Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27498
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Citation: Zhan, Jingyu; Hossain, Md Alamgir; Sethi, Ashish; Ose, Toyoyuki; Moseley, Gregory; Gooley, Paul. "1H, 15N and 13C resonance assignments of the C-terminal domain of the P protein of the Nishigahara strain of rabies virus" Biomol. NMR Assign. 13, 5-8 (2019).
PubMed: 30238347
Assembly members:
RABV_P-protein_CTD, polymer, 115 residues, 13000.82 Da.
Natural source: Common Name: Lyssavirus genus Taxonomy ID: 11286 Superkingdom: viruses Kingdom: ssRNA2 Genus/species: Lyssavirus genus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28a
Entity Sequences (FASTA):
RABV_P-protein_CTD: GHMWSATNEEDDLSVEAEIA
HQIAESFSKKYKFPSRSSGI
FLYNFEQLKMNLDDIVKEAK
NVPGVTRLAHDGSKLPLRCV
LGWVALANSKKFQLLVEANK
LNKIMQDDLNRYASS
Data type | Count |
13C chemical shifts | 477 |
15N chemical shifts | 121 |
1H chemical shifts | 760 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | RABV P-protein CTD | 1 |
Entity 1, RABV P-protein CTD 115 residues - 13000.82 Da.
The first 3 residues GHM represent a non-native part introduced from cloning.
1 | GLY | HIS | MET | TRP | SER | ALA | THR | ASN | GLU | GLU | ||||
2 | ASP | ASP | LEU | SER | VAL | GLU | ALA | GLU | ILE | ALA | ||||
3 | HIS | GLN | ILE | ALA | GLU | SER | PHE | SER | LYS | LYS | ||||
4 | TYR | LYS | PHE | PRO | SER | ARG | SER | SER | GLY | ILE | ||||
5 | PHE | LEU | TYR | ASN | PHE | GLU | GLN | LEU | LYS | MET | ||||
6 | ASN | LEU | ASP | ASP | ILE | VAL | LYS | GLU | ALA | LYS | ||||
7 | ASN | VAL | PRO | GLY | VAL | THR | ARG | LEU | ALA | HIS | ||||
8 | ASP | GLY | SER | LYS | LEU | PRO | LEU | ARG | CYS | VAL | ||||
9 | LEU | GLY | TRP | VAL | ALA | LEU | ALA | ASN | SER | LYS | ||||
10 | LYS | PHE | GLN | LEU | LEU | VAL | GLU | ALA | ASN | LYS | ||||
11 | LEU | ASN | LYS | ILE | MET | GLN | ASP | ASP | LEU | ASN | ||||
12 | ARG | TYR | ALA | SER | SER |
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