Tryptophan Rna-Binding Attenuator Protein-Inhibitory 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
GLU-9
VAL-10
4.6
4.6
3.2
-2.0
101.8
103.2
-1.6
VAL-10
ALA-11
0.8
0.8
7.4
5.8
22.5
21.8
44.6
ALA-11
CYS-12
1.7
1.6
0.9
6.1
93.2
87.8
10.4
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
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
GLY-31
LYS-32
6.3
6.6
63.0
-27.6
68.7
69.6
31.5
LYS-32
GLY-33
5.0
5.1
9.2
-7.0
84.0
75.5
16.0
GLY-33
VAL-34
2.0
2.1
19.2
-14.4
15.6
16.1
35.6
VAL-34
ILE-35
2.5
2.7
-6.3
-0.6
121.4
120.4
8.7
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