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
GLY-64
PRO-65
9.9
10.0
-7.0
0.1
47.2
55.4
41.7
PRO-65
HIS-66
11.6
11.6
6.2
-15.0
159.3
166.3
46.8
HIS-66
ASP-67
12.0
12.2
-7.2
14.4
83.4
79.5
-18.8
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
LEU-121
ALA-122
4.6
4.9
5.9
-2.9
121.6
124.4
-7.1
ALA-122
GLY-123
7.8
8.1
-4.3
1.1
90.7
86.9
22.4
GLY-123
LYS-124
8.3
8.4
2.1
11.3
97.9
95.2
-32.4
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