BMRB Entry 17509
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17509
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Title: NMR structure of the protein YP_557733.1 from Burkholderia xenovorans
Deposition date: 2011-03-04 Original release date: 2011-03-25
Authors: Jaudzems, Kristaps; Serrano, Pedro; Michael, Geralt; Reto, Horst; Wuthrich, Kurt
Citation: Jaudzems, Kristaps; Serrano, Pedro; Michael, Geralt; Reto, Horst; Wuthrich, Kurt. "Null" To be Published ., .-..
Assembly members:
YP_557733.1, polymer, 145 residues, 15414.306 Da.
Natural source: Common Name: Burkholderia xenovorans Taxonomy ID: 36873 Superkingdom: Bacteria Kingdom: not available Genus/species: Burkholderia xenovorans
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
YP_557733.1: IPKHPDSEAVAPDPFNPAAT
QLLDDTSWVLSAWKQADGTA
RAVPSADQGAPITLTLSTST
GQRHASGFSGCNRYMGSYAL
KDGKLSFGTLGGTRMACMTP
GGQIEGAYLNALTHIDRTGV
QMRAPQQMQLVLDNGDTLTF
DRSTR
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 462 |
| 15N chemical shifts | 159 |
| 1H chemical shifts | 969 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | YP_557733.1 | 1 |
Entities:
Entity 1, YP_557733.1 145 residues - 15414.306 Da.
| 1 | ILE | PRO | LYS | HIS | PRO | ASP | SER | GLU | ALA | VAL | ||||
| 2 | ALA | PRO | ASP | PRO | PHE | ASN | PRO | ALA | ALA | THR | ||||
| 3 | GLN | LEU | LEU | ASP | ASP | THR | SER | TRP | VAL | LEU | ||||
| 4 | SER | ALA | TRP | LYS | GLN | ALA | ASP | GLY | THR | ALA | ||||
| 5 | ARG | ALA | VAL | PRO | SER | ALA | ASP | GLN | GLY | ALA | ||||
| 6 | PRO | ILE | THR | LEU | THR | LEU | SER | THR | SER | THR | ||||
| 7 | GLY | GLN | ARG | HIS | ALA | SER | GLY | PHE | SER | GLY | ||||
| 8 | CYS | ASN | ARG | TYR | MET | GLY | SER | TYR | ALA | LEU | ||||
| 9 | LYS | ASP | GLY | LYS | LEU | SER | PHE | GLY | THR | LEU | ||||
| 10 | GLY | GLY | THR | ARG | MET | ALA | CYS | MET | THR | PRO | ||||
| 11 | GLY | GLY | GLN | ILE | GLU | GLY | ALA | TYR | LEU | ASN | ||||
| 12 | ALA | LEU | THR | HIS | ILE | ASP | ARG | THR | GLY | VAL | ||||
| 13 | GLN | MET | ARG | ALA | PRO | GLN | GLN | MET | GLN | LEU | ||||
| 14 | VAL | LEU | ASP | ASN | GLY | ASP | THR | LEU | THR | PHE | ||||
| 15 | ASP | ARG | SER | THR | ARG |
Samples:
sample_1: entity, [U-98% 13C; U-98% 15N], 1 mM; sodium chloride 50 mM; sodium phosphate 20 mM; sodium azide 4.5 mM; H2O 95%; D2O 5%
sample_conditions_1: ionic strength: 0.225 M; pH: 6.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
| 5D APSY-HACACONH | sample_1 | isotropic | sample_conditions_1 |
| 4D APSY-HACANH | sample_1 | isotropic | sample_conditions_1 |
| 5D APSY-CBCACONH | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution
UNIO, Unio Herrmann Wuthrich - chemical shift assignment, processing, structure solution
TOPSPIN, Bruker Biospin - collection, data analysis, processing
CARA, Keller and Wuthrich - chemical shift assignment, data analysis
OPAL, Luginbuhl, Guntert, Billeter and Wuthrich - refinement
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts