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
7.3
7.8
-18.5
22.4
90.6
94.0
-7.9
GLY-64
PRO-65
4.8
5.5
-18.8
0.5
99.5
90.0
-17.3
PRO-65
HIS-66
1.9
2.3
-17.1
47.4
157.0
162.9
67.2
HIS-66
ASP-67
1.2
1.2
9.9
-16.6
67.2
74.6
8.0
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
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
ASP-116
PHE-117
3.2
3.1
3.6
-13.7
89.8
96.2
3.1
PHE-117
ASN-118
1.7
1.3
11.8
4.8
24.0
27.9
42.0
ASN-118
HIS-119
2.1
1.8
-11.1
10.3
94.6
95.3
4.3
HIS-119
PRO-120
5.6
5.3
-2.6
3.2
105.7
116.2
1.5
PRO-120
LEU-121
7.4
7.0
-15.4
19.1
167.6
178.4
8.0
LEU-121
ALA-122
7.6
7.2
-11.2
3.6
117.7
114.8
5.7
ALA-122
GLY-123
3.9
3.7
-4.8
0.5
127.7
125.9
6.8
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