PMC:7605337 / 32455-33140 JSONTXT

{"project":"LitCovid-PD-CLO","denotations":[{"id":"T209","span":{"begin":103,"end":105},"obj":"http://purl.obolibrary.org/obo/CLO_0008922"},{"id":"T210","span":{"begin":103,"end":105},"obj":"http://purl.obolibrary.org/obo/CLO_0050052"},{"id":"T211","span":{"begin":125,"end":126},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T212","span":{"begin":239,"end":240},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"}],"text":"Binding free energy decomposition to its individual components for all mutants is represented in Table S2. In all complexes, a large positive polar solvation free energy disfavors the binding and complex formation, which is compensated by a large negative electrostatic free energy of binding. All variants had similar SASA energies. The vdw free energy of binding ranged from −84.68 ± 0.68 kcal/mol for Q493A to −103.85 ± 0.66 kcal/mol for Y489A. Mutant K417A had the lowest electrostatic contribution to binding −415.67 ± 5.07 kcal/mol and mutants N439K and E484A had the highest electrostatic binding contribution of −989.80 ± 5.6 kcal/mol and −941.20 ± 3.95 kcal/mol, respectively."}

{"project":"LitCovid-PD-CHEBI","denotations":[{"id":"T99","span":{"begin":103,"end":105},"obj":"Chemical"}],"attributes":[{"id":"A99","pred":"chebi_id","subj":"T99","obj":"http://purl.obolibrary.org/obo/CHEBI_29387"}],"text":"Binding free energy decomposition to its individual components for all mutants is represented in Table S2. In all complexes, a large positive polar solvation free energy disfavors the binding and complex formation, which is compensated by a large negative electrostatic free energy of binding. All variants had similar SASA energies. The vdw free energy of binding ranged from −84.68 ± 0.68 kcal/mol for Q493A to −103.85 ± 0.66 kcal/mol for Y489A. Mutant K417A had the lowest electrostatic contribution to binding −415.67 ± 5.07 kcal/mol and mutants N439K and E484A had the highest electrostatic binding contribution of −989.80 ± 5.6 kcal/mol and −941.20 ± 3.95 kcal/mol, respectively."}

{"project":"LitCovid-PD-GO-BP","denotations":[{"id":"T11","span":{"begin":204,"end":213},"obj":"http://purl.obolibrary.org/obo/GO_0009058"}],"text":"Binding free energy decomposition to its individual components for all mutants is represented in Table S2. In all complexes, a large positive polar solvation free energy disfavors the binding and complex formation, which is compensated by a large negative electrostatic free energy of binding. All variants had similar SASA energies. The vdw free energy of binding ranged from −84.68 ± 0.68 kcal/mol for Q493A to −103.85 ± 0.66 kcal/mol for Y489A. Mutant K417A had the lowest electrostatic contribution to binding −415.67 ± 5.07 kcal/mol and mutants N439K and E484A had the highest electrostatic binding contribution of −989.80 ± 5.6 kcal/mol and −941.20 ± 3.95 kcal/mol, respectively."}

{"project":"LitCovid-sentences","denotations":[{"id":"T202","span":{"begin":0,"end":106},"obj":"Sentence"},{"id":"T203","span":{"begin":107,"end":293},"obj":"Sentence"},{"id":"T204","span":{"begin":294,"end":333},"obj":"Sentence"},{"id":"T205","span":{"begin":334,"end":447},"obj":"Sentence"},{"id":"T206","span":{"begin":448,"end":685},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Binding free energy decomposition to its individual components for all mutants is represented in Table S2. In all complexes, a large positive polar solvation free energy disfavors the binding and complex formation, which is compensated by a large negative electrostatic free energy of binding. All variants had similar SASA energies. The vdw free energy of binding ranged from −84.68 ± 0.68 kcal/mol for Q493A to −103.85 ± 0.66 kcal/mol for Y489A. Mutant K417A had the lowest electrostatic contribution to binding −415.67 ± 5.07 kcal/mol and mutants N439K and E484A had the highest electrostatic binding contribution of −989.80 ± 5.6 kcal/mol and −941.20 ± 3.95 kcal/mol, respectively."}