Structural properties data for 1L9A
Chain residue residue number one letter Pos_x Pos_y Pos_z Secondary structure Abs. ASA Rel. ASA Packing density Conservation score
A MET 1 M 94.405 143.922 36.014 C 69 34.4 6 0.320
A ILE 2 I 96.827 141.744 37.978 E 59 31.8 6 0.567
A ILE 3 I 99.615 139.848 36.213 E 1 0.5 8 0.669
A TRP 4 W 101.124 137.127 38.392 C 28 11.6 7 0.684
A PRO 5 P 104.474 136.023 36.861 G 14 9.8 7 0.841
A SER 6 S 103.384 132.350 37.224 G 9 7.6 7 0.427
A TYR 7 Y 100.831 133.055 34.452 G 23 10.7 7 0.864
A ILE 8 I 103.632 133.027 31.863 G 0 0.0 9 0.600
A ASP 9 D 106.276 130.692 33.340 B 23 15.9 9 0.841
A LYS 10 K 107.134 127.772 31.033 T 87 42.2 5 0.430
A LYS 11 K 108.638 125.802 33.929 T 157 76.3 3 0.448
A LYS 12 K 105.302 125.777 35.740 S 36 17.4 6 0.448
A SER 13 S 102.415 123.452 35.016 C 43 36.6 5 0.593
A ARG 14 R 98.870 124.715 34.418 T 134 58.5 6 0.491
A ARG 15 R 97.692 123.873 37.953 T 186 81.2 3 0.449
A GLU 16 E 100.758 125.749 39.252 T 74 42.3 4 0.604
A GLY 17 G 99.901 129.028 37.531 T 4 5.0 9 0.971
A ARG 18 R 100.547 128.874 33.760 C 22 9.6 8 1.000
A LYS 19 K 97.736 130.657 31.895 C 84 40.8 6 0.669
A VAL 20 V 99.620 130.965 28.584 S 0 0.0 7 0.713
A PRO 21 P 100.094 128.034 26.071 C 31 21.8 6 0.537
A GLU 22 E 103.427 126.133 26.104 T 130 74.4 4 0.481
A GLU 23 E 104.647 127.635 22.817 T 161 92.1 3 0.461
A LEU 24 L 104.385 131.183 24.237 T 45 24.5 6 0.415
A ALA 25 A 105.486 130.598 27.846 C 5 4.5 10 0.762
A ILE 26 I 108.699 132.324 28.946 B 7 3.7 8 0.789
A GLU 27 E 111.757 130.570 30.446 S 80 45.7 5 0.489
A LYS 28 K 112.373 132.824 33.448 S 178 86.5 1 0.557
A PRO 29 P 109.692 135.517 33.671 C 24 16.9 6 0.946
A SER 30 S 110.790 138.615 35.543 C 49 41.8 4 0.415
A LEU 31 L 108.940 141.710 36.689 H 34 18.5 7 0.469
A LYS 32 K 111.100 143.806 34.344 H 123 59.7 5 0.393
A ASP 33 D 110.302 141.682 31.269 H 49 33.9 6 0.683
A ILE 34 I 106.613 142.136 32.123 H 0 0.0 9 0.803
A GLU 35 E 107.031 145.862 32.864 H 29 16.5 8 0.383
A LYS 36 K 108.975 146.394 29.635 H 121 58.8 5 0.454
A ALA 37 A 106.572 144.459 27.418 H 2 1.8 8 0.559
A LEU 38 L 103.616 146.271 29.011 H 0 0.0 8 0.389
A LYS 39 K 105.312 149.611 28.325 H 120 58.3 7 0.447
A LYS 40 K 105.855 148.463 24.726 H 124 60.2 4 0.373
A LEU 41 L 102.050 148.157 24.464 T 64 34.9 4 0.528
A GLY 42 G 101.653 151.801 25.503 T 70 88.9 3 0.509
