BMRB Entry 50218
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR50218
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Title: UvrD_CTD
Deposition date: 2020-03-29 Original release date: 2020-10-12
Authors: Kawale, Ashish; Burmann, Bjorn
Citation: Kawale, Ashish; Burmann, Bjorn. "UvrD helicase-RNA polymerase interactions are governed by UvrD's carboxy-terminal Tudor domain" Commun. Biol. ., .-..
Assembly members:
entity_1, polymer, 76 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
Entity Sequences (FASTA):
entity_1: RLRATVSRPVSHQRMGTPMV
ENDSGYKLGQRVRHAKFGEG
TIVNMEGSGEHSRLQVAFQG
QGIKWLVAAYARLESV
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 315 |
| 15N chemical shifts | 71 |
| 1H chemical shifts | 482 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | UvrD_CTD | 1 |
Entities:
Entity 1, UvrD_CTD 76 residues - Formula weight is not available
| 1 | ARG | LEU | ARG | ALA | THR | VAL | SER | ARG | PRO | VAL | ||||
| 2 | SER | HIS | GLN | ARG | MET | GLY | THR | PRO | MET | VAL | ||||
| 3 | GLU | ASN | ASP | SER | GLY | TYR | LYS | LEU | GLY | GLN | ||||
| 4 | ARG | VAL | ARG | HIS | ALA | LYS | PHE | GLY | GLU | GLY | ||||
| 5 | THR | ILE | VAL | ASN | MET | GLU | GLY | SER | GLY | GLU | ||||
| 6 | HIS | SER | ARG | LEU | GLN | VAL | ALA | PHE | GLN | GLY | ||||
| 7 | GLN | GLY | ILE | LYS | TRP | LEU | VAL | ALA | ALA | TYR | ||||
| 8 | ALA | ARG | LEU | GLU | SER | VAL |
Samples:
sample_1: UvrD_CTD, [U-100% 13C; U-100% 15N], 650 uM; potassium phosphate buffer 20 mM; KCl 50 mM
sample_conditions_1: ionic strength: 0.070 M; pH: 6.5; pressure: 1 atm; temperature: 310 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-13C HSQC aliphatic | 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 HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 2D HBCBCGCDHD | sample_1 | isotropic | sample_conditions_1 |
| 2D HBCBCGCDCEHE | sample_1 | isotropic | sample_conditions_1 |
| 15N-(1H) NOE | sample_1 | isotropic | sample_conditions_1 |
| 3D HCACO | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRFAM-SPARKY v1.413 - chemical shift assignment, data analysis
NMR spectrometers:
- Bruker Avance 700 MHz
- Bruker Avance 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts