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
HIS-56
VAL-57
3.4
3.6
-6.8
9.7
163.2
163.4
33.5
VAL-57
PRO-58
2.9
3.1
6.6
-0.1
52.4
52.1
19.5
PRO-58
ALA-59
2.9
3.3
-2.6
0.8
134.7
131.6
-13.1
ALA-59
GLU-60
1.3
1.5
-0.5
-3.5
135.5
138.3
-9.5
GLU-60
LYS-61
2.3
2.3
3.4
1.6
101.6
100.3
-8.5
LYS-61
ALA-62
4.3
4.2
3.1
-6.5
113.1
113.8
5.3
ALA-62
TYR-63
3.6
3.5
2.3
3.8
40.2
42.2
34.0
TYR-63
GLY-64
4.7
4.5
-2.5
6.1
142.5
141.3
14.2
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
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-124
ASP-125
5.5
5.5
-1.2
6.5
110.7
111.7
49.3
ASP-125
LEU-126
3.1
3.0
5.5
-0.9
41.4
45.5
32.3
LEU-126
ASP-127
2.1
1.9
0.0
-0.4
36.8
36.5
11.4
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