TABLE 1.

Secondary structures characteristics of DONPEP.2 sequence analogs^a

Analog	Conformation	Backbone RMSD (Å)	Peptide	PDB code	Chain	Residue range
SWGP			DON mimotope peptide			1–4
SWGS	Strand	0.580	Penicillin amidohydrolase	1pnk	B	64–67
SWGT	Strand	1.264	Sulfhydryl proteinase	9pap		176–179
SWGT	Strand	0.946	Xylanase	1xnb		84–87
TWGP	Strand	0.794	Bluetongue virus coat protein	1bvp	1	118–121
SFGT	Strand	0.734	Creatinase	1chm	A	325–328
SFGT	Strand	0.453	Phosphotransferase	3pmg	A	377–380
WGPF			DON mimotope peptide			2–5
FGSF	Turn	0.897	Fe(III) superoxide dismutase	1isc	A	100–103
FGSY	Strand	0.465	Beta-lactamase	2blt	A	322–325
FGSY	Strand	0.730	Flavodoxin	4fxn		85–88
FGTY	Strand	0.530	Simian virus 40 coat protein	1sva	1	221–224
WGTY	Turn	0.412	Xylanase	1xnb		85–88
FGPW	Strand	0.956	Vitelline membrane protein 1	1vmo	A	126–129
WGTW	Turn	0.820	Glycosyl transferase	1bpl	B	215–218
WGTW	Strand	0.660	Vitelline membrane protein 1	1vmo	A	70–73
GPFP			DON mimotope peptide			3–6
GPFP	Strand	1.080	Adenylosuccinate synthetase	1ade	A	276–279
GPFP	Turn	0.821	N-Cadherin	1nch	A	15–18
GPFP	Turn	0.518	Photosynthetic reaction center	1pcr	H	54–57
GPFT	Turn	0.966	Aconitase	8acn		324–327
GPFT	Turn	0.702	Monellin	1mol	A	9–12
GPYP	Strand	0.909	Dioxygenase	2pcd	M	445–448
GTFP	Strand	1.110	Black beetle virus coat protein	2bbv	C	131–134
GTFP	Turn	0.732	Glycosyl transferase	1xyz	A	806–809
PFPF			DON mimotope peptide			4–7
PFSF	Strand	1.119	N-Acetylneuraminate lyase	1nal	1	112–115
PFSY	Turn	0.888	Acid phosphatase	1kbp	A	218–221
PFTY	Strand	1.127	Dialkyglycine decarboxylase	2dkb		170–173
PYSY	Turn	0.528	Transthyretin	1ttb	A	113–116
PYTF	Strand	0.599	Dethiobiotin synthase	1dts		73–76
PYTF	Strand	0.498	Zinc endopeptidase	1iae		16–19
PYTF	Strand	0.554	Acid phosphatase	1kbp	A	127–130
TYPY	Turn	0.952	Adenylosuccinate synthetase	1ade	A	234–237
TYPY	Strand	1.086	Sulfhydryl proteinase	9pap		85–88

^aThe backbone superpositional RMSD values were based on a least-squares fit of analogs of the DON mimetic peptide, SWGPFPF, with regular secondary structure templates. Each analog was assigned the conformation of the template with which it had the lowest backbone superpositional RMSD. The analogs for SWGP start in strand conformation and then show a preference for forming a turn starting at the glycine residue. The final sections of the peptide analogs favor strand conformations.