3.4.17.23	analysis	receptor binding domain-ACE2 binding assay based on time-resolved FRET, which reliably monitors the interaction in a physiologically relevant and cellular context. The modular assay can monitor the impact of different cellular components, such as heparan sulfate, lipids, and membrane proteins on the receptor binding domain-ACE2 interaction and it can be extended to the full-length spike protein. The assay is high throughput compatible and can detect small-molecule competitive and allosteric modulators of the receptor binding domain-ACE2 interaction	764432	
3.4.17.23	D206G	deleterious missense variant	762786	
3.4.17.23	D355N	variant exhibits lower binding to SARS-CoV-2 S protein	762786	
3.4.17.23	D38V	variant exhibits lower binding to SARS-CoV-2 S protein	762786	
3.4.17.23	D509Yr	variant exhibits lower binding to SARS-CoV-2 S protein	762786	
3.4.17.23	E23K	the variant in the binding region increases disease susceptibility towards SARS-CoV-2	762786	
3.4.17.23	E329G	variant shows a strong binding affinity with SARS-CoV-2 spike protein variants with very strong E329G-V483A, E329G-G476S, strong E329G-A419S, E329G-A348T and moderate E329G-S383C,E329G-F486L interaction	765112	
3.4.17.23	E37K	non-synonymous single nucleotide polymorphism	765112	
3.4.17.23	E484K	mutation forms high-affinity complexes (~40% more than wild-type)	763365	
3.4.17.23	E484K/N501Y	variant possesses both enhanced affinity and antibody resistance	763365