BMRB Entry 51617
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51617
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Title: Nish P3 PubMed: 36989298
Deposition date: 2022-09-06 Original release date: 2023-03-13
Authors: Sethi, Ashish; Gooley, Paul; Dubey, Abhinav; Arthanari, Haribabu
Citation: Sethi, Ashish; Rawlinson, Stephen; Dubey, Abhinav; Ang, Ching-Seng; Choi, Yoon Hee; Yan, Fei; Okada, Kazuma; Rozario, Ashley; Brice, Aaron; Ito, Naoto; Williamson, Nicholas; Hatters, Danny; Bell, Toby; Arthanari, Haribabu; Moseley, Gregory; Gooley, Paul. "Structural insights into the multifunctionality of rabies virus P3 protein" Proc. Natl. Acad. Sci. U. S. A. 120, e2217066120-e2217066120 (2023).
Assembly members:
entity_1, polymer, 297 residues, Formula weight is not available
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28a
Entity Sequences (FASTA):
entity_1: MSKIFVNPSAIRAGLADLEM
AEETVDLINRNIEDNQAHLQ
GEPIEVDSLPEDMSRLHLDD
GKLPDLGRMSKAGEGRHQED
FQMDEGEDPSLLFQSYLDNV
GVQIVRQMRSGERFLKIWSQ
TVEEIISYVTVNFPNPSGRS
SEDKSTQTTSQEPKKETTST
PSQRKSQSLKSRTMAQTASG
PPSLEWSATNEEDDLSVEAE
IAHQIAESFSKKYKFPSRSS
GIFLYNFEQLKMNLDDIVKE
AKNVPGVTRLAHDGSKLPLR
CVLGWVALANSKKFQLLVEA
NKLNKIMQDDLNRYASC
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 202 |
| 15N chemical shifts | 66 |
| 1H chemical shifts | 66 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Nish P3, chain 1 | 1 |
| 2 | Nish P3, chain 2 | 1 |
Entities:
Entity 1, Nish P3, chain 1 297 residues - Formula weight is not available
| 1 | MET | SER | LYS | ILE | PHE | VAL | ASN | PRO | SER | ALA | ||||
| 2 | ILE | ARG | ALA | GLY | LEU | ALA | ASP | LEU | GLU | MET | ||||
| 3 | ALA | GLU | GLU | THR | VAL | ASP | LEU | ILE | ASN | ARG | ||||
| 4 | ASN | ILE | GLU | ASP | ASN | GLN | ALA | HIS | LEU | GLN | ||||
| 5 | GLY | GLU | PRO | ILE | GLU | VAL | ASP | SER | LEU | PRO | ||||
| 6 | GLU | ASP | MET | SER | ARG | LEU | HIS | LEU | ASP | ASP | ||||
| 7 | GLY | LYS | LEU | PRO | ASP | LEU | GLY | ARG | MET | SER | ||||
| 8 | LYS | ALA | GLY | GLU | GLY | ARG | HIS | GLN | GLU | ASP | ||||
| 9 | PHE | GLN | MET | ASP | GLU | GLY | GLU | ASP | PRO | SER | ||||
| 10 | LEU | LEU | PHE | GLN | SER | TYR | LEU | ASP | ASN | VAL | ||||
| 11 | GLY | VAL | GLN | ILE | VAL | ARG | GLN | MET | ARG | SER | ||||
| 12 | GLY | GLU | ARG | PHE | LEU | LYS | ILE | TRP | SER | GLN | ||||
| 13 | THR | VAL | GLU | GLU | ILE | ILE | SER | TYR | VAL | THR | ||||
| 14 | VAL | ASN | PHE | PRO | ASN | PRO | SER | GLY | ARG | SER | ||||
| 15 | SER | GLU | ASP | LYS | SER | THR | GLN | THR | THR | SER | ||||
| 16 | GLN | GLU | PRO | LYS | LYS | GLU | THR | THR | SER | THR | ||||
| 17 | PRO | SER | GLN | ARG | LYS | SER | GLN | SER | LEU | LYS | ||||
| 18 | SER | ARG | THR | MET | ALA | GLN | THR | ALA | SER | GLY | ||||
| 19 | PRO | PRO | SER | LEU | GLU | TRP | SER | ALA | THR | ASN | ||||
| 20 | GLU | GLU | ASP | ASP | LEU | SER | VAL | GLU | ALA | GLU | ||||
| 21 | ILE | ALA | HIS | GLN | ILE | ALA | GLU | SER | PHE | SER | ||||
| 22 | LYS | LYS | TYR | LYS | PHE | PRO | SER | ARG | SER | SER | ||||
| 23 | GLY | ILE | PHE | LEU | TYR | ASN | PHE | GLU | GLN | LEU | ||||
| 24 | LYS | MET | ASN | LEU | ASP | ASP | ILE | VAL | LYS | GLU | ||||
| 25 | ALA | LYS | ASN | VAL | PRO | GLY | VAL | THR | ARG | LEU | ||||
| 26 | ALA | HIS | ASP | GLY | SER | LYS | LEU | PRO | LEU | ARG | ||||
| 27 | CYS | VAL | LEU | GLY | TRP | VAL | ALA | LEU | ALA | ASN | ||||
| 28 | SER | LYS | LYS | PHE | GLN | LEU | LEU | VAL | GLU | ALA | ||||
| 29 | ASN | LYS | LEU | ASN | LYS | ILE | MET | GLN | ASP | ASP | ||||
| 30 | LEU | ASN | ARG | TYR | ALA | SER | CYS |
Samples:
sample_1: Nish P3, [U-100% 13C; U-100% 15N], 0.8 uM; potassium phosphate 50 mM; sodium chloride 150 mM; DTT 1 mM
sample_conditions_1: ionic strength: 0.05 M; pH: 6.8; pressure: 1 atm; temperature: 295 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRFAM-SPARKY - chemical shift assignment
TOPSPIN - collection
NMR spectrometers:
- Bruker Avance 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts