Aspartate Carbamoyltransferase, Catalytic Chain
(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
ILE-224
LEU-225
4.5
4.5
2.4
2.6
97.1
88.6
-32.5
LEU-225
TYR-226
0.8
0.8
3.9
-4.0
48.6
51.0
14.4
TYR-226
MET-227
3.3
3.2
-2.4
3.4
101.3
99.8
-6.8
MET-227
THR-228
4.4
4.4
6.3
-6.2
59.2
64.3
5.3
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
ALA-251
SER-252
11.2
11.5
-10.0
3.1
139.0
142.1
-37.7
SER-252
ASP-253
14.1
14.3
-2.4
5.0
154.6
150.4
10.6
ASP-253
LEU-254
11.6
11.6
4.9
-21.3
76.7
74.9
-33.8
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