This is the supplementary material for the paper:
The cisProline(i-1)-Aromatic(i) Interaction: Folding of the Ala-cisPro-Tyr peptide characterized by NMR and theoretical approaches
Nardi,F., Kemmink,J., Sattler,M. and Wade,R.C.
J. Biomol. NMR (2000) 17, 63-77.

European Molecular Biology Laboratory, Heidelberg, Germany

The SCAN3D database

List of PDB structures analysed in the SCAN3D database (specified by the 4-letter code and the subunit identifier):

1iro, 2erl, 1lkk A,1ctj, 1bpi, 1arb, 1igd, 1ifc, 7rsa, 1cus, 1cse I,1cse E,1ptx, 1aac, 1plc, 1xso A,1ycc, 1rcf, 3ebx, 1rro, 4ptp, 1fus, 135l, 3sdh B,2sga, 2hbg, 2ctc, 256b A,1poa, 2end, 5p21, 2olb A,1xyz B,1eca, 2phy, 1mbd, 3b5c, 1xnb, 2mcm, 2cba, 4xis, 1flp, 4gcr, 1isu B,1tca, 1cka A,2er7 E,1ezm, 2ayh, 3pte, 2rhe, 153l, 1mla, 1tgx C,1whi, 1ptf, 2rn2, 1ppn, 1hfc, 4fgf, 1thb A,1paz, 1csh, 8tln E,2ovo, 3grs, 2sil, 1gmp A,1abe, 3chy, 1lid, 1lam, 1php, 1mrj, 1nif, 1nfp, 1snc, 1scs, 1arv, 1gai, 1fnc, 1dad, 1vsd, 1smd, 3dfr, 1htr B,1htr P,451c, 4icb, 4dfr B,1cnv, 1kap P,1phd, 2cpl, 3lzm, 1fxd, 1edg, 2mhr, 2gdm, 1knb, 2trx A,1sri B,1mba, 2dri, 1fkj, 2wrp R,1ads, 1frd, 1cpc A,1cpc L,1tta B,2utg B,1aky, 3cla, 2msb A,1ctf, 1mol B,1cot, 1gof, 2ltn C,2ltn B,2ccy B,1sbp, 1onc, 1wfa A,1nsc B,1thv, 1rop A,1din, 2bbk J,2bbk L,1iae, 1osa, 8dfr, 1pdo, 1ilk, 1nnc, 3cox, 1gca, 2aza B,1thg, 1kpt B,1vhh, 1nar, 1atl A,2gst B,1amp, 2cyr, 3tgl, 1ida A,1hbq, 1hpi, 1btl, 1mzm, 1bhp, 1ubi, 1lst, 2pii, 1chd, 2bop A,1pgs, 2cyp, 1ido, 1axn, 1hpm, 2ohx B,2tgi, 8fab D,1lau E,1pda, 9wga A,1pk4, 1tad B,1hxn, 1brn M,2sic I,1gd1 R,1mng A,2nad A,4enl, 1byb, 1hyl B,1dup A,1ept A,1tml, 1ept B,1cel A,1muc A,1glq A,1tph 2,1bbh A,2por, 1tgs I,1hyp, 1bmd B,1bdo, 1lmb 3,1pbe, 1gpr, 1tif, 1bgh, 2mnr, 1cmb B,1npk, 1ten, 2hts, 1ede, 1mml, 7aat B,1slt A,1ytb A,2abk, 1vca B,2spc A,2fx2, 1flr L,1hgx B,2lhb, 2rsp A,2cmd, 1fba A,1reg Y,1fiv A,1svb, 1ova C,1rsy, 2prd, 1lis, 1abo A,1cns A,1pnk B,1pnk A,1trk A,1rec, 2ebn, 2chs G,1dvf D,1doi, 1mpp, 1oac B,1rva B,1ukz, 1prn, 1mka A,1rcp B,1daa A,1pne, 1lts E,1lts A,1lts C,1cgt, 2hpd B,1otf A,1dpe, 1dsb B,1aoz A,1oyc, 2tsc A,1puc, 1esf A,1clc, 1gp1 B,2i1b, 1gky, 1pii, 1bam, 2dnj A,1wht A, 1wht B,1alk A,1igs, 6ins E,1acf, 2scp B,1led, 2psp B,1ris, 1lct, 2kau B, 2kau C, 2kau A, 1nba D, 1lki, 2ora, 2pia, 1rcd, 1kpb A,3il8, 1mjc, 1gsa, 1gox, 1frp A, 1fia B, 1poc, 1cdc B,1r69, 1wdc A,3rub S,3rub L,1vid, 1wdc B,1ddt, 1sra, 1cdk B,2pgd, 1ade B, 1hoe, 1pbn, 1bbp B, 1ecp B, 1cfb, 6ldh, 1btn, 1csn, 1tig

