BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 30218

Title: Ocellatin-LB2, 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: Gusmao, K.; dos Santos, D.; Santos, V.; Pilo-Veloso, D.; de Lima, M.; Resende, J.. "NMR structures in different membrane environments of three ocellatin peptides isolated from Leptodactylus labyrinthicus"  . ., .-..

Assembly members:
entity_1, polymer, 24 residues, 2309.751 Da.

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

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):
entity_1: GVVDILKGAAKDIAGHLASK VMNX

Data sets:
Data typeCount
13C chemical shifts56
15N chemical shifts6
1H chemical shifts147

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 24 residues - 2309.751 Da.

1   GLYVALVALASPILELEULYSGLYALAALA
2   LYSASPILEALAGLYHISLEUALASERLYS
3   VALMETASNNH2

Samples:

sample_1: D2O, [U-99.75 2H], 5%; DSS 1 mM; Ocellatin-LB2 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
  • 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