BMRB Entry 25421

Name: NMR structure of spider toxin- G7W/N24S mutant of TRTX-Hhn2b
Published: 2015-12-21

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PDB ID: 2mxo
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25421
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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 spider toxin- G7W/N24S mutant of TRTX-Hhn2b

Deposition date:

2015-01-08

Original release date:

2015-12-21

Authors:

Klint, Julie; Chin, Yanni; Mobli, Medhi

Citation:

Citation: Klint, Julie; Chin, Yanni; Mobli, Medhi. "Rational Engineering Defines a Molecular Switch That Is Essential for Activity of Spider-Venom Peptides against the Analgesics Target NaV1.7" Mol. Pharmacol. 88, 1002-1010 (2015).
PubMed: 26429937

Assembly members:

Assembly members:
GWHhn2b, polymer, 34 residues, 3793.473 Da.

Natural source:

Natural source: Common Name: Chinese bird spider Taxonomy ID: 209901 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Haplopelma hainanum

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pR7

Entity Sequences (FASTA):

Entity Sequences (FASTA):
GWHhn2b: AECKGFWKSCVPGKNECCSG YACSSRDKWCKVLL

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
spectral_peak_list

Data type	Count
13C chemical shifts	145
15N chemical shifts	35
1H chemical shifts	222

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	G7W/N24S Hhn2b	1

Entities:

Entity 1, G7W/N24S Hhn2b 34 residues - 3793.473 Da.

1

ALA

GLU

CYS

LYS

GLY

PHE

TRP

LYS

SER

CYS

2

VAL

PRO

GLY

LYS

ASN

GLU

CYS

SER

GLY

3

TYR

ALA

CYS

SER

ARG

ASP

LYS

TRP

CYS

4

LYS

VAL

LEU

Samples:

sample_1: GWHhn2b, [U-99% 13C; U-99% 15N], 300 uM; Sodium acetate 20 mM; D2O 5%; H2O 95%

sample_conditions_1: ionic strength: 20 mM; pH: 5; 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 HBHA(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 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

CcpNmr_Analysis v2.4, CCPN - chemical shift assignment

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution

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