BMRB Entry 11108

Title:
The solution structure of the thioredoxin domain of human Thioredoxin-like protein 2
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 thioredoxin domain of human Thioredoxin-like protein 2"  .

Assembly members:

Assembly members:
Thioredoxin domain, residues 8-124, polymer, 130 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: cell free synthesis   Host organism: E. coli - cell free   Vector: P050302-06

Experimental source:

Natural source:   Common Name: human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: cell free synthesis   Host organism: E. coli - cell free   Vector: P050302-06

Data sets:
Data typeCount
13C chemical shifts554
15N chemical shifts128
1H chemical shifts867

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Thioredoxin domain, residues 8-1241

Entities:

Entity 1, Thioredoxin domain, residues 8-124 130 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYMETALAALA
2   GLYALAALAGLUALAALAVALALAALAVAL
3   GLUGLUVALGLYSERALAGLYGLNPHEGLU
4   GLULEULEUARGLEULYSALALYSSERLEU
5   LEUVALVALHISPHETRPALAPROTRPALA
6   PROGLNCYSALAGLNMETASNGLUVALMET
7   ALAGLULEUALALYSGLULEUPROGLNVAL
8   SERPHEVALLYSLEUGLUALAGLUGLYVAL
9   PROGLUVALSERGLULYSTYRGLUILESER
10   SERVALPROTHRPHELEUPHEPHELYSASN
11   SERGLNLYSILEASPARGLEUASPGLYALA
12   HISALAPROGLULEUTHRLYSLYSVALGLN
13   ARGHISALASERSERGLYPROSERSERGLY

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 900 MHz

Related Database Links:

PDB
DBJ BAG51059 BAG51067 BAG73204
EMBL CAA09375
GB AAF28841 AAF28844 AAH05289 AAH14372 AIC50652
REF NP_001186797 NP_006532 XP_001090479 XP_002821331 XP_003275520
SP O76003
AlphaFold O76003

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