BMRB Entry 25327
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25327
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Title: Bd0108 PubMed: 25514156
Deposition date: 2014-11-11 Original release date: 2014-12-17
Authors: Prehna, Gerd
Citation: Prehna, Gerd; Ramirez, Benjamin; Lovering, Andrew. "The Lifestyle Switch Protein Bd0108 of Bdellovibrio bacteriovorus Is an Intrinsically Disordered Protein" PLoS One 9, e115390-e115390 (2014).
Assembly members:
Bd0108, polymer, 83 residues, Formula weight is not available
Natural source: Common Name: d-proteobacteria Taxonomy ID: 959 Superkingdom: Bacteria Kingdom: not available Genus/species: Bdellovibrio bacteriovorus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Bd0108: GSHMADENANRPVNPGEDPN
EAFRSTPFEATTSALGDCRE
CIAYRTGATTGKGSRRHDDT
VSREIKGSSATPGGSEKAGT
GRQ
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 271 |
| 1H chemical shifts | 288 |
| 15N chemical shifts | 69 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Bd0108 | 1 |
Entities:
Entity 1, Bd0108 83 residues - Formula weight is not available
| 1 | GLY | SER | HIS | MET | ALA | ASP | GLU | ASN | ALA | ASN | ||||
| 2 | ARG | PRO | VAL | ASN | PRO | GLY | GLU | ASP | PRO | ASN | ||||
| 3 | GLU | ALA | PHE | ARG | SER | THR | PRO | PHE | GLU | ALA | ||||
| 4 | THR | THR | SER | ALA | LEU | GLY | ASP | CYS | ARG | GLU | ||||
| 5 | CYS | ILE | ALA | TYR | ARG | THR | GLY | ALA | THR | THR | ||||
| 6 | GLY | LYS | GLY | SER | ARG | ARG | HIS | ASP | ASP | THR | ||||
| 7 | VAL | SER | ARG | GLU | ILE | LYS | GLY | SER | SER | ALA | ||||
| 8 | THR | PRO | GLY | GLY | SER | GLU | LYS | ALA | GLY | THR | ||||
| 9 | GLY | ARG | GLN |
Samples:
sample_1: Bd0108, [U-99% 13C; U-99% 15N], 1 mM; TRIS 20 mM; sodium chloride 100 mM; beta-mercaptoethanol 2 mM; H2O 95%; D2O 5%
sample_conditions: temperature: 298 K; pH: 7.0; pressure: 1 atm; ionic strength: 0.1 M
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions |
| 3D HNCACB | sample_1 | isotropic | sample_conditions |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions |
| 3D HNCO | sample_1 | isotropic | sample_conditions |
| 3D HCACO | sample_1 | isotropic | sample_conditions |
| 3D HNHA | sample_1 | isotropic | sample_conditions |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY, Goddard - data analysis, chemical shift assignment
TALOS, Cornilescu, Delaglio and Bax - data analysis
TOPSPIN, Bruker Biospin - collection
NMR spectrometers:
- Bruker DRX 600 MHz
- Bruker Avance 800 MHz
- Bruker Avance 900 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts