HEADER HYDROLASE/DNA 21-APR-08 3CW7
TITLE CRYSTAL STRUCTURE OF AN ALKA HOST/GUEST COMPLEX 8OXOGUANINE:CYTOSINE
TITLE 2 BASE PAIR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA-3-METHYLADENINE GLYCOSYLASE 2;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: DNA-3-METHYLADENINE GLYCOSYLASE II, 3-METHYLADENINE-DNA
COMPND 5 GLYCOSYLASE II, INDUCIBLE, TAG II, DNA-3-METHYLADENINE GLYCOSIDASE
COMPND 6 II;
COMPND 7 EC: 3.2.2.21;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: DNA (5'-D(*DGP*DAP*DCP*DAP*DTP*DGP*DAP*(8OG)
COMPND 11 P*DTP*DGP*DCP*DC)-3');
COMPND 12 CHAIN: E, G;
COMPND 13 ENGINEERED: YES;
COMPND 14 OTHER_DETAILS: 8OXOGUANINE CONTAINING DNA;
COMPND 15 MOL_ID: 3;
COMPND 16 MOLECULE: DNA (5'-D(*DGP*DGP*DCP*DAP*DCP*DTP*DCP*DAP*DTP*DGP*DTP*DC)-
COMPND 17 3');
COMPND 18 CHAIN: F, H;
COMPND 19 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_COMMON: STRAIN K12;
SOURCE 4 GENE: ALKA, AIDA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET30;
SOURCE 9 MOL_ID: 2;
SOURCE 10 SYNTHETIC: YES;
SOURCE 11 MOL_ID: 3;
SOURCE 12 SYNTHETIC: YES
KEYWDS ALKA, 8OXOGUANINE, DNA REPAIR, HOST-GUEST COMPLEX, DNA STRUCTURE, DNA
KEYWDS 2 DAMAGE, HYDROLASE, HYDROLASE-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR B.R.BOWMAN,S.LEE,S.WANG,G.L.VERDINE
REVDAT 6 21-FEB-24 3CW7 1 DBREF LINK
REVDAT 5 25-OCT-17 3CW7 1 REMARK
REVDAT 4 24-FEB-09 3CW7 1 VERSN
REVDAT 3 18-NOV-08 3CW7 1 COMPND
REVDAT 2 09-SEP-08 3CW7 1 SOURCE
REVDAT 1 02-SEP-08 3CW7 0
JRNL AUTH B.R.BOWMAN,S.LEE,S.WANG,G.L.VERDINE
JRNL TITL STRUCTURE OF THE E. COLI DNA GLYCOSYLASE ALKA BOUND TO THE
JRNL TITL 2 ENDS OF DUPLEX DNA: A SYSTEM FOR THE STRUCTURE DETERMINATION
JRNL TITL 3 OF LESION-CONTAINING DNA.
JRNL REF STRUCTURE V. 16 1166 2008
JRNL REFN ISSN 0969-2126
JRNL PMID 18682218
JRNL DOI 10.1016/J.STR.2008.04.012
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) : 50.00
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) (%) : 87.9
REMARK 3 NUMBER OF REFLECTIONS : 60806
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) : 0.218
REMARK 3 FREE R VALUE : 0.260
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 8.900
REMARK 3 FREE R VALUE TEST SET COUNT : 6149
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 : 8860
REMARK 3 NUCLEIC ACID ATOMS : 974
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 27
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 61.67
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -5.82200
REMARK 3 B22 (A**2) : -2.03000
REMARK 3 B33 (A**2) : 7.85300
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -10.90000
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) : 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 : 32.44
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 : CNS_TOPPAR:PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : OXO_PAR.TXT*
REMARK 3 PARAMETER FILE 3 : CNS_TOPPAR:DNA-RNA.PARAM
REMARK 3 PARAMETER FILE 4 : DNA-RNA_REP_DIHEDRAL_COMTOUT.PARAM
REMARK 3 PARAMETER FILE 5 : CNS_TOPPAR:WATER_REP.PARAM
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 3CW7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-APR-08.
REMARK 100 THE DEPOSITION ID IS D_1000047286.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
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) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 64696
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 (%) : 95.1
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.7000
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 (%) : 89.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.30
REMARK 200 R MERGE FOR SHELL (I) : 0.32200
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: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.81
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG4000, NACL, NA-HEPES, MGCL2,
REMARK 280 ETHYLENE GLYCOL, PH 8.0, HANGING DROP VAPOR DIFFUSION,
REMARK 280 TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
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 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 50.79700
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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 300 REMARK: BIOLOGICAL UNIT IS A PROTEIN MONOMER
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: OCTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10780 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 54160 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -51.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H
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 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 O GLN B 210 O HOH B 288 2.10
REMARK 500
REMARK 500 REMARK: NULL
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 B 150 C - N - CA ANGL. DEV. = 9.1 DEGREES
REMARK 500 DC F 18 O3' - P - O5' ANGL. DEV. = -14.3 DEGREES
REMARK 500 DC F 18 O3' - P - OP1 ANGL. DEV. = 8.5 DEGREES
REMARK 500 DC F 18 O5' - P - OP1 ANGL. DEV. = -17.1 DEGREES
REMARK 500 DC F 18 C5' - C4' - O4' ANGL. DEV. = 13.1 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 SER A 26 -20.08 89.56
REMARK 500 PRO A 103 -9.73 -58.51
REMARK 500 LEU A 125 -52.68 76.66
REMARK 500 PHE A 245 69.60 -119.16
REMARK 500 TYR A 273 31.12 -99.86
REMARK 500 SER B 26 -22.99 81.01
REMARK 500 ALA B 65 -36.85 -39.98
REMARK 500 ASP B 112 123.28 -172.99
REMARK 500 PRO B 150 -33.41 -37.15
REMARK 500 PRO B 166 -19.25 -49.81
REMARK 500 PRO B 175 173.44 -53.68
REMARK 500 MET B 248 145.60 -10.39
REMARK 500 PRO B 262 31.83 -97.52
REMARK 500 GLU B 275 -85.94 -33.74
REMARK 500 SER C 26 -17.44 85.43
REMARK 500 HIS C 57 67.05 31.05
REMARK 500 ASP C 83 57.65 39.69
REMARK 500 ARG C 102 78.86 -159.34
REMARK 500 LEU C 125 -64.87 72.67
REMARK 500 PHE C 149 72.97 -151.59
REMARK 500 PRO C 262 30.94 -99.44
REMARK 500 TYR C 273 45.98 -100.10
REMARK 500 GLU C 281 93.13 -67.49
REMARK 500 SER D 26 -18.87 86.56
REMARK 500 LEU D 125 11.13 57.24
REMARK 500 ALA D 171 -18.47 -49.88
REMARK 500 LEU D 235 74.63 -116.68
REMARK 500 PHE D 245 74.71 -117.74
REMARK 500 TYR D 273 40.54 -96.10
REMARK 500 ASP D 280 -160.95 -73.22
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 DA F 17 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3CVS RELATED DB: PDB
REMARK 900 RELATED ID: 3CVT RELATED DB: PDB
REMARK 900 RELATED ID: 3CWA RELATED DB: PDB
REMARK 900 RELATED ID: 3CWS RELATED DB: PDB
REMARK 900 RELATED ID: 3CWT RELATED DB: PDB
REMARK 900 RELATED ID: 3CWU RELATED DB: PDB
DBREF 3CW7 E 1 12 PDB 3CW7 3CW7 1 12
DBREF 3CW7 F 14 25 PDB 3CW7 3CW7 14 25
DBREF 3CW7 G 1 12 PDB 3CW7 3CW7 1 12
DBREF 3CW7 H 14 25 PDB 3CW7 3CW7 14 25
DBREF 3CW7 A 1 282 UNP P04395 3MG2_ECOLI 1 282
DBREF 3CW7 B 1 282 UNP P04395 3MG2_ECOLI 1 282
DBREF 3CW7 C 1 282 UNP P04395 3MG2_ECOLI 1 282
DBREF 3CW7 D 1 282 UNP P04395 3MG2_ECOLI 1 282
SEQRES 1 A 282 MET TYR THR LEU ASN TRP GLN PRO PRO TYR ASP TRP SER
SEQRES 2 A 282 TRP MET LEU GLY PHE LEU ALA ALA ARG ALA VAL SER SER
SEQRES 3 A 282 VAL GLU THR VAL ALA ASP SER TYR TYR ALA ARG SER LEU
SEQRES 4 A 282 ALA VAL GLY GLU TYR ARG GLY VAL VAL THR ALA ILE PRO
SEQRES 5 A 282 ASP ILE ALA ARG HIS THR LEU HIS ILE ASN LEU SER ALA
SEQRES 6 A 282 GLY LEU GLU PRO VAL ALA ALA GLU CYS LEU ALA LYS MET
SEQRES 7 A 282 SER ARG LEU PHE ASP LEU GLN CYS ASN PRO GLN ILE VAL
SEQRES 8 A 282 ASN GLY ALA LEU GLY ARG LEU GLY ALA ALA ARG PRO GLY
SEQRES 9 A 282 LEU ARG LEU PRO GLY CYS VAL ASP ALA PHE GLU GLN GLY
SEQRES 10 A 282 VAL ARG ALA ILE LEU GLY GLN LEU VAL SER VAL ALA MET
SEQRES 11 A 282 ALA ALA LYS LEU THR ALA ARG VAL ALA GLN LEU TYR GLY
SEQRES 12 A 282 GLU ARG LEU ASP ASP PHE PRO GLU TYR ILE CYS PHE PRO
SEQRES 13 A 282 THR PRO GLN ARG LEU ALA ALA ALA ASP PRO GLN ALA LEU
SEQRES 14 A 282 LYS ALA LEU GLY MET PRO LEU LYS ARG ALA GLU ALA LEU
SEQRES 15 A 282 ILE HIS LEU ALA ASN ALA ALA LEU GLU GLY THR LEU PRO
SEQRES 16 A 282 MET THR ILE PRO GLY ASP VAL GLU GLN ALA MET LYS THR
SEQRES 17 A 282 LEU GLN THR PHE PRO GLY ILE GLY ARG TRP THR ALA ASN
SEQRES 18 A 282 TYR PHE ALA LEU ARG GLY TRP GLN ALA LYS ASP VAL PHE
SEQRES 19 A 282 LEU PRO ASP ASP TYR LEU ILE LYS GLN ARG PHE PRO GLY
SEQRES 20 A 282 MET THR PRO ALA GLN ILE ARG ARG TYR ALA GLU ARG TRP
SEQRES 21 A 282 LYS PRO TRP ARG SER TYR ALA LEU LEU HIS ILE TRP TYR
SEQRES 22 A 282 THR GLU GLY TRP GLN PRO ASP GLU ALA
SEQRES 1 B 282 MET TYR THR LEU ASN TRP GLN PRO PRO TYR ASP TRP SER
SEQRES 2 B 282 TRP MET LEU GLY PHE LEU ALA ALA ARG ALA VAL SER SER
SEQRES 3 B 282 VAL GLU THR VAL ALA ASP SER TYR TYR ALA ARG SER LEU
SEQRES 4 B 282 ALA VAL GLY GLU TYR ARG GLY VAL VAL THR ALA ILE PRO
SEQRES 5 B 282 ASP ILE ALA ARG HIS THR LEU HIS ILE ASN LEU SER ALA
SEQRES 6 B 282 GLY LEU GLU PRO VAL ALA ALA GLU CYS LEU ALA LYS MET
SEQRES 7 B 282 SER ARG LEU PHE ASP LEU GLN CYS ASN PRO GLN ILE VAL
SEQRES 8 B 282 ASN GLY ALA LEU GLY ARG LEU GLY ALA ALA ARG PRO GLY
SEQRES 9 B 282 LEU ARG LEU PRO GLY CYS VAL ASP ALA PHE GLU GLN GLY
SEQRES 10 B 282 VAL ARG ALA ILE LEU GLY GLN LEU VAL SER VAL ALA MET
SEQRES 11 B 282 ALA ALA LYS LEU THR ALA ARG VAL ALA GLN LEU TYR GLY
SEQRES 12 B 282 GLU ARG LEU ASP ASP PHE PRO GLU TYR ILE CYS PHE PRO
SEQRES 13 B 282 THR PRO GLN ARG LEU ALA ALA ALA ASP PRO GLN ALA LEU
SEQRES 14 B 282 LYS ALA LEU GLY MET PRO LEU LYS ARG ALA GLU ALA LEU
SEQRES 15 B 282 ILE HIS LEU ALA ASN ALA ALA LEU GLU GLY THR LEU PRO
SEQRES 16 B 282 MET THR ILE PRO GLY ASP VAL GLU GLN ALA MET LYS THR
SEQRES 17 B 282 LEU GLN THR PHE PRO GLY ILE GLY ARG TRP THR ALA ASN
SEQRES 18 B 282 TYR PHE ALA LEU ARG GLY TRP GLN ALA LYS ASP VAL PHE
SEQRES 19 B 282 LEU PRO ASP ASP TYR LEU ILE LYS GLN ARG PHE PRO GLY
SEQRES 20 B 282 MET THR PRO ALA GLN ILE ARG ARG TYR ALA GLU ARG TRP
SEQRES 21 B 282 LYS PRO TRP ARG SER TYR ALA LEU LEU HIS ILE TRP TYR
SEQRES 22 B 282 THR GLU GLY TRP GLN PRO ASP GLU ALA
SEQRES 1 C 282 MET TYR THR LEU ASN TRP GLN PRO PRO TYR ASP TRP SER
SEQRES 2 C 282 TRP MET LEU GLY PHE LEU ALA ALA ARG ALA VAL SER SER
SEQRES 3 C 282 VAL GLU THR VAL ALA ASP SER TYR TYR ALA ARG SER LEU
SEQRES 4 C 282 ALA VAL GLY GLU TYR ARG GLY VAL VAL THR ALA ILE PRO
SEQRES 5 C 282 ASP ILE ALA ARG HIS THR LEU HIS ILE ASN LEU SER ALA
SEQRES 6 C 282 GLY LEU GLU PRO VAL ALA ALA GLU CYS LEU ALA LYS MET
SEQRES 7 C 282 SER ARG LEU PHE ASP LEU GLN CYS ASN PRO GLN ILE VAL
SEQRES 8 C 282 ASN GLY ALA LEU GLY ARG LEU GLY ALA ALA ARG PRO GLY
SEQRES 9 C 282 LEU ARG LEU PRO GLY CYS VAL ASP ALA PHE GLU GLN GLY
SEQRES 10 C 282 VAL ARG ALA ILE LEU GLY GLN LEU VAL SER VAL ALA MET
SEQRES 11 C 282 ALA ALA LYS LEU THR ALA ARG VAL ALA GLN LEU TYR GLY
SEQRES 12 C 282 GLU ARG LEU ASP ASP PHE PRO GLU TYR ILE CYS PHE PRO
SEQRES 13 C 282 THR PRO GLN ARG LEU ALA ALA ALA ASP PRO GLN ALA LEU
SEQRES 14 C 282 LYS ALA LEU GLY MET PRO LEU LYS ARG ALA GLU ALA LEU
SEQRES 15 C 282 ILE HIS LEU ALA ASN ALA ALA LEU GLU GLY THR LEU PRO
SEQRES 16 C 282 MET THR ILE PRO GLY ASP VAL GLU GLN ALA MET LYS THR
SEQRES 17 C 282 LEU GLN THR PHE PRO GLY ILE GLY ARG TRP THR ALA ASN
SEQRES 18 C 282 TYR PHE ALA LEU ARG GLY TRP GLN ALA LYS ASP VAL PHE
SEQRES 19 C 282 LEU PRO ASP ASP TYR LEU ILE LYS GLN ARG PHE PRO GLY
SEQRES 20 C 282 MET THR PRO ALA GLN ILE ARG ARG TYR ALA GLU ARG TRP
SEQRES 21 C 282 LYS PRO TRP ARG SER TYR ALA LEU LEU HIS ILE TRP TYR
SEQRES 22 C 282 THR GLU GLY TRP GLN PRO ASP GLU ALA
SEQRES 1 D 282 MET TYR THR LEU ASN TRP GLN PRO PRO TYR ASP TRP SER
SEQRES 2 D 282 TRP MET LEU GLY PHE LEU ALA ALA ARG ALA VAL SER SER
SEQRES 3 D 282 VAL GLU THR VAL ALA ASP SER TYR TYR ALA ARG SER LEU
SEQRES 4 D 282 ALA VAL GLY GLU TYR ARG GLY VAL VAL THR ALA ILE PRO
SEQRES 5 D 282 ASP ILE ALA ARG HIS THR LEU HIS ILE ASN LEU SER ALA
SEQRES 6 D 282 GLY LEU GLU PRO VAL ALA ALA GLU CYS LEU ALA LYS MET
SEQRES 7 D 282 SER ARG LEU PHE ASP LEU GLN CYS ASN PRO GLN ILE VAL
SEQRES 8 D 282 ASN GLY ALA LEU GLY ARG LEU GLY ALA ALA ARG PRO GLY
SEQRES 9 D 282 LEU ARG LEU PRO GLY CYS VAL ASP ALA PHE GLU GLN GLY
SEQRES 10 D 282 VAL ARG ALA ILE LEU GLY GLN LEU VAL SER VAL ALA MET
SEQRES 11 D 282 ALA ALA LYS LEU THR ALA ARG VAL ALA GLN LEU TYR GLY
SEQRES 12 D 282 GLU ARG LEU ASP ASP PHE PRO GLU TYR ILE CYS PHE PRO
SEQRES 13 D 282 THR PRO GLN ARG LEU ALA ALA ALA ASP PRO GLN ALA LEU
SEQRES 14 D 282 LYS ALA LEU GLY MET PRO LEU LYS ARG ALA GLU ALA LEU
SEQRES 15 D 282 ILE HIS LEU ALA ASN ALA ALA LEU GLU GLY THR LEU PRO
SEQRES 16 D 282 MET THR ILE PRO GLY ASP VAL GLU GLN ALA MET LYS THR
SEQRES 17 D 282 LEU GLN THR PHE PRO GLY ILE GLY ARG TRP THR ALA ASN
SEQRES 18 D 282 TYR PHE ALA LEU ARG GLY TRP GLN ALA LYS ASP VAL PHE
SEQRES 19 D 282 LEU PRO ASP ASP TYR LEU ILE LYS GLN ARG PHE PRO GLY
SEQRES 20 D 282 MET THR PRO ALA GLN ILE ARG ARG TYR ALA GLU ARG TRP
SEQRES 21 D 282 LYS PRO TRP ARG SER TYR ALA LEU LEU HIS ILE TRP TYR
SEQRES 22 D 282 THR GLU GLY TRP GLN PRO ASP GLU ALA
SEQRES 1 E 12 DG DA DC DA DT DG DA 8OG DT DG DC DC
SEQRES 1 F 12 DG DG DC DA DC DT DC DA DT DG DT DC
SEQRES 1 G 12 DG DA DC DA DT DG DA 8OG DT DG DC DC
SEQRES 1 H 12 DG DG DC DA DC DT DC DA DT DG DT DC
MODRES 3CW7 8OG E 8 DG
MODRES 3CW7 8OG G 8 DG
HET 8OG E 8 23
HET 8OG G 8 23
HETNAM 8OG 8-OXO-2'-DEOXY-GUANOSINE-5'-MONOPHOSPHATE
HETSYN 8OG 8-OXO-7,8-DIHYDRO-2'-DEOXY-GUANOSINE-5'-MONOPHOSPHATE
FORMUL 5 8OG 2(C10 H14 N5 O8 P)
FORMUL 9 HOH *27(H2 O)
HELIX 1 1 ASP A 11 ALA A 23 1 13
HELIX 2 2 ALA A 65 PRO A 69 5 5
HELIX 3 3 VAL A 70 PHE A 82 1 13
HELIX 4 4 ASN A 87 GLY A 96 1 10
HELIX 5 5 ARG A 97 ALA A 100 5 4
HELIX 6 6 ASP A 112 LEU A 122 1 11
HELIX 7 7 SER A 127 GLY A 143 1 17
HELIX 8 8 THR A 157 ALA A 163 1 7
HELIX 9 9 ASP A 165 ALA A 171 1 7
HELIX 10 10 PRO A 175 GLY A 192 1 18
HELIX 11 11 ASP A 201 GLN A 210 1 10
HELIX 12 12 GLY A 216 TRP A 228 1 13
HELIX 13 13 ASP A 238 PHE A 245 1 8
HELIX 14 14 THR A 249 GLU A 258 1 10
HELIX 15 15 ARG A 259 LYS A 261 5 3
HELIX 16 16 TRP A 263 TYR A 273 1 11
HELIX 17 17 ASP B 11 ARG B 22 1 12
HELIX 18 18 ALA B 65 PRO B 69 5 5
HELIX 19 19 VAL B 70 PHE B 82 1 13
HELIX 20 20 ASN B 87 GLY B 96 1 10
HELIX 21 21 ARG B 97 ALA B 100 5 4
HELIX 22 22 ASP B 112 GLY B 123 1 12
HELIX 23 23 SER B 127 GLY B 143 1 17
HELIX 24 24 THR B 157 ALA B 163 1 7
HELIX 25 25 ASP B 165 MET B 174 1 10
HELIX 26 26 PRO B 175 GLU B 191 1 17
HELIX 27 27 ASP B 201 GLN B 210 1 10
HELIX 28 28 GLY B 216 TRP B 228 1 13
HELIX 29 29 ASP B 238 PHE B 245 1 8
HELIX 30 30 THR B 249 GLU B 258 1 10
HELIX 31 31 ARG B 259 LYS B 261 5 3
HELIX 32 32 TRP B 263 TYR B 273 1 11
HELIX 33 33 ASP C 11 ARG C 22 1 12
HELIX 34 34 ALA C 65 PRO C 69 5 5
HELIX 35 35 VAL C 70 PHE C 82 1 13
HELIX 36 36 ASN C 87 LEU C 95 1 9
HELIX 37 37 ASP C 112 GLY C 123 1 12
HELIX 38 38 SER C 127 GLY C 143 1 17
HELIX 39 39 THR C 157 ALA C 164 1 8
HELIX 40 40 ASP C 165 LEU C 172 1 8
HELIX 41 41 PRO C 175 GLY C 192 1 18
HELIX 42 42 ASP C 201 GLN C 210 1 10
HELIX 43 43 GLY C 216 TRP C 228 1 13
HELIX 44 44 ASP C 238 PHE C 245 1 8
HELIX 45 45 THR C 249 GLU C 258 1 10
HELIX 46 46 ARG C 259 LYS C 261 5 3
HELIX 47 47 TRP C 263 TYR C 273 1 11
HELIX 48 48 ASP D 11 ALA D 23 1 13
HELIX 49 49 ALA D 65 PRO D 69 5 5
HELIX 50 50 VAL D 70 PHE D 82 1 13
HELIX 51 51 ASN D 87 GLY D 96 1 10
HELIX 52 52 GLY D 96 ALA D 101 1 6
HELIX 53 53 ASP D 112 LEU D 122 1 11
HELIX 54 54 SER D 127 GLY D 143 1 17
HELIX 55 55 THR D 157 ALA D 163 1 7
HELIX 56 56 ASP D 165 ALA D 171 1 7
HELIX 57 57 PRO D 175 GLU D 191 1 17
HELIX 58 58 ASP D 201 GLN D 210 1 10
HELIX 59 59 GLY D 216 TRP D 228 1 13
HELIX 60 60 ASP D 238 PHE D 245 1 8
HELIX 61 61 THR D 249 GLU D 258 1 10
HELIX 62 62 ARG D 259 LYS D 261 5 3
HELIX 63 63 TRP D 263 TYR D 273 1 11
SHEET 1 A 5 TYR A 2 ASN A 5 0
SHEET 2 A 5 THR A 58 LEU A 63 -1 O ILE A 61 N TYR A 2
SHEET 3 A 5 TYR A 44 ASP A 53 -1 N ILE A 51 O HIS A 60
SHEET 4 A 5 TYR A 35 VAL A 41 -1 N TYR A 35 O ALA A 50
SHEET 5 A 5 GLU A 28 VAL A 30 -1 N THR A 29 O ALA A 36
SHEET 1 B 2 ARG A 145 LEU A 146 0
SHEET 2 B 2 PHE A 149 ILE A 153 -1 O TYR A 152 N LEU A 146
SHEET 1 C 5 TYR B 2 ASN B 5 0
SHEET 2 C 5 THR B 58 LEU B 63 -1 O ILE B 61 N TYR B 2
SHEET 3 C 5 TYR B 44 ASP B 53 -1 N ASP B 53 O THR B 58
SHEET 4 C 5 TYR B 35 VAL B 41 -1 N TYR B 35 O ALA B 50
SHEET 5 C 5 GLU B 28 VAL B 30 -1 N THR B 29 O ALA B 36
SHEET 1 D 2 GLU B 144 ARG B 145 0
SHEET 2 D 2 ILE B 153 CYS B 154 -1 O CYS B 154 N GLU B 144
SHEET 1 E 5 TYR C 2 ASN C 5 0
SHEET 2 E 5 THR C 58 LEU C 63 -1 O LEU C 59 N LEU C 4
SHEET 3 E 5 TYR C 44 ASP C 53 -1 N ILE C 51 O HIS C 60
SHEET 4 E 5 TYR C 34 VAL C 41 -1 N TYR C 35 O ALA C 50
SHEET 5 E 5 GLU C 28 ALA C 31 -1 N THR C 29 O ALA C 36
SHEET 1 F 2 GLU C 144 LEU C 146 0
SHEET 2 F 2 PHE C 149 CYS C 154 -1 O CYS C 154 N GLU C 144
SHEET 1 G 5 TYR D 2 ASN D 5 0
SHEET 2 G 5 THR D 58 LEU D 63 -1 O ILE D 61 N TYR D 2
SHEET 3 G 5 TYR D 44 ASP D 53 -1 N ILE D 51 O HIS D 60
SHEET 4 G 5 TYR D 34 VAL D 41 -1 N TYR D 35 O ALA D 50
SHEET 5 G 5 GLU D 28 ALA D 31 -1 N THR D 29 O ALA D 36
LINK O3' DA E 7 P 8OG E 8 1555 1555 1.61
LINK O3' 8OG E 8 P DT E 9 1555 1555 1.61
LINK O3' DA G 7 P 8OG G 8 1555 1555 1.58
LINK O3' 8OG G 8 P DT G 9 1555 1555 1.61
CISPEP 1 PRO A 8 PRO A 9 0 -0.49
CISPEP 2 LYS A 261 PRO A 262 0 -0.14
CISPEP 3 PRO B 8 PRO B 9 0 -0.46
CISPEP 4 LYS B 261 PRO B 262 0 0.09
CISPEP 5 PRO C 8 PRO C 9 0 -0.01
CISPEP 6 LYS C 261 PRO C 262 0 -0.25
CISPEP 7 PRO D 8 PRO D 9 0 0.04
CISPEP 8 LYS D 261 PRO D 262 0 0.09
CRYST1 75.522 101.594 103.279 90.00 94.23 90.00 P 1 21 1 8
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 0.013241 0.000000 0.000979 0.00000
SCALE2 0.000000 0.009843 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009709 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
