BMRB Entry 15511
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15511
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Title: 1H,13C and 15N chemical shift assignments for stereo-array isotope labelled (SAIL) C-terminal dimerization domain of SARS coronavirus nucleocapsid protein PubMed: 18561946
Deposition date: 2007-10-06 Original release date: 2008-06-26
Authors: Takeda, Mitsuhiro; Chang, Chung-ke; Ikeya, Teppei; Guntert, Peter; Chang, Yuan-hsiang; Hsu, Yen-lan; Huang, Tai-huang; Kainosho, Masatsune
Citation: Takeda, Mitsuhiro; Chang, Chung-ke; Ikeya, Teppei; Guntert, Peter; Chang, Yuan-hsiang; Hsu, Yen-lan; Huang, Tai-huang; Kainosho, Masatsune. "Solution Structure of the C-terminal Dimerization Domain of SARS Coronavirus Nucleocapsid Protein Solved by the SAIL-NMR Method" J. Mol. Biol. 380, 608-622 (2008).
Assembly members:
SARS_coronavirus_nucleocapsid_protein_residues_248-365, polymer, 128 residues, Formula weight is not available
Natural source: Common Name: not available Taxonomy ID: 248485 Superkingdom: Viruses Kingdom: not available Genus/species: Coronavirus SARS coronavirus
Experimental source: Production method: cell free synthesis Host organism: E. coli - cell free
Entity Sequences (FASTA):
SARS_coronavirus_nucleocapsid_protein_residues_248-365: MHHHHHHAMGTKKSAAEASK
KPRQKRTATKQYNVTQAFGR
RGPEQTQGNFGDQDLIRQGT
DYKHWPQIAQFAPSASAFFG
MSRIGMEVTPSGTWLTYHGA
IKLDDKDPQFKDNVILLNKH
IDAYKTFP
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 347 |
| 15N chemical shifts | 123 |
| 1H chemical shifts | 575 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | subunit1 | 1 |
| 2 | subunit2 | 1 |
Entities:
Entity 1, subunit1 128 residues - Formula weight is not available
| 1 | MET | HIS | HIS | HIS | HIS | HIS | HIS | ALA | MET | GLY | ||||
| 2 | THR | LYS | LYS | SER | ALA | ALA | GLU | ALA | SER | LYS | ||||
| 3 | LYS | PRO | ARG | GLN | LYS | ARG | THR | ALA | THR | LYS | ||||
| 4 | GLN | TYR | ASN | VAL | THR | GLN | ALA | PHE | GLY | ARG | ||||
| 5 | ARG | GLY | PRO | GLU | GLN | THR | GLN | GLY | ASN | PHE | ||||
| 6 | GLY | ASP | GLN | ASP | LEU | ILE | ARG | GLN | GLY | THR | ||||
| 7 | ASP | TYR | LYS | HIS | TRP | PRO | GLN | ILE | ALA | GLN | ||||
| 8 | PHE | ALA | PRO | SER | ALA | SER | ALA | PHE | PHE | GLY | ||||
| 9 | MET | SER | ARG | ILE | GLY | MET | GLU | VAL | THR | PRO | ||||
| 10 | SER | GLY | THR | TRP | LEU | THR | TYR | HIS | GLY | ALA | ||||
| 11 | ILE | LYS | LEU | ASP | ASP | LYS | ASP | PRO | GLN | PHE | ||||
| 12 | LYS | ASP | ASN | VAL | ILE | LEU | LEU | ASN | LYS | HIS | ||||
| 13 | ILE | ASP | ALA | TYR | LYS | THR | PHE | PRO |
Samples:
sample_1: SARS coronavirus nucleocapsid protein residues 248-365, full SAIL isotope labeling, 0.5 ± 0.1 mM; D2O 10%; H2O 90 mM
sample_conditions_1: ionic strength: 50 mM; pH: 6.0; pressure: 1 atm; temperature: 303 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA, Goddard - chemical shift assignment
CYANA v2.2, Guntert, Mumenthaler and Wuthrich - structure solution
NMR spectrometers:
- Bruker DRX 800 MHz
- Bruker Avance 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts