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PDBsum entry 3cvs

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Top Page protein dna_rna Protein-protein interface(s) links
Hydrolase/DNA PDB id
3cvs
Jmol
Contents
Protein chains
282 a.a.
DNA/RNA
Waters ×167
HEADER    HYDROLASE/DNA                           19-APR-08   3CVS
TITLE     CRYSTAL STRUCTURE OF AN ALKA HOST/GUEST COMPLEX
TITLE    2 8OXOGUANINE:ADENINE 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-
COMPND   5 METHYLADENINE-DNA GLYCOSYLASE II, INDUCIBLE, TAG II, DNA-3-
COMPND   6 METHYLADENINE GLYCOSIDASE 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'-
COMPND  17 D(*DGP*DGP*DCP*DAP*DAP*DTP*DCP*DAP*DTP*DGP*DTP*DC)-3');
COMPND  18 CHAIN: F, H;
COMPND  19 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE   3 GENE: ALKA, AIDA;
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   5 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE   6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PET30;
SOURCE   8 MOL_ID: 2;
SOURCE   9 SYNTHETIC: YES;
SOURCE  10 MOL_ID: 3;
SOURCE  11 SYNTHETIC: YES
KEYWDS    ALKA, 8OXOGUANINE, DNA REPAIR, HOST/GUEST COMPLEX, DNA
KEYWDS   2 STRUCTURE, DNA DAMAGE, HYDROLASE, HYDROLASE/DNA COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    B.R.BOWMAN,S.LEE,S.WANG,G.L.VERDINE
REVDAT   4   24-FEB-09 3CVS    1       VERSN
REVDAT   3   18-NOV-08 3CVS    1       COMPND
REVDAT   2   09-SEP-08 3CVS    1       SOURCE
REVDAT   1   02-SEP-08 3CVS    0
JRNL        AUTH   B.R.BOWMAN,S.LEE,S.WANG,G.L.VERDINE
JRNL        TITL   STRUCTURE OF THE E. COLI DNA GLYCOSYLASE ALKA
JRNL        TITL 2 BOUND TO THE ENDS OF DUPLEX DNA: A SYSTEM FOR THE
JRNL        TITL 3 STRUCTURE DETERMINATION 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   1
REMARK   2
REMARK   2 RESOLUTION.    2.40 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) : 2.40
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)   (%) : 93.3
REMARK   3   NUMBER OF REFLECTIONS             : 56188
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) : 0.219
REMARK   3   FREE R VALUE                     : 0.270
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.700
REMARK   3   FREE R VALUE TEST SET COUNT      : 2847
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       : 978
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 167
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 48.20
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -3.68800
REMARK   3    B22 (A**2) : -1.87100
REMARK   3    B33 (A**2) : 5.55900
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : -11.28700
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        : 29.47
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 3CVS COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-APR-08.
REMARK 100 THE RCSB ID CODE IS RCSB047271.
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 : HKL
REMARK 200  DATA SCALING SOFTWARE          : HKL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 60184
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400
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     (%) : 99.2
REMARK 200  DATA REDUNDANCY                : 3.500
REMARK 200  R MERGE                    (I) : 0.07200
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 8.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.49
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.6
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.70
REMARK 200  R MERGE FOR SHELL          (I) : 0.41600
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   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   (%): 55.78
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78
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       50.62350
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 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: 53230 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -50.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D, B, C, G, H, E, F
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: 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      -20.69     81.68
REMARK 500    LEU A 125      -59.27     70.81
REMARK 500    VAL A 126     -178.22    -61.89
REMARK 500    PRO A 246      121.16    -37.65
REMARK 500    TYR A 273       32.53    -98.50
REMARK 500    PRO A 279      156.07    -49.54
REMARK 500    SER B  26      -16.22     73.81
REMARK 500    ALA B  65      -32.80    -32.53
REMARK 500    PHE B 149       71.64   -150.60
REMARK 500    PRO B 150      -37.29    -36.83
REMARK 500    PRO B 175     -179.68    -59.50
REMARK 500    PRO B 246      117.69    -18.46
REMARK 500    MET B 248      145.90    -26.54
REMARK 500    PRO B 250      -32.99    -34.46
REMARK 500    TYR B 273       33.36    -99.24
REMARK 500    GLU B 275      -76.82    -57.39
REMARK 500    SER C  26      -15.55     81.56
REMARK 500    HIS C  57       64.08     35.86
REMARK 500    ALA C 100      -35.76   -137.26
REMARK 500    ARG C 102       78.38   -175.00
REMARK 500    LEU C 125      -62.23     67.41
REMARK 500    LEU C 235       70.89   -115.25
REMARK 500    PRO C 262       37.01    -99.17
REMARK 500    TYR C 273       57.41   -101.56
REMARK 500    THR C 274       87.75   -161.50
REMARK 500    TRP C 277      144.07    -12.43
REMARK 500    GLU C 281       96.38    -53.01
REMARK 500    SER D  26      -17.30     84.22
REMARK 500    HIS D  57       53.17     38.06
REMARK 500    LEU D 125      -29.03     64.83
REMARK 500    LEU D 235       76.97   -117.13
REMARK 500    PHE D 245       68.50   -117.53
REMARK 500    TYR D 273       36.35    -99.13
REMARK 500    GLU D 281       37.44    -80.94
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH C 320        DISTANCE =  5.40 ANGSTROMS
REMARK 525    HOH C 321        DISTANCE =  5.27 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3CVT   RELATED DB: PDB
REMARK 900 RELATED ID: 3CW7   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  3CVS E    1    12  PDB    3CVS     3CVS             1     12
DBREF  3CVS F   14    25  PDB    3CVS     3CVS             1     12
DBREF  3CVS G    1    12  PDB    3CVS     3CVS             1     12
DBREF  3CVS H   14    25  PDB    3CVS     3CVS             1     12
DBREF  3CVS A    1   282  UNP    P04395   3MG2_ECOLI       1    282
DBREF  3CVS B    1   282  UNP    P04395   3MG2_ECOLI       1    282
DBREF  3CVS C    1   282  UNP    P04395   3MG2_ECOLI       1    282
DBREF  3CVS 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  DA  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  DA  DT  DC  DA  DT  DG  DT  DC
MODRES 3CVS 8OG E    8   DG
MODRES 3CVS 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   *167(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  ASP A   83  1                                  14
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  164  1                                   8
HELIX    9   9 ASP A  165  LEU A  172  1                                   8
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  GLY B  192  1                                  18
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  ALA C   23  1                                  13
HELIX   34  34 ALA C   65  PRO C   69  5                                   5
HELIX   35  35 VAL C   70  ASP C   83  1                                  14
HELIX   36  36 ASN C   87  GLY C   96  1                                  10
HELIX   37  37 ARG C   97  ALA C  100  5                                   4
HELIX   38  38 ASP C  112  GLY C  123  1                                  12
HELIX   39  39 SER C  127  GLY C  143  1                                  17
HELIX   40  40 THR C  157  ALA C  164  1                                   8
HELIX   41  41 ASP C  165  ALA C  171  1                                   7
HELIX   42  42 PRO C  175  GLY C  192  1                                  18
HELIX   43  43 ASP C  201  GLN C  210  1                                  10
HELIX   44  44 GLY C  216  TRP C  228  1                                  13
HELIX   45  45 ASP C  238  PHE C  245  1                                   8
HELIX   46  46 THR C  249  GLU C  258  1                                  10
HELIX   47  47 ARG C  259  LYS C  261  5                                   3
HELIX   48  48 TRP C  263  TYR C  273  1                                  11
HELIX   49  49 ASP D   11  ALA D   23  1                                  13
HELIX   50  50 ALA D   65  PRO D   69  5                                   5
HELIX   51  51 VAL D   70  PHE D   82  1                                  13
HELIX   52  52 ASN D   87  GLY D   96  1                                  10
HELIX   53  53 GLY D   96  ALA D  101  1                                   6
HELIX   54  54 ASP D  112  LEU D  122  1                                  11
HELIX   55  55 SER D  127  GLY D  143  1                                  17
HELIX   56  56 THR D  157  ALA D  163  1                                   7
HELIX   57  57 ASP D  165  ALA D  171  1                                   7
HELIX   58  58 PRO D  175  GLU D  191  1                                  17
HELIX   59  59 ASP D  201  GLN D  210  1                                  10
HELIX   60  60 GLY D  216  TRP D  228  1                                  13
HELIX   61  61 ASP D  238  PHE D  245  1                                   8
HELIX   62  62 THR D  249  GLU D  258  1                                  10
HELIX   63  63 ARG D  259  LYS D  261  5                                   3
HELIX   64  64 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 5 TYR B   2  ASN B   5  0
SHEET    2   B 5 THR B  58  LEU B  63 -1  O  LEU B  59   N  LEU B   4
SHEET    3   B 5 TYR B  44  ASP B  53 -1  N  ASP B  53   O  THR B  58
SHEET    4   B 5 TYR B  35  VAL B  41 -1  N  TYR B  35   O  ALA B  50
SHEET    5   B 5 GLU B  28  VAL B  30 -1  N  THR B  29   O  ALA B  36
SHEET    1   C 2 GLU B 144  LEU B 146  0
SHEET    2   C 2 PHE B 149  CYS B 154 -1  O  CYS B 154   N  GLU B 144
SHEET    1   D 5 TYR C   2  ASN C   5  0
SHEET    2   D 5 THR C  58  LEU C  63 -1  O  LEU C  59   N  LEU C   4
SHEET    3   D 5 TYR C  44  ASP C  53 -1  N  ILE C  51   O  HIS C  60
SHEET    4   D 5 TYR C  35  VAL C  41 -1  N  TYR C  35   O  ALA C  50
SHEET    5   D 5 GLU C  28  VAL C  30 -1  N  THR C  29   O  ALA C  36
SHEET    1   E 2 GLU C 144  LEU C 146  0
SHEET    2   E 2 PHE C 149  CYS C 154 -1  O  CYS C 154   N  GLU C 144
SHEET    1   F 5 TYR D   2  ASN D   5  0
SHEET    2   F 5 THR D  58  LEU D  63 -1  O  LEU D  59   N  LEU D   4
SHEET    3   F 5 TYR D  44  ASP D  53 -1  N  ILE D  51   O  HIS D  60
SHEET    4   F 5 TYR D  35  VAL D  41 -1  N  TYR D  35   O  ALA D  50
SHEET    5   F 5 GLU D  28  VAL D  30 -1  N  THR D  29   O  ALA D  36
LINK         O3'  DA E   7                 P   8OG E   8     1555   1555  1.60
LINK         O3' 8OG E   8                 P    DT E   9     1555   1555  1.62
LINK         O3'  DA G   7                 P   8OG G   8     1555   1555  1.60
LINK         O3' 8OG G   8                 P    DT G   9     1555   1555  1.61
CISPEP   1 PRO A    8    PRO A    9          0        -0.76
CISPEP   2 LYS A  261    PRO A  262          0        -0.21
CISPEP   3 PRO B    8    PRO B    9          0        -0.45
CISPEP   4 LYS B  261    PRO B  262          0         0.39
CISPEP   5 PRO C    8    PRO C    9          0        -0.09
CISPEP   6 LYS C  261    PRO C  262          0        -0.81
CISPEP   7 PRO D    8    PRO D    9          0         0.18
CISPEP   8 LYS D  261    PRO D  262          0         0.18
CRYST1   75.174  101.247  102.917  90.00  94.19  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      0.013302  0.000000  0.000975        0.00000
SCALE2      0.000000  0.009877  0.000000        0.00000
SCALE3      0.000000  0.000000  0.009743        0.00000
      
PROCHECK
Go to PROCHECK summary
 References