BMRB Entry 30164

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30164
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
NMR solution structure of the Nav1.7 selective spider venom-derived peptide Pn3a
Deposition date:
2016-08-30
Original release date:
2017-08-31
Authors:
Rosengren, K.; Armstrong, D.; Vetter, I.
Citation:

Citation: Sharma, Gagan; Deuis, Jennifer; Jia, Xinying; Mueller, Alexander; Vetter, Irina; Mobli, Mehdi. "Recombinant production, bioconjugation and membrane binding studies ofPn3a, a selective Na V 1.7 inhibitor"  Biochem. Pharmacol. 181, 114148-114148 (2020).
PubMed: 32663452

Assembly members:

Assembly members:
entity_1, polymer, 35 residues, 4285.990 Da.

Natural source:

Natural source:   Common Name: tarantulas   Taxonomy ID: 6895   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: not available not available

Experimental source:

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: DCRYMFGDCEKDEDCCKHLG CKRKMKYCAWDFTFT

Data sets:
Data typeCount
13C chemical shifts79
15N chemical shifts33
1H chemical shifts204

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 35 residues - 4285.990 Da.

1   ASPCYSARGTYRMETPHEGLYASPCYSGLU
2   LYSASPGLUASPCYSCYSLYSHISLEUGLY
3   CYSLYSARGLYSMETLYSTYRCYSALATRP
4   ASPPHETHRPHETHR

Samples:

sample_1: mu-theraphotoxin-Pn3a 2 ± 0.2 mg/mL

sample_2: mu-theraphotoxin-Pn3a 2 ± 0.2 mg/mL

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

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1
2D 1H-1H TOCSYsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
2D 1H-1H ECOSYsample_2isotropicsample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure calculation

TOPSPIN v2.1, Bruker Biospin - collection

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