Protein Data Bank File : 1bmqb Title : HYDROLASE 24-JUL-98 1BMQ Number of Amino Acid Residues : 88 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 ALA ILE LYS LYS ALA HIS ILE GLU LYS ASP 10 PHE ILE ALA PHE CYS SER SER THR PRO ASP 20 ASN VAL SER TRP ARG HIS PRO THR MET GLY 30 SER VAL PHE ILE GLY ARG LEU ILE GLU HIS 40 MET GLN GLU TYR ALA CYS SER CYS ASP VAL 50 GLU GLU ILE PHE ARG LYS VAL ARG PHE SER 60 PHE GLU GLN PRO ASP GLY ARG ALA GLN MET 70 PRO THR THR GLU ARG VAL THR LEU THR ARG 80 CYS PHE TYR LEU PHE PRO GLY HIS Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 ALA 0.0 166.4 179.2 2 ILE -82.5 145.9 179.5 28.7 131.1 3 LYS -134.1 155.3 179.9 -98.0 126.0 76.3 -96.5 4 LYS -89.5 141.4 178.8 -52.9 161.5 140.9 157.6 5 ALA -133.5 138.1 179.6 6 HIS -52.0 135.7 -179.7 -69.3 -68.5 7 ILE -67.4 -36.4 179.9 -167.1 138.2 8 GLU -126.7 123.6 179.6 -156.6 -169.1 -63.1 9 LYS -170.4 162.1 179.6 -169.1 164.3 86.6 44.2 10 ASP 60.7 33.5 179.0 -48.4 -88.1 11 PHE -106.4 166.4 179.3 -89.5 -71.7 12 ILE -175.1 109.8 179.6 155.1 112.4 13 ALA -100.2 146.6 179.0 14 PHE -133.9 96.2 -179.1 -160.8 28.5 15 CYS -81.2 154.2 -178.6 -64.7 16 SER -72.3 -17.0 -179.4 33.0 17 SER -159.6 -171.1 179.6 72.5 18 THR -100.7 163.3 -179.8 26.9 19 PRO -51.7 150.1 179.6 -23.0 32.1 20 ASP 66.0 -11.0 -178.4 -49.5 -73.1 21 ASN -105.8 151.9 -179.2 -44.6 127.3 22 VAL -83.4 168.0 178.5 -54.6 23 SER -126.2 148.4 -177.4 -75.7 24 TRP -100.3 145.7 -180.0 -65.7 91.5 25 ARG -140.7 139.6 179.7 -166.4 -156.3 65.6 -126.3 26 HIS -104.6 124.8 -180.0 -178.2 168.6 27 PRO -56.0 -6.9 -179.1 -21.7 32.9 28 THR -122.7 -22.0 179.7 -81.4 29 MET -122.8 8.6 179.9 -41.3 163.8 117.1 30 GLY 58.7 -171.9 -179.3 31 SER -48.3 153.5 -179.7 -66.6 32 VAL -90.3 -39.5 179.8 -171.8 33 PHE -57.6 -45.4 -179.7 168.1 78.8 34 ILE -63.2 -41.6 180.0 -76.5 -62.8 35 GLY -68.5 -35.0 179.9 36 ARG -72.3 -43.2 -179.8 -160.4 67.7 61.4 85.1 37 LEU -60.3 -40.3 179.0 178.2 75.1 38 ILE -64.9 -55.5 179.1 -76.9 166.7 39 GLU -45.6 -45.5 -179.0 -98.2 174.4 179.4 40 HIS -75.8 -38.7 179.7 -76.7 83.9 41 MET -58.9 -48.7 -179.7 -79.8 -78.3 -127.5 42 GLN -57.8 -32.3 -177.9 -52.9 -173.0 169.5 43 GLU -88.8 -48.6 -177.9 179.6 80.7 29.5 44 TYR -100.6 2.6 -179.9 -45.6 -93.5 45 ALA -55.7 -29.5 -178.3 46 CYS -80.6 -18.7 -179.2 46.1 47 SER -131.8 -5.2 180.0 19.8 48 CYS -122.8 139.0 178.2 -47.2 49 ASP -72.1 154.4 -178.5 44.2 -70.9 50 VAL -48.1 -26.5 -179.6 -44.7 51 GLU -72.1 -38.8 179.6 -119.5 173.8 118.0 52 GLU -71.9 -33.5 -179.8 -160.0 163.6 -176.2 53 ILE -72.3 -35.1 179.9 -59.1 177.2 54 PHE -66.9 -39.5 179.1 -76.0 -1.6 55 ARG -62.0 -46.6 179.6 172.9 173.6 71.5 59.1 56 LYS -59.7 -28.6 179.4 -123.7 150.8 -122.6 -101.4 57 VAL -74.9 -39.9 179.3 175.1 58 ARG -62.5 -51.7 179.3 -105.7 -150.6 -56.7 -59.3 59 PHE -52.8 -29.9 -179.8 -179.5 -84.2 60 SER -72.2 -10.6 179.7 95.3 61 PHE -109.9 7.6 -178.0 -74.3 -99.0 62 GLU -58.7 -34.9 179.8 -173.2 159.4 45.5 63 GLN -98.8 111.1 -179.9 -91.6 143.5 -145.1 64 PRO -65.1 159.6 -179.4 -13.4 28.3 65 ASP -173.5 70.1 179.4 48.1 21.3 66 GLY 76.6 -62.6 179.4 67 ARG -102.7 60.0 -178.8 -39.9 -82.9 -164.1 -161.6 68 ALA -77.9 148.0 179.0 69 GLN -168.0 137.5 -179.3 66.3 -176.3 109.5 70 MET -118.4 103.3 179.8 178.6 48.1 49.1 71 PRO -62.7 150.1 179.6 -16.6 29.7 72 THR -136.2 141.1 177.8 33.2 73 THR -97.6 123.7 -179.1 77.6 74 GLU -115.8 164.9 179.4 -25.4 -134.9 154.4 75 ARG 39.8 46.8 179.1 -96.0 -152.4 -121.9 -142.8 76 VAL -75.9 128.2 179.9 169.1 77 THR -140.4 25.0 178.3 -173.7 78 LEU -72.8 129.0 -179.5 -70.7 172.1 79 THR -89.4 -17.1 -179.9 48.6 80 ARG -143.3 168.3 179.8 -24.6 148.7 161.4 -103.6 81 CYS -66.7 144.0 179.7 -43.8 82 PHE -116.5 91.2 179.7 174.6 26.7 83 TYR -84.4 140.7 -179.6 -79.0 91.2 84 LEU -87.7 -18.0 179.9 -92.9 -42.6 85 PHE 38.9 54.8 -179.9 -70.3 -68.4 86 PRO -50.8 143.4 -179.3 13.9 -29.3 87 GLY 90.4 -3.0 -179.6 88 HIS -134.2 168.5 0.0 -55.5 -114.5 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 ALA 63.984 46.307 -31.752 2 ILE 61.665 45.623 -28.830 3 LYS 62.899 46.422 -25.333 4 LYS 61.604 45.645 -21.855 5 ALA 60.242 48.384 -19.598 6 HIS 59.194 48.065 -15.944 7 ILE 55.432 47.563 -15.875 8 GLU 55.019 49.895 -12.880 9 LYS 57.249 52.917 -12.266 10 ASP 57.390 56.694 -11.743 11 PHE 54.277 56.558 -9.529 12 ILE 53.499 58.231 -6.186 13 ALA 50.207 58.187 -4.282 14 PHE 49.306 60.635 -1.511 15 CYS 46.303 59.619 0.597 16 SER 44.344 61.942 2.884 17 SER 44.740 59.579 5.834 18 THR 45.927 56.156 