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-62
TYR-63
4.4
4.2
2.3
-6.2
95.3
88.9
13.2
TYR-63
GLY-64
4.0
3.7
17.3
-13.2
29.7
30.0
-9.8
GLY-64
PRO-65
4.4
4.1
22.3
-15.4
68.1
67.1
13.2
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
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
4.4
4.8
-162.0
-179.8
54.2
40.6
-53.6
GLY-123
LYS-124
3.6
5.2
-1.4
-7.8
112.3
98.8
95.0
LYS-124
ASP-125
3.8
4.4
2.9
0.8
87.2
87.7
25.4
ASP-125
LEU-126
4.9
5.1
3.0
6.7
17.0
14.9
44.1
LEU-126
ASP-127
5.6
5.6
5.5
-3.8
82.1
80.8
27.0
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