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

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   Host organism: 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

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.

The sequence does not present any tag neither any additional residue. It is in its native state

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: Yfh1, [U-100% 13C; U-100% 15N], 0.4-0.5 ± 0.1 mM; D2O, [U-100% 2H], 10 ± 2 %; H2O 90 ± 2 %; DTT 1 ± 0.2 mM; HEPES 20 ± 1 mM

sample_conditions_1: ionic strength: 0.004 M; pH: 7.0; pressure: 1 atm; temperature: 323.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1

Software:

XEASY v1.3.2, Bartels et al. - chemical shift assignment, peak picking

NMRDraw v5.5, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

  • Bruker AMX 700 MHz

Related Database Links:

BMRB 17068 6356 17068 19991
PDB
DBJ GAA22128
EMBL CAA98688 CAY78388
GB AAS56486 AHY74893 AJP37633 AJU57746 AJU58449
REF NP_010163
SP Q07540
TPG DAA11740