BMRB Entry 25917

Name: ProTx-II
Published: 2016-07-05

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PDB ID: 2n9t
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25917
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:

ProTx-II

Deposition date:

2015-12-08

Original release date:

2016-07-05

Authors:

Schroeder, Christina

Citation:

Citation: Henriques, Sonia; Deplazes, Evelyn; Lawrence, Nicole; Chenval, Olivier; Inserra, Marco; Thongyoo, Panumart; Marks, Alan; Vetter, Irina; Craik, David; Schroeder, Christina. "Interaction of Tarantula Venom Peptide ProTx-II with Lipid Membranes is a Prerequisite for its Inhibition of Human Voltage-gated Sodium Channel NaV1.7" J. Biol. Chem. 291, 17049-17065 (2016).
PubMed: 27311819

Assembly members:

Assembly members:
entity, polymer, 30 residues, 3839.690 Da.

Natural source:

Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not available not available

Experimental source:

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: YCQKWMWTCDSERKCCEGMV CRLWCKKKLW

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	84
15N chemical shifts	33
1H chemical shifts	218

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 30 residues - 3839.690 Da.

1	TYR	CYS	GLN	LYS	TRP	MET	TRP	THR	CYS	ASP
2	SER	GLU	ARG	LYS	CYS	CYS	GLU	GLY	MET	VAL
3	CYS	ARG	LEU	TRP	CYS	LYS	LYS	LYS	LEU	TRP

Name	Sample	Sample state	Sample conditions
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
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1

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

BMRB Entry 25917

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

1	TYR	CYS	GLN	LYS	TRP	MET	TRP	THR	CYS	ASP
2	SER	GLU	ARG	LYS	CYS	CYS	GLU	GLY	MET	VAL
3	CYS	ARG	LEU	TRP	CYS	LYS	LYS	LYS	LEU	TRP

1	TYR	CYS	GLN	LYS	TRP	MET	TRP	THR	CYS	ASP
2	SER	GLU	ARG	LYS	CYS	CYS	GLU	GLY	MET	VAL
3	CYS	ARG	LEU	TRP	CYS	LYS	LYS	LYS	LEU	TRP

1	TYR	CYS	GLN	LYS	TRP	MET	TRP	THR	CYS	ASP
2	SER	GLU	ARG	LYS	CYS	CYS	GLU	GLY	MET	VAL
3	CYS	ARG	LEU	TRP	CYS	LYS	LYS	LYS	LEU	TRP