Protein Data Bank File : 1bc4 Title : HYDROLASE 05-MAY-98 1BC4 Number of Amino Acid Residues : 110 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 ASN TRP ALA THR PHE GLN GLN LYS HIS ILE 10 ILE ASN THR PRO ILE ILE ASN CYS ASN THR 20 ILE MET ASP ASN ASN ILE TYR ILE VAL GLY 30 GLY GLN CYS LYS ARG VAL ASN THR PHE ILE 40 ILE SER SER ALA THR THR VAL LYS ALA ILE 50 CYS THR GLY VAL ILE ASN MET ASN VAL LEU 60 SER THR THR ARG PHE GLN LEU ASN THR CYS 70 THR ARG THR SER ILE THR PRO ARG PRO CYS 80 PRO TYR SER SER ARG THR GLU THR ASN TYR 90 ILE CYS VAL LYS CYS GLU ASN GLN TYR PRO 100 VAL HIS PHE ALA GLY ILE GLY ARG CYS PRO Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 ASN 0.0 163.9 -178.2 171.4 -118.1 2 TRP -70.4 -37.4 -179.0 -125.6 123.4 3 ALA -68.5 -57.0 179.7 4 THR -62.5 -32.3 177.8 -38.7 5 PHE -72.6 -25.8 178.0 175.8 -90.1 6 GLN -54.9 -33.7 176.3 -171.2 157.1 73.5 7 GLN -80.4 -38.0 -179.7 -102.0 151.0 105.2 8 LYS -44.5 -57.3 179.7 -178.1 73.2 78.1 97.6 9 HIS -99.6 -31.0 -174.7 -77.1 46.3 10 ILE -102.9 65.6 173.2 -39.4 -55.7 11 ILE -95.3 62.8 -176.8 -46.5 93.3 12 ASN -74.2 81.1 179.2 -154.7 41.3 13 THR -118.5 106.9 -179.8 52.0 14 PRO -81.5 37.2 179.6 23.4 -20.0 15 ILE -113.1 164.6 -179.7 -54.4 94.8 16 ILE -97.3 34.0 179.0 56.7 166.2 17 ASN -126.2 91.4 -178.6 -47.2 124.0 18 CYS -76.3 -15.9 -179.9 -46.3 19 ASN -83.0 -50.4 -179.7 44.8 88.2 20 THR -58.2 -34.3 -179.7 28.5 21 ILE -77.0 -39.1 179.8 59.3 93.5 22 MET -93.5 12.8 179.5 67.7 99.7 -177.8 23 ASP -60.3 91.8 -178.7 -88.7 -5.1 24 ASN -172.3 155.5 179.2 -175.3 -134.8 25 ASN -71.9 -10.2 -179.8 -171.7 76.1 26 ILE -85.8 8.4 -180.0 -55.7 171.8 27 TYR -136.0 57.2 -179.7 -76.6 -68.6 28 ILE -151.5 145.9 178.9 -47.5 178.2 29 VAL -109.7 -168.6 -177.8 82.3 30 GLY -97.5 71.4 178.7 31 GLY -165.7 -63.4 179.9 32 GLN -165.2 -65.4 179.3 -89.8 -157.0 133.2 33 CYS -141.7 167.8 -179.6 53.7 34 LYS -77.5 149.7 -179.7 -87.8 176.9 -167.6 -88.1 35 ARG -77.1 -23.8 -179.5 -94.7 -167.2 -149.8 167.3 36 VAL -150.3 103.4 177.8 -170.7 37 ASN -92.6 76.5 -177.8 -45.1 -9.7 38 THR -79.2 116.5 178.8 -51.5 39 PHE -107.0 163.6 178.7 -52.3 -48.3 40 ILE -126.7 124.6 -179.0 -43.9 -59.0 41 ILE -96.5 98.0 -179.5 47.3 172.0 42 SER -176.3 157.9 -179.9 179.4 43 SER -63.9 128.2 -179.4 45.3 44 ALA -54.4 -25.1 -178.5 45 THR -76.7 -33.9 178.5 178.1 46 THR -65.2 -39.9 177.7 34.2 47 VAL -67.8 -31.9 179.7 -172.9 48 LYS -67.4 -23.1 -179.8 -174.3 -158.4 98.6 169.6 49 ALA -79.5 -40.2 179.8 50 ILE -69.4 -20.7 -179.8 53.2 163.5 51 CYS -102.4 25.1 179.8 -135.2 52 THR -96.3 114.3 -179.9 -47.0 53 GLY -160.5 -62.7 -179.6 54 VAL -152.8 -169.4 -179.1 79.5 55 ILE -88.6 26.7 179.8 -170.7 162.5 56 ASN 171.5 110.5 -178.6 -157.6 87.5 57 MET -161.9 -172.5 178.6 -140.0 -144.8 138.5 58 ASN -143.0 114.6 -179.3 -99.3 123.7 59 VAL -125.3 169.6 -179.2 -168.5 60 LEU -144.8 120.6 177.6 48.1 150.2 61 SER -59.2 97.3 -178.7 22.9 62 THR -80.9 -40.3 -179.7 33.6 63 THR -56.6 -92.0 180.0 33.7 64 ARG 177.9 103.1 179.5 56.0 -141.7 -161.3 -111.0 65 PHE -98.3 44.5 179.4 -78.3 72.1 66 GLN 18.2 107.4 179.9 -68.2 140.7 -97.9 67 LEU -102.4 154.0 177.4 42.1 49.6 68 ASN -117.8 94.8 -176.6 -157.1 63.3 69 THR -100.9 126.8 175.7 -46.3 70 CYS -106.8 104.8 -176.9 -66.8 71 THR -101.2 131.4 178.4 -45.9 72 ARG -63.0 105.8 -178.5 -168.1 -154.8 142.3 -84.0 73 THR -105.9 -92.9 -179.1 41.1 74 SER -177.3 177.9 180.0 -146.3 75 ILE 63.8 139.5 180.0 -51.2 168.8 76 THR 59.4 58.8 179.6 -45.6 77 PRO -76.3 125.6 -179.3 22.3 -21.9 78 ARG -132.7 43.1 -3.1 -161.6 -178.4 92.3 115.3 79 PRO -88.4 -11.5 -179.6 23.8 -16.9 80 CYS -106.1 115.5 179.6 -67.6 81 PRO -76.6 145.7 -179.6 22.3 -21.1 82 TYR -131.7 134.8 178.7 -80.7 73.5 83 SER -105.8 109.8 -178.8 53.8 84 SER -83.6 133.9 179.3 -44.1 85 ARG -148.7 125.8 -179.7 -174.6 141.9 143.9 -92.4 86 THR -105.7 146.4 -179.9 -49.8 87 GLU -172.2 -172.1 179.9 56.0 179.2 -53.3 88 THR -57.0 139.4 -179.5 -54.6 89 ASN -112.8 88.0 175.6 -173.3 -143.2 90 TYR -95.8 96.2 -175.8 35.8 -87.1 91 ILE -130.3 163.7 -179.2 -171.4 168.6 92 CYS -105.7 114.1 179.6 -169.8 93 VAL -104.6 161.6 179.4 61.5 94 LYS -118.3 144.5 -177.3 -173.9 -169.2 -107.8 -165.3 95 CYS -119.0 124.8 175.0 -28.1 96 GLU -129.9 144.0 -175.8 172.3 172.0 -67.4 97 ASN 56.9 15.9 -179.7 -101.6 118.1 98 GLN 78.3 -15.4 177.6 -55.6 -153.4 -95.9 99 TYR -98.3 148.7 179.8 107.4 66.7 100 PRO -63.2 91.3 -177.2 19.9 -26.5 101 VAL -87.6 -11.1 -176.7 171.7 102 HIS -151.9 148.3 178.7 6.9 -129.8 103 PHE -99.7 122.4 -179.5 -132.3 -30.5 104 ALA -68.7 -29.2 179.8 105 GLY 129.5 -149.1 -179.3 106 ILE -56.4 178.6 -179.2 53.2 165.7 107 GLY -63.2 -56.6 -178.9 108 ARG -49.4 110.9 -179.7 -78.1 177.1 90.3 116.4 109 CYS -127.5 169.5 179.7 -118.3 110 PRO -77.9 -0.1 0.0 22.9 -21.7 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 ASN -2.227 -0.441 7.791 2 TRP -1.781 -2.860 4.795 3 ALA -4.690 -5.194 5.892 4 THR -7.337 -2.479 6.526 5 PHE -5.926 -0.717 3.418 6 GLN -6.447 -4.034 1.526 7 GLN -10.110 -3.003 1.774 8 LYS -9.167 0.692 1.112 9 HIS -8.250 -0.002 -2.584 10 ILE -9.298 -3.686 -3.012 11 ILE -13.082 -3.928 -2.367 12 ASN -13.226 -6.323 -5.369 13 THR -16.936 -7.243 -5.166 14 PRO -18.543 -8.032 -8.609 15 ILE -22.092 -7.736 -7.101 16 ILE -24.677 -4.902 -7.441 17 ASN -24.886 -4.415 -3.625 18 CYS -22.470 -1.634 -2.489 19 ASN -23.978 -1.596 1.084 20 THR -23.624 -5.331 1.926 21 ILE -19.983 -5.177 0.699 22 MET -19.141 -1.952 2.634 23 ASP -21.231 -3.092 5.679 24 ASN -18.648 -1.934 8.292 25 ASN -17.870 0.988 10.658 26 ILE -14.832 1.767 8.396 27 TYR -17.193 3.124 5.642 28 ILE -19.384 5.880 7.278 29 VAL -19.195 9.681 7.792 30 GLY -20.964 11.943 10.400 31 GLY -24.478 12.287 8.869 32 GLN -25.986 9.019 7.514 33 CYS -23.957 7.503 4.641 34 LYS -20.939 8.535 2.491 35 ARG -21.558 10.676 -0.635 36 VAL -19.123 8.540 -2.711 37 ASN -18.073 4.972 -1.781 38 THR -15.388 4.728 -4.492 39 PHE -13.886 1.207 -4.617 40 ILE -11.024 -0.001 -6.911 41 ILE -11.182 -3.420 -8.661 42 SER -7.554 -4.585 -9.087 43 SER -4.819 -6.632 -7.310 44 ALA -3.510 -4.607 -4.298 45 THR 0.028 -5.512 -5.509 46 THR -0.378 -3.875 -8.989 47 VAL -1.390 -0.696 -7.135 48 LYS 1.631 -1.338 -4.843 49 ALA 3.894 -1.086 -7.956 50 ILE 2.594 2.371 -9.074 51 CYS 3.196 3.678 -5.494 52 THR 6.842 2.411 -5.386 53 GLY 9.348 5.302 -4.986 54 VAL 10.375 6.182 -1.376 55 ILE 8.963 6.040 2.260 56 ASN 6.696 9.112 1.515 57 MET 5.614 10.352 -1.970 58 ASN 2.682 11.103 -4.326 59 VAL 2.102 9.075 -7.550 60 LEU -0.909 8.685 -9.909 61 SER -2.152 5.620 -11.877 62 THR -2.098 7.309 -15.339 63 THR -2.755 4.101 -17.345 64 ARG -6.036 2.653 -15.875 65 PHE -6.539 0.598 -12.654 66 GLN -10.310 -0.039 -13.485 67 LEU -12.434 1.439 -10.614 68 ASN -15.866 0.320 -9.295 69 THR -17.572 3.504 -7.944 70 CYS -20.888 3.401 -6.065 71 THR -22.001 7.071 -5.842 72 ARG -24.839 8.201 -3.506 73 THR -27.352 9.535 -6.100 74 SER -31.151 9.406 -5.351 75 ILE -34.419 7.429 -5.805 76 THR -34.791 3.979 -4.150 77 PRO -33.312 5.086 -0.752 78 ARG -32.282 2.049 1.369 79 PRO -31.856 4.543 2.910 80 CYS -28.996 5.796 0.640 81 PRO -29.304 4.770 -3.086 82 TYR -26.038 3.972 -4.963 83 SER -25.348 3.901 -8.727 84 SER -22.511 1.454 -9.550 85 ARG -20.403 2.258 -12.652 86 THR -17.044 0.709 -13.696 87 GLU -14.533 2.389 -16.068 88 THR -10.868 3.492 -16.536 89 ASN -9.242 4.389 -13.169 90 TYR -6.895 7.386 -13.527 91 ILE -6.436 8.199 -9.818 92 CYS -3.817 9.741 -7.477 93 VAL -2.488 7.413 -4.734 94 LYS -0.054 8.279 -1.898 95 CYS 2.926 6.082 -0.774 96 GLU 4.277 5.631 2.793 97 ASN 6.543 2.656 3.719 98 GLN 6.480 2.272 -0.158 99 TYR 2.919 0.760 -0.064 100 PRO -0.085 2.986 -0.930 101 VAL -0.892 3.820 2.717 102 HIS -3.204 6.756 1.867 103 PHE -5.342 7.828 -1.132 104 ALA -4.471 11.335 -2.469 105 GLY -7.872 11.490 -4.251 106 ILE -8.839 11.757 -7.962 107 GLY -6.231 11.387 -10.756 108 ARG -5.402 15.129 -11.175 109 CYS -2.588 15.660 -8.611 110 PRO 0.098 18.380 -8.009 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 H H H H H H H H H H 10 S S S S C C H H H H 20 H H H T T T T C T T 30 T T/S S S S/S S S S S S 40 S S S/H H H H H H H H 50 H H C C S S S S S S 60 S/T T T T S S S S S S 70 S S/S S S S C T T/P T T/S 80 S S S S S S S S/S S S 90 S S/S S S S/T T T T C C 100 S S S S C C S S S S Kabsch-Sander Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 h H H H H H H H H h 10 S S h H H H 20 H H h t T T t S 30 S S S e E E E E E 40 e S h H H H H H H H 50 h t S S e E E E E E 60 E S e E E E E 70 E E e S S S S S S 80 e E E E E E E e 90 E E E E E E e T E E 100 E E E E E E e Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 ASN 27.0 22.3 81.5 2 TRP 126.4 61.7 50.6 3 ALA 10.6 14.6 84.4 4 THR 49.4 46.2 65.4 5 PHE 161.7 96.9 42.8 6 GLN 48.2 32.4 67.7 7 GLN 66.1 44.5 70.9 8 LYS 83.8 48.3 68.2 9 HIS 149.5 99.5 23.6 10 ILE 121.6 84.7 51.5 11 ILE 132.7 92.4 50.7 12 ASN 49.3 40.8 65.7 13 THR 76.8 71.9 49.1 14 PRO 21.2 17.0 79.4 15 ILE 64.6 45.0 64.0 16 ILE 7.1 4.9 85.6 17 ASN 66.4 54.9 69.5 18 CYS 93.1 93.8 48.4 19 ASN 73.0 60.4 65.7 20 THR 43.9 41.0 76.8 21 ILE 124.1 86.5 46.5 22 MET 130.8 82.1 53.2 23 ASP 39.9 36.1 70.5 24 ASN 61.5 50.8 65.6 25 ASN 5.9 4.9 79.1 26 ILE 63.6 44.3 67.9 27 TYR 155.2 85.7 43.0 28 ILE 75.3 52.5 78.0 29 VAL 39.5 33.2 77.0 30 GLY 0.0 0.0 77.6 31 GLY 0.0 0.0 75.9 32 GLN 28.4 19.1 76.7 33 CYS 83.4 84.1 52.8 34 LYS 107.9 62.2 69.5 35 ARG 22.5 10.8 83.8 36 VAL 59.6 50.2 69.0 37 ASN 115.9 95.8 39.6 38 THR 73.0 68.3 54.0 39 PHE 164.5 98.6 41.3 40 ILE 140.1 97.6 44.4 41 ILE 108.3 75.5 62.9 42 SER 57.9 69.3 63.6 43 SER 34.8 41.6 66.0 44 ALA 63.3 87.2 44.8 45 THR 28.3 26.5 68.4 46 THR 44.6 41.7 71.8 47 VAL 114.9 96.7 35.0 48 LYS 78.6 45.3 68.6 49 ALA 19.0 26.1 80.8 50 ILE 107.0 74.6 49.7 51 CYS 99.2 100.0 44.0 52 THR 52.2 48.9 78.0 53 GLY 13.8 39.6 68.5 54 VAL 41.2 34.7 72.0 55 ILE 35.2 24.5 71.6 56 ASN 36.4 30.1 74.7 57 MET 68.0 42.7 69.8 58 ASN 72.4 59.9 46.6 59 VAL 82.6 69.6 52.4 60 LEU 85.5 57.8 60.9 61 SER 81.8 97.8 49.1 62 THR 23.1 21.6 72.5 63 THR 20.3 18.9 76.0 64 ARG 59.2 28.3 76.3 65 PHE 139.0 83.3 54.4 66 GLN 44.8 30.1 71.6 67 LEU 122.4 82.8 61.8 68 ASN 102.3 84.6 55.8 69 THR 84.7 79.2 61.0 70 CYS 98.6 99.4 44.8 71 THR 61.0 57.1 60.8 72 ARG 130.5 62.5 60.8 73 THR 47.9 44.8 72.3 74 SER 22.6 27.0 69.3 75 ILE 4.0 2.8 84.4 76 THR 7.1 6.6 70.0 77 PRO 47.7 38.3 69.5 78 ARG 56.2 26.9 84.6 79 PRO 32.5 26.1 75.1 80 CYS 91.6 92.3 42.6 81 PRO 108.2 86.9 67.2 82 TYR 166.6 92.1 56.4 83 SER 33.0 39.5 74.4 84 SER 60.2 72.0 63.7 85 ARG 47.1 22.5 90.0 86 THR 61.2 57.2 63.6 87 GLU 65.9 47.6 75.8 88 THR 51.6 48.3 58.7 89 ASN 119.2 98.6 35.6 90 TYR 51.9 28.7 80.4 91 ILE 125.4 87.4 54.5 92 CYS 99.0 99.8 44.2 93 VAL 118.6 99.8 39.5 94 LYS 101.8 58.7 69.2 95 CYS 99.2 100.0 51.7 96 GLU 73.2 52.8 67.0 97 ASN 33.9 28.0 61.0 98 GLN 63.1 42.5 72.8 99 TYR 164.3 90.7 40.7 100 PRO 124.5 100.0 34.4 101 VAL 95.3 80.3 58.4 102 HIS 105.5 70.3 63.2 103 PHE 137.9 82.7 48.5 104 ALA 57.3 78.9 60.1 105 GLY 3.8 11.0 75.5 106 ILE 17.7 12.3 78.1 107 GLY 30.8 88.4 56.3 108 ARG 4.4 2.1 86.8 109 CYS 87.8 88.5 47.3 110 PRO 20.3 16.3 76.9