Peptidyl-Prolyl Cis-Trans Isomerase
(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-36
PRO-37
21.0
20.4
12.1
-6.7
120.4
119.9
-7.8
PRO-37
SER-38
19.5
20.0
-95.7
63.3
80.5
67.0
13.2
SER-38
GLY-39
15.8
16.5
20.2
-36.4
86.8
71.8
0.1
GLY-45
LYS-46
6.4
9.0
-107.3
-2.0
83.4
83.2
11.7
LYS-46
ASN-47
7.9
7.5
-106.4
53.9
155.5
83.2
-19.3
ASN-47
GLY-48
8.8
11.0
44.0
128.4
89.8
149.3
52.3
GLY-48
GLN-49
11.7
12.3
-95.3
126.2
40.4
65.1
-16.9
GLN-49
GLY-50
13.5
16.1
-140.7
23.6
99.0
14.8
-123.3
GLY-50
GLU-51
16.9
17.5
33.9
-177.0
130.4
98.1
58.9
GLU-51
PRO-52
19.7
18.0
-12.5
-3.1
40.6
54.7
11.8
PRO-52
ALA-53
20.9
20.7
-23.2
15.3
104.8
119.9
-4.9
ALA-53
ARG-54
23.7
24.2
10.6
5.7
124.3
105.2
-7.8
ARG-54
VAL-55
25.4
25.7
26.6
-12.8
114.5
103.8
-2.9
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