Header list of 2gvb.pdb file
Complete list - 9 20 Bytes
HEADER DNA-BINDING (VIRAL) 27-JUL-95 2GVB
TITLE REFINED SOLUTION STRUCTURE OF THE TYR 41--> HIS MUTANT OF THE M13 GENE
TITLE 2 V PROTEIN. A COMPARISON WITH THE CRYSTAL STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GENE V PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ENTEROBACTERIA PHAGE M13;
SOURCE 3 ORGANISM_TAXID: 10870;
SOURCE 4 EXPRESSION_SYSTEM_PLASMID: M13
KEYWDS DNA-BINDING (VIRAL)
EXPDTA SOLUTION NMR
AUTHOR P.J.M.FOLKERS,M.NILGES,R.H.A.FOLMER,J.J.PROMPERS,R.N.H.KONINGS,
AUTHOR 2 C.W.HILBERS
REVDAT 4 09-MAR-22 2GVB 1 REMARK SEQADV
REVDAT 3 24-FEB-09 2GVB 1 VERSN
REVDAT 2 01-APR-03 2GVB 1 JRNL
REVDAT 1 15-OCT-95 2GVB 0
SPRSDE 15-OCT-95 2GVB 1GVB
JRNL AUTH J.J.PROMPERS,R.H.FOLMER,M.NILGES,P.J.FOLKERS,R.N.KONINGS,
JRNL AUTH 2 C.W.HILBERS
JRNL TITL REFINED SOLUTION STRUCTURE OF THE TYR41-->HIS MUTANT OF THE
JRNL TITL 2 M13 GENE V PROTEIN. A COMPARISON WITH THE CRYSTAL STRUCTURE.
JRNL REF EUR.J.BIOCHEM. V. 232 506 1995
JRNL REFN ISSN 0014-2956
JRNL PMID 7556200
JRNL DOI 10.1111/J.1432-1033.1995.506ZZ.X
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH P.J.M.FOLKERS,M.NILGES,R.H.A.FOLMER,R.N.H.KONINGS,
REMARK 1 AUTH 2 C.W.HILBERS
REMARK 1 TITL THE SOLUTION STRUCTURE OF THE TYR 41--> HIS MUTANT OF THE
REMARK 1 TITL 2 SINGLE-STRANDED DNA BINDING PROTEIN ENCODED BY GENE V OF THE
REMARK 1 TITL 3 FILAMENTOUS BACTERIOPHAGE M13
REMARK 1 REF J.MOL.BIOL. V. 236 229 1994
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 2
REMARK 1 AUTH P.J.M.FOLKERS,J.P.M.VAN DUYNHOVEN,H.T.M.VAN LIESHOUT,
REMARK 1 AUTH 2 B.J.M.HARMSEN,J.H.VAN BOOM,G.I.TESSER,R.N.H.KONINGS,
REMARK 1 AUTH 3 C.W.HILBERS
REMARK 1 TITL EXPLORING THE DNA BINDING DOMAIN OF GENE V PROTEIN ENCODED
REMARK 1 TITL 2 BY BACTERIOPHAGE M13 WITH THE AID OF SPIN-LABELED
REMARK 1 TITL 3 OLIGONUCLEOTIDES IN COMBINATION WITH H-NMR
REMARK 1 REF BIOCHEMISTRY V. 32 9407 1993
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 3
REMARK 1 AUTH P.J.M.FOLKERS,J.P.M.VAN DUYNHOVEN,A.J.JONKER,B.J.M.HARMSEN,
REMARK 1 AUTH 2 R.N.H.KONINGS,C.W.HILBERS
REMARK 1 TITL SEQUENCE-SPECIFIC H-NMR ASSIGNMENT AND SECONDARY STRUCTURE
REMARK 1 TITL 2 OF THE TYR 41--> HIS MUTANT OF THE SINGLE-STRANDED DNA
REMARK 1 TITL 3 BINDING PROTEIN, GENE V PROTEIN, ENCODED BY THE FILAMENTOUS
REMARK 1 TITL 4 BACTERIOPHAGE M13
REMARK 1 REF EUR.J.BIOCHEM. V. 202 349 1991
REMARK 1 REFN ISSN 0014-2956
REMARK 1 REFERENCE 4
REMARK 1 AUTH P.J.M.FOLKERS,A.P.M.STASSEN,J.P.M.VAN DUYNHOVEN,
REMARK 1 AUTH 2 B.J.M.HARMSEN,R.N.H.KONINGS,C.W.HILBERS
REMARK 1 TITL CHARACTERIZATION OF WILD-TYPE AND MUTANT M13 GENE V PROTEINS
REMARK 1 TITL 2 BY MEANS OF H-NMR
REMARK 1 REF EUR.J.BIOCHEM. V. 200 139 1991
REMARK 1 REFN ISSN 0014-2956
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : GUNTERT,BRAUN,WUTHRICH (DIANA), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2GVB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000178160.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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
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 H THR B 62 O VAL B 84 1.45
REMARK 500 H THR A 62 O VAL A 84 1.45
REMARK 500 O ASP A 36 H ASN A 39 1.54
REMARK 500 O ASP B 36 H ASN B 39 1.54
REMARK 500 H GLY A 18 O TYR A 26 1.57
REMARK 500 H GLY B 18 O TYR B 26 1.57
REMARK 500 OE1 GLN A 31 H LEU A 32 1.59
REMARK 500 OE1 GLN B 31 H LEU B 32 1.59
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 VAL A 4 149.70 172.24
REMARK 500 LYS A 7 170.01 -44.15
REMARK 500 SER A 17 106.98 -54.38
REMARK 500 SER A 20 -78.81 -46.91
REMARK 500 ARG A 21 53.25 -148.62
REMARK 500 LEU A 37 21.40 48.98
REMARK 500 GLU A 40 -52.31 70.68
REMARK 500 TYR A 56 99.34 -47.65
REMARK 500 ALA A 57 171.79 -47.37
REMARK 500 MET A 77 117.49 -160.29
REMARK 500 ARG A 80 68.95 174.47
REMARK 500 LEU A 81 121.35 -31.48
REMARK 500 VAL B 4 149.74 172.27
REMARK 500 LYS B 7 170.03 -44.14
REMARK 500 SER B 17 107.02 -54.43
REMARK 500 SER B 20 -78.85 -46.91
REMARK 500 ARG B 21 53.17 -148.56
REMARK 500 LEU B 37 21.35 49.09
REMARK 500 GLU B 40 -52.36 70.61
REMARK 500 TYR B 56 98.08 -47.58
REMARK 500 ALA B 57 171.75 -46.20
REMARK 500 MET B 77 117.60 -160.27
REMARK 500 ARG B 80 69.07 174.39
REMARK 500 LEU B 81 121.31 -31.55
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2GVA RELATED DB: PDB
DBREF 2GVB A 1 87 UNP P69544 VHED_BPM13 1 87
DBREF 2GVB B 1 87 UNP P69544 VHED_BPM13 1 87
SEQADV 2GVB HIS A 41 UNP P69544 TYR 41 CONFLICT
SEQADV 2GVB HIS B 41 UNP P69544 TYR 41 CONFLICT
SEQRES 1 A 87 MET ILE LYS VAL GLU ILE LYS PRO SER GLN ALA GLN PHE
