Protein Data Bank File : 1qmva Title : PEROXIDASE 07-OCT-99 1QMV Number of Amino Acid Residues : 195 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 SER GLY ASN ALA ARG ILE GLY LYS PRO ALA 10 PRO ASP PHE LYS ALA THR ALA VAL VAL ASP 20 GLY ALA PHE LYS GLU VAL LYS LEU SER ASP 30 TYR LYS GLY LYS TYR VAL VAL LEU PHE PHE 40 TYR PRO LEU ASP PHE THR PHE VAL PRO THR 50 GLU ILE ILE ALA PHE SER ASN ARG ALA GLU 60 ASP PHE ARG LYS LEU GLY CYS GLU VAL LEU 70 GLY VAL SER VAL ASP SER GLN PHE THR HIS 80 LEU ALA TRP ILE ASN THR PRO ARG LYS GLU 90 GLY GLY LEU GLY PRO LEU ASN ILE PRO LEU 100 LEU ALA ASP VAL THR ARG ARG LEU SER GLU 110 ASP TYR GLY VAL LEU LYS THR ASP GLU GLY 120 ILE ALA TYR ARG GLY LEU PHE ILE ILE ASP 130 GLY LYS GLY VAL LEU ARG GLN ILE THR VAL 140 ASN ASP LEU PRO VAL GLY ARG SER VAL ASP 150 GLU ALA LEU ARG LEU VAL GLN ALA PHE GLN 160 TYR THR ASP GLU HIS GLY GLU VAL CYS PRO 170 ALA GLY TRP LYS PRO GLY SER ASP THR ILE 180 LYS PRO ASN VAL ASP ASP SER LYS GLU TYR 190 PHE SER LYS HIS ASN Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 SER 0.0 101.4 179.0 -160.6 2 GLY 67.0 -114.2 171.7 3 ASN -99.0 2.8 -178.1 -69.4 -40.9 4 ALA -88.6 122.1 -179.2 5 ARG -132.4 125.0 174.7 -65.0 -151.7 57.4 106.8 6 ILE -54.2 131.3 -179.3 -58.8 -143.2 7 GLY 90.4 -5.0 177.9 8 LYS -120.9 164.0 178.2 -82.3 124.7 -159.6 176.6 9 PRO -55.2 131.8 179.2 -22.9 36.2 10 ALA -64.1 146.7 177.5 11 PRO -54.9 129.8 179.9 -19.9 32.3 12 ASP -70.2 160.7 177.8 -160.0 6.6 13 PHE -155.7 151.9 174.1 57.3 75.7 14 LYS -131.3 134.9 178.6 -157.5 -162.1 178.8 -146.9 15 ALA -154.9 150.5 172.5 16 THR -78.3 135.3 175.1 -55.8 17 ALA -128.6 161.6 169.6 18 VAL -92.0 119.3 -179.1 -172.7 19 VAL -130.2 117.5 -175.9 173.4 20 ASP 51.3 46.6 179.5 -68.5 -31.2 21 GLY 71.3 6.4 178.3 22 ALA -127.8 168.2 -177.9 23 PHE -90.1 135.4 -178.2 -61.1 -29.3 24 LYS -151.5 150.5 179.2 -173.8 -179.4 -179.1 174.0 25 GLU -86.9 134.2 -179.4 -65.3 -59.5 -70.0 26 VAL -124.1 132.9 175.9 171.0 27 LYS -130.7 148.3 -176.2 43.2 -158.7 -55.5 172.5 28 LEU -55.8 -44.3 177.0 170.7 63.2 29 SER -51.9 -25.7 175.2 99.4 30 ASP -61.6 -23.6 -172.2 -73.4 -12.9 31 TYR -100.1 11.7 178.5 -62.4 -83.8 32 LYS -49.8 133.8 -179.2 -148.6 67.6 -168.7 -164.1 33 GLY 89.3 -8.3 179.1 34 LYS -124.1 157.2 173.7 -87.4 148.8 -172.3 -164.1 35 TYR -78.5 156.4 177.7 -100.2 65.9 36 VAL -132.6 135.4 169.5 171.6 37 VAL -108.2 106.1 -179.3 167.2 38 LEU -100.8 116.6 -178.0 178.6 66.7 39 PHE -122.3 124.8 -179.7 70.5 -79.6 40 PHE -94.1 150.4 177.4 -76.6 82.8 41 TYR -146.7 153.6 -172.7 63.5 -85.9 42 PRO -68.6 -58.4 -170.9 17.9 -31.5 43 LEU -147.5 134.7 169.8 -73.7 173.5 44 ASP -62.6 156.1 179.2 -72.6 6.7 45 PHE 62.2 33.0 176.2 -68.0 -78.5 46 THR -120.5 -157.5 -158.5 57.8 47 PHE -108.5 -63.3 174.4 -51.7 -68.4 48 VAL -66.5 39.4 91.4 174.8 49 PRO 13.2 -33.7 -179.6 23.7 -34.5 50 THR -65.0 -32.1 180.0 78.2 51 GLU -75.6 -44.0 -177.2 -63.3 -177.8 -57.7 52 ILE -62.2 -44.6 -179.5 -62.3 161.6 53 ILE -66.8 -41.4 -179.7 -70.5 156.6 54 ALA -60.5 -45.7 176.0 55 PHE -67.8 -42.2 178.9 -85.1 -70.8 56 SER -63.6 -43.4 -179.9 -173.4 57 ASN -59.8 -34.8 -178.8 -72.9 -6.6 58 ARG -103.6 19.2 -178.4 -66.3 -141.1 -42.8 -83.7 59 ALA -53.0 -39.5 -178.1 60 GLU -68.4 -27.1 174.5 -79.8 -57.0 -43.0 61 ASP -57.2 -38.5 178.5 -71.1 -11.6 62 PHE -80.5 -41.1 -178.2 -65.9 85.6 63 ARG -63.1 -30.3 179.8 -87.0 155.6 -161.0 168.6 64 LYS -67.7 -19.7 177.1 -66.0 -177.8 -60.4 172.7 65 LEU -94.8 -0.9 -177.0 -64.7 -175.1 66 GLY 74.9 34.1 -178.8 67 CYS -123.5 126.7 177.9 -178.1 68 GLU -98.3 149.7 178.6 -68.9 -62.8 -16.4 69 VAL -115.9 129.9 180.0 174.7 70 LEU -125.5 134.3 178.0 -58.2 175.4 71 GLY -109.5 151.3 -178.1 72 VAL -150.6 141.0 173.7 50.5 73 SER -141.5 168.6 177.4 76.2 74 VAL -69.9 -12.7 -179.2 -62.0 75 ASP -62.0 154.8 179.4 -63.0 -82.0 76 SER -75.2 168.7 177.6 80.9 77 GLN -67.0 -29.9 178.7 67.0 -87.7 25.6 78 PHE -68.3 -39.8 175.4 -58.0 -83.1 79 THR -66.4 -39.0 178.2 -61.7 80 HIS -61.0 -45.2 -179.9 -73.8 -16.0 81 LEU -64.9 -39.1 174.7 -179.6 63.9 82 ALA -63.4 -34.5 -177.4 83 TRP -80.0 -30.8 172.3 -160.1 21.5 84 ILE -64.5 -36.0 177.9 -75.0 165.3 85 ASN -82.9 15.8 173.8 -74.6 -29.5 86 THR -112.8 124.6 -177.2 -58.7 87 PRO -57.3 150.5 -179.8 -29.8 41.8 88 ARG -63.9 -31.6 -179.0 -58.9 -179.6 168.3 -172.8 89 LYS -66.6 -21.9 175.9 -35.6 70.1 -156.4 154.7 90 GLU -94.2 1.2 179.9 -60.6 -52.7 -43.7 91 GLY 97.3 14.6 176.2 92 GLY -87.4 -178.7 177.3 93 LEU -98.3 -19.5 -175.4 -65.9 -175.7 94 GLY 58.4 -166.9 179.9 95 PRO -67.7 144.9 -179.1 29.8 -41.5 96 LEU -123.8 151.8 176.1 -64.4 179.7 97 ASN -103.2 8.4 177.3 -55.1 -53.7 98 ILE -129.2 153.5 175.7 55.0 172.5 99 PRO -65.0 143.4 178.4 -18.2 33.6 100 LEU -122.9 107.4 -172.7 -156.2 65.7 101 LEU -87.3 147.3 179.4 -79.1 62.3 102 ALA -100.7 128.3 178.1 103 ASP -114.9 54.7 -173.8 -175.4 24.7 104 VAL -60.1 -32.0 176.9 -171.4 105 THR -77.1 -15.0 -175.5 66.2 106 ARG 72.9 11.1 179.5 -83.0 71.2 174.7 166.4 107 ARG -65.1 -42.2 -178.0 -179.6 171.5 -158.7 170.4 108 LEU -66.8 -46.0 -178.8 -77.0 66.4 109 SER -60.1 -40.0 174.9 -67.0 110 GLU -65.4 -48.9 177.7 -78.0 171.5 -12.1 111 ASP -57.8 -33.0 -178.4 -77.7 -19.3 112 TYR -93.7 0.7 178.5 -78.4 75.9 113 GLY 61.3 33.0 -176.9 114 VAL -110.2 4.8 179.8 -67.9 115 LEU -67.8 133.6 170.5 -157.4 65.6 116 LYS -87.0 93.2 -170.1 175.8 172.0 -178.4 147.8 117 THR -52.1 -40.4 179.6 -48.1 118 ASP -68.7 -13.8 178.2 68.1 -5.0 119 GLU -116.6 -16.1 179.1 -72.7 -169.0 63.3 120 GLY 75.2 19.8 -178.5 121 ILE -119.3 155.6 178.1 63.2 -171.0 122 ALA -81.5 141.4 166.4 123 TYR -68.3 169.9 -179.4 -89.2 -61.2 124 ARG -79.3 75.1 -178.0 -66.8 -169.6 -161.5 -74.3 125 GLY -101.6 129.8 178.1 126 LEU -122.7 136.8 -173.5 169.4 155.6 127 PHE -127.3 131.2 178.7 -64.7 -82.9 128 ILE -105.8 119.0 -175.7 -64.5 174.1 129 ILE -116.2 133.9 -177.7 -60.9 162.2 130 ASP -85.7 -177.7 179.7 65.9 19.7 131 GLY -66.3 -14.6 175.8 132 LYS -93.9 3.0 177.4 -54.0 -173.0 169.4 -160.0 133 GLY 88.2 9.7 -175.5 134 VAL -92.5 135.9 -180.0 172.9 135 LEU -75.2 132.4 -179.3 179.1 61.8 136 ARG -116.8 -19.7 -174.7 -52.1 -51.2 -68.2 -73.7 137 GLN -156.8 142.3 179.8 -156.3 -71.4 -38.5 138 ILE -125.4 126.5 177.7 -67.3 166.5 139 THR -131.0 119.4 -179.1 -67.9 140 VAL -132.3 124.0 178.6 -170.4 141 ASN -108.2 147.9 171.0 -75.0 16.5 142 ASP -64.3 168.6 -174.5 -174.5 8.4 143 LEU -56.3 -39.9 -172.1 -54.6 -173.8 144 PRO -79.1 -3.7 -176.8 10.5 -6.0 145 VAL -125.9 124.3 -179.3 168.8 146 GLY -75.7 161.2 179.0 147 ARG -83.8 -174.9 -178.0 -73.3 163.4 -74.4 -164.6 148 SER -124.2 119.9 177.3 164.9 149 VAL -67.0 -36.7 178.0 177.0 150 ASP -57.1 -47.5 -178.2 -75.6 -21.1 151 GLU -65.0 -39.2 177.7 178.9 61.9 4.4 152 ALA -61.6 -44.0 177.2 153 LEU -62.8 -44.4 178.8 -165.5 61.8 154 ARG -56.9 -44.0 -179.9 -171.5 -170.4 78.4 71.2 155 LEU -68.5 -39.9 175.0 -69.8 169.3 156 VAL -62.4 -44.1 -178.8 175.3 157 GLN -61.3 -44.8 178.3 -72.7 165.7 -22.9 158 ALA -60.0 -51.2 -179.9 159 PHE -60.3 -39.4 177.7 -80.4 -73.2 160 GLN -62.8 -43.0 179.8 -75.9 -179.1 -26.9 161 TYR -62.4 -48.8 -179.4 -165.8 -81.3 162 THR -64.6 -30.3 180.0 65.0 163 ASP -69.7 -39.6 -173.7 -70.9 -23.0 164 GLU -78.8 -50.1 -177.7 -77.7 155.2 42.2 165 HIS -90.8 -12.7 -179.5 -55.8 109.7 166 GLY 60.5 32.5 175.8 167 GLU -115.0 169.7 -177.4 -62.7 -152.1 7.4 168 VAL -121.6 153.6 -177.6 -65.4 169 CYS -98.3 124.4 175.1 -64.9 170 PRO -62.9 169.2 175.8 -24.5 35.5 171 ALA -53.9 135.1 174.8 172 GLY 76.3 5.1 -177.1 173 TRP -52.4 142.1 174.9 178.0 93.6 174 LYS -141.2 154.7 179.0 -80.5 171.7 -169.4 -161.9 175 PRO -46.2 131.3 -177.6 -29.9 39.8 176 GLY 98.4 -10.7 -178.0 177 SER -83.9 159.0 176.4 -73.0 178 ASP -68.0 149.3 175.7 -72.8 -24.2 179 THR -119.7 173.8 -177.0 52.6 180 ILE -122.0 136.6 178.1 -55.6 175.3 181 LYS -87.4 121.7 -170.7 -60.1 161.8 174.6 -173.2 182 PRO -78.2 62.0 173.9 37.3 -45.3 183 ASN -149.5 151.9 -169.4 74.4 61.3 184 VAL -56.8 -47.8 -176.1 179.4 185 ASP -71.2 -47.5 -177.9 -68.1 -21.6 186 ASP -69.9 -21.4 178.8 -67.5 -23.8 187 SER -71.4 -19.8 179.8 62.6 188 LYS -59.0 -30.9 173.9 -54.2 -66.4 -179.8 158.0 189 GLU -56.5 -48.1 176.3 138.9 -173.8 -36.5 190 TYR -65.4 -54.2 -173.2 171.1 -83.7 191 PHE -60.7 -35.9 178.3 -59.2 -57.1 192 SER -75.1 -35.6 176.3 54.1 193 LYS -65.7 -43.8 -175.4 178.1 168.3 169.5 -177.7 194 HIS -89.5 -2.3 -178.2 -72.8 -102.4 195 ASN -132.8 170.9 0.0 -62.6 -79.1 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 SER 22.702 -8.922 75.335 2 GLY 19.656 -6.602 74.803 3 ASN 21.294 -3.355 73.585 4 ALA 24.580 -4.628 75.071 5 ARG 27.054 -5.696 72.409 6 ILE 30.665 -6.749 72.867 7 GLY 32.952 -4.252 71.122 8 LYS 30.517 -1.298 71.229 9 PRO 29.896 1.347 73.903 10 ALA 27.994 -0.183 76.800 11 PRO 24.441 1.117 77.135 12 ASP 24.598 4.262 79.223 13 PHE 22.675 4.408 82.470 14 LYS 21.658 6.759 85.262 15 ALA 20.273 5.382 88.538 16 THR 19.665 6.268 92.166 17 ALA 21.963 4.113 94.362 18 VAL 22.734 3.549 98.033 19 VAL 26.349 4.708 98.523 20 ASP 27.772 4.637 102.068 21 GLY 24.266 4.370 103.568 22 ALA 22.909 7.384 101.651 23 PHE 21.175 7.999 98.340 24 LYS 23.227 9.222 95.384 25 GLU 22.865 9.417 91.604 26 VAL 25.237 7.130 89.691 27 LYS 25.825 7.252 85.914 28 LEU 28.011 5.018 83.721 29 SER 29.710 8.106 82.294 30 ASP 31.031 8.892 85.784 31 TYR 33.455 5.955 85.379 32 LYS 35.113 7.105 82.175 33 GLY 38.798 6.119 82.203 34 LYS 38.223 3.236 84.631 35 TYR 37.042 -0.332 84.162 36 VAL 33.583 -1.175 85.514 37 VAL 32.214 -4.552 86.672 38 LEU 28.397 -4.066 86.483 39 PHE 26.547 -6.969 88.089 40 PHE 22.746 -7.378 88.031 41 TYR 21.012 -9.672 90.535 42 PRO 17.339 -10.624 90.821 43 LEU 15.990 -9.725 94.277 44 ASP 16.831 -8.113 97.577 45 PHE 16.098 -10.214 100.706 46 THR 16.892 -13.508 98.942 47 PHE 19.611 -16.206 99.080 48 VAL 22.387 -16.347 96.476 49 PRO 23.582 -11.336 99.456 50 THR 26.456 -13.800 99.018 51 GLU 27.376 -12.162 95.670 52 ILE 26.914 -8.609 96.915 53 ILE 28.970 -9.269 100.045 54 ALA 31.654 -11.144 98.072 55 PHE 32.092 -8.199 95.662 56 SER 31.901 -5.622 98.503 57 ASN 34.455 -7.471 100.664 58 ARG 36.839 -7.470 97.697 59 ALA 36.078 -4.018 96.324 60 GLU 39.631 -2.850 96.937 61 ASP 40.997 -5.724 94.838 62 PHE 39.246 -4.094 91.860 63 ARG 39.891 -0.441 92.806 64 LYS 43.667 -0.987 92.897 65 LEU 43.291 -1.950 89.232 66 GLY 41.302 1.194 88.367 67 CYS 38.104 -0.883 88.259 68 GLU 34.832 0.073 90.016 69 VAL 32.207 -2.536 90.928 70 LEU 28.503 -1.643 90.773 71 GLY 25.615 -3.921 91.816 72 VAL 22.045 -3.433 90.587 73 SER 18.607 -4.996 91.010 74 VAL 15.076 -3.849 90.191 75 ASP 14.442 -3.159 93.937 76 SER 14.166 0.431 95.157 77 GLN 16.850 2.321 97.061 78 PHE 14.608 2.173 100.155 79 THR 14.591 -1.643 100.014 80 HIS 18.352 -1.637 99.384 81 LEU 18.869 0.581 102.454 82 ALA 16.627 -1.633 104.577 83 TRP 18.734 -4.628 103.526 84 ILE 22.035 -2.802 104.210 85 ASN 20.523 -2.036 107.644 86 THR 19.979 -5.784 108.271 87 PRO 22.929 -7.637 109.827 88 ARG 24.663 -10.232 107.626 89 LYS 24.059 -13.007 110.177 90 GLU 20.332 -12.409 109.576 91 GLY 20.648 -12.608 105.767 92 GLY 21.287 -8.885 105.427 93 LEU 23.968 -7.015 103.517 94 GLY 25.448 -5.058 106.430 95 PRO 27.638 -2.144 105.373 96 LEU 28.912 -2.108 101.808 97 ASN 31.932 -0.738 99.962 98 ILE 30.208 -0.636 96.555 99 PRO 27.221 1.280 95.149 100 LEU 23.960 -0.678 95.049 101 LEU 21.767 0.690 92.238 102 ALA 17.982 0.665 92.040 103 ASP 16.494 -0.264 88.616 104 VAL 12.850 0.365 89.522 105 THR 11.901 1.277 85.931 106 ARG 13.667 -1.888 84.671 107 ARG 15.386 0.320 82.060 108 LEU 18.890 -0.876 82.947 109 SER 17.806 -4.506 83.030 110 GLU 16.099 -4.080 79.646 111 ASP 19.040 -2.270 78.063 112 TYR 21.442 -5.059 79.206 113 GLY 18.965 -7.745 78.116 114 VAL 18.919 -9.576 81.446 115 LEU 15.275 -9.231 82.469 116 LYS 13.574 -12.579 83.177 117 THR 10.311 -11.262 81.632 118 ASP 7.811 -13.600 83.291 119 GLU 9.034 -12.540 86.766 120 GLY 10.177 -8.957 86.132 121 ILE 13.585 -9.573 87.738 122 ALA 17.119 -9.539 86.348 123 TYR 19.046 -12.738 85.716 124 ARG 22.601 -12.917 87.162 125 GLY 24.250 -10.928 84.394 126 LEU 27.715 -9.403 84.898 127 PHE 29.286 -7.036 82.353 128 ILE 32.938 -5.995 82.124 129 ILE 33.221 -2.502 80.607 130 ASP 36.621 -0.910 79.880 131 GLY 37.842 2.641 80.443 132 LYS 36.679 3.783 76.996 133 GLY 33.132 2.686 77.814 134 VAL 33.263 -0.400 75.598 135 LEU 31.713 -3.717 76.642 136 ARG 34.297 -6.496 76.766 137 GLN 32.633 -9.447 78.513 138 ILE 29.184 -10.839 79.277 139 THR 28.563 -13.445 82.020 140 VAL 24.963 -14.537 82.759 141 ASN 23.930 -17.275 85.171 142 ASP 20.484 -18.788 85.687 143 LEU 19.136 -17.957 89.189 144 PRO 20.294 -20.821 91.399 145 VAL 24.074 -20.504 90.884 146 GLY 26.218 -17.587 91.992 147 ARG 29.049 -16.043 89.974 148 SER 32.763 -15.972 90.889 149 VAL 34.580 -12.861 92.099 150 ASP 37.895 -14.605 91.319 151 GLU 36.868 -15.093 87.637 152 ALA 35.644 -11.499 87.339 153 LEU 39.010 -10.288 88.690 154 ARG 40.933 -12.642 86.321 155 LEU 38.957 -11.278 83.370 156 VAL 39.459 -7.643 84.392 157 GLN 43.224 -8.262 84.752 158 ALA 43.303 -10.014 81.388 159 PHE 41.453 -7.296 79.460 160 GLN 43.718 -4.643 81.022 161 TYR 46.839 -6.623 80.088 162 THR 45.730 -7.104 76.462 163 ASP 44.817 -3.409 76.189 164 GLU 48.268 -2.435 77.489 165 HIS 50.628 -4.966 75.898 166 GLY 48.791 -5.749 72.643 167 GLU 49.342 -9.471 73.248 168 VAL 46.444 -11.905 73.744 169 CYS 45.654 -14.103 76.711 170 PRO 45.441 -17.867 76.407 171 ALA 42.863 -20.036 78.095 172 GLY 43.160 -19.862 81.897 173 TRP 45.568 -16.888 81.878 174 LYS 46.360 -15.278 85.262 175 PRO 48.894 -12.514 86.046 176 GLY 52.307 -14.084 85.459 177 SER 51.120 -16.426 82.713 178 ASP 52.588 -16.479 79.222 179 THR 50.784 -14.455 76.519 180 ILE 50.852 -14.782 72.708 181 LYS 51.850 -12.136 70.163 182 PRO 48.947 -12.222 67.698 183 ASN 50.691 -12.632 64.360 184 VAL 51.655 -15.871 62.589 185 ASP 55.432 -15.628 62.920 186 ASP 55.674 -14.215 66.482 187 SER 53.137 -16.717 67.851 188 LYS 55.579 -19.597 67.201 189 GLU 57.489 -18.541 70.347 190 TYR 54.467 -19.463 72.494 191 PHE 53.632 -22.688 70.597 192 SER 57.193 -24.076 70.636 193 LYS 57.607 -23.140 74.315 194 HIS 54.336 -24.724 75.433 195 ASN 54.385 -27.864 73.291 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 T T T T/S S S S S S S 10 S/S S S S S S C T T T 20 T/S S S S S C H H H H 30 3 3 S S S S S S S S 40 S S S C S S S S/X X/H H 50 H H H H H H H H H/H H 60 H H H H H H/S S S S S 70 S S S S C H H H H H 80 H H H H H H T T T T 90 C S S S S/S S S S/S S S 100 S S S S C H H H H H 110 H H H/S S S S/T T T T S 120 S S S S/S S S S S S S/T 130 T T T/S S S S S/S S S S 140 S S S S S S S S/H H H 150 H H H H H H H H H H 160 H H H H H H/S S S S S 170 S S S S S S S S S S 180 S S H H H H H H/H H H 190 H H H H H Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 t T T t t T T t B 10 e E E E E E E T 20 T E E E E E E e G G 30 G g T t E E E E E E 40 e S t T T t h H 50 H H H H H H H h H H 60 H H H h T e E E E E 70 E E E S S h H H H H 80 H H H H h t g G G G 90 g t S S S e E 100 E E e T T h H H H H 110 H h T t B t T T T t 120 B E E E E E E e 130 T T t e E E E E E E 140 E t T T t h H H 150 H H H H H H H H H H 160 H H H H H h B t 170 T T t t T T t B 180 S h H H H H H H H 190 H H H H h Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 SER 60.4 72.3 58.0 2 GLY 15.2 43.8 76.7 3 ASN 30.5 25.3 78.8 4 ALA 72.6 100.0 39.0 5 ARG 53.6 25.7 82.1 6 ILE 65.8 45.9 66.1 7 GLY 8.2 23.6 67.0 8 LYS 63.1 36.4 73.9 9 PRO 34.6 27.8 72.3 10 ALA 72.6 100.0 44.6 11 PRO 107.0 86.0 54.5 12 ASP 41.1 37.2 69.5 13 PHE 157.0 94.1 34.8 14 LYS 70.5 40.7 71.4 15 ALA 64.2 88.4 59.6 16 THR 75.5 70.6 68.8 17 ALA 72.6 100.0 47.6 18 VAL 118.4 99.6 38.6 19 VAL 92.5 77.9 55.8 20 ASP 14.0 12.7 83.1 21 GLY 17.1 49.1 58.8 22 ALA 13.4 18.5 80.4 23 PHE 112.4 67.4 49.9 24 LYS 50.2 28.9 75.8 25 GLU 69.0 49.8 69.8 26 VAL 114.4 96.3 42.7 27 LYS 91.7 52.9 68.2 28 LEU 132.4 89.6 43.3 29 SER 35.6 42.6 66.8 30 ASP 51.5 46.6 70.4 31 TYR 151.0 83.4 43.1 32 LYS 52.9 30.5 82.9 33 GLY 0.5 1.6 75.4 34 LYS 74.3 42.9 73.6 35 TYR 170.1 94.0 50.5 36 VAL 117.3 98.8 40.2 37 VAL 118.8 100.0 28.3 38 LEU 147.8 100.0 28.3 39 PHE 166.8 100.0 34.4 40 PHE 166.8 100.0 38.8 41 TYR 173.5 95.8 48.9 42 PRO 115.6 92.8 51.0 43 LEU 82.5 55.8 59.7 44 ASP 110.3 99.8 43.0 45 PHE 85.6 51.3 63.0 46 THR 68.3 63.9 57.0 47 PHE 9.8 5.9 79.5 48 VAL 84.7 71.3 66.5 49 PRO 112.1 90.1 52.5 50 THR 25.3 23.7 71.6 51 GLU 128.5 92.7 53.4 52 ILE 142.0 98.9 26.0 53 ILE 112.2 78.2 60.4 54 ALA 34.0 46.9 66.5 55 PHE 165.6 99.3 28.7 56 SER 83.6 100.0 53.2 57 ASN 52.4 43.3 77.8 58 ARG 127.0 60.8 66.2 59 ALA 71.6 98.6 56.7 60 GLU 38.4 27.7 73.3 61 ASP 71.3 64.5 58.9 62 PHE 166.7 99.9 34.3 63 ARG 148.0 70.9 73.4 64 LYS 43.6 25.2 84.9 65 LEU 100.2 67.8 65.6 66 GLY 9.8 28.2 69.7 67 CYS 99.2 100.0 40.4 68 GLU 112.0 80.8 50.9 69 VAL 118.1 99.4 32.9 70 LEU 147.6 99.8 28.7 71 GLY 34.8 100.0 43.9 72 VAL 118.8 100.0 35.3 73 SER 83.6 100.0 57.8 74 VAL 116.1 97.7 61.0 75 ASP 86.0 77.8 60.5 76 SER 56.4 67.5 57.8 77 GLN 112.9 76.0 36.0 78 PHE 41.5 24.9 75.6 79 THR 62.3 58.2 66.1 80 HIS 150.2 100.0 55.4 81 LEU 102.5 69.3 58.1 82 ALA 25.0 34.4 69.3 83 TRP 204.5 99.8 45.4 84 ILE 130.6 91.0 44.8 85 ASN 38.0 31.4 69.2 86 THR 75.9 71.0 56.1 87 PRO 54.8 44.0 64.7 88 ARG 155.7 74.5 61.9 89 LYS 39.2 22.6 71.8 90 GLU 36.4 26.3 73.1 91 GLY 3.6 10.3 79.9 92 GLY 34.8 100.0 56.7 93 LEU 147.8 100.0 30.3 94 GLY 31.4 90.1 60.6 95 PRO 19.9 16.0 79.3 96 LEU 142.9 96.7 49.0 97 ASN 42.7 35.3 77.8 98 ILE 142.7 99.4 43.4 99 PRO 111.4 89.4 50.5 100 LEU 147.8 100.0 36.8 101 LEU 147.8 100.0 32.4 102 ALA 70.5 97.1 62.8 103 ASP 108.4 98.1 51.4 104 VAL 50.6 42.6 74.5 105 THR 10.7 10.0 78.7 106 ARG 132.9 63.6 64.5 107 ARG 41.4 19.8 87.7 108 LEU 139.4 94.3 36.5 109 SER 83.6 100.0 38.3 110 GLU 49.1 35.4 69.6 111 ASP 89.0 80.5 64.5 112 TYR 180.8 99.9 28.0 113 GLY 22.9 65.9 73.8 114 VAL 115.8 97.4 42.2 115 LEU 127.2 86.1 54.9 116 LYS 129.4 74.6 64.9 117 THR 7.9 7.4 81.2 118 ASP 18.8 17.1 72.4 119 GLU 64.7 46.7 67.0 120 GLY 16.2 46.7 68.7 121 ILE 133.3 92.9 42.0 122 ALA 72.6 100.0 52.2 123 TYR 121.7 67.2 57.1 124 ARG 194.4 93.1 49.9 125 GLY 34.8 100.0 47.0 126 LEU 143.7 97.2 38.0 127 PHE 166.8 100.0 31.8 128 ILE 143.5 100.0 34.0 129 ILE 142.6 99.4 40.9 130 ASP 100.1 90.6 49.3 131 GLY 25.0 71.9 63.4 132 LYS 13.2 7.6 83.9 133 GLY 26.5 76.2 63.3 134 VAL 84.4 71.1 65.1 135 LEU 147.8 100.0 39.0 136 ARG 155.9 74.6 57.0 137 GLN 113.7 76.5 47.6 138 ILE 109.0 75.9 51.7 139 THR 66.6 62.3 64.4 140 VAL 80.8 68.0 57.3 141 ASN 89.1 73.7 56.6 142 ASP 31.3 28.3 65.8 143 LEU 111.4 75.4 55.7 144 PRO 44.6 35.8 70.4 145 VAL 22.7 19.1 83.4 146 GLY 25.4 73.1 57.9 147 ARG 201.3 96.4 47.6 148 SER 37.1 44.3 69.2 149 VAL 109.9 92.5 44.5 150 ASP 27.7 25.1 86.7 151 GLU 69.5 50.1 68.4 152 ALA 70.5 97.1 37.2 153 LEU 125.3 84.8 57.3 154 ARG 163.2 78.1 59.6 155 LEU 123.6 83.6 55.7 156 VAL 118.8 100.0 32.5 157 GLN 110.3 74.2 43.3 158 ALA 63.5 87.5 48.4 159 PHE 123.1 73.8 60.1 160 GLN 121.1 81.5 57.3 161 TYR 109.3 60.4 57.5 162 THR 82.6 77.3 62.6 163 ASP 62.7 56.7 77.8 164 GLU 40.2 29.0 73.9 165 HIS 70.4 46.9 66.8 166 GLY 0.0 0.0 84.2 167 GLU 103.5 74.7 55.0 168 VAL 52.7 44.3 55.9 169 CYS 90.8 91.5 37.1 170 PRO 99.3 79.8 58.9 171 ALA 0.0 0.0 88.6 172 GLY 1.7 4.9 82.1 173 TRP 198.3 96.7 45.6 174 LYS 43.4 25.0 70.2 175 PRO 66.0 53.0 61.6 176 GLY 0.0 0.0 85.9 177 SER 45.7 54.7 73.0 178 ASP 68.2 61.7 66.3 179 THR 99.9 93.5 49.7 180 ILE 116.3 81.1 42.8 181 LYS 91.5 52.7 74.5 182 PRO 67.3 54.1 64.6 183 ASN 49.4 40.9 75.2 184 VAL 5.8 4.9 86.4 185 ASP 6.1 5.5 80.2 186 ASP 49.2 44.5 75.5 187 SER 71.0 84.9 56.8 188 LYS 53.0 30.6 77.9 189 GLU 41.4 29.9 81.6 190 TYR 140.8 77.8 45.6 191 PHE 73.6 44.1 67.5 192 SER 13.8 16.5 84.0 193 LYS 47.0 27.1 86.4 194 HIS 91.8 61.2 63.2 195 ASN 30.6 25.3 78.5