BMRB Entry 30872

Name: Solution structure of tarantula toxin omega-Avsp1a
Published: 2022-02-25

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PDB ID: 7lvn
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30872
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:

Solution structure of tarantula toxin omega-Avsp1a

Deposition date:

2021-02-26

Original release date:

2022-02-25

Authors:

Chin, Y.; Herzig, V.; King, G.

Citation:

Citation: Herzig, Volker; Chen, Yong-Cyuan; Chin, Yanni K-Y; Dekan, Zoltan; Chang, Yu-Wang; Yu, Hui-Ming; Alewood, Paul; Chen, Chien-Chang; King, Glenn. "The Tarantula Toxin omega-Avsp1a Specifically Inhibits Human Ca V 3.1 and Ca V 3.3 via the Extracellular S3-S4 Loop of the Domain 1 Voltage-Sensor" Biomedicines 10, 1066-1066 (2022).
PubMed: 35625803

Assembly members:

Assembly members:
entity_1, polymer, 37 residues, 4239.845 Da.

Natural source:

Natural source: Common Name: spiders Taxonomy ID: 2042175 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Avicularia Avicularia sp. AVIC29FPM

Experimental source:

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GDCHKFLGWCRGEPDPCCEH LSCSRKHGWCVWDWTVX

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list
- spectral_peak_list_1

Data type	Count
13C chemical shifts	122
15N chemical shifts	39
1H chemical shifts	235

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 37 residues - 4239.845 Da.

1

GLY

ASP

CYS

HIS

LYS

PHE

LEU

GLY

TRP

CYS

2

ARG

GLY

GLU

PRO

ASP

PRO

CYS

GLU

HIS

3

LEU

SER

CYS

SER

ARG

LYS

HIS

GLY

TRP

CYS

4

VAL

TRP

ASP

TRP

THR

VAL

NH2

Samples:

sample_1: Asvp1a 4.7 mg/mL; sodium phosphate 20 mM

sample_conditions_1: ionic strength: 20 mM; pH: 3.6; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

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

CcpNmr Analysis, CCPN - chemical shift assignment, peak picking

TopSpin, Bruker Biospin - collection

TALOS-N, Cornilescu, Delaglio and Bax - geometry optimization

NMR spectrometers:

Bruker AVANCE 600 MHz

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