Protein Data Bank File : 1sgpi Title : COMPLEX (SERINE PROTEASE/INHIBITOR) 26-MAY-95 1SGP Number of Amino Acid Residues : 51 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 VAL ASP CYS SER GLU TYR PRO LYS PRO ALA 10 CYS THR ALA GLU TYR ARG PRO LEU CYS GLY 20 SER ASP ASN LYS THR TYR GLY ASN LYS CYS 30 ASN PHE CYS ASN ALA VAL VAL GLU SER ASN 40 GLY THR LEU THR LEU SER HIS PHE GLY LYS 50 CYS Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 VAL 0.0 132.5 -178.7 -5.5 2 ASP -124.0 120.2 -177.8 -176.7 55.9 3 CYS -99.3 31.6 177.1 -57.8 4 SER -68.1 -39.0 -179.8 -70.6 5 GLU -82.7 29.2 -177.6 -14.1 144.6 87.8 6 TYR -109.3 167.9 -0.8 -77.0 73.3 7 PRO -75.8 168.5 -179.5 27.9 -24.8 8 LYS -127.4 139.3 -177.5 -110.7 85.1 131.4 -39.6 9 PRO -73.1 -17.2 -179.8 26.2 -25.3 10 ALA -150.4 151.2 176.4 11 CYS -126.6 144.2 169.3 -70.5 12 THR -67.1 165.4 -171.9 48.3 13 ALA -118.4 38.9 175.3 14 GLU -83.5 157.4 -178.9 74.7 -75.6 5.2 15 TYR -107.6 114.0 174.9 -173.8 73.3 16 ARG -147.9 87.9 -166.9 -14.3 -119.1 -90.9 87.1 17 PRO -71.4 153.6 178.9 32.6 -37.4 18 LEU -131.5 146.5 -176.5 -53.1 -177.9 19 CYS -106.2 115.4 -178.8 178.3 20 GLY -80.4 166.6 177.1 21 SER -70.3 -10.5 179.1 53.4 22 ASP -92.8 9.1 179.1 56.5 -4.5 23 ASN 70.4 11.6 179.0 -56.7 -65.7 24 LYS -100.3 138.6 172.6 178.8 176.1 168.9 -171.0 25 THR -76.6 121.5 176.7 -64.7 26 TYR -96.6 135.7 -171.7 -74.2 87.0 27 GLY -71.2 -23.6 176.9 28 ASN -160.6 171.9 -178.9 61.7 34.1 29 LYS -62.6 -36.8 179.9 116.3 127.0 -170.9 -164.8 30 CYS -66.5 -40.5 178.7 179.0 31 ASN -66.4 -41.9 179.4 -83.4 67.3 32 PHE -60.4 -48.2 -178.2 173.4 71.8 33 CYS -65.1 -33.9 178.8 -78.7 34 ASN -68.4 -32.1 178.1 -90.0 -14.4 35 ALA -76.1 -32.3 175.6 36 VAL -60.5 -44.1 179.3 168.8 37 VAL -62.0 -46.8 179.0 160.4 38 GLU -58.5 -33.4 179.0 175.9 163.3 6.1 39 SER -86.5 11.4 179.5 77.9 40 ASN 58.8 39.3 175.0 -165.9 34.7 41 GLY 81.4 11.5 -179.7 42 THR -92.0 -20.2 179.7 50.7 43 LEU -80.5 138.3 176.5 177.8 62.2 44 THR -130.0 173.3 179.0 57.7 45 LEU -87.9 122.4 178.5 -178.6 67.6 46 SER -82.2 -55.2 176.0 174.5 47 HIS -165.0 170.9 -179.4 50.5 90.5 48 PHE -86.1 153.6 -175.9 -61.8 -84.6 49 GLY 93.6 179.6 179.4 50 LYS -73.2 155.5 179.4 -71.6 -156.0 -62.0 21.9 51 CYS -74.4 -26.8 0.0 -70.3 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 VAL 22.425 12.984 30.601 2 ASP 25.154 14.906 32.409 3 CYS 24.257 17.105 35.342 4 SER 27.569 19.028 35.539 5 GLU 26.456 22.431 34.884 6 TYR 23.885 22.199 37.579 7 PRO 22.336 23.490 39.579 8 LYS 20.505 26.039 37.625 9 PRO 18.361 28.687 39.112 10 ALA 15.547 28.233 36.669 11 CYS 14.266 25.635 34.332 12 THR 