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
12.3
12.2
9.4
-21.4
100.8
102.3
18.4
LEU-225
TYR-226
8.9
8.8
2.8
-7.2
34.6
27.4
-19.6
TYR-226
MET-227
7.1
7.2
6.1
8.5
89.8
91.0
9.1
MET-227
THR-228
4.0
3.9
5.3
10.8
43.5
54.5
61.3
THR-228
ARG-229
1.4
1.0
-32.3
11.7
101.7
103.9
-1.2
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
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
GLN-246
PHE-247
7.9
9.0
-4.4
47.6
107.8
61.6
-28.1
PHE-247
VAL-248
6.4
5.8
-82.1
-4.1
38.0
23.1
239.9
VAL-248
LEU-249
8.6
7.9
98.5
-99.7
75.1
77.9
-5.3
LEU-249
ARG-250
9.4
10.1
-12.8
7.2
64.1
66.6
-5.5
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