Protein Data Bank File : 1jt8 Title : TRANSLATION 20-AUG-01 1JT8 Number of Amino Acid Residues : 102 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 MET ALA GLU GLN GLN GLN GLU GLN GLN ILE 10 ARG VAL ARG ILE PRO ARG LYS GLU GLU ASN 20 GLU ILE LEU GLY ILE ILE GLU GLN MET LEU 30 GLY ALA SER ARG VAL ARG VAL ARG CYS LEU 40 ASP GLY LYS THR ARG LEU GLY ARG ILE PRO 50 GLY ARG LEU LYS ASN ARG ILE TRP VAL ARG 60 GLU GLY ASP VAL VAL ILE VAL LYS PRO TRP 70 GLU VAL GLN GLY ASP GLN LYS CYS ASP ILE 80 ILE TRP ARG TYR THR LYS THR GLN VAL GLU 90 TRP LEU LYS ARG LYS GLY TYR LEU ASP GLU 100 LEU LEU Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 MET 0.0 35.9 179.9 -147.5 150.3 170.9 2 ALA -165.7 118.8 179.8 3 GLU -139.0 78.6 -179.9 -77.1 -74.6 95.7 4 GLN -130.8 162.5 179.8 -140.2 85.6 -86.5 5 GLN -67.0 147.8 -179.6 -76.6 100.8 -92.1 6 GLN 59.7 65.3 -179.7 -158.8 177.4 -96.1 7 GLU -125.1 136.4 179.7 -152.3 -177.5 92.3 8 GLN -84.2 111.9 -179.5 -155.0 151.1 -94.9 9 GLN -89.8 151.1 -179.9 -75.5 127.0 94.1 10 ILE -67.4 -33.8 179.8 54.5 169.6 11 ARG 62.4 17.7 179.7 -114.7 -93.4 -59.0 -73.7 12 VAL -83.5 -179.5 -179.8 89.7 13 ARG 67.5 67.6 -179.9 -154.9 -164.1 -161.0 137.9 14 ILE -91.6 136.0 179.9 -170.1 81.7 15 PRO -76.4 178.7 -179.7 22.2 -21.5 16 ARG 65.4 101.1 -179.9 -95.0 -131.1 -175.6 105.4 17 LYS -164.0 72.8 -179.7 47.5 -112.8 -161.9 161.0 18 GLU -69.8 -51.8 180.0 -163.9 157.4 -91.0 19 GLU -114.0 25.4 179.8 -139.1 -108.2 99.5 20 ASN 64.1 175.1 179.9 -132.4 74.8 21 GLU -126.2 172.9 -179.9 -73.7 -152.0 -96.6 22 ILE -109.9 161.5 -178.9 -94.6 96.9 23 LEU -125.1 120.7 -177.9 6.7 -60.8 24 GLY -141.2 162.1 178.6 25 ILE -98.1 139.9 -178.9 56.9 155.3 26 ILE -99.5 151.6 179.2 -163.3 60.0 27 GLU -143.8 138.4 178.9 -93.8 -152.9 90.6 28 GLN 167.5 123.6 179.4 -118.3 -100.6 41.6 29 MET -109.7 -29.7 -179.8 -173.0 61.2 -129.3 30 LEU -55.8 -56.5 179.7 -58.9 123.9 31 GLY 85.7 75.8 179.7 32 ALA -120.0 37.5 -179.8 33 SER 69.6 1.3 179.8 -123.8 34 ARG -140.9 155.3 -179.4 60.1 -132.3 -61.8 -82.7 35 VAL -141.2 169.6 179.9 -73.5 36 ARG -113.4 128.0 -179.4 39.4 142.9 79.2 -129.0 37 VAL -120.7 148.6 175.8 -103.4 38 ARG -120.7 135.1 -175.2 31.2 -93.0 -73.6 -95.6 39 CYS -140.2 160.4 176.0 -30.0 40 LEU -93.6 179.5 -172.6 -141.5 48.8 41 ASP 75.3 22.7 176.8 -161.2 -105.4 42 GLY 66.7 56.0 178.2 43 LYS -145.8 154.5 175.8 -100.8 -56.0 132.4 -105.5 44 THR -141.6 117.8 -175.6 -17.2 45 ARG -146.8 164.9 175.4 40.8 -95.5 -45.8 -64.0 46 LEU -97.5 125.1 -175.9 51.4 131.2 47 GLY -95.9 142.9 179.6 48 ARG -121.4 149.5 -179.9 59.6 169.0 -63.3 -75.2 49 ILE -126.9 156.5 -179.9 -118.5 115.1 50 PRO -74.4 167.9 -179.5 22.0 -22.2 51 GLY -57.5 -45.5 -179.8 52 ARG -58.2 -55.1 180.0 -93.0 -89.7 -100.2 125.6 53 LEU -65.6 -34.0 -179.3 -102.2 80.9 54 LYS -52.1 -48.4 -179.8 -155.7 -112.7 155.2 -160.8 55 ASN -89.1 3.6 -179.6 -126.3 102.5 56 ARG -116.1 -15.9 -179.3 -151.3 -159.4 -74.6 -103.1 57 ILE -80.9 -52.4 180.0 48.7 114.4 58 TRP 43.8 53.6 -179.7 -79.1 77.7 59 VAL -70.7 133.8 179.8 -59.9 60 ARG -93.0 -66.9 179.9 -168.0 -137.7 177.3 -86.3 61 GLU -174.5 113.7 179.2 -148.3 74.1 -114.6 62 GLY 99.4 66.5 178.9 63 ASP -125.9 160.5 179.4 -76.7 -84.4 64 VAL -105.7 142.9 -178.9 -129.0 65 VAL -142.6 155.3 177.0 -60.4 66 ILE -99.9 134.5 -176.6 -175.6 -83.6 67 VAL -119.2 153.4 177.8 -33.5 68 LYS -108.3 146.9 -177.9 -140.5 171.8 102.5 79.1 69 PRO -88.4 138.0 -179.1 23.6 -16.9 70 TRP -122.6 117.6 178.5 -74.5 44.1 71 GLU 47.9 -147.8 -180.0 -133.6 -160.9 114.8 72 VAL -148.5 -86.7 -179.8 -96.6 73 GLN 52.2 -158.7 178.9 -51.5 160.0 -81.4 74 GLY -92.5 25.7 -179.9 75 ASP -176.6 136.6 -178.3 39.6 83.2 76 GLN -111.3 154.2 176.6 -67.3 -143.6 154.2 77 LYS -98.2 152.3 -178.2 -106.0 163.0 -158.4 -97.7 78 CYS -143.9 151.7 176.2 71.3 79 ASP -101.6 118.5 -174.8 -145.7 -85.5 80 ILE -113.5 155.0 176.6 42.3 149.5 81 ILE -116.6 128.6 -176.9 -108.9 81.7 82 TRP -97.2 142.2 179.4 148.3 86.8 83 ARG -167.6 142.8 -179.5 -121.3 -87.3 125.4 106.6 84 TYR -105.7 91.2 179.3 -170.4 -104.9 85 THR 59.6 105.0 179.5 -43.1 86 LYS -138.8 -74.7 -179.7 32.4 126.1 93.8 -176.0 87 THR -175.8 -43.8 179.8 9.7 88 GLN -59.4 -57.4 179.3 -160.5 161.7 92.1 89 VAL -65.6 -34.3 179.1 -177.7 90 GLU -61.9 -35.4 179.6 -154.6 -173.2 92.2 91 TRP -65.4 -55.2 -179.6 -123.1 60.3 92 LEU -61.8 -38.0 179.5 49.2 92.7 93 LYS -65.3 -44.6 178.6 -127.9 58.8 122.1 -168.8 94 ARG -57.6 -36.9 178.9 -82.9 166.4 75.0 115.7 95 LYS -64.3 -33.3 -179.9 -135.7 124.0 74.4 -168.3 96 GLY -63.6 -44.9 179.7 97 TYR -66.0 -39.4 -180.0 -32.5 134.0 98 LEU -59.3 -48.8 -179.9 -177.6 -80.4 99 ASP -62.8 -43.2 -179.7 -166.6 -92.9 100 GLU -65.5 -55.3 -179.7 -151.0 -103.4 -95.1 101 LEU -149.5 -171.2 180.0 64.5 122.3 102 LEU 76.4 -57.5 0.0 -144.7 154.0 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 MET -14.198 -6.186 -21.467 2 ALA -16.979 -4.205 -19.687 3 GLU -18.303 -0.654 -20.295 4 GLN -21.677 -0.088 -18.559 5 GLN -23.086 2.520 -16.116 6 GLN -22.464 1.805 -12.389 7 GLU -19.407 -0.463 -12.884 8 GLN -16.650 -1.195 -10.321 9 GLN -13.283 -0.514 -12.032 10 ILE -10.002 -2.077 -10.795 11 ARG -8.273 1.378 -10.792 12 VAL -4.948 -0.525 -10.976 13 ARG -1.928 0.466 -13.164 14 ILE -1.020 3.810 -11.506 15 PRO 1.426 6.137 -13.324 16 