Published March 24, 2022
| Version v1
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Data from: Protein Conformational Space at the Edge of Allostery: Turning a Non-allosteric Malate Dehydrogenase into an "Allosterized" Enzyme using Evolution Guided Punctual Mutations
Authors/Creators
- 1. CNRS, Université de Paris, UPR 9080, Laboratoire de Biochimie Théorique, Institut de Biologie Physico-Chimique, Fondation Edmond de Rothschild, PSL Research University, Paris, France.
- 2. Univ. Lyon, Université Lyon 1, CNRS, UMR5558, Laboratoire de Biométrie et Biologie Évolutive, 43 bd du 11 novembre 1918, F-69622, Villeurbanne, France.
- 3. Univ. Grenoble Alpes, CEA, CNRS, IBS, 38000 Grenoble, France.
Description
This data accompanies the paper entitled Protein Conformational Space at the Edge of Allostery: Turning a Non-allosteric Malate Dehydrogenase into an “Allosterized” Enzyme using Evolution Guided Punctual Mutations
The zip archive contains the results of molecular dynamics simulations of the 4 systems investigated in the paper: wt of A. ful MalDH and three mutants. Each system has been simulated at two temperatures, 300 K and 340 K. Starting configurations of the proteins after equilibration are provided for all the systems in GRO Gromos87 format. Trajectories with the positions of the proteins every 100 ps are provided for all the systems in XTC gromacs format.
Files
maldh.zip
Files
(2.8 GB)
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md5:dcd55de41e38699926f84487dd2b5d70
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Additional details
Funding
- Agence Nationale de la Recherche
- AlloAnc - Ancestral Allostery ANR-16-CE11-0011
- Agence Nationale de la Recherche
- DYNAMO - Dynamique des membranes transductrices d'énergie : biogénèse et organisation supramoléculaire. ANR-11-LABX-0011