Protein Data Bank File : 1guxb Title : COMPLEX (TRANSCRIPTION REG/PEPTIDE) 15-NOV-97 1GUX Number of Amino Acid Residues : 141 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 THR SER LEU SER LEU PHE TYR LYS LYS VAL 10 TYR ARG LEU ALA TYR LEU ARG LEU ASN THR 20 LEU CYS GLU ARG LEU LEU SER GLU HIS PRO 30 GLU LEU GLU HIS ILE ILE TRP THR LEU PHE 40 GLN HIS THR LEU GLN ASN GLU TYR GLU LEU 50 MET ARG ASP ARG HIS LEU ASP GLN ILE MET 60 MET CYS SER MET TYR GLY ILE CYS LYS VAL 70 LYS ASN ILE ASP LEU LYS PHE LYS ILE ILE 80 VAL THR ALA TYR LYS ASP LEU PRO HIS ALA 90 VAL GLN GLU THR PHE LYS ARG VAL LEU ILE 100 LYS GLU GLU GLU TYR ASP SER ILE ILE VAL 110 PHE TYR ASN SER VAL PHE MET GLN ARG LEU 120 LYS THR ASN ILE LEU GLN TYR ALA SER THR 130 ARG PRO PRO THR LEU SER PRO ILE PRO HIS 140 ILE Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 THR 0.0 -53.9 177.7 -32.2 2 SER -59.8 -52.9 179.6 50.6 3 LEU -61.0 -37.2 180.0 -169.2 47.7 4 SER -68.1 -35.9 179.6 61.7 5 LEU -68.8 -47.8 179.5 -170.6 171.2 6 PHE -55.0 -49.7 179.6 -178.3 68.8 7 TYR -63.0 -40.0 177.8 -98.1 -84.4 8 LYS -56.1 -44.9 179.1 -66.4 -163.6 179.8 -62.2 9 LYS -63.6 -45.9 179.1 -76.7 179.1 160.4 -70.1 10 VAL -60.6 -45.6 -179.5 170.4 11 TYR -62.3 -41.0 179.4 -66.9 -31.2 12 ARG -60.0 -46.8 179.1 -73.1 -171.1 -96.7 -135.1 13 LEU -61.2 -52.6 -179.2 -133.2 -153.3 14 ALA -54.3 -48.3 -178.7 15 TYR -66.5 -40.2 179.8 178.3 79.6 16 LEU -59.3 -44.7 180.0 -74.6 170.1 17 ARG -67.0 -39.1 178.7 -62.8 173.7 172.8 176.2 18 LEU -58.4 -52.5 -178.9 -153.6 -137.1 19 ASN -55.6 -39.6 178.6 178.0 -104.9 20 THR -64.4 -48.0 179.3 -61.5 21 LEU -63.8 -43.5 -178.8 -67.4 178.9 22 CYS -65.3 -44.5 -180.0 -70.3 23 GLU -61.2 -26.2 -179.4 -76.5 -167.2 13.7 24 ARG -90.1 -37.0 -177.5 -173.8 -164.3 -54.3 168.1 25 LEU -104.2 -24.0 -176.9 -92.0 23.4 26 LEU -120.8 43.1 179.4 -61.1 173.3 27 SER -48.7 -54.7 174.7 -18.2 28 GLU -88.5 152.0 -176.6 57.6 -66.8 -72.5 29 HIS 80.4 45.5 180.0 -47.2 126.2 30 PRO -65.9 -11.4 -178.0 -25.7 44.2 31 GLU -79.8 -20.6 -178.3 67.1 -73.9 -13.0 32 LEU -66.5 -42.3 -177.9 -60.5 177.7 33 GLU -50.6 -43.1 -178.5 175.6 -167.9 -79.3 34 HIS -71.2 -27.5 178.4 -156.3 -20.8 35 ILE -77.8 -47.2 176.5 -65.9 169.0 36 ILE -55.6 -42.7 179.8 -66.2 163.6 37 TRP -60.4 -43.5 179.3 170.1 -118.1 38 THR -60.5 -41.2 179.2 -56.6 39 LEU -66.5 -45.9 -179.6 -156.4 -139.6 40 PHE -58.1 -51.8 178.8 -169.3 2.0 41 GLN -63.4 -40.7 178.7 -171.6 -78.2 130.8 42 HIS -59.6 -41.4 179.7 163.1 71.3 43 THR -62.0 -43.1 -179.1 -54.5 44 LEU -69.2 -39.6 179.7 -58.3 170.0 45 GLN -81.9 -44.4 -176.2 174.7 179.8 -165.0 46 ASN -99.0 -24.2 -178.9 -56.2 -56.8 47 GLU -122.1 35.5 -177.3 -54.3 -66.9 -14.0 48 TYR -52.7 -22.0 178.6 64.6 79.7 49 GLU -66.5 -13.7 177.6 -68.9 -69.4 65.1 50 LEU -74.1 -18.9 177.9 -111.5 12.8 51 MET -81.8 -20.4 -179.0 -80.5 -61.3 -75.7 52 ARG -56.1 118.3 -178.2 177.5 -177.9 -77.1 100.9 53 ASP 61.7 21.7 179.0 -68.6 -38.8 54 ARG -123.8 -175.8 -175.6 -76.5 -167.8 -88.1 -113.5 55 HIS -120.5 135.5 178.0 -161.1 -82.1 56 LEU -46.5 -41.5 -178.0 -133.8 -149.6 57 ASP -68.7 -15.0 179.6 -60.1 -11.6 58 GLN -78.2 -41.7 176.5 -72.9 162.6 -10.5 59 ILE -64.5 -40.4 179.6 -58.3 -49.0 60 MET -59.1 -49.2 -177.5 175.4 -177.3 69.0 61 MET -68.3 -36.6 178.7 -70.9 -177.8 -86.0 62 CYS -65.9 -38.9 177.8 -79.2 63 SER -64.2 -43.3 179.9 -69.3 64 MET -61.9 -52.3 -177.9 -70.5 174.7 62.8 65 TYR -58.8 -45.0 179.9 -175.4 81.4 66 GLY -61.6 -46.2 177.8 67 ILE -63.1 -52.2 178.8 -68.2 -54.1 68 CYS -58.5 -23.0 176.8 -68.2 69 LYS -69.5 -55.1 178.1 -98.0 -56.4 -132.4 -151.7 70 VAL -59.9 -43.8 -179.5 -96.2 71 LYS -71.0 2.3 179.8 -62.1 -59.8 -178.3 -178.9 72 ASN 43.7 50.8 177.9 -62.6 93.3 73 ILE -106.0 124.1 178.6 -63.1 -84.2 74 ASP -65.8 101.0 178.7 34.8 24.4 75 LEU -148.3 97.0 -179.4 -176.4 69.1 76 LYS -66.3 144.8 178.1 -81.6 -155.6 165.5 -172.5 77 PHE -60.9 -38.6 178.6 -137.6 -46.9 78 LYS -57.2 -39.7 179.9 -179.1 -147.1 67.6 173.8 79 ILE -67.3 -36.2 -178.9 -66.1 -59.7 80 ILE -67.7 -50.6 -178.9 -67.2 172.9 81 VAL -60.8 -37.9 176.8 132.4 82 THR -68.7 -39.6 178.8 -71.5 83 ALA -71.9 -37.6 179.9 84 TYR -55.9 -40.0 179.3 175.5 63.9 85 LYS -56.6 -24.8 179.2 -81.0 175.8 -59.1 176.5 86 ASP -81.0 -2.2 178.1 -72.7 -5.5 87 LEU -71.3 139.0 -179.2 -61.2 -157.7 88 PRO -46.1 -49.3 -179.7 24.9 -40.1 89 HIS -83.3 -12.6 -175.5 66.3 109.6 90 ALA -54.9 133.9 -179.8 91 VAL -131.6 131.3 -176.7 129.9 92 GLN -61.1 -21.3 179.2 67.7 171.0 -120.5 93 GLU -61.1 -28.2 -178.8 -169.6 -168.8 -0.7 94 THR -60.2 -30.1 178.6 -60.3 95 PHE -108.2 -19.8 -179.8 55.7 80.3 96 LYS -86.6 -23.9 -178.5 -68.4 -158.3 159.7 -53.4 97 ARG -130.9 102.0 -176.8 -177.1 163.4 -159.0 -81.5 98 VAL -129.3 139.4 178.8 -170.9 99 LEU -65.9 122.8 178.2 -161.4 -132.4 100 ILE -97.1 -89.9 -178.2 -53.3 -54.8 101 LYS -91.3 -106.6 -178.5 -133.4 -169.8 169.2 -169.7 