Protein Data Bank File : 1c4qa Title : TOXIN 31-AUG-99 1C4Q Number of Amino Acid Residues : 69 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 THR PRO ASP CYS VAL THR GLY LYS VAL GLU 10 TYR THR LYS TYR ASN ASP ASP ASP THR PHE 20 THR VAL LYS VAL GLY ASP LYS GLU LEU ALA 30 THR ASN ARG ALA ASN LEU GLN SER LEU LEU 40 LEU SER ALA GLN ILE THR GLY MET THR VAL 50 THR ILE LYS THR ASN ALA CYS HIS ASN GLY 60 GLY GLY PHE SER GLU VAL ILE PHE ARG Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 THR 0.0 133.0 -179.1 -51.9 2 PRO -70.4 148.0 176.5 34.8 -42.5 3 ASP -66.2 137.8 179.0 -83.4 -0.3 4 CYS -109.8 -56.0 179.7 173.7 5 VAL -143.1 148.3 178.6 -74.5 6 THR -134.5 137.1 179.7 -68.2 7 GLY 161.7 -173.2 177.6 8 LYS -84.1 157.5 178.0 -57.7 -73.8 164.2 -171.9 9 VAL -77.0 119.1 -178.8 175.4 10 GLU -79.7 -41.4 175.9 179.5 -175.7 -7.3 11 TYR -163.1 162.5 176.4 58.4 83.1 12 THR -128.2 159.6 -179.2 50.7 13 LYS -146.2 134.1 176.5 172.8 166.8 -179.4 -64.2 14 TYR -92.4 129.9 -176.3 -167.0 -82.5 15 ASN -100.4 156.9 -176.3 -58.9 -41.7 16 ASP -60.1 -26.1 178.5 -168.8 57.2 17 ASP -91.3 15.4 -179.7 62.1 1.3 18 ASP 71.5 10.0 174.5 -59.5 -63.6 19 THR -84.2 171.4 -175.1 57.4 20 PHE -133.5 125.2 -178.1 -161.3 71.4 21 THR -101.6 139.0 176.2 -72.7 22 VAL -126.3 141.8 175.5 -62.3 23 LYS -111.2 118.8 179.7 172.1 81.6 -175.9 -72.9 24 VAL -134.7 131.5 -179.0 175.8 25 GLY 65.1 -127.4 179.7 26 ASP -106.5 19.1 -178.6 62.9 -6.4 27 LYS -138.7 142.4 170.9 -69.2 -178.2 -175.8 71.9 28 GLU -92.5 135.6 178.8 -80.8 -168.6 -10.8 29 LEU -134.8 150.5 -177.3 -63.3 171.0 30 ALA -130.3 148.0 -179.6 31 THR -126.3 144.8 176.4 -177.2 32 ASN -97.8 7.2 -178.8 68.3 -5.3 33 ARG -87.0 111.3 -176.3 -53.3 -61.4 175.2 90.0 34 ALA -56.8 -39.1 -177.4 35 ASN -57.0 -27.8 -176.4 -70.4 -20.2 36 LEU -78.2 -16.3 -175.2 -83.2 177.8 37 GLN -61.7 -52.0 -177.7 -61.3 173.8 -5.5 38 SER -69.0 -36.4 -179.1 57.0 39 LEU -64.5 -44.3 -179.3 -55.4 -180.0 40 LEU -67.0 -39.8 -178.4 -73.6 163.0 41 LEU -66.4 -41.3 176.9 -168.1 67.4 42 SER -58.6 -43.8 178.7 -71.0 43 ALA -61.9 -37.6 -179.5 44 GLN -66.6 -46.6 -177.3 -177.7 177.8 178.9 45 ILE -65.0 -37.0 -175.8 -71.0 175.1 46 THR -93.6 -1.9 177.1 66.6 47 GLY 74.6 27.1 178.8 48 MET -68.7 156.7 175.8 -54.9 -175.9 93.5 49 THR -94.9 127.2 178.8 -67.7 50 VAL -118.7 152.6 177.1 -58.2 51 THR -121.9 128.2 179.8 -72.3 52 ILE -109.0 129.2 179.1 -65.0 170.2 53 LYS -108.5 131.2 176.9 -66.0 170.9 147.7 -56.8 54 THR -165.9 150.4 176.8 -179.0 55 ASN -88.2 -8.2 177.5 -82.2 130.1 56 ALA -104.1 66.1 -176.9 57 CYS -87.9 75.2 -180.0 -165.1 58 HIS -154.4 162.8 -179.4 50.6 77.6 59 ASN -58.4 125.7 179.4 -161.7 -105.3 60 GLY 90.4 -0.4 178.6 61 GLY -66.0 149.3 -179.9 62 GLY -87.6 159.0 177.3 63 PHE -155.4 159.4 174.9 75.1 -85.8 64 SER -133.3 -19.0 -176.2 55.6 65 GLU -100.9 130.5 -179.2 -64.2 178.6 58.1 66 VAL -146.4 139.2 174.3 -168.1 67 ILE -109.6 131.0 179.7 -64.7 174.8 68 PHE -107.1 119.8 178.6 -61.7 -86.9 69 ARG -121.3 -47.6 0.0 -74.4 -173.3 -112.9 -104.7 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 THR -17.748 12.623 -17.966 2 PRO -20.215 9.910 -19.023 3 ASP -20.462 6.464 -17.388 4 CYS -18.876 3.872 -19.628 5 VAL -19.054 0.552 -17.757 6 THR -20.177 -0.594 -14.314 7 GLY -19.457 -3.941 -12.747 8 LYS -16.967 -6.057 -10.835 9 VAL -13.336 -6.137 -12.023 10 GLU -12.886 -9.356 -14.129 11 TYR -9.086 -9.063 -14.370 12 THR -6.356 -6.429 -14.287 13 LYS -3.152 -6.231 -16.283 14 TYR 0.112 -4.280 -15.786 15 ASN 1.417 -3.001 -19.195 16 ASP 4.934 -2.564 -20.537 17 ASP 4.428 1.213 -20.656 18 ASP 3.448 1.303 -16.965 19 THR -0.232 1.840 -17.702 20 PHE -2.817 -0.400 -16.021 21 THR -5.661 -2.218 -17.728 22 VAL -8.957 -3.255 -16.076 23 LYS -11.676 -5.400 -17.624 24 VAL -15.171 -4.399 -16.409 25 GLY -18.298 -5.397 -18.248 26 ASP -17.531 -5.841 -21.951 27 LYS -14.483 -3.590 -22.168 28 GLU -10.823 -3.448 -21.283 29 LEU -9.894 0.163 -20.358 30 ALA -6.495 1.488 -19.316 31 THR -5.213 4.244 -17.125 32 ASN -1.928 6.068 -16.880 33 ARG -2.541 7.243 -13.321 34 ALA -0.060 5.386 -11.107 35 ASN -2.134 6.069 -7.959 36 LEU -4.994 3.971 -9.331 37 GLN -3.063 0.717 -9.614 38 SER -3.201 -0.333 -5.952 39 LEU -6.755 1.033 -5.595 40 LEU -8.065 -0.970 -8.559 41 LEU -6.296 -4.210 -7.463 42 SER -7.820 -3.690 -3.953 43 ALA -11.255 -3.287 -5.635 44 GLN -10.671 -6.489 -7.564 45 ILE -9.590 -8.536 -4.489 46 THR -12.485 -7.312 -2.366 47 GLY -15.190 -7.594 -5.029 48 MET -16.251 -3.953 -5.191 49 THR -18.525 -2.666 -7.935 50 VAL -16.748 0.040 -9.922 51 THR -18.036 2.503 -12.474 52 ILE -15.493 3.837 -14.960 53 LYS -16.329 7.147 -16.615 54 THR -14.683 8.048 -19.908 55 ASN -15.404 9.610 -23.258 56 ALA -13.119 6.925 -24.887 57 CYS -15.658 4.179 -24.270 58 HIS -14.275 1.422 -26.433 59 ASN -11.975 -1.535 -25.924 60 GLY -8.529 -0.240 -25.053 61 GLY -9.873 3.222 -24.250 62 GLY -8.222 5.380 -21.628 63 PHE -9.706 6.615 -18.343 64 SER -8.904 8.479 -15.160 65 GLU -12.292 8.558 -13.408 66 VAL -13.581 5.673 -11.332 67 ILE -16.238 5.375 -8.618 68 PHE -15.629 2.586 -6.010 69 ARG -18.824 1.281 -4.366 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S S S S/S S S S C S 10 S S S S S/T T T T/S S S 20 S S S/T T T T/S S S S S 30 S S S C C H H H H H 40 H H H H H H H/S S S S 50 S S S S S C C C C S 60 S S S S S/S S S S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 e E E E E E E E E 10 E E E E e T T t e E 20 E E E E e T E E E E 30 E t T h H H H H H 40 H H H H H H h e E E 50 E E E e S t T T 60 E E e E E E E E Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 THR 73.2 68.5 74.1 2 PRO 56.4 45.3 79.2 3 ASP 49.1 44.4 70.0 4 CYS 98.4 99.2 43.1 5 VAL 105.4 88.7 54.2 6 THR 57.3 53.6 64.6 7 GLY 16.1 46.2 63.8 8 LYS 63.7 36.7 81.5 9 VAL 118.8 100.0 45.8 10 GLU 45.8 33.0 75.8 11 TYR 101.4 56.0 66.6 12 THR 99.6 93.2 42.2 13 LYS 60.4 34.8 77.5 14 TYR 78.8 43.5 76.3 15 ASN 98.4 81.4 72.5 16 ASP 0.0 0.0 90.7 17 ASP 26.3 23.8 77.9 18 ASP 28.9 26.1 84.1 19 THR 78.2 73.1 66.2 20 PHE 152.1 91.2 49.5 21 THR 96.6 90.4 56.0 22 VAL 118.7 99.9 29.9 23 LYS 132.0 76.1 61.9 24 VAL 118.7 99.9 45.4 25 GLY 7.1 20.4 73.5 26 ASP 24.6 22.3 77.1 27 LYS 129.4 74.6 61.1 28 GLU 87.1 62.8 61.3 29 LEU 147.6 99.8 38.4 30 ALA 52.6 72.5 67.9 31 THR 105.4 98.6 46.0 32 ASN 32.1 26.6 73.8 33 ARG 76.9 36.8 79.9 34 ALA 10.8 14.8 85.7 35 ASN 0.0 0.0 82.4 36 LEU 130.3 88.2 41.1 37 GLN 111.4 75.0 57.7 38 SER 9.0 10.7 78.3 39 LEU 59.1 40.0 67.7 40 LEU 147.8 100.0 25.8 41 LEU 66.4 44.9 68.8 42 SER 25.2 30.2 71.4 43 ALA 72.6 100.0 44.4 44 GLN 111.3 74.9 61.3 45 ILE 36.7 25.5 70.5 46 THR 36.1 33.7 70.4 47 GLY 8.5 24.4 79.6 48 MET 91.7 57.5 72.3 49 THR 71.1 66.5 60.3 50 VAL 118.8 100.0 36.8 51 THR 106.8 99.9 58.4 52 ILE 143.4 100.0 26.9 53 LYS 123.2 71.1 59.5 54 THR 98.6 92.3 46.9 55 ASN 25.7 21.2 71.8 56 ALA 39.3 54.1 74.6 57 CYS 66.4 67.0 59.2 58 HIS 47.5 31.6 70.3 59 ASN 47.4 39.2 71.7 60 GLY 8.1 23.2 78.3 61 GLY 32.9 94.6 65.3 62 GLY 9.3 26.9 77.6 63 PHE 160.4 96.2 42.4 64 SER 56.9 68.0 65.9 65 GLU 64.4 46.4 73.5 66 VAL 118.1 99.4 34.5 67 ILE 81.3 56.6 66.3 68 PHE 123.6 74.1 43.7 69 ARG 79.5 38.0 71.9