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 25702

Title: Structures of the reduced and oxidized state of the mutant D24A of yeast thioredoxin 1: insight into the mechanism for the closing of the water cavity   PubMed: 26482062

Deposition date: 2015-07-13 Original release date: 2015-10-26

Authors: Iqbal, Anwar; Moraes, Adolfo; Valente, Ana Paula; Almeida, Fabio

Citation: Iqbal, Anwar; Moraes, Adolfo; Valente, Ana Paula; Almeida, Fabio. "Structures of the reduced and oxidized state of the mutant D24A of yeast thioredoxin 1: insights into the mechanism for the closing of the water cavity"  J. Biomol. NMR 63, 417-423 (2015).

Assembly members:
Yeast_Thioredoxin_1_redcuced, polymer, 103 residues, 11201.019 Da.

Natural source:   Common Name: baker's yeast   Taxonomy ID: not available   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Saccharomyces cerevisiae

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

Entity Sequences (FASTA):
Yeast_Thioredoxin_1_redcuced: MVTQFKTASEFDSAIAQDKL VVVAFYATWCGPCKMIAPMI EKFSEQYPQADFYKLDVDEL GDVAQKNEVSAMPTLLLFKN GKEVAKVVGANPAAIKQAIA ANA

Data sets:
Data typeCount
13C chemical shifts380
15N chemical shifts102
1H chemical shifts599

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1reduced form of thioredoxin 1 from Sacharomyces cerevisiae1

Entities:

Entity 1, reduced form of thioredoxin 1 from Sacharomyces cerevisiae 103 residues - 11201.019 Da.

1   METVALTHRGLNPHELYSTHRALASERGLU
2   PHEASPSERALAILEALAGLNASPLYSLEU
3   VALVALVALALAPHETYRALATHRTRPCYS
4   GLYPROCYSLYSMETILEALAPROMETILE
5   GLULYSPHESERGLUGLNTYRPROGLNALA
6   ASPPHETYRLYSLEUASPVALASPGLULEU
7   GLYASPVALALAGLNLYSASNGLUVALSER
8   ALAMETPROTHRLEULEULEUPHELYSASN
9   GLYLYSGLUVALALALYSVALVALGLYALA
10   ASNPROALAALAILELYSGLNALAILEALA
11   ALAASNALA

Samples:

D24A_reduced: yTrx1D24A reduced, [U-100% 13C; U-100% 15N], 850 uM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.02 M; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCD24A_reducedisotropicsample_conditions_1
2D 1H-13C HSQCD24A_reducedisotropicsample_conditions_1
2D 1H-13C HSQC aromaticD24A_reducedisotropicsample_conditions_1
3D CBCA(CO)NHD24A_reducedisotropicsample_conditions_1
3D HNCOD24A_reducedisotropicsample_conditions_1
3D HNCACBD24A_reducedisotropicsample_conditions_1
3D HCCH-TOCSYD24A_reducedisotropicsample_conditions_1
3D HCCH-COSYD24A_reducedisotropicsample_conditions_1
3D HBHA(CO)NHD24A_reducedisotropicsample_conditions_1
3D 1H-15N NOESYD24A_reducedisotropicsample_conditions_1
3D 1H-13C NOESY aliphaticD24A_reducedisotropicsample_conditions_1
3D 1H-13C NOESY aromaticD24A_reducedisotropicsample_conditions_1

Software:

ARIA varia2.3, Brunger, Adams, Clore, Gros, Nilges and Read, Linge, O'Donoghue and Nilges - refinement, structure solution

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 700 MHz

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