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*** 2647 ***elNémo ID: 2605141238332666903Job options:ID = 2605141238332666903 JOBID = 2647 USERID = unknown PRIVAT = 0 NMODES = 5 DQMIN = -100 DQMAX = 100 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = 0 DORMSD = 0 NRBL = 0 CUTOFF = 0 CAONLY = 0 Input data for this run:HEADER 2647 CRYST1 142.494 73.507 96.239 90.00 90.00 90.00 P 21 21 2 1 ATOM 1 N SER A 44 -82.254 12.668 9.472 1.00 46.22 N ANISOU 1 N SER A 44 6699 7168 3694 -866 698 -258 N ATOM 2 CA SER A 44 -82.619 11.279 9.211 1.00 44.94 C ANISOU 2 CA SER A 44 6587 6950 3540 -896 699 -127 C ATOM 3 C SER A 44 -81.360 10.414 9.161 1.00 45.19 C ANISOU 3 C SER A 44 6677 6920 3572 -875 652 27 C ATOM 4 O SER A 44 -80.246 10.929 9.077 1.00 43.90 O ANISOU 4 O SER A 44 6524 6735 3421 -824 619 23 O ATOM 5 CB SER A 44 -83.392 11.153 7.886 1.00 48.25 C ANISOU 5 CB SER A 44 7028 7225 4078 -850 707 -164 C ATOM 6 OG SER A 44 -84.590 11.908 7.878 1.00 45.79 O ANISOU 6 OG SER A 44 6661 6959 3779 -866 747 -302 O ATOM 7 N ALA A 45 -81.547 9.092 9.191 1.00 49.52 N ANISOU 7 N ALA A 45 7262 7435 4119 -913 647 160 N ATOM 8 CA ALA A 45 -80.434 8.174 8.952 1.00 48.35 C ANISOU 8 CA ALA A 45 7169 7198 4005 -886 598 304 C ATOM 9 C ALA A 45 -80.017 8.164 7.486 1.00 46.01 C ANISOU 9 C ALA A 45 6915 6723 3843 -793 573 287 C ATOM 10 O ALA A 45 -78.839 7.945 7.171 1.00 43.50 O ANISOU 10 O ALA A 45 6631 6334 3562 -745 530 350 O ATOM 11 CB ALA A 45 -80.804 6.757 9.398 1.00 45.68 C ANISOU 11 CB ALA A 45 6847 6865 3643 -955 597 450 C ATOM 12 N ASP A 46 -80.959 8.387 6.578 1.00 51.01 N ANISOU 12 N ASP A 46 7543 7288 4548 -770 599 203 N ATOM 13 CA ASP A 46 -80.671 8.327 5.154 1.00 50.06 C ANISOU 13 CA ASP A 46 7458 7015 4547 -690 578 188 C ATOM 14 C ASP A 46 -80.652 9.715 4.506 1.00 50.67 C ANISOU 14 C ASP A 46 7514 7074 4664 -630 581 54 C ATOM 15 O ASP A 46 -80.864 9.843 3.293 1.00 51.90 O ANISOU 15 O ASP A 46 7683 7126 4910 -577 577 14 O ATOM 16 CB ASP A 46 -81.663 7.402 4.452 1.00 50.93 C ANISOU 16 CB ASP A 46 7583 7045 4722 -704 596 210 C ATOM 17 CG ASP A 46 -83.031 7.417 5.087 1.00 54.00 C ANISOU 17 CG ASP A 46 7934 7528 5057 -776 644 166 C ATOM 18 OD1 ASP A 46 -83.618 6.322 5.236 1.00 59.88 O ANISOU 18 OD1 ASP A 46 8688 8259 5806 -825 656 243 O ATOM 19 OD2 ASP A 46 -83.525 8.513 5.426 1.00 54.03 O1- ANISOU 19 OD2 ASP A 46 7893 7614 5020 -784 670 52 O1- ATOM 20 N THR A 47 -80.386 10.760 5.299 1.00 46.21 N ANISOU 20 N THR A 47 6910 6612 4037 -639 586 -14 N ATOM 21 CA THR A 47 -80.142 12.113 4.801 1.00 40.80 C ANISOU 21 CA THR A 47 6199 5906 3397 -582 579 -128 C ATOM 22 C THR A 47 -78.674 12.479 5.005 1.00 38.59 C ANISOU 22 C THR A 47 5933 5626 3104 -544 541 -96 C ATOM 23 O THR A 47 -78.098 12.207 6.061 1.00 42.07 O ANISOU 23 O THR A 47 6370 6155 3460 -582 533 -40 O ATOM 24 CB THR A 47 -81.047 13.134 5.499 1.00 39.36 C ANISOU 24 CB THR A 47 5948 5832 3173 -618 614 -256 C ATOM 25 CG2 THR A 47 -80.678 14.563 5.111 1.00 34.58 C ANISOU 25 CG2 THR A 47 5309 5205 2625 -561 601 -367 C ATOM 26 OG1 THR A 47 -82.413 12.883 5.155 1.00 38.73 O ANISOU 26 OG1 THR A 47 5854 5740 3120 -644 648 -297 O ATOM 27 N LEU A 48 -78.063 13.087 3.995 1.00 34.08 N ANISOU 27 N LEU A 48 5374 4961 2614 -472 517 -129 N ATOM 28 CA LEU A 48 -76.625 13.338 3.985 1.00 34.55 C ANISOU 28 CA LEU A 48 5451 4998 2676 -430 479 -93 C ATOM 29 C LEU A 48 -76.366 14.837 3.968 1.00 35.78 C ANISOU 29 C LEU A 48 5563 5175 2856 -397 476 -204 C ATOM 30 O LEU A 48 -76.717 15.517 2.999 1.00 35.82 O ANISOU 30 O LEU A 48 5557 5110 2943 -355 475 -269 O ATOM 31 CB LEU A 48 -75.965 12.684 2.772 1.00 35.78 C ANISOU 31 CB LEU A 48 5659 5023 2912 -375 450 -24 C ATOM 32 CG LEU A 48 -74.468 12.379 2.894 1.00 37.44 C ANISOU 32 CG LEU A 48 5898 5211 3115 -347 411 52 C ATOM 33 CD1 LEU A 48 -74.060 11.316 1.872 1.00 34.85 C ANISOU 33 CD1 LEU A 48 5617 4768 2857 -313 389 129 C ATOM 34 CD2 LEU A 48 -73.632 13.633 2.724 1.00 33.76 C ANISOU 34 CD2 LEU A 48 5412 4746 2670 -300 393 -15 C ATOM 35 N VAL A 49 -75.708 15.343 5.002 1.00 34.77 N ANISOU 35 N VAL A 49 5408 5141 2663 -414 470 -223 N ATOM 36 CA VAL A 49 -75.497 16.777 5.149 1.00 34.14 C ANISOU 36 CA VAL A 49 5274 5089 2608 -389 468 -338 C ATOM 37 C VAL A 49 -74.109 17.097 4.619 1.00 36.10 C ANISOU 37 C VAL A 49 5547 5268 2902 -329 428 -306 C ATOM 38 O VAL A 49 -73.096 16.744 5.233 1.00 37.89 O ANISOU 38 O VAL A 49 5791 5533 3073 -334 408 -244 O ATOM 39 CB VAL A 49 -75.665 17.239 6.603 1.00 34.07 C ANISOU 39 CB VAL A 49 5206 5235 2503 -446 488 -402 C ATOM 40 CG1 VAL A 49 -75.373 18.700 6.696 1.00 34.00 C ANISOU 40 CG1 VAL A 49 5137 5242 2539 -415 482 -526 C ATOM 41 CG2 VAL A 49 -77.082 16.979 7.074 1.00 34.61 C ANISOU 41 CG2 VAL A 49 5244 5378 2529 -508 530 -444 C ATOM 42 N ALA A 50 -74.059 17.762 3.476 1.00 32.00 N ANISOU 42 N ALA A 50 5027 4649 2481 -274 416 -345 N ATOM 43 CA ALA A 50 -72.796 18.190 2.910 1.00 32.57 C ANISOU 43 CA ALA A 50 5116 4658 2601 -219 381 -324 C ATOM 44 C ALA A 50 -72.523 19.648 3.268 1.00 34.93 C ANISOU 44 C ALA A 50 5352 4989 2930 -203 376 -429 C ATOM 45 O ALA A 50 -73.442 20.450 3.467 1.00 36.68 O ANISOU 45 O ALA A 50 5519 5241 3179 -218 395 -529 O ATOM 46 CB ALA A 50 -72.797 17.999 1.391 1.00 30.79 C ANISOU 46 CB ALA A 50 4925 4310 2463 -172 367 -290 C ATOM 47 N TYR A 51 -71.244 19.969 3.408 1.00 31.53 N ANISOU 47 N TYR A 51 4925 4555 2498 -175 349 -411 N ATOM 48 CA TYR A 51 -70.767 21.340 3.394 1.00 31.47 C ANISOU 48 CA TYR A 51 4866 4539 2552 -146 335 -497 C ATOM 49 C TYR A 51 -69.682 21.415 2.333 1.00 32.49 C ANISOU 49 C TYR A 51 5032 4568 2746 -90 303 -439 C ATOM 50 O TYR A 51 -68.669 20.705 2.423 1.00 30.74 O ANISOU 50 O TYR A 51 4853 4344 2483 -81 285 -359 O ATOM 51 CB TYR A 51 -70.224 21.764 4.745 1.00 32.11 C ANISOU 51 CB TYR A 51 4904 4734 2563 -172 337 -547 C ATOM 52 CG TYR A 51 -69.776 23.195 4.770 1.00 33.88 C ANISOU 52 CG TYR A 51 5065 4946 2861 -142 323 -647 C ATOM 53 CD1 TYR A 51 -70.674 24.229 4.517 1.00 32.21 C ANISOU 53 CD1 TYR A 51 4792 4710 2735 -138 333 -754 C ATOM 54 CD2 TYR A 51 -68.445 23.518 5.032 1.00 33.55 C ANISOU 54 CD2 TYR A 51 5022 4911 2814 -118 298 -635 C ATOM 55 CE1 TYR A 51 -70.259 25.536 4.523 1.00 34.32 C ANISOU 55 CE1 TYR A 51 4996 4955 3088 -111 317 -843 C ATOM 56 CE2 TYR A 51 -68.021 24.823 5.033 1.00 34.32 C ANISOU 56 CE2 TYR A 51 5060 4991 2991 -92 285 -726 C ATOM 57 CZ TYR A 51 -68.931 25.829 4.785 1.00 37.27 C ANISOU 57 CZ TYR A 51 5369 5335 3455 -89 294 -828 C ATOM 58 OH TYR A 51 -68.510 27.134 4.802 1.00 41.28 O ANISOU 58 OH TYR A 51 5811 5817 4057 -63 277 -918 O ATOM 59 N THR A 52 -69.913 22.244 1.317 1.00 30.42 N ANISOU 59 N THR A 52 4749 4225 2584 -56 293 -475 N ATOM 60 CA THR A 52 -69.018 22.359 0.175 1.00 31.29 C ANISOU 60 CA THR A 52 4888 4244 2755 -8 265 -421 C ATOM 61 C THR A 52 -68.058 23.531 0.291 1.00 34.00 C ANISOU 61 C THR A 52 5190 4578 3150 19 243 -465 C ATOM 62 O THR A 52 -67.176 23.665 -0.565 1.00 34.04 O ANISOU 62 O THR A 52 5216 4520 3199 55 220 -419 O ATOM 63 CB THR A 52 -69.818 22.533 -1.117 1.00 29.44 C ANISOU 63 CB THR A 52 4656 3931 2599 10 264 -417 C ATOM 64 CG2 THR A 52 -70.629 21.285 -1.430 1.00 30.66 C ANISOU 64 CG2 THR A 52 4855 4080 2712 -10 284 -365 C ATOM 65 OG1 THR A 52 -70.704 23.651 -0.965 1.00 30.21 O ANISOU 65 OG1 THR A 52 4688 4033 2759 4 270 -511 O ATOM 66 N GLY A 53 -68.228 24.384 1.300 1.00 30.38 N ANISOU 66 N GLY A 53 4669 4183 2690 1 250 -559 N ATOM 67 CA GLY A 53 -67.511 25.639 1.398 1.00 30.48 C ANISOU 67 CA GLY A 53 4628 4180 2773 25 230 -621 C ATOM 68 C GLY A 53 -68.393 26.866 1.338 1.00 33.35 C ANISOU 68 C GLY A 53 4915 4522 3236 25 232 -725 C ATOM 69 O GLY A 53 -67.862 27.980 1.408 1.00 34.63 O ANISOU 69 O GLY A 53 5022 4660 3475 45 213 -783 O ATOM 70 N GLN A 54 -69.720 26.734 1.248 1.00 35.20 N ANISOU 70 N GLN A 54 5136 4761 3478 4 252 -758 N ATOM 71 CA GLN A 54 -70.579 27.871 0.919 1.00 37.59 C ANISOU 71 CA GLN A 54 5367 5017 3899 12 246 -845 C ATOM 72 C GLN A 54 -70.631 28.844 2.094 1.00 41.82 C ANISOU 72 C GLN A 54 5815 5620 4455 -5 252 -978 C ATOM 73 O GLN A 54 -71.284 28.569 3.108 1.00 40.06 O ANISOU 73 O GLN A 54 5566 5495 4157 -46 283 -1043 O ATOM 74 CB GLN A 54 -71.983 27.397 0.545 1.00 34.60 C ANISOU 74 CB GLN A 54 4997 4630 3518 -8 266 -847 C ATOM 75 CG GLN A 54 -73.001 28.535 0.327 1.00 36.59 C ANISOU 75 CG GLN A 54 5169 4842 3894 -3 259 -946 C ATOM 76 CD GLN A 54 -72.717 29.409 -0.923 1.00 39.78 C ANISOU 76 CD GLN A 54 5556 5127 4433 40 217 -911 C ATOM 77 NE2 GLN A 54 -73.257 30.616 -0.927 1.00 31.99 N ANISOU 77 NE2 GLN A 54 4483 4100 3573 48 200 -1001 N ATOM 78 OE1 GLN A 54 -72.040 28.990 -1.868 1.00 38.74 O ANISOU 78 OE1 GLN A 54 5482 4943 4292 63 200 -804 O ATOM 79 N SER A 55 -69.941 29.977 1.966 1.00 41.67 N ANISOU 79 N SER A 55 5743 5552 4538 23 225 -1022 N ATOM 80 CA SER A 55 -70.050 31.067 2.925 1.00 42.96 C ANISOU 80 CA SER A 55 5806 5760 4756 13 227 -1166 C ATOM 81 C SER A 55 -71.173 32.004 2.504 1.00 45.13 C ANISOU 81 C SER A 55 6007 5970 5170 19 218 -1249 C ATOM 82 O SER A 55 -71.181 32.506 1.377 1.00 43.41 O ANISOU 82 O SER A 55 5788 5637 5067 51 186 -1200 O ATOM 83 CB SER A 55 -68.736 31.836 3.023 1.00 47.14 C ANISOU 83 CB SER A 55 6308 6264 5339 41 199 -1177 C ATOM 84 OG SER A 55 -67.740 31.059 3.662 1.00 53.52 O ANISOU 84 OG SER A 55 7168 7151 6018 31 207 -1126 O ATOM 85 N GLY A 56 -72.113 32.249 3.408 1.00 42.37 N ANISOU 85 N GLY A 56 5590 5697 4811 -14 244 -1374 N ATOM 86 CA GLY A 56 -73.221 33.126 3.108 1.00 41.99 C ANISOU 86 CA GLY A 56 5462 5590 4900 -10 235 -1466 C ATOM 87 C GLY A 56 -74.343 32.408 2.386 1.00 38.48 C ANISOU 87 C GLY A 56 5065 5117 4437 -18 247 -1408 C ATOM 88 O GLY A 56 -74.209 31.286 1.904 1.00 35.59 O ANISOU 88 O GLY A 56 4796 4754 3973 -21 257 -1285 O ATOM 89 N ASP A 57 -75.492 33.075 2.350 1.00 37.22 N ANISOU 89 N ASP A 57 4829 4932 4381 -23 245 -1507 N ATOM 90 CA ASP A 57 -76.702 32.469 1.825 1.00 33.98 C ANISOU 90 CA ASP A 57 4448 4508 3956 -36 260 -1479 C ATOM 91 C ASP A 57 -76.496 32.011 0.386 1.00 39.90 C ANISOU 91 C ASP A 57 5279 5155 4725 -4 233 -1325 C ATOM 92 O ASP A 57 -75.868 32.703 -0.429 1.00 37.74 O ANISOU 92 O ASP A 57 4997 4786 4556 32 191 -1275 O ATOM 93 CB ASP A 57 -77.866 33.466 1.886 1.00 36.25 C ANISOU 93 CB ASP A 57 4627 4760 4385 -37 251 -1614 C ATOM 94 CG ASP A 57 -78.323 33.769 3.300 1.00 41.46 C ANISOU 94 CG ASP A 57 5201 5542 5011 -77 287 -1783 C ATOM 95 OD1 ASP A 57 -77.691 33.301 4.274 1.00 45.25 O ANISOU 95 OD1 ASP A 57 5699 6137 5357 -105 316 -1795 O ATOM 96 OD2 ASP A 57 -79.330 34.479 3.443 1.00 42.63 O1- ANISOU 96 OD2 ASP A 57 5257 5674 5266 -82 285 -1906 O1- ATOM 97 N TYR A 58 -77.023 30.826 0.085 1.00 42.96 N ANISOU 97 N TYR A 58 5742 5570 5009 -22 259 -1250 N ATOM 98 CA TYR A 58 -77.074 30.334 -1.283 1.00 38.06 C ANISOU 98 CA TYR A 58 5189 4868 4405 2 238 -1124 C ATOM 99 C TYR A 58 -78.006 31.206 -2.111 1.00 38.41 C ANISOU 99 C TYR A 58 5173 4823 4598 21 207 -1155 C ATOM 100 O TYR A 58 -79.030 31.685 -1.624 1.00 38.89 O ANISOU 100 O TYR A 58 5162 4900 4716 6 216 -1269 O ATOM 101 CB TYR A 58 -77.588 28.892 -1.323 1.00 37.53 C ANISOU 101 CB TYR A 58 5201 4852 4207 -25 275 -1060 C ATOM 102 CG TYR A 58 -76.554 27.797 -1.201 1.00 38.83 C ANISOU 102 CG TYR A 58 5453 5056 4246 -29 287 -958 C ATOM 103 CD1 TYR A 58 -75.565 27.621 -2.171 1.00 39.91 C ANISOU 103 CD1 TYR A 58 5643 5128 4393 4 259 -850 C ATOM 104 CD2 TYR A 58 -76.608 26.887 -0.141 1.00 41.90 C ANISOU 104 CD2 TYR A 58 5869 5547 4505 -70 326 -966 C ATOM 105 CE1 TYR A 58 -74.639 26.597 -2.073 1.00 37.74 C ANISOU 105 CE1 TYR A 58 5442 4883 4014 2 268 -764 C ATOM 106 CE2 TYR A 58 -75.682 25.859 -0.030 1.00 41.09 C ANISOU 106 CE2 TYR A 58 5842 5471 4299 -73 331 -868 C ATOM 107 CZ TYR A 58 -74.704 25.715 -0.996 1.00 39.56 C ANISOU 107 CZ TYR A 58 5698 5205 4129 -35 302 -772 C ATOM 108 OH TYR A 58 -73.797 24.679 -0.861 1.00 41.57 O ANISOU 108 OH TYR A 58 6021 5483 4290 -38 306 -683 O ATOM 109 N GLN A 59 -77.643 31.398 -3.378 1.00 34.46 N ANISOU 109 N GLN A 59 4699 4232 4162 54 168 -1053 N ATOM 110 CA GLN A 59 -78.478 32.071 -4.368 1.00 39.60 C ANISOU 110 CA GLN A 59 5306 4796 4944 72 131 -1046 C ATOM 111 C GLN A 59 -78.874 31.056 -5.434 1.00 34.22 C ANISOU 111 C GLN A 59 4702 4104 4197 73 135 -937 C ATOM 112 O GLN A 59 -78.002 30.463 -6.073 1.00 33.94 O ANISOU 112 O GLN A 59 4735 4062 4097 84 130 -829 O ATOM 113 CB GLN A 59 -77.737 33.260 -4.991 1.00 41.81 C ANISOU 113 CB GLN A 59 5538 4984 5362 104 76 -1014 C ATOM 114 CG GLN A 59 -77.596 34.441 -4.057 1.00 41.42 C ANISOU 114 CG GLN A 59 5390 4925 5422 106 64 -1141 C ATOM 115 CD GLN A 59 -77.176 35.706 -4.781 1.00 50.27 C ANISOU 115 CD GLN A 59 6448 5936 6717 136 3 -1111 C ATOM 116 NE2 GLN A 59 -78.114 36.652 -4.925 1.00 47.49 N ANISOU 116 NE2 GLN A 59 6003 5517 6524 143 -30 -1182 N ATOM 117 OE1 GLN A 59 -76.043 35.815 -5.250 1.00 47.98 O ANISOU 117 OE1 GLN A 59 6190 5617 6423 152 -18 -1021 O ATOM 118 N ILE A 60 -80.182 30.861 -5.628 1.00 33.23 N ANISOU 118 N ILE A 60 4558 3978 4090 61 144 -974 N ATOM 119 CA ILE A 60 -80.651 29.703 -6.382 1.00 32.41 C ANISOU 119 CA ILE A 60 4528 3887 3901 53 161 -894 C ATOM 120 C ILE A 60 -80.136 29.745 -7.818 1.00 38.95 C ANISOU 120 C ILE A 60 5388 4653 4759 81 120 -771 C ATOM 121 O ILE A 60 -80.286 30.736 -8.551 1.00 37.63 O ANISOU 121 O ILE A 60 5168 4416 4715 101 72 -754 O ATOM 122 CB ILE A 60 -82.183 29.580 -6.304 1.00 34.82 C ANISOU 122 CB ILE A 60 4797 4202 4229 35 177 -967 C ATOM 123 CG1 ILE A 60 -82.614 28.167 -6.730 1.00 37.30 C ANISOU 123 CG1 ILE A 60 5191 4552 4429 19 209 -903 C ATOM 124 CG2 ILE A 60 -82.887 30.666 -7.096 1.00 37.64 C ANISOU 124 CG2 ILE A 60 5082 4476 4744 58 126 -983 C ATOM 125 CD1 ILE A 60 -84.067 27.816 -6.409 1.00 35.15 C ANISOU 125 CD1 ILE A 60 4894 4310 4150 -8 239 -980 C ATOM 126 N ASN A 61 -79.482 28.660 -8.213 1.00 35.93 N ANISOU 126 N ASN A 61 5088 4298 4264 80 138 -684 N ATOM 127 CA ASN A 61 -78.974 28.493 -9.561 1.00 33.73 C ANISOU 127 CA ASN A 61 4844 3985 3986 99 108 -571 C ATOM 128 C ASN A 61 -78.668 27.021 -9.783 1.00 32.58 C ANISOU 128 C ASN A 61 4784 3885 3710 89 143 -513 C ATOM 129 O ASN A 61 -77.733 26.469 -9.190 1.00 32.54 O ANISOU 129 O ASN A 61 4821 3914 3629 85 164 -498 O ATOM 130 CB ASN A 61 -77.741 29.365 -9.794 1.00 35.49 C ANISOU 130 CB ASN A 61 5049 4170 4265 120 73 -527 C ATOM 131 CG ASN A 61 -77.464 29.596 -11.279 1.00 35.21 C ANISOU 131 CG ASN A 61 5018 4095 4266 136 31 -420 C ATOM 132 ND2 ASN A 61 -77.418 30.864 -11.677 1.00 35.05 N ANISOU 132 ND2 ASN A 61 4931 4014 4373 149 -18 -408 N ATOM 133 OD1 ASN A 61 -77.336 28.645 -12.064 1.00 32.30 O ANISOU 133 OD1 ASN A 61 4706 3753 3815 134 42 -352 O ATOM 134 N PHE A 62 -79.480 26.371 -10.613 1.00 30.43 N ANISOU 134 N PHE A 62 4532 3613 3418 85 146 -484 N ATOM 135 CA PHE A 62 -79.195 25.022 -11.061 1.00 32.55 C ANISOU 135 CA PHE A 62 4870 3912 3584 79 171 -426 C ATOM 136 C PHE A 62 -79.007 24.958 -12.577 1.00 33.90 C ANISOU 136 C PHE A 62 5051 4064 3766 95 141 -345 C ATOM 137 O PHE A 62 -79.133 23.880 -13.181 1.00 30.58 O ANISOU 137 O PHE A 62 4673 3666 3281 90 158 -312 O ATOM 138 CB PHE A 62 -80.293 24.086 -10.564 1.00 31.77 C ANISOU 138 CB PHE A 62 4789 3846 3436 53 212 -474 C ATOM 139 CG PHE A 62 -80.301 23.939 -9.079 1.00 32.31 C ANISOU 139 CG PHE A 62 4857 3956 3465 30 246 -539 C ATOM 140 CD1 PHE A 62 -79.272 23.271 -8.438 1.00 32.46 C ANISOU 140 CD1 PHE A 62 4922 4006 3405 24 264 -509 C ATOM 141 CD2 PHE A 62 -81.311 24.493 -8.315 1.00 33.62 C ANISOU 141 CD2 PHE A 62 4969 4134 3670 13 257 -631 C ATOM 142 CE1 PHE A 62 -79.253 23.139 -7.060 1.00 32.26 C ANISOU 142 CE1 PHE A 62 4893 4031 3333 -2 293 -561 C ATOM 143 CE2 PHE A 62 -81.307 24.363 -6.927 1.00 32.90 C ANISOU 143 CE2 PHE A 62 4871 4098 3531 -15 291 -693 C ATOM 144 CZ PHE A 62 -80.274 23.690 -6.298 1.00 31.25 C ANISOU 144 CZ PHE A 62 4711 3927 3235 -23 308 -654 C ATOM 145 N ASN A 63 -78.710 26.097 -13.200 1.00 32.97 N ANISOU 145 N ASN A 63 4888 3909 3730 112 95 -312 N ATOM 146 CA ASN A 63 -78.307 26.134 -14.595 1.00 29.39 C ANISOU 146 CA ASN A 63 4439 3452 3276 122 64 -224 C ATOM 147 C ASN A 63 -76.972 25.412 -14.731 1.00 28.78 C ANISOU 147 C ASN A 63 4415 3402 3117 126 79 -174 C ATOM 148 O ASN A 63 -75.973 25.869 -14.157 1.00 28.13 O ANISOU 148 O ASN A 63 4333 3311 3046 133 74 -172 O ATOM 149 CB ASN A 63 -78.195 27.581 -15.101 1.00 33.27 C ANISOU 149 CB ASN A 63 4866 3896 3879 134 9 -190 C ATOM 150 CG ASN A 63 -78.044 27.673 -16.651 1.00 34.32 C ANISOU 150 CG ASN A 63 4992 4038 4011 136 -27 -92 C ATOM 151 ND2 ASN A 63 -78.658 28.693 -17.243 1.00 36.88 N ANISOU 151 ND2 ASN A 63 5254 4325 4434 139 -76 -65 N ATOM 152 OD1 ASN A 63 -77.402 26.826 -17.291 1.00 32.47 O ANISOU 152 OD1 ASN A 63 4801 3847 3688 133 -13 -44 O ATOM 153 N PRO A 64 -76.904 24.286 -15.446 1.00 27.91 N ANISOU 153 N PRO A 64 4346 3326 2931 122 96 -142 N ATOM 154 CA PRO A 64 -75.631 23.566 -15.552 1.00 28.51 C ANISOU 154 CA PRO A 64 4467 3426 2939 127 109 -105 C ATOM 155 C PRO A 64 -74.607 24.262 -16.435 1.00 27.67 C ANISOU 155 C PRO A 64 4342 3319 2851 137 75 -37 C ATOM 156 O PRO A 64 -73.425 23.897 -16.401 1.00 27.48 O ANISOU 156 O PRO A 64 4346 3310 2785 143 82 -13 O ATOM 157 CB PRO A 64 -76.048 22.202 -16.119 1.00 27.47 C ANISOU 157 CB PRO A 64 4371 3326 2740 119 135 -105 C ATOM 158 CG PRO A 64 -77.327 22.459 -16.800 1.00 27.67 C ANISOU 158 CG PRO A 64 4363 3350 2799 113 122 -113 C ATOM 159 CD PRO A 64 -78.014 23.538 -16.045 1.00 27.91 C ANISOU 159 CD PRO A 64 4353 3345 2907 112 109 -154 C ATOM 160 N PHE A 65 -75.004 25.240 -17.229 1.00 27.95 N ANISOU 160 N PHE A 65 4329 3341 2951 138 35 0 N ATOM 161 CA PHE A 65 -74.004 25.982 -17.974 1.00 30.18 C ANISOU 161 CA PHE A 65 4589 3623 3253 142 1 72 C ATOM 162 C PHE A 65 -73.461 27.148 -17.167 1.00 30.77 C ANISOU 162 C PHE A 65 4633 3650 3409 150 -19 62 C ATOM 163 O PHE A 65 -72.480 27.772 -17.590 1.00 37.70 O ANISOU 163 O PHE A 65 5494 4522 4307 153 -43 119 O ATOM 164 CB PHE A 65 -74.582 26.494 -19.318 1.00 32.51 C ANISOU 164 CB PHE A 65 4841 3932 3578 133 -38 136 C ATOM 165 CG PHE A 65 -75.138 25.405 -20.215 1.00 29.46 C ANISOU 165 CG PHE A 65 4476 3604 3114 124 -21 140 C ATOM 166 CD1 PHE A 65 -74.296 24.602 -20.975 1.00 30.52 C ANISOU 166 CD1 PHE A 65 4635 3797 3165 119 -8 170 C ATOM 167 CD2 PHE A 65 -76.510 25.196 -20.309 1.00 29.25 C ANISOU 167 CD2 PHE A 65 4436 3573 3103 119 -19 105 C ATOM 168 CE1 PHE A 65 -74.807 23.592 -21.800 1.00 28.18 C ANISOU 168 CE1 PHE A 65 4348 3555 2803 110 8 161 C ATOM 169 CE2 PHE A 65 -77.026 24.192 -21.128 1.00 28.39 C ANISOU 169 CE2 PHE A 65 4342 3518 2927 110 -3 101 C ATOM 170 CZ PHE A 65 -76.167 23.391 -21.865 1.00 28.27 C ANISOU 170 CZ PHE A 65 4349 3561 2831 105 11 127 C ATOM 171 N SER A 66 -74.071 27.453 -16.012 1.00 30.46 N ANISOU 171 N SER A 66 4581 3578 3414 152 -7 -14 N ATOM 172 CA SER A 66 -73.743 28.669 -15.280 1.00 30.54 C ANISOU 172 CA SER A 66 4545 3541 3519 160 -29 -38 C ATOM 173 C SER A 66 -72.630 28.412 -14.271 1.00 28.38 C ANISOU 173 C SER A 66 4303 3278 3201 166 -4 -69 C ATOM 174 O SER A 66 -72.619 27.378 -13.605 1.00 28.10 O ANISOU 174 O SER A 66 4316 3278 3084 161 36 -106 O ATOM 175 CB SER A 66 -74.963 29.218 -14.558 1.00 30.76 C ANISOU 175 CB SER A 66 4529 3535 3624 158 -32 -117 C ATOM 176 OG SER A 66 -74.624 30.440 -13.933 1.00 34.09 O ANISOU 176 OG SER A 66 4896 3908 4149 166 -57 -148 O ATOM 177 N PRO A 67 -71.672 29.335 -14.189 1.00 28.54 N ANISOU 177 N PRO A 67 4294 3271 3278 174 -29 -46 N ATOM 178 CA PRO A 67 -70.632 29.228 -13.166 1.00 31.81 C ANISOU 178 CA PRO A 67 4728 3695 3661 180 -9 -82 C ATOM 179 C PRO A 67 -71.108 29.692 -11.809 1.00 30.28 C ANISOU 179 C PRO A 67 4504 3489 3511 179 2 -181 C ATOM 180 O PRO A 67 -70.370 29.543 -10.828 1.00 32.88 O ANISOU 180 O PRO A 67 4849 3840 3805 181 21 -220 O ATOM 181 CB PRO A 67 -69.520 30.132 -13.708 1.00 28.55 C ANISOU 181 CB PRO A 67 4287 3256 3304 187 -44 -20 C ATOM 182 CG PRO A 67 -70.254 31.169 -14.434 1.00 28.97 C ANISOU 182 CG PRO A 67 4279 3263 3467 184 -87 12 C ATOM 183 CD PRO A 67 -71.491 30.537 -15.017 1.00 30.43 C ANISOU 183 CD PRO A 67 4476 3467 3617 176 -80 17 C ATOM 184 N SER A 68 -72.317 30.249 -11.731 1.00 32.12 N ANISOU 184 N SER A 68 4690 3694 3819 174 -9 -225 N ATOM 185 CA SER A 68 -73.008 30.499 -10.476 1.00 30.06 C ANISOU 185 CA SER A 68 4398 3439 3586 168 10 -334 C ATOM 186 C SER A 68 -73.852 29.323 -10.038 1.00 29.14 C ANISOU 186 C SER A 68 4326 3373 3372 151 53 -371 C ATOM 187 O SER A 68 -74.592 29.444 -9.072 1.00 31.87 O ANISOU 187 O SER A 68 4644 3736 3730 139 72 -461 O ATOM 188 CB SER A 68 -73.908 31.726 -10.598 1.00 33.10 C ANISOU 188 CB SER A 68 4699 3764 4114 171 -26 -374 C ATOM 189 OG SER A 68 -73.146 32.907 -10.744 1.00 34.94 O ANISOU 189 OG SER A 68 4879 3943 4455 183 -66 -354 O ATOM 190 N LYS A 69 -73.810 28.205 -10.755 1.00 34.26 N ANISOU 190 N LYS A 69 5035 4048 3932 148 69 -308 N ATOM 191 CA LYS A 69 -74.595 27.053 -10.333 1.00 32.59 C ANISOU 191 CA LYS A 69 4865 3880 3639 130 109 -339 C ATOM 192 C LYS A 69 -74.152 26.607 -8.950 1.00 30.21 C ANISOU 192 C LYS A 69 4585 3623 3271 119 141 -389 C ATOM 193 O LYS A 69 -72.987 26.749 -8.575 1.00 30.42 O ANISOU 193 O LYS A 69 4622 3657 3281 127 137 -375 O ATOM 194 CB LYS A 69 -74.453 25.914 -11.330 1.00 31.28 C ANISOU 194 CB LYS A 69 4756 3731 3398 131 118 -266 C ATOM 195 CG LYS A 69 -73.317 24.956 -11.070 1.00 28.94 C ANISOU 195 CG LYS A 69 4517 3464 3013 133 137 -233 C ATOM 196 CD LYS A 69 -73.441 23.743 -12.008 1.00 27.70 C ANISOU 196 CD LYS A 69 4406 3323 2794 131 150 -185 C ATOM 197 CE LYS A 69 -72.906 24.078 -13.377 1.00 27.45 C ANISOU 197 CE LYS A 69 4365 3281 2784 144 120 -119 C ATOM 198 NZ LYS A 69 -71.411 24.127 -13.340 1.00 27.80 N1+ ANISOU 198 NZ LYS A 69 4425 3329 2808 156 112 -84 N1+ ATOM 199 N ILE A 70 -75.107 26.089 -8.180 1.00 34.73 N ANISOU 199 N ILE A 70 5159 4230 3805 96 173 -448 N ATOM 200 CA ILE A 70 -74.879 25.682 -6.793 1.00 33.90 C ANISOU 200 CA ILE A 70 5065 4182 3631 76 204 -496 C ATOM 201 C ILE A 70 -74.984 24.170 -6.631 1.00 32.75 C ANISOU 201 C ILE A 70 4987 4077 3380 57 237 -457 C ATOM 202 O ILE A 70 -74.935 23.658 -5.508 1.00 35.27 O ANISOU 202 O ILE A 70 5319 4450 3630 33 263 -483 O ATOM 203 CB ILE A 70 -75.839 26.410 -5.840 1.00 34.99 C ANISOU 203 CB ILE A 70 5139 4342 3812 57 216 -604 C ATOM 204 CG1 ILE A 70 -77.254 25.849 -5.997 1.00 33.39 C ANISOU 204 CG1 ILE A 70 4938 4151 3597 36 238 -629 C ATOM 205 CG2 ILE A 70 -75.799 27.926 -6.089 1.00 30.67 C ANISOU 205 CG2 ILE A 70 4517 3740 3397 78 177 -645 C ATOM 206 CD1 ILE A 70 -78.311 26.564 -5.195 1.00 31.14 C ANISOU 206 CD1 ILE A 70 4583 3888 3363 17 249 -742 C ATOM 207 N GLY A 71 -75.097 23.454 -7.736 1.00 34.32 N ANISOU 207 N GLY A 71 5223 4251 3566 65 233 -394 N ATOM 208 CA GLY A 71 -75.381 22.035 -7.741 1.00 32.91 C ANISOU 208 CA GLY A 71 5098 4095 3312 48 261 -363 C ATOM 209 C GLY A 71 -75.969 21.642 -9.084 1.00 32.07 C ANISOU 209 C GLY A 71 5001 3957 3226 58 253 -328 C ATOM 210 O GLY A 71 -76.064 22.448 -10.015 1.00 28.82 O ANISOU 210 O GLY A 71 4560 3515 2877 76 225 -317 O ATOM 211 N GLY A 72 -76.372 20.375 -9.160 1.00 28.63 N ANISOU 211 N GLY A 72 4605 3535 2738 42 278 -310 N ATOM 212 CA GLY A 72 -77.023 19.857 -10.340 1.00 28.08 C ANISOU 212 CA GLY A 72 4543 3446 2679 46 277 -289 C ATOM 213 C GLY A 72 -76.169 18.839 -11.070 1.00 27.46 C ANISOU 213 C GLY A 72 4507 3361 2564 58 275 -231 C ATOM 214 O GLY A 72 -76.667 17.787 -11.471 1.00 27.43 O ANISOU 214 O GLY A 72 4525 3358 2541 49 291 -224 O ATOM 215 N LEU A 73 -74.874 19.134 -11.213 1.00 27.31 N ANISOU 215 N LEU A 73 4496 3338 2544 78 255 -196 N ATOM 216 CA LEU A 73 -73.984 18.310 -12.015 1.00 27.12 C ANISOU 216 CA LEU A 73 4501 3308 2495 92 250 -150 C ATOM 217 C LEU A 73 -73.790 16.943 -11.374 1.00 30.04 C ANISOU 217 C LEU A 73 4912 3682 2821 79 273 -139 C ATOM 218 O LEU A 73 -73.233 16.825 -10.273 1.00 27.77 O ANISOU 218 O LEU A 73 4639 3403 2507 72 277 -133 O ATOM 219 CB LEU A 73 -72.635 18.996 -12.207 1.00 27.00 C ANISOU 219 CB LEU A 73 4481 3290 2490 114 225 -121 C ATOM 220 CG LEU A 73 -72.624 20.324 -12.952 1.00 27.01 C ANISOU 220 CG LEU A 73 4439 3281 2542 126 197 -113 C ATOM 221 CD1 LEU A 73 -71.218 20.692 -13.425 1.00 26.90 C ANISOU 221 CD1 LEU A 73 4425 3267 2529 145 175 -72 C ATOM 222 CD2 LEU A 73 -73.599 20.309 -14.103 1.00 27.04 C ANISOU 222 CD2 LEU A 73 4423 3286 2564 123 191 -109 C ATOM 223 N GLY A 74 -74.209 15.909 -12.104 1.00 27.17 N ANISOU 223 N GLY A 74 4560 3309 2452 76 283 -134 N ATOM 224 CA GLY A 74 -74.080 14.531 -11.699 1.00 27.29 C ANISOU 224 CA GLY A 74 4609 3316 2446 64 300 -118 C ATOM 225 C GLY A 74 -75.374 14.080 -11.073 1.00 28.57 C ANISOU 225 C GLY A 74 4772 3483 2601 33 326 -142 C ATOM 226 O GLY A 74 -75.829 12.962 -11.325 1.00 29.43 O ANISOU 226 O GLY A 74 4893 3576 2713 21 340 -139 O ATOM 227 N THR A 75 -75.979 14.962 -10.261 1.00 30.44 N ANISOU 227 N THR A 75 4990 3741 2834 18 332 -171 N ATOM 228 CA THR A 75 -77.164 14.619 -9.484 1.00 28.08 C ANISOU 228 CA THR A 75 4688 3459 2522 -18 360 -199 C ATOM 229 C THR A 75 -78.451 14.819 -10.272 1.00 30.03 C ANISOU 229 C THR A 75 4910 3701 2801 -21 367 -239 C ATOM 230 O THR A 75 -79.407 14.054 -10.108 1.00 30.21 O ANISOU 230 O THR A 75 4936 3725 2818 -47 391 -253 O ATOM 231 CB THR A 75 -77.213 15.473 -8.224 1.00 28.11 C ANISOU 231 CB THR A 75 4675 3501 2507 -35 365 -226 C ATOM 232 CG2 THR A 75 -76.115 15.075 -7.248 1.00 28.25 C ANISOU 232 CG2 THR A 75 4718 3536 2481 -41 362 -185 C ATOM 233 OG1 THR A 75 -77.054 16.843 -8.599 1.00 27.96 O ANISOU 233 OG1 THR A 75 4621 3477 2525 -11 344 -255 O ATOM 234 N ILE A 76 -78.511 15.855 -11.100 1.00 27.71 N ANISOU 234 N ILE A 76 4585 3400 2542 2 345 -254 N ATOM 235 CA ILE A 76 -79.724 16.157 -11.851 1.00 31.05 C ANISOU 235 CA ILE A 76 4979 3820 2998 0 345 -289 C ATOM 236 C ILE A 76 -79.472 16.009 -13.351 1.00 31.21 C ANISOU 236 C ILE A 76 4995 3830 3032 23 325 -265 C ATOM 237 O ILE A 76 -80.074 15.161 -14.022 1.00 27.58 O ANISOU 237 O ILE A 76 4539 3370 2571 18 336 -273 O ATOM 238 CB ILE A 76 -80.230 17.572 -11.511 1.00 28.95 C ANISOU 238 CB ILE A 76 4669 3559 2771 2 332 -330 C ATOM 239 CG1 ILE A 76 -80.681 17.634 -10.052 1.00 28.34 C ANISOU 239 CG1 ILE A 76 4586 3508 2672 -29 358 -372 C ATOM 240 CG2 ILE A 76 -81.354 17.958 -12.455 1.00 31.63 C ANISOU 240 CG2 ILE A 76 4974 3891 3155 6 321 -356 C ATOM 241 CD1 ILE A 76 -81.269 18.935 -9.644 1.00 28.35 C ANISOU 241 CD1 ILE A 76 4535 3516 2721 -30 349 -431 C ATOM 242 N TYR A 77 -78.592 16.853 -13.875 1.00 28.82 N ANISOU 242 N TYR A 77 4680 3527 2744 47 295 -238 N ATOM 243 CA TYR A 77 -78.121 16.760 -15.240 1.00 27.29 C ANISOU 243 CA TYR A 77 4479 3339 2550 65 275 -208 C ATOM 244 C TYR A 77 -76.932 15.818 -15.273 1.00 29.60 C ANISOU 244 C TYR A 77 4806 3632 2811 73 281 -181 C ATOM 245 O TYR A 77 -75.945 16.039 -14.565 1.00 30.86 O ANISOU 245 O TYR A 77 4981 3785 2960 79 276 -161 O ATOM 246 CB TYR A 77 -77.747 18.145 -15.760 1.00 30.10 C ANISOU 246 CB TYR A 77 4801 3697 2939 81 239 -185 C ATOM 247 CG TYR A 77 -78.877 19.130 -15.563 1.00 29.38 C ANISOU 247 CG TYR A 77 4671 3596 2897 75 228 -216 C ATOM 248 CD1 TYR A 77 -80.023 19.047 -16.355 1.00 29.46 C ANISOU 248 CD1 TYR A 77 4657 3613 2923 70 225 -232 C ATOM 249 CD2 TYR A 77 -78.814 20.117 -14.581 1.00 27.55 C ANISOU 249 CD2 TYR A 77 4421 3348 2700 75 222 -237 C ATOM 250 CE1 TYR A 77 -81.068 19.918 -16.181 1.00 29.31 C ANISOU 250 CE1 TYR A 77 4599 3581 2958 66 212 -264 C ATOM 251 CE2 TYR A 77 -79.853 21.005 -14.396 1.00 27.79 C ANISOU 251 CE2 TYR A 77 4407 3364 2787 71 211 -277 C ATOM 252 CZ TYR A 77 -80.986 20.897 -15.199 1.00 31.93 C ANISOU 252 CZ TYR A 77 4910 3890 3331 67 205 -288 C ATOM 253 OH TYR A 77 -82.046 21.766 -15.055 1.00 30.81 O ANISOU 253 OH TYR A 77 4720 3732 3256 64 191 -329 O ATOM 254 N GLU A 78 -77.029 14.770 -16.084 1.00 30.46 N ANISOU 254 N GLU A 78 4920 3746 2909 72 290 -185 N ATOM 255 CA GLU A 78 -75.972 13.781 -16.211 1.00 30.92 C ANISOU 255 CA GLU A 78 5001 3798 2950 81 293 -169 C ATOM 256 C GLU A 78 -75.158 14.030 -17.474 1.00 27.15 C ANISOU 256 C GLU A 78 4502 3348 2464 98 272 -154 C ATOM 257 O GLU A 78 -75.647 14.619 -18.436 1.00 29.62 O ANISOU 257 O GLU A 78 4783 3691 2779 99 259 -155 O ATOM 258 CB GLU A 78 -76.542 12.368 -16.259 1.00 28.53 C ANISOU 258 CB GLU A 78 4709 3479 2652 67 317 -193 C ATOM 259 CG GLU A 78 -77.273 11.941 -15.031 1.00 27.51 C ANISOU 259 CG GLU A 78 4601 3328 2525 43 340 -199 C ATOM 260 CD GLU A 78 -77.725 10.505 -15.124 1.00 28.11 C ANISOU 260 CD GLU A 78 4684 3379 2616 29 360 -214 C ATOM 261 OE1 GLU A 78 -77.018 9.607 -14.611 1.00 27.89 O ANISOU 261 OE1 GLU A 78 4678 3324 2594 28 362 -190 O ATOM 262 OE2 GLU A 78 -78.762 10.279 -15.778 1.00 30.94 O1- ANISOU 262 OE2 GLU A 78 5023 3745 2987 21 370 -249 O1- ATOM 263 N SER A 79 -73.909 13.581 -17.443 1.00 27.11 N ANISOU 263 N SER A 79 4512 3340 2450 110 269 -138 N ATOM 264 CA SER A 79 -72.976 13.603 -18.548 1.00 27.13 C ANISOU 264 CA SER A 79 4494 3375 2438 123 254 -129 C ATOM 265 C SER A 79 -73.084 12.299 -19.337 1.00 31.56 C ANISOU 265 C SER A 79 5046 3947 3000 122 268 -167 C ATOM 266 O SER A 79 -73.781 11.363 -18.947 1.00 35.77 O ANISOU 266 O SER A 79 5590 4449 3551 112 286 -193 O ATOM 267 CB SER A 79 -71.559 13.803 -18.025 1.00 27.03 C ANISOU 267 CB SER A 79 4498 3351 2421 138 243 -102 C ATOM 268 OG SER A 79 -71.138 12.697 -17.246 1.00 27.10 O ANISOU 268 OG SER A 79 4536 3323 2438 139 255 -108 O ATOM 269 N LEU A 80 -72.379 12.226 -20.465 1.00 31.16 N ANISOU 269 N LEU A 80 4967 3942 2932 128 258 -174 N ATOM 270 CA LEU A 80 -72.436 10.989 -21.241 1.00 30.59 C ANISOU 270 CA LEU A 80 4874 3884 2865 127 271 -226 C ATOM 271 C LEU A 80 -71.797 9.839 -20.480 1.00 32.53 C ANISOU 271 C LEU A 80 5144 4071 3145 135 281 -239 C ATOM 272 O LEU A 80 -72.348 8.733 -20.434 1.00 34.44 O ANISOU 272 O LEU A 80 5384 4283 3420 129 296 -276 O ATOM 273 CB LEU A 80 -71.753 11.163 -22.593 1.00 31.99 C ANISOU 273 CB LEU A 80 5008 4137 3009 129 261 -238 C ATOM 274 CG LEU A 80 -72.365 12.178 -23.539 1.00 31.77 C ANISOU 274 CG LEU A 80 4947 4177 2947 117 246 -217 C ATOM 275 CD1 LEU A 80 -71.419 12.429 -24.664 1.00 32.54 C ANISOU 275 CD1 LEU A 80 5005 4355 3003 114 235 -212 C ATOM 276 CD2 LEU A 80 -73.684 11.665 -24.065 1.00 37.46 C ANISOU 276 CD2 LEU A 80 5648 4916 3670 105 258 -259 C ATOM 277 N PHE A 81 -70.627 10.079 -19.896 1.00 32.96 N ANISOU 277 N PHE A 81 5217 4106 3199 148 269 -208 N ATOM 278 CA PHE A 81 -69.982 9.136 -18.999 1.00 33.01 C ANISOU 278 CA PHE A 81 5248 4053 3241 155 270 -203 C ATOM 279 C PHE A 81 -69.524 9.886 -17.755 1.00 36.13 C ANISOU 279 C PHE A 81 5680 4424 3625 159 261 -150 C ATOM 280 O PHE A 81 -69.462 11.119 -17.731 1.00 34.02 O ANISOU 280 O PHE A 81 5412 4185 3330 159 252 -125 O ATOM 281 CB PHE A 81 -68.771 8.450 -19.650 1.00 30.91 C ANISOU 281 CB PHE A 81 4958 3795 2992 172 263 -234 C ATOM 282 CG PHE A 81 -69.083 7.757 -20.947 1.00 37.91 C ANISOU 282 CG PHE A 81 5797 4721 3885 168 272 -301 C ATOM 283 CD1 PHE A 81 -69.068 8.455 -22.161 1.00 33.03 C ANISOU 283 CD1 PHE A 81 5141 4189 3218 163 270 -317 C ATOM 284 CD2 PHE A 81 -69.372 6.397 -20.964 1.00 36.05 C ANISOU 284 CD2 PHE A 81 5549 4440 3708 167 282 -348 C ATOM 285 CE1 PHE A 81 -69.351 7.816 -23.341 1.00 33.66 C ANISOU 285 CE1 PHE A 81 5172 4321 3297 157 279 -384 C ATOM 286 CE2 PHE A 81 -69.649 5.752 -22.162 1.00 40.89 C ANISOU 286 CE2 PHE A 81 6111 5095 4331 164 291 -423 C ATOM 287 CZ PHE A 81 -69.633 6.468 -23.355 1.00 38.02 C ANISOU 287 CZ PHE A 81 5710 4830 3907 158 291 -444 C ATOM 288 N PHE A 82 -69.211 9.127 -16.711 1.00 37.95 N ANISOU 288 N PHE A 82 5937 4601 3880 159 260 -131 N ATOM 289 CA PHE A 82 -68.466 9.671 -15.589 1.00 36.96 C ANISOU 289 CA PHE A 82 5840 4463 3742 164 248 -86 C ATOM 290 C PHE A 82 -66.986 9.566 -15.915 1.00 35.53 C ANISOU 290 C PHE A 82 5650 4284 3568 186 230 -85 C ATOM 291 O PHE A 82 -66.489 8.483 -16.233 1.00 36.84 O ANISOU 291 O PHE A 82 5803 4423 3770 195 226 -107 O ATOM 292 CB PHE A 82 -68.778 8.938 -14.284 1.00 32.79 C ANISOU 292 CB PHE A 82 5341 3889 3227 149 251 -56 C ATOM 293 CG PHE A 82 -67.891 9.341 -13.141 1.00 34.66 C ANISOU 293 CG PHE A 82 5602 4121 3446 153 236 -12 C ATOM 294 CD1 PHE A 82 -67.470 8.403 -12.204 1.00 39.90 C ANISOU 294 CD1 PHE A 82 6285 4745 4130 148 226 24 C ATOM 295 CD2 PHE A 82 -67.483 10.655 -12.990 1.00 35.31 C ANISOU 295 CD2 PHE A 82 5683 4238 3496 161 229 -4 C ATOM 296 CE1 PHE A 82 -66.642 8.772 -11.136 1.00 40.18 C ANISOU 296 CE1 PHE A 82 6339 4786 4143 151 210 65 C ATOM 297 CE2 PHE A 82 -66.650 11.028 -11.938 1.00 39.67 C ANISOU 297 CE2 PHE A 82 6251 4790 4031 165 215 28 C ATOM 298 CZ PHE A 82 -66.234 10.079 -11.005 1.00 38.72 C ANISOU 298 CZ PHE A 82 6152 4641 3920 160 206 62 C ATOM 299 N VAL A 83 -66.296 10.693 -15.833 1.00 32.79 N ANISOU 299 N VAL A 83 5302 3964 3192 196 219 -64 N ATOM 300 CA VAL A 83 -64.877 10.794 -16.115 1.00 32.36 C ANISOU 300 CA VAL A 83 5237 3918 3139 215 203 -63 C ATOM 301 C VAL A 83 -64.209 11.488 -14.940 1.00 33.84 C ANISOU 301 C VAL A 83 5449 4095 3313 221 189 -22 C ATOM 302 O VAL A 83 -64.760 12.451 -14.394 1.00 38.90 O ANISOU 302 O VAL A 83 6098 4747 3933 211 192 -6 O ATOM 303 CB VAL A 83 -64.665 11.557 -17.438 1.00 34.26 C ANISOU 303 CB VAL A 83 5441 4218 3356 217 202 -80 C ATOM 304 CG1 VAL A 83 -63.232 12.003 -17.609 1.00 36.05 C ANISOU 304 CG1 VAL A 83 5658 4464 3576 233 187 -71 C ATOM 305 CG2 VAL A 83 -65.063 10.673 -18.598 1.00 32.09 C ANISOU 305 CG2 VAL A 83 5135 3965 3091 213 213 -130 C ATOM 306 N THR A 84 -63.043 10.993 -14.521 1.00 32.35 N ANISOU 306 N THR A 84 5268 3884 3141 237 174 -12 N ATOM 307 CA THR A 84 -62.356 11.652 -13.410 1.00 35.17 C ANISOU 307 CA THR A 84 5644 4238 3482 242 160 22 C ATOM 308 C THR A 84 -60.848 11.468 -13.505 1.00 31.68 C ANISOU 308 C THR A 84 5193 3790 3053 265 141 22 C ATOM 309 O THR A 84 -60.344 10.531 -14.131 1.00 29.10 O ANISOU 309 O THR A 84 4850 3447 2759 277 136 -2 O ATOM 310 CB THR A 84 -62.837 11.156 -12.035 1.00 33.87 C ANISOU 310 CB THR A 84 5509 4046 3314 228 160 54 C ATOM 311 CG2 THR A 84 -62.585 9.666 -11.868 1.00 34.66 C ANISOU 311 CG2 THR A 84 5616 4099 3455 231 150 63 C ATOM 312 OG1 THR A 84 -62.125 11.852 -11.008 1.00 32.66 O ANISOU 312 OG1 THR A 84 5368 3905 3137 232 146 80 O ATOM 313 N ASN A 85 -60.133 12.384 -12.854 1.00 31.81 N ANISOU 313 N ASN A 85 5216 3820 3051 272 129 43 N ATOM 314 CA ASN A 85 -58.694 12.272 -12.722 1.00 31.57 C ANISOU 314 CA ASN A 85 5180 3783 3032 294 109 46 C ATOM 315 C ASN A 85 -58.292 11.462 -11.503 1.00 32.10 C ANISOU 315 C ASN A 85 5271 3814 3113 298 90 77 C ATOM 316 O ASN A 85 -57.103 11.420 -11.168 1.00 30.00 O ANISOU 316 O ASN A 85 5003 3541 2856 316 69 85 O ATOM 317 CB ASN A 85 -58.049 13.654 -12.663 1.00 32.07 C ANISOU 317 CB ASN A 85 5233 3878 3073 299 103 52 C ATOM 318 CG ASN A 85 -58.723 14.583 -11.677 1.00 31.50 C ANISOU 318 CG ASN A 85 5175 3815 2979 285 107 69 C ATOM 319 ND2 ASN A 85 -58.840 15.844 -12.046 1.00 29.63 N ANISOU 319 ND2 ASN A 85 4919 3603 2737 282 110 65 N ATOM 320 OD1 ASN A 85 -59.117 14.175 -10.585 1.00 35.60 O ANISOU 320 OD1 ASN A 85 5716 4322 3487 276 105 86 O ATOM 321 N ALA A 86 -59.253 10.795 -10.854 1.00 32.12 N ANISOU 321 N ALA A 86 5293 3795 3115 279 96 98 N ATOM 322 CA ALA A 86 -58.991 10.083 -9.611 1.00 32.96 C ANISOU 322 CA ALA A 86 5421 3876 3227 275 76 144 C ATOM 323 C ALA A 86 -58.449 8.686 -9.830 1.00 32.29 C ANISOU 323 C ALA A 86 5329 3736 3204 288 56 149 C ATOM 324 O ALA A 86 -57.822 8.138 -8.913 1.00 32.13 O ANISOU 324 O ALA A 86 5319 3691 3198 292 29 193 O ATOM 325 CB ALA A 86 -60.258 9.998 -8.757 1.00 33.66 C ANISOU 325 CB ALA A 86 5530 3973 3287 243 91 171 C ATOM 326 N ASN A 87 -58.675 8.099 -11.003 1.00 34.60 N ANISOU 326 N ASN A 87 5598 4009 3538 294 67 105 N ATOM 327 CA ASN A 87 -58.166 6.765 -11.297 1.00 36.09 C ANISOU 327 CA ASN A 87 5769 4140 3803 309 48 94 C ATOM 328 C ASN A 87 -58.099 6.573 -12.807 1.00 40.93 C ANISOU 328 C ASN A 87 6343 4764 4444 320 63 19 C ATOM 329 O ASN A 87 -58.573 7.405 -13.591 1.00 39.57 O ANISOU 329 O ASN A 87 6163 4645 4228 313 88 -11 O ATOM 330 CB ASN A 87 -59.009 5.659 -10.634 1.00 37.38 C ANISOU 330 CB ASN A 87 5946 4252 4004 288 42 135 C ATOM 331 CG ASN A 87 -60.374 5.461 -11.278 1.00 37.00 C ANISOU 331 CG ASN A 87 5893 4208 3957 268 74 105 C ATOM 332 ND2 ASN A 87 -61.356 6.242 -10.853 1.00 32.92 N ANISOU 332 ND2 ASN A 87 5400 3732 3377 244 96 122 N ATOM 333 OD1 ASN A 87 -60.551 4.566 -12.103 1.00 37.01 O ANISOU 333 OD1 ASN A 87 5867 4174 4021 273 77 62 O ATOM 334 N THR A 88 -57.492 5.448 -13.200 1.00 42.56 N ANISOU 334 N THR A 88 6521 4923 4729 337 46 -11 N ATOM 335 CA THR A 88 -57.231 5.119 -14.597 1.00 42.95 C ANISOU 335 CA THR A 88 6521 4988 4810 348 57 -95 C ATOM 336 C THR A 88 -58.010 3.887 -15.054 1.00 40.76 C ANISOU 336 C THR A 88 6220 4664 4604 341 63 -132 C ATOM 337 O THR A 88 -57.508 3.089 -15.844 1.00 42.01 O ANISOU 337 O THR A 88 6330 4803 4829 356 57 -200 O ATOM 338 CB THR A 88 -55.735 4.908 -14.825 1.00 42.78 C ANISOU 338 CB THR A 88 6469 4957 4827 376 33 -126 C ATOM 339 CG2 THR A 88 -54.981 6.220 -14.652 1.00 41.07 C ANISOU 339 CG2 THR A 88 6267 4799 4540 381 34 -105 C ATOM 340 OG1 THR A 88 -55.236 3.934 -13.899 1.00 40.82 O ANISOU 340 OG1 THR A 88 6226 4629 4653 388 -4 -87 O ATOM 341 N ASN A 89 -59.235 3.726 -14.566 1.00 45.59 N ANISOU 341 N ASN A 89 6859 5257 5204 318 75 -95 N ATOM 342 CA ASN A 89 -60.127 2.675 -15.021 1.00 48.02 C ANISOU 342 CA ASN A 89 7145 5525 5576 307 85 -130 C ATOM 343 C ASN A 89 -60.954 3.169 -16.205 1.00 43.29 C ANISOU 343 C ASN A 89 6525 4994 4929 296 120 -194 C ATOM 344 O ASN A 89 -60.896 4.333 -16.608 1.00 41.18 O ANISOU 344 O ASN A 89 6263 4801 4582 293 135 -197 O ATOM 345 CB ASN A 89 -61.048 2.196 -13.889 1.00 47.20 C ANISOU 345 CB ASN A 89 7077 5370 5486 283 80 -55 C ATOM 346 CG ASN A 89 -60.290 1.516 -12.746 1.00 47.35 C ANISOU 346 CG ASN A 89 7110 5321 5560 289 40 16 C ATOM 347 ND2 ASN A 89 -60.556 1.965 -11.533 1.00 44.51 N ANISOU 347 ND2 ASN A 89 6794 4973 5143 270 34 101 N ATOM 348 OD1 ASN A 89 -59.501 0.579 -12.952 1.00 47.35 O ANISOU 348 OD1 ASN A 89 7075 5261 5656 310 12 -7 O ATOM 349 N ASP A 90 -61.737 2.261 -16.772 1.00 42.36 N ANISOU 349 N ASP A 90 6379 4851 4866 287 132 -242 N ATOM 350 CA ASP A 90 -62.636 2.637 -17.846 1.00 40.33 C ANISOU 350 CA ASP A 90 6100 4660 4564 274 163 -298 C ATOM 351 C ASP A 90 -63.670 3.641 -17.355 1.00 40.10 C ANISOU 351 C ASP A 90 6116 4666 4453 252 181 -242 C ATOM 352 O ASP A 90 -64.116 3.598 -16.208 1.00 43.89 O ANISOU 352 O ASP A 90 6638 5106 4934 239 176 -175 O ATOM 353 CB ASP A 90 -63.312 1.392 -18.417 1.00 41.64 C ANISOU 353 CB ASP A 90 6225 4784 4813 268 171 -363 C ATOM 354 CG ASP A 90 -62.342 0.512 -19.212 1.00 44.65 C ANISOU 354 CG ASP A 90 6541 5148 5275 290 158 -451 C ATOM 355 OD1 ASP A 90 -61.113 0.747 -19.134 1.00 46.83 O ANISOU 355 OD1 ASP A 90 6811 5431 5551 309 140 -449 O ATOM 356 OD2 ASP A 90 -62.794 -0.399 -19.931 1.00 42.10 O1- ANISOU 356 OD2 ASP A 90 6169 4809 5019 287 166 -529 O1- ATOM 357 N TYR A 91 -64.021 4.577 -18.228 1.00 35.02 N ANISOU 357 N TYR A 91 5461 4104 3742 245 199 -268 N ATOM 358 CA TYR A 91 -65.102 5.505 -17.935 1.00 35.42 C ANISOU 358 CA TYR A 91 5543 4186 3731 226 215 -230 C ATOM 359 C TYR A 91 -66.350 4.736 -17.516 1.00 36.27 C ANISOU 359 C TYR A 91 5662 4246 3873 207 227 -226 C ATOM 360 O TYR A 91 -66.541 3.572 -17.873 1.00 39.36 O ANISOU 360 O TYR A 91 6026 4598 4332 207 229 -269 O ATOM 361 CB TYR A 91 -65.419 6.367 -19.159 1.00 36.25 C ANISOU 361 CB TYR A 91 5619 4378 3777 220 229 -265 C ATOM 362 CG TYR A 91 -64.317 7.298 -19.605 1.00 35.85 C ANISOU 362 CG TYR A 91 5555 4383 3683 231 219 -258 C ATOM 363 CD1 TYR A 91 -63.137 7.427 -18.880 1.00 31.32 C ANISOU 363 CD1 TYR A 91 4999 3781 3121 248 201 -227 C ATOM 364 CD2 TYR A 91 -64.454 8.036 -20.780 1.00 36.56 C ANISOU 364 CD2 TYR A 91 5611 4558 3721 222 227 -280 C ATOM 365 CE1 TYR A 91 -62.130 8.274 -19.309 1.00 31.58 C ANISOU 365 CE1 TYR A 91 5018 3865 3117 256 193 -223 C ATOM 366 CE2 TYR A 91 -63.466 8.896 -21.212 1.00 35.46 C ANISOU 366 CE2 TYR A 91 5457 4472 3543 227 218 -267 C ATOM 367 CZ TYR A 91 -62.305 9.017 -20.479 1.00 36.26 C ANISOU 367 CZ TYR A 91 5577 4541 3660 244 203 -241 C ATOM 368 OH TYR A 91 -61.325 9.880 -20.946 1.00 36.70 O ANISOU 368 OH TYR A 91 5615 4652 3679 246 195 -230 O ATOM 369 N VAL A 92 -67.219 5.394 -16.770 1.00 34.53 N ANISOU 369 N VAL A 92 5477 4032 3611 188 237 -179 N ATOM 370 CA VAL A 92 -68.415 4.761 -16.229 1.00 36.37 C ANISOU 370 CA VAL A 92 5724 4227 3869 165 250 -167 C ATOM 371 C VAL A 92 -69.598 5.179 -17.092 1.00 30.79 C ANISOU 371 C VAL A 92 4999 3567 3132 153 272 -209 C ATOM 372 O VAL A 92 -69.829 6.383 -17.272 1.00 30.25 O ANISOU 372 O VAL A 92 4936 3553 3004 151 276 -199 O ATOM 373 CB VAL A 92 -68.645 5.132 -14.752 1.00 34.78 C ANISOU 373 CB VAL A 92 5568 4008 3640 149 247 -93 C ATOM 374 CG1 VAL A 92 -70.005 4.620 -14.263 1.00 29.07 C ANISOU 374 CG1 VAL A 92 4855 3261 2929 118 266 -83 C ATOM 375 CG2 VAL A 92 -67.518 4.555 -13.945 1.00 29.16 C ANISOU 375 CG2 VAL A 92 4868 3249 2962 160 221 -49 C ATOM 376 N PRO A 93 -70.339 4.261 -17.604 1.00 30.16 N ANISOU 376 N PRO A 93 4895 3467 3096 144 285 -254 N ATOM 377 CA PRO A 93 -71.447 4.617 -18.488 1.00 29.33 C ANISOU 377 CA PRO A 93 4769 3413 2964 133 303 -298 C ATOM 378 C PRO A 93 -72.618 5.233 -17.755 1.00 28.76 C ANISOU 378 C PRO A 93 4726 3344 2858 110 317 -262 C ATOM 379 O PRO A 93 -73.296 4.548 -16.991 1.00 32.09 O ANISOU 379 O PRO A 93 5164 3718 3311 91 327 -245 O ATOM 380 CB PRO A 93 -71.818 3.273 -19.127 1.00 33.89 C ANISOU 380 CB PRO A 93 5307 3957 3611 130 312 -362 C ATOM 381 CG PRO A 93 -71.341 2.231 -18.139 1.00 31.73 C ANISOU 381 CG PRO A 93 5051 3595 3412 130 299 -327 C ATOM 382 CD PRO A 93 -70.119 2.811 -17.498 1.00 31.28 C ANISOU 382 CD PRO A 93 5020 3538 3327 146 278 -273 C ATOM 383 N LEU A 94 -72.874 6.517 -17.994 1.00 29.28 N ANISOU 383 N LEU A 94 4794 3466 2865 111 317 -252 N ATOM 384 CA LEU A 94 -74.073 7.171 -17.493 1.00 29.37 C ANISOU 384 CA LEU A 94 4820 3487 2852 91 329 -238 C ATOM 385 C LEU A 94 -75.126 7.284 -18.599 1.00 29.49 C ANISOU 385 C LEU A 94 4801 3543 2860 85 339 -287 C ATOM 386 O LEU A 94 -75.830 6.311 -18.895 1.00 28.53 O ANISOU 386 O LEU A 94 4665 3402 2773 74 354 -326 O ATOM 387 CB LEU A 94 -73.717 8.547 -16.928 1.00 31.74 C ANISOU 387 CB LEU A 94 5138 3813 3109 96 318 -196 C ATOM 388 CG LEU A 94 -72.865 8.532 -15.651 1.00 30.58 C ANISOU 388 CG LEU A 94 5025 3635 2960 97 309 -148 C ATOM 389 CD1 LEU A 94 -72.163 9.857 -15.526 1.00 27.74 C ANISOU 389 CD1 LEU A 94 4667 3307 2565 110 293 -124 C ATOM 390 CD2 LEU A 94 -73.690 8.235 -14.416 1.00 28.04 C ANISOU 390 CD2 LEU A 94 4727 3288 2638 70 324 -125 C ATOM 391 N LEU A 95 -75.266 8.464 -19.207 1.00 28.84 N ANISOU 391 N LEU A 95 4704 3516 2738 89 330 -283 N ATOM 392 CA LEU A 95 -76.287 8.619 -20.242 1.00 30.77 C ANISOU 392 CA LEU A 95 4915 3806 2972 82 334 -321 C ATOM 393 C LEU A 95 -75.854 8.003 -21.558 1.00 30.34 C ANISOU 393 C LEU A 95 4818 3793 2915 90 332 -369 C ATOM 394 O LEU A 95 -76.706 7.770 -22.418 1.00 29.77 O ANISOU 394 O LEU A 95 4713 3757 2840 81 338 -413 O ATOM 395 CB LEU A 95 -76.650 10.086 -20.461 1.00 27.87 C ANISOU 395 CB LEU A 95 4538 3479 2571 82 319 -293 C ATOM 396 CG LEU A 95 -77.771 10.586 -19.556 1.00 29.31 C ANISOU 396 CG LEU A 95 4737 3637 2763 67 327 -285 C ATOM 397 CD1 LEU A 95 -78.138 12.005 -19.919 1.00 28.30 C ANISOU 397 CD1 LEU A 95 4588 3543 2620 70 306 -265 C ATOM 398 CD2 LEU A 95 -78.998 9.667 -19.592 1.00 28.16 C ANISOU 398 CD2 LEU A 95 4584 3474 2639 50 351 -329 C ATOM 399 N ALA A 96 -74.556 7.742 -21.723 1.00 32.06 N ANISOU 399 N ALA A 96 5033 4014 3136 104 322 -367 N ATOM 400 CA ALA A 96 -74.008 6.975 -22.832 1.00 36.78 C ANISOU 400 CA ALA A 96 5586 4649 3739 111 323 -426 C ATOM 401 C ALA A 96 -73.406 5.672 -22.316 1.00 36.42 C ANISOU 401 C ALA A 96 5547 4532 3759 118 329 -451 C ATOM 402 O ALA A 96 -72.889 5.603 -21.198 1.00 35.17 O ANISOU 402 O ALA A 96 5429 4312 3623 123 323 -403 O ATOM 403 CB ALA A 96 -72.949 7.777 -23.591 1.00 35.95 C ANISOU 403 CB ALA A 96 5459 4614 3585 119 306 -411 C ATOM 404 N THR A 97 -73.488 4.631 -23.141 1.00 41.74 N ANISOU 404 N THR A 97 6175 5214 4469 118 337 -528 N ATOM 405 CA THR A 97 -72.987 3.308 -22.788 1.00 46.33 C ANISOU 405 CA THR A 97 6749 5721 5134 126 338 -560 C ATOM 406 C THR A 97 -71.775 2.913 -23.627 1.00 49.35 C ANISOU 406 C THR A 97 7084 6138 5528 142 330 -617 C ATOM 407 O THR A 97 -71.211 1.840 -23.423 1.00 50.54 O ANISOU 407 O THR A 97 7219 6226 5759 152 325 -651 O ATOM 408 CB THR A 97 -74.094 2.253 -22.956 1.00 40.32 C ANISOU 408 CB THR A 97 5965 4924 4433 112 355 -616 C ATOM 409 CG2 THR A 97 -75.396 2.681 -22.253 1.00 37.24 C ANISOU 409 CG2 THR A 97 5612 4514 4024 93 367 -572 C ATOM 410 OG1 THR A 97 -74.369 2.069 -24.344 1.00 43.94 O ANISOU 410 OG1 THR A 97 6359 5461 4873 110 363 -703 O ATOM 411 N GLU A 98 -71.340 3.766 -24.542 1.00 63.81 N ANISOU 411 N GLU A 98 8891 8070 7286 143 325 -625 N ATOM 412 CA GLU A 98 -70.629 3.276 -25.709 1.00 69.22 C ANISOU 412 CA GLU A 98 9509 8821 7972 147 326 -711 C ATOM 413 C GLU A 98 -69.809 4.351 -26.376 1.00 69.54 C ANISOU 413 C GLU A 98 9535 8961 7927 146 317 -688 C ATOM 414 O GLU A 98 -70.360 5.413 -26.658 1.00 72.70 O ANISOU 414 O GLU A 98 9945 9422 8255 133 314 -639 O ATOM 415 CB GLU A 98 -71.655 2.818 -26.699 1.00 73.48 C ANISOU 415 CB GLU A 98 9997 9416 8507 132 342 -790 C ATOM 416 CG GLU A 98 -71.432 1.568 -27.215 1.00 76.06 C ANISOU 416 CG GLU A 98 10265 9729 8904 137 349 -894 C ATOM 417 CD GLU A 98 -72.241 1.199 -28.429 1.00 80.26 C ANISOU 417 CD GLU A 98 10729 10347 9417 121 364 -990 C ATOM 418 OE1 GLU A 98 -72.078 1.813 -29.467 1.00 77.28 O ANISOU 418 OE1 GLU A 98 10313 10098 8954 111 364 -1012 O ATOM 419 OE2 GLU A 98 -73.067 0.237 -28.314 1.00 81.08 O1- ANISOU 419 OE2 GLU A 98 10818 10391 9597 118 375 -1042 O1- ATOM 420 N TYR A 99 -68.552 4.092 -26.711 1.00 46.80 N ANISOU 420 N TYR A 99 6624 6103 5055 157 311 -723 N ATOM 421 CA TYR A 99 -67.923 5.115 -27.528 1.00 43.29 C ANISOU 421 CA TYR A 99 6156 5773 4521 148 306 -704 C ATOM 422 C TYR A 99 -66.732 4.549 -28.278 1.00 41.17 C ANISOU 422 C TYR A 99 5825 5556 4260 153 307 -786 C ATOM 423 O TYR A 99 -66.119 3.568 -27.859 1.00 43.21 O ANISOU 423 O TYR A 99 6076 5737 4603 172 305 -833 O ATOM 424 CB TYR A 99 -67.536 6.362 -26.714 1.00 42.53 C ANISOU 424 CB TYR A 99 6120 5653 4387 153 290 -592 C ATOM 425 CG TYR A 99 -66.232 6.350 -25.965 1.00 43.35 C ANISOU 425 CG TYR A 99 6248 5702 4521 173 278 -566 C ATOM 426 CD1 TYR A 99 -66.078 5.608 -24.795 1.00 45.62 C ANISOU 426 CD1 TYR A 99 6575 5872 4887 190 274 -554 C ATOM 427 CD2 TYR A 99 -65.156 7.090 -26.414 1.00 41.12 C ANISOU 427 CD2 TYR A 99 5947 5488 4188 171 270 -548 C ATOM 428 CE1 TYR A 99 -64.875 5.614 -24.103 1.00 40.94 C ANISOU 428 CE1 TYR A 99 6003 5233 4321 209 259 -527 C ATOM 429 CE2 TYR A 99 -63.955 7.098 -25.731 1.00 39.21 C ANISOU 429 CE2 TYR A 99 5726 5198 3975 191 259 -527 C ATOM 430 CZ TYR A 99 -63.819 6.358 -24.583 1.00 39.35 C ANISOU 430 CZ TYR A 99 5783 5100 4070 211 252 -518 C ATOM 431 OH TYR A 99 -62.620 6.379 -23.921 1.00 40.36 O ANISOU 431 OH TYR A 99 5927 5184 4223 230 238 -495 O ATOM 432 N ALA A 100 -66.457 5.156 -29.435 1.00 40.95 N ANISOU 432 N ALA A 100 5748 5666 4146 134 310 -804 N ATOM 433 CA ALA A 100 -65.320 4.808 -30.275 1.00 38.89 C ANISOU 433 CA ALA A 100 5420 5486 3871 131 314 -883 C ATOM 434 C ALA A 100 -64.834 6.063 -30.977 1.00 34.91 C ANISOU 434 C ALA A 100 4900 5107 3256 108 308 -824 C ATOM 435 O ALA A 100 -65.614 6.982 -31.243 1.00 36.16 O ANISOU 435 O ALA A 100 5072 5317 3348 89 302 -754 O ATOM 436 CB ALA A 100 -65.677 3.719 -31.297 1.00 32.47 C ANISOU 436 CB ALA A 100 4523 4736 3079 121 331 -1021 C ATOM 437 N TRP A 101 -63.538 6.091 -31.268 1.00 32.95 N ANISOU 437 N TRP A 101 4620 4905 2995 109 307 -852 N ATOM 438 CA TRP A 101 -62.925 7.114 -32.102 1.00 36.87 C ANISOU 438 CA TRP A 101 5084 5537 3389 81 304 -812 C ATOM 439 C TRP A 101 -62.553 6.538 -33.472 1.00 39.59 C ANISOU 439 C TRP A 101 5326 6030 3685 56 321 -931 C ATOM 440 O TRP A 101 -62.290 5.337 -33.603 1.00 37.64 O ANISOU 440 O TRP A 101 5034 5760 3506 70 333 -1053 O ATOM 441 CB TRP A 101 -61.667 7.678 -31.441 1.00 34.74 C ANISOU 441 CB TRP A 101 4848 5224 3129 96 292 -753 C ATOM 442 CG TRP A 101 -61.909 8.715 -30.406 1.00 35.74 C ANISOU 442 CG TRP A 101 5055 5264 3259 106 274 -624 C ATOM 443 CD1 TRP A 101 -61.928 8.531 -29.052 1.00 34.46 C ANISOU 443 CD1 TRP A 101 4963 4957 3174 137 266 -587 C ATOM 444 CD2 TRP A 101 -62.154 10.111 -30.627 1.00 37.10 C ANISOU 444 CD2 TRP A 101 5243 5493 3360 83 261 -517 C ATOM 445 CE2 TRP A 101 -62.318 10.710 -29.359 1.00 35.84 C ANISOU 445 CE2 TRP A 101 5160 5214 3245 105 247 -431 C ATOM 446 CE3 TRP A 101 -62.257 10.913 -31.773 1.00 35.74 C ANISOU 446 CE3 TRP A 101 5022 5463 3094 44 257 -482 C ATOM 447 NE1 TRP A 101 -62.173 9.723 -28.420 1.00 40.81 N ANISOU 447 NE1 TRP A 101 5820 5729 3955 136 251 -476 N ATOM 448 CZ2 TRP A 101 -62.569 12.073 -29.199 1.00 34.37 C ANISOU 448 CZ2 TRP A 101 4999 5036 3025 92 229 -323 C ATOM 449 CZ3 TRP A 101 -62.514 12.274 -31.612 1.00 31.84 C ANISOU 449 CZ3 TRP A 101 4557 4972 2569 31 236 -360 C ATOM 450 CH2 TRP A 101 -62.658 12.839 -30.343 1.00 32.78 C ANISOU 450 CH2 TRP A 101 4749 4961 2746 57 222 -287 C ATOM 451 N ASN A 102 -62.513 7.403 -34.500 1.00 35.43 N ANISOU 451 N ASN A 102 4756 5661 3043 16 320 -895 N ATOM 452 CA ASN A 102 -61.963 6.926 -35.762 1.00 36.48 C ANISOU 452 CA ASN A 102 4788 5955 3119 -13 338 -1008 C ATOM 453 C ASN A 102 -60.438 6.907 -35.651 1.00 39.38 C ANISOU 453 C ASN A 102 5136 6328 3498 -6 340 -1034 C ATOM 454 O ASN A 102 -59.865 7.220 -34.599 1.00 39.19 O ANISOU 454 O ASN A 102 5179 6181 3529 23 327 -966 O ATOM 455 CB ASN A 102 -62.496 7.727 -36.970 1.00 38.61 C ANISOU 455 CB ASN A 102 5008 6409 3255 -64 336 -965 C ATOM 456 CG ASN A 102 -61.919 9.165 -37.108 1.00 40.09 C ANISOU 456 CG ASN A 102 5212 6662 3358 -91 318 -825 C ATOM 457 ND2 ASN A 102 -62.270 9.836 -38.221 1.00 35.44 N ANISOU 457 ND2 ASN A 102 4570 6243 2653 -141 312 -781 N ATOM 458 OD1 ASN A 102 -61.161 9.645 -36.267 1.00 40.67 O ANISOU 458 OD1 ASN A 102 5340 6641 3472 -70 308 -758 O ATOM 459 N GLU A 103 -59.781 6.501 -36.745 1.00 37.18 N ANISOU 459 N GLU A 103 4760 6199 3168 -33 358 -1144 N ATOM 460 CA GLU A 103 -58.336 6.277 -36.749 1.00 35.37 C ANISOU 460 CA GLU A 103 4496 5985 2959 -27 364 -1203 C ATOM 461 C GLU A 103 -57.553 7.561 -36.510 1.00 39.48 C ANISOU 461 C GLU A 103 5056 6526 3419 -40 351 -1070 C ATOM 462 O GLU A 103 -56.461 7.520 -35.926 1.00 43.26 O ANISOU 462 O GLU A 103 5550 6937 3949 -17 348 -1075 O ATOM 463 CB GLU A 103 -57.934 5.626 -38.087 1.00 43.95 C ANISOU 463 CB GLU A 103 5457 7253 3989 -61 389 -1357 C ATOM 464 CG GLU A 103 -56.466 5.754 -38.523 1.00 49.84 C ANISOU 464 CG GLU A 103 6143 8096 4699 -79 399 -1407 C ATOM 465 CD GLU A 103 -55.491 5.016 -37.608 1.00 54.32 C ANISOU 465 CD GLU A 103 6728 8509 5402 -28 394 -1470 C ATOM 466 OE1 GLU A 103 -55.947 4.335 -36.666 1.00 55.61 O ANISOU 466 OE1 GLU A 103 6946 8496 5688 18 382 -1477 O ATOM 467 OE2 GLU A 103 -54.263 5.132 -37.824 1.00 56.10 O1- ANISOU 467 OE2 GLU A 103 6912 8792 5611 -36 400 -1508 O1- ATOM 468 N ASP A 104 -58.097 8.708 -36.927 1.00 38.98 N ANISOU 468 N ASP A 104 5007 6548 3257 -76 341 -949 N ATOM 469 CA ASP A 104 -57.384 9.979 -36.892 1.00 38.06 C ANISOU 469 CA ASP A 104 4910 6470 3080 -98 327 -823 C ATOM 470 C ASP A 104 -58.017 11.002 -35.964 1.00 36.56 C ANISOU 470 C ASP A 104 4815 6160 2915 -82 301 -667 C ATOM 471 O ASP A 104 -57.469 12.097 -35.814 1.00 38.67 O ANISOU 471 O ASP A 104 5105 6437 3152 -96 286 -558 O ATOM 472 CB ASP A 104 -57.265 10.565 -38.313 1.00 38.30 C ANISOU 472 CB ASP A 104 4857 6727 2970 -164 334 -808 C ATOM 473 CG ASP A 104 -58.548 11.234 -38.798 1.00 38.17 C ANISOU 473 CG ASP A 104 4846 6773 2885 -194 318 -713 C ATOM 474 OD1 ASP A 104 -59.659 10.737 -38.523 1.00 39.72 O ANISOU 474 OD1 ASP A 104 5069 6896 3126 -172 316 -739 O ATOM 475 OD2 ASP A 104 -58.443 12.271 -39.479 1.00 42.39 O1- ANISOU 475 OD2 ASP A 104 5354 7431 3322 -243 305 -609 O1- ATOM 476 N GLY A 105 -59.142 10.685 -35.337 1.00 39.58 N ANISOU 476 N GLY A 105 5251 6432 3356 -55 294 -658 N ATOM 477 CA GLY A 105 -59.683 11.513 -34.279 1.00 38.72 C ANISOU 477 CA GLY A 105 5230 6191 3290 -33 272 -534 C ATOM 478 C GLY A 105 -60.611 12.610 -34.718 1.00 36.42 C ANISOU 478 C GLY A 105 4943 5959 2935 -65 253 -420 C ATOM 479 O GLY A 105 -60.907 13.506 -33.918 1.00 33.03 O ANISOU 479 O GLY A 105 4577 5435 2539 -52 232 -313 O ATOM 480 N THR A 106 -61.083 12.568 -35.952 1.00 36.68 N ANISOU 480 N THR A 106 4907 6146 2882 -106 257 -443 N ATOM 481 CA THR A 106 -61.999 13.562 -36.475 1.00 37.25 C ANISOU 481 CA THR A 106 4975 6284 2894 -139 233 -333 C ATOM 482 C THR A 106 -63.448 13.158 -36.282 1.00 38.55 C ANISOU 482 C THR A 106 5163 6392 3091 -123 231 -352 C ATOM 483 O THR A 106 -64.342 13.926 -36.655 1.00 40.79 O ANISOU 483 O THR A 106 5444 6717 3338 -145 208 -266 O ATOM 484 CB THR A 106 -61.721 13.803 -37.970 1.00 40.56 C ANISOU 484 CB THR A 106 5300 6922 3189 -199 236 -334 C ATOM 485 CG2 THR A 106 -60.511 14.730 -38.152 1.00 36.86 C ANISOU 485 CG2 THR A 106 4816 6510 2678 -226 227 -251 C ATOM 486 OG1 THR A 106 -61.481 12.546 -38.641 1.00 36.16 O ANISOU 486 OG1 THR A 106 4676 6456 2607 -204 268 -494 O ATOM 487 N GLN A 107 -63.708 11.978 -35.718 1.00 35.81 N ANISOU 487 N GLN A 107 4836 5951 2817 -87 251 -460 N ATOM 488 CA GLN A 107 -65.077 11.491 -35.597 1.00 36.70 C ANISOU 488 CA GLN A 107 4965 6019 2961 -76 253 -490 C ATOM 489 C GLN A 107 -65.214 10.645 -34.343 1.00 36.50 C ANISOU 489 C GLN A 107 5002 5818 3049 -28 265 -541 C ATOM 490 O GLN A 107 -64.395 9.752 -34.107 1.00 38.45 O ANISOU 490 O GLN A 107 5239 6030 3342 -9 281 -628 O ATOM 491 CB GLN A 107 -65.481 10.675 -36.834 1.00 42.01 C ANISOU 491 CB GLN A 107 5551 6837 3571 -104 270 -599 C ATOM 492 CG GLN A 107 -66.985 10.475 -36.987 1.00 42.08 C ANISOU 492 CG GLN A 107 5564 6840 3586 -105 266 -607 C ATOM 493 CD GLN A 107 -67.364 9.808 -38.310 1.00 55.47 C ANISOU 493 CD GLN A 107 7166 8704 5207 -138 280 -710 C ATOM 494 NE2 GLN A 107 -66.926 10.393 -39.433 1.00 51.09 N ANISOU 494 NE2 GLN A 107 6544 8332 4537 -185 273 -679 N ATOM 495 OE1 GLN A 107 -68.053 8.783 -38.318 1.00 63.05 O ANISOU 495 OE1 GLN A 107 8111 9633 6212 -124 298 -816 O ATOM 496 N LEU A 108 -66.247 10.926 -33.555 1.00 31.88 N ANISOU 496 N LEU A 108 4476 5127 2510 -11 254 -485 N ATOM 497 CA LEU A 108 -66.508 10.249 -32.295 1.00 33.90 C ANISOU 497 CA LEU A 108 4794 5221 2864 28 262 -511 C ATOM 498 C LEU A 108 -67.917 9.690 -32.344 1.00 32.13 C ANISOU 498 C LEU A 108 4571 4974 2663 28 269 -550 C ATOM 499 O LEU A 108 -68.868 10.428 -32.612 1.00 33.89 O ANISOU 499 O LEU A 108 4797 5230 2851 12 255 -490 O ATOM 500 CB LEU A 108 -66.345 11.215 -31.109 1.00 35.15 C ANISOU 500 CB LEU A 108 5027 5270 3059 45 244 -403 C ATOM 501 CG LEU A 108 -66.830 10.816 -29.703 1.00 36.17 C ANISOU 501 CG LEU A 108 5226 5243 3274 77 248 -398 C ATOM 502 CD1 LEU A 108 -65.938 9.749 -29.024 1.00 38.21 C ANISOU 502 CD1 LEU A 108 5499 5423 3598 103 260 -462 C ATOM 503 CD2 LEU A 108 -66.946 12.045 -28.803 1.00 34.66 C ANISOU 503 CD2 LEU A 108 5089 4986 3095 83 228 -291 C ATOM 504 N ASP A 109 -68.055 8.392 -32.125 1.00 31.39 N ANISOU 504 N ASP A 109 4470 4825 2632 45 289 -651 N ATOM 505 CA ASP A 109 -69.357 7.742 -32.195 1.00 32.91 C ANISOU 505 CA ASP A 109 4657 4994 2853 44 299 -700 C ATOM 506 C ASP A 109 -69.760 7.305 -30.798 1.00 36.73 C ANISOU 506 C ASP A 109 5212 5313 3431 72 302 -683 C ATOM 507 O ASP A 109 -68.973 6.671 -30.087 1.00 33.19 O ANISOU 507 O ASP A 109 4784 4781 3047 93 307 -706 O ATOM 508 CB ASP A 109 -69.360 6.526 -33.131 1.00 33.09 C ANISOU 508 CB ASP A 109 4603 5089 2881 36 319 -839 C ATOM 509 CG ASP A 109 -68.931 6.863 -34.538 1.00 40.36 C ANISOU 509 CG ASP A 109 5444 6194 3698 3 319 -869 C ATOM 510 OD1 ASP A 109 -68.988 8.055 -34.920 1.00 38.40 O ANISOU 510 OD1 ASP A 109 5198 6024 3369 -19 300 -770 O ATOM 511 OD2 ASP A 109 -68.515 5.924 -35.265 1.00 45.23 O1- ANISOU 511 OD2 ASP A 109 5989 6879 4318 -3 336 -992 O1- ATOM 512 N ILE A 110 -70.986 7.631 -30.419 1.00 35.07 N ANISOU 512 N ILE A 110 5034 5063 3228 69 299 -642 N ATOM 513 CA ILE A 110 -71.475 7.346 -29.082 1.00 40.15 C ANISOU 513 CA ILE A 110 5742 5565 3946 88 303 -615 C ATOM 514 C ILE A 110 -72.846 6.713 -29.177 1.00 40.35 C ANISOU 514 C ILE A 110 5759 5572 4000 81 316 -663 C ATOM 515 O ILE A 110 -73.726 7.237 -29.863 1.00 37.37 O ANISOU 515 O ILE A 110 5358 5267 3573 64 311 -653 O ATOM 516 CB ILE A 110 -71.564 8.608 -28.209 1.00 41.35 C ANISOU 516 CB ILE A 110 5953 5671 4086 91 286 -504 C ATOM 517 CG1 ILE A 110 -70.202 9.296 -28.114 1.00 39.37 C ANISOU 517 CG1 ILE A 110 5709 5438 3810 97 273 -455 C ATOM 518 CG2 ILE A 110 -72.102 8.218 -26.853 1.00 35.98 C ANISOU 518 CG2 ILE A 110 5332 4865 3474 104 294 -487 C ATOM 519 CD1 ILE A 110 -70.322 10.769 -27.794 1.00 39.40 C ANISOU 519 CD1 ILE A 110 5741 5444 3786 92 251 -354 C ATOM 520 N THR A 111 -73.041 5.612 -28.465 1.00 45.40 N ANISOU 520 N THR A 111 6416 6112 4722 93 331 -707 N ATOM 521 CA THR A 111 -74.367 5.085 -28.215 1.00 42.43 C ANISOU 521 CA THR A 111 6047 5689 4385 86 343 -734 C ATOM 522 C THR A 111 -74.829 5.506 -26.834 1.00 40.37 C ANISOU 522 C THR A 111 5859 5326 4154 91 341 -653 C ATOM 523 O THR A 111 -74.036 5.629 -25.901 1.00 42.14 O ANISOU 523 O THR A 111 6125 5486 4400 103 335 -604 O ATOM 524 CB THR A 111 -74.397 3.567 -28.326 1.00 46.49 C ANISOU 524 CB THR A 111 6527 6158 4981 91 360 -834 C ATOM 525 CG2 THR A 111 -75.803 3.003 -28.082 1.00 46.69 C ANISOU 525 CG2 THR A 111 6556 6134 5050 81 375 -861 C ATOM 526 OG1 THR A 111 -73.829 3.145 -29.568 1.00 48.84 O ANISOU 526 OG1 THR A 111 6749 6554 5254 87 363 -924 O ATOM 527 N LEU A 112 -76.123 5.754 -26.744 1.00 39.69 N ANISOU 527 N LEU A 112 5781 5237 4063 79 346 -644 N ATOM 528 CA LEU A 112 -76.806 6.262 -25.576 1.00 36.54 C ANISOU 528 CA LEU A 112 5439 4765 3680 77 347 -580 C ATOM 529 C LEU A 112 -77.546 5.129 -24.865 1.00 36.74 C ANISOU 529 C LEU A 112 5479 4705 3777 71 368 -614 C ATOM 530 O LEU A 112 -77.844 4.072 -25.441 1.00 32.18 O ANISOU 530 O LEU A 112 4861 4128 3237 68 381 -691 O ATOM 531 CB LEU A 112 -77.788 7.358 -26.005 1.00 31.60 C ANISOU 531 CB LEU A 112 4804 4197 3006 66 336 -550 C ATOM 532 CG LEU A 112 -77.211 8.435 -26.924 1.00 29.34 C ANISOU 532 CG LEU A 112 4489 4006 2651 65 311 -513 C ATOM 533 CD1 LEU A 112 -78.245 9.502 -27.126 1.00 29.25 C ANISOU 533 CD1 LEU A 112 4473 4026 2614 55 295 -471 C ATOM 534 CD2 LEU A 112 -75.884 9.038 -26.432 1.00 29.08 C ANISOU 534 CD2 LEU A 112 4484 3957 2608 77 298 -455 C ATOM 535 N ARG A 113 -77.844 5.365 -23.598 1.00 36.60 N ANISOU 535 N ARG A 113 5513 4615 3779 68 371 -558 N ATOM 536 CA ARG A 113 -78.598 4.404 -22.813 1.00 35.42 C ANISOU 536 CA ARG A 113 5381 4388 3691 55 390 -572 C ATOM 537 C ARG A 113 -80.051 4.444 -23.257 1.00 36.30 C ANISOU 537 C ARG A 113 5471 4526 3797 39 403 -609 C ATOM 538 O ARG A 113 -80.683 5.505 -23.249 1.00 33.75 O ANISOU 538 O ARG A 113 5155 4238 3431 35 397 -580 O ATOM 539 CB ARG A 113 -78.469 4.682 -21.319 1.00 31.45 C ANISOU 539 CB ARG A 113 4934 3819 3195 50 391 -498 C ATOM 540 CG ARG A 113 -78.985 3.541 -20.480 1.00 30.43 C ANISOU 540 CG ARG A 113 4820 3610 3132 33 408 -500 C ATOM 541 CD ARG A 113 -78.786 3.773 -19.007 1.00 32.09 C ANISOU 541 CD ARG A 113 5081 3773 3338 23 407 -425 C ATOM 542 NE ARG A 113 -77.382 3.876 -18.618 1.00 30.13 N ANISOU 542 NE ARG A 113 4852 3510 3087 41 388 -384 N ATOM 543 CZ ARG A 113 -76.545 2.850 -18.562 1.00 29.85 C ANISOU 543 CZ ARG A 113 4810 3425 3109 49 379 -388 C ATOM 544 NH1 ARG A 113 -76.937 1.626 -18.873 1.00 38.57 N1+ ANISOU 544 NH1 ARG A 113 5886 4485 4285 42 388 -433 N1+ ATOM 545 NH2 ARG A 113 -75.276 3.061 -18.219 1.00 29.51 N ANISOU 545 NH2 ARG A 113 4781 3373 3057 67 360 -351 N ATOM 546 N ASP A 114 -80.551 3.286 -23.685 1.00 43.09 N ANISOU 546 N ASP A 114 6297 5368 4708 32 418 -679 N ATOM 547 CA ASP A 114 -81.947 3.098 -24.042 1.00 44.33 C ANISOU 547 CA ASP A 114 6431 5540 4873 16 433 -724 C ATOM 548 C ASP A 114 -82.798 2.947 -22.787 1.00 43.14 C ANISOU 548 C ASP A 114 6321 5315 4755 -3 450 -687 C ATOM 549 O ASP A 114 -82.382 2.323 -21.806 1.00 44.00 O ANISOU 549 O ASP A 114 6461 5350 4909 -9 455 -653 O ATOM 550 CB ASP A 114 -82.081 1.853 -24.920 1.00 46.96 C ANISOU 550 CB ASP A 114 6708 5877 5258 15 444 -819 C ATOM 551 CG ASP A 114 -83.461 1.683 -25.473 1.00 49.00 C ANISOU 551 CG ASP A 114 6934 6165 5519 0 458 -876 C ATOM 552 OD1 ASP A 114 -84.148 2.715 -25.592 1.00 52.89 O ANISOU 552 OD1 ASP A 114 7435 6707 5955 -4 451 -847 O ATOM 553 OD2 ASP A 114 -83.861 0.535 -25.774 1.00 47.67 O1- ANISOU 553 OD2 ASP A 114 6728 5967 5416 -7 473 -950 O1- ATOM 554 N GLY A 115 -84.000 3.516 -22.826 1.00 41.25 N ANISOU 554 N GLY A 115 6079 5102 4493 -16 457 -693 N ATOM 555 CA GLY A 115 -84.948 3.386 -21.740 1.00 34.67 C ANISOU 555 CA GLY A 115 5274 4215 3684 -39 476 -672 C ATOM 556 C GLY A 115 -84.943 4.515 -20.731 1.00 30.85 C ANISOU 556 C GLY A 115 4833 3730 3161 -43 471 -604 C ATOM 557 O GLY A 115 -85.851 4.575 -19.892 1.00 33.21 O ANISOU 557 O GLY A 115 5146 4004 3467 -66 488 -595 O ATOM 558 N VAL A 116 -83.971 5.422 -20.791 1.00 29.27 N ANISOU 558 N VAL A 116 4644 3558 2919 -24 448 -562 N ATOM 559 CA VAL A 116 -83.882 6.464 -19.785 1.00 28.97 C ANISOU 559 CA VAL A 116 4639 3514 2852 -27 442 -506 C ATOM 560 C VAL A 116 -85.015 7.476 -19.932 1.00 30.02 C ANISOU 560 C VAL A 116 4757 3682 2968 -33 439 -520 C ATOM 561 O VAL A 116 -85.449 7.816 -21.039 1.00 35.80 O ANISOU 561 O VAL A 116 5452 4461 3688 -24 425 -549 O ATOM 562 CB VAL A 116 -82.506 7.145 -19.857 1.00 29.82 C ANISOU 562 CB VAL A 116 4760 3639 2930 -4 417 -463 C ATOM 563 CG1 VAL A 116 -82.380 8.251 -18.766 1.00 28.44 C ANISOU 563 CG1 VAL A 116 4615 3459 2733 -7 411 -413 C ATOM 564 CG2 VAL A 116 -81.422 6.085 -19.719 1.00 30.60 C ANISOU 564 CG2 VAL A 116 4869 3700 3056 3 419 -456 C ATOM 565 N THR A 117 -85.484 7.992 -18.790 1.00 36.47 N ANISOU 565 N THR A 117 5595 4479 3783 -49 449 -499 N ATOM 566 CA THR A 117 -86.538 8.994 -18.766 1.00 33.96 C ANISOU 566 CA THR A 117 5258 4185 3461 -54 444 -516 C ATOM 567 C THR A 117 -86.049 10.229 -18.023 1.00 31.38 C ANISOU 567 C THR A 117 4945 3861 3117 -47 427 -477 C ATOM 568 O THR A 117 -85.189 10.141 -17.147 1.00 31.24 O ANISOU 568 O THR A 117 4958 3823 3088 -49 432 -441 O ATOM 569 CB THR A 117 -87.829 8.427 -18.117 1.00 35.02 C ANISOU 569 CB THR A 117 5390 4298 3617 -86 476 -552 C ATOM 570 CG2 THR A 117 -87.793 8.553 -16.635 1.00 30.94 C ANISOU 570 CG2 THR A 117 4903 3759 3092 -109 495 -525 C ATOM 571 OG1 THR A 117 -88.971 9.137 -18.616 1.00 37.41 O ANISOU 571 OG1 THR A 117 5659 4629 3928 -86 469 -590 O ATOM 572 N TRP A 118 -86.554 11.391 -18.433 1.00 35.45 N ANISOU 572 N TRP A 118 5431 4401 3636 -37 405 -484 N ATOM 573 CA TRP A 118 -86.439 12.596 -17.618 1.00 37.28 C ANISOU 573 CA TRP A 118 5663 4628 3872 -35 392 -466 C ATOM 574 C TRP A 118 -87.454 12.548 -16.482 1.00 34.85 C ANISOU 574 C TRP A 118 5357 4308 3576 -64 421 -502 C ATOM 575 O TRP A 118 -88.459 11.832 -16.539 1.00 34.97 O ANISOU 575 O TRP A 118 5364 4321 3602 -83 445 -540 O ATOM 576 CB TRP A 118 -86.687 13.874 -18.434 1.00 37.14 C ANISOU 576 CB TRP A 118 5607 4633 3873 -16 352 -459 C ATOM 577 CG TRP A 118 -85.803 14.030 -19.614 1.00 35.01 C ANISOU 577 CG TRP A 118 5326 4391 3583 5 322 -421 C ATOM 578 CD1 TRP A 118 -86.094 13.685 -20.891 1.00 34.93 C ANISOU 578 CD1 TRP A 118 5290 4419 3562 9 311 -430 C ATOM 579 CD2 TRP A 118 -84.487 14.591 -19.631 1.00 32.12 C ANISOU 579 CD2 TRP A 118 4973 4029 3204 21 301 -370 C ATOM 580 CE2 TRP A 118 -84.033 14.540 -20.962 1.00 34.65 C ANISOU 580 CE2 TRP A 118 5272 4392 3502 32 278 -348 C ATOM 581 CE3 TRP A 118 -83.642 15.117 -18.647 1.00 32.83 C ANISOU 581 CE3 TRP A 118 5084 4094 3295 26 299 -344 C ATOM 582 NE1 TRP A 118 -85.036 13.985 -21.714 1.00 36.99 N ANISOU 582 NE1 TRP A 118 5544 4713 3797 24 285 -387 N ATOM 583 CZ2 TRP A 118 -82.769 14.998 -21.344 1.00 33.47 C ANISOU 583 CZ2 TRP A 118 5125 4260 3333 46 256 -299 C ATOM 584 CZ3 TRP A 118 -82.386 15.574 -19.026 1.00 32.33 C ANISOU 584 CZ3 TRP A 118 5025 4042 3218 43 276 -296 C ATOM 585 CH2 TRP A 118 -81.965 15.517 -20.369 1.00 31.91 C ANISOU 585 CH2 TRP A 118 4952 4030 3144 52 254 -273 C ATOM 586 N THR A 119 -87.189 13.344 -15.449 1.00 30.61 N ANISOU 586 N THR A 119 4824 3768 3037 -68 420 -495 N ATOM 587 CA THR A 119 -87.999 13.276 -14.242 1.00 30.17 C ANISOU 587 CA THR A 119 4767 3715 2981 -101 452 -530 C ATOM 588 C THR A 119 -89.471 13.623 -14.498 1.00 32.69 C ANISOU 588 C THR A 119 5046 4042 3334 -111 456 -590 C ATOM 589 O THR A 119 -90.344 13.147 -13.761 1.00 30.88 O ANISOU 589 O THR A 119 4813 3818 3100 -144 491 -627 O ATOM 590 CB THR A 119 -87.337 14.149 -13.178 1.00 30.46 C ANISOU 590 CB THR A 119 4807 3759 3007 -102 446 -520 C ATOM 591 CG2 THR A 119 -88.322 14.630 -12.125 1.00 37.83 C ANISOU 591 CG2 THR A 119 5715 4712 3949 -131 468 -577 C ATOM 592 OG1 THR A 119 -86.275 13.395 -12.565 1.00 32.87 O ANISOU 592 OG1 THR A 119 5156 4061 3274 -109 458 -472 O ATOM 593 N ASP A 120 -89.785 14.374 -15.553 1.00 28.91 N ANISOU 593 N ASP A 120 4532 3565 2887 -86 421 -598 N ATOM 594 CA ASP A 120 -91.180 14.578 -15.918 1.00 30.61 C ANISOU 594 CA ASP A 120 4707 3785 3137 -93 422 -652 C ATOM 595 C ASP A 120 -91.724 13.477 -16.826 1.00 33.91 C ANISOU 595 C ASP A 120 5127 4209 3548 -98 434 -665 C ATOM 596 O ASP A 120 -92.801 13.632 -17.411 1.00 34.02 O ANISOU 596 O ASP A 120 5106 4232 3590 -98 427 -704 O ATOM 597 CB ASP A 120 -91.370 15.952 -16.555 1.00 33.61 C ANISOU 597 CB ASP A 120 5042 4164 3565 -67 373 -651 C ATOM 598 CG ASP A 120 -90.624 16.119 -17.875 1.00 32.16 C ANISOU 598 CG ASP A 120 4856 3991 3373 -38 333 -594 C ATOM 599 OD1 ASP A 120 -89.994 15.170 -18.400 1.00 30.31 O ANISOU 599 OD1 ASP A 120 4651 3768 3097 -36 344 -567 O ATOM 600 OD2 ASP A 120 -90.617 17.268 -18.344 1.00 31.42 O1- ANISOU 600 OD2 ASP A 120 4726 3893 3318 -19 289 -575 O1- ATOM 601 N GLY A 121 -91.017 12.368 -16.946 1.00 31.75 N ANISOU 601 N GLY A 121 4890 3930 3244 -101 452 -637 N ATOM 602 CA GLY A 121 -91.551 11.215 -17.618 1.00 35.22 C ANISOU 602 CA GLY A 121 5326 4370 3686 -111 470 -662 C ATOM 603 C GLY A 121 -91.234 11.126 -19.097 1.00 37.24 C ANISOU 603 C GLY A 121 5563 4649 3936 -84 441 -653 C ATOM 604 O GLY A 121 -91.578 10.114 -19.713 1.00 34.71 O ANISOU 604 O GLY A 121 5236 4334 3619 -91 455 -681 O ATOM 605 N GLU A 122 -90.572 12.140 -19.667 1.00 33.91 N ANISOU 605 N GLU A 122 5130 4247 3508 -59 400 -615 N ATOM 606 CA GLU A 122 -90.257 12.172 -21.085 1.00 33.54 C ANISOU 606 CA GLU A 122 5059 4241 3446 -39 370 -601 C ATOM 607 C GLU A 122 -88.954 11.433 -21.388 1.00 38.63 C ANISOU 607 C GLU A 122 5729 4891 4059 -31 374 -573 C ATOM 608 O GLU A 122 -87.987 11.474 -20.614 1.00 35.37 O ANISOU 608 O GLU A 122 5350 4452 3638 -28 380 -538 O ATOM 609 CB GLU A 122 -90.160 13.614 -21.586 1.00 31.62 C ANISOU 609 CB GLU A 122 4785 4017 3212 -21 321 -563 C ATOM 610 CG GLU A 122 -91.432 14.435 -21.403 1.00 33.46 C ANISOU 610 CG GLU A 122 4981 4241 3490 -25 308 -594 C ATOM 611 CD GLU A 122 -92.634 13.727 -21.970 1.00 39.19 C ANISOU 611 CD GLU A 122 5682 4986 4222 -36 321 -650 C ATOM 612 OE1 GLU A 122 -92.570 13.332 -23.149 1.00 40.12 O ANISOU 612 OE1 GLU A 122 5781 5149 4314 -30 307 -646 O ATOM 613 OE2 GLU A 122 -93.634 13.548 -21.242 1.00 41.69 O1- ANISOU 613 OE2 GLU A 122 5995 5279 4566 -53 348 -701 O1- ATOM 614 N ALA A 123 -88.934 10.781 -22.554 1.00 38.27 N ANISOU 614 N ALA A 123 5659 4883 3997 -26 370 -594 N ATOM 615 CA ALA A 123 -87.785 9.999 -22.984 1.00 38.68 C ANISOU 615 CA ALA A 123 5722 4946 4027 -18 374 -585 C ATOM 616 C ALA A 123 -86.548 10.863 -23.164 1.00 40.51 C ANISOU 616 C ALA A 123 5963 5199 4232 -1 345 -524 C ATOM 617 O ALA A 123 -86.584 11.908 -23.827 1.00 38.04 O ANISOU 617 O ALA A 123 5622 4926 3905 8 310 -493 O ATOM 618 CB ALA A 123 -88.093 9.274 -24.296 1.00 33.99 C ANISOU 618 CB ALA A 123 5088 4406 3421 -18 373 -634 C ATOM 619 N PHE A 124 -85.442 10.398 -22.585 1.00 35.35 N ANISOU 619 N PHE A 124 5343 4515 3575 3 357 -504 N ATOM 620 CA PHE A 124 -84.122 10.849 -22.988 1.00 33.05 C ANISOU 620 CA PHE A 124 5054 4250 3255 19 334 -459 C ATOM 621 C PHE A 124 -83.682 10.105 -24.250 1.00 36.31 C ANISOU 621 C PHE A 124 5435 4719 3642 23 332 -490 C ATOM 622 O PHE A 124 -83.717 8.869 -24.286 1.00 38.33 O ANISOU 622 O PHE A 124 5690 4956 3916 18 357 -539 O ATOM 623 CB PHE A 124 -83.129 10.582 -21.872 1.00 29.05 C ANISOU 623 CB PHE A 124 4592 3690 2755 23 347 -432 C ATOM 624 CG PHE A 124 -81.726 10.585 -22.330 1.00 28.32 C ANISOU 624 CG PHE A 124 4501 3620 2639 38 332 -405 C ATOM 625 CD1 PHE A 124 -81.072 11.779 -22.562 1.00 28.18 C ANISOU 625 CD1 PHE A 124 4477 3631 2600 49 303 -354 C ATOM 626 CD2 PHE A 124 -81.058 9.408 -22.545 1.00 28.46 C ANISOU 626 CD2 PHE A 124 4521 3629 2662 40 347 -432 C ATOM 627 CE1 PHE A 124 -79.768 11.794 -22.991 1.00 28.15 C ANISOU 627 CE1 PHE A 124 4472 3652 2573 60 291 -331 C ATOM 628 CE2 PHE A 124 -79.754 9.424 -22.987 1.00 29.03 C ANISOU 628 CE2 PHE A 124 4588 3726 2714 54 334 -415 C ATOM 629 CZ PHE A 124 -79.110 10.624 -23.203 1.00 28.27 C ANISOU 629 CZ PHE A 124 4490 3665 2588 63 308 -364 C ATOM 630 N ASP A 125 -83.246 10.836 -25.277 1.00 29.66 N ANISOU 630 N ASP A 125 4560 3947 2761 29 302 -462 N ATOM 631 CA ASP A 125 -82.672 10.173 -26.450 1.00 32.51 C ANISOU 631 CA ASP A 125 4886 4378 3088 29 301 -495 C ATOM 632 C ASP A 125 -81.720 11.119 -27.168 1.00 34.80 C ANISOU 632 C ASP A 125 5157 4735 3331 34 269 -437 C ATOM 633 O ASP A 125 -81.378 12.198 -26.669 1.00 36.95 O ANISOU 633 O ASP A 125 5448 4983 3607 39 248 -371 O ATOM 634 CB ASP A 125 -83.750 9.680 -27.418 1.00 30.09 C ANISOU 634 CB ASP A 125 4533 4127 2773 18 305 -555 C ATOM 635 CG ASP A 125 -84.668 10.778 -27.859 1.00 31.93 C ANISOU 635 CG ASP A 125 4740 4400 2991 13 274 -520 C ATOM 636 OD1 ASP A 125 -84.178 11.896 -28.124 1.00 34.86 O ANISOU 636 OD1 ASP A 125 5104 4804 3338 17 241 -450 O ATOM 637 OD2 ASP A 125 -85.884 10.525 -27.952 1.00 29.81 O1- ANISOU 637 OD2 ASP A 125 4456 4130 2742 6 282 -562 O1- ATOM 638 N ALA A 126 -81.329 10.709 -28.375 1.00 34.86 N ANISOU 638 N ALA A 126 5120 4832 3295 28 265 -467 N ATOM 639 CA ALA A 126 -80.340 11.438 -29.165 1.00 36.93 C ANISOU 639 CA ALA A 126 5356 5173 3502 25 239 -416 C ATOM 640 C ALA A 126 -80.763 12.875 -29.459 1.00 38.15 C ANISOU 640 C ALA A 126 5495 5359 3642 19 198 -334 C ATOM 641 O ALA A 126 -79.900 13.743 -29.636 1.00 38.95 O ANISOU 641 O ALA A 126 5593 5486 3721 19 174 -265 O ATOM 642 CB ALA A 126 -80.079 10.686 -30.468 1.00 33.66 C ANISOU 642 CB ALA A 126 4884 4867 3037 13 245 -477 C ATOM 643 N ASP A 127 -82.072 13.142 -29.547 1.00 33.37 N ANISOU 643 N ASP A 127 4875 4749 3054 14 188 -339 N ATOM 644 CA ASP A 127 -82.529 14.513 -29.741 1.00 29.98 C ANISOU 644 CA ASP A 127 4427 4332 2631 10 145 -260 C ATOM 645 C ASP A 127 -81.990 15.410 -28.643 1.00 36.44 C ANISOU 645 C ASP A 127 5286 5065 3496 23 135 -202 C ATOM 646 O ASP A 127 -81.613 16.565 -28.894 1.00 38.32 O ANISOU 646 O ASP A 127 5506 5318 3734 21 96 -122 O ATOM 647 CB ASP A 127 -84.053 14.579 -29.747 1.00 30.88 C ANISOU 647 CB ASP A 127 4525 4432 2777 7 139 -287 C ATOM 648 CG ASP A 127 -84.668 13.902 -30.951 1.00 30.77 C ANISOU 648 CG ASP A 127 4460 4516 2714 -7 139 -337 C ATOM 649 OD1 ASP A 127 -83.904 13.422 -31.792 1.00 30.84 O ANISOU 649 OD1 ASP A 127 4443 4610 2663 -16 144 -353 O ATOM 650 OD2 ASP A 127 -85.920 13.844 -31.045 1.00 32.10 O1- ANISOU 650 OD2 ASP A 127 4611 4680 2904 -10 136 -367 O1- ATOM 651 N ASP A 128 -81.954 14.893 -27.414 1.00 33.61 N ANISOU 651 N ASP A 128 4977 4617 3179 34 168 -240 N ATOM 652 CA ASP A 128 -81.493 15.692 -26.291 1.00 33.57 C ANISOU 652 CA ASP A 128 5005 4535 3214 45 162 -198 C ATOM 653 C ASP A 128 -80.000 15.952 -26.405 1.00 31.86 C ANISOU 653 C ASP A 128 4797 4338 2971 50 154 -154 C ATOM 654 O ASP A 128 -79.529 17.065 -26.134 1.00 29.75 O ANISOU 654 O ASP A 128 4529 4050 2724 55 127 -92 O ATOM 655 CB ASP A 128 -81.855 14.990 -24.982 1.00 29.90 C ANISOU 655 CB ASP A 128 4586 3989 2787 50 200 -250 C ATOM 656 CG ASP A 128 -83.379 14.902 -24.779 1.00 34.01 C ANISOU 656 CG ASP A 128 5096 4489 3339 42 207 -291 C ATOM 657 OD1 ASP A 128 -84.052 15.961 -24.692 1.00 32.61 O ANISOU 657 OD1 ASP A 128 4898 4299 3195 43 180 -266 O ATOM 658 OD2 ASP A 128 -83.909 13.773 -24.702 1.00 36.83 O1- ANISOU 658 OD2 ASP A 128 5461 4838 3695 35 240 -351 O1- ATOM 659 N VAL A 129 -79.252 14.945 -26.851 1.00 31.29 N ANISOU 659 N VAL A 129 4726 4305 2858 49 175 -189 N ATOM 660 CA VAL A 129 -77.811 15.083 -26.987 1.00 32.03 C ANISOU 660 CA VAL A 129 4825 4421 2925 53 171 -157 C ATOM 661 C VAL A 129 -77.465 16.066 -28.106 1.00 36.36 C ANISOU 661 C VAL A 129 5326 5055 3434 40 133 -89 C ATOM 662 O VAL A 129 -76.591 16.930 -27.936 1.00 35.88 O ANISOU 662 O VAL A 129 5270 4986 3379 42 113 -27 O ATOM 663 CB VAL A 129 -77.190 13.693 -27.209 1.00 29.06 C ANISOU 663 CB VAL A 129 4452 4063 2527 55 203 -225 C ATOM 664 CG1 VAL A 129 -75.705 13.794 -27.459 1.00 28.88 C ANISOU 664 CG1 VAL A 129 4426 4072 2475 59 198 -202 C ATOM 665 CG2 VAL A 129 -77.489 12.805 -26.006 1.00 28.59 C ANISOU 665 CG2 VAL A 129 4438 3909 2515 65 234 -271 C ATOM 666 N VAL A 130 -78.157 15.971 -29.252 1.00 29.66 N ANISOU 666 N VAL A 130 4430 4292 2546 23 120 -96 N ATOM 667 CA VAL A 130 -77.947 16.943 -30.323 1.00 35.23 C ANISOU 667 CA VAL A 130 5087 5087 3212 4 79 -17 C ATOM 668 C VAL A 130 -78.257 18.355 -29.835 1.00 35.61 C ANISOU 668 C VAL A 130 5137 5074 3320 8 39 67 C ATOM 669 O VAL A 130 -77.496 19.301 -30.091 1.00 34.61 O ANISOU 669 O VAL A 130 4994 4966 3190 1 9 148 O ATOM 670 CB VAL A 130 -78.785 16.575 -31.562 1.00 35.60 C ANISOU 670 CB VAL A 130 5080 5240 3205 -16 70 -40 C ATOM 671 CG1 VAL A 130 -78.842 17.735 -32.523 1.00 31.03 C ANISOU 671 CG1 VAL A 130 4451 4744 2597 -39 18 61 C ATOM 672 CG2 VAL A 130 -78.219 15.351 -32.256 1.00 30.74 C ANISOU 672 CG2 VAL A 130 4444 4707 2528 -25 103 -120 C ATOM 673 N PHE A 131 -79.355 18.515 -29.094 1.00 33.11 N ANISOU 673 N PHE A 131 4836 4679 3064 19 39 45 N ATOM 674 CA PHE A 131 -79.714 19.844 -28.615 1.00 33.49 C ANISOU 674 CA PHE A 131 4876 4664 3183 25 1 109 C ATOM 675 C PHE A 131 -78.684 20.385 -27.632 1.00 33.78 C ANISOU 675 C PHE A 131 4946 4630 3259 38 4 134 C ATOM 676 O PHE A 131 -78.486 21.600 -27.545 1.00 37.00 O ANISOU 676 O PHE A 131 5333 5009 3715 38 -35 204 O ATOM 677 CB PHE A 131 -81.095 19.822 -27.971 1.00 31.62 C ANISOU 677 CB PHE A 131 4646 4364 3006 33 6 61 C ATOM 678 CG PHE A 131 -81.500 21.130 -27.368 1.00 32.38 C ANISOU 678 CG PHE A 131 4728 4385 3190 41 -31 106 C ATOM 679 CD1 PHE A 131 -82.159 22.084 -28.129 1.00 31.96 C ANISOU 679 CD1 PHE A 131 4621 4354 3169 32 -85 171 C ATOM 680 CD2 PHE A 131 -81.227 21.408 -26.035 1.00 36.08 C ANISOU 680 CD2 PHE A 131 5231 4763 3713 56 -14 81 C ATOM 681 CE1 PHE A 131 -82.527 23.295 -27.580 1.00 34.81 C ANISOU 681 CE1 PHE A 131 4960 4637 3628 41 -123 206 C ATOM 682 CE2 PHE A 131 -81.596 22.623 -25.471 1.00 36.67 C ANISOU 682 CE2 PHE A 131 5284 4771 3879 63 -48 108 C ATOM 683 CZ PHE A 131 -82.255 23.563 -26.237 1.00 35.07 C ANISOU 683 CZ PHE A 131 5025 4580 3721 57 -103 167 C ATOM 684 N THR A 132 -78.024 19.520 -26.872 1.00 29.71 N ANISOU 684 N THR A 132 4476 4082 2729 50 46 79 N ATOM 685 CA THR A 132 -77.084 20.052 -25.901 1.00 33.73 C ANISOU 685 CA THR A 132 5014 4529 3273 63 47 100 C ATOM 686 C THR A 132 -75.870 20.629 -26.615 1.00 33.98 C ANISOU 686 C THR A 132 5024 4613 3275 54 24 170 C ATOM 687 O THR A 132 -75.466 21.771 -26.369 1.00 35.28 O ANISOU 687 O THR A 132 5176 4744 3486 56 -7 231 O ATOM 688 CB THR A 132 -76.673 18.974 -24.891 1.00 32.96 C ANISOU 688 CB THR A 132 4969 4386 3167 75 94 32 C ATOM 689 CG2 THR A 132 -75.704 19.551 -23.862 1.00 28.09 C ANISOU 689 CG2 THR A 132 4379 3711 2582 88 92 53 C ATOM 690 OG1 THR A 132 -77.835 18.479 -24.206 1.00 34.04 O ANISOU 690 OG1 THR A 132 5124 4478 3332 77 115 -25 O ATOM 691 N PHE A 133 -75.304 19.865 -27.533 1.00 35.16 N ANISOU 691 N PHE A 133 5162 4848 3351 42 37 158 N ATOM 692 CA PHE A 133 -74.071 20.291 -28.173 1.00 36.01 C ANISOU 692 CA PHE A 133 5248 5014 3420 31 22 216 C ATOM 693 C PHE A 133 -74.317 21.436 -29.139 1.00 36.60 C ANISOU 693 C PHE A 133 5268 5143 3494 8 -28 312 C ATOM 694 O PHE A 133 -73.472 22.329 -29.268 1.00 34.29 O ANISOU 694 O PHE A 133 4960 4856 3214 0 -54 386 O ATOM 695 CB PHE A 133 -73.438 19.104 -28.885 1.00 35.81 C ANISOU 695 CB PHE A 133 5216 5072 3316 23 52 162 C ATOM 696 CG PHE A 133 -72.665 18.198 -27.962 1.00 33.51 C ANISOU 696 CG PHE A 133 4973 4723 3035 44 90 97 C ATOM 697 CD1 PHE A 133 -71.400 18.545 -27.531 1.00 28.86 C ANISOU 697 CD1 PHE A 133 4400 4113 2453 52 89 124 C ATOM 698 CD2 PHE A 133 -73.217 17.013 -27.521 1.00 28.82 C ANISOU 698 CD2 PHE A 133 4405 4096 2449 55 123 15 C ATOM 699 CE1 PHE A 133 -70.691 17.720 -26.706 1.00 28.53 C ANISOU 699 CE1 PHE A 133 4398 4021 2422 71 118 71 C ATOM 700 CE2 PHE A 133 -72.512 16.192 -26.694 1.00 28.53 C ANISOU 700 CE2 PHE A 133 4407 4005 2427 73 151 -32 C ATOM 701 CZ PHE A 133 -71.241 16.547 -26.284 1.00 28.38 C ANISOU 701 CZ PHE A 133 4404 3969 2412 81 147 -3 C ATOM 702 N GLU A 134 -75.476 21.437 -29.804 1.00 36.89 N ANISOU 702 N GLU A 134 5274 5220 3524 -4 -46 316 N ATOM 703 CA GLU A 134 -75.822 22.541 -30.685 1.00 37.42 C ANISOU 703 CA GLU A 134 5285 5334 3598 -27 -101 418 C ATOM 704 C GLU A 134 -76.076 23.815 -29.901 1.00 37.80 C ANISOU 704 C GLU A 134 5331 5273 3756 -14 -138 474 C ATOM 705 O GLU A 134 -75.788 24.912 -30.393 1.00 40.99 O ANISOU 705 O GLU A 134 5696 5691 4188 -30 -185 577 O ATOM 706 CB GLU A 134 -77.033 22.164 -31.527 1.00 38.36 C ANISOU 706 CB GLU A 134 5371 5520 3683 -40 -111 402 C ATOM 707 CG GLU A 134 -76.712 21.069 -32.512 1.00 38.23 C ANISOU 707 CG GLU A 134 5337 5630 3557 -59 -83 353 C ATOM 708 CD GLU A 134 -77.455 21.198 -33.802 1.00 38.46 C ANISOU 708 CD GLU A 134 5305 5777 3530 -89 -115 393 C ATOM 709 OE1 GLU A 134 -78.684 21.407 -33.782 1.00 40.70 O ANISOU 709 OE1 GLU A 134 5578 6032 3855 -84 -136 393 O ATOM 710 OE2 GLU A 134 -76.788 21.134 -34.841 1.00 44.01 O1- ANISOU 710 OE2 GLU A 134 5968 6608 4147 -119 -121 427 O1- ATOM 711 N LEU A 135 -76.581 23.682 -28.674 1.00 37.76 N ANISOU 711 N LEU A 135 5366 5164 3818 13 -116 406 N ATOM 712 CA LEU A 135 -76.717 24.822 -27.773 1.00 37.93 C ANISOU 712 CA LEU A 135 5384 5081 3949 27 -144 434 C ATOM 713 C LEU A 135 -75.357 25.427 -27.435 1.00 40.96 C ANISOU 713 C LEU A 135 5773 5440 4349 29 -149 479 C ATOM 714 O LEU A 135 -75.162 26.648 -27.532 1.00 41.46 O ANISOU 714 O LEU A 135 5799 5470 4482 23 -196 559 O ATOM 715 CB LEU A 135 -77.436 24.373 -26.502 1.00 36.96 C ANISOU 715 CB LEU A 135 5300 4873 3871 50 -109 337 C ATOM 716 CG LEU A 135 -77.943 25.439 -25.543 1.00 40.67 C ANISOU 716 CG LEU A 135 5756 5241 4457 65 -133 334 C ATOM 717 CD1 LEU A 135 -78.937 26.372 -26.243 1.00 37.40 C ANISOU 717 CD1 LEU A 135 5280 4822 4107 56 -190 393 C ATOM 718 CD2 LEU A 135 -78.593 24.747 -24.362 1.00 36.71 C ANISOU 718 CD2 LEU A 135 5293 4686 3967 79 -88 230 C ATOM 719 N ILE A 136 -74.411 24.583 -27.009 1.00 37.39 N ANISOU 719 N ILE A 136 5366 4999 3843 38 -104 428 N ATOM 720 CA ILE A 136 -73.051 25.032 -26.727 1.00 37.43 C ANISOU 720 CA ILE A 136 5378 4990 3854 39 -106 463 C ATOM 721 C ILE A 136 -72.404 25.602 -27.982 1.00 42.88 C ANISOU 721 C ILE A 136 6020 5765 4506 10 -140 562 C ATOM 722 O ILE A 136 -71.630 26.567 -27.921 1.00 43.01 O ANISOU 722 O ILE A 136 6017 5757 4567 4 -167 630 O ATOM 723 CB ILE A 136 -72.228 23.863 -26.162 1.00 39.03 C ANISOU 723 CB ILE A 136 5632 5198 3999 53 -54 386 C ATOM 724 CG1 ILE A 136 -72.784 23.408 -24.812 1.00 35.64 C ANISOU 724 CG1 ILE A 136 5247 4684 3609 77 -24 304 C ATOM 725 CG2 ILE A 136 -70.762 24.213 -26.079 1.00 41.14 C ANISOU 725 CG2 ILE A 136 5903 5471 4258 52 -55 422 C ATOM 726 CD1 ILE A 136 -72.296 22.036 -24.421 1.00 31.18 C ANISOU 726 CD1 ILE A 136 4729 4131 2986 87 24 234 C ATOM 727 N ARG A 137 -72.695 24.998 -29.140 1.00 43.50 N ANISOU 727 N ARG A 137 6077 5952 4500 -13 -138 571 N ATOM 728 CA ARG A 137 -72.131 25.477 -30.397 1.00 41.42 C ANISOU 728 CA ARG A 137 5763 5793 4183 -49 -169 667 C ATOM 729 C ARG A 137 -72.653 26.870 -30.749 1.00 42.93 C ANISOU 729 C ARG A 137 5903 5957 4454 -64 -235 781 C ATOM 730 O ARG A 137 -71.913 27.678 -31.320 1.00 42.79 O ANISOU 730 O ARG A 137 5847 5975 4436 -90 -267 882 O ATOM 731 CB ARG A 137 -72.435 24.463 -31.505 1.00 40.21 C ANISOU 731 CB ARG A 137 5590 5769 3918 -70 -151 635 C ATOM 732 CG ARG A 137 -71.644 24.602 -32.823 1.00 45.98 C ANISOU 732 CG ARG A 137 6271 6644 4556 -113 -166 708 C ATOM 733 CD ARG A 137 -72.284 23.759 -33.958 1.00 51.85 C ANISOU 733 CD ARG A 137 6980 7521 5198 -137 -157 674 C ATOM 734 NE ARG A 137 -73.740 23.912 -34.020 1.00 49.80 N ANISOU 734 NE ARG A 137 6710 7235 4978 -132 -182 678 N ATOM 735 CZ ARG A 137 -74.405 24.529 -34.988 1.00 48.27 C ANISOU 735 CZ ARG A 137 6459 7116 4766 -162 -231 767 C ATOM 736 NH1 ARG A 137 -73.782 25.034 -36.045 1.00 50.49 N1+ ANISOU 736 NH1 ARG A 137 6687 7517 4981 -206 -260 867 N1+ ATOM 737 NH2 ARG A 137 -75.729 24.648 -34.891 1.00 42.66 N ANISOU 737 NH2 ARG A 137 5742 6362 4104 -151 -252 759 N ATOM 738 N ASP A 138 -73.894 27.190 -30.382 1.00 41.17 N ANISOU 738 N ASP A 138 5673 5665 4306 -50 -256 768 N ATOM 739 CA ASP A 138 -74.510 28.449 -30.779 1.00 43.32 C ANISOU 739 CA ASP A 138 5888 5906 4664 -64 -323 873 C ATOM 740 C ASP A 138 -74.416 29.552 -29.724 1.00 46.83 C ANISOU 740 C ASP A 138 6329 6212 5253 -42 -349 887 C ATOM 741 O ASP A 138 -74.784 30.690 -30.020 1.00 50.15 O ANISOU 741 O ASP A 138 6696 6593 5766 -52 -411 980 O ATOM 742 CB ASP A 138 -75.982 28.217 -31.143 1.00 44.67 C ANISOU 742 CB ASP A 138 6041 6092 4841 -63 -340 853 C ATOM 743 CG ASP A 138 -76.157 27.372 -32.414 1.00 47.99 C ANISOU 743 CG ASP A 138 6443 6665 5128 -92 -330 860 C ATOM 744 OD1 ASP A 138 -75.198 27.249 -33.209 1.00 47.57 O ANISOU 744 OD1 ASP A 138 6373 6716 4986 -121 -327 909 O ATOM 745 OD2 ASP A 138 -77.256 26.804 -32.606 1.00 47.25 O1- ANISOU 745 OD2 ASP A 138 6347 6591 5015 -87 -324 807 O1- ATOM 746 N ASN A 139 -73.949 29.262 -28.508 1.00 48.70 N ANISOU 746 N ASN A 139 6615 6373 5516 -12 -307 798 N ATOM 747 CA ASN A 139 -73.793 30.284 -27.469 1.00 51.49 C ANISOU 747 CA ASN A 139 6959 6604 6001 7 -327 796 C ATOM 748 C ASN A 139 -72.332 30.309 -27.046 1.00 50.39 C ANISOU 748 C ASN A 139 6845 6460 5842 10 -303 795 C ATOM 749 O ASN A 139 -71.918 29.544 -26.161 1.00 49.89 O ANISOU 749 O ASN A 139 6835 6379 5743 32 -252 702 O ATOM 750 CB ASN A 139 -74.688 30.028 -26.260 1.00 50.59 C ANISOU 750 CB ASN A 139 6872 6404 5945 39 -301 681 C ATOM 751 CG ASN A 139 -76.158 30.164 -26.575 1.00 52.66 C ANISOU 751 CG ASN A 139 7103 6655 6250 38 -329 678 C ATOM 752 ND2 ASN A 139 -76.824 29.021 -26.766 1.00 50.43 N ANISOU 752 ND2 ASN A 139 6852 6428 5880 39 -291 614 N ATOM 753 OD1 ASN A 139 -76.710 31.274 -26.591 1.00 51.86 O ANISOU 753 OD1 ASN A 139 6948 6489 6269 38 -384 726 O ATOM 754 N PRO A 140 -71.511 31.158 -27.665 1.00 50.27 N ANISOU 754 N PRO A 140 6789 6463 5847 -13 -341 902 N ATOM 755 CA PRO A 140 -70.072 31.143 -27.353 1.00 47.00 C ANISOU 755 CA PRO A 140 6397 6056 5407 -13 -317 902 C ATOM 756 C PRO A 140 -69.761 31.422 -25.893 1.00 45.06 C ANISOU 756 C PRO A 140 6177 5700 5245 21 -299 822 C ATOM 757 O PRO A 140 -68.685 31.032 -25.426 1.00 45.21 O ANISOU 757 O PRO A 140 6230 5726 5221 29 -264 785 O ATOM 758 CB PRO A 140 -69.501 32.226 -28.276 1.00 47.74 C ANISOU 758 CB PRO A 140 6428 6175 5535 -48 -372 1043 C ATOM 759 CG PRO A 140 -70.445 32.276 -29.415 1.00 46.36 C ANISOU 759 CG PRO A 140 6214 6070 5331 -75 -408 1117 C ATOM 760 CD PRO A 140 -71.817 31.948 -28.868 1.00 45.23 C ANISOU 760 CD PRO A 140 6086 5871 5229 -47 -402 1034 C ATOM 761 N ALA A 141 -70.667 32.068 -25.153 1.00 44.92 N ANISOU 761 N ALA A 141 6138 5585 5342 39 -320 788 N ATOM 762 CA ALA A 141 -70.494 32.178 -23.707 1.00 45.83 C ANISOU 762 CA ALA A 141 6278 5616 5520 69 -295 691 C ATOM 763 C ALA A 141 -70.333 30.808 -23.073 1.00 43.69 C ANISOU 763 C ALA A 141 6078 5381 5140 85 -230 590 C ATOM 764 O ALA A 141 -69.348 30.537 -22.376 1.00 45.98 O ANISOU 764 O ALA A 141 6401 5664 5405 97 -201 550 O ATOM 765 CB ALA A 141 -71.689 32.896 -23.090 1.00 46.00 C ANISOU 765 CB ALA A 141 6262 5548 5667 84 -323 651 C ATOM 766 N LEU A 142 -71.298 29.931 -23.321 1.00 43.12 N ANISOU 766 N LEU A 142 6028 5346 5009 85 -210 551 N ATOM 767 CA LEU A 142 -71.317 28.616 -22.699 1.00 43.27 C ANISOU 767 CA LEU A 142 6110 5389 4943 98 -153 458 C ATOM 768 C LEU A 142 -70.122 27.770 -23.108 1.00 44.12 C ANISOU 768 C LEU A 142 6250 5565 4946 93 -124 467 C ATOM 769 O LEU A 142 -69.698 26.902 -22.340 1.00 49.03 O ANISOU 769 O LEU A 142 6921 6184 5523 107 -82 399 O ATOM 770 CB LEU A 142 -72.617 27.904 -23.076 1.00 42.95 C ANISOU 770 CB LEU A 142 6075 5376 4867 94 -143 427 C ATOM 771 CG LEU A 142 -73.962 28.314 -22.468 1.00 41.96 C ANISOU 771 CG LEU A 142 5930 5188 4825 103 -154 379 C ATOM 772 CD1 LEU A 142 -74.077 29.811 -22.202 1.00 42.41 C ANISOU 772 CD1 LEU A 142 5929 5169 5017 107 -204 415 C ATOM 773 CD2 LEU A 142 -75.060 27.882 -23.438 1.00 39.18 C ANISOU 773 CD2 LEU A 142 5563 4885 4438 91 -164 395 C ATOM 774 N ASN A 143 -69.564 28.002 -24.300 1.00 45.23 N ANISOU 774 N ASN A 143 6362 5772 5050 70 -146 550 N ATOM 775 CA ASN A 143 -68.568 27.094 -24.874 1.00 48.99 C ANISOU 775 CA ASN A 143 6862 6332 5422 61 -117 548 C ATOM 776 C ASN A 143 -67.168 27.420 -24.351 1.00 48.74 C ANISOU 776 C ASN A 143 6839 6277 5402 68 -111 555 C ATOM 777 O ASN A 143 -66.268 27.856 -25.075 1.00 48.57 O ANISOU 777 O ASN A 143 6791 6302 5364 48 -127 622 O ATOM 778 CB ASN A 143 -68.611 27.134 -26.395 1.00 45.79 C ANISOU 778 CB ASN A 143 6414 6026 4956 28 -139 625 C ATOM 779 CG ASN A 143 -67.873 25.968 -27.004 1.00 46.39 C ANISOU 779 CG ASN A 143 6509 6197 4919 19 -102 591 C ATOM 780 ND2 ASN A 143 -67.816 25.918 -28.332 1.00 47.36 N ANISOU 780 ND2 ASN A 143 6592 6429 4974 -14 -115 647 N ATOM 781 OD1 ASN A 143 -67.325 25.130 -26.276 1.00 45.95 O ANISOU 781 OD1 ASN A 143 6498 6121 4840 40 -63 516 O ATOM 782 N THR A 144 -66.994 27.164 -23.062 1.00 48.88 N ANISOU 782 N THR A 144 6896 6231 5446 94 -86 481 N ATOM 783 CA THR A 144 -65.740 27.419 -22.379 1.00 50.49 C ANISOU 783 CA THR A 144 7112 6408 5665 106 -79 473 C ATOM 784 C THR A 144 -64.774 26.243 -22.457 1.00 55.47 C ANISOU 784 C THR A 144 7781 7091 6205 111 -42 436 C ATOM 785 O THR A 144 -63.650 26.343 -21.949 1.00 54.75 O ANISOU 785 O THR A 144 7701 6985 6118 120 -36 427 O ATOM 786 CB THR A 144 -66.024 27.767 -20.931 1.00 49.58 C ANISOU 786 CB THR A 144 7012 6207 5620 129 -73 412 C ATOM 787 CG2 THR A 144 -66.153 26.482 -20.105 1.00 51.15 C ANISOU 787 CG2 THR A 144 7268 6409 5758 146 -30 328 C ATOM 788 OG1 THR A 144 -64.968 28.595 -20.429 1.00 55.12 O ANISOU 788 OG1 THR A 144 7698 6873 6372 135 -86 427 O ATOM 789 N GLY A 145 -65.184 25.137 -23.075 1.00 60.73 N ANISOU 789 N GLY A 145 8462 7816 6798 105 -20 409 N ATOM 790 CA GLY A 145 -64.293 24.026 -23.329 1.00 56.96 C ANISOU 790 CA GLY A 145 8006 7389 6245 108 9 372 C ATOM 791 C GLY A 145 -63.620 24.102 -24.687 1.00 56.33 C ANISOU 791 C GLY A 145 7887 7404 6110 80 1 423 C ATOM 792 O GLY A 145 -62.596 23.445 -24.904 1.00 57.83 O ANISOU 792 O GLY A 145 8083 7637 6252 81 20 396 O ATOM 793 N GLY A 146 -64.174 24.895 -25.603 1.00 56.33 N ANISOU 793 N GLY A 146 7843 7442 6118 54 -30 496 N ATOM 794 CA GLY A 146 -63.619 25.039 -26.940 1.00 56.06 C ANISOU 794 CA GLY A 146 7764 7515 6023 19 -40 554 C ATOM 795 C GLY A 146 -64.234 24.179 -28.040 1.00 52.64 C ANISOU 795 C GLY A 146 7311 7182 5506 -1 -29 535 C ATOM 796 O GLY A 146 -63.593 24.000 -29.082 1.00 51.31 O ANISOU 796 O GLY A 146 7108 7121 5266 -30 -26 556 O ATOM 797 N PHE A 147 -65.460 23.685 -27.852 1.00 46.33 N ANISOU 797 N PHE A 147 6529 6358 4716 10 -22 493 N ATOM 798 CA PHE A 147 -66.103 22.747 -28.770 1.00 44.31 C ANISOU 798 CA PHE A 147 6258 6190 4388 -4 -7 454 C ATOM 799 C PHE A 147 -66.277 23.340 -30.162 1.00 46.37 C ANISOU 799 C PHE A 147 6456 6563 4598 -47 -37 538 C ATOM 800 O PHE A 147 -66.761 24.470 -30.310 1.00 46.31 O ANISOU 800 O PHE A 147 6423 6533 4640 -60 -79 628 O ATOM 801 CB PHE A 147 -67.471 22.353 -28.214 1.00 40.36 C ANISOU 801 CB PHE A 147 5784 5627 3923 15 -1 407 C ATOM 802 CG PHE A 147 -68.192 21.294 -29.009 1.00 37.90 C ANISOU 802 CG PHE A 147 5459 5392 3548 4 18 352 C ATOM 803 CD1 PHE A 147 -67.597 20.062 -29.252 1.00 35.59 C ANISOU 803 CD1 PHE A 147 5173 5148 3202 8 54 272 C ATOM 804 CD2 PHE A 147 -69.488 21.508 -29.451 1.00 34.60 C ANISOU 804 CD2 PHE A 147 5021 4990 3136 -6 -1 371 C ATOM 805 CE1 PHE A 147 -68.263 19.075 -29.925 1.00 31.48 C ANISOU 805 CE1 PHE A 147 4636 4691 2635 0 72 210 C ATOM 806 CE2 PHE A 147 -70.165 20.532 -30.149 1.00 32.31 C ANISOU 806 CE2 PHE A 147 4716 4769 2791 -15 17 313 C ATOM 807 CZ PHE A 147 -69.555 19.312 -30.385 1.00 35.30 C ANISOU 807 CZ PHE A 147 5099 5195 3117 -12 54 230 C ATOM 808 N ASN A 148 -65.908 22.551 -31.188 1.00 41.59 N ANISOU 808 N ASN A 148 5821 6082 3898 -70 -18 507 N ATOM 809 CA ASN A 148 -66.118 22.906 -32.588 1.00 38.09 C ANISOU 809 CA ASN A 148 5314 5774 3383 -117 -42 576 C ATOM 810 C ASN A 148 -66.672 21.738 -33.394 1.00 36.81 C ANISOU 810 C ASN A 148 5131 5715 3141 -128 -16 494 C ATOM 811 O ASN A 148 -66.545 21.728 -34.623 1.00 36.31 O ANISOU 811 O ASN A 148 5009 5797 2990 -170 -24 523 O ATOM 812 CB ASN A 148 -64.818 23.386 -33.225 1.00 40.87 C ANISOU 812 CB ASN A 148 5628 6212 3688 -150 -47 635 C ATOM 813 CG ASN A 148 -63.759 22.291 -33.284 1.00 45.40 C ANISOU 813 CG ASN A 148 6208 6838 4205 -144 -2 533 C ATOM 814 ND2 ASN A 148 -62.686 22.543 -34.032 1.00 46.27 N ANISOU 814 ND2 ASN A 148 6274 7053 4254 -179 -1 569 N ATOM 815 OD1 ASN A 148 -63.886 21.248 -32.634 1.00 47.01 O ANISOU 815 OD1 ASN A 148 6452 6984 4426 -108 31 426 O ATOM 816 N GLY A 149 -67.286 20.763 -32.739 1.00 35.83 N ANISOU 816 N GLY A 149 5048 5523 3043 -94 12 394 N ATOM 817 CA GLY A 149 -67.760 19.582 -33.421 1.00 36.63 C ANISOU 817 CA GLY A 149 5128 5708 3082 -101 39 302 C ATOM 818 C GLY A 149 -69.190 19.686 -33.933 1.00 40.38 C ANISOU 818 C GLY A 149 5581 6214 3549 -113 19 320 C ATOM 819 O GLY A 149 -69.994 20.503 -33.481 1.00 41.50 O ANISOU 819 O GLY A 149 5738 6277 3753 -105 -11 383 O ATOM 820 N GLU A 150 -69.486 18.823 -34.907 1.00 43.86 N ANISOU 820 N GLU A 150 5979 6775 3912 -133 36 255 N ATOM 821 CA GLU A 150 -70.801 18.714 -35.536 1.00 47.97 C ANISOU 821 CA GLU A 150 6471 7348 4409 -147 21 253 C ATOM 822 C GLU A 150 -71.432 17.369 -35.168 1.00 46.38 C ANISOU 822 C GLU A 150 6292 7103 4226 -120 61 119 C ATOM 823 O GLU A 150 -70.828 16.308 -35.368 1.00 43.54 O ANISOU 823 O GLU A 150 5922 6785 3837 -117 96 20 O ATOM 824 CB GLU A 150 -70.686 18.877 -37.049 1.00 44.46 C ANISOU 824 CB GLU A 150 5946 7094 3854 -199 5 291 C ATOM 825 CG GLU A 150 -70.824 20.316 -37.495 1.00 52.42 C ANISOU 825 CG GLU A 150 6924 8135 4858 -230 -51 450 C ATOM 826 CD GLU A 150 -72.255 20.856 -37.383 1.00 63.38 C ANISOU 826 CD GLU A 150 8315 9466 6299 -222 -89 502 C ATOM 827 OE1 GLU A 150 -72.454 21.914 -36.734 1.00 70.54 O ANISOU 827 OE1 GLU A 150 9244 10262 7294 -209 -124 592 O ATOM 828 OE2 GLU A 150 -73.175 20.244 -37.980 1.00 72.61 O1- ANISOU 828 OE2 GLU A 150 9456 10706 7425 -231 -85 449 O1- ATOM 829 N VAL A 151 -72.643 17.421 -34.627 1.00 39.67 N ANISOU 829 N VAL A 151 5470 6167 3435 -101 53 116 N ATOM 830 CA VAL A 151 -73.272 16.297 -33.948 1.00 36.47 C ANISOU 830 CA VAL A 151 5101 5681 3074 -72 88 7 C ATOM 831 C VAL A 151 -74.411 15.774 -34.804 1.00 35.28 C ANISOU 831 C VAL A 151 4908 5613 2885 -88 88 -40 C ATOM 832 O VAL A 151 -75.340 16.517 -35.135 1.00 37.77 O ANISOU 832 O VAL A 151 5204 5947 3199 -100 54 25 O ATOM 833 CB VAL A 151 -73.774 16.721 -32.565 1.00 36.53 C ANISOU 833 CB VAL A 151 5174 5529 3179 -41 84 31 C ATOM 834 CG1 VAL A 151 -72.627 16.679 -31.602 1.00 38.24 C ANISOU 834 CG1 VAL A 151 5436 5664 3432 -19 100 28 C ATOM 835 CG2 VAL A 151 -74.298 18.149 -32.633 1.00 35.03 C ANISOU 835 CG2 VAL A 151 4970 5325 3013 -51 36 145 C ATOM 836 N THR A 152 -74.355 14.497 -35.142 1.00 32.73 N ANISOU 836 N THR A 152 4565 5333 2537 -87 124 -157 N ATOM 837 CA THR A 152 -75.290 13.904 -36.078 1.00 32.54 C ANISOU 837 CA THR A 152 4489 5408 2467 -105 127 -219 C ATOM 838 C THR A 152 -76.059 12.805 -35.364 1.00 32.32 C ANISOU 838 C THR A 152 4494 5278 2508 -77 160 -322 C ATOM 839 O THR A 152 -75.459 11.942 -34.720 1.00 32.94 O ANISOU 839 O THR A 152 4602 5284 2631 -56 191 -393 O ATOM 840 CB THR A 152 -74.543 13.351 -37.295 1.00 34.50 C ANISOU 840 CB THR A 152 4666 5823 2621 -135 141 -278 C ATOM 841 CG2 THR A 152 -75.436 12.397 -38.103 1.00 34.29 C ANISOU 841 CG2 THR A 152 4585 5884 2560 -147 156 -384 C ATOM 842 OG1 THR A 152 -74.151 14.436 -38.142 1.00 33.74 O ANISOU 842 OG1 THR A 152 4527 5847 2447 -172 105 -168 O ATOM 843 N LYS A 153 -77.382 12.850 -35.457 1.00 32.24 N ANISOU 843 N LYS A 153 4478 5260 2512 -79 150 -326 N ATOM 844 CA LYS A 153 -78.185 11.782 -34.881 1.00 32.00 C ANISOU 844 CA LYS A 153 4471 5146 2544 -59 181 -424 C ATOM 845 C LYS A 153 -78.113 10.580 -35.804 1.00 32.55 C ANISOU 845 C LYS A 153 4480 5315 2574 -72 208 -545 C ATOM 846 O LYS A 153 -78.285 10.713 -37.016 1.00 33.19 O ANISOU 846 O LYS A 153 4493 5546 2572 -100 194 -552 O ATOM 847 CB LYS A 153 -79.630 12.239 -34.686 1.00 31.92 C ANISOU 847 CB LYS A 153 4469 5096 2563 -58 163 -394 C ATOM 848 CG LYS A 153 -80.550 11.242 -33.992 1.00 31.67 C ANISOU 848 CG LYS A 153 4464 4969 2599 -41 195 -483 C ATOM 849 CD LYS A 153 -81.965 11.819 -33.811 1.00 31.61 C ANISOU 849 CD LYS A 153 4461 4929 2620 -41 174 -451 C ATOM 850 CE LYS A 153 -82.948 10.768 -33.354 1.00 31.51 C ANISOU 850 CE LYS A 153 4461 4850 2662 -32 207 -545 C ATOM 851 NZ LYS A 153 -84.353 11.249 -33.453 1.00 31.61 N1+ ANISOU 851 NZ LYS A 153 4460 4860 2688 -37 187 -530 N1+ ATOM 852 N VAL A 154 -77.815 9.413 -35.244 1.00 32.39 N ANISOU 852 N VAL A 154 4477 5216 2612 -52 244 -641 N ATOM 853 CA VAL A 154 -77.815 8.202 -36.050 1.00 32.95 C ANISOU 853 CA VAL A 154 4486 5365 2670 -61 269 -773 C ATOM 854 C VAL A 154 -79.208 7.591 -35.941 1.00 32.98 C ANISOU 854 C VAL A 154 4487 5327 2718 -57 281 -833 C ATOM 855 O VAL A 154 -79.964 7.549 -36.923 1.00 33.50 O ANISOU 855 O VAL A 154 4493 5506 2730 -78 273 -868 O ATOM 856 CB VAL A 154 -76.705 7.229 -35.615 1.00 32.90 C ANISOU 856 CB VAL A 154 4486 5299 2716 -44 297 -849 C ATOM 857 CG1 VAL A 154 -76.773 5.932 -36.422 1.00 33.56 C ANISOU 857 CG1 VAL A 154 4496 5452 2806 -51 323 -1000 C ATOM 858 CG2 VAL A 154 -75.346 7.891 -35.763 1.00 32.89 C ANISOU 858 CG2 VAL A 154 4485 5347 2666 -49 286 -789 C ATOM 859 N ASP A 155 -79.564 7.118 -34.755 1.00 32.48 N ANISOU 859 N ASP A 155 4483 5109 2750 -34 298 -844 N ATOM 860 CA ASP A 155 -80.940 6.755 -34.465 1.00 32.42 C ANISOU 860 CA ASP A 155 4485 5046 2789 -32 307 -877 C ATOM 861 C ASP A 155 -81.287 7.400 -33.126 1.00 32.49 C ANISOU 861 C ASP A 155 4574 4918 2853 -16 301 -789 C ATOM 862 O ASP A 155 -80.668 8.369 -32.670 1.00 32.34 O ANISOU 862 O ASP A 155 4592 4875 2820 -11 282 -694 O ATOM 863 CB ASP A 155 -81.156 5.235 -34.461 1.00 32.72 C ANISOU 863 CB ASP A 155 4496 5044 2893 -26 341 -1009 C ATOM 864 CG ASP A 155 -80.057 4.490 -33.756 1.00 32.57 C ANISOU 864 CG ASP A 155 4503 4933 2940 -9 359 -1037 C ATOM 865 OD1 ASP A 155 -79.637 4.907 -32.639 1.00 37.62 O ANISOU 865 OD1 ASP A 155 5212 5467 3614 6 355 -955 O ATOM 866 OD2 ASP A 155 -79.623 3.460 -34.292 1.00 33.07 O1- ANISOU 866 OD2 ASP A 155 4512 5028 3026 -10 377 -1145 O1- ATOM 867 N THR A 156 -82.281 6.842 -32.446 1.00 31.59 N ANISOU 867 N THR A 156 4484 4713 2805 -10 319 -824 N ATOM 868 CA THR A 156 -82.636 7.371 -31.146 1.00 32.95 C ANISOU 868 CA THR A 156 4726 4766 3027 0 318 -755 C ATOM 869 C THR A 156 -81.514 7.155 -30.140 1.00 32.93 C ANISOU 869 C THR A 156 4775 4674 3063 15 329 -727 C ATOM 870 O THR A 156 -81.327 7.979 -29.247 1.00 32.99 O ANISOU 870 O THR A 156 4833 4623 3080 22 318 -648 O ATOM 871 CB THR A 156 -83.925 6.714 -30.673 1.00 32.14 C ANISOU 871 CB THR A 156 4632 4597 2982 -3 339 -806 C ATOM 872 CG2 THR A 156 -84.970 6.835 -31.741 1.00 31.42 C ANISOU 872 CG2 THR A 156 4484 4602 2852 -16 328 -843 C ATOM 873 OG1 THR A 156 -83.667 5.328 -30.486 1.00 38.92 O ANISOU 873 OG1 THR A 156 5485 5407 3898 0 370 -889 O ATOM 874 N THR A 157 -80.723 6.096 -30.297 1.00 36.08 N ANISOU 874 N THR A 157 5157 5067 3486 20 347 -793 N ATOM 875 CA THR A 157 -79.749 5.710 -29.285 1.00 32.10 C ANISOU 875 CA THR A 157 4699 4467 3032 35 356 -773 C ATOM 876 C THR A 157 -78.302 5.899 -29.720 1.00 32.80 C ANISOU 876 C THR A 157 4771 4608 3085 41 346 -763 C ATOM 877 O THR A 157 -77.407 5.431 -29.017 1.00 34.13 O ANISOU 877 O THR A 157 4967 4704 3298 55 352 -761 O ATOM 878 CB THR A 157 -79.965 4.245 -28.895 1.00 35.46 C ANISOU 878 CB THR A 157 5119 4811 3542 37 383 -852 C ATOM 879 CG2 THR A 157 -81.261 4.060 -28.148 1.00 31.67 C ANISOU 879 CG2 THR A 157 4668 4259 3107 29 396 -847 C ATOM 880 OG1 THR A 157 -80.062 3.470 -30.084 1.00 41.33 O ANISOU 880 OG1 THR A 157 5789 5634 4280 31 391 -955 O ATOM 881 N HIS A 158 -78.044 6.546 -30.865 1.00 35.38 N ANISOU 881 N HIS A 158 5051 5062 3332 30 329 -757 N ATOM 882 CA HIS A 158 -76.702 6.589 -31.461 1.00 35.01 C ANISOU 882 CA HIS A 158 4974 5085 3245 30 324 -766 C ATOM 883 C HIS A 158 -76.432 7.943 -32.102 1.00 32.13 C ANISOU 883 C HIS A 158 4595 4821 2793 15 296 -681 C ATOM 884 O HIS A 158 -77.303 8.514 -32.754 1.00 33.12 O ANISOU 884 O HIS A 158 4694 5018 2872 -1 280 -658 O ATOM 885 CB HIS A 158 -76.521 5.497 -32.516 1.00 31.84 C ANISOU 885 CB HIS A 158 4496 4764 2838 21 340 -888 C ATOM 886 CG HIS A 158 -76.504 4.112 -31.953 1.00 38.72 C ANISOU 886 CG HIS A 158 5369 5531 3810 36 364 -973 C ATOM 887 CD2 HIS A 158 -75.492 3.225 -31.802 1.00 40.00 C ANISOU 887 CD2 HIS A 158 5516 5652 4030 49 373 -1033 C ATOM 888 ND1 HIS A 158 -77.638 3.487 -31.476 1.00 37.60 N ANISOU 888 ND1 HIS A 158 5242 5310 3733 37 377 -1003 N ATOM 889 CE1 HIS A 158 -77.319 2.280 -31.042 1.00 38.70 C ANISOU 889 CE1 HIS A 158 5377 5361 3966 48 393 -1069 C ATOM 890 NE2 HIS A 158 -76.024 2.094 -31.234 1.00 39.53 N ANISOU 890 NE2 HIS A 158 5462 5485 4072 57 389 -1090 N ATOM 891 N VAL A 159 -75.218 8.451 -31.913 1.00 31.47 N ANISOU 891 N VAL A 159 4527 4740 2691 21 286 -631 N ATOM 892 CA VAL A 159 -74.858 9.806 -32.299 1.00 30.98 C ANISOU 892 CA VAL A 159 4461 4748 2564 7 257 -532 C ATOM 893 C VAL A 159 -73.395 9.785 -32.715 1.00 31.19 C ANISOU 893 C VAL A 159 4462 4834 2555 4 259 -539 C ATOM 894 O VAL A 159 -72.649 8.861 -32.396 1.00 31.21 O ANISOU 894 O VAL A 159 4467 4793 2598 19 279 -606 O ATOM 895 CB VAL A 159 -75.103 10.817 -31.149 1.00 35.11 C ANISOU 895 CB VAL A 159 5050 5165 3126 21 241 -432 C ATOM 896 CG1 VAL A 159 -74.682 12.232 -31.537 1.00 38.04 C ANISOU 896 CG1 VAL A 159 5411 5596 3448 8 207 -328 C ATOM 897 CG2 VAL A 159 -76.558 10.826 -30.734 1.00 32.82 C ANISOU 897 CG2 VAL A 159 4778 4820 2871 22 241 -435 C ATOM 898 N SER A 160 -72.991 10.809 -33.460 1.00 33.67 N ANISOU 898 N SER A 160 4747 5252 2795 -18 235 -468 N ATOM 899 CA SER A 160 -71.677 10.825 -34.085 1.00 31.87 C ANISOU 899 CA SER A 160 4480 5113 2516 -30 237 -479 C ATOM 900 C SER A 160 -71.238 12.272 -34.257 1.00 33.39 C ANISOU 900 C SER A 160 4677 5349 2662 -47 206 -352 C ATOM 901 O SER A 160 -72.026 13.113 -34.700 1.00 33.40 O ANISOU 901 O SER A 160 4663 5397 2630 -66 179 -279 O ATOM 902 CB SER A 160 -71.728 10.092 -35.423 1.00 32.52 C ANISOU 902 CB SER A 160 4477 5345 2533 -56 251 -575 C ATOM 903 OG SER A 160 -70.427 9.818 -35.886 1.00 36.47 O ANISOU 903 OG SER A 160 4938 5918 2999 -65 262 -619 O ATOM 904 N ILE A 161 -69.998 12.566 -33.871 1.00 35.01 N ANISOU 904 N ILE A 161 4900 5529 2874 -40 206 -322 N ATOM 905 CA ILE A 161 -69.527 13.938 -33.677 1.00 35.29 C ANISOU 905 CA ILE A 161 4952 5558 2896 -48 176 -198 C ATOM 906 C ILE A 161 -68.354 14.109 -34.617 1.00 34.37 C ANISOU 906 C ILE A 161 4782 5573 2705 -76 177 -194 C ATOM 907 O ILE A 161 -67.250 13.634 -34.330 1.00 37.79 O ANISOU 907 O ILE A 161 5219 5986 3152 -64 195 -242 O ATOM 908 CB ILE A 161 -69.104 14.230 -32.226 1.00 35.09 C ANISOU 908 CB ILE A 161 5001 5378 2952 -14 176 -163 C ATOM 909 CG1 ILE A 161 -69.864 13.362 -31.211 1.00 33.46 C ANISOU 909 CG1 ILE A 161 4844 5050 2820 16 196 -224 C ATOM 910 CG2 ILE A 161 -69.273 15.708 -31.884 1.00 34.68 C ANISOU 910 CG2 ILE A 161 4969 5292 2915 -19 142 -40 C ATOM 911 CD1 ILE A 161 -71.350 13.507 -31.249 1.00 34.31 C ANISOU 911 CD1 ILE A 161 4954 5144 2939 11 188 -214 C ATOM 912 N ALA A 162 -68.573 14.776 -35.737 1.00 35.68 N ANISOU 912 N ALA A 162 4891 5877 2790 -117 155 -136 N ATOM 913 CA ALA A 162 -67.478 15.045 -36.652 1.00 33.89 C ANISOU 913 CA ALA A 162 4607 5789 2481 -152 155 -119 C ATOM 914 C ALA A 162 -66.680 16.261 -36.183 1.00 36.38 C ANISOU 914 C ALA A 162 4950 6057 2815 -155 130 2 C ATOM 915 O ALA A 162 -67.249 17.251 -35.721 1.00 40.02 O ANISOU 915 O ALA A 162 5443 6444 3318 -150 99 104 O ATOM 916 CB ALA A 162 -68.020 15.271 -38.057 1.00 37.99 C ANISOU 916 CB ALA A 162 5050 6489 2897 -202 139 -97 C ATOM 917 N PHE A 163 -65.355 16.186 -36.293 1.00 32.99 N ANISOU 917 N PHE A 163 4505 5667 2362 -162 144 -16 N ATOM 918 CA PHE A 163 -64.533 17.325 -35.912 1.00 36.06 C ANISOU 918 CA PHE A 163 4913 6019 2768 -167 122 94 C ATOM 919 C PHE A 163 -63.673 17.796 -37.090 1.00 35.86 C ANISOU 919 C PHE A 163 4816 6167 2644 -221 116 139 C ATOM 920 O PHE A 163 -63.302 16.998 -37.956 1.00 34.18 O ANISOU 920 O PHE A 163 4545 6086 2357 -244 141 49 O ATOM 921 CB PHE A 163 -63.624 16.982 -34.723 1.00 34.77 C ANISOU 921 CB PHE A 163 4807 5723 2682 -124 141 49 C ATOM 922 CG PHE A 163 -64.365 16.602 -33.472 1.00 36.40 C ANISOU 922 CG PHE A 163 5084 5765 2981 -77 145 19 C ATOM 923 CD1 PHE A 163 -64.846 17.567 -32.614 1.00 34.42 C ANISOU 923 CD1 PHE A 163 4880 5405 2792 -61 120 107 C ATOM 924 CD2 PHE A 163 -64.560 15.274 -33.144 1.00 36.97 C ANISOU 924 CD2 PHE A 163 5170 5794 3083 -50 174 -99 C ATOM 925 CE1 PHE A 163 -65.518 17.215 -31.467 1.00 34.16 C ANISOU 925 CE1 PHE A 163 4907 5237 2834 -24 127 76 C ATOM 926 CE2 PHE A 163 -65.224 14.929 -31.986 1.00 34.06 C ANISOU 926 CE2 PHE A 163 4865 5283 2795 -13 179 -117 C ATOM 927 CZ PHE A 163 -65.705 15.899 -31.159 1.00 32.28 C ANISOU 927 CZ PHE A 163 4685 4965 2616 -2 157 -30 C ATOM 928 N PRO A 164 -63.346 19.091 -37.154 1.00 34.89 N ANISOU 928 N PRO A 164 4689 6049 2519 -245 83 276 N ATOM 929 CA PRO A 164 -62.525 19.586 -38.275 1.00 39.19 C ANISOU 929 CA PRO A 164 5162 6764 2965 -303 76 334 C ATOM 930 C PRO A 164 -61.034 19.338 -38.118 1.00 41.96 C ANISOU 930 C PRO A 164 5506 7129 3307 -302 103 284 C ATOM 931 O PRO A 164 -60.277 19.586 -39.074 1.00 44.96 O ANISOU 931 O PRO A 164 5820 7665 3597 -353 105 311 O ATOM 932 CB PRO A 164 -62.837 21.090 -38.305 1.00 34.78 C ANISOU 932 CB PRO A 164 4603 6180 2431 -327 25 509 C ATOM 933 CG PRO A 164 -63.278 21.410 -36.948 1.00 34.47 C ANISOU 933 CG PRO A 164 4643 5938 2518 -272 14 523 C ATOM 934 CD PRO A 164 -63.942 20.186 -36.377 1.00 34.06 C ANISOU 934 CD PRO A 164 4630 5813 2497 -227 46 389 C ATOM 935 N GLU A 165 -60.601 18.838 -36.968 1.00 36.18 N ANISOU 935 N GLU A 165 4835 6249 2662 -248 122 214 N ATOM 936 CA GLU A 165 -59.217 18.466 -36.716 1.00 35.65 C ANISOU 936 CA GLU A 165 4765 6180 2600 -238 147 151 C ATOM 937 C GLU A 165 -59.221 17.342 -35.697 1.00 38.08 C ANISOU 937 C GLU A 165 5126 6353 2989 -178 172 30 C ATOM 938 O GLU A 165 -60.234 17.131 -35.013 1.00 39.63 O ANISOU 938 O GLU A 165 5372 6440 3246 -146 166 24 O ATOM 939 CB GLU A 165 -58.420 19.668 -36.210 1.00 36.12 C ANISOU 939 CB GLU A 165 4847 6180 2698 -242 125 266 C ATOM 940 CG GLU A 165 -59.344 20.700 -35.581 1.00 41.62 C ANISOU 940 CG GLU A 165 5588 6760 3465 -229 87 381 C ATOM 941 CD GLU A 165 -58.615 21.937 -35.167 1.00 51.37 C ANISOU 941 CD GLU A 165 6833 7940 4745 -236 61 493 C ATOM 942 OE1 GLU A 165 -57.802 21.847 -34.221 1.00 55.08 O ANISOU 942 OE1 GLU A 165 7343 8310 5274 -200 74 456 O ATOM 943 OE2 GLU A 165 -58.830 22.988 -35.815 1.00 56.53 O1- ANISOU 943 OE2 GLU A 165 7449 8654 5375 -280 28 619 O1- ATOM 944 N PRO A 166 -58.124 16.590 -35.581 1.00 39.13 N ANISOU 944 N PRO A 166 5246 6493 3129 -164 198 -67 N ATOM 945 CA PRO A 166 -58.028 15.604 -34.493 1.00 33.94 C ANISOU 945 CA PRO A 166 4642 5691 2563 -107 214 -161 C ATOM 946 C PRO A 166 -58.457 16.241 -33.188 1.00 31.82 C ANISOU 946 C PRO A 166 4456 5255 2379 -70 193 -81 C ATOM 947 O PRO A 166 -58.022 17.338 -32.841 1.00 33.98 O ANISOU 947 O PRO A 166 4749 5497 2666 -76 173 16 O ATOM 948 CB PRO A 166 -56.549 15.221 -34.486 1.00 34.67 C ANISOU 948 CB PRO A 166 4708 5807 2657 -103 231 -227 C ATOM 949 CG PRO A 166 -56.136 15.387 -35.951 1.00 35.99 C ANISOU 949 CG PRO A 166 4783 6181 2711 -163 241 -237 C ATOM 950 CD PRO A 166 -56.948 16.557 -36.475 1.00 36.77 C ANISOU 950 CD PRO A 166 4875 6340 2754 -203 214 -98 C ATOM 951 N ALA A 167 -59.371 15.571 -32.489 1.00 31.62 N ANISOU 951 N ALA A 167 4476 5127 2411 -36 197 -124 N ATOM 952 CA ALA A 167 -59.914 16.110 -31.245 1.00 37.01 C ANISOU 952 CA ALA A 167 5232 5663 3168 -5 180 -60 C ATOM 953 C ALA A 167 -59.919 15.086 -30.092 1.00 32.79 C ANISOU 953 C ALA A 167 4750 4999 2711 42 193 -134 C ATOM 954 O ALA A 167 -60.766 15.183 -29.192 1.00 29.79 O ANISOU 954 O ALA A 167 4421 4516 2380 63 186 -108 O ATOM 955 CB ALA A 167 -61.321 16.670 -31.511 1.00 30.71 C ANISOU 955 CB ALA A 167 4437 4873 2359 -20 162 2 C ATOM 956 N PHE A 168 -58.988 14.114 -30.092 1.00 31.63 N ANISOU 956 N PHE A 168 4585 4855 2578 56 210 -223 N ATOM 957 CA PHE A 168 -58.911 13.150 -28.989 1.00 34.94 C ANISOU 957 CA PHE A 168 5050 5149 3076 98 217 -279 C ATOM 958 C PHE A 168 -58.849 13.861 -27.643 1.00 35.35 C ANISOU 958 C PHE A 168 5171 5083 3178 122 200 -204 C ATOM 959 O PHE A 168 -59.368 13.365 -26.636 1.00 33.50 O ANISOU 959 O PHE A 168 4984 4745 2998 148 200 -213 O ATOM 960 CB PHE A 168 -57.665 12.262 -29.091 1.00 34.90 C ANISOU 960 CB PHE A 168 5013 5154 3092 111 228 -367 C ATOM 961 CG PHE A 168 -57.466 11.588 -30.408 1.00 41.40 C ANISOU 961 CG PHE A 168 5757 6106 3869 86 246 -459 C ATOM 962 CD1 PHE A 168 -58.208 10.475 -30.759 1.00 41.19 C ANISOU 962 CD1 PHE A 168 5706 6083 3863 90 260 -549 C ATOM 963 CD2 PHE A 168 -56.467 12.023 -31.273 1.00 38.96 C ANISOU 963 CD2 PHE A 168 5391 5916 3496 58 251 -465 C ATOM 964 CE1 PHE A 168 -57.989 9.834 -31.982 1.00 47.05 C ANISOU 964 CE1 PHE A 168 6363 6951 4562 66 278 -650 C ATOM 965 CE2 PHE A 168 -56.251 11.387 -32.497 1.00 41.51 C ANISOU 965 CE2 PHE A 168 5630 6373 3768 31 270 -561 C ATOM 966 CZ PHE A 168 -57.007 10.291 -32.853 1.00 40.29 C ANISOU 966 CZ PHE A 168 5449 6226 3635 35 283 -659 C ATOM 967 N VAL A 169 -58.169 15.008 -27.609 1.00 33.82 N ANISOU 967 N VAL A 169 4975 4908 2965 112 186 -131 N ATOM 968 CA VAL A 169 -57.909 15.712 -26.359 1.00 34.06 C ANISOU 968 CA VAL A 169 5060 4838 3043 134 171 -73 C ATOM 969 C VAL A 169 -59.220 16.115 -25.692 1.00 30.70 C ANISOU 969 C VAL A 169 4676 4345 2645 139 163 -30 C ATOM 970 O VAL A 169 -59.431 15.883 -24.498 1.00 29.87 O ANISOU 970 O VAL A 169 4620 4144 2587 165 162 -33 O ATOM 971 CB VAL A 169 -56.995 16.921 -26.635 1.00 31.49 C ANISOU 971 CB VAL A 169 4713 4556 2695 116 158 -7 C ATOM 972 CG1 VAL A 169 -57.227 18.017 -25.630 1.00 32.08 C ANISOU 972 CG1 VAL A 169 4829 4548 2813 127 139 68 C ATOM 973 CG2 VAL A 169 -55.550 16.468 -26.642 1.00 31.04 C ANISOU 973 CG2 VAL A 169 4639 4517 2640 126 166 -55 C ATOM 974 N THR A 170 -60.136 16.675 -26.470 1.00 32.25 N ANISOU 974 N THR A 170 4848 4598 2808 113 157 8 N ATOM 975 CA THR A 170 -61.425 17.119 -25.972 1.00 28.49 C ANISOU 975 CA THR A 170 4399 4066 2358 115 147 44 C ATOM 976 C THR A 170 -62.322 15.979 -25.527 1.00 28.34 C ANISOU 976 C THR A 170 4407 3997 2362 131 164 -18 C ATOM 977 O THR A 170 -63.430 16.264 -25.079 1.00 28.14 O ANISOU 977 O THR A 170 4405 3929 2359 132 160 3 O ATOM 978 CB THR A 170 -62.134 17.938 -27.059 1.00 33.86 C ANISOU 978 CB THR A 170 5039 4828 2999 82 132 100 C ATOM 979 CG2 THR A 170 -61.159 18.912 -27.731 1.00 29.13 C ANISOU 979 CG2 THR A 170 4400 4298 2369 58 117 164 C ATOM 980 OG1 THR A 170 -62.689 17.057 -28.064 1.00 32.59 O ANISOU 980 OG1 THR A 170 4844 4748 2792 66 147 46 O ATOM 981 N GLY A 171 -61.899 14.720 -25.657 1.00 29.56 N ANISOU 981 N GLY A 171 4555 4156 2519 142 182 -94 N ATOM 982 CA GLY A 171 -62.754 13.580 -25.384 1.00 29.55 C ANISOU 982 CA GLY A 171 4569 4111 2546 152 197 -152 C ATOM 983 C GLY A 171 -63.361 13.616 -23.993 1.00 31.02 C ANISOU 983 C GLY A 171 4813 4191 2780 170 194 -128 C ATOM 984 O GLY A 171 -64.580 13.569 -23.802 1.00 31.90 O ANISOU 984 O GLY A 171 4940 4280 2902 164 198 -125 O ATOM 985 N PRO A 172 -62.494 13.673 -22.990 1.00 32.72 N ANISOU 985 N PRO A 172 5061 4347 3025 189 188 -113 N ATOM 986 CA PRO A 172 -62.968 13.894 -21.609 1.00 30.06 C ANISOU 986 CA PRO A 172 4774 3927 2721 200 184 -82 C ATOM 987 C PRO A 172 -64.029 14.970 -21.461 1.00 31.33 C ANISOU 987 C PRO A 172 4941 4085 2877 188 178 -38 C ATOM 988 O PRO A 172 -65.089 14.723 -20.872 1.00 32.43 O ANISOU 988 O PRO A 172 5103 4184 3033 186 185 -45 O ATOM 989 CB PRO A 172 -61.672 14.267 -20.895 1.00 34.49 C ANISOU 989 CB PRO A 172 5350 4462 3293 216 173 -60 C ATOM 990 CG PRO A 172 -60.631 13.410 -21.651 1.00 35.33 C ANISOU 990 CG PRO A 172 5425 4604 3396 222 177 -110 C ATOM 991 CD PRO A 172 -61.041 13.418 -23.068 1.00 28.96 C ANISOU 991 CD PRO A 172 4570 3882 2550 200 185 -132 C ATOM 992 N GLU A 173 -63.772 16.169 -21.989 1.00 31.09 N ANISOU 992 N GLU A 173 4886 4096 2830 177 162 7 N ATOM 993 CA GLU A 173 -64.734 17.263 -21.883 1.00 30.36 C ANISOU 993 CA GLU A 173 4790 3995 2749 166 149 50 C ATOM 994 C GLU A 173 -66.033 16.958 -22.625 1.00 33.36 C ANISOU 994 C GLU A 173 5154 4406 3117 151 155 34 C ATOM 995 O GLU A 173 -67.109 17.440 -22.232 1.00 29.08 O ANISOU 995 O GLU A 173 4619 3833 2597 148 150 47 O ATOM 996 CB GLU A 173 -64.106 18.547 -22.413 1.00 30.35 C ANISOU 996 CB GLU A 173 4758 4029 2743 156 126 108 C ATOM 997 CG GLU A 173 -64.943 19.807 -22.178 1.00 35.38 C ANISOU 997 CG GLU A 173 5386 4639 3416 149 105 156 C ATOM 998 CD GLU A 173 -64.922 20.248 -20.731 1.00 44.37 C ANISOU 998 CD GLU A 173 6556 5701 4602 165 104 151 C ATOM 999 OE1 GLU A 173 -63.999 19.816 -19.992 1.00 46.62 O ANISOU 999 OE1 GLU A 173 6866 5962 4884 181 113 130 O ATOM 1000 OE2 GLU A 173 -65.839 21.004 -20.326 1.00 45.41 O1- ANISOU 1000 OE2 GLU A 173 6682 5799 4772 162 93 162 O1- ATOM 1001 N VAL A 174 -65.963 16.164 -23.690 1.00 30.90 N ANISOU 1001 N VAL A 174 4814 4158 2769 142 165 0 N ATOM 1002 CA VAL A 174 -67.166 15.851 -24.440 1.00 28.68 C ANISOU 1002 CA VAL A 174 4511 3914 2472 128 170 -20 C ATOM 1003 C VAL A 174 -67.912 14.679 -23.829 1.00 30.66 C ANISOU 1003 C VAL A 174 4789 4110 2748 137 192 -78 C ATOM 1004 O VAL A 174 -69.142 14.713 -23.707 1.00 31.17 O ANISOU 1004 O VAL A 174 4859 4159 2824 131 195 -82 O ATOM 1005 CB VAL A 174 -66.825 15.588 -25.914 1.00 32.88 C ANISOU 1005 CB VAL A 174 4990 4554 2950 109 170 -37 C ATOM 1006 CG1 VAL A 174 -68.092 15.291 -26.693 1.00 30.59 C ANISOU 1006 CG1 VAL A 174 4675 4310 2640 93 173 -59 C ATOM 1007 CG2 VAL A 174 -66.105 16.783 -26.518 1.00 32.90 C ANISOU 1007 CG2 VAL A 174 4962 4614 2925 93 147 34 C ATOM 1008 N LEU A 175 -67.187 13.644 -23.434 1.00 30.56 N ANISOU 1008 N LEU A 175 4793 4068 2751 151 206 -119 N ATOM 1009 CA LEU A 175 -67.810 12.435 -22.923 1.00 33.10 C ANISOU 1009 CA LEU A 175 5134 4337 3104 156 224 -168 C ATOM 1010 C LEU A 175 -68.152 12.500 -21.441 1.00 36.17 C ANISOU 1010 C LEU A 175 5574 4643 3528 164 226 -144 C ATOM 1011 O LEU A 175 -69.023 11.741 -20.992 1.00 36.30 O ANISOU 1011 O LEU A 175 5605 4619 3567 160 240 -168 O ATOM 1012 CB LEU A 175 -66.886 11.240 -23.186 1.00 35.23 C ANISOU 1012 CB LEU A 175 5390 4607 3389 167 233 -223 C ATOM 1013 CG LEU A 175 -66.678 10.953 -24.671 1.00 32.41 C ANISOU 1013 CG LEU A 175 4974 4345 2996 155 237 -271 C ATOM 1014 CD1 LEU A 175 -65.450 10.134 -24.945 1.00 30.81 C ANISOU 1014 CD1 LEU A 175 4747 4152 2807 166 241 -323 C ATOM 1015 CD2 LEU A 175 -67.884 10.228 -25.176 1.00 37.33 C ANISOU 1015 CD2 LEU A 175 5578 4982 3625 144 251 -321 C ATOM 1016 N GLY A 176 -67.499 13.376 -20.673 1.00 39.65 N ANISOU 1016 N GLY A 176 6035 5061 3970 172 213 -99 N ATOM 1017 CA GLY A 176 -67.650 13.336 -19.226 1.00 36.98 C ANISOU 1017 CA GLY A 176 5738 4657 3655 177 216 -84 C ATOM 1018 C GLY A 176 -67.959 14.662 -18.552 1.00 40.29 C ANISOU 1018 C GLY A 176 6166 5067 4077 174 205 -47 C ATOM 1019 O GLY A 176 -68.449 14.674 -17.419 1.00 41.53 O ANISOU 1019 O GLY A 176 6349 5185 4246 170 212 -45 O ATOM 1020 N LYS A 177 -67.700 15.789 -19.227 1.00 35.31 N ANISOU 1020 N LYS A 177 5507 4471 3437 172 188 -19 N ATOM 1021 CA LYS A 177 -67.915 17.098 -18.627 1.00 31.37 C ANISOU 1021 CA LYS A 177 5006 3955 2958 171 173 11 C ATOM 1022 C LYS A 177 -68.993 17.899 -19.338 1.00 29.64 C ANISOU 1022 C LYS A 177 4756 3757 2749 158 162 25 C ATOM 1023 O LYS A 177 -69.062 19.117 -19.155 1.00 29.55 O ANISOU 1023 O LYS A 177 4727 3735 2767 157 142 54 O ATOM 1024 CB LYS A 177 -66.619 17.900 -18.604 1.00 32.31 C ANISOU 1024 CB LYS A 177 5116 4081 3079 180 156 43 C ATOM 1025 CG LYS A 177 -65.548 17.276 -17.726 1.00 35.34 C ANISOU 1025 CG LYS A 177 5529 4439 3459 195 162 33 C ATOM 1026 CD LYS A 177 -66.041 17.084 -16.310 1.00 29.27 C ANISOU 1026 CD LYS A 177 4792 3627 2702 195 171 20 C ATOM 1027 CE LYS A 177 -64.940 16.555 -15.395 1.00 33.00 C ANISOU 1027 CE LYS A 177 5290 4079 3169 208 170 22 C ATOM 1028 NZ LYS A 177 -65.442 16.360 -14.026 1.00 30.42 N1+ ANISOU 1028 NZ LYS A 177 4990 3727 2843 201 178 16 N1+ ATOM 1029 N THR A 178 -69.839 17.256 -20.146 1.00 29.06 N ANISOU 1029 N THR A 178 4671 3712 2661 148 171 4 N ATOM 1030 CA THR A 178 -70.896 17.965 -20.862 1.00 27.17 C ANISOU 1030 CA THR A 178 4399 3495 2430 136 157 19 C ATOM 1031 C THR A 178 -72.244 17.362 -20.505 1.00 27.47 C ANISOU 1031 C THR A 178 4448 3511 2478 129 175 -22 C ATOM 1032 O THR A 178 -72.512 16.192 -20.806 1.00 27.21 O ANISOU 1032 O THR A 178 4423 3490 2427 126 195 -59 O ATOM 1033 CB THR A 178 -70.669 17.941 -22.364 1.00 27.43 C ANISOU 1033 CB THR A 178 4393 3602 2426 125 145 37 C ATOM 1034 CG2 THR A 178 -71.694 18.809 -23.044 1.00 27.64 C ANISOU 1034 CG2 THR A 178 4384 3652 2466 112 122 68 C ATOM 1035 OG1 THR A 178 -69.367 18.457 -22.642 1.00 27.47 O ANISOU 1035 OG1 THR A 178 4387 3631 2419 128 131 74 O ATOM 1036 N PHE A 179 -73.092 18.180 -19.887 1.00 27.60 N ANISOU 1036 N PHE A 179 4460 3496 2532 126 167 -19 N ATOM 1037 CA PHE A 179 -74.238 17.715 -19.121 1.00 27.11 C ANISOU 1037 CA PHE A 179 4414 3404 2484 119 188 -61 C ATOM 1038 C PHE A 179 -75.491 17.945 -19.951 1.00 27.62 C ANISOU 1038 C PHE A 179 4446 3490 2559 109 179 -68 C ATOM 1039 O PHE A 179 -75.782 19.084 -20.342 1.00 27.59 O ANISOU 1039 O PHE A 179 4409 3490 2585 109 150 -38 O ATOM 1040 CB PHE A 179 -74.275 18.430 -17.762 1.00 27.03 C ANISOU 1040 CB PHE A 179 4415 3352 2505 121 189 -67 C ATOM 1041 CG PHE A 179 -73.078 18.105 -16.902 1.00 27.80 C ANISOU 1041 CG PHE A 179 4543 3434 2585 129 197 -61 C ATOM 1042 CD1 PHE A 179 -71.841 18.720 -17.145 1.00 26.85 C ANISOU 1042 CD1 PHE A 179 4416 3322 2466 142 177 -26 C ATOM 1043 CD2 PHE A 179 -73.162 17.127 -15.910 1.00 26.87 C ANISOU 1043 CD2 PHE A 179 4461 3299 2451 123 223 -85 C ATOM 1044 CE1 PHE A 179 -70.723 18.387 -16.416 1.00 26.75 C ANISOU 1044 CE1 PHE A 179 4430 3298 2437 151 183 -22 C ATOM 1045 CE2 PHE A 179 -72.043 16.781 -15.157 1.00 26.81 C ANISOU 1045 CE2 PHE A 179 4480 3281 2427 130 226 -72 C ATOM 1046 CZ PHE A 179 -70.820 17.408 -15.413 1.00 28.08 C ANISOU 1046 CZ PHE A 179 4633 3448 2588 146 206 -44 C ATOM 1047 N ILE A 180 -76.191 16.856 -20.269 1.00 27.35 N ANISOU 1047 N ILE A 180 4418 3467 2506 101 201 -106 N ATOM 1048 CA ILE A 180 -77.246 16.894 -21.275 1.00 28.52 C ANISOU 1048 CA ILE A 180 4532 3650 2653 92 193 -115 C ATOM 1049 C ILE A 180 -78.489 17.492 -20.644 1.00 27.59 C ANISOU 1049 C ILE A 180 4406 3499 2579 87 190 -134 C ATOM 1050 O ILE A 180 -78.871 17.096 -19.551 1.00 27.86 O ANISOU 1050 O ILE A 180 4466 3496 2624 82 216 -168 O ATOM 1051 CB ILE A 180 -77.518 15.483 -21.845 1.00 27.97 C ANISOU 1051 CB ILE A 180 4466 3605 2554 86 218 -160 C ATOM 1052 CG1 ILE A 180 -76.233 14.829 -22.351 1.00 27.66 C ANISOU 1052 CG1 ILE A 180 4431 3595 2482 93 222 -156 C ATOM 1053 CG2 ILE A 180 -78.474 15.543 -23.021 1.00 27.91 C ANISOU 1053 CG2 ILE A 180 4418 3649 2536 77 206 -169 C ATOM 1054 CD1 ILE A 180 -75.429 15.714 -23.298 1.00 27.97 C ANISOU 1054 CD1 ILE A 180 4440 3691 2498 94 192 -107 C ATOM 1055 N VAL A 181 -79.118 18.446 -21.325 1.00 27.80 N ANISOU 1055 N VAL A 181 4391 3541 2631 85 159 -111 N ATOM 1056 CA VAL A 181 -80.328 19.080 -20.796 1.00 29.80 C ANISOU 1056 CA VAL A 181 4626 3761 2937 81 152 -135 C ATOM 1057 C VAL A 181 -81.513 18.724 -21.692 1.00 28.98 C ANISOU 1057 C VAL A 181 4495 3688 2828 72 149 -156 C ATOM 1058 O VAL A 181 -81.311 18.458 -22.879 1.00 30.60 O ANISOU 1058 O VAL A 181 4682 3949 2996 70 136 -132 O ATOM 1059 CB VAL A 181 -80.155 20.606 -20.670 1.00 29.60 C ANISOU 1059 CB VAL A 181 4566 3710 2970 88 112 -95 C ATOM 1060 CG1 VAL A 181 -79.017 20.944 -19.718 1.00 27.85 C ANISOU 1060 CG1 VAL A 181 4368 3459 2755 97 117 -85 C ATOM 1061 CG2 VAL A 181 -79.941 21.235 -22.035 1.00 34.54 C ANISOU 1061 CG2 VAL A 181 5153 4378 3594 88 69 -28 C ATOM 1062 N PRO A 182 -82.754 18.721 -21.194 1.00 28.20 N ANISOU 1062 N PRO A 182 4388 3564 2763 65 160 -203 N ATOM 1063 CA PRO A 182 -83.877 18.169 -21.976 1.00 31.68 C ANISOU 1063 CA PRO A 182 4808 4035 3195 57 163 -233 C ATOM 1064 C PRO A 182 -84.301 19.096 -23.108 1.00 33.26 C ANISOU 1064 C PRO A 182 4955 4268 3415 59 114 -188 C ATOM 1065 O PRO A 182 -84.687 20.242 -22.871 1.00 34.80 O ANISOU 1065 O PRO A 182 5120 4430 3673 63 81 -169 O ATOM 1066 CB PRO A 182 -84.992 18.013 -20.934 1.00 28.73 C ANISOU 1066 CB PRO A 182 4440 3620 2856 47 190 -295 C ATOM 1067 CG PRO A 182 -84.662 19.007 -19.892 1.00 31.01 C ANISOU 1067 CG PRO A 182 4728 3866 3188 53 181 -289 C ATOM 1068 CD PRO A 182 -83.172 19.126 -19.844 1.00 29.40 C ANISOU 1068 CD PRO A 182 4548 3666 2958 63 174 -240 C ATOM 1069 N GLU A 183 -84.249 18.585 -24.345 1.00 31.50 N ANISOU 1069 N GLU A 183 4715 4112 3141 53 106 -173 N ATOM 1070 CA GLU A 183 -84.662 19.378 -25.502 1.00 32.35 C ANISOU 1070 CA GLU A 183 4769 4266 3255 50 56 -121 C ATOM 1071 C GLU A 183 -86.036 20.001 -25.293 1.00 30.05 C ANISOU 1071 C GLU A 183 4445 3939 3032 50 35 -142 C ATOM 1072 O GLU A 183 -86.247 21.181 -25.595 1.00 29.85 O ANISOU 1072 O GLU A 183 4379 3903 3060 53 -16 -87 O ATOM 1073 CB GLU A 183 -84.682 18.508 -26.767 1.00 34.23 C ANISOU 1073 CB GLU A 183 4990 4595 3420 39 60 -128 C ATOM 1074 CG GLU A 183 -84.990 19.256 -28.094 1.00 30.71 C ANISOU 1074 CG GLU A 183 4484 4223 2960 29 6 -62 C ATOM 1075 CD GLU A 183 -86.460 19.633 -28.283 1.00 30.60 C ANISOU 1075 CD GLU A 183 4435 4200 2994 27 -19 -77 C ATOM 1076 OE1 GLU A 183 -87.366 18.893 -27.830 1.00 31.65 O ANISOU 1076 OE1 GLU A 183 4581 4306 3139 28 15 -157 O ATOM 1077 OE2 GLU A 183 -86.712 20.670 -28.921 1.00 35.31 O1- ANISOU 1077 OE2 GLU A 183 4983 4815 3616 24 -75 -4 O1- ATOM 1078 N HIS A 184 -86.981 19.227 -24.771 1.00 29.44 N ANISOU 1078 N HIS A 184 4383 3842 2961 46 72 -219 N ATOM 1079 CA HIS A 184 -88.361 19.682 -24.687 1.00 29.99 C ANISOU 1079 CA HIS A 184 4416 3888 3089 45 55 -251 C ATOM 1080 C HIS A 184 -88.608 20.665 -23.553 1.00 31.70 C ANISOU 1080 C HIS A 184 4626 4029 3389 52 46 -265 C ATOM 1081 O HIS A 184 -89.767 20.996 -23.305 1.00 33.76 O ANISOU 1081 O HIS A 184 4857 4264 3707 51 38 -307 O ATOM 1082 CB HIS A 184 -89.314 18.516 -24.476 1.00 29.64 C ANISOU 1082 CB HIS A 184 4387 3848 3026 35 101 -334 C ATOM 1083 CG HIS A 184 -89.249 17.959 -23.093 1.00 34.93 C ANISOU 1083 CG HIS A 184 5103 4466 3704 29 153 -388 C ATOM 1084 CD2 HIS A 184 -90.000 18.213 -21.992 1.00 31.09 C ANISOU 1084 CD2 HIS A 184 4616 3931 3266 24 171 -439 C ATOM 1085 ND1 HIS A 184 -88.265 17.082 -22.694 1.00 34.75 N ANISOU 1085 ND1 HIS A 184 5127 4442 3633 27 189 -389 N ATOM 1086 CE1 HIS A 184 -88.429 16.795 -21.413 1.00 31.06 C ANISOU 1086 CE1 HIS A 184 4691 3931 3181 18 226 -430 C ATOM 1087 NE2 HIS A 184 -89.483 17.459 -20.969 1.00 29.03 N ANISOU 1087 NE2 HIS A 184 4405 3650 2977 15 218 -463 N ATOM 1088 N LEU A 185 -87.586 21.101 -22.824 1.00 31.70 N ANISOU 1088 N LEU A 185 4648 3996 3399 59 49 -242 N ATOM 1089 CA LEU A 185 -87.770 22.177 -21.858 1.00 30.98 C ANISOU 1089 CA LEU A 185 4536 3842 3394 65 34 -258 C ATOM 1090 C LEU A 185 -86.890 23.364 -22.134 1.00 30.87 C ANISOU 1090 C LEU A 185 4495 3810 3424 77 -16 -181 C ATOM 1091 O LEU A 185 -87.282 24.488 -21.834 1.00 35.81 O ANISOU 1091 O LEU A 185 5075 4385 4145 84 -53 -181 O ATOM 1092 CB LEU A 185 -87.496 21.691 -20.421 1.00 30.84 C ANISOU 1092 CB LEU A 185 4561 3795 3362 60 87 -320 C ATOM 1093 CG LEU A 185 -88.532 20.655 -19.995 1.00 34.38 C ANISOU 1093 CG LEU A 185 5026 4251 3785 44 134 -396 C ATOM 1094 CD1 LEU A 185 -88.144 20.008 -18.692 1.00 34.88 C ANISOU 1094 CD1 LEU A 185 5135 4301 3815 32 186 -437 C ATOM 1095 CD2 LEU A 185 -89.925 21.277 -19.923 1.00 29.57 C ANISOU 1095 CD2 LEU A 185 4364 3620 3250 42 116 -445 C ATOM 1096 N TRP A 186 -85.724 23.146 -22.721 1.00 32.63 N ANISOU 1096 N TRP A 186 4740 4070 3587 77 -20 -118 N ATOM 1097 CA TRP A 186 -84.761 24.206 -22.944 1.00 35.26 C ANISOU 1097 CA TRP A 186 5052 4388 3956 84 -63 -40 C ATOM 1098 C TRP A 186 -84.962 24.913 -24.268 1.00 37.94 C ANISOU 1098 C TRP A 186 5338 4760 4316 80 -124 46 C ATOM 1099 O TRP A 186 -84.162 25.784 -24.620 1.00 41.35 O ANISOU 1099 O TRP A 186 5748 5187 4777 80 -164 126 O ATOM 1100 CB TRP A 186 -83.346 23.649 -22.834 1.00 32.10 C ANISOU 1100 CB TRP A 186 4700 4014 3483 84 -35 -17 C ATOM 1101 CG TRP A 186 -82.960 23.442 -21.415 1.00 32.96 C ANISOU 1101 CG TRP A 186 4847 4077 3599 89 6 -76 C ATOM 1102 CD1 TRP A 186 -83.557 22.606 -20.513 1.00 30.97 C ANISOU 1102 CD1 TRP A 186 4625 3814 3326 83 54 -156 C ATOM 1103 CD2 TRP A 186 -81.907 24.104 -20.715 1.00 33.31 C ANISOU 1103 CD2 TRP A 186 4898 4088 3670 97 0 -58 C ATOM 1104 CE2 TRP A 186 -81.917 23.621 -19.385 1.00 33.77 C ANISOU 1104 CE2 TRP A 186 4991 4122 3717 96 45 -130 C ATOM 1105 CE3 TRP A 186 -80.948 25.051 -21.084 1.00 33.54 C ANISOU 1105 CE3 TRP A 186 4905 4108 3732 103 -39 14 C ATOM 1106 NE1 TRP A 186 -82.931 22.703 -19.289 1.00 33.30 N ANISOU 1106 NE1 TRP A 186 4946 4078 3629 86 77 -184 N ATOM 1107 CZ2 TRP A 186 -80.999 24.048 -18.423 1.00 32.22 C ANISOU 1107 CZ2 TRP A 186 4807 3899 3537 103 51 -137 C ATOM 1108 CZ3 TRP A 186 -80.030 25.489 -20.112 1.00 37.41 C ANISOU 1108 CZ3 TRP A 186 5408 4561 4246 111 -31 4 C ATOM 1109 CH2 TRP A 186 -80.069 24.985 -18.799 1.00 33.00 C ANISOU 1109 CH2 TRP A 186 4883 3984 3671 112 13 -74 C ATOM 1110 N GLY A 187 -86.014 24.580 -25.006 1.00 37.28 N ANISOU 1110 N GLY A 187 5231 4713 4219 73 -135 37 N ATOM 1111 CA GLY A 187 -86.246 25.276 -26.257 1.00 47.44 C ANISOU 1111 CA GLY A 187 6464 6040 5523 66 -199 127 C ATOM 1112 C GLY A 187 -86.503 26.753 -26.047 1.00 51.58 C ANISOU 1112 C GLY A 187 6931 6488 6178 74 -260 173 C ATOM 1113 O GLY A 187 -86.120 27.580 -26.878 1.00 49.54 O ANISOU 1113 O GLY A 187 6631 6246 5945 67 -318 279 O ATOM 1114 N ASP A 188 -87.138 27.099 -24.927 1.00 61.50 N ANISOU 1114 N ASP A 188 8181 7664 7523 87 -249 94 N ATOM 1115 CA ASP A 188 -87.446 28.478 -24.540 1.00 63.94 C ANISOU 1115 CA ASP A 188 8429 7887 7978 98 -303 109 C ATOM 1116 C ASP A 188 -86.817 28.789 -23.186 1.00 61.94 C ANISOU 1116 C ASP A 188 8195 7569 7769 108 -272 48 C ATOM 1117 O ASP A 188 -87.540 29.032 -22.216 1.00 65.74 O ANISOU 1117 O ASP A 188 8658 7996 8324 116 -258 -45 O ATOM 1118 CB ASP A 188 -88.957 28.712 -24.474 1.00 64.55 C ANISOU 1118 CB ASP A 188 8460 7931 8136 103 -324 53 C ATOM 1119 CG ASP A 188 -89.504 29.359 -25.716 1.00 72.25 C ANISOU 1119 CG ASP A 188 9372 8924 9157 99 -400 149 C ATOM 1120 OD1 ASP A 188 -90.709 29.164 -25.996 1.00 77.69 O ANISOU 1120 OD1 ASP A 188 10034 9620 9864 99 -411 111 O ATOM 1121 OD2 ASP A 188 -88.737 30.063 -26.409 1.00 74.86 O1- ANISOU 1121 OD2 ASP A 188 9678 9263 9503 93 -451 265 O1- ATOM 1122 N VAL A 189 -85.489 28.765 -23.103 1.00 49.36 N ANISOU 1122 N VAL A 189 6636 5990 6130 107 -260 92 N ATOM 1123 CA VAL A 189 -84.788 29.306 -21.938 1.00 47.75 C ANISOU 1123 CA VAL A 189 6436 5725 5982 117 -245 52 C ATOM 1124 C VAL A 189 -83.528 30.010 -22.408 1.00 46.32 C ANISOU 1124 C VAL A 189 6245 5540 5814 116 -282 154 C ATOM 1125 O VAL A 189 -82.849 29.549 -23.333 1.00 54.23 O ANISOU 1125 O VAL A 189 7271 6611 6724 105 -282 230 O ATOM 1126 CB VAL A 189 -84.418 28.243 -20.877 1.00 44.37 C ANISOU 1126 CB VAL A 189 6077 5318 5463 116 -168 -36 C ATOM 1127 CG1 VAL A 189 -85.208 26.956 -21.057 1.00 37.99 C ANISOU 1127 CG1 VAL A 189 5306 4562 4565 106 -124 -85 C ATOM 1128 CG2 VAL A 189 -82.894 28.019 -20.825 1.00 39.38 C ANISOU 1128 CG2 VAL A 189 5489 4709 4764 116 -151 11 C ATOM 1129 N ASP A 190 -83.223 31.127 -21.787 1.00 41.48 N ANISOU 1129 N ASP A 190 5590 4852 5320 127 -312 150 N ATOM 1130 CA ASP A 190 -81.976 31.783 -22.117 1.00 41.59 C ANISOU 1130 CA ASP A 190 5594 4856 5351 124 -341 241 C ATOM 1131 C ASP A 190 -80.862 31.069 -21.352 1.00 44.45 C ANISOU 1131 C ASP A 190 6024 5245 5619 127 -280 199 C ATOM 1132 O ASP A 190 -80.760 31.206 -20.130 1.00 42.95 O ANISOU 1132 O ASP A 190 5840 5014 5466 137 -253 111 O ATOM 1133 CB ASP A 190 -82.049 33.267 -21.773 1.00 39.56 C ANISOU 1133 CB ASP A 190 5260 4501 5271 134 -400 254 C ATOM 1134 CG ASP A 190 -80.954 34.056 -22.422 1.00 40.39 C ANISOU 1134 CG ASP A 190 5341 4596 5410 127 -446 375 C ATOM 1135 OD1 ASP A 190 -80.092 33.428 -23.038 1.00 45.48 O ANISOU 1135 OD1 ASP A 190 6032 5316 5933 114 -426 438 O ATOM 1136 OD2 ASP A 190 -80.942 35.295 -22.334 1.00 45.80 O1- ANISOU 1136 OD2 ASP A 190 5956 5197 6247 132 -503 408 O1- ATOM 1137 N PRO A 191 -79.999 30.306 -22.030 1.00 45.44 N ANISOU 1137 N PRO A 191 6196 5444 5624 117 -260 255 N ATOM 1138 CA PRO A 191 -79.009 29.499 -21.304 1.00 42.89 C ANISOU 1138 CA PRO A 191 5938 5146 5213 120 -203 211 C ATOM 1139 C PRO A 191 -77.884 30.310 -20.694 1.00 41.70 C ANISOU 1139 C PRO A 191 5776 4950 5117 128 -214 225 C ATOM 1140 O PRO A 191 -77.116 29.762 -19.892 1.00 36.75 O ANISOU 1140 O PRO A 191 5196 4333 4434 133 -170 178 O ATOM 1141 CB PRO A 191 -78.481 28.556 -22.391 1.00 42.00 C ANISOU 1141 CB PRO A 191 5860 5122 4974 107 -188 269 C ATOM 1142 CG PRO A 191 -78.508 29.405 -23.617 1.00 42.34 C ANISOU 1142 CG PRO A 191 5848 5182 5056 94 -251 380 C ATOM 1143 CD PRO A 191 -79.752 30.283 -23.484 1.00 42.33 C ANISOU 1143 CD PRO A 191 5789 5115 5180 100 -294 368 C ATOM 1144 N THR A 192 -77.754 31.583 -21.059 1.00 43.70 N ANISOU 1144 N THR A 192 5967 5153 5484 127 -273 291 N ATOM 1145 CA THR A 192 -76.732 32.444 -20.486 1.00 46.92 C ANISOU 1145 CA THR A 192 6355 5511 5962 134 -287 301 C ATOM 1146 C THR A 192 -77.220 33.193 -19.245 1.00 46.35 C ANISOU 1146 C THR A 192 6242 5357 6012 149 -290 202 C ATOM 1147 O THR A 192 -76.403 33.758 -18.515 1.00 47.54 O ANISOU 1147 O THR A 192 6380 5469 6212 157 -289 178 O ATOM 1148 CB THR A 192 -76.240 33.425 -21.567 1.00 47.13 C ANISOU 1148 CB THR A 192 6330 5526 6052 122 -351 433 C ATOM 1149 CG2 THR A 192 -77.415 34.191 -22.182 1.00 44.74 C ANISOU 1149 CG2 THR A 192 5959 5183 5858 118 -411 475 C ATOM 1150 OG1 THR A 192 -75.283 34.346 -21.013 1.00 54.45 O ANISOU 1150 OG1 THR A 192 7229 6393 7066 128 -368 441 O ATOM 1151 N THR A 193 -78.526 33.204 -18.979 1.00 43.37 N ANISOU 1151 N THR A 193 5840 4958 5683 153 -292 137 N ATOM 1152 CA THR A 193 -79.060 34.046 -17.915 1.00 44.08 C ANISOU 1152 CA THR A 193 5872 4972 5902 164 -302 39 C ATOM 1153 C THR A 193 -79.972 33.319 -16.933 1.00 44.28 C ANISOU 1153 C THR A 193 5921 5020 5885 165 -249 -89 C ATOM 1154 O THR A 193 -80.048 33.702 -15.756 1.00 44.65 O ANISOU 1154 O THR A 193 5941 5036 5987 170 -232 -192 O ATOM 1155 CB THR A 193 -79.821 35.233 -18.510 1.00 44.46 C ANISOU 1155 CB THR A 193 5832 4947 6113 167 -376 83 C ATOM 1156 CG2 THR A 193 -78.899 36.115 -19.302 1.00 45.30 C ANISOU 1156 CG2 THR A 193 5904 5023 6284 163 -432 210 C ATOM 1157 OG1 THR A 193 -80.889 34.765 -19.336 1.00 42.06 O ANISOU 1157 OG1 THR A 193 5530 4675 5776 160 -387 112 O ATOM 1158 N ASP A 194 -80.670 32.280 -17.394 1.00 43.57 N ANISOU 1158 N ASP A 194 5874 4984 5696 156 -222 -87 N ATOM 1159 CA ASP A 194 -81.636 31.602 -16.540 1.00 41.43 C ANISOU 1159 CA ASP A 194 5619 4733 5389 151 -174 -199 C ATOM 1160 C ASP A 194 -80.935 30.944 -15.363 1.00 42.03 C ANISOU 1160 C ASP A 194 5748 4845 5379 147 -115 -266 C ATOM 1161 O ASP A 194 -79.797 30.483 -15.475 1.00 40.29 O ANISOU 1161 O ASP A 194 5577 4654 5076 148 -99 -215 O ATOM 1162 CB ASP A 194 -82.405 30.547 -17.315 1.00 42.05 C ANISOU 1162 CB ASP A 194 5736 4865 5376 142 -156 -177 C ATOM 1163 CG ASP A 194 -83.632 30.097 -16.581 1.00 46.07 C ANISOU 1163 CG ASP A 194 6241 5381 5883 135 -121 -285 C ATOM 1164 OD1 ASP A 194 -83.947 30.753 -15.558 1.00 47.34 O ANISOU 1164 OD1 ASP A 194 6357 5505 6125 137 -118 -375 O ATOM 1165 OD2 ASP A 194 -84.247 29.082 -16.989 1.00 45.54 O1- ANISOU 1165 OD2 ASP A 194 6212 5360 5733 125 -94 -287 O1- ATOM 1166 N VAL A 195 -81.620 30.905 -14.221 1.00 45.40 N ANISOU 1166 N VAL A 195 6158 5272 5822 142 -83 -382 N ATOM 1167 CA VAL A 195 -81.039 30.264 -13.046 1.00 44.98 C ANISOU 1167 CA VAL A 195 6148 5261 5679 133 -28 -442 C ATOM 1168 C VAL A 195 -81.537 28.842 -12.860 1.00 42.06 C ANISOU 1168 C VAL A 195 5844 4954 5184 115 26 -462 C ATOM 1169 O VAL A 195 -81.017 28.130 -11.988 1.00 42.32 O ANISOU 1169 O VAL A 195 5922 5029 5128 104 69 -491 O ATOM 1170 CB VAL A 195 -81.298 31.088 -11.766 1.00 43.73 C ANISOU 1170 CB VAL A 195 5929 5083 5605 131 -23 -560 C ATOM 1171 CG1 VAL A 195 -80.905 32.548 -12.006 1.00 47.39 C ANISOU 1171 CG1 VAL A 195 6315 5469 6220 149 -82 -544 C ATOM 1172 CG2 VAL A 195 -82.750 30.964 -11.291 1.00 42.00 C ANISOU 1172 CG2 VAL A 195 5675 4873 5410 118 -3 -658 C ATOM 1173 N MET A 196 -82.509 28.402 -13.656 1.00 39.02 N ANISOU 1173 N MET A 196 5461 4574 4790 111 22 -445 N ATOM 1174 CA MET A 196 -83.066 27.057 -13.542 1.00 40.10 C ANISOU 1174 CA MET A 196 5653 4763 4822 94 71 -465 C ATOM 1175 C MET A 196 -83.493 26.773 -12.102 1.00 38.14 C ANISOU 1175 C MET A 196 5404 4542 4547 74 118 -567 C ATOM 1176 O MET A 196 -82.951 25.905 -11.414 1.00 37.11 O ANISOU 1176 O MET A 196 5326 4454 4321 60 159 -571 O ATOM 1177 CB MET A 196 -82.071 26.003 -14.034 1.00 34.27 C ANISOU 1177 CB MET A 196 4988 4061 3973 94 90 -390 C ATOM 1178 CG MET A 196 -82.061 25.811 -15.536 1.00 35.86 C ANISOU 1178 CG MET A 196 5195 4267 4163 101 61 -306 C ATOM 1179 SD MET A 196 -83.698 25.667 -16.297 1.00 45.99 S ANISOU 1179 SD MET A 196 6447 5551 5478 95 49 -326 S ATOM 1180 CE MET A 196 -84.402 24.195 -15.572 1.00 34.11 C ANISOU 1180 CE MET A 196 4991 4085 3882 73 117 -395 C ATOM 1181 N ALA A 197 -84.445 27.575 -11.634 1.00 37.10 N ANISOU 1181 N ALA A 197 5204 4387 4505 70 108 -651 N ATOM 1182 CA ALA A 197 -84.977 27.372 -10.296 1.00 35.61 C ANISOU 1182 CA ALA A 197 5001 4238 4291 46 153 -758 C ATOM 1183 C ALA A 197 -85.560 25.978 -10.149 1.00 34.64 C ANISOU 1183 C ALA A 197 4935 4168 4058 19 204 -761 C ATOM 1184 O ALA A 197 -85.330 25.303 -9.141 1.00 37.74 O ANISOU 1184 O ALA A 197 5360 4614 4368 -5 248 -789 O ATOM 1185 CB ALA A 197 -86.034 28.429 -9.996 1.00 38.58 C ANISOU 1185 CB ALA A 197 5287 4581 4791 47 132 -854 C ATOM 1186 N GLU A 198 -86.305 25.530 -11.139 1.00 35.03 N ANISOU 1186 N GLU A 198 4994 4207 4109 22 195 -728 N ATOM 1187 CA GLU A 198 -86.927 24.214 -11.132 1.00 37.88 C ANISOU 1187 CA GLU A 198 5403 4608 4382 -1 239 -730 C ATOM 1188 C GLU A 198 -86.207 23.301 -12.118 1.00 37.57 C ANISOU 1188 C GLU A 198 5428 4573 4276 9 237 -632 C ATOM 1189 O GLU A 198 -86.687 23.092 -13.236 1.00 38.86 O ANISOU 1189 O GLU A 198 5589 4724 4450 18 218 -597 O ATOM 1190 CB GLU A 198 -88.414 24.343 -11.466 1.00 39.04 C ANISOU 1190 CB GLU A 198 5505 4745 4585 -8 236 -786 C ATOM 1191 CG GLU A 198 -89.215 24.956 -10.324 1.00 41.92 C ANISOU 1191 CG GLU A 198 5808 5122 4998 -27 254 -903 C ATOM 1192 CD GLU A 198 -90.387 25.802 -10.797 1.00 50.28 C ANISOU 1192 CD GLU A 198 6791 6139 6173 -16 219 -957 C ATOM 1193 OE1 GLU A 198 -90.397 26.193 -11.991 1.00 50.92 O ANISOU 1193 OE1 GLU A 198 6861 6175 6310 11 169 -892 O ATOM 1194 OE2 GLU A 198 -91.303 26.067 -9.972 1.00 52.01 O1- ANISOU 1194 OE2 GLU A 198 6959 6376 6425 -36 241 -1065 O1- ATOM 1195 N PRO A 199 -85.048 22.757 -11.758 1.00 36.40 N ANISOU 1195 N PRO A 199 5331 4443 4057 8 253 -588 N ATOM 1196 CA PRO A 199 -84.281 21.992 -12.738 1.00 34.32 C ANISOU 1196 CA PRO A 199 5116 4180 3742 21 246 -504 C ATOM 1197 C PRO A 199 -84.954 20.662 -13.001 1.00 37.74 C ANISOU 1197 C PRO A 199 5586 4636 4119 2 280 -506 C ATOM 1198 O PRO A 199 -85.644 20.115 -12.140 1.00 42.70 O ANISOU 1198 O PRO A 199 6219 5284 4721 -25 318 -556 O ATOM 1199 CB PRO A 199 -82.917 21.816 -12.061 1.00 32.84 C ANISOU 1199 CB PRO A 199 4966 4005 3507 23 256 -474 C ATOM 1200 CG PRO A 199 -83.214 21.869 -10.627 1.00 32.99 C ANISOU 1200 CG PRO A 199 4976 4050 3511 -2 287 -542 C ATOM 1201 CD PRO A 199 -84.392 22.765 -10.438 1.00 32.63 C ANISOU 1201 CD PRO A 199 4864 3992 3541 -6 279 -618 C ATOM 1202 N VAL A 200 -84.758 20.149 -14.212 1.00 36.28 N ANISOU 1202 N VAL A 200 5419 4450 3916 15 266 -453 N ATOM 1203 CA VAL A 200 -85.360 18.897 -14.644 1.00 35.38 C ANISOU 1203 CA VAL A 200 5331 4352 3761 1 293 -457 C ATOM 1204 C VAL A 200 -84.280 18.043 -15.293 1.00 35.69 C ANISOU 1204 C VAL A 200 5412 4399 3748 12 294 -399 C ATOM 1205 O VAL A 200 -83.832 18.341 -16.415 1.00 31.39 O ANISOU 1205 O VAL A 200 4856 3860 3210 31 263 -357 O ATOM 1206 CB VAL A 200 -86.520 19.132 -15.621 1.00 37.13 C ANISOU 1206 CB VAL A 200 5513 4571 4022 5 274 -475 C ATOM 1207 CG1 VAL A 200 -87.035 17.812 -16.155 1.00 33.16 C ANISOU 1207 CG1 VAL A 200 5035 4086 3479 -7 302 -481 C ATOM 1208 CG2 VAL A 200 -87.634 19.949 -14.945 1.00 35.49 C ANISOU 1208 CG2 VAL A 200 5258 4352 3876 -5 274 -544 C ATOM 1209 N GLY A 201 -83.889 16.960 -14.618 1.00 34.88 N ANISOU 1209 N GLY A 201 5352 4302 3598 -3 328 -396 N ATOM 1210 CA GLY A 201 -82.902 16.073 -15.213 1.00 29.37 C ANISOU 1210 CA GLY A 201 4688 3606 2864 7 328 -351 C ATOM 1211 C GLY A 201 -83.198 14.582 -15.232 1.00 31.22 C ANISOU 1211 C GLY A 201 4950 3840 3073 -10 360 -360 C ATOM 1212 O GLY A 201 -84.316 14.131 -14.936 1.00 28.08 O ANISOU 1212 O GLY A 201 4546 3441 2681 -32 384 -398 O ATOM 1213 N THR A 202 -82.170 13.806 -15.602 1.00 29.37 N ANISOU 1213 N THR A 202 4741 3601 2816 1 359 -327 N ATOM 1214 CA THR A 202 -82.192 12.353 -15.567 1.00 27.89 C ANISOU 1214 CA THR A 202 4578 3401 2620 -12 384 -330 C ATOM 1215 C THR A 202 -81.496 11.772 -14.348 1.00 27.96 C ANISOU 1215 C THR A 202 4622 3391 2610 -26 399 -302 C ATOM 1216 O THR A 202 -81.583 10.559 -14.122 1.00 28.15 O ANISOU 1216 O THR A 202 4663 3395 2637 -41 418 -297 O ATOM 1217 CB THR A 202 -81.518 11.778 -16.819 1.00 29.81 C ANISOU 1217 CB THR A 202 4815 3651 2859 7 371 -321 C ATOM 1218 CG2 THR A 202 -82.338 12.065 -18.040 1.00 31.91 C ANISOU 1218 CG2 THR A 202 5044 3946 3134 12 359 -348 C ATOM 1219 OG1 THR A 202 -80.204 12.355 -16.959 1.00 30.44 O ANISOU 1219 OG1 THR A 202 4902 3739 2926 29 347 -283 O ATOM 1220 N GLY A 203 -80.799 12.597 -13.583 1.00 28.15 N ANISOU 1220 N GLY A 203 4652 3422 2620 -20 388 -281 N ATOM 1221 CA GLY A 203 -79.924 12.131 -12.534 1.00 29.83 C ANISOU 1221 CA GLY A 203 4897 3628 2810 -29 394 -246 C ATOM 1222 C GLY A 203 -80.616 11.480 -11.350 1.00 29.42 C ANISOU 1222 C GLY A 203 4858 3579 2742 -68 423 -248 C ATOM 1223 O GLY A 203 -81.844 11.515 -11.207 1.00 31.05 O ANISOU 1223 O GLY A 203 5048 3796 2954 -91 442 -285 O ATOM 1224 N PRO A 204 -79.813 10.899 -10.455 1.00 33.49 N ANISOU 1224 N PRO A 204 5400 4089 3234 -79 424 -204 N ATOM 1225 CA PRO A 204 -80.380 10.105 -9.356 1.00 28.85 C ANISOU 1225 CA PRO A 204 4825 3509 2626 -122 450 -187 C ATOM 1226 C PRO A 204 -81.225 10.907 -8.382 1.00 32.33 C ANISOU 1226 C PRO A 204 5247 4000 3039 -153 468 -222 C ATOM 1227 O PRO A 204 -81.966 10.291 -7.602 1.00 35.29 O ANISOU 1227 O PRO A 204 5623 4392 3393 -196 494 -218 O ATOM 1228 CB PRO A 204 -79.132 9.543 -8.667 1.00 28.99 C ANISOU 1228 CB PRO A 204 4871 3517 2625 -122 436 -123 C ATOM 1229 CG PRO A 204 -78.069 10.562 -8.963 1.00 28.62 C ANISOU 1229 CG PRO A 204 4822 3479 2574 -84 410 -125 C ATOM 1230 CD PRO A 204 -78.349 11.027 -10.351 1.00 29.99 C ANISOU 1230 CD PRO A 204 4975 3640 2781 -54 401 -163 C ATOM 1231 N TYR A 205 -81.140 12.249 -8.397 1.00 29.24 N ANISOU 1231 N TYR A 205 4831 3631 2647 -134 456 -259 N ATOM 1232 CA TYR A 205 -81.828 13.106 -7.434 1.00 32.50 C ANISOU 1232 CA TYR A 205 5216 4092 3041 -160 471 -307 C ATOM 1233 C TYR A 205 -82.615 14.205 -8.132 1.00 33.32 C ANISOU 1233 C TYR A 205 5278 4191 3189 -142 463 -371 C ATOM 1234 O TYR A 205 -82.313 14.573 -9.272 1.00 35.80 O ANISOU 1234 O TYR A 205 5588 4474 3541 -105 437 -365 O ATOM 1235 CB TYR A 205 -80.855 13.759 -6.447 1.00 29.48 C ANISOU 1235 CB TYR A 205 4833 3744 2622 -160 461 -295 C ATOM 1236 CG TYR A 205 -80.230 12.747 -5.520 1.00 29.59 C ANISOU 1236 CG TYR A 205 4880 3776 2586 -188 468 -231 C ATOM 1237 CD1 TYR A 205 -80.849 12.388 -4.329 1.00 30.95 C ANISOU 1237 CD1 TYR A 205 5047 4005 2709 -241 496 -232 C ATOM 1238 CD2 TYR A 205 -79.029 12.133 -5.851 1.00 29.29 C ANISOU 1238 CD2 TYR A 205 4876 3702 2553 -163 446 -168 C ATOM 1239 CE1 TYR A 205 -80.285 11.444 -3.477 1.00 32.72 C ANISOU 1239 CE1 TYR A 205 5298 4248 2888 -270 497 -159 C ATOM 1240 CE2 TYR A 205 -78.453 11.204 -5.019 1.00 29.64 C ANISOU 1240 CE2 TYR A 205 4946 3755 2561 -187 446 -102 C ATOM 1241 CZ TYR A 205 -79.078 10.856 -3.833 1.00 33.90 C ANISOU 1241 CZ TYR A 205 5480 4349 3051 -241 470 -92 C ATOM 1242 OH TYR A 205 -78.485 9.913 -3.016 1.00 32.46 O ANISOU 1242 OH TYR A 205 5322 4178 2835 -267 464 -12 O ATOM 1243 N VAL A 206 -83.635 14.713 -7.441 1.00 30.30 N ANISOU 1243 N VAL A 206 4862 3845 2805 -170 483 -431 N ATOM 1244 CA VAL A 206 -84.349 15.905 -7.861 1.00 29.17 C ANISOU 1244 CA VAL A 206 4671 3699 2715 -154 471 -496 C ATOM 1245 C VAL A 206 -84.112 16.999 -6.833 1.00 31.60 C ANISOU 1245 C VAL A 206 4944 4044 3018 -161 468 -542 C ATOM 1246 O VAL A 206 -83.569 16.769 -5.757 1.00 34.56 O ANISOU 1246 O VAL A 206 5332 4461 3338 -185 482 -528 O ATOM 1247 CB VAL A 206 -85.861 15.663 -8.043 1.00 33.27 C ANISOU 1247 CB VAL A 206 5165 4222 3253 -178 494 -549 C ATOM 1248 CG1 VAL A 206 -86.134 14.606 -9.098 1.00 37.32 C ANISOU 1248 CG1 VAL A 206 5704 4699 3775 -170 496 -515 C ATOM 1249 CG2 VAL A 206 -86.505 15.285 -6.725 1.00 33.67 C ANISOU 1249 CG2 VAL A 206 5208 4329 3256 -231 534 -579 C ATOM 1250 N LEU A 207 -84.550 18.204 -7.167 1.00 32.70 N ANISOU 1250 N LEU A 207 5034 4170 3222 -141 448 -599 N ATOM 1251 CA LEU A 207 -84.509 19.309 -6.222 1.00 32.30 C ANISOU 1251 CA LEU A 207 4935 4152 3187 -148 447 -664 C ATOM 1252 C LEU A 207 -85.699 19.194 -5.287 1.00 32.85 C ANISOU 1252 C LEU A 207 4970 4276 3234 -195 485 -740 C ATOM 1253 O LEU A 207 -86.825 19.486 -5.684 1.00 33.29 O ANISOU 1253 O LEU A 207 4990 4319 3341 -197 487 -795 O ATOM 1254 CB LEU A 207 -84.514 20.647 -6.951 1.00 34.08 C ANISOU 1254 CB LEU A 207 5113 4331 3507 -110 406 -695 C ATOM 1255 CG LEU A 207 -84.578 21.865 -6.022 1.00 33.55 C ANISOU 1255 CG LEU A 207 4980 4287 3479 -115 402 -781 C ATOM 1256 CD1 LEU A 207 -83.285 22.060 -5.233 1.00 31.70 C ANISOU 1256 CD1 LEU A 207 4760 4080 3203 -113 399 -761 C ATOM 1257 CD2 LEU A 207 -84.912 23.102 -6.841 1.00 32.00 C ANISOU 1257 CD2 LEU A 207 4727 4030 3399 -80 359 -811 C ATOM 1258 N GLY A 208 -85.456 18.764 -4.047 1.00 34.24 N ANISOU 1258 N GLY A 208 5155 4521 3332 -235 514 -742 N ATOM 1259 CA GLY A 208 -86.516 18.651 -3.063 1.00 31.16 C ANISOU 1259 CA GLY A 208 4729 4202 2908 -288 554 -814 C ATOM 1260 C GLY A 208 -86.976 19.986 -2.506 1.00 32.88 C ANISOU 1260 C GLY A 208 4867 4451 3175 -289 552 -931 C ATOM 1261 O GLY A 208 -88.175 20.255 -2.460 1.00 38.61 O ANISOU 1261 O GLY A 208 5545 5189 3936 -307 568 -1011 O ATOM 1262 N GLU A 209 -86.042 20.840 -2.097 1.00 33.47 N ANISOU 1262 N GLU A 209 4920 4534 3262 -270 531 -948 N ATOM 1263 CA GLU A 209 -86.403 22.102 -1.471 1.00 36.75 C ANISOU 1263 CA GLU A 209 5251 4980 3733 -273 528 -1070 C ATOM 1264 C GLU A 209 -85.177 22.998 -1.431 1.00 38.43 C ANISOU 1264 C GLU A 209 5451 5168 3982 -237 493 -1064 C ATOM 1265 O GLU A 209 -84.076 22.534 -1.106 1.00 34.32 O ANISOU 1265 O GLU A 209 4979 4669 3392 -237 492 -993 O ATOM 1266 CB GLU A 209 -86.930 21.886 -0.046 1.00 43.74 C ANISOU 1266 CB GLU A 209 6100 5985 4535 -337 575 -1143 C ATOM 1267 CG GLU A 209 -87.117 23.169 0.748 1.00 43.02 C ANISOU 1267 CG GLU A 209 5913 5939 4491 -343 575 -1281 C ATOM 1268 CD GLU A 209 -88.509 23.752 0.578 1.00 46.69 C ANISOU 1268 CD GLU A 209 6306 6394 5041 -349 582 -1395 C ATOM 1269 OE1 GLU A 209 -89.474 22.971 0.659 1.00 49.65 O ANISOU 1269 OE1 GLU A 209 6692 6803 5371 -387 616 -1398 O ATOM 1270 OE2 GLU A 209 -88.646 24.979 0.364 1.00 49.06 O1- ANISOU 1270 OE2 GLU A 209 6535 6647 5460 -317 552 -1481 O1- ATOM 1271 N PHE A 210 -85.385 24.277 -1.744 1.00 38.65 N ANISOU 1271 N PHE A 210 5412 5148 4127 -206 462 -1139 N ATOM 1272 CA PHE A 210 -84.340 25.289 -1.717 1.00 34.17 C ANISOU 1272 CA PHE A 210 4817 4549 3618 -172 427 -1148 C ATOM 1273 C PHE A 210 -84.635 26.274 -0.604 1.00 34.62 C ANISOU 1273 C PHE A 210 4781 4665 3708 -192 438 -1289 C ATOM 1274 O PHE A 210 -85.763 26.767 -0.493 1.00 39.62 O ANISOU 1274 O PHE A 210 5346 5301 4406 -204 445 -1390 O ATOM 1275 CB PHE A 210 -84.232 26.052 -3.046 1.00 35.05 C ANISOU 1275 CB PHE A 210 4916 4547 3853 -119 375 -1112 C ATOM 1276 CG PHE A 210 -83.323 27.261 -2.973 1.00 33.21 C ANISOU 1276 CG PHE A 210 4638 4277 3705 -87 337 -1137 C ATOM 1277 CD1 PHE A 210 -81.970 27.134 -3.231 1.00 32.87 C ANISOU 1277 CD1 PHE A 210 4645 4214 3631 -65 318 -1047 C ATOM 1278 CD2 PHE A 210 -83.811 28.506 -2.610 1.00 34.98 C ANISOU 1278 CD2 PHE A 210 4763 4484 4044 -82 320 -1255 C ATOM 1279 CE1 PHE A 210 -81.120 28.210 -3.137 1.00 32.27 C ANISOU 1279 CE1 PHE A 210 4526 4105 3632 -39 286 -1069 C ATOM 1280 CE2 PHE A 210 -82.961 29.590 -2.498 1.00 35.52 C ANISOU 1280 CE2 PHE A 210 4785 4515 4197 -56 286 -1280 C ATOM 1281 CZ PHE A 210 -81.613 29.441 -2.771 1.00 36.04 C ANISOU 1281 CZ PHE A 210 4905 4562 4225 -35 269 -1184 C ATOM 1282 N LYS A 211 -83.615 26.577 0.188 1.00 32.95 N ANISOU 1282 N LYS A 211 4561 4500 3459 -195 437 -1302 N ATOM 1283 CA LYS A 211 -83.649 27.656 1.156 1.00 34.29 C ANISOU 1283 CA LYS A 211 4634 4719 3674 -206 440 -1441 C ATOM 1284 C LYS A 211 -82.241 28.220 1.197 1.00 34.81 C ANISOU 1284 C LYS A 211 4704 4759 3762 -174 408 -1409 C ATOM 1285 O LYS A 211 -81.273 27.478 0.982 1.00 33.41 O ANISOU 1285 O LYS A 211 4609 4579 3507 -166 405 -1291 O ATOM 1286 CB LYS A 211 -84.114 27.188 2.552 1.00 34.33 C ANISOU 1286 CB LYS A 211 4611 4871 3560 -271 493 -1519 C ATOM 1287 CG LYS A 211 -85.618 26.859 2.602 1.00 37.69 C ANISOU 1287 CG LYS A 211 5009 5327 3984 -306 525 -1582 C ATOM 1288 CD LYS A 211 -86.293 27.217 3.922 1.00 38.63 C ANISOU 1288 CD LYS A 211 5037 5577 4064 -361 566 -1736 C ATOM 1289 CE LYS A 211 -87.793 26.877 3.873 1.00 50.37 C ANISOU 1289 CE LYS A 211 6497 7087 5556 -394 597 -1795 C ATOM 1290 NZ LYS A 211 -88.566 27.553 2.758 1.00 49.16 N1+ ANISOU 1290 NZ LYS A 211 6309 6805 5564 -348 561 -1827 N1+ ATOM 1291 N PRO A 212 -82.090 29.525 1.411 1.00 33.91 N ANISOU 1291 N PRO A 212 4502 4617 3766 -154 383 -1510 N ATOM 1292 CA PRO A 212 -80.752 30.131 1.306 1.00 33.73 C ANISOU 1292 CA PRO A 212 4481 4552 3783 -120 349 -1476 C ATOM 1293 C PRO A 212 -79.752 29.603 2.314 1.00 35.88 C ANISOU 1293 C PRO A 212 4787 4927 3919 -144 373 -1457 C ATOM 1294 O PRO A 212 -78.540 29.741 2.091 1.00 35.95 O ANISOU 1294 O PRO A 212 4827 4901 3930 -116 348 -1390 O ATOM 1295 CB PRO A 212 -81.038 31.616 1.510 1.00 34.72 C ANISOU 1295 CB PRO A 212 4487 4635 4068 -103 323 -1614 C ATOM 1296 CG PRO A 212 -82.477 31.754 1.050 1.00 34.57 C ANISOU 1296 CG PRO A 212 4429 4579 4128 -107 323 -1666 C ATOM 1297 CD PRO A 212 -83.157 30.527 1.526 1.00 34.54 C ANISOU 1297 CD PRO A 212 4475 4675 3973 -155 376 -1652 C ATOM 1298 N GLN A 213 -80.221 29.015 3.423 1.00 36.96 N ANISOU 1298 N GLN A 213 4913 5193 3936 -199 419 -1511 N ATOM 1299 CA GLN A 213 -79.350 28.359 4.389 1.00 34.83 C ANISOU 1299 CA GLN A 213 4679 5032 3521 -229 440 -1475 C ATOM 1300 C GLN A 213 -79.021 26.930 4.002 1.00 33.84 C ANISOU 1300 C GLN A 213 4668 4906 3283 -237 449 -1315 C ATOM 1301 O GLN A 213 -77.961 26.426 4.386 1.00 33.72 O ANISOU 1301 O GLN A 213 4701 4930 3182 -240 446 -1242 O ATOM 1302 CB GLN A 213 -80.002 28.396 5.773 1.00 37.16 C ANISOU 1302 CB GLN A 213 4904 5481 3735 -290 483 -1602 C ATOM 1303 CG GLN A 213 -81.482 28.625 5.721 1.00 38.86 C ANISOU 1303 CG GLN A 213 5060 5700 4005 -311 504 -1700 C ATOM 1304 CD GLN A 213 -81.848 29.944 6.366 1.00 43.05 C ANISOU 1304 CD GLN A 213 5460 6262 4634 -315 503 -1890 C ATOM 1305 NE2 GLN A 213 -82.981 29.978 7.043 1.00 41.88 N ANISOU 1305 NE2 GLN A 213 5244 6206 4463 -362 540 -2010 N ATOM 1306 OE1 GLN A 213 -81.114 30.921 6.255 1.00 39.61 O ANISOU 1306 OE1 GLN A 213 4981 5769 4301 -276 469 -1932 O ATOM 1307 N ALA A 214 -79.897 26.288 3.231 1.00 34.92 N ANISOU 1307 N ALA A 214 4846 4994 3430 -238 457 -1263 N ATOM 1308 CA ALA A 214 -79.757 24.902 2.814 1.00 33.01 C ANISOU 1308 CA ALA A 214 4702 4742 3099 -247 466 -1125 C ATOM 1309 C ALA A 214 -80.740 24.620 1.691 1.00 32.70 C ANISOU 1309 C ALA A 214 4685 4618 3123 -232 464 -1097 C ATOM 1310 O ALA A 214 -81.902 25.034 1.757 1.00 32.97 O ANISOU 1310 O ALA A 214 4661 4661 3205 -248 478 -1189 O ATOM 1311 CB ALA A 214 -80.015 23.939 3.984 1.00 33.76 C ANISOU 1311 CB ALA A 214 4811 4969 3047 -312 508 -1115 C ATOM 1312 N PHE A 215 -80.272 23.921 0.669 1.00 33.58 N ANISOU 1312 N PHE A 215 4872 4652 3234 -203 445 -977 N ATOM 1313 CA PHE A 215 -81.159 23.289 -0.288 1.00 31.61 C ANISOU 1313 CA PHE A 215 4656 4347 3008 -199 450 -934 C ATOM 1314 C PHE A 215 -80.929 21.796 -0.184 1.00 31.44 C ANISOU 1314 C PHE A 215 4713 4353 2881 -224 470 -830 C ATOM 1315 O PHE A 215 -79.845 21.353 0.215 1.00 31.38 O ANISOU 1315 O PHE A 215 4744 4369 2810 -224 464 -765 O ATOM 1316 CB PHE A 215 -80.931 23.801 -1.724 1.00 32.53 C ANISOU 1316 CB PHE A 215 4781 4348 3230 -143 408 -892 C ATOM 1317 CG PHE A 215 -79.681 23.277 -2.370 1.00 32.02 C ANISOU 1317 CG PHE A 215 4785 4240 3140 -114 386 -778 C ATOM 1318 CD1 PHE A 215 -79.660 22.027 -2.968 1.00 30.13 C ANISOU 1318 CD1 PHE A 215 4616 3984 2850 -116 394 -687 C ATOM 1319 CD2 PHE A 215 -78.529 24.036 -2.381 1.00 33.31 C ANISOU 1319 CD2 PHE A 215 4937 4382 3338 -84 357 -770 C ATOM 1320 CE1 PHE A 215 -78.535 21.553 -3.534 1.00 29.70 C ANISOU 1320 CE1 PHE A 215 4615 3894 2777 -90 375 -597 C ATOM 1321 CE2 PHE A 215 -77.383 23.549 -2.976 1.00 35.14 C ANISOU 1321 CE2 PHE A 215 5227 4578 3545 -58 338 -671 C ATOM 1322 CZ PHE A 215 -77.394 22.307 -3.553 1.00 29.59 C ANISOU 1322 CZ PHE A 215 4590 3861 2791 -61 347 -588 C ATOM 1323 N THR A 216 -81.962 21.015 -0.488 1.00 31.44 N ANISOU 1323 N THR A 216 4731 4350 2866 -247 493 -816 N ATOM 1324 CA THR A 216 -81.875 19.570 -0.304 1.00 31.42 C ANISOU 1324 CA THR A 216 4793 4370 2775 -277 513 -724 C ATOM 1325 C THR A 216 -82.344 18.865 -1.567 1.00 32.58 C ANISOU 1325 C THR A 216 4981 4435 2963 -256 508 -668 C ATOM 1326 O THR A 216 -83.452 19.120 -2.061 1.00 35.55 O ANISOU 1326 O THR A 216 5328 4788 3391 -256 515 -721 O ATOM 1327 CB THR A 216 -82.645 19.105 0.951 1.00 32.13 C ANISOU 1327 CB THR A 216 4860 4571 2778 -346 556 -761 C ATOM 1328 CG2 THR A 216 -83.587 20.156 1.459 1.00 32.62 C ANISOU 1328 CG2 THR A 216 4837 4682 2875 -364 573 -898 C ATOM 1329 OG1 THR A 216 -83.365 17.895 0.677 1.00 37.30 O ANISOU 1329 OG1 THR A 216 5554 5214 3403 -373 578 -703 O ATOM 1330 N LEU A 217 -81.465 18.038 -2.124 1.00 30.55 N ANISOU 1330 N LEU A 217 4785 4133 2688 -235 492 -568 N ATOM 1331 CA LEU A 217 -81.809 17.165 -3.234 1.00 31.98 C ANISOU 1331 CA LEU A 217 5007 4250 2896 -221 490 -514 C ATOM 1332 C LEU A 217 -82.356 15.857 -2.667 1.00 32.91 C ANISOU 1332 C LEU A 217 5151 4402 2950 -271 522 -475 C ATOM 1333 O LEU A 217 -81.983 15.430 -1.570 1.00 34.18 O ANISOU 1333 O LEU A 217 5322 4626 3040 -307 535 -445 O ATOM 1334 CB LEU A 217 -80.586 16.904 -4.114 1.00 29.67 C ANISOU 1334 CB LEU A 217 4757 3896 2621 -176 457 -438 C ATOM 1335 CG LEU A 217 -79.883 18.164 -4.628 1.00 29.39 C ANISOU 1335 CG LEU A 217 4695 3828 2643 -131 423 -461 C ATOM 1336 CD1 LEU A 217 -78.523 17.864 -5.232 1.00 29.00 C ANISOU 1336 CD1 LEU A 217 4686 3739 2592 -96 397 -386 C ATOM 1337 CD2 LEU A 217 -80.763 18.866 -5.637 1.00 30.76 C ANISOU 1337 CD2 LEU A 217 4834 3958 2894 -110 411 -504 C ATOM 1338 N SER A 218 -83.274 15.242 -3.403 1.00 30.43 N ANISOU 1338 N SER A 218 4846 4051 2664 -275 534 -473 N ATOM 1339 CA SER A 218 -83.978 14.062 -2.931 1.00 33.59 C ANISOU 1339 CA SER A 218 5263 4477 3021 -325 566 -442 C ATOM 1340 C SER A 218 -83.942 12.993 -4.003 1.00 34.07 C ANISOU 1340 C SER A 218 5365 4464 3116 -306 558 -382 C ATOM 1341 O SER A 218 -83.928 13.301 -5.197 1.00 32.72 O ANISOU 1341 O SER A 218 5194 4236 3003 -262 538 -395 O ATOM 1342 CB SER A 218 -85.432 14.369 -2.569 1.00 31.36 C ANISOU 1342 CB SER A 218 4935 4239 2740 -362 598 -526 C ATOM 1343 OG SER A 218 -85.462 15.401 -1.621 1.00 35.36 O ANISOU 1343 OG SER A 218 5394 4818 3225 -379 605 -599 O ATOM 1344 N ALA A 219 -83.918 11.734 -3.560 1.00 31.70 N ANISOU 1344 N ALA A 219 5095 4167 2781 -341 573 -315 N ATOM 1345 CA ALA A 219 -83.773 10.636 -4.499 1.00 32.93 C ANISOU 1345 CA ALA A 219 5284 4249 2977 -324 564 -261 C ATOM 1346 C ALA A 219 -84.910 10.641 -5.511 1.00 35.88 C ANISOU 1346 C ALA A 219 5640 4590 3404 -314 575 -317 C ATOM 1347 O ALA A 219 -86.077 10.838 -5.161 1.00 33.18 O ANISOU 1347 O ALA A 219 5269 4283 3055 -347 602 -371 O ATOM 1348 CB ALA A 219 -83.714 9.301 -3.768 1.00 31.14 C ANISOU 1348 CB ALA A 219 5083 4028 2720 -370 577 -182 C ATOM 1349 N ASN A 220 -84.543 10.490 -6.782 1.00 36.31 N ANISOU 1349 N ASN A 220 5706 4583 3508 -268 552 -309 N ATOM 1350 CA ASN A 220 -85.470 10.132 -7.846 1.00 38.96 C ANISOU 1350 CA ASN A 220 6029 4883 3890 -259 559 -344 C ATOM 1351 C ASN A 220 -85.625 8.618 -7.819 1.00 40.33 C ANISOU 1351 C ASN A 220 6225 5024 4073 -286 574 -297 C ATOM 1352 O ASN A 220 -84.674 7.888 -8.117 1.00 39.81 O ANISOU 1352 O ASN A 220 6186 4919 4023 -268 556 -243 O ATOM 1353 CB ASN A 220 -84.935 10.640 -9.190 1.00 37.84 C ANISOU 1353 CB ASN A 220 5884 4706 3787 -204 526 -353 C ATOM 1354 CG ASN A 220 -85.553 9.940 -10.400 1.00 36.95 C ANISOU 1354 CG ASN A 220 5765 4557 3716 -192 528 -371 C ATOM 1355 ND2 ASN A 220 -84.708 9.670 -11.380 1.00 38.49 N ANISOU 1355 ND2 ASN A 220 5971 4724 3931 -157 505 -349 N ATOM 1356 OD1 ASN A 220 -86.763 9.676 -10.473 1.00 30.09 O ANISOU 1356 OD1 ASN A 220 4878 3693 2862 -216 550 -411 O ATOM 1357 N GLU A 221 -86.817 8.142 -7.442 1.00 41.57 N ANISOU 1357 N GLU A 221 6369 5198 4229 -330 606 -319 N ATOM 1358 CA GLU A 221 -87.054 6.702 -7.342 1.00 45.38 C ANISOU 1358 CA GLU A 221 6866 5644 4731 -362 621 -272 C ATOM 1359 C GLU A 221 -87.208 6.016 -8.699 1.00 46.40 C ANISOU 1359 C GLU A 221 6994 5710 4927 -331 612 -290 C ATOM 1360 O GLU A 221 -87.231 4.782 -8.743 1.00 50.25 O ANISOU 1360 O GLU A 221 7490 6154 5449 -349 618 -253 O ATOM 1361 CB GLU A 221 -88.295 6.421 -6.496 1.00 43.71 C ANISOU 1361 CB GLU A 221 6637 5475 4496 -424 660 -289 C ATOM 1362 CG GLU A 221 -88.202 6.896 -5.072 1.00 44.02 C ANISOU 1362 CG GLU A 221 6672 5592 4462 -466 674 -272 C ATOM 1363 CD GLU A 221 -87.196 6.105 -4.232 1.00 49.28 C ANISOU 1363 CD GLU A 221 7368 6258 5097 -490 662 -168 C ATOM 1364 OE1 GLU A 221 -87.317 4.850 -4.146 1.00 48.72 O ANISOU 1364 OE1 GLU A 221 7311 6149 5053 -519 668 -106 O ATOM 1365 OE2 GLU A 221 -86.284 6.746 -3.644 1.00 46.76 O1- ANISOU 1365 OE2 GLU A 221 7056 5977 4732 -479 645 -149 O1- ATOM 1366 N ASP A 222 -87.325 6.765 -9.795 1.00 50.74 N ANISOU 1366 N ASP A 222 7526 6257 5497 -288 597 -346 N ATOM 1367 CA ASP A 222 -87.325 6.196 -11.136 1.00 49.72 C ANISOU 1367 CA ASP A 222 7389 6084 5419 -257 585 -367 C ATOM 1368 C ASP A 222 -85.993 6.390 -11.857 1.00 49.14 C ANISOU 1368 C ASP A 222 7327 5992 5350 -209 551 -344 C ATOM 1369 O ASP A 222 -85.953 6.324 -13.093 1.00 47.97 O ANISOU 1369 O ASP A 222 7164 5833 5231 -178 538 -376 O ATOM 1370 CB ASP A 222 -88.449 6.802 -11.969 1.00 53.38 C ANISOU 1370 CB ASP A 222 7818 6565 5898 -247 590 -441 C ATOM 1371 CG ASP A 222 -89.808 6.473 -11.429 1.00 59.00 C ANISOU 1371 CG ASP A 222 8513 7289 6614 -292 625 -474 C ATOM 1372 OD1 ASP A 222 -90.177 5.282 -11.498 1.00 59.81 O ANISOU 1372 OD1 ASP A 222 8618 7359 6748 -315 642 -465 O ATOM 1373 OD2 ASP A 222 -90.501 7.398 -10.936 1.00 61.79 O1- ANISOU 1373 OD2 ASP A 222 8848 7685 6945 -305 635 -512 O1- ATOM 1374 N TYR A 223 -84.915 6.643 -11.113 1.00 40.49 N ANISOU 1374 N TYR A 223 6256 4904 4226 -205 537 -292 N ATOM 1375 CA TYR A 223 -83.603 6.824 -11.719 1.00 37.13 C ANISOU 1375 CA TYR A 223 5840 4463 3803 -163 507 -270 C ATOM 1376 C TYR A 223 -83.159 5.539 -12.395 1.00 36.67 C ANISOU 1376 C TYR A 223 5784 4353 3795 -153 501 -259 C ATOM 1377 O TYR A 223 -83.151 4.475 -11.770 1.00 36.23 O ANISOU 1377 O TYR A 223 5740 4263 3764 -180 510 -221 O ATOM 1378 CB TYR A 223 -82.573 7.247 -10.667 1.00 34.53 C ANISOU 1378 CB TYR A 223 5534 4150 3435 -164 495 -218 C ATOM 1379 CG TYR A 223 -81.176 7.376 -11.214 1.00 31.38 C ANISOU 1379 CG TYR A 223 5146 3735 3043 -123 464 -194 C ATOM 1380 CD1 TYR A 223 -80.942 8.091 -12.390 1.00 33.02 C ANISOU 1380 CD1 TYR A 223 5336 3952 3258 -86 447 -228 C ATOM 1381 CD2 TYR A 223 -80.092 6.785 -10.576 1.00 29.30 C ANISOU 1381 CD2 TYR A 223 4906 3449 2776 -124 451 -134 C ATOM 1382 CE1 TYR A 223 -79.671 8.211 -12.929 1.00 29.82 C ANISOU 1382 CE1 TYR A 223 4936 3539 2855 -52 422 -208 C ATOM 1383 CE2 TYR A 223 -78.811 6.914 -11.085 1.00 30.01 C ANISOU 1383 CE2 TYR A 223 5003 3527 2874 -86 424 -119 C ATOM 1384 CZ TYR A 223 -78.611 7.630 -12.272 1.00 31.27 C ANISOU 1384 CZ TYR A 223 5143 3699 3038 -51 412 -159 C ATOM 1385 OH TYR A 223 -77.364 7.774 -12.814 1.00 29.68 O ANISOU 1385 OH TYR A 223 4943 3493 2840 -18 388 -147 O ATOM 1386 N TRP A 224 -82.774 5.652 -13.677 1.00 33.66 N ANISOU 1386 N TRP A 224 5386 3970 3433 -116 484 -292 N ATOM 1387 CA TRP A 224 -82.348 4.485 -14.442 1.00 33.24 C ANISOU 1387 CA TRP A 224 5323 3875 3433 -103 478 -302 C ATOM 1388 C TRP A 224 -81.268 3.693 -13.708 1.00 35.28 C ANISOU 1388 C TRP A 224 5604 4089 3713 -106 466 -241 C ATOM 1389 O TRP A 224 -81.173 2.472 -13.871 1.00 36.89 O ANISOU 1389 O TRP A 224 5799 4239 3978 -111 466 -240 O ATOM 1390 CB TRP A 224 -81.850 4.911 -15.829 1.00 30.69 C ANISOU 1390 CB TRP A 224 4975 3578 3107 -65 459 -343 C ATOM 1391 CG TRP A 224 -80.588 5.729 -15.817 1.00 29.43 C ANISOU 1391 CG TRP A 224 4828 3439 2913 -37 434 -311 C ATOM 1392 CD1 TRP A 224 -80.492 7.076 -15.993 1.00 28.91 C ANISOU 1392 CD1 TRP A 224 4760 3419 2806 -23 422 -309 C ATOM 1393 CD2 TRP A 224 -79.233 5.250 -15.653 1.00 29.04 C ANISOU 1393 CD2 TRP A 224 4793 3362 2879 -21 417 -277 C ATOM 1394 CE2 TRP A 224 -78.384 6.372 -15.725 1.00 28.63 C ANISOU 1394 CE2 TRP A 224 4748 3346 2785 1 398 -258 C ATOM 1395 CE3 TRP A 224 -78.663 3.990 -15.447 1.00 29.37 C ANISOU 1395 CE3 TRP A 224 4837 3348 2973 -23 413 -262 C ATOM 1396 NE1 TRP A 224 -79.178 7.470 -15.930 1.00 28.40 N ANISOU 1396 NE1 TRP A 224 4708 3358 2725 -1 401 -275 N ATOM 1397 CZ2 TRP A 224 -76.999 6.271 -15.587 1.00 28.60 C ANISOU 1397 CZ2 TRP A 224 4755 3329 2782 21 378 -227 C ATOM 1398 CZ3 TRP A 224 -77.289 3.891 -15.319 1.00 29.35 C ANISOU 1398 CZ3 TRP A 224 4845 3330 2977 -1 391 -231 C ATOM 1399 CH2 TRP A 224 -76.474 5.020 -15.390 1.00 28.95 C ANISOU 1399 CH2 TRP A 224 4803 3321 2876 21 375 -216 C ATOM 1400 N GLY A 225 -80.458 4.362 -12.881 1.00 35.49 N ANISOU 1400 N GLY A 225 5656 4133 3696 -102 453 -192 N ATOM 1401 CA GLY A 225 -79.482 3.691 -12.050 1.00 33.35 C ANISOU 1401 CA GLY A 225 5407 3826 3439 -107 438 -126 C ATOM 1402 C GLY A 225 -80.052 2.976 -10.856 1.00 31.28 C ANISOU 1402 C GLY A 225 5158 3546 3182 -155 453 -74 C ATOM 1403 O GLY A 225 -79.299 2.401 -10.069 1.00 31.06 O ANISOU 1403 O GLY A 225 5147 3491 3164 -165 437 -6 O ATOM 1404 N GLY A 226 -81.374 2.967 -10.717 1.00 35.45 N ANISOU 1404 N GLY A 226 5676 4091 3703 -187 481 -101 N ATOM 1405 CA GLY A 226 -82.026 2.515 -9.503 1.00 36.67 C ANISOU 1405 CA GLY A 226 5840 4251 3842 -241 500 -51 C ATOM 1406 C GLY A 226 -82.041 3.597 -8.439 1.00 36.01 C ANISOU 1406 C GLY A 226 5769 4239 3673 -260 507 -33 C ATOM 1407 O GLY A 226 -81.226 4.522 -8.468 1.00 35.09 O ANISOU 1407 O GLY A 226 5660 4150 3522 -229 489 -37 O ATOM 1408 N ALA A 227 -82.961 3.496 -7.495 1.00 42.89 N ANISOU 1408 N ALA A 227 6638 5145 4512 -312 533 -17 N ATOM 1409 CA ALA A 227 -82.986 4.447 -6.398 1.00 38.84 C ANISOU 1409 CA ALA A 227 6129 4710 3918 -336 541 -8 C ATOM 1410 C ALA A 227 -81.656 4.416 -5.648 1.00 36.84 C ANISOU 1410 C ALA A 227 5897 4463 3636 -331 514 66 C ATOM 1411 O ALA A 227 -81.092 3.334 -5.427 1.00 31.92 O ANISOU 1411 O ALA A 227 5288 3792 3048 -340 497 138 O ATOM 1412 CB ALA A 227 -84.135 4.130 -5.445 1.00 39.14 C ANISOU 1412 CB ALA A 227 6156 4790 3925 -403 576 3 C ATOM 1413 N PRO A 228 -81.106 5.579 -5.289 1.00 37.40 N ANISOU 1413 N PRO A 228 5970 4589 3653 -313 505 47 N ATOM 1414 CA PRO A 228 -79.965 5.617 -4.364 1.00 35.25 C ANISOU 1414 CA PRO A 228 5714 4341 3339 -317 482 115 C ATOM 1415 C PRO A 228 -80.393 5.322 -2.935 1.00 34.94 C ANISOU 1415 C PRO A 228 5673 4367 3236 -384 499 168 C ATOM 1416 O PRO A 228 -81.516 5.613 -2.530 1.00 35.74 O ANISOU 1416 O PRO A 228 5755 4522 3304 -424 532 128 O ATOM 1417 CB PRO A 228 -79.451 7.057 -4.485 1.00 32.16 C ANISOU 1417 CB PRO A 228 5315 3990 2913 -281 473 60 C ATOM 1418 CG PRO A 228 -80.671 7.852 -4.854 1.00 36.04 C ANISOU 1418 CG PRO A 228 5779 4509 3404 -286 500 -25 C ATOM 1419 CD PRO A 228 -81.491 6.924 -5.755 1.00 36.53 C ANISOU 1419 CD PRO A 228 5840 4514 3526 -288 512 -37 C ATOM 1420 N ALA A 229 -79.471 4.732 -2.171 1.00 34.10 N ANISOU 1420 N ALA A 229 5584 4261 3113 -398 475 259 N ATOM 1421 CA ALA A 229 -79.743 4.442 -0.768 1.00 33.98 C ANISOU 1421 CA ALA A 229 5563 4321 3024 -466 485 325 C ATOM 1422 C ALA A 229 -79.942 5.723 0.049 1.00 37.63 C ANISOU 1422 C ALA A 229 6005 4898 3393 -485 504 267 C ATOM 1423 O ALA A 229 -80.940 5.857 0.773 1.00 35.58 O ANISOU 1423 O ALA A 229 5723 4715 3079 -541 538 247 O ATOM 1424 CB ALA A 229 -78.610 3.600 -0.190 1.00 36.18 C ANISOU 1424 CB ALA A 229 5862 4576 3309 -472 446 440 C ATOM 1425 N VAL A 230 -79.001 6.666 -0.025 1.00 32.87 N ANISOU 1425 N VAL A 230 5404 4311 2773 -441 484 236 N ATOM 1426 CA VAL A 230 -79.172 7.898 0.741 1.00 37.77 C ANISOU 1426 CA VAL A 230 5996 5035 3319 -456 500 170 C ATOM 1427 C VAL A 230 -80.304 8.697 0.096 1.00 38.11 C ANISOU 1427 C VAL A 230 6012 5078 3388 -446 530 59 C ATOM 1428 O VAL A 230 -80.225 9.117 -1.060 1.00 35.06 O ANISOU 1428 O VAL A 230 5629 4625 3066 -391 520 10 O ATOM 1429 CB VAL A 230 -77.864 8.704 0.871 1.00 36.37 C ANISOU 1429 CB VAL A 230 5823 4871 3124 -413 470 164 C ATOM 1430 CG1 VAL A 230 -76.718 8.043 0.161 1.00 34.49 C ANISOU 1430 CG1 VAL A 230 5618 4540 2946 -366 432 228 C ATOM 1431 CG2 VAL A 230 -78.027 10.152 0.440 1.00 35.32 C ANISOU 1431 CG2 VAL A 230 5662 4754 3002 -377 478 52 C ATOM 1432 N LYS A 231 -81.400 8.844 0.834 1.00 39.63 N ANISOU 1432 N LYS A 231 6176 5350 3532 -502 566 22 N ATOM 1433 CA LYS A 231 -82.630 9.323 0.226 1.00 36.31 C ANISOU 1433 CA LYS A 231 5728 4920 3147 -499 593 -72 C ATOM 1434 C LYS A 231 -82.625 10.829 0.016 1.00 38.01 C ANISOU 1434 C LYS A 231 5911 5160 3373 -463 591 -177 C ATOM 1435 O LYS A 231 -83.303 11.311 -0.906 1.00 35.89 O ANISOU 1435 O LYS A 231 5627 4847 3164 -434 595 -246 O ATOM 1436 CB LYS A 231 -83.828 8.891 1.085 1.00 36.98 C ANISOU 1436 CB LYS A 231 5790 5081 3181 -576 634 -77 C ATOM 1437 CG LYS A 231 -84.077 7.375 1.049 1.00 37.33 C ANISOU 1437 CG LYS A 231 5862 5079 3245 -611 637 22 C ATOM 1438 CD LYS A 231 -84.004 6.813 -0.389 1.00 33.28 C ANISOU 1438 CD LYS A 231 5374 4437 2835 -555 620 27 C ATOM 1439 CE LYS A 231 -84.597 5.415 -0.525 1.00 35.19 C ANISOU 1439 CE LYS A 231 5628 4628 3116 -592 630 92 C ATOM 1440 NZ LYS A 231 -84.587 4.828 -1.917 1.00 36.94 N1+ ANISOU 1440 NZ LYS A 231 5864 4733 3438 -542 616 82 N1+ ATOM 1441 N ASN A 232 -81.842 11.566 0.824 1.00 40.02 N ANISOU 1441 N ASN A 232 6151 5479 3577 -463 580 -188 N ATOM 1442 CA ASN A 232 -81.743 13.020 0.772 1.00 33.49 C ANISOU 1442 CA ASN A 232 5284 4674 2766 -432 574 -286 C ATOM 1443 C ASN A 232 -80.303 13.466 0.960 1.00 32.94 C ANISOU 1443 C ASN A 232 5227 4604 2685 -397 541 -257 C ATOM 1444 O ASN A 232 -79.566 12.887 1.759 1.00 35.80 O ANISOU 1444 O ASN A 232 5609 5007 2986 -421 533 -184 O ATOM 1445 CB ASN A 232 -82.596 13.676 1.848 1.00 34.46 C ANISOU 1445 CB ASN A 232 5350 4908 2834 -484 607 -371 C ATOM 1446 CG ASN A 232 -84.069 13.488 1.607 1.00 36.00 C ANISOU 1446 CG ASN A 232 5522 5105 3050 -513 640 -424 C ATOM 1447 ND2 ASN A 232 -84.650 12.469 2.233 1.00 33.56 N ANISOU 1447 ND2 ASN A 232 5222 4843 2685 -576 668 -373 N ATOM 1448 OD1 ASN A 232 -84.681 14.250 0.862 1.00 38.51 O ANISOU 1448 OD1 ASN A 232 5813 5382 3438 -481 640 -507 O ATOM 1449 N VAL A 233 -79.907 14.487 0.206 1.00 31.47 N ANISOU 1449 N VAL A 233 5028 4370 2561 -342 520 -310 N ATOM 1450 CA VAL A 233 -78.647 15.191 0.394 1.00 31.30 C ANISOU 1450 CA VAL A 233 5005 4353 2536 -308 491 -307 C ATOM 1451 C VAL A 233 -78.996 16.652 0.606 1.00 31.35 C ANISOU 1451 C VAL A 233 4950 4393 2570 -300 495 -422 C ATOM 1452 O VAL A 233 -79.746 17.232 -0.181 1.00 33.83 O ANISOU 1452 O VAL A 233 5240 4661 2954 -278 496 -480 O ATOM 1453 CB VAL A 233 -77.691 15.033 -0.805 1.00 33.22 C ANISOU 1453 CB VAL A 233 5287 4497 2840 -248 458 -256 C ATOM 1454 CG1 VAL A 233 -76.490 15.970 -0.668 1.00 30.46 C ANISOU 1454 CG1 VAL A 233 4925 4151 2497 -213 430 -269 C ATOM 1455 CG2 VAL A 233 -77.240 13.585 -0.966 1.00 31.91 C ANISOU 1455 CG2 VAL A 233 5172 4293 2659 -255 450 -152 C ATOM 1456 N ARG A 234 -78.481 17.228 1.678 1.00 31.76 N ANISOU 1456 N ARG A 234 4971 4526 2571 -317 495 -455 N ATOM 1457 CA ARG A 234 -78.758 18.598 2.066 1.00 31.97 C ANISOU 1457 CA ARG A 234 4928 4592 2626 -314 499 -573 C ATOM 1458 C ARG A 234 -77.437 19.341 1.994 1.00 31.71 C ANISOU 1458 C ARG A 234 4893 4536 2620 -270 465 -570 C ATOM 1459 O ARG A 234 -76.425 18.848 2.490 1.00 33.65 O ANISOU 1459 O ARG A 234 5170 4811 2806 -274 454 -503 O ATOM 1460 CB ARG A 234 -79.365 18.637 3.489 1.00 33.42 C ANISOU 1460 CB ARG A 234 5065 4912 2723 -381 533 -632 C ATOM 1461 CG ARG A 234 -80.059 19.935 3.889 1.00 33.18 C ANISOU 1461 CG ARG A 234 4948 4926 2731 -387 547 -781 C ATOM 1462 CD ARG A 234 -81.130 19.702 4.974 1.00 35.22 C ANISOU 1462 CD ARG A 234 5162 5310 2910 -461 591 -842 C ATOM 1463 NE ARG A 234 -80.536 19.086 6.156 1.00 44.94 N ANISOU 1463 NE ARG A 234 6403 6657 4015 -511 601 -787 N ATOM 1464 CZ ARG A 234 -81.183 18.344 7.046 1.00 41.51 C ANISOU 1464 CZ ARG A 234 5961 6331 3480 -583 635 -768 C ATOM 1465 NH1 ARG A 234 -82.501 18.199 7.007 1.00 42.34 N1+ ANISOU 1465 NH1 ARG A 234 6040 6456 3592 -618 669 -821 N1+ ATOM 1466 NH2 ARG A 234 -80.488 17.724 7.992 1.00 42.09 N ANISOU 1466 NH2 ARG A 234 6051 6498 3442 -624 634 -690 N ATOM 1467 N TYR A 235 -77.422 20.477 1.325 1.00 31.41 N ANISOU 1467 N TYR A 235 4819 4440 2676 -228 447 -634 N ATOM 1468 CA TYR A 235 -76.224 21.302 1.239 1.00 32.54 C ANISOU 1468 CA TYR A 235 4951 4558 2855 -189 416 -640 C ATOM 1469 C TYR A 235 -76.388 22.469 2.204 1.00 33.32 C ANISOU 1469 C TYR A 235 4968 4727 2964 -204 423 -761 C ATOM 1470 O TYR A 235 -77.387 23.191 2.136 1.00 33.05 O ANISOU 1470 O TYR A 235 4878 4690 2991 -210 433 -855 O ATOM 1471 CB TYR A 235 -75.995 21.822 -0.181 1.00 31.11 C ANISOU 1471 CB TYR A 235 4778 4262 2779 -133 385 -621 C ATOM 1472 CG TYR A 235 -75.555 20.831 -1.239 1.00 30.36 C ANISOU 1472 CG TYR A 235 4754 4099 2683 -109 372 -513 C ATOM 1473 CD1 TYR A 235 -76.380 19.791 -1.652 1.00 29.95 C ANISOU 1473 CD1 TYR A 235 4736 4033 2611 -127 391 -474 C ATOM 1474 CD2 TYR A 235 -74.319 20.968 -1.864 1.00 32.84 C ANISOU 1474 CD2 TYR A 235 5094 4362 3022 -69 342 -458 C ATOM 1475 CE1 TYR A 235 -75.992 18.916 -2.651 1.00 29.51 C ANISOU 1475 CE1 TYR A 235 4734 3914 2563 -105 379 -391 C ATOM 1476 CE2 TYR A 235 -73.910 20.084 -2.863 1.00 29.67 C ANISOU 1476 CE2 TYR A 235 4747 3903 2623 -48 331 -374 C ATOM 1477 CZ TYR A 235 -74.753 19.061 -3.259 1.00 29.45 C ANISOU 1477 CZ TYR A 235 4749 3863 2578 -65 349 -344 C ATOM 1478 OH TYR A 235 -74.359 18.184 -4.262 1.00 28.76 O ANISOU 1478 OH TYR A 235 4706 3722 2499 -44 339 -274 O ATOM 1479 N LEU A 236 -75.421 22.662 3.094 1.00 37.37 N ANISOU 1479 N LEU A 236 5471 5305 3424 -212 417 -767 N ATOM 1480 CA LEU A 236 -75.558 23.694 4.116 1.00 35.62 C ANISOU 1480 CA LEU A 236 5164 5167 3202 -232 427 -893 C ATOM 1481 C LEU A 236 -74.864 24.978 3.705 1.00 34.28 C ANISOU 1481 C LEU A 236 4952 4932 3142 -183 394 -948 C ATOM 1482 O LEU A 236 -73.821 24.960 3.053 1.00 32.69 O ANISOU 1482 O LEU A 236 4792 4661 2969 -143 365 -873 O ATOM 1483 CB LEU A 236 -74.979 23.242 5.455 1.00 33.31 C ANISOU 1483 CB LEU A 236 4871 5005 2781 -275 440 -882 C ATOM 1484 CG LEU A 236 -75.932 22.443 6.309 1.00 34.85 C ANISOU 1484 CG LEU A 236 5061 5310 2871 -343 479 -884 C ATOM 1485 CD1 LEU A 236 -75.275 22.171 7.626 1.00 36.40 C ANISOU 1485 CD1 LEU A 236 5244 5643 2944 -386 485 -874 C ATOM 1486 CD2 LEU A 236 -77.252 23.167 6.464 1.00 34.31 C ANISOU 1486 CD2 LEU A 236 4917 5270 2850 -365 505 -1017 C ATOM 1487 N SER A 237 -75.429 26.094 4.149 1.00 34.66 N ANISOU 1487 N SER A 237 4909 5006 3253 -190 400 -1083 N ATOM 1488 CA SER A 237 -74.800 27.402 4.026 1.00 35.77 C ANISOU 1488 CA SER A 237 4990 5098 3503 -152 371 -1154 C ATOM 1489 C SER A 237 -74.280 27.781 5.406 1.00 37.11 C ANISOU 1489 C SER A 237 5104 5390 3606 -181 383 -1241 C ATOM 1490 O SER A 237 -75.062 28.026 6.324 1.00 34.53 O ANISOU 1490 O SER A 237 4710 5162 3246 -223 411 -1352 O ATOM 1491 CB SER A 237 -75.798 28.432 3.506 1.00 36.30 C ANISOU 1491 CB SER A 237 4985 5097 3711 -136 362 -1251 C ATOM 1492 OG SER A 237 -75.168 29.648 3.160 1.00 37.22 O ANISOU 1492 OG SER A 237 5049 5138 3955 -95 326 -1295 O ATOM 1493 N LEU A 238 -72.967 27.808 5.564 1.00 41.55 N ANISOU 1493 N LEU A 238 5690 5954 4143 -161 362 -1193 N ATOM 1494 CA LEU A 238 -72.357 28.126 6.845 1.00 39.85 C ANISOU 1494 CA LEU A 238 5424 5861 3857 -187 370 -1267 C ATOM 1495 C LEU A 238 -71.538 29.393 6.698 1.00 44.95 C ANISOU 1495 C LEU A 238 6011 6448 4620 -145 339 -1337 C ATOM 1496 O LEU A 238 -70.966 29.649 5.637 1.00 42.29 O ANISOU 1496 O LEU A 238 5708 5987 4375 -97 307 -1269 O ATOM 1497 CB LEU A 238 -71.477 26.984 7.353 1.00 38.77 C ANISOU 1497 CB LEU A 238 5360 5795 3575 -206 371 -1151 C ATOM 1498 CG LEU A 238 -72.207 25.650 7.581 1.00 36.12 C ANISOU 1498 CG LEU A 238 5082 5519 3123 -252 398 -1069 C ATOM 1499 CD1 LEU A 238 -71.252 24.633 8.127 1.00 36.98 C ANISOU 1499 CD1 LEU A 238 5251 5690 3108 -269 391 -955 C ATOM 1500 CD2 LEU A 238 -73.388 25.793 8.500 1.00 35.36 C ANISOU 1500 CD2 LEU A 238 4917 5541 2976 -311 437 -1178 C ATOM 1501 N SER A 239 -71.481 30.185 7.775 1.00 47.84 N ANISOU 1501 N SER A 239 6284 6910 4984 -166 348 -1477 N ATOM 1502 CA SER A 239 -70.932 31.531 7.694 1.00 47.50 C ANISOU 1502 CA SER A 239 6162 6807 5078 -131 321 -1574 C ATOM 1503 C SER A 239 -69.566 31.676 8.341 1.00 53.97 C ANISOU 1503 C SER A 239 6977 7683 5846 -124 308 -1572 C ATOM 1504 O SER A 239 -68.958 32.745 8.212 1.00 60.58 O ANISOU 1504 O SER A 239 7755 8461 6802 -91 283 -1639 O ATOM 1505 CB SER A 239 -71.903 32.535 8.330 1.00 51.45 C ANISOU 1505 CB SER A 239 6538 7354 5656 -152 337 -1762 C ATOM 1506 OG SER A 239 -73.248 32.097 8.189 1.00 47.53 O ANISOU 1506 OG SER A 239 6045 6871 5142 -180 363 -1773 O ATOM 1507 N GLY A 240 -69.059 30.636 9.009 1.00 53.35 N ANISOU 1507 N GLY A 240 6956 7711 5602 -154 321 -1495 N ATOM 1508 CA GLY A 240 -67.861 30.787 9.810 1.00 52.85 C ANISOU 1508 CA GLY A 240 6876 7728 5478 -155 310 -1511 C ATOM 1509 C GLY A 240 -66.585 30.899 8.991 1.00 56.64 C ANISOU 1509 C GLY A 240 7408 8093 6021 -100 272 -1417 C ATOM 1510 O GLY A 240 -66.494 30.479 7.832 1.00 55.13 O ANISOU 1510 O GLY A 240 7291 7781 5875 -68 257 -1300 O ATOM 1511 N ASN A 241 -65.564 31.495 9.621 1.00 58.17 N ANISOU 1511 N ASN A 241 7554 8332 6216 -91 258 -1476 N ATOM 1512 CA ASN A 241 -64.206 31.430 9.087 1.00 55.27 C ANISOU 1512 CA ASN A 241 7238 7890 5871 -49 225 -1383 C ATOM 1513 C ASN A 241 -63.557 30.086 9.392 1.00 52.72 C ANISOU 1513 C ASN A 241 7006 7634 5392 -64 224 -1248 C ATOM 1514 O ASN A 241 -62.559 29.732 8.760 1.00 54.71 O ANISOU 1514 O ASN A 241 7322 7812 5655 -29 199 -1144 O ATOM 1515 CB ASN A 241 -63.329 32.567 9.655 1.00 61.11 C ANISOU 1515 CB ASN A 241 7892 8652 6676 -33 209 -1499 C ATOM 1516 CG ASN A 241 -63.515 33.918 8.924 1.00 62.18 C ANISOU 1516 CG ASN A 241 7955 8655 7016 3 191 -1583 C ATOM 1517 ND2 ASN A 241 -62.445 34.395 8.288 1.00 59.32 N ANISOU 1517 ND2 ASN A 241 7603 8194 6742 45 160 -1541 N ATOM 1518 OD1 ASN A 241 -64.594 34.528 8.956 1.00 61.25 O ANISOU 1518 OD1 ASN A 241 7768 8525 6977 -9 203 -1686 O ATOM 1519 N THR A 242 -64.097 29.348 10.355 1.00 50.43 N ANISOU 1519 N THR A 242 6717 7482 4962 -117 249 -1249 N ATOM 1520 CA THR A 242 -63.763 27.954 10.623 1.00 50.64 C ANISOU 1520 CA THR A 242 6828 7565 4847 -139 247 -1109 C ATOM 1521 C THR A 242 -65.020 27.092 10.524 1.00 49.49 C ANISOU 1521 C THR A 242 6719 7439 4646 -177 275 -1061 C ATOM 1522 O THR A 242 -65.249 26.190 11.337 1.00 48.53 O ANISOU 1522 O THR A 242 6616 7434 4388 -226 288 -1011 O ATOM 1523 CB THR A 242 -63.108 27.795 11.996 1.00 47.19 C ANISOU 1523 CB THR A 242 6357 7295 4278 -176 245 -1136 C ATOM 1524 CG2 THR A 242 -61.616 28.078 11.918 1.00 54.58 C ANISOU 1524 CG2 THR A 242 7302 8196 5241 -134 211 -1111 C ATOM 1525 OG1 THR A 242 -63.710 28.706 12.920 1.00 47.10 O ANISOU 1525 OG1 THR A 242 6238 7398 4262 -210 269 -1305 O ATOM 1526 N ALA A 243 -65.846 27.370 9.508 1.00 48.80 N ANISOU 1526 N ALA A 243 6638 7235 4667 -155 281 -1071 N ATOM 1527 CA ALA A 243 -67.215 26.857 9.475 1.00 46.41 C ANISOU 1527 CA ALA A 243 6344 6955 4335 -192 312 -1070 C ATOM 1528 C ALA A 243 -67.246 25.344 9.323 1.00 40.99 C ANISOU 1528 C ALA A 243 5753 6273 3550 -211 314 -915 C ATOM 1529 O ALA A 243 -67.861 24.647 10.137 1.00 42.89 O ANISOU 1529 O ALA A 243 5992 6627 3677 -267 337 -900 O ATOM 1530 CB ALA A 243 -67.998 27.520 8.343 1.00 48.03 C ANISOU 1530 CB ALA A 243 6536 7027 4687 -159 312 -1110 C ATOM 1531 N GLY A 244 -66.608 24.823 8.273 1.00 43.31 N ANISOU 1531 N GLY A 244 6122 6444 3889 -167 289 -800 N ATOM 1532 CA GLY A 244 -66.529 23.378 8.101 1.00 41.10 C ANISOU 1532 CA GLY A 244 5927 6156 3534 -180 285 -656 C ATOM 1533 C GLY A 244 -66.056 22.665 9.351 1.00 40.56 C ANISOU 1533 C GLY A 244 5861 6223 3326 -225 283 -608 C ATOM 1534 O GLY A 244 -66.652 21.670 9.780 1.00 36.26 O ANISOU 1534 O GLY A 244 5345 5739 2695 -272 297 -541 O ATOM 1535 N ALA A 245 -65.003 23.202 9.983 1.00 44.48 N ANISOU 1535 N ALA A 245 6325 6775 3799 -215 263 -644 N ATOM 1536 CA ALA A 245 -64.411 22.552 11.145 1.00 36.59 C ANISOU 1536 CA ALA A 245 5328 5909 2667 -255 253 -589 C ATOM 1537 C ALA A 245 -65.342 22.608 12.344 1.00 37.43 C ANISOU 1537 C ALA A 245 5373 6181 2666 -327 285 -659 C ATOM 1538 O ALA A 245 -65.469 21.624 13.083 1.00 36.89 O ANISOU 1538 O ALA A 245 5326 6212 2478 -379 287 -571 O ATOM 1539 CB ALA A 245 -63.059 23.186 11.462 1.00 35.43 C ANISOU 1539 CB ALA A 245 5155 5778 2528 -223 223 -620 C ATOM 1540 N ASP A 246 -66.020 23.737 12.544 1.00 41.22 N ANISOU 1540 N ASP A 246 5773 6697 3192 -334 311 -816 N ATOM 1541 CA ASP A 246 -66.863 23.875 13.730 1.00 41.34 C ANISOU 1541 CA ASP A 246 5717 6888 3103 -406 345 -904 C ATOM 1542 C ASP A 246 -68.127 23.048 13.585 1.00 42.26 C ANISOU 1542 C ASP A 246 5863 7011 3183 -448 375 -852 C ATOM 1543 O ASP A 246 -68.658 22.540 14.580 1.00 41.38 O ANISOU 1543 O ASP A 246 5729 7052 2943 -519 396 -843 O ATOM 1544 CB ASP A 246 -67.222 25.341 13.965 1.00 39.87 C ANISOU 1544 CB ASP A 246 5425 6730 2992 -398 363 -1102 C ATOM 1545 CG ASP A 246 -66.078 26.125 14.519 1.00 39.02 C ANISOU 1545 CG ASP A 246 5266 6674 2886 -379 341 -1172 C ATOM 1546 OD1 ASP A 246 -65.293 25.551 15.280 1.00 38.65 O ANISOU 1546 OD1 ASP A 246 5235 6730 2721 -402 325 -1102 O ATOM 1547 OD2 ASP A 246 -65.921 27.300 14.135 1.00 47.02 O1- ANISOU 1547 OD2 ASP A 246 6224 7614 4027 -337 335 -1290 O1- ATOM 1548 N ALA A 247 -68.622 22.908 12.350 1.00 37.08 N ANISOU 1548 N ALA A 247 5256 6195 2637 -409 376 -818 N ATOM 1549 CA ALA A 247 -69.830 22.129 12.113 1.00 39.18 C ANISOU 1549 CA ALA A 247 5551 6454 2882 -444 403 -772 C ATOM 1550 C ALA A 247 -69.525 20.644 12.133 1.00 40.62 C ANISOU 1550 C ALA A 247 5816 6631 2986 -465 388 -593 C ATOM 1551 O ALA A 247 -70.327 19.832 12.612 1.00 37.39 O ANISOU 1551 O ALA A 247 5416 6298 2494 -525 410 -542 O ATOM 1552 CB ALA A 247 -70.449 22.520 10.775 1.00 35.90 C ANISOU 1552 CB ALA A 247 5153 5876 2612 -394 406 -801 C ATOM 1553 N LEU A 248 -68.371 20.286 11.588 1.00 41.27 N ANISOU 1553 N LEU A 248 5957 6619 3104 -415 349 -497 N ATOM 1554 CA LEU A 248 -67.853 18.939 11.752 1.00 39.85 C ANISOU 1554 CA LEU A 248 5843 6440 2856 -432 325 -332 C ATOM 1555 C LEU A 248 -67.740 18.598 13.229 1.00 38.32 C ANISOU 1555 C LEU A 248 5615 6434 2511 -504 327 -307 C ATOM 1556 O LEU A 248 -68.207 17.542 13.672 1.00 43.00 O ANISOU 1556 O LEU A 248 6232 7083 3023 -559 332 -204 O ATOM 1557 CB LEU A 248 -66.499 18.848 11.050 1.00 38.00 C ANISOU 1557 CB LEU A 248 5658 6092 2690 -365 281 -266 C ATOM 1558 CG LEU A 248 -65.908 17.531 10.602 1.00 37.47 C ANISOU 1558 CG LEU A 248 5668 5942 2627 -351 249 -105 C ATOM 1559 CD1 LEU A 248 -66.679 17.070 9.398 1.00 34.74 C ANISOU 1559 CD1 LEU A 248 5367 5464 2370 -329 263 -77 C ATOM 1560 CD2 LEU A 248 -64.419 17.741 10.266 1.00 36.80 C ANISOU 1560 CD2 LEU A 248 5603 5793 2587 -292 208 -79 C ATOM 1561 N ALA A 249 -67.158 19.506 14.017 1.00 38.01 N ANISOU 1561 N ALA A 249 5512 6501 2430 -507 323 -403 N ATOM 1562 CA ALA A 249 -66.969 19.239 15.440 1.00 39.08 C ANISOU 1562 CA ALA A 249 5606 6833 2410 -577 322 -383 C ATOM 1563 C ALA A 249 -68.290 19.042 16.164 1.00 40.34 C ANISOU 1563 C ALA A 249 5723 7128 2478 -659 367 -419 C ATOM 1564 O ALA A 249 -68.364 18.243 17.103 1.00 44.27 O ANISOU 1564 O ALA A 249 6219 7762 2842 -728 365 -328 O ATOM 1565 CB ALA A 249 -66.192 20.377 16.091 1.00 40.26 C ANISOU 1565 CB ALA A 249 5683 7072 2541 -564 314 -507 C ATOM 1566 N ALA A 250 -69.336 19.764 15.757 1.00 39.64 N ANISOU 1566 N ALA A 250 5595 7009 2457 -654 405 -550 N ATOM 1567 CA ALA A 250 -70.635 19.639 16.404 1.00 40.40 C ANISOU 1567 CA ALA A 250 5644 7233 2475 -731 451 -601 C ATOM 1568 C ALA A 250 -71.466 18.477 15.857 1.00 41.32 C ANISOU 1568 C ALA A 250 5827 7273 2599 -753 462 -477 C ATOM 1569 O ALA A 250 -72.482 18.120 16.462 1.00 43.44 O ANISOU 1569 O ALA A 250 6066 7655 2783 -826 498 -484 O ATOM 1570 CB ALA A 250 -71.407 20.957 16.281 1.00 40.37 C ANISOU 1570 CB ALA A 250 5556 7235 2546 -719 486 -808 C ATOM 1571 N GLY A 251 -71.047 17.860 14.757 1.00 39.82 N ANISOU 1571 N GLY A 251 5722 6902 2505 -694 433 -366 N ATOM 1572 CA GLY A 251 -71.739 16.706 14.213 1.00 42.81 C ANISOU 1572 CA GLY A 251 6164 7201 2902 -711 439 -248 C ATOM 1573 C GLY A 251 -72.894 17.030 13.302 1.00 40.38 C ANISOU 1573 C GLY A 251 5853 6796 2693 -691 473 -330 C ATOM 1574 O GLY A 251 -73.669 16.126 12.961 1.00 38.38 O ANISOU 1574 O GLY A 251 5637 6499 2445 -716 486 -253 O ATOM 1575 N THR A 252 -73.027 18.297 12.907 1.00 40.60 N ANISOU 1575 N THR A 252 5834 6788 2805 -648 483 -482 N ATOM 1576 CA THR A 252 -74.065 18.769 12.004 1.00 37.44 C ANISOU 1576 CA THR A 252 5423 6292 2512 -623 508 -569 C ATOM 1577 C THR A 252 -73.784 18.371 10.563 1.00 42.61 C ANISOU 1577 C THR A 252 6155 6751 3286 -553 482 -489 C ATOM 1578 O THR A 252 -74.719 18.312 9.757 1.00 40.12 O ANISOU 1578 O THR A 252 5849 6353 3041 -542 500 -511 O ATOM 1579 CB THR A 252 -74.171 20.297 12.093 1.00 37.47 C ANISOU 1579 CB THR A 252 5343 6317 2577 -598 518 -752 C ATOM 1580 CG2 THR A 252 -75.582 20.740 11.864 1.00 37.55 C ANISOU 1580 CG2 THR A 252 5306 6325 2637 -615 555 -864 C ATOM 1581 OG1 THR A 252 -73.795 20.732 13.406 1.00 44.27 O ANISOU 1581 OG1 THR A 252 6136 7353 3331 -643 525 -819 O ATOM 1582 N ILE A 253 -72.519 18.092 10.242 1.00 44.03 N ANISOU 1582 N ILE A 253 6383 6863 3485 -508 442 -402 N ATOM 1583 CA ILE A 253 -72.027 17.888 8.884 1.00 41.65 C ANISOU 1583 CA ILE A 253 6141 6388 3294 -438 415 -344 C ATOM 1584 C ILE A 253 -71.646 16.424 8.720 1.00 41.69 C ANISOU 1584 C ILE A 253 6219 6350 3272 -446 395 -182 C ATOM 1585 O ILE A 253 -71.058 15.823 9.626 1.00 41.12 O ANISOU 1585 O ILE A 253 6155 6361 3110 -482 379 -103 O ATOM 1586 CB ILE A 253 -70.810 18.803 8.610 1.00 45.81 C ANISOU 1586 CB ILE A 253 6658 6871 3877 -378 384 -384 C ATOM 1587 CG1 ILE A 253 -71.255 20.223 8.225 1.00 41.88 C ANISOU 1587 CG1 ILE A 253 6099 6344 3470 -349 396 -533 C ATOM 1588 CG2 ILE A 253 -69.798 18.156 7.657 1.00 40.63 C ANISOU 1588 CG2 ILE A 253 6073 6086 3277 -323 347 -273 C ATOM 1589 CD1 ILE A 253 -72.213 20.283 7.100 1.00 39.65 C ANISOU 1589 CD1 ILE A 253 5830 5955 3282 -326 409 -551 C ATOM 1590 N ASP A 254 -71.975 15.850 7.563 1.00 38.14 N ANISOU 1590 N ASP A 254 5817 5769 2904 -415 392 -135 N ATOM 1591 CA ASP A 254 -71.579 14.478 7.262 1.00 36.68 C ANISOU 1591 CA ASP A 254 5695 5520 2721 -415 370 7 C ATOM 1592 C ASP A 254 -70.415 14.374 6.297 1.00 34.68 C ANISOU 1592 C ASP A 254 5483 5145 2548 -345 332 52 C ATOM 1593 O ASP A 254 -69.834 13.293 6.175 1.00 33.61 O ANISOU 1593 O ASP A 254 5391 4962 2417 -341 305 163 O ATOM 1594 CB ASP A 254 -72.748 13.700 6.677 1.00 36.81 C ANISOU 1594 CB ASP A 254 5734 5482 2771 -435 394 34 C ATOM 1595 CG ASP A 254 -73.825 13.500 7.673 1.00 36.54 C ANISOU 1595 CG ASP A 254 5666 5568 2650 -513 429 20 C ATOM 1596 OD1 ASP A 254 -73.476 13.098 8.800 1.00 36.88 O ANISOU 1596 OD1 ASP A 254 5699 5719 2593 -563 422 81 O ATOM 1597 OD2 ASP A 254 -75.001 13.752 7.331 1.00 34.96 O1- ANISOU 1597 OD2 ASP A 254 5446 5361 2477 -525 463 -51 O1- ATOM 1598 N TRP A 255 -70.056 15.456 5.618 1.00 32.93 N ANISOU 1598 N TRP A 255 5246 4873 2394 -292 327 -32 N ATOM 1599 CA TRP A 255 -68.990 15.376 4.633 1.00 32.28 C ANISOU 1599 CA TRP A 255 5199 4681 2385 -229 294 6 C ATOM 1600 C TRP A 255 -68.569 16.786 4.278 1.00 31.87 C ANISOU 1600 C TRP A 255 5111 4614 2384 -187 290 -91 C ATOM 1601 O TRP A 255 -69.404 17.603 3.873 1.00 31.66 O ANISOU 1601 O TRP A 255 5053 4574 2403 -182 311 -177 O ATOM 1602 CB TRP A 255 -69.446 14.595 3.385 1.00 33.70 C ANISOU 1602 CB TRP A 255 5419 4747 2639 -207 296 48 C ATOM 1603 CG TRP A 255 -68.384 14.426 2.344 1.00 32.52 C ANISOU 1603 CG TRP A 255 5301 4496 2559 -148 266 84 C ATOM 1604 CD1 TRP A 255 -67.045 14.563 2.521 1.00 33.29 C ANISOU 1604 CD1 TRP A 255 5405 4591 2653 -119 234 110 C ATOM 1605 CD2 TRP A 255 -68.573 14.070 0.968 1.00 34.71 C ANISOU 1605 CD2 TRP A 255 5602 4669 2915 -113 265 92 C ATOM 1606 CE2 TRP A 255 -67.300 14.031 0.376 1.00 35.48 C ANISOU 1606 CE2 TRP A 255 5718 4711 3052 -66 234 120 C ATOM 1607 CE3 TRP A 255 -69.696 13.778 0.181 1.00 32.92 C ANISOU 1607 CE3 TRP A 255 5381 4399 2728 -118 287 75 C ATOM 1608 NE1 TRP A 255 -66.387 14.347 1.348 1.00 33.74 N ANISOU 1608 NE1 TRP A 255 5487 4550 2783 -70 215 131 N ATOM 1609 CZ2 TRP A 255 -67.109 13.704 -0.969 1.00 33.90 C ANISOU 1609 CZ2 TRP A 255 5538 4420 2924 -28 226 130 C ATOM 1610 CZ3 TRP A 255 -69.510 13.460 -1.150 1.00 32.86 C ANISOU 1610 CZ3 TRP A 255 5394 4301 2792 -79 278 85 C ATOM 1611 CH2 TRP A 255 -68.225 13.423 -1.711 1.00 34.79 C ANISOU 1611 CH2 TRP A 255 5652 4498 3068 -35 248 111 C ATOM 1612 N GLN A 256 -67.282 17.065 4.453 1.00 31.82 N ANISOU 1612 N GLN A 256 5106 4608 2375 -158 261 -76 N ATOM 1613 CA GLN A 256 -66.713 18.334 4.066 1.00 31.45 C ANISOU 1613 CA GLN A 256 5028 4534 2387 -117 251 -155 C ATOM 1614 C GLN A 256 -65.244 18.093 3.778 1.00 31.20 C ANISOU 1614 C GLN A 256 5026 4457 2372 -76 215 -95 C ATOM 1615 O GLN A 256 -64.646 17.122 4.248 1.00 36.28 O ANISOU 1615 O GLN A 256 5700 5120 2966 -88 197 -10 O ATOM 1616 CB GLN A 256 -66.928 19.415 5.148 1.00 34.99 C ANISOU 1616 CB GLN A 256 5409 5090 2795 -143 265 -258 C ATOM 1617 CG GLN A 256 -65.987 19.396 6.347 1.00 32.56 C ANISOU 1617 CG GLN A 256 5086 4882 2404 -162 249 -245 C ATOM 1618 CD GLN A 256 -64.869 20.394 6.157 1.00 34.41 C ANISOU 1618 CD GLN A 256 5297 5089 2690 -116 226 -294 C ATOM 1619 NE2 GLN A 256 -63.658 20.043 6.590 1.00 32.46 N ANISOU 1619 NE2 GLN A 256 5067 4865 2403 -106 197 -237 N ATOM 1620 OE1 GLN A 256 -65.094 21.472 5.614 1.00 36.30 O ANISOU 1620 OE1 GLN A 256 5499 5282 3011 -90 232 -378 O ATOM 1621 N THR A 257 -64.669 18.990 2.998 1.00 31.59 N ANISOU 1621 N THR A 257 5063 4446 2496 -31 204 -138 N ATOM 1622 CA THR A 257 -63.363 18.778 2.383 1.00 35.18 C ANISOU 1622 CA THR A 257 5546 4837 2985 13 173 -87 C ATOM 1623 C THR A 257 -62.460 19.966 2.682 1.00 35.36 C ANISOU 1623 C THR A 257 5528 4881 3027 35 159 -149 C ATOM 1624 O THR A 257 -62.827 21.115 2.408 1.00 34.05 O ANISOU 1624 O THR A 257 5319 4702 2915 45 169 -229 O ATOM 1625 CB THR A 257 -63.505 18.560 0.852 1.00 33.14 C ANISOU 1625 CB THR A 257 5315 4472 2806 46 172 -64 C ATOM 1626 CG2 THR A 257 -62.154 18.375 0.185 1.00 33.05 C ANISOU 1626 CG2 THR A 257 5325 4403 2829 88 143 -22 C ATOM 1627 OG1 THR A 257 -64.360 17.430 0.581 1.00 29.72 O ANISOU 1627 OG1 THR A 257 4915 4018 2361 25 185 -14 O ATOM 1628 N GLY A 258 -61.282 19.686 3.241 1.00 33.05 N ANISOU 1628 N GLY A 258 5244 4616 2697 44 134 -111 N ATOM 1629 CA GLY A 258 -60.332 20.725 3.536 1.00 35.23 C ANISOU 1629 CA GLY A 258 5482 4911 2991 65 119 -167 C ATOM 1630 C GLY A 258 -59.687 20.581 4.896 1.00 39.64 C ANISOU 1630 C GLY A 258 6025 5574 3464 43 105 -162 C ATOM 1631 O GLY A 258 -60.014 19.692 5.691 1.00 38.10 O ANISOU 1631 O GLY A 258 5846 5445 3187 5 107 -110 O ATOM 1632 N PRO A 259 -58.758 21.482 5.190 1.00 39.91 N ANISOU 1632 N PRO A 259 6022 5626 3514 64 91 -215 N ATOM 1633 CA PRO A 259 -57.985 21.368 6.425 1.00 42.12 C ANISOU 1633 CA PRO A 259 6285 6007 3712 47 73 -211 C ATOM 1634 C PRO A 259 -58.904 21.412 7.633 1.00 40.54 C ANISOU 1634 C PRO A 259 6047 5934 3422 -10 95 -253 C ATOM 1635 O PRO A 259 -59.876 22.165 7.658 1.00 43.33 O ANISOU 1635 O PRO A 259 6360 6305 3798 -26 124 -341 O ATOM 1636 CB PRO A 259 -57.078 22.597 6.373 1.00 50.43 C ANISOU 1636 CB PRO A 259 7292 7049 4821 79 61 -290 C ATOM 1637 CG PRO A 259 -57.934 23.617 5.656 1.00 48.29 C ANISOU 1637 CG PRO A 259 6987 6721 4639 87 85 -371 C ATOM 1638 CD PRO A 259 -58.608 22.806 4.572 1.00 44.64 C ANISOU 1638 CD PRO A 259 6581 6174 4207 93 94 -299 C ATOM 1639 N VAL A 260 -58.600 20.571 8.616 1.00 46.45 N ANISOU 1639 N VAL A 260 6807 6772 4068 -42 79 -186 N ATOM 1640 CA VAL A 260 -59.196 20.631 9.951 1.00 45.88 C ANISOU 1640 CA VAL A 260 6692 6854 3888 -102 95 -222 C ATOM 1641 C VAL A 260 -58.047 20.622 10.947 1.00 45.49 C ANISOU 1641 C VAL A 260 6621 6899 3764 -107 64 -206 C ATOM 1642 O VAL A 260 -56.914 20.272 10.583 1.00 44.27 O ANISOU 1642 O VAL A 260 6500 6681 3639 -68 29 -142 O ATOM 1643 CB VAL A 260 -60.179 19.460 10.192 1.00 46.70 C ANISOU 1643 CB VAL A 260 6830 6988 3926 -150 108 -134 C ATOM 1644 CG1 VAL A 260 -61.512 19.754 9.517 1.00 42.97 C ANISOU 1644 CG1 VAL A 260 6353 6465 3509 -157 147 -190 C ATOM 1645 CG2 VAL A 260 -59.591 18.142 9.697 1.00 48.98 C ANISOU 1645 CG2 VAL A 260 7190 7194 4228 -132 76 11 C ATOM 1646 N PRO A 261 -58.294 21.024 12.202 1.00 51.34 N ANISOU 1646 N PRO A 261 7302 7797 4407 -155 75 -270 N ATOM 1647 CA PRO A 261 -57.166 21.219 13.136 1.00 50.26 C ANISOU 1647 CA PRO A 261 7134 7760 4203 -158 45 -276 C ATOM 1648 C PRO A 261 -56.307 19.985 13.364 1.00 56.36 C ANISOU 1648 C PRO A 261 7960 8532 4923 -158 1 -123 C ATOM 1649 O PRO A 261 -55.075 20.105 13.396 1.00 58.44 O ANISOU 1649 O PRO A 261 8224 8779 5202 -122 -34 -110 O ATOM 1650 CB PRO A 261 -57.870 21.662 14.425 1.00 45.10 C ANISOU 1650 CB PRO A 261 6406 7291 3438 -223 71 -364 C ATOM 1651 CG PRO A 261 -59.232 21.098 14.310 1.00 42.59 C ANISOU 1651 CG PRO A 261 6108 6979 3097 -265 104 -334 C ATOM 1652 CD PRO A 261 -59.576 21.299 12.878 1.00 50.02 C ANISOU 1652 CD PRO A 261 7088 7740 4179 -213 115 -344 C ATOM 1653 N ASP A 262 -56.899 18.808 13.541 1.00 65.91 N ANISOU 1653 N ASP A 262 9210 9757 6078 -196 -2 -7 N ATOM 1654 CA ASP A 262 -56.096 17.613 13.774 1.00 69.52 C ANISOU 1654 CA ASP A 262 9711 10204 6499 -197 -51 144 C ATOM 1655 C ASP A 262 -55.562 17.088 12.445 1.00 70.03 C ANISOU 1655 C ASP A 262 9838 10082 6689 -134 -71 206 C ATOM 1656 O ASP A 262 -55.619 17.745 11.403 1.00 71.12 O ANISOU 1656 O ASP A 262 9982 10113 6928 -89 -51 133 O ATOM 1657 CB ASP A 262 -56.903 16.536 14.512 1.00 75.37 C ANISOU 1657 CB ASP A 262 10464 11032 7141 -267 -51 252 C ATOM 1658 CG ASP A 262 -58.089 16.012 13.705 1.00 75.98 C ANISOU 1658 CG ASP A 262 10579 11015 7273 -276 -19 279 C ATOM 1659 OD1 ASP A 262 -58.033 15.987 12.453 1.00 75.38 O ANISOU 1659 OD1 ASP A 262 10542 10781 7316 -221 -15 273 O ATOM 1660 OD2 ASP A 262 -59.085 15.591 14.342 1.00 72.32 O1- ANISOU 1660 OD2 ASP A 262 10104 10645 6728 -341 3 309 O1- ATOM 1661 N ILE A 263 -55.050 15.869 12.472 1.00 64.39 N ANISOU 1661 N ILE A 263 9166 9330 5970 -133 -113 344 N ATOM 1662 CA ILE A 263 -54.529 15.232 11.274 1.00 60.60 C ANISOU 1662 CA ILE A 263 8738 8683 5604 -78 -134 402 C ATOM 1663 C ILE A 263 -54.852 13.757 11.376 1.00 58.71 C ANISOU 1663 C ILE A 263 8538 8414 5356 -107 -158 547 C ATOM 1664 O ILE A 263 -55.977 13.325 11.095 1.00 52.64 O ANISOU 1664 O ILE A 263 7786 7621 4593 -135 -129 566 O ATOM 1665 CB ILE A 263 -53.005 15.421 11.117 1.00 56.92 C ANISOU 1665 CB ILE A 263 8271 8176 5179 -26 -175 403 C ATOM 1666 CG1 ILE A 263 -52.547 16.832 11.521 1.00 51.85 C ANISOU 1666 CG1 ILE A 263 7575 7610 4515 -14 -162 275 C ATOM 1667 CG2 ILE A 263 -52.587 15.110 9.654 1.00 62.36 C ANISOU 1667 CG2 ILE A 263 9001 8693 5999 35 -181 414 C ATOM 1668 CD1 ILE A 263 -51.159 16.894 12.127 1.00 48.88 C ANISOU 1668 CD1 ILE A 263 7181 7280 4112 6 -209 293 C ATOM 1669 N GLU A 264 -53.840 12.987 11.783 1.00 56.78 N ANISOU 1669 N GLU A 264 8304 8167 5103 -99 -214 648 N ATOM 1670 CA GLU A 264 -54.012 11.570 12.069 1.00 60.19 C ANISOU 1670 CA GLU A 264 8764 8579 5528 -130 -249 799 C ATOM 1671 C GLU A 264 -55.154 11.339 13.048 1.00 61.13 C ANISOU 1671 C GLU A 264 8865 8828 5535 -211 -227 838 C ATOM 1672 O GLU A 264 -55.991 10.448 12.852 1.00 64.60 O ANISOU 1672 O GLU A 264 9328 9223 5993 -241 -220 914 O ATOM 1673 CB GLU A 264 -52.702 11.010 12.622 1.00 62.83 C ANISOU 1673 CB GLU A 264 9095 8924 5854 -116 -318 892 C ATOM 1674 CG GLU A 264 -51.470 11.663 12.013 1.00 64.18 C ANISOU 1674 CG GLU A 264 9262 9028 6095 -45 -333 817 C ATOM 1675 CD GLU A 264 -50.212 10.848 12.230 1.00 66.07 C ANISOU 1675 CD GLU A 264 9508 9228 6368 -19 -404 918 C ATOM 1676 OE1 GLU A 264 -50.342 9.662 12.600 1.00 63.07 O ANISOU 1676 OE1 GLU A 264 9141 8834 5987 -48 -444 1053 O ATOM 1677 OE2 GLU A 264 -49.098 11.388 12.034 1.00 59.99 O1- ANISOU 1677 OE2 GLU A 264 8726 8438 5630 29 -423 864 O1- ATOM 1678 N ASN A 265 -55.219 12.149 14.097 1.00 57.21 N ANISOU 1678 N ASN A 265 8320 8495 4920 -250 -213 778 N ATOM 1679 CA ASN A 265 -56.215 11.937 15.136 1.00 64.11 C ANISOU 1679 CA ASN A 265 9168 9519 5671 -334 -193 814 C ATOM 1680 C ASN A 265 -57.581 12.482 14.734 1.00 62.17 C ANISOU 1680 C ASN A 265 8916 9275 5432 -354 -125 712 C ATOM 1681 O ASN A 265 -58.273 13.091 15.554 1.00 67.94 O ANISOU 1681 O ASN A 265 9599 10155 6059 -408 -91 643 O ATOM 1682 CB ASN A 265 -55.728 12.563 16.451 1.00 62.99 C ANISOU 1682 CB ASN A 265 8970 9570 5394 -371 -206 783 C ATOM 1683 CG ASN A 265 -54.228 12.413 16.636 1.00 60.87 C ANISOU 1683 CG ASN A 265 8703 9284 5141 -330 -269 834 C ATOM 1684 ND2 ASN A 265 -53.751 11.171 16.581 1.00 59.38 N ANISOU 1684 ND2 ASN A 265 8549 9021 4990 -327 -325 993 N ATOM 1685 OD1 ASN A 265 -53.506 13.394 16.809 1.00 58.67 O ANISOU 1685 OD1 ASN A 265 8391 9051 4850 -300 -268 730 O ATOM 1686 N VAL A 266 -57.988 12.245 13.488 1.00 61.64 N ANISOU 1686 N VAL A 266 8889 9048 5484 -313 -107 700 N ATOM 1687 CA VAL A 266 -59.284 12.730 13.023 1.00 63.05 C ANISOU 1687 CA VAL A 266 9062 9216 5679 -328 -47 608 C ATOM 1688 C VAL A 266 -60.397 11.823 13.512 1.00 59.58 C ANISOU 1688 C VAL A 266 8628 8830 5180 -399 -32 696 C ATOM 1689 O VAL A 266 -61.442 12.279 13.986 1.00 57.21 O ANISOU 1689 O VAL A 266 8295 8632 4810 -450 13 629 O ATOM 1690 CB VAL A 266 -59.290 12.826 11.487 1.00 59.96 C ANISOU 1690 CB VAL A 266 8708 8643 5431 -259 -35 565 C ATOM 1691 CG1 VAL A 266 -58.564 11.618 10.892 1.00 59.52 C ANISOU 1691 CG1 VAL A 266 8700 8460 5456 -226 -82 688 C ATOM 1692 CG2 VAL A 266 -60.721 12.922 10.961 1.00 51.43 C ANISOU 1692 CG2 VAL A 266 7632 7536 4375 -280 17 513 C ATOM 1693 N SER A 267 -60.190 10.521 13.363 1.00 66.59 N ANISOU 1693 N SER A 267 9555 9640 6105 -404 -71 843 N ATOM 1694 CA SER A 267 -61.110 9.514 13.876 1.00 73.90 C ANISOU 1694 CA SER A 267 10487 10609 6982 -476 -68 954 C ATOM 1695 C SER A 267 -61.249 9.589 15.391 1.00 72.94 C ANISOU 1695 C SER A 267 10320 10697 6699 -557 -72 994 C ATOM 1696 O SER A 267 -62.358 9.504 15.935 1.00 66.58 O ANISOU 1696 O SER A 267 9493 9993 5814 -627 -35 994 O ATOM 1697 CB SER A 267 -60.600 8.139 13.455 1.00 76.26 C ANISOU 1697 CB SER A 267 10829 10775 7372 -457 -121 1107 C ATOM 1698 OG SER A 267 -60.971 7.145 14.388 1.00 79.73 O ANISOU 1698 OG SER A 267 11262 11292 7741 -533 -145 1253 O ATOM 1699 N GLU A 268 -60.127 9.724 16.094 1.00 83.65 N ANISOU 1699 N GLU A 268 11657 12127 8000 -551 -117 1028 N ATOM 1700 CA GLU A 268 -60.150 9.738 17.551 1.00 85.67 C ANISOU 1700 CA GLU A 268 11865 12593 8091 -630 -127 1076 C ATOM 1701 C GLU A 268 -60.638 11.063 18.124 1.00 80.05 C ANISOU 1701 C GLU A 268 11093 12042 7282 -657 -73 905 C ATOM 1702 O GLU A 268 -60.862 11.145 19.334 1.00 82.20 O ANISOU 1702 O GLU A 268 11315 12510 7405 -733 -69 922 O ATOM 1703 CB GLU A 268 -58.753 9.410 18.103 1.00 83.05 C ANISOU 1703 CB GLU A 268 11531 12288 7736 -614 -199 1172 C ATOM 1704 CG GLU A 268 -57.946 8.362 17.303 1.00 87.62 C ANISOU 1704 CG GLU A 268 12163 12672 8454 -557 -258 1295 C ATOM 1705 CD GLU A 268 -58.695 7.052 17.037 1.00 89.59 C ANISOU 1705 CD GLU A 268 12446 12833 8760 -591 -268 1436 C ATOM 1706 OE1 GLU A 268 -59.329 6.919 15.966 1.00 86.91 O ANISOU 1706 OE1 GLU A 268 12138 12354 8529 -559 -234 1389 O ATOM 1707 OE2 GLU A 268 -58.645 6.149 17.902 1.00 97.81 O1- ANISOU 1707 OE2 GLU A 268 13478 13945 9740 -652 -312 1596 O1- ATOM 1708 N ASN A 269 -60.817 12.096 17.299 1.00 61.97 N ANISOU 1708 N ASN A 269 8799 9675 5072 -601 -32 743 N ATOM 1709 CA ASN A 269 -61.255 13.395 17.786 1.00 58.63 C ANISOU 1709 CA ASN A 269 8310 9384 4581 -620 15 570 C ATOM 1710 C ASN A 269 -62.639 13.794 17.297 1.00 57.36 C ANISOU 1710 C ASN A 269 8141 9200 4454 -635 79 468 C ATOM 1711 O ASN A 269 -63.235 14.719 17.860 1.00 58.00 O ANISOU 1711 O ASN A 269 8158 9411 4469 -669 121 333 O ATOM 1712 CB ASN A 269 -60.249 14.485 17.380 1.00 60.09 C ANISOU 1712 CB ASN A 269 8481 9519 4833 -545 6 449 C ATOM 1713 CG ASN A 269 -59.499 15.087 18.566 1.00 59.60 C ANISOU 1713 CG ASN A 269 8356 9637 4653 -571 -12 405 C ATOM 1714 ND2 ASN A 269 -58.209 15.311 18.369 1.00 58.39 N ANISOU 1714 ND2 ASN A 269 8212 9427 4547 -512 -53 408 N ATOM 1715 OD1 ASN A 269 -60.063 15.336 19.643 1.00 64.71 O ANISOU 1715 OD1 ASN A 269 8944 10477 5167 -644 11 365 O ATOM 1716 N TYR A 270 -63.178 13.130 16.282 1.00 56.09 N ANISOU 1716 N TYR A 270 8035 8881 4396 -611 86 522 N ATOM 1717 CA TYR A 270 -64.479 13.541 15.795 1.00 52.94 C ANISOU 1717 CA TYR A 270 7626 8458 4032 -622 144 422 C ATOM 1718 C TYR A 270 -65.470 12.387 15.855 1.00 55.36 C ANISOU 1718 C TYR A 270 7959 8760 4315 -681 155 537 C ATOM 1719 O TYR A 270 -65.107 11.233 15.590 1.00 58.06 O ANISOU 1719 O TYR A 270 8351 9011 4697 -675 116 689 O ATOM 1720 CB TYR A 270 -64.374 14.083 14.358 1.00 52.54 C ANISOU 1720 CB TYR A 270 7606 8220 4136 -535 153 341 C ATOM 1721 CG TYR A 270 -63.810 15.483 14.302 1.00 47.26 C ANISOU 1721 CG TYR A 270 6894 7569 3494 -490 159 191 C ATOM 1722 CD1 TYR A 270 -62.439 15.698 14.263 1.00 50.72 C ANISOU 1722 CD1 TYR A 270 7340 7977 3956 -442 117 206 C ATOM 1723 CD2 TYR A 270 -64.648 16.595 14.315 1.00 43.73 C ANISOU 1723 CD2 TYR A 270 6393 7168 3056 -498 206 32 C ATOM 1724 CE1 TYR A 270 -61.921 16.997 14.230 1.00 51.69 C ANISOU 1724 CE1 TYR A 270 7418 8113 4109 -403 123 68 C ATOM 1725 CE2 TYR A 270 -64.139 17.888 14.288 1.00 37.97 C ANISOU 1725 CE2 TYR A 270 5615 6448 2364 -459 209 -106 C ATOM 1726 CZ TYR A 270 -62.781 18.082 14.249 1.00 40.73 C ANISOU 1726 CZ TYR A 270 5975 6767 2736 -413 169 -85 C ATOM 1727 OH TYR A 270 -62.271 19.353 14.215 1.00 37.56 O ANISOU 1727 OH TYR A 270 5523 6369 2379 -376 171 -219 O ATOM 1728 N PRO A 271 -66.732 12.670 16.242 1.00 55.15 N ANISOU 1728 N PRO A 271 7893 8833 4229 -740 208 465 N ATOM 1729 CA PRO A 271 -67.814 11.685 16.080 1.00 53.28 C ANISOU 1729 CA PRO A 271 7682 8566 3995 -788 228 552 C ATOM 1730 C PRO A 271 -67.843 11.126 14.668 1.00 58.06 C ANISOU 1730 C PRO A 271 8354 8950 4757 -721 217 592 C ATOM 1731 O PRO A 271 -67.651 9.916 14.485 1.00 57.17 O ANISOU 1731 O PRO A 271 8285 8759 4678 -728 184 742 O ATOM 1732 CB PRO A 271 -69.084 12.497 16.384 1.00 50.02 C ANISOU 1732 CB PRO A 271 7211 8261 3533 -833 292 404 C ATOM 1733 CG PRO A 271 -68.649 13.955 16.366 1.00 48.60 C ANISOU 1733 CG PRO A 271 6983 8111 3370 -786 303 230 C ATOM 1734 CD PRO A 271 -67.222 13.938 16.805 1.00 52.75 C ANISOU 1734 CD PRO A 271 7514 8666 3864 -763 252 289 C ATOM 1735 N GLY A 272 -68.096 12.020 13.683 1.00 62.22 N ANISOU 1735 N GLY A 272 8881 9380 5381 -660 244 456 N ATOM 1736 CA GLY A 272 -67.901 11.802 12.254 1.00 53.64 C ANISOU 1736 CA GLY A 272 7847 8094 4439 -584 233 462 C ATOM 1737 C GLY A 272 -66.472 11.385 11.979 1.00 57.92 C ANISOU 1737 C GLY A 272 8425 8553 5029 -531 176 547 C ATOM 1738 O GLY A 272 -65.545 12.182 12.124 1.00 58.83 O ANISOU 1738 O GLY A 272 8522 8692 5137 -495 160 490 O ATOM 1739 N TYR A 273 -66.285 10.142 11.561 1.00 70.97 N ANISOU 1739 N TYR A 273 10124 10103 6738 -526 146 679 N ATOM 1740 CA TYR A 273 -65.065 9.423 11.893 1.00 72.90 C ANISOU 1740 CA TYR A 273 10388 10328 6982 -513 86 800 C ATOM 1741 C TYR A 273 -63.924 9.656 10.910 1.00 72.20 C ANISOU 1741 C TYR A 273 10326 10106 7001 -425 56 774 C ATOM 1742 O TYR A 273 -63.034 10.468 11.167 1.00 77.75 O ANISOU 1742 O TYR A 273 11010 10852 7680 -396 42 718 O ATOM 1743 CB TYR A 273 -65.404 7.927 12.006 1.00 78.60 C ANISOU 1743 CB TYR A 273 11138 11004 7723 -555 63 959 C ATOM 1744 CG TYR A 273 -64.630 7.134 13.046 1.00 76.34 C ANISOU 1744 CG TYR A 273 10848 10788 7372 -594 8 1109 C ATOM 1745 CD1 TYR A 273 -64.708 7.462 14.395 1.00 82.18 C ANISOU 1745 CD1 TYR A 273 11544 11721 7959 -664 11 1124 C ATOM 1746 CD2 TYR A 273 -63.898 6.007 12.688 1.00 77.38 C ANISOU 1746 CD2 TYR A 273 11011 10794 7595 -568 -49 1238 C ATOM 1747 CE1 TYR A 273 -64.028 6.730 15.349 1.00 85.94 C ANISOU 1747 CE1 TYR A 273 12013 12269 8370 -704 -43 1272 C ATOM 1748 CE2 TYR A 273 -63.227 5.259 13.634 1.00 85.70 C ANISOU 1748 CE2 TYR A 273 12058 11905 8598 -605 -105 1386 C ATOM 1749 CZ TYR A 273 -63.298 5.619 14.968 1.00 88.35 C ANISOU 1749 CZ TYR A 273 12354 12439 8775 -675 -103 1409 C ATOM 1750 OH TYR A 273 -62.615 4.881 15.918 1.00 92.37 O ANISOU 1750 OH TYR A 273 12853 13014 9229 -715 -164 1566 O ATOM 1751 N GLU A 274 -63.942 8.961 9.782 1.00 59.92 N ANISOU 1751 N GLU A 274 8810 8395 5563 -384 47 807 N ATOM 1752 CA GLU A 274 -62.731 8.757 9.002 1.00 51.62 C ANISOU 1752 CA GLU A 274 7784 7224 4607 -313 6 825 C ATOM 1753 C GLU A 274 -62.371 9.970 8.154 1.00 47.21 C ANISOU 1753 C GLU A 274 7219 6624 4096 -251 26 691 C ATOM 1754 O GLU A 274 -63.219 10.782 7.772 1.00 44.20 O ANISOU 1754 O GLU A 274 6824 6254 3717 -251 71 589 O ATOM 1755 CB GLU A 274 -62.892 7.541 8.097 1.00 52.54 C ANISOU 1755 CB GLU A 274 7934 7194 4833 -295 -9 900 C ATOM 1756 CG GLU A 274 -61.814 6.491 8.239 1.00 54.74 C ANISOU 1756 CG GLU A 274 8227 7410 5161 -279 -73 1021 C ATOM 1757 CD GLU A 274 -62.356 5.093 8.012 1.00 55.60 C ANISOU 1757 CD GLU A 274 8353 7431 5340 -304 -88 1127 C ATOM 1758 OE1 GLU A 274 -62.918 4.827 6.922 1.00 51.73 O ANISOU 1758 OE1 GLU A 274 7877 6837 4940 -279 -64 1083 O ATOM 1759 OE2 GLU A 274 -62.212 4.256 8.929 1.00 66.41 O1- ANISOU 1759 OE2 GLU A 274 9718 8839 6677 -351 -126 1257 O1- ATOM 1760 N ALA A 275 -61.083 10.073 7.858 1.00 47.82 N ANISOU 1760 N ALA A 275 7303 6650 4215 -199 -11 698 N ATOM 1761 CA ALA A 275 -60.544 11.069 6.952 1.00 41.54 C ANISOU 1761 CA ALA A 275 6505 5799 3481 -137 -2 594 C ATOM 1762 C ALA A 275 -59.764 10.349 5.863 1.00 42.05 C ANISOU 1762 C ALA A 275 6599 5723 3653 -83 -31 633 C ATOM 1763 O ALA A 275 -59.236 9.255 6.086 1.00 41.99 O ANISOU 1763 O ALA A 275 6606 5679 3668 -85 -72 735 O ATOM 1764 CB ALA A 275 -59.632 12.077 7.683 1.00 34.87 C ANISOU 1764 CB ALA A 275 5628 5042 2577 -127 -15 543 C ATOM 1765 N ILE A 276 -59.704 10.960 4.675 1.00 38.04 N ANISOU 1765 N ILE A 276 6096 5141 3218 -35 -12 551 N ATOM 1766 CA ILE A 276 -58.898 10.434 3.577 1.00 39.12 C ANISOU 1766 CA ILE A 276 6251 5161 3452 17 -36 565 C ATOM 1767 C ILE A 276 -58.176 11.584 2.885 1.00 39.14 C ANISOU 1767 C ILE A 276 6241 5147 3484 65 -30 476 C ATOM 1768 O ILE A 276 -58.667 12.716 2.825 1.00 38.04 O ANISOU 1768 O ILE A 276 6082 5048 3322 62 2 395 O ATOM 1769 CB ILE A 276 -59.735 9.610 2.561 1.00 41.27 C ANISOU 1769 CB ILE A 276 6543 5342 3797 19 -19 576 C ATOM 1770 CG1 ILE A 276 -58.827 8.799 1.613 1.00 41.77 C ANISOU 1770 CG1 ILE A 276 6618 5296 3959 66 -50 600 C ATOM 1771 CG2 ILE A 276 -60.696 10.516 1.802 1.00 40.69 C ANISOU 1771 CG2 ILE A 276 6461 5268 3730 23 28 482 C ATOM 1772 CD1 ILE A 276 -59.558 8.013 0.534 1.00 40.89 C ANISOU 1772 CD1 ILE A 276 6516 5097 3924 72 -34 595 C ATOM 1773 N THR A 277 -56.990 11.280 2.366 1.00 42.38 N ANISOU 1773 N THR A 277 6657 5495 3951 108 -62 492 N ATOM 1774 CA THR A 277 -56.114 12.263 1.751 1.00 40.93 C ANISOU 1774 CA THR A 277 6460 5296 3797 151 -62 423 C ATOM 1775 C THR A 277 -55.681 11.740 0.389 1.00 38.87 C ANISOU 1775 C THR A 277 6210 4933 3627 192 -68 417 C ATOM 1776 O THR A 277 -55.225 10.596 0.271 1.00 38.94 O ANISOU 1776 O THR A 277 6230 4887 3679 201 -98 475 O ATOM 1777 CB THR A 277 -54.906 12.544 2.660 1.00 37.85 C ANISOU 1777 CB THR A 277 6055 4957 3368 161 -97 439 C ATOM 1778 CG2 THR A 277 -53.985 13.588 2.034 1.00 36.02 C ANISOU 1778 CG2 THR A 277 5807 4708 3171 203 -96 367 C ATOM 1779 OG1 THR A 277 -55.388 13.068 3.900 1.00 40.86 O ANISOU 1779 OG1 THR A 277 6419 5447 3658 119 -87 432 O ATOM 1780 N VAL A 278 -55.857 12.562 -0.635 1.00 34.73 N ANISOU 1780 N VAL A 278 5678 4387 3134 212 -41 347 N ATOM 1781 CA VAL A 278 -55.664 12.139 -2.019 1.00 34.07 C ANISOU 1781 CA VAL A 278 5597 4225 3123 242 -38 331 C ATOM 1782 C VAL A 278 -54.743 13.144 -2.698 1.00 31.29 C ANISOU 1782 C VAL A 278 5226 3869 2792 275 -38 276 C ATOM 1783 O VAL A 278 -55.129 14.304 -2.880 1.00 28.86 O ANISOU 1783 O VAL A 278 4904 3591 2470 272 -14 227 O ATOM 1784 CB VAL A 278 -57.006 12.028 -2.762 1.00 34.11 C ANISOU 1784 CB VAL A 278 5608 4210 3142 225 -3 309 C ATOM 1785 CG1 VAL A 278 -56.786 11.701 -4.253 1.00 32.09 C ANISOU 1785 CG1 VAL A 278 5348 3890 2953 254 2 280 C ATOM 1786 CG2 VAL A 278 -57.858 10.973 -2.114 1.00 37.96 C ANISOU 1786 CG2 VAL A 278 6112 4696 3616 191 -4 366 C ATOM 1787 N PRO A 279 -53.527 12.758 -3.077 1.00 29.23 N ANISOU 1787 N PRO A 279 4961 3573 2571 307 -65 283 N ATOM 1788 CA PRO A 279 -52.636 13.719 -3.728 1.00 31.78 C ANISOU 1788 CA PRO A 279 5264 3898 2913 334 -63 234 C ATOM 1789 C PRO A 279 -53.111 13.941 -5.156 1.00 30.82 C ANISOU 1789 C PRO A 279 5135 3748 2827 340 -36 196 C ATOM 1790 O PRO A 279 -53.413 12.987 -5.875 1.00 30.28 O ANISOU 1790 O PRO A 279 5073 3639 2793 342 -33 204 O ATOM 1791 CB PRO A 279 -51.267 13.033 -3.658 1.00 29.29 C ANISOU 1791 CB PRO A 279 4944 3554 2629 362 -100 256 C ATOM 1792 CG PRO A 279 -51.577 11.581 -3.626 1.00 31.86 C ANISOU 1792 CG PRO A 279 5285 3833 2987 356 -117 304 C ATOM 1793 CD PRO A 279 -52.955 11.402 -3.036 1.00 29.64 C ANISOU 1793 CD PRO A 279 5022 3575 2665 318 -97 333 C ATOM 1794 N MET A 280 -53.216 15.208 -5.543 1.00 30.81 N ANISOU 1794 N MET A 280 5115 3770 2819 340 -17 157 N ATOM 1795 CA MET A 280 -53.863 15.620 -6.788 1.00 32.81 C ANISOU 1795 CA MET A 280 5359 4012 3096 338 8 130 C ATOM 1796 C MET A 280 -53.180 16.884 -7.293 1.00 30.17 C ANISOU 1796 C MET A 280 4997 3692 2774 349 9 101 C ATOM 1797 O MET A 280 -52.341 16.826 -8.192 1.00 35.83 O ANISOU 1797 O MET A 280 5701 4398 3517 366 5 92 O ATOM 1798 CB MET A 280 -55.369 15.848 -6.551 1.00 33.29 C ANISOU 1798 CB MET A 280 5427 4087 3134 310 31 126 C ATOM 1799 CG MET A 280 -56.323 15.957 -7.740 1.00 30.90 C ANISOU 1799 CG MET A 280 5118 3771 2851 302 54 109 C ATOM 1800 SD MET A 280 -56.002 14.988 -9.223 1.00 28.39 S ANISOU 1800 SD MET A 280 4796 3422 2569 317 56 105 S ATOM 1801 CE MET A 280 -56.531 13.381 -8.613 1.00 31.97 C ANISOU 1801 CE MET A 280 5276 3843 3027 308 51 134 C ATOM 1802 N ASN A 281 -53.495 18.018 -6.680 1.00 29.89 N ANISOU 1802 N ASN A 281 4948 3683 2726 339 15 83 N ATOM 1803 CA ASN A 281 -52.946 19.305 -7.084 1.00 31.32 C ANISOU 1803 CA ASN A 281 5098 3871 2933 347 14 59 C ATOM 1804 C ASN A 281 -51.536 19.465 -6.523 1.00 31.92 C ANISOU 1804 C ASN A 281 5165 3956 3009 366 -8 55 C ATOM 1805 O ASN A 281 -51.331 19.421 -5.304 1.00 34.25 O ANISOU 1805 O ASN A 281 5464 4274 3276 364 -20 55 O ATOM 1806 CB ASN A 281 -53.862 20.436 -6.625 1.00 28.28 C ANISOU 1806 CB ASN A 281 4693 3502 2551 329 26 34 C ATOM 1807 CG ASN A 281 -55.280 20.304 -7.193 1.00 31.23 C ANISOU 1807 CG ASN A 281 5072 3865 2927 311 46 36 C ATOM 1808 ND2 ASN A 281 -56.269 20.102 -6.317 1.00 32.89 N ANISOU 1808 ND2 ASN A 281 5293 4093 3110 292 56 28 N ATOM 1809 OD1 ASN A 281 -55.482 20.402 -8.396 1.00 26.95 O ANISOU 1809 OD1 ASN A 281 4523 3308 2410 312 52 44 O ATOM 1810 N GLN A 282 -50.581 19.663 -7.429 1.00 30.59 N ANISOU 1810 N GLN A 282 4980 3776 2869 381 -13 52 N ATOM 1811 CA GLN A 282 -49.154 19.734 -7.134 1.00 28.57 C ANISOU 1811 CA GLN A 282 4712 3523 2620 402 -33 45 C ATOM 1812 C GLN A 282 -48.789 21.169 -6.773 1.00 28.42 C ANISOU 1812 C GLN A 282 4661 3518 2618 401 -35 20 C ATOM 1813 O GLN A 282 -48.836 22.066 -7.623 1.00 31.47 O ANISOU 1813 O GLN A 282 5021 3898 3037 395 -25 14 O ATOM 1814 CB GLN A 282 -48.356 19.250 -8.350 1.00 32.44 C ANISOU 1814 CB GLN A 282 5194 3999 3133 415 -34 46 C ATOM 1815 CG GLN A 282 -48.503 17.751 -8.650 1.00 29.05 C ANISOU 1815 CG GLN A 282 4786 3549 2703 421 -37 58 C ATOM 1816 CD GLN A 282 -47.757 17.322 -9.895 1.00 31.01 C ANISOU 1816 CD GLN A 282 5015 3793 2976 431 -34 42 C ATOM 1817 NE2 GLN A 282 -48.501 16.947 -10.938 1.00 31.29 N ANISOU 1817 NE2 GLN A 282 5046 3828 3013 419 -15 37 N ATOM 1818 OE1 GLN A 282 -46.528 17.326 -9.926 1.00 32.62 O ANISOU 1818 OE1 GLN A 282 5201 3998 3194 448 -49 28 O ATOM 1819 N MET A 283 -48.416 21.385 -5.517 1.00 32.14 N ANISOU 1819 N MET A 283 5129 4013 3070 404 -49 5 N ATOM 1820 CA MET A 283 -48.087 22.718 -5.035 1.00 27.77 C ANISOU 1820 CA MET A 283 4539 3474 2539 403 -51 -31 C ATOM 1821 C MET A 283 -46.753 23.194 -5.598 1.00 27.75 C ANISOU 1821 C MET A 283 4511 3460 2572 421 -62 -38 C ATOM 1822 O MET A 283 -45.815 22.410 -5.799 1.00 27.79 O ANISOU 1822 O MET A 283 4529 3462 2570 437 -74 -25 O ATOM 1823 CB MET A 283 -48.028 22.733 -3.511 1.00 28.12 C ANISOU 1823 CB MET A 283 4582 3560 2544 401 -63 -51 C ATOM 1824 CG MET A 283 -49.377 22.722 -2.837 1.00 29.69 C ANISOU 1824 CG MET A 283 4787 3784 2711 376 -49 -60 C ATOM 1825 SD MET A 283 -49.241 22.288 -1.115 1.00 30.11 S ANISOU 1825 SD MET A 283 4844 3905 2691 366 -65 -66 S ATOM 1826 CE MET A 283 -47.723 21.321 -1.143 1.00 30.35 C ANISOU 1826 CE MET A 283 4895 3924 2715 394 -97 -24 C ATOM 1827 N ALA A 284 -46.650 24.504 -5.799 1.00 27.75 N ANISOU 1827 N ALA A 284 4472 3453 2618 415 -58 -61 N ATOM 1828 CA ALA A 284 -45.484 25.005 -6.500 1.00 27.74 C ANISOU 1828 CA ALA A 284 4445 3441 2656 425 -64 -61 C ATOM 1829 C ALA A 284 -45.403 26.515 -6.332 1.00 29.86 C ANISOU 1829 C ALA A 284 4663 3699 2982 418 -65 -90 C ATOM 1830 O ALA A 284 -46.420 27.198 -6.128 1.00 29.69 O ANISOU 1830 O ALA A 284 4626 3670 2985 403 -58 -104 O ATOM 1831 CB ALA A 284 -45.538 24.628 -8.006 1.00 31.02 C ANISOU 1831 CB ALA A 284 4864 3842 3078 419 -52 -26 C ATOM 1832 N LEU A 285 -44.174 27.018 -6.426 1.00 28.07 N ANISOU 1832 N LEU A 285 4409 3470 2785 428 -75 -102 N ATOM 1833 CA LEU A 285 -43.891 28.449 -6.467 1.00 28.50 C ANISOU 1833 CA LEU A 285 4410 3506 2913 421 -79 -123 C ATOM 1834 C LEU A 285 -43.965 28.906 -7.914 1.00 31.10 C ANISOU 1834 C LEU A 285 4722 3811 3285 404 -71 -76 C ATOM 1835 O LEU A 285 -42.980 28.847 -8.653 1.00 32.29 O ANISOU 1835 O LEU A 285 4862 3965 3440 405 -72 -56 O ATOM 1836 CB LEU A 285 -42.514 28.730 -5.891 1.00 28.65 C ANISOU 1836 CB LEU A 285 4406 3536 2944 438 -94 -157 C ATOM 1837 CG LEU A 285 -42.317 28.686 -4.381 1.00 28.60 C ANISOU 1837 CG LEU A 285 4396 3563 2908 450 -106 -209 C ATOM 1838 CD1 LEU A 285 -40.838 28.838 -4.101 1.00 28.78 C ANISOU 1838 CD1 LEU A 285 4398 3596 2941 468 -122 -232 C ATOM 1839 CD2 LEU A 285 -43.103 29.797 -3.731 1.00 28.81 C ANISOU 1839 CD2 LEU A 285 4382 3586 2980 438 -103 -257 C ATOM 1840 N LEU A 286 -45.140 29.355 -8.340 1.00 31.00 N ANISOU 1840 N LEU A 286 4701 3779 3300 386 -65 -57 N ATOM 1841 CA LEU A 286 -45.238 29.959 -9.666 1.00 33.19 C ANISOU 1841 CA LEU A 286 4952 4037 3621 365 -63 -5 C ATOM 1842 C LEU A 286 -44.223 31.097 -9.779 1.00 32.63 C ANISOU 1842 C LEU A 286 4827 3947 3622 361 -74 -6 C ATOM 1843 O LEU A 286 -44.052 31.882 -8.846 1.00 34.80 O ANISOU 1843 O LEU A 286 5071 4203 3948 369 -85 -55 O ATOM 1844 CB LEU A 286 -46.665 30.490 -9.908 1.00 29.96 C ANISOU 1844 CB LEU A 286 4532 3604 3249 348 -61 12 C ATOM 1845 CG LEU A 286 -47.807 29.618 -10.453 1.00 28.78 C ANISOU 1845 CG LEU A 286 4421 3467 3047 339 -49 40 C ATOM 1846 CD1 LEU A 286 -47.880 28.269 -9.749 1.00 28.68 C ANISOU 1846 CD1 LEU A 286 4463 3483 2953 356 -39 14 C ATOM 1847 CD2 LEU A 286 -49.177 30.360 -10.355 1.00 27.95 C ANISOU 1847 CD2 LEU A 286 4294 3331 2994 326 -52 38 C ATOM 1848 N SER A 287 -43.524 31.176 -10.907 1.00 32.79 N ANISOU 1848 N SER A 287 4833 3977 3647 347 -72 41 N ATOM 1849 CA SER A 287 -42.674 32.330 -11.195 1.00 33.83 C ANISOU 1849 CA SER A 287 4910 4088 3857 335 -83 55 C ATOM 1850 C SER A 287 -43.011 32.888 -12.566 1.00 35.44 C ANISOU 1850 C SER A 287 5085 4287 4093 300 -84 135 C ATOM 1851 O SER A 287 -43.156 32.121 -13.523 1.00 35.56 O ANISOU 1851 O SER A 287 5123 4343 4043 288 -72 175 O ATOM 1852 CB SER A 287 -41.191 31.966 -11.164 1.00 32.04 C ANISOU 1852 CB SER A 287 4683 3889 3604 347 -81 36 C ATOM 1853 OG SER A 287 -40.722 31.601 -12.444 1.00 33.47 O ANISOU 1853 OG SER A 287 4861 4103 3752 328 -71 87 O ATOM 1854 N CYS A 288 -43.140 34.217 -12.664 1.00 37.75 N ANISOU 1854 N CYS A 288 5322 4532 4489 283 -101 159 N ATOM 1855 CA CYS A 288 -43.054 34.876 -13.967 1.00 37.64 C ANISOU 1855 CA CYS A 288 5269 4520 4514 245 -108 248 C ATOM 1856 C CYS A 288 -41.634 34.658 -14.453 1.00 37.22 C ANISOU 1856 C CYS A 288 5206 4508 4426 238 -99 259 C ATOM 1857 O CYS A 288 -40.715 35.350 -14.006 1.00 38.13 O ANISOU 1857 O CYS A 288 5287 4600 4603 242 -107 236 O ATOM 1858 CB CYS A 288 -43.377 36.378 -13.888 1.00 40.50 C ANISOU 1858 CB CYS A 288 5566 4811 5013 229 -134 274 C ATOM 1859 SG CYS A 288 -44.028 37.202 -15.429 1.00 42.58 S ANISOU 1859 SG CYS A 288 5783 5063 5333 178 -154 406 S ATOM 1860 N SER A 289 -41.446 33.699 -15.356 1.00 37.69 N ANISOU 1860 N SER A 289 5292 4633 4393 227 -82 286 N ATOM 1861 CA SER A 289 -40.112 33.195 -15.653 1.00 38.32 C ANISOU 1861 CA SER A 289 5371 4762 4426 228 -69 270 C ATOM 1862 C SER A 289 -39.403 33.987 -16.738 1.00 36.96 C ANISOU 1862 C SER A 289 5144 4616 4284 184 -71 342 C ATOM 1863 O SER A 289 -38.171 34.006 -16.774 1.00 35.40 O ANISOU 1863 O SER A 289 4927 4441 4083 183 -65 322 O ATOM 1864 CB SER A 289 -40.212 31.734 -16.068 1.00 32.90 C ANISOU 1864 CB SER A 289 4732 4136 3633 237 -49 250 C ATOM 1865 OG SER A 289 -41.284 31.600 -16.974 1.00 29.37 O ANISOU 1865 OG SER A 289 4288 3712 3158 212 -45 305 O ATOM 1866 N ASN A 290 -40.146 34.655 -17.609 1.00 35.77 N ANISOU 1866 N ASN A 290 4963 4463 4163 146 -81 427 N ATOM 1867 CA ASN A 290 -39.649 35.019 -18.927 1.00 39.87 C ANISOU 1867 CA ASN A 290 5439 5041 4668 95 -78 512 C ATOM 1868 C ASN A 290 -39.495 36.528 -19.050 1.00 42.01 C ANISOU 1868 C ASN A 290 5646 5255 5059 64 -104 582 C ATOM 1869 O ASN A 290 -40.492 37.262 -19.021 1.00 42.10 O ANISOU 1869 O ASN A 290 5640 5209 5146 56 -128 628 O ATOM 1870 CB ASN A 290 -40.595 34.481 -20.000 1.00 36.63 C ANISOU 1870 CB ASN A 290 5041 4692 4183 68 -71 568 C ATOM 1871 CG ASN A 290 -39.934 34.350 -21.347 1.00 38.10 C ANISOU 1871 CG ASN A 290 5193 4980 4303 18 -58 628 C ATOM 1872 ND2 ASN A 290 -40.617 33.670 -22.262 1.00 38.98 N ANISOU 1872 ND2 ASN A 290 5315 5166 4330 -3 -47 655 N ATOM 1873 OD1 ASN A 290 -38.811 34.834 -21.567 1.00 34.85 O ANISOU 1873 OD1 ASN A 290 4741 4588 3912 -3 -55 644 O ATOM 1874 N ALA A 291 -38.249 36.981 -19.228 1.00 42.04 N ANISOU 1874 N ALA A 291 5610 5273 5088 47 -102 592 N ATOM 1875 CA ALA A 291 -37.997 38.386 -19.526 1.00 42.61 C ANISOU 1875 CA ALA A 291 5614 5298 5277 9 -126 673 C ATOM 1876 C ALA A 291 -38.435 38.777 -20.935 1.00 40.65 C ANISOU 1876 C ALA A 291 5330 5102 5014 -54 -136 806 C ATOM 1877 O ALA A 291 -38.749 39.947 -21.155 1.00 39.40 O ANISOU 1877 O ALA A 291 5119 4884 4968 -83 -168 890 O ATOM 1878 CB ALA A 291 -36.515 38.712 -19.331 1.00 42.27 C ANISOU 1878 CB ALA A 291 5539 5261 5260 5 -119 645 C ATOM 1879 N ASP A 292 -38.473 37.831 -21.885 1.00 44.02 N ANISOU 1879 N ASP A 292 5778 5640 5310 -75 -113 825 N ATOM 1880 CA ASP A 292 -38.950 38.136 -23.237 1.00 40.47 C ANISOU 1880 CA ASP A 292 5291 5257 4827 -138 -123 951 C ATOM 1881 C ASP A 292 -40.365 38.684 -23.203 1.00 39.16 C ANISOU 1881 C ASP A 292 5123 5024 4732 -138 -155 1009 C ATOM 1882 O ASP A 292 -40.657 39.722 -23.802 1.00 38.51 O ANISOU 1882 O ASP A 292 4986 4918 4728 -183 -188 1127 O ATOM 1883 CB ASP A 292 -38.913 36.899 -24.126 1.00 39.53 C ANISOU 1883 CB ASP A 292 5197 5271 4551 -153 -90 933 C ATOM 1884 CG ASP A 292 -37.519 36.508 -24.515 1.00 52.07 C ANISOU 1884 CG ASP A 292 6765 6946 6073 -172 -61 901 C ATOM 1885 OD1 ASP A 292 -36.580 37.270 -24.200 1.00 54.50 O ANISOU 1885 OD1 ASP A 292 7038 7215 6455 -179 -67 909 O ATOM 1886 OD2 ASP A 292 -37.359 35.433 -25.139 1.00 56.50 O1- ANISOU 1886 OD2 ASP A 292 7342 7614 6514 -179 -32 860 O1- ATOM 1887 N LEU A 293 -41.255 37.998 -22.502 1.00 41.03 N ANISOU 1887 N LEU A 293 5416 5227 4947 -89 -150 930 N ATOM 1888 CA LEU A 293 -42.647 38.395 -22.374 1.00 41.70 C ANISOU 1888 CA LEU A 293 5502 5247 5093 -83 -178 965 C ATOM 1889 C LEU A 293 -42.887 39.385 -21.236 1.00 38.64 C ANISOU 1889 C LEU A 293 5095 4727 4861 -53 -205 930 C ATOM 1890 O LEU A 293 -44.041 39.611 -20.864 1.00 41.42 O ANISOU 1890 O LEU A 293 5452 5016 5269 -35 -225 924 O ATOM 1891 CB LEU A 293 -43.510 37.146 -22.193 1.00 43.36 C ANISOU 1891 CB LEU A 293 5780 5493 5202 -50 -155 894 C ATOM 1892 CG LEU A 293 -43.785 36.352 -23.477 1.00 37.96 C ANISOU 1892 CG LEU A 293 5102 4932 4389 -86 -139 944 C ATOM 1893 CD1 LEU A 293 -44.513 35.039 -23.186 1.00 33.33 C ANISOU 1893 CD1 LEU A 293 4581 4371 3712 -48 -114 857 C ATOM 1894 CD2 LEU A 293 -44.607 37.205 -24.385 1.00 33.13 C ANISOU 1894 CD2 LEU A 293 4443 4323 3821 -134 -173 1074 C ATOM 1895 N GLY A 294 -41.835 39.969 -20.666 1.00 39.67 N ANISOU 1895 N GLY A 294 5196 4813 5063 -46 -207 898 N ATOM 1896 CA GLY A 294 -41.981 41.131 -19.800 1.00 40.89 C ANISOU 1896 CA GLY A 294 5307 4846 5384 -30 -238 880 C ATOM 1897 C GLY A 294 -41.762 40.927 -18.310 1.00 41.05 C ANISOU 1897 C GLY A 294 5354 4812 5431 28 -226 737 C ATOM 1898 O GLY A 294 -41.889 41.899 -17.553 1.00 39.72 O ANISOU 1898 O GLY A 294 5142 4548 5403 41 -251 706 O ATOM 1899 N CYS A 295 -41.449 39.718 -17.854 1.00 38.05 N ANISOU 1899 N CYS A 295 5039 4491 4928 62 -192 649 N ATOM 1900 CA CYS A 295 -41.298 39.494 -16.425 1.00 37.69 C ANISOU 1900 CA CYS A 295 5018 4405 4897 113 -184 522 C ATOM 1901 C CYS A 295 -40.050 40.207 -15.914 1.00 39.41 C ANISOU 1901 C CYS A 295 5192 4590 5192 116 -189 488 C ATOM 1902 O CYS A 295 -39.045 40.333 -16.617 1.00 43.01 O ANISOU 1902 O CYS A 295 5624 5084 5632 88 -183 538 O ATOM 1903 CB CYS A 295 -41.226 37.997 -16.123 1.00 40.94 C ANISOU 1903 CB CYS A 295 5506 4888 5162 144 -152 453 C ATOM 1904 SG CYS A 295 -42.575 37.001 -16.851 1.00 38.85 S ANISOU 1904 SG CYS A 295 5294 4674 4795 137 -142 491 S ATOM 1905 N GLU A 296 -40.138 40.720 -14.694 1.00 41.02 N ANISOU 1905 N GLU A 296 5378 4727 5483 149 -200 399 N ATOM 1906 CA GLU A 296 -39.033 41.429 -14.069 1.00 40.59 C ANISOU 1906 CA GLU A 296 5276 4635 5510 156 -206 350 C ATOM 1907 C GLU A 296 -38.655 40.695 -12.790 1.00 41.63 C ANISOU 1907 C GLU A 296 5450 4790 5576 205 -189 221 C ATOM 1908 O GLU A 296 -39.492 40.060 -12.143 1.00 41.30 O ANISOU 1908 O GLU A 296 5452 4759 5480 232 -182 166 O ATOM 1909 CB GLU A 296 -39.384 42.913 -13.749 1.00 35.10 C ANISOU 1909 CB GLU A 296 4499 3833 5004 146 -241 355 C ATOM 1910 CG GLU A 296 -40.031 43.709 -14.893 1.00 42.20 C ANISOU 1910 CG GLU A 296 5352 4693 5988 100 -269 489 C ATOM 1911 CD GLU A 296 -39.035 44.246 -15.943 1.00 47.17 C ANISOU 1911 CD GLU A 296 5937 5338 6648 51 -276 599 C ATOM 1912 OE1 GLU A 296 -39.283 44.043 -17.161 1.00 45.78 O ANISOU 1912 OE1 GLU A 296 5768 5215 6413 10 -277 717 O ATOM 1913 OE2 GLU A 296 -38.017 44.886 -15.563 1.00 46.22 O1- ANISOU 1913 OE2 GLU A 296 5771 5184 6608 50 -280 569 O1- ATOM 1914 N GLY A 297 -37.385 40.755 -12.435 1.00 36.49 N ANISOU 1914 N GLY A 297 4785 4153 4928 214 -182 178 N ATOM 1915 CA GLY A 297 -36.979 40.238 -11.158 1.00 35.69 C ANISOU 1915 CA GLY A 297 4710 4070 4782 257 -174 62 C ATOM 1916 C GLY A 297 -36.033 39.067 -11.265 1.00 38.59 C ANISOU 1916 C GLY A 297 5129 4514 5021 272 -152 45 C ATOM 1917 O GLY A 297 -35.804 38.504 -12.344 1.00 38.44 O ANISOU 1917 O GLY A 297 5131 4542 4931 250 -139 114 O ATOM 1918 N PRO A 298 -35.455 38.677 -10.127 1.00 36.30 N ANISOU 1918 N PRO A 298 4853 4241 4698 308 -150 -50 N ATOM 1919 CA PRO A 298 -34.443 37.617 -10.153 1.00 37.54 C ANISOU 1919 CA PRO A 298 5051 4461 4752 325 -136 -71 C ATOM 1920 C PRO A 298 -34.987 36.242 -10.528 1.00 33.84 C ANISOU 1920 C PRO A 298 4654 4045 4161 334 -122 -49 C ATOM 1921 O PRO A 298 -34.197 35.388 -10.933 1.00 36.67 O ANISOU 1921 O PRO A 298 5036 4451 4447 338 -110 -47 O ATOM 1922 CB PRO A 298 -33.886 37.636 -8.725 1.00 39.16 C ANISOU 1922 CB PRO A 298 5248 4666 4964 362 -145 -176 C ATOM 1923 CG PRO A 298 -34.364 38.948 -8.118 1.00 38.37 C ANISOU 1923 CG PRO A 298 5086 4502 4991 357 -161 -212 C ATOM 1924 CD PRO A 298 -35.657 39.219 -8.774 1.00 35.24 C ANISOU 1924 CD PRO A 298 4692 4074 4625 334 -163 -146 C ATOM 1925 N GLN A 299 -36.293 35.997 -10.429 1.00 31.11 N ANISOU 1925 N GLN A 299 4338 3689 3795 335 -121 -37 N ATOM 1926 CA GLN A 299 -36.804 34.694 -10.832 1.00 34.33 C ANISOU 1926 CA GLN A 299 4808 4142 4094 341 -108 -16 C ATOM 1927 C GLN A 299 -36.880 34.525 -12.350 1.00 37.37 C ANISOU 1927 C GLN A 299 5191 4556 4453 306 -96 68 C ATOM 1928 O GLN A 299 -37.126 33.409 -12.815 1.00 36.59 O ANISOU 1928 O GLN A 299 5136 4500 4266 309 -82 79 O ATOM 1929 CB GLN A 299 -38.176 34.437 -10.208 1.00 30.32 C ANISOU 1929 CB GLN A 299 4332 3619 3569 352 -110 -34 C ATOM 1930 CG GLN A 299 -39.330 35.095 -10.918 1.00 32.65 C ANISOU 1930 CG GLN A 299 4608 3882 3916 324 -113 26 C ATOM 1931 CD GLN A 299 -39.298 36.602 -10.740 1.00 39.55 C ANISOU 1931 CD GLN A 299 5412 4694 4922 310 -131 25 C ATOM 1932 NE2 GLN A 299 -39.950 37.337 -11.651 1.00 36.86 N ANISOU 1932 NE2 GLN A 299 5038 4320 4646 278 -140 101 N ATOM 1933 OE1 GLN A 299 -38.684 37.103 -9.791 1.00 38.26 O ANISOU 1933 OE1 GLN A 299 5219 4512 4807 327 -139 -43 O ATOM 1934 N THR A 300 -36.671 35.587 -13.138 1.00 36.53 N ANISOU 1934 N THR A 300 5030 4429 4420 269 -101 129 N ATOM 1935 CA THR A 300 -36.502 35.398 -14.578 1.00 38.22 C ANISOU 1935 CA THR A 300 5235 4693 4593 230 -89 208 C ATOM 1936 C THR A 300 -35.214 34.648 -14.910 1.00 40.46 C ANISOU 1936 C THR A 300 5524 5038 4812 234 -73 182 C ATOM 1937 O THR A 300 -35.030 34.235 -16.060 1.00 40.22 O ANISOU 1937 O THR A 300 5489 5068 4724 204 -58 228 O ATOM 1938 CB THR A 300 -36.499 36.734 -15.340 1.00 36.45 C ANISOU 1938 CB THR A 300 4946 4439 4464 185 -102 292 C ATOM 1939 CG2 THR A 300 -37.719 37.583 -15.011 1.00 32.81 C ANISOU 1939 CG2 THR A 300 4467 3906 4092 182 -124 314 C ATOM 1940 OG1 THR A 300 -35.308 37.462 -15.027 1.00 40.14 O ANISOU 1940 OG1 THR A 300 5367 4886 4999 183 -108 270 O ATOM 1941 N ASP A 301 -34.337 34.461 -13.924 1.00 39.64 N ANISOU 1941 N ASP A 301 5425 4923 4713 269 -77 106 N ATOM 1942 CA ASP A 301 -33.063 33.781 -14.106 1.00 36.57 C ANISOU 1942 CA ASP A 301 5036 4583 4276 278 -66 70 C ATOM 1943 C ASP A 301 -33.253 32.313 -13.741 1.00 39.40 C ANISOU 1943 C ASP A 301 5454 4969 4546 314 -61 21 C ATOM 1944 O ASP A 301 -33.446 32.004 -12.547 1.00 41.11 O ANISOU 1944 O ASP A 301 5700 5157 4761 352 -73 -32 O ATOM 1945 CB ASP A 301 -32.014 34.428 -13.209 1.00 35.97 C ANISOU 1945 CB ASP A 301 4928 4477 4264 296 -78 15 C ATOM 1946 CG ASP A 301 -30.619 33.929 -13.469 1.00 34.50 C ANISOU 1946 CG ASP A 301 4729 4336 4044 301 -68 -18 C ATOM 1947 OD1 ASP A 301 -30.460 32.968 -14.246 1.00 30.71 O ANISOU 1947 OD1 ASP A 301 4267 3912 3490 294 -53 -12 O ATOM 1948 OD2 ASP A 301 -29.683 34.500 -12.854 1.00 35.47 O1- ANISOU 1948 OD2 ASP A 301 4819 4438 4220 312 -77 -60 O1- ATOM 1949 N PRO A 302 -33.199 31.377 -14.700 1.00 36.74 N ANISOU 1949 N PRO A 302 5130 4689 4139 302 -44 35 N ATOM 1950 CA PRO A 302 -33.562 29.983 -14.374 1.00 37.67 C ANISOU 1950 CA PRO A 302 5301 4820 4191 334 -42 -6 C ATOM 1951 C PRO A 302 -32.708 29.376 -13.269 1.00 36.48 C ANISOU 1951 C PRO A 302 5168 4655 4036 380 -57 -77 C ATOM 1952 O PRO A 302 -33.174 28.470 -12.559 1.00 33.68 O ANISOU 1952 O PRO A 302 4858 4288 3649 411 -66 -104 O ATOM 1953 CB PRO A 302 -33.371 29.249 -15.712 1.00 33.46 C ANISOU 1953 CB PRO A 302 4758 4355 3600 309 -21 9 C ATOM 1954 CG PRO A 302 -32.390 30.072 -16.455 1.00 33.77 C ANISOU 1954 CG PRO A 302 4739 4427 3663 273 -12 33 C ATOM 1955 CD PRO A 302 -32.651 31.498 -16.062 1.00 36.21 C ANISOU 1955 CD PRO A 302 5024 4683 4051 258 -26 77 C ATOM 1956 N ALA A 303 -31.472 29.865 -13.110 1.00 37.25 N ANISOU 1956 N ALA A 303 5228 4756 4168 382 -61 -104 N ATOM 1957 CA ALA A 303 -30.591 29.418 -12.035 1.00 33.48 C ANISOU 1957 CA ALA A 303 4760 4268 3693 424 -80 -169 C ATOM 1958 C ALA A 303 -31.173 29.763 -10.669 1.00 36.86 C ANISOU 1958 C ALA A 303 5210 4655 4142 449 -100 -188 C ATOM 1959 O ALA A 303 -31.215 28.916 -9.766 1.00 34.90 O ANISOU 1959 O ALA A 303 4996 4403 3860 483 -116 -221 O ATOM 1960 CB ALA A 303 -29.211 30.052 -12.200 1.00 31.79 C ANISOU 1960 CB ALA A 303 4494 4066 3519 416 -79 -192 C ATOM 1961 N VAL A 304 -31.604 31.016 -10.499 1.00 36.15 N ANISOU 1961 N VAL A 304 5091 4534 4109 430 -100 -169 N ATOM 1962 CA VAL A 304 -32.353 31.405 -9.304 1.00 35.85 C ANISOU 1962 CA VAL A 304 5065 4465 4090 447 -115 -193 C ATOM 1963 C VAL A 304 -33.502 30.431 -9.049 1.00 34.39 C ANISOU 1963 C VAL A 304 4937 4286 3844 458 -114 -182 C ATOM 1964 O VAL A 304 -33.711 29.969 -7.921 1.00 33.21 O ANISOU 1964 O VAL A 304 4814 4138 3666 484 -129 -216 O ATOM 1965 CB VAL A 304 -32.857 32.853 -9.447 1.00 36.40 C ANISOU 1965 CB VAL A 304 5091 4496 4243 419 -113 -169 C ATOM 1966 CG1 VAL A 304 -34.048 33.120 -8.542 1.00 33.90 C ANISOU 1966 CG1 VAL A 304 4788 4154 3937 427 -121 -187 C ATOM 1967 CG2 VAL A 304 -31.733 33.840 -9.166 1.00 34.75 C ANISOU 1967 CG2 VAL A 304 4825 4272 4106 417 -121 -201 C ATOM 1968 N ARG A 305 -34.261 30.093 -10.092 1.00 35.17 N ANISOU 1968 N ARG A 305 5052 4392 3918 436 -98 -132 N ATOM 1969 CA ARG A 305 -35.396 29.190 -9.895 1.00 35.46 C ANISOU 1969 CA ARG A 305 5139 4430 3903 444 -96 -121 C ATOM 1970 C ARG A 305 -34.937 27.837 -9.358 1.00 34.28 C ANISOU 1970 C ARG A 305 5027 4298 3700 476 -107 -151 C ATOM 1971 O ARG A 305 -35.459 27.360 -8.338 1.00 32.44 O ANISOU 1971 O ARG A 305 4825 4060 3440 495 -120 -166 O ATOM 1972 CB ARG A 305 -36.182 29.022 -11.194 1.00 35.78 C ANISOU 1972 CB ARG A 305 5185 4483 3926 414 -77 -67 C ATOM 1973 CG ARG A 305 -37.111 30.191 -11.517 1.00 37.33 C ANISOU 1973 CG ARG A 305 5358 4653 4174 385 -74 -25 C ATOM 1974 CD ARG A 305 -37.896 29.961 -12.818 1.00 33.71 C ANISOU 1974 CD ARG A 305 4904 4216 3689 355 -59 34 C ATOM 1975 NE ARG A 305 -37.422 30.830 -13.880 1.00 34.36 N ANISOU 1975 NE ARG A 305 4937 4313 3806 318 -54 82 N ATOM 1976 CZ ARG A 305 -37.073 30.437 -15.099 1.00 34.61 C ANISOU 1976 CZ ARG A 305 4955 4398 3796 293 -39 113 C ATOM 1977 NH1 ARG A 305 -37.203 29.181 -15.492 1.00 31.94 N1+ ANISOU 1977 NH1 ARG A 305 4649 4099 3388 302 -27 94 N1+ ATOM 1978 NH2 ARG A 305 -36.576 31.330 -15.947 1.00 34.79 N ANISOU 1978 NH2 ARG A 305 4928 4439 3852 255 -36 163 N ATOM 1979 N GLN A 306 -33.940 27.218 -10.022 1.00 33.06 N ANISOU 1979 N GLN A 306 4862 4165 3533 481 -105 -161 N ATOM 1980 CA GLN A 306 -33.434 25.907 -9.607 1.00 33.88 C ANISOU 1980 CA GLN A 306 4993 4276 3604 513 -120 -189 C ATOM 1981 C GLN A 306 -32.697 25.970 -8.268 1.00 34.53 C ANISOU 1981 C GLN A 306 5073 4352 3694 543 -148 -226 C ATOM 1982 O GLN A 306 -32.650 24.968 -7.543 1.00 34.53 O ANISOU 1982 O GLN A 306 5102 4351 3666 568 -170 -235 O ATOM 1983 CB GLN A 306 -32.517 25.317 -10.696 1.00 31.82 C ANISOU 1983 CB GLN A 306 4710 4041 3340 509 -111 -202 C ATOM 1984 CG GLN A 306 -33.224 24.999 -12.023 1.00 33.81 C ANISOU 1984 CG GLN A 306 4962 4316 3569 480 -84 -173 C ATOM 1985 CD GLN A 306 -33.142 23.511 -12.462 1.00 38.76 C ANISOU 1985 CD GLN A 306 5603 4954 4170 495 -85 -198 C ATOM 1986 NE2 GLN A 306 -33.715 23.211 -13.618 1.00 31.24 N ANISOU 1986 NE2 GLN A 306 4644 4031 3194 469 -62 -183 N ATOM 1987 OE1 GLN A 306 -32.576 22.657 -11.767 1.00 43.84 O ANISOU 1987 OE1 GLN A 306 6259 5579 4820 529 -109 -230 O ATOM 1988 N ALA A 307 -32.112 27.123 -7.921 1.00 34.43 N ANISOU 1988 N ALA A 307 5023 4337 3722 538 -151 -246 N ATOM 1989 CA ALA A 307 -31.533 27.284 -6.588 1.00 34.17 C ANISOU 1989 CA ALA A 307 4984 4308 3692 564 -177 -286 C ATOM 1990 C ALA A 307 -32.608 27.245 -5.513 1.00 30.72 C ANISOU 1990 C ALA A 307 4574 3871 3225 567 -186 -283 C ATOM 1991 O ALA A 307 -32.412 26.637 -4.458 1.00 31.40 O ANISOU 1991 O ALA A 307 4678 3975 3278 590 -212 -299 O ATOM 1992 CB ALA A 307 -30.755 28.594 -6.490 1.00 33.81 C ANISOU 1992 CB ALA A 307 4884 4258 3703 555 -175 -315 C ATOM 1993 N ILE A 308 -33.735 27.913 -5.757 1.00 29.26 N ANISOU 1993 N ILE A 308 4390 3673 3054 543 -168 -263 N ATOM 1994 CA ILE A 308 -34.867 27.847 -4.840 1.00 29.21 C ANISOU 1994 CA ILE A 308 4408 3673 3018 542 -172 -264 C ATOM 1995 C ILE A 308 -35.373 26.419 -4.746 1.00 35.60 C ANISOU 1995 C ILE A 308 5270 4491 3766 551 -178 -234 C ATOM 1996 O ILE A 308 -35.695 25.918 -3.659 1.00 36.07 O ANISOU 1996 O ILE A 308 5350 4571 3782 561 -195 -238 O ATOM 1997 CB ILE A 308 -35.974 28.814 -5.301 1.00 29.09 C ANISOU 1997 CB ILE A 308 4377 3635 3041 514 -151 -249 C ATOM 1998 CG1 ILE A 308 -35.521 30.269 -5.132 1.00 29.34 C ANISOU 1998 CG1 ILE A 308 4349 3650 3148 505 -152 -284 C ATOM 1999 CG2 ILE A 308 -37.300 28.506 -4.608 1.00 29.00 C ANISOU 1999 CG2 ILE A 308 4396 3632 2991 509 -149 -246 C ATOM 2000 CD1 ILE A 308 -36.424 31.272 -5.772 1.00 29.32 C ANISOU 2000 CD1 ILE A 308 4321 3612 3205 477 -137 -261 C ATOM 2001 N TYR A 309 -35.413 25.734 -5.888 1.00 33.52 N ANISOU 2001 N TYR A 309 5022 4214 3499 547 -166 -203 N ATOM 2002 CA TYR A 309 -35.861 24.351 -5.942 1.00 30.93 C ANISOU 2002 CA TYR A 309 4737 3885 3131 556 -172 -177 C ATOM 2003 C TYR A 309 -35.038 23.455 -5.020 1.00 34.76 C ANISOU 2003 C TYR A 309 5233 4379 3595 585 -206 -188 C ATOM 2004 O TYR A 309 -35.579 22.533 -4.396 1.00 36.19 O ANISOU 2004 O TYR A 309 5447 4561 3741 591 -222 -164 O ATOM 2005 CB TYR A 309 -35.781 23.889 -7.388 1.00 33.22 C ANISOU 2005 CB TYR A 309 5025 4166 3431 547 -153 -162 C ATOM 2006 CG TYR A 309 -35.961 22.417 -7.615 1.00 34.93 C ANISOU 2006 CG TYR A 309 5272 4374 3625 560 -161 -149 C ATOM 2007 CD1 TYR A 309 -37.206 21.818 -7.474 1.00 30.16 C ANISOU 2007 CD1 TYR A 309 4705 3761 2994 552 -156 -121 C ATOM 2008 CD2 TYR A 309 -34.877 21.625 -7.986 1.00 34.03 C ANISOU 2008 CD2 TYR A 309 5145 4258 3526 579 -174 -171 C ATOM 2009 CE1 TYR A 309 -37.358 20.473 -7.698 1.00 32.25 C ANISOU 2009 CE1 TYR A 309 4991 4010 3252 562 -165 -110 C ATOM 2010 CE2 TYR A 309 -35.018 20.288 -8.208 1.00 31.72 C ANISOU 2010 CE2 TYR A 309 4871 3949 3231 592 -184 -166 C ATOM 2011 CZ TYR A 309 -36.255 19.716 -8.069 1.00 33.17 C ANISOU 2011 CZ TYR A 309 5091 4120 3393 583 -180 -134 C ATOM 2012 OH TYR A 309 -36.382 18.370 -8.290 1.00 37.16 O ANISOU 2012 OH TYR A 309 5610 4602 3909 595 -192 -131 O ATOM 2013 N TYR A 310 -33.738 23.721 -4.896 1.00 34.80 N ANISOU 2013 N TYR A 310 5207 4390 3624 602 -221 -219 N ATOM 2014 CA TYR A 310 -32.879 22.911 -4.033 1.00 37.72 C ANISOU 2014 CA TYR A 310 5583 4769 3982 630 -259 -227 C ATOM 2015 C TYR A 310 -32.757 23.449 -2.606 1.00 35.77 C ANISOU 2015 C TYR A 310 5325 4555 3709 636 -281 -244 C ATOM 2016 O TYR A 310 -32.435 22.677 -1.700 1.00 36.82 O ANISOU 2016 O TYR A 310 5472 4705 3815 653 -316 -232 O ATOM 2017 CB TYR A 310 -31.479 22.786 -4.650 1.00 33.64 C ANISOU 2017 CB TYR A 310 5034 4246 3503 648 -267 -257 C ATOM 2018 CG TYR A 310 -31.403 21.844 -5.833 1.00 32.62 C ANISOU 2018 CG TYR A 310 4909 4096 3389 649 -256 -250 C ATOM 2019 CD1 TYR A 310 -31.325 20.468 -5.666 1.00 32.76 C ANISOU 2019 CD1 TYR A 310 4947 4093 3406 670 -283 -237 C ATOM 2020 CD2 TYR A 310 -31.445 22.342 -7.125 1.00 36.10 C ANISOU 2020 CD2 TYR A 310 5329 4540 3847 626 -220 -257 C ATOM 2021 CE1 TYR A 310 -31.261 19.611 -6.758 1.00 37.81 C ANISOU 2021 CE1 TYR A 310 5582 4716 4069 671 -273 -246 C ATOM 2022 CE2 TYR A 310 -31.389 21.501 -8.231 1.00 36.99 C ANISOU 2022 CE2 TYR A 310 5438 4649 3968 623 -208 -262 C ATOM 2023 CZ TYR A 310 -31.298 20.141 -8.047 1.00 41.06 C ANISOU 2023 CZ TYR A 310 5970 5143 4489 647 -233 -264 C ATOM 2024 OH TYR A 310 -31.240 19.330 -9.160 1.00 39.69 O ANISOU 2024 OH TYR A 310 5783 4967 4331 644 -220 -283 O ATOM 2025 N ALA A 311 -33.013 24.739 -2.377 1.00 35.21 N ANISOU 2025 N ALA A 311 5228 4498 3653 620 -264 -274 N ATOM 2026 CA ALA A 311 -32.921 25.292 -1.031 1.00 35.05 C ANISOU 2026 CA ALA A 311 5189 4519 3609 622 -282 -306 C ATOM 2027 C ALA A 311 -34.075 24.870 -0.141 1.00 39.53 C ANISOU 2027 C ALA A 311 5786 5116 4116 610 -286 -282 C ATOM 2028 O ALA A 311 -33.916 24.861 1.082 1.00 38.39 O ANISOU 2028 O ALA A 311 5633 5024 3930 613 -310 -297 O ATOM 2029 CB ALA A 311 -32.863 26.817 -1.080 1.00 35.68 C ANISOU 2029 CB ALA A 311 5222 4598 3738 609 -262 -355 C ATOM 2030 N MET A 312 -35.224 24.524 -0.720 1.00 43.85 N ANISOU 2030 N MET A 312 6365 5642 4655 593 -264 -245 N ATOM 2031 CA MET A 312 -36.355 24.065 0.074 1.00 43.73 C ANISOU 2031 CA MET A 312 6377 5656 4581 577 -266 -220 C ATOM 2032 C MET A 312 -36.004 22.820 0.881 1.00 41.75 C ANISOU 2032 C MET A 312 6152 5430 4281 591 -305 -179 C ATOM 2033 O MET A 312 -35.147 22.019 0.495 1.00 43.69 O ANISOU 2033 O MET A 312 6406 5647 4547 613 -326 -159 O ATOM 2034 CB MET A 312 -37.531 23.721 -0.827 1.00 43.49 C ANISOU 2034 CB MET A 312 6379 5590 4556 560 -238 -184 C ATOM 2035 CG MET A 312 -38.360 24.871 -1.250 1.00 42.16 C ANISOU 2035 CG MET A 312 6190 5410 4420 539 -206 -210 C ATOM 2036 SD MET A 312 -39.578 24.228 -2.388 1.00 39.61 S ANISOU 2036 SD MET A 312 5906 5048 4097 523 -180 -161 S ATOM 2037 CE MET A 312 -39.286 25.264 -3.832 1.00 31.37 C ANISOU 2037 CE MET A 312 4829 3965 3125 516 -157 -170 C ATOM 2038 N ASP A 313 -36.715 22.632 1.982 1.00 34.14 N ANISOU 2038 N ASP A 313 5198 4519 3254 574 -314 -165 N ATOM 2039 CA ASP A 313 -36.695 21.367 2.714 1.00 36.39 C ANISOU 2039 CA ASP A 313 5511 4826 3488 576 -350 -104 C ATOM 2040 C ASP A 313 -38.128 20.857 2.704 1.00 34.16 C ANISOU 2040 C ASP A 313 5263 4543 3172 549 -331 -61 C ATOM 2041 O ASP A 313 -38.985 21.356 3.441 1.00 32.56 O ANISOU 2041 O ASP A 313 5053 4396 2922 523 -317 -78 O ATOM 2042 CB ASP A 313 -36.150 21.533 4.135 1.00 38.56 C ANISOU 2042 CB ASP A 313 5761 5184 3707 575 -384 -116 C ATOM 2043 CG ASP A 313 -35.645 20.226 4.722 1.00 39.87 C ANISOU 2043 CG ASP A 313 5948 5360 3843 587 -435 -43 C ATOM 2044 OD1 ASP A 313 -36.482 19.405 5.154 1.00 42.91 O ANISOU 2044 OD1 ASP A 313 6361 5761 4182 566 -444 21 O ATOM 2045 OD2 ASP A 313 -34.409 20.009 4.732 1.00 38.13 O1- ANISOU 2045 OD2 ASP A 313 5712 5126 3651 616 -468 -47 O1- ATOM 2046 N ARG A 314 -38.390 19.876 1.843 1.00 36.74 N ANISOU 2046 N ARG A 314 5624 4809 3528 555 -330 -14 N ATOM 2047 CA ARG A 314 -39.764 19.441 1.633 1.00 34.29 C ANISOU 2047 CA ARG A 314 5343 4487 3197 530 -306 20 C ATOM 2048 C ARG A 314 -40.252 18.537 2.753 1.00 36.74 C ANISOU 2048 C ARG A 314 5675 4842 3444 512 -333 82 C ATOM 2049 O ARG A 314 -41.436 18.583 3.107 1.00 39.32 O ANISOU 2049 O ARG A 314 6014 5199 3728 481 -312 93 O ATOM 2050 CB ARG A 314 -39.879 18.755 0.280 1.00 35.36 C ANISOU 2050 CB ARG A 314 5500 4547 3389 542 -293 39 C ATOM 2051 CG ARG A 314 -39.669 19.741 -0.815 1.00 31.53 C ANISOU 2051 CG ARG A 314 4993 4035 2952 547 -261 -13 C ATOM 2052 CD ARG A 314 -39.560 19.097 -2.150 1.00 29.58 C ANISOU 2052 CD ARG A 314 4756 3731 2752 557 -251 -4 C ATOM 2053 NE ARG A 314 -39.398 20.142 -3.148 1.00 29.96 N ANISOU 2053 NE ARG A 314 4779 3769 2835 554 -220 -44 N ATOM 2054 CZ ARG A 314 -38.252 20.760 -3.404 1.00 33.78 C ANISOU 2054 CZ ARG A 314 5232 4255 3350 569 -225 -78 C ATOM 2055 NH1 ARG A 314 -37.095 20.310 -2.925 1.00 32.04 N1+ ANISOU 2055 NH1 ARG A 314 5001 4037 3135 593 -258 -83 N1+ ATOM 2056 NH2 ARG A 314 -38.262 21.856 -4.162 1.00 32.94 N ANISOU 2056 NH2 ARG A 314 5099 4144 3271 558 -198 -104 N ATOM 2057 N ASP A 315 -39.361 17.727 3.337 1.00 37.04 N ANISOU 2057 N ASP A 315 5713 4886 3474 528 -381 125 N ATOM 2058 CA ASP A 315 -39.710 17.045 4.579 1.00 33.17 C ANISOU 2058 CA ASP A 315 5232 4457 2913 504 -413 190 C ATOM 2059 C ASP A 315 -40.095 18.046 5.673 1.00 35.79 C ANISOU 2059 C ASP A 315 5537 4895 3166 476 -399 148 C ATOM 2060 O ASP A 315 -41.066 17.824 6.411 1.00 36.59 O ANISOU 2060 O ASP A 315 5647 5055 3200 439 -393 180 O ATOM 2061 CB ASP A 315 -38.549 16.157 5.035 1.00 33.82 C ANISOU 2061 CB ASP A 315 5309 4530 3009 528 -473 243 C ATOM 2062 CG ASP A 315 -38.449 14.854 4.239 1.00 37.31 C ANISOU 2062 CG ASP A 315 5776 4876 3524 546 -494 300 C ATOM 2063 OD1 ASP A 315 -39.235 14.654 3.294 1.00 34.83 O ANISOU 2063 OD1 ASP A 315 5482 4507 3246 541 -459 293 O ATOM 2064 OD2 ASP A 315 -37.601 14.006 4.587 1.00 38.58 O1- ANISOU 2064 OD2 ASP A 315 5931 5017 3711 566 -548 350 O1- ATOM 2065 N GLN A 316 -39.342 19.149 5.790 1.00 32.41 N ANISOU 2065 N GLN A 316 5071 4494 2747 490 -394 71 N ATOM 2066 CA GLN A 316 -39.647 20.179 6.775 1.00 32.68 C ANISOU 2066 CA GLN A 316 5069 4628 2721 466 -380 10 C ATOM 2067 C GLN A 316 -40.929 20.926 6.438 1.00 36.28 C ANISOU 2067 C GLN A 316 5521 5082 3180 440 -329 -38 C ATOM 2068 O GLN A 316 -41.735 21.208 7.327 1.00 38.57 O ANISOU 2068 O GLN A 316 5796 5457 3403 406 -317 -56 O ATOM 2069 CB GLN A 316 -38.480 21.157 6.894 1.00 35.15 C ANISOU 2069 CB GLN A 316 5338 4957 3063 490 -389 -65 C ATOM 2070 CG GLN A 316 -38.763 22.297 7.866 1.00 40.20 C ANISOU 2070 CG GLN A 316 5927 5695 3652 467 -373 -147 C ATOM 2071 CD GLN A 316 -37.563 23.217 8.135 1.00 43.43 C ANISOU 2071 CD GLN A 316 6286 6127 4088 489 -386 -224 C ATOM 2072 NE2 GLN A 316 -36.737 22.827 9.100 1.00 40.95 N ANISOU 2072 NE2 GLN A 316 5956 5885 3718 494 -430 -203 N ATOM 2073 OE1 GLN A 316 -37.375 24.243 7.477 1.00 36.75 O ANISOU 2073 OE1 GLN A 316 5413 5234 3316 502 -359 -295 O ATOM 2074 N LEU A 317 -41.134 21.272 5.163 1.00 37.37 N ANISOU 2074 N LEU A 317 5670 5133 3397 455 -299 -60 N ATOM 2075 CA LEU A 317 -42.339 21.995 4.775 1.00 33.93 C ANISOU 2075 CA LEU A 317 5229 4688 2975 434 -255 -101 C ATOM 2076 C LEU A 317 -43.603 21.173 5.023 1.00 37.63 C ANISOU 2076 C LEU A 317 5731 5175 3392 402 -244 -47 C ATOM 2077 O LEU A 317 -44.688 21.733 5.230 1.00 37.27 O ANISOU 2077 O LEU A 317 5672 5160 3328 375 -214 -85 O ATOM 2078 CB LEU A 317 -42.238 22.389 3.308 1.00 32.29 C ANISOU 2078 CB LEU A 317 5027 4387 2857 454 -232 -117 C ATOM 2079 CG LEU A 317 -41.425 23.649 3.048 1.00 38.15 C ANISOU 2079 CG LEU A 317 5723 5117 3657 470 -227 -188 C ATOM 2080 CD1 LEU A 317 -41.146 23.816 1.551 1.00 37.38 C ANISOU 2080 CD1 LEU A 317 5633 4933 3638 487 -211 -180 C ATOM 2081 CD2 LEU A 317 -42.164 24.858 3.585 1.00 37.35 C ANISOU 2081 CD2 LEU A 317 5578 5057 3557 448 -203 -262 C ATOM 2082 N ASN A 318 -43.484 19.848 5.001 1.00 37.79 N ANISOU 2082 N ASN A 318 5789 5171 3396 405 -270 39 N ATOM 2083 CA ASN A 318 -44.648 18.977 5.113 1.00 37.95 C ANISOU 2083 CA ASN A 318 5843 5196 3382 376 -261 99 C ATOM 2084 C ASN A 318 -45.016 18.714 6.574 1.00 36.85 C ANISOU 2084 C ASN A 318 5693 5167 3142 338 -277 127 C ATOM 2085 O ASN A 318 -46.203 18.620 6.921 1.00 35.64 O ANISOU 2085 O ASN A 318 5546 5054 2943 301 -253 134 O ATOM 2086 CB ASN A 318 -44.367 17.671 4.366 1.00 34.46 C ANISOU 2086 CB ASN A 318 5440 4669 2984 395 -283 176 C ATOM 2087 CG ASN A 318 -45.623 16.879 4.087 1.00 38.24 C ANISOU 2087 CG ASN A 318 5951 5122 3456 370 -264 224 C ATOM 2088 ND2 ASN A 318 -45.458 15.670 3.527 1.00 34.52 N ANISOU 2088 ND2 ASN A 318 5508 4579 3030 384 -285 288 N ATOM 2089 OD1 ASN A 318 -46.738 17.362 4.325 1.00 37.56 O ANISOU 2089 OD1 ASN A 318 5861 5075 3334 340 -231 198 O ATOM 2090 N ALA A 319 -44.012 18.618 7.444 1.00 36.46 N ANISOU 2090 N ALA A 319 5624 5175 3053 345 -316 141 N ATOM 2091 CA ALA A 319 -44.281 18.419 8.864 1.00 41.77 C ANISOU 2091 CA ALA A 319 6280 5973 3620 304 -334 170 C ATOM 2092 C ALA A 319 -44.771 19.701 9.531 1.00 39.79 C ANISOU 2092 C ALA A 319 5979 5819 3321 279 -301 64 C ATOM 2093 O ALA A 319 -45.638 19.648 10.407 1.00 41.48 O ANISOU 2093 O ALA A 319 6179 6130 3450 233 -289 68 O ATOM 2094 CB ALA A 319 -43.027 17.893 9.568 1.00 40.32 C ANISOU 2094 CB ALA A 319 6087 5824 3408 319 -391 222 C ATOM 2095 N LEU A 320 -44.232 20.856 9.131 1.00 40.11 N ANISOU 2095 N LEU A 320 5986 5835 3420 306 -286 -32 N ATOM 2096 CA LEU A 320 -44.600 22.133 9.736 1.00 35.80 C ANISOU 2096 CA LEU A 320 5382 5369 2852 287 -258 -146 C ATOM 2097 C LEU A 320 -45.846 22.747 9.104 1.00 38.41 C ANISOU 2097 C LEU A 320 5709 5659 3228 274 -210 -199 C ATOM 2098 O LEU A 320 -46.735 23.222 9.819 1.00 38.24 O ANISOU 2098 O LEU A 320 5653 5722 3156 237 -187 -256 O ATOM 2099 CB LEU A 320 -43.429 23.105 9.625 1.00 37.62 C ANISOU 2099 CB LEU A 320 5571 5585 3139 322 -268 -223 C ATOM 2100 CG LEU A 320 -42.131 22.646 10.278 1.00 41.67 C ANISOU 2100 CG LEU A 320 6078 6143 3612 338 -317 -186 C ATOM 2101 CD1 LEU A 320 -41.106 23.748 10.152 1.00 38.21 C ANISOU 2101 CD1 LEU A 320 5592 5692 3234 368 -319 -278 C ATOM 2102 CD2 LEU A 320 -42.399 22.345 11.762 1.00 41.28 C ANISOU 2102 CD2 LEU A 320 6004 6248 3434 294 -335 -170 C ATOM 2103 N ALA A 321 -45.920 22.785 7.769 1.00 35.62 N ANISOU 2103 N ALA A 321 5385 5182 2968 302 -196 -188 N ATOM 2104 CA ALA A 321 -46.938 23.607 7.122 1.00 36.40 C ANISOU 2104 CA ALA A 321 5469 5238 3124 294 -155 -249 C ATOM 2105 C ALA A 321 -48.171 22.818 6.693 1.00 40.96 C ANISOU 2105 C ALA A 321 6089 5785 3687 273 -135 -192 C ATOM 2106 O ALA A 321 -49.292 23.322 6.803 1.00 46.52 O ANISOU 2106 O ALA A 321 6773 6512 4389 247 -105 -242 O ATOM 2107 CB ALA A 321 -46.333 24.328 5.911 1.00 38.47 C ANISOU 2107 CB ALA A 321 5725 5395 3498 332 -150 -278 C ATOM 2108 N PHE A 322 -47.997 21.591 6.205 1.00 38.56 N ANISOU 2108 N PHE A 322 5841 5429 3381 282 -152 -94 N ATOM 2109 CA PHE A 322 -49.097 20.813 5.649 1.00 38.31 C ANISOU 2109 CA PHE A 322 5850 5355 3351 266 -134 -41 C ATOM 2110 C PHE A 322 -49.504 19.633 6.522 1.00 36.14 C ANISOU 2110 C PHE A 322 5601 5141 2991 233 -149 40 C ATOM 2111 O PHE A 322 -50.299 18.799 6.083 1.00 36.21 O ANISOU 2111 O PHE A 322 5646 5108 3005 220 -139 96 O ATOM 2112 CB PHE A 322 -48.735 20.329 4.238 1.00 35.74 C ANISOU 2112 CB PHE A 322 5561 4912 3105 301 -136 0 C ATOM 2113 CG PHE A 322 -48.224 21.428 3.361 1.00 39.82 C ANISOU 2113 CG PHE A 322 6053 5376 3702 329 -125 -62 C ATOM 2114 CD1 PHE A 322 -49.009 22.536 3.100 1.00 36.91 C ANISOU 2114 CD1 PHE A 322 5653 5003 3369 319 -96 -130 C ATOM 2115 CD2 PHE A 322 -46.931 21.392 2.853 1.00 40.29 C ANISOU 2115 CD2 PHE A 322 6113 5392 3804 364 -147 -53 C ATOM 2116 CE1 PHE A 322 -48.524 23.568 2.313 1.00 38.81 C ANISOU 2116 CE1 PHE A 322 5865 5192 3688 342 -90 -176 C ATOM 2117 CE2 PHE A 322 -46.448 22.427 2.070 1.00 35.67 C ANISOU 2117 CE2 PHE A 322 5500 4764 3289 384 -137 -103 C ATOM 2118 CZ PHE A 322 -47.244 23.516 1.808 1.00 33.94 C ANISOU 2118 CZ PHE A 322 5251 4538 3107 372 -110 -160 C ATOM 2119 N GLN A 323 -48.982 19.527 7.735 1.00 37.11 N ANISOU 2119 N GLN A 323 5702 5362 3036 216 -175 52 N ATOM 2120 CA GLN A 323 -49.464 18.508 8.658 1.00 40.25 C ANISOU 2120 CA GLN A 323 6115 5833 3345 174 -190 135 C ATOM 2121 C GLN A 323 -49.200 17.113 8.109 1.00 38.35 C ANISOU 2121 C GLN A 323 5926 5505 3139 189 -219 250 C ATOM 2122 O GLN A 323 -49.946 16.170 8.394 1.00 37.69 O ANISOU 2122 O GLN A 323 5867 5434 3020 155 -221 327 O ATOM 2123 CB GLN A 323 -50.958 18.698 8.963 1.00 38.73 C ANISOU 2123 CB GLN A 323 5913 5694 3108 127 -149 105 C ATOM 2124 CG GLN A 323 -51.267 19.884 9.893 1.00 37.88 C ANISOU 2124 CG GLN A 323 5741 5706 2944 100 -127 -5 C ATOM 2125 CD GLN A 323 -52.759 20.215 9.945 1.00 41.20 C ANISOU 2125 CD GLN A 323 6147 6159 3349 62 -81 -56 C ATOM 2126 NE2 GLN A 323 -53.088 21.480 9.754 1.00 35.92 N ANISOU 2126 NE2 GLN A 323 5432 5489 2728 69 -53 -177 N ATOM 2127 OE1 GLN A 323 -53.595 19.347 10.184 1.00 44.12 O ANISOU 2127 OE1 GLN A 323 6542 6554 3668 25 -74 11 O ATOM 2128 N GLY A 324 -48.154 16.996 7.285 1.00 36.76 N ANISOU 2128 N GLY A 324 5738 5214 3016 237 -240 256 N ATOM 2129 CA GLY A 324 -47.773 15.723 6.689 1.00 32.91 C ANISOU 2129 CA GLY A 324 5289 4635 2581 257 -270 346 C ATOM 2130 C GLY A 324 -48.746 15.184 5.669 1.00 32.45 C ANISOU 2130 C GLY A 324 5262 4492 2575 255 -242 363 C ATOM 2131 O GLY A 324 -48.639 14.016 5.277 1.00 32.55 O ANISOU 2131 O GLY A 324 5303 4436 2630 264 -265 437 O ATOM 2132 N THR A 325 -49.704 16.001 5.230 1.00 32.00 N ANISOU 2132 N THR A 325 5198 4437 2523 244 -195 294 N ATOM 2133 CA THR A 325 -50.655 15.610 4.198 1.00 35.28 C ANISOU 2133 CA THR A 325 5639 4777 2988 243 -166 300 C ATOM 2134 C THR A 325 -50.134 15.804 2.776 1.00 32.39 C ANISOU 2134 C THR A 325 5280 4315 2713 286 -159 267 C ATOM 2135 O THR A 325 -50.822 15.425 1.827 1.00 36.07 O ANISOU 2135 O THR A 325 5763 4719 3220 288 -139 272 O ATOM 2136 CB THR A 325 -51.978 16.364 4.381 1.00 35.40 C ANISOU 2136 CB THR A 325 5640 4841 2969 209 -122 245 C ATOM 2137 CG2 THR A 325 -52.413 16.314 5.837 1.00 33.51 C ANISOU 2137 CG2 THR A 325 5384 4719 2629 162 -125 262 C ATOM 2138 OG1 THR A 325 -51.861 17.709 3.899 1.00 30.96 O ANISOU 2138 OG1 THR A 325 5049 4272 2443 228 -100 152 O ATOM 2139 N ALA A 326 -48.938 16.352 2.608 1.00 36.34 N ANISOU 2139 N ALA A 326 5762 4806 3240 319 -176 235 N ATOM 2140 CA ALA A 326 -48.314 16.499 1.307 1.00 37.66 C ANISOU 2140 CA ALA A 326 5929 4895 3484 355 -172 209 C ATOM 2141 C ALA A 326 -47.519 15.240 0.960 1.00 38.38 C ANISOU 2141 C ALA A 326 6038 4927 3616 379 -207 265 C ATOM 2142 O ALA A 326 -47.194 14.428 1.833 1.00 36.75 O ANISOU 2142 O ALA A 326 5839 4740 3385 372 -243 326 O ATOM 2143 CB ALA A 326 -47.410 17.733 1.289 1.00 36.95 C ANISOU 2143 CB ALA A 326 5806 4824 3408 376 -172 144 C ATOM 2144 N SER A 327 -47.215 15.075 -0.335 1.00 32.09 N ANISOU 2144 N SER A 327 5243 4061 2887 404 -198 245 N ATOM 2145 CA SER A 327 -46.460 13.921 -0.800 1.00 30.18 C ANISOU 2145 CA SER A 327 5008 3759 2701 429 -229 279 C ATOM 2146 C SER A 327 -45.460 14.356 -1.864 1.00 31.57 C ANISOU 2146 C SER A 327 5163 3901 2930 461 -225 226 C ATOM 2147 O SER A 327 -45.504 15.479 -2.368 1.00 32.88 O ANISOU 2147 O SER A 327 5315 4084 3095 461 -196 176 O ATOM 2148 CB SER A 327 -47.386 12.827 -1.349 1.00 32.31 C ANISOU 2148 CB SER A 327 5299 3977 3001 417 -220 313 C ATOM 2149 OG SER A 327 -48.171 13.314 -2.430 1.00 37.60 O ANISOU 2149 OG SER A 327 5969 4632 3686 412 -177 267 O ATOM 2150 N GLU A 328 -44.558 13.446 -2.224 1.00 30.07 N ANISOU 2150 N GLU A 328 4968 3663 2794 487 -255 239 N ATOM 2151 CA GLU A 328 -43.464 13.823 -3.108 1.00 31.17 C ANISOU 2151 CA GLU A 328 5081 3783 2978 516 -254 188 C ATOM 2152 C GLU A 328 -43.972 14.091 -4.523 1.00 32.25 C ANISOU 2152 C GLU A 328 5213 3900 3141 512 -213 146 C ATOM 2153 O GLU A 328 -44.975 13.521 -4.973 1.00 30.57 O ANISOU 2153 O GLU A 328 5015 3665 2935 498 -196 158 O ATOM 2154 CB GLU A 328 -42.390 12.737 -3.133 1.00 30.29 C ANISOU 2154 CB GLU A 328 4960 3626 2925 544 -297 204 C ATOM 2155 CG GLU A 328 -42.945 11.370 -3.496 1.00 32.48 C ANISOU 2155 CG GLU A 328 5247 3844 3251 543 -308 237 C ATOM 2156 CD GLU A 328 -41.901 10.394 -4.008 1.00 36.81 C ANISOU 2156 CD GLU A 328 5769 4331 3884 575 -342 223 C ATOM 2157 OE1 GLU A 328 -40.685 10.721 -4.058 1.00 34.69 O ANISOU 2157 OE1 GLU A 328 5476 4069 3634 599 -359 190 O ATOM 2158 OE2 GLU A 328 -42.318 9.277 -4.369 1.00 38.22 O1- ANISOU 2158 OE2 GLU A 328 5949 4455 4120 575 -351 239 O1- ATOM 2159 N MET A 329 -43.263 14.978 -5.224 1.00 29.60 N ANISOU 2159 N MET A 329 4852 3577 2817 523 -198 99 N ATOM 2160 CA MET A 329 -43.587 15.350 -6.595 1.00 29.79 C ANISOU 2160 CA MET A 329 4863 3597 2858 516 -163 64 C ATOM 2161 C MET A 329 -42.317 15.409 -7.438 1.00 30.56 C ANISOU 2161 C MET A 329 4928 3690 2995 537 -167 23 C ATOM 2162 O MET A 329 -41.193 15.471 -6.920 1.00 30.08 O ANISOU 2162 O MET A 329 4853 3631 2945 557 -194 16 O ATOM 2163 CB MET A 329 -44.370 16.680 -6.648 1.00 28.37 C ANISOU 2163 CB MET A 329 4682 3451 2646 494 -132 54 C ATOM 2164 CG MET A 329 -43.583 17.918 -6.395 1.00 29.80 C ANISOU 2164 CG MET A 329 4839 3659 2825 499 -133 30 C ATOM 2165 SD MET A 329 -44.538 19.383 -6.859 1.00 29.78 S ANISOU 2165 SD MET A 329 4823 3676 2817 473 -99 16 S ATOM 2166 CE MET A 329 -44.489 19.226 -8.642 1.00 32.79 C ANISOU 2166 CE MET A 329 5187 4047 3224 468 -77 8 C ATOM 2167 N SER A 330 -42.520 15.336 -8.754 1.00 30.83 N ANISOU 2167 N SER A 330 4945 3723 3045 530 -141 -4 N ATOM 2168 CA SER A 330 -41.573 15.301 -9.860 1.00 28.67 C ANISOU 2168 CA SER A 330 4634 3458 2801 539 -134 -49 C ATOM 2169 C SER A 330 -41.343 16.708 -10.419 1.00 28.40 C ANISOU 2169 C SER A 330 4578 3466 2747 524 -110 -62 C ATOM 2170 O SER A 330 -42.301 17.475 -10.594 1.00 28.13 O ANISOU 2170 O SER A 330 4553 3447 2688 501 -88 -44 O ATOM 2171 CB SER A 330 -42.098 14.381 -10.974 1.00 29.85 C ANISOU 2171 CB SER A 330 4773 3596 2971 533 -118 -72 C ATOM 2172 OG SER A 330 -41.090 13.956 -11.889 1.00 30.61 O ANISOU 2172 OG SER A 330 4828 3701 3103 545 -118 -125 O ATOM 2173 N PRO A 331 -40.091 17.081 -10.703 1.00 28.52 N ANISOU 2173 N PRO A 331 4561 3497 2779 534 -115 -91 N ATOM 2174 CA PRO A 331 -39.857 18.302 -11.485 1.00 28.36 C ANISOU 2174 CA PRO A 331 4512 3515 2749 514 -91 -99 C ATOM 2175 C PRO A 331 -40.496 18.244 -12.870 1.00 32.88 C ANISOU 2175 C PRO A 331 5068 4115 3309 489 -61 -104 C ATOM 2176 O PRO A 331 -40.728 19.294 -13.487 1.00 28.88 O ANISOU 2176 O PRO A 331 4544 3640 2789 464 -41 -88 O ATOM 2177 CB PRO A 331 -38.326 18.384 -11.576 1.00 28.60 C ANISOU 2177 CB PRO A 331 4508 3555 2803 531 -104 -134 C ATOM 2178 CG PRO A 331 -37.784 17.302 -10.740 1.00 28.87 C ANISOU 2178 CG PRO A 331 4554 3553 2861 563 -139 -143 C ATOM 2179 CD PRO A 331 -38.851 16.320 -10.461 1.00 29.20 C ANISOU 2179 CD PRO A 331 4630 3565 2901 563 -144 -119 C ATOM 2180 N THR A 332 -40.803 17.044 -13.363 1.00 28.43 N ANISOU 2180 N THR A 332 4506 3542 2754 494 -59 -125 N ATOM 2181 CA THR A 332 -41.497 16.862 -14.625 1.00 28.42 C ANISOU 2181 CA THR A 332 4487 3575 2736 469 -32 -135 C ATOM 2182 C THR A 332 -42.986 17.126 -14.525 1.00 28.14 C ANISOU 2182 C THR A 332 4483 3532 2676 451 -19 -96 C ATOM 2183 O THR A 332 -43.635 17.255 -15.568 1.00 29.24 O ANISOU 2183 O THR A 332 4607 3708 2795 426 4 -95 O ATOM 2184 CB THR A 332 -41.307 15.433 -15.142 1.00 31.14 C ANISOU 2184 CB THR A 332 4815 3909 3108 483 -35 -185 C ATOM 2185 CG2 THR A 332 -39.861 14.990 -14.989 1.00 30.81 C ANISOU 2185 CG2 THR A 332 4744 3858 3105 508 -56 -229 C ATOM 2186 OG1 THR A 332 -42.146 14.546 -14.390 1.00 30.89 O ANISOU 2186 OG1 THR A 332 4821 3822 3094 495 -50 -166 O ATOM 2187 N PHE A 333 -43.541 17.153 -13.317 1.00 27.99 N ANISOU 2187 N PHE A 333 4504 3475 2657 460 -33 -65 N ATOM 2188 CA PHE A 333 -44.934 17.482 -13.002 1.00 27.75 C ANISOU 2188 CA PHE A 333 4502 3435 2606 444 -23 -32 C ATOM 2189 C PHE A 333 -45.919 16.379 -13.344 1.00 27.78 C ANISOU 2189 C PHE A 333 4522 3425 2610 439 -15 -36 C ATOM 2190 O PHE A 333 -47.128 16.606 -13.320 1.00 27.60 O ANISOU 2190 O PHE A 333 4517 3401 2569 423 -2 -14 O ATOM 2191 CB PHE A 333 -45.378 18.804 -13.642 1.00 27.57 C ANISOU 2191 CB PHE A 333 4461 3445 2568 417 -4 -11 C ATOM 2192 CG PHE A 333 -44.996 20.000 -12.823 1.00 29.26 C ANISOU 2192 CG PHE A 333 4673 3654 2793 419 -14 3 C ATOM 2193 CD1 PHE A 333 -43.705 20.511 -12.881 1.00 28.52 C ANISOU 2193 CD1 PHE A 333 4551 3572 2714 427 -22 -10 C ATOM 2194 CD2 PHE A 333 -45.896 20.559 -11.914 1.00 31.61 C ANISOU 2194 CD2 PHE A 333 4990 3933 3087 414 -17 21 C ATOM 2195 CE1 PHE A 333 -43.340 21.586 -12.079 1.00 30.44 C ANISOU 2195 CE1 PHE A 333 4785 3806 2972 429 -32 -4 C ATOM 2196 CE2 PHE A 333 -45.534 21.621 -11.123 1.00 27.35 C ANISOU 2196 CE2 PHE A 333 4440 3390 2563 417 -26 20 C ATOM 2197 CZ PHE A 333 -44.256 22.133 -11.204 1.00 27.62 C ANISOU 2197 CZ PHE A 333 4446 3432 2615 425 -35 8 C ATOM 2198 N ALA A 334 -45.447 15.179 -13.626 1.00 28.06 N ANISOU 2198 N ALA A 334 4546 3443 2671 455 -23 -68 N ATOM 2199 CA ALA A 334 -46.350 14.037 -13.672 1.00 32.69 C ANISOU 2199 CA ALA A 334 5149 3999 3272 454 -22 -71 C ATOM 2200 C ALA A 334 -46.766 13.678 -12.249 1.00 31.83 C ANISOU 2200 C ALA A 334 5081 3845 3167 462 -43 -29 C ATOM 2201 O ALA A 334 -45.926 13.594 -11.344 1.00 28.34 O ANISOU 2201 O ALA A 334 4646 3385 2737 481 -70 -17 O ATOM 2202 CB ALA A 334 -45.698 12.828 -14.364 1.00 28.55 C ANISOU 2202 CB ALA A 334 4592 3463 2792 469 -28 -124 C ATOM 2203 N LEU A 335 -48.067 13.462 -12.072 1.00 29.42 N ANISOU 2203 N LEU A 335 4801 3529 2848 446 -31 -7 N ATOM 2204 CA LEU A 335 -48.613 13.050 -10.797 1.00 29.42 C ANISOU 2204 CA LEU A 335 4837 3498 2842 445 -47 35 C ATOM 2205 C LEU A 335 -47.864 11.847 -10.255 1.00 34.51 C ANISOU 2205 C LEU A 335 5482 4098 3534 467 -80 42 C ATOM 2206 O LEU A 335 -47.617 10.878 -10.971 1.00 34.99 O ANISOU 2206 O LEU A 335 5520 4131 3642 477 -85 11 O ATOM 2207 CB LEU A 335 -50.097 12.725 -10.947 1.00 30.67 C ANISOU 2207 CB LEU A 335 5013 3649 2989 423 -26 47 C ATOM 2208 CG LEU A 335 -50.998 13.855 -10.440 1.00 31.76 C ANISOU 2208 CG LEU A 335 5169 3816 3082 403 -10 69 C ATOM 2209 CD1 LEU A 335 -52.450 13.413 -10.276 1.00 30.80 C ANISOU 2209 CD1 LEU A 335 5069 3684 2950 382 5 84 C ATOM 2210 CD2 LEU A 335 -50.434 14.388 -9.128 1.00 29.98 C ANISOU 2210 CD2 LEU A 335 4955 3598 2837 408 -30 92 C ATOM 2211 N LEU A 336 -47.478 11.933 -8.983 1.00 32.11 N ANISOU 2211 N LEU A 336 5196 3787 3216 473 -107 81 N ATOM 2212 CA LEU A 336 -46.894 10.801 -8.321 1.00 33.09 C ANISOU 2212 CA LEU A 336 5321 3866 3384 489 -146 107 C ATOM 2213 C LEU A 336 -47.870 10.249 -7.282 1.00 36.33 C ANISOU 2213 C LEU A 336 5765 4262 3778 470 -156 168 C ATOM 2214 O LEU A 336 -48.521 11.016 -6.559 1.00 31.38 O ANISOU 2214 O LEU A 336 5158 3673 3089 449 -143 193 O ATOM 2215 CB LEU A 336 -45.569 11.186 -7.649 1.00 34.18 C ANISOU 2215 CB LEU A 336 5450 4015 3522 510 -176 111 C ATOM 2216 CG LEU A 336 -44.404 11.480 -8.595 1.00 29.35 C ANISOU 2216 CG LEU A 336 4801 3411 2938 531 -173 52 C ATOM 2217 CD1 LEU A 336 -43.174 11.883 -7.812 1.00 31.24 C ANISOU 2217 CD1 LEU A 336 5033 3662 3176 550 -203 58 C ATOM 2218 CD2 LEU A 336 -44.112 10.256 -9.468 1.00 33.26 C ANISOU 2218 CD2 LEU A 336 5269 3863 3508 546 -182 14 C ATOM 2219 N PRO A 337 -48.015 8.926 -7.214 1.00 35.93 N ANISOU 2219 N PRO A 337 5713 4154 3784 473 -178 192 N ATOM 2220 CA PRO A 337 -47.309 7.928 -8.004 1.00 35.68 C ANISOU 2220 CA PRO A 337 5649 4069 3839 498 -196 154 C ATOM 2221 C PRO A 337 -48.052 7.592 -9.282 1.00 31.72 C ANISOU 2221 C PRO A 337 5131 3559 3363 490 -162 100 C ATOM 2222 O PRO A 337 -47.544 6.851 -10.109 1.00 32.75 O ANISOU 2222 O PRO A 337 5225 3657 3563 508 -169 48 O ATOM 2223 CB PRO A 337 -47.269 6.736 -7.046 1.00 36.89 C ANISOU 2223 CB PRO A 337 5810 4163 4043 500 -242 221 C ATOM 2224 CG PRO A 337 -48.629 6.805 -6.396 1.00 38.25 C ANISOU 2224 CG PRO A 337 6019 4354 4162 464 -224 276 C ATOM 2225 CD PRO A 337 -48.965 8.291 -6.290 1.00 36.76 C ANISOU 2225 CD PRO A 337 5846 4243 3877 449 -188 259 C ATOM 2226 N ALA A 338 -49.246 8.161 -9.446 1.00 31.74 N ANISOU 2226 N ALA A 338 5154 3595 3310 464 -126 105 N ATOM 2227 CA ALA A 338 -50.213 7.655 -10.412 1.00 32.39 C ANISOU 2227 CA ALA A 338 5226 3665 3414 452 -99 71 C ATOM 2228 C ALA A 338 -49.693 7.740 -11.850 1.00 37.18 C ANISOU 2228 C ALA A 338 5789 4295 4041 463 -80 -11 C ATOM 2229 O ALA A 338 -49.983 6.864 -12.681 1.00 36.08 O ANISOU 2229 O ALA A 338 5622 4133 3955 464 -73 -57 O ATOM 2230 CB ALA A 338 -51.525 8.422 -10.258 1.00 29.23 C ANISOU 2230 CB ALA A 338 4855 3305 2946 422 -66 92 C ATOM 2231 N GLN A 339 -48.916 8.771 -12.159 1.00 30.12 N ANISOU 2231 N GLN A 339 4883 3452 3108 469 -72 -32 N ATOM 2232 CA GLN A 339 -48.323 8.933 -13.477 1.00 34.69 C ANISOU 2232 CA GLN A 339 5417 4068 3695 474 -55 -103 C ATOM 2233 C GLN A 339 -46.811 8.740 -13.459 1.00 36.70 C ANISOU 2233 C GLN A 339 5642 4314 3990 501 -80 -133 C ATOM 2234 O GLN A 339 -46.083 9.443 -14.160 1.00 36.05 O ANISOU 2234 O GLN A 339 5531 4282 3883 501 -67 -170 O ATOM 2235 CB GLN A 339 -48.652 10.301 -14.051 1.00 33.02 C ANISOU 2235 CB GLN A 339 5207 3929 3411 454 -23 -103 C ATOM 2236 CG GLN A 339 -50.106 10.603 -14.085 1.00 30.29 C ANISOU 2236 CG GLN A 339 4887 3595 3029 430 0 -77 C ATOM 2237 CD GLN A 339 -50.365 12.040 -14.439 1.00 35.52 C ANISOU 2237 CD GLN A 339 5549 4314 3631 412 21 -63 C ATOM 2238 NE2 GLN A 339 -51.638 12.417 -14.461 1.00 34.73 N ANISOU 2238 NE2 GLN A 339 5468 4224 3503 391 39 -42 N ATOM 2239 OE1 GLN A 339 -49.428 12.819 -14.670 1.00 31.64 O ANISOU 2239 OE1 GLN A 339 5039 3855 3127 416 19 -70 O ATOM 2240 N GLU A 340 -46.324 7.785 -12.660 1.00 35.21 N ANISOU 2240 N GLU A 340 5455 4059 3866 522 -120 -113 N ATOM 2241 CA GLU A 340 -44.889 7.514 -12.636 1.00 36.77 C ANISOU 2241 CA GLU A 340 5618 4239 4112 549 -149 -145 C ATOM 2242 C GLU A 340 -44.430 6.893 -13.956 1.00 41.58 C ANISOU 2242 C GLU A 340 6167 4858 4775 557 -137 -242 C ATOM 2243 O GLU A 340 -43.327 7.185 -14.435 1.00 42.83 O ANISOU 2243 O GLU A 340 6288 5048 4939 569 -137 -293 O ATOM 2244 CB GLU A 340 -44.533 6.618 -11.437 1.00 36.77 C ANISOU 2244 CB GLU A 340 5633 4164 4174 568 -200 -91 C ATOM 2245 CG GLU A 340 -44.295 5.105 -11.742 1.00 41.01 C ANISOU 2245 CG GLU A 340 6130 4623 4831 587 -230 -127 C ATOM 2246 CD GLU A 340 -44.065 4.219 -10.473 1.00 48.27 C ANISOU 2246 CD GLU A 340 7064 5461 5814 601 -288 -49 C ATOM 2247 OE1 GLU A 340 -45.039 3.988 -9.711 1.00 42.03 O ANISOU 2247 OE1 GLU A 340 6313 4650 5005 581 -293 28 O ATOM 2248 OE2 GLU A 340 -42.919 3.737 -10.250 1.00 48.66 O1- ANISOU 2248 OE2 GLU A 340 7082 5471 5935 629 -330 -62 O1- ATOM 2249 N GLN A 341 -45.267 6.066 -14.586 1.00 37.70 N ANISOU 2249 N GLN A 341 5658 4346 4320 548 -124 -276 N ATOM 2250 CA GLN A 341 -44.822 5.445 -15.831 1.00 43.75 C ANISOU 2250 CA GLN A 341 6355 5129 5137 554 -112 -382 C ATOM 2251 C GLN A 341 -44.781 6.417 -17.006 1.00 43.04 C ANISOU 2251 C GLN A 341 6240 5147 4965 531 -68 -430 C ATOM 2252 O GLN A 341 -44.344 6.027 -18.093 1.00 40.62 O ANISOU 2252 O GLN A 341 5871 4880 4683 530 -54 -524 O ATOM 2253 CB GLN A 341 -45.713 4.253 -16.190 1.00 43.86 C ANISOU 2253 CB GLN A 341 6350 5092 5222 551 -111 -414 C ATOM 2254 CG GLN A 341 -46.929 4.624 -17.001 1.00 41.37 C ANISOU 2254 CG GLN A 341 6041 4838 4840 520 -66 -429 C ATOM 2255 CD GLN A 341 -48.012 5.266 -16.159 1.00 48.51 C ANISOU 2255 CD GLN A 341 7016 5738 5677 501 -59 -330 C ATOM 2256 NE2 GLN A 341 -49.081 5.724 -16.826 1.00 45.03 N ANISOU 2256 NE2 GLN A 341 6583 5352 5175 474 -22 -336 N ATOM 2257 OE1 GLN A 341 -47.892 5.366 -14.917 1.00 47.46 O ANISOU 2257 OE1 GLN A 341 6928 5560 5545 509 -86 -251 O ATOM 2258 N PHE A 342 -45.220 7.656 -16.820 1.00 40.96 N ANISOU 2258 N PHE A 342 6019 4935 4610 511 -47 -370 N ATOM 2259 CA PHE A 342 -45.127 8.685 -17.841 1.00 42.20 C ANISOU 2259 CA PHE A 342 6153 5191 4691 487 -12 -394 C ATOM 2260 C PHE A 342 -43.851 9.506 -17.746 1.00 40.04 C ANISOU 2260 C PHE A 342 5866 4952 4397 494 -18 -394 C ATOM 2261 O PHE A 342 -43.574 10.300 -18.648 1.00 44.04 O ANISOU 2261 O PHE A 342 6343 5542 4850 472 7 -415 O ATOM 2262 CB PHE A 342 -46.354 9.595 -17.753 1.00 40.47 C ANISOU 2262 CB PHE A 342 5977 5000 4398 460 10 -328 C ATOM 2263 CG PHE A 342 -47.522 9.083 -18.541 1.00 45.97 C ANISOU 2263 CG PHE A 342 6662 5715 5090 441 33 -356 C ATOM 2264 CD1 PHE A 342 -47.359 8.035 -19.451 1.00 47.31 C ANISOU 2264 CD1 PHE A 342 6774 5894 5306 444 39 -446 C ATOM 2265 CD2 PHE A 342 -48.796 9.566 -18.311 1.00 45.05 C ANISOU 2265 CD2 PHE A 342 6587 5600 4930 422 46 -301 C ATOM 2266 CE1 PHE A 342 -48.445 7.534 -20.163 1.00 45.87 C ANISOU 2266 CE1 PHE A 342 6577 5730 5120 427 59 -478 C ATOM 2267 CE2 PHE A 342 -49.888 9.078 -19.021 1.00 45.30 C ANISOU 2267 CE2 PHE A 342 6606 5647 4957 405 66 -329 C ATOM 2268 CZ PHE A 342 -49.711 8.053 -19.941 1.00 47.17 C ANISOU 2268 CZ PHE A 342 6788 5898 5237 408 73 -416 C ATOM 2269 N ILE A 343 -43.062 9.314 -16.706 1.00 41.43 N ANISOU 2269 N ILE A 343 6058 5069 4615 521 -53 -370 N ATOM 2270 CA ILE A 343 -41.817 10.049 -16.540 1.00 41.74 C ANISOU 2270 CA ILE A 343 6083 5134 4641 531 -62 -373 C ATOM 2271 C ILE A 343 -40.768 9.491 -17.490 1.00 41.50 C ANISOU 2271 C ILE A 343 5981 5134 4651 538 -59 -470 C ATOM 2272 O ILE A 343 -40.687 8.279 -17.730 1.00 39.69 O ANISOU 2272 O ILE A 343 5719 4864 4497 554 -72 -530 O ATOM 2273 CB ILE A 343 -41.364 9.992 -15.072 1.00 39.46 C ANISOU 2273 CB ILE A 343 5834 4779 4381 557 -102 -317 C ATOM 2274 CG1 ILE A 343 -42.399 10.733 -14.212 1.00 35.95 C ANISOU 2274 CG1 ILE A 343 5450 4329 3880 542 -97 -233 C ATOM 2275 CG2 ILE A 343 -39.941 10.532 -14.915 1.00 35.44 C ANISOU 2275 CG2 ILE A 343 5300 4289 3875 572 -116 -336 C ATOM 2276 CD1 ILE A 343 -42.060 10.814 -12.752 1.00 34.78 C ANISOU 2276 CD1 ILE A 343 5339 4138 3739 560 -133 -174 C ATOM 2277 N SER A 344 -39.969 10.394 -18.038 1.00 40.71 N ANISOU 2277 N SER A 344 5853 5107 4507 525 -41 -489 N ATOM 2278 CA SER A 344 -39.056 10.065 -19.118 1.00 43.18 C ANISOU 2278 CA SER A 344 6091 5478 4836 521 -28 -586 C ATOM 2279 C SER A 344 -37.829 9.318 -18.606 1.00 40.48 C ANISOU 2279 C SER A 344 5721 5078 4581 559 -64 -634 C ATOM 2280 O SER A 344 -37.134 9.789 -17.701 1.00 41.83 O ANISOU 2280 O SER A 344 5918 5219 4758 577 -89 -591 O ATOM 2281 CB SER A 344 -38.638 11.351 -19.833 1.00 42.73 C ANISOU 2281 CB SER A 344 6015 5523 4700 487 3 -575 C ATOM 2282 OG SER A 344 -37.398 11.188 -20.480 1.00 44.83 O ANISOU 2282 OG SER A 344 6213 5838 4983 488 8 -657 O ATOM 2283 N GLY A 345 -37.540 8.173 -19.232 1.00 42.23 N ANISOU 2283 N GLY A 345 5882 5289 4873 571 -69 -731 N ATOM 2284 CA GLY A 345 -36.365 7.372 -18.934 1.00 40.26 C ANISOU 2284 CA GLY A 345 5590 4986 4722 607 -105 -794 C ATOM 2285 C GLY A 345 -35.035 8.099 -19.071 1.00 42.22 C ANISOU 2285 C GLY A 345 5806 5287 4948 608 -102 -823 C ATOM 2286 O GLY A 345 -34.013 7.553 -18.647 1.00 46.27 O ANISOU 2286 O GLY A 345 6290 5749 5542 641 -137 -863 O ATOM 2287 N GLU A 346 -35.012 9.298 -19.646 1.00 43.29 N ANISOU 2287 N GLU A 346 5942 5520 4984 571 -63 -801 N ATOM 2288 CA GLU A 346 -33.799 10.104 -19.749 1.00 43.40 C ANISOU 2288 CA GLU A 346 5929 5587 4973 566 -58 -817 C ATOM 2289 C GLU A 346 -33.827 11.280 -18.781 1.00 45.72 C ANISOU 2289 C GLU A 346 6289 5863 5219 566 -67 -709 C ATOM 2290 O GLU A 346 -33.343 12.371 -19.092 1.00 46.96 O ANISOU 2290 O GLU A 346 6435 6087 5320 541 -45 -692 O ATOM 2291 CB GLU A 346 -33.584 10.612 -21.173 1.00 48.68 C ANISOU 2291 CB GLU A 346 6535 6388 5572 520 -9 -875 C ATOM 2292 CG GLU A 346 -33.155 9.570 -22.191 1.00 44.25 C ANISOU 2292 CG GLU A 346 5886 5872 5057 518 3 -1011 C ATOM 2293 CD GLU A 346 -34.316 8.726 -22.650 1.00 48.46 C ANISOU 2293 CD GLU A 346 6415 6395 5603 512 12 -1039 C ATOM 2294 OE1 GLU A 346 -35.481 9.123 -22.386 1.00 44.95 O ANISOU 2294 OE1 GLU A 346 6033 5935 5110 499 19 -948 O ATOM 2295 OE2 GLU A 346 -34.060 7.658 -23.254 1.00 50.52 O1- ANISOU 2295 OE2 GLU A 346 6604 6660 5930 521 12 -1156 O1- ATOM 2296 N ILE A 347 -34.398 11.075 -17.595 1.00 47.04 N ANISOU 2296 N ILE A 347 6520 5942 5410 591 -99 -637 N ATOM 2297 CA ILE A 347 -34.428 12.088 -16.546 1.00 47.69 C ANISOU 2297 CA ILE A 347 6659 6005 5456 593 -111 -547 C ATOM 2298 C ILE A 347 -33.951 11.442 -15.250 1.00 48.02 C ANISOU 2298 C ILE A 347 6725 5958 5564 637 -164 -525 C ATOM 2299 O ILE A 347 -34.560 10.477 -14.769 1.00 45.28 O ANISOU 2299 O ILE A 347 6399 5544 5261 653 -189 -507 O ATOM 2300 CB ILE A 347 -35.828 12.706 -16.396 1.00 45.00 C ANISOU 2300 CB ILE A 347 6374 5671 5054 568 -91 -469 C ATOM 2301 CG1 ILE A 347 -36.095 13.637 -17.594 1.00 48.31 C ANISOU 2301 CG1 ILE A 347 6766 6185 5403 523 -45 -473 C ATOM 2302 CG2 ILE A 347 -35.955 13.445 -15.083 1.00 43.57 C ANISOU 2302 CG2 ILE A 347 6248 5452 4855 579 -112 -390 C ATOM 2303 CD1 ILE A 347 -37.145 14.718 -17.371 1.00 41.71 C ANISOU 2303 CD1 ILE A 347 5978 5362 4510 498 -30 -388 C ATOM 2304 N GLU A 348 -32.847 11.960 -14.704 1.00 59.40 N ANISOU 2304 N GLU A 348 8158 7400 7012 653 -183 -525 N ATOM 2305 CA GLU A 348 -32.244 11.393 -13.498 1.00 57.04 C ANISOU 2305 CA GLU A 348 7873 7028 6772 693 -237 -504 C ATOM 2306 C GLU A 348 -33.037 11.764 -12.250 1.00 53.23 C ANISOU 2306 C GLU A 348 7460 6514 6253 693 -256 -406 C ATOM 2307 O GLU A 348 -33.487 10.892 -11.500 1.00 52.03 O ANISOU 2307 O GLU A 348 7333 6299 6136 710 -290 -367 O ATOM 2308 CB GLU A 348 -30.805 11.888 -13.367 1.00 57.68 C ANISOU 2308 CB GLU A 348 7919 7130 6867 707 -250 -542 C ATOM 2309 CG GLU A 348 -29.903 11.549 -14.528 1.00 58.73 C ANISOU 2309 CG GLU A 348 7977 7303 7035 705 -232 -646 C ATOM 2310 CD GLU A 348 -28.798 12.564 -14.661 1.00 59.84 C ANISOU 2310 CD GLU A 348 8090 7499 7149 697 -219 -669 C ATOM 2311 OE1 GLU A 348 -27.879 12.575 -13.803 1.00 57.07 O ANISOU 2311 OE1 GLU A 348 7736 7113 6834 728 -257 -667 O ATOM 2312 OE2 GLU A 348 -28.871 13.374 -15.612 1.00 59.47 O1- ANISOU 2312 OE2 GLU A 348 8022 7532 7043 658 -172 -683 O1- ATOM 2313 N GLU A 349 -33.191 13.066 -11.997 1.00 46.81 N ANISOU 2313 N GLU A 349 6671 5744 5371 673 -234 -368 N ATOM 2314 CA GLU A 349 -33.967 13.572 -10.865 1.00 42.55 C ANISOU 2314 CA GLU A 349 6187 5190 4788 669 -244 -289 C ATOM 2315 C GLU A 349 -35.449 13.358 -11.132 1.00 40.70 C ANISOU 2315 C GLU A 349 5986 4952 4526 646 -221 -256 C ATOM 2316 O GLU A 349 -36.185 14.278 -11.492 1.00 39.10 O ANISOU 2316 O GLU A 349 5797 4788 4271 617 -186 -236 O ATOM 2317 CB GLU A 349 -33.680 15.037 -10.631 1.00 43.67 C ANISOU 2317 CB GLU A 349 6333 5378 4882 654 -226 -275 C ATOM 2318 CG GLU A 349 -32.254 15.307 -10.231 1.00 46.81 C ANISOU 2318 CG GLU A 349 6702 5780 5306 677 -251 -305 C ATOM 2319 CD GLU A 349 -32.152 16.530 -9.358 1.00 49.00 C ANISOU 2319 CD GLU A 349 6996 6079 5545 671 -252 -273 C ATOM 2320 OE1 GLU A 349 -31.025 16.864 -8.928 1.00 47.72 O ANISOU 2320 OE1 GLU A 349 6810 5922 5399 689 -272 -296 O ATOM 2321 OE2 GLU A 349 -33.211 17.159 -9.106 1.00 46.85 O1- ANISOU 2321 OE2 GLU A 349 6754 5816 5230 649 -233 -232 O1- ATOM 2322 N LYS A 350 -35.886 12.109 -10.945 1.00 42.64 N ANISOU 2322 N LYS A 350 6240 5145 4816 659 -244 -248 N ATOM 2323 CA LYS A 350 -37.286 11.756 -11.132 1.00 39.36 C ANISOU 2323 CA LYS A 350 5854 4718 4383 639 -225 -218 C ATOM 2324 C LYS A 350 -38.159 12.235 -9.975 1.00 36.45 C ANISOU 2324 C LYS A 350 5540 4346 3964 628 -231 -141 C ATOM 2325 O LYS A 350 -39.359 12.453 -10.164 1.00 36.30 O ANISOU 2325 O LYS A 350 5545 4337 3908 604 -204 -117 O ATOM 2326 CB LYS A 350 -37.425 10.242 -11.305 1.00 45.91 C ANISOU 2326 CB LYS A 350 6669 5487 5289 655 -249 -238 C ATOM 2327 CG LYS A 350 -36.670 9.638 -12.509 1.00 45.26 C ANISOU 2327 CG LYS A 350 6522 5411 5264 665 -241 -332 C ATOM 2328 CD LYS A 350 -37.087 8.179 -12.741 1.00 40.09 C ANISOU 2328 CD LYS A 350 5849 4692 4693 676 -260 -357 C ATOM 2329 CE LYS A 350 -36.193 7.460 -13.767 1.00 45.34 C ANISOU 2329 CE LYS A 350 6439 5357 5433 691 -260 -465 C ATOM 2330 NZ LYS A 350 -36.067 8.151 -15.083 1.00 41.59 N1+ ANISOU 2330 NZ LYS A 350 5926 4975 4902 665 -207 -535 N1+ ATOM 2331 N VAL A 351 -37.584 12.399 -8.782 1.00 38.54 N ANISOU 2331 N VAL A 351 5818 4601 4224 644 -267 -106 N ATOM 2332 CA VAL A 351 -38.272 12.940 -7.613 1.00 33.85 C ANISOU 2332 CA VAL A 351 5265 4021 3575 631 -272 -44 C ATOM 2333 C VAL A 351 -37.492 14.138 -7.099 1.00 31.91 C ANISOU 2333 C VAL A 351 5011 3817 3298 634 -274 -53 C ATOM 2334 O VAL A 351 -36.258 14.125 -7.090 1.00 32.51 O ANISOU 2334 O VAL A 351 5059 3891 3404 656 -295 -83 O ATOM 2335 CB VAL A 351 -38.450 11.883 -6.508 1.00 34.40 C ANISOU 2335 CB VAL A 351 5357 4049 3665 641 -318 14 C ATOM 2336 CG1 VAL A 351 -39.297 10.741 -6.993 1.00 35.06 C ANISOU 2336 CG1 VAL A 351 5446 4085 3789 635 -316 24 C ATOM 2337 CG2 VAL A 351 -37.077 11.329 -6.088 1.00 42.17 C ANISOU 2337 CG2 VAL A 351 6313 5005 4702 674 -368 6 C ATOM 2338 N ALA A 352 -38.215 15.188 -6.715 1.00 31.80 N ANISOU 2338 N ALA A 352 5015 3837 3228 612 -251 -34 N ATOM 2339 CA ALA A 352 -37.577 16.363 -6.141 1.00 33.82 C ANISOU 2339 CA ALA A 352 5260 4130 3462 613 -252 -46 C ATOM 2340 C ALA A 352 -37.006 16.012 -4.772 1.00 32.64 C ANISOU 2340 C ALA A 352 5117 3981 3303 630 -298 -19 C ATOM 2341 O ALA A 352 -37.549 15.156 -4.067 1.00 35.51 O ANISOU 2341 O ALA A 352 5505 4330 3656 628 -322 28 O ATOM 2342 CB ALA A 352 -38.565 17.526 -6.010 1.00 33.38 C ANISOU 2342 CB ALA A 352 5215 4104 3363 585 -220 -39 C ATOM 2343 N PRO A 353 -35.905 16.648 -4.373 1.00 35.79 N ANISOU 2343 N PRO A 353 5492 4403 3705 645 -314 -45 N ATOM 2344 CA PRO A 353 -35.229 16.240 -3.117 1.00 37.26 C ANISOU 2344 CA PRO A 353 5679 4597 3883 663 -363 -20 C ATOM 2345 C PRO A 353 -36.084 16.498 -1.874 1.00 30.56 C ANISOU 2345 C PRO A 353 4855 3788 2970 643 -370 23 C ATOM 2346 O PRO A 353 -36.766 17.516 -1.766 1.00 30.32 O ANISOU 2346 O PRO A 353 4827 3792 2904 621 -338 7 O ATOM 2347 CB PRO A 353 -33.946 17.089 -3.096 1.00 36.25 C ANISOU 2347 CB PRO A 353 5514 4490 3769 680 -369 -69 C ATOM 2348 CG PRO A 353 -33.874 17.799 -4.454 1.00 37.19 C ANISOU 2348 CG PRO A 353 5612 4606 3912 669 -323 -115 C ATOM 2349 CD PRO A 353 -35.255 17.786 -5.050 1.00 33.96 C ANISOU 2349 CD PRO A 353 5228 4191 3484 643 -287 -94 C ATOM 2350 N ALA A 354 -36.049 15.548 -0.933 1.00 32.06 N ANISOU 2350 N ALA A 354 5058 3976 3149 648 -414 78 N ATOM 2351 CA ALA A 354 -36.819 15.669 0.306 1.00 36.24 C ANISOU 2351 CA ALA A 354 5606 4558 3607 624 -424 122 C ATOM 2352 C ALA A 354 -36.147 16.584 1.329 1.00 35.40 C ANISOU 2352 C ALA A 354 5476 4519 3455 626 -439 98 C ATOM 2353 O ALA A 354 -36.843 17.208 2.140 1.00 31.78 O ANISOU 2353 O ALA A 354 5020 4122 2933 600 -426 98 O ATOM 2354 CB ALA A 354 -37.057 14.294 0.927 1.00 31.85 C ANISOU 2354 CB ALA A 354 5070 3980 3052 622 -467 203 C ATOM 2355 N LYS A 355 -34.815 16.672 1.300 1.00 32.24 N ANISOU 2355 N LYS A 355 5048 4111 3090 655 -465 70 N ATOM 2356 CA LYS A 355 -34.019 17.571 2.120 1.00 33.47 C ANISOU 2356 CA LYS A 355 5174 4326 3215 661 -479 33 C ATOM 2357 C LYS A 355 -33.381 18.655 1.248 1.00 36.88 C ANISOU 2357 C LYS A 355 5577 4745 3690 671 -446 -44 C ATOM 2358 O LYS A 355 -33.185 18.483 0.035 1.00 35.45 O ANISOU 2358 O LYS A 355 5394 4511 3564 681 -426 -63 O ATOM 2359 CB LYS A 355 -32.926 16.801 2.874 1.00 33.17 C ANISOU 2359 CB LYS A 355 5123 4294 3185 685 -543 66 C ATOM 2360 CG LYS A 355 -33.414 15.676 3.805 1.00 37.84 C ANISOU 2360 CG LYS A 355 5737 4899 3739 673 -587 160 C ATOM 2361 CD LYS A 355 -34.194 16.181 5.028 1.00 36.74 C ANISOU 2361 CD LYS A 355 5603 4858 3500 637 -583 181 C ATOM 2362 CE LYS A 355 -34.712 15.021 5.860 1.00 38.81 C ANISOU 2362 CE LYS A 355 5886 5136 3723 617 -625 286 C ATOM 2363 NZ LYS A 355 -35.723 15.469 6.856 1.00 39.94 N1+ ANISOU 2363 NZ LYS A 355 6034 5378 3765 573 -608 302 N1+ ATOM 2364 N ALA A 356 -33.066 19.782 1.890 1.00 33.07 N ANISOU 2364 N ALA A 356 5067 4317 3182 666 -440 -90 N ATOM 2365 CA ALA A 356 -32.379 20.887 1.235 1.00 35.55 C ANISOU 2365 CA ALA A 356 5347 4621 3540 674 -415 -158 C ATOM 2366 C ALA A 356 -30.942 20.518 0.901 1.00 36.06 C ANISOU 2366 C ALA A 356 5388 4659 3652 706 -443 -176 C ATOM 2367 O ALA A 356 -30.292 19.753 1.613 1.00 38.23 O ANISOU 2367 O ALA A 356 5663 4945 3919 725 -491 -150 O ATOM 2368 CB ALA A 356 -32.392 22.130 2.122 1.00 37.33 C ANISOU 2368 CB ALA A 356 5540 4908 3736 661 -407 -207 C ATOM 2369 N ASP A 357 -30.444 21.081 -0.198 1.00 36.36 N ANISOU 2369 N ASP A 357 5405 4667 3743 709 -413 -219 N ATOM 2370 CA ASP A 357 -29.141 20.739 -0.768 1.00 34.39 C ANISOU 2370 CA ASP A 357 5130 4391 3546 736 -430 -246 C ATOM 2371 C ASP A 357 -28.356 22.040 -0.928 1.00 34.96 C ANISOU 2371 C ASP A 357 5160 4481 3643 734 -411 -307 C ATOM 2372 O ASP A 357 -28.302 22.625 -2.013 1.00 34.63 O ANISOU 2372 O ASP A 357 5101 4420 3636 721 -373 -330 O ATOM 2373 CB ASP A 357 -29.320 20.005 -2.100 1.00 31.75 C ANISOU 2373 CB ASP A 357 4807 4007 3251 736 -410 -238 C ATOM 2374 CG ASP A 357 -28.078 19.250 -2.529 1.00 37.29 C ANISOU 2374 CG ASP A 357 5483 4682 4005 765 -437 -262 C ATOM 2375 OD1 ASP A 357 -26.972 19.592 -2.035 1.00 36.91 O ANISOU 2375 OD1 ASP A 357 5404 4651 3970 784 -461 -294 O ATOM 2376 OD2 ASP A 357 -28.204 18.323 -3.377 1.00 37.99 O1- ANISOU 2376 OD2 ASP A 357 5576 4732 4125 770 -433 -257 O1- ATOM 2377 N LEU A 358 -27.742 22.492 0.173 1.00 36.83 N ANISOU 2377 N LEU A 358 5373 4759 3861 745 -438 -331 N ATOM 2378 CA LEU A 358 -27.113 23.810 0.177 1.00 34.53 C ANISOU 2378 CA LEU A 358 5037 4485 3597 741 -421 -392 C ATOM 2379 C LEU A 358 -25.877 23.845 -0.701 1.00 33.42 C ANISOU 2379 C LEU A 358 4865 4318 3514 756 -418 -427 C ATOM 2380 O LEU A 358 -25.533 24.900 -1.248 1.00 31.38 O ANISOU 2380 O LEU A 358 4573 4056 3294 743 -388 -465 O ATOM 2381 CB LEU A 358 -26.761 24.224 1.601 1.00 31.92 C ANISOU 2381 CB LEU A 358 4685 4214 3231 748 -452 -418 C ATOM 2382 CG LEU A 358 -28.018 24.476 2.433 1.00 36.08 C ANISOU 2382 CG LEU A 358 5229 4781 3698 724 -444 -401 C ATOM 2383 CD1 LEU A 358 -27.710 24.812 3.907 1.00 32.47 C ANISOU 2383 CD1 LEU A 358 4745 4403 3191 727 -476 -431 C ATOM 2384 CD2 LEU A 358 -28.874 25.547 1.768 1.00 35.53 C ANISOU 2384 CD2 LEU A 358 5151 4690 3658 697 -394 -424 C ATOM 2385 N ASP A 359 -25.189 22.717 -0.834 1.00 31.75 N ANISOU 2385 N ASP A 359 4659 4088 3316 782 -450 -415 N ATOM 2386 CA ASP A 359 -24.015 22.706 -1.688 1.00 34.41 C ANISOU 2386 CA ASP A 359 4961 4406 3709 795 -445 -457 C ATOM 2387 C ASP A 359 -24.416 22.897 -3.144 1.00 34.30 C ANISOU 2387 C ASP A 359 4946 4367 3718 770 -396 -457 C ATOM 2388 O ASP A 359 -23.729 23.596 -3.895 1.00 34.13 O ANISOU 2388 O ASP A 359 4887 4349 3732 759 -370 -494 O ATOM 2389 CB ASP A 359 -23.221 21.420 -1.463 1.00 32.23 C ANISOU 2389 CB ASP A 359 4684 4111 3451 830 -495 -450 C ATOM 2390 CG ASP A 359 -22.212 21.560 -0.320 1.00 46.85 C ANISOU 2390 CG ASP A 359 6509 5994 5299 855 -542 -473 C ATOM 2391 OD1 ASP A 359 -21.266 22.364 -0.487 1.00 54.11 O ANISOU 2391 OD1 ASP A 359 7386 6924 6248 859 -532 -530 O ATOM 2392 OD2 ASP A 359 -22.364 20.916 0.754 1.00 42.71 O1- ANISOU 2392 OD2 ASP A 359 6002 5486 4740 869 -590 -432 O1- ATOM 2393 N LYS A 360 -25.551 22.325 -3.541 1.00 32.52 N ANISOU 2393 N LYS A 360 4759 4125 3471 756 -381 -413 N ATOM 2394 CA LYS A 360 -26.055 22.522 -4.893 1.00 34.20 C ANISOU 2394 CA LYS A 360 4970 4327 3696 728 -335 -409 C ATOM 2395 C LYS A 360 -26.536 23.955 -5.091 1.00 38.07 C ANISOU 2395 C LYS A 360 5448 4831 4187 697 -298 -409 C ATOM 2396 O LYS A 360 -26.349 24.528 -6.170 1.00 38.50 O ANISOU 2396 O LYS A 360 5476 4888 4265 673 -265 -417 O ATOM 2397 CB LYS A 360 -27.172 21.515 -5.181 1.00 33.04 C ANISOU 2397 CB LYS A 360 4866 4160 3527 724 -332 -365 C ATOM 2398 CG LYS A 360 -27.595 21.422 -6.620 1.00 40.60 C ANISOU 2398 CG LYS A 360 5819 5113 4493 699 -291 -365 C ATOM 2399 CD LYS A 360 -26.449 20.993 -7.531 1.00 46.82 C ANISOU 2399 CD LYS A 360 6566 5904 5320 708 -289 -413 C ATOM 2400 CE LYS A 360 -26.926 20.910 -8.970 1.00 50.16 C ANISOU 2400 CE LYS A 360 6979 6341 5739 678 -246 -414 C ATOM 2401 NZ LYS A 360 -25.855 20.513 -9.930 1.00 59.59 N1+ ANISOU 2401 NZ LYS A 360 8125 7554 6964 680 -238 -471 N1+ ATOM 2402 N VAL A 361 -27.127 24.569 -4.057 1.00 33.55 N ANISOU 2402 N VAL A 361 4885 4270 3591 693 -306 -401 N ATOM 2403 CA VAL A 361 -27.517 25.972 -4.173 1.00 31.28 C ANISOU 2403 CA VAL A 361 4575 3986 3324 666 -277 -410 C ATOM 2404 C VAL A 361 -26.290 26.846 -4.389 1.00 34.37 C ANISOU 2404 C VAL A 361 4913 4382 3764 666 -273 -455 C ATOM 2405 O VAL A 361 -26.252 27.675 -5.308 1.00 40.51 O ANISOU 2405 O VAL A 361 5663 5150 4578 639 -243 -451 O ATOM 2406 CB VAL A 361 -28.311 26.429 -2.943 1.00 33.24 C ANISOU 2406 CB VAL A 361 4834 4251 3544 664 -288 -412 C ATOM 2407 CG1 VAL A 361 -28.796 27.870 -3.146 1.00 30.70 C ANISOU 2407 CG1 VAL A 361 4481 3920 3262 636 -260 -426 C ATOM 2408 CG2 VAL A 361 -29.462 25.495 -2.693 1.00 36.15 C ANISOU 2408 CG2 VAL A 361 5254 4620 3863 662 -293 -366 C ATOM 2409 N ASP A 362 -25.261 26.655 -3.565 1.00 31.68 N ANISOU 2409 N ASP A 362 4555 4056 3425 694 -306 -492 N ATOM 2410 CA ASP A 362 -24.016 27.400 -3.736 1.00 36.52 C ANISOU 2410 CA ASP A 362 5115 4674 4086 696 -304 -539 C ATOM 2411 C ASP A 362 -23.421 27.178 -5.123 1.00 36.68 C ANISOU 2411 C ASP A 362 5117 4686 4132 683 -280 -538 C ATOM 2412 O ASP A 362 -22.964 28.128 -5.770 1.00 34.98 O ANISOU 2412 O ASP A 362 4861 4470 3958 659 -255 -550 O ATOM 2413 CB ASP A 362 -23.009 27.002 -2.653 1.00 36.49 C ANISOU 2413 CB ASP A 362 5099 4691 4074 733 -348 -578 C ATOM 2414 CG ASP A 362 -23.447 27.424 -1.260 1.00 37.81 C ANISOU 2414 CG ASP A 362 5269 4887 4211 739 -369 -591 C ATOM 2415 OD1 ASP A 362 -24.403 28.218 -1.143 1.00 35.78 O ANISOU 2415 OD1 ASP A 362 5012 4628 3954 715 -347 -585 O ATOM 2416 OD2 ASP A 362 -22.834 26.962 -0.277 1.00 48.80 O1- ANISOU 2416 OD2 ASP A 362 6657 6307 5579 766 -410 -608 O1- ATOM 2417 N GLU A 363 -23.427 25.931 -5.596 1.00 37.38 N ANISOU 2417 N GLU A 363 5231 4771 4201 696 -287 -525 N ATOM 2418 CA GLU A 363 -22.872 25.626 -6.911 1.00 36.87 C ANISOU 2418 CA GLU A 363 5142 4712 4154 683 -263 -536 C ATOM 2419 C GLU A 363 -23.588 26.424 -7.987 1.00 39.06 C ANISOU 2419 C GLU A 363 5411 4995 4434 636 -219 -501 C ATOM 2420 O GLU A 363 -22.956 27.118 -8.794 1.00 35.00 O ANISOU 2420 O GLU A 363 4853 4497 3947 610 -194 -511 O ATOM 2421 CB GLU A 363 -22.981 24.126 -7.186 1.00 35.80 C ANISOU 2421 CB GLU A 363 5032 4568 4003 704 -280 -533 C ATOM 2422 CG GLU A 363 -22.425 23.659 -8.541 1.00 44.82 C ANISOU 2422 CG GLU A 363 6142 5726 5160 690 -255 -560 C ATOM 2423 CD GLU A 363 -23.093 22.375 -9.054 1.00 48.41 C ANISOU 2423 CD GLU A 363 6624 6169 5601 696 -257 -548 C ATOM 2424 OE1 GLU A 363 -22.742 21.279 -8.570 1.00 51.80 O ANISOU 2424 OE1 GLU A 363 7060 6574 6047 733 -295 -566 O ATOM 2425 OE2 GLU A 363 -23.982 22.465 -9.925 1.00 44.56 O1- ANISOU 2425 OE2 GLU A 363 6146 5693 5090 664 -223 -519 O1- ATOM 2426 N ILE A 364 -24.919 26.366 -7.977 1.00 38.06 N ANISOU 2426 N ILE A 364 5324 4858 4280 624 -210 -454 N ATOM 2427 CA ILE A 364 -25.712 26.971 -9.037 1.00 35.17 C ANISOU 2427 CA ILE A 364 4953 4496 3913 581 -173 -412 C ATOM 2428 C ILE A 364 -25.580 28.487 -9.002 1.00 40.17 C ANISOU 2428 C ILE A 364 5548 5122 4591 555 -160 -405 C ATOM 2429 O ILE A 364 -25.352 29.130 -10.031 1.00 40.78 O ANISOU 2429 O ILE A 364 5591 5215 4690 518 -134 -384 O ATOM 2430 CB ILE A 364 -27.180 26.527 -8.909 1.00 34.47 C ANISOU 2430 CB ILE A 364 4916 4394 3789 577 -170 -369 C ATOM 2431 CG1 ILE A 364 -27.298 25.017 -9.145 1.00 35.44 C ANISOU 2431 CG1 ILE A 364 5067 4517 3880 598 -180 -373 C ATOM 2432 CG2 ILE A 364 -28.069 27.331 -9.852 1.00 30.80 C ANISOU 2432 CG2 ILE A 364 4442 3931 3328 534 -138 -321 C ATOM 2433 CD1 ILE A 364 -28.549 24.374 -8.538 1.00 35.42 C ANISOU 2433 CD1 ILE A 364 5118 4495 3844 607 -192 -340 C ATOM 2434 N LEU A 365 -25.730 29.085 -7.816 1.00 40.29 N ANISOU 2434 N LEU A 365 5565 5119 4624 570 -179 -422 N ATOM 2435 CA LEU A 365 -25.787 30.542 -7.753 1.00 39.55 C ANISOU 2435 CA LEU A 365 5431 5008 4588 546 -169 -419 C ATOM 2436 C LEU A 365 -24.422 31.160 -8.003 1.00 40.36 C ANISOU 2436 C LEU A 365 5479 5119 4739 540 -166 -452 C ATOM 2437 O LEU A 365 -24.309 32.120 -8.773 1.00 40.99 O ANISOU 2437 O LEU A 365 5518 5191 4866 502 -146 -425 O ATOM 2438 CB LEU A 365 -26.354 30.993 -6.410 1.00 41.75 C ANISOU 2438 CB LEU A 365 5718 5272 4874 563 -189 -444 C ATOM 2439 CG LEU A 365 -27.826 30.642 -6.244 1.00 36.42 C ANISOU 2439 CG LEU A 365 5088 4589 4160 558 -185 -407 C ATOM 2440 CD1 LEU A 365 -28.327 31.076 -4.906 1.00 37.44 C ANISOU 2440 CD1 LEU A 365 5217 4717 4290 572 -202 -442 C ATOM 2441 CD2 LEU A 365 -28.595 31.321 -7.335 1.00 41.65 C ANISOU 2441 CD2 LEU A 365 5739 5232 4854 519 -159 -354 C ATOM 2442 N THR A 366 -23.373 30.637 -7.354 1.00 41.88 N ANISOU 2442 N THR A 366 5665 5326 4924 574 -189 -506 N ATOM 2443 CA THR A 366 -22.032 31.106 -7.680 1.00 42.22 C ANISOU 2443 CA THR A 366 5654 5379 5008 568 -184 -541 C ATOM 2444 C THR A 366 -21.709 30.819 -9.131 1.00 44.32 C ANISOU 2444 C THR A 366 5905 5671 5265 537 -155 -515 C ATOM 2445 O THR A 366 -20.943 31.560 -9.751 1.00 50.40 O ANISOU 2445 O THR A 366 6623 6451 6074 508 -138 -517 O ATOM 2446 CB THR A 366 -20.980 30.485 -6.748 1.00 43.41 C ANISOU 2446 CB THR A 366 5801 5543 5151 613 -217 -605 C ATOM 2447 CG2 THR A 366 -21.365 30.701 -5.304 1.00 39.22 C ANISOU 2447 CG2 THR A 366 5285 5005 4613 640 -246 -629 C ATOM 2448 OG1 THR A 366 -20.829 29.082 -7.009 1.00 40.78 O ANISOU 2448 OG1 THR A 366 5499 5223 4771 636 -228 -606 O ATOM 2449 N GLY A 367 -22.313 29.769 -9.697 1.00 43.92 N ANISOU 2449 N GLY A 367 5892 5635 5161 538 -149 -491 N ATOM 2450 CA GLY A 367 -22.147 29.499 -11.113 1.00 41.69 C ANISOU 2450 CA GLY A 367 5589 5391 4860 503 -119 -470 C ATOM 2451 C GLY A 367 -22.902 30.478 -11.979 1.00 43.59 C ANISOU 2451 C GLY A 367 5815 5635 5114 450 -91 -400 C ATOM 2452 O GLY A 367 -22.489 30.757 -13.108 1.00 49.65 O ANISOU 2452 O GLY A 367 6543 6443 5879 408 -65 -379 O ATOM 2453 N ALA A 368 -24.011 31.010 -11.470 1.00 45.18 N ANISOU 2453 N ALA A 368 6041 5797 5327 448 -98 -363 N ATOM 2454 CA ALA A 368 -24.808 32.030 -12.138 1.00 43.63 C ANISOU 2454 CA ALA A 368 5828 5590 5159 402 -80 -293 C ATOM 2455 C ALA A 368 -24.306 33.444 -11.857 1.00 45.68 C ANISOU 2455 C ALA A 368 6035 5818 5504 384 -84 -290 C ATOM 2456 O ALA A 368 -24.980 34.411 -12.228 1.00 45.81 O ANISOU 2456 O ALA A 368 6032 5809 5566 349 -78 -230 O ATOM 2457 CB ALA A 368 -26.275 31.905 -11.712 1.00 42.03 C ANISOU 2457 CB ALA A 368 5673 5357 4940 411 -88 -262 C ATOM 2458 N GLY A 369 -23.148 33.585 -11.211 1.00 49.44 N ANISOU 2458 N GLY A 369 6484 6292 6010 407 -95 -353 N ATOM 2459 CA GLY A 369 -22.550 34.886 -10.988 1.00 53.30 C ANISOU 2459 CA GLY A 369 6915 6751 6586 389 -97 -359 C ATOM 2460 C GLY A 369 -23.013 35.595 -9.740 1.00 54.68 C ANISOU 2460 C GLY A 369 7088 6872 6815 413 -120 -391 C ATOM 2461 O GLY A 369 -22.892 36.825 -9.661 1.00 54.54 O ANISOU 2461 O GLY A 369 7019 6817 6888 391 -121 -384 O ATOM 2462 N TYR A 370 -23.573 34.862 -8.781 1.00 48.80 N ANISOU 2462 N TYR A 370 6393 6128 6023 454 -137 -427 N ATOM 2463 CA TYR A 370 -23.927 35.382 -7.470 1.00 48.57 C ANISOU 2463 CA TYR A 370 6358 6069 6027 479 -159 -475 C ATOM 2464 C TYR A 370 -22.840 35.021 -6.465 1.00 49.04 C ANISOU 2464 C TYR A 370 6409 6150 6073 519 -180 -556 C ATOM 2465 O TYR A 370 -22.091 34.053 -6.641 1.00 47.19 O ANISOU 2465 O TYR A 370 6194 5949 5788 538 -184 -570 O ATOM 2466 CB TYR A 370 -25.287 34.840 -7.003 1.00 47.55 C ANISOU 2466 CB TYR A 370 6284 5936 5846 493 -165 -460 C ATOM 2467 CG TYR A 370 -26.462 35.190 -7.907 1.00 46.08 C ANISOU 2467 CG TYR A 370 6107 5728 5675 456 -148 -384 C ATOM 2468 CD1 TYR A 370 -26.793 34.396 -9.007 1.00 45.18 C ANISOU 2468 CD1 TYR A 370 6026 5640 5501 439 -130 -325 C ATOM 2469 CD2 TYR A 370 -27.239 36.318 -7.654 1.00 47.82 C ANISOU 2469 CD2 TYR A 370 6296 5901 5972 439 -151 -375 C ATOM 2470 CE1 TYR A 370 -27.867 34.720 -9.826 1.00 45.78 C ANISOU 2470 CE1 TYR A 370 6107 5701 5586 405 -118 -254 C ATOM 2471 CE2 TYR A 370 -28.305 36.657 -8.468 1.00 46.50 C ANISOU 2471 CE2 TYR A 370 6133 5711 5825 407 -140 -303 C ATOM 2472 CZ TYR A 370 -28.622 35.855 -9.545 1.00 47.74 C ANISOU 2472 CZ TYR A 370 6327 5900 5914 390 -124 -239 C ATOM 2473 OH TYR A 370 -29.689 36.198 -10.343 1.00 50.02 O ANISOU 2473 OH TYR A 370 6618 6171 6218 358 -117 -166 O ATOM 2474 N GLU A 371 -22.749 35.838 -5.413 1.00 52.45 N ANISOU 2474 N GLU A 371 6807 6564 6557 532 -196 -613 N ATOM 2475 CA GLU A 371 -21.753 35.678 -4.356 1.00 53.57 C ANISOU 2475 CA GLU A 371 6931 6731 6691 568 -220 -692 C ATOM 2476 C GLU A 371 -22.353 36.182 -3.048 1.00 51.59 C ANISOU 2476 C GLU A 371 6669 6480 6454 584 -238 -747 C ATOM 2477 O GLU A 371 -22.890 37.296 -2.990 1.00 51.70 O ANISOU 2477 O GLU A 371 6642 6455 6546 562 -230 -755 O ATOM 2478 CB GLU A 371 -20.461 36.459 -4.666 1.00 56.01 C ANISOU 2478 CB GLU A 371 7175 7030 7076 556 -214 -723 C ATOM 2479 CG GLU A 371 -19.770 36.111 -5.980 1.00 59.29 C ANISOU 2479 CG GLU A 371 7587 7459 7484 532 -193 -679 C ATOM 2480 CD GLU A 371 -18.866 34.898 -5.894 1.00 63.83 C ANISOU 2480 CD GLU A 371 8185 8075 7991 565 -205 -711 C ATOM 2481 OE1 GLU A 371 -17.769 35.019 -5.305 1.00 75.27 O ANISOU 2481 OE1 GLU A 371 9601 9537 9463 587 -221 -776 O ATOM 2482 OE2 GLU A 371 -19.255 33.824 -6.408 1.00 57.66 O1- ANISOU 2482 OE2 GLU A 371 7452 7314 7142 570 -201 -676 O1- ATOM 2483 N LYS A 372 -22.262 35.368 -2.004 1.00 46.80 N ANISOU 2483 N LYS A 372 6092 5918 5773 619 -263 -786 N ATOM 2484 CA LYS A 372 -22.712 35.806 -0.692 1.00 46.68 C ANISOU 2484 CA LYS A 372 6057 5924 5756 632 -280 -848 C ATOM 2485 C LYS A 372 -21.926 37.039 -0.264 1.00 47.76 C ANISOU 2485 C LYS A 372 6113 6047 5987 628 -283 -924 C ATOM 2486 O LYS A 372 -20.690 37.029 -0.257 1.00 47.82 O ANISOU 2486 O LYS A 372 6094 6066 6011 641 -292 -957 O ATOM 2487 CB LYS A 372 -22.558 34.670 0.323 1.00 45.25 C ANISOU 2487 CB LYS A 372 5916 5806 5472 666 -310 -866 C ATOM 2488 CG LYS A 372 -23.704 33.660 0.272 1.00 42.43 C ANISOU 2488 CG LYS A 372 5629 5460 5032 666 -310 -804 C ATOM 2489 CD LYS A 372 -23.399 32.354 1.009 1.00 45.16 C ANISOU 2489 CD LYS A 372 6016 5857 5284 696 -343 -795 C ATOM 2490 CE LYS A 372 -23.561 32.492 2.528 1.00 47.62 C ANISOU 2490 CE LYS A 372 6311 6233 5551 708 -369 -851 C ATOM 2491 NZ LYS A 372 -24.951 32.221 3.004 1.00 48.01 N1+ ANISOU 2491 NZ LYS A 372 6395 6306 5542 695 -365 -825 N1+ ATOM 2492 N GLY A 373 -22.642 38.116 0.050 1.00 46.65 N ANISOU 2492 N GLY A 373 5929 5876 5919 611 -276 -957 N ATOM 2493 CA GLY A 373 -22.012 39.281 0.631 1.00 46.04 C ANISOU 2493 CA GLY A 373 5769 5786 5938 610 -283 -1044 C ATOM 2494 C GLY A 373 -21.572 38.996 2.054 1.00 45.54 C ANISOU 2494 C GLY A 373 5691 5798 5814 642 -310 -1135 C ATOM 2495 O GLY A 373 -21.582 37.862 2.537 1.00 49.34 O ANISOU 2495 O GLY A 373 6227 6340 6181 664 -327 -1119 O ATOM 2496 N SER A 374 -21.194 40.063 2.750 1.00 44.90 N ANISOU 2496 N SER A 374 5529 5714 5815 642 -316 -1231 N ATOM 2497 CA SER A 374 -20.778 39.847 4.130 1.00 43.19 C ANISOU 2497 CA SER A 374 5291 5583 5535 668 -342 -1322 C ATOM 2498 C SER A 374 -21.955 39.566 5.056 1.00 43.28 C ANISOU 2498 C SER A 374 5322 5654 5468 668 -349 -1345 C ATOM 2499 O SER A 374 -21.737 39.229 6.221 1.00 47.61 O ANISOU 2499 O SER A 374 5860 6292 5937 686 -372 -1407 O ATOM 2500 CB SER A 374 -19.955 41.040 4.624 1.00 44.21 C ANISOU 2500 CB SER A 374 5322 5702 5773 668 -347 -1431 C ATOM 2501 OG SER A 374 -20.563 42.283 4.313 1.00 44.45 O ANISOU 2501 OG SER A 374 5292 5657 5939 641 -329 -1456 O ATOM 2502 N ASP A 375 -23.190 39.677 4.570 1.00 47.22 N ANISOU 2502 N ASP A 375 5847 6112 5984 647 -329 -1296 N ATOM 2503 CA ASP A 375 -24.378 39.371 5.357 1.00 46.73 C ANISOU 2503 CA ASP A 375 5805 6105 5845 643 -331 -1313 C ATOM 2504 C ASP A 375 -24.932 38.004 5.043 1.00 45.63 C ANISOU 2504 C ASP A 375 5763 5989 5585 648 -333 -1210 C ATOM 2505 O ASP A 375 -26.103 37.739 5.341 1.00 46.97 O ANISOU 2505 O ASP A 375 5960 6182 5704 637 -326 -1196 O ATOM 2506 CB ASP A 375 -25.473 40.409 5.111 1.00 49.90 C ANISOU 2506 CB ASP A 375 6164 6445 6352 618 -311 -1336 C ATOM 2507 CG ASP A 375 -25.701 40.657 3.643 1.00 47.49 C ANISOU 2507 CG ASP A 375 5881 6036 6129 599 -291 -1239 C ATOM 2508 OD1 ASP A 375 -24.965 40.061 2.832 1.00 48.23 O ANISOU 2508 OD1 ASP A 375 6016 6112 6195 604 -290 -1164 O ATOM 2509 OD2 ASP A 375 -26.600 41.452 3.300 1.00 48.20 O1- ANISOU 2509 OD2 ASP A 375 5940 6065 6311 577 -279 -1238 O1- ATOM 2510 N GLY A 376 -24.137 37.151 4.398 1.00 49.43 N ANISOU 2510 N GLY A 376 6293 6460 6029 662 -339 -1141 N ATOM 2511 CA GLY A 376 -24.564 35.822 4.020 1.00 47.37 C ANISOU 2511 CA GLY A 376 6117 6210 5669 668 -342 -1046 C ATOM 2512 C GLY A 376 -25.543 35.755 2.865 1.00 48.55 C ANISOU 2512 C GLY A 376 6309 6294 5845 646 -314 -965 C ATOM 2513 O GLY A 376 -25.842 34.647 2.397 1.00 48.42 O ANISOU 2513 O GLY A 376 6360 6279 5758 650 -315 -888 O ATOM 2514 N ILE A 377 -26.060 36.892 2.392 1.00 45.42 N ANISOU 2514 N ILE A 377 5869 5839 5551 622 -293 -980 N ATOM 2515 CA ILE A 377 -27.053 36.908 1.323 1.00 45.36 C ANISOU 2515 CA ILE A 377 5893 5773 5570 599 -270 -902 C ATOM 2516 C ILE A 377 -26.350 36.960 -0.028 1.00 45.30 C ANISOU 2516 C ILE A 377 5890 5711 5612 589 -257 -838 C ATOM 2517 O ILE A 377 -25.449 37.780 -0.246 1.00 46.87 O ANISOU 2517 O ILE A 377 6031 5881 5895 584 -256 -868 O ATOM 2518 CB ILE A 377 -28.017 38.094 1.480 1.00 45.15 C ANISOU 2518 CB ILE A 377 5813 5707 5634 577 -259 -943 C ATOM 2519 CG1 ILE A 377 -28.793 38.018 2.803 1.00 48.85 C ANISOU 2519 CG1 ILE A 377 6274 6244 6045 583 -268 -1014 C ATOM 2520 CG2 ILE A 377 -28.972 38.146 0.277 1.00 46.89 C ANISOU 2520 CG2 ILE A 377 6063 5864 5888 553 -239 -853 C ATOM 2521 CD1 ILE A 377 -29.789 36.850 2.897 1.00 47.76 C ANISOU 2521 CD1 ILE A 377 6214 6145 5789 582 -265 -953 C ATOM 2522 N TYR A 378 -26.779 36.097 -0.943 1.00 43.52 N ANISOU 2522 N TYR A 378 5726 5476 5335 582 -245 -752 N ATOM 2523 CA TYR A 378 -26.279 36.126 -2.310 1.00 46.08 C ANISOU 2523 CA TYR A 378 6051 5762 5695 564 -229 -689 C ATOM 2524 C TYR A 378 -26.718 37.415 -2.999 1.00 48.35 C ANISOU 2524 C TYR A 378 6288 5987 6096 530 -214 -667 C ATOM 2525 O TYR A 378 -27.917 37.708 -3.077 1.00 48.84 O ANISOU 2525 O TYR A 378 6356 6024 6176 515 -208 -644 O ATOM 2526 CB TYR A 378 -26.790 34.907 -3.085 1.00 46.06 C ANISOU 2526 CB TYR A 378 6120 5772 5610 563 -220 -612 C ATOM 2527 CG TYR A 378 -25.968 33.660 -2.877 1.00 41.01 C ANISOU 2527 CG TYR A 378 5517 5174 4892 593 -235 -617 C ATOM 2528 CD1 TYR A 378 -24.666 33.585 -3.348 1.00 42.68 C ANISOU 2528 CD1 TYR A 378 5704 5388 5123 598 -236 -628 C ATOM 2529 CD2 TYR A 378 -26.486 32.561 -2.194 1.00 40.85 C ANISOU 2529 CD2 TYR A 378 5550 5187 4784 614 -251 -609 C ATOM 2530 CE1 TYR A 378 -23.904 32.451 -3.153 1.00 44.04 C ANISOU 2530 CE1 TYR A 378 5904 5592 5238 627 -255 -637 C ATOM 2531 CE2 TYR A 378 -25.734 31.408 -1.993 1.00 40.18 C ANISOU 2531 CE2 TYR A 378 5494 5131 4643 641 -272 -608 C ATOM 2532 CZ TYR A 378 -24.436 31.359 -2.477 1.00 43.06 C ANISOU 2532 CZ TYR A 378 5832 5494 5036 650 -275 -625 C ATOM 2533 OH TYR A 378 -23.654 30.231 -2.302 1.00 41.87 O ANISOU 2533 OH TYR A 378 5701 5364 4842 679 -300 -628 O ATOM 2534 N ALA A 379 -25.750 38.182 -3.495 1.00 51.55 N ANISOU 2534 N ALA A 379 6640 6364 6582 516 -210 -671 N ATOM 2535 CA ALA A 379 -25.987 39.384 -4.284 1.00 51.00 C ANISOU 2535 CA ALA A 379 6517 6230 6631 479 -200 -632 C ATOM 2536 C ALA A 379 -25.364 39.223 -5.668 1.00 50.75 C ANISOU 2536 C ALA A 379 6489 6195 6598 452 -183 -551 C ATOM 2537 O ALA A 379 -24.628 38.271 -5.940 1.00 48.87 O ANISOU 2537 O ALA A 379 6284 6002 6280 465 -179 -546 O ATOM 2538 CB ALA A 379 -25.419 40.622 -3.577 1.00 49.88 C ANISOU 2538 CB ALA A 379 6292 6055 6606 480 -211 -713 C ATOM 2539 N LYS A 380 -25.662 40.173 -6.550 1.00 54.69 N ANISOU 2539 N LYS A 380 6948 6644 7190 411 -175 -488 N ATOM 2540 CA LYS A 380 -25.078 40.184 -7.893 1.00 57.34 C ANISOU 2540 CA LYS A 380 7273 6986 7527 374 -159 -406 C ATOM 2541 C LYS A 380 -25.337 41.550 -8.507 1.00 58.50 C ANISOU 2541 C LYS A 380 7354 7067 7808 330 -160 -348 C ATOM 2542 O LYS A 380 -26.499 41.936 -8.685 1.00 59.34 O ANISOU 2542 O LYS A 380 7461 7134 7952 315 -166 -305 O ATOM 2543 CB LYS A 380 -25.666 39.074 -8.775 1.00 55.59 C ANISOU 2543 CB LYS A 380 7118 6809 7195 366 -144 -336 C ATOM 2544 CG LYS A 380 -25.138 39.044 -10.194 1.00 54.49 C ANISOU 2544 CG LYS A 380 6963 6696 7043 323 -124 -257 C ATOM 2545 CD LYS A 380 -25.882 38.038 -11.058 1.00 50.38 C ANISOU 2545 CD LYS A 380 6501 6221 6423 312 -110 -195 C ATOM 2546 CE LYS A 380 -25.330 38.030 -12.482 1.00 54.45 C ANISOU 2546 CE LYS A 380 6991 6780 6917 264 -88 -123 C ATOM 2547 NZ LYS A 380 -26.130 37.163 -13.390 1.00 52.64 N1+ ANISOU 2547 NZ LYS A 380 6806 6597 6596 248 -74 -66 N1+ ATOM 2548 N ASP A 381 -24.267 42.278 -8.822 1.00 57.17 N ANISOU 2548 N ASP A 381 7125 6882 7717 308 -159 -346 N ATOM 2549 CA ASP A 381 -24.374 43.605 -9.424 1.00 60.73 C ANISOU 2549 CA ASP A 381 7503 7263 8308 262 -164 -281 C ATOM 2550 C ASP A 381 -25.133 44.584 -8.526 1.00 63.26 C ANISOU 2550 C ASP A 381 7778 7505 8751 274 -187 -334 C ATOM 2551 O ASP A 381 -25.882 45.444 -9.003 1.00 65.98 O ANISOU 2551 O ASP A 381 8085 7785 9200 242 -198 -267 O ATOM 2552 CB ASP A 381 -25.011 43.530 -10.811 1.00 66.47 C ANISOU 2552 CB ASP A 381 8246 8001 9009 213 -154 -147 C ATOM 2553 CG ASP A 381 -24.101 42.884 -11.825 1.00 70.08 C ANISOU 2553 CG ASP A 381 8716 8534 9376 187 -131 -99 C ATOM 2554 OD1 ASP A 381 -23.002 42.437 -11.433 1.00 70.72 O ANISOU 2554 OD1 ASP A 381 8799 8653 9418 211 -123 -171 O ATOM 2555 OD2 ASP A 381 -24.463 42.862 -13.015 1.00 75.46 O1- ANISOU 2555 OD2 ASP A 381 9400 9241 10032 141 -121 9 O1- ATOM 2556 N GLY A 382 -24.929 44.462 -7.210 1.00 60.18 N ANISOU 2556 N GLY A 382 7387 7126 8354 319 -196 -458 N ATOM 2557 CA GLY A 382 -25.517 45.363 -6.241 1.00 56.97 C ANISOU 2557 CA GLY A 382 6927 6659 8060 333 -215 -536 C ATOM 2558 C GLY A 382 -26.870 44.945 -5.696 1.00 58.31 C ANISOU 2558 C GLY A 382 7140 6837 8178 354 -219 -559 C ATOM 2559 O GLY A 382 -27.209 45.321 -4.570 1.00 59.53 O ANISOU 2559 O GLY A 382 7262 6981 8376 378 -231 -664 O ATOM 2560 N VAL A 383 -27.653 44.183 -6.460 1.00 53.47 N ANISOU 2560 N VAL A 383 6594 6249 7473 342 -209 -470 N ATOM 2561 CA VAL A 383 -28.954 43.712 -5.999 1.00 57.11 C ANISOU 2561 CA VAL A 383 7099 6722 7878 360 -211 -486 C ATOM 2562 C VAL A 383 -28.759 42.411 -5.234 1.00 55.38 C ANISOU 2562 C VAL A 383 6951 6588 7502 399 -204 -544 C ATOM 2563 O VAL A 383 -27.893 41.596 -5.571 1.00 54.76 O ANISOU 2563 O VAL A 383 6910 6560 7335 405 -194 -524 O ATOM 2564 CB VAL A 383 -29.943 43.531 -7.172 1.00 59.27 C ANISOU 2564 CB VAL A 383 7406 6979 8134 328 -205 -364 C ATOM 2565 CG1 VAL A 383 -29.565 42.329 -8.055 1.00 57.34 C ANISOU 2565 CG1 VAL A 383 7233 6806 7746 323 -185 -293 C ATOM 2566 CG2 VAL A 383 -31.377 43.394 -6.655 1.00 55.09 C ANISOU 2566 CG2 VAL A 383 6900 6439 7592 342 -211 -389 C ATOM 2567 N LYS A 384 -29.549 42.232 -4.182 1.00 55.06 N ANISOU 2567 N LYS A 384 6922 6565 7431 422 -210 -617 N ATOM 2568 CA LYS A 384 -29.550 40.999 -3.412 1.00 51.02 C ANISOU 2568 CA LYS A 384 6478 6135 6774 455 -208 -658 C ATOM 2569 C LYS A 384 -30.621 40.045 -3.933 1.00 50.65 C ANISOU 2569 C LYS A 384 6506 6107 6630 450 -197 -585 C ATOM 2570 O LYS A 384 -31.659 40.459 -4.460 1.00 49.40 O ANISOU 2570 O LYS A 384 6342 5905 6521 429 -195 -537 O ATOM 2571 CB LYS A 384 -29.782 41.284 -1.932 1.00 44.83 C ANISOU 2571 CB LYS A 384 5660 5377 5996 478 -220 -778 C ATOM 2572 CG LYS A 384 -28.493 41.470 -1.177 1.00 47.82 C ANISOU 2572 CG LYS A 384 6000 5787 6384 497 -230 -861 C ATOM 2573 CD LYS A 384 -28.618 42.502 -0.067 1.00 47.20 C ANISOU 2573 CD LYS A 384 5838 5699 6397 503 -242 -982 C ATOM 2574 CE LYS A 384 -28.836 41.863 1.291 1.00 49.63 C ANISOU 2574 CE LYS A 384 6165 6100 6593 528 -249 -1069 C ATOM 2575 NZ LYS A 384 -28.274 42.747 2.360 1.00 49.22 N1+ ANISOU 2575 NZ LYS A 384 6024 6065 6613 538 -261 -1201 N1+ ATOM 2576 N LEU A 385 -30.354 38.756 -3.776 1.00 46.13 N ANISOU 2576 N LEU A 385 6001 5598 5927 471 -194 -577 N ATOM 2577 CA LEU A 385 -31.289 37.709 -4.163 1.00 46.40 C ANISOU 2577 CA LEU A 385 6109 5657 5866 471 -185 -518 C ATOM 2578 C LEU A 385 -32.407 37.685 -3.118 1.00 46.88 C ANISOU 2578 C LEU A 385 6176 5732 5903 481 -190 -570 C ATOM 2579 O LEU A 385 -32.341 36.965 -2.113 1.00 45.16 O ANISOU 2579 O LEU A 385 5986 5572 5600 503 -197 -618 O ATOM 2580 CB LEU A 385 -30.550 36.382 -4.300 1.00 44.94 C ANISOU 2580 CB LEU A 385 5981 5525 5570 490 -183 -499 C ATOM 2581 CG LEU A 385 -31.128 35.371 -5.282 1.00 40.59 C ANISOU 2581 CG LEU A 385 5492 4985 4945 481 -170 -419 C ATOM 2582 CD1 LEU A 385 -31.916 36.120 -6.284 1.00 38.55 C ANISOU 2582 CD1 LEU A 385 5214 4682 4752 446 -158 -356 C ATOM 2583 CD2 LEU A 385 -30.018 34.592 -5.981 1.00 37.68 C ANISOU 2583 CD2 LEU A 385 5140 4643 4532 487 -165 -395 C ATOM 2584 N GLU A 386 -33.450 38.504 -3.363 1.00 46.91 N ANISOU 2584 N GLU A 386 6150 5686 5987 460 -187 -559 N ATOM 2585 CA GLU A 386 -34.530 38.752 -2.401 1.00 42.72 C ANISOU 2585 CA GLU A 386 5605 5163 5462 464 -190 -624 C ATOM 2586 C GLU A 386 -35.865 38.835 -3.138 1.00 43.61 C ANISOU 2586 C GLU A 386 5735 5237 5598 443 -183 -561 C ATOM 2587 O GLU A 386 -36.170 39.861 -3.753 1.00 44.02 O ANISOU 2587 O GLU A 386 5736 5220 5770 423 -187 -536 O ATOM 2588 CB GLU A 386 -34.270 40.037 -1.616 1.00 42.63 C ANISOU 2588 CB GLU A 386 5503 5125 5570 464 -202 -722 C ATOM 2589 CG GLU A 386 -33.004 40.003 -0.774 1.00 43.54 C ANISOU 2589 CG GLU A 386 5595 5286 5662 485 -211 -796 C ATOM 2590 CD GLU A 386 -32.924 41.134 0.233 1.00 49.42 C ANISOU 2590 CD GLU A 386 6249 6022 6505 488 -222 -916 C ATOM 2591 OE1 GLU A 386 -33.699 42.106 0.111 1.00 51.81 O ANISOU 2591 OE1 GLU A 386 6496 6263 6926 472 -223 -938 O ATOM 2592 OE2 GLU A 386 -32.100 41.035 1.169 1.00 50.09 O1- ANISOU 2592 OE2 GLU A 386 6314 6165 6552 506 -230 -995 O1- ATOM 2593 N LEU A 387 -36.688 37.787 -3.027 1.00 45.45 N ANISOU 2593 N LEU A 387 6034 5511 5723 448 -174 -537 N ATOM 2594 CA LEU A 387 -37.901 37.639 -3.823 1.00 44.32 C ANISOU 2594 CA LEU A 387 5919 5339 5580 430 -165 -470 C ATOM 2595 C LEU A 387 -39.165 37.650 -2.965 1.00 44.72 C ANISOU 2595 C LEU A 387 5968 5405 5617 431 -163 -525 C ATOM 2596 O LEU A 387 -39.156 37.293 -1.780 1.00 44.39 O ANISOU 2596 O LEU A 387 5931 5422 5513 445 -164 -598 O ATOM 2597 CB LEU A 387 -37.863 36.344 -4.641 1.00 42.19 C ANISOU 2597 CB LEU A 387 5728 5102 5202 431 -154 -388 C ATOM 2598 CG LEU A 387 -36.694 36.134 -5.609 1.00 43.35 C ANISOU 2598 CG LEU A 387 5880 5248 5343 427 -151 -333 C ATOM 2599 CD1 LEU A 387 -35.552 35.315 -4.962 1.00 39.48 C ANISOU 2599 CD1 LEU A 387 5415 4810 4777 454 -155 -372 C ATOM 2600 CD2 LEU A 387 -37.221 35.459 -6.868 1.00 36.36 C ANISOU 2600 CD2 LEU A 387 5039 4364 4410 410 -138 -242 C ATOM 2601 N THR A 388 -40.269 38.016 -3.624 1.00 42.70 N ANISOU 2601 N THR A 388 5706 5103 5415 413 -161 -484 N ATOM 2602 CA THR A 388 -41.602 38.133 -3.040 1.00 39.83 C ANISOU 2602 CA THR A 388 5334 4743 5057 408 -158 -529 C ATOM 2603 C THR A 388 -42.499 37.000 -3.536 1.00 40.79 C ANISOU 2603 C THR A 388 5533 4891 5075 404 -144 -461 C ATOM 2604 O THR A 388 -42.570 36.751 -4.749 1.00 39.84 O ANISOU 2604 O THR A 388 5441 4743 4952 393 -141 -369 O ATOM 2605 CB THR A 388 -42.223 39.483 -3.422 1.00 38.27 C ANISOU 2605 CB THR A 388 5060 4462 5018 392 -171 -537 C ATOM 2606 CG2 THR A 388 -43.691 39.560 -3.021 1.00 37.42 C ANISOU 2606 CG2 THR A 388 4945 4353 4921 386 -167 -577 C ATOM 2607 OG1 THR A 388 -41.479 40.555 -2.835 1.00 32.91 O ANISOU 2607 OG1 THR A 388 4301 3756 4448 397 -184 -616 O ATOM 2608 N VAL A 389 -43.199 36.335 -2.607 1.00 41.13 N ANISOU 2608 N VAL A 389 5605 4989 5034 408 -135 -508 N ATOM 2609 CA VAL A 389 -44.140 35.252 -2.924 1.00 40.49 C ANISOU 2609 CA VAL A 389 5593 4933 4860 403 -121 -455 C ATOM 2610 C VAL A 389 -45.554 35.698 -2.592 1.00 41.82 C ANISOU 2610 C VAL A 389 5734 5088 5066 390 -117 -495 C ATOM 2611 O VAL A 389 -45.882 35.925 -1.421 1.00 38.14 O ANISOU 2611 O VAL A 389 5237 4663 4592 390 -115 -586 O ATOM 2612 CB VAL A 389 -43.817 33.945 -2.181 1.00 36.58 C ANISOU 2612 CB VAL A 389 5158 4514 4229 416 -116 -458 C ATOM 2613 CG1 VAL A 389 -44.718 32.834 -2.683 1.00 34.74 C ANISOU 2613 CG1 VAL A 389 4992 4291 3917 409 -103 -394 C ATOM 2614 CG2 VAL A 389 -42.401 33.563 -2.418 1.00 37.00 C ANISOU 2614 CG2 VAL A 389 5227 4576 4256 431 -124 -432 C ATOM 2615 N GLU A 390 -46.399 35.768 -3.626 1.00 43.97 N ANISOU 2615 N GLU A 390 6018 5314 5375 377 -115 -430 N ATOM 2616 CA GLU A 390 -47.794 36.157 -3.463 1.00 43.21 C ANISOU 2616 CA GLU A 390 5898 5199 5322 365 -112 -462 C ATOM 2617 C GLU A 390 -48.598 34.995 -2.901 1.00 44.15 C ANISOU 2617 C GLU A 390 6076 5383 5317 363 -93 -470 C ATOM 2618 O GLU A 390 -48.549 33.878 -3.432 1.00 43.32 O ANISOU 2618 O GLU A 390 6040 5298 5121 365 -84 -399 O ATOM 2619 CB GLU A 390 -48.374 36.618 -4.798 1.00 39.64 C ANISOU 2619 CB GLU A 390 5435 4676 4949 352 -121 -381 C ATOM 2620 CG GLU A 390 -47.636 37.812 -5.368 1.00 41.55 C ANISOU 2620 CG GLU A 390 5613 4852 5323 348 -143 -360 C ATOM 2621 CD GLU A 390 -47.685 39.025 -4.450 1.00 45.49 C ANISOU 2621 CD GLU A 390 6023 5317 5944 351 -156 -465 C ATOM 2622 OE1 GLU A 390 -48.710 39.231 -3.758 1.00 44.85 O ANISOU 2622 OE1 GLU A 390 5915 5241 5884 349 -153 -539 O ATOM 2623 OE2 GLU A 390 -46.665 39.744 -4.379 1.00 48.28 O1- ANISOU 2623 OE2 GLU A 390 6331 5644 6371 354 -169 -482 O1- ATOM 2624 N VAL A 391 -49.335 35.260 -1.818 1.00 41.27 N ANISOU 2624 N VAL A 391 5677 5051 4951 357 -87 -560 N ATOM 2625 CA VAL A 391 -50.144 34.246 -1.161 1.00 39.79 C ANISOU 2625 CA VAL A 391 5537 4933 4650 349 -69 -572 C ATOM 2626 C VAL A 391 -51.504 34.863 -0.856 1.00 37.49 C ANISOU 2626 C VAL A 391 5198 4630 4416 334 -63 -636 C ATOM 2627 O VAL A 391 -51.663 36.082 -0.839 1.00 38.83 O ANISOU 2627 O VAL A 391 5291 4750 4712 333 -75 -693 O ATOM 2628 CB VAL A 391 -49.454 33.701 0.118 1.00 38.35 C ANISOU 2628 CB VAL A 391 5363 4839 4367 353 -66 -622 C ATOM 2629 CG1 VAL A 391 -49.419 34.756 1.223 1.00 40.48 C ANISOU 2629 CG1 VAL A 391 5548 5139 4694 349 -70 -746 C ATOM 2630 CG2 VAL A 391 -50.092 32.389 0.591 1.00 37.10 C ANISOU 2630 CG2 VAL A 391 5269 4749 4076 342 -51 -594 C ATOM 2631 N VAL A 392 -52.510 33.999 -0.657 1.00 38.69 N ANISOU 2631 N VAL A 392 5394 4823 4483 321 -45 -624 N ATOM 2632 CA VAL A 392 -53.879 34.431 -0.384 1.00 37.75 C ANISOU 2632 CA VAL A 392 5235 4701 4406 305 -36 -685 C ATOM 2633 C VAL A 392 -54.082 34.590 1.120 1.00 39.02 C ANISOU 2633 C VAL A 392 5352 4950 4525 292 -25 -802 C ATOM 2634 O VAL A 392 -53.649 33.749 1.922 1.00 39.03 O ANISOU 2634 O VAL A 392 5389 5037 4403 288 -16 -801 O ATOM 2635 CB VAL A 392 -54.892 33.441 -0.989 1.00 37.03 C ANISOU 2635 CB VAL A 392 5210 4611 4249 294 -21 -614 C ATOM 2636 CG1 VAL A 392 -56.309 33.763 -0.545 1.00 37.46 C ANISOU 2636 CG1 VAL A 392 5226 4678 4331 276 -9 -685 C ATOM 2637 CG2 VAL A 392 -54.807 33.470 -2.498 1.00 37.89 C ANISOU 2637 CG2 VAL A 392 5345 4642 4411 302 -33 -515 C ATOM 2638 N THR A 393 -54.725 35.693 1.503 1.00 39.23 N ANISOU 2638 N THR A 393 5292 4957 4656 285 -28 -904 N ATOM 2639 CA THR A 393 -54.992 35.978 2.907 1.00 39.99 C ANISOU 2639 CA THR A 393 5329 5145 4722 270 -16 -1034 C ATOM 2640 C THR A 393 -55.754 34.829 3.550 1.00 36.92 C ANISOU 2640 C THR A 393 4992 4855 4182 246 10 -1025 C ATOM 2641 O THR A 393 -56.869 34.504 3.136 1.00 32.65 O ANISOU 2641 O THR A 393 4473 4295 3637 234 22 -999 O ATOM 2642 CB THR A 393 -55.797 37.269 3.029 1.00 40.69 C ANISOU 2642 CB THR A 393 5315 5184 4961 265 -22 -1144 C ATOM 2643 CG2 THR A 393 -56.279 37.451 4.450 1.00 33.59 C ANISOU 2643 CG2 THR A 393 4351 4394 4016 243 -4 -1288 C ATOM 2644 OG1 THR A 393 -54.988 38.386 2.622 1.00 41.64 O ANISOU 2644 OG1 THR A 393 5375 5218 5229 284 -49 -1161 O ATOM 2645 N GLY A 394 -55.156 34.207 4.562 1.00 36.09 N ANISOU 2645 N GLY A 394 4904 4856 3953 236 17 -1041 N ATOM 2646 CA GLY A 394 -55.855 33.143 5.248 1.00 36.05 C ANISOU 2646 CA GLY A 394 4941 4950 3806 207 39 -1026 C ATOM 2647 C GLY A 394 -55.835 31.798 4.560 1.00 40.34 C ANISOU 2647 C GLY A 394 5590 5476 4263 210 42 -885 C ATOM 2648 O GLY A 394 -56.563 30.892 4.984 1.00 38.81 O ANISOU 2648 O GLY A 394 5432 5347 3968 185 59 -861 O ATOM 2649 N TRP A 395 -55.057 31.641 3.486 1.00 41.16 N ANISOU 2649 N TRP A 395 5737 5492 4407 239 25 -795 N ATOM 2650 CA TRP A 395 -54.598 30.316 3.073 1.00 38.14 C ANISOU 2650 CA TRP A 395 5445 5112 3934 245 22 -678 C ATOM 2651 C TRP A 395 -53.430 29.943 3.993 1.00 37.89 C ANISOU 2651 C TRP A 395 5418 5154 3822 249 10 -680 C ATOM 2652 O TRP A 395 -52.257 29.930 3.608 1.00 36.50 O ANISOU 2652 O TRP A 395 5258 4945 3666 274 -9 -641 O ATOM 2653 CB TRP A 395 -54.216 30.303 1.601 1.00 36.80 C ANISOU 2653 CB TRP A 395 