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
PRO-65
HIS-66
0.6
0.7
-0.3
7.5
176.6
174.6
19.3
HIS-66
ASP-67
0.5
0.4
4.9
-8.7
72.6
73.8
-2.4
ASP-67
PRO-68
3.0
3.0
3.2
8.0
29.6
27.8
49.6
PRO-68
GLU-69
4.5
4.7
-5.0
4.0
138.3
136.2
-11.6
GLU-69
GLY-70
5.9
5.9
-6.2
-1.1
117.5
119.4
-19.9
GLY-70
VAL-71
3.4
3.4
3.3
0.5
41.0
41.7
14.3
VAL-71
GLN-72
1.7
1.8
-2.4
4.2
140.2
139.8
18.3
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
2.7
2.6
-3.0
-6.0
105.6
104.6
-10.6
PHE-117
ASN-118
5.1
5.0
3.1
8.9
13.5
8.4
46.0
ASN-118
HIS-119
4.5
4.3
-3.3
-1.4
100.1
104.1
14.0
HIS-119
PRO-120
7.5
7.3
-2.8
5.1
90.3
98.5
12.0
PRO-120
LEU-121
8.6
8.7
-8.3
9.2
152.2
159.8
9.8
LEU-121
ALA-122
8.5
8.4
-6.9
-0.5
113.7
110.3
-14.7
ALA-122
GLY-123
4.8
4.7
-1.6
2.0
102.6
104.3
9.2
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