Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52515

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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Name: Chemical Shift Assignments for Small Hydrophobic (SH) protein residues 2-12
Published: 2026-02-23

Title:

Chemical Shift Assignments for Small Hydrophobic (SH) protein residues 2-12

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, 11 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: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: PAIQPPLYLTF

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	18
15N chemical shifts	7
1H chemical shifts	37

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	small hydrophobic protein	1

Entities:

Entity 1, small hydrophobic protein 11 residues - Formula weight is not available

Residues 2-12 of mumps small hydrophobic (SH) protein genotype G

1

PRO

ALA

ILE

GLN

PRO

LEU

TYR

LEU

THR

2

PHE

Samples:

sample_1: Small hydrophobic protein 0.6 mM; D2O 10%; DSS 25 uM; sodium phosphate 20 mM

sample_conditions_1: ionic strength: 0 M; pH: 7.2; pressure: 1 atm; temperature: 283 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
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H ROESY	sample_1	isotropic	sample_conditions_1

Software:

ANALYSIS - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III 600 MHz

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

BMRB Entry 52515