Article
Extended Data Fig. 4 | Comparison of ACE2 binding by the SARS-CoV RBD,
SARS-CoV-2 wild-type RBD and SARS-CoV-2 chimeric RBD. a, Buried surface
areas at SARS-CoV RBM–ACE2 and SARS-CoV-2 RBM–ACE2 interfaces. In the
crystals for both the SARS-CoV RBD–ACE2 complex and chimeric RBD–ACE2
complex, two copies of each complex were present in one asymmetric unit.
Numbers for both copies of the complexes are shown. The interaction between
Arg439 on the side loop of the RBM and Glu329 of ACE2 was excluded from the
calculation of the buried surface area of SARS-CoV-2. b, List of contact residues
from RBM and ACE2 that are directly involved in RBM–ACE2 binding. The
engineered Arg439 in the chimeric RBD is shown in orange. Contact residues of
the SARS-CoV RBM–ACE2 complex are taken from PDB 2AJF. c, Binding
affinities between the RBDs and ACE2 measured using SPR.