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
6.5
6.2
-2.8
2.8
81.1
76.9
-4.5
LYS-61
ALA-62
8.0
7.7
7.7
-17.3
150.3
155.7
44.7
ALA-62
TYR-63
6.7
6.5
6.4
-13.3
136.2
129.9
9.9
TYR-63
GLY-64
6.4
5.8
7.4
-5.1
73.2
71.4
-33.7
GLY-64
PRO-65
7.4
6.8
7.6
-0.4
86.4
83.9
-9.6
PRO-65
HIS-66
7.3
7.3
0.2
-19.5
149.9
146.1
82.1
HIS-66
ASP-67
8.3
8.4
-7.8
15.1
94.9
95.7
13.1
ASP-67
PRO-68
11.9
12.1
0.7
5.8
119.4
108.3
-18.6
PRO-68
GLU-69
14.4
14.3
-9.3
-6.9
41.8
34.5
66.5
GLU-69
GLY-70
16.3
16.5
11.5
4.5
148.0
147.9
-64.1
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
LEU-121
ALA-122
1.0
0.9
5.4
-0.9
136.9
139.1
-11.9
ALA-122
GLY-123
4.2
4.2
-4.4
5.3
53.3
48.5
4.9
GLY-123
LYS-124
4.2
4.2
-14.1
17.9
80.3
79.7
6.5
LYS-124
ASP-125
1.3
1.8
-5.3
-2.5
55.1
56.2
32.4
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