BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 34133

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: 2017-05-08 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: GIGAFGLLGFLAAGSKKXKN EQELLELDKWASLWN

Data sets:
Data typeCount
13C chemical shifts97
15N chemical shifts28
1H chemical shifts254

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 35 residues - 3822.411 Da.

1   GLYILEGLYALAPHEGLYLEULEUGLYPHE
2   LEUALAALAGLYSERLYSLYSACALYSASN
3   GLUGLNGLULEULEUGLULEUASPLYSTRP
4   ALASERLEUTRPASN

Samples:

sample_1: D2O, [U-99% 2H], 67.5%; DSS 0.1 mM; H2O 7.5%; HEPES 2 mM; HFIP, [U-98% 2H], 25%; scrFP-tag 0.6 ± 0.1 mM

sample_conditions_1: ionic strength: 2 mM; pH: 6.8 pH*; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H COSYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - refinement, structure calculation

SPARKY, Goddard - chemical shift assignment, peak picking

TOPSPIN, Bruker Biospin - collection, processing

NMR spectrometers:

  • Bruker Avance 600 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts