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
7.7
7.1
2.6
0.2
100.8
101.7
-3.8
PRO-65
HIS-66
5.7
5.3
-0.3
-10.5
6.3
10.9
38.7
HIS-66
ASP-67
4.7
4.3
-9.3
13.2
74.9
75.3
2.7
ASP-67
PRO-68
8.0
7.6
-5.7
-3.9
38.6
44.8
35.8
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
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
2.5
2.2
1.4
4.6
93.9
91.5
-0.2
PHE-117
ASN-118
5.3
5.0
-3.0
-6.3
18.0
23.1
36.3
ASN-118
HIS-119
5.0
4.6
8.4
-2.2
98.9
92.8
14.3
HIS-119
PRO-120
6.5
6.0
2.8
-3.4
106.9
101.3
5.8
PRO-120
LEU-121
5.4
5.0
8.2
-11.0
170.6
164.9
10.3
LEU-121
ALA-122
5.8
5.4
10.0
-0.1
114.0
118.6
-19.6
ALA-122
GLY-123
4.2
3.5
0.4
6.2
115.1
119.3
0.7
GLY-123
LYS-124
1.7
1.1
-5.3
6.3
61.9
58.9
-7.1
LYS-124
ASP-125
3.1
3.3
3.6
-3.2
142.8
141.9
26.0
ASP-125
LEU-126
4.6
4.9
-7.2
11.0
95.2
102.7
5.1
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