BMRB Entry 51288

Title:
Resonance assignment of the enzyme KdgF from Bacteroides eggerthii
Deposition date:
2022-01-23
Original release date:
2022-09-19
Authors:
Petersen, Agnes Beenfeldt; Christensen, Idd Andrea; Aachmann, Finn Lillelund
Citation:

Citation: Petersen, Agnes Beenfeldt; Christensen, Idd Andrea; Ronne, Mette; Stender, Emil; Teze, David; Svensson, Birte; Aachmann, Finn Lillelund. "1H, 13C, 15N resonance assignment of the enzyme KdgF from Bacteroides eggerthii"  Biomol. NMR Assignments 16, 343-347 (2022).
PubMed: 36042150

Assembly members:

Assembly members:
entity_1, polymer, 126 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Bacteroides eggerthii   Taxonomy ID: 28111   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bacteroides eggerthii

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET15b-USER-BeKdgF

Data sets:
Data typeCount
13C chemical shifts423
15N chemical shifts115
1H chemical shifts549

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1KgdF1

Entities:

Entity 1, KgdF 126 residues - Formula weight is not available

Amino acids 1-12 (MGSSHHHHHHGS) is a His-tag only for purification purpose and it is not cleaved from the protein.

1   METGLYSERSERHISHISHISHISHISHIS
2   GLYSERMETLYSTHRCYSSERLYSVALPHE
3   LEULEUGLUASNGLUILESERTRPGLUGLN
4   VALGLYGLUGLYILEGLNARGGLNILELEU
5   GLYTYRASPGLYGLNLEUMETLEUVALLYS
6   VALLYSPHEGLNLYSGLYALAILEGLYASN
7   ALAHISGLUHISPHEHISSERGLNSERTHR
8   TYRVALVALSERGLYVALPHEGLUPHEHIS
9   VALASNGLYGLULYSLYSILEVALLYSALA
10   GLYASPGLYILETYRMETGLUPROASPVAL
11   LEUHISGLYCYSTHRCYSLEUGLUALAGLY
12   ILELEUILEASPTHRPHESERPROMETARG
13   GLUASPPHEILEASNGLU

Samples:

sample_1: KdgF, [U-13C; U-15N], 0.92 mM; sodium phosphate 25 mM; sodium chloride 50 mM; D2O, [U-99% 2H], 10%; H2O 90%

sample_conditions_1: ionic strength: 0.1875 M; pH: 7.2; pressure: 1 atm; temperature: 298.1 K

Experiments:

NameSampleSample stateSample conditions
1D 1Hsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CBCANHsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
TROSY-HNCACBsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.6.1 - processing

CARA v1.8.4.2 - chemical shift assignment

TALOS-N - data analysis

TOPSPIN v4.0.7 - collection

NMR spectrometers:

  • Bruker AVANCE III 800 MHz

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