Protein Data Bank File : 1f86a Title : TRANSPORT PROTEIN 29-JUN-00 1F86 Number of Amino Acid Residues : 115 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 CYS PRO LEU MET VAL LYS VAL LEU ASP ALA 10 VAL ARG GLY SER PRO ALA ILE ASN VAL ALA 20 VAL HIS VAL PHE ARG LYS ALA ALA ASP ASP 30 THR TRP GLU PRO PHE ALA SER GLY LYS THR 40 SER GLU SER GLY GLU LEU HIS GLY LEU THR 50 THR GLU GLU GLU PHE VAL GLU GLY ILE TYR 60 LYS VAL GLU ILE ASP THR LYS SER TYR TRP 70 LYS ALA LEU GLY ILE SER PRO PHE HIS GLU 80 HIS ALA GLU VAL VAL PHE THR ALA ASN ASP 90 SER GLY PRO ARG ARG TYR THR ILE ALA ALA 100 LEU LEU SER PRO TYR SER TYR SER THR MET 110 ALA VAL VAL THR ASN Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 CYS 0.0 107.6 -176.0 -69.6 2 PRO -85.3 -5.0 179.6 28.5 -31.6 3 LEU -140.8 120.4 177.0 178.0 60.5 4 MET -129.9 144.1 178.3 -169.0 -89.1 -83.9 5 VAL -122.9 135.8 -179.0 178.6 6 LYS -130.2 130.0 -176.0 174.6 53.4 -171.7 136.8 7 VAL -130.9 129.8 -179.3 -168.5 8 LEU -120.1 150.5 -179.1 -64.3 -54.4 9 ASP -108.3 109.9 -175.2 179.7 -33.5 10 ALA -77.9 -11.4 173.6 11 VAL -79.9 -44.3 -174.2 170.7 12 ARG -93.6 -19.9 -173.1 -64.4 168.8 170.1 64.6 13 GLY 69.7 45.5 -172.2 14 SER -149.2 165.5 165.6 68.1 15 PRO -56.1 149.5 172.6 10.9 -21.4 16 ALA -95.2 106.8 -171.9 17 ILE -92.3 145.7 175.6 -58.8 163.2 18 ASN 62.6 37.3 175.4 -63.8 -35.2 19 VAL -89.1 123.7 177.5 178.7 20 ALA -75.5 140.7 -179.0 21 VAL -135.6 128.0 175.6 -179.8 22 HIS -120.4 132.0 178.8 -62.5 -110.1 23 VAL -111.4 135.6 178.3 -176.7 24 PHE -122.8 155.6 178.3 -56.4 88.1 25 ARG -132.3 131.4 -179.0 -176.7 -175.5 175.3 -83.6 26 LYS -69.7 129.2 -174.9 -85.8 -105.6 -142.7 1.3 27 ALA -89.1 175.1 -176.3 28 ALA -61.8 -26.7 -178.0 29 ASP -96.3 16.5 171.3 38.6 -132.1 30 ASP 77.5 12.6 176.2 -158.2 -152.0 31 THR -100.8 166.0 177.9 58.9 32 TRP -86.2 112.8 -177.6 -68.1 105.8 33 GLU -95.0 134.6 175.6 -68.6 -162.7 -40.5 34 PRO -59.7 133.2 -175.8 -27.1 42.0 35 PHE -117.8 -47.2 179.4 179.3 83.1 36 ALA -164.6 158.8 173.5 37 SER -152.2 165.3 178.2 -39.0 38 GLY -177.0 -168.9 177.2 39 LYS -139.7 151.9 -179.1 69.2 -160.5 33.2 156.2 40 THR -69.8 145.9 177.1 62.0 41 SER -78.6 -173.7 174.1 72.4 42 GLU -62.7 -19.3 175.7 48.9 -98.9 -137.1 43 SER -95.6 6.9 -178.6 70.9 44 GLY 78.8 12.5 -175.8 45 GLU -111.6 152.5 179.7 -66.3 177.9 5.0 46 LEU -133.8 110.4 179.6 169.0 51.0 47 HIS -110.4 164.8 172.8 -58.2 74.6 48 GLY 82.3 8.9 -177.2 49 LEU -64.9 -40.9 -173.3 -81.7 165.0 50 THR -151.1 -175.4 -177.8 -171.0 51 THR -124.3 159.3 175.9 68.2 52 GLU -61.8 -33.8 179.0 -3.9 -118.9 60.4 53 GLU -66.0 -43.2 -175.4 -92.9 -174.7 -156.3 54 GLU -79.1 -25.4 -175.4 -68.4 -68.3 154.7 55 PHE -86.2 72.4 -177.2 -168.6 41.0 56 VAL -77.6 173.6 172.1 -64.1 57 GLU -55.0 149.4 171.5 -74.4 -166.0 77.3 58 GLY 164.2 -178.6 173.1 59 ILE -99.3 120.3 -177.8 -58.5 174.1 60 TYR -114.6 148.9 175.8 -67.3 83.8 61 LYS -124.9 119.3 172.6 175.8 -171.2 -45.5 -171.4 62 VAL -101.1 116.3 179.7 173.8 63 GLU -106.2 118.6 -177.8 171.4 -149.2 106.2 64 ILE -103.2 120.8 -169.7 -53.6 171.7 65 ASP -85.8 73.3 -174.3 -62.2 156.3 66 THR -69.4 -35.9 -178.7 58.8 67 LYS -65.3 -41.2 -179.3 -175.1 173.2 -117.8 -104.9 68 SER -66.0 -33.3 175.0 37.9 69 TYR -61.9 -54.9 -179.0 173.3 76.7 70 TRP -61.9 -43.0 177.4 -67.1 113.4 71 LYS -67.9 -37.6 173.7 -70.9 -179.6 65.3 -110.8 72 ALA -64.9 -14.0 169.8 73 LEU -97.1 11.0 174.5 -63.1 167.7 74 GLY 75.9 21.7 -179.8 75 ILE -119.1 139.6 -174.0 -57.8 -51.0 76 SER -96.2 98.2 -173.5 -168.1 77 PRO -92.1 176.1 -179.3 43.5 -43.3 78 PHE -76.9 -52.7 -168.5 -174.7 77.0 79 HIS -84.4 151.7 168.6 -57.4 90.5 80 GLU -73.1 -41.9 -178.2 -72.9 -62.6 -56.5 81 HIS -161.0 172.5 170.8 40.1 -107.4 82 ALA -110.8 133.4 -177.7 83 GLU -117.4 141.0 173.8 -44.6 84.3 -175.9 84 VAL -132.7 114.6 -174.2 -175.0 85 VAL -118.9 123.5 -170.2 -174.5 86 PHE -156.5 150.4 168.8 60.8 -79.4 87 THR -81.1 130.8 -178.0 -62.4 88 ALA -116.3 147.8 166.3 89 ASN 62.8 25.4 -178.5 -55.2 -51.1 90 ASP -82.3 -6.8 168.9 -154.3 53.6 91 SER -118.9 28.4 -179.5 -43.2 92 GLY 100.6 173.6 -174.0 93 PRO -63.2 136.8 169.9 11.1 -21.9 94 ARG -131.5 166.5 173.6 -58.1 -67.2 -174.5 -88.3 95 ARG -110.1 133.4 -173.6 -64.4 -179.0 78.0 158.4 96 TYR -117.6 127.7 165.4 -61.6 84.0 97 THR -111.7 120.0 178.9 -63.7 98 ILE -104.1 115.8 -178.6 -55.7 -54.8 99 ALA -112.7 145.5 175.9 100 ALA -138.2 136.6 177.9 101 LEU -112.4 118.8 -170.6 179.4 56.2 102 LEU -107.0 134.1 165.6 -52.5 -173.8 103 SER -129.5 163.5 -176.8 -62.5 104 PRO -57.6 -37.7 -177.5 -31.6 42.4 105 TYR -115.0 14.6 180.0 -76.1 76.3 106 SER -157.4 158.4 163.7 173.7 107 TYR -150.5 160.5 173.3 60.4 