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 50584

Title: Ebola Virus Glycoprotein Interacts with Cholesterol to Enhance Membrane Fusion and Cell Entry, wt   PubMed: 33462517

Deposition date: 2020-11-19 Original release date: 2020-12-22

Authors: Lee, Jinwoo; Liang, Binyong; Tamm, Lukas

Citation: Lee, Jinwoo; Kreutzberger, Alex; Odongo, Laura; Nelson, Elizabeth; Nyenhuis, David; Kiessling, Volker; Liang, Binyong; Cafiso, David; White, Judith; Tamm, Lukas. "Ebola virus glycoprotein interacts with cholesterol to enhance membrane fusion and cell entry"  Nat. Struct. Mol. Biol. 28, 181-189 (2021).

Assembly members:
entity_1, polymer, 47 residues, 5132 Da.

Natural source:   Common Name: Zaire ebolavirus   Taxonomy ID: 186538   Superkingdom: Viruses   Kingdom: not available   Genus/species: Ebolavirus ZEBOV

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET24a

Entity Sequences (FASTA):
entity_1: GSDKTLPDQGDNDNWWTGWR QWIPAGIGVTGVVIAVIALF AIAKFVF

Data sets:
Data typeCount
15N chemical shifts82
1H chemical shifts82

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1Ebola GP2 MPER/TM1

Entities:

Entity 1, Ebola GP2 MPER/TM 47 residues - 5132 Da.

The first residue is G630, followed by S631, D632, sequentially and all the way to the last one F676.

1   GLYSERASPLYSTHRLEUPROASPGLNGLY
2   ASPASNASPASNTRPTRPTHRGLYTRPARG
3   GLNTRPILEPROALAGLYILEGLYVALTHR
4   GLYVALVALILEALAVALILEALALEUPHE
5   ALAILEALALYSPHEVALPHE

Samples:

sample_1: Ebola GP2 MPER/TM, [U-99% 13C; U-99% 15N], 0.5 mM; sodium phosphate 25 mM; sodium chloride 100 mM; DHPC 188 mM; DMPC 94 mM

sample_2: Ebola GP2 MPER/TM, [U-99% 13C; U-99% 15N], 0.5 mM; Cholesterol 15%; sodium phosphate 25 mM; sodium chloride 100 mM; DHPC 188 mM; DMPC 94 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 5.5; pressure: 1 atm; temperature: 318 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1

Software:

NMRPipe - processing

SPARKY - data analysis

NMR spectrometers:

  • Bruker AVANCE III 800 MHz

Related Database Links:

UNP Q05320
AlphaFold Q8JS62

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