BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 30211

Title: Ocellatin-LB1

Deposition date: 2016-12-17 Original release date: 2017-12-08

Authors: Gusmao, K.; Santos, D.; de Lima, M.; Pilo-Veloso, D.; Resende, J.

Citation: Gusmao, K.; Santos, D.; Verly, R.; de Lima, M.; Pilo-Veloso, D.; Resende, J.. "NMR structures in different membrane environments of three ocellatin peptides isolated from Leptodactylus labyrinthicus"  . ., .-..

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

Natural source:   Common Name: not available   Taxonomy ID: not available   Superkingdom: not available   Kingdom: not available   Genus/species: not available not available

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):
entity_1: GVVDILKGAAKDIAGHLASK VMX

Data sets:
Data typeCount
13C chemical shifts68
15N chemical shifts20
1H chemical shifts145

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: DSS 1 mM; H2O 40%; Ocellatin-LB1 2.0 mM; TFE, d2, 60%; potassium phosphate 20 mM

sample_conditions_1: pH: 7; pressure: 1 atm; temperature: 293.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H TOCSYsample_1not availablesample_conditions_1
2D 1H-1H NOESYsample_1not availablesample_conditions_1
2D 1H-13C HSQCsample_1not availablesample_conditions_1
2D 1H-15N HSQCsample_1not availablesample_conditions_1

Software:

Molmol, Koradi, Billeter and Wuthrich - data analysis

NMRPipe, Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A. - processing

NMRView, Johnson BA, Blevins RA. - chemical shift assignment

Procheck 3.5.4, Laskowski, MacArthur, Smith, Jones, Hutchinson, Morris, Moss and Thornton - data analysis

X-PLOR_NIH 2.17.0, SCHWIETERS, KUSZEWSKI, TJANDRA AND CLORE - refinement, structure calculation

xwinnmr, Bruker Biospin - collection

NMR spectrometers:

  • 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