Protein Data Bank File : 1icfi Title : HYDROLASE 07-JAN-99 1ICF Number of Amino Acid Residues : 65 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 LEU THR LYS CYS GLN GLU GLU VAL SER HIS 10 ILE PRO ALA VAL HIS PRO GLY SER PHE ARG 20 PRO LYS CYS ASP GLU ASN GLY ASN TYR LEU 30 PRO LEU GLN CYS TYR GLY SER ILE GLY TYR 40 CYS TRP CYS VAL PHE PRO ASN GLY THR GLU 50 VAL PRO ASN THR ARG SER ARG GLY HIS HIS 60 ASN CYS SER GLU SER Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 LEU 0.0 131.9 -180.0 -136.0 59.6 2 THR -76.6 166.6 179.0 65.2 3 LYS -53.2 -46.4 179.5 -172.9 -171.5 -161.4 -91.2 4 CYS -62.1 -45.1 -179.4 -173.3 5 GLN -64.2 -38.2 179.6 -75.7 161.6 -10.3 6 GLU -68.4 -36.8 179.2 -47.1 -157.1 -74.2 7 GLU -66.0 -47.3 179.3 -61.2 -170.5 -22.0 8 VAL -57.1 -42.2 -177.4 155.3 9 SER -66.5 -9.0 -179.7 97.7 10 HIS -98.2 -9.4 -178.9 -69.9 -37.7 11 ILE -109.3 134.5 179.9 -46.3 -88.4 12 PRO -72.4 167.8 179.2 27.4 -38.0 13 ALA -58.8 -46.1 177.7 14 VAL -98.4 103.7 -177.3 175.9 15 HIS -137.9 62.8 179.9 54.8 102.7 16 PRO -61.3 126.0 178.6 16.7 -22.8 17 GLY 95.1 -10.8 178.7 18 SER -103.8 141.8 176.6 -40.1 19 PHE -87.4 136.1 177.6 170.2 74.1 20 ARG -133.9 125.3 -179.4 -170.2 -142.0 -122.5 176.0 21 PRO -71.8 162.4 177.0 28.0 -37.5 22 LYS -110.9 131.8 179.7 -86.8 -137.5 -166.0 43.3 23 CYS -116.0 152.8 177.9 -39.6 24 ASP -88.8 -179.2 -178.0 68.1 10.0 25 GLU -56.1 -27.7 -179.0 -52.9 177.4 -33.7 26 ASN -89.9 -0.6 179.8 -59.8 -49.3 27 GLY 88.4 7.6 179.4 28 ASN -87.2 158.6 176.1 -54.7 -59.0 29 TYR -73.1 140.4 174.6 -72.4 -87.1 30 LEU -70.6 146.6 180.0 -66.6 169.6 31 PRO -54.3 -39.0 -179.6 -28.8 34.7 32 LEU -97.7 126.8 179.9 176.8 67.4 33 GLN -121.4 142.7 -179.2 -70.0 -60.0 -45.0 34 CYS -129.8 140.5 178.5 -64.1 35 TYR -109.7 91.6 -175.9 -166.1 -10.4 36 GLY -55.2 -35.1 -178.2 37 SER -61.9 -42.0 -176.9 172.6 38 ILE -99.7 -11.1 177.7 55.8 166.5 39 GLY 77.2 49.5 178.7 40 TYR -143.4 144.3 177.2 -75.7 -78.4 41 CYS -127.0 158.9 179.8 -64.1 42 TRP -160.8 165.3 178.2 59.8 84.4 43 CYS -91.0 153.1 178.1 -52.2 44 VAL -131.5 160.6 177.5 -62.4 45 PHE -88.0 172.4 179.9 -67.1 -65.1 46 PRO -59.5 -20.6 179.6 -35.6 42.6 47 ASN -91.6 10.0 179.4 56.6 18.5 48 GLY 87.8 -10.0 179.8 49 THR -71.2 139.7 -180.0 -72.2 50 GLU -69.7 138.8 178.0 173.5 163.9 -11.0 51 VAL -81.1 127.8 -179.3 -179.9 52 PRO -52.0 142.2 178.4 -16.5 14.9 53 ASN 53.5 42.5 -178.9 -155.7 30.6 54 THR -120.1 -4.8 -179.9 -150.8 55 ARG -77.5 121.4 -179.9 -143.9 174.3 -179.6 96.4 56 SER -164.1 -179.9 177.4 78.5 57 ARG -112.7 14.2 -179.8 -77.1 -151.1 174.0 140.3 58 GLY -104.2 -161.7 -179.9 59 HIS -84.6 145.4 -178.8 -58.2 -102.0 60 HIS -121.6 159.8 177.2 -65.9 84.1 61 ASN -141.2 67.2 -178.7 -151.8 160.2 62 CYS -80.2 144.4 -179.6 -43.4 63 SER -112.8 169.9 179.1 30.9 64 GLU -125.6 -169.0 179.7 52.1 -151.0 -84.2 65 SER -135.5 -16.0 0.0 148.1 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 LEU 39.022 23.574 15.316 2 THR 40.267 20.263 13.881 3 LYS 38.037 17.742 12.094 4 CYS 37.947 15.594 15.255 5 GLN 37.166 18.586 17.498 6 GLU 34.285 19.813 15.332 7 GLU 32.728 16.338 15.368 8 VAL 32.981 16.057 19.161 9 SER 31.448 19.504 19.554 10 HIS 28.252 18.410 17.783 11 ILE 27.338 15.579 20.181 12 PRO 26.036 16.316 23.676 13 ALA 27.573 15.001 26.939 14 VAL 24.726 12.503 27.480 15 HIS 24.431 10.649 24.146 16 PRO 23.351 7.015 24.443 17 GLY 23.573 5.358 21.025 18 SER 25.560 8.079 19.163 19 PHE 29.224 7.663 18.299 20 ARG 31.378 10.563 19.383 21 PRO 35.095 10.474 18.527 22 LYS 37.948 10.987 21.024 23 CYS 40.642 13.564 20.183 24 ASP 44.100 14.098 21.733 25 GLU 45.543 17.408 23.038 26 ASN 46.599 18.384 19.482 27 GLY 43.135 17.823 17.964 28 ASN 44.000 14.553 16.250 29 TYR 41.821 11.398 16.380 30 LEU 43.217 8.976 18.891 31 PRO 44.359 5.861 16.908 32 LEU 41.815 3.693 18.822 33 GLN 38.138 4.741 18.599 34 CYS 35.258 3.099 20.499 35 TYR 31.488 3.074 19.946 36 GLY 30.241 2.479 23.474 37 SER 26.621 1.840 22.537 38 ILE 27.294 -1.255 20.403 39 GLY 30.472 -2.449 22.090 40 TYR 33.166 -2.276 19.405 41 CYS 36.488 -0.458 19.087 42 TRP 38.725 -0.021 16.048 43 CYS 41.797 1.780 14.737 44 VAL 41.581 4.878 12.529 45 PHE 43.897 6.722 10.159 46 PRO 44.786 10.356 10.876 47 ASN 41.794 11.369 8.733 48 GLY 39.281 9.443 10.833 49 THR 38.878 6.585 8.370 50 GLU 38.667 3.106 9.873 51 VAL 41.608 0.739 9.428 52 PRO 40.411 -2.444 7.646 53 ASN 39.739 -5.560 9.698 54 THR 40.285 -3.710 12.948 55 ARG 36.755 -3.688 14.465 56 SER 36.546 -6.016 17.460 57 ARG 35.823 -6.612 21.158 58 GLY 39.413 -7.652 21.734 59 HIS 42.697 -5.871 22.327 60 HIS 44.032 -3.407 19.829 61 ASN 47.437 -2.030 18.921 62 CYS 46.636 1.005 16.789 63 SER 49.355 3.334 15.589 64 GLU 49.699 7.017 14.663 65 SER 52.082 8.929 12.400 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C H H H H H H H H H 10 3 C S S S S S/S S S S 20 S S S S/T T T T/S S S S 30 S S S S S/T T T T/S S S 40 S S/S S S S/T T T T/S S S 50 S S C S S S S/S S S S 60 S/S S S S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 h H H H H H H h T 10 t S S t T T t 20 B t T T t B 30 e E E E E T T T T E 40 E E E e t T T t B 50 t T T t B S S 60 Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 LEU 61.9 41.9 79.1 2 THR 54.5 51.0 74.9 3 LYS 58.8 33.9 81.0 4 CYS 98.7 99.5 47.4 5 GLN 93.6 63.0 57.6 6 GLU 58.1 41.9 71.4 7 GLU 79.9 57.6 63.4 8 VAL 78.6 66.2 59.4 9 SER 38.3 45.8 69.1 10 HIS 29.5 19.7 82.2 11 ILE 108.6 75.7 59.2 12 PRO 35.8 28.8 80.0 13 ALA 9.0 12.4 78.2 14 VAL 4.6 3.9 75.8 15 HIS 107.6 71.6 62.1 16 PRO 23.8 19.1 80.0 17 GLY 16.1 46.3 74.1 18 SER 40.9 49.0 66.5 19 PHE 116.2 69.7 54.6 20 ARG 141.3 67.6 58.9 21 PRO 118.8 95.4 46.9 22 LYS 41.3 23.8 76.2 23 CYS 90.2 90.9 49.9 24 ASP 69.4 62.8 67.5 25 GLU 0.0 0.0 90.8 26 ASN 20.0 16.5 86.6 27 GLY 34.8 100.0 65.8 28 ASN 41.6 34.4 79.9 29 TYR 170.5 94.2 53.2 30 LEU 90.2 61.1 62.1 31 PRO 95.5 76.7 61.4 32 LEU 82.4 55.8 57.3 33 GLN 144.7 97.4 42.9 34 CYS 62.7 63.2 54.1 35 TYR 136.3 75.3 55.5 36 GLY 0.0 0.0 78.3 37 SER 49.0 58.6 66.6 38 ILE 73.5 51.2 67.5 39 GLY 8.6 24.8 77.7 40 TYR 102.4 56.6 66.1 41 CYS 68.4 69.0 50.4 42 TRP 186.5 91.0 44.1 43 CYS 86.7 87.4 43.9 44 VAL 115.6 97.3 55.2 45 PHE 86.2 51.7 58.8 46 PRO 40.1 32.2 71.0 47 ASN 30.5 25.3 73.4 48 GLY 32.1 92.2 57.9 49 THR 32.7 30.6 77.0 50 GLU 91.1 65.8 62.5 51 VAL 74.9 63.0 52.4 52 PRO 30.4 24.4 72.7 53 ASN 0.0 0.0 90.0 54 THR 88.7 83.0 53.0 55 ARG 119.5 57.2 60.5 56 SER 44.0 52.6 68.6 57 ARG 62.5 29.9 81.3 58 GLY 6.1 17.6 74.3 59 HIS 0.0 0.0 89.5 60 HIS 134.8 89.7 61.2 61 ASN 0.0 0.0 88.1 62 CYS 94.8 95.6 47.8 63 SER 7.0 8.4 83.8 64 GLU 19.6 14.1 73.8 65 SER 12.8 15.3 76.3