Protein Data Bank File : 1qgva Title : TRANSCRIPTION 06-MAY-99 1QGV Number of Amino Acid Residues : 131 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 SER TYR MET LEU PRO HIS LEU HIS ASN GLY 10 TRP GLN VAL ASP GLN ALA ILE LEU SER GLU 20 GLU ASP ARG VAL VAL VAL ILE ARG PHE GLY 30 HIS ASP TRP ASP PRO THR CYS MET LYS MET 40 ASP GLU VAL LEU TYR SER ILE ALA GLU LYS 50 VAL LYS ASN PHE ALA VAL ILE TYR LEU VAL 60 ASP ILE THR GLU VAL PRO ASP PHE ASN LYS 70 MET TYR GLU LEU TYR ASP PRO CYS THR VAL 80 MET PHE PHE PHE ARG ASN LYS HIS ILE MET 90 ILE ASP LEU GLY ILE ASN TRP ALA MET GLU 100 ASP LYS GLN GLU MET VAL ASP ILE ILE GLU 110 THR VAL TYR ARG GLY ALA ARG LYS GLY ARG 120 GLY LEU VAL VAL SER PRO LYS ASP TYR SER 130 THR Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 SER 0.0 2.2 178.5 0.0 2 TYR 178.9 137.3 -178.9 0.0 0.0 3 MET -53.1 -43.4 -178.8 -164.8 76.2 91.0 4 LEU -127.1 89.7 -179.5 -84.2 18.9 5 PRO -67.5 149.5 176.3 -11.3 26.9 6 HIS -89.8 138.5 177.7 -93.1 -95.5 7 LEU -102.9 120.6 -173.8 -64.5 179.6 8 HIS -89.1 -6.8 177.5 -60.6 -68.3 9 ASN -160.2 176.0 -179.7 50.5 51.6 10 GLY -60.3 -38.9 -179.5 11 TRP -60.6 -44.0 179.0 -173.8 77.1 12 GLN -63.3 -38.8 178.5 -82.0 176.1 25.6 13 VAL -64.5 -48.3 179.5 174.0 14 ASP -57.6 -42.4 -179.2 -170.3 64.7 15 GLN -68.3 -32.9 -179.6 -67.6 -67.6 -64.2 16 ALA -64.6 -38.9 -179.5 17 ILE -73.3 -46.1 179.4 -63.0 172.5 18 LEU -69.2 -25.9 -178.3 -50.2 165.9 19 SER -73.9 -14.6 -180.0 81.7 20 GLU -104.3 119.1 179.5 -66.8 -67.5 -26.6 21 GLU -94.4 -28.9 -176.2 -83.6 112.8 33.9 22 ASP -121.6 4.6 -179.1 -59.6 -49.7 23 ARG -129.0 151.5 176.1 -64.5 -170.7 -64.3 174.6 24 VAL -74.8 141.5 178.3 -62.7 25 VAL -102.0 116.1 -177.8 175.9 26 VAL -100.8 120.5 -178.4 179.5 27 ILE -125.2 122.9 178.0 -58.1 -176.4 28 ARG -89.7 122.1 178.9 173.8 -82.2 -95.4 167.3 29 PHE -113.4 125.6 178.8 -77.0 97.5 30 GLY 174.8 -168.4 178.2 31 HIS -97.5 126.1 -177.5 -67.3 -67.5 32 ASP -53.3 -33.2 -178.5 -65.7 -24.7 33 TRP -82.1 -15.8 -176.4 61.5 -92.2 34 ASP -62.1 137.0 -179.4 -177.8 -77.4 35 PRO -57.7 -31.8 -179.9 20.3 -31.9 36 THR -72.2 -38.6 177.0 -58.7 37 CYS -66.4 -36.1 179.2 -72.4 38 MET -60.5 -46.2 179.8 -67.9 -174.9 171.8 39 LYS -66.7 -41.4 179.2 -60.6 178.5 156.1 -152.6 40 MET -65.4 -43.3 -178.9 178.8 70.9 6.4 41 ASP -63.5 -38.2 -179.7 -67.9 -4.4 42 GLU -61.6 -46.6 179.3 178.3 173.3 162.0 43 VAL -65.3 -48.7 -179.7 163.7 44 LEU -57.8 -42.9 -179.0 -70.8 168.8 45 TYR -65.0 -38.5 -179.2 172.6 96.8 46 SER -68.9 -17.5 178.8 70.2 47 ILE -117.1 2.0 -178.2 56.5 96.1 48 ALA -55.7 -44.0 179.9 49 GLU -66.5 -46.1 -178.7 -57.9 -102.6 35.9 50 LYS -52.2 -41.5 -177.5 -171.1 153.3 -170.3 -103.9 51 VAL -95.7 2.6 -177.0 -55.9 52 LYS -47.9 -35.7 -179.0 -155.9 166.9 -89.4 -177.5 53 ASN -65.2 -25.0 -175.4 -68.8 -20.8 54 PHE -133.7 3.1 -179.7 55.1 92.8 55 ALA -152.5 146.7 176.7 56 VAL -129.5 136.6 -176.5 62.6 57 ILE -113.2 137.6 179.2 -51.3 156.8 58 TYR -134.4 155.4 179.5 -64.1 105.0 59 LEU -116.3 138.8 180.0 -50.4 177.5 60 VAL -134.7 128.8 176.8 169.2 61 ASP -90.4 122.4 -176.1 179.3 92.1 62 ILE -75.2 -8.5 176.1 55.3 -175.8 63 THR -78.4 -45.6 -179.4 -77.5 64 GLU -73.8 -39.2 -179.7 156.7 176.6 -114.9 65 VAL -121.5 83.3 179.5 -177.7 66 PRO -80.0 -11.9 -179.5 25.0 -24.1 67 ASP -39.8 -53.6 -176.3 -47.1 -138.1 68 PHE -90.0 15.1 -178.0 -35.2 75.8 69 ASN -60.2 -1.4 178.5 -78.5 -6.5 70 LYS -97.7 -8.3 -179.3 -99.0 168.6 175.8 -102.6 71 MET -82.9 -21.3 179.1 -110.1 157.9 5.8 72 TYR -138.3 -5.0 -179.5 35.6 83.3 73 GLU 67.3 39.5 -177.3 0.0 0.0 0.0 74 LEU 50.6 40.2 180.0 172.4 129.1 75 TYR -19.8 -63.1 179.8 0.0 0.0 76 ASP 129.9 -74.7 179.5 0.0 0.0 77 PRO -52.6 166.4 179.3 -21.4 26.5 78 CYS -74.4 124.3 -179.6 -144.9 79 THR -119.5 147.1 178.5 76.6 80 VAL -112.4 131.9 179.9 176.4 81 MET -118.9 150.0 -175.5 -71.2 -157.6 -43.0 82 PHE -121.2 134.6 178.5 -57.4 91.0 83 PHE -131.1 139.4 176.5 -55.2 86.6 84 PHE -138.7 124.0 -178.0 -172.5 -100.8 85 ARG 48.8 49.6 177.0 -69.5 -178.7 -177.6 149.5 86 ASN 70.2 7.6 179.0 -58.4 -36.2 87 LYS -109.2 135.7 177.8 -173.3 158.3 115.0 176.1 88 HIS -76.4 124.5 -178.7 168.1 55.7 89 ILE -101.2 124.1 -179.9 -49.9 -59.8 90 MET -88.4 147.3 -179.8 -64.3 171.8 -58.0 91 ILE -127.6 130.8 178.0 -42.3 -179.6 92 ASP -110.0 121.2 180.0 -164.4 -24.0 93 LEU -93.1 -6.4 179.8 -60.6 178.1 94 GLY 78.2 1.0 -105.1 95 ILE -129.5 78.0 -177.7 -37.8 -83.9 96 ASN -122.0 30.0 178.8 61.1 2.9 97 TRP -131.9 139.3 178.4 82.0 91.9 98 ALA -72.4 132.5 179.4 99 MET -108.5 140.6 179.4 32.3 -156.1 85.6 100 GLU -62.2 -59.3 -178.3 -21.9 -132.1 -56.3 101 ASP -70.3 124.0 178.5 -50.1 -102.4 102 LYS -72.5 -19.4 -180.0 59.2 -153.4 -142.4 50.0 103 GLN -68.5 -29.6 178.3 -176.6 58.0 37.5 104 GLU -65.1 -37.5 179.2 -175.6 179.0 2.2 105 MET -70.2 -38.9 177.5 -173.0 51.8 81.7 106 VAL -60.3 -44.0 179.7 172.1 107 ASP -57.6 -49.5 179.4 -77.5 16.9 108 ILE -63.9 -43.7 -178.9 -64.8 163.2 109 ILE -63.8 -44.0 179.0 -68.0 172.3 110 GLU -64.0 -41.1 178.8 175.2 -175.8 -29.6 111 THR -62.2 -47.3 178.9 -69.3 112 VAL -61.0 -46.8 179.6 171.6 113 TYR -60.3 -48.6 -176.3 167.8 73.1 114 ARG -67.1 -30.5 178.1 -65.4 174.8 72.6 168.4 115 GLY -78.6 -45.6 -178.8 116 ALA -63.2 -36.9 -177.9 117 ARG -71.0 -16.8 178.3 76.2 161.3 168.7 -165.9 118 LYS -98.1 6.8 177.7 62.7 171.8 76.6 173.8 119 GLY 109.0 0.2 -179.1 120 ARG -77.0 137.8 176.2 -54.7 -162.0 166.3 -81.5 121 GLY -101.4 -12.3 178.5 122 LEU -130.3 128.1 177.7 161.6 74.1 123 VAL -124.2 148.5 179.4 70.2 124 VAL -114.0 141.5 176.7 -172.1 125 SER -134.8 90.0 -179.7 -169.0 126 PRO -52.7 90.6 180.0 16.7 -31.7 127 LYS -113.0 33.5 179.4 -57.4 -171.8 131.2 11.7 128 ASP -108.3 60.9 179.5 177.3 41.3 129 TYR -68.9 143.9 178.5 -18.5 103.1 130 SER 144.7 -32.2 0.0 91.7 131 THR 0.0 0.0 0.0 0.0 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 SER -26.605 9.777 12.427 2 TYR -26.126 12.183 9.444 3 MET -24.354 11.396 6.201 4 LEU -21.690 14.061 6.863 5 PRO -21.552 14.757 10.600 6 HIS -20.349 18.125 11.898 7 LEU -17.401 18.045 14.360 8 HIS -18.072 20.735 16.923 9 ASN -14.706 21.382 18.628 10 GLY -11.036 20.497 18.470 11 TRP -11.502 17.414 20.620 12 GLN -14.112 15.955 18.224 13 VAL -11.887 16.582 15.174 14 ASP -8.986 14.905 16.947 15 GLN -11.152 11.958 17.879 16 ALA -12.480 11.617 14.309 17 ILE -8.920 11.334 13.083 18 LEU -7.697 8.993 15.812 19 SER -10.797 6.826 15.443 20 GLU -10.126 5.520 11.897 21 GLU -7.509 2.839 11.492 22 ASP -8.286 1.799 7.883 23 ARG -10.045 4.671 6.075 24 VAL -8.958 8.147 5.045 25 VAL -10.646 10.801 7.147 26 VAL -11.855 13.541 4.828 27 ILE -12.553 16.831 6.591 28 ARG -14.116 19.920 5.035 29 PHE -12.955 23.066 6.832 30 GLY -14.778 26.304 6.030 31 HIS -17.742 28.521 6.831 32 ASP -21.034 26.671 6.570 33 TRP -22.769 29.593 4.822 34 ASP -20.023 30.155 2.231 35 PRO -21.038 29.418 -1.377 36 THR -17.967 27.260 -1.900 37 CYS -18.769 25.152 1.162 38 MET -22.359 24.655 -0.083 39 LYS -21.063 23.263 -3.362 40 MET -18.387 21.198 -1.622 41 ASP -20.890 19.757 0.879 42 GLU -23.304 18.845 -1.921 43 VAL -20.653 16.844 -3.763 44 LEU -19.346 15.183 -0.600 45 TYR -22.824 14.141 0.468 46 SER -23.524 12.696 -2.993 47 ILE -20.398 10.417 -2.888 48 ALA -20.266 9.568 0.845 49 GLU -21.828 6.134 0.346 50 LYS -19.712 5.371 -2.701 51 VAL -16.410 5.897 -0.851 52 LYS -17.528 4.369 2.442 53 ASN -15.252 1.286 2.281 54 PHE -12.151 3.484 2.366 55 ALA -13.129 6.998 3.437 56 VAL -15.250 8.751 6.003 57 ILE -16.283 12.447 5.654 58 TYR -16.816 15.157 8.283 59 LEU -17.639 18.885 8.219 60 VAL -16.066 21.535 10.413 61 ASP -17.093 25.164 10.677 62 ILE -13.921 27.196 11.224 63 THR -15.714 29.959 13.111 64 GLU -16.899 27.407 15.641 65 VAL -13.741 25.301 15.495 66 PRO -10.750 27.650 14.994 67 ASP -8.164 25.218 16.421 68 PHE -6.658 23.939 13.142 69 ASN -6.731 27.323 11.347 70 LYS -2.925 27.151 10.977 71 MET -3.185 24.058 8.742 72 TYR -4.744 25.939 5.805 73 GLU -4.435 29.290 7.557 74 LEU -8.207 29.680 7.691 75 TYR -7.493 29.533 3.981 76 ASP -10.951 30.971 3.506 77 PRO -12.430 29.197 0.478 78 CYS -13.907 25.904 1.395 79 THR -11.035 23.415 1.751 80 VAL -10.904 19.648 2.178 81 MET -8.069 18.063 4.177 82 PHE -7.051 14.416 4.324 83 PHE -5.763 12.216 7.160 84 PHE -4.753 8.566 7.169 85 ARG -3.682 6.646 10.274 86 ASN -3.224 9.972 12.076 87 LYS -1.039 11.471 9.403 88 HIS -2.000 14.551 7.412 89 ILE -1.709 13.560 3.740 90 MET -0.521 16.210 1.282 91 ILE -1.715 16.400 -2.352 92 ASP 0.048 18.015 -5.249 93 LEU -2.327 18.848 -8.086 94 GLY 0.391 20.155 -10.373 95 ILE -8.676 21.057 -2.656 96 ASN -10.453 24.422 -2.189 97 TRP -12.699 24.655 -5.243 98 ALA -16.190 23.352 -5.853 99 MET -16.017 20.779 -8.664 100 GLU -18.955 20.071 -10.923 101 ASP -18.378 16.296 -11.128 102 LYS -18.809 14.281 -8.029 103 GLN -16.679 11.662 -9.788 104 GLU -13.751 14.040 -9.622 105 MET -14.151 14.098 -5.797 106 VAL -14.383 10.272 -5.688 107 ASP -11.126 10.231 -7.729 108 ILE -9.199 12.479 -5.418 109 ILE -10.369 10.624 -2.285 110 GLU -9.549 7.204 -3.802 111 THR -6.177 8.558 -4.970 112 VAL -5.380 9.872 -1.478 113 TYR -6.449 6.577 0.128 114 ARG -4.556 4.254 -2.251 115 GLY -1.404 6.317 -1.948 116 ALA -1.611 6.807 1.833 117 ARG -2.222 3.135 2.607 118 LYS 1.019 2.133 0.922 119 GLY 2.953 4.711 2.978 120 ARG 2.832 7.987 1.039 121 GLY 2.626 11.266 2.915 122 LEU 2.406 13.045 -0.461 123 VAL 0.096 11.982 -3.257 124 VAL -0.253 13.510 -6.693 125 SER -3.381 14.158 -8.729 126 PRO -2.332 15.735 -12.112 127 LYS -5.018 18.343 -12.618 128 ASP -2.812 20.508 -14.796 129 TYR -4.499 19.787 -18.140 130 SER -3.215 21.792 -21.145 131 THR 0.000 0.000 0.000 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C C S S S S S S S/H H 10 H H H H H H H H H 3 20 C S S S S S S S S S 30 S C C H H H H H H H 40 H H H H H H H H/T T T 50 T/T T T T/S S S S S S S 60 S/T T T T C C C T T T 70 T C C C C C S S S S 80 S S S/T T T T/S S S S S 90 S S S S/X X/C S S S S S 100 H H H H H H H H H H 110 H H H H H H H H H C 120 S S S S S S S/S S S X/P 130 S/X Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S B h H 10 H H H H H H H H h t 20 S S S E E E E E E E 30 t T T h H H H H H H 40 H H H H H H H H H H 50 H h T e E E E E E E 60 E e T T t t T T T T 70 t S S S S E E 80 E E E E T T E E E E 90 E E S S 100 h H H H H H H H H H 110 H H H H H H h T T t 120 e E E E e 130 Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 SER 0.0 0.0 93.8 2 TYR 129.7 71.7 78.2 3 MET 111.8 70.2 59.9 4 LEU 139.8 94.6 37.6 5 PRO 78.7 63.2 68.1 6 HIS 101.0 67.2 71.1 7 LEU 132.7 89.8 43.4 8 HIS 67.1 44.7 77.5 9 ASN 53.1 44.0 66.7 10 GLY 29.4 84.5 56.5 11 TRP 42.8 20.9 80.0 12 GLN 92.7 62.4 59.1 13 VAL 118.5 99.8 27.9 14 ASP 49.5 44.8 61.0 15 GLN 83.0 55.9 62.3 16 ALA 65.8 90.7 50.6 17 ILE 125.1 87.2 42.1 18 LEU 80.4 54.4 81.9 19 SER 31.9 38.1 81.1 20 GLU 116.6 84.1 72.0 21 GLU 16.3 11.7 87.8 22 ASP 25.7 23.3 77.4 23 ARG 147.8 70.7 62.8 24 VAL 118.8 100.0 35.8 25 VAL 116.9 98.4 42.8 26 VAL 118.8 100.0 29.2 27 ILE 143.5 100.0 32.0 28 ARG 207.8 99.5 43.9 29 PHE 166.6 99.9 32.9 30 GLY 34.8 100.0 46.1 31 HIS 112.3 74.8 59.1 32 ASP 63.8 57.8 73.1 33 TRP 30.6 14.9 77.7 34 ASP 85.5 77.3 50.7 35 PRO 39.9 32.0 73.2 36 THR 75.9 71.0 61.3 37 CYS 99.2 100.0 56.5 38 MET 47.4 29.7 79.0 39 LYS 48.9 28.2 74.2 40 MET 159.4 100.0 39.6 41 ASP 84.0 76.0 55.5 42 GLU 16.3 11.8 80.9 43 VAL 106.6 89.7 55.9 44 LEU 147.8 100.0 25.8 45 TYR 65.6 36.3 64.0 46 SER 50.9 60.9 59.2 47 ILE 143.5 100.0 39.5 48 ALA 66.8 91.9 47.4 49 GLU 50.0 36.1 70.4 50 LYS 76.6 44.2 73.4 51 VAL 118.6 99.8 34.2 52 LYS 77.8 44.9 82.5 53 ASN 0.0 0.0 80.1 54 PHE 130.9 78.5 45.7 55 ALA 72.6 100.0 37.5 56 VAL 94.1 79.2 59.7 57 ILE 142.5 99.3 32.6 58 TYR 150.6 83.2 40.2 59 LEU 136.4 92.3 50.7 60 VAL 118.8 100.0 42.3 61 ASP 94.2 85.2 68.3 62 ILE 142.0 99.0 52.9 63 THR 20.9 19.5 81.4 64 GLU 71.5 51.6 72.8 65 VAL 118.4 99.7 50.8 66 PRO 59.6 47.9 86.9 67 ASP 43.9 39.7 60.7 68 PHE 128.2 76.9 46.0 69 ASN 94.4 78.1 55.1 70 LYS 0.0 0.0 90.4 71 MET 104.2 65.4 50.2 72 TYR 157.2 86.9 47.8 73 GLU 110.6 79.8 72.4 74 LEU 67.2 45.5 67.5 75 TYR 163.5 90.3 61.9 76 ASP 93.5 84.6 60.5 77 PRO 62.6 50.3 75.1 78 CYS 99.2 100.0 44.3 79 THR 93.5 87.5 51.1 80 VAL 118.8 100.0 33.5 81 MET 146.0 91.6 38.0 82 PHE 164.7 98.7 30.7 83 PHE 155.7 93.3 37.9 84 PHE 161.8 97.0 49.5 85 ARG 92.8 44.4 76.1 86 ASN 55.7 46.0 66.2 87 LYS 70.0 40.4 80.0 88 HIS 91.5 60.9 52.5 89 ILE 141.5 98.6 46.5 90 MET 46.8 29.4 72.8 91 ILE 134.4 93.6 35.7 92 ASP 39.9 36.1 62.8 93 LEU 109.4 74.0 49.0 94 GLY 7.4 21.3 64.6 95 ILE 141.4 98.5 31.4 96 ASN 53.4 44.2 61.7 97 TRP 122.7 59.9 58.9 98 ALA 62.1 85.6 46.2 99 MET 156.1 97.9 43.4 100 GLU 0.0 0.0 89.2 101 ASP 26.5 24.0 74.6 102 LYS 84.1 48.5 65.1 103 GLN 62.5 42.1 76.0 104 GLU 101.6 73.3 59.1 105 MET 159.4 100.0 23.7 106 VAL 112.6 94.8 50.2 107 ASP 47.5 43.0 74.7 108 ILE 143.4 99.9 33.0 109 ILE 143.5 100.0 23.5 110 GLU 82.9 59.8 60.3 111 THR 64.5 60.3 63.2 112 VAL 118.7 99.9 27.8 113 TYR 149.5 82.6 49.9 114 ARG 79.8 38.2 76.9 115 GLY 29.0 83.5 52.4 116 ALA 72.6 99.9 49.3 117 ARG 102.6 49.1 70.5 118 LYS 50.6 29.2 82.2 119 GLY 1.8 5.2 83.1 120 ARG 73.1 35.0 75.1 121 GLY 24.9 71.5 62.2 122 LEU 65.5 44.3 63.7 123 VAL 109.1 91.8 38.4 124 VAL 54.1 45.6 59.8 125 SER 72.5 86.7 38.3 126 PRO 32.1 25.7 77.9 127 LYS 148.6 85.7 50.8 128 ASP 29.5 26.7 82.2 129 TYR 39.8 22.0 86.6 130 SER 7.1 8.5 91.8 131 THR 106.9 100.0 0.0