BMRB Entry 30217

Title:
Ocellatin-LB1, solution structure in SDS micelle by NMR spectroscopy
Deposition date:
2016-12-19
Original release date:
2017-03-24
Authors:
Gusmao, K.; dos Santos, D.; Santos, V.; Pilo-Veloso, D.; de Lima, M.; Resende, J.
Citation:

Citation: Gusmao, Karla; Dos Santos, Daniel; Santos, Virgilio; Cortes, Maria Esperanza; Reis, Pablo; Santos, Vera; Pilo-Veloso, Dorila; Verly, Rodrigo; de Lima, Maria Elena; Resende, Jarbas. "Ocellatin peptides from the skin secretion of the South American frog Leptodactylus labyrinthicus (Leptodactylidae): characterization, antimicrobial activities and membrane interactions"  J. Venom. Anim. Toxins Incl. Trop. Dis. 23, 4-4 (2017).
PubMed: 28115922

Assembly members:

Assembly members:
entity_1, polymer, 23 residues, 2195.648 Da.

Natural source:

Natural source:   Common Name: frogs and toads   Taxonomy ID: 326590   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Leptodactylus labyrinthicus

Experimental source:

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GVVDILKGAAKDIAGHLASK VMX

Data sets:
Data typeCount
13C chemical shifts59
15N chemical shifts18
1H chemical shifts140

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 23 residues - 2195.648 Da.

1   GLYVALVALASPILELEULYSGLYALAALA
2   LYSASPILEALAGLYHISLEUALASERLYS
3   VALMETNH2

Samples:

sample_1: D2O, [U-99.75 2H], 5%; DSS 1 mM; Ocellatin-LB1 2 mM; SDS, d-25, 400 mM

sample_conditions_1: pH: 4; pressure: 1 atm; temperature: 303.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HMQCsample_1isotropicsample_conditions_1

Software:

Molmol, Koradi, Billeter and Wuthrich - data analysis

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis

Procheck, Laskowski, MacArthur, Smith, Jones, Hutchinson, Morris, Moss and Thornton - data analysis

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - geometry optimization, refinement, structure calculation

xwinnmr, Bruker Biospin - collection

NMR spectrometers:

  • Bruker AvanceIII 800 MHz

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