BMRB Entry 30190

Name: Solution NMR structure of gHwTx-IV
Published: 2017-02-16

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PDB ID: 5tlr
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30190
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 NMR structure of gHwTx-IV

Deposition date:

2016-10-11

Original release date:

2017-02-16

Authors:

Agwa, A.; Schroeder, C.

Citation:

Citation: Agwa, A.; Lawrence, N.; Deplazes, E.; Cheneval, O.; Chen, R.; Craik, D.; Schroeder, C.; Henriques, S.. "Spider peptide toxin HwTx-IV engineered to bind to lipid membranes has an increased inhibitory potency at human voltage-gated sodium channel hNaV1.7." Biochim. Biophys. Acta 1859, 835-844 (2017).
PubMed: 28115115

Assembly members:

Assembly members:
entity_1, polymer, 36 residues, 4036.820 Da.

Natural source:

Natural source: Common Name: Chinese bird spider Taxonomy ID: 29017 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Haplopelma schmidti

Experimental source:

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GCLGIWKACNPSNDQCCKSS KLVCSRKTRWCKWQIX

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	89
15N chemical shifts	31
1H chemical shifts	229

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 36 residues - 4036.820 Da.

1

GLY

CYS

LEU

GLY

ILE

TRP

LYS

ALA

CYS

ASN

2

PRO

SER

ASN

ASP

GLN

CYS

LYS

SER

3

LYS

LEU

VAL

CYS

SER

ARG

LYS

THR

ARG

TRP

4

CYS

LYS

TRP

GLN

ILE

NH2

Samples:

sample_1: entity_1 mM; D2O, [U-2H], 10%; H2O 90%

sample_2: entity_1 mM; D2O, [U-2H], 100%

sample_conditions_1: pH: 4.0; pressure: 1 atm; temperature: 298 K

sample_conditions_2: pH: 4.0; pressure: 1 atm; temperature: 298 K

sample_conditions_3: pH: 4.0; pressure: 1 atm; temperature: 283 K

Experiments:

Name	Sample	Sample state	Sample conditions
1D 1H	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
1D 1H	sample_1	isotropic	sample_conditions_3
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_3
1D 1H	sample_2	isotropic	sample_conditions_2
2D 1H-1H NOESY	sample_2	isotropic	sample_conditions_2
2D 1H-1H TOCSY	sample_2	isotropic	sample_conditions_2
2D E.COSY	sample_2	isotropic	sample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

CcpNMR, CCPN - chemical shift assignment

MOLPROBITY, Richardson - data analysis

TALOS-N, Cornilescu, Delaglio and Bax - data analysis

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 500 MHz

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