Protein Data Bank File : 1c3ma Title : SUGAR BINDING PROTEIN 28-JUL-99 1C3M Number of Amino Acid Residues : 145 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 ALA SER ASP ILE ALA VAL GLN ALA GLY PRO 10 TRP GLY GLY ASN GLY GLY LYS ARG TRP LEU 20 GLN THR ALA HIS GLY GLY LYS ILE THR SER 30 ILE ILE ILE LYS GLY GLY THR CYS ILE PHE 40 SER ILE GLN PHE VAL TYR LYS ASP LYS ASP 50 ASN ILE GLU TYR HIS SER GLY LYS PHE GLY 60 VAL LEU GLY ASP LYS ALA GLU THR ILE THR 70 PHE ALA GLU ASP GLU ASP ILE THR ALA ILE 80 SER GLY THR PHE GLY ALA TYR TYR HIS MET 90 THR VAL VAL THR SER LEU THR PHE GLN THR 100 ASN LYS LYS VAL TYR GLY PRO PHE GLY THR 110 VAL ALA SER SER SER PHE SER LEU PRO LEU 120 THR LYS GLY LYS PHE ALA GLY PHE PHE GLY 130 ASN SER GLY ASP VAL LEU ASP SER ILE GLY 140 GLY VAL VAL VAL PRO Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 ALA 0.0 31.3 -173.6 2 SER 19.2 53.0 174.2 -156.2 3 ASP -139.0 -63.5 179.3 161.8 -153.1 4 ILE -107.3 29.3 -178.1 77.4 147.7 5 ALA -80.4 -35.3 175.6 6 VAL -109.4 111.1 179.7 -170.7 7 GLN -113.4 106.5 -179.0 -61.0 -175.8 -174.6 8 ALA -94.7 127.2 -177.9 9 GLY 102.3 -148.5 0.1 10 PRO -83.4 170.8 177.5 37.5 -44.6 11 TRP -117.8 139.0 -177.5 -67.1 -90.6 12 GLY 129.1 -154.3 -177.7 13 GLY -95.1 -170.3 -176.9 14 ASN -106.6 -0.4 179.5 -63.6 -47.4 15 GLY -73.0 178.7 178.4 16 GLY 66.1 -172.4 -179.3 17 LYS -115.1 146.8 -179.3 -61.9 169.8 174.8 -179.1 18 ARG -63.7 135.1 177.9 175.1 57.2 45.1 88.8 19 TRP -139.9 161.5 178.6 56.2 -87.5 20 LEU -148.9 140.0 178.3 -178.9 135.3 21 GLN -144.8 118.5 176.3 -171.5 56.0 -114.6 22 THR -118.1 -179.9 -178.3 64.3 23 ALA -97.9 8.5 179.6 24 HIS 48.0 48.3 179.1 -62.9 -84.6 25 GLY 92.1 -13.0 -179.7 26 GLY -95.6 -128.1 -177.6 27 LYS -143.5 143.6 175.9 -156.5 -165.8 138.0 171.2 28 ILE -76.0 122.4 -178.7 -61.6 -58.2 29 THR -103.8 -29.0 177.3 55.3 30 SER -142.7 149.6 175.6 -70.0 31 ILE -125.4 126.8 178.2 -58.1 -179.8 32 ILE -111.2 112.5 -178.0 -63.4 143.8 33 ILE -114.0 130.2 176.4 -59.0 135.6 34 LYS -113.4 99.6 -178.3 -65.3 -169.4 -170.8 164.3 35 GLY -118.8 145.1 179.1 36 GLY -149.7 -118.5 178.5 37 THR -70.3 -15.4 174.7 61.6 38 CYS -154.0 -176.9 178.1 69.5 39 ILE -90.8 107.2 -177.6 -60.4 -56.8 40 PHE -80.1 -32.9 -175.6 -54.7 119.2 41 SER -159.3 145.4 176.2 -176.0 42 ILE -137.0 144.7 -178.6 -164.8 165.0 43 GLN -149.0 144.0 -177.5 -176.7 176.8 32.6 44 PHE -118.5 144.1 173.5 -48.8 89.0 45 VAL -114.1 137.5 180.0 178.3 46 TYR -147.8 163.8 179.0 62.7 91.5 47 LYS -120.7 139.4 179.0 -72.5 -171.2 -158.2 -57.2 48 ASP -86.2 -178.9 179.2 56.1 16.9 49 LYS -53.9 -22.2 -179.8 -78.5 -152.3 157.2 63.6 50 ASP -101.5 16.8 -179.6 -45.2 -64.0 51 ASN 66.9 19.8 174.2 -70.7 -60.5 52 ILE -81.9 136.8 -179.9 -64.2 90.1 53 GLU -94.7 137.1 -179.3 -172.0 174.5 76.2 54 TYR -132.2 153.6 175.3 -53.6 78.1 55 HIS -116.3 134.7 176.8 -66.7 60.4 56 SER -83.4 169.9 174.5 73.8 57 GLY -77.7 176.5 178.2 58 LYS -83.3 140.1 175.2 -70.0 -170.0 -163.7 47.5 59 PHE -114.8 110.0 -175.1 -51.6 108.9 60 GLY 101.9 133.5 -177.9 61 VAL -115.4 -9.9 178.9 -70.1 62 LEU -77.9 -173.9 -178.9 -66.4 -167.7 63 GLY 89.7 144.2 179.2 64 ASP -110.1 -72.2 179.6 39.3 -80.2 65 LYS -67.5 150.4 -179.2 148.9 -112.8 -51.0 -175.0 66 ALA -136.9 151.7 176.9 67 GLU -120.5 139.1 -178.3 -81.1 152.0 -73.2 68 THR -128.7 132.7 175.0 -67.2 69 ILE -115.3 132.6 -179.4 57.5 -171.9 70 THR -124.5 122.9 -176.3 -61.0 71 PHE -83.8 149.9 175.8 -47.9 121.1 72 ALA -69.4 163.0 -178.0 73 GLU -67.2 -23.4 178.5 -88.5 141.1 59.0 74 ASP -108.4 29.4 179.2 59.2 159.5 75 GLU -116.0 133.3 178.5 168.8 165.8 35.3 76 ASP -134.6 148.9 177.9 -88.9 -75.6 77 ILE -70.6 134.3 -179.7 -59.2 163.3 78 THR -119.3 -11.1 178.6 58.7 79 ALA -165.3 150.3 174.1 80 ILE -133.3 150.0 179.5 58.4 173.3 81 SER -155.5 171.1 -179.6 55.2 82 GLY 174.2 -163.5 179.7 83 THR -140.4 157.5 174.9 60.6 84 PHE -137.4 155.8 -178.7 51.9 95.2 85 GLY -178.0 -173.1 -178.0 86 ALA -68.8 137.2 177.3 87 TYR -139.5 101.0 -175.3 173.6 62.9 88 TYR 63.6 -131.1 -177.3 -76.4 61.6 89 HIS -110.2 33.1 178.4 -69.7 54.0 90 MET -132.2 156.5 -179.7 29.5 -164.4 49.8 91 THR -97.4 124.9 -178.4 -60.3 92 VAL -138.9 172.6 177.6 -58.0 93 VAL -74.9 126.3 -178.3 178.3 94 THR -101.5 -30.3 177.3 48.0 95 SER -149.2 155.6 -179.5 66.5 96 LEU -138.6 146.2 176.8 -76.3 172.5 97 THR -134.8 137.0 177.6 -65.9 98 PHE -118.6 137.4 178.8 -61.3 83.9 99 GLN -119.9 137.1 178.8 -169.1 -172.0 -60.4 100 THR -126.7 -179.2 178.7 64.2 101 ASN -71.0 -8.4 -180.0 50.3 -27.0 102 LYS -106.5 -37.0 -179.7 -56.5 -60.7 -162.8 55.1 103 LYS -172.6 178.6 179.7 70.3 137.9 149.7 -68.1 104 VAL -105.6 134.8 178.5 -177.7 105 TYR -115.5 137.3 -179.7 -61.0 85.8 106 GLY 100.9 -164.9 0.4 107 PRO -63.4 148.7 177.4 34.8 -41.4 108 PHE -110.9 144.7 -178.5 -63.7 95.5 109 GLY 79.9 -153.1 -177.6 110 THR -118.5 124.8 -179.4 -52.4 111 VAL -66.7 99.4 -179.7 -178.4 112 ALA -82.3 -169.4 -175.6 113 SER -79.9 -40.9 -179.0 -169.5 114 SER -90.3 121.6 179.2 -71.0 115 SER -95.9 159.4 174.9 -59.3 116 PHE -150.3 149.4 -179.7 69.1 80.7 117 SER -144.4 134.2 177.0 -165.7 118 LEU -134.8 82.9 179.0 -152.6 -142.8 119 PRO -89.8 154.3 179.4 31.5 -34.7 120 LEU -115.6 122.3 176.4 -64.2 -173.6 121 THR -82.2 -25.1 -178.5 -71.8 122 LYS -150.6 140.8 179.8 -164.9 89.4 89.5 51.1 123 GLY 110.1 -178.7 -178.5 124 LYS -144.4 162.5 175.5 -51.2 174.2 -58.5 162.8 125 PHE -88.8 111.2 176.7 -74.8 85.1 126 ALA -77.9 -20.0 -178.5 127 GLY 171.7 -155.7 -177.6 128 PHE -143.8 164.4 178.1 -60.2 -80.8 129 PHE -152.7 172.7 -179.9 75.9 102.4 130 GLY 161.1 -156.0 -179.6 131 ASN -127.8 145.2 177.9 -85.9 47.5 132 SER -153.0 157.0 179.0 76.0 133 GLY -147.7 -108.2 178.0 134 ASP -75.0 -37.0 179.7 -82.0 167.0 135 VAL -128.0 -172.9 -179.7 -60.2 136 LEU -89.6 100.7 -179.0 -177.1 63.5 137 ASP -66.7 -41.2 -179.3 -63.9 -100.9 138 SER -158.9 161.7 179.1 70.8 139 ILE -151.8 148.7 177.9 -171.3 157.6 140 GLY -147.4 179.6 -179.5 141 GLY -114.1 147.6 178.4 142 VAL -107.0 106.7 -175.6 179.8 143 VAL -108.5 143.2 179.5 -53.2 144 VAL -136.4 162.8 179.7 -65.6 145 PRO -57.4 141.6 0.0 -31.1 42.0 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 ALA 40.420 45.345 36.667 2 SER 39.081 48.111 34.318 3 ASP 38.286 45.199 32.168 4 ILE 35.719 44.859 35.031 5 ALA 36.147 48.254 36.823 6 VAL 32.915 50.012 35.767 7 GLN 29.779 47.951 36.356 8 ALA 26.572 49.811 35.419 9 GLY 23.314 48.430 36.739 10 PRO 22.116 45.671 37.152 11 TRP 18.393 45.968 36.482 12 GLY 16.019 43.251 37.619 13 GLY 15.681 41.348 40.884 14 ASN 17.866 40.243 43.796 15 GLY 17.628 36.522 43.429 16 GLY 20.244 34.146 42.146 17 LYS 23.991 34.396 42.251 18 ARG 26.315 37.008 40.807 19 TRP 28.127 36.272 37.541 20 LEU 30.318 38.234 35.210 21 GLN 31.512 37.648 31.640 22 THR 33.843 39.778 29.571 23 ALA 35.684 39.277 26.329 24 HIS 39.080 39.475 28.098 25 GLY 40.264 42.333 25.906 26 GLY 38.675 40.995 22.740 27 LYS 35.095 41.177 21.505 28 ILE 31.676 39.589 22.255 29 THR 30.808 37.867 18.930 30 SER 27.518 36.026 19.632 31 ILE 24.755 36.156 22.125 32 ILE 22.644 33.040 22.648 33 ILE 19.276 33.902 24.302 34 LYS 16.539 31.503 25.532 35 GLY 13.504 33.738 25.988 36 GLY 9.856 33.056 26.672 37 THR 7.685 34.640 29.333 38 CYS 11.074 35.897 30.703 39 ILE 14.793 35.500 29.836 40 PHE 15.503 31.968 30.962 41 SER 19.091 31.818 29.871 42 ILE 21.876 33.879 28.279 43 GLN 25.254 32.749 26.928 44 PHE 28.166 34.472 25.173 45 VAL 30.674 33.582 22.486 46 TYR 33.709 35.848 22.357 47 LYS 37.180 36.334 20.826 48 ASP 40.247 37.496 22.760 49 LYS 42.757 39.903 21.191 50 ASP 44.294 37.006 19.155 51 ASN 41.039 35.733 17.655 52 ILE 40.693 32.534 19.668 53 GLU 36.977 31.942 20.152 54 TYR 35.501 31.080 23.562 55 HIS 32.118 30.157 24.972 56 SER 30.983 31.291 28.407 57 GLY 28.858 28.978 30.550 58 LYS 25.063 29.452 30.595 59 PHE 23.632 32.035 33.018 60 GLY 20.119 30.893 33.779 61 VAL 19.529 27.210 33.080 62 LEU 15.903 26.841 32.036 63 GLY 14.498 27.254 28.525 64 ASP 14.352 24.955 25.445 65 LYS 14.285 26.958 22.175 66 ALA 17.044 29.566 21.391 67 GLU 17.737 32.660 19.318 68 THR 21.284 33.560 18.402 69 ILE 22.628 36.848 17.158 70 THR 26.089 36.836 15.676 71 PHE 27.758 40.184 14.976 72 ALA 29.661 41.303 11.894 73 GLU 33.341 42.112 12.582 74 ASP 32.890 45.858 12.453 75 GLU 29.749 45.699 14.590 76 ASP 29.683 46.623 18.300 77 ILE 26.967 46.846 20.930 78 THR 26.138 50.492 21.653 79 ALA 23.155 50.030 23.945 80 ILE 21.230 47.413 25.829 81 SER 17.769 47.858 27.189 82 GLY 14.991 45.673 28.444 83 THR 12.285 45.158 30.999 84 PHE 12.053 43.307 34.271 85 GLY 8.965 42.209 36.174 86 ALA 7.198 39.474 38.063 87 TYR 7.811 35.889 37.059 88 TYR 5.903 33.809 39.557 89 HIS 6.771 35.544 42.765 90 MET 10.220 36.920 41.905 91 THR 11.460 39.861 39.799 92 VAL 13.571 38.794 36.834 93 VAL 14.662 40.125 33.466 94 THR 11.707 39.603 31.125 95 SER 12.990 40.988 27.833 96 LEU 16.270 42.256 26.396 97 THR 17.112 44.322 23.366 98 PHE 20.547 44.845 21.920 99 GLN 21.537 47.724 19.760 100 THR 24.661 47.919 17.674 101 ASN 26.106 50.399 15.180 102 LYS 24.363 48.268 12.484 103 LYS 20.912 47.454 13.908 104 VAL 18.530 46.621 16.759 105 TYR 18.003 43.001 17.835 106 GLY 14.958 41.889 19.815 107 PRO 12.996 42.357 21.926 108 PHE 13.683 38.797 23.132 109 GLY 11.413 37.347 25.838 110 THR 8.350 39.313 27.023 111 VAL 8.058 43.110 27.335 112 ALA 7.069 43.671 31.008 113 SER 6.298 46.886 32.784 114 SER 9.615 48.221 34.071 115 SER 12.101 49.448 31.514 116 PHE 15.794 50.132 31.812 117 SER 18.057 51.515 29.130 118 LEU 21.855 51.770 28.894 119 PRO 23.094 53.510 25.688 120 LEU 26.752 54.553 25.463 121 THR 27.662 57.871 23.902 122 LYS 31.360 56.970 24.334 123 GLY 32.914 53.676 25.404 124 LYS 32.198 49.975 24.817 125 PHE 30.682 46.965 26.466 126 ALA 33.609 44.792 27.571 127 GLY 30.916 42.411 28.806 128 PHE 27.996 41.874 31.144 129 PHE 27.262 40.843 34.668 130 GLY 24.227 40.178 36.782 131 ASN 22.542 37.484 38.795 132 SER 21.147 34.158 37.660 133 GLY 19.707 30.926 39.006 134 ASP 17.068 29.017 37.071 135 VAL 16.522 32.130 34.955 136 LEU 18.159 35.513 34.445 137 ASP 17.395 37.546 37.603 138 SER 19.202 40.745 36.595 139 ILE 21.709 42.107 34.115 140 GLY 24.024 45.063 33.745 141 GLY 26.958 46.159 31.597 142 VAL 30.686 46.104 32.141 143 VAL 31.807 49.233 30.258 144 VAL 35.248 50.458 29.214 145 PRO 36.796 53.364 27.201 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C T T T T/S S S S S/P C 10 S S S S S S S S S S 20 S S S/T T T T/S S S S S/S 30 S S S S S/T T T T C S 40 S 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 S S S S S S S S 70 S S S S S S S S S/S S 80 S S S S S S/T T T T/S S 90 S S S S S S S S S S/T 100 T T T/S S S S/P S C S S 110 S S S/S S S S S S S S 120 S/S S S S C C S S S S 130 S S/T T T T/S S S S/S S S 140 S S S S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S S E E E E E 10 E E e S S E E E E 20 E E e T T t E E E E 30 E E E E E e S e E E 40 E E E E E E E e T T 50 t e E E E e B S 60 S S E E E E 70 e t T T t e E E E E 80 E E E E E E E T T E 90 E E E E E E E E E E 100 e S e E E E E E E e 110 S E E E E E E e 120 S S E E E E E E E 130 E E e S e E E E E E 140 E E E E Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 ALA 4.7 6.5 79.8 2 SER 32.8 39.3 62.8 3 ASP 70.1 63.4 57.8 4 ILE 82.2 57.3 62.2 5 ALA 40.3 55.5 74.6 6 VAL 36.3 30.5 75.5 7 GLN 104.5 70.3 53.9 8 ALA 44.0 60.7 54.3 9 GLY 27.5 78.9 49.1 10 PRO 94.8 76.2 59.8 11 TRP 140.0 68.3 51.0 12 GLY 34.8 100.0 45.6 13 GLY 29.1 83.7 65.5 14 ASN 0.0 0.0 90.4 15 GLY 7.8 22.6 79.9 16 GLY 23.4 67.2 66.0 17 LYS 0.6 0.3 90.3 18 ARG 97.9 46.9 70.3 19 TRP 184.1 89.8 43.0 20 LEU 108.5 73.4 48.5 21 GLN 123.4 83.0 47.6 22 THR 105.3 98.5 49.9 23 ALA 70.0 96.4 56.1 24 HIS 51.5 34.3 84.3 25 GLY 7.1 20.3 80.5 26 GLY 27.8 79.9 64.4 27 LYS 124.3 71.7 67.5 28 ILE 139.2 97.0 38.9 29 THR 90.9 85.0 48.2 30 SER 73.9 88.4 47.1 31 ILE 143.5 100.0 24.2 32 ILE 109.7 76.5 51.8 33 ILE 143.5 100.0 32.4 34 LYS 139.0 80.2 58.5 35 GLY 34.8 99.9 57.0 36 GLY 15.0 43.1 63.1 37 THR 19.4 18.1 70.8 38 CYS 99.2 100.0 40.8 39 ILE 143.5 100.0 38.9 40 PHE 134.1 80.4 55.2 41 SER 81.8 97.9 53.4 42 ILE 143.2 99.8 28.1 43 GLN 114.4 77.0 52.4 44 PHE 166.1 99.6 25.0 45 VAL 108.1 91.0 55.5 46 TYR 163.7 90.5 50.3 47 LYS 112.4 64.8 65.9 48 ASP 93.3 84.4 61.5 49 LYS 28.1 16.2 84.0 50 ASP 18.6 16.9 78.3 51 ASN 24.9 20.6 77.2 52 ILE 56.7 39.5 77.3 53 GLU 71.3 51.4 68.9 54 TYR 96.1 53.1 67.7 55 HIS 62.2 41.4 71.8 56 SER 79.1 94.6 54.6 57 GLY 0.0 0.0 80.2 58 LYS 97.9 56.5 77.7 59 PHE 141.2 84.7 53.5 60 GLY 34.8 100.0 66.4 61 VAL 43.9 37.0 77.7 62 LEU 67.2 45.5 70.2 63 GLY 29.9 86.0 51.8 64 ASP 4.3 3.9 75.3 65 LYS 47.2 27.2 87.1 66 ALA 51.1 70.3 58.9 67 GLU 60.6 43.7 67.4 68 THR 59.3 55.5 66.2 69 ILE 129.3 90.1 34.2 70 THR 38.6 36.1 75.2 71 PHE 165.9 99.5 43.8 72 ALA 27.8 38.3 84.3 73 GLU 0.0 0.0 89.6 74 ASP 23.8 21.5 77.8 75 GLU 133.5 96.3 53.5 76 ASP 52.7 47.7 59.4 77 ILE 137.8 96.0 29.4 78 THR 65.5 61.2 63.3 79 ALA 62.6 86.2 55.6 80 ILE 141.8 98.8 31.3 81 SER 52.1 62.3 62.1 82 GLY 29.4 84.4 57.5 83 THR 98.3 91.9 59.5 84 PHE 122.1 73.2 55.0 85 GLY 19.2 55.2 59.8 86 ALA 15.8 21.8 84.4 87 TYR 135.6 74.9 46.3 88 TYR 24.9 13.8 80.0 89 HIS 0.0 0.0 85.1 90 MET 45.4 28.5 78.3 91 THR 57.5 53.8 58.4 92 VAL 118.8 100.0 44.6 93 VAL 118.8 100.0 42.1 94 THR 101.4 94.8 57.2 95 SER 81.8 97.9 50.2 96 LEU 147.2 99.6 25.7 97 THR 81.2 76.0 55.0 98 PHE 165.6 99.3 23.3 99 GLN 70.4 47.4 65.8 100 THR 106.9 100.0 48.7 101 ASN 60.0 49.6 68.4 102 LYS 94.5 54.5 77.2 103 LYS 52.7 30.4 77.0 104 VAL 50.8 42.8 63.3 105 TYR 152.5 84.3 49.6 106 GLY 30.7 88.1 56.2 107 PRO 58.1 46.7 72.1 108 PHE 151.5 90.8 44.8 109 GLY 33.2 95.4 62.2 110 THR 37.9 35.5 76.9 111 VAL 48.8 41.1 65.8 112 ALA 51.4 70.8 64.7 113 SER 0.0 0.0 86.4 114 SER 37.8 45.3 69.3 115 SER 21.5 25.7 73.5 116 PHE 157.3 94.3 41.6 117 SER 30.8 36.8 62.8 118 LEU 121.6 82.3 41.8 119 PRO 47.0 37.7 73.3 120 LEU 129.4 87.5 55.3 121 THR 0.0 0.0 85.0 122 LYS 8.0 4.6 88.4 123 GLY 28.8 82.8 62.7 124 LYS 74.5 43.0 77.2 125 PHE 165.4 99.1 39.7 126 ALA 56.9 78.4 59.4 127 GLY 34.8 100.0 44.1 128 PHE 166.2 99.6 22.2 129 PHE 164.1 98.4 45.6 130 GLY 34.8 100.0 53.5 131 ASN 104.5 86.4 70.7 132 SER 73.5 87.9 57.3 133 GLY 6.4 18.3 77.7 134 ASP 28.6 25.9 63.6 135 VAL 112.4 94.6 38.6 136 LEU 147.8 100.0 38.0 137 ASP 102.5 92.8 52.7 138 SER 82.4 98.6 50.2 139 ILE 142.5 99.3 25.8 140 GLY 34.8 100.0 43.1 141 GLY 34.8 100.0 37.3 142 VAL 118.8 100.0 45.1 143 VAL 96.7 81.4 43.9 144 VAL 99.6 83.8 58.7 145 PRO 17.3 13.9 79.9