BMRB Entry 50219
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50219
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Title: Mfd_RID
Deposition date: 2020-03-30 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: RNLAELHIGQPVVHLEHGVG
RYAGMTTLEAGGITGEYLML
TYANDAKLYVPVSSLHLISR
YAGGAEENAPLHKLGG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 303 |
| 15N chemical shifts | 63 |
| 1H chemical shifts | 488 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | RID | 1 |
Entities:
Entity 1, RID 76 residues - Formula weight is not available
| 1 | ARG | ASN | LEU | ALA | GLU | LEU | HIS | ILE | GLY | GLN | ||||
| 2 | PRO | VAL | VAL | HIS | LEU | GLU | HIS | GLY | VAL | GLY | ||||
| 3 | ARG | TYR | ALA | GLY | MET | THR | THR | LEU | GLU | ALA | ||||
| 4 | GLY | GLY | ILE | THR | GLY | GLU | TYR | LEU | MET | LEU | ||||
| 5 | THR | TYR | ALA | ASN | ASP | ALA | LYS | LEU | TYR | VAL | ||||
| 6 | PRO | VAL | SER | SER | LEU | HIS | LEU | ILE | SER | ARG | ||||
| 7 | TYR | ALA | GLY | GLY | ALA | GLU | GLU | ASN | ALA | PRO | ||||
| 8 | LEU | HIS | LYS | LEU | GLY | GLY |
Samples:
sample_1: RID, [U-100% 13C; U-100% 15N], 600 uM; 1x PBS buffer 152 mM
sample_conditions_1: ionic strength: 152 mM; pH: 7.4; 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 aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | 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 HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | 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 |
| 2D HBCBCGCDCEHE | sample_1 | isotropic | sample_conditions_1 |
| 2D HBCBCGCDHD | 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