Chemotaxis Protein Chea
(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
GLY-453
ILE-454
8.8
8.7
63.0
-73.9
142.9
130.6
78.5
ILE-454
ASP-455
6.2
6.2
-170.7
142.8
44.2
32.7
148.7
ASP-455
LYS-456
6.0
6.2
-4.1
12.7
77.9
66.7
-17.0
LYS-456
GLU-457
3.1
3.2
6.5
2.9
158.3
168.3
-70.2
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
PHE-491
SER-492
10.2
9.9
-120.6
101.7
109.7
73.4
-94.0
GLY-504
VAL-505
20.3
20.0
-6.8
-55.2
82.0
60.7
582.0
VAL-505
GLY-506
17.1
18.9
157.8
158.5
161.9
88.4
-1378.5
GLY-506
MET-507
15.7
15.2
-60.0
-119.3
67.7
34.7
961.2
MET-507
ASP-508
12.9
13.3
17.6
-6.0
93.4
103.2
-34.4
ASP-508
VAL-509
15.8
14.5
16.8
-6.6
142.6
124.3
-44.3
VAL-509
VAL-510
18.2
17.8
17.3
-9.3
152.9
168.3
-68.2
VAL-510
LYS-511
15.6
16.2
9.3
-9.4
101.7
116.8
-20.7
LYS-511
ASN-512
14.7
14.7
18.7
7.2
100.9
92.9
-69.5
ASN-512
VAL-513
18.4
18.3
-8.1
1.9
35.1
31.7
24.4
VAL-513
VAL-514
19.7
19.7
-8.8
2.3
38.5
36.1
31.3
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