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These 4 oseltamivr structure-based analogues were found to adopt the most promising conformations by identifying the guanidinium side chain of Arg156 as a prospective partner for making polar contacts, but none of the modified 4-amino groups of oseltamivir in the 4 favorable conformations was found to make polar contacts with the guanidinium side chain of Arg156.
This is followed by the generation of subgroups with the most promising conformations via the P-SaMI data pattern [ 10].
This identifies the most promising conformations using the P-SaMI data pattern [ 10] from different clusters of snapshots of an FFR model identified by [ 6].
An RFFR model is achieved by eliminating redundancy in the FFR model through clustering its set of conformations, thus generating subgroups, which should contain the most promising conformations [ 6].
The purpose of this approach is to define a data pattern which is able to dynamically perform the selection of the most promising conformations from clusters of similar snapshots.
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