Protein Data Bank File : 1vtx Title : NEUROTOXIN 13-MAR-97 1VTX Number of Amino Acid Residues : 42 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 CYS ALA LYS LYS ARG ASN TRP CYS GLY LYS 10 THR GLU ASP CYS CYS CYS PRO MET LYS CYS 20 VAL TYR ALA TRP TYR ASN GLU GLN GLY SER 30 CYS GLN SER THR ILE SER ALA LEU TRP LYS 40 LYS CYS Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 CYS 0.0 167.1 179.6 -159.9 2 ALA -130.4 161.9 -180.0 3 LYS -104.7 178.2 -179.9 -80.0 86.5 117.1 145.7 4 LYS -67.4 143.4 180.0 -63.8 143.6 87.9 -104.4 5 ARG 77.1 18.2 -179.8 -42.0 114.4 133.9 71.1 6 ASN -98.8 124.9 179.9 -77.0 -111.3 7 TRP -54.3 136.0 -180.0 -101.2 -26.8 8 CYS -102.7 155.2 -180.0 179.9 9 GLY -167.0 -123.9 180.0 10 LYS -57.5 -179.2 -179.9 63.8 -125.4 163.8 -80.6 11 THR -53.7 134.6 179.8 -177.7 12 GLU -174.0 -47.4 179.5 -153.5 -133.4 34.6 13 ASP 72.3 153.1 179.5 -147.4 -89.9 14 CYS -107.8 -175.7 -179.9 -42.5 15 CYS -97.6 102.1 -179.7 -79.2 16 CYS -37.4 147.9 0.2 43.5 17 PRO -77.3 7.0 -179.9 24.7 -24.2 18 MET -60.6 126.0 179.9 -67.7 137.3 46.6 19 LYS -133.8 144.7 -180.0 -163.8 -130.1 -137.3 159.6 20 CYS -50.8 119.5 -179.4 -85.6 21 VAL -120.3 170.1 -179.8 179.2 22 TYR -113.1 146.4 179.8 -167.8 -67.5 23 ALA -98.8 -102.7 179.4 24 TRP -152.7 -83.3 179.4 24.1 -65.7 25 TYR -81.6 5.7 -179.6 89.1 -63.0 26 ASN -132.8 80.8 179.6 -92.1 -42.6 27 GLU -51.6 -20.9 179.8 166.2 166.5 36.4 28 GLN -40.4 -33.1 -179.8 -56.9 -88.0 -102.6 29 GLY 63.3 169.9 179.9 30 SER -148.6 152.7 179.8 38.9 31 CYS -73.1 118.7 -179.8 -62.5 32 GLN -147.9 135.4 180.0 -68.9 178.6 29.8 33 SER -53.7 111.4 -179.8 79.2 34 THR -89.8 153.8 179.9 61.5 35 ILE -61.5 -42.4 179.5 -75.9 -78.3 36 SER -62.7 -18.1 179.8 80.2 37 ALA -62.6 -18.6 179.6 38 LEU -62.0 -39.6 179.5 -65.4 169.2 39 TRP -61.4 -21.6 179.6 -33.1 152.3 40 LYS -125.5 39.4 -179.6 49.8 -174.3 -70.2 137.0 41 LYS -34.4 112.6 179.9 -122.8 -93.7 118.7 -165.2 42 CYS -46.0 -26.9 0.0 -163.3 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 CYS 2.024 0.084 -1.314 2 ALA 5.787 0.167 -1.810 3 LYS 8.214 2.308 -3.803 4 LYS 11.057 1.432 -6.171 5 ARG 14.099 -0.234 -4.607 6 ASN 11.866 -1.575 -1.836 7 TRP 12.542 -5.114 -0.609 8 CYS 9.693 -7.483 -1.489 9 GLY 8.309 -10.319 0.635 10 LYS 4.906 -11.249 2.053 11 THR 1.694 -9.755 0.666 12 GLU 1.997 -5.992 0.177 13 ASP 2.238 -5.169 -3.528 14 CYS 4.104 -2.224 -5.044 15 CYS 2.986 0.945 -6.814 16 CYS 2.420 0.159 -10.494 17 PRO 4.040 -0.143 -12.788 18 MET 6.392 -1.203 -9.996 19 LYS 6.152 -4.959 -9.439 20 CYS 7.973 -7.305 -7.058 21 VAL 11.170 -8.297 -8.862 22 TYR 14.149 -10.533 -8.054 23 ALA 17.802 -9.523 -7.738 24 TRP 20.475 -12.207 -7.300 25 TYR 22.047 -12.863 -3.909 26 ASN 18.987 -11.184 -2.386 27 GLU 15.824 -13.153 -3.119 28 GLN 14.208 -10.372 -1.096 29 GLY 13.553 -8.845 -4.521 30 SER 12.568 -5.206 -5.037 31 CYS 9.733 -3.187 -6.527 32 GLN 10.679 -2.125 -10.055 33 SER 8.637 -1.101 -13.095 34 THR 8.449 -4.291 -15.150 35 ILE 8.034 -4.385 -18.922 36 SER 4.938 -6.555 -18.559 37 ALA 3.672 -3.724 -16.364 38 LEU 2.893 -1.981 -19.647 39 TRP -0.054 -4.321 -20.142 40 LYS -1.270 -2.885 -16.842 41 LYS 0.027 0.667 -17.255 42 CYS -0.395 2.140 -13.774 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 S S 10 S S S S S/T T/P T T S S 20 S S S/T T T T C S S S 30 S S S H H H H 3 3 3/S 40 S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 t T T t B S 10 S t T e E E E 20 E S S t T T t E 30 E E E e G G G G G G 40 g Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 CYS 60.4 60.9 71.3 2 ALA 65.2 89.9 55.2 3 LYS 24.8 14.3 80.0 4 LYS 86.0 49.6 65.1 5 ARG 48.1 23.0 83.7 6 ASN 69.0 57.1 66.9 7 TRP 62.3 30.4 81.2 8 CYS 77.7 78.3 59.2 9 GLY 6.5 18.6 78.2 10 LYS 8.5 4.9 85.4 11 THR 0.0 0.0 84.9 12 GLU 53.2 38.4 82.0 13 ASP 9.4 8.5 85.3 14 CYS 98.7 99.5 41.8 15 CYS 50.8 51.2 56.7 16 CYS 57.8 58.3 58.6 17 PRO 89.7 72.0 52.1 18 MET 143.0 89.7 45.0 19 LYS 65.1 37.6 77.4 20 CYS 64.4 64.9 46.2 21 VAL 74.7 62.9 72.3 22 TYR 81.1 44.8 73.2 23 ALA 44.8 61.7 62.6 24 TRP 33.9 16.6 70.4 25 TYR 47.8 26.4 72.8 26 ASN 84.6 69.9 58.6 27 GLU 20.1 14.5 80.9 28 GLN 61.3 41.3 71.4 29 GLY 32.8 94.2 64.7 30 SER 66.9 80.0 62.5 31 CYS 97.9 98.7 42.7 32 GLN 65.7 44.2 68.7 33 SER 40.6 48.6 60.1 34 THR 78.6 73.5 65.6 35 ILE 15.2 10.6 74.7 36 SER 39.7 47.5 68.8 37 ALA 72.0 99.2 58.2 38 LEU 70.9 47.9 55.6 39 TRP 49.9 24.3 73.0 40 LYS 51.7 29.8 75.0 41 LYS 53.8 31.0 76.2 42 CYS 65.0 65.5 64.9