Protein Data Bank File : 1cxqa Title : TRANSFERASE 30-AUG-99 1CXQ Number of Amino Acid Residues : 143 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 GLY ARG GLY LEU GLY PRO LEU GLN ILE TRP 10 GLN THR ASP PHE THR LEU GLU PRO ARG MET 20 ALA PRO ARG SER TRP LEU ALA VAL THR VAL 30 ASP THR ALA SER SER ALA ILE VAL VAL THR 40 GLN HIS GLY ARG VAL THR SER VAL ALA ALA 50 GLN HIS HIS TRP ALA THR ALA ILE ALA VAL 60 LEU GLY ARG PRO LYS ALA ILE LYS THR ASP 70 ASN GLY SER CYS PHE THR SER LYS SER THR 80 ARG GLU TRP LEU ALA ARG TRP GLY ILE ALA 90 HIS THR THR GLY ILE PRO GLY GLN ALA MET 100 VAL GLU ARG ALA ASN ARG LEU LEU LYS ASP 110 LYS ILE ARG VAL LEU ALA GLU GLY ASP GLY 120 PHE MET LYS ARG ILE PRO THR SER LYS GLN 130 GLY GLU LEU LEU ALA LYS ALA MET TYR ALA 140 LEU ASN HIS Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 GLY 0.0 131.7 -178.8 2 ARG -68.1 -42.9 -172.0 -176.2 179.0 62.5 78.5 3 GLY 60.6 -120.1 174.9 4 LEU -97.3 8.8 -175.2 -62.5 169.0 5 GLY -70.3 175.7 -174.3 6 PRO -61.4 146.3 178.3 13.7 -23.1 7 LEU -67.1 150.9 -171.8 -58.9 173.1 8 GLN -86.8 73.4 -173.4 -69.3 162.7 73.4 9 ILE -122.3 128.5 175.7 -57.2 173.4 10 TRP -103.5 159.8 162.6 -63.2 -6.4 11 GLN -118.9 136.0 -179.3 -62.7 170.4 10.7 12 THR -130.9 141.9 177.5 -57.8 13 ASP -149.5 165.4 166.5 -163.9 -160.1 14 PHE -108.5 141.2 176.5 -80.7 94.0 15 THR -138.4 136.2 -174.3 -167.9 16 LEU -90.0 125.2 -175.6 -178.0 56.7 17 GLU -131.2 92.1 179.6 178.0 46.7 80.7 18 PRO -58.1 -19.7 174.6 -28.9 41.2 19 ARG -61.2 -21.4 -177.9 -64.2 176.0 -158.7 -90.4 20 MET -102.5 10.7 177.3 -69.8 -81.1 174.6 21 ALA -62.4 148.2 6.2 22 PRO -75.3 -20.7 177.5 26.3 -37.5 23 ARG -90.7 66.0 -172.6 -64.2 -167.2 -62.8 158.5 24 SER -86.6 -6.7 175.5 45.3 25 TRP -85.2 115.5 177.5 -86.2 113.3 26 LEU -97.3 120.8 170.1 -56.2 -177.8 27 ALA -90.4 125.5 -172.9 28 VAL -126.6 123.9 170.3 179.1 29 THR -115.2 135.2 167.1 -73.0 30 VAL -114.5 129.7 171.2 62.8 31 ASP -79.7 114.8 -175.8 171.0 24.2 32 THR -69.7 -18.0 179.3 69.4 33 ALA -74.5 -37.6 -171.7 34 SER -117.7 -16.7 -172.2 64.6 35 SER 73.1 9.3 174.9 -62.3 36 ALA -64.7 146.8 177.3 37 ILE -118.5 143.5 165.2 -67.7 162.6 38 VAL -120.5 133.0 176.0 175.1 39 VAL -131.7 137.7 172.2 56.5 40 THR -131.2 154.9 178.8 54.7 41 GLN -111.9 151.1 -169.8 67.3 -178.3 130.6 42 HIS -143.5 146.3 176.0 -57.3 -85.1 43 GLY -75.2 -31.1 -175.8 44 ARG -139.4 148.0 176.1 -51.5 -69.0 -56.3 -88.6 45 VAL -86.0 106.4 -176.0 60.0 46 THR -142.2 163.6 171.2 66.3 47 SER -55.4 -47.7 -177.6 -67.5 48 VAL -66.5 -32.8 176.6 168.5 49 ALA -61.7 -43.4 177.0 50 ALA -57.8 -43.1 179.8 51 GLN -64.9 -44.7 175.5 -62.7 160.3 27.9 52 HIS -59.0 -43.0 177.3 -70.4 -6.6 53 HIS -58.3 -51.8 -178.1 167.1 76.6 54 TRP -64.2 -34.7 177.2 -77.7 -36.9 55 ALA -56.3 -46.3 177.8 56 THR -64.8 -43.0 179.2 -65.4 57 ALA -61.3 -37.5 177.1 58 ILE -64.3 -41.3 176.6 -67.4 165.7 59 ALA -58.5 -38.1 -177.3 60 VAL -80.7 -50.0 -169.2 173.5 61 LEU -100.6 -15.8 -170.6 -60.8 171.6 62 GLY 95.2 174.7 -179.1 63 ARG -83.7 121.1 -178.9 -173.0 -176.7 32.2 -163.2 64 PRO -78.7 162.0 170.3 34.5 -36.8 65 LYS -77.0 -34.4 -177.3 -65.3 -61.3 -168.2 -90.3 66 ALA -154.4 155.3 174.8 67 ILE -129.7 131.7 173.2 -56.8 171.1 68 LYS -100.1 131.1 172.4 165.2 70.5 176.4 75.5 69 THR -137.0 178.1 166.1 69.4 70 ASP -86.8 -174.6 -175.7 73.5 9.9 71 ASN -92.6 27.9 176.0 -72.3 -69.7 72 GLY -63.1 152.1 -174.9 73 SER -61.7 -29.6 178.4 61.2 74 CYS -68.9 -17.9 -179.7 62.8 75 PHE -102.8 -23.3 -175.9 -64.5 -48.0 76 THR -106.1 4.3 177.6 61.1 77 SER -63.5 156.8 173.4 65.8 78 LYS -57.5 -41.4 179.8 178.7 -174.0 -161.8 143.1 79 SER -58.1 -50.0 -179.5 171.3 80 THR -66.6 -41.3 177.4 -65.9 81 ARG -58.7 -40.9 178.2 -65.1 -170.4 70.7 -169.0 82 GLU -67.4 -39.4 179.4 173.1 58.7 12.5 83 TRP -63.3 -43.8 178.4 -171.9 98.2 84 LEU -66.7 -37.9 177.0 -70.6 165.5 85 ALA -64.4 -39.3 176.2 86 ARG -55.7 -39.3 178.6 178.1 -157.3 -52.4 169.6 87 TRP -83.3 -10.8 -175.7 -84.2 97.4 88 GLY 69.1 33.4 179.6 89 ILE -104.5 124.2 175.9 -61.4 164.9 90 ALA -70.5 146.2 -177.4 91 HIS -129.0 132.5 174.2 -177.8 -155.6 92 THR -130.7 145.4 168.9 -178.4 93 THR -112.8 10.8 172.4 63.9 94 GLY 87.5 -155.0 -172.3 95 ILE -90.4 123.1 177.4 -60.8 172.9 96 PRO -66.0 59.5 -34.0 -18.3 30.9 97 GLY 125.6 11.7 173.5 98 GLN -145.5 51.8 174.8 56.0 -176.5 51.6 99 ALA -59.6 -34.1 -176.5 100 MET -65.9 -42.5 179.6 -68.2 179.2 80.0 101 VAL -71.4 -31.9 175.8 74.7 102 GLU -63.2 -40.2 175.1 -73.0 179.8 15.5 103 ARG -63.8 -43.6 178.1 172.9 174.7 -177.9 -90.0 104 ALA -58.8 -43.1 179.6 105 ASN -57.0 -46.2 -178.0 -69.8 -16.2 106 ARG -67.3 -46.1 179.9 165.1 171.6 61.3 73.8 107 LEU -61.2 -39.9 -179.4 -70.3 172.2 108 LEU -67.6 -47.4 -179.9 -179.6 65.3 109 LYS -63.9 -38.6 178.1 -69.3 -177.3 -64.1 -171.7 110 ASP -62.5 -44.1 179.9 -72.1 -7.4 111 LYS -64.2 -42.0 175.4 -172.6 65.1 70.3 175.8 112 ILE -56.1 -47.3 179.9 -69.7 166.7 113 ARG -59.5 -48.7 -178.4 -179.6 164.0 171.6 177.0 114 VAL -59.3 -47.1 -178.0 166.2 115 LEU -64.6 -44.2 -179.2 -63.4 172.5 116 ALA -60.5 -50.6 179.8 117 GLU -61.4 -36.5 174.9 -67.4 -174.6 -3.9 118 GLY -57.1 -36.9 177.8 119 ASP -83.9 3.3 178.5 -74.2 -13.8 120 GLY 86.7 11.4 179.3 121 PHE -98.1 101.9 -175.3 -52.6 -44.0 122 MET -91.4 -10.4 -179.9 -53.5 -52.3 -64.8 123 LYS -130.9 -120.1 -178.5 -67.1 -178.6 -174.9 -41.3 124 ARG -75.7 141.4 175.0 -168.3 -175.0 66.8 86.0 125 ILE -76.7 131.4 175.9 -60.0 156.3 126 PRO -51.8 139.3 -172.6 -28.7 38.8 127 THR -54.6 -40.8 -177.2 -54.8 128 SER -68.5 -11.3 -177.5 68.3 129 LYS -104.6 -10.3 -170.1 -60.9 -61.3 177.4 176.1 130 GLN -68.2 -43.8 -174.2 -74.0 174.1 8.1 131 GLY -60.2 -46.4 179.5 132 GLU -69.0 -33.6 179.7 -69.5 -164.5 21.3 133 LEU -67.1 -43.0 178.2 -166.9 151.2 134 LEU -61.3 -44.3 176.9 -174.4 65.5 135 ALA -61.9 -37.2 177.3 136 LYS -63.9 -40.4 177.4 -173.7 -176.6 -65.3 172.1 137 ALA -64.1 -43.4 178.4 138 MET -61.9 -46.9 173.5 -178.5 171.5 154.9 139 TYR -53.7 -47.2 -174.1 154.2 74.8 140 ALA -60.7 -38.2 -177.5 141 LEU -83.6 -23.6 -175.1 -64.4 176.7 142 ASN -96.7 -34.0 -167.2 -99.3 -13.5 143 HIS -113.8 -63.6 0.0 -64.9 -65.9 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 GLY 22.810 32.813 47.065 2 ARG 25.045 31.154 49.576 3 GLY 22.439 28.696 50.796 4 LEU 24.388 26.066 52.772 5 GLY 27.649 26.899 51.035 6 PRO 30.850 28.040 52.764 7 LEU 30.878 31.249 54.767 8 GLN 32.362 34.345 53.111 9 ILE 35.565 34.502 55.165 10 TRP 39.014 35.522 53.940 11 GLN 42.488 35.102 55.361 12 THR 45.028 37.866 54.574 13 ASP 48.765 38.124 55.180 14 PHE 51.866 39.892 53.917 15 THR 54.887 37.912 52.658 16 LEU 58.230 39.338 51.596 17 GLU 59.436 38.303 48.108 18 PRO 62.715 39.907 47.010 19 ARG 62.225 38.659 43.473 20 MET 59.575 41.425 43.284 21 ALA 61.722 44.259 44.719 22 PRO 61.408 47.194 45.085 23 ARG 57.727 46.359 45.656 24 SER 58.651 43.116 47.375 25 TRP 55.861 43.047 49.960 26 LEU 53.145 40.782 48.638 27 ALA 49.712 41.224 50.210 28 VAL 47.921 37.896 49.846 29 THR 44.245 37.104 50.432 30 VAL 42.756 33.644 50.203 31 ASP 39.001 33.260 50.043 32 THR 38.407 30.330 52.354 33 ALA 35.129 29.542 50.525 34 SER 36.674 28.987 47.121 35 SER 40.457 28.912 47.717 36 ALA 40.858 31.776 45.205 37 ILE 43.800 34.073 45.847 38 VAL 44.279 37.773 45.257 39 VAL 47.834 39.160 45.425 40 THR 49.101 42.718 45.122 41 GLN 52.622 44.076 45.551 42 HIS 53.636 46.958 47.748 43 GLY 56.808 48.883 48.547 44 ARG 56.180 48.982 52.299 45 VAL 54.158 46.982 54.810 46 THR 51.712 49.583 56.112 47 SER 48.079 49.942 57.115 48 VAL 47.287 51.802 53.914 49 ALA 48.959 49.037 51.836 50 ALA 46.628 46.495 53.480 51 GLN 43.646 48.733 52.690 52 HIS 44.710 49.187 49.082 53 HIS 45.094 45.431 48.807 54 TRP 41.641 44.717 50.232 55 ALA 40.060 47.327 47.978 56 THR 41.385 45.329 45.027 57 ALA 40.408 42.002 46.602 58 ILE 36.820 43.253 47.067 59 ALA 36.702 44.244 43.370 60 VAL 37.770 40.718 42.448 61 LEU 36.028 38.524 45.029 62 GLY 33.153 40.611 46.357 63 ARG 32.694 41.947 49.830 64 PRO 33.466 39.298 52.477 65 LYS 31.593 38.901 55.727 66 ALA 34.836 38.617 57.689 67 ILE 38.619 38.678 57.345 68 LYS 41.125 36.800 59.497 69 THR 44.635 38.203 59.912 70 ASP 47.434 38.036 62.459 71 ASN 48.106 40.783 64.963 72 GLY 50.567 42.741 62.846 73 SER 50.392 46.511 63.301 74 CYS 49.127 47.066 59.732 75 PHE 46.047 45.037 60.636 76 THR 45.369 46.194 64.169 77 SER 45.863 49.896 63.677 78 LYS 43.086 52.391 64.250 79 SER 43.248 53.225 60.562 80 THR 42.687 49.644 59.450 81 ARG 39.994 49.038 62.010 82 GLU 38.143 52.104 60.767 83 TRP 38.545 51.106 57.093 84 LEU 37.075 47.663 57.746 85 ALA 34.212 49.215 59.754 86 ARG 33.512 51.592 56.825 87 TRP 33.088 48.530 54.621 88 GLY 31.056 46.586 57.211 89 ILE 33.565 43.728 57.257 90 ALA 34.146 41.836 60.506 91 HIS 37.789 41.390 61.495 92 THR 39.319 38.679 63.672 93 THR 42.876 37.966 64.639 94 GLY 41.854 34.651 66.228 95 ILE 42.403 33.148 69.596 96 PRO 45.043 35.009 71.664 97 GLY 44.332 29.639 62.550 98 GLN 45.291 30.762 59.049 99 ALA 46.893 27.732 57.491 100 MET 45.183 28.455 54.174 101 VAL 46.937 31.808 53.653 102 GLU 50.252 30.300 54.777 103 ARG 49.777 27.685 52.060 104 ALA 48.873 30.368 49.569 105 ASN 52.036 32.304 50.416 106 ARG 54.194 29.251 49.768 107 LEU 52.398 28.251 46.538 108 LEU 52.653 31.806 45.268 109 LYS 56.364 32.264 46.028 110 ASP 57.096 28.864 44.466 111 LYS 55.107 29.755 41.347 112 ILE 56.776 33.168 41.065 113 ARG 60.158 31.454 41.192 114 VAL 59.218 28.876 38.543 115 LEU 57.778 31.520 36.181 116 ALA 60.724 33.860 36.705 117 GLU 63.312 31.166 36.095 118 GLY 61.342 30.099 33.010 119 ASP 61.799 33.622 31.663 120 GLY 65.546 33.459 32.474 121 PHE 