BMRB Entry 25271

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25271

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Title:
NMR assignments of the prolyl peptidyl isomerase domain of the ribosome-associated molecular chaperone trigger factor from Escherichia coli
Deposition date:
2014-10-07
Original release date:
2019-07-11
Authors:
Huang, Chih-Ting; Hsu, Shang-Te Danny
Citation:

Citation: Huang, Chih-Ting; Hsu, Shang-Te Danny. "NMR assignments of the peptidyl-prolyl cis-trans isomerase domain of trigger factor from E. coli."  Biomol. NMR Assign. 10, 149-152 (2016).
PubMed: 26527152

Assembly members:

Assembly members:
trigger_factor, polymer, 99 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: pET14b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
trigger_factor: QATWKEKDGAVEAEDRVTID FTGSVDGEEFEGGKASDFVL AMGQGRMIPGFEDGIKGHKA GEEFTIDVTFPEEYHAENLK GKAAKFAINLKKVEERELP

Data sets:
Data typeCount
13C chemical shifts353
15N chemical shifts96
1H chemical shifts548

Additional metadata:

  • Assembly
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Assembly:

Entity Assembly IDEntity NameEntity ID
1PPIase1

Entities:

Entity 1, PPIase 99 residues - Formula weight is not available

1   GLNALATHRTRPLYSGLULYSASPGLYALA
2   VALGLUALAGLUASPARGVALTHRILEASP
3   PHETHRGLYSERVALASPGLYGLUGLUPHE
4   GLUGLYGLYLYSALASERASPPHEVALLEU
5   ALAMETGLYGLNGLYARGMETILEPROGLY
6   PHEGLUASPGLYILELYSGLYHISLYSALA
7   GLYGLUGLUPHETHRILEASPVALTHRPHE
8   PROGLUGLUTYRHISALAGLUASNLEULYS
9   GLYLYSALAALALYSPHEALAILEASNLEU
10   LYSLYSVALGLUGLUARGGLULEUPRO

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