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Biological Magnetic Resonance Data Bank


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BMRB Entry 30349

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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/BMR30349
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Title: Solution Structure of HIV-1 GP41 Transmembrane Domain in Bicelles   PubMed: 29277995

Deposition date: 2017-09-24 Original release date: 2018-01-19

Authors: Chiliveri, S.; Louis, J.; Ghirlando, R.; Baber, J.; Bax, A.

Citation: Chiliveri, S.; Louis, J.; Ghirlando, R.; Baber, J.; Bax, A.. "Tilted, Uninterrupted, Monomeric HIV-1 gp41 Transmembrane Helix from Residual Dipolar Couplings."  J. Am. Chem. Soc. 140, 34-37 (2018).

Assembly members:
entity_1, polymer, 40 residues, 4650.604 Da.

Natural source:   Common Name: HIV-1   Taxonomy ID: 11676   Superkingdom: Viruses   Kingdom: not available   Genus/species: Lentivirus HIV-1

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):
entity_1: NWLWYIRIFIIIVGSLIGLR IVFAVLSLVNRVRQGYSPLS

Data sets:
Data typeCount
13C chemical shifts77
15N chemical shifts38
1H chemical shifts38

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 40 residues - 4650.604 Da.

1   ASNTRPLEUTRPTYRILEARGILEPHEILE
2   ILEILEVALGLYSERLEUILEGLYLEUARG
3   ILEVALPHEALAVALLEUSERLEUVALASN
4   ARGVALARGGLNGLYTYRSERPROLEUSER

Samples:

sample_4: HIV-1 GP41 Transmembrane domain, [U-100% 15N; U-80% 2H], 40 uM; MES buffer 25 mM

sample_5: HIV-1 GP41 Transmembrane domain, [U-100% 15N; U-80% 2H], 70 uM; MES buffer 25 mM

sample_6: HIV-1 GP41 Transmembrane domain, [U-100% 15N; U-80% 2H], 300 uM; MES buffer 25 mM

sample_1: HIV-1 GP41 Transmembrane domain, [U-100% 13C; U-100% 15N; U-80% 2H], 500 uM; MES buffer 25 mM

sample_2: HIV-1 GP41 Transmembrane domain, [U-100% 15N; 80%-2H], 100 uM; MES buffer 25 mM

sample_3: HIV-1 GP41 Transmembrane domain, [U-100% 15N; 80%-2H], 100 uM; MES buffer 25 mM

sample_conditions_1: ionic strength: 25 mM; pH: 6.5; pressure: 1 bar; temperature: 318 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D TROSYsample_1isotropicsample_conditions_1
2D ARTSYsample_1isotropicsample_conditions_1
2D ARTSYsample_2anisotropicsample_conditions_1
2D ARTSYsample_3anisotropicsample_conditions_1
2D ARTSYsample_4anisotropicsample_conditions_1
2D ARTSYsample_5isotropicsample_conditions_1
2D TROSYsample_6isotropicsample_conditions_1

Software:

CcpNMR, CCPN - chemical shift assignment

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

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

NMR spectrometers:

  • Bruker AvanceII 900 MHz
  • Bruker AvanceIII 800 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts