BMRB Entry 16000
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR16000
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Title: Solution structure of the nucleocapsid-binding domain of the measles virus phosphoprotein PubMed: 20058326
Deposition date: 2008-10-23 Original release date: 2010-05-06
Authors: Gely, Stephane; Bourhis, Jean Marie; Longhi, Sonia; Darbon, Herve; Bernard, Cedric
Citation: Gely, Stephane; Lowry, David; Bernard, Cedric; Jensen, Malene; Blackledge, Martin; Costanzo, Stephanie; Bourhis, Jean-Marie; Darbon, Herve; Daughdrill, Gary; Longhi, Sonia. "Solution structure of the C-terminal X domain of the measles virus phosphoprotein and interaction with the intrinsically disordered C-terminal domain of the nucleoprotein." J. Mol. Recognit. 23, 435-447 (2010).
Assembly members:
XD_domain, polymer, 44 residues, 5169.205 Da.
Natural source: Common Name: Measles Taxonomy ID: 11234 Superkingdom: virus Kingdom: not available Genus/species: Morbillivirus not available
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
XD_domain: SVIRSIIKSSRLEEDRKRYL
MTLLDDIKGANDLAKFHQML
VKII
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 289 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | XD_domain | 1 |
Entities:
Entity 1, XD_domain 44 residues - 5169.205 Da.
| 1 | SER | VAL | ILE | ARG | SER | ILE | ILE | LYS | SER | SER | ||||
| 2 | ARG | LEU | GLU | GLU | ASP | ARG | LYS | ARG | TYR | LEU | ||||
| 3 | MET | THR | LEU | LEU | ASP | ASP | ILE | LYS | GLY | ALA | ||||
| 4 | ASN | ASP | LEU | ALA | LYS | PHE | HIS | GLN | MET | LEU | ||||
| 5 | VAL | LYS | ILE | ILE |
Samples:
sample_1: XD domain 1.5 uM; H2O 90%; D2O 10%
sample_2: XD domain 1.06 uM; H2O 90%; D2O 10%
sample_conditions_1: pH: 7; pressure: 1 atm; temperature: 300 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
ARIA v1.2, Linge, O, . - chemical shift assignment, refinement, structure solution
NMR spectrometers:
- Bruker DRX 500 MHz