. 2004 Jan 19;199(2):271–281. doi: 10.1084/jem.20031690

Table II.

Comparison of Peptide Coordination in the p4α and p6α Binding Modes of B^*2705:pVIPR

	p4α conformation				p6α conformation
Peptide residue	Atom	Contact residue	Distance	Interaction	Atom	Contact residue	Distance	Interaction
			Å				Å
pArg1	all contacts formed by pArg1-p4α are identical to those observed in -p6α conformation
pArg2	all contacts formed by pArg2-p4α are identical to those observed in -p6α conformation
pLys3
	pLys3^N ^*	Tyr99^OH ^*	3.02	H bond	pLys3^N ^*	Tyr99^OH ^*	2.96	H bond
	pLys3^O ^‡	pArg6^NH1 ^‡	3.00	H bond	pLys3^O ^*	Tyr99^OH ^*	3.43	H bond
	pLys3^NZ ^‡	pArg5^O ^‡	2.78	H bond	pLys3^NZ ^‡	pTrp4^O ^‡	2.82	H bond
pTrp4	solvent exposed				solvent exposed
	pTrp4^O ^‡	pArg6^NH2 ^‡	3.00	H bond	pTrp4^O ^‡	pLys3^NZ ^‡	2.82	H bond
					pTrp4 ^‡	pArg6 ^‡	∼3.3	v.d. Waals
pArg5	solvent exposed
	pArg5^NH1 ^§	Gln155^OE1 ^§	3.20	H bond	pArg5^NH1 ^*	Asp116^OD1 ^*	3.04	salt bridge
	pArg5^O ^‡	pLys3^NZ ^‡	2.78	H bond	pArg5^NH2 ^*	Asp116^OD2 ^*	3.10	salt bridge
pArg6					solvent exposed
	pArg6^NH1 ^¶	Ile66^O ^¶	2.74	H bond	pArg6 ^‡	pTrp4 ^‡	∼3.3	v.d. Waals
	pArg6^NH1 ^‡	pLys3^O ^‡	3.00	H bond
	pArg6^NH2 ^‡	pTrp4^O ^‡	3.00	H bond
pTrp7
	pTrp7 ^§	Val152 ^§	∼3.5	v.d. Waals	pTrp7 ^§	Leu156 ^§	∼3.5	v.d. Waals
pHis8	all contacts formed by pHis8-p4α are identical to those observed in -p6α conformation
pLeu9	all contacts formed by pLeu9-p4α are identical to those observed in -p6α conformation

Only direct contacts are included, and water-mediated interactions are omitted. Interacting atoms are specified for polar interactions only because v.d. Waals contacts are too numerous and less specific.

β-sheet floor.

^‡

Intrapeptide contacts.

^§

Helix α2.

^¶

Helix α1.