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 27776

Title: ssNMR assignment of membrane embedded Rhomboid protease GlpG   PubMed: 31603315

Deposition date: 2019-02-05 Original release date: 2020-02-28

Authors: Shi, Chaowei; Chevelkov, Veniamin; Bohg, Claudia; Lange, Sascha; Lange, Adam

Citation: Shi, Chaowei; Oster, Carl; Bohg, Claudia; Li, Longmei; Lange, Sascha; Chevelkov, Veniamin; Lange, Adam. "Structure and Dynamics of the Rhomboid Protease GlpG in Liposomes Studied by Solid-State NMR"  J. Am. Chem. Soc. 141, 17314-17321 (2019).

Assembly members:
GlpG, polymer, 211 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: pET15b

Entity Sequences (FASTA):
GlpG: MGSSHHHHHHSSGLVPRGSH MAALRERAGPVTWVMMIACV VVFIAMQILGDQEVMLWLAW PFDPTLKFEFWRYFTHALMH FSLMHILFNLLWWWYLGGAV EKRLGSGKLIVITLISALLS GYVQQKFSGPWFGGLSGVVY ALMGYVWLRGERDPQSGIYL QRGLIIFALIWIVAGWFDLF GMSMANGAHIAGLAVGLAMA FVDSLNARKRK

Data sets:
Data typeCount
13C chemical shifts279
15N chemical shifts90
1H chemical shifts90

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1GlpG1

Entities:

Entity 1, GlpG 211 residues - Formula weight is not available

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   METALAALALEUARGGLUARGALAGLYPRO
4   VALTHRTRPVALMETMETILEALACYSVAL
5   VALVALPHEILEALAMETGLNILELEUGLY
6   ASPGLNGLUVALMETLEUTRPLEUALATRP
7   PROPHEASPPROTHRLEULYSPHEGLUPHE
8   TRPARGTYRPHETHRHISALALEUMETHIS
9   PHESERLEUMETHISILELEUPHEASNLEU
10   LEUTRPTRPTRPTYRLEUGLYGLYALAVAL
11   GLULYSARGLEUGLYSERGLYLYSLEUILE
12   VALILETHRLEUILESERALALEULEUSER
13   GLYTYRVALGLNGLNLYSPHESERGLYPRO
14   TRPPHEGLYGLYLEUSERGLYVALVALTYR
15   ALALEUMETGLYTYRVALTRPLEUARGGLY
16   GLUARGASPPROGLNSERGLYILETYRLEU
17   GLNARGGLYLEUILEILEPHEALALEUILE
18   TRPILEVALALAGLYTRPPHEASPLEUPHE
19   GLYMETSERMETALAASNGLYALAHISILE
20   ALAGLYLEUALAVALGLYLEUALAMETALA
21   PHEVALASPSERLEUASNALAARGLYSARG
22   LYS

Samples:

sample_1: GlpG, [U-13C; U-15N; U-2H], 35 % w/w; E.coli total lipid extract 35 % w/w; TRIS 20 mM; sodium chloride 100 mM; H2O 30 % w/w; beta-mercaptoethanol 1 mM

sample_conditions_1: ionic strength: 0.12 M; pH: 8; pressure: 1 atm; temperature: 283 K

Experiments:

NameSampleSample stateSample conditions
2D (H)NHsample_1isotropicsample_conditions_1
3D (H)CaNHsample_1isotropicsample_conditions_1
3D (H)CoNHsample_1isotropicsample_conditions_1
3D (H)Ca(Co)NHsample_1isotropicsample_conditions_1
3D (H)CaCo(N)Hsample_1isotropicsample_conditions_1
3D (H)Cb(Ca)NHsample_1isotropicsample_conditions_1
3D (H)CbCa(N)Hsample_1isotropicsample_conditions_1
3D (H)Co(Ca)NHsample_1isotropicsample_conditions_1
3D (H)CoCa(N)Hsample_1isotropicsample_conditions_1
3D H(N)(Co)(Ca)NHsample_1isotropicsample_conditions_1
3D (H)N(Co)(Ca)NHsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment, data analysis

TOPSPIN, Bruker Biospin - collection, processing

NMR spectrometers:

  • Bruker Avance HD 600 MHz

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