Table 1.
Amino Acid | Residue # | Ratio (%) | In/Out |
---|---|---|---|
ILE | 239 | 16.5 | i |
ALA | 240 | 0 | i |
GLN | 241 | 39.1 | |
SER | 242 | 78.5 | o |
LEU | 243 | 6.3 | i |
CYS | 244 | 4.1 | i |
GLY | 245 | 13.5 | i |
GLU | 246 | 56.4 | o |
ASP | 247 | 3.6 | i |
LEU | 248 | 7.8 | i |
ILE | 249 | 25.5 | |
ILE | 250 | 0.1 | i |
Using the NMR data from Lukavsky et al.20 and an algorithm developed by Braun et al.44, the solvent accessibility of the putative NES was calculate (hydrophobic residues bolded). The first two columns are the amino acid identity and residue number. The third is the side chain surface area, normalized to a “random coil” of that residue. Resides are classified as solvent exposed if this normalized value exceeds 50% (labelled “o”) and buried if the normalized value is less than 20% (labelled “i”).