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
7.0
6.0
5.4
-3.3
90.2
88.2
-14.3
GLY-64
PRO-65
5.7
4.7
4.2
0.5
100.4
98.3
-4.9
PRO-65
HIS-66
4.1
3.7
0.5
-27.0
169.4
162.7
57.5
HIS-66
ASP-67
4.1
4.1
-12.7
23.8
84.3
80.4
2.9
ASP-67
PRO-68
7.6
7.4
-2.4
-2.2
42.6
57.3
12.0
PRO-68
GLU-69
9.7
9.6
-4.3
-10.9
37.9
22.4
32.0
GLU-69
GLY-70
11.0
11.0
17.7
5.6
133.6
130.7
-38.8
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
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
PHE-117
ASN-118
4.5
4.3
-5.4
-11.2
24.2
32.4
36.6
ASN-118
HIS-119
3.8
3.1
13.7
-3.5
90.0
83.2
11.2
HIS-119
PRO-120
4.5
3.3
7.0
-5.8
102.2
97.0
8.3
PRO-120
LEU-121
3.8
3.4
10.2
-16.8
166.5
158.3
15.6
LEU-121
ALA-122
4.7
4.1
12.3
-0.4
123.3
126.9
-15.3
ALA-122
GLY-123
2.3
1.1
-2.8
3.3
64.6
59.3
10.2
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