|
domain
|
mutated site
|
mutation
|
ΔΔUVDW
|
ΔΔUCoul
|
ΔΔWGB
|
ΔΔEele
|
ΔΔEtot-np
|
ΔΔWnp
|
ΔΔEtot
|
|---|
|
Rad53-FHA1
|
1
|
pT→pS
|
3.12
|
-8.36
|
5.71
|
-2.65
|
0.46
|
0.03
|
0.49
|
|
Rad53-FHA1
|
1
|
pT→pS
|
0.23
|
-9.64
|
10.93
|
1.29
|
1.52
|
-0.12
|
1.40
|
|
Dun1-FHA
|
1
|
pT→pS
|
2.30
|
3.00
|
-0.71
|
2.29
|
4.59
|
0.06
|
4.66
|
|
Ki67-FHA
|
1
|
pT→pS
|
3.22
|
2.25
|
-1.67
|
0.58
|
3.80
|
0.14
|
3.94
|
|
Dun1-FHA
|
2
|
pT→pS
|
0.49
|
-1.30
|
-0.26
|
-1.57
|
-1.07
|
0.00
|
-1.07
|
|
Ki67-FHA
|
2
|
pS→pT
|
0.70
|
3.33
|
-2.02
|
1.30
|
2.01
|
0.09
|
2.10
|
|
BRCT
|
1
|
pS→pT
|
0.06
|
7.17
|
-6.75
|
0.41
|
0.47
|
0.08
|
0.56
|
|
WW
|
1
|
pS→pT
|
-1.85
|
1.67
|
0.10
|
1.78
|
-0.07
|
0.05
|
-0.02
|
- We selected residues within 5 to 7 Å around pThr/pSer residues. The residues selected are in the Additional file 1. Table S3. The notations are the same in Table 2.
