Nucleocapsid Protein
(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
SER-392
GLY-393
10.8
10.9
5.0
-39.9
20.7
28.4
-96.6
GLY-393
GLY-394
9.0
9.1
2.2
71.1
90.5
90.4
-21.6
GLY-394
ASN-395
11.6
10.7
163.3
-111.5
104.7
167.3
-121.6
ASN-395
THR-396
9.4
11.9
-70.3
-84.7
70.5
71.6
150.3
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
SER-438
ASP-439
16.1
16.5
-103.5
-76.3
84.4
39.6
564.5
ASP-439
MET-440
15.6
15.6
167.4
-12.3
112.6
121.4
-228.2
MET-440
ARG-441
11.9
12.2
-2.6
14.0
2.8
9.2
-35.3
ARG-441
THR-442
12.7
13.2
-7.9
6.1
73.4
77.7
8.2
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