BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 17720

Title: Solution Structure of N-terminal Cytosolic Domain of Rhomboid Intramembrane Protease from Escherichia Coli   PubMed: 22963263

Deposition date: 2011-06-20 Original release date: 2012-09-24

Authors: Sherratt, Allison; Ghasriani, Houman; Goto, Natalie

Citation: Sherratt, Allison; Blais, David; Ghasriani, Houman; Pezacki, John Paul; Goto, Natalie. "Activity-based protein profiling of the Escherichia coli GlpG rhomboid protein delineates the catalytic core."  Biochemistry 51, 7794-7803 (2012).

Assembly members:
NGlpG, polymer, 63 residues, 7142.065 Da.

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

Entity Sequences (FASTA):
NGlpG: MLMITSFANPRVAQAFVDYM ATQGVILTIQQHNQSDVWLA DESQAERVRAELARFLENPA DLD

Data sets:
Data typeCount
13C chemical shifts251
15N chemical shifts68
1H chemical shifts394

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1NGlpG1

Entities:

Entity 1, NGlpG 63 residues - 7142.065 Da.

1   METLEUMETILETHRSERPHEALAASNPRO
2   ARGVALALAGLNALAPHEVALASPTYRMET
3   ALATHRGLNGLYVALILELEUTHRILEGLN
4   GLNHISASNGLNSERASPVALTRPLEUALA
5   ASPGLUSERGLNALAGLUARGVALARGALA
6   GLULEUALAARGPHELEUGLUASNPROALA
7   ASPLEUASP

Samples:

sample_1: Nglpg, [U-100% 13C; U-100% 15N], 1.0 ± 0.05 mM; H2O 90%; D2O 10%

sample_2: Nglpg, [U-100% 13C; U-100% 15N], 1.0 ± 0.05 mM; D2O 100%

sample_conditions_1: ionic strength: 0.15 M; pH: 6.5; pressure: 1 atm; temperature: 293.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

X-PLOR NIH v2.22, Schwieters, Kuszewski, Tjandra and Clore - refinement

NMR spectrometers:

  • Varian INOVA 500 MHz

Related Database Links:

BMRB 19713
PDB
DBJ BAB37690 BAE77868 BAG79214 BAI27681 BAI32850
EMBL CAP77869 CAQ33744 CAR00366 CAR05025 CAR10074
GB AAG58528 AAN44906 AAN82639 AAP19275 AAT48182
REF NP_312294 NP_709199 WP_000541600 WP_000928708 WP_000928709
SP A1AGU7 A7ZSV4 A8A5N2 A8AQX4 B1IP42

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