BMRB Entry 5468

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR5468

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Title:
Backbone 1H, 13C, 15N and Cb chemical shift assignments for 6-phosphogluconolactonase from Trypanosoma brucei
Deposition date:
2002-07-22
Original release date:
2003-03-18
Authors:
Miclet, Emeric; Duffieux, Francis; Lallemand, Jean-Yves; Stoven, Veronique
Citation:

Citation: Miclet, Emeric; Duffieux, Francis; Lallemand, Jean-Yves; Stoven, Veronique. "Letter to the Editor: Backbone HN, N, Ca, C', and Cb assignment of the 6-phosphogluconolactonase, a 266-residue enzyme of the pentose-phosphate pathway from human parasite Trypanosoma brucei."  J. Biomol. NMR 25, 249-250 (2003).

Assembly members:

Assembly members:
6-phosphogluconolactonase, polymer, 266 residues, 28645 Da.

Natural source:

Natural source:   Common Name: African trypanosome   Taxonomy ID: 5702   Superkingdom: Eukaryota   Kingdom: not available   Genus/species: Trypanosoma brucei

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
6-phosphogluconolactonase: MSFKPTISVHATPQELSAAG CRKIVEIIEASGSQQWPLSI ALAGGSTPKMTYARLHDEHL NLLREKRALRFFMGDERMVP ADSTDSNYNMAREVLLHDIP DDLVFPFDTSAVTPSAEATS ADAMRVAEAYGKQLASLLPL KSVGEAGPKVPVFDVVLLGL GSDGHTASIFPGSQAEKETD GKVVVSVGFPSETMKPKVWR VTLSPATIMQARNVIVLATG AEKKWVVDGILADTAHKAPV ARFLRGCEGNVSFLLDKEIA ENLAKF

Data sets:
Data typeCount
13C chemical shifts748
15N chemical shifts240
1H chemical shifts466

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
16PGL1

Entities:

Entity 1, 6PGL 266 residues - 28645 Da.

1   METSERPHELYSPROTHRILESERVALHIS
2   ALATHRPROGLNGLULEUSERALAALAGLY
3   CYSARGLYSILEVALGLUILEILEGLUALA
4   SERGLYSERGLNGLNTRPPROLEUSERILE
5   ALALEUALAGLYGLYSERTHRPROLYSMET
6   THRTYRALAARGLEUHISASPGLUHISLEU
7   ASNLEULEUARGGLULYSARGALALEUARG
8   PHEPHEMETGLYASPGLUARGMETVALPRO
9   ALAASPSERTHRASPSERASNTYRASNMET
10   ALAARGGLUVALLEULEUHISASPILEPRO
11   ASPASPLEUVALPHEPROPHEASPTHRSER
12   ALAVALTHRPROSERALAGLUALATHRSER
13   ALAASPALAMETARGVALALAGLUALATYR
14   GLYLYSGLNLEUALASERLEULEUPROLEU
15   LYSSERVALGLYGLUALAGLYPROLYSVAL
16   PROVALPHEASPVALVALLEULEUGLYLEU
17   GLYSERASPGLYHISTHRALASERILEPHE
18   PROGLYSERGLNALAGLULYSGLUTHRASP
19   GLYLYSVALVALVALSERVALGLYPHEPRO
20   SERGLUTHRMETLYSPROLYSVALTRPARG
21   VALTHRLEUSERPROALATHRILEMETGLN
22   ALAARGASNVALILEVALLEUALATHRGLY
23   ALAGLULYSLYSTRPVALVALASPGLYILE
24   LEUALAASPTHRALAHISLYSALAPROVAL
25   ALAARGPHELEUARGGLYCYSGLUGLYASN
26   VALSERPHELEULEUASPLYSGLUILEALA
27   GLUASNLEUALALYSPHE

Samples:

sample_1: 6-phosphogluconolactonase, [U-100% 15N; U-100% 13C; U-80% 2H], 1.4 mM; Na phosphate buffer 50 mM; NaCl 200 mM

sample_2: 6-phosphogluconolactonase, [U-100% 15N; U-100% 13C], 1.4 mM; Na phosphate buffer 50 mM; NaCl 200 mM

Experiment-cond_1: ionic strength: 0.25 M; pH: 6.0; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
1N-15N HSQCnot availablenot availableExperiment-cond_1
HNCAnot availablenot availableExperiment-cond_1
HN(CO)CAnot availablenot availableExperiment-cond_1
HNCACBnot availablenot availableExperiment-cond_1
HN(CO)CACBnot availablenot availableExperiment-cond_1
HNCOnot availablenot availableExperiment-cond_1
HN(CA)COnot availablenot availableExperiment-cond_1
HBHA(CO)NHnot availablenot availableExperiment-cond_1
HNHAnot availablenot availableExperiment-cond_1
CBCACOHAnot availablenot availableExperiment-cond_1

Software:

Gifa v4.3 - Fourrier Transform, NMR data processing, apodization, linear prediction, phasing

xeasy v1.3 -

NMR spectrometers:

  • Bruker DRX 800 MHz
  • Bruker DRX 600 MHz
  • Varian INOVA 600 MHz

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