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, 1987] calculated for the amino acid residues at the column corresponding to the mutation site in the multiple sequence alignment of the target human protein sequence with its homologs. These scores were calculated using the PROPHECY program (available in the EMBOSS suite) [Rice et al., 2000]. We calculated and G (a,b) scores for both wild-types as well as mutations. In addition, we also considered the differences in the and G (a,b) scores of wild-types and mutations. The MSAs used for calculating the amino acid frequencies for both and G (a,b)scores were obtained using ClustalW-2 [Chenna et al., 2003] and no further manual curation was done to the alignments. The homologs of the target human sequence were identified by PSI-BLAST [Altschul et al., 1997] searches on the nonredundant (NR) database with an E-value 1 × 10–15 with 3–4 rounds of iteration until convergence is reached. see more From PSI-BLAST hits, homologs shorter than 70% of the query sequence length were removed before considering them for multiple sequence alignment by ClustalW-2. While searching for homologs we made sure that only the relevant domain containing the given mutation was used as the query. Domain boundaries were identified using ProDom [Servant et al., 2002] (http://prodom.prabi.fr/profom/current/html/home.php). We considered secondary structural status and solvent accessibility status of the amino acid residues at the mutation sites. These structural features at the mutation sites were extracted for both wild-type and mutant amino acid residues from the predictions made on the target human protein using ACCpro (solvent accessibility) and SSpro v4.5 (secondary structural status) of the SCRATCH suite [Cheng et al., 2005]. All the residues with predicted solvent accessibility values