BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 4792

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

Data sets:
Data typeCount
1H chemical shifts446
13C chemical shifts321
15N chemical shifts89

Additional metadata:

  • Assembly
  • Samples and Experiments
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  • Spectrometers
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Related Database Links:

PDB 2AN7
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