BMRB Entry 26906
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26906
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Title: Backbone chemical shift assignment of the C-terminal domain of Respiratory Syncytial Virus phosphoprotein PubMed: 28031463
Deposition date: 2016-09-22 Original release date: 2017-02-15
Authors: Lassoued, Safa; Pereira, Nelson; Fix, Jenna; Galloux, Marie; Sizun, Christina; Eleouet, Jean-Francois
Citation: Pereira, Nelson; Cardone, Christophe; Lassoued, Safa; Galloux, Marie; Fix, Jenna; Assrir, Nadine; Lescop, Ewen; Bontems, Francois; Eleouet, Jean-Francois; Sizun, Christina. "New Insights into Structural Disorder in Human Respiratory Syncytial Virus Phosphoprotein and Implications for Binding of Protein Partners" J. Biol. Chem. 292, 2120-2131 (2017).
Assembly members:
P-CTD, polymer, 83 residues, 9323.1498 Da.
Natural source: Common Name: human RSV Taxonomy ID: 11250 Superkingdom: Viruses Kingdom: not available Genus/species: Orthopneumovirus HRSV
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
P-CTD: GSSARDGIRDAMVGLREEMI
EKIRTEALMTNDRLEAMARL
RNEESEKMAKDTSDEVSLNP
TSEKLNNLLEGNDSDNDLSL
EDF
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 238 |
| 15N chemical shifts | 81 |
| 1H chemical shifts | 159 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | P-CTD | 1 |
Entities:
Entity 1, P-CTD 83 residues - 9323.1498 Da.
P-CTD is a phosphoprotein fragment corresponding to the C-terminal domains of hRSV (residues S161-DF241). The two N-terminal residues (GS) are left over from a cleaved GST-tag.
| 1 | GLY | SER | SER | ALA | ARG | ASP | GLY | ILE | ARG | ASP | ||||
| 2 | ALA | MET | VAL | GLY | LEU | ARG | GLU | GLU | MET | ILE | ||||
| 3 | GLU | LYS | ILE | ARG | THR | GLU | ALA | LEU | MET | THR | ||||
| 4 | ASN | ASP | ARG | LEU | GLU | ALA | MET | ALA | ARG | LEU | ||||
| 5 | ARG | ASN | GLU | GLU | SER | GLU | LYS | MET | ALA | LYS | ||||
| 6 | ASP | THR | SER | ASP | GLU | VAL | SER | LEU | ASN | PRO | ||||
| 7 | THR | SER | GLU | LYS | LEU | ASN | ASN | LEU | LEU | GLU | ||||
| 8 | GLY | ASN | ASP | SER | ASP | ASN | ASP | LEU | SER | LEU | ||||
| 9 | GLU | ASP | PHE |
Samples:
P-CTD_15N13C: P-CTD, [U-13C; U-15N; U-2H], 0.15 ± 2e-06 mM; sodium phosphate 20.00 ± 0.002 mM; soudim chloride 100.00 ± 0.01 mM
CondSet1: ionic strength: 0.100 M; pH: 6.500; pressure: 1.000 atm; temperature: 288.000 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | P-CTD_15N13C | isotropic | CondSet1 |
| 3D HNCA | P-CTD_15N13C | isotropic | CondSet1 |
| 3D HN(CO)CA | P-CTD_15N13C | isotropic | CondSet1 |
| 3D HNHA | P-CTD_15N13C | isotropic | CondSet1 |
| 3D HNCO | P-CTD_15N13C | isotropic | CondSet1 |
| 3D HNCACB | P-CTD_15N13C | isotropic | CondSet1 |
| 3D CBCA(CO)NH | P-CTD_15N13C | isotropic | CondSet1 |
Software:
CcpNmr_Analysis v2.2, CCPN - chemical shift assignment, data analysis, peak picking
Topspin v3.1, Bruker - collection, processing
NMR spectrometers:
- Bruker Avance 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts