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Exact(17)
The native and the mutant structures were superimposed to observe the structural consequences due to the mutation and 2(g)).
The wild and the mutant structures were superimposed to detect the effect of structural changes due to the mutation).
Each residue was mutated to 15 uncharged amino-acids and the mutant structures were refined by MD simulations.
The mutant structures were generated in a four-step procedure.
Mutant structures were determined with the Molecular Replacement technique using the program CNS [34] and the wt-KaiC structure with PDB ID 3DVL [19] as the search model.
The differences between the mutant structures were tested by refining with interchanged starting models.
Similar(42)
Energy minimization of mutant structures was performed with Phenix46.
In this way, our method is applicable even when no mutant structures are available.
The PSTAIRE helix of the mutant structures is rotated from its native position by 16 degrees (Fig. 5).
Thus, the only significant difference between the wild-type and mutant structures is that the PfLDH-W107fA specificity loop is found in the open conformation, consistent with weaker binding of substrate.
Mutant structure was generated using Schrodinger Glide software through Maestro interface.
Related(20)
mutant constructs were
mutant conditions were
variant structures were
mutant structures behaved
mutant alleles were
mutant plasmids were
mutant structures showed
mutant pups were
mutant embryos were
mutant clones were
mutant strains were
mutant phenotypes were
mutant databases were
mutant enzymes were
mutant sequences were
mutant subclones were
mutant flies were
mutant leaves were
mutant mice were
mutant structures bound
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