Header list of 1pfs.pdb file
Complete list - 6 20 Bytes
HEADER DNA BINDING PROTEIN 03-AUG-96 1PFS
TITLE SOLUTION NMR STRUCTURE OF THE SINGLE-STRANDED DNA BINDING PROTEIN OF
TITLE 2 THE FILAMENTOUS PSEUDOMONAS PHAGE PF3, MINIMIZED AVERAGE STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PF3 SINGLE-STRANDED DNA BINDING PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PF3 SSDBP;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 OTHER_DETAILS: DIMERIC
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS PHAGE PF3;
SOURCE 3 ORGANISM_TAXID: 10872;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: MC4100;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PPF3VF36H
KEYWDS DNA-BINDING PROTEIN, VIRAL, BACTERIOPHAGE PF3, SINGLE-STRANDED DNA,
KEYWDS 2 DNA BINDING PROTEIN
EXPDTA SOLUTION NMR
AUTHOR R.H.A.FOLMER,M.NILGES,R.N.H.KONINGS,C.W.HILBERS
REVDAT 4 06-NOV-19 1PFS 1 KEYWDS REMARK
REVDAT 3 24-FEB-09 1PFS 1 VERSN
REVDAT 2 01-APR-03 1PFS 1 JRNL
REVDAT 1 12-FEB-97 1PFS 0
JRNL AUTH R.H.FOLMER,M.NILGES,R.N.KONINGS,C.W.HILBERS
JRNL TITL SOLUTION STRUCTURE OF THE SINGLE-STRANDED DNA BINDING
JRNL TITL 2 PROTEIN OF THE FILAMENTOUS PSEUDOMONAS PHAGE PF3: SIMILARITY
JRNL TITL 3 TO OTHER PROTEINS BINDING TO SINGLE-STRANDED NUCLEIC ACIDS.
JRNL REF EMBO J. V. 14 4132 1995
JRNL REFN ISSN 0261-4189
JRNL PMID 7556054
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH R.H.FOLMER,P.J.FOLKERS,A.KAAN,A.J.JONKER,J.M.AELEN,
REMARK 1 AUTH 2 R.N.KONINGS,C.W.HILBERS
REMARK 1 TITL SECONDARY STRUCTURE OF THE SINGLE-STRANDED DNA BINDING
REMARK 1 TITL 2 PROTEIN ENCODED BY FILAMENTOUS PHAGE PF3 AS DETERMINED BY
REMARK 1 TITL 3 NMR
REMARK 1 REF EUR.J.BIOCHEM. V. 224 663 1994
REMARK 1 REFN ISSN 0014-2956
REMARK 1 REFERENCE 2
REMARK 1 AUTH R.G.LUITEN,D.G.PUTTERMAN,J.G.SCHOENMAKERS,R.N.KONINGS,
REMARK 1 AUTH 2 L.A.DAY
REMARK 1 TITL NUCLEOTIDE SEQUENCE OF THE GENOME OF PF3, AN INC(P)-1
REMARK 1 TITL 2 PLASMID-SPECIFIC FILAMENTOUS BACTERIOPHAGE OF PSEUDOMONAS
REMARK 1 TITL 3 AERUGINOSA
REMARK 1 REF J.VIROL. V. 56 268 1985
REMARK 1 REFN ISSN 0022-538X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 30 STRUCTURES WERE CALCULATED USING THE
REMARK 3 GEOMETRIC FORCE FIELD 'PARALLDHG.PRO'. THESE WERE SUBSEQUENTLY
REMARK 3 REFINED IN A 7 ANGSTROM SHELL OF WATER MOLECULES USING THE OPLS
REMARK 3 FORCE FIELD (TOPOPLSXX.PRO) AND AVERAGED. THIS AVERAGED
REMARK 3 STRUCTURE WAS ENERGY MINIMIZED USING AGAIN 'PARALLDHG.PRO'. THE
REMARK 3 PROGRAM WAS MODIFIED TO USE FLOATING CHIRALITY. CHIRAL-CENTER
REMARK 3 RESTRAINT (A**3) : 0.352
REMARK 4
REMARK 4 1PFS 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_1000175648.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 4.4
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 13C- AND 15N-EDITED 3D NOESY;
REMARK 210 HMQC-J; HAHB; HACAHB-COSY; HNHB;
REMARK 210 15N SPIN-ECHO HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS; AMX
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 80
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : OVERALL ENERGY
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 O THR B 6 H PHE B 28 1.54
REMARK 500 O THR A 6 H PHE A 28 1.54
REMARK 500 O ASN A 60 H GLU A 67 1.58
REMARK 500 O ASN B 60 H GLU B 67 1.58
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 ASN A 63 24.40 49.08
REMARK 500 ASN B 63 24.42 49.05
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 ARG A 12 0.31 SIDE CHAIN
REMARK 500 ARG A 58 0.29 SIDE CHAIN
REMARK 500 ARG A 77 0.30 SIDE CHAIN
REMARK 500 ARG B 12 0.31 SIDE CHAIN
REMARK 500 ARG B 58 0.28 SIDE CHAIN
REMARK 500 ARG B 77 0.30 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1PFS A 1 78 UNP P03672 VHED_BPPF3 1 78
DBREF 1PFS B 1 78 UNP P03672 VHED_BPPF3 1 78
SEQRES 1 A 78 MET ASN ILE GLN ILE THR PHE THR ASP SER VAL ARG GLN
SEQRES 2 A 78 GLY THR SER ALA LYS GLY ASN PRO TYR THR PHE GLN GLU
SEQRES 3 A 78 GLY PHE LEU HIS LEU GLU ASP LYS PRO HIS PRO LEU GLN
SEQRES 4 A 78 CYS GLN PHE PHE VAL GLU SER VAL ILE PRO ALA GLY SER
SEQRES 5 A 78 TYR GLN VAL PRO TYR ARG ILE ASN VAL ASN ASN GLY ARG
SEQRES 6 A 78 PRO GLU LEU ALA PHE ASP PHE LYS ALA MET LYS ARG ALA
SEQRES 1 B 78 MET ASN ILE GLN ILE THR PHE THR ASP SER VAL ARG GLN
SEQRES 2 B 78 GLY THR SER ALA LYS GLY ASN PRO TYR THR PHE GLN GLU
SEQRES 3 B 78 GLY PHE LEU HIS LEU GLU ASP LYS PRO HIS PRO LEU GLN
SEQRES 4 B 78 CYS GLN PHE PHE VAL GLU SER VAL ILE PRO ALA GLY SER
SEQRES 5 B 78 TYR GLN VAL PRO TYR ARG ILE ASN VAL ASN ASN GLY ARG
SEQRES 6 B 78 PRO GLU LEU ALA PHE ASP PHE LYS ALA MET LYS ARG ALA
SHEET 1 A 5 LEU A 38 PHE A 43 0
SHEET 2 A 5 PHE A 24 LEU A 29 -1 N LEU A 29 O LEU A 38
SHEET 3 A 5 ASN A 2 PHE A 7 -1 N THR A 6 O PHE A 28
SHEET 4 A 5 GLY A 51 ASN A 62 -1 N VAL A 55 O ILE A 3
SHEET 5 A 5 LYS A 76 ARG A 77 -1 N LYS A 76 O GLN A 54
SHEET 1 B 2 VAL A 11 THR A 15 0
SHEET 2 B 2 PRO A 21 GLN A 25 -1 N PHE A 24 O ARG A 12
SHEET 1 C 2 TYR A 57 ASN A 62 0
SHEET 2 C 2 ARG A 65 ASP A 71 -1 O ARG A 65 N ASN A 62
SHEET 1 D 5 LEU B 38 PHE B 43 0
SHEET 2 D 5 PHE B 24 LEU B 29 -1 N LEU B 29 O LEU B 38
SHEET 3 D 5 ASN B 2 PHE B 7 -1 N THR B 6 O PHE B 28
SHEET 4 D 5 GLY B 51 ASN B 62 -1 N VAL B 55 O ILE B 3
SHEET 5 D 5 LYS B 76 ARG B 77 -1 N LYS B 76 O GLN B 54
SHEET 1 E 2 VAL B 11 THR B 15 0
SHEET 2 E 2 PRO B 21 GLN B 25 -1 N PHE B 24 O ARG B 12
SHEET 1 F 2 TYR B 57 ASN B 62 0
SHEET 2 F 2 ARG B 65 ASP B 71 -1 O ARG B 65 N ASN B 62
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 - 6 20 Bytes