Maltodextrin-Binding Protein (Male178 Mutant)
(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-111
ALA-112
8.5
8.6
0.3
-8.9
112.6
117.9
33.3
ALA-112
LEU-113
7.4
7.5
-7.4
-0.2
11.6
15.4
76.5
LEU-113
SER-114
7.3
7.4
-1.8
1.6
78.6
77.5
-33.2
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
PHE-258
VAL-259
11.5
11.7
10.6
-5.4
109.3
111.9
58.6
VAL-259
GLY-260
9.4
9.7
5.4
-2.1
120.9
120.8
3.8
GLY-260
VAL-261
11.3
11.6
-2.8
3.0
54.6
49.3
23.1
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
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
ILE-317
ALA-318
7.3
7.3
-7.8
11.3
110.6
107.1
-13.0
ALA-318
ALA-319
5.5
5.6
0.0
-5.9
112.4
114.2
4.3
ALA-319
THR-320
2.6
2.8
4.3
-3.7
63.4
64.4
14.0
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