BMRB Logo

Biological Magnetic Resonance Data Bank


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

Search Archive Validation Tools Deposit Data NMR Statistics Spectroscopists' Corner Programmers' Corner Home
Site Map FTP Access Structural Genomics
and other "omics"
Metabolomics Educational Outreach NMR Data Formats Useful NMR Links
Search Menu

BMRB Entry 20016


Entry Atomic Coordinates and Restraints
BMRB number (explain)



Link to Entry: bmr20016.str Data Visualizations

System Studied: PROTEIN
Title: NMR structure of Temporin-SHa in micellar SDS
Entry 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, 40, 10513-10525 (2008).    PubMed: 18795798
System Components: entity, Polymer, 13 residues, 1382.743 Da
Natural Source:
Common Name: Rana saharica    Taxonomy ID: 70019     Superkingdom: Eukaryota     Kingdom: Metazoa     Genus/species: Rana saharica

Experimental Data:

Number of:
TypeValuesSets
Assigned Chemical Shifts1
- 1H Chemical Shifts103
- 13C Chemical Shifts48

Metadata:

Entry Information
Entry Citation
Molecular System
Monomeric Polymer
Polymer Residue
Natural Source
Experimental Source
Sample
Software
NMR Spectrometer
NMR Applied Experiment
Sample Conditions
Chemical Shift Reference
Constraint Statistics

Related
Database Links:
EMBL
AM74899