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
VAL-57
PRO-58
9.7
9.6
-5.2
3.5
67.5
69.3
4.0
PRO-58
ALA-59
7.8
7.6
-1.9
1.4
82.1
79.1
-2.6
ALA-59
GLU-60
4.0
3.8
-1.7
1.9
40.2
37.9
15.0
GLU-60
LYS-61
4.6
4.7
-5.4
4.6
99.0
96.6
-15.1
LYS-61
ALA-62
7.6
7.9
-6.4
8.7
146.1
143.3
15.7
ALA-62
TYR-63
6.1
6.4
-4.7
-1.2
77.2
76.0
10.6
TYR-63
GLY-64
4.2
4.9
4.5
-7.8
143.9
139.8
24.8
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
LEU-121
ALA-122
2.2
2.7
3.1
0.3
18.3
19.6
25.8
ALA-122
GLY-123
2.5
2.7
1.5
1.4
90.3
91.4
0.9
GLY-123
LYS-124
3.1
2.5
0.7
-0.8
138.3
135.0
-18.8
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