Protein Data Bank File : 1g2ra Title : STRUCTURAL GENOMICS, UNKNOWN FUNCTION 20-OCT-00 1G2R Number of Amino Acid Residues : 94 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 ARG LYS ILE PRO LEU ARG LYS SER VAL VAL 10 SER ASN GLU VAL ILE ASP LYS ARG ASP LEU 20 LEU ARG ILE VAL LYS ASN LYS GLU GLY GLN 30 VAL PHE ILE ASP PRO THR GLY LYS ALA ASN 40 GLY ARG GLY ALA TYR ILE LYS LEU ASP ASN 50 ALA GLU ALA LEU GLU ALA LYS LYS LYS LYS 60 VAL PHE ASN ARG SER PHE SER MET GLU VAL 70 GLU GLU SER PHE TYR ASP GLU LEU ILE ALA 80 TYR VAL ASP HIS LYS VAL LYS ARG ARG GLU 90 LEU GLY LEU GLU Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 ARG 0.0 -13.9 177.9 -66.7 165.8 65.8 179.1 2 LYS 49.4 56.2 -174.5 -70.8 -180.0 -64.4 176.1 3 ILE -77.5 128.8 174.4 -77.1 113.9 4 PRO -57.2 137.1 174.3 -25.4 32.5 5 LEU -98.9 127.2 -176.3 -56.9 -172.8 6 ARG -93.5 166.6 179.9 -47.4 -54.0 -64.3 -86.1 7 LYS -100.0 138.1 178.3 -66.0 -57.6 -175.1 37.1 8 SER -72.5 134.7 174.6 168.9 9 VAL -75.9 -15.6 177.5 -68.4 10 VAL -84.2 -50.8 -172.6 167.4 11 SER -104.5 -14.4 -171.8 62.7 12 ASN 64.8 20.6 177.0 -53.4 -48.9 13 GLU -100.1 157.5 173.9 -71.8 -168.3 -3.0 14 VAL -70.8 135.7 -178.8 177.0 15 ILE -98.0 126.7 173.6 -53.9 166.0 16 ASP -58.4 145.2 178.7 -72.8 1.0 17 LYS -51.0 -43.6 -179.3 175.6 -176.3 -170.9 -33.7 18 ARG -62.1 -25.3 -172.6 160.2 85.4 167.6 166.6 19 ASP -99.5 0.8 -174.8 -66.5 -22.7 20 LEU -72.0 130.8 174.3 -167.6 60.5 21 LEU -132.7 127.7 179.3 -175.9 61.0 22 ARG -100.6 132.2 172.3 -169.3 178.7 -162.0 -132.3 23 ILE -113.1 131.4 -174.9 -67.5 79.9 24 VAL -119.8 141.4 170.8 172.2 25 LYS -116.6 122.6 179.9 176.4 -129.5 -171.9 169.7 26 ASN -90.9 178.7 -177.8 66.3 23.6 27 LYS -71.0 -18.4 177.9 -81.8 86.4 27.7 -95.5 28 GLU -85.3 1.8 178.0 -73.7 77.1 23.7 29 GLY 81.3 15.6 177.0 30 GLN -90.6 140.7 -178.5 -65.6 171.7 138.7 31 VAL -122.0 131.5 -178.5 176.6 32 PHE -150.9 163.1 176.9 58.5 -88.7 33 ILE -81.7 136.3 -178.7 -62.8 170.2 34 ASP -121.7 83.4 -180.0 178.7 18.3 35 PRO -59.0 -25.2 179.2 -13.5 26.3 36 THR -89.6 -16.6 -176.9 87.9 37 GLY 73.7 10.8 -173.3 38 LYS -102.9 1.6 -179.7 -69.3 169.6 98.9 -41.3 39 ALA -78.2 152.8 172.0 40 ASN -88.9 151.4 -176.5 -46.5 -71.9 41 GLY 127.3 -174.9 -179.2 42 ARG -90.3 127.3 -177.7 -177.0 172.0 -64.0 -94.7 43 GLY -101.1 147.3 172.8 44 ALA -138.9 138.9 -172.3 45 TYR -115.9 145.4 170.7 -64.6 -84.0 46 ILE -135.2 164.9 168.3 68.1 166.9 47 LYS -75.1 149.6 173.0 -63.1 -176.7 -170.7 175.4 48 LEU -80.6 81.0 -169.6 -163.6 -41.9 49 ASP -151.0 132.2 -176.9 172.8 -81.8 50 ASN -61.9 -37.2 178.5 -69.7 -49.4 51 ALA -62.9 -42.7 179.6 52 GLU -68.2 -38.9 177.6 -66.9 -144.3 -5.5 53 ALA -63.0 -42.1 178.0 54 LEU -63.1 -45.2 180.0 175.0 57.5 55 GLU -64.5 -35.3 177.7 -175.2 75.2 -11.0 56 ALA -55.4 -43.7 178.6 57 LYS -71.7 -42.4 -175.2 -179.8 174.7 178.5 -175.5 58 LYS -61.3 -36.2 -177.9 -66.6 173.4 56.3 174.0 59 LYS -99.9 0.6 -177.4 -57.9 -56.6 -171.7 172.3 60 LYS 46.3 52.7 -167.4 -61.7 174.5 173.8 59.6 61 VAL -64.6 -31.6 -177.3 71.2 62 PHE -78.3 -17.5 -180.0 -55.2 -68.8 63 ASN -61.5 -44.8 174.6 -66.3 19.9 64 ARG -61.8 -52.2 179.6 -42.9 -160.8 -164.3 -132.7 65 SER -59.3 -40.1 -170.3 -65.0 66 PHE -103.6 0.7 179.3 -62.8 -28.4 67 SER 53.2 48.6 178.3 -59.7 68 MET -159.0 163.4 173.2 61.6 174.9 -78.3 69 GLU -86.3 97.6 178.6 -174.9 170.6 14.7 70 VAL -70.8 138.2 -178.7 177.6 71 GLU -63.9 140.2 174.8 -66.1 -77.7 -36.0 72 GLU -56.6 -37.0 175.9 178.6 -153.0 113.8 73 SER -54.8 -36.9 177.2 68.2 74 PHE -64.5 -45.9 177.3 177.4 71.4 75 TYR -57.4 -40.2 179.2 -75.4 -71.2 76 ASP -69.2 -35.1 175.4 -68.2 -21.3 77 GLU -62.1 -46.4 -178.3 175.6 -167.8 -1.2 78 LEU -63.3 -39.9 176.7 179.1 61.5 79 ILE -59.4 -45.7 -177.5 -76.9 166.2 80 ALA -69.5 -38.0 178.3 81 TYR -60.2 -51.6 -179.2 176.1 -88.7 82 VAL -63.2 -43.2 -179.3 172.2 83 ASP -57.7 -47.0 -178.1 177.1 61.6 84 HIS -65.7 -43.5 -178.9 -179.6 -111.7 85 LYS -68.1 -39.9 177.1 -64.2 -135.9 134.1 -126.0 86 VAL -64.3 -38.9 177.2 170.4 87 LYS -63.7 -45.2 178.6 -179.9 178.8 170.5 173.1 88 ARG -60.8 -41.7 -179.3 -71.2 -178.9 48.4 87.6 89 ARG -66.0 -38.0 -179.3 -66.0 -179.9 145.2 -149.4 90 GLU -68.2 -29.5 177.3 -70.4 -24.5 -57.7 91 LEU -86.7 1.9 -179.4 -70.3 178.7 92 GLY 70.6 24.2 179.1 93 LEU -82.8 -20.3 173.7 -55.3 175.5 94 GLU -157.8 1.8 0.0 57.9 176.3 -81.9 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 ARG 17.014 7.699 12.351 2 LYS 16.206 10.152 9.575 3 ILE 13.817 7.729 8.126 4 PRO 12.864 8.480 4.557 5 LEU 9.230 9.405 4.097 6 ARG 7.576 7.766 1.120 7 LYS 4.943 9.012 -1.300 8 SER 1.418 7.637 -1.418 9 VAL 0.352 6.016 -4.700 10 VAL -3.178 7.124 -3.856 11 SER -2.752 10.825 -2.981 12 ASN 0.760 11.556 -4.229 13 GLU 1.474 13.062 -0.796 14 VAL 4.400 12.472 1.565 15 ILE 3.431 9.928 4.208 16 ASP 4.263 10.423 7.925 17 LYS 6.452 7.582 9.257 18 ARG 3.713 6.520 11.701 19 ASP 1.246 6.243 8.797 20 LEU 3.300 4.233 6.337 21 LEU 1.773 1.089 4.903 22 ARG 3.484 -1.103 2.312 23 ILE 1.666 -3.272 -0.282 24 VAL 3.877 -5.754 -2.164 25 LYS 3.539 -7.629 -5.453 26 ASN 5.854 -10.638 -5.932 27 LYS 6.986 -12.246 -9.202 28 GLU 4.310 -14.892 -8.878 29 GLY 1.627 -12.178 -9.182 30 GLN 0.597 -12.305 -5.522 31 VAL -0.231 -9.023 -3.809 32 PHE -0.176 -8.690 -0.010 33 ILE 0.120 -6.253 2.819 34 ASP 3.656 -6.092 4.322 35 PRO 3.429 -4.650 7.830 36 THR 7.189 -4.975 8.572 37 GLY 8.438 -3.429 5.307 38 LYS 11.102 -6.164 4.958 39 ALA 9.489 -8.204 2.154 40 ASN 10.907 -8.684 -1.329 41 GLY 8.807 -8.008 -4.375 42 ARG 7.702 -4.662 -5.795 43 GLY 6.408 -2.188 -3.123 44 ALA 3.703 0.503 -3.313 45 TYR 2.845 2.739 -0.330 46 ILE -0.283 4.288 1.052 47 LYS -1.198 6.123 4.240 48 LEU -2.798 4.051 7.023 49 ASP -5.971 6.034 6.441 50 ASN -9.532 4.920 5.608 51 ALA -9.892 7.493 2.851 52 GLU -6.737 6.226 1.100 53 ALA -7.746 2.555 1.426 54 LEU -11.135 3.376 -0.118 55 GLU -9.600 5.429 -2.920 56 ALA -7.121 2.596 -3.614 57 LYS -10.097 0.359 -4.426 58 LYS -12.116 3.002 -6.257 59 LYS -9.198 3.744 -8.563 60 LYS -7.714 0.201 -8.597 61 VAL -4.465 2.011 -7.847 62 PHE -2.223 -1.049 -7.521 63 ASN -3.321 -2.430 -10.892 64 ARG -1.610 0.493 -12.372 65 SER 1.452 0.273 -10.098 66 PHE 1.901 -3.489 -10.625 67 SER 0.803 -3.901 -14.223 68 MET -1.823 -6.524 -13.360 69 GLU -5.496 -6.952 -12.439 70 VAL -5.352 -7.123 -8.623 71 GLU -8.247 -9.147 -7.138 72 GLU -11.171 -7.259 -5.631 73 SER -10.721 -9.439 -2.551 74 PHE -7.331 -7.825 -1.974 75 TYR -8.794 -4.314 -2.106 76 ASP -11.482 -5.400 0.353 77 GLU -8.841 -6.978 2.586 78 LEU -6.866 -3.690 2.588 79 ILE -10.005 -1.697 3.500 80 ALA -10.715 -4.020 6.393 81 TYR -7.069 -4.043 7.504 82 VAL -6.866 -0.249 7.518 83 ASP -10.274 0.146 9.197 84 HIS -9.187 -2.145 12.047 85 LYS -5.767 -0.511 12.482 86 VAL -7.194 3.046 12.401 87 LYS -9.749 2.078 15.049 88 ARG -6.997 0.656 17.288 89 ARG -4.897 3.794 16.838 90 GLU -7.817 6.123 17.611 91 LEU -8.447 4.175 20.816 92 GLY -4.759 4.432 21.701 93 LEU -4.195 0.655 21.546 94 GLU -1.203 1.136 19.272 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C S S S S S S S/T T T 10 T S S S S S/T T T T/S S 20 S S S S S S/T T T T/S S 30 S S S S/T T T T S S S 40 S/S S S S S S S C H H 50 H H H H H H H H H H/H 60 H H H H H H H S S S 70 S/H H H H H H H H H H 80 H H H H H H H H H H 90 H H/S