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 26857

Title: Backbone 1H, 15N assignments of lipoprotein signal peptidase in complex with globomycin   PubMed: 27618661

Deposition date: 2016-07-22 Original release date: 2016-11-22

Authors: Laguerre, Aisha

Citation: Laguerre, Aisha; Lohr, Frank; Henrich, Erik; Hoffmann, Beate; Abdul-Manan, Norzehan; Connolly, Peter; Perozo, Eduardo; Moore, Jonathan; Bernhard, Frank; Dotsch, Volker. "From Nanodiscs to Isotropic Bicelles: A Procedure for Solution Nuclear Magnetic Resonance Studies of Detergent-Sensitive Integral Membrane Proteins"  Structure 24, 1830-1841 (2016).

Assembly members:
lipoprotein_signal_peptidase, polymer, 194 residues, Formula weight is not available

Natural source:   Common Name: enterobacteria   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:   Production method: cell free synthesis   Host organism: Escherichia coli

Entity Sequences (FASTA):
lipoprotein_signal_peptidase: MGSSHHHHHHSSAWSHPQFE KSGLVPRGSHMSQSICSTGL RWLWLVVVVLIIDLGSKYLI LQNFALGDTVPLFPSLNLHY ARNYGAAFSFLADSGGWQRW FFAGIAIGISVILAVMMYRS KATQKLNNIAYALIIGGALG NLFDRLWHGFVVDMIDFYVG DWHFATFNLADTAICVGAAL IVLEGFLPSRAKKQ

Data sets:
Data typeCount
13C chemical shifts485
15N chemical shifts178
1H chemical shifts178

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Lipoprotein signal peptide1

Entities:

Entity 1, Lipoprotein signal peptide 194 residues - Formula weight is not available

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERALATRPSERHISPROGLNPHEGLU
3   LYSSERGLYLEUVALPROARGGLYSERHIS
4   METSERGLNSERILECYSSERTHRGLYLEU
5   ARGTRPLEUTRPLEUVALVALVALVALLEU
6   ILEILEASPLEUGLYSERLYSTYRLEUILE
7   LEUGLNASNPHEALALEUGLYASPTHRVAL
8   PROLEUPHEPROSERLEUASNLEUHISTYR
9   ALAARGASNTYRGLYALAALAPHESERPHE
10   LEUALAASPSERGLYGLYTRPGLNARGTRP
11   PHEPHEALAGLYILEALAILEGLYILESER
12   VALILELEUALAVALMETMETTYRARGSER
13   LYSALATHRGLNLYSLEUASNASNILEALA
14   TYRALALEUILEILEGLYGLYALALEUGLY
15   ASNLEUPHEASPARGLEUTRPHISGLYPHE
16   VALVALASPMETILEASPPHETYRVALGLY
17   ASPTRPHISPHEALATHRPHEASNLEUALA
18   ASPTHRALAILECYSVALGLYALAALALEU
19   ILEVALLEUGLUGLYPHELEUPROSERARG
20   ALALYSLYSGLN

Samples:

sample_1: lipoprotein signal peptidase, [U-13C; U-15N; U-2H], 300 uM; sodium acetate buffer 20 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 20 mM; pH: 4.0; pressure: 1 atm; temperature: 318 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 950 MHz

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