65.349 35.588 35.650 122 MET 67.364 33.707 38.225 123 LYS 67.438 36.527 40.788 124 ARG 65.293 39.705 40.863 125 ILE 62.647 40.035 38.160 126 PRO 63.171 43.212 36.094 127 THR 60.732 45.817 37.318 128 SER 59.011 46.185 33.959 129 LYS 58.202 42.444 33.873 130 GLN 56.883 42.037 37.444 131 GLY 53.275 43.036 37.054 132 GLU 52.499 40.541 34.331 133 LEU 54.516 37.820 36.065 134 LEU 52.613 38.351 39.328 135 ALA 49.314 38.271 37.428 136 LYS 50.440 35.052 35.713 137 ALA 51.164 33.466 39.094 138 MET 47.746 34.488 40.364 139 TYR 46.125 33.070 37.212 140 ALA 48.084 29.850 37.569 141 LEU 46.896 29.270 41.111 142 ASN 43.250 30.335 40.562 143 HIS 42.122 29.057 37.147 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C T T T T/S S S S/S S S 10 S S S S S S S/T T T T 20 C/P C C S S S S S S S 30 S/T T T T S S S S S S 40 S S S/S S S S/H H H H H 50 H H H H H H H H H H 60 H S S S S/S S S S S S 70 S H H H H H H/H H H H 80 H H H H H H H H/S S S 90 S S S C C C/X X/C H H H 100 H H H H H H H H H H 110 H H H H H H H H H H 120 T T T T C C C C H H 130 H H H H H H H H H H 140 H H H Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 t T T t e E E 10 E E E E E E e G G G 20 g T t e E E E E E E 30 E e T T t e E E E E 40 E E S S h H H H H 50 H H H H H H H H H H 60 H h e E E E e 70 S h H H H H h H H H 80 H H H H H H H h t E 90 E E h H H 100 H H H H H H H H H H 110 H H H H H H H H h T 120 t S S S h H H H H 130 H H H H H H H H H H 140 H H h Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 GLY 0.0 0.0 94.5 2 ARG 115.7 55.4 75.3 3 GLY 0.0 0.0 82.0 4 LEU 0.0 0.0 92.6 5 GLY 14.8 42.6 62.4 6 PRO 43.5 34.9 73.9 7 LEU 46.8 31.7 74.5 8 GLN 84.8 57.1 65.4 9 ILE 87.5 60.9 58.2 10 TRP 199.3 97.2 40.4 11 GLN 129.2 86.9 48.6 12 THR 106.4 99.5 39.7 13 ASP 88.9 80.4 64.2 14 PHE 159.0 95.3 36.2 15 THR 96.1 89.9 52.3 16 LEU 73.5 49.7 63.5 17 GLU 127.0 91.6 35.6 18 PRO 39.7 31.9 73.8 19 ARG 163.3 78.2 58.4 20 MET 159.4 100.0 38.8 21 ALA 45.7 62.9 59.8 22 PRO 40.6 32.6 75.1 23 ARG 80.5 38.5 77.0 24 SER 69.7 83.3 53.9 25 TRP 144.0 70.2 53.3 26 LEU 147.8 100.0 32.8 27 ALA 72.4 99.7 47.0 28 VAL 118.8 100.0 44.6 29 THR 106.9 100.0 42.9 30 VAL 114.6 96.4 43.5 31 ASP 93.7 84.8 54.0 32 THR 85.6 80.1 55.9 33 ALA 58.3 80.3 66.4 34 SER 36.5 43.7 73.1 35 SER 37.5 44.8 71.4 36 ALA 49.6 68.3 66.1 37 ILE 136.1 94.8 41.9 38 VAL 117.4 98.8 31.6 39 VAL 118.5 99.7 28.6 40 THR 80.6 75.4 53.8 41 GLN 142.1 95.6 51.5 42 HIS 128.8 85.8 53.2 43 GLY 17.4 49.9 63.2 44 ARG 28.6 13.7 81.6 45 VAL 70.2 59.1 47.0 46 THR 47.2 44.2 65.7 47 SER 67.1 80.3 64.5 48 VAL 41.3 34.7 76.9 49 ALA 65.3 89.9 59.8 50 ALA 72.2 99.4 42.0 51 GLN 133.6 89.9 50.3 52 HIS 41.1 27.3 69.9 53 HIS 149.9 99.8 48.4 54 TRP 205.0 100.0 27.6 55 ALA 33.2 45.7 65.7 56 THR 49.6 46.4 59.8 57 ALA 72.6 100.0 37.9 58 ILE 128.9 89.8 38.7 59 ALA 13.2 18.1 78.2 60 VAL 63.7 53.6 57.9 61 LEU 127.8 86.5 52.9 62 GLY 3.7 10.6 80.0 63 ARG 84.2 40.3 67.5 64 PRO 122.3 98.2 40.8 65 LYS 44.9 25.9 84.5 66 ALA 54.8 75.5 45.4 67 ILE 143.5 100.0 32.6 68 LYS 148.3 85.5 49.3 69 THR 106.9 100.0 47.8 70 ASP 49.5 44.8 74.7 71 ASN 40.6 33.6 72.9 72 GLY 7.0 20.2 75.5 73 SER 0.0 0.0 91.4 74 CYS 87.8 88.5 49.0 75 PHE 163.4 98.0 44.4 76 THR 68.7 64.3 64.1 77 SER 52.3 62.6 79.1 78 LYS 0.0 0.0 86.8 79 SER 34.7 41.5 70.7 80 THR 106.9 100.0 51.6 81 ARG 56.7 27.1 82.5 82 GLU 37.4 27.0 77.8 83 TRP 188.0 91.7 49.4 84 LEU 144.9 98.0 38.1 85 ALA 20.9 28.8 84.3 86 ARG 68.3 32.7 81.1 87 TRP 126.9 61.9 53.7 88 GLY 1.3 3.8 79.8 89 ILE 143.5 100.0 39.8 90 ALA 13.8 19.1 74.5 91 HIS 133.3 88.7 51.5 92 THR 46.5 43.5 61.3 93 THR 82.7 77.4 69.5 94 GLY 19.4 55.9 65.2 95 ILE 0.0 0.0 83.5 96 PRO 9.0 7.2 79.2 97 GLY 0.0 0.0 83.9 98 GLN 135.0 90.9 63.6 99 ALA 1.2 1.7 83.1 100 MET 92.6 58.1 65.7 101 VAL 118.8 100.0 52.2 102 GLU 43.4 31.3 78.3 103 ARG 71.8 34.4 75.5 104 ALA 70.6 97.2 40.4 105 ASN 107.3 88.8 50.4 106 ARG 77.3 37.0 73.8 107 LEU 103.6 70.1 65.5 108 LEU 147.8 100.0 29.7 109 LYS 108.1 62.3 67.6 110 ASP 34.6 31.3 72.3 111 LYS 106.8 61.6 52.7 112 ILE 143.5 100.0 25.8 113 ARG 82.8 39.6 80.5 114 VAL 26.7 22.5 75.0 115 LEU 113.4 76.8 49.7 116 ALA 72.6 100.0 46.9 117 GLU 98.0 70.7 67.6 118 GLY 0.0 0.0 85.3 119 ASP 53.5 48.4 70.1 120 GLY 4.1 11.9 73.4 121 PHE 122.3 73.3 51.2 122 MET 59.0 37.0 79.0 123 LYS 6.2 3.6 90.0 124 ARG 109.7 52.5 74.0 125 ILE 143.5 100.0 30.4 126 PRO 74.9 60.1 60.9 127 THR 39.1 36.6 78.5 128 SER 10.7 12.8 73.2 129 LYS 57.1 32.9 74.2 130 GLN 143.8 96.8 60.1 131 GLY 4.9 14.0 80.5 132 GLU 0.0 0.0 86.9 133 LEU 143.3 97.0 41.7 134 LEU 135.6 91.7 42.1 135 ALA 17.3 23.8 75.4 136 LYS 78.7 45.4 65.7 137 ALA 72.6 100.0 41.5 138 MET 121.5 76.2 57.4 139 TYR 49.9 27.6 70.3 140 ALA 55.9 77.0 56.0 141 LEU 126.6 85.7 48.1 142 ASN 108.7 89.9 55.4 143 HIS 37.7 25.1 70.9