Acetolactate Synthase, Mitochondrial
(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
ALA-280
GLN-281
8.6
7.7
-47.8
-12.6
29.6
62.3
539.1
GLN-281
ASP-282
7.0
5.4
46.9
7.3
127.2
124.7
-356.0
ASP-282
GLU-283
10.0
8.8
15.2
-16.5
73.5
80.9
-34.7
GLU-283
PHE-284
10.7
9.4
-13.9
15.9
76.1
64.9
20.2
PHE-284
VAL-285
7.6
7.0
2.9
-3.7
167.2
168.7
8.8
VAL-285
MET-286
7.9
7.5
2.2
-5.5
100.3
100.2
-35.1
MET-286
GLN-287
11.7
11.2
3.0
0.8
74.8
80.5
-3.2
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
ASN-452
LYS-453
23.1
22.7
8.7
-8.9
56.8
59.0
-25.8
LYS-453
TRP-454
25.3
25.2
3.3
-7.4
79.7
79.4
2.1
TRP-454
LYS-455
22.5
22.8
2.4
5.4
45.8
44.8
71.4
LYS-455
LYS-456
20.0
20.1
-14.4
-10.4
160.1
160.3
-280.2
LYS-456
GLU-457
22.4
22.2
38.0
-23.4
78.1
85.5
100.4
GLU-457
TYR-458
23.3
23.9
8.7
-8.6
87.3
86.2
148.4
TYR-458
PRO-459
20.0
21.0
-16.3
22.2
106.9
115.1
108.2
PRO-459
TYR-460
17.1
18.4
-73.1
15.7
99.4
100.9
-102.0
TYR-460
ALA-461
14.3
15.9
37.5
-65.5
21.7
29.9
-333.2
ALA-461
TYR-462
16.4
15.1
-14.6
91.8
106.3
105.8
326.7
TYR-462
MET-463
15.7
14.5
25.7
-20.0
12.0
34.6
46.3
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