Protein Data Bank File : 1d1h Title : TOXIN 16-SEP-99 1D1H Number of Amino Acid Residues : 35 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 GLU CYS ARG TYR LEU PHE GLY GLY CYS LYS 10 THR THR SER ASP CYS CYS LYS HIS LEU GLY 20 CYS LYS PHE ARG ASP LYS TYR CYS ALA TRP 30 ASP PHE THR PHE SER Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 GLU 0.0 124.7 -179.8 -49.3 -166.3 -179.0 2 CYS -54.1 97.5 178.9 127.3 3 ARG -81.3 95.4 -179.6 -94.7 -8.2 172.9 -144.1 4 TYR -52.1 -168.5 179.6 -153.4 49.4 5 LEU -59.3 116.0 179.9 -165.5 81.0 6 PHE 86.4 28.5 179.8 -163.2 -106.4 7 GLY -103.2 126.5 179.9 8 GLY -52.8 117.0 -179.6 9 CYS -124.5 135.8 179.1 48.5 10 LYS -79.9 -19.7 179.3 -50.3 -62.7 -174.2 -124.6 11 THR -160.1 -176.0 179.1 126.4 12 THR -72.0 -29.1 -180.0 -78.9 13 SER -84.1 13.6 -179.6 95.8 14 ASP -110.7 5.6 -179.9 -79.1 26.5 15 CYS -115.9 167.5 -180.0 -51.1 16 CYS -54.4 -146.3 -177.8 -52.9 17 LYS -92.1 -71.4 -178.4 -68.0 121.2 99.0 178.6 18 HIS -61.3 -11.6 -178.8 -79.8 -75.7 19 LEU -95.1 156.5 179.0 -75.5 135.2 20 GLY -144.1 129.8 -179.2 21 CYS -77.0 123.2 -180.0 -154.5 22 LYS -106.5 117.1 -179.9 -72.9 -56.9 -134.0 -42.4 23 PHE -55.8 79.6 179.9 75.3 131.4 24 ARG -178.2 -69.7 -179.8 10.6 150.9 125.2 165.6 25 ASP -70.6 -30.8 179.7 -66.7 -19.2 26 LYS 88.3 -19.3 179.8 -146.8 72.7 112.4 -51.7 27 TYR -90.9 -167.2 -179.9 63.7 178.3 28 CYS -115.2 120.8 179.9 -52.2 29 ALA -117.8 144.9 -179.8 30 TRP -42.0 150.5 -179.8 -65.5 135.0 31 ASP 173.6 92.0 -179.8 -126.6 78.0 32 PHE 177.5 99.1 -179.7 -170.1 -126.7 33 THR 87.7 -179.9 180.0 -28.9 34 PHE -95.3 94.1 -180.0 -111.2 124.3 35 SER -166.3 67.4 0.0 178.0 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 GLU -9.322 1.140 -5.934 2 CYS -7.052 3.180 -3.666 3 ARG -6.527 0.696 -0.901 4 TYR -5.742 2.936 2.016 5 LEU -3.631 1.691 4.930 6 PHE -4.495 -1.995 5.359 7 GLY -6.358 -2.267 2.068 8 GLY -6.276 -5.503 0.102 9 CYS -4.147 -4.830 -2.968 10 LYS -3.374 -7.142 -5.885 11 THR -0.320 -5.019 -6.641 12 THR 1.441 -1.776 -5.812 13 SER -0.712 -0.001 -8.379 14 ASP -3.782 -1.147 -6.448 15 CYS -3.262 1.126 -3.438 16 CYS -3.770 4.797 -2.673 17 LYS -0.983 7.347 -2.903 18 HIS 1.153 7.296 0.218 19 LEU 0.610 3.544 0.275 20 GLY 2.515 0.814 -1.513 21 CYS 1.612 -2.840 -2.028 22 LYS 4.294 -5.193 -0.717 23 PHE 4.358 -8.704 -2.176 24 ARG 3.911 -10.395 1.204 25 ASP 1.286 -8.922 3.533 26 LYS -1.075 -8.407 0.592 27 TYR -2.266 -5.112 2.086 28 CYS -1.103 -1.554 1.521 29 ALA 1.622 -0.056 3.698 30 TRP 3.029 3.471 3.651 31 ASP 5.827 4.032 1.148 32 PHE 6.648 7.396 -0.408 33 THR 9.519 9.683 0.573 34 PHE 11.526 9.734 3.802 35 SER 8.974 9.734 6.624 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C S S S S C S S S S 10 T T T T C T T T T/S S 20 S S/T T T T S S S S S/S 30 S S S/S S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 B t T T t S 10 g G G G B S e E E 20 E e T T T t e E E E 30 e S S Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 GLU 21.1 15.2 93.9 2 CYS 38.0 38.3 64.9 3 ARG 118.8 56.9 68.7 4 TYR 41.0 22.7 67.2 5 LEU 74.5 50.4 57.2 6 PHE 23.3 14.0 77.6 7 GLY 23.5 67.4 62.9 8 GLY 5.8 16.7 73.6 9 CYS 98.8 99.6 50.0 10 LYS 19.2 11.1 82.9 11 THR 43.7 40.8 70.6 12 THR 30.1 28.2 79.2 13 SER 8.5 10.2 85.4 14 ASP 75.3 68.2 63.7 15 CYS 99.2 100.0 51.1 16 CYS 92.0 92.7 38.5 17 LYS 3.6 2.1 82.8 18 HIS 43.3 28.8 65.6 19 LEU 147.8 100.0 42.2 20 GLY 27.4 78.8 57.4 21 CYS 93.3 94.1 56.8 22 LYS 105.2 60.6 72.6 23 PHE 0.0 0.0 86.3 24 ARG 65.7 31.4 76.2 25 ASP 52.2 47.2 66.9 26 LYS 29.8 17.2 89.1 27 TYR 113.1 62.5 58.9 28 CYS 99.2 100.0 43.7 29 ALA 45.1 62.1 59.7 30 TRP 99.1 48.3 58.6 31 ASP 43.6 39.5 82.9 32 PHE 42.7 25.6 86.6 33 THR 18.6 17.4 75.5 34 PHE 0.0 0.0 87.6 35 SER 7.0 8.4 88.7