BMRB Entry 51531
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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/BMR51531
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Title: 1H and 13C chemical shifts of a peptide derived from the membrane proximal external region of HIV-1 gp41 in 25% HFIP PubMed: 36400835
Deposition date: 2022-07-24 Original release date: 2022-11-28
Authors: Jimenez, M. Angeles; Partida-Hanon, Angelica; Nieva, Jose
Citation: Torralba, Johana; de la Arada, Igor; Partida-Hanon, Angelica; Rujas, Edurne; Arribas, Madalen; Insausti, Sara; Valotteau, Claire; Valle, Javier; Andreu, David; Caaveiro, Jose; Jimenez, Maria Angeles; Apellaniz, Beatriz; Redondo-Morata, Lorena; Nieva, Jose. "Molecular recognition of a membrane-anchored HIV-1 pan-neutralizing epitope" Commun. Biol. 5, 1265-1265 (2022).
Assembly members:
entity_1, polymer, 25 residues, 3213.9 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: NWFDITNWLWYIKLFIMIVG
KKKKK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 198 |
| 1H chemical shifts | 415 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | C-MPER-TMD690 | 1 |
Entities:
Entity 1, C-MPER-TMD690 25 residues - 3213.9 Da.
The sequence corresponds to residues 671-690 of HIV-1 Env protein. It contains a C-terminal Lys-tag.
| 1 | ASN | TRP | PHE | ASP | ILE | THR | ASN | TRP | LEU | TRP | ||||
| 2 | TYR | ILE | LYS | LEU | PHE | ILE | MET | ILE | VAL | GLY | ||||
| 3 | LYS | LYS | LYS | LYS | LYS |
Samples:
sample_1: C-MPER-TMD690 0.9 mM; H2O 67,5%; D2O, [U-100% 2H], 7,5%; HFIP, [U-98% 2H], 25%; HEPES 2 mM; DSS 0.1 mM
sample_2: C-MPER-TMD690 0.9 mM; D2O, [U-100% 2H], 75%; HFIP, [U-98% 2H], 25%; HEPES 2 mM; DSS 0.1 mM
sample_conditions_1: ionic strength: 2 mM; pH: 7.0; pressure: 1 atm; temperature: 308 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 |
| 2D 1H-13C HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H COSY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_2 | isotropic | sample_conditions_1 |
Software:
TOPSPIN - collection, processing
SPARKY - chemical shift assignment
CYANA - structure solution
NMR spectrometers:
- Bruker Avance 600 MHz