Protein Data Bank File : 1avob Title : PROTEASOME ACTIVATOR 18-SEP-97 1AVO Number of Amino Acid Residues : 140 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 ALA VAL ASN CYS ASN GLU LYS ILE VAL VAL 10 LEU LEU GLN ARG LEU LYS PRO GLU ILE LYS 20 ASP VAL ILE GLU GLN LEU ASN LEU VAL THR 30 THR TRP LEU GLN LEU GLN ILE PRO ARG ILE 40 GLU ASP GLY ASN ASN PHE GLY VAL ALA VAL 50 GLN GLU LYS VAL PHE GLU LEU MET THR SER 60 LEU HIS THR LYS LEU GLU GLY PHE HIS THR 70 GLN ILE SER LYS TYR PHE SER GLU ARG GLY 80 ASP ALA VAL THR LYS ALA ALA LYS GLN PRO 90 HIS VAL GLY ASP TYR ARG GLN LEU VAL HIS 100 GLU LEU ASP GLU ALA GLU TYR ARG ASP ILE 110 ARG LEU MET VAL MET GLU ILE ARG ASN ALA 120 TYR ALA VAL LEU TYR ASP ILE ILE LEU LYS 130 ASN PHE GLU LYS LEU LYS LYS PRO ARG GLY Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 ALA 0.0 151.3 178.7 2 VAL -97.8 117.6 -177.9 -171.7 3 ASN -92.1 168.8 178.6 -62.9 -28.9 4 CYS -71.1 166.1 -179.7 -55.6 5 ASN -87.0 104.3 -178.0 -174.9 -22.2 6 GLU -48.0 -52.5 -178.6 -61.1 174.7 4.6 7 LYS -55.3 -25.7 -179.7 -48.9 173.3 -158.4 72.5 8 ILE -88.4 -49.9 178.4 -77.3 -175.1 9 VAL -49.4 -39.1 179.2 172.3 10 VAL -71.1 -37.3 179.6 -37.6 11 LEU -64.2 -40.6 179.2 -70.8 176.9 12 LEU -62.5 -30.9 179.5 -73.7 179.7 13 GLN -64.9 -25.9 -179.1 -68.5 -38.2 -64.7 14 ARG -94.0 -26.1 -177.7 -57.4 171.7 66.2 177.0 15 LEU -78.1 -50.7 -178.5 173.7 58.2 16 LYS -42.9 -43.1 -180.0 -67.0 -172.1 -64.2 -164.1 17 PRO -68.5 -33.8 -179.4 -29.6 46.6 18 GLU -67.5 -34.4 179.3 -69.5 -48.4 -48.3 19 ILE -68.1 -49.0 178.4 -66.7 178.4 20 LYS -54.5 -40.4 179.6 178.7 -162.3 171.2 176.3 21 ASP -64.7 -45.3 -180.0 -68.7 -21.6 22 VAL -63.9 -50.9 -178.2 -116.3 23 ILE -54.7 -35.6 178.0 -51.2 -74.0 24 GLU -75.4 -41.8 179.5 -73.1 -170.6 12.7 25 GLN -65.0 -42.8 179.9 -50.4 -46.2 -35.9 26 LEU -59.5 -26.2 -179.6 -173.6 45.8 27 ASN -83.8 -32.0 178.3 -80.6 -9.5 28 LEU -65.4 -56.6 -178.9 -96.2 46.0 29 VAL -50.5 -48.1 178.8 167.9 30 THR -58.4 -47.5 178.7 -62.1 31 THR -60.1 -49.4 178.4 -52.5 32 TRP -49.2 -50.5 -179.7 170.1 76.2 33 LEU -59.8 -47.9 -179.2 -173.2 54.1 34 GLN -60.6 -39.6 -179.8 -40.1 -169.1 -126.8 35 LEU -63.6 -12.4 179.3 -67.2 -175.6 36 GLN -87.1 -12.2 -178.3 -100.3 13.2 -104.6 37 ILE -68.0 123.4 -178.9 -52.5 -167.7 38 PRO -78.4 167.3 178.6 38.5 -38.2 39 ARG -55.4 133.7 -177.6 -162.3 -160.9 -39.5 137.7 40 ILE -65.4 115.1 -178.2 -58.3 -171.7 41 GLU -125.5 163.8 -178.6 -70.8 -177.5 4.6 42 ASP -66.1 -42.6 178.7 -153.0 4.8 43 GLY -128.1 170.0 179.2 44 ASN 73.6 65.4 -178.6 -167.5 14.2 45 ASN -122.7 21.7 -179.3 -54.9 -52.8 46 PHE -64.7 -52.1 -179.8 177.9 57.4 47 GLY -56.9 -38.5 178.5 48 VAL -61.9 -40.2 177.4 168.3 49 ALA -62.9 -37.6 178.4 50 VAL -66.8 -40.7 -179.8 167.1 51 GLN -65.7 -35.5 179.7 -57.9 179.0 -25.5 52 GLU -66.6 -33.9 -179.9 -60.6 -179.6 -23.4 53 LYS -73.5 -36.8 178.6 173.7 92.6 -160.6 164.0 54 VAL -68.8 -42.2 178.7 174.7 55 PHE -56.1 -42.2 178.7 -146.8 82.9 56 GLU -55.8 -40.3 -178.2 -80.6 176.1 27.1 57 LEU -66.7 -49.9 179.4 166.4 97.6 58 MET -51.4 -43.1 178.0 -69.3 -179.3 -178.0 59 THR -60.5 -35.2 179.1 -69.6 60 SER -75.1 -46.2 178.1 -28.6 61 LEU -51.2 -46.3 -177.5 -69.2 -171.8 62 HIS -61.4 -51.7 -179.7 -169.5 -93.3 63 THR -49.1 -48.1 179.8 -74.9 64 LYS -61.1 -50.6 -177.5 175.8 -177.8 -63.6 -160.9 65 LEU -71.5 -29.0 -179.1 -58.5 178.0 66 GLU -61.9 -31.6 179.1 -158.8 170.4 29.5 67 GLY -64.6 -43.9 -179.9 68 PHE -44.4 -49.7 179.3 -65.3 3.8 69 HIS -35.4 -65.3 -175.2 -119.8 141.5 70 THR -71.4 -27.6 -180.0 75.0 71 GLN -60.1 -16.3 -177.9 -63.2 174.7 24.0 72 ILE -78.6 -42.4 179.3 -69.3 163.8 73 SER -69.1 -37.7 -179.3 -55.5 74 LYS -58.3 -36.1 179.6 -174.2 -177.6 178.0 166.9 75 TYR -57.9 -54.9 -179.3 165.9 60.0 76 PHE -64.5 -27.0 -179.9 -64.7 -65.8 77 SER -78.7 -43.8 -179.4 178.0 78 GLU -65.3 -40.5 179.9 -83.4 -171.8 -56.5 79 ARG -67.6 -49.4 -179.9 -148.0 -166.4 176.5 -113.8 80 GLY -48.5 -47.2 179.8 81 ASP -65.3 -39.5 -179.9 -61.5 -1.4 82 ALA -64.4 -46.3 -179.3 83 VAL -58.6 -43.9 178.0 177.2 84 THR -57.5 -52.3 178.4 -71.6 85 LYS -63.0 -42.4 179.8 -67.1 -170.6 -148.1 146.6 86 ALA -52.5 -48.3 179.8 87 ALA -63.4 -50.9 178.5 88 LYS -66.9 -21.7 -179.0 -67.7 -177.7 175.0 173.6 89 GLN -131.3 67.6 -179.8 -43.7 -69.7 -14.9 90 PRO -61.6 -12.9 178.4 29.4 -42.0 91 HIS -83.0 -19.6 -177.6 49.8 115.7 92 VAL -91.7 108.8 -177.3 -167.5 93 GLY -77.6 -18.4 -179.7 94 ASP -66.2 -25.8 178.9 -57.0 87.8 95 TYR -74.0 -31.0 179.1 -70.6 -34.4 96 ARG -76.0 -36.1 179.4 -72.0 150.0 -157.5 -98.9 97 GLN -67.4 -38.7 180.0 -107.5 -68.8 110.7 98 LEU -57.9 -50.3 179.3 -179.4 49.8 99 VAL -51.9 -38.6 -179.5 173.1 100 HIS -78.4 -21.9 178.9 -58.0 116.0 101 GLU -76.0 -34.3 178.7 -66.4 -65.1 -35.6 102 LEU -65.2 -41.4 -179.3 -62.6 170.2 103 ASP -65.9 -44.2 -179.5 -69.9 -12.3 104 GLU -61.6 -42.4 -179.9 -89.1 -173.6 25.3 105 ALA -67.4 -42.1 -178.6 106 GLU -63.1 -31.2 -179.8 -170.4 64.5 8.0 107 TYR -70.4 -42.3 179.9 174.6 87.1 108 ARG -64.5 -27.1 180.0 -68.1 -165.4 -133.6 -98.9 109 ASP -77.5 -46.3 178.1 -73.6 -20.4 110 ILE -51.9 -44.7 180.0 -60.3 178.9 111 ARG -61.6 -45.9 178.2 -178.5 167.4 -139.0 -80.6 112 LEU -64.4 -36.2 179.5 -91.1 174.9 113 MET -69.0 -37.2 -179.2 -59.4 -167.4 -103.9 114 VAL -69.7 -35.4 -178.7 174.1 115 MET -68.8 -45.3 179.4 -168.6 174.1 -106.5 116 GLU -71.8 -16.6 178.1 -84.2 -178.6 -6.9 117 ILE -81.9 -43.9 -179.3 -71.3 -179.3 118 ARG -56.9 -48.3 -179.2 172.1 -166.6 68.1 -162.2 119 ASN -59.3 -28.0 -180.0 -66.3 -13.0 120 ALA -75.0 -40.7 -179.5 121 TYR -62.0 -44.3 -178.5 -77.0 -64.8 122 ALA -61.8 -56.1 -178.7 123 VAL -60.0 -34.2 -179.7 173.6 124 LEU -71.2 -51.5 179.5 -113.0 -169.7 125 TYR -53.1 -54.6 -179.5 171.9 85.8 126 ASP -50.7 -53.8 179.8 -179.1 72.1 127 ILE -67.6 -37.0 178.4 -164.4 163.3 128 ILE -67.4 -41.2 -179.6 -59.7 -90.8 129 LEU -61.6 -54.0 -178.8 -95.8 -73.6 130 LYS -53.5 -38.4 -177.8 -66.8 -177.9 170.0 143.9 131 ASN -111.1 27.3 -177.9 -50.3 -85.1 132 PHE -60.0 -42.9 -179.4 -157.9 70.6 133 GLU -47.3 -59.1 179.4 -129.3 -179.8 14.6 134 LYS -72.8 -28.5 177.6 -60.0 -92.6 179.3 -80.5 135 LEU -67.5 -41.1 -178.8 -62.5 -178.0 136 LYS -82.1 -37.1 -178.1 -161.9 147.6 -150.3 160.6 137 LYS -132.3 74.6 -179.1 -62.8 169.8 164.5 -170.5 138 PRO -57.2 -18.1 -178.7 27.4 -40.9 139 ARG -120.5 -15.9 179.7 -74.1 172.8 175.7 150.0 140 GLY 128.3 176.1 0.0 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 ALA 146.519 51.073 31.372 2 VAL 143.395 52.594 32.942 3 ASN 143.075 51.599 36.533 4 CYS 140.132 51.313 38.968 5 ASN 139.403 54.194 41.272 6 GLU 141.528 53.463 44.314 7 LYS 139.788 55.579 46.939 8 ILE 136.678 53.608 46.140 9 VAL 138.180 50.151 45.824 10 VAL 139.495 50.507 49.370 11 LEU 136.135 51.727 50.636 12 LEU 134.527 48.681 48.993 13 GLN 137.111 46.689 50.836 14 ARG 135.706 47.811 54.198 15 LEU 132.123 47.652 53.153 16 LYS 131.859 44.224 51.681 17 PRO 132.529 42.509 55.002 18 GLU 129.983 44.645 56.748 19 ILE 127.370 43.579 54.204 20 LYS 128.250 39.916 54.629 21 ASP 127.813 40.372 58.394 22 VAL 124.293 41.850 58.326 23 ILE 122.969 39.343 55.871 24 GLU 124.204 36.538 58.099 25 GLN 122.972 37.905 61.401 26 LEU 119.781 38.779 59.782 27 ASN 119.457 35.160 58.736 28 LEU 120.145 33.827 62.153 29 VAL 117.636 36.124 63.835 30 THR 115.001 35.244 61.286 31 