Protein Data Bank File : 1c7ka Title : HYDROLASE 19-FEB-00 1C7K Number of Amino Acid Residues : 132 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 THR VAL THR VAL THR TYR ASP PRO SER ASN 10 ALA PRO SER PHE GLN GLN GLU ILE ALA ASN 20 ALA ALA GLN ILE TRP ASN SER SER VAL ARG 30 ASN VAL GLN LEU ARG ALA GLY GLY ASN ALA 40 ASP PHE SER TYR TYR GLU GLY ASN ASP SER 50 ARG GLY SER TYR ALA GLN THR ASP GLY HIS 60 GLY ARG GLY TYR ILE PHE LEU ASP TYR GLN 70 GLN ASN GLN GLN TYR ASP SER THR ARG VAL 80 THR ALA HIS GLU THR GLY HIS VAL LEU GLY 90 LEU PRO ASP HIS TYR GLN GLY PRO CYS SER 100 GLU LEU MET SER GLY GLY GLY PRO GLY PRO 110 SER CYS THR ASN PRO TYR PRO ASN ALA GLN 120 GLU ARG SER ARG VAL ASN ALA LEU TRP ALA 130 ASN GLY Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 THR 0.0 131.3 175.4 -54.2 2 VAL -103.4 149.5 178.4 159.6 3 THR -109.3 129.0 173.9 -64.0 4 VAL -110.0 130.0 -171.1 176.0 5 THR -103.9 133.1 177.1 -60.5 6 TYR -120.4 158.7 177.0 63.7 -90.2 7 ASP -116.2 107.8 -179.9 178.1 6.3 8 PRO -90.4 0.2 -165.2 38.6 -39.1 9 SER -67.5 -22.1 179.8 72.4 10 ASN -89.6 11.0 175.0 -63.2 -69.5 11 ALA -128.2 68.6 -173.2 12 PRO -62.2 -24.2 -177.5 28.0 -42.4 13 SER -81.1 -9.6 -168.3 -54.3 14 PHE -119.0 18.8 -174.3 -72.1 -75.2 15 GLN -60.1 -45.6 -177.4 -70.7 -51.1 -80.4 16 GLN -66.6 -38.0 -175.8 -173.7 61.3 -124.4 17 GLU -73.2 -32.1 173.6 -69.8 -63.2 1.8 18 ILE -66.5 -44.1 175.4 -67.5 164.2 19 ALA -58.9 -44.7 179.4 20 ASN -59.9 -45.7 -176.8 -68.8 159.6 21 ALA -66.9 -37.4 178.2 22 ALA -65.6 -41.4 179.3 23 GLN -65.9 -37.4 176.2 -176.7 63.0 36.5 24 ILE -62.3 -47.3 177.8 -76.5 158.5 25 TRP -65.0 -45.1 -177.7 -82.2 109.3 26 ASN -60.2 -34.0 -179.0 -76.1 -15.3 27 SER -77.8 -11.6 -172.6 86.8 28 SER -104.0 -30.2 -173.2 -71.9 29 VAL -122.7 158.8 -172.4 -61.0 30 ARG -103.7 -38.3 -166.5 -172.6 179.8 -4.5 116.0 31 ASN -91.7 -7.5 176.4 -71.8 161.2 32 VAL -142.0 147.6 174.8 58.0 33 GLN -134.6 149.9 179.2 -64.4 -75.2 104.0 34 LEU -106.8 136.6 177.1 -59.7 166.8 35 ARG -139.4 140.4 173.5 -69.9 -78.6 -172.5 -81.8 36 ALA -76.7 141.1 170.3 37 GLY 174.4 -170.7 -178.3 38 GLY -81.9 169.8 -177.2 39 ASN 49.9 51.7 -168.5 -66.0 -28.1 40 ALA -74.9 150.9 172.8 41 ASP -76.1 -36.2 177.3 -59.6 123.0 42 PHE -145.6 161.6 -169.1 70.0 102.9 43 SER -138.0 154.8 175.5 -57.3 44 TYR -110.5 140.0 177.5 -64.5 -95.7 45 TYR -132.4 170.0 -178.6 -64.3 -86.8 46 GLU -141.8 158.1 174.6 63.1 -177.0 -115.9 47 GLY 165.6 -156.6 178.1 48 ASN -110.9 126.8 170.1 -87.4 -53.9 49 ASP -148.4 116.9 -176.3 -169.0 -47.4 50 SER -61.3 -17.7 175.0 68.0 51 ARG -71.7 -13.9 -173.2 -66.5 173.4 -76.4 -162.8 52 