BMRB Entry 34776

Name: Spider toxin Pha1b (PnTx3-6) from Phoneutria nigriventer targeting CaV2.x calcium channels and TRPA1 channel
Published: 2023-06-15

Click here to enlarge.

PDB ID: 8bwb
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34776
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

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

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Spider toxin Pha1b (PnTx3-6) from Phoneutria nigriventer targeting CaV2.x calcium channels and TRPA1 channel

Deposition date:

2022-12-06

Original release date:

2023-06-15

Authors:

Mironov, P.; Chernaya, E.; Paramonov, A.; Shenkarev, Z.

Citation:

Citation: Lyukmanova, Ekaterina; Mironov, Pavel; Kulbatskii, Dmitrii; Shulepko, Mikhail; Paramonov, Alexander; Chernaya, Elizaveta; Logashina, Yulia; Andreev, Yaroslav; Kirpichnikov, Mikhail; Shenkarev, Zakhar. "Recombinant Production, NMR Solution Structure, and Membrane Interaction of the Pha1b Toxin, a TRPA1 Modulator from the Brazilian Armed Spider Phoneutria nigriventer" Toxins (Basel) 15, 378-378 (2023).
PubMed: 37368679

Assembly members:

Assembly members:
entity_1, polymer, 55 residues, 6055.089 Da.

Natural source:

Natural source: Common Name: Brazilian armed spider Taxonomy ID: 6918 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Phoneutria nigriventer

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-32a(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: ACIPRGEICTDDCECCGCDN QCYCPPGSSLGIFKCSCAHA NKYFCNRKKEKCKKA

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	145
15N chemical shifts	57
1H chemical shifts	335

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 55 residues - 6055.089 Da.

1

ALA

CYS

ILE

PRO

ARG

GLY

GLU

ILE

CYS

THR

2

ASP

CYS

GLU

CYS

GLY

CYS

ASP

ASN

3

GLN

CYS

TYR

CYS

PRO

GLY

SER

LEU

4

GLY

ILE

PHE

LYS

CYS

SER

CYS

ALA

HIS

ALA

5

ASN

LYS

TYR

PHE

CYS

ASN

ARG

LYS

GLU

6

LYS

CYS

LYS

ALA

Samples:

sample_1: Pha1b 1.7 mM; D2O, [U-99% 2H], 5%

sample_2: Pha1b, [U-100% 15N], 2.7 mM; D2O, [U-99% 2H], 5%; sodium acetate 20 uM

sample_conditions_1: ionic strength: 1 mM; pH: 4.5; pressure: 1 atm; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1

Software:

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

CARA v1.9.1.7, Keller and Wuthrich - chemical shift assignment, peak picking

TopSpin v4.0.7, Bruker Biospin - processing

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