Protein Data Bank File : 1ecma Title : CHORISMATE MUTASE 28-NOV-94 1ECM Number of Amino Acid Residues : 91 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 ASN PRO LEU LEU ALA LEU ARG GLU LYS ILE 10 SER ALA LEU ASP GLU LYS LEU LEU ALA LEU 20 LEU ALA GLU ARG ARG GLU LEU ALA VAL GLU 30 VAL GLY LYS ALA LYS LEU LEU SER HIS ARG 40 PRO VAL ARG ASP ILE ASP ARG GLU ARG ASP 50 LEU LEU GLU ARG LEU ILE THR LEU GLY LYS 60 ALA HIS HIS LEU ASP ALA HIS TYR ILE THR 70 ARG LEU PHE GLN LEU ILE ILE GLU ASP SER 80 VAL LEU THR GLN GLN ALA LEU LEU GLN GLN 90 HIS Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 ASN 0.0 140.4 179.8 -172.8 -86.4 2 PRO -58.9 -60.0 -179.0 27.6 -43.4 3 LEU -52.4 -41.9 -178.4 -152.3 57.6 4 LEU -66.8 -43.5 -179.9 -66.2 -174.2 5 ALA -61.4 -35.3 179.6 6 LEU -71.1 -45.0 178.9 -64.4 176.7 7 ARG -58.1 -35.5 178.4 -75.4 179.1 172.3 -178.0 8 GLU -66.4 -31.4 178.9 -67.8 -168.4 -12.4 9 LYS -72.2 -39.6 178.6 -80.6 -175.5 177.7 178.1 10 ILE -64.3 -46.4 -179.7 -72.3 179.9 11 SER -60.8 -35.0 178.9 -60.6 12 ALA -72.7 -38.6 178.6 13 LEU -65.3 -45.5 179.2 -174.6 157.6 14 ASP -59.3 -30.0 177.9 -72.9 -14.7 15 GLU -69.3 -36.3 177.6 -113.8 -172.0 -80.8 16 LYS -70.5 -37.2 178.5 -67.3 177.3 -166.9 -69.0 17 LEU -59.9 -43.8 178.8 -77.0 175.4 18 LEU -58.8 -41.1 -180.0 -68.8 -172.8 19 ALA -62.8 -44.2 178.7 20 LEU -66.7 -34.3 179.6 -63.4 178.0 21 LEU -70.4 -35.8 179.1 -65.4 169.9 22 ALA -73.9 -43.6 179.0 23 GLU -61.6 -41.3 179.9 -169.9 -172.1 -13.9 24 ARG -61.8 -32.8 178.8 -162.6 -173.0 -163.5 -80.6 25 ARG -67.9 -37.9 179.0 -87.8 -164.1 175.1 -179.7 26 GLU -57.8 -50.4 -179.9 -80.7 174.7 44.1 27 LEU -59.9 -37.6 179.1 -67.4 174.1 28 ALA -63.5 -34.4 178.6 29 VAL -66.3 -45.8 178.4 163.6 30 GLU -57.2 -51.2 178.9 -70.3 -66.5 -80.0 31 VAL -60.0 -24.0 178.9 178.0 32 GLY -70.6 -39.8 178.3 33 LYS -66.6 -45.3 179.2 -67.8 166.5 -177.9 173.7 34 ALA -58.4 -42.2 179.4 35 LYS -70.7 -20.2 179.8 -67.1 -178.8 -178.4 176.9 36 LEU -70.6 -59.9 -179.0 -163.1 68.0 37 LEU -64.7 -52.5 179.6 -37.1 179.9 38 SER -65.8 -14.0 179.4 -55.9 39 HIS 55.2 50.4 179.0 -70.8 104.7 40 ARG -102.2 155.9 179.6 -51.2 179.4 172.8 -170.0 41 PRO -75.6 150.9 -179.7 33.9 -45.1 42 VAL -60.4 -56.1 -178.6 168.5 43 ARG -76.5 132.9 -179.9 -154.5 86.9 -172.8 -70.6 44 ASP -137.7 82.5 -179.1 -179.6 -18.7 45 ILE -56.4 -25.7 179.3 -57.7 -174.5 46 ASP -71.8 -40.5 177.4 -75.1 -49.7 47 ARG -64.7 -40.3 179.5 157.5 69.0 169.7 155.5 48 GLU -61.6 -33.0 179.8 -56.3 179.7 2.8 49 ARG -69.2 -43.0 -178.4 -68.2 175.4 -175.0 177.6 50 ASP -72.5 -33.3 179.5 -53.6 -30.8 51 LEU -67.2 -48.1 -179.9 170.7 177.2 52 LEU -66.1 -43.7 178.6 -91.1 165.0 53 GLU -59.5 -42.0 179.2 -83.9 174.4 2.3 54 ARG -62.4 -43.2 178.9 174.2 -175.0 177.8 -98.1 55 LEU -66.7 -37.9 178.2 -68.0 172.3 56 ILE -64.1 -37.4 177.6 -69.6 176.2 57 THR -67.1 -53.0 178.5 -68.2 58 LEU -59.7 -36.6 -178.9 -66.7 166.2 59 GLY -65.1 -32.6 -179.8 60 LYS -62.6 -33.4 177.6 60.9 -178.0 170.9 66.8 61 ALA -63.8 -32.3 -180.0 62 HIS -89.2 -5.3 -179.9 -73.4 -67.8 63 HIS 71.9 30.4 177.9 -63.7 -42.7 64 LEU -102.3 128.8 179.8 -71.8 175.1 65 ASP -81.0 155.4 -179.8 57.2 -60.0 66 ALA -58.2 -32.8 -178.8 67 HIS -64.5 -50.4 179.6 -177.3 59.4 68 TYR -64.1 -44.3 179.8 173.2 47.7 69 ILE -63.4 -43.0 -179.8 -62.6 168.6 70 THR -60.8 -52.2 -179.7 -56.2 71 ARG -59.2 -45.5 -179.3 -78.6 -163.1 -65.4 166.0 72 LEU -67.0 -45.5 -178.4 -162.5 54.3 73 PHE -74.1 -26.2 176.3 -80.7 88.8 74 GLN -66.0 -32.1 -179.9 -87.6 174.8 -2.6 75 LEU -71.9 -41.9 178.9 -153.6 -168.8 76 ILE -65.7 -39.3 178.4 -61.4 172.4 77 ILE -71.6 -41.0 178.3 -71.0 173.1 78 GLU -55.8 -48.3 179.6 170.6 -178.6 -30.3 79 ASP -64.7 -35.5 179.5 173.6 72.8 80 SER -63.5 -40.0 178.3 -172.5 81 VAL -70.8 -39.0 178.1 168.3 82 LEU -60.1 -43.8 179.1 -80.0 -178.1 83 THR -60.0 -43.7 -178.7 -60.9 84 GLN -71.8 -41.7 179.1 -71.6 169.9 86.2 85 GLN -64.4 -22.8 178.1 -85.6 161.9 -169.1 86 ALA -75.0 -44.6 -179.7 87 LEU -58.4 -40.7 -179.4 -170.1 65.3 88 LEU -66.7 -43.4 -179.2 -49.4 -158.1 89 GLN -69.2 -3.9 179.3 -61.9 171.2 176.4 90 GLN -100.5 6.5 -179.5 -64.0 -40.1 112.6 91 HIS -145.6 59.9 0.0 -61.5 109.8 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 ASN 38.936 12.066 59.852 2 PRO 37.638 10.250 56.753 3 LEU 34.729 12.627 56.202 4 LEU 36.886 15.711 56.828 5 ALA 39.746 15.058 54.446 6 LEU 37.284 14.647 51.519 7 ARG 35.346 17.785 52.350 8 GLU 38.549 19.796 52.204 9 LYS 38.998 18.410 48.742 10 ILE 35.437 19.343 47.854 11 SER 35.897 22.891 49.238 12 ALA 39.080 23.347 47.189 13 LEU 37.361 22.058 44.068 14 ASP 34.396 24.421 44.567 15 GLU 36.915 27.269 44.750 16 LYS 38.282 26.332 41.332 17 LEU 34.701 26.279 39.909 18 LEU 34.153 29.871 41.047 19 ALA 37.282 31.025 39.234 20 LEU 36.162 29.395 35.944 21 LEU 32.599 30.816 36.195 22 ALA 33.940 34.316 36.643 23 GLU 36.422 33.885 33.855 24 ARG 33.579 32.605 31.674 25 ARG 31.646 35.740 32.443 26 GLU 34.623 37.821 31.310 27 LEU 34.683 36.016 27.962 28 ALA 30.926 36.542 27.618 29 VAL 31.583 40.283 28.034 30 GLU 34.231 40.190 25.327 31 VAL 31.794 38.380 23.058 32 GLY 29.431 41.145 24.156 33 LYS 31.759 43.814 22.765 34 ALA 32.219 41.921 19.463 35 LYS 28.460 41.643 18.856 36 LEU 28.280 45.343 19.566 37 LEU 30.671 46.463 16.804 38 SER 29.821 43.586 14.510 39 HIS 26.245 44.428 15.528 40 ARG 25.117 40.810 15.959 41 PRO 22.260 39.786 18.281 42 VAL 23.153 38.389 21.764 43 ARG 21.192 35.158 21.578 44 ASP 22.340 32.480 19.129 45 ILE 20.229 29.439 19.837 46 ASP 22.185 27.515 17.207 47 ARG 25.576 27.914 18.895 48 GLU 23.928 26.891 22.164 49 ARG 22.659 23.667 20.596 50 ASP 26.093 22.592 19.347 51 LEU 27.815 23.653 22.532 52 LEU 25.406 21.634 24.665 53 GLU 25.521 18.587 22.421 54 ARG 29.338 18.602 22.544 55 LEU 29.345 18.805 26.362 56 ILE 26.795 16.003 26.652 57 THR 29.113 13.854 24.443 58 LEU 32.252 14.726 26.421 59 GLY 30.285 14.183 29.625 60 LYS 29.316 10.582 28.935 61 ALA 33.026 9.771 29.006 62 HIS 33.098 11.315 32.531 63 HIS 29.926 9.439 33.451 64 LEU 27.999 12.651 33.834 65 ASP 24.477 12.325 32.456 66 ALA 22.831 14.614 29.911 67 HIS 20.113 15.810 32.302 68 TYR 22.462 17.288 34.874 69 ILE 24.737 18.755 32.181 70 THR 21.824 20.333 30.308 71 ARG 20.385 21.906 33.462 72 LEU 23.674 23.204 34.783 73 PHE 24.855 24.647 31.467 74 GLN 21.559 26.253 30.527 75 LEU 21.895 28.287 33.748 76 ILE 25.485 29.286 32.893 77 ILE 24.362 30.238 29.392 78 GLU 21.319 32.001 30.842 79 ASP 23.620 34.091 33.005 80 SER 25.883 34.610 30.010 81 VAL 23.051 36.150 27.912 82 LEU 22.040 38.290 30.913 83 THR 25.637 39.487 31.152 84 GLN 25.807 40.499 27.463 85 GLN 22.440 42.221 27.321 86 ALA 23.540 44.391 30.201 87 LEU 26.665 45.446 28.321 88 LEU 24.560 46.363 25.360 89 GLN 22.093 48.470 27.344 90 GLN 25.049 50.467 28.639 91 HIS 25.853 51.535 25.107 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 H H H H H H H H H H 10 H H H H H H H H H H 20 H H H H H H H H H H 30 H H H H H H/T T T T/S S 40 S S C H H H H H H H 50 H H H H H H H H H H 60 H H H C H H H 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 90 H 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 H 10 H H H H H H H H H H 20 H H H H H H H H H H 30 H H H H H H H h T t 40 S h H H H H H H 50 H H H H H H H H H H 60 H h T t h H H 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 90 t Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 ASN 48.7 40.3 62.8 2 PRO 15.7 12.6 82.0 3 LEU 50.2 34.0 76.3 4 LEU 43.6 29.5 76.9 5 ALA 18.1 24.9 78.9 6 LEU 49.4 33.5 72.7 7 ARG 73.2 35.0 66.4 8 GLU 16.7 12.1 82.6 9 LYS 31.6 18.2 78.2 10 ILE 43.0 30.0 74.3 11 SER 18.8 22.4 78.3 12 ALA 26.1 36.0 76.5 13 LEU 49.7 33.6 69.9 14 ASP 45.0 40.7 62.4 15 GLU 24.4 17.6 78.9 16 LYS 30.5 17.6 80.7 17 LEU 60.7 41.1 67.4 18 LEU 30.7 20.8 76.6 19 ALA 14.0 19.3 77.8 20 LEU 42.0 28.4 79.3 21 LEU 73.0 49.4 59.5 22 ALA 19.0 26.2 77.2 23 GLU 51.5 37.2 71.0 24 ARG 137.2 65.7 53.5 25 ARG 76.6 36.7 81.8 26 GLU 27.6 19.9 74.5 27 LEU 42.9 29.0 72.0 28 ALA 66.5 91.6 59.9 29 VAL 77.4 65.1 54.4 30 GLU 51.4 37.1 70.8 31 VAL 48.1 40.5 67.1 32 GLY 34.8 99.9 51.8 33 LYS 71.4 41.2 68.9 34 ALA 21.7 29.9 72.8 35 LYS 146.3 84.4 56.5 36 LEU 103.5 70.0 55.2 37 LEU 25.2 17.0 77.6 38 SER 39.0 46.7 71.5 39 HIS 21.2 14.1 84.9 40 ARG 54.2 25.9 74.8 41 PRO 21.9 17.6 83.4 42 VAL 113.8 95.8 46.2 43 ARG 99.2 47.5 67.4 44 ASP 44.3 40.1 73.7 45 ILE 60.0 41.8 78.5 46 ASP 19.5 17.7 82.7 47 ARG 59.3 28.4 74.2 48 GLU 118.7 85.6 48.8 49 ARG 59.8 28.6 80.1 50 ASP 26.6 24.0 80.4 51 LEU 127.4 86.2 52.9 52 LEU 122.6 83.0 48.0 53 GLU 26.9 19.4 78.7 54 ARG 52.8 25.3 73.8 55 LEU 110.6 74.8 48.0 56 ILE 91.0 63.4 59.7 57 THR 37.4 35.0 69.9 58 LEU 64.9 43.9 71.0 59 GLY 31.8 91.4 54.1 60 LYS 40.2 23.2 80.9 61 ALA 12.9 17.8 79.9 62 HIS 32.3 21.5 74.0 63 HIS 9.8 6.5 89.8 64 LEU 70.8 47.9 60.2 65 ASP 27.1 24.5 72.8 66 ALA 34.2 47.2 59.1 67 HIS 40.3 26.8 81.6 68 TYR 77.6 42.9 67.7 69 ILE 134.6 93.8 40.7 70 THR 70.7 66.1 58.9 71 ARG 70.3 33.7 77.2 72 LEU 72.5 49.1 60.6 73 PHE 113.8 68.2 47.9 74 GLN 55.3 37.2 65.3 75 LEU 43.0 29.1 76.0 76 ILE 113.4 79.0 44.6 77 ILE 131.3 91.5 48.4 78 GLU 37.3 26.9 68.9 79 ASP 78.3 70.9 61.8 80 SER 71.6 85.6 67.8 81 VAL 98.3 82.7 64.9 82 LEU 44.0 29.8 81.8 83 THR 82.5 77.2 56.8 84 GLN 137.8 92.7 47.2 85 GLN 74.8 50.4 60.5 86 ALA 22.9 31.5 81.3 87 LEU 115.1 77.9 46.4 88 LEU 109.3 73.9 54.5 89 GLN 27.6 18.6 84.2 90 GLN 39.2 26.4 78.7 91 HIS 60.7 40.4 69.4