GLY 97.7 -169.4 177.2 53 SER -72.1 155.6 -179.2 -53.0 54 TYR -157.0 166.8 -179.6 60.2 85.1 55 ALA -125.5 132.3 170.8 56 GLN -108.3 99.9 -167.5 -177.9 79.6 -45.2 57 THR -151.6 151.1 171.3 -177.6 58 ASP -79.1 -2.9 -175.9 64.1 -2.1 59 GLY 74.7 9.4 175.0 60 HIS -139.1 51.5 169.2 -160.6 67.8 61 GLY 102.5 -12.6 -170.3 62 ARG -120.6 147.1 168.9 -70.8 -169.4 -175.8 105.1 63 GLY 130.6 -141.2 -179.9 64 TYR -154.5 161.3 -178.9 64.0 86.7 65 ILE -122.9 134.0 175.5 -68.6 169.9 66 PHE -106.5 122.0 178.6 -178.4 94.1 67 LEU -101.9 115.8 -177.3 -65.1 172.9 68 ASP -85.7 138.2 -178.8 172.0 -124.3 69 TYR -62.9 -44.9 -178.4 -68.1 -39.3 70 GLN -66.1 -45.3 -179.3 -84.2 -44.9 117.2 71 GLN -60.4 -39.5 -176.6 -172.3 -174.3 54.1 72 ASN -76.5 -11.7 169.8 -79.8 -84.8 73 GLN -91.2 -33.9 -175.2 -69.9 170.8 -90.8 74 GLN -84.8 -27.5 179.9 -71.0 -6.9 125.3 75 TYR -116.2 164.0 176.0 -65.7 -104.4 76 ASP -65.4 122.7 -174.1 -174.8 -88.8 77 SER -69.9 -28.8 174.9 -179.0 78 THR -65.4 -42.4 178.3 -38.2 79 ARG -63.9 -44.7 -179.7 174.1 172.0 172.5 96.0 80 VAL -60.1 -45.7 -175.5 170.3 81 THR -69.1 -42.0 179.2 -57.3 82 ALA -65.6 -37.8 178.0 83 HIS -59.7 -56.1 -177.3 169.7 91.3 84 GLU -63.2 -34.3 175.6 -63.9 -60.1 -31.1 85 THR -62.7 -31.8 173.3 -56.7 86 GLY -56.3 -34.1 176.4 87 HIS -66.1 -36.4 178.4 -68.8 -47.7 88 VAL -65.5 -30.7 177.5 173.8 89 LEU -80.4 -11.2 171.1 -64.8 175.6 90 GLY 119.9 -0.7 -175.8 91 LEU -90.1 141.9 -178.4 -63.6 -178.6 92 PRO -87.9 162.6 167.8 33.6 -35.4 93 ASP -62.8 139.5 174.9 -77.0 125.8 94 HIS -140.3 70.5 -166.7 -173.3 -128.0 95 TYR -63.1 -21.9 -176.7 -61.9 -45.6 96 GLN -83.0 -3.3 -176.9 65.3 -88.2 45.7 97 GLY -75.2 163.4 179.4 98 PRO -79.6 176.3 179.6 35.0 -41.3 99 CYS -59.2 -29.8 178.4 -176.5 100 SER -66.1 -13.6 170.5 58.7 101 GLU -90.9 122.2 174.9 -73.4 -173.8 18.4 102 LEU -66.6 -32.7 -172.2 175.3 59.5 103 MET -81.6 4.4 166.5 -59.1 -47.5 -62.9 104 SER -78.8 -10.6 171.8 64.5 105 GLY 61.1 -131.1 -178.3 106 GLY -81.6 -1.9 -177.3 107 GLY -50.2 -51.1 -180.0 108 PRO -71.6 -9.2 171.9 -19.0 30.9 109 GLY 96.5 170.5 -173.3 110 PRO -70.5 -14.2 172.2 13.8 -15.4 111 SER -72.7 -15.3 177.2 66.5 112 CYS -86.5 117.9 -175.8 173.5 113 THR -114.6 1.0 -174.3 64.0 114 ASN -63.4 120.0 178.8 169.8 41.8 115 PRO -101.0 4.7 -174.0 40.0 -38.5 116 TYR -95.9 138.3 170.1 -65.5 111.6 117 PRO -68.7 149.4 178.5 26.7 -33.8 118 ASN -83.8 -178.6 -176.6 73.4 12.3 119 ALA -59.1 -40.7 -177.2 120 GLN -70.3 -41.3 176.5 -59.0 58.4 45.5 121 GLU -61.5 -43.0 174.9 -68.0 171.2 -37.5 122 ARG -59.9 -46.9 -179.7 -60.7 174.6 -165.4 -148.2 123 SER -60.5 -40.0 -178.1 -162.1 124 ARG -67.8 -42.6 176.7 -66.7 -154.2 -74.9 -30.0 125 VAL -62.2 -44.6 178.0 168.4 126 ASN -56.6 -41.6 179.4 -80.0 -34.4 127 ALA -68.4 -37.7 -179.4 128 LEU -64.8 -25.0 -177.7 -73.2 167.9 129 TRP -107.6 7.6 -174.5 -69.3 90.5 130 ALA -59.3 -35.1 178.8 131 ASN -111.9 27.1 179.4 -54.4 -74.5 132 GLY 84.9 -167.9 0.0 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 THR 41.127 -0.127 3.354 2 VAL 43.838 2.149 4.770 3 THR 44.129 3.172 8.387 4 VAL 45.001 6.753 9.323 5 THR 46.057 7.158 12.959 6 TYR 45.175 10.224 15.012 7 ASP 46.254 11.516 18.394 8 PRO 43.437 13.223 20.388 9 SER 45.361 13.667 23.590 10 ASN 46.158 17.414 23.232 11 ALA 42.478 18.375 22.971 12 PRO 41.229 17.297 26.360 13 SER 38.012 19.299 26.184 14 PHE 36.952 17.623 22.921 15 GLN 37.482 13.902 23.566 16 GLN 33.865 12.887 23.071 17 GLU 33.397 15.022 19.949 18 ILE 36.611 13.656 18.374 19 ALA 35.462 10.106 19.050 20 ASN 32.071 10.989 17.597 21 ALA 33.607 12.530 14.484 22 ALA 35.900 9.585 13.923 23 GLN 32.999 7.130 14.292 24 ILE 30.895 9.203 11.816 25 TRP 33.632 9.083 9.186 26 ASN 34.351 5.394 9.834 27 SER 30.623 4.627 9.455 28 SER 30.420 6.601 6.234 29 VAL 33.374 5.579 4.094 30 ARG 34.948 2.308 2.918 31 ASN 38.476 2.987 1.756 32 VAL 39.977 4.772 4.815 33 GLN 39.409 4.310 8.498 34 LEU 40.491 6.449 11.436 35 ARG 41.936 4.920 14.586 36 ALA 43.431 6.535 17.719 37 GLY 46.930 5.436 18.546 38 GLY 50.628 6.098 18.659 39 ASN 52.988 7.337 15.949 40 ALA 49.979 9.284 14.714 41 ASP 49.540 10.822 11.277 42 PHE 47.557 13.803 12.526 43 SER 46.715 15.373 15.919 44 TYR 44.069 17.570 17.543 45 TYR 44.709 20.706 19.652 46 GLU 42.427 23.296 21.271 47 GLY 42.454 26.953 22.217 48 ASN 41.177 30.382 21.193 49 ASP 41.314 31.712 17.658 50 SER 38.684 34.225 16.596 51 ARG 38.852 32.774 13.035 52 GLY 37.425 29.536 14.377 53 SER 38.700 25.983 14.054 54 TYR 41.101 25.099 11.269 55 ALA 43.202 22.353 9.737 56 GLN 46.903 22.463 8.819 57 THR 47.075 19.469 6.500 58 ASP 48.389 18.032 3.255 59 GLY 44.863 16.726 2.631 60 HIS 45.992 13.095 2.702 61 GLY 46.105 12.131 6.331 62 ARG 48.809 14.339 7.901 63 GLY 48.968 17.473 9.955 64 TYR 46.825 18.849 12.771 65 ILE 43.455 20.345 13.587 66 PHE 42.937 23.309 15.950 67 LEU 39.540 23.340 17.709 68 ASP 38.427 26.831 18.785 69 TYR 36.443 27.243 21.963 70 GLN 33.983 29.889 20.741 71 GLN 33.084 28.181 17.485 72 ASN 32.504 24.848 19.221 73 GLN 30.108 26.486 21.666 74 GLN 28.188 28.585 19.121 75 TYR 27.984 25.789 16.493 76 ASP 27.467 22.058 16.903 77 SER 30.897 20.687 17.886 78 THR 30.366 17.340 16.194 79 ARG 29.752 19.093 12.857 80 VAL 32.769 21.365 13.353 81 THR 35.077 18.510 14.289 82 ALA 33.845 16.177 11.540 83 HIS 34.150 19.083 9.065 84 GLU 37.746 19.884 9.854 85 THR 38.610 16.178 9.842 86 GLY 37.165 16.153 6.304 87 HIS 40.005 18.460 5.245 88 VAL 42.589 15.953 6.512 89 LEU 40.794 13.340 4.399 90 GLY 41.139 15.594 1.330 91 LEU 37.845 17.543 0.981 92 PRO 37.820 21.313 0.356 93 ASP 35.757 24.089 1.909 94 HIS 32.499 24.799 0.061 95 TYR 30.974 27.559 2.210 96 GLN 28.071 28.303 -0.151 97 GLY 26.755 24.732 0.178 98 PRO 23.665 23.752 2.207 99 CYS 23.554 22.066 5.624 100 SER 23.352 18.661 3.926 101 GLU 26.985 19.221 2.845 102 LEU 29.362 18.673 5.765 103 MET 31.998 20.670 3.896 104 SER 29.977 23.858 3.895 105 GLY 31.099 24.190 7.498 106 GLY 29.690 27.205 9.242 107 GLY 28.134 28.660 6.034 108 PRO 24.573 27.491 6.864 109 GLY 24.851 28.869 10.418 110 PRO 24.480 27.499 13.922 111 SER 20.975 26.081 13.301 112 CYS 22.668 23.460 11.077 113 THR 23.808 20.570 13.273 114 ASN 24.291 17.814 10.663 115 PRO 27.670 16.102 11.119 116 TYR 27.360 13.498 8.359 117 PRO 28.962 13.773 4.903 118 ASN 26.528 13.445 1.979 119 ALA 26.662 10.836 -0.749 120 GLN 28.955 12.938 -3.013 121 GLU 31.319 13.758 -0.154 122 ARG 31.511 10.047 0.763 123 SER 32.165 9.086 -2.840 124 ARG 34.935 11.634 -3.175 125 VAL 36.700 10.457 -0.015 126 ASN 36.432 6.838 -1.226 127 ALA 37.967 7.762 -4.521 128 LEU 40.788 9.792 -2.926 129 TRP 41.784 6.780 -0.788 130 ALA 41.137 4.024 -3.379 131 ASN 44.828 3.541 -3.922 132 GLY 46.043 4.423 -0.384 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S S S S S S S/T T T 10 T C C H H H H H H H 20 H H H H H H H H H C 30 S S S S S S S C C C 40 S S S S S/S S S S T T 50 T T/S S S S S S S/T T T 60 T/S S S S/S S S S S/H H H 70 H H H H H H H H H H 80 H H H H H H H H H H/S 90 S S S S S S S S S C 100 T T T T/T T T T C C C 110 S S S S S/S S S S/H H H 120 H H H H H H H H H H/S 130 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 E E 10 g G G h H H H H H H 20 H H H H H H H H h S 30 e E E E E E e S S 40 e E E E E E E t T 50 T t E E E E e S S 60 S e E E E E E E H H 70 H H H H h h H H H H 80 H H H H H H H H H h 90 t t T T t t T T 100 g G G G g T T T t T 110 T t S h H H 120 H H H H H H H H h T 130 T t Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 THR 61.6 57.6 77.0 2 VAL 66.7 56.2 64.8 3 THR 51.8 48.5 65.6 4 VAL 113.0 95.1 38.2 5 THR 80.1 75.0 67.6 6 TYR 164.3 90.8 36.0 7 ASP 73.2 66.2 64.8 8 PRO 96.8 77.8 53.8 9 SER 25.3 30.3 84.5 10 ASN 57.2 47.3 74.9 11 ALA 72.6 100.0 47.4 12 PRO 48.1 38.6 81.0 13 SER 34.7 41.5 69.3 14 PHE 150.9 90.5 49.0 15 GLN 76.5 51.5 67.8 16 GLN 25.2 17.0 83.2 17 GLU 95.5 68.9 64.9 18 ILE 142.0 99.0 38.2 19 ALA 27.8 