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
4.8
5.4
-11.2
-0.4
97.5
90.5
-6.2
PRO-65
HIS-66
1.1
1.7
5.6
12.1
18.2
19.0
51.3
HIS-66
ASP-67
1.3
0.8
5.5
-9.4
81.9
85.1
14.8
ASP-67
PRO-68
3.9
4.0
4.2
1.5
53.1
52.0
13.3
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
3.2
3.1
-6.1
-2.2
82.3
80.4
6.2
PHE-117
ASN-118
0.6
0.8
3.1
10.2
30.8
32.3
42.4
ASN-118
HIS-119
1.5
1.4
-6.3
-0.6
84.1
85.6
18.8
HIS-119
PRO-120
5.1
5.0
-0.7
1.4
104.0
109.8
1.2
PRO-120
LEU-121
6.9
6.8
-8.5
9.9
165.0
168.8
7.3
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