BMRB Entry 50098
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50098
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Title: Nipah virus phosphoprotein, residues 1-100 PubMed: 32348724
Deposition date: 2019-11-29 Original release date: 2020-01-10
Authors: Jensen, Malene; Blackledge, Martin
Citation: Jensen, Malene Ringkjybing; Yabukarski, Filip; Communie, Guillaume; Condamine, Eric; Mas, Caroline; Volchkova, Valentina; Tarbouriech, Nicolas; Bourhis, Jean-Marie; Volchkov, Viktor; Blackledge, Martin; Jamin, Marc. "Structural Description of the Nipah Virus Phosphoprotein and Its Interaction With STAT1" Biophys. J. 118, 2470-2488 (2020).
Assembly members:
Nipah virus phosphoprotein, residues 1-100, polymer, 108 residues, Formula weight is not available
Natural source: Common Name: Nipah virus Taxonomy ID: 121791 Superkingdom: Virus Kingdom: not available Genus/species: henipavirus Nipah virus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: na
Entity Sequences (FASTA):
Nipah virus phosphoprotein, residues 1-100: MDKLELVNDGLNIIDFIQKN
QKEIQKTYGRSSIQQPSIKD
QTKAWEDFLQCTSGESEQVE
GGMSKDDGDVERRNLEDLSS
TSPTDGTIGKRVSNTRDWAE
LEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 285 |
| 15N chemical shifts | 97 |
| 1H chemical shifts | 97 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Nipah virus phosphoprotein | 1 |
Entities:
Entity 1, Nipah virus phosphoprotein 108 residues - Formula weight is not available
| 1 | MET | ASP | LYS | LEU | GLU | LEU | VAL | ASN | ASP | GLY | ||||
| 2 | LEU | ASN | ILE | ILE | ASP | PHE | ILE | GLN | LYS | ASN | ||||
| 3 | GLN | LYS | GLU | ILE | GLN | LYS | THR | TYR | GLY | ARG | ||||
| 4 | SER | SER | ILE | GLN | GLN | PRO | SER | ILE | LYS | ASP | ||||
| 5 | GLN | THR | LYS | ALA | TRP | GLU | ASP | PHE | LEU | GLN | ||||
| 6 | CYS | THR | SER | GLY | GLU | SER | GLU | GLN | VAL | GLU | ||||
| 7 | GLY | GLY | MET | SER | LYS | ASP | ASP | GLY | ASP | VAL | ||||
| 8 | GLU | ARG | ARG | ASN | LEU | GLU | ASP | LEU | SER | SER | ||||
| 9 | THR | SER | PRO | THR | ASP | GLY | THR | ILE | GLY | LYS | ||||
| 10 | ARG | VAL | SER | ASN | THR | ARG | ASP | TRP | ALA | GLU | ||||
| 11 | LEU | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: entity_1, [U-13C; U-15N], 0.5 mM; Bis-Tris ph 6.0 20 mM; NaCl 150 mM; Arginine 50 mM; glutamate 50 mM; TCEP 0.5 mM
sample_conditions_1: ionic strength: 150 mM; pH: 6.0; pressure: 1 atm; temperature: 298 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 HNCACO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCOCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCOCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY, Goddard - peak picking
NMR spectrometers:
- Agilent Unity 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts