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:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 89 residues - 10016.225 Da.

1   METGLYHISHISHISHISHISHISLEUPRO
2   THRSERPHEARGGLYTHRSERVALASPGLY
3   SERPHESERVALASPALASERGLYASNLEU
4   LEUILETHRARGASPILEARGASNLEUPHE
5   ASPALAPHELEUSERALAVALGLYGLUGLU
6   PROLEUGLNGLNSERLEUASPARGLEUARG
7   ALATYRILEALAALAGLULEUGLNGLUPRO
8   ALAARGGLYGLNALALEUALALEUMETGLN
9   GLNTYRILEASPTYRLYSLYSGLULEU

Samples:

sample_1: Lipase-interaction domain 1, [U-13C; U-15N], 530 uM; Na3PO4 20 mM

sample_conditions_1: ionic strength: 20 mM; pH: 7.4; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, data analysis, processing

CARA, Keller and Wuthrich - chemical shift assignment, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

AMBER, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - geometry optimization, refinement

NMR spectrometers:

  • Bruker AvanceIII 600 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts