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
LYS-61
ALA-62
2.1
1.8
4.3
-2.8
110.4
113.3
-10.6
ALA-62
TYR-63
4.1
3.8
5.8
2.3
59.3
63.1
42.4
TYR-63
GLY-64
6.3
6.1
-5.5
14.5
113.2
116.3
18.0
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
ALA-122
GLY-123
8.7
8.5
-2.7
2.6
123.3
125.6
-8.1
GLY-123
LYS-124
7.5
7.3
-2.3
9.2
147.0
146.2
29.4
LYS-124
ASP-125
5.4
5.2
-4.2
6.4
83.2
79.9
2.7
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