BMRB Entry 25917

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PDB ID:
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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NMR-STAR v3 text file.
XML gzip file.
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All files associated with the entry

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:
Data typeCount
13C chemical shifts84
15N chemical shifts33
1H chemical shifts218

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 30 residues - 3839.690 Da.

1   TYRCYSGLNLYSTRPMETTRPTHRCYSASP
2   SERGLUARGLYSCYSCYSGLUGLYMETVAL
3   CYSARGLEUTRPCYSLYSLYSLYSLEUTRP

Samples:

sample_1: entity 2 mg; H2O 90%; D2O 10%

sample_2: entity 2 mg; D2O 100%

sample_conditions_1: pH: 3.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1

Software:

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

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

Molmol, Koradi, Billeter and Wuthrich - data analysis

TOPSPIN, Bruker Biospin - collection, processing

XEASY, Bartels et al. - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker Avance 600 MHz

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