Protein Data Bank File : 1dm9a Title : STRUCTURAL GENOMICS 14-DEC-99 1DM9 Number of Amino Acid Residues : 104 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 PRO ALA VAL GLU VAL ARG LEU ASP LYS TRP 10 LEU TRP ALA ALA ARG PHE TYR LYS THR ARG 20 ALA LEU ALA ARG GLU MET ILE GLU GLY GLY 30 LYS VAL HIS TYR ASN GLY GLN ARG SER LYS 40 PRO SER LYS ILE VAL GLU LEU ASN ALA THR 50 LEU THR LEU ARG GLN GLY ASN ASP GLU ARG 60 THR VAL ILE VAL LYS ALA ILE THR GLU GLN 70 ARG ARG PRO ALA SER GLU ALA ALA LEU LEU 80 TYR GLU GLU THR ALA GLU SER VAL GLU LYS 90 ARG GLU LYS MET ALA LEU ALA ARG LYS LEU 100 ASN ALA LEU THR Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 PRO 0.0 91.2 179.6 -29.3 39.4 2 ALA -92.7 40.8 177.8 3 VAL -136.7 27.9 179.3 -49.9 4 GLU -121.6 107.9 179.6 -45.1 -150.3 -42.5 5 VAL -122.7 131.1 -178.9 174.4 6 ARG -73.8 149.9 179.9 -61.9 166.0 45.5 106.7 7 LEU -60.1 -39.6 -178.9 176.4 69.0 8 ASP -65.6 -41.4 177.6 63.2 -9.1 9 LYS -64.0 -45.5 178.4 179.4 63.5 135.1 -56.3 10 TRP -56.3 -49.1 -178.4 -168.7 90.3 11 LEU -60.1 -35.6 178.1 -71.0 161.6 12 TRP -72.1 -44.0 179.6 167.0 78.1 13 ALA -60.6 -39.3 179.7 14 ALA -77.3 -0.4 178.4 15 ARG 66.9 24.6 179.1 -45.4 -175.5 68.5 82.7 16 PHE -75.5 -28.5 179.0 -74.4 113.6 17 TYR -136.0 146.4 -177.8 -60.6 108.5 18 LYS -59.5 -35.1 -179.1 -55.4 154.7 -165.1 -173.1 19 THR -134.6 160.7 177.2 54.3 20 ARG -65.5 -35.6 -178.8 -68.0 -175.4 -75.2 -63.2 21 ALA -63.1 -37.9 178.3 22 LEU -69.8 -43.0 178.2 169.2 57.2 23 ALA -58.0 -40.1 179.2 24 ARG -63.9 -39.5 178.9 -165.4 168.3 80.9 86.0 25 GLU -67.1 -37.6 -179.9 -72.9 172.2 42.6 26 MET -67.5 -39.8 178.9 -63.8 -65.7 -74.1 27 ILE -62.4 -48.9 -179.5 -70.8 168.7 28 GLU -66.2 -27.3 175.6 -66.6 -170.1 19.8 29 GLY -77.8 -2.7 -177.4 30 GLY 72.7 19.5 -180.0 31 LYS -89.0 -2.8 174.8 -72.3 156.1 -175.7 -170.7 32 VAL -129.1 128.5 176.9 174.5 33 HIS -118.0 148.8 179.8 -88.3 4.1 34 TYR -117.4 119.1 -176.7 -172.5 102.3 35 ASN 46.7 46.3 175.3 -71.3 -23.1 36 GLY 78.8 9.6 -178.9 37 GLN -139.5 161.9 175.4 -63.0 -173.8 -93.3 38 ARG -52.3 143.5 177.5 170.2 175.8 -66.6 -86.4 39 SER -125.0 -160.1 -179.0 -171.1 40 LYS -147.9 152.8 -179.9 55.1 173.7 176.1 -176.6 41 PRO -50.1 -38.8 -176.0 -27.6 38.2 42 SER -85.8 -1.7 178.1 64.5 43 LYS -54.2 130.9 -179.5 170.0 59.9 -179.6 -172.6 44 ILE -84.9 126.7 -177.1 -53.8 -50.6 45 VAL -71.4 138.3 176.8 175.6 46 GLU -115.8 147.7 177.8 -61.5 154.6 -59.0 47 LEU -63.9 146.8 -179.8 -60.3 179.0 48 ASN 68.4 15.1 177.2 -64.7 -49.0 49 ALA -75.7 154.7 178.0 50 THR -104.3 120.5 179.2 -63.8 51 LEU -112.1 133.9 178.2 -53.6 -176.6 52 THR -119.7 124.9 -176.8 -70.9 53 LEU -143.6 153.5 179.4 56.4 90.7 54 ARG -88.0 128.1 178.1 0.0 0.0 0.0 0.0 55 GLN -118.2 94.7 -178.5 -80.6 -57.2 -119.1 56 GLY 64.3 -106.7 176.7 57 ASN -117.7 11.6 178.7 -160.4 52.3 58 ASP -93.0 152.2 175.3 -69.5 55.7 59 GLU -118.3 135.9 178.4 177.6 -173.0 -61.3 60 ARG -132.8 140.6 176.9 -64.0 -136.8 -102.2 162.0 61 THR -116.1 119.8 179.8 -63.2 62 VAL -124.3 156.7 178.9 -55.0 63 ILE -109.1 129.7 179.6 -57.6 -64.1 64 VAL -72.6 122.5 -179.8 175.1 65 LYS -109.5 -17.6 179.4 -75.4 -49.0 -176.8 -164.7 66 ALA -155.7 156.6 176.3 67 ILE -123.0 142.8 -176.9 65.8 156.5 68 THR -162.4 167.4 178.9 -170.7 69 GLU -115.0 -3.6 -179.3 -59.5 -132.2 -58.7 70 GLN -95.8 137.8 176.6 -44.6 -173.1 -55.4 71 ARG -97.5 109.0 -179.9 173.7 -175.5 174.9 86.7 72 ARG -96.2 -176.6 -179.5 -50.3 -119.0 60.8 -154.9 73 PRO -66.1 156.2 -178.1 28.8 -42.8 74 ALA -28.0 -64.3 -179.1 75 SER -70.5 -32.7 -179.2 -155.3 76 GLU -70.8 -50.0 -179.9 0.0 0.0 0.0 77 ALA -55.9 -55.8 179.3 78 ALA -28.2 -22.5 178.5 79 LEU -84.1 9.2 179.1 -88.1 -65.7 80 LEU -89.8 -4.7 -178.2 -76.6 157.0 81 TYR -152.4 168.2 178.2 61.7 88.8 82 GLU -132.5 108.5 177.7 -152.6 155.4 81.6 83 GLU -61.0 142.3 -178.9 -179.1 168.7 5.5 84 THR -73.3 153.2 179.8 64.5 85 ALA -60.8 -40.2 -179.8 86 GLU -63.5 -37.7 179.9 177.5 -177.2 -27.1 87 SER -68.2 -43.9 -180.0 174.0 88 VAL -61.5 -46.5 178.8 -55.5 89 GLU -57.8 -47.5 -178.3 -51.6 -179.8 66.2 90 LYS -59.7 -41.4 -179.3 -82.6 -160.1 -162.8 68.8 91 ARG -62.8 -51.0 -179.9 -95.3 -172.9 -31.0 169.9 92 GLU -52.8 -62.1 -178.6 -48.6 -73.4 47.2 93 LYS -47.4 -44.5 179.5 -69.8 -163.7 -177.9 -171.9 94 MET -64.1 -36.1 179.1 -93.4 177.1 74.5 95 ALA -65.2 -47.7 179.0 96 LEU -57.8 -56.2 179.5 -79.2 -73.2 97 ALA -51.8 -39.8 179.1 98 ARG -58.0 -57.1 179.7 0.0 0.0 0.0 0.0 99 LYS -59.3 -20.8 179.3 0.0 0.0 0.0 0.0 100 LEU -77.4 -58.7 179.4 -113.0 -154.3 101 ASN -54.9 -16.6 179.5 0.0 0.0 102 ALA -75.1 -54.9 -179.8 103 LEU -74.7 34.7 -179.5 0.0 0.0 104 THR -166.2 12.6 0.0 0.0 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 PRO 33.871 40.837 13.943 2 ALA 30.078 41.011 14.238 3 VAL 29.791 37.803 12.257 4 GLU 30.928 35.580 15.168 5 VAL 28.276 33.618 17.077 6 ARG 29.259 30.783 19.452 7 LEU 27.926 27.296 18.971 8 ASP 26.375 27.193 22.438 9 LYS 24.528 30.512 21.875 10 TRP 23.531 29.374 18.382 11 LEU 22.042 26.079 19.604 12 TRP 19.997 27.996 22.191 13 ALA 18.941 30.610 19.594 14 ALA 17.862 27.782 17.279 15 ARG 15.861 26.362 20.244 16 PHE 17.551 22.949 20.291 17 TYR 18.175 23.253 24.042 18 LYS 16.309 25.439 26.622 19 THR 19.361 27.300 27.886 20 ARG 22.869 27.999 26.680 21 ALA 24.255 26.133 29.748 22 LEU 22.404 23.029 28.686 23 ALA 23.606 23.448 25.052 24 ARG 27.140 23.771 26.521 25 GLU 26.710 20.478 28.489 26 MET 25.515 18.594 25.475 27 ILE 28.492 19.859 23.443 28 GLU 30.938 18.828 26.199 29 GLY 29.218 15.439 26.482 30 GLY 29.998 14.964 22.788 31 LYS 26.211 14.876 22.132 32 VAL 26.541 17.620 19.534 33 HIS 29.050 17.221 16.698 34 TYR 30.189 19.981 14.282 35 ASN 31.158 18.672 10.822 36 GLY 31.392 15.188 12.186 37 GLN 33.565 15.869 15.211 38 ARG 33.555 16.834 18.847 39 SER 33.240 20.585 19.129 40 LYS 33.405 23.187 21.891 41 PRO 31.022 25.790 23.286 42 SER 33.065 28.727 21.872 43 LYS 33.250 27.374 18.316 44 ILE 32.154 30.091 15.896 45 VAL 29.300 28.841 13.760 46 GLU 29.676 28.905 9.963 47 LEU 26.867 28.863 7.403 48 ASN 26.310 25.380 5.867 49 ALA 28.086 23.541 8.655 50 THR 26.653 20.119 9.494 51 LEU 25.556 19.692 13.094 52 THR 24.478 16.300 14.483 53 LEU 22.759 16.571 17.818 54 ARG 20.809 14.548 20.326 55 GLN 17.165 15.599 20.950 56 GLY 15.988 13.620 23.991 57 ASN 16.539 10.257 22.363 58 ASP 16.231 11.515 18.770 59 GLU 19.182 12.268 16.528 60 ARG 18.908 15.104 14.066 61 THR 21.430 16.224 11.464 62 VAL 20.951 19.864 10.434 63 ILE 22.663 22.280 8.091 64 VAL 23.197 25.856 9.421 65 LYS 21.321 28.320 7.136 66 ALA 21.511 31.490 9.316 67 ILE 23.321 32.978 12.349 68 THR 21.773 35.167 15.025 69 GLU 22.048 35.921 18.743 70 GLN 18.332 36.141 19.323 71 ARG 16.193 33.211 20.442 72 ARG 12.919 33.818 18.550 73 PRO 9.605 31.886 18.723 74 ALA 9.066 28.144 18.146 75 SER 8.205 28.311 14.430 76 GLU 10.510 31.323 13.839 77 ALA 13.829 30.087 15.280 78 ALA 13.298 26.789 13.443 79 LEU 14.295 28.808 10.315 80 LEU 18.064 29.075 11.272 81 TYR 18.670 25.571 9.922 82 GLU 17.447 22.865 7.543 83 GLU 17.330 19.302 8.836 84 THR 18.671 16.888 6.175 85 ALA 16.187 14.693 4.325 86 GLU 18.216 11.679 5.444 87 SER 17.917 12.866 9.037 88 VAL 14.110 13.365 8.828 89 GLU 13.692 9.897 7.264 90 LYS 15.805 8.193 9.890 91 ARG 13.832 9.824 12.655 92 GLU 10.507 8.898 11.024 93 LYS 11.437 5.301 10.396 94 MET 12.508 4.870 13.999 95 ALA 9.249 6.454 15.168 96 LEU 7.196 4.178 12.876 97 ALA 9.025 1.017 13.942 98 ARG 8.376 2.131 17.512 99 LYS 4.631 2.416 16.868 100 LEU 4.857 -0.982 15.111 101 ASN 6.458 -3.026 17.875 102 ALA 3.693 -1.335 19.849 103 LEU 0.726 -2.711 17.862 104 THR 2.264 -6.151 18.404 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C C S S S S/H H H H H 10 H H H H H C C C H H 20 H H H H H H H H H H 30 C C T T T T/S S S S S 40 S S S S S S S S S S 50 S S S S/T T T T/S S S S 60 S S S S S S S S S/S S 70 S S S/H H H H H H 3 C 80 S S S S/H H H H H H H 90 H H H H H H H H H H 100 H H H H Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 t T T t h H H H H 10 H H H h T t S S h H 20 H H H H H H H H h T 30 e E E E e T E E e t 40 T T t B t T T e E 50 E E E E E T T E E E 60 E E E E e S 70 h H H H H h T e 80 E E E h H H H H H H 90 H H H H H H H H H H 100 H H h t Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 PRO 18.6 15.0 86.5 2 ALA 0.0 0.0 83.9 3 VAL 17.9 15.1 73.5 4 GLU 68.6 49.5 59.0 5 VAL 110.8 93.3 48.9 6 ARG 108.3 51.8 64.7 7 LEU 147.8 100.0 31.2 8 ASP 102.7 92.9 44.4 9 LYS 123.3 71.1 62.0 10 TRP 205.0 100.0 28.0 11 LEU 147.8 100.0 25.7 12 TRP 159.9 78.0 63.0 13 ALA 72.6 100.0 51.4 14 ALA 72.6 100.0 34.9 15 ARG 145.7 69.7 73.3 16 PHE 165.7 99.3 39.7 17 TYR 168.0 92.8 45.3 18 LYS 16.1 9.3 80.2 19 THR 36.4 34.1 69.5 20 ARG 102.9 49.3 63.9 21 ALA 12.3 17.0 80.1 22 LEU 87.3 59.0 61.1 23 ALA 72.6 100.0 42.4 24 ARG 89.1 42.7 73.3 25 GLU 31.9 23.0 73.4 26 MET 130.5 81.9 48.2 27 ILE 143.5 100.0 43.7 28 GLU 64.8 46.7 72.0 29 GLY 10.0 28.6 75.3 30 GLY 31.6 90.7 75.3 31 LYS 59.8 34.5 67.8 32 VAL 118.8 100.0 41.4 33 HIS 88.4 58.9 68.2 34 TYR 170.4 94.1 48.7 35 ASN 54.4 45.0 70.0 36 GLY 1.9 5.4 69.9 37 GLN 18.5 12.5 88.6 38 ARG 76.1 36.4 79.6 39 SER 73.6 88.0 44.8 40 LYS 52.1 30.1 70.1 41 PRO 106.9 85.8 51.9 42 SER 44.7 53.5 69.8 43 LYS 107.7 62.1 64.1 44 ILE 84.3 58.8 73.1 45 VAL 118.8 100.0 36.5 46 GLU 46.7 33.7 79.8 47 LEU 62.3 42.1 71.9 48 ASN 43.3 35.8 75.7 49 ALA 68.0 93.6 60.8 50 THR 64.1 59.9 63.0 51 LEU 147.8 100.0 30.2 52 THR 66.1 61.8 63.7 53 LEU 147.2 99.6 39.3 54 ARG 182.0 87.1 63.4 55 GLN 113.3 76.2 60.0 56 GLY 0.0 0.0 86.6 57 ASN 1.0 0.8 87.5 58 ASP 41.6 37.6 67.5 59 GLU 43.7 31.6 72.8 60 ARG 165.6 79.3 57.4 61 THR 79.8 74.7 57.9 62 VAL 118.8 100.0 34.6 63 ILE 104.6 72.9 62.9 64 VAL 118.8 100.0 39.0 65 LYS 94.5 54.5 74.1 66 ALA 35.8 49.3 60.9 67 ILE 106.8 74.4 50.4 68 THR 72.2 67.6 52.8 69 GLU 56.8 41.0 65.3 70 GLN 30.6 20.6 78.3 71 ARG 160.5 76.8 62.0 72 ARG 73.5 35.2 72.8 73 PRO 47.3 38.0 73.8 74 ALA 8.8 12.1 81.3 75 SER 0.0 0.0 82.4 76 GLU 105.8 76.4 59.6 77 ALA 70.5 97.1 58.2 78 ALA 40.4 55.7 71.5 79 LEU 23.4 15.9 89.3 80 LEU 134.0 90.6 46.4 81 TYR 162.4 89.7 49.0 82 GLU 35.0 25.2 70.9 83 GLU 126.4 91.2 57.5 84 THR 69.5 65.0 55.3 85 ALA 7.6 10.5 77.0 86 GLU 31.9 23.0 84.9 87 SER 77.3 92.5 66.7 88 VAL 71.2 59.9 65.7 89 GLU 48.6 35.1 63.3 90 LYS 56.3 32.5 77.1 91 ARG 144.2 69.0 71.5 92 GLU 48.0 34.6 66.1 93 LYS 25.3 14.6 80.2 94 MET 30.3 19.0 86.0 95 ALA 20.6 28.4 73.1 96 LEU 35.6 24.1 73.8 97 ALA 18.1 24.9 72.9 98 ARG 151.8 72.7 79.2 99 LYS 115.2 66.4 74.1 100 LEU 22.3 15.1 82.5 101 ASN 54.6 45.1 80.0 102 ALA 18.8 25.9 81.7 103 LEU 84.6 57.2 81.1 104 THR 42.0 39.3 76.9