102 GLU -82.7 -49.8 178.8 38.6 -92.4 -38.0 103 GLU -154.0 26.8 179.0 -82.2 159.9 52.5 104 GLU -94.5 139.4 179.3 -179.2 77.3 20.2 105 TYR -125.3 145.2 179.4 -74.2 76.6 106 ASP -157.6 -173.1 -179.0 -135.9 -49.0 107 SER -71.0 169.2 -179.7 80.2 108 ILE -65.3 -28.3 178.2 -166.5 174.5 109 ILE -65.2 -36.7 179.0 -69.6 177.0 110 VAL -69.9 -40.3 178.1 177.6 111 PHE -63.1 -40.8 179.3 166.7 69.0 112 TYR -61.4 -62.6 -178.7 174.1 76.0 113 ASN -59.0 -42.2 -177.2 -67.2 -28.3 114 SER -90.7 -21.3 -178.1 -60.3 115 VAL -125.9 -66.1 -177.6 -168.2 116 PHE -53.5 -60.3 -176.5 -180.0 89.1 117 MET -61.6 -31.1 177.6 -175.4 -92.8 -73.9 118 GLN -64.6 -47.6 -178.2 -62.2 -51.7 -38.7 119 ARG -68.3 -36.7 -177.7 -168.7 89.7 44.4 98.2 120 LEU -106.5 3.6 -179.5 -74.5 124.4 121 LYS -43.4 -54.5 -179.4 -167.6 -159.3 -70.0 -82.9 122 THR -63.6 -38.4 178.8 68.3 123 ASN -66.0 -41.9 -179.7 -172.5 -85.5 124 ILE -67.2 -42.9 -179.4 -67.4 177.0 125 LEU -62.1 -25.5 -179.7 -104.6 9.3 126 GLN -59.6 -16.9 179.1 86.2 -167.3 -48.1 127 TYR -84.9 1.8 178.5 -65.2 -66.4 128 ALA -79.1 -20.0 -179.5 129 SER -75.4 153.4 179.7 171.8 130 THR -88.1 -1.0 -179.6 41.7 131 ARG -74.2 161.1 179.7 75.3 -157.5 50.5 138.5 132 PRO -62.6 125.6 179.7 -27.9 42.9 133 PRO -76.3 144.4 177.6 30.2 -41.3 134 THR -88.8 94.6 -174.8 10.7 135 LEU -87.2 153.4 179.5 -53.6 179.0 136 SER -80.1 139.5 -179.9 -78.6 137 PRO -59.4 136.3 178.4 -26.1 41.1 138 ILE -66.1 127.4 -179.1 -70.9 177.7 139 PRO -62.0 133.8 -179.6 34.1 -41.6 140 HIS -54.3 126.2 -179.7 60.6 3.8 141 ILE 70.2 -43.8 0.0 -165.9 -164.8 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 THR 39.961 14.086 67.571 2 SER 38.287 15.911 64.685 3 LEU 36.313 17.884 67.285 4 SER 39.384 18.289 69.461 5 LEU 41.299 19.619 66.463 6 PHE 38.403 21.883 65.602 7 TYR 38.263 23.280 69.143 8 LYS 42.000 23.776 69.229 9 LYS 41.738 25.943 66.104 10 VAL 38.778 27.820 67.511 11 TYR 40.537 28.476 70.845 12 ARG 43.673 29.705 69.085 13 LEU 41.646 32.179 66.982 14 ALA 39.548 33.261 69.942 15 TYR 42.563 33.857 72.194 16 LEU 44.510 35.753 69.573 17 ARG 41.643 38.161 69.100 18 LEU 41.155 38.355 72.915 19 ASN 44.828 39.174 73.448 20 THR 44.712 41.991 70.889 21 LEU 41.733 43.717 72.516 22 CYS 43.185 43.226 76.023 23 GLU 46.668 44.473 75.237 24 ARG 44.928 47.554 73.894 25 LEU 42.136 48.217 76.437 26 LEU 43.383 46.499 79.602 27 SER 46.985 47.631 79.321 28 GLU 46.880 48.142 83.080 29 HIS 45.002 