BMRB Entry 30955
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30955
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NMR-STAR v3 text file.
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Title: SARS-CoV-2 Nucleocapsid N-terminal domain (N-NTD) protein PubMed: 35638584
Deposition date: 2021-09-29 Original release date: 2022-06-03
Authors: Sarkar, S.; Runge, B.; Russell, R.; Calero, D.; Zeinalilathori, S.; Quinn, C.; Lu, M.; Calero, G.; Gronenborn, A.; Polenova, T.
Citation: Sarkar, Sucharita; Runge, Brent; Russell, Ryan; Movellan, Kumar Tekwani; Calero, Daniel; Zeinalilathori, Somayeh; Quinn, Caitlin; Lu, Manman; Calero, Guillermo; Gronenborn, Angela; Polenova, Tatyana. "Atomic-Resolution Structure of SARS-CoV-2 Nucleocapsid Protein N-Terminal Domain" J. Am. Chem. Soc. 144, 10543-10555 (2022).
Assembly members:
entity_1, polymer, 136 residues, 14994.733 Da.
Natural source: Common Name: 2019-nCoV, 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 BL21(DE3)
Entity Sequences (FASTA):
entity_1: SRRPQGLPNNTASWFTALTQ
HGKEDLKFPRGQGVPINTNS
SPDDQIGYYRRATRRIRGGD
GKMKDLSPRWYFYYLGTGPE
AGLPYGANKDGIIWVATEGA
LNTPKDHIGTRNPANNAAIV
LQLPQGTTLPKGFYAE
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 595 |
| 15N chemical shifts | 147 |
| 1H chemical shifts | 133 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | unit_1 | 1 |
Entities:
Entity 1, unit_1 136 residues - 14994.733 Da.
| 1 | SER | ARG | ARG | PRO | GLN | GLY | LEU | PRO | ASN | ASN | ||||
| 2 | THR | ALA | SER | TRP | PHE | THR | ALA | LEU | THR | GLN | ||||
| 3 | HIS | GLY | LYS | GLU | ASP | LEU | LYS | PHE | PRO | ARG | ||||
| 4 | GLY | GLN | GLY | VAL | PRO | ILE | ASN | THR | ASN | SER | ||||
| 5 | SER | PRO | ASP | ASP | GLN | ILE | GLY | TYR | TYR | ARG | ||||
| 6 | ARG | ALA | THR | ARG | ARG | ILE | ARG | GLY | GLY | ASP | ||||
| 7 | GLY | LYS | MET | LYS | ASP | LEU | SER | PRO | ARG | TRP | ||||
| 8 | TYR | PHE | TYR | TYR | LEU | GLY | THR | GLY | PRO | GLU | ||||
| 9 | ALA | GLY | LEU | PRO | TYR | GLY | ALA | ASN | LYS | ASP | ||||
| 10 | GLY | ILE | ILE | TRP | VAL | ALA | THR | GLU | GLY | ALA | ||||
| 11 | LEU | ASN | THR | PRO | LYS | ASP | HIS | ILE | GLY | THR | ||||
| 12 | ARG | ASN | PRO | ALA | ASN | ASN | ALA | ALA | ILE | VAL | ||||
| 13 | LEU | GLN | LEU | PRO | GLN | GLY | THR | THR | LEU | PRO | ||||
| 14 | LYS | GLY | PHE | TYR | ALA | GLU |
Samples:
sample_1: N-NTD, [U-100% 13C; U-100% 15N], 30 mg/mL
sample_conditions_1: ionic strength: 50 mM; pH: 6.2; pressure: 1 atm; temperature: 298.15 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D CORD 25 ms | sample_1 | isotropic | sample_conditions_1 |
| 2D CORD 100 ms | sample_1 | isotropic | sample_conditions_1 |
| 2D CORD 250 ms | sample_1 | isotropic | sample_conditions_1 |
| 2D CORD 500 ms | sample_1 | isotropic | sample_conditions_1 |
| 2D NCACX 25 ms | sample_1 | isotropic | sample_conditions_1 |
| 2D NCOCX 25 ms | sample_1 | isotropic | sample_conditions_1 |
| 2D CP RFDR | sample_1 | isotropic | sample_conditions_1 |
| 2D hNH HETCOR | sample_1 | isotropic | sample_conditions_1 |
| 2D hCH HETCOR | sample_1 | isotropic | sample_conditions_1 |
| 3D hCANH | sample_1 | isotropic | sample_conditions_1 |
| 3D hCONH | sample_1 | isotropic | sample_conditions_1 |
Software:
TopSpin, Bruker Biospin - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
CcpNmr Analysis, Stevens TJ, Fogh RH, Boucher W, Higman VA, Eisenmenger F, Bardiaux B, van Rossum BJ, Oschkinat H, Laue ED - data analysis
NMRFAM-SPARKY, Lee W, Tonelli M, Markley JL - chemical shift assignment
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure calculation
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