Protein Data Bank File : 1hd6 Title : PHEROMONE 09-NOV-00 1HD6 Number of Amino Acid Residues : 37 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 ASP ILE CYS ASP ILE ALA ILE ALA GLN CYS 10 SER LEU THR LEU CYS GLN ASP CYS GLU ASN 20 THR PRO ILE CYS GLU LEU ALA VAL LYS GLY 30 SER CYS PRO PRO PRO TRP SER Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 ASP 0.0 174.8 -174.7 62.9 59.3 2 ILE -52.8 -31.8 176.5 -169.0 71.6 3 CYS -63.4 -44.5 178.6 -152.8 4 ASP -68.8 -35.1 168.0 -178.2 -89.5 5 ILE -53.8 -55.8 178.4 -59.1 -174.8 6 ALA -55.7 -37.5 178.3 7 ILE -68.9 -40.4 172.9 -66.2 159.9 8 ALA -58.8 -48.4 -176.5 9 GLN -73.7 -17.2 -166.7 -74.2 -157.0 38.3 10 CYS 37.4 69.2 -168.7 37.2 11 SER -127.9 116.3 176.7 178.1 12 LEU -67.6 -36.8 177.9 -67.1 -150.3 13 THR -60.6 -50.1 -178.9 -39.8 14 LEU -61.8 -26.9 176.8 -134.6 167.7 15 CYS -62.7 -26.6 178.5 -88.3 16 GLN -67.9 -13.6 168.8 -55.3 -166.6 -59.9 17 ASP -73.8 -30.8 -170.3 -64.9 41.9 18 CYS -73.8 140.0 177.4 177.8 19 GLU -48.8 -64.0 -176.7 -176.8 -91.0 -79.7 20 ASN -90.5 64.4 -176.4 59.8 -15.1 21 THR -38.7 -63.3 -177.5 -44.8 22 PRO -62.4 -29.0 175.6 24.4 -35.2 23 ILE -70.5 -38.4 170.7 -59.8 -67.1 24 CYS -58.6 -52.1 177.0 -175.4 25 GLU -51.4 -46.4 -176.0 -73.3 178.7 37.7 26 LEU -66.3 -49.8 178.4 -163.7 147.2 27 ALA -60.4 -37.8 177.9 28 VAL -63.7 -49.5 166.3 159.5 29 LYS -52.8 -38.0 170.4 -116.9 153.3 66.2 164.7 30 GLY -51.1 -50.1 -168.3 31 SER -83.4 -30.6 -178.7 -54.9 32 CYS -141.7 139.2 -172.2 -65.5 33 PRO -70.6 134.7 -178.7 27.6 -34.8 34 PRO -78.8 152.8 -11.8 31.6 -35.8 35 PRO -67.9 163.9 -168.6 28.0 -31.6 36 TRP -93.1 164.2 172.8 -64.9 -104.9 37 SER -74.1 89.3 0.0 40.8 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 ASP -8.019 -7.271 -3.662 2 ILE -6.754 -6.321 -0.170 3 CYS -3.402 -5.248 -1.644 4 ASP -5.298 -2.882 -3.912 5 ILE -7.376 -1.847 -0.874 6 ALA -4.067 -0.922 0.835 7 ILE -3.060 0.935 -2.363 8 ALA -6.350 2.887 -2.403 9 GLN -5.832 3.601 1.287 10 CYS -2.083 4.057 0.612 11 SER -1.568 2.298 3.945 12 LEU 1.568 0.458 5.035 13 THR -0.245 -1.421 7.828 14 LEU -2.865 -2.700 5.393 15 CYS -0.002 -3.672 3.035 16 GLN 0.953 -6.326 5.615 17 ASP -2.295 -8.090 4.584 18 CYS -0.960 -8.206 0.997 19 GLU 0.830 -11.286 -0.349 20 ASN 3.743 -9.363 -1.873 21 THR 4.080 -7.041 1.131 22 PRO 7.224 -5.000 0.133 23 ILE 5.875 -4.642 -3.431 24 CYS 2.652 -3.348 -1.848 25 GLU 4.773 -1.024 0.325 26 LEU 6.672 0.195 -2.764 27 ALA 3.523 0.756 -4.840 28 VAL 1.919 2.505 -1.844 29 LYS 4.878 4.925 -1.707 30 GLY 4.204 5.109 -5.466 31 SER 0.605 6.218 -4.837 32 CYS 1.078 8.554 -1.824 33 PRO 4.194 10.456 -0.673 34 PRO 5.896 9.042 2.473 35 PRO 5.336 9.259 5.361 36 TRP 1.645 8.494 4.788 37 SER -1.551 9.976 6.216 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 3 3 C H 20 H H H H H H H H H H 30 H H C C/P 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 h 10 h H H H H h T t T h 20 H H H H H H H H H H 30 H h S S Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 ASP 13.7 12.4 76.8 2 ILE 77.2 53.8 58.5 3 CYS 79.9 80.6 51.7 4 ASP 26.8 24.2 76.2 5 ILE 64.8 45.1 65.8 6 ALA 72.6 100.0 46.0 7 ILE 94.0 65.5 60.3 8 ALA 14.2 19.5 79.3 9 GLN 59.3 39.9 62.5 10 CYS 88.0 88.7 51.6 11 SER 56.2 67.2 62.6 12 LEU 96.2 65.1 53.2 13 THR 3.7 3.5 88.6 14 LEU 116.0 78.5 61.3 15 CYS 99.2 100.0 42.7 16 GLN 41.5 27.9 78.6 17 ASP 44.6 40.4 65.7 18 CYS 96.2 97.0 49.4 19 GLU 0.9 0.6 82.5 20 ASN 58.4 48.3 58.3 21 THR 74.6 69.8 62.7 22 PRO 37.1 29.8 72.2 23 ILE 41.3 28.8 73.4 24 CYS 98.0 98.7 40.0 25 GLU 78.4 56.6 53.6 26 LEU 22.1 14.9 78.0 27 ALA 37.3 51.4 61.3 28 VAL 118.8 100.0 45.5 29 LYS 74.9 43.2 67.1 30 GLY 1.2 3.3 78.7 31 SER 47.8 57.1 67.6 32 CYS 66.7 67.2 54.6 33 PRO 17.3 13.9 77.6 34 PRO 73.6 59.1 56.7 35 PRO 10.1 8.1 79.0 36 TRP 169.5 82.7 50.1 37 SER 0.0 0.0 82.4