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 16850

Title: Thioredoxin   PubMed: 22505815

Deposition date: 2010-04-08 Original release date: 2016-09-12

Authors: Dikiy, Alexander; Yakimov, Aleksandr; Elena, Dobrovolskaya

Citation: Dobrovolska, Olena; Rychkov, Georgy; Shumilina, Elena; Nerinovski, Kirill; Schmidt, Alexander; Shabalin, Konstantin; Yakimov, Alexander; Dikiy, Alexander. "Structural insights into interaction between mammalian methionine sulfoxide reductase B1 and thioredoxin"  J. Biomed. Biotechnol. 2012, 586539-586539 (2012).

Assembly members:
thioredoxin, polymer, 113 residues, 12787.5293 Da.

Natural source:   Common Name: Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET21

Entity Sequences (FASTA):
thioredoxin: MVKQIESKTAFQEALDAAGD KLVVVDFSATWCGPSKMIKP FFHSLSEKYSNVIFLEVDVD DCQDVASECEVKCMPTFQFF KKGQKVGEFSGANKEKLEAT INELVLEHHHHHH

Data typeCount
13C chemical shifts386
15N chemical shifts198
1H chemical shifts568

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1thioredoxin, 11
2thioredoxin, 21

Entities:

Entity 1, thioredoxin, 1 113 residues - 12787.5293 Da.

1   METVALLYSGLNILEGLUSERLYSTHRALA
2   PHEGLNGLUALALEUASPALAALAGLYASP
3   LYSLEUVALVALVALASPPHESERALATHR
4   TRPCYSGLYPROSERLYSMETILELYSPRO
5   PHEPHEHISSERLEUSERGLULYSTYRSER
6   ASNVALILEPHELEUGLUVALASPVALASP
7   ASPCYSGLNASPVALALASERGLUCYSGLU
8   VALLYSCYSMETPROTHRPHEGLNPHEPHE
9   LYSLYSGLYGLNLYSVALGLYGLUPHESER
10   GLYALAASNLYSGLULYSLEUGLUALATHR
11   ILEASNGLULEUVALLEUGLUHISHISHIS
12   HISHISHIS

Samples:

one: thioredoxin, [U-98% 13C; U-98% 15N], 1.5 ± 0.0001 mM; H2O 95%; D2O 5%

standart: ionic strength: 0.025 M; pH: 5.1; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC/HMQConeisotropicstandart
CBCANH (h{CA|Cca}NH)oneisotropicstandart
3D CBCA(CO)NHoneisotropicstandart
3D HNCAoneisotropicstandart
3D HBHA(CO)NHoneisotropicstandart
HBHANH (H{ca|cca}NH)oneisotropicstandart
2D 1H-13C HSQC/HMQConeisotropicstandart
3D 1H-15N NOESYoneisotropicstandart

Software:

CcpNmr_Analysis v2.1, CCPN - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker Avance 600 MHz

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