BMRB Entry 17217
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR17217
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Title: Solution Structure of the C-terminal Dimerization Domain of SARS Coronavirus Nucleocapsid Protein Solved by the SAIL-NMR Method PubMed: 18561946
Deposition date: 2010-09-29 Original release date: 2010-11-10
Authors: Takeda, Mitsuhiro; Chang, Chung-ke; Ikeya, Teppei; Guntert, Peter; Chang, Yuan-hsiang; Hsu, Yen-Ian; Huang, Tai-huang; Kainosho, Masatsune
Citation: Takeda, Mitsuhiro; Chang, Chung-ke; Ikeya, Teppei; Guntert, Peter; Chang, Yuan-hsiang; Hsu, Yen-Ian; 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, polymer, 128 residues, Formula weight is not available
dT10, polymer, 10 residues, Formula weight is not available
Natural source: Common Name: SARS coronavirus Taxonomy ID: 227859 Superkingdom: virus Kingdom: not available Genus/species: Betacoronavirus Severe acute respiratory syndrome-related coronavirus
Experimental source: Production method: cell free synthesis Host organism: Escherichia coli
Entity Sequences (FASTA):
SARS: MHHHHHHAMGTKKSAAEASK
KPRQKRTATKQYNVTQAFGR
RGPEQTQGNFGDQDLIRQGT
DYKHWPQIAQFAPSASAFFG
MSRIGMEVTPSGTWLTYHGA
IKLDDKDPQFKDNVILLNKH
IDAYKTFP
dT10: XXXXXXXXXX
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | SARS | 1 |
2 | dT10 | 2 |
Entities:
Entity 1, SARS 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 |
Entity 2, dT10 10 residues - Formula weight is not available
X=5AT
1 | 5AT | 5AT | 5AT | 5AT | 5AT | 5AT | 5AT | 5AT | 5AT | 5AT |
Samples:
sample_1: SARS, [U-15N], 0.5 mM; sodium phosphate 10 mM; sodium chloride 50 mM; EDTA 1 mM; DSS 1 mM; sodium azide 0.01%; dT10 titrated mM; H2O 90%; D2O 10%
sample_conditions_1: pH: 6.0; pressure: ambient atm; temperature: 303 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
xwinnmr, Bruker Biospin - processing
iNMR, Nucleomatica, Italy - processing
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz