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 19991

Title: NMR assignement of salt stabilised Yeast Frataxin YFH1.   PubMed: 25988154

Deposition date: 2014-05-28 Original release date: 2015-10-22

Authors: Vilanova, Bartolome; Sanfelice, Domenico; Martorell, Gabriel; Pastore, Annalisa; Temussi, Piero

Citation: Vilanova, Bartolome; Sanfelice, Domenico; Martorell, Gabriel; Temussi, Piero; Pastore, Annalisa. "Trapping a salt-dependent unfolding intermediate of the marginally stable protein Yfh1"  Front. Mol. Biosci. ., .-. (2014).

Assembly members:
Yeast_Frataxin_Yfh1, polymer, 123 residues, 13783.4 Da.

Natural source:   Common Name: E. Coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
Yeast_Frataxin_Yfh1: MESSTDGQVVPQEVLNLPLE KYHEEADDYLDHLLDSLEEL SEAHPDCIPDVELSHGVMTL EIPAFGTYVINKQPPNKQIW LASPLSGPNRFDLLNGEWVS LRNGTKLTDILTEEVEKAIS KSQ

Data sets:
Data typeCount
13C chemical shifts486
15N chemical shifts110
1H chemical shifts752

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1yeast frataxin1

Entities:

Entity 1, yeast frataxin 123 residues - 13783.4 Da.

1   METGLUSERSERTHRASPGLYGLNVALVAL
2   PROGLNGLUVALLEUASNLEUPROLEUGLU
3   LYSTYRHISGLUGLUALAASPASPTYRLEU
4   ASPHISLEULEUASPSERLEUGLUGLULEU
5   SERGLUALAHISPROASPCYSILEPROASP
6   VALGLULEUSERHISGLYVALMETTHRLEU
7   GLUILEPROALAPHEGLYTHRTYRVALILE
8   ASNLYSGLNPROPROASNLYSGLNILETRP
9   LEUALASERPROLEUSERGLYPROASNARG
10   PHEASPLEULEUASNGLYGLUTRPVALSER
11   LEUARGASNGLYTHRLYSLEUTHRASPILE
12   LEUTHRGLUGLUVALGLULYSALAILESER
13   LYSSERGLN

Samples:

sample_1: Yeast Frataxin, Yfh1, [U-98% 13C; U-98% 15N], 1 ± 0.1 mM; HEPES 20 mM; NaCl 100 mM; TCEP 2 mM; Yfh1 1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.1 M; pH: 7; pressure: 1 atm; temperature: 298.2 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

XEASY, Bartels et al. - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 800 MHz

Related Database Links:

BMRB 17068 17641
PDB
DBJ GAA22128
EMBL CAA98688 CAY78388
GB AAS56486 AHY74893 AJP37633 AJU57746 AJU58449
REF NP_010163
SP Q07540
TPG DAA11740

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts