BMRB Entry 52513
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52513
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
All files associated with the entry
Citation: Devantier, Kira; Toft-Bertelsen, Trine; Prestel, Andreas; Kjar, Viktoria; Sahin, Cagla; Giulini, Marco; Louka, Stavroula; Spiess, Katja; Manandhar, Asmita; Qvortrup, Katrine; Ulven, Trond; Bentzen, Bo; Bonvin, Alexandre Mjj; MacAulay, Nanna; Kragelund, Birthe; Rosenkilde, Mette. "The SH protein of mumps virus is a druggable pentameric viroporin" Sci. Adv. 11, eads3071-eads3071 (2025).
PubMed: 40479045
Assembly members:
entity_1, polymer, 58 residues, Formula weight is not available
Natural source: Common Name: Mumps orthorubulavirus Taxonomy ID: 2560602 Superkingdom: Viruses Kingdom: not available Genus/species: Mumps orthorubulavirus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pGEX-4T-1
Entity Sequences (FASTA):
entity_1: GSPAIQPPLYLTFLLLILLY
LIITLYVWIILTVTYKTAVR
HAALYQRSFFHWSFDHSL
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 151 |
| 15N chemical shifts | 53 |
| 1H chemical shifts | 82 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | small hydrophobic protein | 1 |
Entities:
Entity 1, small hydrophobic protein 58 residues - Formula weight is not available
GS from thrombin cleavage site. Followed by residues 2-57 of mumps small hydrophobic (SH) protein genotype G
| 1 | GLY | SER | PRO | ALA | ILE | GLN | PRO | PRO | LEU | TYR | ||||
| 2 | LEU | THR | PHE | LEU | LEU | LEU | ILE | LEU | LEU | TYR | ||||
| 3 | LEU | ILE | ILE | THR | LEU | TYR | VAL | TRP | ILE | ILE | ||||
| 4 | LEU | THR | VAL | THR | TYR | LYS | THR | ALA | VAL | ARG | ||||
| 5 | HIS | ALA | ALA | LEU | TYR | GLN | ARG | SER | PHE | PHE | ||||
| 6 | HIS | TRP | SER | PHE | ASP | HIS | SER | LEU |
Samples:
sample_1: Small hydrophobic protein, [U-99% 13C; U-99% 15N], 0.6 mM; D2O 10%; TFE 66%; H2O 24%; DSS 25 uM
sample_conditions_1: ionic strength: 0 M; pH: 6; pressure: 1 atm; temperature: 310 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D 15N-separated NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D (H)CCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
ANALYSIS - chemical shift assignment
NMR spectrometers:
- Bruker AVANCE III 600 MHz
- Bruker AVANCE III 750 MHz
- Bruker AVANCE III 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks