Protein Data Bank File : 1htrp Title : ASPARTYL PROTEASE 21-OCT-94 1HTR Number of Amino Acid Residues : 43 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 ALA VAL VAL LYS VAL PRO LEU LYS LYS PHE 10 LYS SER ILE ARG GLU THR MET LYS GLU LYS 20 GLY LEU LEU GLY GLU PHE LEU ARG THR HIS 30 LYS TYR ASP PRO ALA TRP LYS TYR ARG PHE 40 GLY ASP LEU Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 ALA 0.0 154.5 176.5 2 VAL -118.7 116.1 179.9 174.2 3 VAL -123.6 148.3 -176.3 -44.6 4 LYS -116.3 130.5 179.8 158.9 154.3 84.8 173.4 5 VAL -106.4 121.1 179.6 168.2 6 PRO -72.9 144.2 178.8 7.1 -10.1 7 LEU -114.7 154.5 177.0 -62.3 -178.3 8 LYS -128.3 154.3 -176.6 -72.5 -167.1 144.4 -151.4 9 LYS -94.3 135.3 -178.2 168.8 112.3 154.3 -156.9 10 PHE -134.3 177.5 -179.1 -68.3 78.9 11 LYS -76.0 142.0 177.7 -75.6 -81.6 -169.6 23.0 12 SER -80.5 161.5 178.3 68.9 13 ILE -58.3 -40.0 -177.9 -68.5 162.3 14 ARG -60.0 -41.8 -178.8 -170.3 -164.8 -64.4 -100.6 15 GLU -65.8 -48.4 179.7 -77.9 177.6 71.5 16 THR -60.4 -43.6 176.9 -59.6 17 MET -63.5 -36.1 177.0 -68.0 175.3 75.0 18 LYS -61.4 -46.5 -179.6 179.8 125.8 146.9 -172.7 19 GLU -63.3 -33.4 -178.5 -98.2 -177.3 3.1 20 LYS -91.5 5.4 -178.9 -38.9 -73.9 -131.0 29.2 21 GLY 66.1 31.6 178.0 22 LEU -108.9 -5.4 -174.6 -48.6 155.8 23 LEU -55.1 -60.4 -177.3 -176.9 59.9 24 GLY -39.2 -57.3 -175.5 25 GLU -79.1 -19.9 178.5 65.6 169.7 58.9 26 PHE -76.1 -35.3 -178.2 168.2 -72.6 27 LEU -60.1 -41.0 -176.7 -89.6 -162.0 28 ARG -99.1 17.4 177.8 -50.9 155.4 -14.0 -156.2 29 THR -120.0 -6.2 -178.9 -87.6 30 HIS -126.4 127.4 179.7 -68.2 71.6 31 LYS -111.2 143.9 -179.6 -171.8 -75.4 -154.6 59.5 32 TYR -148.2 141.0 174.7 178.5 65.0 33 ASP -115.4 123.5 -179.4 -177.2 -51.3 34 PRO -52.7 -26.9 -178.4 -20.4 31.2 35 ALA -70.2 -12.9 -179.3 36 TRP -66.8 -16.2 178.8 -67.2 -18.1 37 LYS -66.9 -27.4 -176.9 -178.8 171.9 177.9 -168.2 38 TYR -105.0 14.9 -171.2 -42.6 -68.9 39 ARG -55.2 -35.6 -178.0 -58.2 -155.4 63.5 -144.6 40 PHE -65.3 155.2 179.0 -37.9 64.6 41 GLY -117.4 -17.7 -179.9 42 ASP -76.9 174.8 178.7 54.1 29.4 43 LEU -120.7 -140.2 0.0 -72.6 135.8 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 ALA 15.610 12.351 3.095 2 VAL 19.228 11.831 4.101 3 VAL 21.227 15.010 3.560 4 LYS 24.829 15.673 3.874 5 VAL 26.459 18.880 4.881 6 PRO 30.098 19.178 3.904 7 LEU 32.558 20.435 6.525 8 LYS 35.790 22.239 5.888 9 LYS 38.719 22.458 8.132 10 PHE 39.755 25.935 9.247 11 LYS 42.236 27.277 11.741 12 SER 41.318 26.901 15.379 13 ILE 41.268 29.800 17.755 14 ARG 44.224 28.093 19.454 15 GLU 46.209 27.952 16.301 16 THR 45.493 31.553 15.427 17 MET 46.445 32.854 18.907 18 LYS 49.648 30.801 18.717 19 GLU 50.453 32.462 15.364 20 LYS 49.875 35.958 16.622 21 GLY 51.779 34.820 19.672 22 LEU 49.131 35.512 22.278 23 LEU 48.467 31.950 23.381 24 GLY 50.951 31.353 26.144 25 GLU 49.862 34.095 28.349 26 PHE 46.217 33.730 27.703 27 LEU 46.762 30.078 28.532 28 ARG 48.321 30.753 31.842 29 THR 46.040 33.624 32.708 30 HIS 42.898 31.419 32.153 31 LYS 41.754 28.182 33.815 32 TYR 39.194 25.772 32.405 33 ASP 38.018 22.259 33.155 34 PRO 36.317 20.680 30.078 35 ALA 33.618 19.117 32.265 36 TRP 32.296 22.636 33.025 37 LYS 30.504 22.620 29.650 38 TYR 27.910 20.278 30.784 39 ARG 27.090 21.496 34.337 40 PHE 23.741 22.790 33.388 41 GLY 20.319 21.241 33.400 42 ASP 18.529 24.057 31.628 43 LEU 18.156 24.258 27.853 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 10 S H H H H H H H H H 20 H C H H H H H H H H/S 30 S S S S/H H H 3 3 3/S S 40 S S/S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 10 h H H H H H H H h 20 T h H H H H H h T t 30 g G G G G G g 40 Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 ALA 4.8 6.7 80.9 2 VAL 0.0 0.0 85.4 3 VAL 25.0 21.1 74.2 4 LYS 10.0 5.8 84.8 5 VAL 21.6 18.2 70.3 6 PRO 23.7 19.1 78.2 7 LEU 14.0 9.4 84.4 8 LYS 21.7 12.5 80.4 9 LYS 0.3 0.2 88.5 10 PHE 29.6 17.8 82.1 11 LYS 75.2 43.4 85.2 12 SER 32.2 38.5 74.3 13 ILE 4.8 3.4 78.6 14 ARG 59.7 28.6 68.4 15 GLU 61.5 44.4 65.9 16 THR 61.6 57.6 61.9 17 MET 123.7 77.6 41.9 18 LYS 28.6 16.5 77.5 19 GLU 55.0 39.7 74.6 20 LYS 60.4 34.9 71.1 21 GLY 4.4 12.5 81.2 22 LEU 62.9 42.6 68.8 23 LEU 128.1 86.6 40.4 24 GLY 6.2 17.8 67.5 25 GLU 25.8 18.6 83.2 26 PHE 78.7 47.2 58.1 27 LEU 81.2 54.9 62.9 28 ARG 31.4 15.0 83.0 29 THR 29.4 27.5 79.0 30 HIS 64.4 42.9 65.3 31 LYS 38.5 22.2 77.5 32 TYR 71.3 39.4 64.0 33 ASP 57.5 52.1 49.4 34 PRO 28.4 22.8 79.6 35 ALA 13.8 19.1 73.9 36 TRP 98.4 48.0 65.9 37 LYS 35.9 20.7 83.5 38 TYR 45.5 25.1 78.9 39 ARG 37.9 18.1 80.3 40 PHE 40.5 24.3 88.0 41 GLY 0.0 0.0 84.3 42 ASP 14.2 12.9 73.6 43 LEU 0.0 0.0 88.1