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Database: PDB
Entry: 3KTU
LinkDB: 3KTU
Original site: 3KTU 
HEADER    HYDROLASE,LYASE/DNA                     26-NOV-09   3KTU              
TITLE     STRUCTURE OF HUMAN 8-OXOGUANINE GLYCOSYLASE 1 BOUND TO FLUORNINATED   
TITLE    2 OXOG-CONTAINING DNA                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: N-GLYCOSYLASE/DNA LYASE;                                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: SEQUENCE DATABASE RESIDUES 12-325;                         
COMPND   5 SYNONYM: 8-OXOGUANINE DNA GLYCOSYLASE, DNA-(APURINIC OR APYRIMIDINIC 
COMPND   6 SITE) LYASE;                                                         
COMPND   7 EC: 3.2.2.-, 4.2.99.18;                                              
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: DNA (5'-D(*GP*GP*TP*AP*GP*AP*CP*CP*TP*GP*GP*AP*C)-3');     
COMPND  11 CHAIN: B;                                                            
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: DNA (5'-D(*GP*TP*CP*CP*AP*(FDG)P*GP*TP*CP*TP*AP*C)-3');    
COMPND  15 CHAIN: C;                                                            
COMPND  16 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: MMH, MUTM, OGG1, OGH1;                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;                            
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET30A;                                   
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  14 ORGANISM_TAXID: 32630;                                               
SOURCE  15 OTHER_DETAILS: SYNTHETIC DNA;                                        
SOURCE  16 MOL_ID: 3;                                                           
SOURCE  17 SYNTHETIC: YES;                                                      
SOURCE  18 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  19 ORGANISM_TAXID: 32630;                                               
SOURCE  20 OTHER_DETAILS: SYNTHETIC DNA                                         
KEYWDS    8-OXOGUANINE, 2'-FLUORO-8-OXOGUANINE, PROTEIN-DNA COMPLEX, DNA        
KEYWDS   2 GLYCOSYLASE, BASE EXCSION REPAIR, DNA DAMAGE, DNA REPAIR, HYDROLASE, 
KEYWDS   3 LYASE-DNA COMPLEX                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.L.VERDINE,S.M.LEE                                                   
REVDAT   4   06-SEP-23 3KTU    1       REMARK                                   
REVDAT   3   13-OCT-21 3KTU    1       REMARK SEQADV LINK                       
REVDAT   2   01-NOV-17 3KTU    1       SOURCE REMARK                            
REVDAT   1   14-JUL-10 3KTU    0                                                
JRNL        AUTH   G.L.VERDINE,S.M.LEE                                          
JRNL        TITL   STRUCTURAL INVESTIGATION OF HOGG1 BOUND TO A FLUORINATED     
JRNL        TITL 2 OXOG ANALOG                                                  
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   G.L.VERDINE,C.M.CRENSHAW,K.S.OO,P.S.KUTCHUKIAN               
REMARK   1  TITL   A CATALYTIC CHECKPOINT IN BASE EXCISION BY THE HUMAN         
REMARK   1  TITL 2 8-OXOGUANINE DNA GLYCOSYLASE HOGG1                           
REMARK   1  REF    TO BE PUBLISHED                                              
REMARK   1  REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.21                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 94.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 23379                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.225                           
REMARK   3   FREE R VALUE                     : 0.257                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.400                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2316                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2485                                    
REMARK   3   NUCLEIC ACID ATOMS       : 510                                     
REMARK   3   HETEROGEN ATOMS          : 2                                       
REMARK   3   SOLVENT ATOMS            : 72                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 58.94                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 4.66600                                              
REMARK   3    B22 (A**2) : 4.66600                                              
REMARK   3    B33 (A**2) : -9.33300                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.351 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.198 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.012 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.028 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 42.65                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : DNA-RNA_REP.PARAM                              
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  5  : FOG_PAR.TXT                                    
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3KTU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-DEC-09.                  
REMARK 100 THE DEPOSITION ID IS D_1000056439.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24522                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
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     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 9.200                              
REMARK 200  R MERGE                    (I) : 0.11200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 9.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.39700                            
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: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 1EBM                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.39                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.03                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: CALCIUM CHLORIDE, SODIUM CACODYLATE,     
REMARK 280  PH 6.0, PEG 8000, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
REMARK 290       7555   Y,X,-Z+2/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+1/3                                          
REMARK 290      10555   -Y,-X,-Z+1/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+5/6                                            
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      141.66667            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       70.83333            
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      106.25000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       35.41667            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      177.08333            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      141.66667            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000       70.83333            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       35.41667            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      106.25000            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000      177.08333            
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: 3950 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17130 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 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    80                                                      
REMARK 465     ASP A    81                                                      
REMARK 465     LYS A    82                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLN A 125    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 126    CG   CD   CE   NZ                                   
REMARK 470     GLN A 325    CG   CD   OE1  NE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A 309   C   -  N   -  CA  ANGL. DEV. =   9.3 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    CYS A  28      108.96   -171.46                                   
REMARK 500    CYS A 149       53.56     33.38                                   
REMARK 500    LEU A 170     -144.30   -103.56                                   
REMARK 500    ASP A 174     -131.57     55.05                                   
REMARK 500    GLU A 218      -31.99   -143.68                                   
REMARK 500    ALA A 258      -10.79   -140.42                                   
REMARK 500    THR A 284      -70.10   -105.74                                   
REMARK 500    ALA A 288      151.73    -45.96                                   
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                              CA A   2  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 241   O                                                      
REMARK 620 2 LEU A 243   O    95.8                                              
REMARK 620 3 VAL A 246   O    88.8  82.4                                        
REMARK 620 4  DC C  26   OP1 173.7  77.9  91.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FDG C 23                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 1                    
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3IH7   RELATED DB: PDB                                   
REMARK 900 HOGG1 DISULPHIDE CROSS-LINKED TO UNDAMAGED DNA                       
REMARK 900 RELATED ID: 1EBM   RELATED DB: PDB                                   
REMARK 900 HOGG1 COMPLEXED WITH OXOG CONTAINING DNA                             
DBREF  3KTU A   12   325  UNP    O15527   OGG1_HUMAN      12    325             
DBREF  3KTU B    1    13  PDB    3KTU     3KTU             1     13             
DBREF  3KTU C   18    29  PDB    3KTU     3KTU            18     29             
SEQADV 3KTU SER A    9  UNP  O15527              EXPRESSION TAG                 
SEQADV 3KTU GLU A   10  UNP  O15527              EXPRESSION TAG                 
SEQADV 3KTU PHE A   11  UNP  O15527              EXPRESSION TAG                 
SEQADV 3KTU CYS A  149  UNP  O15527    ASN   149 ENGINEERED MUTATION            
SEQRES   1 A  317  SER GLU PHE GLY HIS ARG THR LEU ALA SER THR PRO ALA          
SEQRES   2 A  317  LEU TRP ALA SER ILE PRO CYS PRO ARG SER GLU LEU ARG          
SEQRES   3 A  317  LEU ASP LEU VAL LEU PRO SER GLY GLN SER PHE ARG TRP          
SEQRES   4 A  317  ARG GLU GLN SER PRO ALA HIS TRP SER GLY VAL LEU ALA          
SEQRES   5 A  317  ASP GLN VAL TRP THR LEU THR GLN THR GLU GLU GLN LEU          
SEQRES   6 A  317  HIS CYS THR VAL TYR ARG GLY ASP LYS SER GLN ALA SER          
SEQRES   7 A  317  ARG PRO THR PRO ASP GLU LEU GLU ALA VAL ARG LYS TYR          
SEQRES   8 A  317  PHE GLN LEU ASP VAL THR LEU ALA GLN LEU TYR HIS HIS          
SEQRES   9 A  317  TRP GLY SER VAL ASP SER HIS PHE GLN GLU VAL ALA GLN          
