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. Author manuscript; available in PMC: 2009 Dec 28.
Published in final edited form as: Protein Eng Des Sel. 2005 Jun 24;18(7):309–319. doi: 10.1093/protein/gzi038

Table II.

Peptide sequences from fragment-library selection

Class 1
* MDGHPERHDAGDHHHHHGVRQ
ERHDAGDHHHHHGVRQWRLIS
RHDAGDHHHHHGVRQWRLIS
Class 2
ITNSPGRFRHHHVLARRHALYR D (6/20)
MTSAGWTAMHYISARRHAMRSMKFAQ E (2/20)
NYTTQRAEWNRQDAHRHHHQEARRGQ A1
* MKVRRDVMRWHHHHRMARRKANR B
DHHHHHGAARPVFRRGLYQKRG F
DHRHHHGVARVREQMARYV
Class 3
VTMFDVDAYFGLAVWSSGDLRAFQ
VTMFDVDAYFGLAVW (2/20)
* MFDYDAFYGYNGSAVGSPTLQHVRLQP
* MNFDEYLRLLR

Only the fragment domain of the peptides is shown. Class 1 peptides are derived from peptide C (Table I) and the putative minimal epitope is underlined. Class 2 sequences contain portions of the ARRXA motif. Conserved residues are in bold. Sequences derived from parent peptides A and B, as well as new peptides D, E, and F, are labeled. The C-terminal RGQ in the sequence derived from peptide A is encoded by part of the 3’-constant region. Class 3 peptide sequences were aligned using CLUSTALW (http://npsa-pbil.ibcp.fr) with key residues determined automatically. Clone frequency (out of 20) is shown and differing residues are italicized as described in Table I. Peptide sequences translated from alternate start codons are marked (*).