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 25529

Title: NMR Solution Structure and Model Membrane Interaction Studies of the Peptide Hylin a1 from the Arboreal South American Frog Hypsiboas albopunctatus   PubMed: 26059694

Authors: Alves, Eliane; Oliveira, Aline; Alves, Eliane

Citation: Alves, Eliane; Junior, Edson; Cilli, Eduardo; Castro, Mariana; Fontes, Wagner; Magalhaes, Mariana; Liao, Luciano; Oliveira, Aline. "Micelle Bound Structure and Model Membrane Interaction Studies of the Peptide Hylin a1 from the Arboreal South American Frog Hypsiboas albopunctatus"  Protein Pept. Lett. 22, 719-726 (2015).

Assembly members:
entity, polymer, 18 residues, 1867.386 Da.

Natural source:   Common Name: Spotted tree frog   Taxonomy ID: 279985   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Hypsiboas albopunctatus

Experimental source:   Production method: obtained from a collaborator   Host organism: Hypsiboas albopunctatus

Entity Sequences (FASTA):
entity: IFGAILPLALGALKNLIK

Data sets:
Data typeCount
1H chemical shifts123

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 18 residues - 1867.386 Da.

1   ILEPHEGLYALAILELEUPROLEUALALEU
2   GLYALALEULYSASNLEUILELYS

Samples:

sample_1: Hylin a1 1 mM; SDS-d25, [U-2H], 100 mM; D2O, [U-99% 2H], 10%; H2O 90%; TMSP 1 mg/uL

sample_conditions_1: pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H COSYsample_1isotropicsample_conditions_1

Software:

X-PLOR_NIH v2.28, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

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

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

NMRView, Johnson, One Moon Scientific - chemical shift assignment

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

Molmol, Koradi, Billeter and Wuthrich - data analysis

NMR spectrometers:

  • Bruker Avance 500 MHz

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