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
LEU-225
TYR-226
4.6
4.8
-15.8
16.3
134.7
131.2
-8.4
TYR-226
MET-227
3.1
3.0
8.6
-3.1
72.6
75.9
31.5
MET-227
THR-228
0.5
0.1
-5.4
-19.2
116.1
115.6
-49.9
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-245
GLN-246
10.3
13.6
-136.5
13.2
129.1
138.0
-377.4
GLN-246
PHE-247
11.5
11.9
-6.3
31.7
107.0
76.4
-2.0
PHE-247
VAL-248
8.9
8.7
-113.4
24.7
35.1
29.5
235.2
VAL-248
LEU-249
8.9
9.1
26.1
-32.4
76.7
73.7
7.6
LEU-249
ARG-250
8.0
8.6
-28.0
31.9
40.7
38.6
-13.1
ARG-250
ALA-251
11.0
11.4
9.2
-9.5
74.3
66.2
5.8
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