Published October 28, 2024 | Version 1.1
Dataset Open

β-Carotene alleviates substrate inhibition of a transferase caused by asymmetric cooperativity

Authors/Creators

  • 1. Leibniz Institute for Food Systems Biology at the Technical University of Munich; 85354 Freising, Germany
  • 2. Chemoinformatics and Protein Modelling, School of Life Sciences, Technical University of Munich; 85354 Freising, Germany

Contributors

Data collector:

Project leader:

  • 1. Leibniz Institute for Food Systems Biology at the Technical University of Munich; 85354 Freising, Germany
  • 2. Chemoinformatics and Protein Modelling, School of Life Sciences, Technical University of Munich; 85354 Freising, Germany
  • 3. Biotechnology of Natural Products, School of Life Sciences, Technical University of Munich; 85354 Freising, Germany

Description

Initial topology, parameter and coordinates files of the Molecular dynamics (MD) simulations of NbUGT72AY1. Five systems were simulated and analysed:

NbUGT72AY1 (PDB 9J9K, complex V):

  • system 1: structure APO
  • system 2: structure in complex with scopoletin 
  • system 3: structure in complex with UDPG
  • system 4: structure in complex with UDPG and scopoletin

We used ACEMD3 (v3.7.1) as the molecular engine and AMBER as the force field. The three replicas of 1 µs (xtc files) were concatenated in a single trajectory for each system. Water molecules and ions atoms were remove from the original trajectories and topology before the upload (dry_trj.pdb).

Files

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md5:d6d95ab3dd802bf591bcd8e368257835
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