CYS A1221   SG  123.4 118.2                                        
REMARK 620 4 CYS A1133   SG  108.0  91.9 109.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A2003  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A1912   ND1                                                    
REMARK 620 2 CYS A1298   SG  107.6                                              
REMARK 620 3 CYS A1358   SG  104.8 117.9                                        
REMARK 620 4 CYS A1289   SG  106.1 107.5 112.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A2001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A1380   NE2                                                    
REMARK 620 2 CYS A1193   SG  117.5                                              
REMARK 620 3 CYS A1273   SG  113.2  99.0                                        
REMARK 620 4 CYS A1271   SG   92.2 119.1 117.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FE2 A2004  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A1881   NE2                                                    
REMARK 620 2 HIS A1382   NE2  98.2                                              
REMARK 620 3 OGA A2005   O1  158.3  89.7                                        
REMARK 620 4 HOH A2149   O    91.5 168.6  79.1                                  
REMARK 620 5 OGA A2005   O2'  89.2  95.1  69.9  79.0                            
REMARK 620 6 ASP A1384   OD1 105.5  80.9  95.6 102.4 165.1                      
REMARK 620 N                    1     2     3     4     5                       
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 2001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 2002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 2003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 A 2004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OGA A 2005                
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 PROTEIN CONSTRUCT COMPRISES UNP RESIDUES 1129-1480 AND 1844-1936     
REMARK 999 CONNECTED BY A (GGGGS)3 LINKER.                                      
DBREF  4NM6 A 1129  1828  UNP    Q6N021   TET2_HUMAN    1129   1480             
DBREF  4NM6 A 1844  1936  UNP    Q6N021   TET2_HUMAN    1844   1936             
DBREF  4NM6 B    1    12  PDB    4NM6     4NM6             1     12             
DBREF  4NM6 C    1    12  PDB    4NM6     4NM6             1     12             
SEQADV 4NM6 GLY A 1126  UNP  Q6N021              EXPRESSION TAG                 
SEQADV 4NM6 GLY A 1127  UNP  Q6N021              EXPRESSION TAG                 
SEQADV 4NM6 SER A 1128  UNP  Q6N021              EXPRESSION TAG                 
SEQADV 4NM6 GLY A 1829  UNP  Q6N021              LINKER                         
SEQADV 4NM6 GLY A 1830  UNP  Q6N021              LINKER                         
SEQADV 4NM6 GLY A 1831  UNP  Q6N021              LINKER                         
SEQADV 4NM6 GLY A 1832  UNP  Q6N021              LINKER                         
SEQADV 4NM6 SER A 1833  UNP  Q6N021              LINKER                         
SEQADV 4NM6 GLY A 1834  UNP  Q6N021              LINKER                         
SEQADV 4NM6 GLY A 1835  UNP  Q6N021              LINKER                         
SEQADV 4NM6 GLY A 1836  UNP  Q6N021              LINKER                         
SEQADV 4NM6 GLY A 1837  UNP  Q6N021              LINKER                         
SEQADV 4NM6 SER A 1838  UNP  Q6N021              LINKER                         
SEQADV 4NM6 GLY A 1839  UNP  Q6N021              LINKER                         
SEQADV 4NM6 GLY A 1840  UNP  Q6N021              LINKER                         
SEQADV 4NM6 GLY A 1841  UNP  Q6N021              LINKER                         
SEQADV 4NM6 GLY A 1842  UNP  Q6N021              LINKER                         
SEQADV 4NM6 SER A 1843  UNP  Q6N021              LINKER                         
SEQRES   1 A  463  GLY GLY SER ASP PHE PRO SER CYS ARG CYS VAL GLU GLN          
SEQRES   2 A  463  ILE ILE GLU LYS ASP GLU GLY PRO PHE TYR THR HIS LEU          
SEQRES   3 A  463  GLY ALA GLY PRO ASN VAL ALA ALA ILE ARG GLU ILE MET          
SEQRES   4 A  463  GLU GLU ARG PHE GLY GLN LYS GLY LYS ALA ILE ARG ILE          
SEQRES   5 A  463  GLU ARG VAL ILE TYR THR GLY LYS GLU GLY LYS SER SER          
SEQRES   6 A  463  GLN GLY CYS PRO ILE ALA LYS TRP VAL VAL ARG ARG SER          
SEQRES   7 A  463  SER SER GLU GLU LYS LEU LEU CYS LEU VAL ARG GLU ARG          
SEQRES   8 A  463  ALA GLY HIS THR CYS GLU ALA ALA VAL ILE VAL ILE LEU          
SEQRES   9 A  463  ILE LEU VAL TRP GLU GLY ILE PRO LEU SER LEU ALA ASP          
SEQRES  10 A  463  LYS LEU TYR SER GLU LEU THR GLU THR LEU ARG LYS TYR          
SEQRES  11 A  463  GLY THR LEU THR ASN ARG ARG CYS ALA LEU ASN GLU GLU          
SEQRES  12 A  463  ARG THR CYS ALA CYS GLN GLY LEU ASP PRO GLU THR CYS          
SEQRES  13 A  463  GLY ALA SER PHE SER PHE GLY CYS SER TRP SER MET TYR          
SEQRES  14 A  463  TYR ASN GLY CYS LYS PHE ALA ARG SER LYS ILE PRO ARG          
SEQRES  15 A  463  LYS PHE LYS LEU LEU GLY ASP ASP PRO LYS GLU GLU GLU          
SEQRES  16 A  463  LYS LEU GLU SER HIS LEU GLN ASN LEU SER THR LEU MET          
SEQRES  17 A  463  ALA PRO THR TYR LYS LYS LEU ALA PRO ASP ALA TYR ASN          
SEQRES  18 A  463  ASN GLN ILE GLU TYR GLU HIS ARG ALA PRO GLU CYS ARG          
SEQRES  19 A  463  LEU GLY LEU LYS GLU GLY ARG PRO PHE SER GLY VAL THR          
SEQRES  20 A  463  ALA CYS LEU ASP PHE CYS ALA HIS ALA HIS ARG ASP LEU          
SEQRES  21 A  463  HIS ASN MET GLN ASN GLY SER THR LEU VAL CYS THR LEU          
SEQRES  22 A  463  THR ARG GLU ASP ASN ARG GLU PHE GLY GLY LYS PRO GLU          
SEQRES  23 A  463  ASP GLU GLN LEU HIS VAL LEU PRO LEU TYR LYS VAL SER          
SEQRES  24 A  463  ASP VAL ASP GLU PHE GLY SER VAL GLU ALA GLN GLU GLU          
SEQRES  25 A  463  LYS LYS ARG SER GLY ALA ILE GLN VAL LEU SER SER PHE          
SEQRES  26 A  463  ARG ARG LYS VAL ARG MET LEU ALA GLU PRO VAL LYS THR          
SEQRES  27 A  463  CYS ARG GLN ARG LYS LEU GLU ALA LYS LYS ALA ALA ALA          
SEQRES  28 A  463  GLU LYS LEU SER GLY GLY GLY GLY SER GLY GLY GLY GLY          
SEQRES  29 A  463  SER GLY GLY GLY GLY SER ASP GLU VAL TRP SER ASP SER          
SEQRES  30 A  463  GLU GLN SER PHE LEU ASP PRO ASP ILE GLY GLY VAL ALA          
SEQRES  31 A  463  VAL ALA PRO THR HIS GLY SER ILE LEU ILE GLU CYS ALA          
SEQRES  32 A  463  LYS ARG GLU LEU HIS ALA THR THR PRO LEU LYS ASN PRO          
SEQRES  33 A  463  ASN ARG ASN HIS PRO THR ARG ILE SER LEU VAL PHE TYR          
SEQRES  34 A  463  GLN HIS LYS SER MET ASN GLU PRO LYS HIS GLY LEU ALA          
SEQRES  35 A  463  LEU TRP GLU ALA LYS MET ALA GLU LYS ALA ARG GLU LYS          
SEQRES  36 A  463  GLU GLU GLU CYS GLU LYS TYR GLY                              
SEQRES   1 B   12   DA  DC  DC  DA  DC 5CM  DG  DG  DT  DG  DG  DT              
SEQRES   1 C   12   DA  DC  DC  DA  DC 5CM  DG  DG  DT  DG  DG  DT              
MODRES 4NM6 5CM B    6   DC                                                     
MODRES 4NM6 5CM C    6   DC                                                     
HET    5CM  B   6      20                                                       
HET    5CM  C   6      20                                                       
HET     ZN  A2001       1                                                       
HET     ZN  A2002       1                                                       
HET     ZN  A2003       1                                                       
HET    FE2  A2004       1                                                       
HET    OGA  A2005      10                                                       
HETNAM     5CM 5-METHYL-2'-DEOXY-CYTIDINE-5'-MONOPHOSPHATE                      
HETNAM      ZN ZINC ION                                                         
HETNAM     FE2 FE (II) ION                                                      
HETNAM     OGA N-OXALYLGLYCINE                                                  
FORMUL   2  5CM    2(C10 H16 N3 O7 P)                                           
FORMUL   4   ZN    3(ZN 2+)                                                     
FORMUL   7  FE2    FE 2+                                                        
FORMUL   8  OGA    C4 H5 N O5                                                   
FORMUL   9  HOH   *131(H2 O)                                                    
HELIX    1   1 ASN A 1156  GLY A 1169  1                                  14    
HELIX    2   2 LYS A 1171  LYS A 1173  5                                   3    
HELIX    3   3 PRO A 1237  GLY A 1256  1                                  20    
HELIX    4   4 ARG A 1261  LEU A 1265  5                                   5    
HELIX    5   5 ASP A 1315  ALA A 1341  1                                  27    
HELIX    6   6 ALA A 1341  GLU A 1350  1                                  10    
HELIX    7   7 ALA A 1355  ARG A 1359  5                                   5    
HELIX    8   8 GLU A 1401  ARG A 1404  5                                   4    
HELIX    9   9 SER A 1431  GLY A 1442  1                                  12    
HELIX   10  10 SER A 1850  ASP A 1856  1                                   7    
HELIX   11  11 GLU A 1909  HIS A 1912  5                                   4    
HELIX   12  12 GLY A 1913  GLU A 1923  1                                  11    
SHEET    1   A 7 ALA A1153  GLY A1154  0                                        
SHEET    2   A 7 VAL A1225  VAL A1232 -1  O  VAL A1225   N  GLY A1154           
SHEET    3   A 7 ILE A1871  GLU A1874 -1  O  ILE A1873   N  ILE A1230           
SHEET    4   A 7 THR A1393  THR A1399 -1  N  THR A1393   O  GLU A1874           
SHEET    5   A 7 ARG A1896  TYR A1902 -1  O  PHE A1901   N  LEU A1394           
SHEET    6   A 7 GLY A1370  LEU A1375 -1  N  THR A1372   O  VAL A1900           
SHEET    7   A 7 ALA A1283  GLY A1288 -1  N  PHE A1287   O  VAL A1371           
SHEET    1   B 5 ALA A1153  GLY A1154  0                                        
SHEET    2   B 5 VAL A1225  VAL A1232 -1  O  VAL A1225   N  GLY A1154           
SHEET    3   B 5 LEU A1209  GLU A1215 -1  N  LEU A1212   O  ILE A1228           
SHEET    4   B 5 ILE A1175  TYR A1182  1  N  VAL A1180   O  VAL A1213           
SHEET    5   B 5 TYR A1421  VAL A1423 -1  O  LYS A1422   N  ILE A1181           
SHEET    1   C 5 ILE A1444  VAL A1446  0                                        
SHEET    2   C 5 TRP A1198  VAL A1200 -1  N  VAL A1199   O  GLN A1445           
SHEET    3   C 5 VAL A1862  VAL A1864  1  O  ALA A1863   N  VAL A1200           
SHEET    4   C 5 HIS A1416  LEU A1418 -1  N  LEU A1418   O  VAL A1862           
SHEET    5   C 5 ALA A1882  THR A1883 -1  O  ALA A1882   N  VAL A1417           
SHEET    1   D 2 TRP A1291  SER A1292  0                                        
SHEET    2   D 2 GLY A1297  CYS A1298 -1  O  GLY A1297   N  SER A1292           
SHEET    1   E 2 ARG A1451  LEU A1457  0                                        
SHEET    2   E 2 SER A1843  ASP A1849 -1  O  VAL A1846   N  VAL A1454           
LINK         O3'  DC B   5                 P   5CM B   6     1555   1555  1.61  
LINK         O3' 5CM B   6                 P    DG B   7     1555   1555  1.61  
LINK         O3'  DC C   5                 P   5CM C   6     1555   1555  1.61  
LINK         O3' 5CM C   6                 P    DG C   7     1555   1555  1.61  
LINK         SG  CYS A1135                ZN    ZN A2002     1555   1555  2.20  
LINK         ND1 HIS A1219                ZN    ZN A2002     1555   1555  2.23  
LINK         SG  CYS A1221                ZN    ZN A2002     1555   1555  2.24  
LINK         ND1 HIS A1912                ZN    ZN A2003     1555   1555  2.28  
LINK         NE2 HIS A1380                ZN    ZN A2001     1555   1555  2.28  
LINK         SG  CYS A1133                ZN    ZN A2002     1555   1555  2.42  
LINK         SG  CYS A1193                ZN    ZN A2001     1555   1555  2.43  
LINK         SG  CYS A1298                ZN    ZN A2003     1555   1555  2.47  
LINK         SG  CYS A1273                ZN    ZN A2001     1555   1555  2.48  
LINK         SG  CYS A1271                ZN    ZN A2001     1555   1555  2.53  
LINK         SG  CYS A1358                ZN    ZN A2003     1555   1555  2.53  
LINK         SG  CYS A1289                ZN    ZN A2003     1555   1555  2.54  
LINK         NE2 HIS A1881                FE   FE2 A2004     1555   1555  2.23  
LINK         NE2 HIS A1382                FE   FE2 A2004     1555   1555  2.35  
LINK        FE   FE2 A2004                 O1  OGA A2005     1555   1555  2.40  
LINK        FE   FE2 A2004                 O   HOH A2149     1555   1555  2.41  
LINK        FE   FE2 A2004                 O2' OGA A2005     1555   1555  2.42  
LINK         OD1 ASP A1384                FE   FE2 A2004     1555   1555  2.47  
CISPEP   1 LEU A 1151    GLY A 1152          0        15.84                     
CISPEP   2 GLN A 1191    GLY A 1192          0       -19.58                     
CISPEP   3 GLU A 1411    ASP A 1412          0        19.26                     
CISPEP   4 LEU A 1447    SER A 1448          0         7.06                     
SITE     1 AC1  4 CYS A1193  CYS A1271  CYS A1273  HIS A1380                    
SITE     1 AC2  4 CYS A1133  CYS A1135  HIS A1219  CYS A1221                    
SITE     1 AC3  4 CYS A1289  CYS A1298  CYS A1358  HIS A1912                    
SITE     1 AC4  5 HIS A1382  ASP A1384  HIS A1881  OGA A2005                    
SITE     2 AC4  5 HOH A2149                                                     
SITE     1 AC5 13 ARG A1261  CYS A1374  HIS A1382  ASP A1384                    
SITE     2 AC5 13 HIS A1416  HIS A1881  THR A1883  ARG A1896                    
SITE     3 AC5 13 SER A1898  FE2 A2004  HOH A2142  HOH A2149                    
SITE     4 AC5 13 5CM B   6                                                     
CRYST1   48.296   88.186  262.962  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      0.020706  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011340  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003803        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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