PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
34955621-7	2022	The increase in the number of interface residues, interface area and intermolecular forces such as hydrogen bonds, salt bridges and non-bonded contacts corroborated with the increase in the binding affinity of the spike mutants to ACE2.	Hydrogen	99-107	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	214-219	
34955621-8	2022	Further, 75 ns all-atom molecular dynamics simulation investigations show variations in the geometric properties such as root mean square deviation (RMSD), radius of gyration (Rg), total solvent accessible surface area (SASA) and number of hydrogen bonds (NHBs) in the mutant spike:ACE2 complexes with respect to the native spike:ACE2 complex.	Hydrogen	240-248	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	276-281