BMRB Entry 30161
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30161
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Solution structure of response regulator protein from Burkholderia multivorans
Deposition date: 2016-08-26 Original release date: 2016-09-09
Authors: Yang, F.; Lim, Y.-B.; Barnwal, R.; Varani, G.
Citation: Yang, F.; Lim, Y.-B.; Barnwal, R.; Varani, G.. "Solution structure of response regulator protein from Burkholderia multivorans" . ., .-..
Assembly members:
entity_1, polymer, 125 residues, 13024.712 Da.
Natural source: Common Name: Burkholderia multivorans Taxonomy ID: 87883 Superkingdom: Bacteria Kingdom: not available Genus/species: Burkholderia multivorans
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity_1: MIRTILAIDDSATMRALLHA
TLAQAGYEVTVAADGEAGFD
LAATTAYDLVLTDQNMPRKS
GLELIAALRQLSAYADTPIL
VLTTEGSDAFKAAARDAGAT
GWIEKPIDPGVLVELVATLS
EPAAN
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 468 |
| 15N chemical shifts | 111 |
| 1H chemical shifts | 736 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 125 residues - 13024.712 Da.
| 1 | MET | ILE | ARG | THR | ILE | LEU | ALA | ILE | ASP | ASP | ||||
| 2 | SER | ALA | THR | MET | ARG | ALA | LEU | LEU | HIS | ALA | ||||
| 3 | THR | LEU | ALA | GLN | ALA | GLY | TYR | GLU | VAL | THR | ||||
| 4 | VAL | ALA | ALA | ASP | GLY | GLU | ALA | GLY | PHE | ASP | ||||
| 5 | LEU | ALA | ALA | THR | THR | ALA | TYR | ASP | LEU | VAL | ||||
| 6 | LEU | THR | ASP | GLN | ASN | MET | PRO | ARG | LYS | SER | ||||
| 7 | GLY | LEU | GLU | LEU | ILE | ALA | ALA | LEU | ARG | GLN | ||||
| 8 | LEU | SER | ALA | TYR | ALA | ASP | THR | PRO | ILE | LEU | ||||
| 9 | VAL | LEU | THR | THR | GLU | GLY | SER | ASP | ALA | PHE | ||||
| 10 | LYS | ALA | ALA | ALA | ARG | ASP | ALA | GLY | ALA | THR | ||||
| 11 | GLY | TRP | ILE | GLU | LYS | PRO | ILE | ASP | PRO | GLY | ||||
| 12 | VAL | LEU | VAL | GLU | LEU | VAL | ALA | THR | LEU | SER | ||||
| 13 | GLU | PRO | ALA | ALA | ASN |
Samples:
sample_1: HEPES 25 mM; response regulator protein, [U-13C; U-15N], 0.9 mM
sample_2: HEPES 25 mM; response regulator protein, [U-13C; U-15N], 0.9 mM
sample_conditions_1: ionic strength: 100 mM; 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_2 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | 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 |
Software:
CYANA, Guntert, Mumenthaler and Wuthrich - refinement
CcpNMR, CCPN - chemical shift assignment
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
TALOS, Cornilescu, Delaglio and Bax - geometry optimization
TOPSPIN, Bruker Biospin - collection
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 500 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts