PMC:7605337 / 34483-35126
Annnotations
LitCovid-PD-MONDO
Most natural mutants exhibited similar binding affinities compared to wild-type nCOV-2019 with a few exceptions. Mutation T478I which is one of the most frequent mutations based on the GISAID database has a binding affinity which is about 6 kcal/mol higher than that of the wild-type. S494P and A475V showed a slightly lower binding affinity than the wild-type complex. Other natural mutants showed binding affinities similar to wild-type RBD. N439K demonstrated a high electrostatic energy which is compensated by large polar solvation energy and this mutant has a total binding energy of −48.27 ± 3.07 kcal/mol which is similar to nCOV-2019.
LitCovid-PD-CLO
Most natural mutants exhibited similar binding affinities compared to wild-type nCOV-2019 with a few exceptions. Mutation T478I which is one of the most frequent mutations based on the GISAID database has a binding affinity which is about 6 kcal/mol higher than that of the wild-type. S494P and A475V showed a slightly lower binding affinity than the wild-type complex. Other natural mutants showed binding affinities similar to wild-type RBD. N439K demonstrated a high electrostatic energy which is compensated by large polar solvation energy and this mutant has a total binding energy of −48.27 ± 3.07 kcal/mol which is similar to nCOV-2019.
LitCovid-sentences
Most natural mutants exhibited similar binding affinities compared to wild-type nCOV-2019 with a few exceptions. Mutation T478I which is one of the most frequent mutations based on the GISAID database has a binding affinity which is about 6 kcal/mol higher than that of the wild-type. S494P and A475V showed a slightly lower binding affinity than the wild-type complex. Other natural mutants showed binding affinities similar to wild-type RBD. N439K demonstrated a high electrostatic energy which is compensated by large polar solvation energy and this mutant has a total binding energy of −48.27 ± 3.07 kcal/mol which is similar to nCOV-2019.
LitCovid-PubTator
Most natural mutants exhibited similar binding affinities compared to wild-type nCOV-2019 with a few exceptions. Mutation T478I which is one of the most frequent mutations based on the GISAID database has a binding affinity which is about 6 kcal/mol higher than that of the wild-type. S494P and A475V showed a slightly lower binding affinity than the wild-type complex. Other natural mutants showed binding affinities similar to wild-type RBD. N439K demonstrated a high electrostatic energy which is compensated by large polar solvation energy and this mutant has a total binding energy of −48.27 ± 3.07 kcal/mol which is similar to nCOV-2019.