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 20018

Title: NMR structure of Temporin-SHc in micellar SDS   PubMed: 18795798

Deposition date: 2008-04-09 Original release date: 2009-01-16

Authors: Abbassi, Feten; Galanth, Cecile; Lequin, Olivier; Saito, Kazuko; Piesse, Christophe; Zargarian, Loussin; Hani, Khaled; Nicolas, Pierre; Amiche, Mohamed; Ladram, Ali

Citation: Abbassi, Feten; Galanth, Cecile; Amiche, Mohamed; Saito, Kazuko; Piesse, Christophe; Zargarian, Loussine; Hani, Khaled; Nicolas, Pierre; Lequin, Olivier; Ladram, Ali. "Solution structure and model membrane interactions of temporins-SH, antimicrobial peptides from amphibian skin. A NMR spectroscopy and differential scanning calorimetry study"  Biochemistry 47, 10513-10525 (2008).

Assembly members:
Temporin-SHc, polymer, 14 residues, 1466.719 Da.

Natural source:   Common Name: Rana saharica   Taxonomy ID: 70019   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Rana saharica

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):
Temporin-SHc: FLSHIAGFLSNLFX

Data sets:
Data typeCount
13C chemical shifts52
1H chemical shifts100

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1Temporin-SHc1

Entities:

Entity 1, Temporin-SHc 14 residues - 1466.719 Da.

1   PHELEUSERHISILEALAGLYPHELEUSER
2   ASNLEUPHENH2

Samples:

sample_1: entity 1.5 mM; SDS, [U-99% 2H], 80 mM; DSS 0.1 mM

sample_conditions_1: pH: 5; temperature: 309.5 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

Software:

XEASY, Bartels et al. - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 500 MHz

Related Database Links:

EMBL AM748901