Protein Data Bank File : 1fsee Title : TRANSCRIPTION 08-SEP-00 1FSE Number of Amino Acid Residues : 64 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 LEU LEU THR LYS ARG GLU ARG GLU VAL PHE 10 GLU LEU LEU VAL GLN ASP LYS THR THR LYS 20 GLU ILE ALA SER GLU LEU PHE ILE SER GLU 30 LYS THR VAL ARG ASN HIS ILE SER ASN ALA 40 MET GLN LYS LEU GLY VAL LYS GLY ARG SER 50 GLN ALA VAL VAL GLU LEU LEU ARG MET GLY 60 GLU LEU GLU LEU Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 LEU 0.0 -49.6 -177.6 -89.0 167.5 2 LEU 29.9 123.6 172.9 -60.3 -172.3 3 THR -71.7 168.1 174.9 58.5 4 LYS -54.2 -45.3 -178.9 -107.6 -40.1 138.5 -69.4 5 ARG -76.4 -33.3 173.5 -148.6 79.5 176.5 -163.2 6 GLU -55.7 -47.3 178.4 -74.1 169.2 -12.4 7 ARG -56.8 -50.7 177.8 -162.2 162.2 -63.8 -99.9 8 GLU -59.8 -33.2 -177.1 -49.5 -171.4 -21.1 9 VAL -68.3 -46.7 -176.1 162.7 10 PHE -67.1 -38.7 172.9 -85.0 85.7 11 GLU -55.9 -36.9 178.0 -74.5 -177.6 -10.4 12 LEU -77.2 -31.7 176.3 -97.8 35.8 13 LEU -55.5 -37.8 -171.6 -127.2 2.5 14 VAL -91.9 4.6 -179.8 -67.7 15 GLN -107.5 16.8 172.4 -91.1 138.9 71.5 16 ASP 70.7 46.2 178.2 -162.5 27.5 17 LYS -111.7 151.2 173.0 -42.9 -151.9 138.2 -40.0 18 THR -80.8 162.6 176.6 170.4 19 THR -52.8 -43.1 176.6 56.5 20 LYS -67.8 -26.7 176.9 137.5 -92.0 -159.3 86.2 21 GLU -76.3 -36.9 178.6 -90.2 158.4 4.8 22 ILE -64.6 -41.6 175.5 -63.3 -176.2 23 ALA -61.5 -37.0 179.4 24 SER -68.8 -43.2 -177.0 -137.0 25 GLU -75.1 -29.1 -179.4 -168.0 173.2 -43.1 26 LEU -95.2 1.6 -178.1 -61.4 170.9 27 PHE 53.1 41.9 174.2 -41.2 -85.3 28 ILE -128.4 162.9 -177.7 56.6 -173.4 29 SER -76.9 161.5 -176.4 92.7 30 GLU -61.3 -42.3 -178.3 -72.0 179.0 53.1 31 LYS -60.6 -37.5 175.3 -165.4 171.4 -125.8 153.7 32 THR -65.3 -43.8 176.7 -73.0 33 VAL -59.9 -43.1 177.1 176.2 34 ARG -69.6 -36.0 175.0 -67.1 155.9 56.5 -126.2 35 ASN -61.6 -44.5 174.4 -73.5 -18.8 36 HIS -56.2 -37.9 -179.4 -75.6 -37.9 37 ILE -68.5 -48.9 178.3 -72.0 162.5 38 SER -59.8 -42.5 -178.2 -43.6 39 ASN -63.4 -44.7 175.7 -77.5 -22.9 40 ALA -61.6 -34.0 177.4 41 MET -66.5 -39.7 179.6 -76.6 170.3 41.3 42 GLN -64.2 -41.6 179.5 -131.7 139.1 -101.6 43 LYS -70.3 -24.1 177.6 -71.8 -171.8 -66.2 -153.0 44 LEU -87.1 -15.3 179.5 -76.9 169.0 45 GLY 75.3 29.1 -179.9 46 VAL -125.7 167.7 -171.2 -56.2 47 LYS -110.2 3.1 -177.7 0.0 0.0 0.0 0.0 48 GLY -156.6 169.5 -171.2 49 ARG -67.7 -45.3 178.9 -159.4 134.6 107.2 -171.0 50 SER -68.1 -36.4 175.8 76.2 51 GLN -61.9 -36.5 178.6 -58.2 93.6 -57.6 52 ALA -66.0 -52.4 177.1 53 VAL -57.0 -45.8 -179.4 164.4 54 VAL -60.3 -52.5 177.8 162.0 55 GLU -53.4 -44.7 177.3 -106.6 -66.6 -76.8 56 LEU -60.6 -36.1 -179.6 -60.9 174.5 57 LEU -71.2 -34.8 180.0 -70.1 161.0 58 ARG -67.1 -34.4 -179.0 -84.6 -169.0 -158.6 -75.6 59 MET -78.7 -19.4 -172.0 -57.0 171.7 155.8 60 GLY 89.1 0.6 178.9 61 GLU -68.5 -35.8 -179.7 -84.2 -51.9 -35.8 62 LEU -111.4 149.7 -178.4 -132.8 28.0 63 GLU 24.3 86.4 174.5 -178.4 -147.8 -77.2 64 LEU -164.7 1.7 0.0 -109.6 -37.4 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 LEU 14.379 -1.383 42.163 2 LEU 17.290 -3.576 41.040 3 THR 18.462 -6.806 42.704 4 LYS 22.132 -7.050 43.705 5 ARG 23.248 -9.015 40.620 6 GLU 21.155 -6.830 38.326 7 ARG 23.125 -3.892 39.705 8 GLU 26.511 -5.500 39.167 9 VAL 25.475 -6.429 35.639 10 PHE 24.557 -2.832 34.757 11 GLU 27.718 -1.478 36.469 12 LEU 29.672 -3.727 34.075 13 LEU 27.551 -2.654 31.090 14 VAL 28.710 0.909 31.349 15 GLN 32.343 -0.028 31.559 16 ASP 32.086 -1.234 27.967 17 LYS 31.848 -4.977 28.476 18 THR 29.952 -7.537 26.448 19 THR 27.307 -9.793 27.924 20 LYS 29.856 -12.559 27.569 21 GLU 32.568 -10.568 29.376 22 ILE 30.041 -9.796 32.105 23 ALA 29.186 -13.491 32.302 24 SER 32.885 -14.171 32.596 25 GLU 33.425 -11.686 35.426 26 LEU 30.365 -12.627 37.506 27 PHE 30.926 -16.343 36.869 28 ILE 27.346 -16.760 35.511 29 SER 26.089 -17.791 32.040 30 GLU 25.337 -15.346 29.241 31 LYS 21.625 -16.236 29.281 32 THR 21.468 -15.349 32.999 33 VAL 23.178 -11.988 32.328 34 ARG 20.646 -11.161 29.617 35 ASN 17.793 -12.316 31.845 36 HIS 19.013 -9.915 34.533 37 ILE 18.955 -7.165 31.907 38 SER 15.467 -8.004 30.677 39 ASN 14.055 -8.313 34.200 40 ALA 15.520 -4.901 35.065 41 MET 14.026 -3.538 31.832 42 GLN 10.548 -4.762 32.783 43 LYS 10.704 -3.152 36.244 44 LEU 11.859 0.099 34.606 45 GLY 9.025 0.215 32.084 46 VAL 11.316 0.447 29.057 47 LYS 11.901 -1.570 25.888 48 GLY 15.634 -1.686 25.298 49 ARG 19.057 -1.839 26.865 50 SER 20.117 1.726 26.288 51 GLN 16.725 3.053 27.424 52 ALA 17.324 1.013 30.569 53 VAL 20.833 2.378 31.072 54 VAL 19.657 5.956 30.390 55 GLU 16.723 5.772 32.808 56 LEU 19.002 4.430 35.517 57 LEU 21.454 7.289 35.078 58 ARG 18.561 9.713 35.184 59 MET 17.398 8.228 38.461 60 GLY 20.855 8.349 40.041 61 GLU 20.702 4.549 40.430 62 LEU 23.628 4.095 38.043 63 GLU 27.034 5.825 37.983 64 LEU 26.202 8.549 40.528 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C C H H H H H H H H 10 H H H H H H C H H H 20 H H H H H H H C H H 30 H H H H H H H H H H 40 H H H H H/S S S S/H H H 50 H H H H H H H H H H/T 60 T T T/S 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 10 H H H h T T t h H H 20 H H H H H h T t h H 30 H H H H H H H H H H 40 H H H H h t S h H H 50 H H H H H H H H h T 60 t S Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 LEU 21.3 14.4 81.5 2 LEU 146.6 99.2 44.8 3 THR 33.6 31.4 81.2 4 LYS 44.5 25.7 83.2 5 ARG 119.2 57.1 60.4 6 GLU 134.3 96.9 47.9 7 ARG 155.9 74.6 65.1 8 GLU 77.3 55.8 60.2 9 VAL 118.8 100.0 29.7 10 PHE 166.8 100.0 32.4 11 GLU 61.3 44.2 61.3 12 LEU 129.2 87.4 52.0 13 LEU 135.7 91.8 46.4 14 VAL 89.7 75.5 55.2 15 GLN 50.8 34.2 66.1 16 ASP 0.0 0.0 88.4 17 LYS 114.0 65.7 68.8 18 THR 54.6 51.1 63.9 19 THR 87.7 82.0 56.3 20 LYS 54.6 31.5 76.2 21 GLU 64.6 46.6 64.5 22 ILE 143.5 100.0 34.6 23 ALA 66.0 90.9 54.9 24 SER 13.9 16.6 82.1 25 GLU 51.1 36.9 65.3 26 LEU 131.9 89.2 48.6 27 PHE 13.6 8.1 92.0 28 ILE 105.7 73.6 56.6 29 SER 23.3 27.8 75.2 30 GLU 57.1 41.2 67.0 31 LYS 31.5 18.2 90.3 32 THR 56.5 52.9 67.5 33 VAL 118.8 100.0 33.3 34 ARG 89.8 43.0 69.4 35 ASN 41.5 34.3 74.0 36 HIS 112.1 74.6 51.9 37 ILE 137.7 96.0 33.3 38 SER 32.7 39.1 72.5 39 ASN 46.0 38.1 78.5 40 ALA 72.6 100.0 44.0 41 MET 124.6 78.2 56.5 42 GLN 17.5 11.8 87.9 43 LYS 111.4 64.2 64.1 44 LEU 140.5 95.0 43.1 45 GLY 0.0 0.0 83.0 46 VAL 94.0 79.1 55.4 47 LYS 108.0 62.3 78.2 48 GLY 20.8 59.9 67.4 49 ARG 113.5 54.3 51.2 50 SER 9.8 11.7 78.2 51 GLN 60.1 40.5 70.7 52 ALA 72.6 100.0 37.8 53 VAL 94.9 79.9 37.0 54 VAL 50.6 42.6 68.9 55 GLU 89.6 64.7 50.7 56 LEU 147.6 99.9 27.0 57 LEU 95.8 64.8 61.3 58 ARG 46.9 22.4 81.6 59 MET 79.3 49.8 70.1 60 GLY 21.0 60.2 66.8 61 GLU 81.1 58.5 66.9 62 LEU 145.4 98.4 38.0 63 GLU 14.2 10.3 74.5 64 LEU 53.0 35.8 75.5