BMRB Entry 52446
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52446
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Title: SARS-CoV-2 Fusion Domain: K825A Mutant PubMed: 39002677
Deposition date: 2024-05-07 Original release date: 2024-07-19
Authors: Birtles, Daniel; Lee, Jinwoo
Citation: Birtles, Daniel; Guiyab, Lijon; Abbas, Wafa; Lee, Jinwoo. "Positive residues of the SARS-CoV-2 fusion domain are key contributors to the initiation of membrane fusion" J. Biol. Chem. 300, 107564-107564 (2024).
Assembly members:
entity_1, polymer, 40 residues, 4367.01 Da.
Natural source: Common Name: SARS-CoV-2 Taxonomy ID: 2697049 Superkingdom: Viruses Kingdom: not available Genus/species: Betacoronavirus HCoV-SARS
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET41
Entity Sequences (FASTA):
entity_1: SFIEDLLFNAVTLADAGFIK
QYGDCLGDIAARDLICAQKF
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 65 |
| 15N chemical shifts | 39 |
| 19F chemical shifts | 4 |
| 1H chemical shifts | 39 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | SARS-CoV-2 Fusion Domain mutant K825A | 1 |
Entities:
Entity 1, SARS-CoV-2 Fusion Domain mutant K825A 40 residues - 4367.01 Da.
| 1 | SER | PFF | ILE | GLU | ASP | LEU | LEU | PFF | ASN | ALA | |
| 2 | VAL | THR | LEU | ALA | ASP | ALA | GLY | PFF | ILE | LYS | |
| 3 | GLN | TYR | GLY | ASP | CYS | LEU | GLY | ASP | ILE | ALA | |
| 4 | ALA | ARG | ASP | LEU | ILE | CYS | ALA | GLN | LYS | PFF |
Samples:
sample_1: SARS-CoV-2 Fusion Domain mutant K825A, [U-15N], 360 uM; SARS-CoV-2 Fusion Domain mutant K825A, [U-13C], 360 uM
sample_2: SARS-CoV-2 Fusion Domain mutant K825A, 19F-Phe, 360 uM
sample_conditions_1: pH: 5.0; temperature: 296 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 1H 19F | sample_2 | isotropic | sample_conditions_1 |
Software:
SPARKY - chemical shift assignment
MestReNova - chemical shift assignment
NMR spectrometers:
- Bruker AVANCE III 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts