BMRB Entry 30598

Name: Solution structure of scorpion Hottentotta jayakari venom toxin Hj1a
Published: 2020-02-07

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PDB ID: 6ohx
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR30598
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 scorpion Hottentotta jayakari venom toxin Hj1a

Deposition date:

2019-04-08

Original release date:

2020-02-07

Authors:

Chin, Y.; Chow, C.; King, G.

Citation:

Citation: Chow, Chun Yuen; Chin, Yanni K-Y; Walker, Andrew; Guo, Shaodong; Blomster, Linda; Ward, Micaiah; Herzig, Volker; Rokyta, Darin; King, Glenn. "Venom Peptides with Dual Modulatory Activity on the Voltage-Gated Sodium Channel Na V 1.1 Provide Novel Leads for Development of Antiepileptic Drugs" ACS Pharmacol. Transl. Sci. 3, 119-134 (2020).
PubMed: 32259093

Assembly members:

Assembly members:
entity_1, polymer, 67 residues, 7559.603 Da.

Natural source:

Natural source: Common Name: scorpions Taxonomy ID: 224597 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Hottentotta jayakari

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GEEVRDAYIAQPHNCVYHCF RDSYCNDLCIKHGAESGECK WFTSSGNACWCVKLPKSEPI KVPGKCH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list

Data type	Count
13C chemical shifts	262
15N chemical shifts	66
1H chemical shifts	419

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 67 residues - 7559.603 Da.

1

GLY

GLU

VAL

ARG

ASP

ALA

TYR

ILE

ALA

2

GLN

PRO

HIS

ASN

CYS

VAL

TYR

HIS

CYS

PHE

3

ARG

ASP

SER

TYR

CYS

ASN

ASP

LEU

CYS

ILE

4

LYS

HIS

GLY

ALA

GLU

SER

GLY

GLU

CYS

LYS

5

TRP

PHE

THR

SER

GLY

ASN

ALA

CYS

TRP

6

CYS

VAL

LYS

LEU

PRO

LYS

SER

GLU

PRO

ILE

7

LYS

VAL

PRO

GLY

LYS

CYS

HIS

Samples:

sample_1: Hj1a, [U-13C; U-15N], 663 uM; MES 20 mM; D2O 5%

sample_conditions_1: ionic strength: 0 mM; pH: 6; pressure: 1 atm; temperature: 298 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
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1

Software:

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

Analysis, CCPN - chemical shift assignment

CcpNMR, CCPN - peak picking

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

Rowland NMR Toolkit, Gregory P. Mullen - processing

NMR spectrometers:

Bruker AvanceIII 900 MHz

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