BMRB Entry 52010
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52010
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Title: SARS-CoV-2 Nucleocapsid protein NTD Y109A mutant PubMed: 37901441
Deposition date: 2023-06-30 Original release date: 2023-11-15
Authors: Estelle, Aidan; Forsythe, Heather; Yu, Zhen; Hughes, Kaitlyn; Lasher, Brittany; Allen, Patrick; Reardon, Patrick; Hendrix, David; Barbar, Elisar
Citation: Estelle, Aidan; Forsythe, Heather; Yu, Zhen; Hughes, Kaitlyn; Lasher, Brittany; Allen, Patrick; Reardon, Patrick; Hendrix, David; Barbar, Elisar. "RNA structure and multiple weak interactions balance the interplay between RNA binding and phase separation of SARS-CoV-2 nucleocapsid" PNAS Nexus 2, pgad333-pgad333 (2023).
Assembly members:
entity_1, polymer, 132 residues, Formula weight is not available
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: pET24d
Entity Sequences (FASTA):
entity_1: GAHMNNTASWFTALTQHGKE
DLKFPRGQGVPINTNSSPDD
QIGYYRRATRRIRGGDGKMK
DLSPRWAFYYLGTGPEAGLP
YGANKDGIIWVATEGALNTP
KDHIGTRNPANNAAIVLQLP
QGTTLPKGFYAE
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 106 |
| 1H chemical shifts | 106 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | NTD Y109A | 1 |
Entities:
Entity 1, NTD Y109A 132 residues - Formula weight is not available
N-terminal domain of the nucleocapsid with a Y-to-A mutation at residue 109.
| 1 | GLY | ALA | HIS | MET | ASN | ASN | THR | ALA | SER | TRP | ||||
| 2 | PHE | THR | ALA | LEU | THR | GLN | HIS | GLY | LYS | GLU | ||||
| 3 | ASP | LEU | LYS | PHE | PRO | ARG | GLY | GLN | GLY | VAL | ||||
| 4 | PRO | ILE | ASN | THR | ASN | SER | SER | PRO | ASP | ASP | ||||
| 5 | GLN | ILE | GLY | TYR | TYR | ARG | ARG | ALA | THR | ARG | ||||
| 6 | ARG | ILE | ARG | GLY | GLY | ASP | GLY | LYS | MET | LYS | ||||
| 7 | ASP | LEU | SER | PRO | ARG | TRP | ALA | PHE | TYR | TYR | ||||
| 8 | LEU | GLY | THR | GLY | PRO | GLU | ALA | GLY | LEU | PRO | ||||
| 9 | TYR | GLY | ALA | ASN | LYS | ASP | GLY | ILE | ILE | TRP | ||||
| 10 | VAL | ALA | THR | GLU | GLY | ALA | LEU | ASN | THR | PRO | ||||
| 11 | LYS | ASP | HIS | ILE | GLY | THR | ARG | ASN | PRO | ALA | ||||
| 12 | ASN | ASN | ALA | ALA | ILE | VAL | LEU | GLN | LEU | PRO | ||||
| 13 | GLN | GLY | THR | THR | LEU | PRO | LYS | GLY | PHE | TYR | ||||
| 14 | ALA | GLU |
Samples:
sample_1: NTD Y109A, [U-100% 15N], 500 uM; sodium chloride 20 mM; sodium phosphate 20 mM
sample_conditions_1: ionic strength: 0.04 M; pH: 6.5; pressure: 1 atm; temperature: 298.15 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRViewJ v9.2.0-b27 - chemical shift assignment
NMR spectrometers:
- Bruker Avance 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts