Protein Data Bank File : 2pspa Title : TREFOIL FAMILY OF PEPTIDES 01-FEB-96 2PSP Number of Amino Acid Residues : 105 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 LYS PRO ALA ALA CYS ARG CYS SER ARG GLN 10 ASP PRO LYS ASN ARG VAL ASN CYS GLY PHE 20 PRO GLY ILE THR SER ASP GLN CYS PHE THR 30 SER GLY CYS CYS PHE ASP SER GLN VAL PRO 40 GLY VAL PRO TRP CYS PHE LYS PRO LEU PRO 50 ALA GLN GLU SER GLU GLU CYS VAL MET GLN 60 VAL SER ALA ARG LYS ASN CYS GLY TYR PRO 70 GLY ILE SER PRO GLU ASP CYS ALA ALA ARG 80 ASN CYS CYS PHE SER ASP THR ILE PRO GLU 90 VAL PRO TRP CYS PHE PHE PRO MET SER VAL 100 GLU ASP CYS HIS TYR Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 LYS 0.0 129.1 -179.5 -166.6 172.6 -179.8 170.1 2 PRO -74.6 155.9 178.4 -7.3 28.5 3 ALA -65.4 144.5 -176.1 4 ALA -42.0 -46.3 -179.2 5 CYS -64.6 -26.8 179.2 -55.7 6 ARG -69.9 -16.7 178.3 -52.2 174.8 66.2 -162.4 7 CYS -101.7 -54.5 -177.5 -57.9 8 SER -71.5 -24.9 -178.9 68.9 9 ARG -80.5 11.8 -179.9 -64.6 -158.4 169.3 156.6 10 GLN -105.0 145.6 176.7 -47.3 -168.3 39.2 11 ASP -75.8 124.0 179.6 -178.3 -36.8 12 PRO -48.8 -33.6 179.5 -35.9 42.8 13 LYS -72.1 -13.2 -179.3 -64.5 -58.2 -167.9 -173.5 14 ASN -100.2 -1.1 -179.2 -70.3 -24.4 15 ARG -56.5 138.4 178.6 -77.7 -179.5 -168.1 171.3 16 VAL -107.4 122.7 -177.9 -178.6 17 ASN -56.9 140.1 178.8 -177.8 63.3 18 CYS -131.6 136.7 177.6 171.8 19 GLY 81.1 -176.7 -179.3 20 PHE -90.0 160.5 179.6 52.1 -83.0 21 PRO -55.6 132.3 179.1 -29.5 42.0 22 GLY 82.0 2.7 179.0 23 ILE -60.7 138.5 -176.7 -171.7 -178.8 24 THR -78.3 167.1 178.1 64.3 25 SER -58.4 -44.9 -178.8 47.5 26 ASP -65.3 -44.3 179.5 -65.1 -49.4 27 GLN -62.9 -38.2 179.8 -73.4 175.4 -18.2 28 CYS -63.4 -49.1 179.9 178.2 29 PHE -64.7 -44.9 178.6 -80.3 -48.0 30 THR -57.0 -37.4 178.6 -67.5 31 SER -72.9 -2.8 -179.4 -66.9 32 GLY 88.7 18.6 178.5 33 CYS -114.6 174.1 -179.1 -75.3 34 CYS -102.8 143.2 178.1 -57.1 35 PHE -124.1 132.0 178.0 -176.5 84.8 36 ASP -146.7 118.6 -179.7 178.4 16.5 37 SER -101.8 10.2 -177.1 68.4 38 GLN -93.3 -18.9 -178.8 -60.5 -171.3 -74.0 39 VAL -105.3 124.5 179.9 -177.0 40 PRO -78.4 150.9 175.5 32.7 -40.5 41 GLY 74.5 10.8 179.3 42 VAL -132.9 160.8 -180.0 -62.6 43 PRO -53.6 134.0 177.4 -34.1 45.4 44 TRP -86.1 -31.5 175.6 -77.1 17.0 45 CYS -111.2 118.4 -177.4 -174.8 46 PHE -135.3 158.4 -179.6 52.4 -74.7 47 LYS -68.9 133.0 179.7 -172.6 160.5 86.2 64.1 48 PRO -74.2 160.4 175.7 27.1 -37.8 49 LEU -64.1 158.5 179.9 -75.4 170.5 50 PRO -60.0 143.3 178.2 -29.9 43.8 51 ALA -70.9 146.9 179.8 52 GLN -119.6 -178.0 179.9 -67.6 -58.5 155.1 53 GLU -55.8 -39.0 179.0 48.8 -98.4 79.5 54 SER -141.2 160.6 -179.8 57.9 55 GLU -69.8 -19.6 177.9 -142.7 -170.4 -20.0 56 GLU -70.1 -20.0 -179.0 -69.5 73.0 17.1 57 CYS -91.3 -2.4 -179.8 -71.4 58 VAL -83.8 122.2 179.1 167.3 59 MET -173.4 164.7 176.7 63.3 -164.8 66.7 60 GLN -71.0 147.1 179.8 -68.6 -174.8 145.4 61 VAL -48.8 -34.2 -178.4 137.4 62 SER -78.2 -12.5 179.7 14.3 63 ALA -92.4 -5.0 -178.2 64 ARG -64.2 129.1 176.7 -64.0 176.3 179.2 -160.3 65 LYS -104.1 116.8 -178.5 -75.2 -178.2 -58.6 -56.0 66 ASN -54.8 113.5 179.3 -158.9 -17.7 67 CYS -104.9 10.4 -177.4 167.8 68 GLY -143.6 -141.9 -178.6 69 TYR -153.2 168.5 -179.5 53.2 81.9 70 PRO -57.5 113.1 177.8 -21.8 39.3 71 GLY 96.7 6.8 179.7 72 ILE -60.2 140.6 -177.8 -179.9 170.0 73 SER -85.2 160.8 179.3 47.1 74 PRO -56.1 -49.3 -178.5 -30.8 41.1 75 GLU -62.8 -39.2 178.2 45.3 -88.9 -62.3 76 ASP -69.0 -38.2 179.3 -86.3 4.6 77 CYS -65.2 -40.3 179.1 178.0 78 ALA -66.9 -30.5 179.9 79 ALA -66.6 -46.3 179.8 80 ARG -68.5 9.2 -179.9 -103.1 146.1 100.0 126.8 81 ASN 69.1 25.6 -179.5 -163.3 30.9 82 CYS -109.1 177.8 -179.2 -61.4 83 CYS -97.0 143.4 -179.7 -53.1 84 PHE -126.5 133.9 177.7 -177.2 86.2 85 SER -159.0 115.9 -179.2 -178.7 86 ASP -112.2 30.5 -178.7 57.9 8.2 87 THR -98.8 -8.5 -179.7 63.8 88 ILE -118.3 138.6 179.7 -47.0 -62.6 89 PRO -70.4 160.6 174.6 -25.2 38.6 90 GLU 54.4 3.7 180.0 -71.1 177.7 42.8 91 VAL -114.9 152.9 179.5 -59.5 92 PRO -58.4 133.3 178.2 -32.7 44.4 93 TRP -81.1 -22.7 178.7 -66.6 -9.7 94 CYS -116.5 117.1 -174.8 -173.3 95 PHE -140.4 154.9 -178.6 57.4 -88.4 96 PHE -68.2 136.0 179.1 -67.9 -72.6 97 PRO -80.5 170.5 -178.7 34.4 -39.2 98 MET -132.2 124.3 179.3 -76.3 177.7 177.2 99 SER -57.6 146.0 -173.7 57.6 100 VAL -79.7 8.3 -178.3 -49.3 101 GLU -56.9 -31.3 179.6 -52.7 84.7 62.3 102 ASP -71.9 -23.3 -175.4 60.8 -61.2 103 CYS -69.0 139.2 -178.7 -50.5 104 HIS -163.3 170.0 177.4 59.9 -85.4 105 TYR -100.0 -177.0 0.0 -68.7 -70.6 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 LYS 42.034 24.712 61.695 2 PRO 38.762 22.669 61.425 3 ALA 35.427 24.280 62.317 4 ALA 34.583 23.895 66.028 5 CYS 31.801 21.292 65.768 6 ARG 34.107 18.907 63.886 7 CYS 36.149 18.871 67.106 8 SER 33.759 19.315 70.070 9 ARG 30.973 17.013 68.891 10 GLN 33.120 13.907 69.314 11 ASP 33.197 11.618 72.326 12 PRO 36.806 11.863 73.605 13 LYS 36.893 8.052 73.822 14 ASN 36.120 7.836 70.063 15 ARG 38.977 10.157 69.039 16 VAL 41.306 9.035 66.206 17 ASN 44.854 10.116 66.798 18 CYS 46.328 12.709 64.467 19 GLY 49.934 13.678 63.876 20 PHE 53.192 12.693 65.503 21 PRO 54.002 12.347 69.243 22 GLY 54.592 15.778 70.739 23 ILE 52.992 17.771 67.907 24 THR 52.074 21.187 69.329 25 SER 48.610 22.684 69.584 26 ASP 49.403 25.109 66.717 27 GLN 50.951 22.403 64.514 28 CYS 47.951 20.170 65.179 29 PHE 45.478 22.854 64.098 30 THR 47.596 23.882 61.124 31 SER 47.620 20.207 59.996 32 GLY 43.812 20.170 59.828 33 CYS 43.353 18.397 63.136 34 CYS 41.754 19.232 66.463 35 PHE 43.728 19.880 69.606 36 ASP 42.388 19.501 73.145 37 SER 44.654 19.275 76.225 38 GLN 41.827 18.977 78.769 39 VAL 40.745 15.356 78.725 40 PRO 43.239 12.840 80.143 41 GLY 44.044 9.466 78.556 42 VAL 42.753 10.179 75.046 43 PRO 44.444 11.640 71.971 44 TRP 45.174 15.362 72.380 45 CYS 45.587 15.918 68.592 46 PHE 42.733 14.135 66.829 47 LYS 41.053 13.859 63.432 48 PRO 38.047 16.110 62.926 49 LEU 34.611 14.691 62.086 50 PRO 33.862 14.793 58.322 51 ALA 32.875 18.223 57.043 52 GLN 29.225 18.479 56.050 53 GLU 27.126 20.759 53.837 54 SER 26.787 22.996 56.907 55 GLU 28.264 22.906 60.430 56 GLU 24.777 22.150 61.916 57 CYS 25.001 18.821 60.136 58 VAL 28.279 17.848 61.812 59 MET 27.904 15.268 64.561 60 GLN 28.862 11.715 65.381 61 VAL 26.968 9.049 63.482 62 SER 25.359 7.882 66.745 63 ALA 23.856 11.285 67.447 64 ARG 21.827 11.352 64.200 65 LYS 18.049 11.770 64.685 66 ASN 16.139 10.216 61.760 67 CYS 14.413 12.996 59.811 68 GLY 13.251 10.769 56.920 69 TYR 12.383 7.227 55.771 70 PRO 13.842 4.211 53.882 71 GLY 14.865 5.430 50.444 72 ILE 14.424 9.157 50.879 73 SER 16.220 11.092 48.234 74 PRO 18.853 13.740 48.865 75 GLU 16.524 16.481 47.455 76 ASP 13.474 15.422 49.444 77 CYS 15.626 15.282 52.542 78 ALA 16.913 18.756 51.771 79 ALA 13.299 19.912 51.329 80 ARG 12.326 18.623 54.822 81 ASN 15.112 20.867 56.153 82 CYS 17.476 17.987 56.988 83 CYS 21.045 16.750 56.577 84 PHE 21.749 13.944 54.166 85 SER 24.643 11.511 54.272 86 ASP 24.550 7.963 52.867 87 THR 28.140 6.845 53.443 88 ILE 27.817 5.058 56.803 89 PRO 25.771 1.851 57.419 90 GLU 22.854 1.410 59.840 91 VAL 22.458 5.040 60.585 92 PRO 19.728 7.345 59.201 93 TRP 20.823 8.961 55.916 94 CYS 18.469 11.922 56.449 95 PHE 18.869 13.560 59.878 96 PHE 18.024 16.658 61.906 97 PRO 20.711 19.296 62.074 98 MET 21.853 20.796 65.421 99 SER 22.435 24.478 66.031 100 VAL 26.069 25.212 66.784 101 GLU 25.934 26.955 70.205 102 ASP 27.476 23.918 71.974 103 CYS 30.555 23.880 69.730 104 HIS 33.911 25.115 71.034 105 TYR 37.649 24.360 70.952 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C C H H H H H H C C 10 T T T T/S S S S S S C 20 C C C H H H H H H H 30 H H/S S S S S S S/S S S 40 S C C S S S S S S S/S 50 S S S T T T T/S S S S/T 60 T T T/S S S S S C C S 70 S S S/H H H H H H H H 80 H S S S S S S/S S S S 90 C C S S S S S S S C 100 C S S S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 h H H H H H h t 10 g G G G g B S t 20 T T t h H H H H H H 30 h T t E E e S t T 40 T t e E E 50 S g G G G g g 60 G G G g B S t T 70 T t h H H H H H H h 80 T t E E e S t T T 90 t e E E g G 100 G G g Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 LYS 85.0 49.0 61.4 2 PRO 118.6 95.2 48.5 3 ALA 33.6 46.3 70.8 4 ALA 54.9 75.6 58.5 5 CYS 99.1 99.9 49.2 6 ARG 152.0 72.8 47.9 7 CYS 93.6 94.3 45.0 8 SER 70.9 84.8 67.2 9 ARG 191.2 91.5 54.8 10 GLN 139.8 94.1 55.1 11 ASP 50.5 45.7 66.7 12 PRO 82.6 66.3 59.0 13 LYS 35.4 20.4 83.2 14 ASN 47.1 39.0 83.2 15 ARG 198.3 94.9 48.0 16 VAL 32.1 27.0 74.9 17 ASN 41.2 34.1 74.2 18 CYS 79.0 79.6 53.4 19 GLY 17.0 48.9 54.8 20 PHE 52.1 31.2 70.0 21 PRO 6.1 4.9 81.9 22 GLY 0.0 0.0 85.7 23 ILE 135.1 94.1 49.3 24 THR 37.2 34.8 77.8 25 SER 42.8 51.2 54.1 26 ASP 4.7 4.2 84.4 27 GLN 61.3 41.3 65.4 28 CYS 99.2 100.0 42.0 29 PHE 137.0 82.2 53.5 30 THR 12.1 11.3 84.7 31 SER 37.3 44.6 68.5 32 GLY 8.8 25.3 77.9 33 CYS 89.4 90.1 39.6 34 CYS 98.7 99.5 31.0 35 PHE 134.6 80.7 46.4 36 ASP 86.6 78.4 63.7 37 SER 44.0 52.6 52.2 38 GLN 15.2 10.2 89.7 39 VAL 72.2 60.7 60.8 40 PRO 20.9 16.8 83.2 41 GLY 0.0 0.0 81.5 42 VAL 111.5 93.8 51.8 43 PRO 83.9 67.4 63.6 44 TRP 88.2 43.0 74.9 45 CYS 94.9 95.7 39.3 46 PHE 163.5 98.1 53.3 47 LYS 69.1 39.8 63.7 48 PRO 116.0 93.2 54.8 49 LEU 123.4 83.5 53.6 50 PRO 39.5 31.7 82.0 51 ALA 27.0 37.2 76.2 52 GLN 117.1 78.8 66.9 53 GLU 58.4 42.1 74.5 54 SER 39.4 47.1 71.3 55 GLU 93.0 67.1 51.5 56 GLU 75.2 54.3 62.2 57 CYS 94.0 94.7 47.2 58 VAL 116.5 98.0 45.7 59 MET 157.0 98.5 44.4 60 GLN 115.0 77.4 62.6 61 VAL 71.7 60.3 55.3 62 SER 13.7 16.3 79.7 63 ALA 35.3 48.6 66.8 64 ARG 198.1 94.8 45.4 65 LYS 74.0 42.7 68.2 66 ASN 57.2 47.3 66.8 67 CYS 92.3 93.0 48.8 68 GLY 34.8 100.0 56.7 69 TYR 92.7 51.2 69.8 70 PRO 7.4 6.0 77.8 71 GLY 1.5 4.4 78.0 72 ILE 138.7 96.7 49.6 73 SER 49.9 59.7 65.6 74 PRO 54.2 43.6 64.0 75 GLU 25.1 18.1 74.0 76 ASP 45.5 41.1 73.8 77 CYS 99.2 100.0 41.4 78 ALA 21.9 30.1 82.1 79 ALA 12.7 17.5 85.3 80 ARG 91.6 43.8 69.6 81 ASN 5.9 4.9 85.8 82 CYS 97.6 98.4 44.2 83 CYS 99.1 99.9 41.7 84 PHE 138.7 83.2 51.7 85 SER 68.5 81.9 70.9 86 ASP 56.1 50.8 54.2 87 THR 21.5 20.1 83.9 88 ILE 75.6 52.7 64.4 89 PRO 25.0 20.1 78.2 90 GLU 0.0 0.0 84.4 91 VAL 101.1 85.1 52.6 92 PRO 87.5 70.3 67.6 93 TRP 98.4 48.0 74.4 94 CYS 98.7 99.5 37.5 95 PHE 165.1 99.0 49.5 96 PHE 81.2 48.7 59.0 97 PRO 92.5 74.3 53.6 98 MET 94.0 58.9 72.8 99 SER 29.5 35.3 78.0 100 VAL 69.7 58.7 70.4 101 GLU 21.0 15.2 84.1 102 ASP 37.9 34.3 79.3 103 CYS 96.1 96.9 57.7 104 HIS 36.1 24.0 79.5 105 TYR 113.1 62.5 59.6