38.4 80.2 20 ASN 70.0 57.9 67.1 21 ALA 72.6 100.0 51.0 22 ALA 66.7 91.9 59.8 23 GLN 32.1 21.6 79.1 24 ILE 124.2 86.5 45.4 25 TRP 204.1 99.6 28.7 26 ASN 106.2 87.9 69.8 27 SER 36.5 43.6 80.4 28 SER 82.7 98.9 56.3 29 VAL 116.6 98.1 51.4 30 ARG 54.9 26.3 87.8 31 ASN 95.1 78.6 59.8 32 VAL 117.8 99.2 31.5 33 GLN 110.8 74.6 66.8 34 LEU 145.7 98.6 32.8 35 ARG 80.7 38.6 77.3 36 ALA 37.7 51.9 64.4 37 GLY 6.2 17.9 73.5 38 GLY 0.0 0.0 80.2 39 ASN 0.0 0.0 90.9 40 ALA 67.2 92.5 66.8 41 ASP 69.9 63.2 69.1 42 PHE 164.8 98.8 40.4 43 SER 63.5 75.9 59.4 44 TYR 179.3 99.1 31.3 45 TYR 95.3 52.7 63.4 46 GLU 126.6 91.4 52.0 47 GLY 20.4 58.7 53.9 48 ASN 33.0 27.3 71.7 49 ASP 87.5 79.1 65.8 50 SER 0.0 0.0 88.3 51 ARG 31.8 15.2 90.2 52 GLY 30.7 88.3 70.3 53 SER 83.6 100.0 52.5 54 TYR 104.0 57.4 68.3 55 ALA 71.4 98.3 47.8 56 GLN 42.3 28.4 74.5 57 THR 94.3 88.2 61.8 58 ASP 47.9 43.3 76.9 59 GLY 21.9 62.9 72.1 60 HIS 86.1 57.4 75.7 61 GLY 32.6 93.8 45.1 62 ARG 53.7 25.7 85.1 63 GLY 13.0 37.3 64.2 64 TYR 104.7 57.9 58.8 65 ILE 143.5 100.0 39.1 66 PHE 136.3 81.7 57.2 67 LEU 147.8 100.0 35.6 68 ASP 107.1 96.9 60.3 69 TYR 106.3 58.7 72.0 70 GLN 47.9 32.3 84.9 71 GLN 106.9 71.9 55.9 72 ASN 118.4 98.0 52.1 73 GLN 41.3 27.8 85.2 74 GLN 58.3 39.2 75.8 75 TYR 120.7 66.7 57.5 76 ASP 66.7 60.4 67.6 77 SER 71.7 85.7 59.7 78 THR 87.2 81.6 58.5 79 ARG 200.2 95.8 55.0 80 VAL 105.9 89.1 54.8 81 THR 106.9 100.0 45.8 82 ALA 72.6 100.0 49.4 83 HIS 140.9 93.8 52.3 84 GLU 125.1 90.3 50.5 85 THR 106.8 99.9 40.7 86 GLY 34.8 100.0 48.3 87 HIS 127.0 84.6 63.1 88 VAL 118.8 100.0 41.7 89 LEU 147.3 99.7 31.0 90 GLY 29.3 84.2 64.7 91 LEU 146.4 99.1 37.8 92 PRO 41.2 33.1 80.1 93 ASP 72.2 65.3 65.8 94 HIS 79.9 53.2 75.7 95 TYR 49.4 27.3 83.0 96 GLN 25.9 17.4 80.6 97 GLY 32.5 93.3 56.0 98 PRO 46.3 37.2 78.7 99 CYS 59.1 59.6 58.5 100 SER 21.3 25.5 73.5 101 GLU 106.8 77.1 65.4 102 LEU 147.7 99.9 50.4 103 MET 158.2 99.2 50.9 104 SER 83.6 100.0 62.3 105 GLY 29.4 84.5 66.8 106 GLY 20.7 59.4 68.2 107 GLY 18.1 52.1 71.1 108 PRO 101.5 81.5 67.1 109 GLY 20.3 58.4 65.8 110 PRO 58.7 47.1 70.1 111 SER 0.0 0.0 87.4 112 CYS 92.8 93.5 57.9 113 THR 36.4 34.0 76.9 114 ASN 84.8 70.1 59.6 115 PRO 101.9 81.9 44.6 116 TYR 68.5 37.8 70.5 117 PRO 124.4 99.9 41.6 118 ASN 83.1 68.7 69.2 119 ALA 15.5 21.4 79.4 120 GLN 32.1 21.6 80.0 121 GLU 136.1 98.2 50.4 122 ARG 126.7 60.7 64.7 123 SER 20.1 24.0 78.8 124 ARG 105.6 50.5 58.9 125 VAL 118.8 100.0 34.7 126 ASN 101.3 83.8 63.3 127 ALA 14.9 20.5 77.7 128 LEU 71.3 48.2 73.5 129 TRP 199.7 97.4 45.8 130 ALA 40.3 55.5 79.3 131 ASN 3.5 2.9 86.6 132 GLY 21.7 62.3 63.5