ARG 4.417 7.956 -11.708 17 LYS 6.927 5.410 -10.303 18 GLU 10.605 6.514 -10.412 19 GLU 11.784 4.271 -7.520 20 ASN 8.591 2.115 -7.265 21 GLU 6.356 2.159 -4.139 22 ILE 5.899 -0.067 -1.056 23 LEU 2.634 -1.879 -0.033 24 GLY 1.496 -2.011 3.627 25 ILE -1.569 -2.484 5.842 26 ILE -2.589 0.388 8.176 27 GLU -3.735 0.124 11.805 28 GLN -5.048 2.796 14.252 29 MET -8.236 3.222 16.352 30 LEU -7.353 6.434 18.295 31 GLY -7.503 8.652 15.160 32 ALA -4.923 11.463 15.580 33 SER -4.530 12.422 11.861 34 ARG -1.705 9.791 11.677 35 VAL -1.513 5.951 11.508 36 ARG 1.091 3.157 11.646 37 VAL 1.785 0.912 8.620 38 ARG 3.820 -2.262 8.088 39 CYS 4.666 -3.112 4.473 40 LEU 6.183 -5.597 2.077 41 ASP 8.669 -4.652 -0.629 42 GLY 10.951 -4.315 2.487 43 LYS 9.466 -1.293 4.361 44 THR 8.120 -0.118 7.740 45 ARG 6.690 3.413 7.900 46 LEU 4.246 5.773 9.610 47 GLY 1.503 6.713 7.095 48 ARG -0.074 10.173 6.796 49 ILE -3.322 11.223 5.049 50 PRO -4.614 14.581 3.696 51 GLY -7.390 16.639 5.397 52 ARG -10.045 15.356 2.926 53 LEU -9.124 11.663 3.453 54 LYS -8.542 12.278 7.217 55 ASN -12.300 12.875 7.812 56 ARG -13.249 10.329 5.075 57 ILE -11.018 7.321 6.009 58 TRP -12.258 6.666 9.605 59 VAL -10.126 3.470 9.759 60 ARG -11.126 1.170 12.657 61 GLU -8.556 -1.690 12.681 62 GLY -7.233 -3.902 9.831 63 ASP -7.308 -1.940 6.521 64 VAL -5.013 -2.096 3.431 65 VAL -3.137 0.977 2.133 66 ILE -0.592 1.913 -0.576 67 VAL 2.469 3.797 0.784 68 LYS 5.047 6.290 -0.538 69 PRO 8.668 6.320 0.751 70 TRP 10.056 9.259 2.794 71 GLU 13.871 9.593 3.284 72 VAL 15.421 6.380 4.798 73 GLN 17.218 6.267 8.223 74 GLY 16.170 3.360 10.525 75 ASP 12.473 4.176 9.802 76 GLN 10.650 5.673 6.797 77 LYS 7.740 8.133 6.565 78 CYS 5.027 7.326 4.039 79 ASP 2.045 8.927 2.312 80 ILE -0.790 6.378 2.408 81 ILE -4.104 5.823 0.662 82 TRP -6.747 3.897 2.676 83 ARG -9.102 1.274 1.179 84 TYR -10.728 -1.979 2.404 85 THR -10.147 -4.646 -0.315 86 LYS -10.534 -3.152 -3.834 87 THR -7.994 -4.166 -6.551 88 GLN -4.869 -1.930 -6.362 89 VAL -3.701 -3.351 -2.984 90 GLU -5.023 -6.802 -4.048 91 TRP -2.643 -6.629 -7.066 92 LEU 0.504 -5.821 -5.009 93 LYS -0.537 -8.378 -2.319 94 ARG -1.003 -11.126 -4.974 95 LYS 2.551 -10.258 -6.138 96 GLY 3.824 -10.895 -2.565 97 TYR 2.523 -14.508 -2.617 98 LEU 3.941 -15.022 -6.154 99 ASP 7.472 -13.986 -5.048 100 GLU 7.257 -16.160 -1.879 101 LEU 5.830 -19.288 -3.610 102 LEU 3.582 -20.453 -6.528 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 C C 10 C S S S S S T T T T/S 20 S S S S S S S S S S/S 30 S S S S S S S S S/T T 40 T T S S S S S S S S/H 50 H H H H H H H S S S 60 S/S S S S S S/S S S S S 70 S T T T T/S S S S S S 80 S/S