Protein Data Bank File : 1prtf Title : TOXIN 22-NOV-93 1PRT Number of Amino Acid Residues : 98 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 LEU PRO THR HIS LEU TYR LYS ASN PHE THR 10 VAL GLN GLU LEU ALA LEU LYS LEU LYS GLY 20 LYS ASN GLN GLU PHE CYS LEU THR ALA PHE 30 MET SER GLY ARG SER LEU VAL ARG ALA CYS 40 LEU SER ASP ALA GLY HIS GLU HIS ASP THR 50 TRP PHE ASP THR MET LEU GLY PHE ALA ILE 60 SER ALA TYR ALA LEU LYS SER ARG ILE ALA 70 LEU THR VAL GLU ASP SER PRO TYR PRO GLY 80 THR PRO GLY ASP LEU LEU GLU LEU GLN ILE 90 CYS PRO LEU ASN GLY TYR CYS GLU Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 LEU 0.0 64.4 -179.9 -45.4 178.4 2 PRO -60.3 81.2 179.4 -27.9 43.1 3 THR -72.8 166.5 179.1 -49.6 4 HIS -155.9 159.7 179.4 -60.6 -69.0 5 LEU -128.5 148.1 179.8 -160.3 153.5 6 TYR -138.7 113.8 179.7 -61.5 79.5 7 LYS -98.7 161.5 177.7 -69.8 174.1 162.9 -178.2 8 ASN 46.6 44.2 175.1 -51.7 -95.8 9 PHE -103.5 157.3 -179.7 -91.2 -84.2 10 THR -112.8 145.7 179.1 -92.2 11 VAL -82.9 122.3 -178.3 -138.5 12 GLN -111.2 -30.1 -178.1 -118.8 -165.5 16.0 13 GLU -133.1 142.2 179.3 -59.2 -155.9 76.2 14 LEU -139.6 134.0 -180.0 -170.1 39.8 15 ALA -155.4 130.2 178.8 16 LEU -109.2 113.1 -178.0 -176.3 45.0 17 LYS -137.2 -173.6 -177.8 -80.1 139.4 70.0 100.6 18 LEU -118.7 127.4 179.1 -146.4 41.1 19 LYS -106.8 100.1 -178.4 -175.2 -172.2 -172.3 -57.8 20 GLY 67.2 -105.6 178.8 21 LYS -130.0 35.3 178.7 -116.3 67.4 175.0 -176.0 22 ASN -130.0 142.9 179.5 -68.6 97.2 23 GLN -70.2 155.5 -179.1 -57.0 -111.8 43.5 24 GLU -163.7 134.4 175.0 -169.3 -143.9 38.5 25 PHE -129.7 150.4 -177.8 98.6 -76.0 26 CYS -143.8 154.3 177.6 -47.6 27 LEU -134.6 157.2 176.9 54.9 93.7 28 THR -120.8 119.7 178.9 -56.4 29 ALA -97.3 131.6 -178.7 30 PHE -132.6 142.1 176.5 142.6 88.8 31 MET -131.2 127.0 -177.4 -166.0 170.6 98.9 32 SER -36.4 -51.9 -179.6 -174.1 33 GLY -63.0 -6.9 -174.5 34 ARG -151.1 -157.3 -179.6 42.5 -128.5 -104.2 -154.3 35 SER -70.6 178.7 -179.6 75.5 36 LEU -99.6 137.7 179.2 -58.9 179.7 37 VAL -106.8 108.9 180.0 -173.6 38 ARG -104.9 129.5 178.8 -107.8 106.0 68.9 137.5 39 ALA -138.2 144.5 -180.0 40 CYS -126.6 144.0 179.0 -64.6 41 LEU -115.6 120.6 -178.9 -146.4 -154.1 42 SER -108.8 147.1 178.6 -62.4 43 ASP -69.4 99.7 -178.1 166.0 52.7 44 ALA -56.3 15.2 -179.0 45 GLY 79.9 -55.9 179.7 46 HIS -54.7 95.7 180.0 -82.9 179.1 47 GLU -69.6 103.9 -179.9 -155.9 62.2 -85.6 48 HIS 170.0 -30.5 179.4 159.3 -121.3 49 ASP -57.5 84.5 176.7 -82.0 -38.0 50 THR -66.3 -21.3 179.0 -68.7 51 TRP -42.3 -50.2 -178.3 -158.8 48.0 52 PHE -52.9 -53.8 -177.4 -163.2 -86.6 53 ASP -65.7 -40.0 179.7 -70.0 -74.6 54 THR -63.8 -52.9 179.8 -33.1 55 MET -62.6 -34.0 -178.8 -64.3 -68.5 -51.4 56 LEU -64.7 -44.8 -179.9 -167.3 -123.0 57 GLY -66.0 -45.7 179.9 58 PHE -56.4 -45.1 178.6 -158.7 64.0 59 ALA -65.9 -30.8 178.7 60 ILE -71.1 -39.7 177.6 -66.0 176.7 61 SER -63.3 -46.3 178.9 -50.9 62 ALA -57.9 -45.5 178.8 63 TYR -61.9 -42.7 -177.5 175.6 -86.2 64 ALA -64.4 -45.0 179.9 65 LEU -73.0 -17.4 -178.5 -65.6 165.9 66 LYS 66.2 25.2 -178.9 -68.0 -174.0 -168.4 168.6 67 SER -84.3 156.8 177.3 78.3 68 ARG -77.5 141.4 -179.5 -57.2 176.0 -171.7 60.9 69 ILE -113.6 172.6 175.7 54.3 159.8 70 ALA -132.9 117.4 -176.9 71 LEU -125.8 144.8 -179.8 76.6 -177.3 72 THR -110.8 109.9 -179.9 -60.4 73 VAL -112.4 151.1 176.2 -33.4 74 GLU -92.8 -153.1 -180.0 -163.9 -172.7 -85.2 75 ASP -137.5 154.5 179.5 -98.8 -16.6 76 SER -107.2 133.5 -179.7 55.6 77 PRO -67.4 32.4 179.6 29.9 -42.1 78 TYR -162.5 107.9 -179.9 4.5 73.0 79 PRO -55.4 158.2 -178.6 26.8 -42.7 80 GLY 76.3 19.3 -178.4 81 THR -131.4 134.0 179.4 -70.4 82 PRO -63.7 137.8 179.7 -39.9 47.8 83 GLY -88.7 173.0 -179.4 84 ASP -82.8 128.0 180.0 -161.5 85.3 85 LEU -80.8 120.6 -177.7 161.8 151.7 86 LEU -107.6 -19.6 -179.7 -40.2 95.6 87 GLU -156.8 146.6 177.3 177.5 -148.5 86.3 88 LEU -137.2 137.8 179.3 -176.5 58.7 89 GLN -133.4 130.6 -179.8 166.5 178.5 57.6 90 ILE -94.1 110.5 179.6 -65.4 165.8 91 CYS -62.4 155.3 180.0 -58.9 92 PRO -45.5 134.3 -177.7 -40.9 52.9 93 LEU -63.6 143.1 -176.6 -53.7 171.4 94 ASN 69.1 -2.4 179.6 -60.9 -64.6 95 GLY -131.4 -144.3 -177.9 96 TYR -128.2 157.0 177.2 -63.1 78.5 97 CYS -80.2 138.5 177.9 -93.8 98 GLU -78.6 144.1 0.0 82.8 -171.4 82.3 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 LEU -34.604 2.897 -19.450 2 PRO -35.841 5.611 -21.888 3 THR -32.350 6.887 -22.539 4 HIS -31.751 9.979 -24.661 5 LEU -28.904 11.835 -26.252 6 TYR -28.380 15.539 -26.607 7 LYS -25.675 16.837 -28.814 8 ASN -24.155 20.293 -28.964 9 PHE -25.536 21.440 -25.632 10 THR -23.791 23.712 -23.166 11 VAL -23.326 23.260 -19.387 12 GLN -25.076 26.154 -17.658 13 GLU -25.490 25.064 -14.080 14 LEU -23.246 22.805 -12.120 15 ALA -23.997 21.758 -8.565 16 LEU -22.645 19.488 -5.838 17 LYS -25.165 19.005 -3.059 18 LEU -26.466 16.488 -0.595 19 LYS -29.606 14.469 -1.246 20 GLY -30.713 13.409 2.187 21 LYS -27.420 11.772 3.198 22 ASN -26.030 10.912 -0.198 23 GLN -23.712 12.975 -2.287 24 GLU -25.115 14.270 -5.542 25 PHE -24.110 16.395 -8.472 26 CYS -26.102 17.797 -11.347 27 LEU -25.702 19.800 -14.450 28 THR -28.073 21.667 -16.666 29 ALA -27.298 21.353 -20.379 30 PHE -28.814 24.100 -22.404 31 MET -29.397 24.801 -26.056 32 SER -30.802 28.109 -27.260 33 GLY -33.662 26.678 -29.204 34 ARG -34.955 24.891 -26.161 35 SER -35.524 23.553 -22.704 36 LEU -32.906 22.648 -20.124 37 VAL -31.669 19.093 -19.922 38 ARG -30.984 18.340 -16.290 39 ALA -29.231 15.175 -15.269 40 CYS -27.782 14.132 -11.896 41 LEU -25.182 11.613 -10.929 42 SER -25.745 10.394 -7.400 43 ASP -23.299 8.652 -5.110 44 ALA -24.715 5.102 -5.330 45 GLY -23.795 4.351 -1.700 46 HIS -21.315 1.704 -2.893 47 GLU -18.003 3.267 -1.939 48 HIS -15.796 2.250 -4.876 49 ASP -17.672 4.102 -7.594 50 THR -14.726 6.223 -8.662 51 TRP -17.261 6.943 -11.337 52 PHE -18.707 9.743 -9.242 53 ASP -15.418 11.574 -8.880 54 THR -14.333 10.914 -12.403 55 MET -17.551 12.082 -14.005 56 LEU -17.560 14.979 -11.591 57 GLY -14.139 16.095 -12.697 58 PHE -14.973 15.504 -16.341 59 ALA -18.132 17.594 -15.920 60 ILE -16.103 20.306 -14.228 61 SER -13.684 20.369 -17.195 62 ALA -16.592 20.524 -19.622 63 TYR -17.938 23.424 -17.582 64 ALA -14.460 25.001 -17.455 65 LEU -13.652 24.745 -21.156 66 LYS -17.082 26.118 -22.122 67 SER -17.312 23.369 -24.745 68 ARG -20.503 21.947 -26.186 69 ILE -21.040 18.549 -24.742 70 ALA -23.039 15.605 -25.964 71 LEU -24.820 13.904 -23.040 72 THR -26.794 10.738 -22.487 73 VAL -29.411 10.751 -19.734 74 GLU -31.734 7.967 -18.773 75 ASP -35.085 8.930 -17.289 76 SER -36.835 9.423 -13.949 77 PRO -40.417 8.110 -13.387 78 TYR -41.631 11.561 -12.253 79 PRO -41.497 14.651 -14.517 80 GLY -39.855 17.896 -13.395 81 THR -36.996 15.743 -12.078 82 PRO -33.413 15.379 -13.403 83 GLY -32.663 12.039 -14.935 84 ASP -29.514 10.008 -14.346 85 LEU -26.424 10.956 -16.424 86 LEU -24.815 7.842 -17.944 87 GLU -22.286 9.205 -20.387 88 LEU -20.732 12.565 -21.108 89 GLN -18.775 13.640 -24.206 90 ILE -16.785 16.852 -24.754 91 CYS -17.229 18.012 -28.377 92 PRO -14.176 19.279 -30.304 93 LEU -12.988 22.448 -28.712 94 ASN -14.078 25.539 -30.594 95 GLY -16.493 23.426 -32.675 96 TYR -19.432 21.011 -32.690 97 CYS -19.977 17.409 -32.016 98 GLU -20.729 15.935 -35.356 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C S S S S S S S/S S S 10 S S S/S S S S S S/T T T 20 T/S S S S S S S S S S 30 S/T T T T/S S S S S S S 40 S S S C C C C C H H 50 H H 3 3/H H H H H H H 60 H H H H H H/S S S S S/S 70 S S S S S S S/S S S S/S 80 S S S S S S/S S S S S 90 S S/T T T T/S S S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 E E E E E E E 10 E E E E E E E E E T 20 T E E E E E E E E E 30 e T T t e E E E E E 40 E E e S t T T h H 50 H H H H H H H H H H 60 H H H H H h t e E E 70 E E E e S S S S 80 S E E E E E E E E 90 e t T T t Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 LEU 25.3 17.2 84.8 2 PRO 38.5 30.9 80.5 3 THR 61.4 57.5 55.8 4 HIS 74.1 49.3 72.0 5 LEU 72.5 49.1 65.5 6 TYR 132.1 73.0 47.3 7 LYS 86.3 49.8 70.5 8 ASN 93.7 77.5 47.4 9 PHE 164.2 98.4 46.8 10 THR 58.4 54.6 63.1 11 VAL 116.1 97.8 43.9 12 GLN 75.0 50.5 55.2 13 GLU 53.9 38.9 78.6 14 LEU 121.7 82.3 41.6 15 ALA 33.0 45.5 66.4 16 LEU 76.0 51.4 63.9 17 LYS 35.3 20.4 82.1 18 LEU 57.9 39.2 72.9 19 LYS 43.1 24.9 83.2 20 GLY 0.0 0.0 83.1 21 LYS 5.7 3.3 85.4 22 ASN 56.7 46.9 74.6 23 GLN 53.8 36.2 62.5 24 GLU 114.7 82.7 44.5 25 PHE 165.6 99.3 30.1 26 CYS 78.1 78.8 53.8 27 LEU 146.3 99.0 32.4 28 THR 103.6 96.9 44.9 29 ALA 72.6 100.0 34.6 30 PHE 110.7 66.4 62.3 31 MET 100.9 63.3 62.0 32 SER 7.7 9.2 72.8 33 GLY 0.0 0.0 72.9 34 ARG 81.4 39.0 69.9 35 SER 6.8 8.1 75.5 36 LEU 93.2 63.1 66.9 37 VAL 103.1 86.8 43.0 38 ARG 104.5 50.0 67.0 39 ALA 72.6 100.0 41.5 40 CYS 85.2 85.9 55.0 41 LEU 144.1 97.5 42.6 42 SER 50.1 60.0 58.4 43 ASP 87.2 78.9 56.3 44 ALA 18.7 25.7 86.3 45 GLY 9.0 25.9 84.0 46 HIS 4.7 3.1 87.1 47 GLU 9.3 6.7 92.0 48 HIS 0.0 0.0 88.8 49 ASP 67.1 60.8 65.9 50 THR 16.3 15.3 87.0 51 TRP 103.2 50.3 64.6 52 PHE 147.5 88.4 47.8 53 ASP 22.9 20.7 70.3 54 THR 29.3 27.5 70.5 55 MET 138.9 87.1 40.7 56 LEU 117.4 79.4 39.0 57 GLY 6.0 17.2 70.1 58 PHE 90.8 54.4 62.6 59 ALA 72.2 99.5 38.4 60 ILE 63.0 43.9 59.0 61 SER 38.4 45.9 59.6 62 ALA 72.1 99.2 42.7 63 TYR 79.3 43.8 67.0 64 ALA 25.0 34.4 69.0 65 LEU 74.1 50.1 60.3 66 LYS 10.6 6.1 93.7 67 SER 77.9 93.2 56.4 68 ARG 136.7 65.4 67.1 69 ILE 143.1 99.7 35.2 70 ALA 70.7 97.3 47.7 71 LEU 147.8 100.0 32.0 72 THR 87.9 82.3 47.7 73 VAL 111.9 94.2 45.0 74 GLU 104.0 75.1 49.5 75 ASP 63.2 57.2 62.1 76 SER 69.8 83.6 54.4 77 PRO 32.7 26.2 74.5 78 TYR 53.6 29.6 68.0 79 PRO 5.3 4.2 88.7 80 GLY 0.0 0.0 85.5 81 THR 62.2 58.2 63.9 82 PRO 85.4 68.6 60.6 83 GLY 33.3 95.8 67.8 84 ASP 52.5 47.5 67.5 85 LEU 146.9 99.4 30.6 86 LEU 94.7 64.1 61.0 87 GLU 50.6 36.5 72.8 88 LEU 146.8 99.3 30.1 89 GLN 53.2 35.8 68.7 90 ILE 119.7 83.4 44.3 91 CYS 98.5 99.3 49.5 92 PRO 39.6 31.8 75.7 93 LEU 70.7 47.9 67.1 94 ASN 0.4 0.3 87.6 95 GLY 16.6 47.8 69.2 96 TYR 54.9 30.3 76.9 97 CYS 92.8 93.5 50.4 98 GLU 0.0 0.0 95.2