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
4.9
4.9
-2.1
-2.6
71.0
73.9
-0.4
TYR-63
GLY-64
2.2
2.0
7.4
-4.6
50.1
48.0
-29.2
GLY-64
PRO-65
1.6
1.4
8.3
0.7
88.5
85.7
9.6
PRO-65
HIS-66
3.5
3.5
-4.3
-4.9
48.6
44.9
85.7
HIS-66
ASP-67
6.5
6.6
-6.5
5.9
117.1
116.5
13.9
ASP-67
PRO-68
9.2
9.4
1.7
3.5
110.2
110.5
-45.8
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
3.8
3.8
-1.8
1.2
90.8
88.9
-10.1
PRO-120
LEU-121
4.0
4.5
-1.8
0.0
48.5
47.6
5.7
LEU-121
ALA-122
3.0
3.5
-4.3
0.8
21.0
21.3
36.4
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