BMRB Entry 15389
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15389
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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
- assigned_chemical_shifts
Data type | Count |
15N chemical shifts | 21 |
1H chemical shifts | 120 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | HIV fusion peptide | 1 |
Entities:
Entity 1, HIV fusion peptide 31 residues - Formula weight is not available
1 | ALA | VAL | GLY | ILE | GLY | ALA | LEU | PHE | LEU | GLY | ||||
2 | PHE | LEU | GLY | ALA | ALA | GLY | SER | THR | VAL | GLY | ||||
3 | ALA | ALA | SER | GLY | GLY | GLY | LYS | LYS | LYS | LYS | ||||
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:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D NOESY | sample_2 | isotropic | sample_conditions_1 |
2D TOCSY | sample_2 | isotropic | sample_conditions_1 |
3D_15N-separated_NOESY | sample_1 | isotropic | sample_conditions_1 |
HNHA | sample_1 | isotropic | sample_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
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts