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
GLY-64
PRO-65
5.8
6.2
-16.2
0.7
92.9
88.7
-21.7
PRO-65
HIS-66
2.2
2.6
-17.4
36.9
156.4
153.8
102.6
HIS-66
ASP-67
2.0
1.8
0.6
-3.4
84.2
89.8
21.5
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
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-115
ASP-116
6.2
6.2
-3.6
15.1
154.4
150.9
57.6
ASP-116
PHE-117
4.1
4.0
5.0
-9.0
95.4
102.4
6.4
PHE-117
ASN-118
0.6
0.5
8.7
-1.5
36.9
40.7
50.1
ASN-118
HIS-119
2.2
2.2
-2.7
8.1
77.7
75.7
-19.8
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