Protein Data Bank File : 1fm0d Title : TRANSFERASE 15-AUG-00 1FM0 Number of Amino Acid Residues : 81 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 MET ILE LYS VAL LEU PHE PHE ALA GLN VAL 10 ARG GLU LEU VAL GLY THR ASP ALA THR GLU 20 VAL ALA ALA ASP PHE PRO THR VAL GLU ALA 30 LEU ARG GLN HIS MET ALA ALA GLN SER ASP 40 ARG TRP ALA LEU ALA LEU GLU ASP GLY LYS 50 LEU LEU ALA ALA VAL ASN GLN THR LEU VAL 60 SER PHE ASP HIS PRO LEU THR ASP GLY ASP 70 GLU VAL ALA PHE PHE PRO PRO VAL THR GLY 80 GLY Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 MET 0.0 169.9 166.4 -50.9 -92.8 -74.0 2 ILE -102.4 127.9 179.7 -55.7 -171.6 3 LYS -91.7 128.8 -178.6 175.0 92.6 149.2 -167.8 4 VAL -118.9 124.2 179.0 -168.8 5 LEU -110.8 148.9 -179.9 -56.1 -179.5 6 PHE -128.8 148.9 -179.9 -50.1 97.9 7 PHE -136.0 154.6 173.8 -62.1 94.1 8 ALA 52.6 -133.7 -177.6 9 GLN -57.8 -34.6 179.5 -68.2 97.5 -45.7 10 VAL -61.9 -50.0 176.1 175.3 11 ARG -55.1 -45.5 -179.6 -179.1 177.1 68.2 75.2 12 GLU -61.0 -43.9 -177.3 -69.9 178.9 -23.0 13 LEU -75.3 -41.9 179.4 -170.2 49.8 14 VAL -69.2 -27.3 174.9 -57.7 15 GLY 86.3 12.8 176.5 16 THR -150.4 154.3 178.9 -175.1 17 ASP -86.8 -22.8 -171.3 -74.7 -143.9 18 ALA -165.6 147.4 174.0 19 THR -153.5 168.1 -179.6 -169.0 20 GLU -115.7 144.3 177.0 -64.4 -162.7 -28.9 21 VAL -134.5 146.6 175.6 -172.0 22 ALA -61.0 159.3 -179.2 23 ALA -87.6 58.1 -178.9 24 ASP -111.0 33.2 178.7 -58.4 -56.7 25 PHE -133.9 130.2 -176.3 -56.8 101.3 26 PRO -67.0 -31.8 -175.2 21.2 -29.4 27 THR -142.6 167.9 173.1 58.6 28 VAL -54.9 -44.7 -179.8 173.1 29 GLU -60.1 -43.5 177.4 176.5 59.0 20.3 30 ALA -61.1 -41.5 174.8 31 LEU -62.7 -45.9 177.9 174.4 64.0 32 ARG -55.2 -46.9 -179.7 -175.1 -159.2 66.4 74.9 33 GLN -62.8 -44.0 177.8 -75.6 178.6 -141.8 34 HIS -58.5 -46.7 -179.0 170.6 69.7 35 MET -68.3 -40.3 177.4 -57.7 -64.6 -76.3 36 ALA -59.3 -29.6 -176.1 37 ALA -79.2 -2.9 -176.2 38 GLN -75.5 -30.8 -179.7 -61.3 -52.4 -56.3 39 SER -167.5 167.4 179.1 77.9 40 ASP -65.1 -36.2 177.6 -70.0 -15.3 41 ARG -67.6 -43.3 177.9 -81.5 -179.4 61.9 145.5 42 TRP -64.0 -37.3 177.5 -80.5 90.3 43 ALA -64.5 -43.7 178.7 44 LEU -62.5 -42.3 -179.9 -178.2 58.8 45 ALA -65.6 -38.1 -171.7 46 LEU -105.5 -1.0 178.8 -60.1 175.7 47 GLU -100.1 6.3 178.9 -64.3 -178.7 -21.5 48 ASP -67.4 134.0 -177.7 -179.4 52.0 49 GLY -63.2 -20.9 -179.5 50 LYS -97.2 2.3 179.6 -63.1 178.9 179.4 -179.1 51 LEU -56.3 139.7 176.2 -171.0 75.6 52 LEU -109.9 154.6 177.5 -64.4 174.4 53 ALA -135.0 145.4 173.6 54 ALA -128.8 145.8 173.8 55 VAL -127.5 126.1 -175.8 169.0 56 ASN 48.6 48.3 173.2 -59.0 -35.3 57 GLN 63.5 25.0 171.7 -52.3 88.9 33.1 58 THR -127.5 137.7 176.9 -61.9 59 LEU -66.2 132.3 -177.5 -79.1 178.7 60 VAL -139.2 161.3 169.5 -62.6 61 SER -65.3 152.8 175.9 162.4 62 PHE -66.9 -14.5 174.2 -79.7 73.6 63 ASP -80.9 -3.4 -178.3 -69.2 -22.3 64 HIS -59.4 135.2 -180.0 -160.5 -88.8 65 PRO -70.4 153.7 177.0 29.4 -40.5 66 LEU -112.7 150.9 -179.9 -71.1 -177.3 67 THR -137.8 144.7 175.2 -55.1 68 ASP -49.6 132.0 -179.4 -175.3 34.9 69 GLY 94.6 -7.8 -179.0 70 ASP -68.6 153.2 167.8 -78.7 -10.5 71 GLU -107.3 120.6 178.9 179.7 172.9 -73.5 72 VAL -110.6 141.1 175.8 -176.8 73 ALA -130.8 139.3 175.0 74 PHE -118.5 132.4 -175.1 -65.8 113.7 75 PHE -159.1 160.0 179.5 48.6 84.9 76 PRO -81.2 171.2 173.4 14.8 -7.1 77 PRO -46.2 138.8 -173.7 -27.1 35.7 78 VAL -82.3 156.1 -176.6 -54.3 79 THR -137.2 30.9 175.4 57.7 80 GLY -77.8 -172.6 177.5 81 GLY 79.8 9.4 0.0 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 MET 24.908 26.524 -9.320 2 ILE 23.440 27.616 -5.988 3 LYS 21.152 25.071 -4.082 4 VAL 18.222 26.620 -2.096 5 LEU 16.374 24.730 0.696 6 PHE 13.072 25.619 2.481 7 PHE 11.561 24.524 5.866 8 ALA 8.260 24.524 7.821 9 GLN 5.665 27.198 6.771 10 VAL 8.066 28.596 4.155 11 ARG 8.374 25.150 2.490 12 GLU 4.577 24.657 2.574 13 LEU 3.861 28.011 0.871 14 VAL 6.602 27.895 -1.815 15 GLY 5.470 24.344 -2.689 16 THR 8.851 22.630 -3.032 17 ASP 11.552 21.422 -0.593 18 ALA 14.556 22.461 -2.723 19 THR 15.544 24.122 -6.016 20 GLU 18.629 25.294 -7.968 21 VAL 19.544 28.793 -9.203 22 ALA 22.487 30.076 -11.303 23 ALA 25.237 31.887 -9.341 24 ASP 24.225 35.360 -10.593 25 PHE 23.420 37.115 -7.297 26 PRO 25.865 39.107 -5.127 27 THR 24.170 38.444 -1.736 28 VAL 21.532 36.429 0.129 29 GLU 19.211 39.504 -0.067 30 ALA 19.527 39.763 -3.877 31 LEU 18.643 36.036 -4.144 32 ARG 15.660 36.490 -1.727 33 GLN 14.292 39.379 -3.880 34 HIS 14.670 37.332 -7.115 35 MET 12.793 34.341 -5.655 36 ALA 10.033 36.541 -4.108 37 ALA 9.400 38.014 -7.573 38 GLN 8.446 34.620 -9.129 39 SER 4.829 34.542 -7.850 40 ASP 2.393 35.923 -5.258 41 ARG 2.840 32.761 -3.091 42 TRP 6.665 33.019 -3.236 43 ALA 6.432 36.741 -2.273 44 LEU 4.252 35.985 0.764 45 ALA 6.618 33.213 1.927 46 LEU 9.834 35.210 1.513 47 GLU 8.880 38.846 2.373 48 ASP 8.250 38.229 6.109 49 GLY 10.235 40.514 8.458 50 LYS 11.136 37.604 10.752 51 LEU 12.526 35.321 7.992 52 LEU 15.904 33.678 8.783 53 ALA 18.732 32.638 6.389 54 ALA 21.670 30.191 6.485 55 VAL 24.631 29.783 4.113 56 ASN 26.626 26.525 4.271 57 GLN 24.754 25.488 7.450 58 THR 25.533 28.670 9.445 59 LEU 23.039 31.497 10.340 60 VAL 23.955 34.725 8.486 61 SER 22.904 38.309 7.764 62 PHE 20.983 38.905 4.526 63 ASP 24.008 40.994 3.405 64 HIS 26.174 37.819 3.331 65 PRO 27.916 37.277 -0.055 66 LEU 27.106 34.296 -2.284 67 THR 29.463 31.979 -4.205 68 ASP 28.983 29.212 -6.799 69 GLY 28.399 25.897 -4.986 70 ASP 26.897 27.373 -1.804 71 GLU 23.854 25.857 -0.026 72 VAL 21.352 28.557 1.078 73 ALA 18.321 27.925 3.352 74 PHE 15.289 30.165 4.146 75 PHE 13.084 29.353 7.197 76 PRO 10.869 30.915 9.937 77 PRO 11.780 31.607 13.603 78 VAL 12.729 28.357 15.351 79 THR 10.713 26.503 18.046 80 GLY 12.917 23.717 19.484 81 GLY 13.951 22.989 23.063 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S S S S S S H H H 10 H H H H H/S S S S/S S S 20 S S S S S S S/H H H H 30 H H H H H H H H H H 40 H H H H H H H C C S 50 S S S S/T T T T/S S S S 60 S C S S S S S S/S S S 70 S/S S S S S S S/S S S S 80 S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 E E E E E h H H H 10 H H H H h t e E E E 20 E S S h H H H 30 H H H H H H h T h H 40 H H H H H H h t T T 50 t E E E E e T E E e 60 t T T t B t T T e 70 E E E E E 80 Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 MET 72.3 45.4 78.6 2 ILE 141.5 98.6 46.7 3 LYS 82.3 47.5 64.2 4 VAL 118.8 100.0 33.4 5 LEU 110.5 74.7 49.4 6 PHE 166.8 100.0 33.7 7 PHE 70.0 42.0 60.3 8 ALA 25.5 35.1 70.8 9 GLN 28.5 19.2 72.9 10 VAL 110.2 92.8 42.7 11 ARG 118.7 56.8 71.7 12 GLU 34.2 24.7 82.1 13 LEU 101.1 68.4 59.6 14 VAL 118.7 100.0 39.5 15 GLY 12.4 35.6 82.5 16 THR 58.3 54.5 65.3 17 ASP 31.8 28.8 73.2 18 ALA 53.1 73.2 57.7 19 THR 62.0 58.0 52.0 20 GLU 53.8 38.8 64.1 21 VAL 100.5 84.6 45.0 22 ALA 32.4 44.6 67.6 23 ALA 57.0 78.5 60.9 24 ASP 21.5 19.5 71.0 25 PHE 132.9 79.7 50.3 26 PRO 31.6 25.4 72.5 27 THR 70.7 66.1 61.0 28 VAL 118.8 100.0 31.4 29 GLU 88.6 63.9 69.9 30 ALA 47.9 66.0 61.2 31 LEU 147.0 99.4 23.2 32 ARG 167.5 80.2 46.0 33 GLN 50.2 33.8 79.8 34 HIS 81.7 54.4 57.9 35 MET 149.0 93.5 29.7 36 ALA 68.8 94.8 61.4 37 ALA 15.6 21.4 85.5 38 GLN 72.5 48.8 71.3 39 SER 36.9 44.1 69.8 40 ASP 0.0 0.0 85.5 41 ARG 68.3 32.7 76.0 42 TRP 165.3 80.6 44.0 43 ALA 50.0 68.8 71.3 44 LEU 24.7 16.7 79.0 45 ALA 67.3 92.7 49.3 46 LEU 147.8 100.0 33.2 47 GLU 52.4 37.8 75.4 48 ASP 40.8 36.9 73.2 49 GLY 0.0 0.0 83.9 50 LYS 23.0 13.2 82.6 51 LEU 143.2 96.9 46.1 52 LEU 89.4 60.5 57.7 53 ALA 72.6 100.0 41.2 54 ALA 62.4 85.9 48.5 55 VAL 114.8 96.6 47.4 56 ASN 56.4 46.6 75.6 57 GLN 41.1 27.7 79.7 58 THR 22.4 20.9 83.2 59 LEU 52.9 35.8 64.1 60 VAL 100.4 84.5 55.4 61 SER 19.2 23.0 76.7 62 PHE 121.6 72.9 58.0 63 ASP 8.7 7.9 81.1 64 HIS 83.8 55.8 54.4 65 PRO 40.3 32.4 76.3 66 LEU 147.5 99.8 43.5 67 THR 19.0 17.8 81.8 68 ASP 37.6 34.0 68.7 69 GLY 3.6 10.2 86.1 70 ASP 95.7 86.6 59.2 71 GLU 85.6 61.8 61.7 72 VAL 118.8 100.0 31.3 73 ALA 61.2 84.3 43.9 74 PHE 166.8 100.0 26.1 75 PHE 134.9 80.9 39.2 76 PRO 101.4 81.5 49.7 77 PRO 68.2 54.8 58.7 78 VAL 21.1 17.8 76.9 79 THR 2.2 2.1 90.1 80 GLY 0.0 0.0 86.4 81 GLY 0.0 0.0 87.6