HEADER HYDROLASE/DNA 03-JUN-02 1LWY
TITLE HOGG1 BOROHYDRIDE-TRAPPED INTERMEDIATE WITHOUT 8-OXOGUANINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 5'-
COMPND 3 D(*GP*GP*TP*AP*GP*AP*CP*CP*TP*GP*GP*AP*CP*GP*C)-3';
COMPND 4 CHAIN: D;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: 5'-D(*GP*CP*GP*TP*CP*CP*AP*(PED)
COMPND 8 P*GP*TP*CP*TP*AP*CP*C)-3';
COMPND 9 CHAIN: E;
COMPND 10 ENGINEERED: YES;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: 8-OXOGUANINE DNA GLYCOSYLASE;
COMPND 13 CHAIN: A;
COMPND 14 FRAGMENT: CORE FRAGMENT (RESIDUES 12 TO 327);
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 GENE: OGG1;
SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 11 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS DNA REPAIR, DNA GLYCOSYLASE, PROTEIN/DNA, BOROHYDRIDE,
KEYWDS 2 COVALENT TRAPPING, PRODUCT-ASSISTED CATALYSIS, REACTION
KEYWDS 3 INTERMEDIATE, HYDROLASE/DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.C.FROMME,S.D.BRUNER,W.YANG,M.KARPLUS,G.L.VERDINE
REVDAT 3 24-FEB-09 1LWY 1 VERSN
REVDAT 2 04-MAR-03 1LWY 1 JRNL
REVDAT 1 25-FEB-03 1LWY 0
JRNL AUTH J.C.FROMME,S.D.BRUNER,W.YANG,M.KARPLUS,G.L.VERDINE
JRNL TITL PRODUCT-ASSISTED CATALYSIS IN BASE EXCISION DNA
JRNL TITL 2 REPAIR
JRNL REF NAT.STRUCT.BIOL. V. 10 204 2003
JRNL REFN ISSN 1072-8368
JRNL PMID 12592398
JRNL DOI 10.1038/NSB902
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.01 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
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) : 2.01
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 86.1
REMARK 3 NUMBER OF REFLECTIONS : 31075
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) : 0.222
REMARK 3 FREE R VALUE : 0.258
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 3082
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) : 2.01
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.08
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 60.53
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2760
REMARK 3 BIN FREE R VALUE : 0.3167
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 228
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 : 2476
REMARK 3 NUCLEIC ACID ATOMS : 598
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 214
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.27
REMARK 3 ESD FROM SIGMAA (A) : 0.24
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) : 0.32
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.30
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) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1LWY COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JUN-02.
REMARK 100 THE RCSB ID CODE IS RCSB016362.
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 : 6.3
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 : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35772
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 4.300
REMARK 200 R MERGE (I) : 0.07100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.52600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: 1EBM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.36
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.82
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CACODYLATE, CALCIUM ACETATE,
REMARK 280 PEG 8000, PH 6.3, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 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 140.87333
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 70.43667
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 105.65500
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 35.21833
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 176.09167
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 140.87333
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 70.43667
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 35.21833
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 105.65500
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 176.09167
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: D, E, 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 ALA A 4
REMARK 465 MET A 5
REMARK 465 ALA A 6
REMARK 465 ASP A 7
REMARK 465 ILE A 8
REMARK 465 GLY A 80
REMARK 465 ASP A 81
REMARK 465 LYS A 82
REMARK 465 SER A 326
REMARK 465 ARG A 327
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 PED E 23 O3P
REMARK 470 LYS A 98 CG CD CE NZ
REMARK 470 ARG A 134 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 325 CB CG CD OE1 NE2
