BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 15364

Title: Solution Structure of Human Immunodificiency Virus Type-2 Nucleocapsid Protein   PubMed: 17202191

Authors: Matsui, T.; Kodera, Y.; Tanaka, T.; Endoh, H.; Tanaka, H.; Miyauchi, E.; Komatsu, H.; Kohno, T.; Maeda, T.

Citation: Matsui, T.; Kodera, Y.; Endoh, H.; Miyauchi, E.; Komatsu, H.; Sato, K.; Tanaka, T.; Kohno, T.; Maeda, T.. "RNA recognition mechanism of the minimal active domain of the human immunodeficiency virus type-2 nucleocapsid protein"  J. Biochem. 141, 269-277 (2007).

Assembly members:
Gag_polyprotein_(Pr55Gag), polymer, 49 residues, Formula weight is not available
ZN, non-polymer, 65.409 Da.

Natural source:   Common Name: HIV-2   Taxonomy ID: not available   Superkingdom: not available   Kingdom: not available   Genus/species: not available not available

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

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

Data sets:
Data typeCount
13C chemical shifts163
15N chemical shifts54
1H chemical shifts300
heteronuclear NOE values45
T1 relaxation values46
T2 relaxation values46

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1NCp81
2Zn12
3Zn22

Entities:

Entity 1, NCp8 49 residues - Formula weight is not available

1   ALAGLNGLNARGLYSVALILEARGCYSTRP
2   ASNCYSGLYLYSGLUGLYHISSERALAARG
3   GLNCYSARGALAPROARGARGGLNGLYCYS
4   TRPLYSCYSGLYLYSTHRGLYHISVALMET
5   ALALYSCYSPROGLUARGGLNALAGLY

Entity 2, Zn1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: Gag polyprotein (Pr55Gag), [U-98% 13C; U-98% 15N], 1.5 mM; ZINC ION 3.2 mM; DSS 0.5 mM; H2O 90%; D2O 10%

sample_2: Gag polyprotein (Pr55Gag) 1.5 mM; ZINC ION 3.2 mM; DSS 0.5 mM; D2O 99.6%

sample_conditions_1: pH: 5.8; 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
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HNHBsample_1isotropicsample_conditions_1
15N T1sample_1isotropicsample_conditions_1
15N T2sample_1isotropicsample_conditions_1
{1H}-15N NOEsample_1isotropicsample_conditions_1

Software:

ANSIG v3.3, Kraulis - collection

AZARA v2.7, Boucher - processing

X-PLOR NIH v2.9.9, Schwieters, Kuszewski, Tjandra and Clore - refinement

NMR spectrometers:

  • Bruker DMX 500 MHz

Related Database Links:

BMRB 15196
PDB
GB AAA43932 AAQ99470
SP P18041 P18042