BMRB Entry 31079

Name: Structural and functional characterisation of Tst2, a novel TRPV1 inhibitory peptide from the Australian sea anemone Telmatactis stephensoni
Published: 2023-10-07

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PDB ID: 8sem
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR31079
MolProbity Validation Chart

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Structural and functional characterisation of Tst2, a novel TRPV1 inhibitory peptide from the Australian sea anemone Telmatactis stephensoni

Deposition date:

2023-04-10

Original release date:

2023-10-07

Authors:

Elnahriry, K.; Wai, D.; Norton, R.

Citation:

Citation: Elnahriry, K.; Wai, D.; Ashwood, L.; Naseem, M.; Szanto, T.; Guo, S.; Panyi, G.; Prentis, P.; Norton, R.. "Structural and functional characterisation of Tst2, a novel TRPV1 inhibitory peptide from the Australian sea anemone Telmatactis stephensoni." Biochim. Biophys. Acta Proteins Proteom. 1872, 140952-140952 (2023).
PubMed: 37640250

Assembly members:

Assembly members:
entity_1, polymer, 39 residues, 4035.715 Da.

Natural source:

Natural source: Common Name: sea anemones Taxonomy ID: 2835637 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Telmatactis stephensoni

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GCKGQDAPCSKSKDCCGEAS MCSKGADGKKTCMIDKLWG

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list
- spectral_peak_list_1

Data type	Count
13C chemical shifts	110
15N chemical shifts	39
1H chemical shifts	200

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 39 residues - 4035.715 Da.

1

GLY

CYS

LYS

GLY

GLN

ASP

ALA

PRO

CYS

SER

2

LYS

SER

LYS

ASP

CYS

GLY

GLU

ALA

SER

3

MET

CYS

SER

LYS

GLY

ALA

ASP

GLY

LYS

4

THR

CYS

MET

ILE

ASP

LYS

LEU

TRP

GLY

Samples:

sample_1: Tst2, [U-100% 13C; U-100% 15N], 550 uM

sample_conditions_1: ionic strength: 0.55 mM; pH: 4.7; pressure: 1 bar; temperature: 293 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1

Software:

X-PLOR NIH v2.48, Schwieters, Kuszewski, Tjandra and Clore - refinement

CYANA v3.98.13, Guntert, Mumenthaler and Wuthrich - structure calculation

Sparky v3.134, Goddard - chemical shift assignment, peak picking

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