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Database: PDB
Entry: 5D9Y
LinkDB: 5D9Y
Original site: 5D9Y 
HEADER    OXIDOREDUCTASE/DNA                      19-AUG-15   5D9Y              
TITLE     CRYSTAL STRUCTURE OF TET2-5FC COMPLEX                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: METHYLCYTOSINE DIOXYGENASE TET2,METHYLCYTOSINE DIOXYGENASE 
COMPND   3 TET2;                                                                
COMPND   4 CHAIN: A;                                                            
COMPND   5 EC: 1.14.11.-,1.14.11.-;                                             
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: DNA (5'-D(*AP*CP*TP*GP*TP*(5FC)P*GP*AP*AP*GP*CP*T)-3');    
COMPND   9 CHAIN: B;                                                            
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MOL_ID: 3;                                                           
COMPND  12 MOLECULE: DNA (5'-D(*AP*GP*CP*TP*TP*CP*GP*AP*CP*AP*GP*T)-3');        
COMPND  13 CHAIN: C;                                                            
COMPND  14 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;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  11 ORGANISM_TAXID: 32630;                                               
SOURCE  12 MOL_ID: 3;                                                           
SOURCE  13 SYNTHETIC: YES;                                                      
SOURCE  14 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  15 ORGANISM_TAXID: 32630                                                
KEYWDS    5-METHYLCYTOSINE DIOXYGENASE, TET2, 5-FORMYLCYTOSINE, PROTEIN-DNA     
KEYWDS   2 COMPLEX, OXIDOREDUCTASE-DNA COMPLEX                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.HU,J.CHENG,Q.RAO,Z.LI,J.LI,Y.XU                                     
REVDAT   2   18-NOV-15 5D9Y    1       JRNL   REMARK                            
REVDAT   1   04-NOV-15 5D9Y    0                                                
JRNL        AUTH   L.HU,J.LU,J.CHENG,Q.RAO,Z.LI,H.HOU,Z.LOU,L.ZHANG,W.LI,       
JRNL        AUTH 2 W.GONG,M.LIU,C.SUN,X.YIN,J.LI,X.TAN,P.WANG,Y.WANG,D.FANG,    
JRNL        AUTH 3 Q.CUI,P.YANG,C.HE,H.JIANG,C.LUO,Y.XU                         
JRNL        TITL   STRUCTURAL INSIGHT INTO SUBSTRATE PREFERENCE FOR             
JRNL        TITL 2 TET-MEDIATED OXIDATION.                                      
JRNL        REF    NATURE                        V. 527   118 2015              
JRNL        REFN                   ESSN 1476-4687                               
JRNL        PMID   26524525                                                     
JRNL        DOI    10.1038/NATURE15713                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.97 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
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) : 1.97                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.77                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 74.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 57919                          
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                     : 0.248                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.380                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3114                            
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 36.7732 -  5.5156    0.99     3296   195  0.1643 0.2272        
REMARK   3     2  5.5156 -  4.3802    0.99     3312   200  0.1535 0.2078        
REMARK   3     3  4.3802 -  3.8272    1.00     3321   200  0.1574 0.1959        
REMARK   3     4  3.8272 -  3.4775    0.99     3318   188  0.1775 0.2192        
REMARK   3     5  3.4775 -  3.2284    1.00     3338   183  0.2057 0.2325        
REMARK   3     6  3.2284 -  3.0382    1.00     3336   179  0.2144 0.2420        
REMARK   3     7  3.0382 -  2.8861    1.00     3384   185  0.2279 0.2643        
REMARK   3     8  2.8861 -  2.7605    0.97     3210   176  0.2336 0.2986        
REMARK   3     9  2.7605 -  2.6543    0.96     3179   176  0.2397 0.2834        
REMARK   3    10  2.6543 -  2.5627    0.93     3152   167  0.2430 0.3044        
REMARK   3    11  2.5627 -  2.4826    0.87     2887   171  0.2340 0.2963        
REMARK   3    12  2.4826 -  2.4116    0.81     2678   146  0.2387 0.2460        
REMARK   3    13  2.4116 -  2.3482    0.74     2498   139  0.2436 0.3249        
REMARK   3    14  2.3482 -  2.2909    0.66     2164   135  0.2534 0.3159        
REMARK   3    15  2.2909 -  2.2388    0.60     2060   115  0.2623 0.2982        
REMARK   3    16  2.2388 -  2.1912    0.54     1778   100  0.2767 0.3084        
REMARK   3    17  2.1912 -  2.1473    0.51     1713    96  0.2898 0.3028        
REMARK   3    18  2.1473 -  2.1068    0.45     1493    89  0.2875 0.3349        
REMARK   3    19  2.1068 -  2.0692    0.41     1365    81  0.2964 0.3099        
REMARK   3    20  2.0692 -  2.0341    0.38     1268    75  0.3000 0.2942        
REMARK   3    21  2.0341 -  2.0013    0.33     1050    61  0.2939 0.3174        
REMARK   3    22  2.0013 -  1.9705    0.29     1005    57  0.3000 0.3612        
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)     : 0.240            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.400           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 24.08                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 33.62                          
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      :  0.009           3900                                  
REMARK   3   ANGLE     :  1.159           5364                                  
REMARK   3   CHIRALITY :  0.045            580                                  
REMARK   3   PLANARITY :  0.005            620                                  
REMARK   3   DIHEDRAL  : 19.428           1517                                  
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 5D9Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-AUG-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000212869.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-DEC-14                          
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                       : BL19U1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 57919                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.970                              
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     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY                : 6.000                              
REMARK 200  R MERGE                    (I) : 0.05500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.97                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.04                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.62400                            
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: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 4NM6                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.12                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 21% PEGMME2000, 0.1M 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      134.01000            
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      134.01000            
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       24.07700            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       43.97900            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       24.07700            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       43.97900            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      134.01000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       24.07700            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       43.97900            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      134.01000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       24.07700            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       43.97900            
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: 4350 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21690 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 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  1127                                                      
REMARK 465     SER A  1128                                                      
REMARK 465     ASP A  1129                                                      
REMARK 465     PHE A  1130                                                      
REMARK 465     PRO A  1131                                                      
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  1922                                                      
REMARK 465     GLU A  1923                                                      
REMARK 465     LYS A  1924                                                      
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 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500     DC C   9   O3'    DC C   9   C3'    -0.038                       
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     DA B   1   O4' -  C1' -  N9  ANGL. DEV. =   3.5 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    LYS A1304      -71.49    -49.89                                   
REMARK 500    HIS A1893       65.07   -161.10                                   
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 A2003  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1133   SG                                                     
REMARK 620 2 CYS A1135   SG  105.9                                              
REMARK 620 3 HIS A1219   ND1  88.6 101.9                                        
REMARK 620 4 CYS A1221   SG  119.7 107.3 130.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A2004  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1193   SG                                                     
REMARK 620 2 CYS A1271   SG  118.8                                              
REMARK 620 3 CYS A1273   SG  104.6 114.7                                        
REMARK 620 4 HIS A1380   NE2 108.9  96.7 113.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A2005  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1289   SG                                                     
REMARK 620 2 CYS A1298   SG  112.9                                              
REMARK 620 3 CYS A1358   SG  115.0 114.6                                        
REMARK 620 4 HIS A1912   ND1 102.9 107.7 102.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE A2002  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A1382   NE2                                                    
REMARK 620 2 ASP A1384   OD2 106.9                                              
REMARK 620 3 HIS A1881   NE2  96.3  95.1                                        
REMARK 620 4 OGA A2001   O1   85.9 114.4 148.5                                  
REMARK 620 5 OGA A2001   O2' 102.7 150.2  78.1  70.8                            
REMARK 620 6 HOH A2136   O   177.2  76.0  83.6  92.6  74.5                      
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 OGA A 2001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FE 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 ZN A 2004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 2005                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5DEU   RELATED DB: PDB                                   
DBREF  5D9Y A 1129  1828  UNP    Q6N021   TET2_HUMAN    1129   1480             
DBREF  5D9Y A 1844  1936  UNP    Q6N021   TET2_HUMAN    1844   1936             
DBREF  5D9Y B    1    12  PDB    5D9Y     5D9Y             1     12             
DBREF  5D9Y C    1    12  PDB    5D9Y     5D9Y             1     12             
SEQADV 5D9Y GLY A 1127  UNP  Q6N021              EXPRESSION TAG                 
SEQADV 5D9Y SER A 1128  UNP  Q6N021              EXPRESSION TAG                 
SEQADV 5D9Y GLY A 1829  UNP  Q6N021              LINKER                         
SEQADV 5D9Y GLY A 1830  UNP  Q6N021              LINKER                         
SEQADV 5D9Y GLY A 1831  UNP  Q6N021              LINKER                         
SEQADV 5D9Y GLY A 1832  UNP  Q6N021              LINKER                         
SEQADV 5D9Y SER A 1833  UNP  Q6N021              LINKER                         
SEQADV 5D9Y GLY A 1834  UNP  Q6N021              LINKER                         
SEQADV 5D9Y GLY A 1835  UNP  Q6N021              LINKER                         
SEQADV 5D9Y GLY A 1836  UNP  Q6N021              LINKER                         
SEQADV 5D9Y GLY A 1837  UNP  Q6N021              LINKER                         
SEQADV 5D9Y SER A 1838  UNP  Q6N021              LINKER                         
SEQADV 5D9Y GLY A 1839  UNP  Q6N021              LINKER                         
SEQADV 5D9Y GLY A 1840  UNP  Q6N021              LINKER                         
SEQADV 5D9Y GLY A 1841  UNP  Q6N021              LINKER                         
SEQADV 5D9Y GLY A 1842  UNP  Q6N021              LINKER                         
SEQADV 5D9Y SER A 1843  UNP  Q6N021              LINKER                         
SEQRES   1 A  462  GLY SER ASP PHE PRO SER CYS ARG CYS VAL GLU GLN ILE          
SEQRES   2 A  462  ILE GLU LYS ASP GLU GLY PRO PHE TYR THR HIS LEU GLY          
SEQRES   3 A  462  ALA GLY PRO ASN VAL ALA ALA ILE ARG GLU ILE MET GLU          
SEQRES   4 A  462  GLU ARG PHE GLY GLN LYS GLY LYS ALA ILE ARG ILE GLU          
SEQRES   5 A  462  ARG VAL ILE TYR THR GLY LYS GLU GLY LYS SER SER GLN          
SEQRES   6 A  462  GLY CYS PRO ILE ALA LYS TRP VAL VAL ARG ARG SER SER          
SEQRES   7 A  462  SER GLU GLU LYS LEU LEU CYS LEU VAL ARG GLU ARG ALA          
SEQRES   8 A  462  GLY HIS THR CYS GLU ALA ALA VAL ILE VAL ILE LEU ILE          
SEQRES   9 A  462  LEU VAL TRP GLU GLY ILE PRO LEU SER LEU ALA ASP LYS          
SEQRES  10 A  462  LEU TYR SER GLU LEU THR GLU THR LEU ARG LYS TYR GLY          
SEQRES  11 A  462  THR LEU THR ASN ARG ARG CYS ALA LEU ASN GLU GLU ARG          
SEQRES  12 A  462  THR CYS ALA CYS GLN GLY LEU ASP PRO GLU THR CYS GLY          
SEQRES  13 A  462  ALA SER PHE SER PHE GLY CYS SER TRP SER MET TYR TYR          
SEQRES  14 A  462  ASN GLY CYS LYS PHE ALA ARG SER LYS ILE PRO ARG LYS          
SEQRES  15 A  462  PHE LYS LEU LEU GLY ASP ASP PRO LYS GLU GLU GLU LYS          
SEQRES  16 A  462  LEU GLU SER HIS LEU GLN ASN LEU SER THR LEU MET ALA          
SEQRES  17 A  462  PRO THR TYR LYS LYS LEU ALA PRO ASP ALA TYR ASN ASN          
SEQRES  18 A  462  GLN ILE GLU TYR GLU HIS ARG ALA PRO GLU CYS ARG LEU          
SEQRES  19 A  462  GLY LEU LYS GLU GLY ARG PRO PHE SER GLY VAL THR ALA          
SEQRES  20 A  462  CYS LEU ASP PHE CYS ALA HIS ALA HIS ARG ASP LEU HIS          
SEQRES  21 A  462  ASN MET GLN ASN GLY SER THR LEU VAL CYS THR LEU THR          
SEQRES  22 A  462  ARG GLU ASP ASN ARG GLU PHE GLY GLY LYS PRO GLU ASP          
SEQRES  23 A  462  GLU GLN LEU HIS VAL LEU PRO LEU TYR LYS VAL SER ASP          
SEQRES  24 A  462  VAL ASP GLU PHE GLY SER VAL GLU ALA GLN GLU GLU LYS          
SEQRES  25 A  462  LYS ARG SER GLY ALA ILE GLN VAL LEU SER SER PHE ARG          
SEQRES  26 A  462  ARG LYS VAL ARG MET LEU ALA GLU PRO VAL LYS THR CYS          
SEQRES  27 A  462  ARG GLN ARG LYS LEU GLU ALA LYS LYS ALA ALA ALA GLU          
SEQRES  28 A  462  LYS LEU SER GLY GLY GLY GLY SER GLY GLY GLY GLY SER          
SEQRES  29 A  462  GLY GLY GLY GLY SER ASP GLU VAL TRP SER ASP SER GLU          
SEQRES  30 A  462  GLN SER PHE LEU ASP PRO ASP ILE GLY GLY VAL ALA VAL          
SEQRES  31 A  462  ALA PRO THR HIS GLY SER ILE LEU ILE GLU CYS ALA LYS          
SEQRES  32 A  462  ARG GLU LEU HIS ALA THR THR PRO LEU LYS ASN PRO ASN          
SEQRES  33 A  462  ARG ASN HIS PRO THR ARG ILE SER LEU VAL PHE TYR GLN          
SEQRES  34 A  462  HIS LYS SER MET ASN GLU PRO LYS HIS GLY LEU ALA LEU          
SEQRES  35 A  462  TRP GLU ALA LYS MET ALA GLU LYS ALA ARG GLU LYS GLU          
SEQRES  36 A  462  GLU GLU CYS GLU LYS TYR GLY                                  
SEQRES   1 B   12   DA  DC  DT  DG  DT 5FC  DG  DA  DA  DG  DC  DT              
SEQRES   1 C   12   DA  DG  DC  DT  DT  DC  DG  DA  DC  DA  DG  DT              
HET    5FC  B   6      21                                                       
HET    OGA  A2001      10                                                       
HET     FE  A2002       1                                                       
HET     ZN  A2003       1                                                       
HET     ZN  A2004       1                                                       
HET     ZN  A2005       1                                                       
HETNAM     5FC 5-FORMYL-2'-DEOXY-CYTIDINE-5'-MONOPHOSPHATE                      
HETNAM     OGA N-OXALYLGLYCINE                                                  
HETNAM      FE FE (III) ION                                                     
HETNAM      ZN ZINC ION                                                         
HETSYN     5FC 2'-DEOXY-5-FORMYLCYTIDINE-5'-MONOPHOSPHATE                       
FORMUL   2  5FC    C10 H14 N3 O8 P                                              
FORMUL   4  OGA    C4 H5 N O5                                                   
FORMUL   5   FE    FE 3+                                                        
FORMUL   6   ZN    3(ZN 2+)                                                     
FORMUL   9  HOH   *262(H2 O)                                                    
HELIX    1 AA1 ILE A 1140  GLY A 1145  1                                   6    
HELIX    2 AA2 ASN A 1156  GLY A 1169  1                                  14    
HELIX    3 AA3 PRO A 1237  GLY A 1256  1                                  20    
HELIX    4 AA4 ARG A 1261  LEU A 1265  5                                   5    
HELIX    5 AA5 ASP A 1315  ALA A 1341  1                                  27    
HELIX    6 AA6 ALA A 1341  ILE A 1349  1                                   9    
HELIX    7 AA7 ALA A 1355  ARG A 1359  5                                   5    
HELIX    8 AA8 GLU A 1401  ARG A 1404  5                                   4    
HELIX    9 AA9 SER A 1431  GLY A 1442  1                                  12    
HELIX   10 AB1 SER A 1850  ASP A 1856  1                                   7    
HELIX   11 AB2 GLU A 1909  HIS A 1912  5                                   4    
HELIX   12 AB3 GLY A 1913  ALA A 1919  1                                   7    
SHEET    1 AA1 7 ALA A1153  GLY A1154  0                                        
SHEET    2 AA1 7 VAL A1225  VAL A1232 -1  O  VAL A1225   N  GLY A1154           
SHEET    3 AA1 7 ILE A1871  GLU A1874 -1  O  ILE A1873   N  ILE A1230           
SHEET    4 AA1 7 THR A1393  THR A1399 -1  N  THR A1393   O  GLU A1874           
SHEET    5 AA1 7 ARG A1896  TYR A1902 -1  O  PHE A1901   N  LEU A1394           
SHEET    6 AA1 7 GLY A1370  LEU A1375 -1  N  THR A1372   O  VAL A1900           
SHEET    7 AA1 7 ALA A1283  GLY A1288 -1  N  PHE A1287   O  VAL A1371           
SHEET    1 AA2 5 ALA A1153  GLY A1154  0                                        
SHEET    2 AA2 5 VAL A1225  VAL A1232 -1  O  VAL A1225   N  GLY A1154           
SHEET    3 AA2 5 LEU A1209  GLU A1215 -1  N  LEU A1210   O  LEU A1231           
SHEET    4 AA2 5 ILE A1175  TYR A1182  1  N  ARG A1176   O  LEU A1209           
SHEET    5 AA2 5 TYR A1421  VAL A1423 -1  O  LYS A1422   N  ILE A1181           
SHEET    1 AA3 5 ILE A1444  VAL A1446  0                                        
SHEET    2 AA3 5 TRP A1198  VAL A1200 -1  N  VAL A1199   O  GLN A1445           
SHEET    3 AA3 5 VAL A1862  VAL A1864  1  O  ALA A1863   N  VAL A1200           
SHEET    4 AA3 5 HIS A1416  LEU A1418 -1  N  LEU A1418   O  VAL A1862           
SHEET    5 AA3 5 ALA A1882  THR A1883 -1  O  ALA A1882   N  VAL A1417           
SHEET    1 AA4 2 TRP A1291  SER A1292  0                                        
SHEET    2 AA4 2 GLY A1297  CYS A1298 -1  O  GLY A1297   N  SER A1292           
SHEET    1 AA5 2 ARG A1451  LEU A1457  0                                        
SHEET    2 AA5 2 SER A1843  ASP A1849 -1  O  SER A1848   N  ARG A1452           
LINK         SG  CYS A1133                ZN    ZN A2003     1555   1555  2.24  
LINK         SG  CYS A1135                ZN    ZN A2003     1555   1555  2.58  
LINK         SG  CYS A1193                ZN    ZN A2004     1555   1555  2.37  
LINK         ND1 HIS A1219                ZN    ZN A2003     1555   1555  2.10  
LINK         SG  CYS A1221                ZN    ZN A2003     1555   1555  2.11  
LINK         SG  CYS A1271                ZN    ZN A2004     1555   1555  2.19  
LINK         SG  CYS A1273                ZN    ZN A2004     1555   1555  2.17  
LINK         SG  CYS A1289                ZN    ZN A2005     1555   1555  2.32  
LINK         SG  CYS A1298                ZN    ZN A2005     1555   1555  2.21  
LINK         SG  CYS A1358                ZN    ZN A2005     1555   1555  2.41  
LINK         NE2 HIS A1380                ZN    ZN A2004     1555   1555  2.11  
LINK         NE2 HIS A1382                FE    FE A2002     1555   1555  2.27  
LINK         OD2 ASP A1384                FE    FE A2002     1555   1555  2.12  
LINK         NE2 HIS A1881                FE    FE A2002     1555   1555  2.17  
LINK         ND1 HIS A1912                ZN    ZN A2005     1555   1555  2.15  
LINK         O3'  DT B   5                 P   5FC B   6     1555   1555  1.61  
LINK         O3' 5FC B   6                 P    DG B   7     1555   1555  1.62  
LINK         O1  OGA A2001                FE    FE A2002     1555   1555  2.36  
LINK         O2' OGA A2001                FE    FE A2002     1555   1555  2.17  
LINK        FE    FE A2002                 O   HOH A2136     1555   1555  2.06  
CISPEP   1 SER A 1132    CYS A 1133          0         7.96                     
SITE     1 AC1 13 ARG A1261  CYS A1374  HIS A1382  ASP A1384                    
SITE     2 AC1 13 HIS A1416  HIS A1881  THR A1883  ARG A1896                    
SITE     3 AC1 13 SER A1898   FE A2002  HOH A2136  HOH A2255                    
SITE     4 AC1 13 5FC B   6                                                     
SITE     1 AC2  5 HIS A1382  ASP A1384  HIS A1881  OGA A2001                    
SITE     2 AC2  5 HOH A2136                                                     
SITE     1 AC3  4 CYS A1133  CYS A1135  HIS A1219  CYS A1221                    
SITE     1 AC4  4 CYS A1193  CYS A1271  CYS A1273  HIS A1380                    
SITE     1 AC5  4 CYS A1289  CYS A1298  CYS A1358  HIS A1912                    
CRYST1   48.154   87.958  268.020  90.00  90.00  90.00 C 2 2 21      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.020767  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011369  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003731        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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