BMRB Entry 34376

Title:
The N-terminal domain of rhomboid protease YqgP
Deposition date:
2019-03-13
Original release date:
2020-01-06
Authors:
Began, J.; Strisovsky, K.; Veverka, V.
Citation:

Citation: Began, Jakub; Cordier, Baptiste; Brezinova, Jana; Delisle, Jordan; Hexnerova, Rozalie; Srb, Pavel; Rampirova, Petra; Kozisek, Milan; Baudet, Mathieu; Coute, Yohann; Galinier, Anne; Veverka, Vaclav; Doan, Thierry; Strisovsky, Kvido. "Rhomboid intramembrane protease YqgP licenses bacterial membrane protein quality control as adaptor of FtsH AAA protease"  Embo J. 39, e102935-e102935 (2020).
PubMed: 31930742

Assembly members:

Assembly members:
entity_1, polymer, 185 residues, 21836.576 Da.

Natural source:

Natural source:   Common Name: Bacillus subtilis   Taxonomy ID: 1423   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bacillus subtilis

Experimental source:

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

Data sets:
Data typeCount
13C chemical shifts773
15N chemical shifts192
1H chemical shifts1279

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 185 residues - 21836.576 Da.

1   METPHELEULEUGLUTYRTHRTYRTRPLYS
2   ILEALAALAHISLEUVALASNSERGLYTYR
3   GLYVALILEGLNALAGLYGLUSERASPGLU
4   ILETRPLEUGLUALAPROASPLYSSERSER
5   HISASPLEUVALARGLEUTYRLYSHISASP
6   LEUASPPHEARGGLNGLUMETVALARGASP
7   ILEGLUGLUGLNALAGLUARGVALGLUARG
8   VALARGHISGLNLEUGLYARGARGARGMET
9   LYSLEULEUASNVALPHEPHESERTHRGLU
10   ALAPROVALASPASPTRPGLUGLUILEALA
11   LYSLYSTHRPHEGLULYSGLYTHRVALSER
12   VALGLUPROALAILEVALARGGLYTHRMET
13   LEUARGASPASPLEUGLNALAVALPHEPRO
14   SERPHEARGTHRGLUASPCYSSERGLUGLU
15   HISALASERPHEGLUASNALAGLNMETALA
16   ARGGLUARGPHELEUSERLEUVALLEULYS
17   GLNGLUGLUGLNARGLYSTHRGLUALAALA
18   VALPHEGLNASNGLYLYSLEUGLUARGGLU
19   ASNLEUTYRPHEGLN

Samples:

sample_1: YqgP, [U-13C; U-15N], 1 mM; sodium chloride 150 mM; sodium phosphate 25 mM

sample_conditions_1: ionic strength: 175 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

TopSpin, Bruker Biospin - processing

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

Sparky, Goddard - chemical shift assignment

YASARA, YASARA - refinement

NMR spectrometers:

  • Bruker AVANCE III 850 MHz

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