BMRB Entry 17985

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR17985
MolProbity Validation Chart

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Title:
Structure of BST-2/Tetherin Transmembrane Domain
Deposition date:
2011-10-07
Original release date:
2011-12-12
Authors:
Skasko, Mark; Wang, Yan; Tian, Ye; Tokarev, Andrey; Munguia, Jason; Ruiz, Autumn; Stephens, Edward; Opella, Stanley; Guatelli, John
Citation:

Citation: Skasko, Mark; Wang, Yan; Tian, Ye; Tokarev, Andrey; Munguia, Jason; Ruiz, Autumn; Stephens, Edward; Opella, Stanley; Guatelli, John. "HIV-1 Vpu protein antagonizes innate restriction factor BST-2 via lipid-embedded helix-helix interactions."  J. Biol. Chem. 287, 58-67 (2012).
PubMed: 22072710

Assembly members:

Assembly members:
BST-2, polymer, 24 residues, 2529.350 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET31b(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
BST-2: LLLGIGILVLLIIVILGVPL IIFT

Data sets:
Data typeCount
13C chemical shifts24
15N chemical shifts23
1H chemical shifts23

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1BST-21

Entities:

Entity 1, BST-2 24 residues - 2529.350 Da.

1   LEULEULEUGLYILEGLYILELEUVALLEU
2   LEUILEILEVALILELEUGLYVALPROLEU
3   ILEILEPHETHR

Samples:

sample_1: BST-2, [U-100% 15N], 0.5 mM; H2O, [U-100% 15N], 90%; D2O, [U-100% 15N], 10%

sample_conditions_1: ionic strength: 0 M; pH: 7.4; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1

Software:

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView, Johnson, One Moon Scientific - data analysis

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ BAA05679 BAD96844 BAF83788 BAG64608
GB AAH33873 ACX46128 ADI58594 ADI58595 EAW84602
REF NP_001266147 NP_001266560 NP_004326
SP Q10589
AlphaFold Q10589

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