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
4.8
4.3
-3.3
11.1
133.3
135.0
20.4
GLY-64
PRO-65
2.5
2.4
0.1
-14.0
86.6
92.6
-21.4
PRO-65
HIS-66
1.3
2.0
-22.7
30.4
107.7
111.1
26.6
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
8.1
7.7
-1.0
0.5
131.1
138.3
-3.5
PRO-120
LEU-121
9.7
9.2
0.3
-3.6
46.8
50.2
-12.4
LEU-121
ALA-122
6.5
5.8
8.5
-4.6
117.3
122.1
-32.0
ALA-122
GLY-123
4.1
3.7
-165.1
178.7
106.0
104.0
52.9
GLY-123
LYS-124
2.9
4.4
22.1
-29.4
11.9
19.4
3.8
LYS-124
ASP-125
3.3
3.3
-6.6
9.1
122.3
114.6
-4.8
ASP-125
LEU-126
1.3
1.4
-1.6
9.9
131.4
129.2
14.2
LEU-126
ASP-127
2.1
1.8
12.2
-10.8
26.5
25.0
12.5
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