Outer Surface Protein A
(All numbering and residues are taken from first PDB file)
Bending Residue Dihedral Analysis
Residue
iResidue
i+1Distance of hinge axis to residue i in
(A) Distance of hinge axis to residue i in
(A) Change in
(deg) Change in
(deg) Angle of psi(i) axis to hinge axis
(deg) Angle of psi(i) axis to hinge axis
(deg) Percentage Progress
THR-108
LEU-109
16.8
15.8
1.3
1.5
108.6
109.5
-14.1
LEU-109
VAL-110
13.1
12.4
10.9
-8.9
54.4
62.4
59.8
VAL-110
SER-111
12.5
12.4
5.9
-9.1
92.1
98.7
39.6
SER-111
LYS-112
9.2
9.2
5.4
-9.0
137.0
132.0
24.6
LYS-112
LYS-113
6.3
6.3
1.8
-6.8
95.8
99.9
-0.6
LYS-113
VAL-114
4.0
3.9
-4.3
-1.0
44.0
47.6
33.6
VAL-114
THR-115
0.7
0.7
1.9
-5.4
104.8
105.3
25.0
THR-115
SER-116
2.5
2.4
-7.3
13.2
49.4
47.6
-27.5
SER-116
LYS-117
5.0
4.8
6.1
10.3
126.9
134.3
-78.0
LYS-117
ASP-118
6.9
6.6
-22.1
3.2
107.3
108.4
18.6
ASP-118
LYS-119
10.2
9.8
17.0
-12.5
51.8
53.0
96.8
LYS-119
SER-120
9.0
8.7
3.5
12.3
14.2
12.0
92.9
SER-120
SER-121
8.0
7.7
-24.8
15.9
94.1
97.9
-134.9
Graph shows rotational transition at bending residues and can be used
to identify hinge bending residues.
Probably only informative for interdomain rotations greater than 20 degrees