BMRB Entry 30521

Name: Solution NMR structure of spider toxin analogue [E17K]ProTx-II
Published: 2018-12-13

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PDB ID: 6mk4
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30521
MolProbity Validation Chart

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Solution NMR structure of spider toxin analogue [E17K]ProTx-II PubMed: 30507158

Deposition date: 2018-09-25 Original release date: 2018-12-13

Authors: Schroeder, C.

Citation: Lawrence, N.; Wu, B.; Ligutti, J.; Cheneval, O.; Agwa, A.; Benfield, A.; Biswas, K.; Craik, D.; Miranda, L.; Henriques, S.; Schroeder, C.. "Peptide-Membrane Interactions Affect the Inhibitory Potency and Selectivity of Spider Toxins ProTx-II and GpTx-1" ACS Chem. Biol. 14, 118-130 (2019).

Assembly members:
entity_1, polymer, 30 residues, 3839.754 Da.

Natural source: Common Name: Peruvian green velvet tarantula Taxonomy ID: 213387 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Thrixopelma pruriens

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):
entity_1: YCQKWMWTCDSERKCCKGMV CRLWCKKKLW

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	86
15N chemical shifts	28
1H chemical shifts	219

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 30 residues - 3839.754 Da.

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

Samples:

sample_1: [E17K]ProTx-II 2 mg/mL

sample_conditions_1: ionic strength: 0 mM; pH: 3.5; pressure: 1 Pa; temperature: 298 K

sample_conditions_2: ionic strength: 0 mM; pH: 3.5; pressure: 1 Pa; temperature: 298 K

Experiments:

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

Software:

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

CYANA, Guntert, Mumenthaler and Wuthrich - chemical shift assignment, peak picking, structure calculation

NMR spectrometers:

Bruker AvanceIII 600 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts

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