BMRB Entry 27176
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27176
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Title: 1H, 13C, and 15N Chemical Shift Assignments for truncated forms of the coronavirus nsp1 protein and its solubility domain GB1 PubMed: 28750053
Deposition date: 2017-07-13 Original release date: 2017-08-10
Authors: Vazquez, Leonardo; Almeida, Marcius
Citation: Vazquez, Leonardo; Lima, Luis; Almeida, Marcius. "Comprehensive structural analysis of designed incomplete polypeptide chains of the replicase nonstructural protein 1 from the severe acute respiratory syndrome coronavirus" PLoS ONE 12, e0182132-e0182132 (2017).
Assembly members:
nsp1(13-25), polymer, 99 residues, Formula weight is not available
Natural source: Common Name: SARS coronavirus Taxonomy ID: 227859 Superkingdom: Viruses Kingdom: not available Genus/species: SARS coronavirus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
nsp1(13-25): MGHVQLSLPVLQVRDHGRAP
IKVESQEHKLVPRGSFQYKL
ILNGKTLKGETTTEAVDAAT
AEKVFKQYANDNGVDGEWTY
DDATKTFTVTESGHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 247 |
| 15N chemical shifts | 86 |
| 1H chemical shifts | 201 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Coronavirus nsp1 truncated proteins; nsp1(13-25) | 1 |
Entities:
Entity 1, Coronavirus nsp1 truncated proteins; nsp1(13-25) 99 residues - Formula weight is not available
| 1 | MET | GLY | HIS | VAL | GLN | LEU | SER | LEU | PRO | VAL | ||||
| 2 | LEU | GLN | VAL | ARG | ASP | HIS | GLY | ARG | ALA | PRO | ||||
| 3 | ILE | LYS | VAL | GLU | SER | GLN | GLU | HIS | LYS | LEU | ||||
| 4 | VAL | PRO | ARG | GLY | SER | PHE | GLN | TYR | LYS | LEU | ||||
| 5 | ILE | LEU | ASN | GLY | LYS | THR | LEU | LYS | GLY | GLU | ||||
| 6 | THR | THR | THR | GLU | ALA | VAL | ASP | ALA | ALA | THR | ||||
| 7 | ALA | GLU | LYS | VAL | PHE | LYS | GLN | TYR | ALA | ASN | ||||
| 8 | ASP | ASN | GLY | VAL | ASP | GLY | GLU | TRP | THR | TYR | ||||
| 9 | ASP | ASP | ALA | THR | LYS | THR | PHE | THR | VAL | THR | ||||
| 10 | GLU | SER | GLY | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
All_samples: potassium phosphate 2 mM; sodium chloride 250 mM; DTT 1 mM; sodium azide 3 mM; nsp1(13-25), [U-13C; U-15N], 2 mM
Condition_of_all_samples: ionic strength: 250 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | All_samples | isotropic | Condition_of_all_samples |
| 2D 1H-13C HSQC aliphatic | All_samples | isotropic | Condition_of_all_samples |
| 2D 1H-13C HSQC aromatic | All_samples | isotropic | Condition_of_all_samples |
| 3D CBCA(CO)NH | All_samples | isotropic | Condition_of_all_samples |
| 3D HNCACB | All_samples | isotropic | Condition_of_all_samples |
| 3D HNCO | All_samples | isotropic | Condition_of_all_samples |
| 3D HNCA | All_samples | isotropic | Condition_of_all_samples |
| 3D HBHA(CO)NH | All_samples | isotropic | Condition_of_all_samples |
Software:
XEASY, Keller and Wuthrich - chemical shift assignment
NMR spectrometers:
- Bruker Avance 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts