BMRB Entry 19243

Title:
Backbone chemical shifts of isolated Domain 1 from E. coli HisJ
Deposition date:
2013-05-15
Original release date:
2013-09-30
Authors:
Chu, Byron; Vogel, Hans
Citation:

Citation: Chu, Byron; Dewolf, Timothy; Vogel, Hans. "Role of the Two Structural Domains from the Periplasmic Escherichia coli Histidine-binding Protein HisJ."  J. Biol. Chem. 288, 31409-31422 (2013).
PubMed: 24036119

Assembly members:

Assembly members:
D1, polymer, 148 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-15

Data sets:
Data typeCount
13C chemical shifts425
15N chemical shifts139
1H chemical shifts139

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Domain 1 from E. coli HisJ1

Entities:

Entity 1, Domain 1 from E. coli HisJ 148 residues - Formula weight is not available

1   GLYGLYMETALAILEPROGLNASNILEARG
2   ILEGLYTHRASPPROTHRTYRALAPROPHE
3   GLUSERLYSASNSERGLNGLYGLULEUVAL
4   GLYPHEASPILEASPLEUALALYSGLULEU
5   CYSLYSARGILEASNTHRGLNCYSTHRPHE
6   VALGLUASNPROLEUASPALALEUILEPRO
7   SERLEULYSALALYSLYSILEASPALAILE
8   METSERSERLEUSERILETHRGLULYSARG
9   GLNGLNGLUILEALAPHETHRASPLYSLEU
10   TYRALAALAGLYGLYGLYGLYSERGLYLEU
11   PHEGLYVALGLYTHRGLYMETGLYLEUARG
12   LYSGLUASPASNGLULEUARGGLUALALEU
13   ASNLYSALAPHEALAGLUMETARGALAASP
14   GLYTHRTYRGLULYSLEUALALYSLYSTYR
15   PHEASPPHEASPVALTYRGLYGLY

Samples:

sample_1: D1, [U-13C; U-15N; U-2H], 1 mM; sodium phosphate 50 mM; D2O 10%; H2O 90%; DSS 0.5 mM

sample_conditions_1: ionic strength: 0 M; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - peak picking

NMR spectrometers:

  • Bruker Avance 700 MHz

Related Database Links:

EMBL CAJ55342 CAJ55343 CAJ55344
GB AEW46917 AEW46918 AEW46919 AHA92022 AHS49988

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