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
7.9
8.4
-20.1
23.6
97.4
101.1
-11.6
GLY-64
PRO-65
5.2
5.7
-19.4
0.0
105.6
96.8
-30.0
PRO-65
HIS-66
1.9
2.1
-13.2
45.9
160.0
168.3
82.4
HIS-66
ASP-67
0.2
0.1
33.7
-34.3
61.2
70.2
12.7
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
3.9
3.7
12.3
5.4
16.8
20.1
50.6
ASN-118
HIS-119
3.9
3.7
-13.0
11.6
98.5
101.9
4.0
HIS-119
PRO-120
7.1
7.1
-7.6
-3.4
100.3
112.7
-10.9
PRO-120
LEU-121
8.8
8.5
-2.1
16.1
160.9
173.4
38.6
LEU-121
ALA-122
8.5
8.4
-12.9
5.1
111.7
109.9
-1.7
ALA-122
GLY-123
4.9
4.8
21.0
-31.3
65.4
61.1
-11.2
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