BMRB Entry 30211

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30211
MolProbity Validation Chart

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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:

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: 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_1: GVVDILKGAAKDIAGHLASK VMX

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

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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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 HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks