Protein Data Bank File : 1lpba Title : HYDROLASE(CARBOXYLIC ESTERASE) 19-AUG-94 1LPB Number of Amino Acid Residues : 85 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 GLY ILE ILE ILE ASN LEU ASP GLU GLY GLU 10 LEU CYS LEU ASN SER ALA GLN CYS LYS SER 20 ASN CYS CYS GLN HIS ASP THR ILE LEU SER 30 LEU SER ARG CYS ALA LEU LYS ALA ARG GLU 40 ASN SER GLU CYS SER ALA PHE THR LEU TYR 50 GLY VAL TYR TYR LYS CYS PRO CYS GLU ARG 60 GLY LEU THR CYS GLU GLY ASP LYS SER LEU 70 VAL GLY SER ILE THR ASN THR ASN PHE GLY 80 ILE CYS HIS ASN VAL Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 GLY 0.0 146.9 -177.9 2 ILE 30.9 73.5 179.7 175.4 55.3 3 ILE -176.8 116.6 -175.8 -177.8 165.7 4 ILE -95.5 171.9 179.2 -140.8 76.5 5 ASN 54.4 34.0 179.1 -100.1 13.4 6 LEU -65.4 153.7 179.0 -94.6 38.2 7 ASP -95.9 164.1 -179.9 -61.5 -54.2 8 GLU -60.0 141.5 -178.7 -65.0 96.4 44.1 9 GLY 86.7 -13.9 178.1 10 GLU -81.6 139.2 -179.9 -139.3 139.5 37.3 11 LEU -63.1 150.5 179.4 -65.1 138.7 12 CYS -151.0 162.1 179.8 44.6 13 LEU -110.3 -26.6 -178.3 -86.2 -61.6 14 ASN -153.6 145.3 -179.9 -178.4 -84.1 15 SER -53.0 -26.7 179.4 -67.2 16 ALA -56.8 -31.5 -179.4 17 GLN -73.4 -22.9 -176.4 -39.7 -179.4 -125.5 18 CYS -91.4 132.6 178.4 -54.1 19 LYS -54.2 -51.1 175.8 -65.4 169.8 164.8 -178.6 20 SER -79.1 119.7 -177.1 62.6 21 ASN -75.9 70.7 179.8 -47.5 110.9 22 CYS -157.7 101.5 176.0 178.2 23 CYS -91.1 126.4 -174.8 -178.2 24 GLN -132.1 155.5 175.8 -164.2 -98.7 9.8 25 HIS -153.4 146.4 -177.8 67.2 157.6 26 ASP -76.5 -33.0 179.6 -66.9 65.5 27 THR -132.8 172.3 -179.1 64.9 28 ILE -64.1 -48.4 179.8 -178.2 54.5 29 LEU -98.5 74.3 179.2 -72.3 162.9 30 SER -166.1 145.0 -178.4 58.6 31 LEU -63.5 144.3 -179.0 -62.8 175.0 32 SER -112.0 141.2 -179.4 68.5 33 ARG -130.2 166.8 -179.1 -46.4 -170.9 -147.1 -92.2 34 CYS -69.5 133.7 180.0 -56.3 35 ALA -131.3 157.3 178.4 36 LEU -73.5 149.2 178.7 -61.5 163.2 37 LYS -67.4 151.9 -179.0 -61.5 -165.5 -153.5 -68.0 38 ALA -60.6 130.0 178.4 39 ARG -78.8 171.7 180.0 79.3 -170.3 55.9 -178.9 40 GLU -57.9 143.1 177.9 -172.4 164.3 -29.4 41 ASN 70.5 7.7 178.6 -58.0 -54.0 42 SER -112.5 171.1 -178.7 58.9 43 GLU -67.9 141.5 -178.4 -72.4 157.9 38.0 44 CYS -141.1 -172.6 178.1 44.9 45 SER -141.2 150.9 178.6 173.1 46 ALA -76.1 139.2 179.4 47 PHE -40.2 137.9 -179.1 155.6 77.1 48 THR -125.4 173.8 179.6 61.1 49 LEU -100.4 -15.1 -179.4 71.9 -51.2 50 TYR -76.4 -10.1 178.7 -73.8 -48.4 51 GLY 86.6 -30.5 178.9 52 VAL -120.8 163.4 -178.4 -44.0 53 TYR -129.7 160.4 174.1 -63.1 86.7 54 TYR -97.4 -20.9 177.7 -75.4 -76.2 55 LYS -142.9 146.4 -177.6 -67.8 177.7 -173.4 178.5 56 CYS -86.4 154.2 178.4 -71.8 57 PRO -69.0 163.8 -179.3 26.6 -43.1 58 CYS -74.8 168.3 178.1 -53.1 59 GLU -77.4 -177.9 -177.8 -60.2 166.8 -57.4 60 ARG -61.9 143.7 178.7 13.7 -174.6 61.8 102.6 61 GLY 74.3 6.0 -178.3 62 LEU -111.3 146.3 179.1 -105.0 36.1 63 THR -113.2 131.9 177.8 -53.4 64 CYS -86.8 97.6 -179.9 -175.3 65 GLU -85.7 128.9 179.0 -63.4 -177.6 -2.5 66 GLY 175.1 177.1 179.8 67 ASP -73.5 127.0 178.8 -78.8 82.7 68 LYS -109.3 117.0 -179.1 -162.3 172.6 -44.6 -56.4 69 SER -118.0 167.0 178.0 -177.6 70 LEU -75.0 -39.5 177.2 177.7 -82.2 71 VAL -67.9 -46.2 179.2 157.8 72 GLY -53.6 -31.5 178.8 73 SER -72.3 -51.6 -179.5 -52.0 74 ILE -67.7 -23.2 179.6 120.5 -74.8 75 THR -95.7 -5.1 179.7 -163.6 76 ASN 60.4 49.7 -177.9 -159.4 -106.8 77 THR -134.5 30.2 179.8 -55.6 78 ASN -84.5 67.7 -178.8 -86.2 -48.4 79 PHE -76.1 154.6 179.4 -61.4 -23.7 80 GLY -170.3 -166.0 179.0 81 ILE -127.2 145.3 -180.0 -64.8 175.3 82 CYS -70.5 114.1 -179.9 -63.7 83 HIS -123.2 146.0 178.7 -78.4 143.9 84 ASN -75.5 110.4 180.0 -172.8 175.4 85 VAL 69.8 116.2 0.0 139.2 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 GLY -1.461 1.603 32.125 2 ILE -4.145 -0.647 33.662 3 ILE -5.940 2.196 35.406 4 ILE -9.325 3.444 34.252 5 ASN -11.180 6.789 34.642 6 LEU -8.038 8.861 34.092 7 ASP -7.999 12.664 34.002 8 GLU -6.775 14.959 31.279 9 GLY -2.984 15.182 31.209 10 GLU -2.647 11.735 32.770 11 LEU -0.649 9.292 30.604 12 CYS -2.572 6.608 28.773 13 LEU -2.096 3.701 26.436 14 ASN -5.666 3.690 25.116 15 SER -8.771 5.980 25.030 16 ALA -10.761 3.473 27.064 17 GLN -8.745 4.668 30.078 18 CYS -9.672 8.356 29.673 19 LYS -12.838 9.954 31.056 20 SER -12.717 12.194 27.985 21 ASN -12.519 9.339 25.532 22 CYS -9.381 10.564 23.818 23 CYS -5.870 9.388 24.608 24 GLN -3.864 11.796 22.505 25 HIS -0.349 12.578 21.365 26 ASP 1.036 15.098 18.889 27 THR 3.584 12.914 17.124 28 ILE 4.340 9.225 16.558 29 LEU 7.318 9.016 18.915 30 SER 5.860 10.811 21.940 31 LEU 3.880 9.916 25.057 32 SER 0.109 10.224 24.991 33 ARG -2.143 11.618 27.715 34 CYS -5.854 12.139 28.144 35 ALA -7.143 15.182 26.281 36 LEU -10.545 16.848 25.866 37 LYS -12.514 16.113 22.680 38 ALA -12.413 18.802 19.963 39 ARG -14.874 21.691 20.436 40 GLU -16.800 23.105 17.462 41 ASN -14.767 24.599 14.577 42 SER -11.413 23.207 15.657 43 GLU -9.337 20.298 14.392 44 CYS -10.377 16.709 15.023 45 SER -9.890 13.138 13.905 46 ALA -12.311 10.524 12.738 47 PHE -12.989 7.889 15.433 48 THR -10.264 5.244 15.223 49 LEU -9.287 1.612 15.882 50 TYR -5.760 2.440 17.068 51 GLY -6.942 3.670 20.454 52 VAL -5.030 6.949 20.349 53 TYR -5.372 10.105 18.260 54 TYR -3.136 12.885 16.967 55 LYS -6.280 15.012 17.185 56 CYS -9.352 14.222 19.230 57 PRO -12.826 13.334 17.959 58 CYS -15.484 16.061 18.338 59 GLU -17.871 16.577 21.236 60 ARG -21.516 15.523 21.164 61 GLY -23.730 16.407 18.243 62 LEU -20.713 17.324 16.218 63 THR -19.302 15.864 13.012 64 CYS -15.639 15.864 12.150 65 GLU -15.713 16.911 8.494 66 GLY -12.690 16.213 6.350 67 ASP -11.271 13.790 3.828 68 LYS -11.567 10.239 5.056 69 SER -9.177 7.931 3.191 70 LEU -8.220 4.254 3.206 71 VAL -4.617 5.307 3.657 72 GLY -5.809 7.879 6.226 73 SER -7.419 5.103 8.240 74 ILE -4.338 2.827 8.462 75 THR -2.228 5.883 9.084 76 ASN -4.552 7.466 11.762 77 THR -4.720 10.740 9.786 78 ASN -8.413 11.069 8.979 79 PHE -8.362 14.730 9.975 80 GLY -11.174 17.276 9.656 81 ILE -12.852 20.111 11.608 82 CYS -15.741 19.871 14.064 83 HIS -18.970 21.042 12.433 84 ASN -22.577 21.292 13.544 85 VAL -24.206 18.693 11.328 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C S S S S/S S S S S S 10 S S S T T T T T T T 20 T/S S S S S S C C S S 30 S S S S/S S S S S C C 40 S S S S S C C T T T 50 T/S S S S/S S S S S S S 60 S S S S S S S C H H 70 H H H H H H C S S S 80 S S S S/S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S B t B T t 10 B S g G G G B S S 20 S e E E e S S S S S 30 E E e B t T 40 T e E E E e S S 50 e E E S S B t T 60 e E E E E S h H 70 H H H H H h t e E E 80 E E E E e Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 GLY 14.5 41.6 68.0 2 ILE 0.0 0.0 90.3 3 ILE 42.0 29.3 79.6 4 ILE 31.8 22.2 76.5 5 ASN 28.2 23.3 68.8 6 LEU 140.5 95.1 50.0 7 ASP 43.0 38.9 78.3 8 GLU 74.4 53.7 60.1 9 GLY 4.8 13.7 70.9 10 GLU 58.8 42.4 70.6 11 LEU 67.9 45.9 66.9 12 CYS 99.2 100.0 46.5 13 LEU 34.3 23.2 78.9 14 ASN 59.1 48.9 61.9 15 SER 68.7 82.2 58.0 16 ALA 14.4 19.9 79.7 17 GLN 134.9 90.7 50.3 18 CYS 99.2 100.0 54.0 19 LYS 74.2 42.8 85.1 20 SER 68.4 81.8 57.6 21 ASN 47.0 38.8 80.4 22 CYS 99.2 100.0 41.4 23 CYS 99.2 100.0 51.0 24 GLN 114.9 77.3 58.3 25 HIS 132.5 88.2 60.4 26 ASP 15.8 14.3 81.4 27 THR 31.0 29.0 71.3 28 ILE 24.4 17.0 74.3 29 LEU 4.0 2.7 83.5 30 SER 43.9 52.5 81.7 31 LEU 32.5 22.0 79.5 32 SER 76.3 91.2 54.9 33 ARG 103.8 49.7 65.3 34 CYS 99.0 99.8 50.0 35 ALA 43.9 60.5 65.5 36 LEU 41.4 28.0 80.5 37 LYS 121.6 70.1 59.1 38 ALA 60.8 83.7 66.5 39 ARG 36.3 17.4 86.0 40 GLU 72.1 52.0 64.2 41 ASN 40.3 33.3 73.9 42 SER 39.9 47.7 70.7 43 GLU 49.6 35.8 72.8 44 CYS 99.2 100.0 44.7 45 SER 83.4 99.7 48.6 46 ALA 57.9 79.8 70.3 47 PHE 16.1 9.6 84.4 48 THR 99.1 92.7 61.0 49 LEU 42.2 28.5 71.6 50 TYR 96.4 53.2 67.1 51 GLY 24.2 69.5 73.2 52 VAL 91.1 76.7 62.5 53 TYR 170.6 94.3 55.6 54 TYR 142.8 78.9 58.1 55 LYS 118.5 68.4 56.6 56 CYS 93.1 93.9 41.6 57 PRO 103.7 83.3 56.3 58 CYS 97.2 98.0 47.3 59 GLU 64.6 46.6 62.9 60 ARG 0.0 0.0 90.2 61 GLY 0.0 0.0 80.5 62 LEU 132.8 89.8 63.4 63 THR 44.8 41.9 75.1 64 CYS 90.5 91.2 55.2 65 GLU 65.9 47.5 74.8 66 GLY 15.0 43.2 76.2 67 ASP 0.0 0.0 87.8 68 LYS 68.1 39.3 80.7 69 SER 30.7 36.7 75.1 70 LEU 15.6 10.6 76.9 71 VAL 21.4 18.0 67.5 72 GLY 28.5 81.9 56.1 73 SER 43.4 51.9 75.4 74 ILE 52.7 36.8 65.5 75 THR 58.1 54.3 61.5 76 ASN 112.8 93.3 52.7 77 THR 52.9 49.5 61.6 78 ASN 114.0 94.3 58.1 79 PHE 116.9 70.1 63.9 80 GLY 25.6 73.5 56.7 81 ILE 73.1 51.0 67.0 82 CYS 99.2 100.0 42.9 83 HIS 89.9 59.8 69.3 84 ASN 40.0 33.1 74.2 85 VAL 0.0 0.0 95.1