BMRB Entry 50584
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50584
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NMR-STAR v3 text file.
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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).
PubMed: 33462517
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
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 82 |
| 1H chemical shifts | 82 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Ebola GP2 MPER/TM | 1 |
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 | GLY | SER | ASP | LYS | THR | LEU | PRO | ASP | GLN | GLY | ||||
| 2 | ASP | ASN | ASP | ASN | TRP | TRP | THR | GLY | TRP | ARG | ||||
| 3 | GLN | TRP | ILE | PRO | ALA | GLY | ILE | GLY | VAL | THR | ||||
| 4 | GLY | VAL | VAL | ILE | ALA | VAL | ILE | ALA | LEU | PHE | ||||
| 5 | ALA | ILE | ALA | LYS | PHE | VAL | PHE |
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:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
Software:
NMRPipe - processing
SPARKY - data analysis
NMR spectrometers:
- Bruker AVANCE III 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks