Table 1C.
GROUP 5 POSITIONS | CORE AND SURFACE RESIDUES CORE | SURFACES | ||
---|---|---|---|---|
6 | Val-7 | Gin-130 Thr-74 |
Gly-179 Asn-62 |
|
70 | Asn-193 Thr-74 Lys-71 Leu-24 |
Gin-130 Ala-72 Ala-57 |
||
79 | Val-80 | Val-69 | Ala-202 Glu-108 Ala-72 Asp-47 |
Gin-130 Thr-74 Pro-63 Lys-31 |
105 | Thr-178 | Ala-220 | Glu-226 Asp-211 Asp-194 Lys-128 He-106 Thr-74 Gly-50 Ser-46 Arg-28 |
Arg-213 Ala-206 Gin-130 Met-126 Met-96 Thr-61 Tyr-48 Glu-39 Glu-4 |
148 | Gly-79 | Ala-202 GLn-130 Thr-74 |
Ala-149 Glu-108 Gln-43 |
|
157 | Val-158 | Asn-193 Gin-130 Ala-72 |
Lys-190 Thr-174 |
|
173 | Val-174 | Ala-57 | Pro-212 Thr-74 Leu-24 |
Gly-79 Ala-72 |
194 | Thr-74 Ser-104 Glu-195 |
Gly-79 Gin-130 Ile-244 |
Notes: (A) It displays the core residues identified by the Talana program. The residues in each group are located at the core of the protein structure. The occurrences of valine and isoleucine are more frequent compared to other amino acids, showing that these hydrophobic amino acids potentially play a more vital role in stabilizing the chemical structure of the proteins. (B) It displays the surface residues identified using Talana. These residues are located on the surface of protein structures and are distant from each other. (C) It shows the identification of correlated mutation sets and their core and surface characteristics for group 5.