BMRB Entry 51288
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51288
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Title: Resonance assignment of the enzyme KdgF from Bacteroides eggerthii PubMed: 36042150
Deposition date: 2022-01-23 Original release date: 2022-09-19
Authors: Petersen, Agnes Beenfeldt; Christensen, Idd Andrea; Aachmann, Finn Lillelund
Citation: Petersen, Agnes Beenfeldt; Christensen, Idd Andrea; Ronne, Mette; Stender, Emil; Teze, David; Svensson, Birte; Aachmann, Finn Lillelund. "1H, 13C, 15N resonance assignment of the enzyme KdgF from Bacteroides eggerthii" Biomol. NMR Assignments 16, 343-347 (2022).
Assembly members:
entity_1, polymer, 126 residues, Formula weight is not available
Natural source: Common Name: Bacteroides eggerthii Taxonomy ID: 28111 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacteroides eggerthii
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET15b-USER-BeKdgF
Entity Sequences (FASTA):
entity_1: MGSSHHHHHHGSMKTCSKVF
LLENEISWEQVGEGIQRQIL
GYDGQLMLVKVKFQKGAIGN
AHEHFHSQSTYVVSGVFEFH
VNGEKKIVKAGDGIYMEPDV
LHGCTCLEAGILIDTFSPMR
EDFINE
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 423 |
| 15N chemical shifts | 115 |
| 1H chemical shifts | 549 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | KgdF | 1 |
Entities:
Entity 1, KgdF 126 residues - Formula weight is not available
Amino acids 1-12 (MGSSHHHHHHGS) is a His-tag only for purification purpose and it is not cleaved from the protein.
| 1 | MET | GLY | SER | SER | HIS | HIS | HIS | HIS | HIS | HIS | ||||
| 2 | GLY | SER | MET | LYS | THR | CYS | SER | LYS | VAL | PHE | ||||
| 3 | LEU | LEU | GLU | ASN | GLU | ILE | SER | TRP | GLU | GLN | ||||
| 4 | VAL | GLY | GLU | GLY | ILE | GLN | ARG | GLN | ILE | LEU | ||||
| 5 | GLY | TYR | ASP | GLY | GLN | LEU | MET | LEU | VAL | LYS | ||||
| 6 | VAL | LYS | PHE | GLN | LYS | GLY | ALA | ILE | GLY | ASN | ||||
| 7 | ALA | HIS | GLU | HIS | PHE | HIS | SER | GLN | SER | THR | ||||
| 8 | TYR | VAL | VAL | SER | GLY | VAL | PHE | GLU | PHE | HIS | ||||
| 9 | VAL | ASN | GLY | GLU | LYS | LYS | ILE | VAL | LYS | ALA | ||||
| 10 | GLY | ASP | GLY | ILE | TYR | MET | GLU | PRO | ASP | VAL | ||||
| 11 | LEU | HIS | GLY | CYS | THR | CYS | LEU | GLU | ALA | GLY | ||||
| 12 | ILE | LEU | ILE | ASP | THR | PHE | SER | PRO | MET | ARG | ||||
| 13 | GLU | ASP | PHE | ILE | ASN | GLU |
Samples:
sample_1: KdgF, [U-13C; U-15N], 0.92 mM; sodium phosphate 25 mM; sodium chloride 50 mM; D2O, [U-99% 2H], 10%; H2O 90%
sample_conditions_1: ionic strength: 0.1875 M; pH: 7.2; pressure: 1 atm; temperature: 298.1 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 1D 1H | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCANH | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N TROSY | sample_1 | isotropic | sample_conditions_1 |
| TROSY-HNCACB | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v3.6.1 - processing
CARA v1.8.4.2 - chemical shift assignment
TALOS-N - data analysis
TOPSPIN v4.0.7 - collection
NMR spectrometers:
- Bruker AVANCE III 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts