BMRB Entry 26034

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:

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:

Assembly members:
10E8p, polymer, 36 residues, 4624.739 Da.

Natural source:

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

Experimental source:

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):

Entity Sequences (FASTA):
10E8p: KKKKDKWASLWNWFDITNWL WYIKLFIMIVGKKKKK

Data sets:
Data typeCount
13C chemical shifts87
1H chemical shifts294

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
110E8p1

Entities:

Entity 1, 10E8p 36 residues - 4624.739 Da.

1   LYSLYSLYSLYSASPLYSTRPALASERLEU
2   TRPASNTRPPHEASPILETHRASNTRPLEU
3   TRPTYRILELYSLEUPHEILEMETILEVAL
4   GLYLYSLYSLYSLYSLYS

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:

NameSampleSample stateSample conditions
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_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