BMRB Entry 26034
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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/BMR26034
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Title: NMR assignment and structure of a peptide derived from the membrane proximal external region of HIV-1 gp41 in the presence of dodecylphosphocholine micelles PubMed: 27905530
Deposition date: 2016-04-14 Original release date: 2017-02-16
Authors: Jimenez, M. Angeles; Nieva, Jose; Rujas, Edurne; Partida-Hanon, Angelica; Bruix, Marta
Citation: Rujas, Edurne; Partida-Hanon, Angelica; Gulzar, Naveed; Morante, Koldo; Apellaniz, Beatriz; Garcia-Porras, Miguel; Bruix, Marta; Tsumoto, Kouhei; Scott, Jamie; Jimenez, M. Angeles; Caaveiro, Jose; Nieva, Jose. "Structural basis for broad neutralization of HIV-1 through the molecular recognition of 10E8 helical epitope at the membrane interface" Sci Rep 6, 38177-38177 (2016).
Assembly members:
10E8p, polymer, 36 residues, 4624.739 Da.
Natural source: Common Name: HIV-1 Taxonomy ID: 11676 Superkingdom: Viruses Kingdom: not available Genus/species: Lintivirus not available
Experimental source: Production method: chemical synthesis
Entity Sequences (FASTA):
10E8p: KKKKDKWASLWNWFDITNWL
WYIKLFIMIVGKKKKK
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 87 |
1H chemical shifts | 294 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | 10E8p | 1 |
Entities:
Entity 1, 10E8p 36 residues - 4624.739 Da.
1 | LYS | LYS | LYS | LYS | ASP | LYS | TRP | ALA | SER | LEU | ||||
2 | TRP | ASN | TRP | PHE | ASP | ILE | THR | ASN | TRP | LEU | ||||
3 | TRP | TYR | ILE | LYS | LEU | PHE | ILE | MET | ILE | VAL | ||||
4 | GLY | LYS | LYS | LYS | LYS | LYS |
Samples:
sample_1: 10E8p 0.5 mM; DPC, [U-2H], 20 mM; HEPES 2 mM; DSS 0.1 mM; H2O 90%; D2O, [U-2H], 10%
sample_2: 10E8p 0.5 mM; DPC, [U-2H], 20 mM; HEPES 2 mM; DSS 0.1 mM; D2O, [U-2H], 100%
sample_conditions_1: ionic strength: 2 mM; pH: 7; pressure: 1 atm; temperature: 308 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
2D 1H-1H NOESY | sample_1 | 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 aliphatic | sample_2 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection, processing
SPARKY, Goddard - chemical shift assignment
TALOS, Cornilescu, Delaglio and Bax - dihedral angle restraints
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz