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
4.3
4.0
-4.9
12.2
153.6
155.8
22.5
GLY-64
PRO-65
2.1
2.0
-0.5
-14.6
102.1
99.5
-25.8
PRO-65
HIS-66
2.0
2.1
-18.7
28.8
91.7
96.7
12.6
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
9.3
9.5
-6.0
-6.0
118.2
124.3
-18.1
PRO-120
LEU-121
10.2
10.2
13.6
-6.5
76.3
72.6
9.9
LEU-121
ALA-122
6.6
6.4
6.9
-3.2
140.1
143.2
-60.7
ALA-122
GLY-123
5.2
5.4
-139.3
146.9
80.8
80.1
29.7
GLY-123
LYS-124
4.5
5.9
25.8
-34.2
32.7
40.7
34.0
LYS-124
ASP-125
4.8
5.0
-11.9
17.6
110.2
110.0
24.8
ASP-125
LEU-126
3.8
3.9
15.4
-6.6
22.3
26.5
37.3
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