PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
33728680-4	2021	Using all atom molecular dynamics simulations, we demonstrated that Y501 in mutated RBD can be well coordinated by Y41 and K353 in hACE2 through hydrophobic interactions, increasing the overall binding affinity between RBD and hACE2 by about 0.81 kcal/mol.	y501	68-72	angiotensin converting enzyme 2	Homo sapiens	131-136
33728680-4	2021	Using all atom molecular dynamics simulations, we demonstrated that Y501 in mutated RBD can be well coordinated by Y41 and K353 in hACE2 through hydrophobic interactions, increasing the overall binding affinity between RBD and hACE2 by about 0.81 kcal/mol.	y501	68-72	angiotensin converting enzyme 2	Homo sapiens	227-232
33914735-2	2021	We present a 2.9-A resolution cryo-electron microscopy (cryo-EM) structure of the complex between the ACE2 receptor and N501Y spike protein ectodomains that shows Y501 inserted into a cavity at the binding interface near Y41 of ACE2.	y501	163-167	angiotensin converting enzyme 2	Homo sapiens	102-106
33914735-2	2021	We present a 2.9-A resolution cryo-electron microscopy (cryo-EM) structure of the complex between the ACE2 receptor and N501Y spike protein ectodomains that shows Y501 inserted into a cavity at the binding interface near Y41 of ACE2.	y501	163-167	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	126-131
33914735-2	2021	We present a 2.9-A resolution cryo-electron microscopy (cryo-EM) structure of the complex between the ACE2 receptor and N501Y spike protein ectodomains that shows Y501 inserted into a cavity at the binding interface near Y41 of ACE2.	y501	163-167	angiotensin converting enzyme 2	Homo sapiens	228-232