Protein Data Bank File : 1qky Title : NEUROTOXIN 17-AUG-99 1QKY Number of Amino Acid Residues : 38 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 ASP GLU ALA ILE ARG CYS THR GLY THR LYS 10 ASP CYS TYR ILE PRO CYS ARG TYR ILE THR 20 GLY CYS PHE ASN SER ARG CYS ILE ASN LYS 30 SER CYS LYS CYS TYR GLY CYS THR Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 ASP 0.0 -100.5 179.5 -80.9 75.5 2 GLU -142.4 122.4 -172.9 172.2 162.2 64.2 3 ALA 49.4 -161.0 172.6 4 ILE -139.1 129.4 175.2 -61.9 -66.5 5 ARG -119.1 169.8 -172.9 -61.0 -153.9 -154.6 -86.5 6 CYS -142.7 138.0 173.0 38.8 7 THR -59.0 -37.5 173.6 -46.8 8 GLY -170.8 179.1 179.9 9 THR -42.0 -57.7 -173.9 -47.9 10 LYS -69.0 -22.6 175.3 -68.7 177.4 65.4 -175.8 11 ASP -74.3 -37.4 -178.2 -161.3 82.9 12 CYS -59.0 -28.8 176.2 -171.3 13 TYR -56.0 -31.2 -178.7 -55.8 -19.5 14 ILE -63.6 -69.0 -178.2 -53.7 168.3 15 PRO -64.9 -26.1 173.0 27.1 -35.8 16 CYS -61.0 -59.2 179.9 -164.9 17 ARG -66.8 -21.0 173.0 -173.5 141.0 59.5 -171.8 18 TYR -78.5 -43.1 -175.3 -130.0 -85.0 19 ILE -91.4 -74.9 179.8 -60.5 160.7 20 THR -58.3 -31.0 -177.9 -77.2 21 GLY 81.5 -52.4 172.9 22 CYS -61.8 157.3 -172.4 -64.8 23 PHE -91.1 -47.7 -171.9 -171.0 83.7 24 ASN -48.8 101.2 -174.7 -173.9 18.5 25 SER -141.4 168.7 -174.5 42.5 26 ARG -153.1 147.2 172.2 -135.1 -81.4 175.7 170.6 27 CYS -100.4 134.5 172.9 -72.3 28 ILE -141.4 130.6 -172.7 -165.8 72.4 29 ASN 46.1 51.1 -173.3 -65.7 -76.4 30 LYS 55.3 4.6 -172.9 -153.2 -161.8 165.0 -176.9 31 SER -98.9 130.8 173.5 -48.6 32 CYS -69.4 146.2 172.3 -83.0 33 LYS -140.7 117.8 172.8 -65.9 -62.7 -167.6 73.1 34 CYS -99.1 138.7 172.9 -55.0 35 TYR -81.9 -18.4 -172.7 -67.8 -88.5 36 GLY 108.9 -154.3 173.4 37 CYS -72.7 156.9 176.4 -84.3 38 THR -54.2 129.9 0.0 43.1 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 ASP 6.473 -2.802 12.800 2 GLU 6.654 0.896 11.685 3 ALA 4.380 2.335 8.952 4 ILE 3.835 0.171 5.823 5 ARG 6.210 0.433 2.818 6 CYS 6.075 -1.051 -0.714 7 THR 8.597 -2.230 -3.362 8 GLY 6.245 -0.428 -5.799 9 THR 2.544 0.225 -6.507 10 LYS 1.602 -3.407 -7.339 11 ASP 3.426 -4.729 -4.252 12 CYS 1.501 -2.288 -1.987 13 TYR -1.752 -4.035 -2.945 14 ILE -0.520 -6.988 -0.805 15 PRO -0.315 -5.330 2.700 16 CYS -3.267 -3.084 1.729 17 ARG -5.504 -6.107 0.999 18 TYR -3.952 -7.926 4.015 19 ILE -4.451 -5.051 6.556 20 THR -7.044 -2.591 5.176 21 GLY -8.710 -5.492 3.227 22 CYS -9.986 -2.940 0.730 23 PHE -7.890 -2.421 -2.432 24 ASN -7.654 1.339 -3.322 25 SER -4.018 2.217 -2.418 26 ARG -0.986 4.329 -3.414 27 CYS 2.786 4.403 -2.677 28 ILE 4.283 7.771 -1.585 29 ASN 7.942 8.032 -0.319 30 LYS 7.980 4.178 -0.671 31 SER 5.146 4.197 1.963 32 CYS 1.760 2.572 1.324 33 LYS -1.390 4.663 1.789 34 CYS -4.799 2.974 1.387 35 TYR -7.855 5.171 0.781 36 GLY -10.068 2.259 1.922 37 CYS -12.639 0.685 -0.382 38 THR -13.523 2.400 -3.659 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C S S S S S S H H H 10 H H H 3 3/T T T T C C 20 S S S S C C T T T T/S 30 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 S B S h H H 10 H H H H H H H H H h 20 t S e E E E E T T 30 E E E E e Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 ASP 0.0 0.0 94.4 2 GLU 0.0 0.0 86.6 3 ALA 23.4 32.2 73.9 4 ILE 78.1 54.4 57.4 5 ARG 81.8 39.1 73.7 6 CYS 96.9 97.7 46.1 7 THR 14.5 13.5 80.1 8 GLY 4.2 11.9 71.7 9 THR 38.0 35.5 68.0 10 LYS 16.3 9.4 80.2 11 ASP 57.4 51.9 68.4 12 CYS 98.6 99.4 44.1 13 TYR 122.2 67.5 58.3 14 ILE 35.8 24.9 76.2 15 PRO 96.3 77.4 50.2 16 CYS 97.2 97.9 54.5 17 ARG 69.7 33.3 76.1 18 TYR 14.0 7.8 82.7 19 ILE 49.6 34.6 68.5 20 THR 67.6 63.2 55.8 21 GLY 8.5 24.4 78.6 22 CYS 68.2 68.7 57.9 23 PHE 90.3 54.1 66.1 24 ASN 68.3 56.5 58.7 25 SER 83.6 100.0 48.1 26 ARG 73.9 35.4 70.4 27 CYS 84.7 85.4 53.0 28 ILE 60.0 41.8 77.8 29 ASN 0.9 0.8 82.8 30 LYS 54.1 31.2 73.4 31 SER 69.4 83.0 63.1 32 CYS 96.1 96.9 40.4 33 LYS 47.6 27.5 74.1 34 CYS 87.0 87.7 53.1 35 TYR 56.3 31.1 80.3 36 GLY 15.3 44.1 60.9 37 CYS 32.7 32.9 70.4 38 THR 11.9 11.2 82.4