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
LYS-61
ALA-62
2.6
3.0
-1.3
-12.1
53.3
56.4
71.7
ALA-62
TYR-63
3.5
3.5
-16.5
24.1
112.0
109.1
-19.6
TYR-63
GLY-64
7.2
7.3
-13.2
19.1
115.7
116.8
15.6
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
LYS-124
ASP-125
9.1
8.9
-14.8
5.9
76.9
74.3
18.5
ASP-125
LEU-126
6.6
6.6
-9.7
12.8
130.8
129.4
9.1
LEU-126
ASP-127
3.0
3.0
-8.9
6.0
107.7
110.7
4.7
ASP-127
PHE-128
2.2
2.4
-32.3
31.8
102.6
102.8
8.5
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