ParDOCK: an all atom energy based Monte Carlo docking protocol for protein-ligand complexes
A Gupta, A Gandhimathi, P Sharma… - Protein and peptide …, 2007 - ingentaconnect.com
We report here an all-atom energy based Monte Carlo docking procedure tested on a
dataset of 226 proteinligand complexes. Average root mean square deviation (RMSD) from
crystal conformation was observed to be∼ 0.53 Å. The correlation coefficient (r2) for the
predicted binding free energies calculated using the docked structures against experimental
binding affinities was 0.72. The docking protocol is web-enabled as a free software at www.
scfbioiitd. res. in/dock.
dataset of 226 proteinligand complexes. Average root mean square deviation (RMSD) from
crystal conformation was observed to be∼ 0.53 Å. The correlation coefficient (r2) for the
predicted binding free energies calculated using the docked structures against experimental
binding affinities was 0.72. The docking protocol is web-enabled as a free software at www.
scfbioiitd. res. in/dock.
We report here an all-atom energy based Monte Carlo docking procedure tested on a dataset of 226 proteinligand complexes. Average root mean square deviation (RMSD) from crystal conformation was observed to be ∼ 0.53 Å. The correlation coefficient (r2) for the predicted binding free energies calculated using the docked structures against experimental binding affinities was 0.72. The docking protocol is web-enabled as a free software at www.scfbioiitd. res.in/dock.
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