Protein Data Bank File : 1deeh Title : IMMUNE SYSTEM 15-NOV-99 1DEE Number of Amino Acid Residues : 54 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 PHE ASN LYS ASP GLN GLN SER ALA PHE TYR 10 GLU ILE LEU ASN MET PRO ASN LEU ASN GLU 20 ALA GLN ARG ASN GLY PHE ILE GLN SER LEU 30 LYS ASP ASP PRO SER GLN SER THR ASN VAL 40 LEU GLY GLU ALA LYS LYS LEU ASN GLU SER 50 GLN ALA PRO LYS Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 PHE 0.0 -162.3 179.3 59.8 94.2 2 ASN 27.9 73.5 177.9 -114.4 151.7 3 LYS -56.1 -23.0 178.6 0.0 0.0 0.0 0.0 4 ASP -62.7 -44.8 -178.9 -63.6 124.4 5 GLN -62.7 -55.3 -179.9 -171.3 -171.6 37.2 6 GLN -70.6 -25.9 178.5 61.1 178.2 -125.1 7 SER -76.5 -36.9 178.4 68.7 8 ALA -65.9 -41.7 179.8 9 PHE -57.9 -54.8 -180.0 -165.1 108.3 10 TYR -64.1 -21.9 179.5 -72.8 -55.8 11 GLU -77.4 -53.1 179.4 -155.0 69.1 61.7 12 ILE -59.9 -43.5 179.0 -67.0 178.7 13 LEU -61.3 -19.8 -179.5 -121.5 -173.5 14 ASN -104.4 16.3 179.2 -115.2 -113.5 15 MET -90.4 118.2 -179.5 -85.5 176.3 -130.3 16 PRO -64.5 -46.9 -177.8 31.8 -45.1 17 ASN -80.5 -14.0 178.2 -52.5 -60.6 18 LEU -78.5 145.6 178.2 -65.6 -177.6 19 ASN -89.5 159.7 -179.0 65.1 63.3 20 GLU -45.8 -44.9 -179.3 -108.6 -75.9 -72.5 21 ALA -62.2 -35.1 179.8 22 GLN -75.2 -38.5 -179.4 -63.6 173.8 -41.0 23 ARG -61.9 -43.4 179.3 -166.9 174.5 -49.8 123.3 24 ASN -76.8 -22.8 178.6 -61.4 -27.9 25 GLY -70.1 -52.5 178.5 26 PHE -61.3 -28.1 178.9 -80.6 107.6 27 ILE -78.5 -31.8 177.4 -75.5 168.0 28 GLN -62.2 -38.7 179.0 -119.8 -48.1 -90.8 29 SER -65.3 -46.1 178.5 -65.3 30 LEU -57.9 -32.3 179.0 -70.2 -174.4 31 LYS -77.7 -42.6 -179.2 177.7 175.3 163.5 70.3 32 ASP -62.4 -38.4 -178.0 -77.4 15.1 33 ASP -157.1 75.0 -179.6 -175.0 29.6 34 PRO -51.7 -19.5 179.2 25.7 -41.6 35 SER -61.9 -28.8 -179.4 65.6 36 GLN -89.6 7.1 -178.9 -68.8 -107.7 96.7 37 SER -40.8 -43.2 -179.6 -62.4 38 THR -66.2 -49.0 -179.9 -42.3 39 ASN -69.9 -35.6 179.3 -56.2 77.5 40 VAL -69.2 -39.5 178.5 166.8 41 LEU -62.5 -44.5 179.7 173.7 48.9 42 GLY -55.0 -52.5 -179.8 43 GLU -58.5 -39.8 178.6 -68.0 -60.8 137.8 44 ALA -65.2 -43.4 179.7 45 LYS -64.7 -39.3 180.0 -172.7 146.8 62.3 179.6 46 LYS -68.6 -26.2 179.0 -174.0 167.3 172.1 63.5 47 LEU -84.3 -45.0 179.2 178.1 54.9 48 ASN -59.5 -39.1 179.3 -176.2 78.5 49 GLU -51.6 -54.8 -177.7 155.8 -150.1 80.6 50 SER -67.6 -41.6 -179.1 67.5 51 GLN -76.4 0.8 179.2 -59.3 -170.2 153.4 52 ALA -72.9 114.5 -179.7 53 PRO -67.7 -50.3 -179.3 32.4 -43.0 54 LYS 84.8 -80.5 0.0 175.9 63.2 -161.3 66.0 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 PHE 56.040 13.772 47.750 2 ASN 53.249 11.224 48.324 3 LYS 51.540 11.309 44.941 4 ASP 49.056 9.209 46.932 5 GLN 48.190 12.190 49.127 6 GLN 47.560 14.749 46.402 7 SER 45.858 12.267 44.036 8 ALA 43.584 11.134 46.844 9 PHE 43.027 14.833 47.548 10 TYR 42.035 15.699 43.976 11 GLU 39.831 12.610 43.924 12 ILE 37.958 13.447 47.138 13 LEU 37.759 17.097 46.098 14 ASN 36.083 15.718 42.971 15 MET 33.489 13.559 44.703 16 PRO 29.880 14.564 43.794 17 ASN 27.789 12.759 46.424 18 LEU 29.873 13.763 49.454 19 ASN 28.703 16.941 51.167 20 GLU 31.185 19.759 51.825 21 ALA 31.571 18.734 55.469 22 GLN 32.436 15.155 54.508 23 ARG 34.828 16.283 51.783 24 ASN 36.842 18.448 54.173 25 GLY 36.653 15.737 56.818 26 PHE 38.268 13.169 54.519 27 ILE 40.772 15.851 53.533 28 GLN 41.605 16.565 57.162 29 SER 42.594 12.882 57.372 30 LEU 44.785 13.013 54.252 31 LYS 46.515 15.938 55.949 32 ASP 46.584 14.148 59.339 33 ASP 48.218 10.919 58.132 34 PRO 49.041 10.884 54.369 35 SER 50.376 7.327 54.723 36 GLN 46.700 6.341 54.824 37 SER 45.769 8.179 51.613 38 THR 44.597 4.935 49.987 39 ASN 42.412 3.726 52.866 40 VAL 41.110 7.224 53.530 41 LEU 40.303 7.512 49.837 42 GLY 38.537 4.165 50.034 43 GLU 36.184 5.112 52.880 44 ALA 35.311 8.353 51.095 45 LYS 34.761 6.367 47.906 46 LYS 32.684 3.823 49.855 47 LEU 30.660 6.772 51.190 48 ASN 30.249 8.651 47.899 49 GLU 29.138 5.291 46.527 50 SER 26.198 4.984 48.922 51 GLN 25.018 8.580 48.825 52 ALA 24.882 8.412 45.020 53 PRO 21.185 8.941 44.085 54 LYS 21.261 7.922 40.364 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 C C C H H 20 H H H H H H H H H H 30 H H H H C H H H H H 40 H H H H H H H H H H 50 H H/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 T t S S S h H 20 H H H H H H H H H H 30 H H h T T h H H H H 40 H H H H H H H H H H 50 H h Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 PHE 12.2 7.3 89.0 2 ASN 82.3 68.0 62.1 3 LYS 102.5 59.1 82.3 4 ASP 35.9 32.4 84.0 5 GLN 102.8 69.2 55.3 6 GLN 40.5 27.3 73.4 7 SER 24.1 28.9 74.0 8 ALA 71.4 98.3 47.5 9 PHE 99.1 59.4 47.1 10 TYR 43.5 24.0 72.5 11 GLU 50.8 36.7 66.8 12 ILE 143.5 100.0 33.0 13 LEU 76.9 52.1 57.8 14 ASN 18.4 15.2 86.5 15 MET 147.1 92.3 44.3 16 PRO 42.0 33.8 86.2 17 ASN 95.0 78.6 56.9 18 LEU 147.8 100.0 46.8 19 ASN 47.1 39.0 76.1 20 GLU 40.4 29.1 85.3 21 ALA 5.0 6.9 84.8 22 GLN 107.7 72.5 62.4 23 ARG 168.7 80.8 60.7 24 ASN 47.8 39.5 73.7 25 GLY 4.8 13.9 75.9 26 PHE 132.4 79.4 45.2 27 ILE 119.4 83.2 43.7 28 GLN 61.8 41.6 73.0 29 SER 42.6 51.0 62.9 30 LEU 146.8 99.4 45.9 31 LYS 38.2 22.1 89.4 32 ASP 35.1 31.8 76.2 33 ASP 44.8 40.5 70.5 34 PRO 90.5 72.7 73.6 35 SER 20.9 25.0 83.5 36 GLN 66.5 44.7 76.4 37 SER 82.7 98.9 45.6 38 THR 14.6 13.7 79.2 39 ASN 24.7 20.4 80.4 40 VAL 101.2 85.2 50.9 41 LEU 119.2 80.6 49.2 42 GLY 11.6 33.4 67.1 43 GLU 37.9 27.4 70.9 44 ALA 72.6 100.0 33.6 45 LYS 54.2 31.3 68.0 46 LYS 41.0 23.6 85.8 47 LEU 97.1 65.7 65.6 48 ASN 97.1 80.3 51.4 49 GLU 36.6 26.4 76.7 50 SER 30.7 36.7 73.6 51 GLN 86.7 58.4 75.8 52 ALA 43.2 59.5 75.9 53 PRO 29.0 23.3 86.6 54 LYS 0.0 0.0 92.0