Table 1. Model predicted effects on stability of 41 observed mutations in EBOV GP.

The one observed mutation that is also on the watch list is indicated in red. The two mutations that our methods falsely excludes as non-functional are indicated in blue. All numerical entries are ΔΔG values in units of kcal/mol.

Mutation	Antibody binda	Dimer bindb	Trimer bindc	Monomer foldd
N107D	0.00	−0.09	0.00	1.31
L111F	0.00	0.00	0.00	2.31
I129V	0.00	0.05	0.02	0.77
D150A	0.00	0.00	0.01	0.6
D163N	0.00	1.12	0.57	0.39
I170L	0.00	0.01	0.02	2.31
I170F	0.00	0.03	0.05	16.48
V181I	0.00	0.05	0.00	−0.73
T206M	−0.30	−0.33	0.01	−0.14
G212D	0.00	0.19	−0.04	−0.11
Y213H	0.00	0.41	−0.01	1.27
Y214H	0.00	−0.01	0.00	0.18
T216P	0.00	−0.01	0.00	2.27
R219K	0.00	0.00	0.00	0.00
A222V	0.00	0.00	0.00	−0.11
E229K	0.00	0.00	0.00	−0.17
T230A	0.00	0.00	0.00	0.62
T240N	0.00	0.00	0.00	0.86
S246P	0.00	0.00	0.00	−1.11
L254I	0.00	0.00	0.00	0.81
L254V	0.00	0.00	0.00	1.39
Q255R	0.00	0.00	0.00	0.1
I260R	0	0	0	1.78
T262A	0	0	0	−0.08
W275L	0	0	0	0.09
A503V	−0.17	0.09	0	0.1
Q508R	0.16	−0.03	0	0.54
Y517C	0.01	0.26	0.01	1.38
G524D	−0.01	0.14	2.31	2.12
A526T	0.00	0.02	0.56	0.80
I527T	0.00	0.18	0.15	1.04
P537L	0.00	0.23	0.42	0.53
I544T	0.00	0.36	−0.01	0.47
E545D	0.00	0.5	0.00	0.46
N550K	4.59	0.01	0.00	0.62
D552N	1.76	0.23	0.00	0.13
A562D	−0.06	2.98	0.02	0.67
L571R	0.00	0.05	2.34	0.27
L573R	0.00	2.78	−0.25	1.30
W597F	0.00	0.07	0.48	−0.11
W597C	0.00	0.35	3.51	0.26

Notes.

^aBinding affinity between GP and the KZ52 antibody.

^bBinding affinity between GP1 and GP2.

^cBinding affinity between three GP1-GP2 dimers.

^dFolding stability for GP2.