45.200 84.722 30 PRO 47.052 42.439 82.978 31 GLU 45.632 39.753 85.290 32 LEU 42.221 40.025 83.679 33 GLU 42.973 38.567 80.206 34 HIS 43.667 35.111 81.615 35 ILE 40.419 35.347 83.631 36 ILE 38.415 36.606 80.633 37 TRP 40.024 33.736 78.685 38 THR 38.846 31.233 81.245 39 LEU 35.239 32.491 80.984 40 PHE 35.431 32.591 77.120 41 GLN 36.809 29.045 76.906 42 HIS 34.283 27.772 79.478 43 THR 31.477 29.229 77.303 44 LEU 32.720 27.522 74.119 45 GLN 33.161 24.157 75.745 46 ASN 30.257 24.162 78.214 47 GLU 27.681 26.683 76.963 48 TYR 28.242 26.071 73.231 49 GLU 24.498 26.488 72.368 50 LEU 25.214 30.195 72.840 51 MET 27.250 29.856 69.587 52 ARG 24.300 28.599 67.508 53 ASP 23.683 31.104 64.695 54 ARG 26.028 33.471 66.427 55 HIS 29.646 34.684 66.092 56 LEU 32.655 33.788 68.202 57 ASP 33.541 37.494 68.637 58 GLN 30.211 38.132 70.240 59 ILE 31.030 35.617 72.964 60 MET 34.495 37.214 73.205 61 MET 33.283 40.746 73.785 62 CYS 30.610 39.622 76.235 63 SER 33.276 37.694 78.221 64 MET 35.523 40.792 78.383 65 TYR 32.691 43.012 79.517 66 GLY 31.395 40.534 82.162 67 ILE 34.759 39.924 83.850 68 CYS 35.592 43.648 83.976 69 LYS 32.107 44.063 85.483 70 VAL 32.798 41.770 88.533 71 LYS 36.323 43.177 88.824 72 ASN 34.785 46.637 88.917 73 ILE 37.194 47.816 86.250 74 ASP 35.743 50.757 84.330 75 LEU 35.418 49.414 80.757 76 LYS 32.418 50.412 78.685 77 PHE 30.971 48.033 76.089 78 LYS 31.051 50.978 73.628 79 ILE 34.799 51.225 74.174 80 ILE 35.137 47.482 73.564 81 VAL 33.038 47.615 70.393 82 THR 35.013 50.637 69.119 83 ALA 38.284 48.779 69.719 84 TYR 36.786 45.658 68.134 85 LYS 36.298 47.568 64.855 86 ASP 40.061 47.872 64.385 87 LEU 40.524 44.112 64.077 88 PRO 41.321 43.431 60.349 89 HIS 38.320 41.190 59.721 90 ALA 35.990 43.159 62.073 91 VAL 32.612 44.273 60.798 92 GLN 30.199 46.418 62.836 93 GLU 27.206 44.249 61.981 94 THR 28.739 41.669 64.330 95 PHE 27.913 43.875 67.324 96 LYS 25.047 45.872 65.913 97 ARG 23.096 42.814 64.772 98 VAL 23.018 39.823 67.084 99 LEU 20.524 36.973 67.366 100 ILE 18.569 37.422 70.593 101 LYS 15.633 35.039 70.942 102 GLU 13.919 33.041 68.154 103 GLU 14.441 35.345 65.204 104 GLU 14.672 38.670 66.999 105 TYR 17.870 40.638 66.431 106 ASP 19.353 43.470 68.465 107 SER 22.693 44.976 69.583 108 ILE 25.362 42.981 71.388 109 ILE 24.418 44.798 74.606 110 VAL 20.921 43.278 74.306 111 PHE 22.418 39.866 73.692 112 TYR 24.671 40.378 76.787 113 ASN 21.984 41.535 