Protein Data Bank File : 1b69a Title : INTEGRASE/DNA 21-JAN-99 1B69 Number of Amino Acid Residues : 69 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 GLU LYS ARG ARG ASP ASN ARG GLY ARG ILE 10 LEU LYS THR GLY GLU SER GLN ARG LYS ASP 20 GLY ARG TYR LEU TYR LYS TYR ILE ASP SER 30 PHE GLY GLU PRO GLN PHE VAL TYR SER TRP 40 LYS LEU VAL ALA THR ASP ARG VAL PRO ALA 50 GLY LYS ARG ASP ALA ILE SER LEU ARG GLU 60 LYS ILE ALA GLU LEU GLN LYS ASP ILE Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 GLU 0.0 124.4 179.4 -51.1 176.2 -41.7 2 LYS -131.5 126.2 179.0 -110.9 97.3 67.0 138.9 3 ARG -78.2 168.3 -179.5 -72.4 169.0 77.1 163.4 4 ARG -131.5 173.5 179.0 -54.6 -146.7 -135.1 162.7 5 ASP -84.0 -164.4 179.6 50.2 0.9 6 ASN -75.5 -1.0 -179.8 -57.2 -36.5 7 ARG -105.0 -108.0 -179.9 -58.5 -64.7 -155.5 164.9 8 GLY -153.8 15.1 180.0 9 ARG -82.3 -164.0 -179.5 -77.8 169.8 -53.0 167.0 10 ILE -130.8 119.3 178.9 -60.4 -84.9 11 LEU -89.8 143.4 180.0 -74.9 157.5 12 LYS -89.4 160.4 -179.7 -86.3 -85.0 158.5 56.2 13 THR -46.8 162.8 179.9 -65.4 14 GLY 79.0 -36.5 -179.2 15 GLU -92.3 158.2 179.8 -65.5 166.3 40.6 16 SER -176.1 -162.8 179.6 46.3 17 GLN -143.3 141.1 -178.9 55.1 -169.6 -176.1 18 ARG -84.6 -154.2 -179.0 -129.5 -166.4 93.6 164.4 19 LYS -86.6 -20.7 -179.3 -53.5 143.1 78.6 -48.2 20 ASP -83.0 4.2 179.9 -61.5 -15.1 21 GLY 81.6 -19.1 179.8 22 ARG -67.5 152.6 -179.4 64.9 -165.4 58.0 165.9 23 TYR -76.9 153.2 -179.9 -68.0 -64.7 24 LEU -141.7 125.4 -180.0 162.1 57.0 25 TYR -119.0 106.5 180.0 167.1 66.0 26 LYS -95.3 137.6 179.6 -147.4 -167.7 -157.0 -154.4 27 TYR -153.8 129.6 -179.5 71.9 88.2 28 ILE -72.6 119.4 -179.4 -43.6 -73.1 29 ASP -81.1 173.1 -179.3 23.8 -55.7 30 SER -66.6 11.7 179.9 -62.9 31 PHE -100.1 -29.9 -179.8 -82.5 -85.4 32 GLY 101.0 27.5 180.0 33 GLU -137.6 115.8 -180.0 0.8 -175.1 -30.2 34 PRO -42.8 151.9 -179.7 -29.3 31.1 35 GLN -127.8 133.8 -178.6 -174.1 129.7 123.3 36 PHE -98.9 133.5 176.5 -90.8 71.6 37 VAL -128.8 118.2 -177.5 179.7 38 TYR -103.5 160.3 179.4 -74.1 -85.8 39 SER -179.0 169.7 -179.9 164.0 40 TRP -118.8 -34.9 -179.1 -77.6 105.4 41 LYS -94.2 126.8 179.0 -53.2 157.0 45.0 155.9 42 LEU -72.4 -34.7 178.7 177.7 58.2 43 VAL -136.0 153.8 -178.1 -44.5 44 ALA -69.4 65.7 179.0 45 THR -151.8 -31.6 -179.9 -45.1 46 ASP -68.1 -164.1 179.9 -79.1 49.6 47 ARG -130.0 -160.0 179.8 -71.6 -69.9 -148.5 165.7 48 VAL -157.1 124.0 179.4 -66.1 49 PRO -42.7 132.4 179.7 -29.5 30.8 50 ALA -50.6 146.9 -179.8 51 GLY 97.6 -19.6 179.8 52 LYS -87.5 153.6 180.0 -80.6 45.8 171.9 -171.0 53 ARG -81.0 126.3 -179.8 -50.6 -134.4 -57.1 165.6 54 ASP -56.3 155.7 -179.9 43.2 33.8 55 ALA -168.5 159.2 178.6 56 ILE -70.9 172.0 179.6 64.4 -173.9 57 SER -76.6 141.9 -179.0 92.1 58 LEU -45.2 -33.0 -179.9 -158.1 145.4 59 ARG -61.5 -29.6 179.0 -75.8 -94.5 160.9 164.4 60 GLU -76.2 -35.2 178.9 -76.3 -71.4 -55.5 61 LYS -68.6 -53.8 179.1 -59.9 -161.3 176.5 -160.8 62 ILE -49.1 -42.8 179.8 -85.2 169.8 63 ALA -55.0 -34.2 -179.6 64 GLU -72.6 -39.0 -179.8 -67.5 -168.3 -66.0 65 LEU -68.1 -29.2 -180.0 -43.2 -175.6 66 GLN -79.2 -37.9 -180.0 -71.6 -172.5 31.8 67 LYS -74.5 -94.6 -180.0 -77.0 164.7 167.0 -75.6 68 ASP -157.2 -44.6 -179.5 -166.3 -17.7 69 ILE -151.0 36.8 0.0 -169.8 173.9 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 GLU 16.125 -11.804 10.164 2 LYS 13.599 -9.211 11.442 3 ARG 13.058 -5.789 9.840 4 ARG 12.396 -2.726 12.052 5 ASP 10.441 0.544 11.822 6 ASN 12.025 3.979 11.286 7 ARG 12.972 3.844 15.003 8 GLY 14.529 0.737 16.613 9 ARG 11.536 -1.480 17.451 10 ILE 10.628 -4.749 15.643 11 LEU 7.800 -5.022 13.075 12 LYS 6.207 -8.474 12.563 13 THR 5.738 -10.018 9.085 14 GLY 2.818 -8.568 7.102 15 GLU 3.616 -5.168 8.679 16 SER 6.035 -2.611 7.202 17 GLN 6.327 1.103 6.286 18 ARG 5.877 2.945 2.962 19 LYS 7.870 5.964 1.705 20 ASP 5.821 8.489 3.737 21 GLY 7.093 6.898 6.981 22 ARG 3.487 5.919 7.770 23 TYR 2.969 2.240 8.645 24 LEU 1.475 -0.126 6.037 25 TYR 0.059 -3.625 6.717 26 LYS -0.644 -5.701 3.575 27 TYR -2.564 -8.990 4.002 28 ILE -4.217 -11.337 1.487 29 ASP -7.916 -11.647 2.423 30 SER -9.994 -14.814 1.865 31 PHE -10.808 -13.298 -1.566 32 GLY -7.304 -13.598 -3.086 33 GLU -6.621 -9.841 -3.420 34 PRO -4.058 -8.005 -1.163 35 GLN -5.595 -5.433 1.251 36 PHE -3.998 -2.093 2.301 37 VAL -4.305 -0.716 5.879 38 TYR -2.659 2.695 6.583 39 SER -1.798 4.379 9.898 40 TRP 0.868 6.544 11.637 41 LYS 0.948 5.155 15.205 42 LEU 2.204 1.562 15.578 43 VAL 0.506 1.389 19.002 44 ALA -2.083 3.649 20.614 45 THR 0.633 5.593 22.458 46 ASP 2.687 7.384 19.778 47 ARG 1.568 10.682 18.139 48 VAL 1.047 11.972 14.555 49 PRO 2.585 15.016 12.722 50 ALA 0.117 17.917 12.717 51 GLY -1.907 18.061 9.461 52 LYS -2.358 14.263 9.463 53 ARG -5.779 12.693 10.156 54 ASP -5.928 11.150 13.647 55 ALA -6.444 7.368 13.703 56 ILE -6.080 4.386 16.036 57 SER -2.784 2.519 15.957 58 LEU -2.501 -0.021 13.126 59 ARG -2.343 -2.598 15.938 60 GLU -5.932 -1.643 16.807 61 LYS -6.974 -2.079 13.160 62 ILE -5.222 -5.452 12.769 63 ALA -7.083 -6.508 15.936 64 GLU -10.344 -5.866 14.042 65 LEU -9.238 -7.961 11.053 66 GLN -8.329 -10.832 13.404 67 LYS -11.620 -10.665 15.324 68 ASP -14.528 -10.043 12.911 69 ILE -15.444 -6.343 12.587 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S S S/T T T T/S S S S 10 C T T T T C C T T T 20 T/S S S S S S S S S/T T 30 T T/S S S S S S S S S 40 S C C C S S S S S S 50 S S S S S S H H H H 60 H H H H H H H H/S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S S S 10 t T e E E E e S S 20 S e E E E E E E e T 30 T t e E E E E E E S 40 S t T T t t T 50 T t h H H H 60 H H H H H H h Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 GLU 0.0 0.0 95.6 2 LYS 55.7 32.1 76.9 3 ARG 13.4 6.4 85.6 4 ARG 82.8 39.6 75.7 5 ASP 110.5 100.0 51.2 6 ASN 53.2 44.0 71.4 7 ARG 36.7 17.6 89.3 8 GLY 12.1 34.9 75.0 9 ARG 130.2 62.3 62.7 10 ILE 76.9 53.6 64.4 11 LEU 142.9 96.7 49.5 12 LYS 45.9 26.5 85.5 13 THR 0.0 0.0 87.5 14 GLY 12.8 36.9 64.1 15 GLU 127.1 91.7 49.9 16 SER 47.7 57.1 65.8 17 GLN 113.3 76.2 67.6 18 ARG 107.3 51.4 64.8 19 LYS 26.8 15.5 89.3 20 ASP 60.2 54.5 74.6 21 GLY 16.1 46.2 78.4 22 ARG 140.0 67.0 57.2 23 TYR 165.1 91.2 55.7 24 LEU 128.4 86.9 46.9 25 TYR 143.6 79.3 38.1 26 LYS 82.9 47.8 57.9 27 TYR 136.8 75.6 52.1 28 ILE 53.3 37.2 68.9 29 ASP 86.3 78.1 61.5 30 SER 0.0 0.0 82.6 31 PHE 29.3 17.6 83.4 32 GLY 6.6 19.1 70.1 33 GLU 36.4 26.3 73.8 34 PRO 76.7 61.6 59.4 35 GLN 71.0 47.8 73.9 36 PHE 91.1 54.6 56.4 37 VAL 101.0 85.0 43.9 38 TYR 105.5 58.3 59.9 39 SER 79.0 94.5 52.8 40 TRP 160.2 78.1 53.3 41 LYS 132.0 76.1 62.1 42 LEU 138.0 93.4 50.5 43 VAL 63.7 53.6 68.7 44 ALA 32.4 44.6 70.3 45 THR 14.1 13.2 81.9 46 ASP 56.3 50.9 72.5 47 ARG 6.0 2.9 85.6 48 VAL 90.5 76.2 47.1 49 PRO 45.7 36.7 69.5 50 ALA 0.0 0.0 91.3 51 GLY 0.0 0.0 81.9 52 LYS 98.3 56.7 63.9 53 ARG 0.0 0.0 93.8 54 ASP 2.8 2.6 81.3 55 ALA 40.2 55.3 79.1 56 ILE 66.3 46.2 66.1 57 SER 83.2 99.6 51.3 58 LEU 146.1 98.9 39.6 59 ARG 113.2 54.2 66.8 60 GLU 56.1 40.5 65.7 61 LYS 113.6 65.5 60.0 62 ILE 128.3 89.4 46.7 63 ALA 36.9 50.9 67.2 64 GLU 60.6 43.7 67.0 65 LEU 92.8 62.8 58.1 66 GLN 32.6 22.0 75.1 67 LYS 25.6 14.8 82.3 68 ASP 3.4 3.1 82.9 69 ILE 0.0 0.0 86.7