12.098 25.954 31.176 13 ALA 8.822 24.005 31.497 14 GLU 8.542 21.731 28.506 15 TYR 7.710 18.105 29.187 16 ARG 10.221 15.446 28.104 17 PRO 10.258 13.031 30.898 18 LEU 13.034 11.072 32.659 19 CYS 12.673 8.279 35.293 20 GLY 14.754 8.767 38.496 21 SER 16.158 6.029 40.809 22 ASP 13.593 7.310 43.418 23 ASN 10.819 6.082 41.075 24 LYS 9.678 9.582 40.336 25 THR 9.080 10.854 36.790 26 TYR 11.068 14.145 36.418 27 GLY 9.443 16.402 33.785 28 ASN 12.603 17.451 31.996 29 LYS 16.314 17.192 32.222 30 CYS 16.682 20.489 34.070 31 ASN 14.241 19.476 36.759 32 PHE 15.987 16.053 37.012 33 CYS 19.495 17.519 37.280 34 ASN 18.452 20.128 39.956 35 ALA 17.070 17.277 42.011 36 VAL 20.299 15.238 41.522 37 VAL 22.169 18.303 42.966 38 GLU 19.671 18.735 45.728 39 SER 20.198 15.134 46.753 40 ASN 23.920 15.738 46.900 41 GLY 24.546 13.244 44.081 42 THR 22.542 10.290 45.379 43 LEU 19.679 10.296 42.804 44 THR 20.520 8.715 39.507 45 LEU 18.786 8.128 36.142 46 SER 16.896 4.817 35.927 47 HIS 15.766 5.211 32.281 48 PHE 14.391 7.751 29.782 49 GLY 10.655 8.361 29.573 50 LYS 8.165 8.175 32.444 51 CYS 8.620 5.805 35.336 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C C T T T T/P C C S S 10 S S S S/S S S S S S T 20 T T T/S S S S S H H H 30 H H H H H H H H H H 40 C S S S S S S S S S 50 S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 t T T t S 10 e E E E 20 e T t e E E S h H H 30 H H H H H H H H h T 40 T t e E E E E e 50 Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 VAL 96.0 80.8 40.0 2 ASP 16.8 15.2 81.5 3 CYS 86.7 87.4 42.2 4 SER 15.5 18.5 85.1 5 GLU 24.1 17.4 75.1 6 TYR 178.7 98.8 50.8 7 PRO 49.5 39.8 63.8 8 LYS 116.4 67.1 63.0 9 PRO 12.8 10.3 80.7 10 ALA 6.1 8.4 79.5 11 CYS 84.9 85.6 68.6 12 THR 6.6 6.1 88.4 13 ALA 4.4 6.1 89.0 14 GLU 59.7 43.1 72.2 15 TYR 67.8 37.5 62.8 16 ARG 42.5 20.3 78.1 17 PRO 99.8 80.2 51.5 18 LEU 136.1 92.1 41.1 19 CYS 94.5 95.2 60.9 20 GLY 34.8 100.0 53.5 21 SER 47.1 56.4 72.0 22 ASP 56.4 51.0 67.3 23 ASN 11.9 9.8 83.5 24 LYS 53.8 31.0 78.6 25 THR 81.2 76.0 57.3 26 TYR 164.4 90.8 51.5 27 GLY 17.6 50.5 55.8 28 ASN 116.2 96.1 68.4 29 LYS 90.7 52.3 64.8 30 CYS 85.4 86.1 62.7 31 ASN 49.1 40.7 72.1 32 PHE 163.1 97.8 29.9 33 CYS 99.2 100.0 38.2 34 ASN 87.4 72.3 56.9 35 ALA 52.0 71.6 63.0 36 VAL 96.0 80.8 47.2 37 VAL 69.3 58.3 63.3 38 GLU 8.0 5.8 84.6 39 SER 52.6 62.9 72.1 40 ASN 0.0 0.0 90.8 41 GLY 10.1 28.9 75.7 42 THR 19.1 17.8 86.0 43 LEU 134.1 90.7 56.9 44 THR 28.3 26.5 75.6 45 LEU 118.7 80.3 45.1 46 SER 44.1 52.7 63.2 47 HIS 67.8 45.1 72.1 48 PHE 51.6 30.9 67.7 49 GLY 8.6 24.9 72.0 50 LYS 59.2 34.1 77.8 51 CYS 85.4 86.1 66.3