Myosin Light Chain Kinase, Green Fluorescent Protein, Calmodulin Chimera
(All numbering and residues are taken from first PDB file)
Bending Residue Dihedral Analysis
Residue i
Residue i+1
Distance of hinge axis to residue i in conformer 1 (A)
Distance of hinge axis to residue i in conformer 2 (A)
Change in psi (i) (deg)
Change in phi (i+1) (deg)
Angle of psi(i) axis to hinge axis conformer 1 (deg)
Angle of psi(i) axis to hinge axis conformer 2 (deg)
Percentage Progress
GLY-329
ILE-330
4.9
5.3
-5.1
15.4
117.8
111.8
-10.9
ILE-330
THR-331
1.4
2.0
-16.9
-26.6
42.7
56.4
51.5
THR-331
THR-332
3.7
4.8
-1.7
29.0
66.5
90.4
20.5
THR-332
LYS-333
4.2
6.8
4.9
-24.3
69.2
21.9
-18.5
LYS-333
GLN-334
7.5
8.2
0.1
-7.2
49.6
54.7
-0.8
GLN-334
LEU-335
5.4
4.8
-15.2
-21.9
76.9
75.2
36.5
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 i
Residue i+1
Distance of hinge axis to residue i in conformer 1 (A)
Distance of hinge axis to residue i in conformer 2 (A)
Change in psi (i) (deg)
Change in phi (i+1) (deg)
Angle of psi(i) axis to hinge axis conformer 1 (deg)
Angle of psi(i) axis to hinge axis conformer 2 (deg)
Percentage Progress
ILE-355
ASN-356
4.0
3.7
2.3
26.5
30.4
20.8
36.9
ASN-356
GLU-357
3.4
3.6
13.3
-8.9
62.1
68.7
0.8
GLU-357
VAL-358
4.9
5.0
32.2
-58.8
109.8
99.6
7.3
GLY-364
THR-365
5.8
5.7
39.8
-47.4
132.9
156.5
4.0
THR-365
ILE-366
4.4
3.9
17.4
22.3
68.9
81.3
16.9
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