BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 25271

Title: NMR assignments of the prolyl peptidyl isomerase domain of the ribosome-associated molecular chaperone trigger factor from Escherichia coli   PubMed: 26527152

Deposition date: 2014-10-07 Original release date: 2019-07-11

Authors: Huang, Chih-Ting; Hsu, Shang-Te Danny

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).

Assembly members:
trigger_factor, polymer, 99 residues, Formula weight is not available

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET14b

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
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

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

Samples:

PPIase: trigger factor, [U-98% 13C; U-98% 15N], 0.5 mM; D2O, [U-100% 2H], 10%; TRIS 20 mM; potassium chloride 100 mM; H2O 90%

sample_conditions_1: ionic strength: 0.1 M; pH: 7.6; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCPPIaseisotropicsample_conditions_1
2D 1H-13C HSQCPPIaseisotropicsample_conditions_1
2D 1H-13C HSQC aromaticPPIaseisotropicsample_conditions_1
3D HNCOPPIaseisotropicsample_conditions_1
3D HNCACBPPIaseisotropicsample_conditions_1
3D CBCA(CO)NHPPIaseisotropicsample_conditions_1
3D C(CO)NHPPIaseisotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment, peak picking

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

PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 850 MHz

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