6.962 19 PRO 44.028 52.852 6.528 20 ASP 40.873 52.262 8.593 21 ASN 40.934 55.957 9.493 22 VAL 38.792 58.903 8.450 23 SER 39.786 62.184 6.852 24 TRP 38.198 65.491 7.802 25 ARG 36.182 67.949 5.744 26 HIS 34.530 71.270 6.602 27 PRO 31.118 72.012 4.988 28 THR 32.321 75.565 4.369 29 MET 36.041 75.131 3.732 30 GLY 35.954 71.622 2.317 31 SER 38.545 68.955 3.092 32 VAL 41.547 69.802 5.257 33 PHE 44.059 67.585 3.489 34 ILE 43.325 69.390 0.199 35 GLY 43.671 72.867 1.693 36 ARG 46.982 72.043 3.336 37 LEU 48.458 70.449 0.211 38 ILE 47.505 73.544 -1.761 39 GLU 48.885 75.877 0.913 40 HIS 52.182 73.985 0.761 41 MET 52.225 73.539 -2.988 42 GLN 51.939 77.292 -3.513 43 GLU 54.864 77.831 -1.144 44 TYR 57.383 75.022 -1.697 45 ALA 56.633 74.082 -5.307 46 CYS 59.690 76.139 -6.266 47 SER 62.386 74.492 -4.103 48 CYS 61.104 71.092 -2.971 49 ASP 60.387 68.000 -5.057 50 VAL 56.819 66.721 -4.657 51 GLU 58.166 64.097 -2.230 52 GLU 59.627 66.664 0.168 53 ILE 56.430 68.716 0.020 54 PHE 54.226 65.725 0.823 55 ARG 56.387 65.047 3.875 56 LYS 56.020 68.681 4.885 57 VAL 52.255 68.228 4.582 58 ARG 52.425 65.169 6.830 59 PHE 54.558 66.975 9.403 60 SER 51.800 69.608 9.417 61 PHE 49.477 66.913 10.771 62 GLU 51.965 65.782 13.412 63 GLN 50.082 67.338 16.333 64 PRO 46.609 65.789 16.890 65 ASP 43.644 67.940 17.912 66 GLY 40.147 66.454 17.830 67 ARG 40.014 66.190 14.045 68 ALA 43.273 64.254 13.747 69 GLN 44.476 62.549 10.566 70 MET 47.849 61.400 9.227 71 PRO 48.267 61.494 5.417 72 THR 50.398 58.756 3.863 73 THR 52.270 58.437 0.598 74 GLU 51.796 54.965 -0.852 75 ARG 53.187 52.893 -3.709 76 VAL 55.988 55.367 -4.275 77 THR 58.105 54.229 -7.193 78 LEU 59.663 57.521 -8.271 79 THR 63.300 56.943 -9.233 80 ARG 64.286 60.631 -9.094 81 CYS 63.268 63.952 -7.544 82 PHE 60.283 65.580 -9.256 83 TYR 60.638 69.350 -9.261 84 LEU 57.672 71.377 -10.520 85 PHE 59.874 74.356 -11.417 86 PRO 56.895 76.734 -11.277 87 GLY 57.256 79.585 -13.748 88 HIS 58.954 77.199 -16.153 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S S S S S S S S S/S 10 S S S S S S C C C S 20 S S S S S S/T T T T C 30 H H H H H H H H H H 40 H H H H/T T T T C H H 50 H H H H H H H H H H 60 H H C T T T T/S S S S 70 S S S S S/S S S S S/S S 80 S S S S S S S/S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 S S S 10 E E E S S t T T 20 t e E E T T T E 30 E H H H H H H H H H 40 H H H H h T T t h H 50 H H H H H H H H H h 60 T t S S S 70 E E E S S 80 t T T t Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 ALA 0.0 0.0 88.7 2 ILE 0.0 0.0 88.0 3 LYS 18.7 10.8 87.9 4 LYS 0.0 0.0 90.2 5 ALA 4.2 5.8 88.2 6 HIS 26.7 17.8 77.7 7 ILE 0.0 0.0 88.0 8 GLU 77.6 56.0 60.4 9 LYS 108.7 62.7 66.1 10 ASP 49.8 45.1 69.8 11 PHE 51.5 30.8 75.6 12 ILE 121.7 84.8 40.7 13 ALA 31.1 42.8 67.7 14 PHE 157.4 94.4 37.5 15 CYS 45.1 45.5 77.4 16 SER 45.6 54.6 55.8 17 SER 73.4 87.8 73.8 18 THR 72.0 67.3 60.2 19 PRO 34.7 27.9 81.4 20 ASP 0.0 0.0 85.2 21 ASN 48.3 40.0 79.4 22 VAL 22.8 19.2 78.9 23 SER 58.9 70.5 66.9 24 TRP 129.7 63.3 66.7 25 ARG 68.1 32.6 77.1 26 HIS 74.3 49.5 56.3 27 PRO 32.8 26.3 84.3 28 THR 19.2 17.9 76.2 29 MET 30.2 19.0 78.9 30 GLY 9.6 27.5 73.5 31 SER 50.5 60.4 57.4 32 VAL 66.2 55.7 71.7 33 PHE 150.7 90.4 38.6 34 ILE 52.8 36.8 60.2 35 GLY 6.4 18.5 70.1 36 ARG 142.7 68.3 60.2 37 LEU 117.7 79.6 36.4 38 ILE 57.3 39.9 64.6 39 GLU 39.8 28.7 76.8 40 HIS 126.0 83.9 44.7 41 MET 96.2 60.4 48.0 42 GLN 31.2 21.0 77.0 43 GLU 35.5 25.6 78.3 44 TYR 115.6 63.8 53.6 45 ALA 58.7 80.8 48.5 46 CYS 36.2 36.4 77.2 47 SER 20.7 24.7 69.3 48 CYS 87.2 87.9 53.1 49 ASP 94.0 85.1 54.3 50 VAL 109.5 92.1 28.2 51 GLU 73.7 53.2 60.0 52 GLU 75.4 54.4 73.1 53 ILE 143.5 100.0 38.2 54 PHE 146.7 87.9 34.7 55 ARG 98.5 47.2 73.0 56 LYS 109.7 63.3 61.2 57 VAL 118.8 100.0 36.2 58 ARG 144.4 69.1 52.5 59 PHE 38.5 23.1 82.6 60 SER 63.7 76.2 59.6 61 PHE 152.3 91.3 53.6 62 GLU 48.3 34.8 68.9 63 GLN 4.9 3.3 83.0 64 PRO 40.0 32.1 73.7 65 ASP 16.9 15.3 84.7 66 GLY 0.0 0.0 79.9 67 ARG 54.0 25.8 73.3 68 ALA 36.9 50.8 70.2 69 GLN 139.3 93.8 51.2 70 MET 95.9 60.2 59.6 71 PRO 124.5 100.0 37.4 72 THR 73.1 68.4 59.7 73 THR 88.0 82.3 50.2 74 GLU 70.6 50.9 62.8 75 ARG 32.9 15.7 86.8 76 VAL 87.2 73.4 66.6 77 THR 70.0 65.5 67.0 78 LEU 131.6 89.0 53.4 79 THR 49.6 46.4 75.7 80 ARG 15.5 7.4 92.1 81 CYS 33.1 33.4 73.2 82 PHE 70.8 42.5 61.0 83 TYR 110.6 61.1 63.4 84 LEU 94.3 63.8 51.9 85 PHE 43.1 25.8 69.6 86 PRO 75.3 60.5 64.6 87 GLY 0.0 0.0 79.8 88 HIS 23.4 15.6 84.6