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
3.8
3.6
-12.8
8.9
119.4
118.6
2.2
GLY-64
PRO-65
3.3
3.2
-7.6
0.9
103.1
103.2
-38.2
PRO-65
HIS-66
3.6
3.9
-22.8
35.4
133.0
140.7
104.8
HIS-66
ASP-67
3.6
4.0
4.4
-7.3
36.9
40.8
-22.1
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
HIS-119
PRO-120
5.0
4.8
-1.9
1.8
117.5
117.7
-6.2
PRO-120
LEU-121
7.5
7.1
-6.9
9.2
154.1
151.3
14.7
LEU-121
ALA-122
5.5
5.1
-4.9
6.1
86.3
84.3
65.7
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