BMRB Entry 26612

Title:
Transmembrane domain of E. coli OmpA in 8 m Urea
Deposition date:
2015-07-15
Original release date:
2020-08-30
Authors:
Burmann, Bjoern; Hiller, Sebastian
Citation:

Citation: Mas, G.; Burmann, Sebastian; Sharpe, T.; Claudi, B.; Burmann, D.; Hiller, Sebastian. "Regulation of chaperone function by coupled folding and oligomerization"  Sci. Adv. ., .-..

Assembly members:

Assembly members:
tOmpA, polymer, 177 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: pET28b

Data sets:
Data typeCount
13C chemical shifts487
15N chemical shifts168
1H chemical shifts168

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1tOmpA1

Entities:

Entity 1, tOmpA 177 residues - Formula weight is not available

this is the transmembrane domain of E. coli OmpA (1-177)

1   METALAPROLYSASPASNTHRTRPTYRTHR
2   GLYALALYSLEUGLYTRPSERGLNTYRHIS
3   ASPTHRGLYPHEILEASNASNASNGLYPRO
4   THRHISGLUASNGLNLEUGLYALAGLYALA
5   PHEGLYGLYTYRGLNVALASNPROTYRVAL
6   GLYPHEGLUMETGLYTYRASPTRPLEUGLY
7   ARGMETPROTYRLYSGLYSERVALGLUASN
8   GLYALATYRLYSALAGLNGLYVALGLNLEU
9   THRALALYSLEUGLYTYRPROILETHRASP
10   ASPLEUASPILETYRTHRARGLEUGLYGLY
11   METVALTRPARGALAASPTHRLYSSERASN
12   VALTYRGLYLYSASNHISASPTHRGLYVAL
13   SERPROVALPHEALAGLYGLYVALGLUTYR
14   ALAILETHRPROGLUILEALATHRARGLEU
15   GLUTYRGLNTRPTHRASNASNILEGLYASP
16   ALAHISTHRILEGLYTHRARGPROASPASN
17   GLYMETLEUSERLEUGLYVALSERTYRARG
18   PHEGLYGLNGLYGLUALAALA

Samples:

sample_1: tOmpA, [U-13C; U-15N; U-2H], 1 mM; D2O 10%; DSS 50 uM; MES 25 mM; NaCl 150 mM; urea 8 M; H2O 90%

sample_conditions_1: ionic strength: 150 mM; pH: 6.5; pressure: 1 atm; temperature: 288.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
5D APSY HNCOCACBsample_1isotropicsample_conditions_1
4D APSY HNCACBsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.0, Bruker Biospin, Guntert, Herrmann and Wuthrich, Keller and Wuthrich - chemical shift assignment, collection, processing

NMR spectrometers:

  • Bruker Ascend 700 MHz

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