HEADER HYDROLASE/DNA 21-AUG-00 1FN7
TITLE COUPLING OF DAMAGE RECOGNITION AND CATALYSIS BY A HUMAN BASE-EXCISION
TITLE 2 DNA REPAIR PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA (5'-D(*GP*GP*TP*AP*GP*AP*CP*CP*TP*GP*GP*AP*CP*GP*C)-
COMPND 3 3');
COMPND 4 CHAIN: C;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: DNA (5'-D(*GP*CP*GP*TP*CP*CP*AP*(3DR)
COMPND 8 P*GP*TP*CP*TP*AP*CP*C)-3');
COMPND 9 CHAIN: D;
COMPND 10 ENGINEERED: YES;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: 8-OXOGUANINE DNA GLYCOSYLASE 1;
COMPND 13 CHAIN: A;
COMPND 14 SYNONYM: HOGG1, DNA GLYCOSYLASE/AP LYASE;
COMPND 15 EC: 3.2.2.-;
COMPND 16 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 MOL_ID: 2;
SOURCE 4 SYNTHETIC: YES;
SOURCE 5 MOL_ID: 3;
SOURCE 6 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 7 ORGANISM_COMMON: HUMAN;
SOURCE 8 ORGANISM_TAXID: 9606;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PET30A-TRUNC.HOGG1
KEYWDS DNA REPAIR, DNA GLYCOSYLASE, PROTEIN/DNA, HELIX HAIRPIN HELIX, BASE
KEYWDS 2 RECOGNITION, OXOGUANINE, HYDROXYGUANINE, BASE FLIPPING, FLIPPED-OUT
KEYWDS 3 BASE, EXTRAHELICAL DNA, MECHANISM-BASED INHIBITOR, BASE-EXICISION
KEYWDS 4 REPAIR, AP LYASE, DNA GLYCOSIDASE, HYDROLASE-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR D.P.G.NORMAN,S.D.BRUNER,G.L.VERDINE
REVDAT 4 07-FEB-24 1FN7 1 SEQADV LINK
REVDAT 3 24-FEB-09 1FN7 1 VERSN
REVDAT 2 01-APR-03 1FN7 1 JRNL
REVDAT 1 21-APR-01 1FN7 0
JRNL AUTH D.P.NORMAN,S.D.BRUNER,G.L.VERDINE
JRNL TITL COUPLING OF SUBSTRATE RECOGNITION AND CATALYSIS BY A HUMAN
JRNL TITL 2 BASE-EXCISION DNA REPAIR PROTEIN.
JRNL REF J.AM.CHEM.SOC. V. 123 359 2001
JRNL REFN ISSN 0002-7863
JRNL PMID 11456534
JRNL DOI 10.1021/JA003144M
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.D.BRUNER,D.P.G.NORMAN,G.L.VERDINE
REMARK 1 TITL STRUCTURAL BASIS FOR RECOGNITION AND REPAIR OF THE
REMARK 1 TITL 2 ENDOGENOUS MUTAGEN 8-OXOGUANINE IN DNA
REMARK 1 REF NATURE V. 403 859 2000
REMARK 1 REFN ISSN 0028-0836
REMARK 1 DOI 10.1038/35002510
REMARK 2
REMARK 2 RESOLUTION. 2.60 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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.85
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 294195.160
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 87.0
REMARK 3 NUMBER OF REFLECTIONS : 14841
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.221
REMARK 3 FREE R VALUE : 0.270
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1505
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.76
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 69.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1752
REMARK 3 BIN R VALUE (WORKING SET) : 0.2640
REMARK 3 BIN FREE R VALUE : 0.3610
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 175
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.027
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2439
REMARK 3 NUCLEIC ACID ATOMS : 598
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 132
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 35.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.05000
REMARK 3 B22 (A**2) : 4.05000
REMARK 3 B33 (A**2) : -8.10000
REMARK 3 B12 (A**2) : 6.93000
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) : 0.32
REMARK 3 ESD FROM SIGMAA (A) : 0.32
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.42
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.46
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 20.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.900
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.150 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.980 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.460 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.300 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.34
REMARK 3 BSOL : 39.06
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.PA
REMARK 3 PARAMETER FILE 2 : DNA-RNA_REP.PA
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARA
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : DNA-RNA.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 CONFORMATION OF THE ABASIC DEOXYRIBOSE RING WAS DETERMINED BY
REMARK 3 MODELING IT AS RNA
REMARK 3 (C3'-ENDO) AND DNA (C2'-ENDO), AND PERFORMING SIMULATED ANNEALING
REMARK 3 ON
REMARK 3 BOTH MODELS. WHEN MODELED IN THE C2'-ENDO CONFORMATION, R AND RFREE
REMARK 3 WERE LOWER, AND THE MODEL FIT THE EXPERIMENTAL FO-FC OMIT DENSITY
REMARK 3 BETTER
REMARK 4
REMARK 4 1FN7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY NDB.
REMARK 100 THE DEPOSITION ID IS D_1000011734.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-MAR-00
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0332
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : SBC-1
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17653
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.6
REMARK 200 DATA REDUNDANCY : 4.740
REMARK 200 R MERGE (I) : 0.07300
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) : 2.54
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.15
REMARK 200 R MERGE FOR SHELL (I) : 0.35200
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: NULL
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.87
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM SODIUM CACODYLATE PH 6.5, 200
REMARK 280 MM CALCIUM ACETATE, 16-18% PEG, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 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 140.67600
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 70.33800
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 105.50700
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 35.16900
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 175.84500
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 140.67600
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 70.33800
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 35.16900
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 105.50700
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 175.84500
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 APPLY THE FOLLOWING TO CHAINS: C, D, A
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 GLU A 71 CG CD OE1 OE2
REMARK 470 GLN A 84 CG CD OE1 NE2
REMARK 470 ARG A 87 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 122 CG CD OE1 OE2
REMARK 470 GLN A 125 CG CD OE1 NE2
REMARK 470 GLN A 128 CG CD OE1 NE2
REMARK 470 ARG A 134 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 164 CG CD OE1 NE2
REMARK 470 GLN A 227 CG CD OE1 NE2
REMARK 470 SER A 286 OG
REMARK 470 LYS A 289 CG CD CE NZ
REMARK 470 GLN A 294 CG CD OE1 NE2
REMARK 470 GLN A 325 CG CD OE1 NE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OE1 GLU A 32 N LEU A 106 2.19
REMARK 500 O CYS A 241 O HOH A 425 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 410 O HOH A 410 10665 1.78
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 28 112.14 -173.87
REMARK 500 GLU A 122 -72.57 -64.24
REMARK 500 LEU A 170 -90.68 -102.69
REMARK 500 ASP A 174 -127.27 53.53
REMARK 500 GLN A 287 -78.14 -104.06
REMARK 500 PRO A 309 -37.08 -39.85
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EBM RELATED DB: PDB
REMARK 900 1EBM CONTAINS A CATALYTICALLY INACTIVE MUTANT BOUND TO AN OXOG-
REMARK 900 CONTAINING DNA
DBREF 1FN7 A 9 325 UNP O15527 OGG1_HUMAN 12 325
DBREF 1FN7 C 1 15 PDB 1FN7 1FN7 1 15
DBREF 1FN7 D 16 30 PDB 1FN7 1FN7 16 30
SEQADV 1FN7 GLY A 9 UNP O15527 ARG 9 CONFLICT
SEQADV 1FN7 SER A 10 UNP O15527 ARG 10 CONFLICT
SEQADV 1FN7 GLU A 11 UNP O15527 MET 11 CONFLICT
SEQRES 1 C 15 DG DG DT DA DG DA DC DC DT DG DG DA DC
SEQRES 2 C 15 DG DC
SEQRES 1 D 15 DG DC DG DT DC DC DA 3DR DG DT DC DT DA
SEQRES 2 D 15 DC DC
SEQRES 1 A 317 GLY SER GLU 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 ASN 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
HET 3DR D 23 11
HET CA D1001 1
HETNAM 3DR 1',2'-DIDEOXYRIBOFURANOSE-5'-PHOSPHATE
HETNAM CA CALCIUM ION
HETSYN 3DR ABASIC DIDEOXYRIBOSE
FORMUL 2 3DR C5 H11 O6 P
FORMUL 4 CA CA 2+
FORMUL 5 HOH *132(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 5 ASP A 117 GLN A 125 1 9
HELIX 6 6 LYS A 126 GLN A 128 5 3
HELIX 7 7 ASP A 136 CYS A 146 1 11
HELIX 8 8 ASN A 151 GLY A 167 1 17
HELIX 9 9 SER A 183 GLY A 189 1 7
HELIX 10 10 GLU A 191 LYS A 198 1 8
HELIX 11 11 LEU A 199 GLY A 200 5 2
HELIX 12 12 LEU A 201 GLY A 202 5 2
HELIX 13 13 TYR A 203 GLN A 219 1 17
HELIX 14 14 GLY A 221 ARG A 229 1 9
HELIX 15 15 SER A 232 CYS A 241 1 10
HELIX 16 16 GLY A 247 LEU A 259 1 13
HELIX 17 17 ASP A 268 SER A 280 1 13
HELIX 18 18 SER A 292 GLY A 308 1 17
HELIX 19 19 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 N LEU A 73 O ILE A 26
SHEET 3 A 5 GLN A 62 GLN A 68 -1 O VAL A 63 N TYR A 78
SHEET 4 A 5 HIS A 54 LEU A 59 -1 N TRP A 55 O LEU A 66
SHEET 5 A 5 ARG A 48 SER A 51 -1 O ARG A 48 N 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 VAL A 176 N LEU A 173
LINK O3' DA D 22 P 3DR D 23 1555 1555 1.61
LINK O3' 3DR D 23 P DG D 24 1555 1555 1.61
CRYST1 92.113 92.113 211.014 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 0.010856 0.006268 0.000000 0.00000
SCALE2 0.000000 0.012536 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004739 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
