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
TYR-63
GLY-64
6.3
7.2
-2.7
5.1
94.5
99.1
-4.8
GLY-64
PRO-65
4.7
5.5
-2.3
-1.1
104.9
103.5
1.7
PRO-65
HIS-66
3.1
3.5
2.0
20.7
8.7
3.6
62.9
HIS-66
ASP-67
2.8
2.9
11.4
-12.6
75.4
75.9
2.6
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
PHE-117
ASN-118
3.5
3.7
4.7
7.3
19.4
16.2
35.6
ASN-118
HIS-119
2.9
3.3
-10.0
3.5
92.4
99.0
13.3
HIS-119
PRO-120
4.8
5.4
-6.9
1.9
95.7
104.2
3.2
PRO-120
LEU-121
5.3
5.7
-6.1
14.7
156.3
167.9
24.7
LEU-121
ALA-122
5.4
5.9
-12.7
-1.7
119.8
114.4
-17.8
ALA-122
GLY-123
2.1
2.8
-0.6
-3.7
115.0
112.5
6.1
GLY-123
LYS-124
1.3
0.7
3.1
-9.6
63.1
63.5
-15.2
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