BMRB

Biological Magnetic Resonance Data Bank


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BMRB Entry 15597

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15597

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Title: glutathione peroxidase-type tryparedoxin peroxidase, oxidized form   PubMed: 19636927

Deposition date: 2007-12-18 Original release date: 2008-06-05

Authors: Melchers, Johannes; Muhle-Goll, Claudia; Krauth-Siegel, Luise

Citation: Melchers, Johannes; Krauth-Siegel, Luise; Muhle-Goll, Claudia. "1H, 13C, and 15N assignment of the oxidized and reduced forms of T. brucei glutathione peroxidase-type tryparedoxin peroxidase"  Biomol. NMR Assignments 2, 65-68 (2008).

Assembly members:
Px, polymer, 167 residues, Formula weight is not available

Natural source:   Common Name: Trypanosoma brucei   Taxonomy ID: 5691   Superkingdom: Eukaryota   Kingdom: not available   Genus/species: Trypanosoma brucei

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

Entity Sequences (FASTA):
Px: GMGSSIFDFEVLDADHKPYN LVQHKGSPLLIYNVASKCGY TKGGYETATTLYNKYKSQGF TVLAFPSNQFGGQEPGNEEE IKEFVCTKFKAEFPIMAKIN VNGENAHPLYEYMKKTKPGI LATKAIKWNFTSFLIDRDGV PVERFSPGASVKDIEEKLIP LLGSARL

Data sets:
Data typeCount
13C chemical shifts537
15N chemical shifts155
1H chemical shifts1032

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Px monomer1

Entities:

Entity 1, Px monomer 167 residues - Formula weight is not available

1   GLYMETGLYSERSERILEPHEASPPHEGLU
2   VALLEUASPALAASPHISLYSPROTYRASN
3   LEUVALGLNHISLYSGLYSERPROLEULEU
4   ILETYRASNVALALASERLYSCYSGLYTYR
5   THRLYSGLYGLYTYRGLUTHRALATHRTHR
6   LEUTYRASNLYSTYRLYSSERGLNGLYPHE
7   THRVALLEUALAPHEPROSERASNGLNPHE
8   GLYGLYGLNGLUPROGLYASNGLUGLUGLU
9   ILELYSGLUPHEVALCYSTHRLYSPHELYS
10   ALAGLUPHEPROILEMETALALYSILEASN
11   VALASNGLYGLUASNALAHISPROLEUTYR
12   GLUTYRMETLYSLYSTHRLYSPROGLYILE
13   LEUALATHRLYSALAILELYSTRPASNPHE
14   THRSERPHELEUILEASPARGASPGLYVAL
15   PROVALGLUARGPHESERPROGLYALASER
16   VALLYSASPILEGLUGLULYSLEUILEPRO
17   LEULEUGLYSERALAARGLEU

Samples:

sample_1: Px, [U-13C; U-15N], 1 mM; NaPO4 50 mM; KCl 100 mM; H2O 90%; D2O 10%

sample_2: Px 1 mM; NaPO4 50 mM; KCl 100 mM; D2O 100%

sample_3: Px, [U-15N], 1 mM; NaPO4 50 mM; KCl 100 mM; H2O 90%; D2O 10%

sample_4: Px, [U-13C; U-15N], 1 mM; NaPO4 50 mM; KCl 100 mM; D2O 100%

sample_conditions_1: ionic strength: 150 mM; pH: 6.8; pressure: 1 atm; temperature: 297 K

sample_conditions_2: ionic strength: 150 mM; pH: 6.8; pressure: 1 atm; temperature: 307 K

Experiments:

NameSampleSample stateSample conditions
3D HNCAsample_1isotropicsample_conditions_2
3D HNCACBsample_1isotropicsample_conditions_2
3D CBCA(CO)NHsample_1isotropicsample_conditions_2
3D H(CCO)NHsample_1isotropicsample_conditions_2
3D 1H-15N NOESYsample_3isotropicsample_conditions_1
3D HCCH-TOCSYsample_4isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_4isotropicsample_conditions_1

Software:

NMRView, Johnson, One Moon Scientific - chemical shift assignment

NMR spectrometers:

  • Bruker DRX 900 MHz
  • Bruker DRX 800 MHz
  • Bruker DRX 500 MHz

Related Database Links:

BMRB 15598
PDB
EMBL CAC83349 CBH12136
GB AAX69963 AAZ12179
REF XP_011774419 XP_845738

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