Peptide Abc Transporter, Periplasmic Peptide-Binding Protein
(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
TYR-240
PRO-241
7.2
7.4
-1.1
0.7
46.8
45.7
4.5
PRO-241
ALA-242
7.3
7.2
-16.5
4.6
70.7
75.7
15.8
ALA-242
ALA-243
4.6
4.1
3.1
-5.1
130.8
136.8
9.7
ALA-243
GLY-244
1.7
1.9
-16.3
-17.2
64.9
68.4
26.6
GLY-244
THR-245
2.0
2.2
40.2
0.7
63.4
53.9
44.8
THR-245
GLN-246
5.2
5.5
7.5
-2.1
66.1
64.1
-0.9
GLN-246
ALA-247
7.9
8.0
-2.1
-2.5
92.9
92.9
-3.0
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
VAL-482
MET-483
10.7
10.8
9.2
-9.7
100.8
102.5
0.5
MET-483
SER-484
7.1
7.2
-1.5
0.4
133.0
133.2
0.9
SER-484
GLY-485
3.9
3.9
-21.5
-20.0
48.9
47.9
53.8
GLY-485
ALA-486
1.0
1.9
23.8
-29.5
98.0
77.2
10.2
ALA-486
TRP-487
2.6
3.0
12.6
15.8
68.0
82.7
16.8
TRP-487
MET-488
6.0
6.6
-42.0
29.3
34.1
32.2
19.3
MET-488
TYR-489
8.2
8.0
5.3
5.0
79.1
76.9
3.1
TYR-489
GLN-490
11.4
11.4
6.5
-1.8
145.1
143.9
-6.9
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