S/S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 B t T T 10 T t B g G G e E 20 E E E E E e T T t e 30 E E E E T T t 40 S E E E E E E e h H 50 H H H H H H H H H h 60 H H H H H H h t 70 h H H H H H H H H H 80 H H H H H H H H H H 90 h T t Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 ARG 25.5 12.2 81.9 2 LYS 0.0 0.0 92.7 3 ILE 100.9 70.3 55.1 4 PRO 29.6 23.8 74.2 5 LEU 83.2 56.3 66.7 6 ARG 100.5 48.1 64.6 7 LYS 51.7 29.8 75.1 8 SER 83.6 100.0 59.2 9 VAL 82.0 69.0 59.3 10 VAL 111.3 93.7 42.5 11 SER 55.0 65.7 65.0 12 ASN 15.0 12.4 87.7 13 GLU 46.4 33.5 82.5 14 VAL 53.6 45.1 59.8 15 ILE 143.5 100.0 48.4 16 ASP 23.4 21.2 76.0 17 LYS 71.8 41.4 65.4 18 ARG 85.4 40.9 82.5 19 ASP 73.4 66.5 63.2 20 LEU 107.2 72.6 56.5 21 LEU 140.7 95.2 39.1 22 ARG 176.1 84.3 57.9 23 ILE 143.5 100.0 29.3 24 VAL 118.8 100.0 47.7 25 LYS 128.7 74.2 53.3 26 ASN 99.8 82.5 65.2 27 LYS 42.1 24.3 80.8 28 GLU 38.7 27.9 80.7 29 GLY 18.0 51.8 63.3 30 GLN 41.5 27.9 79.4 31 VAL 115.2 97.0 30.2 32 PHE 95.7 57.4 63.7 33 ILE 135.7 94.6 36.0 34 ASP 101.7 92.0 49.5 35 PRO 62.6 50.2 70.5 36 THR 28.9 27.0 73.6 37 GLY 17.3 49.7 72.2 38 LYS 20.2 11.6 90.5 39 ALA 49.5 68.2 65.1 40 ASN 0.0 0.0 88.9 41 GLY 29.3 84.1 62.1 42 ARG 55.7 26.6 79.6 43 GLY 32.3 92.7 61.3 44 ALA 67.8 93.5 40.3 45 TYR 155.2 85.7 53.7 46 ILE 143.5 100.0 34.6 47 LYS 128.7 74.2 62.4 48 LEU 141.3 95.6 37.3 49 ASP 61.1 55.3 55.2 50 ASN 60.8 50.3 64.4 51 ALA 7.2 9.9 81.8 52 GLU 128.1 92.4 49.0 53 ALA 71.6 98.7 45.5 54 LEU 59.1 40.0 64.7 55 GLU 86.8 62.6 55.1 56 ALA 72.6 100.0 37.9 57 LYS 105.7 61.0 60.2 58 LYS 61.7 35.6 70.5 59 LYS 63.6 36.7 80.7 60 LYS 56.4 32.5 83.0 61 VAL 103.5 87.1 43.9 62 PHE 166.8 100.0 24.1 63 ASN 98.9 81.8 52.4 64 ARG 47.3 22.6 80.4 65 SER 55.4 66.3 52.7 66 PHE 165.9 99.5 37.4 67 SER 6.1 7.3 89.0 68 MET 110.9 69.5 60.6 69 GLU 9.8 7.1 86.3 70 VAL 117.7 99.1 38.0 71 GLU 19.4 14.0 87.2 72 GLU 31.4 22.6 79.9 73 SER 13.8 16.5 78.0 74 PHE 155.8 93.4 42.9 75 TYR 176.2 97.4 44.0 76 ASP 63.6 57.6 69.7 77 GLU 47.7 34.4 68.1 78 LEU 147.5 99.8 26.1 79 ILE 91.2 63.6 58.1 80 ALA 14.5 20.0 77.4 81 TYR 133.9 74.0 39.0 82 VAL 118.8 100.0 39.8 83 ASP 33.1 29.9 79.5 84 HIS 43.7 29.1 73.0 85 LYS 117.7 67.9 65.5 86 VAL 94.1 79.2 62.7 87 LYS 41.9 24.2 73.5 88 ARG 126.7 60.7 62.7 89 ARG 166.9 79.9 67.9 90 GLU 34.4 24.8 73.7 91 LEU 57.5 38.9 66.1 92 GLY 4.7 13.6 85.2 93 LEU 64.9 43.9 71.7 94 GLU 90.8 65.5 75.8