Table 1.

Peptides derived from 33-mer 1 and their occupancy on DQ2. Gln -> Glu deamidation sites are underlined.

No.	Peptide sequence	%pH 5.5	%pH 7.3
1	LQLQPFPQPELPYPQPELPYPQPELPYPQPQPF	81.2	28.4
2	PFPQPELPY	1	0.1
3	PQPELPYPQ	7.2	1.7
4	LQLQPFPQPELPYPQ	59.1	14.2
5	LQLQPFPQPELPYPQPELPY	74.2	26.4
6	PQPELPYPQPELPY	30	5.4
7	PQPELPYPQPELPYPQPELPY	59.4	11.6
8	PFPQPELPYPQPELPYPQPELPYPQPQP	66.5	20.8
9	LQPFPQPELPYPQPELPYPQPELPYPQPQP	79.9	22.7
10	QLQPFPQPELPYPQPELPYPQPELPYPQPQP	78.6	23.9
11	LQLQPFPQPELPYPQPQLPYPQPQLPYPQPQPF	68	25
12	LQLQPFPQPQLPYPQPELPYPQPQLPYPQPQPF	54.9	17
13	LQLQPFPQPQLPYPQPQLPYPQPELPYPQPQPF	43.5	11.9
14	LQLQPFPQPELPYPQPELPYPQPQLPYPQPQPF	79.1	27
15	LQLQPFPQPELPYPQPQLPYPQPELPYPQPQPF	72.5	33.8
16	LQLQPFPQPQLPYPQPELPYPQPELPYPQPQPF	73.4	28.2

%_{pH 5.5} and %_{pH 7.3} are the equilibrium occupancies of the corresponding peptides in the DQ2 binding site as measured by peptide exchange assay at 37°C after 45 h at pH 5.5 and pH 7.3, respectively. The abundance of DQ2 bound peptide was calculated, from the data in Fig. 1 as the percentage (×100%) of total peptide.