Peptidyl-Prolyl Cis-Trans Isomerase Slyd
(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
VAL-57
PRO-58
2.4
3.0
4.8
2.7
61.4
61.0
12.5
PRO-58
ALA-59
3.4
4.2
-11.1
11.3
123.1
122.8
10.9
ALA-59
GLU-60
3.2
3.7
-1.8
-9.7
143.2
147.2
-22.8
GLU-60
LYS-61
2.0
2.7
10.6
4.9
97.8
94.5
-11.5
LYS-61
ALA-62
2.1
2.0
-0.6
-12.9
54.9
58.1
32.9
ALA-62
TYR-63
2.5
2.1
-9.4
25.5
126.7
126.6
33.6
TYR-63
GLY-64
5.2
5.0
-20.0
24.5
135.1
139.6
10.5
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
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-123
LYS-124
8.2
8.3
8.6
-10.6
26.2
17.5
-12.5
LYS-124
ASP-125
7.2
7.2
-17.9
19.2
96.3
100.1
29.4
ASP-125
LEU-126
4.6
4.6
18.7
-12.4
34.5
42.5
34.3
LEU-126
ASP-127
2.3
2.0
-1.6
-3.4
126.1
131.4
9.8
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