Spike Glycoprotein
(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
ARG-328
PHE-329
12.9
7.7
-1.5
-17.0
35.1
41.9
13.9
PHE-329
PRO-330
11.5
6.0
-17.9
-14.8
47.7
36.7
36.2
PRO-330
ASN-331
13.4
7.2
7.5
-34.3
97.1
101.3
9.3
ASN-331
ILE-332
16.0
9.6
128.1
-24.9
147.6
159.5
-96.4
ILE-332
THR-333
16.0
8.3
-168.6
-152.8
74.3
93.9
-11.2
THR-333
ASN-334
12.7
11.0
-81.5
48.0
34.8
61.4
44.1
ASN-334
LEU-335
13.5
9.8
79.6
33.8
135.2
54.8
-28.0
LEU-335
CYS-336
10.7
10.3
-28.9
-128.5
80.5
50.8
126.4
CYS-336
PRO-337
9.6
9.1
50.9
-17.0
84.2
115.6
-35.1
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
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
ALA-520
PRO-521
9.3
10.1
-1.1
25.0
34.9
76.8
-21.5
PRO-521
ALA-522
7.5
7.9
-60.2
-173.5
88.1
97.3
86.3
ALA-522
THR-523
4.1
4.2
68.4
-42.3
113.0
60.6
5.3
THR-523
VAL-524
2.0
1.8
-130.3
-1.7
91.5
70.5
-140.9
VAL-524
CYS-525
1.7
1.7
33.6
-8.0
117.2
175.1
-14.5
CYS-525
GLY-526
3.8
2.4
-11.5
-11.6
64.1
71.3
10.1
GLY-526
PRO-527
6.9
5.3
34.3
-6.1
130.0
98.4
-5.6
PRO-527
LYS-528
8.1
8.2
-166.8
26.3
25.3
37.1
186.1
LYS-528
LYS-529
9.0
7.1
108.9
-141.1
101.0
72.7
0.7
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