BMRB Entry 11114

Title:
The solution structure of the second thioredoxin-like domain of human Protein disulfide-isomerase
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-like domain of human Protein disulfide-isomerase"  .

Assembly members:

Assembly members:
Thioredoxin like domain, polymer, 121 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: P040628-09

Data sets:
Data typeCount
13C chemical shifts519
15N chemical shifts109
1H chemical shifts784

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Thioredoxin like domain1

Entities:

Entity 1, Thioredoxin like domain 121 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYPROVALLYS
2   VALLEUVALGLYLYSASNPHEGLUASPVAL
3   ALAPHEASPGLULYSLYSASNVALPHEVAL
4   GLUPHETYRALAPROTRPCYSGLYHISCYS
5   LYSGLNLEUALAPROILETRPASPLYSLEU
6   GLYGLUTHRTYRLYSASPHISGLUASNILE
7   VALILEALALYSMETASPSERTHRALAASN
8   GLUVALGLUALAVALLYSVALHISSERPHE
9   PROTHRLEULYSPHEPHEPROALASERALA
10   ASPARGTHRVALILEASPTYRASNGLYGLU
11   ARGTHRLEUASPGLYPHELYSLYSPHELEU
12   GLUSERGLYGLYGLNSERGLYPROSERSER
13   GLY

Samples:

sample_1: Thioredoxin like domain, [U-13C; U-15N], 1.2 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%

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 v0.9044, Kobayashi, N. - data analysis

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

NMR spectrometers:

  • Bruker AVANCE 900 MHz

Related Database Links:

BMRB 4302
PDB
DBJ BAG53171 BAG54732
EMBL CAA30112
GB AAH14504 AIC63098 EAW89691 EAW89694 EAW89696
REF XP_008011468

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