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
8.3
8.0
-14.0
24.3
168.1
164.7
114.7
TYR-63
GLY-64
8.9
8.9
-15.5
16.7
113.2
113.8
-22.4
GLY-64
PRO-65
5.9
5.9
-16.8
0.2
88.5
81.8
-32.3
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
LEU-121
ALA-122
14.2
13.9
-2.9
4.9
81.1
84.3
31.5
ALA-122
GLY-123
11.4
11.0
21.4
-25.1
61.5
48.4
-31.6
GLY-123
LYS-124
10.6
10.2
9.3
-11.4
15.6
22.4
-11.1
LYS-124
ASP-125
11.8
11.4
-15.3
15.3
122.6
120.3
13.6
ASP-125
LEU-126
10.0
9.6
11.0
-8.5
67.8
76.3
25.2
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