Header list of 1ncp.pdb file
Complete list - 4 201 Bytes
HEADER VIRAL PROTEIN 27-NOV-91 1NCP
TITLE STRUCTURAL CHARACTERIZATION OF A 39 RESIDUE SYNTHETIC PEPTIDE
TITLE 2 CONTAINING THE TWO ZINC BINDING DOMAINS FROM THE HIV-1 P7
TITLE 3 NUCLEOCAPSID PROTEIN BY CD AND NMR SPECTROSCOPY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HIV-1 P7 NUCLEOCAPSID PROTEIN;
COMPND 3 CHAIN: N;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: HIV-1 P7 NUCLEOCAPSID PROTEIN;
COMPND 7 CHAIN: C;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;
SOURCE 3 ORGANISM_TAXID: 11676;
SOURCE 4 MOL_ID: 2;
SOURCE 5 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;
SOURCE 6 ORGANISM_TAXID: 11676
KEYWDS NUCLEOCAPSID PROTEIN, VIRAL PROTEIN
EXPDTA SOLUTION NMR
AUTHOR G.M.CLORE,J.G.OMICHINSKI,A.M.GRONENBORN
REVDAT 4 04-JUL-18 1NCP 1 REMARK SSBOND
REVDAT 3 24-FEB-09 1NCP 1 VERSN
REVDAT 2 01-APR-03 1NCP 1 JRNL
REVDAT 1 31-OCT-93 1NCP 0
JRNL AUTH J.G.OMICHINSKI,G.M.CLORE,K.SAKAGUCHI,E.APPELLA,
JRNL AUTH 2 A.M.GRONENBORN
JRNL TITL STRUCTURAL CHARACTERIZATION OF A 39-RESIDUE SYNTHETIC
JRNL TITL 2 PEPTIDE CONTAINING THE TWO ZINC BINDING DOMAINS FROM THE
JRNL TITL 3 HIV-1 P7 NUCLEOCAPSID PROTEIN BY CD AND NMR SPECTROSCOPY.
JRNL REF FEBS LETT. V. 292 25 1991
JRNL REFN ISSN 0014-5793
JRNL PMID 1959614
JRNL DOI 10.1016/0014-5793(91)80825-N
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NULL
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THIS ENTRY CONTAINS SOLUTION NMR STRUCTURE OF A 39 RESIDUE
REMARK 3 SYNTHETIC PEPTIDE CONTAINING THE TWO ZINC BINDING DOMAINS
REMARK 3 FROM THE HIV-1 P7 NUCLEOCAPSID PROTEIN. THE TWO DOMAINS
REMARK 3 ARE COMPLETELY INDEPENDENT AND WERE SOLVED SEPARATELY. THE
REMARK 3 FIRST DOMAIN (CHAIN *N*, RESIDUES 1 - 17) WAS BASED ON 147
REMARK 3 APPROXIMATE INTERPROTON DISTANCE RESTRAINTS. THE SECOND
REMARK 3 DOMAIN (CHAIN *C*, RESIDUES 22 - 39) WAS BASED ON 148
REMARK 3 APPROXIMATE INTERPROTON DISTANCE RESTRAINTS. THE LINKER
REMARK 3 REGION IS HIGHLY FLEXIBLE AND CANNOT BE DEFINED FROM THE
REMARK 3 NMR DATA.
REMARK 3
REMARK 3 THE METHOD USED TO DETERMINE THE STRUCTURES IS THE HYBRID
REMARK 3 METRIC MATRIX DISTANCE GEOMETRY-DYNAMICAL SIMULATED
REMARK 3 ANNEALING METHOD (NILGES, CLORE, AND GRONENBORN, FEBS
REMARK 3 LETT. 229, 317 (1988)).
REMARK 3
REMARK 3 A TOTAL OF 15 SIMULATED ANNEALING STRUCTURES WAS CALCULATED
REMARK 3 FOR EACH DOMAIN. THE COORDINATES OF THE DOMAINS WERE THEN
REMARK 3 AVERAGED AND SUBJECTED TO RESTRAINED REGULARIZATION TO
REMARK 3 YIELD THE RESTRAINED MINIMIZED STRUCTURES. ONLY THESE
REMARK 3 COORDINATES ARE LISTED. THE FIRST CHAIN IS THE N-TERMINAL
REMARK 3 DOMAIN, AND THE SECOND IS THE C-TERMINAL DOMAIN.
REMARK 3
REMARK 3 THE FIELD PRESENTED IN COLUMNS 61 - 66 IN THIS COORDINATE
REMARK 3 FILE REPRESENTS THE ATOMIC RMS DEVIATION OF THE INDIVIDUAL
REMARK 3 STRUCTURES ABOUT THE MEAN COORDINATE POSITIONS FOR EACH
REMARK 3 DOMAIN.
REMARK 3
REMARK 3 THE COORDINATES OF THE TWO DOMAINS HAVE BEEN BEST FITTED TO
REMARK 3 EACH OTHER.
REMARK 4
REMARK 4 1NCP 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_1000175235.
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: N, C
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 C 61 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS N 16 SG
REMARK 620 2 CYS C 27 SG 107.5
REMARK 620 3 HIS C 32 NE2 110.4 109.3
REMARK 620 4 HIS N 11 NE2 117.9 105.7 7.5
REMARK 620 5 CYS N 6 SG 116.3 8.8 105.3 100.8
REMARK 620 6 CYS C 24 SG 112.8 109.0 107.8 103.5 103.7
REMARK 620 7 CYS N 3 SG 115.6 106.4 107.4 102.8 100.9 3.1
REMARK 620 8 CYS C 37 SG 3.2 110.3 110.3 117.8 119.1 110.1 112.9
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN N 60 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 27 SG
REMARK 620 2 HIS C 32 NE2 115.9
REMARK 620 3 HIS N 11 NE2 113.3 8.1
REMARK 620 4 CYS N 6 SG 9.7 113.2 109.3
REMARK 620 5 CYS C 24 SG 116.9 114.2 110.8 112.4
REMARK 620 6 CYS N 3 SG 114.4 114.4 110.5 109.4 3.7
REMARK 620 7 CYS C 37 SG 103.0 100.6 108.7 112.7 102.8 106.2
REMARK 620 8 CYS N 16 SG 100.6 100.6 108.7 110.3 105.2 108.6 2.8
REMARK 620 N 1 2 3 4 5 6 7
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN N 60
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 61
DBREF 1NCP N 1 17 UNP P04585 POL_HV1H2 389 405
DBREF 1NCP C 22 39 UNP P24740 POL_HV1U4 410 427
SEQRES 1 N 17 VAL LYS CYS PHE ASN CYS GLY LYS GLU GLY HIS THR ALA
SEQRES 2 N 17 ARG ASN CYS ARG
SEQRES 1 C 18 LYS GLY CYS TRP LYS CYS GLY LYS GLU GLY HIS GLN MET
SEQRES 2 C 18 LYS ASP CYS THR GLU
HET ZN N 60 1
HET ZN C 61 1
HETNAM ZN ZINC ION
FORMUL 3 ZN 2(ZN 2+)
SHEET 1 A 2 LYS N 2 CYS N 16 0
SHEET 2 A 2 CYS C 24 CYS C 37 1 N CYS C 24 O LYS N 2
LINK ZN ZN C 61 SG CYS N 16 1555 1555 1.98
LINK ZN ZN C 61 SG CYS C 27 1555 1555 2.30
LINK ZN ZN C 61 NE2 HIS C 32 1555 1555 2.00
LINK ZN ZN C 61 NE2 HIS N 11 1555 1555 2.10
LINK ZN ZN C 61 SG CYS N 6 1555 1555 2.45
LINK ZN ZN C 61 SG CYS C 24 1555 1555 2.29
LINK ZN ZN C 61 SG CYS N 3 1555 1555 2.42
LINK ZN ZN C 61 SG CYS C 37 1555 1555 2.30
LINK ZN ZN N 60 SG CYS C 27 1555 1555 2.20
LINK ZN ZN N 60 NE2 HIS C 32 1555 1555 1.94
LINK ZN ZN N 60 NE2 HIS N 11 1555 1555 2.00
LINK ZN ZN N 60 SG CYS N 6 1555 1555 2.30
LINK ZN ZN N 60 SG CYS C 24 1555 1555 2.19
LINK ZN ZN N 60 SG CYS N 3 1555 1555 2.30
LINK ZN ZN N 60 SG CYS C 37 1555 1555 2.62
LINK ZN ZN N 60 SG CYS N 16 1555 1555 2.30
SITE 1 AC1 8 CYS C 24 CYS C 27 HIS C 32 CYS C 37
SITE 2 AC1 8 CYS N 3 CYS N 6 HIS N 11 CYS N 16
SITE 1 AC2 8 CYS C 24 CYS C 27 HIS C 32 CYS C 37
SITE 2 AC2 8 CYS N 3 CYS N 6 HIS N 11 CYS N 16
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 - 4 201 Bytes