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BMRB Entry 7384 BMRB - Biological Magnetic Resonance Bank

BMRB Entry 7384

Title:
Solution Structure of Human Immunodificiency Virus Type-2 Nucleocapsid Protein
Deposition date:
2007-03-21
Original release date:
2008-08-14
Authors:
Matsui, T.; Kodera, Y.; Tanaka, T.; Endoh, H.; Tanaka, H.; Miyauchi, E.; Komatsu, H.; Kohno, T.; Maeda, T.
Citation:

Citation: Matsui, Takashi; Kodera, Yoshio; Miyauchi, Emi; Tanaka, Hidekazu; Endoh, Hiroshi; Komatsu, Hiroyoshi; Tanaka, Takeshi; Kohno, Toshiyuki; Maeda, Tadakazu. "Structural role of the secondary active domain of HIV-2 NCp8 in multi-functionality."  Biochem. Biophys. Res. Commun. 358, 673-678 (2007).
PubMed: 17511966

Assembly members:

Assembly members:
Gag_polyprotein_(Pr55Gag), polymer, 49 residues, 65.409 Da.
ZN, non-polymer, 65.409 Da.

Natural source:

Natural source:   Common Name: HIV-2   Taxonomy ID: 11709   Superkingdom: Viruses   Kingdom: not available   Genus/species: Lentivirus Human immunodeficiency virus 2

Experimental source:

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Gag_polyprotein_(Pr55Gag): AQQRKVIRCWNCGKEGHSAR QCRAPRRQGCWKCGKTGHVM AKCPERQAG

Data sets:
Data typeCount
13C chemical shifts163
15N chemical shifts54
1H chemical shifts300

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1Gag_polyprotein_(Pr55Gag)1
2ZINC 12
3ZINC 22

Entities:

Entity 1, Gag_polyprotein_(Pr55Gag) 49 residues - 65.409 Da.

1   ALAGLNGLNARGLYSVALILEARGCYSTRP
2   ASNCYSGLYLYSGLUGLYHISSERALAARG
3   GLNCYSARGALAPROARGARGGLNGLYCYS
4   TRPLYSCYSGLYLYSTHRGLYHISVALMET
5   ALALYSCYSPROGLUARGGLNALAGLY

Entity 2, ZINC 1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: Gag_polyprotein_(Pr55Gag), [U-13C; U-15N], 1.5 mM; ZnCl2 3.2 mM; H2O 90%; D2O 10%

sample_2: Gag_polyprotein_(Pr55Gag), [U-13C; U-15N], 1.5 mM; ZnCl2 3.2 mM; D2O 99.96%

sample_conditions_1: ionic strength: . .; pH: 5.8; pressure: 1 atm; temperature: 288 K

Experiments:

NameSampleSample stateSample conditions
3D_13C-separated_NOESYsample_1isotropicsample_conditions_1
3D_15N-separated_NOESYsample_1isotropicsample_conditions_1
2D NOESYsample_2isotropicsample_conditions_1
HNHAsample_1isotropicsample_conditions_1
2D TOCSYsample_2isotropicsample_conditions_1

Software:

ANSIG v3.3, Kraulis, P.J. - collection

AZARA v2.7, Boucher, W. - processing

X-PLOR NIH v2.9.9, PARDI, A. - structure solution

X-PLOR NIH v2.9.9, PARDI, A. - refinement

NMR spectrometers:

  • Bruker DMX 500 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks