BMRB Entry 11105

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

Assembly members:

Assembly members:
Thioredoxin domain, polymer, 137 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:

Experimental source:   Production method: cell free synthesis   Host organism: E. coli - cell free   Vector: P050314-13

Data sets:
Data typeCount
13C chemical shifts609
15N chemical shifts139
1H chemical shifts926

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Thioredoxin domain1

Entities:

Entity 1, Thioredoxin domain 137 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYTYRILELYS
2   TYRPHEASNASPLYSTHRILEASPGLUGLU
3   LEUGLUARGASPLYSARGVALTHRTRPILE
4   VALGLUPHEPHEALAASNTRPSERASNASP
5   CYSGLNSERPHEALAPROILETYRALAASP
6   LEUSERLEULYSTYRASNCYSTHRGLYLEU
7   ASNPHEGLYLYSVALASPVALGLYARGTYR
8   THRASPVALSERTHRARGTYRLYSVALSER
9   THRSERPROLEUTHRLYSGLNLEUPROTHR
10   LEUILELEUPHEGLNGLYGLYLYSGLUALA
11   METARGARGPROGLNILEASPLYSLYSGLY
12   ARGALAVALSERTRPTHRPHESERGLUGLU
13   ASNVALILEARGGLUPHEASNLEUASNGLU
14   LEUSERGLYPROSERSERGLY

Samples:

sample_1: Thioredoxin domain, [U-13C; U-15N], 0.4 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: 298 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 BAC11569 BAD96778 BAE01711 BAG35827 BAH12650
EMBL CAH89604
GB AAD27740 AAG43122 AAH00666 AAH83678 AAH93062
REF NP_001007644 NP_001127174 NP_001137484 NP_001182688 NP_001272093
SP Q2TBU2 Q4R5B4 Q5RF53 Q5XIK2 Q9Y320
AlphaFold Q5XIK2 Q2TBU2 Q4R5B4 Q5RF53 Q9Y320

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