BMRB Entry 30522

Name: Solution NMR structure of spider toxin analogue [F5A,M6F,T26L,K28R]GpTx-1
Published: 2018-12-13

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PDB ID: 6mk5
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR30522
MolProbity Validation Chart

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Nicholas Rego and David Koes
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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 [F5A,M6F,T26L,K28R]GpTx-1

Deposition date:

2018-09-25

Original release date:

2018-12-13

Authors:

Schroeder, C.

Citation:

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).
PubMed: 30507158

Assembly members:

Assembly members:
entity_1, polymer, 34 residues, 4068.863 Da.

Natural source:

Natural source: Common Name: Tarantula spider Taxonomy ID: 1749325 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Grammostola porteri

Experimental source:

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: DCLGAFRKCIPDNDKCCRPN LVCSRLHRWCKYVF

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	96
15N chemical shifts	36
1H chemical shifts	231

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 34 residues - 4068.863 Da.

1

ASP

CYS

LEU

GLY

ALA

PHE

ARG

LYS

CYS

ILE

2

PRO

ASP

ASN

ASP

LYS

CYS

ARG

PRO

ASN

3

LEU

VAL

CYS

SER

ARG

LEU

HIS

ARG

TRP

CYS

4

LYS

TYR

VAL

PHE

Samples:

sample_1: [AFLR]GpTx-1 2 mg/mL

sample_2: [AFLR]GpTx-1 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 1H-1H TOCSY	sample_1	anisotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	anisotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	anisotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	anisotropic	sample_conditions_2
E. COSY	sample_2	anisotropic	sample_conditions_2

Software:

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

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

TOPSPIN, Bruker Biospin - peak picking

NMR spectrometers:

Bruker AvanceIII 600 MHz

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