Protein Data Bank File : 1i0va Title : HYDROLASE 30-JAN-01 1I0V Number of Amino Acid Residues : 104 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 ALA CYS ASP TYR THR CYS GLY SER ASN CYS 10 TYR SER SER SER ASP VAL SER THR ALA GLN 20 ALA ALA GLY TYR LYS LEU HIS GLU ASP GLY 30 GLU THR VAL GLY SER ASN SER TYR PRO HIS 40 LYS TYR ASN ASN TYR GLU GLY PHE ASP PHE 50 SER VAL SER SER PRO TYR TYR GLU TRP PRO 60 ILE LEU SER SER GLY ASP VAL TYR SER GLY 70 GLY SER PRO GLY ALA ASP ARG VAL VAL PHE 80 ASN GLU ASN ASN GLN LEU ALA GLY VAL ILE 90 THR HIS THR GLY ALA SER GLY ASN ASN PHE 100 VAL GLU CYS THR Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 ALA 0.0 153.2 -179.7 2 CYS -87.8 138.0 176.7 -43.3 3 ASP -77.5 -31.2 178.4 -72.8 134.7 4 TYR -139.5 129.7 179.0 -61.2 -82.6 5 THR -118.4 115.2 179.6 -58.7 6 CYS -109.9 92.5 -178.1 -60.2 7 GLY 67.9 -111.9 179.9 8 SER -100.7 -9.2 -179.1 -54.7 9 ASN -84.1 134.5 -177.2 -66.1 -27.2 10 CYS -112.5 122.7 -179.6 -177.7 11 TYR -123.7 143.1 176.8 -60.3 -66.3 12 SER -99.6 166.8 179.3 66.6 13 SER -60.0 -33.3 179.8 -66.0 14 SER -66.8 -34.2 178.6 57.1 15 ASP -64.0 -44.7 -179.1 -69.8 -38.2 16 VAL -64.5 -44.7 -179.9 174.1 17 SER -60.9 -43.4 179.9 -68.1 18 THR -62.5 -46.9 179.7 -62.3 19 ALA -63.3 -47.3 -179.6 20 GLN -58.1 -41.6 -179.8 176.0 178.3 168.8 21 ALA -60.7 -42.5 179.9 22 ALA -65.3 -47.3 -179.9 23 GLY -62.7 -41.8 -179.4 24 TYR -65.0 -40.3 179.6 -170.9 67.1 25 LYS -59.0 -47.1 179.4 -179.9 0.0 0.0 0.0 26 LEU -61.5 -42.0 179.4 -77.3 167.4 27 HIS -59.3 -46.7 -179.4 168.9 67.5 28 GLU -63.3 -35.4 -179.6 -70.7 -61.7 -62.1 29 ASP -83.5 -8.5 -179.8 -65.0 -30.4 30 GLY 70.9 37.0 179.9 31 GLU -123.9 161.4 -179.6 -54.7 -176.6 -35.0 32 THR -138.9 168.6 179.0 65.8 33 VAL -142.5 148.7 179.6 -17.9 34 GLY 86.7 160.5 -180.0 35 SER -67.5 -21.5 179.3 -66.5 36 ASN -92.8 5.8 178.5 -63.2 -32.4 37 SER 52.9 68.1 178.1 -64.6 38 TYR -93.5 144.9 0.2 -67.2 -71.9 39 PRO -81.4 150.2 177.7 35.6 -43.7 40 HIS -138.7 165.4 -178.8 68.3 66.3 41 LYS -57.5 138.5 177.0 -177.5 178.8 0.0 0.0 42 TYR -109.2 114.2 -177.1 175.6 70.7 43 ASN -75.8 -15.0 -178.7 -60.6 148.8 44 ASN 58.9 47.6 178.5 -168.5 27.2 45 TYR -63.5 -31.7 -180.0 -64.0 -44.9 46 GLU -60.4 -30.0 179.7 -80.1 68.3 24.8 47 GLY 82.2 30.6 179.1 48 PHE -62.5 146.1 -179.9 -65.1 -58.6 49 ASP -95.4 77.1 179.8 -149.4 0.0 50 PHE -72.0 147.8 -178.9 -63.7 -50.5 51 SER -84.0 -8.7 179.3 -57.7 52 VAL -113.1 156.0 -178.4 -61.4 53 SER -75.2 153.9 178.3 62.0 54 SER -83.2 174.5 -0.3 63.2 55 PRO -64.3 154.3 179.0 -26.7 42.8 56 TYR -114.3 151.1 179.3 -58.1 -59.4 57 TYR -133.8 143.4 178.8 -60.5 -77.8 58 GLU -112.3 146.5 -178.4 56.9 164.4 -61.5 59 TRP -145.1 137.2 -179.5 170.0 -102.7 60 PRO -67.7 144.0 174.4 -21.0 38.2 61 ILE -121.1 130.1 -175.9 178.6 165.5 62 LEU -105.4 140.7 -179.7 -47.9 176.7 63 SER -68.9 -12.4 179.7 62.4 64 SER -75.5 -18.4 -179.3 63.1 65 GLY 93.8 -11.2 179.6 66 ASP -85.9 158.0 178.9 -63.4 -52.3 67 VAL -81.4 138.9 -179.4 172.3 68 TYR -58.6 130.6 -179.2 -177.8 67.1 69 SER -130.0 4.5 -178.7 61.9 70 GLY 131.4 172.3 -179.6 71 GLY 88.6 -159.3 -178.7 72 SER -68.5 127.9 -179.9 175.5 73 PRO -83.9 -4.4 -178.1 37.0 -44.6 74 GLY 73.1 -167.1 -177.9 75 ALA -100.2 -8.8 -175.4 76 ASP -101.0 147.4 -178.9 -46.2 -29.4 77 ARG -142.6 148.2 173.3 -48.5 -81.9 -176.5 -84.7 78 VAL -105.1 139.4 179.9 -64.5 79 VAL -115.0 126.2 -179.7 -177.7 80 PHE -132.9 163.8 -179.5 58.6 84.5 81 ASN -109.8 -171.8 -178.6 70.8 5.2 82 GLU -58.9 -29.8 -179.2 -157.7 58.4 58.7 83 ASN -91.0 11.0 -179.1 -55.0 -52.4 84 ASN 63.2 36.4 177.6 -163.2 -169.5 85 GLN -99.3 138.7 179.4 -67.5 176.6 -64.3 86 LEU -74.4 124.1 178.7 178.0 63.5 87 ALA -92.2 -41.9 179.4 88 GLY 171.8 177.8 179.0 89 VAL -123.5 123.9 -177.2 -178.2 90 ILE -126.7 167.0 -178.0 60.7 179.9 91 THR -151.1 152.1 177.1 -179.6 92 HIS -82.2 -18.1 -179.0 -75.2 -57.2 93 THR -63.5 128.8 -179.8 -59.1 94 GLY 81.8 6.6 179.3 95 ALA -119.8 145.9 -179.4 96 SER -70.7 141.0 179.1 176.8 97 GLY 49.9 -125.9 -179.3 98 ASN -99.0 17.9 178.6 0.0 0.0 99 ASN -75.4 168.7 179.6 -70.9 164.3 100 PHE -126.7 154.1 173.7 -76.4 -74.0 101 VAL -134.0 157.7 -179.3 -69.5 102 GLU -79.6 148.4 176.9 -75.4 -170.8 -65.8 103 CYS -80.3 149.8 -177.3 -59.4 104 THR -91.8 156.0 0.0 53.2 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 ALA 5.677 5.930 29.789 2 CYS 7.132 7.637 26.708 3 ASP 6.457 6.275 23.258 4 TYR 9.629 8.121 22.252 5 THR 12.372 9.301 24.576 6 CYS 14.769 11.868 23.132 7 GLY 17.387 12.369 25.802 8 SER 15.288 13.835 28.608 9 ASN 12.299 14.729 26.428 10 CYS 9.265 12.468 26.537 11 TYR 6.847 12.178 23.633 12 SER 3.634 10.258 23.141 13 SER 2.455 9.048 19.752 14 SER -0.079 11.886 19.763 15 ASP 2.727 14.441 20.175 16 VAL 4.466 12.956 17.167 17 SER 1.313 12.812 15.039 18 THR 0.500 16.427 15.793 19 ALA 4.017 17.607 14.917 20 GLN 4.125 15.454 11.786 21 ALA 0.773 16.790 10.562 22 ALA 2.003 20.385 10.811 23 GLY 5.269 19.630 9.056 24 TYR 3.609 17.673 6.275 25 LYS 1.086 20.433 5.604 26 LEU 3.870 22.991 5.165 27 HIS 5.719 20.564 2.930 28 GLU 2.659 20.075 0.734 29 ASP 2.112 23.823 0.471 30 GLY 5.755 24.505 -0.336 31 GLU 6.227 26.793 2.656 32 THR 8.717 26.862 5.512 33 VAL 9.176 28.351 8.966 34 GLY 12.237 29.293 10.990 35 SER 15.720 30.387 9.994 36 ASN 16.593 26.775 9.141 37 SER 13.608 26.569 6.796 38 TYR 11.642 23.661 8.245 39 PRO 10.478 21.284 7.023 40 HIS 13.477 20.492 4.876 41 LYS 15.029 17.397 3.364 42 TYR 16.652 14.930 5.741 43 ASN 19.572 13.298 3.904 44 ASN 19.970 10.422 6.366 45 TYR 23.752 10.788 6.529 46 GLU 23.478 8.791 9.757 47 GLY 22.293 5.810 7.739 48 PHE 19.262 4.915 9.850 49 ASP 17.348 1.889 8.604 50 PHE 13.875 3.402 8.237 51 SER 11.006 1.082 7.288 52 VAL 9.507 3.617 4.882 53 SER 10.869 4.931 1.589 54 SER 12.620 8.248 0.997 55 PRO 12.680 11.164 0.311 56 TYR 12.660 12.106 3.990 57 TYR 11.879 15.458 5.583 58 GLU 12.599 16.656 9.090 59 TRP 10.421 18.893 11.240 60 PRO 10.993 19.957 14.856 61 ILE 9.007 18.399 17.663 62 LEU 9.034 20.486 20.852 63 SER 9.054 19.345 24.459 64 SER 6.668 22.215 25.236 65 GLY 3.900 20.361 23.430 66 ASP 3.386 23.259 21.037 67 VAL 3.800 23.028 17.274 68 TYR 6.999 24.592 15.933 69 SER 6.366 28.114 14.676 70 GLY 9.857 29.561 14.390 71 GLY 12.691 30.298 16.763 72 SER 14.924 27.654 18.296 73 PRO 13.857 24.205 17.060 74 GLY 15.394 22.428 20.025 75 ALA 17.223 19.151 19.464 76 ASP 14.373 16.828 18.461 77 ARG 12.875 16.062 15.063 78 VAL 10.188 13.941 13.499 79 VAL 11.132 12.472 10.129 80 PHE 8.389 11.763 7.602 81 ASN 8.298 10.916 3.918 82 GLU 6.451 12.016 0.796 83 ASN 3.443 9.849 1.708 84 ASN 3.222 11.409 5.173 85 GLN 4.476 8.167 6.702 86 LEU 6.452 8.397 9.930 87 ALA 10.057 7.307 9.387 88 GLY 11.235 7.986 12.918 89 VAL 11.940 10.437 15.719 90 ILE 15.540 11.568 16.081 91 THR 17.543 13.943 18.233 92 HIS 20.836 15.824 18.429 93 THR 20.879 15.045 22.147 94 GLY 23.540 12.476 22.990 95 ALA 25.094 12.841 19.537 96 SER 28.332 14.617 18.662 97 GLY 28.087 18.006 16.984 98 ASN 25.190 18.201 14.540 99 ASN 24.805 14.428 14.273 100 PHE 21.603 12.591 15.191 101 VAL 20.720 9.465 17.136 102 GLU 17.293 7.854 17.241 103 CYS 15.015 8.487 20.172 104 THR 14.232 5.302 22.113 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C C C C T T T T/S S S 10 S S/H H H H H H H H H 20 H H H H H H H H H H/S 30 S S S S/T T T T C/P S S 40 S S S T T T T S S S 50 S/S S S S/P S/S S S S S S 60 S S/T T T T/S S S S S S 70 S S C C S S S S S S 80 S/T T T T/S S S S S S S 90 S S/T T T T C C S S S 100 S S S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S E E E T T E E 10 E h H H H H H H H H 20 H H H H H H H H H h 30 t B T T T T B S E 40 E E t T T t 50 S S S e E E E E E 60 e t T T t S S 70 S e E E E E E 80 E e T t e E E E E E 90 E e T T t t T T t 100 E E e Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 ALA 0.0 0.0 91.3 2 CYS 75.7 76.3 61.1 3 ASP 50.4 45.6 70.4 4 TYR 127.6 70.5 52.7 5 THR 62.5 58.5 71.6 6 CYS 99.1 99.9 42.9 7 GLY 14.6 42.0 66.9 8 SER 0.0 0.0 87.9 9 ASN 74.9 62.0 70.8 10 CYS 47.3 47.7 64.0 11 TYR 177.4 98.0 45.4 12 SER 42.6 51.0 79.3 13 SER 23.7 28.3 71.1 14 SER 12.3 14.8 83.3 15 ASP 62.4 56.4 64.9 16 VAL 116.2 97.8 33.6 17 SER 22.7 27.1 78.5 18 THR 36.5 34.2 70.7 19 ALA 66.6 91.8 49.7 20 GLN 130.5 87.8 48.9 21 ALA 18.7 25.7 80.6 22 ALA 48.7 67.1 57.3 23 GLY 34.8 100.0 41.2 24 TYR 138.2 76.4 61.0 25 LYS 103.0 59.4 77.0 26 LEU 114.0 77.2 54.9 27 HIS 117.9 78.5 56.2 28 GLU 70.4 50.8 73.0 29 ASP 43.6 39.5 72.1 30 GLY 0.0 0.0 83.0 31 GLU 42.4 30.6 73.6 32 THR 55.8 52.2 69.9 33 VAL 89.7 75.5 55.1 34 GLY 28.7 82.4 68.2 35 SER 0.0 0.0 89.0 36 ASN 47.6 39.4 68.2 37 SER 32.8 39.2 77.0 38 TYR 174.7 96.5 50.1 39 PRO 123.1 98.9 41.3 40 HIS 85.5 56.9 72.3 41 LYS 98.2 56.6 75.9 42 TYR 173.6 95.9 40.4 43 ASN 67.8 56.1 60.6 44 ASN 95.6 79.0 55.5 45 TYR 22.9 12.6 87.4 46 GLU 107.3 77.4 58.4 47 GLY 7.8 22.4 86.4 48 PHE 137.9 82.7 55.8 49 ASP 13.9 12.6 90.7 50 PHE 162.3 97.3 49.2 51 SER 0.0 0.0 84.5 52 VAL 94.6 79.7 63.0 53 SER 16.7 20.0 86.4 54 SER 33.5 40.1 62.8 55 PRO 54.8 44.0 69.4 56 TYR 159.9 88.4 44.8 57 TYR 149.5 82.6 52.5 58 GLU 126.8 91.5 43.5 59 TRP 204.1 99.6 31.7 60 PRO 124.5 100.0 32.8 61 ILE 138.7 96.6 38.3 62 LEU 114.1 77.2 68.8 63 SER 38.9 46.6 77.7 64 SER 30.4 36.4 77.4 65 GLY 8.8 25.2 86.9 66 ASP 18.2 16.5 82.8 67 VAL 67.0 56.4 61.5 68 TYR 179.6 99.2 41.6 69 SER 9.2 11.0 80.6 70 GLY 23.7 68.1 64.2 71 GLY 0.0 0.0 82.8 72 SER 9.8 11.8 74.0 73 PRO 105.1 84.4 62.6 74 GLY 0.8 2.3 80.9 75 ALA 47.5 65.5 73.9 76 ASP 109.3 98.9 58.9 77 ARG 199.4 95.4 50.5 78 VAL 118.8 100.0 31.9 79 VAL 118.8 100.0 32.5 80 PHE 166.8 100.0 40.3 81 ASN 120.0 99.3 57.5 82 GLU 70.5 50.9 71.0 83 ASN 37.6 31.1 79.3 84 ASN 80.7 66.8 57.4 85 GLN 66.9 45.0 75.0 86 LEU 108.5 73.4 62.5 87 ALA 72.1 99.4 38.0 88 GLY 24.4 70.0 49.9 89 VAL 118.8 100.0 27.1 90 ILE 143.5 100.0 30.4 91 THR 104.9 98.1 51.7 92 HIS 108.6 72.3 59.3 93 THR 49.9 46.6 68.5 94 GLY 0.0 0.0 76.9 95 ALA 67.2 92.5 62.7 96 SER 1.7 2.0 86.4 97 GLY 0.0 0.0 88.9 98 ASN 53.9 44.6 84.5 99 ASN 38.8 32.1 79.4 100 PHE 152.7 91.5 52.2 101 VAL 60.3 50.7 68.5 102 GLU 63.3 45.7 61.0 103 CYS 97.9 98.7 46.9 104 THR 10.0 9.4 87.8