BMRB Entry 36181

Title:
Solution structure of peptidyl-prolyl cis/trans isomerase domain of Trigger Factor in complex with MBP
Deposition date:
2018-04-21
Original release date:
2018-09-04
Authors:
Kawagoe, S.; Nakagawa, H.; Kumeta, H.; Ishimori, K.; Saio, T.
Citation:

Citation: Kawagoe, Soichiro; Nakagawa, Hiroshi; Kumeta, Hiroyuki; Ishimori, Koichiro; Saio, Tomohide. "Structural insight into proline cis/trans isomerization of unfolded proteins catalyzed by the Trigger Factor chaperone"  J. Biol. Chem. 293, 15095-15106 (2018).
PubMed: 30093407

Assembly members:

Assembly members:
Maltose-binding periplasmic protein,Trigger factor, polymer, 142 residues, 15134.620 Da.

Natural source:

Natural source:   Common Name: Escherichia coli K-12   Taxonomy ID: 83333   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

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

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts391
15N chemical shifts119
1H chemical shifts765

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 142 residues - 15134.620 Da.

1   GLYILEALAGLUALAALAPHEASNLYSGLY
2   GLUTHRALAMETTHRILEASNGLYPROTRP
3   ALATRPSERASNILEASPTHRSERLYSVAL
4   GLYSERGLYSERGLYSERGLYSERGLYSER
5   GLNALATHRTRPLYSGLULYSASPGLYALA
6   VALGLUALAGLUASPARGVALTHRILEASP
7   PHETHRGLYSERVALASPGLYGLUGLUPHE
8   GLUGLYGLYLYSALASERASPPHEVALLEU
9   ALAMETGLYGLNGLYARGMETILEPROGLY
10   PHEGLUASPGLYILELYSGLYHISLYSALA
11   GLYGLUGLUPHETHRILEASPVALTHRPHE
12   PROGLUGLUTYRHISALAGLUASNLEULYS
13   GLYLYSALAALALYSPHEALAILEASNLEU
14   LYSLYSVALGLUGLUARGGLULEUPROGLU
15   LEUTHR

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