THR 115.507 31.496 61.794 32 TRP 115.471 31.959 65.537 33 LEU 112.196 33.770 65.118 34 GLN 110.603 31.250 62.840 35 LEU 111.580 28.469 65.228 36 GLN 109.640 30.430 67.864 37 ILE 106.380 30.098 65.997 38 PRO 103.940 27.955 68.013 39 ARG 101.575 25.183 67.021 40 ILE 98.769 26.585 64.969 41 GLU 95.907 26.744 67.361 42 ASP 92.402 28.129 67.272 43 GLY 92.592 30.922 69.831 44 ASN 95.235 33.030 71.556 45 ASN 97.180 34.349 68.596 46 PHE 98.094 37.831 69.574 47 GLY 101.647 36.813 70.239 48 VAL 101.558 34.952 66.992 49 ALA 100.415 38.204 65.392 50 VAL 103.333 40.005 67.027 51 GLN 105.828 37.507 65.641 52 GLU 104.331 37.988 62.195 53 LYS 104.784 41.750 62.276 54 VAL 108.445 41.597 63.363 55 PHE 108.947 39.025 60.753 56 GLU 107.656 41.380 58.150 57 LEU 110.373 43.771 59.100 58 MET 113.190 41.262 59.030 59 THR 111.999 40.324 55.613 60 SER 112.220 43.874 54.205 61 LEU 115.592 44.386 55.745 62 HIS 116.703 41.268 53.979 63 THR 115.253 42.283 50.667 64 LYS 116.912 45.676 50.953 65 LEU 120.298 44.349 52.010 66 GLU 120.478 41.496 49.573 67 GLY 120.804 43.998 46.728 68 PHE 123.899 45.752 48.132 69 HIS 125.831 42.553 47.634 70 THR 125.505 42.667 43.822 71 GLN 125.597 46.435 43.258 72 ILE 129.350 46.177 43.779 73 SER 130.154 43.913 40.854 74 LYS 127.897 45.993 38.679 75 TYR 130.105 48.972 39.428 76 PHE 133.211 47.344 37.984 77 SER 131.260 46.020 35.122 78 GLU 129.576 49.264 34.300 79 ARG 132.814 51.129 34.747 80 GLY 134.893 48.624 32.781 81 ASP 132.513 49.120 29.923 82 ALA 132.525 52.911 30.138 83 VAL 136.324 53.114 30.063 84 THR 136.343 50.790 27.082 85 LYS 133.869 52.914 25.072 86 ALA 135.629 56.087 26.227 87 ALA 138.773 54.546 24.802 88 LYS 137.211 53.283 21.566 89 GLN 135.463 56.618 21.014 90 PRO 138.000 59.182 22.314 91 HIS 136.078 61.867 20.483 92 VAL 132.998 61.283 22.642 93 GLY 133.523 63.211 25.803 94 ASP 130.381 61.921 27.464 95 TYR 132.088 58.594 27.987 96 ARG 134.880 60.150 29.986 97 GLN 132.345 62.048 31.992 98 LEU 130.303 58.881 32.488 99 VAL 133.295 57.154 33.988 100 HIS 133.616 59.930 36.548 101 GLU 129.957 59.959 37.213 102 LEU 130.025 56.239 38.062 103 ASP 132.783 56.744 40.617 104 GLU 131.001 59.631 42.257 105 ALA 127.859 57.618 42.412 106 GLU 129.557 54.534 43.751 107 TYR 130.993 56.767 46.381 108 ARG 127.593 58.219 47.231 109 ASP 126.193 54.688 47.487 110 ILE 128.816 53.254 49.763 111 ARG 127.967 55.997 52.242 112 LEU 124.307 55.165 