Protein Data Bank File : 1b9la Title : ISOMERASE 11-FEB-99 1B9L Number of Amino Acid Residues : 119 Amino Acid Sequence : 1 2 3 4 5 6 7 8 9 10 0 ALA GLN PRO ALA ALA ILE ILE ARG ILE LYS 10 ASN LEU ARG LEU ARG THR PHE ILE GLY ILE 20 LYS GLU GLU GLU ILE ASN ASN ARG GLN ASP 30 ILE VAL ILE ASN VAL THR ILE HIS TYR PRO 40 ALA ASP LYS ALA ARG THR SER GLU ASP ILE 50 ASN ASP ALA LEU ASN TYR ARG THR VAL THR 60 LYS ASN ILE ILE GLN HIS VAL GLU ASN ASN 70 ARG PHE SER LEU LEU GLU LYS LEU THR GLN 80 ASP VAL LEU ASP ILE ALA ARG GLU HIS HIS 90 TRP VAL THR TYR ALA GLU VAL GLU ILE ASP 100 LYS LEU HIS ALA LEU ARG TYR ALA ASP SER 110 VAL SER MET THR LEU SER TRP GLN ARG Main and Side Chain Dihedral Angles : Residue Type Phi Psi Omega Chi 1 Chi 2 Chi 3 Chi 4 1 ALA 0.0 146.6 179.8 2 GLN -126.9 74.5 -179.0 -143.4 103.2 -87.9 3 PRO -32.9 52.5 178.8 -33.5 46.0 4 ALA -145.9 109.0 178.4 5 ALA -84.8 137.4 -179.4 6 ILE -116.4 124.5 -179.9 -52.8 179.4 7 ILE -109.5 129.4 178.9 -76.5 -177.1 8 ARG -120.4 134.8 176.9 -68.0 -166.7 -177.8 74.9 9 ILE -110.7 104.9 -176.5 -65.5 176.8 10 LYS -91.9 127.4 178.2 -66.6 171.9 178.2 166.4 11 ASN 47.3 59.8 178.5 -64.5 141.6 12 LEU -78.6 111.4 -178.0 176.6 67.0 13 ARG -95.3 114.5 -177.3 -53.6 -172.7 -159.4 -102.9 14 LEU -132.9 166.5 178.6 -94.6 41.1 15 ARG -129.8 140.5 178.6 -86.5 -169.9 -173.2 133.8 16 THR -164.2 177.2 -179.5 -160.0 17 PHE -92.5 126.5 178.9 -57.0 -88.7 18 ILE -138.8 119.2 179.0 -49.6 -174.9 19 GLY 128.6 177.0 -178.9 20 ILE -123.0 -15.3 179.3 51.0 -73.5 21 LYS -65.9 140.0 -179.2 -62.4 -168.0 169.9 -153.9 22 GLU -37.2 -49.4 -179.2 -76.2 -85.4 -37.6 23 GLU -67.6 -39.5 179.8 -166.7 -164.3 -37.4 24 GLU -67.4 -32.3 -180.0 -58.6 -172.2 -65.7 25 ILE -85.8 -21.8 179.4 61.8 179.4 26 ASN -88.3 -29.7 -178.6 -81.6 -58.6 27 ASN -124.1 137.1 179.6 -52.2 113.2 28 ARG -71.7 154.4 179.2 -48.9 179.4 77.4 99.2 29 GLN -120.0 163.4 178.2 -75.3 151.2 80.8 30 ASP -91.4 128.6 178.2 -74.2 -57.3 31 ILE -132.4 151.2 179.0 61.3 -178.6 32 VAL -123.9 126.6 180.0 -179.4 33 ILE -109.3 135.9 177.6 -59.8 177.4 34 ASN -126.5 125.8 -177.7 -89.9 99.5 35 VAL -119.4 129.3 179.0 -179.6 36 THR -118.5 121.5 -178.7 -46.8 37 ILE -125.5 133.6 179.6 -66.7 162.9 38 HIS -115.4 146.1 176.5 -70.9 -141.9 39 TYR -162.5 155.7 -179.7 69.0 -86.5 40 PRO -45.6 121.3 -178.9 -37.9 49.2 41 ALA -59.4 -29.5 -179.8 42 ASP -66.8 -47.3 179.4 45.2 -85.8 43 LYS -61.0 -28.4 -179.4 -64.8 -174.5 172.8 -174.9 44 ALA -56.6 -40.2 179.8 45 ARG -77.1 -31.5 178.2 -131.3 105.9 -65.7 96.5 46 THR -73.9 19.5 -178.9 -53.8 47 SER -76.4 -26.3 177.0 -175.3 48 GLU -99.1 28.8 -179.4 58.2 178.7 -76.8 49 ASP -128.6 -57.1 179.0 -178.3 -83.4 50 ILE -89.7 168.6 -178.0 52.8 -170.8 51 ASN -101.3 -33.3 -178.6 54.4 -61.8 52 ASP -81.0 35.5 -179.4 -48.9 80.9 53 ALA -64.0 150.6 179.7 54 LEU -73.5 122.5 -179.6 -156.2 -170.8 55 ASN -114.0 104.1 -179.4 -169.8 -1.6 56 TYR -59.8 -21.4 -180.0 62.9 75.9 57 ARG -71.0 -39.7 179.9 -113.4 169.6 -64.8 -92.3 58 THR -71.8 -42.2 178.9 -69.3 59 VAL -57.0 -51.4 179.4 -179.6 60 THR -57.1 -54.5 -179.6 -54.8 61 LYS -44.3 -54.4 -179.1 -171.8 -172.8 86.0 62.7 62 ASN -60.1 -41.7 179.8 -57.5 -23.2 63 ILE -61.0 -45.3 179.8 -61.9 176.9 64 ILE -60.6 -57.4 -179.1 -66.4 176.7 65 GLN -51.2 -51.9 -179.3 -163.6 171.6 -17.6 66 HIS -63.5 -42.2 -177.8 178.7 -99.1 67 VAL -70.4 -45.4 -179.7 175.7 68 GLU -73.9 -28.8 -179.6 -68.5 -170.5 -29.6 69 ASN -92.1 27.7 180.0 -64.5 174.1 70 ASN -151.6 174.6 178.6 -87.5 110.4 71 ARG -124.7 141.0 -178.7 -75.7 176.8 163.9 -91.9 72 PHE -125.0 139.7 -179.7 -59.0 84.3 73 SER -79.0 -48.7 -178.2 36.8 74 LEU -134.3 149.4 179.1 -82.4 51.4 75 LEU -53.9 -40.5 179.9 -111.6 -169.2 76 GLU -55.8 -43.8 -180.0 -61.6 81.1 3.5 77 LYS -66.4 -48.1 178.8 -112.5 78.7 172.4 -165.2 78 LEU -57.4 -47.1 179.9 171.1 52.7 79 THR -62.6 -42.8 178.8 -43.7 80 GLN -61.6 -48.6 178.7 -174.6 66.7 -112.9 81 ASP -54.9 -43.9 178.6 -78.5 32.6 82 VAL -67.4 -47.9 -179.5 -168.3 83 LEU -50.6 -49.0 179.6 174.7 58.2 84 ASP -56.5 -48.2 179.0 -63.7 -37.4 85 ILE -57.4 -36.3 -179.5 -62.2 -178.2 86 ALA -69.1 -44.6 -178.8 87 ARG -93.3 20.3 -177.5 72.2 -161.4 -176.3 67.9 88 GLU -66.9 -38.1 -179.1 -173.1 -170.5 -81.2 89 HIS -71.1 145.7 -179.6 -167.2 -82.4 90 HIS -73.1 3.4 177.7 65.9 -77.5 91 TRP -96.6 -22.5 -178.5 -80.4 9.6 92 VAL -58.1 120.1 179.3 -173.4 93 THR -93.8 -40.5 -179.3 -76.9 94 TYR -146.7 142.8 179.2 171.9 76.8 95 ALA -141.5 135.5 -179.8 96 GLU -135.4 139.0 -178.1 -168.1 -172.0 -33.2 97 VAL -137.0 119.0 176.2 169.1 98 GLU -110.2 134.8 178.0 -179.2 -178.2 14.4 99 ILE -126.4 119.1 179.6 -63.6 -179.7 100 ASP -93.2 128.1 176.1 -75.5 76.6 101 LYS -103.3 96.9 -178.1 -177.8 177.6 169.6 170.0 102 LEU -57.8 128.9 179.5 -86.1 9.8 103 HIS 50.4 55.4 178.9 -49.6 -55.8 104 ALA -90.6 -26.6 178.3 105 LEU -115.2 137.5 177.9 -79.4 -22.4 106 ARG -74.1 149.0 179.4 46.8 174.5 55.5 -106.6 107 TYR 75.9 5.2 178.4 -47.6 -32.5 108 ALA -129.3 143.4 179.3 109 ASP -60.1 -42.9 176.3 -69.2 18.4 110 SER -172.8 178.5 176.7 76.5 111 VAL -133.2 137.6 -179.4 53.3 112 SER -128.0 162.8 178.7 76.7 113 MET -128.1 124.9 177.1 174.4 83.1 -96.6 114 THR -117.1 145.2 178.3 -49.7 115 LEU -144.3 148.0 178.1 -66.9 175.1 116 SER -138.6 168.6 -178.7 63.2 117 TRP -142.3 142.8 -178.6 173.7 90.9 118 GLN -118.9 165.6 178.6 -98.4 -84.3 25.9 119 ARG 64.6 171.8 0.0 -74.5 153.1 -77.6 -84.6 Alpha Carbon Cartesian Coordinates : Residue Type X Y Z 1 ALA -6.265 43.982 -33.874 2 GLN -5.131 40.363 -33.183 3 PRO -8.505 38.427 -33.589 4 ALA -8.278 35.998 -30.632 5 ALA -10.225 36.454 -27.397 6 ILE -8.647 34.609 -24.495 7 ILE -10.714 33.264 -21.655 8 ARG -8.944 32.078 -18.550 9 ILE -10.334 29.931 -15.799 10 LYS -7.879 30.584 -12.966 11 ASN -7.102 28.167 -10.147 12 LEU -10.087 25.860 -10.249 13 ARG -9.434 23.943 -6.978 14 LEU -10.699 20.372 -6.878 15 ARG -9.936 17.089 -5.112 16 THR -9.966 13.644 -6.724 17 PHE -8.025 10.365 -6.740 18 ILE -4.789 10.305 -8.758 19 GLY -2.295 7.477 -8.632 20 ILE -2.076 3.755 -8.050 21 LYS -0.303 3.659 -4.714 22 GLU -2.490 2.475 -1.789 23 GLU -2.474 5.957 -0.246 24 GLU -3.179 7.782 -3.508 25 ILE -6.165 5.495 -4.205 26 ASN -7.578 5.588 -0.666 27 ASN -7.343 9.370 -0.285 28 ARG -8.294 12.191 -2.579 29 GLN -5.622 14.756 -3.371 30 ASP -5.611 18.459 -4.004 31 ILE -5.144 19.590 -7.611 32 VAL -5.433 23.069 -9.083 33 ILE -6.630 23.309 -12.661 34 ASN -5.951 26.283 -14.995 35 VAL -7.662 26.564 -18.378 36 THR -6.739 28.845 -21.293 37 ILE -9.181 29.003 -24.243 38 HIS -8.782 31.028 -27.441 39 TYR -11.459 31.862 -29.954 40 PRO -12.223 34.456 -32.719 41 ALA -12.494 37.932 -31.211 42 ASP -15.325 39.022 -33.560 43 LYS -17.760 36.308 -32.463 44 ALA -17.046 37.373 -28.851 45 ARG -18.973 40.665 -29.197 46 THR -21.920 38.987 -31.052 47 SER -22.455 37.236 -27.671 48 GLU -25.494 39.293 -26.584 49 ASP -26.817 38.457 -30.094 50 ILE -26.431 34.702 -30.795 51 ASN -27.463 31.680 -28.670 52 ASP -24.741 29.036 -29.219 53 ALA -22.248 31.169 -27.237 54 LEU -19.130 29.819 -25.492 55 ASN -20.069 29.529 -21.850 56 TYR -17.147 29.353 -19.410 57 ARG -19.720 28.398 -16.768 58 THR -20.692 25.252 -18.635 59 VAL -17.103 24.367 -19.383 60 THR -16.266 24.605 -15.681 61 LYS -19.436 22.692 -14.713 62 ASN -18.446 19.842 -16.960 63 ILE -14.830 19.844 -15.733 64 ILE -15.920 19.688 -12.086 65 GLN -18.490 16.963 -12.653 66 HIS -16.090 14.813 -14.618 67 VAL -13.119 15.303 -12.266 68 GLU -14.768 14.772 -8.877 69 ASN -16.900 11.834 -10.057 70 ASN -14.006 9.689 -11.240 71 ARG -10.661 8.094 -10.347 72 PHE -7.516 8.638 -12.338 73 SER -4.497 6.476 -12.892 74 LEU -2.093 9.116 -14.276 75 LEU -1.934 12.945 -14.434 76 GLU -1.691 12.684 -18.192 77 LYS -5.118 10.981 -18.546 78 LEU -6.738 13.523 -16.223 79 THR -5.200 16.513 -18.004 80 GLN -6.219 15.154 -21.458 81 ASP -9.798 14.489 -20.308 82 VAL -10.010 18.047 -19.090 83 LEU -8.336 19.443 -22.252 84 ASP -10.943 17.661 -24.371 85 ILE -13.714 19.101 -22.182 86 ALA -12.151 22.536 -22.667 87 ARG -11.958 22.435 -26.502 88 GLU -15.355 20.767 -26.982 89 HIS -17.101 23.841 -28.290 90 HIS -16.745 24.724 -31.983 91 TRP -15.452 28.279 -31.411 92 VAL -12.314 27.145 -29.645 93 THR -9.194 27.898 -31.743 94 TYR -6.595 26.982 -29.157 95 ALA -6.938 25.347 -25.709 96 GLU -4.328 24.808 -22.938 97 VAL -4.706 23.065 -19.574 98 GLU -2.274 22.978 -16.696 99 ILE -2.948 20.730 -13.649 100 ASP -0.914 21.040 -10.430 101 LYS -0.805 17.949 -8.219 102 LEU -0.092 19.733 -4.947 103 HIS 2.742 18.374 -2.827 104 ALA 3.276 15.378 -5.056 105 LEU 7.039 15.548 -4.518 106 ARG 8.313 16.108 -1.060 107 TYR 10.297 19.355 -0.797 108 ALA 8.541 20.878 -3.836 109 ASP 5.352 23.027 -3.922 110 SER 3.859 20.883 -6.712 111 VAL 4.373 19.159 -10.021 112 SER 2.218 20.031 -13.004 113 MET 1.290 18.677 -16.380 114 THR 0.367 21.028 -19.191 115 LEU -1.140 19.961 -22.542 116 SER -2.505 22.028 -25.446 117 TRP -4.473 21.726 -28.669 118 GLN -4.568 23.650 -31.969 119 ARG -6.945 24.315 -34.885 Richards-Kundrot Secondary Structure Assignment : 1 2 3 4 5 6 7 8 9 10 0 C C S S S S S S S S 10 S/S S S S S S S C C C 20 H H H H H H H/S S S S 30 S S S S S S S S S S/H 40 H H H H 3 3 3 C S S 50 S S C C H H H H H H 60 H H H H H H H H H H/S 70 S S S S/H H H H H H H 80 H H H H H H H H C C 90 S S S S/S S S S S S S 100 S S S C T T T T C S 110 S 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 e E E E E E E E 10 E E E E E E E E e S 20 h H H H H H h E E 30 E E E E E E E E E E 40 H H H H H h G G g t 50 S S h H H H H H 60 H H H H H H H H h e 70 E E S h H H H H H H 80 H H H H H H h t t T 90 T t e E E E E E E E 100 E E e t t T T t e E 110 E E E E E E E E e Buried Surface Area Percentages : Residue Type Buried Area % Buried % Polar Cover 1 ALA 0.0 0.0 88.3 2 GLN 0.0 0.0 84.8 3 PRO 46.4 37.3 72.1 4 ALA 42.4 58.4 72.5 5 ALA 50.7 69.9 58.5 6 ILE 97.2 67.7 67.8 7 ILE 110.4 76.9 48.9 8 ARG 99.2 47.5 65.7 9 ILE 123.3 85.9 46.9 10 LYS 45.8 26.4 80.2 11 ASN 62.6 51.8 74.5 12 LEU 121.4 82.2 40.5 13 ARG 65.8 31.5 76.1 14 LEU 135.0 91.3 43.7 15 ARG 65.3 31.3 79.9 16 THR 106.9 100.0 43.8 17 PHE 138.9 83.2 67.9 18 ILE 141.4 98.5 41.5 19 GLY 30.8 88.4 63.1 20 ILE 35.6 24.8 69.9 21 LYS 25.6 14.7 81.4 22 GLU 13.2 9.5 83.2 23 GLU 9.8 7.1 83.5 24 GLU 103.3 74.5 65.2 25 ILE 86.2 60.1 75.1 26 ASN 44.9 37.1 75.1 27 ASN 34.8 28.8 73.9 28 ARG 126.9 60.7 60.1 29 GLN 111.2 74.8 62.9 30 ASP 55.4 50.2 66.1 31 ILE 143.5 100.0 31.7 32 VAL 110.1 92.7 53.9 33 ILE 143.5 100.0 29.1 34 ASN 81.3 67.2 66.9 35 VAL 118.8 100.0 34.4 36 THR 80.9 75.7 60.6 37 ILE 143.5 100.0 30.6 38 HIS 112.5 74.9 41.0 39 TYR 161.3 89.1 38.2 40 PRO 86.2 69.2 69.1 41 ALA 44.7 61.6 65.7 42 ASP 23.3 21.1 69.9 43 LYS 94.9 54.7 62.1 44 ALA 68.5 94.3 61.0 45 ARG 50.0 23.9 84.9 46 THR 53.1 49.7 65.6 47 SER 42.4 50.7 71.5 48 GLU 0.0 0.0 90.6 49 ASP 31.3 28.4 69.2 50 ILE 86.4 60.2 64.1 51 ASN 11.5 9.5 83.9 52 ASP 27.8 25.1 81.7 53 ALA 53.4 73.5 67.1 54 LEU 145.5 98.4 30.9 55 ASN 57.0 47.1 77.4 56 TYR 79.5 43.9 65.2 57 ARG 51.3 24.6 82.2 58 THR 47.5 44.5 71.5 59 VAL 107.6 90.6 43.5 60 THR 80.8 75.6 42.3 61 LYS 58.4 33.7 80.6 62 ASN 80.7 66.8 60.7 63 ILE 143.5 100.0 25.7 64 ILE 84.2 58.7 55.1 65 GLN 47.6 32.0 83.8 66 HIS 95.3 63.4 59.8 67 VAL 118.8 100.0 33.5 68 GLU 76.2 55.0 71.6 69 ASN 32.1 26.5 78.5 70 ASN 51.0 42.2 72.2 71 ARG 87.7 42.0 64.3 72 PHE 155.0 92.9 53.1 73 SER 36.0 43.1 59.3 74 LEU 62.8 42.5 70.8 75 LEU 129.1 87.3 42.7 76 GLU 57.0 41.2 57.2 77 LYS 44.5 25.7 78.1 78 LEU 147.8 100.0 23.0 79 THR 106.9 100.0 38.6 80 GLN 69.0 46.5 70.2 81 ASP 67.8 61.4 63.3 82 VAL 118.8 100.0 27.5 83 LEU 142.3 96.3 50.4 84 ASP 61.7 55.9 73.7 85 ILE 119.6 83.3 55.7 86 ALA 72.6 100.0 40.2 87 ARG 141.4 67.7 54.8 88 GLU 29.1 21.0 86.7 89 HIS 110.0 73.3 58.7 90 HIS 37.2 24.8 81.0 91 TRP 193.1 94.2 44.0 92 VAL 118.6 99.9 47.1 93 THR 51.8 48.4 61.7 94 TYR 135.7 75.0 58.0 95 ALA 72.6 100.0 38.5 96 GLU 83.2 60.0 57.8 97 VAL 118.7 99.9 38.6 98 GLU 76.9 55.5 71.6 99 ILE 143.5 100.0 36.5 100 ASP 79.0 71.5 61.2 101 LYS 147.1 84.8 49.9 102 LEU 105.5 71.4 57.6 103 HIS 31.8 21.1 81.3 104 ALA 60.7 83.7 53.7 105 LEU 58.8 39.8 70.1 106 ARG 33.3 16.0 82.6 107 TYR 20.7 11.4 84.9 108 ALA 37.3 51.4 75.1 109 ASP 0.0 0.0 83.9 110 SER 72.0 86.2 63.4 111 VAL 65.0 54.7 58.8 112 SER 65.1 77.9 68.8 113 MET 108.7 68.2 59.8 114 THR 66.3 62.0 63.2 115 LEU 98.9 66.9 57.7 116 SER 50.9 60.9 59.1 117 TRP 133.0 64.9 67.4 118 GLN 65.8 44.3 66.8 119 ARG 24.5 11.7 83.1