BMRB Entry 17985

Name: Structure of BST-2/Tetherin Transmembrane Domain
Published: 2011-12-12

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PDB ID: 2lk9
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR17985
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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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:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	24
15N chemical shifts	23
1H chemical shifts	23

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	BST-2	1

Entities:

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

1

LEU

GLY

ILE

GLY

ILE

LEU

VAL

LEU

2

LEU

ILE

VAL

ILE

LEU

GLY

VAL

PRO

LEU

3

ILE

PHE

THR

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_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

PDB	2LK9
DBJ	BAA05679 BAD96844 BAF83788 BAG64608
GB	AAH33873 ACX46128 ADI58594 ADI58595 EAW84602
REF	NP_001266147 NP_001266560 NP_004326
SP	Q10589
AlphaFold	Q10589