51.846 113 MET 124.905 51.420 52.167 114 VAL 126.876 51.906 55.398 115 MET 124.105 54.179 56.540 116 GLU 121.387 51.691 55.701 117 ILE 123.248 48.833 57.388 118 ARG 123.736 50.679 60.675 119 ASN 120.079 51.492 60.541 120 ALA 119.214 47.800 60.136 121 TYR 121.086 46.797 63.217 122 ALA 119.389 49.623 65.135 123 VAL 115.882 49.049 63.996 124 LEU 116.225 45.265 64.530 125 TYR 117.704 45.500 67.926 126 ASP 114.995 47.959 68.865 127 ILE 112.067 45.892 67.643 128 ILE 113.290 42.542 68.958 129 LEU 113.843 44.197 72.298 130 LYS 110.465 45.876 72.659 131 ASN 108.534 42.697 71.845 132 PHE 110.779 40.062 73.244 133 GLU 108.186 38.719 75.686 134 LYS 105.814 37.735 72.897 135 LEU 108.472 36.868 70.371 136 LYS 109.888 34.350 72.846 137 LYS 106.654 33.317 74.578 138 PRO 103.737 34.099 72.287 139 ARG 101.312 32.385 74.580 140 GLY 102.737 32.669 78.077 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S S S S/H H H H H H 10 H H H H H H/H H H H H 20 H H H H H H H H H H 30 H H H H H H H C S S 40 S S C C H H H H H H 50 H H H H H H H H H H 60 H H H H H H H H H H 70 H H H H H H H H H H 80 H H H H H H H H H H 90 C H H H H 3 3/H H H H 100 H H H H H H H H H H 110 H H H H H H H H H H 120 H H H H H H H H H H 130 H H/H H H H 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 10 H H H H H H H H H H 20 H H H H H H H H H H 30 H H H H H h t 40 S S h H H H H H 50 H H H H H H H H H H 60 H H H H H H H H H H 70 H H H H H H H H H H 80 H H H H H H H H h T 90 T t h H H H H H H H 100 H H H H H H H H H H 110 H H H H H H H H H H 120 H H H H H H H H H H 130 h H H H H H h S Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 ALA 0.1 0.2 91.5 2 VAL 39.6 33.4 71.4 3 ASN 21.4 17.7 84.3 4 CYS 39.9 40.2 63.6 5 ASN 85.8 71.0 66.5 6 GLU 16.3 11.8 81.7 7 LYS 9.8 5.7 83.3 8 ILE 138.2 96.3 39.9 9 VAL 77.6 65.3 50.9 10 VAL 37.3 31.4 63.8 11 LEU 101.6 68.7 50.8 12 LEU 147.7 99.9 34.9 13 GLN 68.8 46.3 66.9 14 ARG 30.7 14.7 82.5 15 LEU 145.0 98.1 27.9 16 LYS 96.9 55.9 59.4 17 PRO 61.8 49.6 74.1 18 GLU 58.4 42.2 70.3 19 ILE 141.4 98.5 36.3 20 LYS 52.0 30.0 81.4 21 ASP 54.3 49.1 77.1 22 VAL 114.2 96.1 38.0 23 ILE 127.7 89.0 52.4 24 GLU 56.0 40.4 70.6 25 GLN 72.4 48.7 63.6 26 LEU 145.3 98.3 36.8 27 ASN 51.2 42.4 69.3 28 LEU 33.0 22.3 82.2 29 VAL 76.2 64.1 44.4 30 THR 80.9 75.7 51.2 31 THR 38.5 36.1 70.9 32 TRP 137.0 66.8 49.8 33 LEU 147.8 100.0 31.9 34 GLN 66.6 44.8 58.4 35 LEU 33.0 22.3 79.5 36 GLN 112.8 75.9 61.8 37 ILE 81.0 56.4 65.5 38 PRO 99.6 80.0 60.2 39 ARG 30.8 14.7 87.0 40 ILE 0.0 0.0 89.3 41 GLU 83.5 60.2 78.6 42 ASP 0.0 0.0 90.2 43 GLY 3.0 8.7 82.2 44 ASN 39.6 32.8 78.1 45 ASN 70.7 58.4 77.4 46 PHE 32.7 19.6 70.2 47 GLY 34.8 100.0 49.3 48 VAL 95.1 80.0 57.4 49 ALA 31.3 43.1 70.4 50 VAL 98.3 82.7 44.9 51 GLN 148.0 99.6 39.8 52 GLU 38.0 27.4 71.8 53 LYS 40.7 23.4 84.0 54 VAL 116.9 98.4 33.1 55 PHE 121.5 72.8 56.5 56 GLU 39.0 28.1 78.3 57 LEU 106.8 72.3 47.8 58 MET 159.2 99.9 31.7 59 THR 35.1 32.9 70.3 60 SER 28.3 33.9 71.5 61 LEU 135.7 91.8 35.2 62 HIS 103.0 68.6 62.6 63 THR 20.1 18.8 80.0 64 LYS 79.5 45.8 67.0 65 LEU 147.7 99.9 29.3 66 GLU 51.3 37.0 77.6 67 GLY 9.0 25.8 80.9 68 PHE 156.8 94.0 45.5 69 HIS 65.3 43.5 58.8 70 THR 17.2 16.1 81.2 71 GLN 77.5 52.1 62.6 72 ILE 131.9 91.9 44.5 73 SER 9.4 11.3 77.2 74 LYS 45.8 26.4 78.0 75 TYR 175.1 96.8 44.4 76 PHE 104.9 62.9 50.2 77 SER 21.1 25.2 81.5 78 GLU 63.9 46.1 59.7 79 ARG 183.1 87.6 48.4 80 GLY 2.4 7.0 75.7 81 ASP 30.6 27.7 78.6 82 ALA 71.3 98.2 47.9 83 VAL 92.9 78.2 46.2 84 THR 43.4 40.6 66.7 85 LYS 79.7 46.0 60.5 86 ALA 63.4 87.3 56.0 87 ALA 20.1 27.7 75.1 88 LYS 40.4 23.3 75.8 89 GLN 78.0 52.5 59.4 90 PRO 58.6 47.1 82.7 91 HIS 29.3 19.5 76.5 92 VAL 75.8 63.8 64.7 93 GLY 6.0 17.2 77.7 94 ASP 8.0 7.2 74.4 95 TYR 125.2 69.2 53.2 96 ARG 86.3 41.3 70.8 97 GLN 46.7 31.4 79.7 98 LEU 79.5 53.8 57.7 99 VAL 108.6 91.4 51.8 100 HIS 48.8 32.5 78.7 101 GLU 62.0 44.7 76.7 102 LEU 120.8 81.7 51.0 103 ASP 101.5 91.9 58.5 104 GLU 54.5 39.4 82.9 105 ALA 25.4 35.0 76.7 106 GLU 128.0 92.4 39.3 107 TYR 69.6 38.5 60.7 108 ARG 53.1 25.4 79.1 109 ASP 61.1 55.3 65.2 110 ILE 134.7 93.9 35.3 111 ARG 57.2 27.4 73.8 112 LEU 55.9 37.8 72.8 113 MET 154.2 96.8 41.2 114 VAL 41.9 35.3 62.9 115 MET 87.5 54.9 75.9 116 GLU 81.0 58.5 60.4 117 ILE 135.7 94.6 35.4 118 ARG 61.7 29.5 75.2 119 ASN 63.7 52.7 66.1 120 ALA 70.1 96.5 43.7 121 TYR 99.5 55.0 60.6 122 ALA 19.5 26.8 70.9 123 VAL 50.0 42.1 60.9 124 LEU 129.7 87.8 34.9 125 TYR 32.0 17.7 73.2 126 ASP 53.0 48.0 66.2 127 ILE 109.9 76.6 50.6 128 ILE 121.8 84.9 31.5 129 LEU 62.7 42.4 64.8 130 LYS 44.6 25.7 87.7 131 ASN 74.4 61.6 53.1 132 PHE 90.0 54.0 60.2 133 GLU 8.8 6.3 82.0 134 LYS 106.6 61.5 62.8 135 LEU 147.8 100.0 35.8 136 LYS 79.6 45.9 64.3 137 LYS 48.0 27.7 77.7 138 PRO 114.2 91.7 54.1 139 ARG 169.9 81.3 69.0 140 GLY 3.0 8.5 80.5