BMRB Entry 15234

Title:
1H, 15N backbone chemical shift assignment of D122Y mutant of the C terminal domain of human frataxin   PubMed: 18537827
Deposition date:
2007-05-04
Original release date:
2008-05-18
Authors:
Pastore, Chiara; Pastore, Annalisa; Correia, Ana; Gomes, Claudio
Citation:

Citation: Correia, Ana; Pastore, Chiara; Adinolfi, Salvatore; Pastore, Annalisa; Gomes, Claudio. "Dynamics, stability and iron-binding activity of frataxin clinical mutants."  FEBS J. 275, 3680-3690 (2008).

Assembly members:

Assembly members:
hfraD122Y, polymer, 123 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

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

Experimental source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

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

Data sets:
Data typeCount
15N chemical shifts106
1H chemical shifts106

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1hfraD122Y1

Entities:

Entity 1, hfraD122Y 123 residues - Formula weight is not available

1   GLYALAMETASPGLUTHRTHRTYRGLUARG
2   LEUALAGLUGLUTHRLEUASPSERLEUALA
3   GLUPHEPHEGLUASPLEUALAASPLYSPRO
4   TYRTHRPHEGLUTYRTYRASPVALSERPHE
5   GLYSERGLYVALLEUTHRVALLYSLEUGLY
6   GLYASPLEUGLYTHRTYRVALILEASNLYS
7   GLNTHRPROASNLYSGLNILETRPLEUSER
8   SERPROSERSERGLYPROLYSARGTYRASP
9   TRPTHRGLYLYSASNTRPVALTYRSERHIS
10   ASPGLYVALSERLEUHISGLULEULEUALA
11   ALAGLULEUTHRLYSALALEULYSTHRLYS
12   LEUASPLEUSERSERLEUALATYRSERGLY
13   LYSASPALA

Samples:

sample_1: hfraD122Y, [U-98% 15N], 0.5 mM; NaP 20 mM; NaCl 50 mM; DTT 2 mM

sample_conditions_1: pH: 7.0; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

XEASY, Bartels et al. - chemical shift assignment

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

BMRB 15233 15235 15736 15906 16581 4342
PDB
GB AAH23633 AAH48097 ADQ32463 AIC54401 AIC62492
REF NP_000135 XP_001137864 XP_003824802 XP_004048150 XP_010344443
SP Q16595
AlphaFold Q16595

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks