. 2010 Nov 17;20(2):278–290. doi: 10.1002/pro.559

Table II.

Peptide Coordination in B*2705:pCAC

Peptide position	Peptide residue	Contact residue	Distance in [Å]	Interaction
p1	pSer1^N	Tyr7^OH	2.9	HB
	pSer1^N	Tyr171^OH	2.7	HB
	pSer1^OG	Arg62^NH1	3.1	HB
	pSer1^OG	Glu163(A)^OE2	2.9	HB
	pSer1^OG	*Arg145^NH2	2.8	HB
	pSer1^O	Tyr159^OH	2.6	HB
	pSer1	Trp167	∼3.4	vdW
p2	pArg2^NE	Glu45^OE1	2.8	SB
	pArg2^NH1	Thr24^OG1	2.9	HB
	pArg2^NH2	Thr24^OG1	3.1	HB
	pArg2^NH2	Glu45^OE1	2.9	SB
	pArg2^O	Glu163(A)^OE2	3.3	HB
	pArg2^O	Arg62^NH1	2.9	HB
	pArg2^NE	Glu45^OE1	2.9	SB
	pArg2^NH2	Glu45^OE1	2.9	SB
	pArg2^N	Glu63(A)^OE1	3.1	HB
	pArg2^N	Glu63(B)^OE2	2.9	HB
	pArg2^N	Glu63(B)^OE1	3.3	HB
p3	pArg3^N	Tyr99^OH	3.0	HB
	pArg3^NE	pArg5^O	2.7	HB
	pArg3^NH2	pArg5^O	2.8	HB
	pArg3	Tyr99, Leu156, Tyr159	3.6-4.0	vdW
p4	pTrp4^NE1	*pGlu253^OE2	2.8	HB
	pTrp4^O	pArg6^NH2	2.8	HB
	pTrp4	Arg62, Gln65, Ile66	3.6-4.0	vdW
p5	pArg5^NE	Gln155^OE1	3.1	HB
	pArg5^NH1	Gln155^OE1	3.0	HB
	pArg5^O	pArg3^NH2	2.8	HB
	pArg5^O	pArg3^NE	2.7	HB
p6	pArg6(B)^NH2	pArg3^O	2.8	HB
	pArg6(B)^NH1	Ile66^O	3.3	HB
p7	pTrp7	His114, Trp147, Val152, Gln155, Leu156	∼3.5	vdW
p8	pAsn8^ND2	Glu76^OE1	2.9	HB
	pAsn8^ND2	Asp77^OD1	3.0	HB
	pAsn8^O	Trp147^NE1	2.9	HB
p9	pArg9^N	Asp77^OD1	3.0	HB
	pArg9^NE	Asp116^OD2	2.8	SB
	pArg9^NH1	Asp77^OD2	2.8	SB
	pArg9^NH1	Asp74^OD1	2.9	SB
	pArg9^NH2	Asp116^OD2	2.5	SB
	pArg9^O	Lys146^NZ	3.4	HB
	pArg9^OXT	Tyr84^OH	3.0	HB
	pArg9^OXT	Thr143^OG1	2.6	HB

Only direct contacts are included, and water-mediated contacts are omitted. Distance cut-off for hydrogen bonds (HB) and salt bridges (SB) is 3.3°Å. Letters in parenthesis indicate the conformations of the amino acid side chains. Interactions between peptide residues are listed according to their first occurrence in the sequence. Interactions of amino acids to a symmetry-related B*2705:pCAC complex are indicated by an asterisk.