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 19683

Title: NMR structure of the S-linked glycopeptide sublancin 168   PubMed: 24405370

Deposition date: 2013-12-13 Original release date: 2014-03-10

Authors: Garcia De Gonzalo, Chantal; Zhu, Lingyang; Oman, Trent; van der Donk, Wilfred

Citation: Garcia De Gonzalo, Chantal; Zhu, Lingyang; Oman, Trent; van der Donk, Wilfred. "NMR structure of the s-linked glycopeptide sublancin 168."  ACS Chem. Biol. 9, 796-801 (2014).

Assembly members:
sublancin, polymer, 37 residues, 3723.305 Da.
entity_GLC, non-polymer, 180.156 Da.

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

Experimental source:   Production method: purified from the natural source   Host organism: Bacillus subtilis

Entity Sequences (FASTA):
sublancin: GLGKAQCAALWLQCASGGTI GCGGGAVACQNYRQFCR

Data sets:
Data typeCount
13C chemical shifts65
15N chemical shifts42
1H chemical shifts220

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1sublancin1
2entity_GLC2

Entities:

Entity 1, sublancin 37 residues - 3723.305 Da.

1   GLYLEUGLYLYSALAGLNCYSALAALALEU
2   TRPLEUGLNCYSALASERGLYGLYTHRILE
3   GLYCYSGLYGLYGLYALAVALALACYSGLN
4   ASNTYRARGGLNPHECYSARG

Entity 2, entity_GLC - C6 H12 O6 - 180.156 Da.

1   entity_GLC

Samples:

sample_1: 13C,15N-labeled sublancin, [U-98% 13C; U-98% 15N], 2 mM; H2O 90%; D2O 10%

sample_2: sublancin 2 mM; H2O 90%; D2O 10%

sample_3: 15N-labeled sublancin, [U-100% 15N], 2 mM; H2O 90%; D2O 10%

sample_conditions: pH: 7; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_3isotropicsample_conditions
2D 1H-13C HSQCsample_2isotropicsample_conditions
2D 1H-1H TOCSYsample_2isotropicsample_conditions
2D DQF-COSYsample_2isotropicsample_conditions
2D 1H-1H NOESYsample_2isotropicsample_conditions
3D CBCA(CO)NHsample_1isotropicsample_conditions
3D HNCAsample_1isotropicsample_conditions
3D HNHAsample_3isotropicsample_conditions
3D 1H-15N NOESYsample_3isotropicsample_conditions
3D 1H-15N TOCSYsample_3isotropicsample_conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions

Software:

X-PLOR_NIH v2.34, Schwieters, Kuszewski, Tjandra and Clore - refinement

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - chemical shift assignment, peak picking

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Agilent VNMRS 750 MHz

Related Database Links:

PDB
EMBL CAB14066 CEI57357 CEJ77782
GB AAC12992 AAC63531 AFQ58095 AGG61541 AIC40591
REF NP_046571 NP_390031 WP_009967544
SP P68577 P68578

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