Putative Abc Transporter, Periplasmic Binding Protein, Amino Acid
(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
SER-134
TRP-135
8.1
8.2
3.1
-7.2
140.3
138.0
3.9
TRP-135
SER-136
5.1
5.5
-4.4
23.2
120.1
112.0
17.3
SER-136
GLY-137
1.5
2.0
-16.8
-15.4
52.5
39.4
40.1
GLY-137
ALA-138
2.1
2.5
8.3
11.3
56.1
64.8
25.2
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
ALA-224
PRO-225
7.3
7.7
-22.5
-1.0
105.9
105.2
-20.1
PRO-225
ALA-226
6.8
8.6
35.4
20.2
114.8
84.6
-12.9
ALA-226
ASP-227
6.3
7.5
-20.1
17.1
126.6
126.4
13.6
ASP-227
GLU-228
5.7
5.3
-22.1
26.1
112.2
76.6
-1.1
GLU-228
LYS-229
2.1
3.3
-29.2
-32.1
41.9
36.1
75.1
LYS-229
VAL-230
1.1
2.5
1.1
-22.6
72.1
82.2
1.3
VAL-230
GLY-231
3.7
3.1
4.2
-20.4
119.8
130.5
22.4
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