BMRB Entry 15459
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15459
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NMR-STAR v3 text file.
XML gzip file.
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Citation: Parsons, Lisa; Grishaev, Alexander; Bax, Ad. "The periplasmic domain of TolR from Haemophilus influenzae forms a dimer with a large hydrophobic groove: NMR solution structure and comparison to SAXS data" Biochemistry 47, 3131-3142 (2008).
PubMed: 18269247
Assembly members:
TolR, polymer, 74 residues, Formula weight is not available
Natural source: Common Name: Haemophilus influenzae Taxonomy ID: 727 Superkingdom: Bacteria Kingdom: not available Genus/species: Haemophilus influenzae
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pet28
Entity Sequences (FASTA):
TolR: GSVPVILEVAGIGKYAISIG
GERQEGLTEEMVTQLSRQEF
DKDNNTLFLVGGAKEVPYEE
VIKALNLLHLAGIK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 312 |
| 15N chemical shifts | 77 |
| 1H chemical shifts | 526 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | subunit 1 | 1 |
| 2 | subunit 2 | 1 |
Entities:
Entity 1, subunit 1 74 residues - Formula weight is not available
residues 19 & 20 are from the cloning tag. Residues 21-92 correspond to residues 59-130 in the full native protein.
| 1 | GLY | SER | VAL | PRO | VAL | ILE | LEU | GLU | VAL | ALA | ||||
| 2 | GLY | ILE | GLY | LYS | TYR | ALA | ILE | SER | ILE | GLY | ||||
| 3 | GLY | GLU | ARG | GLN | GLU | GLY | LEU | THR | GLU | GLU | ||||
| 4 | MET | VAL | THR | GLN | LEU | SER | ARG | GLN | GLU | PHE | ||||
| 5 | ASP | LYS | ASP | ASN | ASN | THR | LEU | PHE | LEU | VAL | ||||
| 6 | GLY | GLY | ALA | LYS | GLU | VAL | PRO | TYR | GLU | GLU | ||||
| 7 | VAL | ILE | LYS | ALA | LEU | ASN | LEU | LEU | HIS | LEU | ||||
| 8 | ALA | GLY | ILE | LYS |
Samples:
sample_1: TolR, [U-99% 13C; U-99% 15N], 0.5 – 1.0 mM; sodium phosphate 50 mM; sodium chloride50 – 100 mM; EDTA 0.05 mM; D2O5 – 10%
sample_conditions_1: pH: 6.7; pressure: 1 atm; temperature: 303 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 CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY, Goddard - data analysis, peak picking
NMR spectrometers:
- Bruker DRX 600 MHz
Related Database Links:
| PDB | |
| EMBL | CBW28683 CBY81984 CBY86494 CKG87573 |
| GB | AAC22042 AAC44595 AAX87439 ABQ97704 ABQ99958 |
| REF | NP_438545 WP_005634116 WP_005649190 WP_005652225 WP_011961713 |
| SP | P43769 |
| AlphaFold | P43769 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks