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 15389

Title: solution structure of hiv-1 gp41 fusion domain bound to DPC micelle   PubMed: 17963720

Deposition date: 2007-07-18 Original release date: 2008-06-18

Authors: Li, Y; Tamm, L.

Citation: Tamm, Lukas; Lai, Alex; Li, Yinling. "Combined NMR and EPR spectroscopy to determine structures of viral fusion domains in membranes"  Biochim. Biophys. Acta 1768, 3052-3060 (2007).

Assembly members:
Envelope_glycoprotein, polymer, 31 residues, Formula weight is not available

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   Vector: PET31b(+)

Entity Sequences (FASTA):
Envelope_glycoprotein: AVGIGALFLGFLGAAGSTVG AASGGGKKKKK

Data sets:
Data typeCount
15N chemical shifts21
1H chemical shifts120

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HIV fusion peptide1

Entities:

Entity 1, HIV fusion peptide 31 residues - Formula weight is not available

1   ALAVALGLYILEGLYALALEUPHELEUGLY
2   PHELEUGLYALAALAGLYSERTHRVALGLY
3   ALAALASERGLYGLYGLYLYSLYSLYSLYS
4   LYS

Samples:

sample_1: Envelope glycoprotein, [U-15N], 1 mM; D38-DPC 200 mM; NAN3 0.05%; DTT 5 mM; D4-ACETIC ACID 20 mM; H2O 95%; D2O 5%

sample_2: Envelope glycoprotein 2 mM; D38-DPC 400 mM; NAN3 0.05%; DTT 5 mM; D4-ACETIC ACID 20 mM; H2O 95%; D2O 5%

sample_conditions_1: pH: 7.4; pressure: 1 atm; temperature: 303 K

Experiments:

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

Software:

VNMR, Varian - collection

NMRPipe v2.4, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY v3.110, Goddard - data analysis

DYANA v1.5, Guntert, Braun and Wuthrich - structure solution

OPAL v2.6, Luginbuhl, Guntert, Billeter and Wuthrich - refinement

NMR spectrometers:

  • Bruker AVANCE 600 MHz
  • Varian INOVA 600 MHz
  • Varian INOVA 500 MHz

Related Database Links:

PDB
GB AAB68317 AAB68318 AAB68319 AAB68320 AAB68321

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