BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 11113

Title: The solution structure of the thioredoxin-like domain of human Thioredoxin-related transmembrane protein

Deposition date: 2010-02-18 Original release date: 2011-02-18

Authors: Tochio, N.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.

Citation: Tochio, N.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "The solution structure of the thioredoxin-like domain of human Thioredoxin-related transmembrane protein"  . ., .-..

Assembly members:
thioredoxin like domain, polymer, 126 residues, Formula weight is not available

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

Entity Sequences (FASTA):
thioredoxin like domain: GSSGSSGNVRVITDENWREL LEGDWMIEFYAPWCPACQNL QPEWESFAEWGEDLEVNIAK VDVTEQPGLSGRFIINALPT IYHCKDGEFRRYQGPRTKKD FINFISDKEWKSIEPVSSWF SGPSSG

Data sets:
Data typeCount
13C chemical shifts564
15N chemical shifts131
1H chemical shifts846

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1thioredoxin like domain1

Entities:

Entity 1, thioredoxin like domain 126 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYASNVALARG
2   VALILETHRASPGLUASNTRPARGGLULEU
3   LEUGLUGLYASPTRPMETILEGLUPHETYR
4   ALAPROTRPCYSPROALACYSGLNASNLEU
5   GLNPROGLUTRPGLUSERPHEALAGLUTRP
6   GLYGLUASPLEUGLUVALASNILEALALYS
7   VALASPVALTHRGLUGLNPROGLYLEUSER
8   GLYARGPHEILEILEASNALALEUPROTHR
9   ILETYRHISCYSLYSASPGLYGLUPHEARG
10   ARGTYRGLNGLYPROARGTHRLYSLYSASP
11   PHEILEASNPHEILESERASPLYSGLUTRP
12   LYSSERILEGLUPROVALSERSERTRPPHE
13   SERGLYPROSERSERGLY

Samples:

sample_1: thioredoxin like domain, [U-13C; U-15N], 1.3 mM; d-Tris HCl, [U-2H], 20 mM; NaCl 100 mM; d-DTT, [U-2H], 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 v0.926, Kobayashi, N. - data analysis

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

NMR spectrometers:

  • Bruker AVANCE 900 MHz

Related Database Links:

PDB

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts