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
6.3
6.1
7.1
5.7
76.0
76.4
-10.8
GLY-64
PRO-65
7.6
7.5
1.3
0.8
115.5
105.3
-9.0
PRO-65
HIS-66
9.1
9.2
1.9
-19.9
149.8
156.5
88.6
HIS-66
ASP-67
10.7
10.8
-13.7
20.3
100.2
96.1
4.6
ASP-67
PRO-68
14.2
14.4
3.4
2.8
139.3
128.8
-29.1
PRO-68
GLU-69
16.7
16.7
-10.5
-4.7
59.6
43.4
64.9
GLU-69
GLY-70
18.7
18.9
12.0
3.0
136.8
137.6
-59.6
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
PRO-120
LEU-121
5.1
5.3
-0.1
-6.9
42.3
42.8
18.5
LEU-121
ALA-122
3.2
3.4
1.6
-2.1
140.0
143.2
10.3
ALA-122
GLY-123
6.3
6.5
-4.9
0.7
77.5
72.1
19.4
GLY-123
LYS-124
6.5
6.8
0.9
4.4
92.1
88.2
-21.0
LYS-124
ASP-125
3.5
4.1
-3.0
-0.2
39.5
43.5
14.2
ASP-125
LEU-126
2.8
3.2
-2.1
9.7
119.6
120.9
12.8
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