86.3 108 SER -124.3 141.4 174.2 -65.2 109 THR -131.3 149.0 -179.1 42.7 110 MET -146.6 149.1 177.5 93.9 101.6 171.1 111 ALA -118.9 129.5 168.3 112 VAL -105.9 125.4 -177.2 175.3 113 VAL -120.7 124.0 -179.0 -176.9 114 THR -127.4 153.0 -178.3 174.3 115 ASN -106.0 -71.7 0.0 -168.0 159.9 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 CYS 15.565 30.777 25.268 2 PRO 13.288 30.331 28.186 3 LEU 16.024 30.149 30.838 4 MET 18.993 32.530 31.041 5 VAL 21.478 33.022 33.854 6 LYS 23.496 36.218 34.430 7 VAL 26.273 36.530 37.044 8 LEU 28.156 39.642 38.157 9 ASP 31.225 40.107 40.367 10 ALA 30.761 42.856 42.971 11 VAL 34.511 42.891 43.879 12 ARG 35.681 43.606 40.349 13 GLY 32.694 45.517 38.919 14 SER 32.526 43.114 36.012 15 PRO 30.670 40.122 34.594 16 ALA 31.549 36.899 36.447 17 ILE 33.095 34.874 33.642 18 ASN 33.405 31.075 33.483 19 VAL 30.979 30.446 36.357 20 ALA 29.667 26.858 36.239 21 VAL 25.899 26.518 36.554 22 HIS 23.945 23.299 37.075 23 VAL 20.149 23.118 36.765 24 PHE 18.125 20.335 38.406 25 ARG 14.443 19.508 38.188 26 LYS 12.522 17.707 40.896 27 ALA 11.370 14.268 39.659 28 ALA 8.174 12.406 40.420 29 ASP 9.920 10.576 43.253 30 ASP 11.065 13.860 44.808 31 THR 14.776 13.731 44.041 32 TRP 16.774 16.357 42.169 33 GLU 17.403 15.136 38.600 34 PRO 20.083 16.775 36.440 35 PHE 18.405 18.959 33.824 36 ALA 21.021 21.195 32.133 37 SER 24.386 22.790 32.792 38 GLY 26.769 25.291 31.288 39 LYS 29.150 28.142 32.145 40 THR 28.918 31.896 31.884 41 SER 30.458 33.692 28.927 42 GLU 32.669 36.767 28.824 43 SER 29.529 38.830 29.419 44 GLY 28.577 36.814 32.462 45 GLU 25.676 35.250 30.655 46 LEU 24.606 31.698 30.074 47 HIS 22.216 31.070 27.167 48 GLY 21.272 27.822 25.623 49 LEU 20.508 25.779 28.728 50 THR 17.150 24.435 27.456 51 THR 14.349 24.704 24.954 52 GLU 10.684 25.703 25.303 53 GLU 9.747 22.065 24.529 54 GLU 12.036 20.597 27.194 55 PHE 11.426 23.216 29.873 56 VAL 8.155 21.796 31.119 57 GLU 6.375 22.684 34.343 58 GLY 8.238 21.637 37.453 59 ILE 10.298 22.717 40.431 60 TYR 13.766 23.743 39.255 61 LYS 16.987 24.391 41.151 62 VAL 19.645 26.563 39.579 63 GLU 22.950 25.991 41.329 64 ILE 25.614 28.624 40.641 65 ASP 29.061 27.348 41.547 66 THR 30.291 30.462 43.325 67 LYS 32.934 28.716 45.464 68 SER 34.667 27.279 42.379 69 TYR 34.547 30.776 40.823 70 TRP 36.138 32.571 43.810 71 LYS 38.717 29.823 44.190 72 ALA 39.693 29.836 40.435 73 LEU 40.398 33.545 41.207 74 GLY 42.548 32.605 44.154 75 ILE 39.940 33.675 46.853 76 SER 38.336 31.635 49.857 77 PRO 34.591 32.484 49.966 78 PHE 31.845 31.665 52.417 79 HIS 29.212 29.814 50.392 80 GLU 29.508 26.529 48.562 81 HIS 27.147 27.748 45.836 82 ALA 24.188 30.104 45.295 83 GLU 20.863 28.303 44.826 84 VAL 17.716 29.443 43.208 85 VAL 14.702 27.149 43.640 86 PHE 11.397 27.951 41.936 87 THR 8.315 26.524 40.272 88 ALA 8.386 27.239 36.543 89 ASN 5.756 27.346 33.824 90 ASP 2.779 26.547 36.057 91 SER 0.609 29.196 34.252 92 GLY 2.025 28.322 30.846 93 PRO 5.420 29.014 29.330 94 ARG 7.430 31.935 30.629 95 ARG 10.929 33.200 30.105 96 TYR 13.134 33.360 33.170 97 THR 16.324 35.360 33.708 98 ILE 18.075 34.297 36.947 99 ALA 20.633 36.904 37.993 100 ALA 23.185 36.730 40.787 101 LEU 25.494 39.411 42.211 102 LEU 28.474 37.813 43.965 103 SER 30.682 38.885 46.861 104 PRO 32.923 36.594 48.939 105 TYR 30.529 36.533 51.960 106 SER 27.245 37.495 50.301 107 TYR 25.148 37.242 47.185 108 SER 21.930 38.616 45.840 109 THR 19.726 36.866 43.359 110 MET 16.760 38.132 41.391 111 ALA 14.416 36.656 38.810 112 VAL 12.900 38.477 35.875 113 VAL 9.944 36.570 34.506 114 THR 8.354 37.590 31.218 115 ASN 5.490 36.231 29.192 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C S S S S S S S S/T T 10 T T S S S S C S S S 20 S S S S S S S/T T T T/S 30 S S S S C S S S S S 40 S/T T T T/S S S S S C C 50 T T T T C S S S S/S S 60 S S S S S/H H H H H H 70 H H H H/S S S S S C S 80 S S S S S S S C T T 90 T T/S S S S S S S S S 100 S S S/T T T T/S S S S S 110 S S S S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 e E E E E E E E e 10 T T T E E e T T e E 20 E E E E E E e T T t 30 e E E E E E E E E e 40 t T T e E E S 50 t T T T t S E E E 60 E E E E h H H H H H 70 H H h T t S S 80 E E E E E E E t T 90 T t E E E E E E 100 E E E T T E E E E E 110 E E E E Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 CYS 58.1 58.6 72.1 2 PRO 118.7 95.3 53.7 3 LEU 147.8 100.0 27.8 4 MET 122.2 76.6 58.6 5 VAL 118.8 100.0 28.4 6 LYS 141.1 81.4 43.8 7 VAL 118.8 100.0 33.4 8 LEU 92.1 62.3 56.9 9 ASP 110.5 100.0 51.1 10 ALA 47.7 65.6 68.8 11 VAL 52.4 44.1 67.5 12 ARG 122.5 58.6 63.6 13 GLY 0.0 0.0 81.7 14 SER 51.4 61.5 58.5 15 PRO 82.6 66.3 60.0 16 ALA 72.6 100.0 42.2 17 ILE 75.0 52.3 72.8 18 ASN 32.0 26.4 71.5 19 VAL 118.3 99.6 41.8 20 ALA 42.9 59.1 67.9 21 VAL 118.8 100.0 34.2 22 HIS 81.2 54.0 66.8 23 VAL 118.8 100.0 30.3 24 PHE 129.3 77.5 53.1 25 ARG 144.0 68.9 57.7 26 LYS 127.3 73.4 57.8 27 ALA 65.4 90.1 80.6 28 ALA 0.0 0.0 87.3 29 ASP 20.5 18.5 78.6 30 ASP 21.2 19.2 78.4 31 THR 23.8 22.3 79.2 32 TRP 149.5 72.9 56.8 33 GLU 54.5 39.3 70.7 34 PRO 29.3 23.6 73.4 35 PHE 141.5 84.8 51.4 36 ALA 56.4 77.7 57.7 37 SER 48.8 58.4 67.8 38 GLY 13.5 38.8 58.6 39 LYS 55.3 31.9 77.1 40 THR 106.9 100.0 51.5 41 SER 43.7 52.2 79.5 42 GLU 13.6 9.8 72.2 43 SER 32.4 38.8 70.7 44 GLY 34.8 100.0 63.8 45 GLU 92.4 66.7 60.9 46 LEU 133.6 90.4 52.1 47 HIS 68.5 45.6 64.6 48 GLY 5.7 16.4 72.1 49 LEU 144.0 97.4 43.8 50 THR 97.2 90.9 38.3 51 THR 31.4 29.3 67.4 52 GLU 32.9 23.8 72.8 53 GLU 0.0 0.0 89.0 54 GLU 36.9 26.6 81.6 55 PHE 165.4 99.2 41.5 56 VAL 42.1 35.4 86.3 57 GLU 53.5 38.6 79.6 58 GLY 20.0 57.5 63.3 59 ILE 76.4 53.2 63.2 60 TYR 181.0 100.0 36.9 61 LYS 124.0 71.5 45.9 62 VAL 118.8 100.0 27.4 63 GLU 108.1 78.0 52.0 64 ILE 143.5 100.0 29.1 65 ASP 88.6 80.2 64.5 66 THR 101.8 95.2 39.8 67 LYS 113.4 65.4 69.3 68 SER 30.5 36.4 68.1 69 TYR 167.0 92.2 45.3 70 TRP 201.3 98.2 39.5 71 LYS 65.8 37.9 77.1 72 ALA 8.7 12.0 86.0 73 LEU 94.0 63.6 69.5 74 GLY 0.0 0.0 81.0 75 ILE 77.1 53.7 64.7 76 SER 8.8 10.5 75.4 77 PRO 122.6 98.5 53.0 78 PHE 55.1 33.0 70.7 79 HIS 98.8 65.8 67.2 80 GLU 38.5 27.8 74.2 81 HIS 90.6 60.3 67.5 82 ALA 72.6 100.0 38.2 83 GLU 83.1 59.9 67.1 84 VAL 96.4 81.1 44.5 85 VAL 68.1 57.4 53.7 86 PHE 129.9 77.9 43.7 87 THR 52.7 49.3 64.6 88 ALA 72.6 100.0 47.0 89 ASN 113.6 94.0 54.1 90 ASP 36.8 33.3 76.7 91 SER 12.3 14.7 85.9 92 GLY 11.3 32.5 67.1 93 PRO 22.5 18.0 73.0 94 ARG 151.4 72.5 62.6 95 ARG 78.0 37.3 73.0 96 TYR 166.8 92.2 42.6 97 THR 71.8 67.1 51.1 98 ILE 142.5 99.3 27.6 99 ALA 56.9 78.3 53.3 100 ALA 71.9 99.0 38.5 101 LEU 67.4 45.6 64.6 102 LEU 146.7 99.3 33.4 103 SER 51.1 61.1 51.0 104 PRO 91.1 73.1 39.9 105 TYR 45.4 25.1 73.7 106 SER 21.4 25.6 72.5 107 TYR 140.2 77.5 65.3 108 SER 18.4 22.0 71.5 109 THR 82.9 77.6 49.8 110 MET 54.2 34.0 71.2 111 ALA 43.8 60.4 54.8 112 VAL 46.3 39.0 62.1 113 VAL 69.4 58.4 56.5 114 THR 41.5 38.8 66.9 115 ASN 36.6 30.3 81.3