Protein Data Bank File : 1pyta Title : TERNARY COMPLEX (ZYMOGEN) 21-JUN-95 1PYT Number of Amino Acid Residues : 94 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 LYS GLU ASP PHE VAL GLY HIS GLN VAL LEU 10 ARG ILE THR ALA ALA ASP GLU ALA GLU VAL 20 GLN THR VAL LYS GLU LEU GLU ASP LEU GLU 30 HIS LEU GLN LEU ASP PHE TRP ARG GLY PRO 40 GLY GLN PRO GLY SER PRO ILE ASP VAL ARG 50 VAL PRO PHE PRO SER LEU GLN ALA VAL LYS 60 VAL PHE LEU GLU ALA HIS GLY ILE ARG TYR 70 ARG ILE MET ILE GLU ASP VAL GLN SER LEU 80 LEU ASP GLU GLU GLN GLU GLN MET PHE ALA 90 SER GLN SER ARG Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 LYS 0.0 159.6 -179.2 -51.8 -173.5 68.2 -74.1 2 GLU -55.5 148.5 -179.7 -79.0 -63.6 72.5 3 ASP -104.3 130.1 179.1 -168.6 -47.5 4 PHE -131.5 13.8 179.9 -56.8 -68.6 5 VAL -55.2 125.5 178.2 174.2 6 GLY 80.7 -3.3 178.7 7 HIS -68.2 166.0 179.9 -71.0 -142.9 8 GLN -147.3 143.1 178.4 -63.6 -160.4 -21.4 9 VAL -104.9 130.9 -177.9 -178.9 10 LEU -115.2 153.0 177.2 -81.6 33.8 11 ARG -113.4 96.1 -178.9 176.5 104.2 88.7 167.9 12 ILE -84.5 152.0 177.9 -55.5 169.1 13 THR -136.2 107.7 178.8 -36.0 14 ALA -92.5 114.1 -179.1 15 ALA -55.8 -51.8 -179.4 16 ASP -136.5 164.2 -178.6 65.6 -41.3 17 GLU -33.1 -37.5 178.7 -122.8 -46.9 -43.1 18 ALA -60.2 -53.0 -179.5 19 GLU -60.8 -24.5 179.1 -60.2 -163.1 23.3 20 VAL -72.9 -48.1 178.9 175.7 21 GLN -59.3 -33.0 -179.8 -55.1 -176.3 165.1 22 THR -73.8 -31.3 177.6 -53.8 23 VAL -75.1 -22.9 176.9 52.1 24 LYS -80.2 -29.9 179.2 -99.0 -161.4 -167.9 59.2 25 GLU -71.4 -0.3 179.0 -91.3 143.4 19.7 26 LEU -107.3 -17.4 -179.3 -162.7 58.1 27 GLU -78.0 -34.1 179.3 -179.0 158.7 45.8 28 ASP -63.7 -32.6 -179.6 -61.8 -32.9 29 LEU -66.0 81.2 -179.1 -65.2 171.2 30 GLU -51.8 -41.8 -179.0 -60.9 179.4 49.1 31 HIS -57.4 -19.5 -179.2 81.2 -86.7 32 LEU -72.8 -26.4 -179.8 -68.6 -176.2 33 GLN 56.3 52.2 -179.9 -75.7 171.5 -61.1 34 LEU -77.8 141.3 177.9 -91.4 13.4 35 ASP -114.7 97.0 -178.5 169.2 33.1 36 PHE -74.0 104.9 178.1 -82.1 85.8 37 TRP -74.0 -31.7 179.3 -76.9 18.0 38 ARG -140.7 74.1 -177.7 -162.4 167.7 179.8 170.5 39 GLY -47.4 165.1 180.0 40 PRO -51.6 141.0 178.4 -32.6 42.6 41 GLY -147.2 -138.8 179.2 42 GLN -71.8 149.1 179.3 -50.7 173.1 90.3 43 PRO -63.0 154.4 -179.6 -25.4 40.6 44 GLY 98.8 -40.7 178.7 45 SER -69.8 156.4 179.4 -52.5 46 PRO -83.2 149.0 179.1 28.2 -41.1 47 ILE -117.7 103.7 -179.9 -73.7 161.2 48 ASP -98.7 135.5 -178.4 -63.2 -73.8 49 VAL -148.0 143.3 175.7 60.6 50 ARG -101.3 117.3 -179.4 171.4 -178.0 50.8 95.3 51 VAL -110.3 122.3 -179.6 -12.8 52 PRO -53.8 155.3 -179.4 -34.1 46.0 53 PHE -57.2 -42.8 -179.8 -179.1 79.4 54 PRO -66.8 -23.8 -179.5 -30.4 47.6 55 SER -99.2 6.9 -177.2 -33.6 56 LEU -59.5 -60.4 -179.0 -153.3 38.6 57 GLN -67.4 -41.2 178.9 -131.7 81.9 84.2 58 ALA -62.5 -38.3 -179.9 59 VAL -68.8 -46.0 179.3 168.2 60 LYS -54.6 -64.2 179.0 -76.1 168.7 175.5 171.7 61 VAL -51.8 -31.2 178.4 175.0 62 PHE -62.4 -50.3 179.4 173.5 -84.6 63 LEU -59.9 -60.6 -180.0 -99.6 12.0 64 GLU -47.4 -50.3 -180.0 -59.1 -171.8 4.6 65 ALA -58.6 -27.2 -179.2 66 HIS -96.8 5.7 -179.1 -80.0 79.2 67 GLY 58.0 52.0 179.6 68 ILE -120.3 127.0 -177.6 -64.6 -173.0 69 ARG -84.5 136.0 -179.5 46.1 -175.6 -52.6 -175.0 70 TYR -149.1 151.1 177.5 66.3 85.0 71 ARG -130.0 161.6 -179.0 53.3 155.7 -44.7 -128.3 72 ILE -96.4 110.2 179.9 -59.1 168.1 73 MET -75.6 -52.0 -179.8 -63.6 -59.4 -27.3 74 ILE -121.3 122.5 -177.8 -60.5 177.8 75 GLU -78.6 -33.7 179.2 166.3 -161.8 -35.2 76 ASP -150.6 99.8 179.9 -173.2 -47.9 77 VAL -57.0 -40.3 -179.3 175.0 78 GLN -58.3 -38.8 179.8 -171.9 67.1 40.4 79 SER -60.9 -32.5 176.9 -86.7 80 LEU -67.7 -56.3 179.6 -89.3 -163.6 81 LEU -50.9 -37.9 -179.8 -148.1 144.3 82 ASP -63.5 -34.0 177.7 -83.1 12.7 83 GLU -72.7 -53.3 178.5 -101.9 157.4 29.5 84 GLU -46.9 -55.6 -179.3 -176.6 174.9 72.4 85 GLN -58.0 -34.7 -179.9 -110.4 60.9 128.4 86 GLU -73.6 -28.5 179.2 -120.3 -60.7 -35.0 87 GLN -73.1 -49.8 179.1 -172.2 -90.2 4.6 88 MET -51.0 -46.5 -179.7 -70.2 177.2 83.5 89 PHE -64.9 -47.2 -179.6 -176.6 -89.9 90 ALA -57.0 -24.9 -178.4 91 SER -109.9 31.3 -177.5 55.0 92 GLN -99.9 129.4 178.2 63.1 172.0 -23.2 93 SER -162.9 169.4 179.2 65.5 94 ARG -105.4 -59.8 0.0 -46.4 -99.9 54.5 -101.6 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 LYS 16.786 96.911 -18.346 2 GLU 20.196 96.569 -16.704 3 ASP 23.267 95.913 -18.844 4 PHE 25.594 93.126 -17.764 5 VAL 27.595 92.462 -20.900 6 GLY 31.091 91.475 -19.875 7 HIS 30.527 91.514 -16.134 8 GLN 32.089 88.635 -14.199 9 VAL 31.416 86.842 -10.972 10 LEU 34.643 85.955 -9.206 11 ARG 35.260 83.565 -6.340 12 ILE 37.625 85.232 -3.908 13 THR 39.152 83.219 -1.049 14 ALA 40.657 85.147 1.846 15 ALA 42.929 82.687 3.605 16 ASP 42.844 84.475 6.940 17 GLU 41.117 87.418 8.643 18 ALA 43.784 89.661 7.104 19 GLU 42.854 88.709 3.560 20 VAL 39.225 89.320 4.595 21 GLN 39.708 92.931 5.773 22 THR 41.386 93.762 2.421 23 VAL 38.504 92.416 0.284 24 LYS 36.301 94.574 2.545 25 GLU 38.597 97.567 1.926 26 LEU 37.342 97.190 -1.630 27 GLU 33.705 97.143 -0.491 28 ASP 33.951 100.650 0.923 29 LEU 34.985 101.787 -2.583 30 GLU 31.533 102.777 -3.719 31 HIS 32.609 103.771 -7.226 32 LEU 33.431 100.130 -8.151 33 GLN 29.764 99.074 -7.949 34 LEU 30.455 95.592 -6.719 35 ASP 27.544 93.265 -6.344 36 PHE 28.552 90.853 -3.612 37 TRP 26.720 87.583 -4.299 38 ARG 28.402 85.918 -1.319 39 GLY 29.727 88.830 0.692 40 PRO 32.701 88.521 3.123 41 GLY 32.482 86.176 6.087 42 GLN 34.730 83.873 8.091 43 PRO 37.990 83.263 6.235 44 GLY 37.814 80.049 4.234 45 SER 34.220 80.580 3.074 46 PRO 33.823 81.686 -0.531 47 ILE 33.308 85.369 -1.528 48 ASP 31.359 85.513 -4.750 49 VAL 31.061 88.963 -6.302 50 ARG 29.881 90.415 -9.614 51 VAL 32.346 93.076 -10.640 52 PRO 31.197 95.362 -13.486 53 PHE 33.258 95.511 -16.616 54 PRO 34.779 98.926 -16.013 55 SER 35.919 97.891 -12.535 56 LEU 37.011 94.491 -13.803 57 GLN 40.751 94.909 -14.361 58 ALA 41.255 97.297 -11.454 59 VAL 39.627 94.860 -9.046 60 LYS 41.732 91.927 -10.295 61 VAL 45.126 93.697 -10.050 62 PHE 44.010 94.951 -6.629 63 LEU 43.495 91.317 -5.710 64 GLU 46.639 90.050 -7.515 65 ALA 48.771 92.788 -5.932 66 HIS 47.603 91.712 -2.481 67 GLY 48.311 88.092 -3.224 68 ILE 44.670 87.104 -2.920 69 ARG 43.364 84.183 -4.938 70 TYR 40.276 84.286 -7.118 71 ARG 38.939 82.321 -9.982 72 ILE 36.301 83.303 -12.493 73 MET 33.025 81.461 -11.780 74 ILE 30.929 83.194 -14.441 75 GLU 32.787 84.733 -17.367 76 ASP 30.010 86.914 -18.806 77 VAL 26.856 87.410 -16.735 78 GLN 24.830 88.906 -19.580 79 SER 25.205 85.703 -21.536 80 LEU 23.612 83.622 -18.711 81 LEU 20.724 86.028 -18.307 82 ASP 20.435 85.808 -22.061 83 GLU 19.948 82.033 -21.860 84 GLU 17.492 82.220 -18.980 85 GLN 15.371 84.766 -20.775 86 GLU 15.462 82.599 -23.911 87 GLN 14.266 79.528 -22.042 88 MET 11.365 81.426 -20.466 89 PHE 10.184 82.621 -23.837 90 ALA 10.529 79.172 -25.364 91 SER 8.317 77.914 -22.532 92 GLN 5.397 80.410 -22.382 93 SER 1.676 79.649 -22.322 94 ARG -1.448 80.192 -20.335 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 H H H H H 20 H H H H H H H H H C 30 C C S S S S S/S S S S 40 C C C S S S S S S S/S 50 S S S C H H H H H H 60 H H H H H H H/S S S S 70 S S S/S S S S/H H H H H 80 H H H H H H H H H H 90 H H/S S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 t T T t E E E 10 E E E S h H H H H 20 H H H H h T T t g G 30 G G g E E E E t 40 t T T t E E E E 50 E h H H H H H H H H 60 H H H H H h T t E E 70 E E E E S h H H H H 80 H H H H H H H H H H 90 h t Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 LYS 15.9 9.2 92.8 2 GLU 20.5 14.8 76.7 3 ASP 21.2 19.1 78.0 4 PHE 131.5 78.8 55.1 5 VAL 30.7 25.8 78.2 6 GLY 18.6 53.5 64.0 7 HIS 130.2 86.7 54.0 8 GLN 126.1 84.9 46.4 9 VAL 116.3 97.9 33.6 10 LEU 147.8 100.0 32.9 11 ARG 131.7 63.1 62.7 12 ILE 141.8 98.8 29.5 13 THR 61.0 57.1 70.7 14 ALA 72.0 99.1 47.1 15 ALA 17.8 24.5 77.1 16 ASP 34.9 31.6 66.4 17 GLU 45.6 32.9 66.7 18 ALA 18.9 26.0 79.5 19 GLU 97.6 70.4 62.0 20 VAL 117.0 98.5 56.8 21 GLN 42.1 28.3 82.1 22 THR 84.9 79.5 56.1 23 VAL 118.6 99.8 28.5 24 LYS 84.8 48.9 70.0 25 GLU 50.9 36.7 78.2 26 LEU 143.3 96.9 30.0 27 GLU 77.2 55.7 56.8 28 ASP 15.7 14.2 79.1 29 LEU 75.8 51.3 64.9 30 GLU 0.0 0.0 93.1 31 HIS 28.1 18.7 70.1 32 LEU 137.2 92.9 44.7 33 GLN 19.9 13.4 84.3 34 LEU 141.4 95.6 36.4 35 ASP 62.4 56.5 76.3 36 PHE 148.6 89.1 46.0 37 TRP 101.4 49.5 62.9 38 ARG 78.4 37.6 79.2 39 GLY 19.9 57.2 55.6 40 PRO 118.0 94.7 45.8 41 GLY 5.9 16.9 81.4 42 GLN 7.3 4.9 84.5 43 PRO 90.2 72.5 62.9 44 GLY 4.4 12.8 78.8 45 SER 45.6 54.6 74.3 46 PRO 94.6 76.0 69.0 47 ILE 139.4 97.1 41.7 48 ASP 94.2 85.2 45.5 49 VAL 117.0 98.5 33.8 50 ARG 169.8 81.3 44.5 51 VAL 118.8 100.0 33.0 52 PRO 113.5 91.2 57.0 53 PHE 47.9 28.7 67.2 54 PRO 31.6 25.4 75.5 55 SER 73.0 87.3 48.6 56 LEU 135.9 91.9 57.5 57 GLN 27.1 18.2 78.3 58 ALA 18.1 25.0 73.8 59 VAL 117.5 98.9 27.7 60 LYS 146.7 84.6 52.5 61 VAL 30.7 25.9 72.5 62 PHE 120.4 72.2 50.4 63 LEU 147.8 100.0 27.2 64 GLU 52.9 38.2 73.2 65 ALA 22.7 31.2 76.2 66 HIS 77.5 51.6 60.0 67 GLY 0.0 0.0 81.6 68 ILE 141.8 98.8 47.4 69 ARG 21.4 10.2 86.0 70 TYR 154.1 85.1 46.6 71 ARG 70.9 33.9 70.5 72 ILE 91.7 63.9 63.3 73 MET 112.9 70.8 67.0 74 ILE 111.5 77.7 46.3 75 GLU 18.2 13.1 76.7 76 ASP 75.3 68.2 65.4 77 VAL 106.0 89.2 36.2 78 GLN 114.4 77.0 58.7 79 SER 22.6 27.0 77.9 80 LEU 63.1 42.7 70.7 81 LEU 104.1 70.4 65.2 82 ASP 44.4 40.2 74.6 83 GLU 26.8 19.3 78.2 84 GLU 39.1 28.2 72.9 85 GLN 79.0 53.2 64.5 86 GLU 30.8 22.2 77.3 87 GLN 32.9 22.2 77.4 88 MET 51.2 32.1 85.7 89 PHE 36.1 21.6 85.2 90 ALA 20.7 28.5 77.8 91 SER 33.9 40.6 82.0 92 GLN 53.6 36.1 74.4 93 SER 6.5 7.8 81.1 94 ARG 3.2 1.5 88.1