SEQRES  10 A  317  LYS PHE GLN GLY VAL ARG LEU LEU ARG GLN ASP PRO ILE          
SEQRES  11 A  317  GLU CYS LEU PHE SER PHE ILE CYS SER SER CYS ASN ASN          
SEQRES  12 A  317  ILE ALA ARG ILE THR GLY MET VAL GLU ARG LEU CYS GLN          
SEQRES  13 A  317  ALA PHE GLY PRO ARG LEU ILE GLN LEU ASP ASP VAL THR          
SEQRES  14 A  317  TYR HIS GLY PHE PRO SER LEU GLN ALA LEU ALA GLY PRO          
SEQRES  15 A  317  GLU VAL GLU ALA HIS LEU ARG LYS LEU GLY LEU GLY TYR          
SEQRES  16 A  317  ARG ALA ARG TYR VAL SER ALA SER ALA ARG ALA ILE LEU          
SEQRES  17 A  317  GLU GLU GLN GLY GLY LEU ALA TRP LEU GLN GLN LEU ARG          
SEQRES  18 A  317  GLU SER SER TYR GLU GLU ALA HIS LYS ALA LEU CYS ILE          
SEQRES  19 A  317  LEU PRO GLY VAL GLY THR LYS VAL ALA ASP CYS ILE CYS          
SEQRES  20 A  317  LEU MET ALA LEU ASP LYS PRO GLN ALA VAL PRO VAL ASP          
SEQRES  21 A  317  VAL HIS MET TRP HIS ILE ALA GLN ARG ASP TYR SER TRP          
SEQRES  22 A  317  HIS PRO THR THR SER GLN ALA LYS GLY PRO SER PRO GLN          
SEQRES  23 A  317  THR ASN LYS GLU LEU GLY ASN PHE PHE ARG SER LEU TRP          
SEQRES  24 A  317  GLY PRO TYR ALA GLY TRP ALA GLN ALA VAL LEU PHE SER          
SEQRES  25 A  317  ALA ASP LEU ARG GLN                                          
SEQRES   1 B   13   DG  DG  DT  DA  DG  DA  DC  DC  DT  DG  DG  DA  DC          
SEQRES   1 C   12   DG  DT  DC  DC  DA FDG  DG  DT  DC  DT  DA  DC              
MODRES 3KTU FDG C   23   DG                                                     
HET    FDG  C  23      24                                                       
HET     CA  A   2       1                                                       
HET     CA  C   1       1                                                       
HETNAM     FDG 2-AMINO-9-(2-DEOXY-2-FLUORO-5-O-PHOSPHONO-BETA-D-                
HETNAM   2 FDG  ARABINOFURANOSYL)-7,9-DIHYDRO-1H-PURINE-6,8-DIONE               
HETNAM      CA CALCIUM ION                                                      
FORMUL   3  FDG    C10 H13 F N5 O8 P                                            
FORMUL   4   CA    2(CA 2+)                                                     
FORMUL   6  HOH   *72(H2 O)                                                     
HELIX    1   1 THR A   19  TRP A   23  5                                   5    
HELIX    2   2 ARG A   34  LEU A   39  1                                   6    
HELIX    3   3 THR A   89  PHE A  100  1                                  12    
HELIX    4   4 THR A  105  ASP A  117  1                                  13    
HELIX    5   6 ASP A  136  CYS A  146  1                                  11    
HELIX    6   7 ASN A  151  GLY A  167  1                                  17    
HELIX    7   8 SER A  183  ALA A  188  1                                   6    
HELIX    8   9 GLU A  191  LEU A  199  1                                   9    
HELIX    9  10 TYR A  203  GLU A  218  1                                  16    
HELIX   10  11 GLY A  221  GLN A  227  1                                   7    
HELIX   11  12 LEU A  228  SER A  231  5                                   4    
HELIX   12  13 SER A  232  CYS A  241  1                                  10    
HELIX   13  14 GLY A  247  LEU A  259  1                                  13    
HELIX   14  15 ASP A  268  SER A  280  1                                  13    
HELIX   15  16 SER A  292  GLY A  308  1                                  17    
HELIX   16  17 TYR A  310  ARG A  324  1                                  15    
SHEET    1   A 5 ALA A  24  PRO A  27  0                                        
SHEET    2   A 5 GLN A  72  TYR A  78 -1  O  CYS A  75   N  ALA A  24           
SHEET    3   A 5 GLN A  62  GLN A  68 -1  N  THR A  67   O  HIS A  74           
SHEET    4   A 5 HIS A  54  LEU A  59 -1  N  LEU A  59   O  GLN A  62           
SHEET    5   A 5 ARG A  48  SER A  51 -1  N  ARG A  48   O  SER A  56           
SHEET    1   B 2 ARG A 169  LEU A 173  0                                        
SHEET    2   B 2 VAL A 176  HIS A 179 -1  O  TYR A 178   N  LEU A 170           
LINK         O3'  DA C  22                 P   FDG C  23     1555   1555  1.63  
LINK         O3' FDG C  23                 P    DG C  24     1555   1555  1.62  
LINK        CA    CA A   2                 O   CYS A 241     1555   1555  2.58  
LINK        CA    CA A   2                 O   LEU A 243     1555   1555  2.83  
LINK        CA    CA A   2                 O   VAL A 246     1555   1555  2.84  
LINK        CA    CA A   2                 OP1  DC C  26     1555   1555  2.64  
LINK        CA    CA C   1                 OP1  DG C  24     1555   1555  2.91  
SITE     1 AC1 15 GLY A  42  SER A 147  ASN A 150  ASN A 151                    
SITE     2 AC1 15 ILE A 152  LYS A 249  MET A 257  PRO A 266                    
SITE     3 AC1 15 ASP A 268  HIS A 270  GLN A 315  PHE A 319                    
SITE     4 AC1 15  DA C  22   DG C  24  HOH C 109                               
SITE     1 AC2  4 CYS A 241  LEU A 243  VAL A 246   DC C  26                    
SITE     1 AC3  2 VAL A 269   DG C  24                                          
CRYST1   92.400   92.400  212.500  90.00  90.00 120.00 P 65 2 2     12          
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      0.010823  0.006248  0.000000        0.00000                         
SCALE2      0.000000  0.012497  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004706        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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