S S S S C H H H H 90 H H H H H H H H H H 100 H/S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S 10 S S S 20 E E E E E E S S 30 S e E E E E E E E 40 T T E E E E E E e h 50 H H H H H H H h 60 S E E E E E e B 70 t T T t E E E E E 80 E E E S S h H H H 90 H H H H H H H H H H 100 h Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 MET 0.0 0.0 96.0 2 ALA 21.9 30.2 83.7 3 GLU 3.0 2.1 91.4 4 GLN 19.2 12.9 90.6 5 GLN 0.0 0.0 84.9 6 GLN 0.0 0.0 91.4 7 GLU 95.4 68.9 69.7 8 GLN 0.0 0.0 90.7 9 GLN 33.6 22.6 84.6 10 ILE 46.7 32.5 68.1 11 ARG 60.5 29.0 83.1 12 VAL 104.6 88.0 42.7 13 ARG 6.0 2.9 87.8 14 ILE 53.5 37.3 81.0 15 PRO 35.1 28.2 71.4 16 ARG 0.0 0.0 88.7 17 LYS 68.8 39.7 78.2 18 GLU 0.0 0.0 91.4 19 GLU 2.7 2.0 84.9 20 ASN 28.2 23.3 80.3 21 GLU 97.8 70.5 51.6 22 ILE 126.6 88.2 49.6 23 LEU 123.3 83.4 50.2 24 GLY 33.8 97.1 53.5 25 ILE 81.3 56.6 62.8 26 ILE 142.7 99.4 32.7 27 GLU 95.1 68.6 60.5 28 GLN 124.0 83.4 50.0 29 MET 66.4 41.7 82.9 30 LEU 9.8 6.6 85.7 31 GLY 5.1 14.7 80.6 32 ALA 22.1 30.4 72.3 33 SER 31.0 37.1 65.2 34 ARG 66.5 31.8 76.3 35 VAL 108.0 90.9 38.9 36 ARG 55.2 26.4 76.3 37 VAL 118.8 100.0 34.9 38 ARG 98.6 47.2 68.9 39 CYS 95.9 96.7 49.0 40 LEU 45.2 30.6 72.1 41 ASP 49.3 44.6 66.3 42 GLY 0.0 0.0 83.0 43 LYS 115.6 66.7 65.4 44 THR 19.1 17.9 74.3 45 ARG 205.3 98.3 41.8 46 LEU 90.3 61.1 64.3 47 GLY 34.8 100.0 46.3 48 ARG 112.6 53.9 66.5 49 ILE 136.7 95.3 40.0 50 PRO 66.5 53.4 68.2 51 GLY 0.0 0.0 74.6 52 ARG 54.8 26.2 85.7 53 LEU 105.0 71.1 49.3 54 LYS 101.3 58.4 70.8 55 ASN 28.1 23.3 80.9 56 ARG 75.5 36.1 78.4 57 ILE 126.3 88.0 33.6 58 TRP 29.6 14.5 86.6 59 VAL 110.1 92.6 47.1 60 ARG 46.8 22.4 77.3 61 GLU 90.9 65.6 68.9 62 GLY 7.9 22.7 74.5 63 ASP 97.7 88.4 53.4 64 VAL 93.5 78.7 48.9 65 VAL 118.8 100.0 36.8 66 ILE 119.9 83.5 55.0 67 VAL 118.8 100.0 41.7 68 LYS 61.5 35.4 72.3 69 PRO 93.4 75.0 69.5 70 TRP 123.7 60.4 64.6 71 GLU 34.0 24.5 78.5 72 VAL 19.7 16.6 79.5 73 GLN 46.2 31.1 85.5 74 GLY 0.0 0.0 82.4 75 ASP 24.4 22.1 80.2 76 GLN 139.8 94.1 56.7 77 LYS 68.3 39.4 58.9 78 CYS 99.2 100.0 42.4 79 ASP 78.7 71.2 57.1 80 ILE 142.9 99.6 33.7 81 ILE 67.9 47.3 64.8 82 TRP 146.7 71.6 52.7 83 ARG 97.9 46.9 66.8 84 TYR 46.2 25.5 83.7 85 THR 33.1 31.0 67.7 86 LYS 153.1 88.3 60.5 87 THR 76.2 71.2 57.0 88 GLN 127.9 86.1 49.1 89 VAL 114.8 96.6 40.4 90 GLU 62.4 45.0 64.7 91 TRP 71.5 34.9 73.8 92 LEU 131.3 88.8 40.8 93 LYS 131.9 76.1 51.6 94 ARG 58.2 27.9 77.2 95 LYS 55.2 31.8 71.0 96 GLY 25.2 72.4 56.6 97 TYR 67.6 37.4 63.8 98 LEU 54.3 36.7 73.0 99 ASP 7.4 6.7 82.8 100 GLU 29.3 21.2 76.7 101 LEU 42.8 29.0 79.3 102 LEU 22.7 15.4 75.1