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 withring H (i-2) -0.25 ppm
in SCAN3Da: 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 withring H3(i-1) -0.25 ppm
in SCAN3Da: 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
3.62a
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
4a
-2
8a
3-2
-14a
cis
Ala
H-
5.2
-
6.9
Pro
-3
2.3b
-2
8.2b
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


Imprint/Privacy