Protein Data Bank File : 1swub Title : PROTEIN BINDING 12-OCT-98 1SWU Number of Amino Acid Residues : 116 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 ALA GLY ILE THR GLY THR TRP TYR ASN GLN 10 LEU GLY SER THR PHE ILE VAL THR ALA GLY 20 ALA ASP GLY ALA LEU THR GLY THR PHE GLU 30 SER ASN ALA GLU SER ARG TYR VAL LEU THR 40 GLY ARG TYR ASP SER ALA PRO ALA THR ASP 50 GLY SER GLY THR ALA LEU GLY TRP THR VAL 60 ALA TRP LYS ASN ASN TYR ARG ASN ALA HIS 70 SER ALA THR THR TRP SER GLY GLN TYR VAL 80 GLY GLY ALA GLU ALA ARG ILE ASN THR GLN 90 TRP LEU LEU THR SER GLY THR THR GLU ALA 100 ASN ALA TRP LYS SER THR LEU VAL GLY HIS 110 ASP THR PHE THR LYS VAL Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 ALA 0.0 -36.0 -177.4 2 GLY 74.2 7.6 -174.5 3 ILE -92.4 -40.7 -179.5 -63.2 164.2 4 THR -52.7 133.2 174.3 -66.4 5 GLY 132.6 -159.9 -173.0 6 THR -102.5 135.1 -179.2 -58.7 7 TRP -129.3 151.1 -176.3 -66.6 86.9 8 TYR -130.0 137.4 167.4 -56.1 99.7 9 ASN -89.3 -169.5 180.0 76.8 -5.2 10 GLN -101.1 13.2 -174.3 35.0 -93.7 86.7 11 LEU -121.1 13.9 175.6 -74.7 -169.3 12 GLY 93.5 11.2 175.7 13 SER -101.8 152.7 -180.0 -63.6 14 THR -133.0 143.5 160.6 -53.4 15 PHE -137.9 175.6 -174.7 66.7 84.2 16 ILE -141.0 124.1 -173.7 -151.5 -170.4 17 VAL -137.5 146.5 166.4 68.3 18 THR -113.8 127.1 176.8 -62.5 19 ALA -98.1 103.7 -172.7 20 GLY -76.8 163.2 -177.5 21 ALA -61.2 -26.9 -170.0 22 ASP -95.1 5.8 178.4 64.5 -20.7 23 GLY 89.5 6.6 178.9 24 ALA -81.9 146.3 164.5 25 LEU -114.8 129.1 177.4 -57.6 175.5 26 THR -138.8 143.7 175.4 58.3 27 GLY 167.7 -150.2 -175.7 28 THR -137.9 146.3 174.4 -58.4 29 PHE -117.4 131.6 -175.4 -163.4 -82.5 30 GLU -141.8 -175.7 159.2 52.1 -143.4 162.9 31 SER -81.9 -76.6 26.4 100.7 32 ASN 26.8 159.7 -175.4 53.7 -57.7 33 ALA -58.2 -36.5 -174.9 34 GLU -67.5 -14.7 -179.0 -69.4 84.4 -6.4 35 SER -105.0 9.5 -178.1 -71.0 36 ARG -105.4 137.2 -176.6 -69.6 -173.7 -164.6 116.8 37 TYR -137.7 150.0 174.5 -56.3 81.5 38 VAL -69.4 139.7 171.4 171.9 39 LEU -124.4 147.0 175.9 72.6 99.5 40 THR -147.8 143.4 177.9 -171.8 41 GLY -168.0 -162.3 -175.3 42 ARG -140.7 152.7 174.3 -57.5 -72.8 -62.3 160.6 43 TYR -141.7 159.2 173.1 73.6 -75.3 44 ASP -73.6 106.8 -177.1 -179.8 2.9 45 SER -81.6 -2.7 178.0 66.6 46 ALA -136.3 64.7 -175.5 47 PRO -64.6 164.1 -179.8 25.1 -35.1 48 ALA -63.4 161.4 179.7 49 THR -113.4 32.5 175.5 59.8 50 ASP -109.0 15.9 179.9 65.2 5.1 51 GLY 94.9 -3.0 179.0 52 SER -73.0 158.0 176.6 -66.7 53 GLY -76.9 178.6 -175.9 54 THR -104.9 112.4 -178.0 -60.4 55 ALA -67.6 144.6 177.9 56 LEU -160.1 166.2 169.4 40.1 74.5 57 GLY -160.8 160.9 176.7 58 TRP -154.1 164.9 -179.7 68.5 88.8 59 THR -125.6 141.3 163.1 -53.5 60 VAL -124.5 122.9 163.2 171.8 61 ALA -87.2 128.6 -170.7 62 TRP -85.9 56.2 176.4 -61.7 108.1 63 LYS -128.5 131.6 168.8 173.5 -174.1 175.8 -2.5 64 ASN -139.0 -167.7 -176.9 62.9 21.2 65 ASN -72.1 -7.8 -171.1 -73.6 -9.0 66 TYR -115.5 -19.4 -175.3 -50.6 -78.3 67 ARG -163.9 162.9 -177.1 65.6 167.9 131.2 179.6 68 ASN -150.1 106.6 -179.6 -167.6 -8.0 69 ALA -87.9 3.0 179.1 70 HIS 49.3 53.1 -175.3 -57.9 -49.7 71 SER -157.3 164.3 177.7 66.4 72 ALA -146.9 141.4 172.3 73 THR -112.0 135.8 165.1 -59.9 74 THR -112.7 134.0 172.5 64.4 75 TRP -107.0 127.2 176.2 -65.2 -103.0 76 SER -122.2 129.0 -174.1 -178.5 77 GLY -170.7 -158.3 177.2 78 GLN -145.4 146.9 173.6 54.2 -175.6 135.2 79 TYR -89.6 133.2 177.3 161.8 84.3 80 VAL -120.8 118.3 -177.4 -173.0 81 GLY -86.2 -164.6 178.0 82 GLY 103.2 -170.7 -171.5 83 ALA -55.1 -37.6 -176.2 84 GLU -115.1 70.5 -171.8 -53.4 -59.3 171.6 85 ALA -70.3 149.6 -173.5 86 ARG -150.1 154.8 165.3 -28.4 65.6 156.1 -69.2 87 ILE -117.3 113.3 -178.4 -62.2 171.0 88 ASN -100.5 121.1 -174.8 -65.4 -41.2 89 THR -129.4 158.5 159.1 74.3 90 GLN -118.3 152.8 -172.3 -59.2 -173.5 -95.0 91 TRP -140.5 155.8 175.9 56.9 -103.7 92 LEU -127.3 122.7 177.1 -61.9 168.4 93 LEU -110.9 111.9 176.5 160.5 60.7 94 THR -104.7 129.2 170.4 -49.8 95 SER -99.7 142.5 166.9 -66.9 96 GLY -61.8 130.3 -180.0 97 THR -135.2 165.4 162.4 69.6 98 THR -71.7 164.7 179.8 61.9 99 GLU -61.9 -34.7 178.3 -77.1 -63.0 100.5 100 ALA -63.1 -25.6 180.0 101 ASN -103.9 8.5 -173.7 -66.7 -38.2 102 ALA -65.2 -28.1 177.7 103 TRP -58.5 -28.8 -177.9 69.3 -86.1 104 LYS -110.1 26.7 -178.2 53.6 174.1 177.0 176.3 105 SER -80.5 -18.8 -165.3 65.3 106 THR -130.1 120.6 169.1 -49.1 107 LEU -92.2 148.8 174.5 -65.4 165.2 108 VAL -124.5 148.1 174.8 61.1 109 GLY -165.5 -167.4 -179.5 110 HIS -139.3 152.3 172.8 46.2 93.5 111 ASP -156.8 143.5 -178.2 -150.7 1.9 112 THR -113.9 130.5 179.0 -61.4 113 PHE -110.7 141.9 177.2 -63.8 -88.3 114 THR -131.1 166.4 -178.1 62.9 115 LYS -85.3 -13.0 177.7 -71.7 -157.6 -172.2 -175.0 116 VAL -123.4 155.8 0.0 -37.5 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 ALA 36.484 0.209 24.915 2 GLY 37.669 -1.561 21.673 3 ILE 35.697 0.700 19.361 4 THR 38.257 3.206 18.072 5 GLY 39.520 2.360 14.584 6 THR 38.304 1.260 11.178 7 TRP 35.266 -0.948 10.585 8 TYR 33.881 -2.566 7.441 9 ASN 30.413 -3.813 6.463 10 GLN 29.914 -6.487 3.833 11 LEU 28.731 -4.084 1.081 12 GLY 31.826 -1.992 0.490 13 SER 31.382 0.684 3.220 14 THR 34.038 1.744 5.749 15 PHE 34.027 3.949 8.593 16 ILE 36.581 5.279 10.850 17 VAL 35.678 6.250 14.406 18 THR 37.224 7.564 17.589 19 ALA 35.515 6.596 20.864 20 GLY 36.288 9.481 23.259 21 ALA 36.686 9.086 27.015 22 ASP 33.445 11.071 27.477 23 GLY 31.202 8.752 25.421 24 ALA 31.561 10.556 22.109 25 LEU 31.832 8.886 18.722 26 THR 33.419 11.009 15.967 27 GLY 34.672 10.089 12.515 28 THR 33.892 9.524 8.867 29 PHE 31.745 7.081 6.879 30 GLU 32.832 6.241 3.285 31 SER 33.103 3.816 0.420 32 ASN 37.140 8.839 -2.731 33 ALA 36.265 12.177 -1.240 34 GLU 32.852 12.336 -2.899 35 SER 31.888 9.215 -0.902 36 ARG 33.048 10.454 2.556 37 TYR 30.647 11.932 5.163 38 VAL 30.922 13.160 8.739 39 LEU 29.651 10.835 11.450 40 THR 28.856 11.638 15.079 41 GLY 27.293 9.554 17.864 42 ARG 27.465 8.270 21.420 43 TYR 28.400 5.045 23.194 44 ASP 28.147 3.620 26.719 45 SER 31.609 4.327 28.242 46 ALA 30.905 2.175 31.319 47 PRO 29.237 -1.042 29.975 48 ALA 27.980 -3.797 32.186 49 THR 30.481 -6.403 33.359 50 ASP 28.221 -9.428 32.836 51 GLY 29.265 -10.363 29.269 52 SER 26.801 -7.993 27.619 53 GLY 27.782 -5.870 24.597 54 THR 28.315 -2.119 24.592 55 ALA 25.359 0.009 23.384 56 LEU 26.102 2.720 20.844 57 GLY 24.618 4.702 17.980 58 TRP 25.616 7.246 15.348 59 THR 24.255 9.457 12.565 60 VAL 25.379 10.331 9.049 61 ALA 23.604 13.098 7.151 62 TRP 24.204 12.272 3.470 63 LYS 25.521 15.731 2.588 64 ASN 29.178 16.547 1.918 65 ASN 30.901 19.240 -0.162 66 TYR 30.166 17.284 -3.360 67 ARG 26.597 16.003 -3.036 68 ASN 23.424 16.066 -1.016 69 ALA 20.900 13.211 -0.889 70 HIS 18.627 15.151 1.539 71 SER 18.629 12.171 3.896 72 ALA 20.166 10.844 7.090 73 THR 