HEADER HYDROLASE, LYASE/DNA 25-OCT-02 1N3A
TITLE STRUCTURAL AND BIOCHEMICAL EXPLORATION OF A CRITICAL AMINO ACID IN
TITLE 2 HUMAN 8-OXOGUANINE GLYCOSYLASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA COMPLEMENT STRAND;
COMPND 3 CHAIN: B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: DNA INHIBITOR STRAND;
COMPND 7 CHAIN: C;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: N-GLYCOSYLASE/DNA LYASE;
COMPND 11 CHAIN: A;
COMPND 12 SYNONYM: HOGG1 ENZYME, 8-OXOGUANOSINE DNA GLYCOSYLASE/DNA-(APURINIC
COMPND 13 OR APYRIMIDINIC SITE) LYASE;
COMPND 14 EC: 3.2.2.-, 4.2.99.18;
COMPND 15 ENGINEERED: YES;
COMPND 16 MUTATION: 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 GENE: OGG1;
SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 11 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 12 EXPRESSION_SYSTEM_STRAIN: BL21 DE3;
SOURCE 13 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 14 EXPRESSION_SYSTEM_PLASMID: PET30A
KEYWDS HHH-GPD, GLYCOSYLASE, DNA-REPAIR, OXOGUANINE, HYDROLASE, LYASE-DNA
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR D.P.NORMAN,S.J.CHUNG,G.L.VERDINE
REVDAT 4 14-FEB-24 1N3A 1 REMARK
REVDAT 3 27-OCT-21 1N3A 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1N3A 1 VERSN
REVDAT 1 04-MAR-03 1N3A 0
JRNL AUTH D.P.NORMAN,S.J.CHUNG,G.L.VERDINE
JRNL TITL STRUCTURAL AND BIOCHEMICAL EXPLORATION OF A CRITICAL AMINO
JRNL TITL 2 ACID IN HUMAN 8-OXOGUANINE GLYCOSYLASE
JRNL REF BIOCHEMISTRY V. 42 1564 2003
JRNL REFN ISSN 0006-2960
JRNL PMID 12578369
JRNL DOI 10.1021/BI026823D
REMARK 2
REMARK 2 RESOLUTION. 2.20 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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.93
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) (%) : 95.1
REMARK 3 NUMBER OF REFLECTIONS : 26543
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) : 0.240
REMARK 3 FREE R VALUE : 0.262
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1346
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.34
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3948
REMARK 3 BIN R VALUE (WORKING SET) : 0.3120
REMARK 3 BIN FREE R VALUE : 0.3270
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.40
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 227
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.022
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2440
REMARK 3 NUCLEIC ACID ATOMS : 598
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 148
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 28.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 48.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 5.28000
REMARK 3 B22 (A**2) : 5.28000
REMARK 3 B33 (A**2) : -10.57000
REMARK 3 B12 (A**2) : 4.05000
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) : 0.35
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.33
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 20.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.890
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) : 1.360 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.170 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.950 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.920 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 42.75
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
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
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1N3A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-OCT-02.
REMARK 100 THE DEPOSITION ID IS D_1000017464.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-APR-01
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : A1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.93
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29555
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
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 (%) : 95.9
REMARK 200 DATA REDUNDANCY : 5.100
REMARK 200 R MERGE (I) : 0.06400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.34
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.40300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.700
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: 1FN7
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.36
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.88
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CACODYLATE, CALCIUM ACETATE, 16-18%
REMARK 280 PEG 8000, PH 6.5, 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 140.85133
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 70.42567
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 105.63850
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 35.21283
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 176.06417
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 140.85133
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 70.42567
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 35.21283
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 105.63850
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 176.06417
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: B, C, 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 OE2 GLU A 32 O HOH A 450 1.94
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 O3' DC B 15 O3' DC B 15 11655 1.89
REMARK 500 O2 DC B 15 O2 DC B 15 11655 2.18
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 28 102.17 -171.74
REMARK 500 PHE A 127 72.32 -116.84
REMARK 500 LEU A 170 -94.47 -100.06
REMARK 500 ASP A 174 -131.00 53.02
REMARK 500 GLU A 218 -23.64 -143.66
REMARK 500 TYR A 310 30.11 -99.40
REMARK 500 ARG A 324 42.85 -69.85
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 C 1 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 DA C 22 OP2
REMARK 620 2 HOH C 32 O 100.3
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
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: 1EBM RELATED DB: PDB
REMARK 900 K249Q HOGG1 BOUND TO OXOG CONTAINING DNA
REMARK 900 RELATED ID: 1FN7 RELATED DB: PDB
REMARK 900 WILD-TYPE HOGG1 BOUND TO ABASIC THF INHIBITOR
REMARK 900 RELATED ID: 1KO9 RELATED DB: PDB
REMARK 900 UNBOUND HOGG1
REMARK 900 RELATED ID: 1N39 RELATED DB: PDB
REMARK 900 D268E HOGG1 BOUND TO ABASIC THF INHIBITOR
DBREF 1N3A A 12 325 UNP O15527 OGG1_HUMAN 12 325
DBREF 1N3A B 1 15 PDB 1N3A 1N3A 1 15
DBREF 1N3A C 16 30 PDB 1N3A 1N3A 16 30
SEQADV 1N3A GLY A 9 UNP O15527 CLONING ARTIFACT
SEQADV 1N3A SER A 10 UNP O15527 CLONING ARTIFACT
SEQADV 1N3A GLU A 11 UNP O15527 CLONING ARTIFACT
SEQADV 1N3A GLN A 268 UNP O15527 ASP 268 ENGINEERED MUTATION
SEQRES 1 B 15 DG DG DT DA DG DA DC DC DT DG DG DA DC
SEQRES 2 B 15 DG DC
SEQRES 1 C 15 DG DC DG DT DC DC DA 3DR DG DT DC DT DA
SEQRES 2 C 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 GLN
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 C 23 11
HET CA C 1 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 *148(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 PHE A 127 1 11
HELIX 6 6 ASP A 136 CYS A 146 1 11
HELIX 7 7 ASN A 151 GLY A 167 1 17
HELIX 8 8 SER A 183 GLY A 189 1 7
HELIX 9 9 GLU A 191 LEU A 199 1 9
HELIX 10 10 TYR A 203 GLU A 218 1 16
HELIX 11 11 GLY A 221 LEU A 228 1 8
HELIX 12 12 ARG A 229 SER A 231 5 3
HELIX 13 13 SER A 232 CYS A 241 1 10
HELIX 14 14 GLY A 247 LEU A 259 1 13
HELIX 15 15 GLN A 268 SER A 280 1 13
HELIX 16 16 SER A 292 GLY A 308 1 17
HELIX 17 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 VAL A 63 GLN A 68 -1 N THR A 67 O HIS A 74
SHEET 4 A 5 HIS A 54 VAL A 58 -1 N TRP A 55 O LEU A 66
SHEET 5 A 5 ARG A 48 SER A 51 -1 N SER A 51 O HIS A 54
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 C 22 P 3DR C 23 1555 1555 1.60
LINK O3' 3DR C 23 P DG C 24 1555 1555 1.60
LINK CA CA C 1 OP2 DA C 22 1555 1555 3.04
LINK CA CA C 1 O HOH C 32 1555 1555 2.47
SITE 1 AC1 2 DA C 22 HOH C 32
CRYST1 92.366 92.366 211.277 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 0.010826 0.006251 0.000000 0.00000
SCALE2 0.000000 0.012501 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004733 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
