Protein Data Bank File : 1c6w Title : TOXIN 23-DEC-99 1C6W Number of Amino Acid Residues : 33 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 GLY ASP CYS LEU PRO HIS LEU LYS LEU CYS 10 LYS GLU ASN LYS ASP CYS CYS SER LYS LYS 20 CYS LYS ARG ARG GLY THR ASN ILE GLU LYS 30 ARG CYS ARG Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 GLY 0.0 54.3 -180.0 2 ASP -120.7 63.7 -179.8 42.5 45.5 3 CYS -89.2 64.4 179.8 -61.4 4 LEU -55.0 164.1 -175.1 -57.7 177.6 5 PRO -90.2 -87.9 179.8 32.2 -23.2 6 HIS -70.3 162.4 179.6 164.2 -78.1 7 LEU -71.3 69.6 -179.6 61.4 153.9 8 LYS -70.3 158.5 -179.9 -169.8 -172.7 -53.7 -60.7 9 LEU -70.4 136.5 179.9 30.9 154.1 10 CYS -142.0 178.8 179.9 88.5 11 LYS -117.8 -42.9 179.9 -78.0 111.0 -66.2 84.3 12 GLU -118.6 156.9 -180.0 -175.5 175.4 -64.8 13 ASN -62.4 -46.9 179.8 58.2 80.0 14 LYS -39.2 -32.5 179.8 -176.9 178.0 -66.7 -60.1 15 ASP -39.2 -37.5 179.8 -179.2 67.9 16 CYS -115.2 153.2 179.2 -94.3 17 CYS -62.5 -37.7 179.9 -76.6 18 SER -70.9 -6.1 -179.7 -61.6 19 LYS 27.8 42.3 179.7 -62.3 -172.3 -61.8 72.4 20 LYS -135.6 69.3 -180.0 177.2 55.8 60.3 178.2 21 CYS -103.1 133.9 -179.3 178.3 22 LYS -127.4 144.4 -179.6 -58.4 -63.5 -61.9 -177.7 23 ARG -117.8 69.8 -179.9 42.1 75.5 53.4 115.3 24 ARG -96.0 56.8 -180.0 -54.6 -58.6 -58.1 -119.2 25 GLY -138.2 -167.0 179.8 26 THR -87.0 -54.1 179.7 53.4 27 ASN -71.0 164.6 179.6 -61.2 61.0 28 ILE -70.8 -19.5 180.0 -58.6 175.3 29 GLU -38.4 97.6 -179.4 -65.2 179.9 -69.6 30 LYS -92.0 131.0 -179.3 -153.3 162.2 64.5 175.6 31 ARG -92.2 150.6 -179.0 -53.5 -58.5 -177.6 -120.8 32 CYS -86.1 100.9 179.3 -101.6 33 ARG -117.5 -2.4 0.0 -45.4 -60.1 -61.4 -121.0 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 GLY 2.158 -0.419 -1.809 2 ASP 3.036 3.182 -1.252 3 CYS 6.577 3.067 0.118 4 LEU 7.173 6.706 -0.786 5 PRO 10.667 8.255 -0.251 6 HIS 10.689 11.707 1.335 7 LEU 8.146 12.949 3.911 8 LYS 5.701 14.022 1.171 9 LEU 2.357 15.719 1.857 10 CYS -0.562 13.380 2.578 11 LYS -4.078 13.430 4.071 12 GLU -4.261 9.982 5.726 13 ASN -1.479 7.853 7.293 14 LYS -2.196 4.911 4.934 15 ASP -0.663 7.142 2.233 16 CYS 2.719 5.654 3.132 17 CYS 3.845 2.083 3.772 18 SER 5.388 3.502 6.953 19 LYS 1.827 4.733 7.712 20 LYS 3.177 7.415 10.050 21 CYS 2.388 10.697 8.346 22 LYS 1.859 13.785 10.589 23 ARG 0.471 17.314 10.011 24 ARG 1.955 19.456 12.792 25 GLY 1.546 22.464 10.568 26 THR -1.262 24.818 9.590 27 ASN -2.368 23.056 6.388 28 ILE -3.578 19.423 6.435 29 GLU -0.387 18.676 4.442 30 LYS 0.728 15.664 6.422 31 ARG 4.351 14.590 5.889 32 CYS 5.246 10.924 5.412 33 ARG 7.210 9.301 8.251 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C C S S S S S S S S 10 S C C C C T T T T/S S 20 S S S S C C C S S S 30 S S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S e E E 10 S g G G G g T T t E 20 E E S S S S E 30 E E E Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 GLY 0.0 0.0 79.7 2 ASP 66.7 60.4 65.4 3 CYS 25.2 25.4 70.9 4 LEU 100.3 67.9 55.0 5 PRO 35.9 28.8 71.9 6 HIS 39.9 26.6 68.8 7 LEU 89.2 60.3 62.0 8 LYS 88.0 50.7 59.3 9 LEU 56.2 38.0 70.6 10 CYS 99.2 100.0 49.6 11 LYS 44.2 25.5 74.9 12 GLU 50.2 36.2 70.8 13 ASN 53.5 44.2 65.7 14 LYS 43.2 24.9 80.1 15 ASP 72.2 65.3 61.7 16 CYS 94.4 95.1 56.7 17 CYS 67.3 67.8 59.3 18 SER 22.6 27.0 75.7 19 LYS 70.6 40.7 79.8 20 LYS 51.3 29.6 77.0 21 CYS 99.2 100.0 48.6 22 LYS 66.3 38.2 66.5 23 ARG 100.9 48.3 67.9 24 ARG 28.4 13.6 82.9 25 GLY 4.7 13.6 78.4 26 THR 0.0 0.0 90.1 27 ASN 32.1 26.5 83.5 28 ILE 39.6 27.6 79.6 29 GLU 75.1 54.2 69.5 30 LYS 149.1 86.0 55.9 31 ARG 126.5 60.6 59.5 32 CYS 98.4 99.2 42.6 33 ARG 75.8 36.3 69.0