Header list of 1pru.pdb file
Complete list - 25 201 Bytes
HEADER DNA-BINDING PROTEIN 08-MAY-95 1PRU
TITLE PURINE REPRESSOR DNA-BINDING DOMAIN DNA BINDING
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PURINE REPRESSOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: DNA-BINDING;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PAR2156NCOI;
SOURCE 8 EXPRESSION_SYSTEM_GENE: PURR
KEYWDS PURINE REPRESSOR, DNA-BINDING PROTEIN
EXPDTA SOLUTION NMR
AUTHOR A.NAGADOI,S.MORIKAWA,H.NAKAMURA,M.ENARI,K.KOBAYASHI,H.YAMAMOTO,
AUTHOR 2 G.SAMPEI,K.MIZOBUCHI,M.A.SCHUMACHER,R.G.BRENNAN,Y.NISHIMURA
REVDAT 4 22-FEB-12 1PRU 1 JRNL VERSN
REVDAT 3 24-FEB-09 1PRU 1 VERSN
REVDAT 2 01-APR-03 1PRU 1 JRNL
REVDAT 1 08-MAR-96 1PRU 0
JRNL AUTH A.NAGADOI,S.MORIKAWA,H.NAKAMURA,M.ENARI,K.KOBAYASHI,
JRNL AUTH 2 H.YAMAMOTO,G.SAMPEI,K.MIZOBUCHI,M.A.SCHUMACHER,R.G.BRENNAN,
JRNL AUTH 3 Y.NISHIMURA
JRNL TITL STRUCTURAL COMPARISON OF THE FREE AND DNA-BOUND FORMS OF THE
JRNL TITL 2 PURINE REPRESSOR DNA-BINDING DOMAIN.
JRNL REF STRUCTURE V. 3 1217 1995
JRNL REFN ISSN 0969-2126
JRNL PMID 8591032
JRNL DOI 10.1016/S0969-2126(01)00257-X
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.A.SCHUMACHER,K.Y.CHOI,H.ZALKIN,R.G.BRENNAN
REMARK 1 TITL CRYSTAL STRUCTURE OF LACI MEMBER, PURR, BOUND TO DNA: MINOR
REMARK 1 TITL 2 GROOVE BINDING BY ALPHA HELICES
REMARK 1 REF SCIENCE V. 266 763 1994
REMARK 1 REFN ISSN 0036-8075
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : EMBOSS, PRESTO
REMARK 3 AUTHORS : NAKAI,KIDERA,NAKAMURA (EMBOSS), MORIKAMI,NAKAI,
REMARK 3 KIDERA,SAITO,NAKAMURA (PRESTO)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1PRU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 12 -82.49 -154.49
REMARK 500 VAL A 13 -75.66 -141.68
REMARK 500 THR A 25 -78.72 -109.79
REMARK 500 PHE A 27 107.11 -57.62
REMARK 500 TYR A 45 127.84 -37.92
REMARK 500 ALA A 49 87.59 -161.86
REMARK 500 ARG A 52 -137.91 -166.36
REMARK 500 SER A 53 88.80 -167.62
REMARK 500 LYS A 55 -149.88 61.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1PRV RELATED DB: PDB
DBREF 1PRU A 2 56 UNP P0ACP7 PURR_ECOLI 1 55
SEQRES 1 A 56 MET ALA THR ILE LYS ASP VAL ALA LYS ARG ALA ASN VAL
SEQRES 2 A 56 SER THR THR THR VAL SER HIS VAL ILE ASN LYS THR ARG
SEQRES 3 A 56 PHE VAL ALA GLU GLU THR ARG ASN ALA VAL TRP ALA ALA
SEQRES 4 A 56 ILE LYS GLU LEU HIS TYR SER PRO SER ALA VAL ALA ARG
SEQRES 5 A 56 SER LEU LYS VAL
HELIX 1 H1 ILE A 4 ALA A 11 1 8
HELIX 2 H2 THR A 15 ASN A 23 1 9
HELIX 3 H3 GLU A 30 GLU A 42 1 13
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 - 25 201 Bytes