Biology Reference
In-Depth Information
162
95 N
95 CA
95 C
-39.74
-39.48
-39.35
CDRH3
31.73
33.82
35.17
10.01
8.42
6.39
96 N
96 CA
96 C
-39.48
-39.34
-39.35
33.82
35.19
35.17
8.42
7.91
6.39
97 N
97 CA
97 C
-40.06
-40.21
-38.83
36.14
36.31
36.56
5.84
4.39
3.77
98 N
98 CA
98 C
-38.18
-36.84
-36.23
37.58
37.99
38.94
4.28
3.83
4.86
99N
99 CA
99 C
-35.56
-34.89
-33.59
38.34
39.06
38.36
5.82
6.91
7.27
100N
100 CA
100 C
-32.74
-31.42
-31.58
39.10
38.62
37.84
7.95
8.39
9.70
100A N
100A CA
100A C
-32.72
-33.08
-32.61
37.20
36.38
34.94
9.80
10.97
10.75
101 N
101 CA
101 C
-32.06
-31.55
-32.69
34.39
33.01
32.04
11.82
11.83
11.66
102 N
102 CA
102 C
-32.40
-33.35
-33.52
31.12
30.08
29.06
10.65
10.23
11.35
Comparison with Experimental Results
As discussed in Chapter 1, CDRH3 of an antibody molecule confers fine
specificity. Their structures have been determined experimentally in several
antibody crystal structures (Kabat
et al
., 1991). Due to the “anchoring”
amino acid residues at the two ends of CDRH3, they all form loops (Figs. 6-
2 to 6-11), similar to the above prediction.
