BMRB Entry 51675
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51675
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NMR-STAR v3 text file.
XML gzip file.
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Citation: Okeke, Damasus; Lidman, Jens; Matecko-Burmann, Irena; Burmann, Bjorn. "Thumb-domain dynamics modulate the functional repertoire of DNA-Polymerase IV (DinB)" Nucleic Acids Res. 51, 7036-7052 (2023).
PubMed: 37260088
Assembly members:
entity_1, polymer, 77 residues, Formula weight is not available
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28d-SUMO
Entity Sequences (FASTA):
entity_1: TPAEVPAFLQTLPLAKIPGV
GKVSAAKLEAMGLRTCGDVQ
KCDLVMLLKRFGKFGRILWE
RSQGIDERDVNSERLRK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 248 |
| 15N chemical shifts | 51 |
| 1H chemical shifts | 360 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | DinB-Thumb | 1 |
Entities:
Entity 1, DinB-Thumb 77 residues - Formula weight is not available
| 1 | THR | PRO | ALA | GLU | VAL | PRO | ALA | PHE | LEU | GLN | ||||
| 2 | THR | LEU | PRO | LEU | ALA | LYS | ILE | PRO | GLY | VAL | ||||
| 3 | GLY | LYS | VAL | SER | ALA | ALA | LYS | LEU | GLU | ALA | ||||
| 4 | MET | GLY | LEU | ARG | THR | CYS | GLY | ASP | VAL | GLN | ||||
| 5 | LYS | CYS | ASP | LEU | VAL | MET | LEU | LEU | LYS | ARG | ||||
| 6 | PHE | GLY | LYS | PHE | GLY | ARG | ILE | LEU | TRP | GLU | ||||
| 7 | ARG | SER | GLN | GLY | ILE | ASP | GLU | ARG | ASP | VAL | ||||
| 8 | ASN | SER | GLU | ARG | LEU | ARG | LYS |
Samples:
sample_1: DinB-Thumb, [U-100% 13C; U-100% 15N], 500 uM; KPi 50 mM; KCl 300 mM; Arginine 50 mM; Glutamine 50 mM; EDTA 1 mM; TCEP 1 mM; CHAPSO 0.1 mM; D2O 10%
sample_conditions_1: ionic strength: 400 mM; pH: 7.5; 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_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | 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 (H)CCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN - collection
NMRPipe - processing
CARA - chemical shift assignment
NMR spectrometers:
- Bruker AVANCE III 700 MHz
- Bruker AVANCE III 900 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks