BMRB Entry 11100

Title:
The solution structure of the first thioredoxin domain of mouse Protein disulfide-isomerase A6
Deposition date:
2010-02-18
Original release date:
2011-02-17
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 first thioredoxin domain of mouse Protein disulfide-isomerase A6"  .

Assembly members:

Assembly members:
1st thioredoxin domain, polymer, 130 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: P050509-11

Data sets:
Data typeCount
13C chemical shifts536
15N chemical shifts128
1H chemical shifts825

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
11st thioredoxin domain1

Entities:

Entity 1, 1st thioredoxin domain 130 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYALAVALSER
2   GLYLEUTYRSERSERSERASPASPVALILE
3   GLULEUTHRPROSERASNPHEASNARGGLU
4   VALILEGLNSERASPGLYLEUTRPLEUVAL
5   GLUPHETYRALAPROTRPCYSGLYHISCYS
6   GLNARGLEUTHRPROGLUTRPLYSLYSALA
7   ALATHRALALEULYSASPVALVALLYSVAL
8   GLYALAVALASNALAASPLYSHISGLNSER
9   LEUGLYGLYGLNTYRGLYVALGLNGLYPHE
10   PROTHRILELYSILEPHEGLYALAASNLYS
11   ASNLYSPROGLUASPTYRGLNGLYGLYARG
12   THRGLYGLUALAILEVALASPALAALALEU
13   SERALALEUARGSERGLYPROSERSERGLY

Samples:

sample_1: 1st thioredoxin domain, [U-13C; U-15N], 1.3 mM; d-Tris-HCl, [U-2H], 20 mM; sodium chloride 100 mM; d-DTT, [U-2H], 1 mM; sodium azide 0.02%; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 120 M; pH: 7.0; pressure: 1 atm; temperature: 296 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_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