Protein Data Bank File : 1ay7b Title : COMPLEX (ENZYME/INHIBITOR) 14-NOV-97 1AY7 Number of Amino Acid Residues : 89 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 LYS LYS ALA VAL ILE ASN GLY GLU GLN ILE 10 ARG SER ILE SER ASP LEU HIS GLN THR LEU 20 LYS LYS GLU LEU ALA LEU PRO GLU TYR TYR 30 GLY GLU ASN LEU ASP ALA LEU TRP ASP CYS 40 LEU THR GLY TRP VAL GLU TYR PRO LEU VAL 50 LEU GLU TRP ARG GLN PHE GLU GLN SER LYS 60 GLN LEU THR GLU ASN GLY ALA GLU SER VAL 70 LEU GLN VAL PHE ARG GLU ALA LYS ALA GLU 80 GLY CYS ASP ILE THR ILE ILE LEU SER Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 LYS 0.0 136.2 -174.6 174.6 85.8 158.6 151.3 2 LYS -112.1 131.7 179.6 -69.4 -176.3 -171.8 170.4 3 ALA -127.1 133.7 -175.4 4 VAL -122.5 131.4 178.6 176.0 5 ILE -120.2 120.3 176.6 -67.1 177.7 6 ASN -90.6 99.5 -162.7 -69.7 -56.1 7 GLY -66.5 -27.1 178.6 8 GLU -72.6 -16.1 -176.1 77.3 -75.3 6.8 9 GLN -97.1 -3.0 -174.9 -56.4 172.6 7.9 10 ILE -104.0 118.3 -172.9 -44.0 -75.2 11 ARG -120.8 5.4 -178.4 -64.2 -77.5 161.3 173.1 12 SER -139.8 157.9 -177.2 76.4 13 ILE -79.8 -30.4 179.2 173.1 77.2 14 SER -57.4 -48.2 -179.9 -175.3 15 ASP -68.6 -32.5 173.8 -70.2 -24.0 16 LEU -59.2 -46.7 177.0 179.2 54.8 17 HIS -63.6 -39.9 -179.4 -82.7 -68.9 18 GLN -64.8 -37.1 179.4 -60.4 -56.5 -64.0 19 THR -69.4 -41.8 170.3 -62.5 20 LEU -61.0 -39.5 -177.2 -61.5 169.4 21 LYS -61.3 -37.3 177.3 -178.4 179.0 179.4 176.1 22 LYS -75.0 -51.3 -171.9 175.3 -157.6 104.8 -134.0 23 GLU -73.1 -25.6 -180.0 -70.5 -70.0 -49.4 24 LEU -102.2 0.4 180.0 -64.4 -178.8 25 ALA 57.0 52.4 178.1 26 LEU -76.5 164.9 -175.3 -63.2 -174.5 27 PRO -62.6 156.7 179.1 -4.5 7.6 28 GLU -65.6 -22.7 177.0 -164.6 60.1 34.7 29 TYR -89.6 8.0 177.5 60.3 70.8 30 TYR -44.1 129.3 -174.2 173.9 58.2 31 GLY -75.6 -7.8 176.2 32 GLU 55.8 55.3 174.2 -63.9 -179.4 14.5 33 ASN -159.2 170.3 -171.8 58.2 73.0 34 LEU -68.4 -31.5 177.7 -63.5 172.5 35 ASP -72.8 -30.9 172.3 -56.3 -72.4 36 ALA -71.1 -33.1 -178.4 37 LEU -70.2 -39.7 177.0 173.4 56.2 38 TRP -61.8 -40.6 176.7 172.0 -111.1 39 ASP -60.5 -36.5 -176.2 177.5 43.9 40 CYS -79.0 -31.5 -178.5 -72.2 41 LEU -75.6 -23.5 -175.3 -69.7 -179.8 42 THR -98.3 -4.7 -178.4 58.0 43 GLY -145.1 17.9 -173.0 44 TRP -157.2 -42.2 -173.5 174.2 -87.6 45 VAL -66.2 148.9 172.9 172.4 46 GLU -75.0 138.9 -179.8 179.1 -179.3 -26.4 47 TYR -133.0 136.5 24.9 -66.0 -50.5 48 PRO -80.4 148.6 173.3 18.2 -28.1 49 LEU -121.9 139.5 170.9 166.4 69.8 50 VAL -113.2 121.6 -178.5 177.9 51 LEU -114.3 114.2 177.3 173.8 65.1 52 GLU -96.8 109.8 -179.9 -62.9 151.3 81.7 53 TRP -111.8 101.1 -172.8 -170.0 -33.9 54 ARG -85.0 156.1 -179.7 -71.3 -180.0 175.0 159.4 55 GLN 45.9 53.4 -175.9 -63.1 -55.4 115.2 56 PHE -63.9 -44.6 -176.1 176.5 66.9 57 GLU -63.4 -29.3 167.9 -67.4 -76.4 -16.6 58 GLN -64.3 -37.8 -179.6 -115.2 175.2 -53.8 59 SER -67.4 -31.8 -179.9 62.1 60 LYS -60.0 -43.5 180.0 -95.6 -123.1 -122.8 103.6 61 GLN -57.6 -80.6 -179.2 -55.5 -165.1 -175.0 62 LEU -37.9 -40.0 -176.2 39.0 89.4 63 THR -89.8 -7.4 -177.5 58.4 64 GLU 77.2 10.2 -173.7 105.9 -111.0 -73.3 65 ASN 76.8 32.1 148.6 -77.0 -132.2 66 GLY -65.2 -40.5 175.2 67 ALA -61.3 -42.5 -179.0 68 GLU -67.1 -31.6 179.1 -169.7 65.8 34.9 69 SER -66.4 -36.6 179.5 -82.2 70 VAL -64.7 -46.7 -177.2 168.9 71 LEU -64.4 -29.5 177.6 176.7 61.8 72 GLN -65.9 -37.0 178.3 -179.9 53.7 41.2 73 VAL -58.8 -49.2 177.6 179.5 74 PHE -60.6 -37.5 -177.8 -81.1 -80.4 75 ARG -69.4 -36.5 175.8 -68.4 -156.6 -106.7 -113.6 76 GLU -67.4 -36.9 174.7 -70.7 174.6 10.4 77 ALA -64.7 -39.2 -179.5 78 LYS -66.8 -39.2 179.7 177.3 172.9 165.7 65.9 79 ALA -68.9 -18.6 171.8 80 GLU -88.0 2.1 176.1 -63.9 -142.5 -7.8 81 GLY 98.5 7.4 168.1 82 CYS -73.8 141.4 -175.2 -65.0 83 ASP -87.1 82.1 178.4 -170.5 -9.8 84 ILE -114.9 131.1 171.9 -64.4 162.7 85 THR -112.2 124.8 178.4 -62.9 86 ILE -106.6 128.8 177.3 -67.3 164.8 87 ILE -126.8 117.7 176.3 -63.1 160.3 88 LEU -99.1 157.2 168.9 -57.6 178.7 89 SER -140.7 -3.6 0.0 65.9 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 LYS 12.583 45.824 0.582 2 LYS 14.231 44.102 -2.418 3 ALA 15.694 40.539 -2.229 4 VAL 17.534 38.942 -5.161 5 ILE 18.269 35.235 -5.522 6 ASN 20.579 34.236 -8.411 7 GLY 19.104 30.806 -8.900 8 GLU 21.945 29.326 -10.977 9 GLN 24.352 29.805 -8.057 10 ILE 22.401 28.049 -5.282 11 ARG 23.237 24.351 -5.274 12 SER 22.385 23.396 -1.637 13 ILE 19.218 24.057 0.470 14 SER 21.555 25.285 3.229 15 ASP 23.025 28.022 1.020 16 LEU 19.422 28.937 -0.093 17 HIS 18.502 29.415 3.568 18 GLN 21.743 31.375 4.200 19 THR 21.008 33.605 1.170 20 LEU 17.473 34.172 2.433 21 LYS 18.806 35.026 5.937 22 LYS 21.010 37.747 4.333 23 GLU 18.628 39.106 1.711 24 LEU 15.552 39.290 4.029 25 ALA 17.503 40.361 7.144 26 LEU 16.115 37.464 9.208 27 PRO 16.901 37.188 12.904 28 GLU 20.296 35.766 13.916 29 TYR 18.453 32.840 15.463 30 TYR 16.701 31.887 12.199 31 GLY 16.169 28.153 12.219 32 GLU 17.094 27.590 8.483 33 ASN 14.075 25.428 7.709 34 LEU 10.647 25.911 6.111 35 ASP 8.707 26.334 9.344 36 ALA 11.058 29.039 10.560 37 LEU 10.826 30.792 7.175 38 TRP 7.016 30.781 7.438 39 ASP 7.270 32.223 11.041 40 CYS 9.563 35.017 9.740 41 LEU 7.364 35.905 6.752 42 THR 4.307 36.223 8.983 43 GLY 6.100 37.998 11.819 44 TRP 9.402 39.761 11.101 45 VAL 10.146 40.551 7.488 46 GLU 9.697 44.110 6.230 47 TYR 6.903 44.739 3.692 48 PRO 6.372 45.583 0.928 49 LEU 8.904 42.981 -0.264 50 VAL 9.938 42.361 -3.855 51 LEU 11.655 38.977 -4.339 52 GLU 13.488 38.611 -7.671 53 TRP 14.304 34.929 -8.106 54 ARG 16.378 34.826 -11.251 55 GLN 16.926 31.569 -13.156 56 PHE 14.266 29.871 -11.054 57 GLU 14.010 26.741 -13.291 58 GLN 17.746 26.217 -12.807 59 SER 17.376 26.397 -9.043 60 LYS 14.627 23.751 -9.318 61 GLN 17.031 21.324 -10.935 62 LEU 20.057 21.398 -8.632 63 THR 17.853 21.367 -5.526 64 GLU 15.265 18.592 -6.270 65 ASN 12.458 21.148 -5.746 66 GLY 13.811 22.257 -2.437 67 ALA 13.389 25.416 -4.545 68 GLU 9.720 24.787 -5.205 69 SER 9.043 24.188 -1.530 70 VAL 10.552 27.530 -0.650 71 LEU 8.668 29.378 -3.372 72 GLN 5.403 27.724 -2.171 73 VAL 5.971 29.273 1.305 74 PHE 6.235 32.768 -0.265 75 ARG 3.118 32.116 -2.366 76 GLU 1.203 31.096 0.781 77 ALA 2.278 34.221 2.642 78 LYS 1.173 36.367 -0.303 79 ALA -2.191 34.513 -0.298 80 GLU -2.650 35.428 3.395 81 GLY -2.210 39.100 2.571 82 CYS 1.506 39.751 3.091 83 ASP 2.536 42.353 0.495 84 ILE 4.998 40.302 -1.516 85 THR 5.710 40.579 -5.228 86 ILE 7.459 37.570 -6.692 87 ILE 9.224 38.000 -10.020 88 LEU 10.810 34.944 -11.546 89 SER 13.043 34.865 -14.597 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S S S S S/T T T T/S S 10 S S/H H H H H H H H H 20 H H H H H C C C C C 30 C C H H H H H H H H 40 H H H/S S S S C S S S 50 S S S S S/H H H H H H 60 H H H H C H H H H H 70 H H H H H H H H H H 80 H S S S S 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 G G g 10 h H H H H H H H H 20 H H H h T t t T T t 30 S h H H H H H H H 40 H H H h t S S E E 50 E E E E h H H H H H 60 H H h T h H H H H H 70 H H H H H H H H H h 80 T t e E E E E E e Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 LYS 112.3 64.8 69.4 2 LYS 31.3 18.1 82.3 3 ALA 72.5 99.9 44.2 4 VAL 82.2 69.2 75.0 5 ILE 143.3 99.9 29.5 6 ASN 69.9 57.9 71.0 7 GLY 34.8 100.0 59.8 8 GLU 86.0 62.0 64.4 9 GLN 47.2 31.7 78.6 10 ILE 131.3 91.5 50.8 11 ARG 95.4 45.7 72.7 12 SER 41.9 50.1 74.3 13 ILE 71.5 49.8 60.3 14 SER 23.6 28.2 74.5 15 ASP 41.2 37.3 72.3 16 LEU 146.2 98.9 28.4 17 HIS 144.0 95.8 43.7 18 GLN 76.6 51.6 77.4 19 THR 84.1 78.7 56.1 20 LEU 147.7 99.9 29.6 21 LYS 134.6 77.6 70.0 22 LYS 43.0 24.8 81.7 23 GLU 107.3 77.4 60.6 24 LEU 147.8 100.0 24.8 25 ALA 21.1 29.1 85.9 26 LEU 147.8 100.0 31.5 27 PRO 116.1 93.3 36.8 28 GLU 10.1 7.3 86.1 29 TYR 24.9 13.7 76.7 30 TYR 179.0 98.9 39.9 31 GLY 10.5 30.0 71.4 32 GLU 86.3 62.3 69.6 33 ASN 54.2 44.8 72.8 34 LEU 84.4 57.1 60.3 35 ASP 0.0 0.0 84.1 36 ALA 55.0 75.7 65.5 37 LEU 147.8 100.0 30.3 38 TRP 122.9 60.0 63.7 39 ASP 19.2 17.4 78.8 40 CYS 91.8 92.6 41.5 41 LEU 147.8 100.0 33.7 42 THR 73.1 68.4 60.4 43 GLY 6.8 19.7 82.9 44 TRP 96.9 47.3 68.8 45 VAL 118.1 99.5 41.6 46 GLU 33.4 24.1 76.4 47 TYR 144.4 79.8 48.9 48 PRO 38.5 30.9 79.8 49 LEU 147.8 100.0 33.2 50 VAL 78.0 65.7 56.4 51 LEU 147.8 100.0 26.0 52 GLU 102.0 73.6 53.1 53 TRP 204.9 99.9 29.5 54 ARG 98.1 47.0 76.8 55 GLN 68.5 46.1 77.1 56 PHE 157.3 94.3 45.9 57 GLU 35.2 25.4 75.6 58 GLN 85.4 57.5 71.7 59 SER 82.0 98.1 45.1 60 LYS 119.5 68.9 73.3 61 GLN 23.4 15.7 81.8 62 LEU 131.2 88.8 58.8 63 THR 98.8 92.4 53.2 64 GLU 10.5 7.6 86.0 65 ASN 65.1 53.9 64.5 66 GLY 25.7 73.8 60.7 67 ALA 72.5 99.9 42.4 68 GLU 88.7 64.0 60.6 69 SER 40.8 48.8 62.4 70 VAL 118.8 100.0 28.7 71 LEU 147.0 99.4 39.1 72 GLN 72.2 48.6 73.8 73 VAL 103.3 87.0 46.6 74 PHE 166.8 100.0 21.4 75 ARG 114.9 55.0 65.8 76 GLU 61.6 44.5 66.3 77 ALA 72.6 100.0 38.2 78 LYS 73.8 42.5 75.6 79 ALA 10.9 15.1 82.2 80 GLU 45.4 32.8 73.1 81 GLY 0.8 2.3 86.7 82 CYS 78.5 79.1 51.0 83 ASP 29.5 26.7 68.0 84 ILE 143.5 100.0 42.1 85 THR 46.1 43.1 63.8 86 ILE 129.8 90.5 37.5 87 ILE 58.2 40.6 63.4 88 LEU 96.5 65.3 54.1 89 SER 29.1 34.8 75.6