BMRB Entry 36181

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR36181
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

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):

Entity Sequences (FASTA):
Maltose-binding periplasmic protein,Trigger factor: GIAEAAFNKGETAMTINGPW AWSNIDTSKVGSGSGSGSGS QATWKEKDGAVEAEDRVTID FTGSVDGEEFEGGKASDFVL AMGQGRMIPGFEDGIKGHKA GEEFTIDVTFPEEYHAENLK GKAAKFAINLKKVEERELPE LT

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

Additional metadata:

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

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

Samples:

sample_1: MBP238-266-PPD fusion, [U-99% 13C; U-99% 15N], 1 mM; KPi 20 mM; KCl 100 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 295 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAHAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
2D HBCBCGCDHDsample_1isotropicsample_conditions_1
2D HBCBCGCDCEHEsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

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

OLIVIA, Masashi Yokochi - chemical shift assignment, data analysis

NMR spectrometers:

  • Varian UNITY 800 MHz
  • Varian UNITY 600 MHz

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