Protein Data Bank File : 1gefb Title : HYDROLASE 08-NOV-00 1GEF Number of Amino Acid Residues : 116 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 MET TYR ARG LYS GLY ALA GLN ALA GLU ARG 10 GLU LEU ILE LYS LEU LEU GLU LYS HIS GLY 20 PHE ALA VAL VAL ARG SER ALA GLY SER LYS 30 LYS VAL ASP LEU VAL ALA GLY ASN GLY LYS 40 LYS TYR LEU CYS ILE GLU VAL LYS VAL THR 50 LYS LYS ASP HIS LEU TYR VAL GLY LYS ARG 60 ASP MET GLY ARG LEU ILE GLU PHE SER ARG 70 ARG PHE GLY GLY ILE PRO VAL LEU ALA VAL 80 LYS PHE LEU ASN VAL GLY TRP ARG PHE ILE 90 GLU VAL SER PRO LYS ILE GLU LYS PHE VAL 100 PHE THR PRO SER SER GLY VAL SER LEU GLU 110 VAL LEU LEU GLY ILE GLN Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 MET 0.0 -44.8 -177.8 173.1 177.8 -76.5 2 TYR -104.4 6.8 -179.1 -54.9 104.5 3 ARG -64.1 -54.8 -178.9 -68.1 177.0 -73.9 -89.1 4 LYS -60.3 -34.1 179.2 67.8 176.4 63.8 65.7 5 GLY -70.8 -42.8 -179.8 6 ALA -61.7 -38.9 179.1 7 GLN -67.4 -44.7 180.0 -177.4 -178.8 -42.5 8 ALA -59.7 -42.0 179.9 9 GLU -60.2 -43.2 179.5 -72.0 174.8 40.8 10 ARG -63.9 -40.6 -179.7 -81.7 177.5 -76.0 158.4 11 GLU -68.5 -40.7 -179.7 -52.5 173.9 -34.3 12 LEU -67.1 -35.3 179.7 -177.9 53.7 13 ILE -58.7 -43.2 179.7 -71.9 169.0 14 LYS -62.9 -45.3 179.1 -62.0 -67.1 179.3 51.5 15 LEU -57.9 -43.1 179.9 -80.0 44.1 16 LEU -66.4 -46.6 179.2 -67.6 165.8 17 GLU -58.3 -41.7 179.6 -75.5 171.3 169.9 18 LYS -58.6 -24.0 179.3 -173.8 178.8 73.7 -65.7 19 HIS -98.6 12.5 177.7 -77.1 65.0 20 GLY 92.6 7.4 -180.0 21 PHE -93.1 144.4 176.2 -78.5 -96.9 22 ALA -98.4 129.4 -176.5 23 VAL -126.7 146.1 176.4 -168.6 24 VAL -125.1 139.5 178.9 -67.0 25 ARG -98.1 124.2 -179.0 -180.0 160.9 61.5 75.2 26 SER -65.6 129.5 179.4 169.2 27 ALA -75.5 117.7 -179.3 28 GLY 87.2 -18.3 179.6 29 SER 54.2 39.5 -179.1 -62.6 30 LYS -50.4 -50.6 -179.2 -62.6 -178.1 178.6 -60.0 31 LYS -106.5 -48.0 178.8 -85.9 57.5 174.5 54.4 32 VAL -141.0 174.0 -179.9 -56.0 33 ASP -93.6 -43.4 -179.4 -63.0 -51.0 34 LEU -135.9 154.3 175.1 -48.4 176.0 35 VAL -133.9 125.3 -179.2 172.1 36 ALA -129.9 149.6 178.8 37 GLY -147.9 146.4 179.7 38 ASN -124.6 23.8 179.7 72.4 -18.3 39 GLY 80.6 0.4 178.8 40 LYS -132.3 -47.1 179.9 -66.7 178.8 -65.7 -176.3 41 LYS -133.0 163.7 179.2 -58.0 -165.4 -172.7 -53.3 42 TYR -126.4 142.8 178.7 -55.5 -90.8 43 LEU -125.9 139.4 177.2 -48.2 172.7 44 CYS -118.9 116.5 -173.9 -62.0 45 ILE -117.7 134.7 176.8 -50.6 168.6 46 GLU -108.3 122.8 -178.9 175.0 61.1 13.5 47 VAL -105.7 127.6 178.5 177.1 48 LYS -120.1 151.3 179.5 -55.5 -64.3 -173.1 -174.4 49 VAL -139.6 139.1 178.7 -174.3 50 THR -152.2 147.2 178.9 -175.7 51 LYS -85.5 -15.8 -178.9 -58.8 -173.8 -60.4 178.9 52 LYS -81.8 175.3 179.0 -59.1 163.9 64.8 -178.8 53 ASP -100.2 18.0 177.9 55.9 21.2 54 HIS -161.5 153.4 -179.0 61.6 -71.2 55 LEU -143.5 135.5 178.7 -179.4 69.5 56 TYR -90.6 127.8 180.0 -71.6 -76.0 57 VAL -117.8 117.9 -179.0 -173.4 58 GLY -79.5 164.0 -179.6 59 LYS -73.2 -45.0 -179.7 56.0 -179.4 179.0 -60.5 60 ARG -57.8 -47.1 179.8 -179.9 174.3 -179.7 176.2 61 ASP -55.7 -44.5 179.5 -174.7 22.4 62 MET -73.7 -29.5 179.1 -65.7 -55.0 91.5 63 GLY -62.5 -38.1 179.1 64 ARG -66.2 -43.9 179.6 -177.2 -165.2 61.9 -94.9 65 LEU -61.8 -49.0 -179.5 170.2 63.5 66 ILE -59.5 -44.9 180.0 -68.4 173.2 67 GLU -64.2 -41.3 179.7 177.2 49.5 39.5 68 PHE -68.8 -40.1 -179.3 177.8 -84.5 69 SER -68.0 -34.6 179.5 -58.3 70 ARG -64.0 -47.7 179.8 -171.1 -150.1 68.4 -177.1 71 ARG -65.6 -48.3 -179.1 -76.7 176.3 57.8 67.1 72 PHE -63.4 -44.8 -177.9 -172.5 -87.1 73 GLY 101.9 43.3 179.2 74 GLY -133.9 167.4 179.8 75 ILE -82.3 122.6 179.8 -60.6 166.1 76 PRO -73.4 109.5 -178.3 33.7 -42.0 77 VAL -116.4 136.0 176.7 179.6 78 LEU -105.5 123.2 179.3 171.5 62.1 79 ALA -115.0 119.1 -179.5 80 VAL -116.7 124.8 178.2 -179.7 81 LYS -100.9 109.1 178.0 -179.4 -171.5 177.0 -173.1 82 PHE -89.8 109.5 -178.7 -68.6 92.9 83 LEU -54.8 131.6 179.6 -66.1 169.3 84 ASN 78.0 6.8 178.6 -65.9 159.2 85 VAL -135.1 -53.1 179.2 31.9 86 GLY 151.6 -176.4 -179.8 87 TRP -97.1 145.3 177.3 -71.8 91.2 88 ARG -139.1 140.6 -177.7 -64.0 -59.7 -69.9 -178.8 89 PHE -127.5 154.5 178.4 -54.1 -97.7 90 ILE -154.1 132.5 177.0 -171.1 176.7 91 GLU -80.1 120.2 -178.8 170.4 174.9 168.8 92 VAL -80.5 138.5 -178.9 67.5 93 SER -98.2 149.8 180.0 49.2 94 PRO -53.0 -34.3 178.7 -31.0 43.9 95 LYS -79.4 50.6 -178.9 49.8 -172.5 -68.2 -177.2 96 ILE -83.9 147.1 179.5 -175.0 61.9 97 GLU -152.2 176.3 -179.8 -167.2 174.5 -59.6 98 LYS -67.2 135.6 179.4 52.7 -160.1 -63.1 -61.3 99 PHE -153.6 166.0 179.2 66.7 -71.0 100 VAL -108.3 132.6 -178.1 -176.3 101 PHE -108.3 127.0 179.2 -156.7 73.3 102 THR -120.5 167.5 -179.8 59.8 103 PRO -60.5 8.8 179.0 23.0 -38.4 104 SER -131.1 10.2 -178.5 65.8 105 SER -76.6 -40.0 179.9 -62.7 106 GLY -109.7 -129.7 179.4 107 VAL -141.9 170.2 179.3 -65.4 108 SER -73.2 163.0 179.7 70.2 109 LEU -61.6 -39.4 -179.8 -175.8 56.3 110 GLU -61.6 -42.3 179.7 -66.6 66.0 45.5 111 VAL -74.5 -34.1 178.9 44.8 112 LEU -59.6 -47.1 -178.1 175.4 74.1 113 LEU -75.5 -13.6 179.6 -59.0 173.9 114 GLY 103.0 -8.9 179.2 115 ILE -62.6 -27.2 179.9 -50.5 -61.2 116 GLN 61.4 -119.9 0.0 -166.3 65.7 60.5 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 MET 8.944 19.372 -1.775 2 TYR 8.011 16.060 -0.155 3 ARG 4.208 16.295 -0.043 4 LYS 3.320 14.461 -3.263 5 GLY 5.880 11.816 -2.423 6 ALA 4.645 11.274 1.140 7 GLN 1.113 10.880 -0.223 8 ALA 2.165 8.435 -2.954 9 GLU 3.973 6.230 -0.437 10 ARG 0.872 5.945 1.759 11 GLU -1.295 5.035 -1.227 12 LEU 1.122 2.419 -2.527 13 ILE 1.332 0.842 0.922 14 LYS -2.443 0.311 0.807 15 LEU -2.322 -1.216 -2.688 16 LEU 0.337 -3.695 -1.571 17 GLU -1.508 -4.592 1.631 18 LYS -4.655 -5.139 -0.435 19 HIS -2.617 -7.775 -2.263 20 GLY -1.460 -9.567 0.879 21 PHE 1.869 -7.856 1.530 22 ALA 3.021 -6.653 4.943 23 VAL 4.818 -3.352 4.346 24 VAL 7.110 -1.057 6.295 25 ARG 7.925 2.545 5.371 26 SER 11.587 3.431 5.771 27 ALA 12.228 6.265 8.216 28 GLY 14.126 8.949 6.322 29 SER 14.192 6.728 3.213 30 LYS 17.984 6.489 3.425 31 LYS 18.222 3.556 0.999 32 VAL 14.679 2.801 -0.185 33 ASP 11.132 3.995 0.584 34 LEU 9.342 0.714 1.286 35 VAL 10.114 -2.920 2.010 36 ALA 7.315 -5.439 1.557 37 GLY 7.020 -9.186 2.010 38 ASN 4.172 -11.667 1.655 39 GLY 5.660 -14.799 3.174 40 LYS 6.827 -15.767 -0.308 41 LYS 8.699 -12.824 -1.833 42 TYR 10.265 -9.563 -0.688 43 LEU 10.233 -6.206 -2.473 44 CYS 12.514 -3.192 -1.921 45 ILE 10.836 -0.149 -3.409 46 GLU 11.906 3.297 -4.551 47 VAL 8.845 5.481 -5.098 48 LYS 8.802 8.365 -7.560 49 VAL 5.927 10.764 -8.272 50 THR 5.476 13.264 -11.093 51 LYS 2.806 15.535 -12.573 52 LYS 4.439 15.117 -15.981 53 ASP 3.988 12.334 -18.535 54 HIS 7.634 11.305 -18.329 55 LEU 10.342 10.939 -15.708 56 TYR 14.127 10.776 -15.926 57 VAL 15.654 8.011 -13.809 58 GLY 19.395 8.171 -13.192 59 LYS 21.856 5.300 -12.900 60 ARG 23.247 6.245 -9.488 61 ASP 19.762 6.458 -7.981 62 MET 18.996 2.954 -9.283 63 GLY 22.438 1.742 -8.252 64 ARG 21.571 2.464 -4.623 65 LEU 18.266 0.563 -4.898 66 ILE 19.929 -2.427 -6.564 67 GLU 22.749 -2.612 -4.004 68 PHE 20.374 -2.437 -1.053 69 SER 18.034 -5.020 -2.571 70 ARG 20.999 -7.265 -3.332 71 ARG 22.139 -7.135 0.303 72 PHE 18.647 -7.407 1.750 73 GLY 17.504 -10.208 -0.513 74 GLY 14.577 -8.519 -2.222 75 ILE 13.451 -7.567 -5.724 76 PRO 14.564 -3.993 -6.629 77 VAL 11.388 -2.241 -7.756 78 LEU 10.874 1.244 -9.135 79 ALA 7.309 2.455 -8.545 80 VAL 6.245 5.568 -10.443 81 LYS 2.971 7.344 -9.787 82 PHE 2.034 9.485 -12.800 83 LEU -0.443 11.983 -11.350 84 ASN -3.864 11.859 -13.024 85 VAL -3.069 8.647 -14.903 86 GLY -1.741 5.842 -12.699 87 TRP 1.014 3.608 -11.333 88 ARG 3.640 1.770 -13.368 89 PHE 6.271 -0.608 -12.009 90 ILE 9.522 -2.095 -13.217 91 GLU 12.026 -4.480 -11.683 92 VAL 15.335 -2.644 -12.119 93 SER 18.313 -4.618 -13.418 94 PRO 21.945 -4.440 -12.182 95 LYS 22.806 -3.456 -15.744 96 ILE 21.045 -0.183 -14.952 97 GLU 21.656 3.070 -16.797 98 LYS 19.878 6.378 -17.390 99 PHE 16.447 6.072 -19.017 100 VAL 13.115 7.897 -19.361 101 PHE 10.014 6.386 -17.767 102 THR 6.555 7.001 -19.212 103 PRO 3.125 5.676 -18.187 104 SER 3.727 2.790 -20.606 105 SER 7.318 1.825 -19.676 106 GLY 6.823 -0.880 -17.045 107 VAL 3.755 -2.826 -15.940 108 SER 0.708 -2.619 -13.659 109 LEU 1.014 -3.786 -10.049 110 GLU -1.160 -6.798 -10.858 111 VAL 1.084 -7.942 -13.712 112 LEU 4.226 -7.184 -11.717 113 LEU 3.056 -9.495 -8.919 114 GLY 1.891 -12.288 -11.210 115 ILE -1.815 -11.712 -10.662 116 GLN -1.799 -10.765 -14.355 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 H H H H H H H H H H/S 20 S S S S S S/T T T T/T T 30 T T S S S S S/T T T T/S 40 S S S S S S S S S S 50 S C S S S S S S/H H H 60 H H H H H H H H H H 70 H H H/S S S S S S/S S S 80 S S/T T T T S S S S S 90 S S S S S S S S/S S S 100 S S S C S S S S/H H H 110 H H H H/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 H 10 H H H H H H H H h T 20 t E E E E e t T T t 30 S e E E E E e S S 40 e E E E E E E E E E 50 S S S E E E h H H 60 H H H H H H H H H H 70 H H h t E E E E E E 80 E E e T T E E E E E 90 E e S S E E 100 E t T T t S B h H H 110 H H h T t Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 MET 23.1 14.5 85.0 2 TYR 17.8 9.8 80.2 3 ARG 16.2 7.7 91.5 4 LYS 88.4 51.0 62.8 5 GLY 15.0 43.0 61.7 6 ALA 26.2 36.1 81.2 7 GLN 65.1 43.8 82.2 8 ALA 72.6 100.0 44.7 9 GLU 114.8 82.8 51.3 10 ARG 68.9 33.0 75.1 11 GLU 84.3 60.8 64.1 12 LEU 147.7 100.0 23.9 13 ILE 118.6 82.6 48.2 14 LYS 43.0 24.8 80.3 15 LEU 97.2 65.8 55.5 16 LEU 147.2 99.6 24.3 17 GLU 71.6 51.6 68.3 18 LYS 52.1 30.0 77.3 19 HIS 123.5 82.3 52.5 20 GLY 0.0 0.0 80.7 21 PHE 158.7 95.2 44.6 22 ALA 0.0 0.1 83.0 23 VAL 118.6 99.8 40.9 24 VAL 21.6 18.2 77.4 25 ARG 91.1 43.6 72.5 26 SER 53.4 63.9 70.8 27 ALA 0.0 0.0 92.3 28 GLY 0.0 0.0 81.3 29 SER 57.7 69.0 82.2 30 LYS 21.7 12.5 84.2 31 LYS 72.1 41.6 61.5 32 VAL 115.8 97.5 44.9 33 ASP 99.9 90.4 59.0 34 LEU 147.8 100.0 31.9 35 VAL 94.6 79.7 38.7 36 ALA 71.9 99.1 39.6 37 GLY 26.5 76.2 57.0 38 ASN 98.1 81.1 55.9 39 GLY 0.0 0.0 83.2 40 LYS 32.9 19.0 87.9 41 LYS 49.8 28.7 70.7 42 TYR 72.6 40.1 69.1 43 LEU 141.9 96.0 28.0 44 CYS 99.2 100.0 38.1 45 ILE 141.3 98.4 33.1 46 GLU 123.5 89.1 54.2 47 VAL 118.2 99.5 36.6 48 LYS 122.9 70.9 55.9 49 VAL 116.3 97.9 38.6 50 THR 95.8 89.6 42.7 51 LYS 39.1 22.5 73.6 52 LYS 62.0 35.8 79.8 53 ASP 19.2 17.4 69.5 54 HIS 97.3 64.8 58.0 55 LEU 111.2 75.3 46.2 56 TYR 46.8 25.9 72.2 57 VAL 116.2 97.8 40.6 58 GLY 8.6 24.8 69.6 59 LYS 53.9 31.1 69.2 60 ARG 0.0 0.0 88.0 61 ASP 80.9 73.2 66.0 62 MET 159.4 100.0 33.2 63 GLY 12.8 36.8 66.2 64 ARG 134.6 64.4 76.6 65 LEU 147.8 100.0 45.4 66 ILE 121.7 84.8 45.2 67 GLU 69.2 50.0 70.3 68 PHE 115.1 69.0 44.1 69 SER 82.9 99.2 46.3 70 ARG 58.5 28.0 83.3 71 ARG 52.9 25.3 87.9 72 PHE 92.2 55.3 55.0 73 GLY 2.9 8.4 82.0 74 GLY 31.6 90.9 51.8 75 ILE 91.6 63.8 52.0 76 PRO 105.6 84.8 53.6 77 VAL 118.2 99.5 35.0 78 LEU 147.7 99.9 26.0 79 ALA 72.6 100.0 32.8 80 VAL 118.8 100.0 31.7 81 LYS 147.4 85.0 49.1 82 PHE 166.8 100.0 43.9 83 LEU 110.2 74.5 55.4 84 ASN 0.0 0.0 85.6 85 VAL 57.9 48.7 66.4 86 GLY 8.2 23.5 70.4 87 TRP 177.3 86.5 40.3 88 ARG 149.6 71.6 60.9 89 PHE 165.1 99.0 31.2 90 ILE 88.8 61.9 52.7 91 GLU 56.0 40.4 62.6 92 VAL 114.4 96.3 35.5 93 SER 38.1 45.6 57.8 94 PRO 33.8 27.2 65.9 95 LYS 7.4 4.2 86.8 96 ILE 121.1 84.4 52.8 97 GLU 26.6 19.2 72.3 98 LYS 42.6 24.6 80.1 99 PHE 111.7 67.0 51.4 100 VAL 67.0 56.4 55.0 101 PHE 166.7 99.9 34.1 102 THR 60.5 56.6 61.7 103 PRO 92.3 74.1 41.6 104 SER 14.7 17.6 86.3 105 SER 58.3 69.8 70.5 106 GLY 29.9 86.0 54.3 107 VAL 67.4 56.7 61.9 108 SER 47.5 56.8 69.1 109 LEU 140.3 95.0 33.8 110 GLU 69.7 50.3 60.2 111 VAL 80.5 67.7 63.2 112 LEU 125.8 85.1 40.7 113 LEU 132.8 89.8 36.5 114 GLY 2.8 8.1 84.7 115 ILE 45.8 31.9 68.2 116 GLN 26.9 18.1 74.8