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 34286

Title: Solution structure of lipase binding domain LID1 of foldase from Pseudomonas aeruginosa   PubMed: 32107397

Deposition date: 2018-06-14 Original release date: 2018-12-17

Authors: Viegas, A.; Jaeger, K.; Etzkorn, M.; Gohlke, H.; Verma, N.; Dollinger, P.; Kovacic, F.

Citation: Viegas, Aldino; Dollinger, Peter; Verma, Neha; Kubiak, Jakub; Viennet, Thibault; Seidel, Claus; Gohlke, Holger; Etzkorn, Manuel; Kovacic, Filip; Jaeger, Karl-Erich. "Structural and dynamic insights revealing how lipase binding domain MD1 of Pseudomonas aeruginosa foldase affects lipase activation"  Sci. Rep. 10, 3578-3578 (2020).

Assembly members:
Lipase chaperone, polymer, 89 residues, 10016.225 Da.

Natural source:   Common Name: Pseudomonas aeruginosa PAO1   Taxonomy ID: 208964   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Pseudomonas aeruginosa

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):
Lipase chaperone: MGHHHHHHLPTSFRGTSVDG SFSVDASGNLLITRDIRNLF DAFLSAVGEEPLQQSLDRLR AYIAAELQEPARGQALALMQ QYIDYKKEL

Data sets:
Data typeCount
13C chemical shifts326
15N chemical shifts71
1H chemical shifts568

Additional metadata:

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