A LEU 43 L 100.414 150.880 28.976 C 37 20.2 6 0.434
A GLU 44 E 101.544 151.874 32.476 C 135 77.2 5 0.370
A PRO 45 P 102.682 148.991 34.701 C 16 11.2 8 0.300
A LYS 46 K 103.047 149.109 38.458 C 129 62.7 4 0.259
A ILE 47 I 105.477 146.603 39.980 C 52 28.1 6 0.385
A TYR 48 Y 104.863 145.199 43.478 C 93 43.5 6 0.511
A ARG 49 R 108.038 143.372 44.562 S 164 71.6 3 0.305
A ASP 50 D 106.597 142.168 47.888 S 104 72.0 2 0.401
A LYS 51 K 103.579 139.998 46.978 C 99 48.1 4 0.541
A ARG 52 R 103.388 136.225 46.469 C 126 55.0 6 0.350
A TYR 53 Y 101.219 133.943 44.358 C 26 12.1 6 0.769
A PRO 54 P 99.325 131.740 46.878 G 97 68.3 6 0.835
A ARG 55 R 100.215 128.586 44.887 G 133 58.0 6 0.476
A GLN 56 Q 103.841 129.411 45.682 G 8 4.4 5 0.311
A HIS 57 H 103.633 131.273 49.012 T 129 70.9 4 0.333
A TRP 58 W 107.244 130.341 49.870 T 169 70.2 2 0.324
A GLU 59 E 108.485 132.309 46.810 C 86 49.2 4 0.415
A ILE 60 I 108.452 136.158 46.824 C 81 43.7 4 0.478
A ALA 61 A 108.312 136.904 43.093 C 43 39.0 4 0.536
A GLY 62 G 106.377 140.227 42.814 C 2 2.5 7 0.600
A ARG 63 R 103.471 140.999 40.468 C 47 20.5 6 0.343
A VAL 64 V 102.724 143.867 38.068 E 0 0.0 9 0.561
A GLU 65 E 99.434 145.747 37.632 E 42 24.0 7 0.484
A VAL 66 V 97.900 147.594 34.673 C 7 4.5 8 0.295
A ASP 67 D 94.715 149.520 33.950 C 144 99.7 2 0.352
A TYR 68 Y 94.112 147.490 30.740 C 77 36.0 5 0.383
A LYS 69 K 90.569 146.314 30.060 C 184 89.4 1 0.308
A GLY 70 G 90.450 143.649 27.390 S 22 27.9 3 0.305
A ASN 71 N 90.991 139.901 27.411 C 104 71.0 4 0.241
A LYS 72 K 93.401 139.206 30.278 H 56 27.2 5 0.319
A LEU 73 L 94.469 136.123 28.327 H 54 29.4 6 0.215
A CYS 74 C 94.982 138.117 25.108 H 57 39.5 5 0.228
A LEU 75 L 97.075 140.632 27.002 H 4 2.1 7 0.571
A LEU 76 L 99.143 137.831 28.535 H 0 0.0 10 0.449
A LYS 77 K 99.713 136.063 25.195 H 75 36.4 8 0.375
A GLU 78 E 100.788 139.405 23.725 H 75 42.9 6 0.335
A ILE 79 I 103.295 140.188 26.471 H 0 0.0 8 0.583
A ALA 80 A 104.638 136.680 25.956 H 4 3.6 9 0.631
A LYS 81 K 105.207 137.294 22.237 H 112 54.4 4 0.477
A ILE 82 I 107.012 140.590 22.931 H 51 27.5 6 0.302
A ILE 83 I 109.507 139.031 25.355 H 37 19.9 5 0.574
A LYS 84 K 111.043 136.873 22.579 C 105 51.0 3 0.444
A GLY 85 G 111.575 138.533 19.182 S 76 96.5 2 0.354
A LYS 86 K 115.387 138.141 19.084 C 182 88.4 1 0.254
A ASN 87 N 117.378 135.368 20.910 C 203 100.0 3 0.342