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