Protein (Eukaryotic Peptide Chain Release Factor Subunit 1)
(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
ASP-142
ASP-143
6.3
6.8
-23.9
-7.6
86.8
97.2
43.2
ASP-143
SER-144
3.3
3.3
35.6
-21.1
77.3
60.3
31.1
SER-144
LYS-145
1.2
1.3
25.0
9.6
32.0
34.3
49.1
LYS-145
PHE-146
2.2
2.0
-19.0
12.7
84.0
78.5
3.8
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
GLU-273
VAL-274
11.3
12.7
44.5
-26.8
79.8
67.9
-11.2
VAL-274
LEU-275
10.4
10.7
-128.2
165.9
35.7
78.7
-47.3
LEU-275
SER-276
7.3
7.4
-18.7
57.5
99.2
134.4
38.7
SER-276
ASN-277
7.3
6.8
27.2
13.4
9.2
35.3
72.8
ASN-277
VAL-278
6.9
6.0
-37.8
-5.1
102.0
87.9
7.1
VAL-278
LYS-279
5.3
3.8
-14.1
21.8
141.4
128.0
12.2
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