Protein Data Bank File : 1kp6a Title : TOXIN 28-MAY-99 1KP6 Number of Amino Acid Residues : 79 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 ASN ASN ALA PHE CYS ALA GLY PHE GLY LEU 10 SER CYS LYS TRP GLU CYS TRP CYS THR ALA 20 HIS GLY THR GLY ASN GLU LEU ARG TYR ALA 30 THR ALA ALA GLY CYS GLY ASP HIS LEU SER 40 LYS SER TYR TYR ASP ALA ARG ALA GLY HIS 50 CYS LEU PHE SER ASP ASP LEU ARG ASN GLN 60 PHE TYR SER HIS CYS SER SER LEU ASN ASN 70 ASN MET SER CYS ARG SER LEU SER LYS Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 ASN 0.0 161.8 -178.5 69.8 79.4 2 ASN -67.2 -39.5 -178.7 -75.8 -25.3 3 ALA -59.8 -53.2 -179.9 4 PHE -75.5 -30.0 -179.9 -81.6 57.7 5 CYS -71.8 -56.3 179.9 -180.0 6 ALA -66.8 -27.8 179.8 7 GLY -82.2 -47.9 -176.6 8 PHE -123.4 -5.0 -176.7 -48.1 -61.1 9 GLY 79.1 22.6 -179.4 10 LEU -112.9 144.6 -179.5 -63.4 176.8 11 SER 66.4 27.1 178.7 76.1 12 CYS -80.3 156.1 -179.1 -61.3 13 LYS -111.5 -14.2 -179.5 -64.8 169.5 -172.4 167.7 14 TRP -138.6 142.9 176.9 -60.8 102.2 15 GLU -130.5 114.0 -178.1 174.0 161.1 -5.2 16 CYS -127.1 163.0 178.4 -54.4 17 TRP -161.6 153.3 178.0 59.9 95.0 18 CYS -82.6 146.4 179.7 -57.7 19 THR -129.1 150.3 179.7 54.6 20 ALA -74.9 139.8 176.9 21 HIS -66.0 148.9 176.9 -79.3 -42.0 22 GLY 80.8 -50.2 179.5 23 THR -97.8 -27.0 -177.7 56.6 24 GLY 74.8 11.8 179.6 25 ASN -67.6 143.9 178.4 -74.6 -19.7 26 GLU -71.6 141.4 -178.9 -60.2 -166.0 -0.7 27 LEU -120.5 93.9 -178.2 -57.5 170.3 28 ARG -61.0 -39.9 -178.9 71.2 -178.3 -68.8 122.8 29 TYR -69.8 -36.2 177.1 -59.9 -67.9 30 ALA -68.6 -41.0 178.7 31 THR -62.5 -48.2 179.9 -61.6 32 ALA -59.8 -38.0 -179.4 33 ALA -63.4 -15.3 179.1 34 GLY -123.1 23.7 -177.7 35 CYS -134.5 172.3 179.6 -161.1 36 GLY 64.6 -120.7 180.0 37 ASP -60.5 -17.8 -178.5 -67.7 -34.8 38 HIS -90.5 -7.7 -179.3 -49.5 -83.6 39 LEU -147.1 103.3 -178.6 -179.4 56.4 40 SER -50.8 137.5 179.4 -45.1 41 LYS 75.4 11.0 179.5 -61.8 165.7 -168.4 171.3 42 SER -104.5 163.3 178.8 68.8 43 TYR -132.5 122.0 178.0 176.2 83.6 44 TYR -92.0 118.6 178.8 176.8 67.2 45 ASP -95.4 100.2 -179.4 172.1 22.6 46 ALA -63.9 -20.8 179.4 47 ARG -71.6 -45.0 179.6 -61.9 -177.2 69.6 -170.4 48 ALA -93.3 -16.7 -178.0 49 GLY 70.9 34.9 -178.2 50 HIS -121.3 156.3 178.8 -65.6 172.3 51 CYS -104.5 128.7 -179.6 -164.9 52 LEU -119.1 147.0 176.7 -65.5 84.9 53 PHE -155.1 153.7 179.7 30.5 80.9 54 SER -89.5 -56.1 175.6 -165.5 55 ASP -65.9 154.4 -179.9 -78.9 -4.5 56 ASP -81.0 95.8 -179.9 -173.4 -4.2 57 LEU -103.4 19.6 -178.9 -53.4 -177.2 58 ARG -57.1 -36.2 -179.7 -70.4 180.0 -65.9 164.0 59 ASN -64.7 -42.9 -179.4 -83.1 -0.9 60 GLN -67.3 -44.0 -179.9 -71.2 108.9 116.7 61 PHE -68.7 -34.0 179.1 -160.3 64.3 62 TYR -62.8 -46.0 179.6 175.2 81.3 63 SER -58.1 -42.0 178.9 178.1 64 HIS -62.8 -53.0 -180.0 168.2 74.4 65 CYS -60.9 -41.1 179.4 -63.3 66 SER -62.6 -38.9 179.8 -65.1 67 SER -60.1 -26.6 -179.6 72.7 68 LEU -94.2 5.7 -179.2 -60.5 -177.6 69 ASN 66.4 41.5 179.8 -163.6 48.6 70 ASN -125.3 164.3 176.8 -64.8 -35.4 71 ASN -96.4 177.6 179.7 -76.3 136.2 72 MET -135.5 138.1 177.0 174.6 -170.2 80.4 73 SER -123.5 139.5 177.7 -72.4 74 CYS -134.4 154.9 176.7 -66.8 75 ARG -121.8 131.6 176.8 -64.4 -173.3 -168.0 128.3 76 SER -83.8 129.2 -179.7 170.9 77 LEU -90.9 73.9 -177.8 -54.1 -175.7 78 SER -85.3 134.7 176.9 46.9 79 LYS -98.6 44.8 0.0 -173.8 178.8 164.8 54.0 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 ASN 11.495 7.642 26.092 2 ASN 13.193 4.319 26.789 3 ALA 10.702 3.007 29.367 4 PHE 7.623 3.260 27.175 5 CYS 9.411 2.478 23.916 6 ALA 11.197 -0.708 24.974 7 GLY 8.164 -1.603 27.064 8 PHE 5.195 -0.878 24.788 9 GLY 6.581 0.429 21.498 10 LEU 5.301 3.875 22.506 11 SER 7.164 7.211 22.427 12 CYS 9.891 5.709 20.203 13 LYS 11.927 8.027 17.964 14 TRP 13.198 5.594 15.315 15 GLU 11.681 2.684 13.399 16 CYS 14.234 0.608 11.479 17 TRP 14.526 -2.674 9.549 18 CYS 17.009 -4.637 7.448 19 THR 16.411 -4.747 3.680 20 ALA 17.631 -7.077 0.957 21 HIS 20.313 -5.872 -1.458 22 GLY 18.997 -5.517 -4.995 23 THR 15.296 -5.852 -4.292 24 GLY 15.027 -3.563 -1.287 25 ASN 12.576 -6.029 0.284 26 GLU 12.044 -5.814 4.042 27 LEU 13.566 -8.736 5.940 28 ARG 11.656 -9.477 9.131 29 TYR 13.798 -12.366 10.355 30 ALA 17.053 -10.449 9.912 31 THR 15.384 -7.491 11.661 32 ALA 14.113 -9.643 14.595 33 ALA 17.595 -11.178 15.024 34 GLY 19.041 -7.782 15.938 35 CYS 16.151 -6.410 17.988 36 GLY 14.353 -6.911 21.295 37 ASP 16.494 -9.169 23.480 38 HIS 19.350 -8.645 21.049 39 LEU 19.501 -4.889 21.420 40 SER 19.002 -3.279 24.819 41 LYS 16.320 -0.584 24.836 42 SER 14.782 -1.725 21.557 43 TYR 11.267 -2.954 20.865 44 TYR 10.562 -5.499 18.136 45 ASP 7.176 -4.929 16.564 46 ALA 6.141 -8.328 15.170 47 ARG 3.119 -6.850 13.339 48 ALA 5.255 -4.626 11.105 49 GLY 8.409 -6.718 11.433 50 HIS 10.279 -3.540 12.464 51 CYS 12.716 -2.541 15.244 52 LEU 11.926 0.567 17.302 53 PHE 13.979 2.636 19.761 54 SER 13.987 5.960 21.659 55 ASP 17.769 6.357 22.049 56 ASP 19.522 6.533 18.649 57 LEU 20.684 2.952 18.170 58 ARG 20.950 3.259 14.383 59 ASN 24.717 2.624 14.427 60 GLN 24.240 -0.572 16.323 61 PHE 21.334 -1.707 14.179 62 TYR 23.255 -0.714 11.032 63 SER 26.181 -2.905 12.082 64 HIS 23.736 -5.788 12.598 65 CYS 22.016 -5.567 9.202 66 SER 25.441 -5.135 7.547 67 SER 26.890 -8.207 