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
LEU-166
PHE-167
3.1
2.8
-4.0
10.9
100.8
104.5
32.5
PHE-167
ARG-168
3.7
3.4
11.6
-28.8
107.2
101.8
86.3
ARG-168
HIS-169
5.8
5.4
14.4
-32.6
123.8
104.6
12.7
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
17.4
17.1
-9.3
11.8
49.0
52.0
-3.5
PRO-269
ASP-270
14.3
14.1
-5.4
32.7
104.6
98.3
38.8
ASP-270
ILE-271
10.8
10.7
13.7
-6.7
69.6
42.2
-26.7
ILE-271
ALA-272
8.0
8.0
-28.9
11.7
64.7
60.8
47.9
ALA-272
ILE-273
4.8
5.1
-9.8
1.6
128.5
134.4
-23.9
ILE-273
ASN-274
1.6
2.0
0.8
-13.1
122.5
117.6
38.3
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