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 17641

Title: Assigment of the 1H, 13C, and 15N resonances of the yeast frataxin (Yfh1) under heat denaturation (50 C)   PubMed: 22342930

Deposition date: 2011-05-12 Original release date: 2015-09-03

Authors: Adrover, Miquel; Pastore, Annalisa; Temussi, Piero Andrea

Citation: Adrover, Miquel; Martorell, Gabriel; Martin, Stephen; Urosev, Dunja; Konarev, Petr; Svergun, Dmitri; Daura, Xavier; Temussi, Pierandrea; Pastore, Annalisa. "The role of hydration in protein stability: comparison of the cold and heat unfolded states of Yfh1."  J. Mol. Biol. 417, 413-424 (2012).

Assembly members:
Yfh1, polymer, 123 residues, 13783.4 Da.

Natural source:   Common Name: baker's yeast   Taxonomy ID: 4932   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Saccharomyces cerevisiae

Experimental source:   Production method: recombinant technology' 'Escherichia coli

Entity Sequences (FASTA):
Yfh1: MESSTDGQVVPQEVLNLPLE KYHEEADDYLDHLLDSLEEL SEAHPDCIPDVELSHGVMTL EIPAFGTYVINKQPPNKQIW LASPLSGPNRFDLLNGEWVS LRNGTKLTDILTEEVEKAIS KSQ

Data sets:
Data typeCount
13C chemical shifts236
15N chemical shifts104
1H chemical shifts535

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