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-59
GLU-60
5.3
5.4
1.4
-7.2
47.0
48.5
-13.9
GLU-60
LYS-61
4.4
4.7
5.5
8.0
100.9
98.2
-23.4
LYS-61
ALA-62
1.9
1.6
-2.4
-13.6
13.9
19.5
106.8
ALA-62
TYR-63
3.0
3.1
-15.2
23.3
81.8
84.9
-49.7
TYR-63
GLY-64
6.7
6.7
-14.8
20.3
127.5
128.2
6.7
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
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-122
GLY-123
9.7
10.2
18.3
-28.0
106.5
102.3
48.5
GLY-123
LYS-124
10.0
10.4
13.0
-8.5
71.0
62.5
11.8
LYS-124
ASP-125
8.2
8.4
-20.1
14.4
63.8
68.2
30.5
ASP-125
LEU-126
6.4
6.7
7.3
-3.7
35.8
33.8
20.2
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