9.277 68 LEU 24.130 -10.171 7.515 69 ASN 24.938 -8.495 4.187 70 ASN 21.748 -6.440 4.198 71 ASN 20.998 -2.731 4.007 72 MET 19.046 -0.774 6.642 73 SER 16.119 1.640 6.333 74 CYS 14.858 3.848 9.129 75 ARG 11.959 6.260 9.633 76 SER 12.306 9.166 12.048 77 LEU 9.201 9.278 14.252 78 SER 8.917 13.064 14.155 79 LYS 6.269 15.212 15.824 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 H H H H H H H H C C 10 S S S S/S S S S S S S/T 20 T T T S S S S/H H H H 30 H H H H H/T T T T/S S S 40 S/S S S S S/T T T T S S 50 S S S/T T T T H H H H 60 H H H H H H H H H/S S 70 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 h H H H H H H H h 10 S e E E E E E E t 20 T T T t B h H H H 30 H H h G g G G G g T 40 e E E E E T T T T E 50 E E E e S h H H H 60 H H H H H H H h T t 70 E E E E E E e Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 ASN 46.6 38.5 72.3 2 ASN 80.6 66.6 68.3 3 ALA 7.1 9.8 80.6 4 PHE 67.8 40.7 68.3 5 CYS 99.2 100.0 57.2 6 ALA 49.1 67.7 69.5 7 GLY 9.0 25.8 72.4 8 PHE 54.8 32.9 66.5 9 GLY 32.2 92.7 45.8 10 LEU 43.0 29.1 70.7 11 SER 37.5 44.8 77.7 12 CYS 98.6 99.4 46.4 13 LYS 58.3 33.6 82.0 14 TRP 159.1 77.6 59.8 15 GLU 118.0 85.1 45.6 16 CYS 99.2 100.0 30.5 17 TRP 184.1 89.8 51.3 18 CYS 99.2 100.0 41.8 19 THR 96.4 90.2 58.5 20 ALA 52.1 71.7 66.4 21 HIS 77.1 51.3 86.4 22 GLY 0.0 0.0 81.7 23 THR 36.2 33.8 79.8 24 GLY 7.2 20.7 80.9 25 ASN 30.7 25.4 76.7 26 GLU 70.8 51.1 71.4 27 LEU 95.3 64.5 66.9 28 ARG 118.4 56.7 70.6 29 TYR 13.6 7.5 82.8 30 ALA 60.1 82.7 52.3 31 THR 106.9 100.0 47.4 32 ALA 46.4 63.9 60.8 33 ALA 31.6 43.5 70.0 34 GLY 30.9 88.9 55.5 35 CYS 99.2 100.0 46.7 36 GLY 18.5 53.1 71.4 37 ASP 0.0 0.0 87.8 38 HIS 53.3 35.5 79.4 39 LEU 123.4 83.5 54.0 40 SER 1.2 1.4 82.0 41 LYS 76.3 44.0 71.6 42 SER 83.6 100.0 46.3 43 TYR 115.0 63.5 64.9 44 TYR 144.7 79.9 51.6 45 ASP 76.7 69.5 52.6 46 ALA 22.9 31.5 74.9 47 ARG 0.0 0.0 92.9 48 ALA 39.0 53.7 76.2 49 GLY 34.1 98.1 61.4 50 HIS 144.4 96.1 52.9 51 CYS 99.2 100.0 36.9 52 LEU 131.7 89.1 49.2 53 PHE 166.8 100.0 36.6 54 SER 81.6 97.6 58.2 55 ASP 55.0 49.8 73.0 56 ASP 61.3 55.5 70.4 57 LEU 130.6 88.4 52.2 58 ARG 119.0 57.0 56.1 59 ASN 2.0 1.6 83.9 60 GLN 66.9 45.0 61.7 61 PHE 166.3 99.7 36.1 62 TYR 61.0 33.7 72.2 63 SER 17.8 21.3 75.9 64 HIS 112.8 75.1 57.9 65 CYS 98.8 99.6 45.0 66 SER 48.8 58.3 72.1 67 SER 23.8 28.5 78.7 68 LEU 80.2 54.2 72.1 69 ASN 16.3 13.5 84.5 70 ASN 104.1 86.1 49.4 71 ASN 48.4 40.0 77.2 72 MET 138.1 86.6 43.8 73 SER 42.1 50.4 63.5 74 CYS 90.2 90.9 35.9 75 ARG 88.4 42.3 70.9 76 SER 39.2 46.9 61.9 77 LEU 97.6 66.0 67.5 78 SER 18.7 22.4 88.7 79 LYS 0.0 0.0 94.0