SEQRES 2 A 87 THR THR ARG SER GLY VAL SER ARG GLN GLY LYS PRO TYR
SEQRES 3 A 87 SER LEU ASN GLU GLN LEU CYS TYR VAL ASP LEU GLY ASN
SEQRES 4 A 87 GLU HIS PRO VAL LEU VAL LYS ILE THR LEU ASP GLU GLY
SEQRES 5 A 87 GLN PRO ALA TYR ALA PRO GLY LEU TYR THR VAL HIS LEU
SEQRES 6 A 87 SER SER PHE LYS VAL GLY GLN PHE GLY SER LEU MET ILE
SEQRES 7 A 87 ASP ARG LEU ARG LEU VAL PRO ALA LYS
SEQRES 1 B 87 MET ILE LYS VAL GLU ILE LYS PRO SER GLN ALA GLN PHE
SEQRES 2 B 87 THR THR ARG SER GLY VAL SER ARG GLN GLY LYS PRO TYR
SEQRES 3 B 87 SER LEU ASN GLU GLN LEU CYS TYR VAL ASP LEU GLY ASN
SEQRES 4 B 87 GLU HIS PRO VAL LEU VAL LYS ILE THR LEU ASP GLU GLY
SEQRES 5 B 87 GLN PRO ALA TYR ALA PRO GLY LEU TYR THR VAL HIS LEU
SEQRES 6 B 87 SER SER PHE LYS VAL GLY GLN PHE GLY SER LEU MET ILE
SEQRES 7 B 87 ASP ARG LEU ARG LEU VAL PRO ALA LYS
HELIX 1 H1A LYS A 7 SER A 9 5 3
HELIX 2 H2A HIS A 64 SER A 67 5 4
HELIX 3 H1B LYS B 7 SER B 9 5 3
HELIX 4 H2B HIS B 64 SER B 67 5 4
SHEET 1 S1A 5 PRO A 42 THR A 48 0
SHEET 2 S1A 5 LYS A 24 ASP A 36 -1 O VAL A 35 N VAL A 43
SHEET 3 S1A 5 LYS A 3 ILE A 6 -1 O GLU A 5 N TYR A 34
SHEET 4 S1A 5 GLY A 59 HIS A 64 -1 O TYR A 61 N VAL A 4
SHEET 5 S1A 5 ARG A 82 ALA A 86 -1 O ARG A 82 N HIS A 64
SHEET 1 S1B 5 PHE A 13 SER A 20 0
SHEET 2 S1B 5 LYS A 24 ASP A 36 -1 O TYR A 26 N GLY A 18
SHEET 3 S1B 5 LYS A 3 ILE A 6 -1 O GLU A 5 N TYR A 34
SHEET 4 S1B 5 GLY A 59 HIS A 64 -1 O TYR A 61 N VAL A 4
SHEET 5 S1B 5 ARG A 82 ALA A 86 -1 O ARG A 82 N HIS A 64
SHEET 1 S2A 2 PHE A 68 GLY A 71 0
SHEET 2 S2A 2 SER A 75 ILE A 78 -1 O MET A 77 N LYS A 69
SHEET 1 S1C 5 PRO B 42 THR B 48 0
SHEET 2 S1C 5 LYS B 24 ASP B 36 -1 O VAL B 35 N VAL B 43
SHEET 3 S1C 5 LYS B 3 ILE B 6 -1 O GLU B 5 N TYR B 34
SHEET 4 S1C 5 GLY B 59 HIS B 64 -1 O TYR B 61 N VAL B 4
SHEET 5 S1C 5 ARG B 82 ALA B 86 -1 O ARG B 82 N HIS B 64
SHEET 1 S1D 5 PHE B 13 SER B 20 0
SHEET 2 S1D 5 LYS B 24 ASP B 36 -1 O TYR B 26 N GLY B 18
SHEET 3 S1D 5 LYS B 3 ILE B 6 -1 O GLU B 5 N TYR B 34
SHEET 4 S1D 5 GLY B 59 HIS B 64 -1 O TYR B 61 N VAL B 4
SHEET 5 S1D 5 ARG B 82 ALA B 86 -1 O ARG B 82 N HIS B 64
SHEET 1 S2B 2 PHE B 68 GLY B 71 0
SHEET 2 S2B 2 SER B 75 ILE B 78 -1 O MET B 77 N LYS B 69
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
Complete list - 9 20 Bytes