BMRB Entry 11104

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

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

Assembly members:

Assembly members:
2nd thioredoxin domain, polymer, 120 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source:   Production method: cell free synthesis   Host organism: E. coli - cell free   Vector: P050425-14

Data sets:
Data typeCount
13C chemical shifts518
15N chemical shifts112
1H chemical shifts791

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
12nd thioredoxin domain1

Entities:

Entity 1, 2nd thioredoxin domain 120 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYVALTHRLEU
2   SERLEUTHRLYSASPASNPHEASPASPVAL
3   VALASNASNALAASPILEILELEUVALGLU
4   PHETYRALAPROTRPCYSGLYHISCYSLYS
5   LYSLEUALAPROGLUTYRGLULYSALAALA
6   LYSGLULEUSERLYSARGSERPROPROILE
7   PROLEUALALYSVALASPALATHRGLUGLN
8   THRASPLEUALALYSARGPHEASPVALSER
9   GLYTYRPROTHRLEULYSILEPHEARGLYS
10   GLYARGPROPHEASPTYRASNGLYPROARG
11   GLULYSTYRGLYILEVALASPTYRMETILE
12   GLUGLNSERGLYSERGLYPROSERSERGLY

Samples:

sample_1: Thioredoxin domain, [U-13C; U-15N], 1.2 mM; d-Tris HCl 20 mM; sodium chloride 100 mM; d-DTT 1 mM; sodium azide 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 900 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