BMRB Entry 34130
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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/BMR34130
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Title: NMR assignment and structure of a peptide derived from the fusion peptide of HIV-1 gp41 in the presence of dodecylphosphocholine micelles PubMed: 28930470
Deposition date: 2017-05-04 Original release date: 2017-11-28
Authors: Jimenez, M.; Serrano, S.; Nieva, J.; Huarte, N.
Citation: Serrano, S.; Huarte, N.; Rujas, E.; Andreu, D.; Nieva, J.; Jimenez, M.. "Structure-Related Roles for the Conservation of the HIV-1 Fusion Peptide Sequence Revealed by Nuclear Magnetic Resonance" Biochemistry 56, 5503-5511 (2017).
Assembly members:
entity_1, polymer, 35 residues, 3822.411 Da.
Natural source: Common Name: HIV-1 Taxonomy ID: 11676 Superkingdom: Viruses Kingdom: not available Genus/species: Lentivirus HIV-1
Experimental source: Production method: chemical synthesis
Entity Sequences (FASTA):
entity_1: GIGALFLGFLGAAGSKKXKN
EQELLELDKWASLWN
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 45 |
| 1H chemical shifts | 258 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 35 residues - 3822.411 Da.
| 1 | GLY | ILE | GLY | ALA | LEU | PHE | LEU | GLY | PHE | LEU | ||||
| 2 | GLY | ALA | ALA | GLY | SER | LYS | LYS | ACA | LYS | ASN | ||||
| 3 | GLU | GLN | GLU | LEU | LEU | GLU | LEU | ASP | LYS | TRP | ||||
| 4 | ALA | SER | LEU | TRP | ASN |
Samples:
sample_1: D2O, [U-99% 2H], 10%; DPC, [U-98% 2H], 20 mM; DSS 0.1 mM; H2O 90%; HEPES 2.0 mM; wtFP-tag 0.6 ± 0.1 mM
sample_conditions_1: ionic strength: 2 mM; pH: 6.8 pH*; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-1H COSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation
SPARKY, Goddard - chemical shift assignment, peak picking
TOPSPIN, Bruker Biospin - collection, processing
NMR spectrometers:
- Bruker Avance 600 MHz