|
Mutant
|
Mutation
|
Expression
|
Binding
|
ASA
|
|---|
|
1
|
E327
|
98
|
83
|
123
|
|
2
|
K333
|
86
|
90
|
176
|
|
3*
|
K344
|
95
|
102
|
159
|
|
4
|
K390
|
104
|
1
|
44
|
|
5
|
D392
|
110
|
95
|
69
|
|
6
|
D393
|
30
|
100
|
10
|
|
7
|
K411
|
90
|
103
|
33
|
|
8
|
D414
|
120
|
130
|
113
|
|
9
|
D415
|
90
|
102
|
97
|
|
10*
|
R426
|
73
|
7
|
95
|
|
11
|
N427
|
100
|
111
|
121
|
|
12
|
D429
|
103
|
0
|
9
|
|
13
|
T431
|
131
|
64
|
59
|
|
14
|
K439
|
85
|
87
|
65
|
|
15
|
R441
|
10
|
15
|
3
|
|
16*
|
Y442
|
105
|
110
|
68
|
|
17*
|
R444
|
80
|
86
|
52
|
|
18
|
H445
|
124
|
103
|
113
|
|
19
|
K447
|
87
|
85
|
138
|
|
20
|
R449
|
96
|
101
|
178
|
|
21
|
F451
|
69
|
71
|
64
|
|
22
|
D454
|
50
|
4
|
25
|
|
23
|
I455
|
77
|
6
|
89
|
|
24
|
D463
|
87
|
81
|
70
|
|
25*
|
L472
|
95
|
99
|
172
|
|
26
|
N473
|
100
|
0
|
70
|
|
27
|
W476
|
80
|
76
|
126
|
|
28
|
F483
|
91
|
3
|
2
|
|
29
|
Q492
|
95
|
3
|
5
|
|
30
|
Y494
|
50
|
7
|
21
|
|
31
|
R495
|
97
|
19
|
7
|
|
32
|
E502
|
110
|
84
|
175
|
|
33
|
S17–276
|
90
|
0
| |
|
34
|
S319–518
|
100
|
100
| |
- The mutants that significantly decrease binding to ACE2 are shown in bold. The * denotes mutant residues that are naturally occurring in various SCV strains (see Fig. 6A). The binding and expression values for the individual mutants are expressed as a percentage of the value for the S319–518 (wt) that is assumed 100%. The values of accessible surface area (ASA, Å2) for mutant residues were calculated from the crystal structure of the S RBD-ACE2 complex (coordinates provided by S. Harrison) by using the Lee and Richards' algorithm [23] with a probe radius of 1.4 Å.
