Fusion Glycoprotein F0
(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
ASN-457
LYS-458
10.3
10.3
0.0
-2.4
93.8
94.2
-1.9
LYS-458
SER-459
7.7
8.0
2.2
-0.5
26.4
23.1
6.2
SER-459
LEU-460
7.4
8.2
16.3
-13.0
72.1
66.3
21.1
LEU-460
SER-461
7.4
7.1
-1.3
-1.8
63.4
70.3
20.6
SER-461
ASP-462
4.9
4.2
16.4
-8.9
66.2
64.0
29.1
ASP-462
ALA-463
2.4
3.8
5.3
-8.5
28.4
27.3
-29.4
ALA-463
LEU-464
2.9
3.3
2.0
-2.1
95.0
95.8
7.0
LEU-464
GLN-465
4.4
2.6
3.4
-1.2
102.9
99.0
7.4
GLN-465
HIS-466
3.1
1.5
5.1
1.7
34.8
29.1
37.9
HIS-466
LEU-467
2.3
2.2
-16.4
16.5
131.6
120.7
-17.3
LEU-467
ALA-468
4.4
2.8
-5.7
-3.3
75.0
72.2
16.3
ALA-468
GLN-469
7.1
5.5
-11.7
14.7
113.2
112.2
4.9
GLN-469
SER-470
7.5
6.6
-4.7
14.4
169.7
163.8
60.5
SER-470
ASP-471
6.8
5.9
-54.0
45.6
104.2
99.7
-62.1
ASP-471
THR-472
9.6
8.2
-30.5
28.2
83.4
80.1
-52.9
THR-472
TYR-473
11.9
10.7
0.8
-4.6
34.3
41.6
-22.3
TYR-473
LEU-474
11.7
11.2
2.9
-12.5
46.2
37.6
-31.9
LEU-474
SER-475
11.6
10.9
-3.5
8.7
87.2
80.5
-13.0
SER-475
ALA-476
15.1
13.8
25.1
-21.2
76.2
90.5
0.2
ALA-476
ILE-477
16.4
15.7
-0.5
2.0
167.6
160.2
10.8
ILE-477
GLU-478
15.2
15.4
2.0
9.8
63.0
66.7
36.2
GLU-478
ASP-479
16.9
16.5
-15.8
1.7
78.2
77.9
8.7
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