Endoplasmic Reticulum Aminopeptidase 1
(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
LYS-700
ALA-701
8.5
8.2
-1.1
4.1
103.2
103.2
-10.8
ALA-701
PHE-702
8.1
8.1
-10.4
6.1
52.3
57.6
46.0
PHE-702
LEU-703
6.1
5.8
-6.7
4.0
103.8
108.2
-33.1
LEU-703
ILE-704
3.7
3.5
1.1
-5.5
41.8
37.3
-7.1
ILE-704
ARG-705
2.9
3.1
5.7
-4.7
105.8
101.4
-0.6
ARG-705
LEU-706
4.7
4.8
1.8
-1.9
122.8
118.3
12.7
LEU-706
LEU-707
2.3
2.6
-4.6
4.4
122.7
128.2
26.6
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