BMRB Entry 27049

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27049

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Title:
Trypanosoma brucei brucei Tryparedoxin reduced
Deposition date:
2017-03-18
Original release date:
2018-03-14
Authors:
Wagner, Annika; Diehl, Erika; Krauth-Siegel, R. Luise; Hellmich, Ute
Citation:

Citation: Wagner, Annika; Diehl, Erika; Krauth-Siegel, R. Luise; Hellmich, Ute. "Backbone NMR assignments of tryparedoxin, the central protein in the hydroperoxide detoxification cascade of African trypanosomes, in the oxidized and reduced form"  Biomol NMR Assign 11, 193-196 (2017).
PubMed: 28573456

Assembly members:

Assembly members:
Tryparedoxin, polymer, 147 residues, 16076.2 Da.

Natural source:

Natural source:   Common Name: Trypanosoma brucei   Taxonomy ID: 56917   Superkingdom: Eukaryota   Kingdom: not available   Genus/species: Trypanosoma brucei

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pETtrx_1b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Tryparedoxin: GAMGSGLAKYLPGATNLLSK SGEVSLGSLVGKTVFLYFSA SWCPPCRGFTPVLAEFYEKH HVAKNFEVVLISWDENESDF HDYYGKMPWLALPFDQRSTV SELGKTFGVESIPTLITINA DTGAIIGTQARTRVIEDPDG ANFPWPN

Data sets:
Data typeCount
13C chemical shifts413
15N chemical shifts132
1H chemical shifts132

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Tpx monomer reduced1

Entities:

Entity 1, Tpx monomer reduced 147 residues - 16076.2 Da.

1   GLYALAMETGLYSERGLYLEUALALYSTYR
2   LEUPROGLYALATHRASNLEULEUSERLYS
3   SERGLYGLUVALSERLEUGLYSERLEUVAL
4   GLYLYSTHRVALPHELEUTYRPHESERALA
5   SERTRPCYSPROPROCYSARGGLYPHETHR
6   PROVALLEUALAGLUPHETYRGLULYSHIS
7   HISVALALALYSASNPHEGLUVALVALLEU
8   ILESERTRPASPGLUASNGLUSERASPPHE
9   HISASPTYRTYRGLYLYSMETPROTRPLEU
10   ALALEUPROPHEASPGLNARGSERTHRVAL
11   SERGLULEUGLYLYSTHRPHEGLYVALGLU
12   SERILEPROTHRLEUILETHRILEASNALA
13   ASPTHRGLYALAILEILEGLYTHRGLNALA
14   ARGTHRARGVALILEGLUASPPROASPGLY
15   ALAASNPHEPROTRPPROASN

Samples:

U-15N-Tpx: Tryparedoxin, [U-15N], 475 uM; sodium chloride 125 mM; potassium phosphate 25 mM; TCEP 2 mM

U-13C-15N-Tpx: Tryparedoxin, [U-13C; U-15N], 255 uM; sodium chloride 125 mM; potassium phosphate 25 mM; TCEP 2 mM

15N-Arg-Tpx: Tryparedoxin, [U-15N]-Arg, 300 uM; sodium chloride 125 mM; potassium phosphate 25 mM; TCEP 2 mM

15N-Trp-Tpx: Tryparedoxin, [U-15N]-Trp, 338 uM; sodium chloride 125 mM; potassium phosphate 25 mM; TCEP 2 mM

15N-Lys-Tpx: Tryparedoxin, [U-15N]-Lys, 153 uM; sodium chloride 125 mM; potassium phosphate 25 mM; TCEP 2 mM

13C-15N-Pro-Tpx: Tryparedoxin, [U-13C; U-15N]-Pro, 338 uM; sodium chloride 125 mM; potassium phosphate 25 mM; TCEP 2 mM

15N-Cys-Tpx: Tryparedoxin, [U-15N]-Cys, 214 uM; sodium chloride 125 mM; potassium phosphate 25 mM; TCEP 2 mM

sample_conditions_1: ionic strength: 125 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCU-15N-Tpxisotropicsample_conditions_1
3D HNCOU-13C-15N-Tpxisotropicsample_conditions_1
3D HNCAU-13C-15N-Tpxisotropicsample_conditions_1
3D HNCACBU-13C-15N-Tpxisotropicsample_conditions_1
3D HNCO13C-15N-Pro-Tpxisotropicsample_conditions_1
2D 1H-15N HSQC15N-Arg-Tpxisotropicsample_conditions_1
2D 1H-15N HSQC15N-Trp-Tpxisotropicsample_conditions_1
2D 1H-15N HSQC15N-Lys-Tpxisotropicsample_conditions_1
2D 1H-15N HSQC15N-Cys-Tpxisotropicsample_conditions_1
3D HN(CO)CAU-13C-15N-Tpxisotropicsample_conditions_1

Software:

TOPSPIN vTopSpin 3.5pl5, Bruker Biospin - collection, processing

XEASY, Keller and Wuthrich - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

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