p14300 and p14311 (CPU, GRO_A7) to FAH

[Shahlosolieva]

Releasing new CPU (GRO_A7 core) projects p14300 and p14311 to FAH.
These projects are designed to help us understand the role of conserved residues in an extremophilic β-galactosidase. We are running molecular simulations of β-galactosidase and its mutated variants to explore how these subtle sequence changes affect the behavior of this enzyme at various temperatures. We will analyze the trajectory data to formulate explanations for the mechanisms that cause differences in catalytic efficiencies. In the future, a better understanding of how evolved mutations help optimize enzyme efficiency may lead to improved methods for computational enzyme design. These projects have the same aims as p14188-p14190.

Project: 14300
stats credit: 1850
timeout: 15
deadline 20
k-factor v=0.75
number of atoms: 127200

Project: 14311
stats credit: 1510
timeout: 15
deadline 20
k-factor v=0.75
number of atoms: 127200