Header list of 1zrp.pdb file
Complete list - v 29 2 Bytes
HEADER ELECTRON TRANSPORT 10-JUL-92 1ZRP
TITLE SOLUTION-STATE STRUCTURE BY NMR OF ZINC-SUBSTITUTED RUBREDOXIN FROM
TITLE 2 THE MARINE HYPERTHERMOPHILIC ARCHAEBACTERIUM PYROCOCCUS FURIOSUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RUBREDOXIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PYROCOCCUS FURIOSUS;
SOURCE 3 ORGANISM_TAXID: 2261
KEYWDS ELECTRON TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 40
AUTHOR P.R.BLAKE,J.B.PARK,Z.H.ZHOU,D.R.HARE,M.W.W.ADAMS,M.F.SUMMERS
REVDAT 4 29-NOV-17 1ZRP 1 REMARK HELIX
REVDAT 3 24-FEB-09 1ZRP 1 VERSN
REVDAT 2 01-APR-03 1ZRP 1 JRNL
REVDAT 1 31-OCT-93 1ZRP 0
JRNL AUTH P.R.BLAKE,J.B.PARK,Z.H.ZHOU,D.R.HARE,M.W.ADAMS,M.F.SUMMERS
JRNL TITL SOLUTION-STATE STRUCTURE BY NMR OF ZINC-SUBSTITUTED
JRNL TITL 2 RUBREDOXIN FROM THE MARINE HYPERTHERMOPHILIC ARCHAEBACTERIUM
JRNL TITL 3 PYROCOCCUS FURIOSUS.
JRNL REF PROTEIN SCI. V. 1 1508 1992
JRNL REFN ISSN 0961-8368
JRNL PMID 1303769
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH P.R.BLAKE,M.W.DAY,B.T.HSU,L.JOSHUA-TOR,J.-B.PARK,D.R.HARE,
REMARK 1 AUTH 2 M.W.W.ADAMS,D.C.REES,M.F.SUMMERS
REMARK 1 TITL COMPARISON OF THE X-RAY STRUCTURE OF NATIVE RUBREDOXIN FROM
REMARK 1 TITL 2 PYROCOCCUS FURIOSUS WITH THE NMR STRUCTURE OF THE
REMARK 1 TITL 3 ZINC-SUBSTITUTED PROTEIN
REMARK 1 REF PROTEIN SCI. V. 1 1522 1992
REMARK 1 REFN ISSN 0961-8368
REMARK 1 REFERENCE 2
REMARK 1 AUTH P.R.BLAKE,B.LEE,M.F.SUMMERS,M.W.ADAMS,J.B.PARK,Z.H.ZHOU,
REMARK 1 AUTH 2 A.BAX
REMARK 1 TITL QUANTITATIVE MEASUREMENT OF SMALL THROUGH-HYDROGEN-BOND AND
REMARK 1 TITL 2 'THROUGH-SPACE' 1H-113CD AND 1H-199HG J COUPLINGS IN
REMARK 1 TITL 3 METAL-SUBSTITUTED RUBREDOXIN FROM PYROCOCCUS FURIOSUS
REMARK 1 REF J.BIOMOL.NMR V. 2 527 1992
REMARK 1 REFN ISSN 0925-2738
REMARK 1 REFERENCE 3
REMARK 1 AUTH P.R.BLAKE,J.B.PARK,M.W.W.ADAMS,M.F.SUMMERS
REMARK 1 TITL NOVEL OBSERVATION OF NH...S(CYS) HYDROGEN-BOND-MEDIATED
REMARK 1 TITL 2 SCALAR COUPLING IN 113CD-SUBSTITUTED RUBREDOXIN FROM
REMARK 1 TITL 3 PYROCOCCUS FURIOSUS
REMARK 1 REF J.AM.CHEM.SOC. V. 114 4931 1992
REMARK 1 REFN ISSN 0002-7863
REMARK 1 REFERENCE 4
REMARK 1 AUTH P.R.BLAKE,J.-B.PARK,F.O.BRYANT,S.AONO,J.K.MAGNUSON,
REMARK 1 AUTH 2 E.ECCLESTON,J.B.HOWARD,M.F.SUMMERS,M.W.W.ADAMS
REMARK 1 TITL DETERMINANTS OF PROTEIN HYPERTHERMOSTABILITY: PURIFICATION
REMARK 1 TITL 2 AND AMINO ACID SEQUENCE OF RUBREDOXIN FROM THE
REMARK 1 TITL 3 HYPERTHERMOPHILIC ARCHAEBACTERIUM PYROCOCCUS FURIOSUS AND
REMARK 1 TITL 4 SECONDARY STRUCTURE OF THE ZINC ADDUCT BY NMR
REMARK 1 REF BIOCHEMISTRY V. 30 10885 1991
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DSPACE
REMARK 3 AUTHORS : HARE RESEARCH INC.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1ZRP COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000177531.
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 : 40
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 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 54 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 38 SG
REMARK 620 2 CYS A 41 SG 106.6
REMARK 620 3 CYS A 5 SG 106.4 106.9
REMARK 620 4 CYS A 8 SG 106.8 122.4 106.7
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 54
DBREF 1ZRP A 1 53 UNP P24297 RUBR_PYRFU 1 53
SEQRES 1 A 53 ALA LYS TRP VAL CYS LYS ILE CYS GLY TYR ILE TYR ASP
SEQRES 2 A 53 GLU ASP ALA GLY ASP PRO ASP ASN GLY ILE SER PRO GLY
SEQRES 3 A 53 THR LYS PHE GLU GLU LEU PRO ASP ASP TRP VAL CYS PRO
SEQRES 4 A 53 ILE CYS GLY ALA PRO LYS SER GLU PHE GLU LYS LEU GLU
SEQRES 5 A 53 ASP
HET ZN A 54 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
HELIX 1 HC1 ASP A 13 GLY A 17 5 5
HELIX 2 HC2 ASP A 18 GLY A 22 5 5
HELIX 3 HC3 LYS A 28 LEU A 32 5 5
HELIX 4 HC4 PRO A 44 PHE A 48 5 5
SHEET 1 BSA 3 TYR A 10 GLU A 14 0
SHEET 2 BSA 3 ALA A 1 CYS A 5 -1
SHEET 3 BSA 3 PHE A 48 LEU A 51 -1
SHEET 1 BSB 2 GLY A 17 PRO A 19 0
SHEET 2 BSB 2 ILE A 23 SER A 24 -1
SHEET 1 BSC 2 TRP A 36 CYS A 38 0
SHEET 2 BSC 2 PRO A 44 LYS A 45 -1
LINK ZN ZN A 54 SG CYS A 38 1555 1555 2.31
LINK ZN ZN A 54 SG CYS A 41 1555 1555 2.30
LINK ZN ZN A 54 SG CYS A 5 1555 1555 2.31
LINK ZN ZN A 54 SG CYS A 8 1555 1555 2.30
SITE 1 AC1 4 CYS A 5 CYS A 8 CYS A 38 CYS A 41
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
MODEL 1
Complete list - v 29 2 Bytes