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
GLU-60
LYS-61
8.6
8.6
0.8
4.2
116.0
120.6
-32.3
LYS-61
ALA-62
6.4
6.4
-3.8
3.6
131.4
127.7
-6.8
ALA-62
TYR-63
5.9
5.9
-1.4
4.1
122.6
122.1
12.3
TYR-63
GLY-64
8.3
8.3
-4.4
-3.8
90.8
93.1
-15.5
GLY-64
PRO-65
10.2
10.0
0.6
-1.4
50.8
44.1
0.9
PRO-65
HIS-66
11.6
11.5
0.7
13.5
22.6
33.1
148.3
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
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
PRO-120
LEU-121
7.6
7.2
4.2
4.8
54.4
51.1
40.4
LEU-121
ALA-122
5.5
5.3
-2.0
0.0
126.3
123.3
4.6
ALA-122
GLY-123
8.4
8.2
1.5
-1.0
92.3
94.8
17.6
GLY-123
LYS-124
8.4
8.2
0.7
-4.8
87.4
84.4
-29.0
LYS-124
ASP-125
4.9
4.6
-0.4
1.8
155.7
157.1
11.7
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