BMRB Entry 11109

Title:
The solution structure of the third thioredoxin domain of mouse Protein disulfide-isomerase A4
Deposition date:
2010-02-18
Original release date:
2011-02-18
Authors:
Tochio, N.; Sato, M.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.
Citation:

Citation: Tochio, N.; Sato, M.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "The solution structure of the third thioredoxin domain of mouse Protein disulfide-isomerase A4"  .

Assembly members:

Assembly members:
3rd thioredoxin domain, polymer, 133 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: house mouse   Taxonomy ID: 10090   Superkingdom: Eukaryotae   Kingdom: Metazoause   Genus/species: Mus musculusse

Experimental source:

Experimental source:   Production method: cell free synthesis   Host organism: E. coli - cell free   Vector: P050425-15

Data sets:
Data typeCount
13C chemical shifts575
15N chemical shifts122
1H chemical shifts859

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
13rd thioredoxin domain1

Entities:

Entity 1, 3rd thioredoxin domain 133 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYPROVALLYS
2   VALVALVALGLYLYSTHRPHEASPALAILE
3   VALMETASPPROLYSLYSASPVALLEUILE
4   GLUPHETYRALAPROTRPCYSGLYHISCYS
5   LYSGLNLEUGLUPROILETYRTHRSERLEU
6   GLYLYSLYSTYRLYSGLYGLNLYSASPLEU
7   VALILEALALYSMETASPALATHRALAASN
8   ASPILETHRASNASPGLNTYRLYSVALGLU
9   GLYPHEPROTHRILETYRPHEALAPROSER
10   GLYASPLYSLYSASNPROILELYSPHEGLU
11   GLYGLYASNARGASPLEUGLUHISLEUSER
12   LYSPHEILEASPGLUHISALATHRLYSARG
13   SERARGTHRLYSGLUGLULEUSERGLYPRO
14   SERSERGLY

Samples:

sample_1: Thioredoxin domain, [U-13C; U-15N], 1.3 mM; d-Tris HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 296 K

Experiments:

NameSampleSample stateSample conditions
3D 15N-SEPARATED NOESYsample_1isotropiccondition_1
3D 13C-SEPARATED NOESYsample_1isotropiccondition_1

Software:

xwinnmr v3.5, Bruker - collection

NMRPipe v20031121, Delaglio, F. - processing

NMRView v5.0.4, Johnson, B.A. - data analysis

Kujira v0.955, Kobayashi, N. - data analysis

CYANA v2.0.17, Guntert, P. - structure solution

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB

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