Collagen-Like Peptide
(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
GLY-130
PRO-131
15.9
16.2
-15.6
25.8
42.0
47.1
-1.1
PRO-131
PRO-132
13.3
13.5
-12.0
33.5
99.3
108.6
-10.6
PRO-132
GLY-133
9.8
10.1
149.2
-59.9
109.7
62.4
-11.8
GLY-133
SER-134
9.8
7.1
0.1
173.3
104.4
131.4
87.3
SER-134
GLY-135
6.5
4.7
102.2
155.5
79.0
78.3
-90.5
GLY-135
TYR-136
4.1
2.9
-106.1
29.1
69.6
129.0
47.0
TYR-136
ILE-137
0.9
0.5
-151.6
-2.5
87.0
66.5
70.1
ILE-137
PRO-138
4.4
4.3
26.4
6.6
80.6
69.7
13.1
PRO-138
GLU-139
7.7
7.6
10.3
-9.0
35.9
34.8
0.5
GLU-139
ALA-140
9.8
9.9
-0.9
-0.9
79.9
77.5
1.5
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