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 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: Began, J.. "The N-terminal domain of rhomboid protease YqgP"  Embo J. ., .-. (2019).

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

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

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

Entity Sequences (FASTA):
entity_1: MFLLEYTYWKIAAHLVNSGY GVIQAGESDEIWLEAPDKSS HDLVRLYKHDLDFRQEMVRD IEEQAERVERVRHQLGRRRM KLLNVFFSTEAPVDDWEEIA KKTFEKGTVSVEPAIVRGTM LRDDLQAVFPSFRTEDCSEE HASFENAQMARERFLSLVLK QEEQRKTEAAVFQNGKLERE NLYFQ

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 simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts