Protein Data Bank File : 1pnh Title : TOXIN 25-AUG-93 1PNH Number of Amino Acid Residues : 31 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 THR VAL CYS ASN LEU ARG ARG CYS GLN LEU 10 SER CYS ARG SER LEU GLY LEU LEU GLY LYS 20 CYS ILE GLY VAL LYS CYS GLU CYS VAL LYS 30 HIS Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 THR 0.0 -60.8 180.0 -72.3 2 VAL -144.6 -153.1 -180.0 84.9 3 CYS -135.9 117.4 -180.0 144.8 4 ASN -69.7 97.6 -180.0 -78.7 33.2 5 LEU -56.2 -64.8 180.0 153.8 120.6 6 ARG -44.8 -41.9 180.0 -99.3 109.5 -158.2 -88.3 7 ARG -70.4 -44.4 180.0 -167.5 174.9 -103.2 -88.2 8 CYS -62.6 -46.8 180.0 120.2 9 GLN -56.7 -62.6 180.0 -70.2 -145.4 64.0 10 LEU -51.5 -31.4 -180.0 65.4 72.4 11 SER -61.3 -50.7 -180.0 -118.6 12 CYS -68.4 -41.9 -180.0 -68.0 13 ARG -46.2 -25.9 180.0 -158.5 126.0 77.0 82.7 14 SER -53.1 -40.9 180.0 -155.6 15 LEU -72.1 -23.1 -180.0 -102.8 61.9 16 GLY 119.4 -34.2 180.0 17 LEU -69.9 -157.4 -180.0 77.0 169.6 18 LEU -121.2 159.2 180.0 86.1 128.4 19 GLY -123.3 158.9 180.0 20 LYS -147.4 142.9 -180.0 -124.5 81.8 119.0 100.8 21 CYS -106.4 103.2 180.0 -136.6 22 ILE -99.9 110.6 -180.0 -87.3 103.8 23 GLY 71.3 -89.9 180.0 24 VAL -142.8 18.8 -180.0 90.4 25 LYS -135.3 121.2 -180.0 -72.0 -142.3 87.4 134.9 26 CYS -97.6 151.7 -180.0 -127.1 27 GLU -149.4 156.0 180.0 -163.2 135.0 -55.9 28 CYS -90.9 120.6 -180.0 -48.8 29 VAL -127.8 155.4 -180.0 -64.5 30 LYS -96.9 148.8 180.0 155.3 -84.8 -150.8 -76.6 31 HIS -82.2 178.4 0.0 -156.8 -78.5 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 THR 2.073 0.000 -1.245 2 VAL -0.702 -0.968 -3.630 3 CYS -4.008 -2.810 -3.697 4 ASN -4.210 -6.570 -4.080 5 LEU -6.795 -6.830 -6.833 6 ARG -7.037 -10.606 -6.747 7 ARG -7.278 -10.272 -2.985 8 CYS -9.740 -7.404 -3.172 9 GLN -11.774 -9.297 -5.742 10 LEU -11.855 -12.564 -3.833 11 SER -12.656 -10.367 -0.857 12 CYS -15.842 -9.074 -2.440 13 ARG -16.485 -12.477 -3.967 14 SER -17.138 -13.441 -0.366 15 LEU -20.509 -11.750 -0.676 16 GLY -20.961 -13.632 -3.928 17 LEU -20.677 -10.676 -6.275 18 LEU -17.457 -9.556 -7.918 19 GLY -14.745 -7.136 -6.861 20 LYS -12.504 -4.690 -8.683 21 CYS -9.421 -2.712 -7.731 22 ILE -9.672 0.787 -9.153 23 GLY -6.447 2.710 -8.676 24 VAL -5.797 1.933 -5.030 25 LYS -9.333 1.284 -3.848 26 CYS -11.170 -1.990 -4.330 27 GLU -14.940 -2.318 -4.240 28 CYS -17.601 -4.988 -4.587 29 VAL -19.520 -4.659 -7.832 30 LYS -22.112 -6.819 -9.549 31 HIS -21.681 -8.250 -13.026 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S S S/H H H H H H H 10 H H H H 3 S S S S S 20 S/T T T T/S S S S S S S/S 30 S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 h H H H H H H 10 H H H h T t S E E E 20 E E T T E E E E E 30 Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 THR 0.0 0.0 90.0 2 VAL 35.8 30.2 75.5 3 CYS 83.5 84.1 51.9 4 ASN 37.6 31.1 71.8 5 LEU 85.5 57.8 64.9 6 ARG 15.0 7.2 81.0 7 ARG 50.0 23.9 76.6 8 CYS 85.3 86.0 47.8 9 GLN 99.6 67.0 55.3 10 LEU 59.4 40.2 72.0 11 SER 29.8 35.7 67.4 12 CYS 91.2 91.9 51.7 13 ARG 52.3 25.0 80.3 14 SER 16.2 19.4 82.2 15 LEU 28.3 19.2 77.6 16 GLY 4.1 11.7 80.9 17 LEU 101.2 68.5 55.6 18 LEU 114.4 77.4 48.5 19 GLY 34.8 100.0 47.2 20 LYS 79.4 45.8 56.2 21 CYS 93.9 94.7 43.4 22 ILE 22.3 15.5 78.9 23 GLY 0.0 0.0 80.0 24 VAL 37.0 31.1 70.1 25 LYS 15.9 9.2 86.1 26 CYS 87.6 88.3 52.6 27 GLU 18.9 13.6 78.3 28 CYS 64.8 65.3 45.7 29 VAL 59.2 49.8 58.9 30 LYS 25.8 14.9 76.2 31 HIS 0.0 0.0 77.7