79.281 114 SER 19.261 39.208 78.025 115 VAL 21.032 36.001 77.014 116 PHE 24.759 35.725 77.710 117 MET 24.840 37.242 81.202 118 GLN 21.720 35.323 82.255 119 ARG 23.352 32.061 81.201 120 LEU 26.763 32.764 82.664 121 LYS 25.950 34.873 85.759 122 THR 26.984 32.228 88.351 123 ASN 30.125 31.348 86.404 124 ILE 31.023 35.054 86.098 125 LEU 30.253 35.825 89.744 126 GLN 32.750 33.226 90.895 127 TYR 35.346 35.889 89.971 128 ALA 34.019 38.223 92.702 129 SER 36.028 36.173 95.207 130 THR 39.510 37.020 96.381 131 ARG 40.686 33.400 96.170 132 PRO 43.175 32.307 93.472 133 PRO 41.224 31.670 90.291 134 THR 41.558 28.205 88.699 135 LEU 42.386 29.388 85.160 136 SER 42.134 27.708 81.747 137 PRO 45.509 27.079 80.023 138 ILE 46.344 29.722 77.456 139 PRO 45.960 28.027 74.023 140 HIS 49.143 27.013 72.174 141 ILE 50.369 29.499 69.501 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 H H H H 20 H H H H H H H C C C 30 C H H H H H H H H H 40 H H H H H H C T T T 50 T/T T T T H H H H H H 60 H H H H H H H H H H 70 H H S S S S/H H H H H 80 H H H H H 3 3 C S S 90 S S/H H H H H H/S S S S/T 100 T T T/S S S S S/H H H H 110 H H H H H/H H H H H H 120 H/H H H H H H 3 3 3 C 130 S S S S/S S S S S S S 140 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 H H H H 20 H H H H H h S S t T 30 h H H H H H H H H H 40 H H H H H H h G G G 50 g T T t h H H H H H 60 H H H H H H H H H H 70 h T t h H H H H 80 H H H H h T t T T t 90 t h H H H H h E E e 100 S S S e E E h H H H 110 H H H H h H H H H H 120 H H H H H h G G g S 130 S 140 Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 THR 0.0 0.0 94.1 2 SER 0.0 0.0 79.7 3 LEU 33.8 22.9 72.0 4 SER 32.4 38.7 67.2 5 LEU 51.1 34.5 67.5 6 PHE 50.0 30.0 62.9 7 TYR 131.5 72.6 49.1 8 LYS 69.4 40.0 74.4 9 LYS 54.0 31.1 76.2 10 VAL 92.8 78.2 37.2 11 TYR 146.4 80.9 40.7 12 ARG 140.9 67.4 59.4 13 LEU 71.5 48.4 70.1 14 ALA 71.9 99.1 34.3 15 TYR 157.7 87.1 42.8 16 LEU 61.3 41.5 73.5 17 ARG 162.8 77.9 49.5 18 LEU 147.8 100.0 30.6 19 ASN 84.2 69.7 65.8 20 THR 50.5 47.2 73.6 21 LEU 147.8 100.0 35.9 22 CYS 96.0 96.8 42.0 23 GLU 32.9 23.8 87.2 24 ARG 129.7 62.1 61.4 25 LEU 126.5 85.6 43.7 26 LEU 145.2 98.3 40.3 27 SER 30.7 36.7 87.4 28 GLU 39.9 28.8 75.4 29 HIS 98.5 65.6 51.8 30 PRO 38.9 31.2 86.5 31 GLU 42.1 30.4 63.8 32 LEU 146.7 99.3 30.3 33 GLU 115.1 83.1 50.4 34 HIS 95.2 63.4 56.7 35 ILE 136.4 95.0 34.1 36 ILE 143.5 100.0 31.3 37 TRP 203.5 99.3 32.6 38 THR 95.0 88.9 66.0 39 LEU 147.7 99.9 45.2 40 PHE 166.3 99.7 36.3 41 GLN 124.1 83.5 54.3 42 HIS 113.1 75.3 66.5 43 THR 106.7 99.9 36.5 44 LEU 143.9 97.4 28.7 45 GLN 62.9 42.3 86.2 46 ASN 60.4 49.9 72.6 47 GLU 92.2 66.5 59.2 48 TYR 63.2 34.9 82.5 49 GLU 64.4 46.4 77.2 50 LEU 147.8 100.0 46.9 51 MET 112.6 70.7 53.5 52 ARG 69.4 33.2 86.6 53 ASP 20.6 18.6 72.3 54 ARG 190.1 91.0 55.7 55 HIS 83.1 55.3 72.0 56 LEU 132.9 89.9 37.2 57 ASP 109.6 99.2 40.6 58 GLN 140.0 94.2 39.2 59 ILE 143.5 100.0 34.4 60 MET 158.9 99.7 33.6 61 MET 159.4 100.0 26.7 62 CYS 99.2 100.0 34.5 63 SER 83.6 100.0 45.7 64 MET 159.4 100.0 28.2 65 TYR 147.0 81.2 49.2 66 GLY 34.7 99.7 52.8 67 ILE 143.5 100.0 32.8 68 CYS 98.1 98.9 39.5 69 LYS 61.9 35.7 81.8 70 VAL 104.7 88.1 47.6 71 LYS 122.5 70.7 52.2 72 ASN 9.6 8.0 89.6 73 ILE 121.8 84.9 51.7 74 ASP 0.0 0.0 81.8 75 LEU 137.0 92.7 41.5 76 LYS 26.4 15.3 76.9 77 PHE 159.4 95.6 27.0 78 LYS 48.4 27.9 66.6 79 ILE 78.6 54.7 58.1 80 ILE 143.5 100.0 31.6 81 VAL 99.0 83.3 36.0 82 THR 43.8 41.0 69.2 83 ALA 65.8 90.6 51.9 84 TYR 180.1 99.5 35.2 85 LYS 99.8 57.6 68.0 86 ASP 25.0 22.6 86.3 87 LEU 142.6 96.5 42.4 88 PRO 14.3 11.5 78.5 89 HIS 92.2 61.4 66.2 90 ALA 72.4 99.7 57.8 91 VAL 33.8 28.5 85.1 92 GLN 57.9 39.0 58.1 93 GLU 43.0 31.0 66.3 94 THR 91.9 86.0 55.6 95 PHE 159.6 95.7 34.7 96 LYS 64.0 36.9 70.0 97 ARG 90.3 43.2 68.0 98 VAL 117.9 99.2 48.7 99 LEU 130.9 88.6 62.1 100 ILE 128.7 89.7 41.6 101 LYS 29.7 17.1 81.4 102 GLU 24.1 17.4 74.0 103 GLU 10.8 7.8 77.6 104 GLU 35.4 25.6 76.6 105 TYR 121.7 67.2 65.5 106 ASP 50.6 45.8 62.4 107 SER 46.7 55.9 64.0 108 ILE 140.5 97.9 29.8 109 ILE 63.1 44.0 66.3 110 VAL 69.2 58.3 68.6 111 PHE 166.8 100.0 35.1 112 TYR 168.7 93.2 35.9 113 ASN 52.7 43.6 60.4 114 SER 37.0 44.2 63.5 115 VAL 101.2 85.2 58.0 116 PHE 166.8 100.0 31.5 117 MET 118.0 74.0 60.4 118 GLN 66.0 44.4 73.3 119 ARG 113.1 54.2 65.0 120 LEU 146.9 99.4 39.1 121 LYS 81.5 47.0 64.1 122 THR 0.1 0.1 78.8 123 ASN 89.8 74.3 59.4 124 ILE 135.3 94.3 37.8 125 LEU 67.6 45.7 59.8 126 GLN 60.6 40.8 78.8 127 TYR 167.4 92.5 45.6 128 ALA 29.2 40.2 73.9 129 SER 63.8 76.3 78.5 130 THR 0.0 0.0 93.1 131 ARG 42.9 20.5 80.4 132 PRO 15.2 12.2 74.7 133 PRO 80.3 64.5 53.7 134 THR 0.0 0.0 89.9 135 LEU 120.2 81.4 55.3 136 SER 70.3 84.1 57.4 137 PRO 13.5 10.8 86.8 138 ILE 83.2 58.0 63.5 139 PRO 109.7 88.1 47.9 140 HIS 57.9 38.5 72.7 141 ILE 17.7 12.3 86.3