BMRB Entry 31124

Name: NMR structure of the funnel-web spider toxin Hc3a
Published: 2024-03-08

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PDB ID: 8uwf
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR31124
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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:

NMR structure of the funnel-web spider toxin Hc3a

Deposition date:

2023-11-06

Original release date:

2024-03-08

Authors:

Budusan, E.; Payne, C.; Gonzalez, T.; Clark, R.; Rosengren, K.; Rash, L.; Cristofori-Armstrong, B.

Citation:

Citation: Budusan, E.; Payne, C.; Gonzalez, T.; Obergrussberger, A.; Becker, N.; Clark, R.; Rosengren, K.; Rash, L.; Cristofori-Armstrong, B.. "The funnel-web spider venom derived single knot peptide Hc3a modulates acid-sensing ion channel 1a desensitisation" .

Assembly members:

Assembly members:
entity_1, polymer, 39 residues, 4495.241 Da.

Natural source:

Natural source: Common Name: Hadronyche cerberea Taxonomy ID: 1107879 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Hadronyche cerberea

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GNECIRKWLSCVDRKNDCCE GLECWKRRGNKSSVCVPIT

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	116
15N chemical shifts	40
1H chemical shifts	269

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 - 4495.241 Da.

1

GLY

ASN

GLU

CYS

ILE

ARG

LYS

TRP

LEU

SER

2

CYS

VAL

ASP

ARG

LYS

ASN

ASP

CYS

GLU

3

GLY

LEU

GLU

CYS

TRP

LYS

ARG

GLY

ASN

4

LYS

SER

VAL

CYS

VAL

PRO

ILE

THR

Samples:

sample_1: Hc3a 4 ± 0.1 mg/mL

sample_conditions_1: ionic strength: 0 mM; pH: 3.5; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 0 mM; pH: 3.5; pressure: 1 atm; temperature: 288 K

sample_conditions_3: ionic strength: 0 mM; pH: 3.5; pressure: 1 atm; temperature: 293 K

sample_conditions_4: ionic strength: 0 mM; pH: 3.5; pressure: 1 atm; temperature: 303 K

sample_conditions_5: ionic strength: 0 mM; pH: 3.5; pressure: 1 atm; temperature: 308 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_2
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_3
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_4
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_5

Software:

CARA, Keller and Wuthrich - chemical shift assignment, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - refinement, structure calculation

MolProbity, Richardson - data analysis

NMR spectrometers:

Bruker AVANCE 900 MHz

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