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 25277

Title: Solution structure of the lantibiotic self-resistance lipoprotein MlbQ from Microbispora ATCC PTA-5024   PubMed: 25923468

Deposition date: 2014-10-09 Original release date: 2015-07-13

Authors: Pozzi, Roberta; Schwartz, Paul; Linke, Dirk; Kulik, Andreas; Nega, Mulugeta; Wohlleben, Wolfgang; Stegmann, Evi; Coles, Murray

Citation: Pozzi, Roberta; Coles, Murray; Schwartz, Paul; Linke, Dirk; Kulik, Andreas; Nega, Mulugeta; Wohlleben, Wolfgang; Stegmann, Evi. "Distinct mechanisms contribute to immunity in the lantibiotic NAI-107 producer strain Microbispora ATCC PTA-5024"  Environ. Microbiol. 18, 118-132 (2016).

Assembly members:
MlbQ, polymer, 147 residues, 15456.215 Da.

Natural source:   Common Name: high GC Gram+   Taxonomy ID: 316330   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Microbispora ATCC PTA-5024

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET30

Entity Sequences (FASTA):
MlbQ: HHHHHHSSGLVPRGSGMKET AAAKFERQHMDSPDLGTDDD DKTGGGRADPAHRSPVPLPS PTSNKQDISEANLAYLWPLT VDHGTIECLPSDNAVFVAPD GTTYALNDRAEKAGHPPITP IRAKGSGGGYISLGALLSTT LNLCGKG

Data sets:
Data typeCount
13C chemical shifts347
15N chemical shifts82
1H chemical shifts573

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1MlbQ1

Entities:

Entity 1, MlbQ 147 residues - 15456.215 Da.

Residues -5-36 represent a non-native cloning/affinity tag

1   HISHISHISHISHISHISSERSERGLYLEU
2   VALPROARGGLYSERGLYMETLYSGLUTHR
3   ALAALAALALYSPHEGLUARGGLNHISMET
4   ASPSERPROASPLEUGLYTHRASPASPASP
5   ASPLYSTHRGLYGLYGLYARGALAASPPRO
6   ALAHISARGSERPROVALPROLEUPROSER
7   PROTHRSERASNLYSGLNASPILESERGLU
8   ALAASNLEUALATYRLEUTRPPROLEUTHR
9   VALASPHISGLYTHRILEGLUCYSLEUPRO
10   SERASPASNALAVALPHEVALALAPROASP
11   GLYTHRTHRTYRALALEUASNASPARGALA
12   GLULYSALAGLYHISPROPROILETHRPRO
13   ILEARGALALYSGLYSERGLYGLYGLYTYR
14   ILESERLEUGLYALALEULEUSERTHRTHR
15   LEUASNLEUCYSGLYLYSGLY

Samples:

15N-labelled: MlbQ, [U-100% 15N], 0.5 mM; TRIS 20 mM; sodium chloride 250 mM; H2O 90%; D2O 10%

13C-15N-labelled: MlbQ, [U-100% 13C; U-100% 15N], 0.5 mM; TRIS 20 mM; sodium chloride 250 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.240 M; pH: 8.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCO13C-15N-labelledisotropicsample_conditions_1
3D C(CO)NH13C-15N-labelledisotropicsample_conditions_1
3D HCCH-TOCSY13C-15N-labelledisotropicsample_conditions_1
3D CCH NOESY13C-15N-labelledisotropicsample_conditions_1
3D CNH NOESY13C-15N-labelledisotropicsample_conditions_1
3D 1H-15N NOESY15N-labelledisotropicsample_conditions_1
3D 1H-13C NOESY13C-15N-labelledisotropicsample_conditions_1
3D HNHA15N-labelledisotropicsample_conditions_1
3D HNHB15N-labelledisotropicsample_conditions_1
3D 3JHBHA(CO)NH13C-15N-labelledisotropicsample_conditions_1
3D NNH NOESY15N-labelledisotropicsample_conditions_1
3D HN(CA)NNH13C-15N-labelledisotropicsample_conditions_1
3D HNCA13C-15N-labelledisotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

SPARKY, Goddard - chemical shift assignment, data analysis

X-PLOR_NIH v2.9.4, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

NMR-SPIRIT v1.1, In house - refinement

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

GB ETK34049.1

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