BMRB Entry 4792
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR4792
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Title: Backbone NMR Assignment and Secondary Structure of the Dimeric ParD Protein PubMed: 11743881
Deposition date: 2000-07-21 Original release date: 2002-04-04
Authors: Oberer, Monika; Prytulla, Stefan; Keller, Walter
Citation: Oberer, Monika; Zangger, Klaus; Prytulla, Stefan; Keller, Walter. "The Anti-toxin ParD of Plasmid RK2 Consists of two Structurally Distinct Moieties and Belongs to the Ribbon-helix-helix Family of DNA-binding Proteins" Biochem. J. 361, 41-47 (2002).
Assembly members:
ParD, polymer, 83 residues, 9103.18 Da.
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):
ParD: MSRLTIDMTDQQHQSLKALA
ALQGKTIKQYALERLFPGDA
DADQAWQELKTMLGNRINDG
LAGKVSTKSVGEILDEELSG
DRA
- assigned_chemical_shifts
Data type | Count |
1H chemical shifts | 446 |
13C chemical shifts | 321 |
15N chemical shifts | 89 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | ParD subunit 1 | 1 |
2 | ParD subunit 2 | 1 |
Entities:
Entity 1, ParD subunit 1 83 residues - 9103.18 Da.
1 | MET | SER | ARG | LEU | THR | ILE | ASP | MET | THR | ASP | ||||
2 | GLN | GLN | HIS | GLN | SER | LEU | LYS | ALA | LEU | ALA | ||||
3 | ALA | LEU | GLN | GLY | LYS | THR | ILE | LYS | GLN | TYR | ||||
4 | ALA | LEU | GLU | ARG | LEU | PHE | PRO | GLY | ASP | ALA | ||||
5 | ASP | ALA | ASP | GLN | ALA | TRP | GLN | GLU | LEU | LYS | ||||
6 | THR | MET | LEU | GLY | ASN | ARG | ILE | ASN | ASP | GLY | ||||
7 | LEU | ALA | GLY | LYS | VAL | SER | THR | LYS | SER | VAL | ||||
8 | GLY | GLU | ILE | LEU | ASP | GLU | GLU | LEU | SER | GLY | ||||
9 | ASP | ARG | ALA |
Samples:
sample_1: ParD, [U-98% 13C; U-98% 15N], 0.6 mM
sample_2: ParD, [U-98% 15N], 0.5 mM
sample_3: ParD 0.5 mM
Cond1: pH: 6.0; temperature: 306 K; ionic strength: 0.11 M
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H15N HSQC | not available | not available | Cond1 |
2D NOESY | not available | not available | Cond1 |
2D TOCSY | not available | not available | Cond1 |
3D 15N NOESY-HSQC | not available | not available | Cond1 |
3D 15N TOCSY-HSQC | not available | not available | Cond1 |
3D HNCO | not available | not available | Cond1 |
3D HN(CO)CA | not available | not available | Cond1 |
3D CBCA(CO)NH | not available | not available | Cond1 |
3D HNCACB | not available | not available | Cond1 |
Software:
XEASY v1.3 -
NMR spectrometers:
- Varian Unity INOVA 600 MHz
Related Database Links:
PDB | |
EMBL | CAE54490 CAG30890 CAK12703 |
GB | AAA26418 AAA91498 AAA92774 AAA98334 AAB67690 |
PIR | A47048 |
REF | WP_011205807 WP_032072691 YP_006941366 YP_006941448 YP_006941534 |
SP | P22995 |
TPE | CAJ85710 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts