BMRB Entry 19683
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19683
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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
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 65 |
| 15N chemical shifts | 42 |
| 1H chemical shifts | 220 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | sublancin | 1 |
| 2 | entity_GLC | 2 |
Entities:
Entity 1, sublancin 37 residues - 3723.305 Da.
| 1 | GLY | LEU | GLY | LYS | ALA | GLN | CYS | ALA | ALA | LEU | ||||
| 2 | TRP | LEU | GLN | CYS | ALA | SER | GLY | GLY | THR | ILE | ||||
| 3 | GLY | CYS | GLY | GLY | GLY | ALA | VAL | ALA | CYS | GLN | ||||
| 4 | ASN | TYR | ARG | GLN | PHE | CYS | ARG |
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:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_3 | isotropic | sample_conditions |
| 2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions |
| 2D 1H-1H TOCSY | sample_2 | isotropic | sample_conditions |
| 2D DQF-COSY | sample_2 | isotropic | sample_conditions |
| 2D 1H-1H NOESY | sample_2 | isotropic | sample_conditions |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions |
| 3D HNCA | sample_1 | isotropic | sample_conditions |
| 3D HNHA | sample_3 | isotropic | sample_conditions |
| 3D 1H-15N NOESY | sample_3 | isotropic | sample_conditions |
| 3D 1H-15N TOCSY | sample_3 | isotropic | sample_conditions |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_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