List of the configurational search hits

List of the hits with_ring H (i-2) -0.25 ppm
in SCAN3D^a:	GPF(28) 1gmp A, GPY(56) 1fus, PPF(10) 1tgx C, SPF(404) 1thg, YPF(4) 1mng A
in CSD:	PVANSB, PVANSB, ANTAML10
List of the hits with_ring H3(i-1) -0.25 ppm
in SCAN3D^a:	APY(72) 1lct, APF(284) 2olb A, APF(17) 1lst, MPF(367) 1pnk B, PPY(39) 2erl, PPF(24) 1nif, SPY(133) 1rcd, YPY(237) 1ade B, VPF(251) 3tgl
in CSD:	ALPRAL10, ANTAHC10, DUTLAF10, DUTLAF10, GIPKAR10, JUJHUR, JUXHAL, LACSUD, LINCOA, PAANTD, PAANTD01, PVANTS, SUMNOD, VEDJIX, VOWZUC
^a The three first letters give the peptide sequence; the number in parentheses is the residue number of the aromatic residue; this is followed by the PDB 4-letter code and the subunit identifier.

Table S1

¹H- and ¹³C NMR chemical shifts [ppm]^b of Ala-Pro-Tyr measured at T = 273 K
Res.		H	C	H	C	H3, H2 or H	C	H3, H2	C	H3, H2 or H, H
*trans*
Ala	i-2	8.44	50.8	4.51	17.8	1.30
Pro	i-1		63.3	4.37	31.9	1.78, 2.21	27.4	1.93, 1.20	50.4	3.60, 3.78
Tyr	i	8.33	58.0	4.46	38.7	3.02, 3.04			50.4	7.15, 6.84
*cis*
Ala	i-2	8.20	51.0	3.62^a	17.4	1.20
Pro	i-1		62.8	4.44	34.0	2.10, 2.18	24.3	1.55, 1.84	50.9	3.46, 3.36
Tyr	i	8.55	58.5	4.45	38.4	3.18, 2.88			129.9	7.14, 6.81
^a The values characteristic of the cis-transproline(i-1)-aromatic(i) interaction are given in bold. ^b The chemical shifts are given with respect to the DSS reference compound (Wishart and Sykes, 1994).

Table S2

¹H-¹H J-coupling constants [Hz] of Ala-Pro-Tyr measured at T = 273 K
*trans*
Ala	H-	5.9		-		6.9
Pro	-3	5.8		-2		8.3	3-2		-		3-3	7.0		3-2		7.0
	2-3	7.0		2-2		7.0	3-2		-		3-3	-		3-2		-
	2-3	10.40-		2-2		10.40-	3-2		-
Tyr	H-	6.8		-3		4^a	-2		8^a		3-2	-14^a
*cis*
Ala	H-	5.2		-		6.9
Pro	-3	2.3^b		-2		8.2^b	3-2		-12.6		3-3	6.7		3-2		1.4
	2-3	11.6		2-2		7.3	3-2		-12.6		3-3	8.9		3-2		9.8
	2-3	2.5		2-2		7.4	3-2		-12.0
Tyr	H-	7.2		-3		11.4	-2		4.7		3-2	-13.9
List of the inter residue ROESY peaks^c of Ala-Pro-Tyr measured at T = 273 K
*trans*	YH-P		YH-P3		Y-P3			Y-P3		Y-A			Y-A		A-P3
	A-P2
*cis*	YH-P		YH-A		Y-P3			Y-A		P-A			P-A
^a The ³J-coupling of Tyr in the trans form is extracted from the fit between experimental and simulated 1D spectra. ^b The small coupling constant found between H and H3 ( around 85) of cisPro and the larger coupling constant found between H and H2 ( around 20) of cisPro confirm the stereospecific assignment of the proline side chain. ^c The inter residue ROESY peaks are given with the one amino acid letter code plus the hydrogen type and position.

1H-NMR spectra of Ala-Pro-Tyr measured at T = 273 K

TOCSY spectra of Ala-Pro-Tyr measured at T = 273 K

ROESY spectra of Ala-Pro-Tyr measured at T = 273 K

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This is the supplementary material for the paper: The cisProline(i-1)-Aromatic(i) Interaction: Folding of the Ala-cisPro-Tyr peptide characterized by NMR and theoretical approaches Nardi,F., Kemmink,J., Sattler,M. and Wade,R.C. J. Biomol. NMR (2000) 17, 63-77.