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 D 15 O3' DC D 15 11655 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 THR A 19 59.93 -117.05
REMARK 500 LEU A 22 47.47 -102.07
REMARK 500 CYS A 28 105.32 -171.55
REMARK 500 GLN A 43 -62.00 -94.04
REMARK 500 LEU A 170 -90.17 -99.54
REMARK 500 ASP A 174 -129.94 55.64
REMARK 500 GLU A 218 -30.93 -144.55
REMARK 500 LYS A 261 76.98 -113.68
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1HU0 RELATED DB: PDB
REMARK 900 1HU0 IS THE CRYSTAL STRUCTURE OF AN HOGG1-DNA BOROHYDRIDE
REMARK 900 TRAPPED INTERMEDIATE COMPLEX
REMARK 900 RELATED ID: 1LWV RELATED DB: PDB
REMARK 900 1LWV IS BOROHYDRIDE-TRAPPED HOGG1 INTERMEDIATE STRUCTURE CO
REMARK 900 -CRYSTALLIZED WITH 8-AMINOGUANINE
REMARK 900 RELATED ID: 1LWW RELATED DB: PDB
REMARK 900 1LWW IS BOROHYDRIDE-TRAPPED HOGG1 INTERMEDIATE STRUCTURE CO
REMARK 900 -CRYSTALLIZED WITH 8-BROMOGUANINE
REMARK 900 RELATED ID: 1EBM RELATED DB: PDB
REMARK 900 1EBM IS THE CRYSTAL STRUCTURE OF THE HUMAN 8-OXOGUANINE
REMARK 900 GLYCOSYLASE (HOGG1) BOUND TO A SUBSTRATE OLIGONUCLEOTIDE
REMARK 900 RELATED ID: 1FN7 RELATED DB: PDB
REMARK 900 1FN7 IS THE COUPLING OF DAMAGE RECOGNITION AND CATALYSIS BY
REMARK 900 A HUMAN BASE-EXCISION DNA REPAIR PROTEIN
DBREF 1LWY A 12 327 UNP O15527 OGG1_HUMAN 12 327
DBREF 1LWY D 1 15 PDB 1LWY 1LWY 1 15
DBREF 1LWY E 16 30 PDB 1LWY 1LWY 16 30
SEQADV 1LWY ALA A 4 UNP O15527 CLONING ARTIFACT
SEQADV 1LWY MET A 5 UNP O15527 CLONING ARTIFACT
SEQADV 1LWY ALA A 6 UNP O15527 CLONING ARTIFACT
SEQADV 1LWY ASP A 7 UNP O15527 CLONING ARTIFACT
SEQADV 1LWY ILE A 8 UNP O15527 CLONING ARTIFACT
SEQADV 1LWY GLY A 9 UNP O15527 CLONING ARTIFACT
SEQADV 1LWY SER A 10 UNP O15527 CLONING ARTIFACT
SEQADV 1LWY GLU A 11 UNP O15527 CLONING ARTIFACT
SEQRES 1 D 15 DG DG DT DA DG DA DC DC DT DG DG DA DC
SEQRES 2 D 15 DG DC
SEQRES 1 E 15 DG DC DG DT DC DC DA PED DG DT DC DT DA
SEQRES 2 E 15 DC DC
SEQRES 1 A 324 ALA MET ALA ASP ILE GLY SER GLU GLY HIS ARG THR LEU
SEQRES 2 A 324 ALA SER THR PRO ALA LEU TRP ALA SER ILE PRO CYS PRO
SEQRES 3 A 324 ARG SER GLU LEU ARG LEU ASP LEU VAL LEU PRO SER GLY
SEQRES 4 A 324 GLN SER PHE ARG TRP ARG GLU GLN SER PRO ALA HIS TRP
SEQRES 5 A 324 SER GLY VAL LEU ALA ASP GLN VAL TRP THR LEU THR GLN
SEQRES 6 A 324 THR GLU GLU GLN LEU HIS CYS THR VAL TYR ARG GLY ASP
SEQRES 7 A 324 LYS SER GLN ALA SER ARG PRO THR PRO ASP GLU LEU GLU
SEQRES 8 A 324 ALA VAL ARG LYS TYR PHE GLN LEU ASP VAL THR LEU ALA
SEQRES 9 A 324 GLN LEU TYR HIS HIS TRP GLY SER VAL ASP SER HIS PHE
SEQRES 10 A 324 GLN GLU VAL ALA GLN LYS PHE GLN GLY VAL ARG LEU LEU
SEQRES 11 A 324 ARG GLN ASP PRO ILE GLU CYS LEU PHE SER PHE ILE CYS
SEQRES 12 A 324 SER SER ASN ASN ASN ILE ALA ARG ILE THR GLY MET VAL
SEQRES 13 A 324 GLU ARG LEU CYS GLN ALA PHE GLY PRO ARG LEU ILE GLN
SEQRES 14 A 324 LEU ASP ASP VAL THR TYR HIS GLY PHE PRO SER LEU GLN
SEQRES 15 A 324 ALA LEU ALA GLY PRO GLU VAL GLU ALA HIS LEU ARG LYS
SEQRES 16 A 324 LEU GLY LEU GLY TYR ARG ALA ARG TYR VAL SER ALA SER
SEQRES 17 A 324 ALA ARG ALA ILE LEU GLU GLU GLN GLY GLY LEU ALA TRP
SEQRES 18 A 324 LEU GLN GLN LEU ARG GLU SER SER TYR GLU GLU ALA HIS
SEQRES 19 A 324 LYS ALA LEU CYS ILE LEU PRO GLY VAL GLY THR LYS VAL
SEQRES 20 A 324 ALA ASP CYS ILE CYS LEU MET ALA LEU ASP LYS PRO GLN
SEQRES 21 A 324 ALA VAL PRO VAL ASP VAL HIS MET TRP HIS ILE ALA GLN
SEQRES 22 A 324 ARG ASP TYR SER TRP HIS PRO THR THR SER GLN ALA LYS
SEQRES 23 A 324 GLY PRO SER PRO GLN THR ASN LYS GLU LEU GLY ASN PHE
SEQRES 24 A 324 PHE ARG SER LEU TRP GLY PRO TYR ALA GLY TRP ALA GLN
SEQRES 25 A 324 ALA VAL LEU PHE SER ALA ASP LEU ARG GLN SER ARG
HET PED E 23 11
HETNAM PED PENTANE-3,4-DIOL-5-PHOSPHATE
HETSYN PED OPEN FORM OF 1'-2'-DIDEOXYRIBOFURANOSE-5'-PHOSPHATE
FORMUL 2 PED C5 H13 O6 P
FORMUL 4 HOH *214(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 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 ALA A 188 1 6
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 SER A 232 CYS A 241 1 10
HELIX 13 13 GLY A 247 LEU A 259 1 13
HELIX 14 14 ASP A 268 SER A 280 1 13
HELIX 15 15 SER A 292 GLY A 308 1 17
HELIX 16 16 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 VAL A 176 N LEU A 173
LINK C1' PED E 23 NZ LYS A 249 1555 1555 1.46
LINK O3' DA E 22 P PED E 23 1555 1555 1.60
LINK O3' PED E 23 P DG E 24 1555 1555 1.60
CRYST1 92.032 92.032 211.310 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 0.010866 0.006273 0.000000 0.00000
SCALE2 0.000000 0.012547 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004732 0.00000
(ATOM LINES ARE NOT SHOWN.)
END