BMRB Entry 15691
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15691
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Title: Structure of the DBD domain of E. coli antitoxin RelB PubMed: 18501926
Deposition date: 2008-03-23 Original release date: 2008-06-27
Authors: Li, Guang-Yao; Zhang, Yonglong; Inouye, Masayori; Ikura, Mitsuhiko
Citation: Li, Guang-Yao; Zhang, Yonglong; Inouye, Masayori; Ikura, Mitsuhiko. "Structural mechanism of transcriptional autorepression of the Escherichia coli RelB/RelE antitoxin/toxin module" J. Mol. Biol. 380, 107-119 (2008).
Assembly members:
RelB, polymer, 53 residues, 5993.9 Da.
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Eubacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
RelB: GSHMGSINLRIDDELKARSY
AALEKMGVTPSEALRLMLEY
IADNERLPFKQTL
- assigned_chemical_shifts
- RDCs
| Data type | Count |
| 15N chemical shifts | 52 |
| 1H chemical shifts | 362 |
| residual dipolar couplings | 42 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
| 2 | entity_2 | 1 |
Entities:
Entity 1, entity_1 53 residues - 5993.9 Da.
Residues 1-3 represent a non-native affinity tag. This is a DNA binding domain of a antitoxin protein.
| 1 | GLY | SER | HIS | MET | GLY | SER | ILE | ASN | LEU | ARG | ||||
| 2 | ILE | ASP | ASP | GLU | LEU | LYS | ALA | ARG | SER | TYR | ||||
| 3 | ALA | ALA | LEU | GLU | LYS | MET | GLY | VAL | THR | PRO | ||||
| 4 | SER | GLU | ALA | LEU | ARG | LEU | MET | LEU | GLU | TYR | ||||
| 5 | ILE | ALA | ASP | ASN | GLU | ARG | LEU | PRO | PHE | LYS | ||||
| 6 | GLN | THR | LEU |
Samples:
sample_1: RelBN, [U-100% 13C; U-100% 15N], 0.5-1.0 mM; sodium phosphate 20 mM; sodium chloride 100 mM; DTT 1 mM; sodium azide 1 uM
sample_2: RelBN, [U-100% 13C; U-100% 15N], 0.5-1.0 mM; sodium phosphate 20 mM; sodium chloride 100 mM; DTT 1 mM; sodium azide 1 uM
sample_conditions_1: ionic strength: 0.12 M; pH: 7.0; pressure: 1 atm; temperature: 303 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | 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 H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
VNMR v6.1C, Varian - collection
XEASY, Bartels et al. - chemical shift assignment
NMR spectrometers:
- Varian INOVA 600 MHz
Related Database Links:
| PDB | |
| DBJ | BAA15263 BAI25453 BAJ43364 BAN94923 |
| EMBL | CAA26250 CAQ98463 CBG34538 CBK86917 CCF87937 |
| GB | AAC74637 AAN43138 AAP17029 AAS76441 ABF03723 |
| REF | NP_416082 NP_707431 WP_000534857 WP_000534858 WP_001408098 |
| SP | P0C079 P0C080 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts