Protein Data Bank File : 1qmca Title : INTEGRASE 25-SEP-99 1QMC Number of Amino Acid Residues : 52 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 MET ILE GLN ASN PHE ARG VAL TYR TYR ARG 10 ASP SER ARG ASN PRO LEU TRP LYS GLY PRO 20 ALA LYS LEU LEU TRP LYS GLY GLU GLY ALA 30 VAL VAL ILE GLN ASP ASN SER ASP ILE LYS 40 VAL VAL PRO ARG ARG LYS ALA LYS ILE ILE 50 ARG ASP Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 MET 0.0 -29.7 -179.8 -89.9 -171.1 -84.4 2 ILE -115.2 160.8 179.9 44.0 -80.9 3 GLN -139.3 -65.1 -179.7 -45.2 -151.7 44.4 4 ASN -139.0 79.6 179.7 36.5 -117.8 5 PHE -105.8 130.9 179.6 -76.4 77.9 6 ARG -80.6 109.5 -179.3 -71.4 -179.9 176.8 -165.5 7 VAL -101.8 128.1 179.1 -174.6 8 TYR -110.5 142.4 -178.6 -54.5 -88.9 9 TYR -135.7 143.9 179.3 48.6 -70.0 10 ARG -83.1 177.4 -180.0 -88.1 -131.8 -68.4 168.9 11 ASP -132.0 155.7 -179.7 -92.6 -40.1 12 SER -53.7 -68.5 179.7 -142.6 13 ARG -93.3 20.1 179.8 63.1 -145.3 -167.7 164.7 14 ASN -135.0 110.3 -179.4 -109.1 135.8 15 PRO -68.5 -42.1 -179.6 25.4 -34.4 16 LEU -55.3 158.0 -179.7 73.0 -44.6 17 TRP -90.9 149.5 179.9 -67.2 82.7 18 LYS -87.8 153.8 -179.0 -105.0 -93.5 138.6 126.0 19 GLY -38.9 169.1 179.7 20 PRO -78.5 85.7 -179.8 30.4 -32.5 21 ALA -65.8 166.6 -179.9 22 LYS -83.8 132.4 -179.9 -44.4 -176.0 95.2 147.8 23 LEU -73.3 126.8 180.0 -166.4 62.5 24 LEU -122.3 -45.2 -179.8 -73.0 178.5 25 TRP -144.8 144.8 179.7 -176.4 79.0 26 LYS -153.2 98.4 -179.3 -168.2 172.1 93.0 87.0 27 GLY -135.2 -92.3 -179.7 28 GLU -61.0 -149.2 179.9 -49.9 -119.5 42.5 29 GLY -85.5 15.8 179.7 30 ALA -129.4 145.5 -179.5 31 VAL -124.4 128.9 179.5 -74.4 32 VAL -92.8 125.7 -179.4 -175.7 33 ILE -143.4 149.7 179.5 43.0 100.1 34 GLN -105.5 123.8 -179.7 177.9 166.9 95.7 35 ASP -79.5 -31.8 179.7 -169.3 57.9 36 ASN -158.2 -77.2 179.5 -13.9 -112.9 37 SER -119.0 -22.8 179.7 -35.8 38 ASP -100.2 147.4 179.9 -77.5 -81.8 39 ILE -101.5 130.7 179.9 -46.8 -179.5 40 LYS -124.0 158.1 -180.0 -53.5 147.7 179.1 -94.9 41 VAL -124.9 129.0 -180.0 -168.9 42 VAL -131.7 139.6 180.0 -169.9 43 PRO -52.4 138.5 -180.0 -24.9 32.8 44 ARG -56.8 -29.3 179.7 -179.0 68.5 -163.3 -77.7 45 ARG -66.5 -31.1 180.0 -176.6 155.9 -96.5 174.2 46 LYS -106.7 23.8 179.6 -58.8 -168.5 -153.3 -168.9 47 ALA -133.4 158.8 -179.9 48 LYS -145.7 110.1 179.8 -63.6 165.9 64.4 -164.4 49 ILE -86.8 147.6 -179.9 -175.2 177.4 50 ILE -146.0 160.2 179.7 -51.1 -175.4 51 ARG -95.4 136.5 -179.8 -147.5 -175.0 -166.1 -169.2 52 ASP -56.4 125.4 0.0 68.1 -40.1 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 MET -2.741 13.718 -4.283 2 ILE -0.700 10.945 -2.676 3 GLN 2.967 10.613 -1.743 4 ASN 3.720 7.956 0.857 5 PHE 0.611 6.068 1.958 6 ARG 0.858 2.660 3.632 7 VAL -1.497 0.319 1.783 8 TYR -2.513 -3.003 3.310 9 TYR -4.173 -5.821 1.356 10 ARG -5.943 -9.077 2.224 11 ASP -5.425 -12.469 0.587 12 SER -7.656 -15.161 -0.932 13 ARG -6.728 -18.028 1.384 14 ASN -5.256 -15.592 3.922 15 PRO -7.550 -13.495 6.225 16 LEU -4.745 -11.403 7.728 17 TRP -3.701 -8.204 5.948 18 LYS -0.463 -7.845 3.990 19 GLY 2.281 -5.348 4.821 20 PRO 2.086 -1.609 3.956 21 ALA 2.888 -1.721 0.249 22 LYS 3.849 1.404 -1.702 23 LEU 0.999 3.356 -3.295 24 LEU 1.309 3.571 -7.083 25 TRP -2.222 3.792 -8.482 26 LYS -5.714 4.253 -7.049 27 GLY -8.719 4.655 -9.325 28 GLU -11.337 2.028 -10.133 29 GLY -12.114 -0.837 -7.716 30 ALA -8.501 -2.023 -7.864 31 VAL -5.333 -0.598 -6.310 32 VAL -1.790 -1.034 -7.609 33 ILE 0.915 -1.313 -4.955 34 GLN 4.532 -2.448 -4.709 35 ASP 5.487 -4.758 -1.839 36 ASN 9.216 -4.424 -2.537 37 SER 10.441 -4.605 -6.132 38 ASP 7.414 -6.180 -7.837 39 ILE 4.106 -4.413 -8.406 40 LYS 0.841 -6.103 -7.458 41 VAL -2.823 -5.151 -7.784 42 VAL -5.524 -5.868 -5.211 43 PRO -9.259 -4.926 -5.177 44 ARG -10.006 -1.751 -3.209 45 ARG -12.555 -3.796 -1.259 46 LYS -9.743 -6.034 -0.003 47 ALA -7.254 -3.186 0.461 48 LYS -6.729 -0.382 2.975 49 ILE -4.668 2.743 2.312 50 ILE -3.174 4.792 5.144 51 ARG -0.978 7.852 5.675 52 ASP 2.566 7.439 6.998 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S S S/S S S S S S S 10 S/T T T T S S S S S S/S 20 S S S S/S S S S/T T T T/S 30 S S S S/T T T T/S S S S 40 S S S/T T T T/S S S S S 50 S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S e E E E E E e 10 S S S E E E 20 E E E E E E e S e E 30 E E E E e S S e E E 40 E E E e T e E E E E 50 E e Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 MET 0.0 0.0 88.7 2 ILE 86.6 60.3 48.9 3 GLN 14.8 9.9 84.9 4 ASN 38.7 32.0 75.1 5 PHE 130.7 78.3 54.1 6 ARG 77.7 37.2 70.3 7 VAL 117.9 99.2 34.6 8 TYR 130.4 72.1 47.3 9 TYR 170.2 94.0 40.1 10 ARG 111.8 53.5 62.7 11 ASP 59.5 53.9 66.0 12 SER 7.5 9.0 82.8 13 ARG 0.0 0.0 89.3 14 ASN 55.7 46.1 61.3 15 PRO 33.8 27.1 83.3 16 LEU 62.2 42.1 71.4 17 TRP 131.2 64.0 62.5 18 LYS 81.3 46.9 77.3 19 GLY 9.9 28.6 56.7 20 PRO 77.1 61.9 56.9 21 ALA 70.7 97.4 55.3 22 LYS 40.2 23.2 83.6 23 LEU 146.4 99.0 36.3 24 LEU 84.9 57.4 57.9 25 TRP 91.6 44.7 64.7 26 LYS 118.6 68.4 53.9 27 GLY 12.2 35.1 67.4 28 GLU 5.0 3.6 80.8 29 GLY 0.2 0.6 70.6 30 ALA 39.3 54.1 54.8 31 VAL 116.9 98.4 32.9 32 VAL 88.2 74.3 38.1 33 ILE 143.5 100.0 35.9 34 GLN 111.2 74.8 55.4 35 ASP 82.0 74.2 64.4 36 ASN 35.1 29.0 80.1 37 SER 8.4 10.0 81.5 38 ASP 13.1 11.8 77.5 39 ILE 74.8 52.1 62.0 40 LYS 76.6 44.2 69.9 41 VAL 61.6 51.8 56.5 42 VAL 100.0 84.2 45.1 43 PRO 62.1 49.9 60.7 44 ARG 111.9 53.6 67.4 45 ARG 0.2 0.1 86.5 46 LYS 83.8 48.3 64.5 47 ALA 72.0 99.2 42.8 48 LYS 69.1 39.9 66.1 49 ILE 121.1 84.4 42.8 50 ILE 60.6 42.2 67.9 51 ARG 41.9 20.1 77.7 52 ASP 54.3 49.2 77.4