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
ARG-165
LEU-166
3.1
3.0
-17.5
25.9
73.1
70.2
20.7
LEU-166
PHE-167
4.8
4.6
1.9
0.5
86.9
79.2
-11.5
PHE-167
ARG-168
4.7
4.3
5.1
-23.5
102.0
101.1
76.7
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
15.6
15.5
8.4
4.6
132.6
129.7
-39.1
PRO-269
ASP-270
12.7
12.5
8.4
12.5
69.6
80.0
49.0
ASP-270
ILE-271
9.4
9.2
-5.6
6.6
108.8
134.6
-33.4
ILE-271
ALA-272
6.3
6.4
-19.5
-10.4
61.5
59.7
71.9
ALA-272
ILE-273
3.2
3.4
-16.4
15.6
133.6
132.5
5.8
ILE-273
ASN-274
0.2
0.3
0.6
-8.5
123.8
120.1
12.1
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