BMRB Entry 52514

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52514

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Title:
Chemical Shift Assignments for Small Hydrophobic (SH) protein residues 1-34 in DHPC
Deposition date:
2024-06-20
Original release date:
2026-02-23
Authors:
Devantier, Kira; Kragelund, Birthe
Citation:

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:

Assembly members:
entity_1, polymer, 35 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Mumps orthorubulavirus   Taxonomy ID: 2560602   Superkingdom: Viruses   Kingdom: not available   Genus/species: Mumps orthorubulavirus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pGEX-4T-1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSPAIQPPLYLTFLLLILLY LIITLYVWIILTVTY

Data sets:
Data typeCount
13C chemical shifts89
15N chemical shifts29
1H chemical shifts49

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1small hydrophobic protein1

Entities:

Entity 1, small hydrophobic protein 35 residues - Formula weight is not available

GS from thrombin cleavage site. Followed by residues 2-34 of mumps small hydrophobic (SH) protein genotype G

1   GLYSERPROALAILEGLNPROPROLEUTYR
2   LEUTHRPHELEULEULEUILELEULEUTYR
3   LEUILEILETHRLEUTYRVALTRPILEILE
4   LEUTHRVALTHRTYR

Samples:

sample_1: Small hydrophobic protein, [U-99% 13C; U-99% 15N], 0.8 mM; D2O 10%; DSS 25 uM; DHPC 400 mM

sample_conditions_1: ionic strength: 0 M; pH: 7.2; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
2D 1H-15N TROSYsample_1isotropicsample_conditions_1

Software:

ANALYSIS - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE III 750 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks