BMRB Entry 16039
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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/BMR16039
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Title: NMR structure of the unphosphorylated form of OdhI, OdhI. PubMed: 19368890
Deposition date: 2008-11-20 Original release date: 2009-04-29
Authors: Barthe, Philippe; Roumestand, Christian; Canova, Marc; Hurard, Corinne; Molle, Virginie; Cohen-Gonsaud, Martin
Citation: Barthe, Philippe; Roumestand, Christian; Canova, Marc; Kremer, Laurent; Hurard, Corinne; Molle, Virginie; Cohen-Gonsaud, Martin. "Dynamic and Structural Characterization of a Bacterial FHA Protein Reveals a New Autoinhibition Mechanism" Structure 17, 568-578 (2009).
Assembly members:
OdhI, polymer, 143 residues, 15700.225 Da.
Natural source: Common Name: Corynebacterium glutamicum Taxonomy ID: 1718 Superkingdom: Bacteria Kingdom: not available Genus/species: Corynebacterium glutamicum
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
OdhI: MSDNNGTPEPQVETTSVFRA
DLLKEMESSTGTAPASTGAE
NLPAGSALLVVKRGPNAGAR
FLLDQPTTTAGRHPESDIFL
DDVTVSRRHAEFRINEGEFE
VVDVGSLNGTYVNREPRNAQ
VMQTGDEIQIGKFRLVFLAG
PAE
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 145 |
| 1H chemical shifts | 970 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | OdhI | 1 |
Entities:
Entity 1, OdhI 143 residues - 15700.225 Da.
| 1 | MET | SER | ASP | ASN | ASN | GLY | THR | PRO | GLU | PRO | ||||
| 2 | GLN | VAL | GLU | THR | THR | SER | VAL | PHE | ARG | ALA | ||||
| 3 | ASP | LEU | LEU | LYS | GLU | MET | GLU | SER | SER | THR | ||||
| 4 | GLY | THR | ALA | PRO | ALA | SER | THR | GLY | ALA | GLU | ||||
| 5 | ASN | LEU | PRO | ALA | GLY | SER | ALA | LEU | LEU | VAL | ||||
| 6 | VAL | LYS | ARG | GLY | PRO | ASN | ALA | GLY | ALA | ARG | ||||
| 7 | PHE | LEU | LEU | ASP | GLN | PRO | THR | THR | THR | ALA | ||||
| 8 | GLY | ARG | HIS | PRO | GLU | SER | ASP | ILE | PHE | LEU | ||||
| 9 | ASP | ASP | VAL | THR | VAL | SER | ARG | ARG | HIS | ALA | ||||
| 10 | GLU | PHE | ARG | ILE | ASN | GLU | GLY | GLU | PHE | GLU | ||||
| 11 | VAL | VAL | ASP | VAL | GLY | SER | LEU | ASN | GLY | THR | ||||
| 12 | TYR | VAL | ASN | ARG | GLU | PRO | ARG | ASN | ALA | GLN | ||||
| 13 | VAL | MET | GLN | THR | GLY | ASP | GLU | ILE | GLN | ILE | ||||
| 14 | GLY | LYS | PHE | ARG | LEU | VAL | PHE | LEU | ALA | GLY | ||||
| 15 | PRO | ALA | GLU |
Samples:
sample_1: OdhI, [U-100% 15N], 0.3 mM; H2O 95%; D2O 5%; NaCl 150 mM
sample_conditions_1: ionic strength: 0.15 M; pH: 6.2; pressure: 1 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
NMR spectrometers:
- Bruker Avance 500 MHz
- Bruker Avance 600 MHz
Related Database Links:
| BMRB | 16038 |
| PDB | |
| DBJ | BAB98834 BAF54493 |
| EMBL | CAF21450 CCH24605 |
| GB | AGG66772 AGN19176 AGN22201 AGT05407 AIK85116 |
| REF | NP_600658 WP_003856253 WP_015651203 |
| SP | Q8NQJ3 |
Download simulated HSQC data in one of the following formats:
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