Carboxy Terminus Of Hsp70-Interacting 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
ASP-220
GLU-221
4.3
2.4
-45.8
2.0
120.9
22.8
19.8
GLU-221
LYS-222
2.2
1.6
-156.2
10.6
66.4
47.4
-85.2
LYS-222
ARG-223
3.4
4.7
-5.1
-32.5
132.1
78.4
-14.4
ARG-223
LYS-224
3.5
4.8
-50.7
25.5
72.1
47.4
10.7
LYS-224
LYS-225
4.8
2.9
-159.8
-55.7
74.2
20.9
-113.1
ASP-220
GLU-221
11.0
4.0
-45.8
2.0
84.3
133.3
-15.1
GLU-221
LYS-222
7.4
6.7
-156.2
10.6
143.4
144.0
159.4
LYS-222
ARG-223
4.6
4.7
-5.1
-32.5
75.2
128.5
-0.5
ARG-223
LYS-224
4.2
3.8
-50.7
25.5
121.8
120.8
-13.9
LYS-224
LYS-225
6.9
7.6
-159.8
-55.7
134.2
137.9
146.9
LYS-225
ARG-226
7.3
7.4
18.5
-43.0
32.6
44.9
-16.3
ASP-220
GLU-221
4.3
2.4
-45.8
2.0
120.9
22.8
19.8
GLU-221
LYS-222
2.2
1.6
-156.2
10.6
66.4
47.4
-85.2
LYS-222
ARG-223
3.4
4.7
-5.1
-32.5
132.1
78.4
-14.4
ARG-223
LYS-224
3.5
4.8
-50.7
25.5
72.1
47.4
10.7
LYS-224
LYS-225
4.8
2.9
-159.8
-55.7
74.2
20.9
-113.1
ASP-220
GLU-221
11.0
4.0
-45.8
2.0
84.3
133.3
-15.1
GLU-221
LYS-222
7.4
6.7
-156.2
10.6
143.4
144.0
159.4
LYS-222
ARG-223
4.6
4.7
-5.1
-32.5
75.2
128.5
-0.5
ARG-223
LYS-224
4.2
3.8
-50.7
25.5
121.8
120.8
-13.9
LYS-224
LYS-225
6.9
7.6
-159.8
-55.7
134.2
137.9
146.9
LYS-225
ARG-226
7.3
7.4
18.5
-43.0
32.6
44.9
-16.3
ARG-226
ASP-227
4.8
5.9
151.0
-164.4
40.2
43.4
-17.6
ASP-227
ILE-228
6.5
7.5
-24.6
1.8
145.4
116.6
-5.3
ILE-228
PRO-229
5.8
6.4
2.9
7.6
59.9
68.8
0.1
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