PMC:7605337 / 34483-35126 JSONTXT

{"project":"LitCovid-PD-MONDO","denotations":[{"id":"T225","span":{"begin":80,"end":89},"obj":"Disease"},{"id":"T226","span":{"begin":633,"end":642},"obj":"Disease"}],"attributes":[{"id":"A225","pred":"mondo_id","subj":"T225","obj":"http://purl.obolibrary.org/obo/MONDO_0100096"},{"id":"A226","pred":"mondo_id","subj":"T226","obj":"http://purl.obolibrary.org/obo/MONDO_0100096"}],"text":"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."}

{"project":"LitCovid-PD-CLO","denotations":[{"id":"T223","span":{"begin":95,"end":96},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T224","span":{"begin":201,"end":204},"obj":"http://purl.obolibrary.org/obo/CLO_0051582"},{"id":"T225","span":{"begin":205,"end":206},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T226","span":{"begin":308,"end":309},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T227","span":{"begin":463,"end":464},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T228","span":{"begin":560,"end":563},"obj":"http://purl.obolibrary.org/obo/CLO_0051582"},{"id":"T229","span":{"begin":564,"end":565},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"}],"text":"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."}

{"project":"LitCovid-sentences","denotations":[{"id":"T218","span":{"begin":0,"end":112},"obj":"Sentence"},{"id":"T219","span":{"begin":113,"end":284},"obj":"Sentence"},{"id":"T220","span":{"begin":285,"end":369},"obj":"Sentence"},{"id":"T221","span":{"begin":370,"end":443},"obj":"Sentence"},{"id":"T222","span":{"begin":444,"end":643},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"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."}

{"project":"LitCovid-PubTator","denotations":[{"id":"752","span":{"begin":80,"end":84},"obj":"Species"},{"id":"753","span":{"begin":633,"end":637},"obj":"Species"}],"attributes":[{"id":"A752","pred":"tao:has_database_id","subj":"752","obj":"Tax:2697049"},{"id":"A753","pred":"tao:has_database_id","subj":"753","obj":"Tax:2697049"}],"namespaces":[{"prefix":"Tax","uri":"https://www.ncbi.nlm.nih.gov/taxonomy/"},{"prefix":"MESH","uri":"https://id.nlm.nih.gov/mesh/"},{"prefix":"Gene","uri":"https://www.ncbi.nlm.nih.gov/gene/"},{"prefix":"CVCL","uri":"https://web.expasy.org/cellosaurus/CVCL_"}],"text":"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."}