BMRB Entry 34045
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34045
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Title: Solution NMR structure of the X domain of Peste des Petits Ruminants phosphoprotein
Deposition date: 2016-09-21 Original release date: 2017-10-19
Authors: Pereira, N.; Piuzzi, M.; Bontems, F.; Eleouet, J.; Sizun, C.
Citation: Pereira, N.; Basbous, N.; Piuzzi, M.; Bontems, F.; Eleouet, J.; Sizun, C.. "Solution structure of the X domain of Peste des Petits Ruminants Virus phosphoprotein and interaction with the nucleoprotein" . ., .-..
Assembly members:
entity_1, polymer, 53 residues, 5964.977 Da.
Natural source: Common Name: Small ruminant morbillivirus Taxonomy ID: 31604 Superkingdom: Viruses Kingdom: not available Genus/species: Morbillivirus Small ruminant morbillivirus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3)
Entity Sequences (FASTA):
entity_1: GSSSRSVIRSIIKSSKLNID
HKDYLLDLLNDVKGSKDLKE
FHKMLTAILAKQP
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 440 |
| 15N chemical shifts | 53 |
| 1H chemical shifts | 746 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 53 residues - 5964.977 Da.
| 1 | GLY | SER | SER | SER | ARG | SER | VAL | ILE | ARG | SER | ||||
| 2 | ILE | ILE | LYS | SER | SER | LYS | LEU | ASN | ILE | ASP | ||||
| 3 | HIS | LYS | ASP | TYR | LEU | LEU | ASP | LEU | LEU | ASN | ||||
| 4 | ASP | VAL | LYS | GLY | SER | LYS | ASP | LEU | LYS | GLU | ||||
| 5 | PHE | HIS | LYS | MET | LEU | THR | ALA | ILE | LEU | ALA | ||||
| 6 | LYS | GLN | PRO |
Samples:
sample_1: PPRV_PXD, [U-13C; U-15N], 200 ± 20 uM; sodium chloride 300 ± 30 mM; sodium phosphate 20 ± 2 mM
sample_2: PPRV_PXD, [U-13C; U-15N], 200 ± 20 uM; sodium chloride 300 ± 30 mM; sodium phosphate 20 ± 2 mM
sample_conditions_1: ionic strength: 300 mM; pH: 7.4; pressure: 1 bar; temperature: 288.0 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(COCA)CB | sample_1 | isotropic | sample_conditions_1 |
| 2D NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_2 | isotropic | sample_conditions_1 |
| 2D NOESY | sample_2 | isotropic | sample_conditions_1 |
Software:
Analysis v2.2.2, CCPN - chemical shift assignment, peak picking
CYANA v3.97, Guntert, Mumenthaler and Wuthrich - structure calculation
TOPSPIN v2.2.2, Bruker Biospin - processing
Talos+, Yang Shen, NIDDK - data analysis
NMR spectrometers:
- Bruker AvanceIII 800 MHz
- Bruker AvanceIII 950 MHz