Lysr-Type Regulatory 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
PHE-167
ARG-168
2.4
2.1
10.3
-25.4
81.7
78.4
34.6
ARG-168
HIS-169
2.8
2.4
14.5
-37.1
124.0
108.8
96.3
HIS-169
ARG-170
5.9
6.0
35.4
-43.8
75.1
79.3
32.7
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
LEU-268
PRO-269
14.8
14.6
-8.5
9.0
69.1
72.8
-16.9
PRO-269
ASP-270
11.4
11.2
-1.1
21.0
130.1
123.9
81.2
ASP-270
ILE-271
8.0
7.8
19.6
-8.7
68.1
42.7
36.3
ILE-271
ALA-272
6.5
6.4
-22.8
9.7
89.1
83.5
-2.6
ALA-272
ILE-273
3.5
4.0
-11.4
6.2
140.2
150.1
-47.2
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