20.887 7.372 8.465 74 THR 21.039 6.461 12.140 75 TRP 22.647 3.181 13.280 76 SER 21.666 1.830 16.693 77 GLY 23.429 -1.263 17.968 78 GLN 25.998 -2.843 20.229 79 TYR 29.725 -3.606 20.095 80 VAL 30.689 -7.185 20.909 81 GLY 34.339 -7.760 21.759 82 GLY 36.418 -10.941 21.703 83 ALA 38.203 -12.991 19.128 84 GLU 35.681 -11.979 16.498 85 ALA 34.763 -8.380 17.442 86 ARG 31.716 -6.945 15.721 87 ILE 29.354 -3.965 15.779 88 ASN 25.816 -5.326 15.196 89 THR 23.357 -2.627 14.126 90 GLN 19.908 -1.844 12.894 91 TRP 19.448 1.410 10.996 92 LEU 16.832 3.983 9.904 93 LEU 17.321 6.085 6.739 94 THR 14.979 9.082 6.595 95 SER 14.672 11.213 3.459 96 GLY 13.207 14.689 3.462 97 THR 9.778 14.472 1.898 98 THR 6.616 16.483 1.442 99 GLU 3.906 15.612 3.925 100 ALA 2.037 13.741 1.148 101 ASN 5.047 11.451 0.709 102 ALA 5.938 11.089 4.442 103 TRP 4.593 7.531 4.562 104 LYS 7.470 6.471 2.341 105 SER 10.195 8.603 3.990 106 THR 11.994 5.930 6.056 107 LEU 13.889 2.755 5.171 108 VAL 14.926 0.203 7.804 109 GLY 17.700 -2.368 7.658 110 HIS 20.598 -4.021 9.429 111 ASP 24.330 -4.099 9.048 112 THR 27.207 -5.852 10.779 113 PHE 30.678 -4.309 10.953 114 THR 33.973 -6.129 11.448 115 LYS 37.606 -5.088 11.787 116 VAL 38.756 -7.026 8.730 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C C C S S S S S S/T T 10 T T/S S S S S S S S S/T 20 T T T/S S S S S S S S 30 S/X X/T T T T/S S S S S S 40 S S S S S S S S/T T T 50 T/S S S S S S S S S S 60 S S S T T T T C C S 70 S S S S S S S S S S 80 S S S S S S S S S S 90 S S S S S S S S/T T T 100 T/T T T T S S S S S S 110 S S 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 S 10 S S e E E E E E E e 20 T T e E E E E E E E 30 g G G G g E E E E 40 E E E e S S S S 50 S E E E E E E E 60 E E E e S S e E E E 70 E E E E E E E E E E 80 t T T e E E E E E 90 E E E E E e g G G 100 G G G G e E E E E E 110 E E E E e Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 ALA 32.5 44.7 74.9 2 GLY 9.6 27.6 76.9 3 ILE 142.0 99.0 27.3 4 THR 45.6 42.7 70.8 5 GLY 9.1 26.2 73.0 6 THR 70.4 65.9 52.9 7 TRP 204.9 99.9 39.4 8 TYR 99.4 54.9 72.3 9 ASN 113.3 93.8 60.4 10 GLN 40.0 26.9 79.9 11 LEU 22.6 15.3 87.2 12 GLY 0.0 0.0 86.5 13 SER 59.9 71.7 67.0 14 THR 86.0 80.5 54.8 15 PHE 164.6 98.7 27.0 16 ILE 56.6 39.4 74.1 17 VAL 115.6 97.3 42.7 18 THR 34.2 32.0 74.3 19 ALA 71.8 98.9 47.4 20 GLY 14.6 42.0 74.5 21 ALA 0.0 0.0 90.2 22 ASP 21.2 19.2 77.2 23 GLY 32.8 94.3 69.1 24 ALA 48.9 67.4 67.0 25 LEU 145.4 98.4 36.5 26 THR 37.1 34.7 70.4 27 GLY 19.5 56.0 64.7 28 THR 66.4 62.1 57.9 29 PHE 154.2 92.4 38.2 30 GLU 104.8 75.6 53.2 31 SER 39.8 47.6 72.5 32 ASN 47.6 39.4 86.4 33 ALA 36.4 50.1 70.3 34 GLU 59.1 42.7 68.1 35 SER 65.2 78.0 74.9 36 ARG 105.5 50.5 68.5 37 TYR 164.3 90.7 56.2 38 VAL 5.4 4.5 84.1 39 LEU 147.1 99.5 42.3 40 THR 27.4 25.7 70.6 41 GLY 23.6 67.9 57.2 42 ARG 64.7 31.0 78.7 43 TYR 171.1 94.5 41.1 44 ASP 52.8 47.8 67.8 45 SER 49.8 59.6 70.6 46 ALA 3.4 4.7 83.6 47 PRO 82.2 66.0 79.5 48 ALA 25.7 35.3 78.4 49 THR 0.0 0.0 90.7 50 ASP 29.6 26.8 79.6 51 GLY 0.0 0.0 87.8 52 SER 33.2 39.7 82.6 53 GLY 29.9 85.8 71.2 54 THR 94.4 88.3 47.9 55 ALA 14.8 20.4 73.2 56 LEU 143.2 96.9 37.2 57 GLY 20.4 58.6 62.8 58 TRP 198.8 97.0 26.3 59 THR 57.9 54.1 57.6 60 VAL 118.6 99.8 37.6 61 ALA 22.1 30.5 66.2 62 TRP 159.1 77.6 47.3 63 LYS 63.9 36.9 78.9 64 ASN 101.3 83.8 59.9 65 ASN 10.2 8.4 80.0 66 TYR 84.2 46.5 69.4 67 ARG 85.8 41.1 80.9 68 ASN 79.0 65.3 60.7 69 ALA 24.4 33.7 76.4 70 HIS 28.0 18.6 87.2 71 SER 74.0 88.6 54.9 72 ALA 42.3 58.2 59.7 73 THR 101.0 94.5 40.9 74 THR 49.2 46.0 65.7 75 TRP 193.5 94.4 36.1 76 SER 11.1 13.2 80.5 77 GLY 22.3 64.1 63.7 78 GLN 68.8 46.3 68.6 79 TYR 156.6 86.5 46.6 80 VAL 77.3 65.0 74.0 81 GLY 22.5 64.7 63.4 82 GLY 0.0 0.0 82.4 83 ALA 0.4 0.6 81.9 84 GLU 11.4 8.2 86.3 85 ALA 63.4 87.3 60.3 86 ARG 120.6 57.7 64.8 87 ILE 142.0 98.9 28.5 88 ASN 74.1 61.3 64.7 89 THR 105.8 98.9 43.0 90 GLN 28.4 19.1 77.2 91 TRP 149.8 73.1 57.2 92 LEU 55.9 37.8 68.1 93 LEU 107.2 72.5 58.4 94 THR 45.5 42.6 74.4 95 SER 42.4 50.7 65.7 96 GLY 0.0 0.0 76.9 97 THR 82.4 77.1 61.2 98 THR 21.4 20.0 82.0 99 GLU 0.0 0.0 85.4 100 ALA 1.8 2.5 86.7 101 ASN 60.9 50.4 69.5 102 ALA 41.1 56.6 80.3 103 TRP 31.9 15.6 82.4 104 LYS 65.6 37.9 73.9 105 SER 67.9 81.3 69.5 106 THR 68.0 63.6 70.6 107 LEU 33.8 22.9 71.8 108 VAL 32.2 27.1 71.7 109 GLY 20.8 59.8 50.9 110 HIS 22.0 14.6 79.5 111 ASP 93.6 84.7 63.2 112 THR 61.4 57.4 68.6 113 PHE 166.7 99.9 40.3 114 THR 51.8 48.5 63.6 115 LYS 94.1 54.3 65.0 116 VAL 0.0 0.0 81.2