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 17068

Title: Assigment of the 1H, 13C, and 15N resonances of the yeast frataxin (Yfh1) under cold denaturation   PubMed: 20979399

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

Citation: Adrover, Miquel; Esposito, Veronica; Martorell, Gabriel; Pastore, Annalisa; Temussi, Piero Andrea. "Understanding cold denaturation: the case study of yfh1."  J. Am. Chem. Soc. 132, 16240-16246 (2010).

Assembly members:
Yeast_frataxin_(Yfh1), polymer, 123 residues, 13783.4 Da.

Natural source:   Common Name: baker   Taxonomy ID: 4932   Superkingdom: not available   Kingdom: not available   Genus/species: Eukaryota Fungi

Experimental source:   Production method: cell free synthesis   Host organism: Escherichia coli

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

Data sets:
Data typeCount
13C chemical shifts210
15N chemical shifts92
1H chemical shifts592

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1Frataxin1

Entities:

Entity 1, 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-100% 13C; U-100% 15N], 0.4 – 0.5 mM; D2O 90 ± 2 %; H2O 10 ± 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: 272.0 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

Software:

XEASY v1.3.2, Bartels et al., Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - chemical shift assignment, peak picking, processing

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

BMRB 6356 17641 19991
PDB
DBJ GAA22128
EMBL CAA98688 CAY78388
GB AAS56486 AHY74893 AJP37633 AJU57746 AJU58449
REF NP_010163
SP Q07540
TPG DAA11740