BMRB Entry 18849
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18849
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Title: Chemical shift assignments and secondary structure prediction of the C-terminal domain of the response regulator BfmR from Acinetobacter baumannii PubMed: 23264007
Deposition date: 2012-11-20 Original release date: 2012-11-26
Authors: Olson, Andrew; Thompson, Richele; Melander, Christian; Cavanagh, John
Citation: Olson, Andrew; Thompson, Richele; Melander, Christian; Cavanagh, John. "Chemical shift assignments and secondary structure prediction of the C-terminal domain of the response regulator BfmR from Acinetobacter baumannii." Biomol. NMR Assignments ., .-. (2012).
Assembly members:
BfmrC, polymer, 117 residues, Formula weight is not available
Natural source: Common Name: Acinetobacter baumannii Taxonomy ID: 470 Superkingdom: Bacteria Kingdom: not available Genus/species: Acinetobacter baumannii
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
BfmrC: EDEVAQRIEFDDLVIDNGGR
SVTLNGELVDFTSAEYDLLW
LLASNAGRILSREDIFERLR
GIEYDGQDRSIDVRISRIRP
KIGDDPENPKRIKTVRSKGY
LFVKETNGLLEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 420 |
| 15N chemical shifts | 96 |
| 1H chemical shifts | 686 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | BfmrC | 1 |
Entities:
Entity 1, BfmrC 117 residues - Formula weight is not available
| 1 | GLU | ASP | GLU | VAL | ALA | GLN | ARG | ILE | GLU | PHE | ||||
| 2 | ASP | ASP | LEU | VAL | ILE | ASP | ASN | GLY | GLY | ARG | ||||
| 3 | SER | VAL | THR | LEU | ASN | GLY | GLU | LEU | VAL | ASP | ||||
| 4 | PHE | THR | SER | ALA | GLU | TYR | ASP | LEU | LEU | TRP | ||||
| 5 | LEU | LEU | ALA | SER | ASN | ALA | GLY | ARG | ILE | LEU | ||||
| 6 | SER | ARG | GLU | ASP | ILE | PHE | GLU | ARG | LEU | ARG | ||||
| 7 | GLY | ILE | GLU | TYR | ASP | GLY | GLN | ASP | ARG | SER | ||||
| 8 | ILE | ASP | VAL | ARG | ILE | SER | ARG | ILE | ARG | PRO | ||||
| 9 | LYS | ILE | GLY | ASP | ASP | PRO | GLU | ASN | PRO | LYS | ||||
| 10 | ARG | ILE | LYS | THR | VAL | ARG | SER | LYS | GLY | TYR | ||||
| 11 | LEU | PHE | VAL | LYS | GLU | THR | ASN | GLY | LEU | LEU | ||||
| 12 | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: BfmrC, [U-100% 13C; U-100% 15N], 1 mM; Tris-HCl 0.025 M; KCl 0.05 M
sample_2: BfmrC, [U-100% 13C], 1 mM; Tris-HCl 0.025 M; KCl 0.05 M
sample_conditions_1: ionic strength: 0.05 M; pH: 6.5; pressure: 1 atm; temperature: 273 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis
SPARKY, Goddard - chemical shift assignment
NMR spectrometers:
- Bruker Avance 700 MHz
- Varian INOVA 600 MHz
Related Database Links:
| DBJ | BAN88679 BAP35785 BAP67858 GAB01456 GAB75315 |
| EMBL | CAG67634 CAM87883 CAP02024 CDG76603 CDG77731 |
| GB | AAX40744 ABO11188 ACC56017 ACJ40594 ACJ59134 |
| REF | WP_000076438 WP_000076439 WP_000076440 WP_000076441 WP_000076442 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts