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
ALA-62
TYR-63
3.1
3.1
-13.0
22.4
142.8
136.3
60.3
TYR-63
GLY-64
0.2
0.3
-15.9
17.3
86.3
88.7
-12.3
GLY-64
PRO-65
3.6
3.9
-16.5
1.6
57.3
50.7
43.1
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
PRO-120
LEU-121
9.0
8.6
-9.2
4.4
144.0
144.1
-41.4
LEU-121
ALA-122
6.0
5.6
1.5
5.3
84.9
84.1
29.3
ALA-122
GLY-123
4.9
4.8
-4.2
4.1
153.0
161.9
5.6
GLY-123
LYS-124
5.0
4.9
7.8
-3.2
35.9
45.0
40.1
LYS-124
ASP-125
3.4
2.9
-11.4
4.3
95.8
94.6
-31.4
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