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
TYR-63
GLY-64
2.5
2.6
-14.5
10.1
165.3
164.3
-36.8
GLY-64
PRO-65
0.5
0.3
-8.3
0.4
126.0
127.1
-41.6
PRO-65
HIS-66
1.8
2.2
-18.8
33.8
101.7
108.4
50.1
HIS-66
ASP-67
4.8
5.0
28.2
-25.0
13.6
21.4
51.2
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
HIS-119
PRO-120
8.7
8.9
-6.9
-4.8
95.2
92.6
-5.9
PRO-120
LEU-121
10.7
10.7
6.4
6.2
79.6
74.8
39.6
LEU-121
ALA-122
7.9
7.8
-6.5
7.5
52.1
50.0
24.2
ALA-122
GLY-123
5.6
5.6
22.6
-29.1
115.8
107.7
28.0
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