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. 2002 Jul;11(7):1702–1713. doi: 10.1110/ps.4820102

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Fig. 2. — The distribution of discrepancies between the different alignments as a function of sequence identity. Alignment discrepancy is measured as the percentage of differently aligned residues in the shorter of two alignments. The discrepancies have been calculated for a comprehensive benchmark of protein pairs consisting of 742 protein pairs selected from the Structural Classification of Proteins (SCOP) database. (A) PSI-BLAST (Altschul et al. 1997) alignments versus FASTA (Pearson and Lipman 1988) alignments. (B) PSI-BLAST alignments versus CE (Shindyalov and Bourne 1998) structural alignments.

Fig. 2. — The distribution of discrepancies between the different alignments as a function of sequence identity. Alignment discrepancy is measured as the percentage of differently aligned residues in the shorter of two alignments. The discrepancies have been calculated for a comprehensive benchmark of protein pairs consisting of 742 protein pairs selected from the Structural Classification of Proteins (SCOP) database. (A) PSI-BLAST (Altschul et al. 1997) alignments versus FASTA (Pearson and Lipman 1988) alignments. (B) PSI-BLAST alignments versus CE (Shindyalov and Bourne 1998) structural alignments.