5311 4837 3835 270 11 -594 C ATOM 2654 CG TRP A 395 -55.381 30.328 0.670 1.00 37.90 C ANISOU 2654 CG TRP A 395 5461 4916 4022 264 21 -567 C ATOM 2655 CD1 TRP A 395 -56.679 30.638 0.976 1.00 38.53 C ANISOU 2655 CD1 TRP A 395 5509 5011 4120 243 37 -624 C ATOM 2656 CD2 TRP A 395 -55.370 29.995 -0.728 1.00 39.62 C ANISOU 2656 CD2 TRP A 395 5722 5060 4272 277 17 -477 C ATOM 2657 CE2 TRP A 395 -56.690 30.143 -1.206 1.00 37.92 C ANISOU 2657 CE2 TRP A 395 5500 4815 4093 264 27 -481 C ATOM 2658 CE3 TRP A 395 -54.370 29.598 -1.620 1.00 35.25 C ANISOU 2658 CE3 TRP A 395 5207 4468 3718 296 5 -400 C ATOM 2659 NE1 TRP A 395 -57.472 30.534 -0.152 1.00 36.28 N ANISOU 2659 NE1 TRP A 395 5247 4659 3880 245 39 -571 N ATOM 2660 CZ2 TRP A 395 -57.029 29.915 -2.538 1.00 42.56 C ANISOU 2660 CZ2 TRP A 395 6117 5341 4712 270 25 -407 C ATOM 2661 CZ3 TRP A 395 -54.712 29.364 -2.929 1.00 38.44 C ANISOU 2661 CZ3 TRP A 395 5638 4817 4150 300 5 -332 C ATOM 2662 CH2 TRP A 395 -56.029 29.524 -3.382 1.00 40.45 C ANISOU 2662 CH2 TRP A 395 5886 5048 4437 286 14 -334 C ATOM 2663 N THR A 396 -53.797 29.662 5.251 1.00 38.33 N ANISOU 2663 N THR A 396 5456 5323 3785 220 20 -728 N ATOM 2664 CA THR A 396 -52.843 29.506 6.350 1.00 40.53 C ANISOU 2664 CA THR A 396 5719 5696 3986 216 6 -751 C ATOM 2665 C THR A 396 -51.755 28.475 6.058 1.00 42.09 C ANISOU 2665 C THR A 396 5985 5877 4130 236 -16 -642 C ATOM 2666 O THR A 396 -50.567 28.708 6.324 1.00 38.28 O ANISOU 2666 O THR A 396 5487 5407 3650 255 -36 -653 O ATOM 2667 CB THR A 396 -53.595 29.107 7.621 1.00 33.90 C ANISOU 2667 CB THR A 396 4860 4989 3032 172 22 -793 C ATOM 2668 CG2 THR A 396 -52.625 28.606 8.652 1.00 35.72 C ANISOU 2668 CG2 THR A 396 5093 5323 3156 165 4 -777 C ATOM 2669 OG1 THR A 396 -54.324 30.235 8.122 1.00 37.32 O ANISOU 2669 OG1 THR A 396 5206 5456 3517 155 39 -927 O ATOM 2670 N ASP A 397 -52.154 27.304 5.558 1.00 44.79 N ANISOU 2670 N ASP A 397 6399 6195 4425 232 -12 -542 N ATOM 2671 CA ASP A 397 -51.185 26.273 5.221 1.00 43.98 C ANISOU 2671 CA ASP A 397 6357 6067 4287 252 -35 -443 C ATOM 2672 C ASP A 397 -50.111 26.824 4.291 1.00 43.30 C ANISOU 2672 C ASP A 397 6266 5896 4291 290 -49 -438 C ATOM 2673 O ASP A 397 -48.911 26.682 4.557 1.00 42.54 O ANISOU 2673 O ASP A 397 6170 5813 4178 308 -72 -425 O ATOM 2674 CB ASP A 397 -51.916 25.091 4.594 1.00 48.28 C ANISOU 2674 CB ASP A 397 6968 6574 4803 244 -26 -351 C ATOM 2675 CG ASP A 397 -52.701 24.301 5.611 1.00 58.75 C ANISOU 2675 CG ASP A 397 8305 7991 6026 204 -19 -331 C ATOM 2676 OD1 ASP A 397 -52.539 24.580 6.829 1.00 57.69 O ANISOU 2676 OD1 ASP A 397 8130 7962 5826 182 -22 -380 O ATOM 2677 OD2 ASP A 397 -53.494 23.422 5.194 1.00 64.42 O1- ANISOU 2677 OD2 ASP A 397 9068 8683 6726 191 -8 -269 O1- ATOM 2678 N TYR A 398 -50.532 27.489 3.210 1.00 37.67 N ANISOU 2678 N TYR A 398 5543 5097 3673 300 -38 -448 N ATOM 2679 CA TYR A 398 -49.593 28.195 2.349 1.00 37.16 C ANISOU 2679 CA TYR A 398 5461 4959 3697 329 -49 -448 C ATOM 2680 C TYR A 398 -48.851 29.287 3.108 1.00 35.57 C ANISOU 2680 C TYR A 398 5192 4790 3532 334 -60 -536 C ATOM 2681 O TYR A 398 -47.625 29.408 2.993 1.00 37.91 O ANISOU 2681 O TYR A 398 5485 5073 3847 356 -77 -528 O ATOM 2682 CB TYR A 398 -50.328 28.794 1.144 1.00 40.38 C ANISOU 2682 CB TYR A 398 5861 5283 4197 330 -37 -440 C ATOM 2683 CG TYR A 398 -50.622 27.807 0.042 1.00 35.74 C ANISOU 2683 CG TYR A 398 5337 4648 3594 334 -32 -349 C ATOM 2684 CD1 TYR A 398 -50.416 26.443 0.235 1.00 37.13 C ANISOU 2684 CD1 TYR A 398 5571 4852 3686 335 -36 -289 C ATOM 2685 CD2 TYR A 398 -51.142 28.226 -1.172 1.00 32.85 C ANISOU 2685 CD2 TYR A 398 4968 4213 3299 336 -25 -326 C ATOM 2686 CE1 TYR A 398 -50.688 25.532 -0.767 1.00 33.19 C ANISOU 2686 CE1 TYR A 398 5121 4310 3181 339 -31 -219 C ATOM 2687 CE2 TYR A 398 -51.427 27.311 -2.174 1.00 35.73 C ANISOU 2687 CE2 TYR A 398 5385 4547 3645 338 -19 -253 C ATOM 2688 CZ TYR A 398 -51.189 25.968 -1.962 1.00 32.04 C ANISOU 2688 CZ TYR A 398 4971 4105 3099 340 -21 -206 C ATOM 2689 OH TYR A 398 -51.461 25.054 -2.944 1.00 30.75 O ANISOU 2689 OH TYR A 398 4851 3910 2924 342 -15 -146 O ATOM 2690 N ILE A 399 -49.578 30.118 3.857 1.00 35.32 N ANISOU 2690 N ILE A 399 5100 4800 3519 315 -49 -629 N ATOM 2691 CA ILE A 399 -48.917 31.152 4.654 1.00 36.25 C ANISOU 2691 CA ILE A 399 5144 4955 3675 319 -58 -728 C ATOM 2692 C ILE A 399 -47.822 30.534 5.509 1.00 34.98 C ANISOU 2692 C ILE A 399 4997 4872 3421 325 -76 -715 C ATOM 2693 O ILE A 399 -46.668 30.973 5.489 1.00 37.18 O ANISOU 2693 O ILE A 399 5253 5135 3737 346 -93 -732 O ATOM 2694 CB ILE A 399 -49.927 31.906 5.539 1.00 39.68 C ANISOU 2694 CB ILE A 399 5509 5448 4120 293 -42 -841 C ATOM 2695 CG1 ILE A 399 -50.745 32.928 4.746 1.00 42.18 C ANISOU 2695 CG1 ILE A 399 5782 5672 4571 294 -33 -879 C ATOM 2696 CG2 ILE A 399 -49.191 32.627 6.683 1.00 36.52 C ANISOU 2696 CG2 ILE A 399 5035 5126 3714 291 -51 -947 C ATOM 2697 CD1 ILE A 399 -52.171 33.077 5.260 1.00 40.92 C ANISOU 2697 CD1 ILE A 399 5591 5556 4400 265 -12 -945 C ATOM 2698 N THR A 400 -48.175 29.500 6.276 1.00 36.45 N ANISOU 2698 N THR A 400 5219 5144 3486 304 -75 -679 N ATOM 2699 CA THR A 400 -47.202 28.857 7.150 1.00 34.40 C ANISOU 2699 CA THR A 400 4971 4965 3133 306 -98 -656 C ATOM 2700 C THR A 400 -46.031 28.305 6.361 1.00 35.99 C ANISOU 2700 C THR A 400 5220 5097 3357 339 -120 -574 C ATOM 2701 O THR A 400 -44.896 28.329 6.853 1.00 36.04 O ANISOU 2701 O THR A 400 5211 5138 3344 354 -143 -585 O ATOM 2702 CB THR A 400 -47.865 27.740 7.963 1.00 38.42 C ANISOU 2702 CB THR A 400 5516 5567 3514 273 -96 -605 C ATOM 2703 CG2 THR A 400 -46.857 27.033 8.868 1.00 35.68 C ANISOU 2703 CG2 THR A 400 5179 5304 3072 273 -127 -565 C ATOM 2704 OG1 THR A 400 -48.943 28.271 8.751 1.00 44.80 O ANISOU 2704 OG1 THR A 400 6273 6456 4294 237 -72 -692 O ATOM 2705 N ALA A 401 -46.295 27.801 5.147 1.00 33.99 N ANISOU 2705 N ALA A 401 5020 4752 3143 351 -114 -498 N ATOM 2706 CA ALA A 401 -45.238 27.297 4.278 1.00 37.16 C ANISOU 2706 CA ALA A 401 5459 5086 3572 381 -131 -431 C ATOM 2707 C ALA A 401 -44.232 28.388 3.927 1.00 36.48 C ANISOU 2707 C ALA A 401 5326 4960 3574 404 -138 -483 C ATOM 2708 O ALA A 401 -43.021 28.179 4.029 1.00 35.08 O ANISOU 2708 O ALA A 401 5151 4788 3390 424 -160 -471 O ATOM 2709 CB ALA A 401 -45.846 26.714 2.995 1.00 39.21 C ANISOU 2709 CB ALA A 401 5770 5265 3864 385 -117 -360 C ATOM 2710 N ILE A 402 -44.711 29.544 3.456 1.00 36.46 N ANISOU 2710 N ILE A 402 5279 4911 3664 400 -122 -537 N ATOM 2711 CA ILE A 402 -43.798 30.638 3.124 1.00 36.26 C ANISOU 2711 CA ILE A 402 5203 4842 3733 416 -129 -582 C ATOM 2712 C ILE A 402 -42.907 30.947 4.311 1.00 36.07 C ANISOU 2712 C ILE A 402 5136 4893 3678 421 -146 -651 C ATOM 2713 O ILE A 402 -41.673 30.961 4.198 1.00 31.36 O ANISOU 2713 O ILE A 402 4535 4285 3095 442 -164 -643 O ATOM 2714 CB ILE A 402 -44.569 31.892 2.680 1.00 37.97 C ANISOU 2714 CB ILE A 402 5366 5003 4059 406 -115 -635 C ATOM 2715 CG1 ILE A 402 -44.746 31.911 1.168 1.00 36.12 C ANISOU 2715 CG1 ILE A 402 5158 4674 3890 411 -108 -561 C ATOM 2716 CG2 ILE A 402 -43.841 33.138 3.156 1.00 38.28 C ANISOU 2716 CG2 ILE A 402 5324 5041 4178 413 -124 -727 C ATOM 2717 CD1 ILE A 402 -45.412 30.694 0.635 1.00 37.66 C ANISOU 2717 CD1 ILE A 402 5426 4867 4015 406 -99 -479 C ATOM 2718 N ASP A 403 -43.533 31.193 5.474 1.00 37.73 N ANISOU 2718 N ASP A 403 5308 5188 3840 400 -141 -723 N ATOM 2719 CA ASP A 403 -42.804 31.408 6.718 1.00 32.48 C ANISOU 2719 CA ASP A 403 4598 4619 3124 399 -157 -792 C ATOM 2720 C ASP A 403 -41.691 30.383 6.857 1.00 35.23 C ANISOU 2720 C ASP A 403 4994 4993 3400 417 -184 -719 C ATOM 2721 O ASP A 403 -40.520 30.737 7.044 1.00 35.60 O ANISOU 2721 O ASP A 403 5012 5045 3470 437 -202 -749 O ATOM 2722 CB ASP A 403 -43.765 31.310 7.903 1.00 34.65 C ANISOU 2722 CB ASP A 403 4848 5007 3313 366 -146 -847 C ATOM 2723 CG ASP A 403 -44.729 32.480 8.006 1.00 34.25 C ANISOU 2723 CG ASP A 403 4725 4944 3342 349 -123 -953 C ATOM 2724 OD1 ASP A 403 -44.582 33.465 7.263 1.00 39.80 O ANISOU 2724 OD1 ASP A 403 5391 5553 4176 364 -121 -987 O ATOM 2725 OD2 ASP A 403 -45.652 32.410 8.842 1.00 35.61 O1- ANISOU 2725 OD2 ASP A 403 4875 5204 3450 319 -109 -1002 O1- ATOM 2726 N THR A 404 -42.050 29.098 6.729 1.00 34.66 N ANISOU 2726 N THR A 404 4992 4928 3249 412 -188 -622 N ATOM 2727 CA THR A 404 -41.077 28.018 6.880 1.00 35.80 C ANISOU 2727 CA THR A 404 5180 5090 3333 429 -218 -547 C ATOM 2728 C THR A 404 -40.029 28.074 5.782 1.00 35.19 C ANISOU 2728 C THR A 404 5117 4920 3336 462 -227 -518 C ATOM 2729 O THR A 404 -38.821 28.003 6.049 1.00 33.50 O ANISOU 2729 O THR A 404 4891 4721 3118 482 -252 -523 O ATOM 2730 CB THR A 404 -41.788 26.667 6.861 1.00 33.74 C ANISOU 2730 CB THR A 404 4985 4839 2996 414 -221 -450 C ATOM 2731 CG2 THR A 404 -40.805 25.555 7.144 1.00 33.98 C ANISOU 2731 CG2 THR A 404 5050 4888 2974 431 -259 -375 C ATOM 2732 OG1 THR A 404 -42.828 26.657 7.847 1.00 37.14 O ANISOU 2732 OG1 THR A 404 5399 5362 3351 377 -209 -478 O ATOM 2733 N MET A 405 -40.491 28.210 4.533 1.00 36.81 N ANISOU 2733 N MET A 405 5343 5033 3610 465 -205 -488 N ATOM 2734 CA MET A 405 -39.603 28.307 3.380 1.00 34.69 C ANISOU 2734 CA MET A 405 5084 4684 3414 489 -208 -460 C ATOM 2735 C MET A 405 -38.690 29.520 3.479 1.00 35.42 C ANISOU 2735 C MET A 405 5113 4768 3579 499 -212 -534 C ATOM 2736 O MET A 405 -37.519 29.457 3.084 1.00 36.96 O ANISOU 2736 O MET A 405 5306 4938 3801 521 -226 -523 O ATOM 2737 CB MET A 405 -40.433 28.363 2.084 1.00 36.58 C ANISOU 2737 CB MET A 405 5347 4846 3707 481 -183 -420 C ATOM 2738 CG MET A 405 -39.831 27.590 0.890 1.00 34.08 C ANISOU 2738 CG MET A 405 5072 4471 3407 498 -186 -350 C ATOM 2739 SD MET A 405 -40.431 28.176 -0.717 1.00 33.97 S ANISOU 2739 SD MET A 405 5056 4377 3473 488 -158 -324 S ATOM 2740 CE MET A 405 -42.087 27.500 -0.781 1.00 29.29 C ANISOU 2740 CE MET A 405 4506 3788 2836 467 -140 -289 C ATOM 2741 N SER A 406 -39.203 30.642 3.977 1.00 34.01 N ANISOU 2741 N SER A 406 4876 4607 3440 485 -200 -615 N ATOM 2742 CA SER A 406 -38.311 31.774 4.150 1.00 34.70 C ANISOU 2742 CA SER A 406 4897 4685 3604 495 -206 -690 C ATOM 2743 C SER A 406 -37.153 31.401 5.072 1.00 35.99 C ANISOU 2743 C SER A 406 5050 4917 3706 511 -234 -711 C ATOM 2744 O SER A 406 -36.012 31.808 4.837 1.00 35.25 O ANISOU 2744 O SER A 406 4931 4799 3664 529 -245 -731 O ATOM 2745 CB SER A 406 -39.079 32.989 4.668 1.00 35.78 C ANISOU 2745 CB SER A 406 4962 4832 3799 477 -193 -787 C ATOM 2746 OG SER A 406 -38.372 34.181 4.359 1.00 37.40 O ANISOU 2746 OG SER A 406 5105 4985 4121 485 -195 -842 O ATOM 2747 N GLN A 407 -37.411 30.585 6.097 1.00 36.30 N ANISOU 2747 N GLN A 407 5111 5047 3635 502 -248 -700 N ATOM 2748 CA GLN A 407 -36.311 30.156 6.956 1.00 38.40 C ANISOU 2748 CA GLN A 407 5368 5383 3838 516 -280 -707 C ATOM 2749 C GLN A 407 -35.309 29.336 6.160 1.00 37.50 C ANISOU 2749 C GLN A 407 5301 5212 3737 544 -299 -630 C ATOM 2750 O GLN A 407 -34.144 29.728 6.024 1.00 39.17 O ANISOU 2750 O GLN A 407 5484 5405 3993 564 -312 -659 O ATOM 2751 CB GLN A 407 -36.812 29.370 8.173 1.00 33.22 C ANISOU 2751 CB GLN A 407 4726 4839 3056 496 -295 -690 C ATOM 2752 CG GLN A 407 -37.740 30.156 9.074 1.00 34.86 C ANISOU 2752 CG GLN A 407 4878 5126 3241 466 -276 -782 C ATOM 2753 CD GLN A 407 -36.994 31.106 9.985 1.00 40.79 C ANISOU 2753 CD GLN A 407 5548 5948 4003 468 -287 -894 C ATOM 2754 NE2 GLN A 407 -37.132 32.397 9.719 1.00 39.29 N ANISOU 2754 NE2 GLN A 407 5295 5712 3921 468 -266 -990 N ATOM 2755 OE1 GLN A 407 -36.321 30.687 10.942 1.00 41.94 O ANISOU 2755 OE1 GLN A 407 5682 6190 4062 469 -316 -897 O ATOM 2756 N GLN A 408 -35.757 28.202 5.602 1.00 37.77 N ANISOU 2756 N GLN A 408 5401 5214 3736 544 -299 -538 N ATOM 2757 CA GLN A 408 -34.872 27.343 4.817 1.00 35.67 C ANISOU 2757 CA GLN A 408 5174 4894 3486 569 -316 -473 C ATOM 2758 C GLN A 408 -34.009 28.151 3.866 1.00 36.22 C ANISOU 2758 C GLN A 408 5213 4896 3651 585 -305 -504 C ATOM 2759 O GLN A 408 -32.858 27.781 3.605 1.00 36.47 O ANISOU 2759 O GLN A 408 5247 4912 3697 608 -325 -492 O ATOM 2760 CB GLN A 408 -35.689 26.307 4.047 1.00 36.01 C ANISOU 2760 CB GLN A 408 5278 4890 3512 563 -306 -390 C ATOM 2761 CG GLN A 408 -36.443 25.353 4.933 1.00 34.33 C ANISOU 2761 CG GLN A 408 5098 4737 3208 546 -320 -342 C ATOM 2762 CD GLN A 408 -37.634 24.671 4.273 1.00 34.30 C ANISOU 2762 CD GLN A 408 5143 4693 3197 531 -299 -283 C ATOM 2763 NE2 GLN A 408 -38.320 23.836 5.033 1.00 37.81 N ANISOU 2763 NE2 GLN A 408 5614 5187 3565 512 -311 -237 N ATOM 2764 OE1 GLN A 408 -37.960 24.923 3.122 1.00 37.60 O ANISOU 2764 OE1 GLN A 408 5571 5042 3675 532 -273 -279 O ATOM 2765 N LEU A 409 -34.527 29.280 3.380 1.00 36.64 N ANISOU 2765 N LEU A 409 5234 4913 3774 570 -276 -546 N ATOM 2766 CA LEU A 409 -33.867 30.043 2.330 1.00 37.85 C ANISOU 2766 CA LEU A 409 5360 4998 4022 577 -263 -557 C ATOM 2767 C LEU A 409 -32.907 31.074 2.906 1.00 37.38 C ANISOU 2767 C LEU A 409 5234 4957 4011 585 -273 -638 C ATOM 2768 O LEU A 409 -31.836 31.300 2.334 1.00 37.51 O ANISOU 2768 O LEU A 409 5234 4941 4079 598 -277 -640 O ATOM 2769 CB LEU A 409 -34.923 30.707 1.438 1.00 36.38 C ANISOU 2769 CB LEU A 409 5171 4756 3897 555 -232 -545 C ATOM 2770 CG LEU A 409 -35.529 29.909 0.276 1.00 37.29 C ANISOU 2770 CG LEU A 409 5341 4825 4001 549 -217 -464 C ATOM 2771 CD1 LEU A 409 -34.671 29.975 -0.975 1.00 38.85 C ANISOU 2771 CD1 LEU A 409 5536 4973 4251 555 -211 -433 C ATOM 2772 CD2 LEU A 409 -35.717 28.467 0.669 1.00 32.90 C ANISOU 2772 CD2 LEU A 409 4843 4304 3355 557 -232 -416 C ATOM 2773 N LYS A 410 -33.276 31.700 4.025 1.00 37.55 N ANISOU 2773 N LYS A 410 5213 5036 4017 575 -276 -710 N ATOM 2774 CA LYS A 410 -32.336 32.524 4.774 1.00 38.06 C ANISOU 2774 CA LYS A 410 5212 5136 4114 584 -290 -796 C ATOM 2775 C LYS A 410 -31.030 31.776 4.998 1.00 39.20 C ANISOU 2775 C LYS A 410 5371 5307 4215 610 -320 -777 C ATOM 2776 O LYS A 410 -29.943 32.315 4.761 1.00 39.52 O ANISOU 2776 O LYS A 410 5375 5324 4317 624 -326 -811 O ATOM 2777 CB LYS A 410 -32.966 32.917 6.115 1.00 42.85 C ANISOU 2777 CB LYS A 410 5778 5831 4673 569 -293 -874 C ATOM 2778 CG LYS A 410 -32.425 34.196 6.728 1.00 45.84 C ANISOU 2778 CG LYS A 410 6067 6228 5121 570 -295 -991 C ATOM 2779 CD LYS A 410 -33.483 34.874 7.602 1.00 47.62 C ANISOU 2779 CD LYS A 410 6241 6509 5342 546 -282 -1077 C ATOM 2780 CE LYS A 410 -34.769 35.196 6.812 1.00 45.70 C ANISOU 2780 CE LYS A 410 6011 6193 5158 528 -254 -1051 C ATOM 2781 NZ LYS A 410 -34.507 35.860 5.498 1.00 43.65 N1+ ANISOU 2781 NZ LYS A 410 5745 5813 5028 533 -243 -1018 N1+ ATOM 2782 N ALA A 411 -31.135 30.511 5.438 1.00 37.42 N ANISOU 2782 N ALA A 411 5199 5128 3892 616 -342 -717 N ATOM 2783 CA ALA A 411 -29.971 29.649 5.623 1.00 36.07 C ANISOU 2783 CA ALA A 411 5044 4975 3685 642 -377 -687 C ATOM 2784 C ALA A 411 -29.216 29.394 4.326 1.00 35.61 C ANISOU 2784 C ALA A 411 5006 4834 3691 659 -371 -648 C ATOM 2785 O ALA A 411 -27.999 29.193 4.353 1.00 37.41 O ANISOU 2785 O ALA A 411 5219 5064 3931 682 -394 -658 O ATOM 2786 CB ALA A 411 -30.403 28.314 6.234 1.00 37.05 C ANISOU 2786 CB ALA A 411 5221 5150 3708 641 -403 -615 C ATOM 2787 N ALA A 412 -29.912 29.357 3.189 1.00 37.91 N ANISOU 2787 N ALA A 412 5325 5060 4018 646 -341 -604 N ATOM 2788 CA ALA A 412 -29.222 29.191 1.916 1.00 40.84 C ANISOU 2788 CA ALA A 412 5705 5367 4445 655 -331 -574 C ATOM 2789 C ALA A 412 -28.600 30.488 1.417 1.00 40.76 C ANISOU 2789 C ALA A 412 5637 5323 4525 649 -313 -625 C ATOM 2790 O ALA A 412 -27.721 30.439 0.551 1.00 45.09 O ANISOU 2790 O ALA A 412 6179 5838 5115 656 -310 -614 O ATOM 2791 CB ALA A 412 -30.176 28.637 0.853 1.00 39.68 C ANISOU 2791 CB ALA A 412 5606 5175 4296 641 -307 -508 C ATOM 2792 N GLY A 413 -29.018 31.628 1.956 1.00 38.75 N ANISOU 2792 N GLY A 413 5337 5078 4308 635 -304 -683 N ATOM 2793 CA GLY A 413 -28.546 32.921 1.524 1.00 40.15 C ANISOU 2793 CA GLY A 413 5454 5215 4587 626 -289 -728 C ATOM 2794 C GLY A 413 -29.443 33.633 0.539 1.00 38.57 C ANISOU 2794 C GLY A 413 5247 4952 4455 599 -259 -698 C ATOM 2795 O GLY A 413 -28.938 34.417 -0.274 1.00 41.70 O ANISOU 2795 O GLY A 413 5607 5300 4937 588 -247 -695 O ATOM 2796 N ILE A 414 -30.753 33.390 0.586 1.00 33.57 N ANISOU 2796 N ILE A 414 4645 4320 3789 585 -249 -670 N ATOM 2797 CA ILE A 414 -31.713 33.932 -0.370 1.00 40.46 C ANISOU 2797 CA ILE A 414 5517 5136 4720 560 -225 -631 C ATOM 2798 C ILE A 414 -32.870 34.553 0.400 1.00 41.20 C ANISOU 2798 C ILE A 414 5587 5241 4828 547 -220 -678 C ATOM 2799 O ILE A 414 -33.415 33.927 1.318 1.00 38.05 O ANISOU 2799 O ILE A 414 5212 4899 4344 552 -227 -694 O ATOM 2800 CB ILE A 414 -32.252 32.854 -1.335 1.00 40.79 C ANISOU 2800 CB ILE A 414 5627 5165 4707 556 -214 -544 C ATOM 2801 CG1 ILE A 414 -31.116 32.085 -2.021 1.00 36.65 C ANISOU 2801 CG1 ILE A 414 5122 4640 4162 570 -219 -511 C ATOM 2802 CG2 ILE A 414 -33.174 33.495 -2.358 1.00 40.31 C ANISOU 2802 CG2 ILE A 414 5559 5051 4708 528 -192 -501 C ATOM 2803 CD1 ILE A 414 -31.478 30.668 -2.349 1.00 36.50 C ANISOU 2803 CD1 ILE A 414 5169 4634 4065 577 -220 -455 C ATOM 2804 N GLY A 415 -33.258 35.769 0.012 1.00 40.43 N ANISOU 2804 N GLY A 415 5435 5088 4838 529 -210 -698 N ATOM 2805 CA GLY A 415 -34.357 36.451 0.681 1.00 36.85 C ANISOU 2805 CA GLY A 415 4947 4638 4418 517 -206 -755 C ATOM 2806 C GLY A 415 -35.691 36.004 0.129 1.00 37.41 C ANISOU 2806 C GLY A 415 5064 4690 4459 502 -192 -694 C ATOM 2807 O GLY A 415 -35.914 36.027 -1.086 1.00 44.35 O ANISOU 2807 O GLY A 415 5961 5514 5375 490 -182 -618 O ATOM 2808 N LEU A 416 -36.579 35.569 1.017 1.00 34.93 N ANISOU 2808 N LEU A 416 4767 4430 4074 500 -190 -725 N ATOM 2809 CA LEU A 416 -37.947 35.206 0.660 1.00 37.48 C ANISOU 2809 CA LEU A 416 5128 4741 4373 485 -176 -682 C ATOM 2810 C LEU A 416 -38.904 35.900 1.621 1.00 40.93 C ANISOU 2810 C LEU A 416 5515 5204 4835 473 -173 -770 C ATOM 2811 O LEU A 416 -38.818 35.699 2.835 1.00 41.18 O ANISOU 2811 O LEU A 416 5532 5315 4799 476 -179 -837 O ATOM 2812 CB LEU A 416 -38.146 33.692 0.712 1.00 35.09 C ANISOU 2812 CB LEU A 416 4906 4484 3940 491 -176 -619 C ATOM 2813 CG LEU A 416 -39.377 33.145 -0.016 1.00 36.59 C ANISOU 2813 CG LEU A 416 5146 4650 4107 477 -160 -553 C ATOM 2814 CD1 LEU A 416 -39.147 33.247 -1.487 1.00 37.33 C ANISOU 2814 CD1 LEU A 416 5252 4678 4255 473 -153 -482 C ATOM 2815 CD2 LEU A 416 -39.716 31.706 0.382 1.00 35.99 C ANISOU 2815 CD2 LEU A 416 5138 4627 3910 481 -161 -512 C ATOM 2816 N SER A 417 -39.802 36.721 1.083 1.00 47.71 N ANISOU 2816 N SER A 417 6339 5998 5789 458 -165 -773 N ATOM 2817 CA SER A 417 -40.784 37.441 1.884 1.00 49.05 C ANISOU 2817 CA SER A 417 6453 6183 6002 446 -161 -864 C ATOM 2818 C SER A 417 -42.143 37.384 1.201 1.00 49.23 C ANISOU 2818 C SER A 417 6497 6162 6046 430 -150 -817 C ATOM 2819 O SER A 417 -42.234 37.531 -0.019 1.00 53.47 O ANISOU 2819 O SER A 417 7049 6625 6641 425 -150 -734 O ATOM 2820 CB SER A 417 -40.369 38.904 2.100 1.00 47.44 C ANISOU 2820 CB SER A 417 6148 5931 5946 445 -172 -953 C ATOM 2821 OG SER A 417 -39.920 39.485 0.890 1.00 45.62 O ANISOU 2821 OG SER A 417 5905 5605 5824 443 -178 -883 O ATOM 2822 N ALA A 418 -43.196 37.194 1.991 1.00 47.10 N ANISOU 2822 N ALA A 418 6224 5945 5729 419 -140 -870 N ATOM 2823 CA ALA A 418 -44.547 37.009 1.473 1.00 43.08 C ANISOU 2823 CA ALA A 418 5739 5407 5224 404 -128 -832 C ATOM 2824 C ALA A 418 -45.281 38.331 1.263 1.00 43.09 C ANISOU 2824 C ALA A 418 5658 5335 5380 395 -133 -888 C ATOM 2825 O ALA A 418 -45.022 39.336 1.926 1.00 48.22 O ANISOU 2825 O ALA A 418 6224 5980 6119 396 -141 -991 O ATOM 2826 CB ALA A 418 -45.368 36.131 2.417 1.00 42.20 C ANISOU 2826 CB ALA A 418 5660 5388 4984 394 -114 -859 C ATOM 2827 N SER A 419 -46.242 38.294 0.347 1.00 40.12 N ANISOU 2827 N SER A 419 5304 4901 5038 385 -129 -821 N ATOM 2828 CA SER A 419 -47.130 39.416 0.068 1.00 40.59 C ANISOU 2828 CA SER A 419 5292 4885 5246 375 -138 -859 C ATOM 2829 C SER A 419 -48.543 38.860 -0.019 1.00 42.89 C ANISOU 2829 C SER A 419 5619 5193 5486 363 -124 -843 C ATOM 2830 O SER A 419 -48.844 38.067 -0.918 1.00 42.18 O ANISOU 2830 O SER A 419 5600 5090 5335 360 -118 -737 O ATOM 2831 CB SER A 419 -46.733 40.126 -1.223 1.00 43.04 C ANISOU 2831 CB SER A 419 5582 5090 5679 374 -157 -772 C ATOM 2832 OG SER A 419 -47.682 41.111 -1.600 1.00 49.99 O ANISOU 2832 OG SER A 419 6399 5890 6705 363 -171 -787 O ATOM 2833 N GLN A 420 -49.407 39.266 0.906 1.00 44.66 N ANISOU 2833 N GLN A 420 5787 5448 5732 354 -118 -954 N ATOM 2834 CA GLN A 420 -50.756 38.724 0.999 1.00 42.84 C ANISOU 2834 CA GLN A 420 5584 5246 5445 340 -101 -955 C ATOM 2835 C GLN A 420 -51.757 39.653 0.323 1.00 41.11 C ANISOU 2835 C GLN A 420 5310 4932 5379 334 -115 -959 C ATOM 2836 O GLN A 420 -51.674 40.879 0.455 1.00 39.74 O ANISOU 2836 O GLN A 420 5043 4698 5359 336 -133 -1032 O ATOM 2837 CB GLN A 420 -51.169 38.507 2.461 1.00 38.31 C ANISOU 2837 CB GLN A 420 4984 4784 4789 328 -83 -1075 C ATOM 2838 CG GLN A 420 -50.205 37.682 3.303 1.00 41.98 C ANISOU 2838 CG GLN A 420 5489 5352 5108 332 -76 -1078 C ATOM 2839 CD GLN A 420 -50.799 37.323 4.667 1.00 42.57 C ANISOU 2839 CD GLN A 420 5545 5553 5078 311 -58 -1175 C ATOM 2840 NE2 GLN A 420 -50.017 36.655 5.506 1.00 41.76 N ANISOU 2840 NE2 GLN A 420 5468 5550 4850 310 -56 -1180 N ATOM 2841 OE1 GLN A 420 -51.949 37.651 4.955 1.00 40.58 O ANISOU 2841 OE1 GLN A 420 5251 5311 4857 294 -46 -1244 O ATOM 2842 N SER A 421 -52.710 39.054 -0.390 1.00 39.59 N ANISOU 2842 N SER A 421 5171 4724 5147 326 -107 -883 N ATOM 2843 CA SER A 421 -53.847 39.785 -0.929 1.00 41.38 C ANISOU 2843 CA SER A 421 5348 4873 5500 319 -120 -890 C ATOM 2844 C SER A 421 -55.045 38.847 -1.037 1.00 42.41 C ANISOU 2844 C SER A 421 5538 5044 5531 307 -99 -861 C ATOM 2845 O SER A 421 -54.938 37.631 -0.845 1.00 43.36 O ANISOU 2845 O SER A 421 5740 5239 5495 304 -76 -820 O ATOM 2846 CB SER A 421 -53.512 40.425 -2.284 1.00 41.90 C ANISOU 2846 CB SER A 421 5402 4830 5686 322 -149 -782 C ATOM 2847 OG SER A 421 -52.975 39.487 -3.190 1.00 41.23 O ANISOU 2847 OG SER A 421 5408 4761 5497 323 -142 -654 O ATOM 2848 N SER A 422 -56.199 39.437 -1.336 1.00 41.79 N ANISOU 2848 N SER A 422 5413 4911 5556 300 -108 -885 N ATOM 2849 CA SER A 422 -57.424 38.673 -1.518 1.00 40.94 C ANISOU 2849 CA SER A 422 5351 4829 5375 288 -90 -862 C ATOM 2850 C SER A 422 -57.322 37.782 -2.758 1.00 42.03 C ANISOU 2850 C SER A 422 5580 4950 5439 290 -90 -711 C ATOM 2851 O SER A 422 -56.440 37.948 -3.609 1.00 42.14 O ANISOU 2851 O SER A 422 5608 4919 5483 297 -107 -625 O ATOM 2852 CB SER A 422 -58.616 39.618 -1.638 1.00 40.74 C ANISOU 2852 CB SER A 422 5245 4738 5497 283 -107 -923 C ATOM 2853 OG SER A 422 -58.415 40.537 -2.706 1.00 42.20 O ANISOU 2853 OG SER A 422 5390 4809 5835 290 -145 -852 O ATOM 2854 N TRP A 423 -58.239 36.814 -2.849 1.00 41.27 N ANISOU 2854 N TRP A 423 5542 4895 5244 279 -68 -685 N ATOM 2855 CA TRP A 423 -58.162 35.848 -3.938 1.00 41.31 C ANISOU 2855 CA TRP A 423 5631 4897 5168 280 -64 -559 C ATOM 2856 C TRP A 423 -58.327 36.524 -5.296 1.00 42.84 C ANISOU 2856 C TRP A 423 5803 5003 5473 281 -93 -474 C ATOM 2857 O TRP A 423 -57.662 36.150 -6.267 1.00 42.15 O ANISOU 2857 O TRP A 423 5758 4905 5351 283 -99 -372 O ATOM 2858 CB TRP A 423 -59.203 34.746 -3.757 1.00 40.54 C ANISOU 2858 CB TRP A 423 5590 4854 4961 268 -36 -555 C ATOM 2859 CG TRP A 423 -59.096 33.720 -4.835 1.00 41.78 C ANISOU 2859 CG TRP A 423 5826 5010 5038 269 -31 -440 C ATOM 2860 CD1 TRP A 423 -58.290 32.617 -4.842 1.00 42.55 C ANISOU 2860 CD1 TRP A 423 5994 5154 5020 274 -17 -390 C ATOM 2861 CD2 TRP A 423 -59.791 33.715 -6.082 1.00 41.94 C ANISOU 2861 CD2 TRP A 423 5857 4983 5095 265 -41 -365 C ATOM 2862 CE2 TRP A 423 -59.368 32.578 -6.793 1.00 37.65 C ANISOU 2862 CE2 TRP A 423 5389 4467 4450 267 -30 -280 C ATOM 2863 CE3 TRP A 423 -60.736 34.562 -6.666 1.00 45.37 C ANISOU 2863 CE3 TRP A 423 6240 5357 5643 260 -62 -363 C ATOM 2864 NE1 TRP A 423 -58.452 31.922 -6.014 1.00 41.98 N ANISOU 2864 NE1 TRP A 423 5972 5067 4912 273 -16 -298 N ATOM 2865 CZ2 TRP A 423 -59.861 32.262 -8.043 1.00 36.06 C ANISOU 2865 CZ2 TRP A 423 5211 4244 4245 261 -35 -200 C ATOM 2866 CZ3 TRP A 423 -61.222 34.245 -7.920 1.00 42.84 C ANISOU 2866 CZ3 TRP A 423 5947 5014 5316 255 -70 -271 C ATOM 2867 CH2 TRP A 423 -60.784 33.103 -8.590 1.00 42.17 C ANISOU 2867 CH2 TRP A 423 5937 4968 5120 255 -55 -194 C ATOM 2868 N ASN A 424 -59.206 37.524 -5.386 1.00 44.11 N ANISOU 2868 N ASN A 424 5891 5102 5768 277 -114 -514 N ATOM 2869 CA ASN A 424 -59.387 38.209 -6.658 1.00 42.80 C ANISOU 2869 CA ASN A 424 5697 4853 5713 275 -148 -422 C ATOM 2870 C ASN A 424 -58.149 39.007 -7.024 1.00 45.12 C ANISOU 2870 C ASN A 424 5955 5099 6089 280 -174 -381 C ATOM 2871 O ASN A 424 -57.722 39.018 -8.184 1.00 43.82 O ANISOU 2871 O ASN A 424 5809 4908 5931 274 -190 -265 O ATOM 2872 CB ASN A 424 -60.604 39.120 -6.597 1.00 44.50 C ANISOU 2872 CB ASN A 424 5835 5007 6068 271 -170 -477 C ATOM 2873 CG ASN A 424 -61.846 38.453 -7.151 1.00 48.09 C ANISOU 2873 CG ASN A 424 6328 5473 6470 262 -162 -439 C ATOM 2874 ND2 ASN A 424 -62.320 38.926 -8.322 1.00 45.38 N ANISOU 2874 ND2 ASN A 424 5963 5065 6215 257 -196 -349 N ATOM 2875 OD1 ASN A 424 -62.361 37.498 -6.551 1.00 42.27 O ANISOU 2875 OD1 ASN A 424 5640 4808 5614 258 -126 -484 O ATOM 2876 N GLU A 425 -57.558 39.672 -6.040 1.00 50.14 N ANISOU 2876 N GLU A 425 6536 5731 6784 288 -176 -477 N ATOM 2877 CA GLU A 425 -56.384 40.491 -6.289 1.00 49.77 C ANISOU 2877 CA GLU A 425 6447 5636 6828 292 -200 -450 C ATOM 2878 C GLU A 425 -55.174 39.627 -6.637 1.00 48.82 C ANISOU 2878 C GLU A 425 6402 5570 6577 295 -183 -375 C ATOM 2879 O GLU A 425 -54.410 39.964 -7.546 1.00 48.21 O ANISOU 2879 O GLU A 425 6320 5456 6540 290 -202 -284 O ATOM 2880 CB GLU A 425 -56.133 41.349 -5.055 1.00 48.56 C ANISOU 2880 CB GLU A 425 6212 5473 6765 300 -204 -591 C ATOM 2881 CG GLU A 425 -55.385 42.611 -5.286 1.00 54.95 C ANISOU 2881 CG GLU A 425 6940 6197 7743 302 -239 -587 C ATOM 2882 CD GLU A 425 -55.190 43.346 -3.986 1.00 60.46 C ANISOU 2882 CD GLU A 425 7554 6897 8519 310 -238 -746 C ATOM 2883 OE1 GLU A 425 -54.424 44.336 -3.955 1.00 67.73 O ANISOU 2883 OE1 GLU A 425 8404 7756 9574 314 -263 -766 O ATOM 2884 OE2 GLU A 425 -55.807 42.904 -2.989 1.00 51.76 O1- ANISOU 2884 OE2 GLU A 425 6457 5869 7342 311 -211 -853 O1- ATOM 2885 N TRP A 426 -55.011 38.494 -5.944 1.00 44.08 N ANISOU 2885 N TRP A 426 5870 5057 5823 300 -149 -410 N ATOM 2886 CA TRP A 426 -53.894 37.576 -6.172 1.00 41.73 C ANISOU 2886 CA TRP A 426 5641 4811 5404 306 -134 -353 C ATOM 2887 C TRP A 426 -54.060 36.788 -7.464 1.00 42.66 C ANISOU 2887 C TRP A 426 5822 4935 5453 298 -130 -234 C ATOM 2888 O TRP A 426 -53.065 36.422 -8.108 1.00 40.56 O ANISOU 2888 O TRP A 426 5587 4683 5141 298 -129 -166 O ATOM 2889 CB TRP A 426 -53.784 36.627 -4.982 1.00 38.75 C ANISOU 2889 CB TRP A 426 5307 4519 4896 313 -105 -424 C ATOM 2890 CG TRP A 426 -53.018 35.346 -5.189 1.00 37.95 C ANISOU 2890 CG TRP A 426 5291 4475 4655 319 -88 -364 C ATOM 2891 CD1 TRP A 426 -51.680 35.142 -4.983 1.00 39.51 C ANISOU 2891 CD1 TRP A 426 5502 4696 4815 330 -89 -358 C ATOM 2892 CD2 TRP A 426 -53.556 34.071 -5.592 1.00 36.19 C ANISOU 2892 CD2 TRP A 426 5143 4290 4319 315 -69 -310 C ATOM 2893 CE2 TRP A 426 -52.487 33.155 -5.626 1.00 33.74 C ANISOU 2893 CE2 TRP A 426 4885 4018 3915 325 -62 -274 C ATOM 2894 CE3 TRP A 426 -54.836 33.621 -5.924 1.00 35.58 C ANISOU 2894 CE3 TRP A 426 5088 4212 4217 304 -59 -292 C ATOM 2895 NE1 TRP A 426 -51.353 33.827 -5.255 1.00 38.65 N ANISOU 2895 NE1 TRP A 426 5470 4633 4582 334 -74 -303 N ATOM 2896 CZ2 TRP A 426 -52.660 31.834 -5.976 1.00 32.16 C ANISOU 2896 CZ2 TRP A 426 4756 3853 3610 324 -46 -224 C ATOM 2897 CZ3 TRP A 426 -55.003 32.310 -6.266 1.00 30.97 C ANISOU 2897 CZ3 TRP A 426 4577 3667 3523 303 -41 -242 C ATOM 2898 CH2 TRP A 426 -53.928 31.429 -6.289 1.00 31.74 C ANISOU 2898 CH2 TRP A 426 4723 3798 3538 313 -35 -209 C ATOM 2899 N THR A 427 -55.302 36.508 -7.850 1.00 42.42 N ANISOU 2899 N THR A 427 5805 4899 5413 289 -127 -215 N ATOM 2900 CA THR A 427 -55.557 35.973 -9.181 1.00 40.74 C ANISOU 2900 CA THR A 427 5633 4687 5158 278 -129 -106 C ATOM 2901 C THR A 427 -55.237 37.008 -10.266 1.00 42.05 C ANISOU 2901 C THR A 427 5748 4793 5438 266 -163 -23 C ATOM 2902 O THR A 427 -54.667 36.663 -11.310 1.00 40.38 O ANISOU 2902 O THR A 427 5563 4601 5180 256 -164 68 O ATOM 2903 CB THR A 427 -57.009 35.498 -9.261 1.00 41.48 C ANISOU 2903 CB THR A 427 5747 4790 5224 272 -119 -115 C ATOM 2904 CG2 THR A 427 -57.394 35.070 -10.678 1.00 33.52 C ANISOU 2904 CG2 THR A 427 4768 3784 4184 259 -125 -9 C ATOM 2905 OG1 THR A 427 -57.200 34.411 -8.341 1.00 40.53 O ANISOU 2905 OG1 THR A 427 5680 4733 4985 278 -87 -172 O ATOM 2906 N ASP A 428 -55.560 38.290 -10.023 1.00 43.10 N ANISOU 2906 N ASP A 428 5799 4854 5722 264 -192 -56 N ATOM 2907 CA ASP A 428 -55.213 39.332 -10.991 1.00 44.78 C ANISOU 2907 CA ASP A 428 5956 5003 6057 249 -230 32 C ATOM 2908 C ASP A 428 -53.706 39.532 -11.085 1.00 43.11 C ANISOU 2908 C ASP A 428 5740 4798 5842 249 -230 58 C ATOM 2909 O ASP A 428 -53.182 39.807 -12.172 1.00 39.83 O ANISOU 2909 O ASP A 428 5315 4374 5447 230 -247 164 O ATOM 2910 CB ASP A 428 -55.881 40.668 -10.645 1.00 43.68 C ANISOU 2910 CB ASP A 428 5722 4773 6102 249 -265 -14 C ATOM 2911 CG ASP A 428 -55.574 41.755 -11.687 1.00 41.83 C ANISOU 2911 CG ASP A 428 5425 4464 6005 230 -311 94 C ATOM 2912 OD1 ASP A 428 -56.072 41.632 -12.837 1.00 44.91 O ANISOU 2912 OD1 ASP A 428 5827 4856 6382 211 -327 205 O ATOM 2913 OD2 ASP A 428 -54.811 42.701 -11.377 1.00 36.16 O1- ANISOU 2913 OD2 ASP A 428 4644 3691 5403 231 -331 73 O1- ATOM 2914 N LYS A 429 -53.002 39.440 -9.952 1.00 44.13 N ANISOU 2914 N LYS A 429 5870 4949 5948 267 -213 -38 N ATOM 2915 CA LYS A 429 -51.548 39.543 -9.978 1.00 44.86 C ANISOU 2915 CA LYS A 429 5961 5053 6029 269 -211 -21 C ATOM 2916 C LYS A 429 -50.968 38.487 -10.907 1.00 44.97 C ANISOU 2916 C LYS A 429 6047 5131 5909 261 -193 66 C ATOM 2917 O LYS A 429 -50.128 38.782 -11.767 1.00 43.86 O ANISOU 2917 O LYS A 429 5892 4986 5786 246 -204 145 O ATOM 2918 CB LYS A 429 -50.966 39.381 -8.567 1.00 43.94 C ANISOU 2918 CB LYS A 429 5846 4969 5880 291 -193 -141 C ATOM 2919 CG LYS A 429 -51.423 40.378 -7.475 1.00 41.43 C ANISOU 2919 CG LYS A 429 5450 4607 5685 299 -206 -258 C ATOM 2920 CD LYS A 429 -51.106 41.839 -7.795 1.00 42.15 C ANISOU 2920 CD LYS A 429 5448 4604 5965 291 -243 -244 C ATOM 2921 CE LYS A 429 -49.679 42.026 -8.263 1.00 42.90 C ANISOU 2921 CE LYS A 429 5541 4696 6064 286 -248 -185 C ATOM 2922 NZ LYS A 429 -48.721 41.285 -7.375 1.00 46.45 N1+ ANISOU 2922 NZ LYS A 429 6033 5220 6395 305 -220 -254 N1+ ATOM 2923 N LYS A 430 -51.410 37.242 -10.735 1.00 41.12 N ANISOU 2923 N LYS A 430 5629 4704 5288 270 -165 50 N ATOM 2924 CA LYS A 430 -50.992 36.158 -11.613 1.00 42.14 C ANISOU 2924 CA LYS A 430 5821 4893 5297 264 -147 118 C ATOM 2925 C LYS A 430 -51.349 36.460 -13.070 1.00 43.87 C ANISOU 2925 C LYS A 430 6024 5104 5543 236 -164 229 C ATOM 2926 O LYS A 430 -50.490 36.421 -13.960 1.00 40.48 O ANISOU 2926 O LYS A 430 5593 4700 5089 220 -166 299 O ATOM 2927 CB LYS A 430 -51.652 34.849 -11.153 1.00 39.56 C ANISOU 2927 CB LYS A 430 5562 4618 4850 276 -120 79 C ATOM 2928 CG LYS A 430 -51.208 34.324 -9.773 1.00 35.88 C ANISOU 2928 CG LYS A 430 5122 4183 4329 298 -103 -12 C ATOM 2929 CD LYS A 430 -51.801 32.941 -9.498 1.00 30.58 C ANISOU 2929 CD LYS A 430 4518 3561 3538 305 -78 -25 C ATOM 2930 CE LYS A 430 -53.319 32.942 -9.516 1.00 28.59 C ANISOU 2930 CE LYS A 430 4266 3297 3301 296 -76 -34 C ATOM 2931 NZ LYS A 430 -53.875 31.577 -9.360 1.00 28.22 N1+ ANISOU 2931 NZ LYS A 430 4284 3295 3143 298 -52 -37 N1+ ATOM 2932 N SER A 431 -52.628 36.776 -13.320 1.00 43.91 N ANISOU 2932 N SER A 431 6010 5077 5596 227 -178 245 N ATOM 2933 CA SER A 431 -53.139 36.893 -14.686 1.00 39.66 C ANISOU 2933 CA SER A 431 5461 4544 5062 200 -195 352 C ATOM 2934 C SER A 431 -52.357 37.914 -15.502 1.00 39.50 C ANISOU 2934 C SER A 431 5383 4496 5127 175 -224 441 C ATOM 2935 O SER A 431 -52.106 37.707 -16.695 1.00 40.02 O ANISOU 2935 O SER A 431 5454 4609 5143 148 -227 536 O ATOM 2936 CB SER A 431 -54.622 37.265 -14.650 1.00 38.34 C ANISOU 2936 CB SER A 431 5272 4335 4961 198 -212 345 C ATOM 2937 OG SER A 431 -55.131 37.466 -15.950 1.00 39.63 O ANISOU 2937 OG SER A 431 5418 4503 5135 171 -234 453 O ATOM 2938 N LYS A 432 -51.956 39.016 -14.879 1.00 40.27 N ANISOU 2938 N LYS A 432 5422 4524 5354 180 -246 409 N ATOM 2939 CA LYS A 432 -51.274 40.096 -15.571 1.00 41.28 C ANISOU 2939 CA LYS A 432 5486 4611 5586 154 -278 496 C ATOM 2940 C LYS A 432 -49.761 40.083 -15.345 1.00 39.16 C ANISOU 2940 C LYS A 432 5220 4366 5294 156 -263 479 C ATOM 2941 O LYS A 432 -49.082 41.057 -15.677 1.00 38.06 O ANISOU 2941 O LYS A 432 5022 4185 5255 137 -288 533 O ATOM 2942 CB LYS A 432 -51.893 41.436 -15.153 1.00 41.35 C ANISOU 2942 CB LYS A 432 5414 4514 5784 155 -319 479 C ATOM 2943 CG LYS A 432 -53.153 41.777 -15.956 1.00 40.87 C ANISOU 2943 CG LYS A 432 5327 4422 5779 136 -351 557 C ATOM 2944 CD LYS A 432 -54.192 42.509 -15.128 1.00 43.22 C ANISOU 2944 CD LYS A 432 5574 4633 6216 154 -374 477 C ATOM 2945 CE LYS A 432 -55.266 43.181 -16.005 1.00 42.38 C ANISOU 2945 CE LYS A 432 5417 4473 6213 132 -421 572 C ATOM 2946 NZ LYS A 432 -54.871 44.564 -16.470 1.00 42.73 N1+ ANISOU 2946 NZ LYS A 432 5369 4427 6439 109 -475 658 N1+ ATOM 2947 N GLY A 433 -49.220 38.999 -14.804 1.00 39.00 N ANISOU 2947 N GLY A 433 5262 4408 5147 179 -226 411 N ATOM 2948 CA GLY A 433 -47.781 38.831 -14.748 1.00 39.86 C ANISOU 2948 CA GLY A 433 5377 4550 5217 180 -212 404 C ATOM 2949 C GLY A 433 -47.036 39.813 -13.878 1.00 39.14 C ANISOU 2949 C GLY A 433 5233 4399 5242 192 -226 346 C ATOM 2950 O GLY A 433 -45.814 39.887 -13.969 1.00 39.98 O ANISOU 2950 O GLY A 433 5330 4523 5337 188 -220 354 O ATOM 2951 N THR A 434 -47.728 40.575 -13.032 1.00 39.84 N ANISOU 2951 N THR A 434 5278 4418 5442 206 -244 280 N ATOM 2952 CA THR A 434 -47.065 41.566 -12.184 1.00 35.95 C ANISOU 2952 CA THR A 434 4722 3866 5071 216 -258 212 C ATOM 2953 C THR A 434 -46.675 40.933 -10.850 1.00 41.78 C ANISOU 2953 C THR A 434 5495 4645 5735 251 -232 85 C ATOM 2954 O THR A 434 -47.139 41.305 -9.766 1.00 39.24 O ANISOU 2954 O THR A 434 5144 4297 5470 269 -235 -18 O ATOM 2955 CB THR A 434 -47.956 42.781 -11.976 1.00 37.17 C ANISOU 2955 CB THR A 434 4797 3923 5401 212 -294 198 C ATOM 2956 CG2 THR A 434 -48.219 43.465 -13.309 1.00 42.13 C ANISOU 2956 CG2 THR A 434 5386 4511 6112 174 -328 341 C ATOM 2957 OG1 THR A 434 -49.200 42.371 -11.405 1.00 38.59 O ANISOU 2957 OG1 THR A 434 5000 4110 5553 228 -286 132 O ATOM 2958 N TYR A 435 -45.798 39.943 -10.955 1.00 41.03 N ANISOU 2958 N TYR A 435 5459 4622 5509 257 -207 92 N ATOM 2959 CA TYR A 435 -45.408 39.202 -9.771 1.00 37.94 C ANISOU 2959 CA TYR A 435 5107 4279 5032 288 -185 -10 C ATOM 2960 C TYR A 435 -44.083 38.504 -10.024 1.00 38.00 C ANISOU 2960 C TYR A 435 5151 4341 4949 292 -170 10 C ATOM 2961 O TYR A 435 -43.747 38.161 -11.168 1.00 37.92 O ANISOU 2961 O TYR A 435 5159 4355 4894 272 -165 97 O ATOM 2962 CB TYR A 435 -46.478 38.181 -9.385 1.00 36.72 C ANISOU 2962 CB TYR A 435 5012 4166 4775 299 -167 -40 C ATOM 2963 CG TYR A 435 -46.495 36.947 -10.247 1.00 36.64 C ANISOU 2963 CG TYR A 435 5073 4213 4635 294 -148 28 C ATOM 2964 CD1 TYR A 435 -47.117 36.944 -11.483 1.00 34.56 C ANISOU 2964 CD1 TYR A 435 4813 3945 4374 270 -153 121 C ATOM 2965 CD2 TYR A 435 -45.885 35.772 -9.812 1.00 35.86 C ANISOU 2965 CD2 TYR A 435 5033 4176 4416 313 -127 -3 C ATOM 2966 CE1 TYR A 435 -47.141 35.799 -12.269 1.00 36.49 C ANISOU 2966 CE1 TYR A 435 5115 4248 4500 264 -134 170 C ATOM 2967 CE2 TYR A 435 -45.901 34.626 -10.584 1.00 35.43 C ANISOU 2967 CE2 TYR A 435 5036 4169 4257 309 -111 48 C ATOM 2968 CZ TYR A 435 -46.531 34.640 -11.811 1.00 37.53 C ANISOU 2968 CZ TYR A 435 5302 4434 4524 285 -113 129 C ATOM 2969 OH TYR A 435 -46.540 33.491 -12.568 1.00 32.05 O ANISOU 2969 OH TYR A 435 4657 3792 3728 281 -96 165 O ATOM 2970 N GLN A 436 -43.336 38.310 -8.935 1.00 35.11 N ANISOU 2970 N GLN A 436 4788 3997 4555 316 -163 -77 N ATOM 2971 CA GLN A 436 -42.138 37.483 -8.964 1.00 37.24 C ANISOU 2971 CA GLN A 436 5097 4322 4732 328 -149 -77 C ATOM 2972 C GLN A 436 -42.530 36.024 -8.802 1.00 36.97 C ANISOU 2972 C GLN A 436 5141 4347 4559 342 -130 -81 C ATOM 2973 O GLN A 436 -42.552 35.268 -9.777 1.00 36.37 O ANISOU 2973 O GLN A 436 5104 4300 4416 332 -119 -16 O ATOM 2974 CB GLN A 436 -41.155 37.927 -7.882 1.00 34.31 C ANISOU 2974 CB GLN A 436 4691 3950 4397 347 -155 -163 C ATOM 2975 CG GLN A 436 -40.537 39.286 -8.217 1.00 37.44 C ANISOU 2975 CG GLN A 436 5008 4283 4933 330 -173 -148 C ATOM 2976 CD GLN A 436 -39.530 39.771 -7.209 1.00 38.41 C ANISOU 2976 CD GLN A 436 5089 4405 5099 348 -179 -238 C ATOM 2977 NE2 GLN A 436 -38.652 40.670 -7.641 1.00 39.01 N ANISOU 2977 NE2 GLN A 436 5109 4440 5273 333 -190 -214 N ATOM 2978 OE1 GLN A 436 -39.530 39.343 -6.056 1.00 39.46 O ANISOU 2978 OE1 GLN A 436 5239 4578 5178 373 -174 -326 O ATOM 2979 N LEU A 437 -42.865 35.637 -7.576 1.00 38.17 N ANISOU 2979 N LEU A 437 5311 4521 4670 363 -126 -159 N ATOM 2980 CA LEU A 437 -43.288 34.293 -7.254 1.00 33.94 C ANISOU 2980 CA LEU A 437 4844 4036 4015 376 -112 -164 C ATOM 2981 C LEU A 437 -44.718 34.342 -6.753 1.00 35.52 C ANISOU 2981 C LEU A 437 5047 4229 4218 371 -109 -192 C ATOM 2982 O LEU A 437 -45.187 35.371 -6.250 1.00 37.42 O ANISOU 2982 O LEU A 437 5234 4437 4548 367 -119 -240 O ATOM 2983 CB LEU A 437 -42.372 33.663 -6.192 1.00 35.45 C ANISOU 2983 CB LEU A 437 5056 4273 4141 400 -113 -222 C ATOM 2984 CG LEU A 437 -40.897 33.771 -6.570 1.00 35.64 C ANISOU 2984 CG LEU A 437 5065 4300 4178 406 -118 -210 C ATOM 2985 CD1 LEU A 437 -40.005 33.210 -5.496 1.00 33.34 C ANISOU 2985 CD1 LEU A 437 4787 4051 3829 431 -124 -266 C ATOM 2986 CD2 LEU A 437 -40.677 33.040 -7.892 1.00 32.20 C ANISOU 2986 CD2 LEU A 437 4663 3875 3697 395 -108 -133 C ATOM 2987 N ALA A 438 -45.402 33.211 -6.898 1.00 30.77 N ANISOU 2987 N ALA A 438 4505 3659 3526 372 -96 -167 N ATOM 2988 CA ALA A 438 -46.717 33.036 -6.308 1.00 34.23 C ANISOU 2988 CA ALA A 438 4955 4104 3947 369 -89 -198 C ATOM 2989 C ALA A 438 -46.879 31.567 -5.959 1.00 33.37 C ANISOU 2989 C ALA A 438 4915 4047 3718 377 -76 -191 C ATOM 2990 O ALA A 438 -46.588 30.692 -6.787 1.00 35.01 O ANISOU 2990 O ALA A 438 5164 4264 3876 379 -70 -135 O ATOM 2991 CB ALA A 438 -47.825 33.510 -7.250 1.00 34.36 C ANISOU 2991 CB ALA A 438 4956 4079 4019 349 -90 -152 C ATOM 2992 N ILE A 439 -47.303 31.296 -4.727 1.00 30.77 N ANISOU 2992 N ILE A 439 4593 3753 3347 381 -73 -248 N ATOM 2993 CA ILE A 439 -47.512 29.921 -4.284 1.00 33.11 C ANISOU 2993 CA ILE A 439 4949 4095 3536 385 -64 -234 C ATOM 2994 C ILE A 439 -48.881 29.477 -4.772 1.00 31.60 C ANISOU 2994 C ILE A 439 4784 3894 3327 371 -50 -205 C ATOM 2995 O ILE A 439 -49.897 30.129 -4.512 1.00 32.17 O ANISOU 2995 O ILE A 439 4828 3956 3439 358 -46 -238 O ATOM 2996 CB ILE A 439 -47.370 29.773 -2.752 1.00 35.05 C ANISOU 2996 CB ILE A 439 5188 4396 3732 389 -68 -297 C ATOM 2997 CG1 ILE A 439 -47.438 28.295 -2.342 1.00 32.52 C ANISOU 2997 CG1 ILE A 439 4929 4118 3307 391 -66 -263 C ATOM 2998 CG2 ILE A 439 -48.413 30.582 -1.982 1.00 33.29 C ANISOU 2998 CG2 ILE A 439 4922 4185 3543 374 -62 -365 C ATOM 2999 CD1 ILE A 439 -47.047 28.042 -0.906 1.00 33.84 C ANISOU 2999 CD1 ILE A 439 5092 4353 3414 393 -76 -304 C ATOM 3000 N ASP A 440 -48.907 28.389 -5.521 1.00 30.19 N ANISOU 3000 N ASP A 440 4655 3718 3097 372 -43 -148 N ATOM 3001 CA ASP A 440 -50.169 27.883 -6.028 1.00 30.94 C ANISOU 3001 CA ASP A 440 4778 3807 3173 359 -30 -121 C ATOM 3002 C ASP A 440 -49.963 26.434 -6.399 1.00 29.25 C ANISOU 3002 C ASP A 440 4618 3607 2889 365 -24 -79 C ATOM 3003 O ASP A 440 -48.888 25.870 -6.192 1.00 33.25 O ANISOU 3003 O ASP A 440 5139 4127 3367 380 -33 -74 O ATOM 3004 CB ASP A 440 -50.680 28.714 -7.211 1.00 28.75 C ANISOU 3004 CB ASP A 440 4470 3488 2965 347 -30 -91 C ATOM 3005 CG ASP A 440 -52.154 28.487 -7.478 1.00 28.98 C ANISOU 3005 CG ASP A 440 4512 3510 2988 332 -19 -82 C ATOM 3006 OD1 ASP A 440 -52.751 27.620 -6.796 1.00 33.56 O ANISOU 3006 OD1 ASP A 440 5127 4119 3507 330 -7 -98 O ATOM 3007 OD2 ASP A 440 -52.722 29.164 -8.354 1.00 29.68 O1- ANISOU 3007 OD2 ASP A 440 4574 3568 3134 321 -23 -56 O1- ATOM 3008 N SER A 441 -51.014 25.831 -6.918 1.00 27.46 N ANISOU 3008 N SER A 441 4417 3376 2642 354 -12 -55 N ATOM 3009 CA SER A 441 -51.017 24.443 -7.318 1.00 30.19 C ANISOU 3009 CA SER A 441 4808 3729 2935 358 -6 -22 C ATOM 3010 C SER A 441 -51.378 24.365 -8.792 1.00 29.38 C ANISOU 3010 C SER A 441 4705 3610 2850 350 3 13 C ATOM 3011 O SER A 441 -52.075 25.235 -9.323 1.00 27.12 O ANISOU 3011 O SER A 441 4392 3309 2603 337 5 19 O ATOM 3012 CB SER A 441 -52.011 23.647 -6.479 1.00 31.33 C ANISOU 3012 CB SER A 441 4983 3890 3031 348 3 -27 C ATOM 3013 OG SER A 441 -53.061 24.492 -6.056 1.00 33.15 O ANISOU 3013 OG SER A 441 5189 4123 3283 332 11 -59 O ATOM 3014 N LEU A 442 -50.872 23.328 -9.456 1.00 32.05 N ANISOU 3014 N LEU A 442 5065 3953 3159 358 5 34 N ATOM 3015 CA LEU A 442 -51.189 23.035 -10.855 1.00 29.23 C ANISOU 3015 CA LEU A 442 4706 3598 2803 348 14 60 C ATOM 3016 C LEU A 442 -52.035 21.763 -10.872 1.00 29.22 C ANISOU 3016 C LEU A 442 4741 3597 2765 346 25 63 C ATOM 3017 O LEU A 442 -51.588 20.715 -10.384 1.00 31.57 O ANISOU 3017 O LEU A 442 5064 3893 3040 359 21 59 O ATOM 3018 CB LEU A 442 -49.910 22.866 -11.677 1.00 26.98 C ANISOU 3018 CB LEU A 442 4406 3326 2519 356 10 68 C ATOM 3019 CG LEU A 442 -49.107 24.103 -12.093 1.00 29.47 C ANISOU 3019 CG LEU A 442 4679 3644 2873 351 2 78 C ATOM 3020 CD1 LEU A 442 -48.360 24.718 -10.946 1.00 28.55 C ANISOU 3020 CD1 LEU A 442 4554 3517 2779 365 -11 52 C ATOM 3021 CD2 LEU A 442 -48.111 23.751 -13.169 1.00 31.55 C ANISOU 3021 CD2 LEU A 442 4928 3935 3126 350 5 88 C ATOM 3022 N GLY A 443 -53.259 21.861 -11.395 1.00 26.78 N ANISOU 3022 N GLY A 443 4431 3286 2458 329 37 72 N ATOM 3023 CA GLY A 443 -54.207 20.767 -11.359 1.00 26.73 C ANISOU 3023 CA GLY A 443 4455 3277 2425 324 49 71 C ATOM 3024 C GLY A 443 -54.071 19.798 -12.515 1.00 28.32 C ANISOU 3024 C GLY A 443 4659 3486 2614 325 56 77 C ATOM 3025 O GLY A 443 -53.138 19.852 -13.315 1.00 29.67 O ANISOU 3025 O GLY A 443 4810 3674 2789 330 53 78 O ATOM 3026 N GLN A 444 -55.054 18.903 -12.614 1.00 34.95 N ANISOU 3026 N GLN A 444 5519 4320 3440 318 68 74 N ATOM 3027 CA GLN A 444 -54.955 17.754 -13.510 1.00 31.06 C ANISOU 3027 CA GLN A 444 5028 3832 2940 320 75 65 C ATOM 3028 C GLN A 444 -55.884 17.786 -14.709 1.00 33.18 C ANISOU 3028 C GLN A 444 5281 4124 3204 303 89 64 C ATOM 3029 O GLN A 444 -55.531 17.249 -15.757 1.00 36.75 O ANISOU 3029 O GLN A 444 5713 4600 3649 302 94 50 O ATOM 3030 CB GLN A 444 -55.217 16.461 -12.734 1.00 29.52 C ANISOU 3030 CB GLN A 444 4864 3608 2743 327 74 60 C ATOM 3031 CG GLN A 444 -53.950 15.885 -12.208 1.00 31.16 C ANISOU 3031 CG GLN A 444 5078 3802 2961 347 55 58 C ATOM 3032 CD GLN A 444 -52.918 15.752 -13.313 1.00 34.83 C ANISOU 3032 CD GLN A 444 5512 4284 3437 357 54 37 C ATOM 3033 NE2 GLN A 444 -51.710 16.278 -13.086 1.00 33.94 N ANISOU 3033 NE2 GLN A 444 5387 4179 3330 370 40 36 N ATOM 3034 OE1 GLN A 444 -53.214 15.198 -14.368 1.00 31.67 O ANISOU 3034 OE1 GLN A 444 5096 3897 3039 351 65 17 O ATOM 3035 N GLY A 445 -57.060 18.368 -14.611 1.00 30.29 N ANISOU 3035 N GLY A 445 4915 3755 2838 288 95 74 N ATOM 3036 CA GLY A 445 -57.992 18.296 -15.714 1.00 34.02 C ANISOU 3036 CA GLY A 445 5372 4250 3303 272 105 75 C ATOM 3037 C GLY A 445 -58.678 16.939 -15.771 1.00 31.87 C ANISOU 3037 C GLY A 445 5119 3966 3022 272 119 52 C ATOM 3038 O GLY A 445 -58.281 15.962 -15.133 1.00 32.14 O ANISOU 3038 O GLY A 445 5175 3974 3062 284 117 40 O ATOM 3039 N ALA A 446 -59.723 16.891 -16.593 1.00 31.33 N ANISOU 3039 N ALA A 446 5038 3918 2947 256 129 48 N ATOM 3040 CA ALA A 446 -60.792 15.906 -16.463 1.00 30.99 C ANISOU 3040 CA ALA A 446 5013 3857 2904 250 143 29 C ATOM 3041 C ALA A 446 -60.303 14.489 -16.173 1.00 31.75 C ANISOU 3041 C ALA A 446 5126 3927 3011 262 145 6 C ATOM 3042 O ALA A 446 -60.929 13.774 -15.387 1.00 35.35 O ANISOU 3042 O ALA A 446 5608 4347 3477 260 150 6 O ATOM 3043 CB ALA A 446 -61.654 15.925 -17.737 1.00 31.10 C ANISOU 3043 CB ALA A 446 5001 3910 2906 235 151 20 C ATOM 3044 N VAL A 447 -59.225 14.045 -16.822 1.00 30.75 N ANISOU 3044 N VAL A 447 4978 3815 2888 274 140 -13 N ATOM 3045 CA VAL A 447 -58.645 12.728 -16.572 1.00 31.34 C ANISOU 3045 CA VAL A 447 5060 3857 2992 288 136 -38 C ATOM 3046 C VAL A 447 -57.195 12.907 -16.155 1.00 33.20 C ANISOU 3046 C VAL A 447 5294 4086 3236 307 118 -31 C ATOM 3047 O VAL A 447 -56.556 13.928 -16.441 1.00 33.38 O ANISOU 3047 O VAL A 447 5301 4142 3240 307 114 -20 O ATOM 3048 CB VAL A 447 -58.705 11.781 -17.793 1.00 31.58 C ANISOU 3048 CB VAL A 447 5056 3910 3034 286 146 -89 C ATOM 3049 CG1 VAL A 447 -59.973 10.948 -17.795 1.00 30.50 C ANISOU 3049 CG1 VAL A 447 4928 3748 2913 276 159 -105 C ATOM 3050 CG2 VAL A 447 -58.576 12.576 -19.059 1.00 32.10 C ANISOU 3050 CG2 VAL A 447 5082 4050 3063 274 153 -98 C ATOM 3051 N SER A 448 -56.666 11.884 -15.491 1.00 31.59 N ANISOU 3051 N SER A 448 5102 3835 3064 322 106 -36 N ATOM 3052 CA SER A 448 -55.245 11.886 -15.159 1.00 32.99 C ANISOU 3052 CA SER A 448 5274 4005 3257 342 86 -36 C ATOM 3053 C SER A 448 -54.440 11.624 -16.437 1.00 34.83 C ANISOU 3053 C SER A 448 5461 4274 3499 348 90 -86 C ATOM 3054 O SER A 448 -54.283 10.485 -16.883 1.00 34.21 O ANISOU 3054 O SER A 448 5362 4178 3459 356 89 -130 O ATOM 3055 CB SER A 448 -54.938 10.853 -14.087 1.00 30.04 C ANISOU 3055 CB SER A 448 4922 3571 2921 356 66 -20 C ATOM 3056 OG SER A 448 -53.539 10.646 -14.050 1.00 33.20 O ANISOU 3056 OG SER A 448 5306 3963 3346 378 46 -33 O ATOM 3057 N ASP A 449 -53.916 12.675 -17.025 1.00 32.21 N ANISOU 3057 N ASP A 449 5108 3995 3134 342 95 -83 N ATOM 3058 CA ASP A 449 -53.083 12.527 -18.205 1.00 35.31 C ANISOU 3058 CA ASP A 449 5453 4439 3524 342 100 -129 C ATOM 3059 C ASP A 449 -52.228 13.779 -18.304 1.00 36.73 C ANISOU 3059 C ASP A 449 5621 4658 3677 338 96 -103 C ATOM 3060 O ASP A 449 -52.743 14.854 -18.639 1.00 38.34 O ANISOU 3060 O ASP A 449 5822 4897 3849 318 103 -68 O ATOM 3061 CB ASP A 449 -53.920 12.345 -19.479 1.00 33.95 C ANISOU 3061 CB ASP A 449 5249 4322 3328 320 121 -160 C ATOM 3062 CG ASP A 449 -53.065 12.349 -20.768 1.00 39.68 C ANISOU 3062 CG ASP A 449 5917 5127 4033 310 130 -208 C ATOM 3063 OD1 ASP A 449 -52.127 13.173 -20.897 1.00 35.85 O ANISOU 3063 OD1 ASP A 449 5417 4676 3528 308 126 -191 O ATOM 3064 OD2 ASP A 449 -53.340 11.523 -21.682 1.00 42.60 O1- ANISOU 3064 OD2 ASP A 449 6249 5531 4405 303 143 -269 O1- ATOM 3065 N PRO A 450 -50.925 13.661 -18.094 1.00 41.11 N ANISOU 3065 N PRO A 450 6163 5206 4250 355 83 -120 N ATOM 3066 CA PRO A 450 -50.041 14.839 -18.061 1.00 39.73 C ANISOU 3066 CA PRO A 450 5977 5061 4057 352 78 -94 C ATOM 3067 C PRO A 450 -50.284 15.867 -19.160 1.00 38.04 C ANISOU 3067 C PRO A 450 5732 4920 3802 322 93 -74 C ATOM 3068 O PRO A 450 -49.973 17.048 -18.961 1.00 38.91 O ANISOU 3068 O PRO A 450 5840 5038 3905 315 87 -33 O ATOM 3069 CB PRO A 450 -48.643 14.222 -18.189 1.00 38.06 C ANISOU 3069 CB PRO A 450 5738 4851 3871 371 69 -141 C ATOM 3070 CG PRO A 450 -48.788 12.854 -17.615 1.00 39.53 C ANISOU 3070 CG PRO A 450 5940 4974 4105 393 56 -167 C ATOM 3071 CD PRO A 450 -50.199 12.402 -17.881 1.00 39.75 C ANISOU 3071 CD PRO A 450 5981 4995 4126 379 71 -166 C ATOM 3072 N TYR A 451 -50.856 15.455 -20.300 1.00 35.16 N ANISOU 3072 N TYR A 451 5338 4607 3413 303 109 -100 N ATOM 3073 CA TYR A 451 -51.073 16.411 -21.384 1.00 35.70 C ANISOU 3073 CA TYR A 451 5372 4755 3438 269 118 -70 C ATOM 3074 C TYR A 451 -51.831 17.640 -20.902 1.00 34.16 C ANISOU 3074 C TYR A 451 5200 4535 3243 259 110 1 C ATOM 3075 O TYR A 451 -51.478 18.769 -21.256 1.00 35.16 O ANISOU 3075 O TYR A 451 5304 4695 3359 241 104 45 O ATOM 3076 CB TYR A 451 -51.817 15.773 -22.571 1.00 32.28 C ANISOU 3076 CB TYR A 451 4906 4386 2973 248 136 -106 C ATOM 3077 CG TYR A 451 -52.420 16.820 -23.477 1.00 30.24 C ANISOU 3077 CG TYR A 451 4622 4199 2668 211 139 -51 C ATOM 3078 CD1 TYR A 451 -51.701 17.332 -24.552 1.00 30.53 C ANISOU 3078 CD1 TYR A 451 4607 4331 2662 182 144 -43 C ATOM 3079 CD2 TYR A 451 -53.703 17.323 -23.242 1.00 28.95 C ANISOU 3079 CD2 TYR A 451 4485 4009 2507 204 134 -4 C ATOM 3080 CE1 TYR A 451 -52.249 18.307 -25.383 1.00 29.84 C ANISOU 3080 CE1 TYR A 451 4493 4311 2535 145 141 22 C ATOM 3081 CE2 TYR A 451 -54.247 18.296 -24.033 1.00 29.58 C ANISOU 3081 CE2 TYR A 451 4539 4145 2556 172 130 53 C ATOM 3082 CZ TYR A 451 -53.526 18.790 -25.115 1.00 32.23 C ANISOU 3082 CZ TYR A 451 4822 4575 2848 141 131 72 C ATOM 3083 OH TYR A 451 -54.092 19.767 -25.912 1.00 32.95 O ANISOU 3083 OH TYR A 451 4884 4724 2910 106 122 143 O ATOM 3084 N TYR A 452 -52.889 17.448 -20.110 1.00 34.40 N ANISOU 3084 N TYR A 452 5271 4509 3291 268 108 11 N ATOM 3085 CA TYR A 452 -53.713 18.595 -19.746 1.00 33.22 C ANISOU 3085 CA TYR A 452 5134 4340 3148 257 100 65 C ATOM 3086 C TYR A 452 -52.947 19.573 -18.864 1.00 31.57 C ANISOU 3086 C TYR A 452 4932 4097 2966 268 85 92 C ATOM 3087 O TYR A 452 -53.069 20.792 -19.039 1.00 32.64 O ANISOU 3087 O TYR A 452 5048 4240 3112 252 77 136 O ATOM 3088 CB TYR A 452 -55.004 18.127 -19.075 1.00 33.15 C ANISOU 3088 CB TYR A 452 5161 4285 3150 263 105 60 C ATOM 3089 CG TYR A 452 -55.850 17.296 -20.002 1.00 32.56 C ANISOU 3089 CG TYR A 452 5074 4244 3053 250 119 34 C ATOM 3090 CD1 TYR A 452 -56.493 17.879 -21.117 1.00 37.46 C ANISOU 3090 CD1 TYR A 452 5663 4924 3647 223 121 58 C ATOM 3091 CD2 TYR A 452 -55.957 15.916 -19.824 1.00 30.05 C ANISOU 3091 CD2 TYR A 452 4770 3902 2746 264 128 -15 C ATOM 3092 CE1 TYR A 452 -57.264 17.107 -22.007 1.00 27.65 C ANISOU 3092 CE1 TYR A 452 4404 3724 2380 210 135 28 C ATOM 3093 CE2 TYR A 452 -56.712 15.148 -20.694 1.00 33.76 C ANISOU 3093 CE2 TYR A 452 5222 4404 3202 252 141 -49 C ATOM 3094 CZ TYR A 452 -57.363 15.745 -21.779 1.00 30.51 C ANISOU 3094 CZ TYR A 452 4779 4058 2755 226 146 -31 C ATOM 3095 OH TYR A 452 -58.110 14.957 -22.622 1.00 36.49 O ANISOU 3095 OH TYR A 452 5515 4853 3495 215 160 -71 O ATOM 3096 N LEU A 453 -52.139 19.075 -17.924 1.00 32.96 N ANISOU 3096 N LEU A 453 5130 4236 3158 293 80 67 N ATOM 3097 CA LEU A 453 -51.307 19.996 -17.155 1.00 32.54 C ANISOU 3097 CA LEU A 453 5076 4161 3128 302 66 84 C ATOM 3098 C LEU A 453 -50.331 20.727 -18.074 1.00 31.63 C ANISOU 3098 C LEU A 453 4917 4094 3007 287 64 100 C ATOM 3099 O LEU A 453 -50.297 21.963 -18.102 1.00 31.84 O ANISOU 3099 O LEU A 453 4925 4120 3053 274 56 140 O ATOM 3100 CB LEU A 453 -50.576 19.256 -16.030 1.00 31.45 C ANISOU 3100 CB LEU A 453 4965 3982 3001 331 57 56 C ATOM 3101 CG LEU A 453 -49.937 20.115 -14.935 1.00 30.72 C ANISOU 3101 CG LEU A 453 4878 3863 2930 343 41 66 C ATOM 3102 CD1 LEU A 453 -49.871 19.326 -13.672 1.00 31.89 C ANISOU 3102 CD1 LEU A 453 5062 3975 3080 364 32 51 C ATOM 3103 CD2 LEU A 453 -48.540 20.554 -15.309 1.00 31.19 C ANISOU 3103 CD2 LEU A 453 4907 3945 2998 347 35 62 C ATOM 3104 N TYR A 454 -49.574 19.971 -18.879 1.00 29.71 N ANISOU 3104 N TYR A 454 4652 3895 2742 286 73 68 N ATOM 3105 CA TYR A 454 -48.607 20.574 -19.782 1.00 29.39 C ANISOU 3105 CA TYR A 454 4566 3913 2687 266 75 81 C ATOM 3106 C TYR A 454 -49.268 21.599 -20.698 1.00 34.16 C ANISOU 3106 C TYR A 454 5141 4562 3277 229 75 140 C ATOM 3107 O TYR A 454 -48.733 22.697 -20.894 1.00 34.52 O ANISOU 3107 O TYR A 454 5159 4621 3337 212 66 185 O ATOM 3108 CB TYR A 454 -47.921 19.497 -20.614 1.00 31.91 C ANISOU 3108 CB TYR A 454 4858 4286 2981 266 88 24 C ATOM 3109 CG TYR A 454 -47.095 18.490 -19.845 1.00 32.21 C ANISOU 3109 CG TYR A 454 4913 4280 3045 301 82 -31 C ATOM 3110 CD1 TYR A 454 -46.374 18.846 -18.719 1.00 28.54 C ANISOU 3110 CD1 TYR A 454 4469 3763 2612 325 65 -24 C ATOM 3111 CD2 TYR A 454 -47.028 17.166 -20.268 1.00 37.32 C ANISOU 3111 CD2 TYR A 454 5549 4939 3693 311 90 -94 C ATOM 3112 CE1 TYR A 454 -45.612 17.907 -18.026 1.00 30.89 C ANISOU 3112 CE1 TYR A 454 4780 4022 2936 357 53 -67 C ATOM 3113 CE2 TYR A 454 -46.275 16.217 -19.572 1.00 34.11 C ANISOU 3113 CE2 TYR A 454 5153 4484 3325 344 77 -140 C ATOM 3114 CZ TYR A 454 -45.572 16.590 -18.459 1.00 31.06 C ANISOU 3114 CZ TYR A 454 4790 4047 2965 366 58 -121 C ATOM 3115 OH TYR A 454 -44.824 15.646 -17.796 1.00 28.43 O ANISOU 3115 OH TYR A 454 4464 3668 2671 398 41 -158 O ATOM 3116 N ASN A 455 -50.441 21.273 -21.258 1.00 31.34 N ANISOU 3116 N ASN A 455 4786 4226 2897 215 82 147 N ATOM 3117 CA ASN A 455 -51.104 22.216 -22.150 1.00 31.04 C ANISOU 3117 CA ASN A 455 4717 4232 2847 180 77 211 C ATOM 3118 C ASN A 455 -51.561 23.457 -21.404 1.00 31.65 C ANISOU 3118 C ASN A 455 4802 4244 2978 181 57 263 C ATOM 3119 O ASN A 455 -51.411 24.579 -21.899 1.00 33.26 O ANISOU 3119 O ASN A 455 4971 4467 3199 156 43 326 O ATOM 3120 CB ASN A 455 -52.306 21.579 -22.844 1.00 31.75 C ANISOU 3120 CB ASN A 455 4806 4356 2902 167 86 201 C ATOM 3121 CG ASN A 455 -52.818 22.445 -23.987 1.00 28.60 C ANISOU 3121 CG ASN A 455 4364 4025 2478 125 78 270 C ATOM 3122 ND2 ASN A 455 -54.069 22.856 -23.923 1.00 28.51 N ANISOU 3122 ND2 ASN A 455 4363 3986 2485 120 67 306 N ATOM 3123 OD1 ASN A 455 -52.057 22.778 -24.887 1.00 28.99 O ANISOU 3123 OD1 ASN A 455 4370 4152 2495 97 79 295 O ATOM 3124 N ASN A 456 -52.167 23.260 -20.234 1.00 31.49 N ANISOU 3124 N ASN A 456 4824 4151 2989 208 54 239 N ATOM 3125 CA ASN A 456 -52.655 24.369 -19.427 1.00 32.21 C ANISOU 3125 CA ASN A 456 4919 4182 3138 211 37 268 C ATOM 3126 C ASN A 456 -51.550 25.370 -19.130 1.00 33.99 C ANISOU 3126 C ASN A 456 5119 4392 3403 211 23 289 C ATOM 3127 O ASN A 456 -51.714 26.581 -19.335 1.00 33.20 O ANISOU 3127 O ASN A 456 4987 4277 3350 194 6 341 O ATOM 3128 CB ASN A 456 -53.234 23.826 -18.121 1.00 32.16 C ANISOU 3128 CB ASN A 456 4957 4116 3144 239 41 223 C ATOM 3129 CG ASN A 456 -54.722 23.669 -18.187 1.00 34.13 C ANISOU 3129 CG ASN A 456 5219 4355 3392 232 45 227 C ATOM 3130 ND2 ASN A 456 -55.195 22.455 -17.955 1.00 31.62 N ANISOU 3130 ND2 ASN A 456 4935 4036 3044 243 60 188 N ATOM 3131 OD1 ASN A 456 -55.448 24.628 -18.474 1.00 36.05 O ANISOU 3131 OD1 ASN A 456 5439 4589 3668 216 32 265 O ATOM 3132 N PHE A 457 -50.412 24.888 -18.645 1.00 29.12 N ANISOU 3132 N PHE A 457 4515 3774 2777 231 29 250 N ATOM 3133 CA PHE A 457 -49.453 25.787 -18.035 1.00 33.95 C ANISOU 3133 CA PHE A 457 5109 4356 3434 238 16 256 C ATOM 3134 C PHE A 457 -48.216 26.062 -18.866 1.00 31.70 C ANISOU 3134 C PHE A 457 4787 4121 3137 221 17 276 C ATOM 3135 O PHE A 457 -47.461 26.969 -18.521 1.00 34.02 O ANISOU 3135 O PHE A 457 5058 4392 3475 220 6 290 O ATOM 3136 CB PHE A 457 -49.054 25.239 -16.661 1.00 34.72 C ANISOU 3136 CB PHE A 457 5244 4411 3537 273 16 200 C ATOM 3137 CG PHE A 457 -50.207 25.157 -15.736 1.00 33.47 C ANISOU 3137 CG PHE A 457 5115 4211 3391 284 15 183 C ATOM 3138 CD1 PHE A 457 -50.734 26.315 -15.186 1.00 31.80 C ANISOU 3138 CD1 PHE A 457 4887 3961 3236 280 2 195 C ATOM 3139 CD2 PHE A 457 -50.826 23.933 -15.486 1.00 31.79 C ANISOU 3139 CD2 PHE A 457 4942 3999 3139 295 27 155 C ATOM 3140 CE1 PHE A 457 -51.831 26.262 -14.352 1.00 31.28 C ANISOU 3140 CE1 PHE A 457 4841 3866 3179 286 4 172 C ATOM 3141 CE2 PHE A 457 -51.930 23.867 -14.648 1.00 31.52 C ANISOU 3141 CE2 PHE A 457 4932 3933 3112 300 28 142 C ATOM 3142 CZ PHE A 457 -52.432 25.040 -14.074 1.00 29.44 C ANISOU 3142 CZ PHE A 457 4650 3640 2896 295 18 148 C ATOM 3143 N LEU A 458 -47.986 25.333 -19.941 1.00 32.76 N ANISOU 3143 N LEU A 458 4908 4325 3214 204 32 272 N ATOM 3144 CA LEU A 458 -46.778 25.537 -20.711 1.00 32.58 C ANISOU 3144 CA LEU A 458 4845 4361 3173 184 36 283 C ATOM 3145 C LEU A 458 -47.053 26.035 -22.114 1.00 32.84 C ANISOU 3145 C LEU A 458 4831 4470 3174 136 37 347 C ATOM 3146 O LEU A 458 -46.116 26.465 -22.794 1.00 36.70 O ANISOU 3146 O LEU A 458 5279 5015 3651 109 39 374 O ATOM 3147 CB LEU A 458 -45.962 24.237 -20.778 1.00 31.52 C ANISOU 3147 CB LEU A 458 4719 4258 2997 203 53 210 C ATOM 3148 CG LEU A 458 -45.713 23.553 -19.433 1.00 33.47 C ANISOU 3148 CG LEU A 458 5012 4437 3269 249 48 154 C ATOM 3149 CD1 LEU A 458 -45.174 22.145 -19.625 1.00 28.66 C ANISOU 3149 CD1 LEU A 458 4408 3851 2631 267 59 87 C ATOM 3150 CD2 LEU A 458 -44.775 24.383 -18.571 1.00 29.07 C ANISOU 3150 CD2 LEU A 458 4450 3839 2757 263 34 157 C ATOM 3151 N SER A 459 -48.299 26.000 -22.561 1.00 33.76 N ANISOU 3151 N SER A 459 4952 4598 3277 122 35 377 N ATOM 3152 CA SER A 459 -48.614 26.354 -23.938 1.00 32.27 C ANISOU 3152 CA SER A 459 4718 4496 3047 75 33 441 C ATOM 3153 C SER A 459 -48.492 27.853 -24.146 1.00 34.01 C ANISOU 3153 C SER A 459 4900 4701 3322 45 8 535 C ATOM 3154 O SER A 459 -48.998 28.645 -23.339 1.00 31.66 O ANISOU 3154 O SER A 459 4613 4314 3103 60 -13 558 O ATOM 3155 CB SER A 459 -50.023 25.901 -24.286 1.00 31.04 C ANISOU 3155 CB SER A 459 4576 4351 2865 71 34 444 C ATOM 3156 OG SER A 459 -50.381 26.359 -25.567 1.00 34.47 O ANISOU 3156 OG SER A 459 4965 4872 3262 23 27 516 O ATOM 3157 N SER A 460 -47.819 28.239 -25.236 1.00 31.31 N ANISOU 3157 N SER A 460 4506 4448 2943 0 8 589 N ATOM 3158 CA SER A 460 -47.842 29.638 -25.644 1.00 32.36 C ANISOU 3158 CA SER A 460 4593 4574 3127 -38 -20 699 C ATOM 3159 C SER A 460 -49.273 30.125 -25.811 1.00 33.31 C ANISOU 3159 C SER A 460 4713 4663 3281 -47 -45 760 C ATOM 3160 O SER A 460 -49.592 31.263 -25.451 1.00 36.52 O ANISOU 3160 O SER A 460 5102 4992 3781 -51 -76 822 O ATOM 3161 CB SER A 460 -47.064 29.835 -26.944 1.00 31.49 C ANISOU 3161 CB SER A 460 4424 4588 2952 -95 -14 757 C ATOM 3162 OG SER A 460 -45.678 29.693 -26.753 1.00 31.52 O ANISOU 3162 OG SER A 460 4419 4610 2948 -91 3 713 O ATOM 3163 N ALA A 461 -50.144 29.269 -26.357 1.00 31.94 N ANISOU 3163 N ALA A 461 4552 4545 3039 -51 -33 738 N ATOM 3164 CA ALA A 461 -51.557 29.604 -26.510 1.00 36.70 C ANISOU 3164 CA ALA A 461 5156 5120 3668 -56 -55 785 C ATOM 3165 C ALA A 461 -52.148 30.172 -25.227 1.00 33.15 C ANISOU 3165 C ALA A 461 4735 4534 3325 -17 -73 767 C ATOM 3166 O ALA A 461 -52.984 31.079 -25.268 1.00 32.62 O ANISOU 3166 O ALA A 461 4646 4420 3327 -28 -105 833 O ATOM 3167 CB ALA A 461 -52.344 28.360 -26.940 1.00 36.98 C ANISOU 3167 CB ALA A 461 5214 5216 3620 -50 -32 726 C ATOM 3168 N ASN A 462 -51.712 29.658 -24.077 1.00 36.99 N ANISOU 3168 N ASN A 462 5265 4960 3827 27 -55 677 N ATOM 3169 CA ASN A 462 -52.317 29.954 -22.786 1.00 34.19 C ANISOU 3169 CA ASN A 462 4941 4497 3552 64 -64 636 C ATOM 3170 C ASN A 462 -51.574 31.025 -21.997 1.00 33.80 C ANISOU 3170 C ASN A 462 4872 4375 3596 73 -82 646 C ATOM 3171 O ASN A 462 -51.850 31.210 -20.805 1.00 37.16 O ANISOU 3171 O ASN A 462 5319 4721 4079 106 -85 592 O ATOM 3172 CB ASN A 462 -52.422 28.672 -21.973 1.00 34.67 C ANISOU 3172 CB ASN A 462 5060 4545 3567 103 -35 535 C ATOM 3173 CG ASN A 462 -53.544 27.807 -22.428 1.00 29.86 C ANISOU 3173 CG ASN A 462 4472 3970 2905 101 -24 519 C ATOM 3174 ND2 ASN A 462 -53.388 26.492 -22.296 1.00 28.56 N ANISOU 3174 ND2 ASN A 462 4342 3831 2678 120 3 448 N ATOM 3175 OD1 ASN A 462 -54.562 28.319 -22.887 1.00 29.04 O ANISOU 3175 OD1 ASN A 462 4348 3864 2822 83 -42 570 O ATOM 3176 N THR A 463 -50.658 31.750 -22.627 1.00 33.44 N ANISOU 3176 N THR A 463 4782 4359 3566 43 -93 710 N ATOM 3177 CA THR A 463 -49.976 32.831 -21.942 1.00 36.18 C ANISOU 3177 CA THR A 463 5101 4633 4013 49 -112 720 C ATOM 3178 C THR A 463 -50.177 34.140 -22.699 1.00 37.44 C ANISOU 3178 C THR A 463 5197 4779 4250 7 -150 836 C ATOM 3179 O THR A 463 -50.758 34.180 -23.784 1.00 39.68 O ANISOU 3179 O THR A 463 5459 5121 4499 -28 -162 914 O ATOM 3180 CB THR A 463 -48.481 32.514 -21.741 1.00 36.86 C ANISOU 3180 CB THR A 463 5192 4748 4066 56 -92 680 C ATOM 3181 CG2 THR A 463 -47.680 32.694 -23.020 1.00 30.70 C ANISOU 3181 CG2 THR A 463 4368 4059 3237 8 -90 754 C ATOM 3182 OG1 THR A 463 -47.948 33.326 -20.678 1.00 38.43 O ANISOU 3182 OG1 THR A 463 5379 4863 4360 78 -105 652 O ATOM 3183 N ALA A 464 -49.703 35.221 -22.084 1.00 40.20 N ANISOU 3183 N ALA A 464 5514 5048 4712 11 -172 848 N ATOM 3184 CA ALA A 464 -49.771 36.567 -22.638 1.00 37.21 C ANISOU 3184 CA ALA A 464 5067 4633 4438 -26 -214 958 C ATOM 3185 C ALA A 464 -48.648 37.386 -22.024 1.00 38.70 C ANISOU 3185 C ALA A 464 5225 4764 4715 -21 -221 946 C ATOM 3186 O ALA A 464 -48.025 36.981 -21.037 1.00 39.63 O ANISOU 3186 O ALA A 464 5375 4860 4822 16 -198 846 O ATOM 3187 CB ALA A 464 -51.123 37.225 -22.367 1.00 39.11 C ANISOU 3187 CB ALA A 464 5289 4791 4779 -18 -248 977 C ATOM 3188 N GLU A 465 -48.400 38.547 -22.626 1.00 42.39 N ANISOU 3188 N GLU A 465 5626 5207 5274 -61 -256 1054 N ATOM 3189 CA GLU A 465 -47.365 39.451 -22.143 1.00 42.94 C ANISOU 3189 CA GLU A 465 5654 5216 5444 -62 -268 1054 C ATOM 3190 C GLU A 465 -47.704 39.954 -20.742 1.00 44.72 C ANISOU 3190 C GLU A 465 5879 5323 5790 -15 -279 958 C ATOM 3191 O GLU A 465 -48.876 40.071 -20.363 1.00 46.57 O ANISOU 3191 O GLU A 465 6117 5504 6074 3 -294 934 O ATOM 3192 CB GLU A 465 -47.213 40.625 -23.121 1.00 41.60 C ANISOU 3192 CB GLU A 465 5408 5037 5360 -119 -310 1203 C ATOM 3193 CG GLU A 465 -46.089 41.569 -22.797 1.00 44.84 C ANISOU 3193 CG GLU A 465 5769 5391 5877 -129 -322 1218 C ATOM 3194 CD GLU A 465 -45.500 42.230 -24.023 1.00 56.09 C ANISOU 3194 CD GLU A 465 7133 6869 7310 -198 -343 1369 C ATOM 3195 OE1 GLU A 465 -44.243 42.266 -24.080 1.00 57.02 O ANISOU 3195 OE1 GLU A 465 7239 7022 7404 -212 -324 1364 O ATOM 3196 OE2 GLU A 465 -46.271 42.689 -24.916 1.00 50.61 O1- ANISOU 3196 OE2 GLU A 465 6402 6185 6641 -238 -379 1493 O1- ATOM 3197 N VAL A 466 -46.669 40.240 -19.951 1.00 40.40 N ANISOU 3197 N VAL A 466 5322 4741 5288 3 -270 894 N ATOM 3198 CA VAL A 466 -46.922 40.916 -18.685 1.00 41.78 C ANISOU 3198 CA VAL A 466 5476 4809 5590 39 -285 808 C ATOM 3199 C VAL A 466 -47.533 42.274 -18.993 1.00 41.36 C ANISOU 3199 C VAL A 466 5345 4663 5706 14 -337 890 C ATOM 3200 O VAL A 466 -46.965 43.082 -19.739 1.00 42.61 O ANISOU 3200 O VAL A 466 5447 4811 5932 -26 -362 996 O ATOM 3201 CB VAL A 466 -45.639 41.031 -17.847 1.00 43.07 C ANISOU 3201 CB VAL A 466 5635 4959 5772 60 -269 729 C ATOM 3202 CG1 VAL A 466 -45.870 41.945 -16.638 1.00 38.62 C ANISOU 3202 CG1 VAL A 466 5029 4288 5358 88 -290 645 C ATOM 3203 CG2 VAL A 466 -45.222 39.668 -17.378 1.00 40.60 C ANISOU 3203 CG2 VAL A 466 5397 4720 5308 91 -226 640 C ATOM 3204 N GLY A 467 -48.710 42.517 -18.440 1.00 42.04 N ANISOU 3204 N GLY A 467 5424 4685 5866 37 -354 846 N ATOM 3205 CA GLY A 467 -49.552 43.625 -18.823 1.00 39.68 C ANISOU 3205 CA GLY A 467 5055 4301 5722 16 -406 924 C ATOM 3206 C GLY A 467 -50.856 43.157 -19.393 1.00 39.28 C ANISOU 3206 C GLY A 467 5029 4278 5617 11 -414 965 C ATOM 3207 O GLY A 467 -51.810 43.941 -19.493 1.00 41.39 O ANISOU 3207 O GLY A 467 5245 4468 6013 5 -457 1002 O ATOM 3208 N GLN A 468 -50.932 41.887 -19.730 1.00 39.41 N ANISOU 3208 N GLN A 468 5119 4399 5455 14 -374 951 N ATOM 3209 CA GLN A 468 -52.050 41.339 -20.453 1.00 40.21 C ANISOU 3209 CA GLN A 468 5245 4547 5485 3 -377 998 C ATOM 3210 C GLN A 468 -52.452 40.060 -19.754 1.00 37.45 C ANISOU 3210 C GLN A 468 4975 4244 5010 42 -331 879 C ATOM 3211 O GLN A 468 -51.608 39.374 -19.177 1.00 41.35 O ANISOU 3211 O GLN A 468 5513 4775 5425 62 -294 802 O ATOM 3212 CB GLN A 468 -51.656 41.103 -21.928 1.00 47.73 C ANISOU 3212 CB GLN A 468 6193 5601 6341 -48 -380 1132 C ATOM 3213 CG GLN A 468 -51.400 42.407 -22.718 1.00 48.71 C ANISOU 3213 CG GLN A 468 6233 5683 6592 -95 -433 1277 C ATOM 3214 CD GLN A 468 -51.019 42.142 -24.157 1.00 49.19 C ANISOU 3214 CD GLN A 468 6285 5864 6540 -152 -433 1409 C ATOM 3215 NE2 GLN A 468 -50.116 42.946 -24.702 1.00 45.59 N ANISOU 3215 NE2 GLN A 468 5773 5409 6139 -194 -455 1511 N ATOM 3216 OE1 GLN A 468 -51.576 41.256 -24.787 1.00 54.97 O ANISOU 3216 OE1 GLN A 468 7056 6689 7141 -160 -416 1419 O ATOM 3217 N ALA A 469 -53.746 39.756 -19.768 1.00 38.20 N ANISOU 3217 N ALA A 469 5086 4332 5096 51 -336 865 N ATOM 3218 CA ALA A 469 -54.226 38.567 -19.069 1.00 38.11 C ANISOU 3218 CA ALA A 469 5145 4358 4976 84 -294 757 C ATOM 3219 C ALA A 469 -53.668 37.311 -19.727 1.00 40.05 C ANISOU 3219 C ALA A 469 5450 4716 5051 75 -256 769 C ATOM 3220 O ALA A 469 -53.822 37.122 -20.938 1.00 37.89 O ANISOU 3220 O ALA A 469 5170 4507 4720 42 -263 860 O ATOM 3221 CB ALA A 469 -55.749 38.530 -19.066 1.00 33.47 C ANISOU 3221 CB ALA A 469 4557 3743 4416 90 -308 747 C ATOM 3222 N ALA A 470 -53.017 36.459 -18.930 1.00 40.12 N ANISOU 3222 N ALA A 470 5509 4750 4983 104 -218 676 N ATOM 3223 CA ALA A 470 -52.593 35.144 -19.393 1.00 37.18 C ANISOU 3223 CA ALA A 470 5192 4473 4461 103 -181 664 C ATOM 3224 C ALA A 470 -53.699 34.144 -19.096 1.00 35.73 C ANISOU 3224 C ALA A 470 5059 4305 4212 123 -161 607 C ATOM 3225 O ALA A 470 -54.125 34.046 -17.945 1.00 37.73 O ANISOU 3225 O ALA A 470 5332 4512 4492 152 -153 525 O ATOM 3226 CB ALA A 470 -51.303 34.714 -18.711 1.00 36.08 C ANISOU 3226 CB ALA A 470 5077 4348 4282 124 -156 599 C ATOM 3227 N PRO A 471 -54.192 33.392 -20.085 1.00 38.95 N ANISOU 3227 N PRO A 471 5485 4782 4531 105 -151 645 N ATOM 3228 CA PRO A 471 -55.342 32.505 -19.818 1.00 37.12 C ANISOU 3228 CA PRO A 471 5296 4558 4250 121 -134 593 C ATOM 3229 C PRO A 471 -55.047 31.400 -18.815 1.00 33.32 C ANISOU 3229 C PRO A 471 4874 4083 3705 154 -99 495 C ATOM 3230 O PRO A 471 -55.837 31.184 -17.890 1.00 34.13 O ANISOU 3230 O PRO A 471 4999 4147 3822 175 -92 434 O ATOM 3231 CB PRO A 471 -55.683 31.946 -21.213 1.00 32.76 C ANISOU 3231 CB PRO A 471 4742 4091 3615 92 -131 656 C ATOM 3232 CG PRO A 471 -55.090 32.901 -22.163 1.00 35.84 C ANISOU 3232 CG PRO A 471 5075 4502 4039 55 -159 758 C ATOM 3233 CD PRO A 471 -53.848 33.433 -21.516 1.00 35.72 C ANISOU 3233 CD PRO A 471 5048 4451 4073 64 -159 740 C ATOM 3234 N VAL A 472 -53.953 30.663 -18.989 1.00 34.58 N ANISOU 3234 N VAL A 472 5055 4292 3792 157 -78 480 N ATOM 3235 CA VAL A 472 -53.574 29.655 -18.001 1.00 35.67 C ANISOU 3235 CA VAL A 472 5243 4429 3880 189 -52 398 C ATOM 3236 C VAL A 472 -52.076 29.749 -17.700 1.00 36.23 C ANISOU 3236 C VAL A 472 5309 4506 3950 197 -49 383 C ATOM 3237 O VAL A 472 -51.664 29.702 -16.537 1.00 33.99 O ANISOU 3237 O VAL A 472 5043 4189 3684 222 -45 326 O ATOM 3238 CB VAL A 472 -53.950 28.228 -18.463 1.00 37.87 C ANISOU 3238 CB VAL A 472 5563 4762 4065 191 -27 375 C ATOM 3239 CG1 VAL A 472 -54.058 27.279 -17.239 1.00 36.65 C ANISOU 3239 CG1 VAL A 472 5459 4583 3883 222 -9 298 C ATOM 3240 CG2 VAL A 472 -55.220 28.194 -19.362 1.00 31.42 C ANISOU 3240 CG2 VAL A 472 4735 3967 3235 170 -32 414 C ATOM 3241 N ASN A 473 -51.247 29.882 -18.742 1.00 36.34 N ANISOU 3241 N ASN A 473 5296 4571 3941 173 -50 433 N ATOM 3242 CA ASN A 473 -49.788 29.853 -18.590 1.00 36.52 C ANISOU 3242 CA ASN A 473 5312 4608 3954 179 -44 417 C ATOM 3243 C ASN A 473 -49.325 31.174 -17.980 1.00 34.94 C ANISOU 3243 C ASN A 473 5075 4348 3853 180 -66 429 C ATOM 3244 O ASN A 473 -48.811 32.073 -18.653 1.00 36.77 O ANISOU 3244 O ASN A 473 5259 4585 4127 153 -82 492 O ATOM 3245 CB ASN A 473 -49.114 29.578 -19.933 1.00 34.42 C ANISOU 3245 CB ASN A 473 5023 4426 3629 149 -36 461 C ATOM 3246 CG ASN A 473 -47.585 29.455 -19.834 1.00 34.43 C ANISOU 3246 CG ASN A 473 5016 4451 3617 154 -27 437 C ATOM 3247 ND2 ASN A 473 -47.010 28.727 -20.780 1.00 36.47 N ANISOU 3247 ND2 ASN A 473 5266 4790 3802 137 -9 436 N ATOM 3248 OD1 ASN A 473 -46.941 29.948 -18.899 1.00 35.76 O ANISOU 3248 OD1 ASN A 473 5182 4567 3837 174 -34 409 O ATOM 3249 N VAL A 474 -49.487 31.267 -16.662 1.00 32.98 N ANISOU 3249 N VAL A 474 4844 4045 3642 210 -67 364 N ATOM 3250 CA VAL A 474 -49.170 32.488 -15.921 1.00 34.36 C ANISOU 3250 CA VAL A 474 4979 4158 3918 215 -88 353 C ATOM 3251 C VAL A 474 -47.670 32.677 -15.733 1.00 33.63 C ANISOU 3251 C VAL A 474 4872 4075 3831 220 -86 340 C ATOM 3252 O VAL A 474 -47.220 33.789 -15.432 1.00 35.08 O ANISOU 3252 O VAL A 474 5010 4214 4105 216 -104 346 O ATOM 3253 CB VAL A 474 -49.910 32.478 -14.566 1.00 36.57 C ANISOU 3253 CB VAL A 474 5277 4394 4224 241 -87 277 C ATOM 3254 CG1 VAL A 474 -49.529 33.655 -13.728 1.00 41.45 C ANISOU 3254 CG1 VAL A 474 5849 4956 4946 249 -105 245 C ATOM 3255 CG2 VAL A 474 -51.404 32.562 -14.775 1.00 34.07 C ANISOU 3255 CG2 VAL A 474 4961 4060 3926 233 -92 292 C ATOM 3256 N ALA A 475 -46.876 31.630 -15.918 1.00 33.52 N ANISOU 3256 N ALA A 475 4891 4115 3732 228 -66 320 N ATOM 3257 CA ALA A 475 -45.438 31.757 -15.751 1.00 34.33 C ANISOU 3257 CA ALA A 475 4978 4227 3838 234 -65 302 C ATOM 3258 C ALA A 475 -44.775 32.386 -16.961 1.00 34.44 C ANISOU 3258 C ALA A 475 4945 4273 3867 197 -70 376 C ATOM 3259 O ALA A 475 -43.585 32.723 -16.892 1.00 34.86 O ANISOU 3259 O ALA A 475 4974 4331 3939 195 -70 369 O ATOM 3260 CB ALA A 475 -44.814 30.383 -15.462 1.00 33.30 C ANISOU 3260 CB ALA A 475 4894 4138 3621 259 -45 248 C ATOM 3261 N ARG A 476 -45.528 32.562 -18.049 1.00 35.78 N ANISOU 3261 N ARG A 476 5098 4469 4027 164 -74 448 N ATOM 3262 CA ARG A 476 -44.982 33.037 -19.314 1.00 36.11 C ANISOU 3262 CA ARG A 476 5094 4562 4062 120 -78 530 C ATOM 3263 C ARG A 476 -43.915 32.071 -19.814 1.00 34.81 C ANISOU 3263 C ARG A 476 4942 4479 3806 117 -52 502 C ATOM 3264 O ARG A 476 -42.928 32.465 -20.427 1.00 34.95 O ANISOU 3264 O ARG A 476 4920 4535 3823 90 -51 536 O ATOM 3265 CB ARG A 476 -44.424 34.464 -19.189 1.00 39.45 C ANISOU 3265 CB ARG A 476 5460 4932 4596 103 -102 575 C ATOM 3266 CG ARG A 476 -45.454 35.586 -19.349 1.00 39.77 C ANISOU 3266 CG ARG A 476 5463 4911 4737 83 -134 642 C ATOM 3267 CD ARG A 476 -46.484 35.595 -18.214 1.00 39.97 C ANISOU 3267 CD ARG A 476 5512 4864 4808 121 -141 574 C ATOM 3268 NE ARG A 476 -47.535 36.587 -18.441 1.00 43.53 N ANISOU 3268 NE ARG A 476 5924 5258 5359 103 -173 632 N ATOM 3269 CZ ARG A 476 -48.600 36.761 -17.665 1.00 41.07 C ANISOU 3269 CZ ARG A 476 5618 4887 5101 126 -182 585 C ATOM 3270 NH1 ARG A 476 -48.794 36.030 -16.581 1.00 39.61 N1+ ANISOU 3270 NH1 ARG A 476 5480 4698 4873 163 -161 484 N1+ ATOM 3271 NH2 ARG A 476 -49.491 37.694 -17.986 1.00 40.80 N ANISOU 3271 NH2 ARG A 476 5537 4798 5166 108 -215 642 N ATOM 3272 N PHE A 477 -44.096 30.792 -19.527 1.00 34.13 N ANISOU 3272 N PHE A 477 4905 4415 3649 146 -33 435 N ATOM 3273 CA PHE A 477 -43.258 29.803 -20.176 1.00 34.07 C ANISOU 3273 CA PHE A 477 4900 4486 3560 141 -11 406 C ATOM 3274 C PHE A 477 -43.631 29.703 -21.652 1.00 33.19 C ANISOU 3274 C PHE A 477 4758 4462 3390 94 -3 466 C ATOM 3275 O PHE A 477 -44.804 29.802 -22.021 1.00 32.69 O ANISOU 3275 O PHE A 477 4699 4398 3323 81 -10 507 O ATOM 3276 CB PHE A 477 -43.394 28.441 -19.515 1.00 31.41 C ANISOU 3276 CB PHE A 477 4616 4142 3176 182 3 322 C ATOM 3277 CG PHE A 477 -42.566 27.401 -20.188 1.00 34.28 C ANISOU 3277 CG PHE A 477 4974 4579 3472 179 23 282 C ATOM 3278 CD1 PHE A 477 -41.228 27.270 -19.883 1.00 29.23 C ANISOU 3278 CD1 PHE A 477 4322 3944 2838 193 26 240 C ATOM 3279 CD2 PHE A 477 -43.112 26.602 -21.200 1.00 35.47 C ANISOU 3279 CD2 PHE A 477 5122 4798 3558 160 39 282 C ATOM 3280 CE1 PHE A 477 -40.461 26.328 -20.522 1.00 32.92 C ANISOU 3280 CE1 PHE A 477 4776 4478 3253 191 43 194 C ATOM 3281 CE2 PHE A 477 -42.345 25.661 -21.848 1.00 32.35 C ANISOU 3281 CE2 PHE A 477 4710 4473 3108 156 57 232 C ATOM 3282 CZ PHE A 477 -41.015 25.517 -21.507 1.00 31.70 C ANISOU 3282 CZ PHE A 477 4616 4391 3038 172 60 186 C ATOM 3283 N SER A 478 -42.620 29.519 -22.506 1.00 36.07 N ANISOU 3283 N SER A 478 5089 4910 3708 67 11 471 N ATOM 3284 CA SER A 478 -42.846 29.527 -23.956 1.00 35.30 C ANISOU 3284 CA SER A 478 4951 4916 3546 14 18 532 C ATOM 3285 C SER A 478 -41.638 28.876 -24.630 1.00 33.80 C ANISOU 3285 C SER A 478 4732 4822 3288 -3 44 488 C ATOM 3286 O SER A 478 -40.602 29.524 -24.803 1.00 31.33 O ANISOU 3286 O SER A 478 4381 4529 2994 -25 43 513 O ATOM 3287 CB SER A 478 -43.066 30.944 -24.465 1.00 34.14 C ANISOU 3287 CB SER A 478 4757 4763 3452 -32 -7 649 C ATOM 3288 OG SER A 478 -43.535 30.955 -25.807 1.00 36.62 O ANISOU 3288 OG SER A 478 5035 5179 3700 -84 -5 720 O ATOM 3289 N ASP A 479 -41.788 27.607 -25.003 1.00 37.42 N ANISOU 3289 N ASP A 479 5205 5339 3676 7 65 418 N ATOM 3290 CA ASP A 479 -40.747 26.854 -25.694 1.00 38.78 C ANISOU 3290 CA ASP A 479 5343 5608 3785 -7 90 357 C ATOM 3291 C ASP A 479 -41.330 26.246 -26.962 1.00 37.59 C ANISOU 3291 C ASP A 479 5161 5574 3545 -45 107 358 C ATOM 3292 O ASP A 479 -42.212 25.361 -26.880 1.00 34.57 O ANISOU 3292 O ASP A 479 4811 5180 3144 -22 112 312 O ATOM 3293 CB ASP A 479 -40.141 25.765 -24.802 1.00 39.89 C ANISOU 3293 CB ASP A 479 5518 5698 3940 50 98 244 C ATOM 3294 CG ASP A 479 -39.205 24.834 -25.568 1.00 42.58 C ANISOU 3294 CG ASP A 479 5819 6137 4223 38 123 165 C ATOM 3295 OD1 ASP A 479 -38.547 25.274 -26.549 1.00 45.57 O ANISOU 3295 OD1 ASP A 479 6138 6618 4559 -13 136 193 O ATOM 3296 OD2 ASP A 479 -39.117 23.654 -25.187 1.00 44.34 O1- ANISOU 3296 OD2 ASP A 479 6065 6337 4446 79 129 73 O1- ATOM 3297 N PRO A 480 -40.856 26.648 -28.141 1.00 38.81 N ANISOU 3297 N PRO A 480 5252 5851 3642 -107 117 405 N ATOM 3298 CA PRO A 480 -41.462 26.146 -29.380 1.00 35.03 C ANISOU 3298 CA PRO A 480 4739 5501 3072 -149 132 409 C ATOM 3299 C PRO A 480 -41.343 24.650 -29.527 1.00 36.85 C ANISOU 3299 C PRO A 480 4972 5774 3258 -123 158 276 C ATOM 3300 O PRO A 480 -42.182 24.052 -30.210 1.00 38.02 O ANISOU 3300 O PRO A 480 5109 5987 3349 -137 167 258 O ATOM 3301 CB PRO A 480 -40.692 26.886 -30.480 1.00 39.56 C ANISOU 3301 CB PRO A 480 5237 6203 3590 -222 139 479 C ATOM 3302 CG PRO A 480 -40.076 28.066 -29.788 1.00 44.37 C ANISOU 3302 CG PRO A 480 5850 6722 4285 -219 118 549 C ATOM 3303 CD PRO A 480 -39.782 27.617 -28.393 1.00 37.36 C ANISOU 3303 CD PRO A 480 5023 5700 3473 -144 115 461 C ATOM 3304 N ALA A 481 -40.345 24.015 -28.898 1.00 37.45 N ANISOU 3304 N ALA A 481 5057 5809 3364 -83 167 180 N ATOM 3305 CA ALA A 481 -40.339 22.555 -28.867 1.00 38.08 C ANISOU 3305 CA ALA A 481 5143 5897 3430 -48 184 54 C ATOM 3306 C ALA A 481 -41.518 22.028 -28.053 1.00 38.83 C ANISOU 3306 C ALA A 481 5306 5882 3567 -1 171 43 C ATOM 3307 O ALA A 481 -42.138 21.021 -28.425 1.00 36.29 O ANISOU 3307 O ALA A 481 4981 5589 3217 6 182 -20 O ATOM 3308 CB ALA A 481 -39.014 22.033 -28.317 1.00 32.42 C ANISOU 3308 CB ALA A 481 4419 5148 2750 -14 190 -38 C ATOM 3309 N VAL A 482 -41.873 22.732 -26.971 1.00 37.29 N ANISOU 3309 N VAL A 482 5165 5566 3438 28 147 103 N ATOM 3310 CA VAL A 482 -42.959 22.287 -26.106 1.00 32.42 C ANISOU 3310 CA VAL A 482 4610 4848 2859 70 135 93 C ATOM 3311 C VAL A 482 -44.287 22.439 -26.823 1.00 33.33 C ANISOU 3311 C VAL A 482 4723 5007 2936 41 135 145 C ATOM 3312 O VAL A 482 -45.142 21.543 -26.800 1.00 31.91 O ANISOU 3312 O VAL A 482 4564 4813 2747 58 141 100 O ATOM 3313 CB VAL A 482 -42.930 23.073 -24.781 1.00 35.77 C ANISOU 3313 CB VAL A 482 5082 5150 3358 103 112 136 C ATOM 3314 CG1 VAL A 482 -44.310 23.102 -24.128 1.00 30.96 C ANISOU 3314 CG1 VAL A 482 4524 4462 2776 124 99 164 C ATOM 3315 CG2 VAL A 482 -41.878 22.483 -23.849 1.00 35.19 C ANISOU 3315 CG2 VAL A 482 5027 5018 3324 148 110 62 C ATOM 3316 N ASP A 483 -44.475 23.582 -27.477 1.00 35.38 N ANISOU 3316 N ASP A 483 4951 5318 3176 -7 126 244 N ATOM 3317 CA ASP A 483 -45.663 23.789 -28.296 1.00 34.41 C ANISOU 3317 CA ASP A 483 4813 5251 3011 -41 122 302 C ATOM 3318 C ASP A 483 -45.795 22.703 -29.353 1.00 34.56 C ANISOU 3318 C ASP A 483 4793 5389 2948 -62 147 230 C ATOM 3319 O ASP A 483 -46.867 22.111 -29.519 1.00 35.79 O ANISOU 3319 O ASP A 483 4965 5545 3087 -55 149 208 O ATOM 3320 CB ASP A 483 -45.606 25.172 -28.938 1.00 32.10 C ANISOU 3320 CB ASP A 483 4479 5006 2712 -94 105 426 C ATOM 3321 CG ASP A 483 -45.788 26.289 -27.925 1.00 34.60 C ANISOU 3321 CG ASP A 483 4827 5195 3123 -74 76 496 C ATOM 3322 OD1 ASP A 483 -46.641 26.136 -27.010 1.00 33.06 O ANISOU 3322 OD1 ASP A 483 4685 4897 2979 -33 66 478 O ATOM 3323 OD2 ASP A 483 -45.082 27.317 -28.043 1.00 31.68 O1- ANISOU 3323 OD2 ASP A 483 4426 4830 2781 -101 64 565 O1- ATOM 3324 N GLU A 484 -44.705 22.410 -30.067 1.00 35.49 N ANISOU 3324 N GLU A 484 4857 5611 3017 -88 167 182 N ATOM 3325 CA GLU A 484 -44.756 21.356 -31.077 1.00 37.62 C ANISOU 3325 CA GLU A 484 5079 6004 3213 -109 193 94 C ATOM 3326 C GLU A 484 -45.195 20.041 -30.456 1.00 35.14 C ANISOU 3326 C GLU A 484 4804 5610 2938 -53 200 -14 C ATOM 3327 O GLU A 484 -46.158 19.422 -30.923 1.00 34.55 O ANISOU 3327 O GLU A 484 4724 5570 2832 -58 207 -44 O ATOM 3328 CB GLU A 484 -43.399 21.201 -31.780 1.00 35.81 C ANISOU 3328 CB GLU A 484 4781 5889 2935 -140 215 40 C ATOM 3329 CG GLU A 484 -43.409 21.534 -33.267 1.00 42.07 C ANISOU 3329 CG GLU A 484 5494 6870 3620 -217 229 79 C ATOM 3330 CD GLU A 484 -44.550 20.835 -34.034 1.00 50.96 C ANISOU 3330 CD GLU A 484 6602 8074 4685 -233 237 45 C ATOM 3331 OE1 GLU A 484 -45.511 21.531 -34.467 1.00 42.44 O ANISOU 3331 OE1 GLU A 484 5523 7028 3574 -266 220 151 O ATOM 3332 OE2 GLU A 484 -44.495 19.584 -34.184 1.00 49.10 O1- ANISOU 3332 OE2 GLU A 484 6349 7864 4444 -211 258 -91 O1- ATOM 3333 N ALA A 485 -44.516 19.615 -29.381 1.00 32.75 N ANISOU 3333 N ALA A 485 4539 5198 2706 -1 195 -69 N ATOM 3334 CA ALA A 485 -44.909 18.386 -28.697 1.00 34.13 C ANISOU 3334 CA ALA A 485 4751 5286 2930 50 196 -157 C ATOM 3335 C ALA A 485 -46.403 18.391 -28.359 1.00 35.64 C ANISOU 3335 C ALA A 485 4991 5415 3133 61 186 -112 C ATOM 3336 O ALA A 485 -47.139 17.470 -28.739 1.00 33.46 O ANISOU 3336 O ALA A 485 4708 5161 2844 64 196 -171 O ATOM 3337 CB ALA A 485 -44.064 18.189 -27.442 1.00 35.61 C ANISOU 3337 CB ALA A 485 4979 5355 3194 101 183 -186 C ATOM 3338 N LEU A 486 -46.873 19.444 -27.679 1.00 33.72 N ANISOU 3338 N LEU A 486 4792 5099 2920 65 165 -14 N ATOM 3339 CA LEU A 486 -48.310 19.613 -27.455 1.00 34.63 C ANISOU 3339 CA LEU A 486 4945 5168 3045 69 155 33 C ATOM 3340 C LEU A 486 -49.102 19.441 -28.757 1.00 34.74 C ANISOU 3340 C LEU A 486 4914 5299 2987 26 166 37 C ATOM 3341 O LEU A 486 -50.132 18.757 -28.789 1.00 34.71 O ANISOU 3341 O LEU A 486 4927 5280 2982 37 170 5 O ATOM 3342 CB LEU A 486 -48.583 20.988 -26.836 1.00 31.12 C ANISOU 3342 CB LEU A 486 4528 4658 2637 66 132 138 C ATOM 3343 CG LEU A 486 -48.053 21.281 -25.425 1.00 34.51 C ANISOU 3343 CG LEU A 486 5005 4969 3138 107 118 139 C ATOM 3344 CD1 LEU A 486 -48.189 22.754 -25.079 1.00 31.47 C ANISOU 3344 CD1 LEU A 486 4623 4543 2790 94 96 235 C ATOM 3345 CD2 LEU A 486 -48.731 20.435 -24.346 1.00 32.20 C ANISOU 3345 CD2 LEU A 486 4771 4578 2886 152 116 93 C ATOM 3346 N ALA A 487 -48.631 20.054 -29.845 1.00 32.39 N ANISOU 3346 N ALA A 487 4556 5126 2625 -25 170 77 N ATOM 3347 CA ALA A 487 -49.360 19.967 -31.104 1.00 33.62 C ANISOU 3347 CA ALA A 487 4663 5410 2702 -71 178 89 C ATOM 3348 C ALA A 487 -49.384 18.543 -31.648 1.00 37.39 C ANISOU 3348 C ALA A 487 5108 5951 3147 -65 204 -42 C ATOM 3349 O ALA A 487 -50.370 18.140 -32.281 1.00 36.79 O ANISOU 3349 O ALA A 487 5016 5932 3032 -81 209 -58 O ATOM 3350 CB ALA A 487 -48.751 20.915 -32.138 1.00 33.93 C ANISOU 3350 CB ALA A 487 4638 5580 2673 -134 176 166 C ATOM 3351 N VAL A 488 -48.316 17.771 -31.433 1.00 35.30 N ANISOU 3351 N VAL A 488 4829 5678 2904 -43 219 -140 N ATOM 3352 CA VAL A 488 -48.371 16.354 -31.770 1.00 32.46 C ANISOU 3352 CA VAL A 488 4440 5347 2545 -28 239 -274 C ATOM 3353 C VAL A 488 -49.392 15.646 -30.898 1.00 33.02 C ANISOU 3353 C VAL A 488 4573 5289 2684 19 231 -298 C ATOM 3354 O VAL A 488 -50.317 15.001 -31.409 1.00 32.07 O ANISOU 3354 O VAL A 488 4437 5205 2543 12 240 -341 O ATOM 3355 CB VAL A 488 -46.988 15.698 -31.636 1.00 38.03 C ANISOU 3355 CB VAL A 488 5114 6054 3279 -9 251 -374 C ATOM 3356 CG1 VAL A 488 -46.954 14.398 -32.441 1.00 40.44 C ANISOU 3356 CG1 VAL A 488 5355 6443 3569 -13 275 -518 C ATOM 3357 CG2 VAL A 488 -45.890 16.648 -32.068 1.00 35.00 C ANISOU 3357 CG2 VAL A 488 4692 5756 2850 -47 254 -325 C ATOM 3358 N LEU A 489 -49.238 15.766 -29.563 1.00 36.91 N ANISOU 3358 N LEU A 489 5135 5635 3255 64 214 -269 N ATOM 3359 CA LEU A 489 -50.099 15.068 -28.606 1.00 31.44 C ANISOU 3359 CA LEU A 489 4501 4817 2627 107 206 -287 C ATOM 3360 C LEU A 489 -51.573 15.292 -28.910 1.00 31.68 C ANISOU 3360 C LEU A 489 4547 4860 2631 90 205 -241 C ATOM 3361 O LEU A 489 -52.392 14.373 -28.795 1.00 30.62 O ANISOU 3361 O LEU A 489 4424 4688 2521 106 210 -294 O ATOM 3362 CB LEU A 489 -49.793 15.542 -27.178 1.00 33.40 C ANISOU 3362 CB LEU A 489 4817 4933 2940 144 186 -232 C ATOM 3363 CG LEU A 489 -48.517 15.070 -26.479 1.00 38.02 C ANISOU 3363 CG LEU A 489 5407 5462 3578 177 181 -283 C ATOM 3364 CD1 LEU A 489 -48.100 16.052 -25.389 1.00 36.08 C ANISOU 3364 CD1 LEU A 489 5209 5138 3363 194 162 -206 C ATOM 3365 CD2 LEU A 489 -48.639 13.629 -25.930 1.00 38.06 C ANISOU 3365 CD2 LEU A 489 5426 5387 3647 216 179 -367 C ATOM 3366 N LYS A 490 -51.925 16.512 -29.307 1.00 32.96 N ANISOU 3366 N LYS A 490 4704 5071 2749 56 195 -141 N ATOM 3367 CA LYS A 490 -53.298 16.838 -29.646 1.00 33.20 C ANISOU 3367 CA LYS A 490 4741 5118 2755 38 189 -91 C ATOM 3368 C LYS A 490 -53.807 16.089 -30.880 1.00 34.73 C ANISOU 3368 C LYS A 490 4877 5432 2885 9 207 -156 C ATOM 3369 O LYS A 490 -55.010 16.144 -31.148 1.00 33.90 O ANISOU 3369 O LYS A 490 4777 5338 2764 -1 202 -131 O ATOM 3370 CB LYS A 490 -53.417 18.349 -29.846 1.00 32.90 C ANISOU 3370 CB LYS A 490 4700 5105 2696 7 168 35 C ATOM 3371 CG LYS A 490 -54.684 18.962 -29.287 1.00 35.54 C ANISOU 3371 CG LYS A 490 5078 5359 3065 16 148 106 C ATOM 3372 CD LYS A 490 -54.616 20.458 -29.456 1.00 38.62 C ANISOU 3372 CD LYS A 490 5456 5762 3456 -13 123 225 C ATOM 3373 CE LYS A 490 -55.225 20.856 -30.787 1.00 41.43 C ANISOU 3373 CE LYS A 490 5757 6244 3740 -64 116 279 C ATOM 3374 NZ LYS A 490 -54.520 22.012 -31.404 1.00 41.51 N1+ ANISOU 3374 NZ LYS A 490 5723 6324 3723 -107 99 377 N1+ ATOM 3375 N ARG A 491 -52.943 15.387 -31.624 1.00 33.48 N ANISOU 3375 N ARG A 491 4659 5369 2694 -4 226 -247 N ATOM 3376 CA ARG A 491 -53.367 14.531 -32.730 1.00 37.00 C ANISOU 3376 CA ARG A 491 5041 5931 3086 -28 246 -335 C ATOM 3377 C ARG A 491 -52.855 13.098 -32.553 1.00 39.50 C ANISOU 3377 C ARG A 491 5338 6212 3457 4 263 -480 C ATOM 3378 O ARG A 491 -52.508 12.410 -33.518 1.00 35.73 O ANISOU 3378 O ARG A 491 4784 5850 2941 -17 283 -581 O ATOM 3379 CB ARG A 491 -52.927 15.108 -34.079 1.00 33.08 C ANISOU 3379 CB ARG A 491 4465 5620 2483 -90 254 -313 C ATOM 3380 CG ARG A 491 -51.436 15.422 -34.222 1.00 33.37 C ANISOU 3380 CG ARG A 491 4468 5708 2503 -104 261 -321 C ATOM 3381 CD ARG A 491 -51.191 16.683 -35.093 1.00 35.76 C ANISOU 3381 CD ARG A 491 4729 6143 2715 -166 253 -207 C ATOM 3382 NE ARG A 491 -49.779 17.056 -35.207 1.00 40.72 N ANISOU 3382 NE ARG A 491 5325 6819 3329 -183 260 -207 N ATOM 3383 CZ ARG A 491 -49.331 18.247 -35.596 1.00 39.79 C ANISOU 3383 CZ ARG A 491 5186 6769 3164 -228 249 -93 C ATOM 3384 NH1 ARG A 491 -50.159 19.244 -35.893 1.00 36.89 N1+ ANISOU 3384 NH1 ARG A 491 4825 6423 2767 -260 225 40 N1+ ATOM 3385 NH2 ARG A 491 -48.022 18.434 -35.731 1.00 39.08 N ANISOU 3385 NH2 ARG A 491 5061 6728 3060 -244 260 -112 N ATOM 3386 N THR A 492 -52.836 12.614 -31.315 1.00 41.16 N ANISOU 3386 N THR A 492 5611 6265 3763 55 254 -492 N ATOM 3387 CA THR A 492 -52.372 11.268 -31.025 1.00 41.81 C ANISOU 3387 CA THR A 492 5678 6290 3919 89 262 -614 C ATOM 3388 C THR A 492 -53.443 10.514 -30.254 1.00 46.27 C ANISOU 3388 C THR A 492 6294 6733 4555 122 255 -626 C ATOM 3389 O THR A 492 -54.152 11.095 -29.428 1.00 49.33 O ANISOU 3389 O THR A 492 6750 7036 4958 133 241 -533 O ATOM 3390 CB THR A 492 -51.048 11.280 -30.231 1.00 42.92 C ANISOU 3390 CB THR A 492 5836 6359 4115 118 252 -619 C ATOM 3391 CG2 THR A 492 -50.477 9.881 -30.110 1.00 51.21 C ANISOU 3391 CG2 THR A 492 6852 7363 5244 149 256 -750 C ATOM 3392 OG1 THR A 492 -50.086 12.086 -30.915 1.00 40.81 O ANISOU 3392 OG1 THR A 492 5523 6204 3779 84 258 -598 O ATOM 3393 N ASN A 493 -53.558 9.217 -30.552 1.00 59.70 N ANISOU 3393 N ASN A 493 7953 8428 6302 134 266 -745 N ATOM 3394 CA ASN A 493 -54.453 8.317 -29.824 1.00 63.71 C ANISOU 3394 CA ASN A 493 8501 8815 6893 164 261 -767 C ATOM 3395 C ASN A 493 -53.995 8.126 -28.376 1.00 70.89 C ANISOU 3395 C ASN A 493 9476 9567 7890 207 240 -726 C ATOM 3396 O ASN A 493 -52.810 7.849 -28.138 1.00 70.74 O ANISOU 3396 O ASN A 493 9440 9526 7911 225 232 -763 O ATOM 3397 CB ASN A 493 -54.481 6.965 -30.520 1.00 63.16 C ANISOU 3397 CB ASN A 493 8358 8774 6867 167 275 -912 C ATOM 3398 CG ASN A 493 -55.872 6.493 -30.798 1.00 62.65 C ANISOU 3398 CG ASN A 493 8292 8708 6805 159 284 -934 C ATOM 3399 ND2 ASN A 493 -56.011 5.612 -31.781 1.00 64.72 N ANISOU 3399 ND2 ASN A 493 8472 9049 7070 146 301 -1061 N ATOM 3400 OD1 ASN A 493 -56.822 6.909 -30.135 1.00 59.40 O ANISOU 3400 OD1 ASN A 493 7949 8227 6394 164 275 -845 O ATOM 3401 N PRO A 494 -54.900 8.220 -27.392 1.00 67.04 N ANISOU 3401 N PRO A 494 9061 8977 7435 222 228 -655 N ATOM 3402 CA PRO A 494 -54.523 7.876 -26.003 1.00 71.62 C ANISOU 3402 CA PRO A 494 9698 9417 8096 259 208 -621 C ATOM 3403 C PRO A 494 -54.032 6.443 -25.824 1.00 74.28 C ANISOU 3403 C PRO A 494 10004 9686 8535 286 200 -715 C ATOM 3404 O PRO A 494 -53.460 6.129 -24.775 1.00 73.04 O ANISOU 3404 O PRO A 494 9881 9428 8445 315 178 -689 O ATOM 3405 CB PRO A 494 -55.821 8.122 -25.215 1.00 74.16 C ANISOU 3405 CB PRO A 494 10086 9670 8422 260 204 -545 C ATOM 3406 CG PRO A 494 -56.920 8.084 -26.261 1.00 74.17 C ANISOU 3406 CG PRO A 494 10054 9752 8376 232 223 -575 C ATOM 3407 CD PRO A 494 -56.298 8.678 -27.485 1.00 63.71 C ANISOU 3407 CD PRO A 494 8669 8567 6973 204 234 -599 C ATOM 3408 N ASP A 495 -54.246 5.563 -26.802 1.00 82.70 N ANISOU 3408 N ASP A 495 11001 10803 9619 277 215 -823 N ATOM 3409 CA ASP A 495 -53.660 4.228 -26.754 1.00 84.42 C ANISOU 3409 CA ASP A 495 11171 10958 9946 302 206 -926 C ATOM 3410 C ASP A 495 -52.230 4.221 -27.275 1.00 83.58 C ANISOU 3410 C ASP A 495 11004 10912 9840 305 206 -996 C ATOM 3411 O ASP A 495 -51.398 3.449 -26.787 1.00 85.94 O ANISOU 3411 O ASP A 495 11286 11129 10237 335 185 -1040 O ATOM 3412 CB ASP A 495 -54.508 3.247 -27.571 1.00 85.11 C ANISOU 3412 CB ASP A 495 11201 11071 10067 292 222 -1028 C ATOM 3413 CG ASP A 495 -55.948 3.185 -27.104 1.00 83.68 C ANISOU 3413 CG ASP A 495 11074 10831 9889 287 224 -967 C ATOM 3414 OD1 ASP A 495 -56.277 3.798 -26.062 1.00 78.66 O ANISOU 3414 OD1 ASP A 495 10520 10127 9241 294 212 -852 O ATOM 3415 OD2 ASP A 495 -56.755 2.541 -27.805 1.00 84.70 O1- ANISOU 3415 OD2 ASP A 495 11160 10991 10032 275 240 -1042 O1- ATOM 3416 N ASP A 496 -51.931 5.061 -28.263 1.00 77.59 N ANISOU 3416 N ASP A 496 10207 10298 8975 272 227 -1004 N ATOM 3417 CA ASP A 496 -50.588 5.163 -28.831 1.00 75.80 C ANISOU 3417 CA ASP A 496 9918 10150 8733 268 231 -1070 C ATOM 3418 C ASP A 496 -49.662 5.721 -27.747 1.00 73.90 C ANISOU 3418 C ASP A 496 9734 9827 8516 293 207 -987 C ATOM 3419 O ASP A 496 -49.317 6.903 -27.713 1.00 71.67 O ANISOU 3419 O ASP A 496 9480 9598 8156 276 210 -906 O ATOM 3420 CB ASP A 496 -50.627 6.030 -30.089 1.00 72.03 C ANISOU 3420 CB ASP A 496 9393 9853 8124 218 258 -1073 C ATOM 3421 CG ASP A 496 -49.257 6.244 -30.726 1.00 75.71 C ANISOU 3421 CG ASP A 496 9791 10419 8557 204 268 -1134 C ATOM 3422 OD1 ASP A 496 -48.210 5.924 -30.116 1.00 69.75 O ANISOU 3422 OD1 ASP A 496 9036 9589 7876 235 251 -1160 O ATOM 3423 OD2 ASP A 496 -49.239 6.714 -31.882 1.00 75.18 O1- ANISOU 3423 OD2 ASP A 496 9665 10514 8386 159 291 -1159 O1- ATOM 3424 N THR A 497 -49.250 4.835 -26.836 1.00 69.21 N ANISOU 3424 N THR A 497 9155 9102 8039 333 181 -1007 N ATOM 3425 CA THR A 497 -48.408 5.246 -25.717 1.00 61.48 C ANISOU 3425 CA THR A 497 8230 8041 7089 360 154 -932 C ATOM 3426 C THR A 497 -46.995 5.616 -26.156 1.00 54.60 C ANISOU 3426 C THR A 497 7309 7241 6197 357 157 -978 C ATOM 3427 O THR A 497 -46.396 6.535 -25.591 1.00 49.45 O ANISOU 3427 O THR A 497 6697 6582 5509 360 148 -899 O ATOM 3428 CB THR A 497 -48.348 4.126 -24.692 1.00 63.44 C ANISOU 3428 CB THR A 497 8498 8137 7468 400 121 -939 C ATOM 3429 CG2 THR A 497 -49.707 3.923 -24.030 1.00 59.96 C ANISOU 3429 CG2 THR A 497 8120 7620 7041 400 117 -866 C ATOM 3430 OG1 THR A 497 -47.938 2.927 -25.364 1.00 64.72 O ANISOU 3430 OG1 THR A 497 8573 8297 7720 410 120 -1077 O ATOM 3431 N ALA A 498 -46.441 4.916 -27.148 1.00 58.68 N ANISOU 3431 N ALA A 498 7732 7827 6736 350 171 -1111 N ATOM 3432 CA ALA A 498 -45.051 5.161 -27.525 1.00 54.99 C ANISOU 3432 CA ALA A 498 7211 7425 6259 348 173 -1167 C ATOM 3433 C ALA A 498 -44.875 6.539 -28.162 1.00 52.20 C ANISOU 3433 C ALA A 498 6858 7209 5767 305 198 -1105 C ATOM 3434 O ALA A 498 -43.870 7.217 -27.915 1.00 48.80 O ANISOU 3434 O ALA A 498 6433 6792 5315 306 193 -1072 O ATOM 3435 CB ALA A 498 -44.553 4.055 -28.453 1.00 50.99 C ANISOU 3435 CB ALA A 498 6594 6967 5812 348 184 -1338 C ATOM 3436 N THR A 499 -45.842 6.978 -28.972 1.00 50.07 N ANISOU 3436 N THR A 499 6581 7038 5405 265 223 -1083 N ATOM 3437 CA THR A 499 -45.770 8.329 -29.520 1.00 52.86 C ANISOU 3437 CA THR A 499 6939 7511 5636 221 240 -1002 C ATOM 3438 C THR A 499 -46.033 9.381 -28.445 1.00 49.26 C ANISOU 3438 C THR A 499 6579 6969 5167 233 220 -852 C ATOM 3439 O THR A 499 -45.311 10.380 -28.356 1.00 49.60 O ANISOU 3439 O THR A 499 6630 7046 5168 220 219 -791 O ATOM 3440 CB THR A 499 -46.757 8.494 -30.680 1.00 55.87 C ANISOU 3440 CB THR A 499 7281 8022 5925 175 266 -1013 C ATOM 3441 CG2 THR A 499 -46.710 9.921 -31.242 1.00 49.22 C ANISOU 3441 CG2 THR A 499 6441 7299 4962 126 276 -911 C ATOM 3442 OG1 THR A 499 -46.440 7.553 -31.712 1.00 58.94 O ANISOU 3442 OG1 THR A 499 7568 8507 6318 161 286 -1166 O ATOM 3443 N ARG A 500 -47.075 9.187 -27.629 1.00 48.50 N ANISOU 3443 N ARG A 500 6551 6767 5110 254 206 -795 N ATOM 3444 CA ARG A 500 -47.375 10.165 -26.590 1.00 46.05 C ANISOU 3444 CA ARG A 500 6324 6382 4790 264 190 -667 C ATOM 3445 C ARG A 500 -46.188 10.336 -25.655 1.00 46.71 C ANISOU 3445 C ARG A 500 6431 6395 4923 294 168 -649 C ATOM 3446 O ARG A 500 -45.839 11.461 -25.284 1.00 40.93 O ANISOU 3446 O ARG A 500 5728 5667 4154 287 163 -568 O ATOM 3447 CB ARG A 500 -48.620 9.744 -25.822 1.00 42.91 C ANISOU 3447 CB ARG A 500 5987 5884 4433 282 179 -628 C ATOM 3448 CG ARG A 500 -49.885 9.752 -26.662 1.00 48.83 C ANISOU 3448 CG ARG A 500 6722 6701 5130 252 198 -630 C ATOM 3449 CD ARG A 500 -51.112 9.437 -25.823 1.00 52.36 C ANISOU 3449 CD ARG A 500 7232 7047 5616 268 189 -586 C ATOM 3450 NE ARG A 500 -51.740 10.644 -25.301 1.00 50.67 N ANISOU 3450 NE ARG A 500 7076 6819 5358 258 184 -472 N ATOM 3451 CZ ARG A 500 -51.660 11.041 -24.037 1.00 45.71 C ANISOU 3451 CZ ARG A 500 6511 6097 4761 280 165 -404 C ATOM 3452 NH1 ARG A 500 -50.921 10.386 -23.152 1.00 39.45 N1+ ANISOU 3452 NH1 ARG A 500 5733 5220 4034 313 148 -423 N1+ ATOM 3453 NH2 ARG A 500 -52.324 12.129 -23.656 1.00 41.74 N ANISOU 3453 NH2 ARG A 500 6049 5588 4223 268 162 -316 N ATOM 3454 N GLN A 501 -45.517 9.232 -25.311 1.00 45.65 N ANISOU 3454 N GLN A 501 6274 6196 4875 328 154 -728 N ATOM 3455 CA GLN A 501 -44.347 9.324 -24.450 1.00 42.24 C ANISOU 3455 CA GLN A 501 5857 5699 4491 358 130 -717 C ATOM 3456 C GLN A 501 -43.245 10.134 -25.113 1.00 46.04 C ANISOU 3456 C GLN A 501 6293 6283 4917 334 144 -731 C ATOM 3457 O GLN A 501 -42.631 10.994 -24.465 1.00 43.42 O ANISOU 3457 O GLN A 501 5994 5928 4575 341 132 -665 O ATOM 3458 CB GLN A 501 -43.851 7.924 -24.075 1.00 43.97 C ANISOU 3458 CB GLN A 501 6051 5833 4824 397 108 -802 C ATOM 3459 CG GLN A 501 -42.875 7.889 -22.869 1.00 42.93 C ANISOU 3459 CG GLN A 501 5951 5604 4756 435 72 -769 C ATOM 3460 CD GLN A 501 -43.401 8.607 -21.618 1.00 40.47 C ANISOU 3460 CD GLN A 501 5730 5221 4426 444 54 -644 C ATOM 3461 NE2 GLN A 501 -42.572 9.466 -21.051 1.00 38.09 N ANISOU 3461 NE2 GLN A 501 5449 4919 4105 451 43 -596 N ATOM 3462 OE1 GLN A 501 -44.532 8.395 -21.182 1.00 38.76 O ANISOU 3462 OE1 GLN A 501 5558 4956 4214 444 52 -597 O ATOM 3463 N GLU A 502 -42.995 9.890 -26.412 1.00 53.23 N ANISOU 3463 N GLU A 502 7123 7313 5788 304 171 -818 N ATOM 3464 CA GLU A 502 -42.001 10.667 -27.155 1.00 54.62 C ANISOU 3464 CA GLU A 502 7249 7606 5900 271 188 -829 C ATOM 3465 C GLU A 502 -42.201 12.161 -26.931 1.00 52.74 C ANISOU 3465 C GLU A 502 7058 7389 5592 247 188 -698 C ATOM 3466 O GLU A 502 -41.232 12.910 -26.747 1.00 53.52 O ANISOU 3466 O GLU A 502 7153 7503 5680 242 185 -668 O ATOM 3467 CB GLU A 502 -42.078 10.332 -28.649 1.00 57.15 C ANISOU 3467 CB GLU A 502 7478 8076 6159 228 221 -922 C ATOM 3468 CG GLU A 502 -40.864 10.773 -29.485 1.00 63.15 C ANISOU 3468 CG GLU A 502 8164 8966 6865 194 240 -970 C ATOM 3469 CD GLU A 502 -40.935 10.339 -30.954 1.00 72.93 C ANISOU 3469 CD GLU A 502 9304 10369 8039 148 274 -1075 C ATOM 3470 OE1 GLU A 502 -41.927 9.686 -31.353 1.00 71.09 O ANISOU 3470 OE1 GLU A 502 9059 10148 7805 145 281 -1117 O ATOM 3471 OE2 GLU A 502 -39.985 10.645 -31.715 1.00 75.40 O1- ANISOU 3471 OE2 GLU A 502 9546 10804 8297 114 294 -1122 O1- ATOM 3472 N GLN A 503 -43.461 12.599 -26.882 1.00 44.01 N ANISOU 3472 N GLN A 503 5996 6273 4451 233 190 -620 N ATOM 3473 CA GLN A 503 -43.764 14.004 -26.668 1.00 39.89 C ANISOU 3473 CA GLN A 503 5515 5761 3880 211 186 -498 C ATOM 3474 C GLN A 503 -43.571 14.417 -25.221 1.00 40.09 C ANISOU 3474 C GLN A 503 5611 5660 3962 249 160 -433 C ATOM 3475 O GLN A 503 -43.032 15.496 -24.954 1.00 40.06 O ANISOU 3475 O GLN A 503 5617 5660 3943 240 154 -370 O ATOM 3476 CB GLN A 503 -45.189 14.294 -27.115 1.00 43.65 C ANISOU 3476 CB GLN A 503 6007 6268 4309 185 194 -445 C ATOM 3477 CG GLN A 503 -45.440 13.921 -28.563 1.00 41.24 C ANISOU 3477 CG GLN A 503 5628 6103 3937 143 219 -506 C ATOM 3478 CD GLN A 503 -44.308 14.348 -29.460 1.00 40.03 C ANISOU 3478 CD GLN A 503 5405 6076 3730 106 235 -531 C ATOM 3479 NE2 GLN A 503 -43.751 13.405 -30.209 1.00 42.39 N ANISOU 3479 NE2 GLN A 503 5632 6450 4024 99 253 -655 N ATOM 3480 OE1 GLN A 503 -43.929 15.514 -29.471 1.00 38.04 O ANISOU 3480 OE1 GLN A 503 5158 5851 3442 81 231 -443 O ATOM 3481 N PHE A 504 -44.005 13.582 -24.276 1.00 41.67 N ANISOU 3481 N PHE A 504 5857 5751 4226 289 143 -448 N ATOM 3482 CA PHE A 504 -43.798 13.909 -22.869 1.00 39.52 C ANISOU 3482 CA PHE A 504 5645 5372 3998 323 117 -392 C ATOM 3483 C PHE A 504 -42.319 14.079 -22.582 1.00 40.37 C ANISOU 3483 C PHE A 504 5732 5477 4131 338 106 -417 C ATOM 3484 O PHE A 504 -41.924 14.957 -21.803 1.00 42.03 O ANISOU 3484 O PHE A 504 5973 5653 4345 346 93 -358 O ATOM 3485 CB PHE A 504 -44.395 12.829 -21.971 1.00 37.05 C ANISOU 3485 CB PHE A 504 5373 4955 3748 358 99 -407 C ATOM 3486 CG PHE A 504 -45.884 12.838 -21.943 1.00 35.26 C ANISOU 3486 CG PHE A 504 5181 4713 3501 346 106 -366 C ATOM 3487 CD1 PHE A 504 -46.578 14.002 -22.173 1.00 33.27 C ANISOU 3487 CD1 PHE A 504 4945 4501 3194 317 116 -294 C ATOM 3488 CD2 PHE A 504 -46.592 11.675 -21.723 1.00 39.40 C ANISOU 3488 CD2 PHE A 504 5717 5182 4069 362 102 -400 C ATOM 3489 CE1 PHE A 504 -47.957 14.019 -22.153 1.00 34.94 C ANISOU 3489 CE1 PHE A 504 5186 4699 3391 307 121 -261 C ATOM 3490 CE2 PHE A 504 -47.971 11.685 -21.724 1.00 40.26 C ANISOU 3490 CE2 PHE A 504 5856 5282 4161 349 111 -367 C ATOM 3491 CZ PHE A 504 -48.650 12.865 -21.940 1.00 37.66 C ANISOU 3491 CZ PHE A 504 5543 4994 3771 322 121 -299 C ATOM 3492 N ASP A 505 -41.483 13.269 -23.228 1.00 36.67 N ANISOU 3492 N ASP A 505 5203 5048 3681 341 113 -511 N ATOM 3493 CA ASP A 505 -40.052 13.381 -23.010 1.00 37.63 C ANISOU 3493 CA ASP A 505 5298 5170 3829 355 103 -544 C ATOM 3494 C ASP A 505 -39.538 14.756 -23.417 1.00 38.98 C ANISOU 3494 C ASP A 505 5453 5417 3939 320 117 -490 C ATOM 3495 O ASP A 505 -38.719 15.348 -22.706 1.00 40.87 O ANISOU 3495 O ASP A 505 5708 5621 4200 335 102 -462 O ATOM 3496 CB ASP A 505 -39.329 12.279 -23.777 1.00 43.69 C ANISOU 3496 CB ASP A 505 5992 5979 4629 360 111 -667 C ATOM 3497 CG ASP A 505 -39.626 10.908 -23.238 1.00 43.16 C ANISOU 3497 CG ASP A 505 5935 5815 4649 401 89 -720 C ATOM 3498 OD1 ASP A 505 -40.458 10.797 -22.310 1.00 44.05 O ANISOU 3498 OD1 ASP A 505 6114 5839 4785 420 70 -654 O ATOM 3499 OD2 ASP A 505 -39.037 9.941 -23.749 1.00 43.34 O1- ANISOU 3499 OD2 ASP A 505 5895 5852 4721 411 89 -828 O1- ATOM 3500 N VAL A 506 -40.005 15.285 -24.552 1.00 37.24 N ANISOU 3500 N VAL A 506 5199 5303 3647 272 143 -471 N ATOM 3501 CA VAL A 506 -39.547 16.605 -24.979 1.00 36.88 C ANISOU 3501 CA VAL A 506 5134 5328 3551 233 153 -407 C ATOM 3502 C VAL A 506 -40.040 17.668 -24.010 1.00 37.84 C ANISOU 3502 C VAL A 506 5319 5372 3686 241 134 -301 C ATOM 3503 O VAL A 506 -39.291 18.569 -23.608 1.00 38.05 O ANISOU 3503 O VAL A 506 5347 5386 3724 240 126 -261 O ATOM 3504 CB VAL A 506 -40.008 16.905 -26.420 1.00 40.18 C ANISOU 3504 CB VAL A 506 5499 5883 3886 174 180 -398 C ATOM 3505 CG1 VAL A 506 -39.747 18.384 -26.785 1.00 32.05 C ANISOU 3505 CG1 VAL A 506 4455 4913 2810 129 184 -300 C ATOM 3506 CG2 VAL A 506 -39.332 15.972 -27.395 1.00 32.20 C ANISOU 3506 CG2 VAL A 506 4410 4968 2856 160 201 -516 C ATOM 3507 N ILE A 507 -41.305 17.571 -23.613 1.00 38.76 N ANISOU 3507 N ILE A 507 5484 5436 3809 250 128 -262 N ATOM 3508 CA ILE A 507 -41.877 18.515 -22.665 1.00 35.66 C ANISOU 3508 CA ILE A 507 5145 4969 3433 259 111 -176 C ATOM 3509 C ILE A 507 -41.152 18.438 -21.325 1.00 36.49 C ANISOU 3509 C ILE A 507 5286 4984 3596 302 88 -185 C ATOM 3510 O ILE A 507 -40.957 19.455 -20.641 1.00 35.61 O ANISOU 3510 O ILE A 507 5194 4838 3499 305 76 -132 O ATOM 3511 CB ILE A 507 -43.382 18.233 -22.538 1.00 35.49 C ANISOU 3511 CB ILE A 507 5162 4916 3406 260 111 -150 C ATOM 3512 CG1 ILE A 507 -44.065 18.642 -23.845 1.00 33.89 C ANISOU 3512 CG1 ILE A 507 4922 4811 3143 212 129 -120 C ATOM 3513 CG2 ILE A 507 -43.986 18.918 -21.310 1.00 32.74 C ANISOU 3513 CG2 ILE A 507 4872 4478 3091 279 92 -87 C ATOM 3514 CD1 ILE A 507 -45.407 18.042 -24.041 1.00 34.95 C ANISOU 3514 CD1 ILE A 507 5076 4938 3266 211 134 -125 C ATOM 3515 N GLN A 508 -40.717 17.247 -20.933 1.00 35.69 N ANISOU 3515 N GLN A 508 5188 4844 3530 337 79 -254 N ATOM 3516 CA GLN A 508 -40.152 17.152 -19.592 1.00 37.54 C ANISOU 3516 CA GLN A 508 5458 4993 3813 377 52 -251 C ATOM 3517 C GLN A 508 -38.701 17.592 -19.576 1.00 38.47 C ANISOU 3517 C GLN A 508 5542 5133 3943 381 48 -273 C ATOM 3518 O GLN A 508 -38.270 18.268 -18.632 1.00 37.49 O ANISOU 3518 O GLN A 508 5440 4965 3839 396 30 -241 O ATOM 3519 CB GLN A 508 -40.305 15.734 -19.041 1.00 34.93 C ANISOU 3519 CB GLN A 508 5146 4599 3528 413 35 -297 C ATOM 3520 CG GLN A 508 -41.733 15.397 -18.711 1.00 31.05 C ANISOU 3520 CG GLN A 508 4699 4068 3032 413 36 -264 C ATOM 3521 CD GLN A 508 -41.916 13.948 -18.443 1.00 36.33 C ANISOU 3521 CD GLN A 508 5372 4683 3747 439 22 -309 C ATOM 3522 NE2 GLN A 508 -43.155 13.544 -18.202 1.00 33.65 N ANISOU 3522 NE2 GLN A 508 5068 4311 3408 437 24 -284 N ATOM 3523 OE1 GLN A 508 -40.953 13.181 -18.454 1.00 39.86 O ANISOU 3523 OE1 GLN A 508 5791 5117 4239 461 9 -367 O ATOM 3524 N ALA A 509 -37.945 17.246 -20.623 1.00 37.50 N ANISOU 3524 N ALA A 509 5359 5082 3806 364 64 -333 N ATOM 3525 CA ALA A 509 -36.537 17.616 -20.652 1.00 38.88 C ANISOU 3525 CA ALA A 509 5497 5283 3994 366 62 -361 C ATOM 3526 C ALA A 509 -36.361 19.130 -20.711 1.00 41.97 C ANISOU 3526 C ALA A 509 5885 5703 4360 335 69 -289 C ATOM 3527 O ALA A 509 -35.353 19.658 -20.230 1.00 44.19 O ANISOU 3527 O ALA A 509 6156 5969 4665 345 59 -290 O ATOM 3528 CB ALA A 509 -35.851 16.932 -21.821 1.00 38.51 C ANISOU 3528 CB ALA A 509 5379 5320 3933 348 83 -448 C ATOM 3529 N ALA A 510 -37.335 19.840 -21.287 1.00 40.54 N ANISOU 3529 N ALA A 510 5707 5558 4139 298 83 -225 N ATOM 3530 CA ALA A 510 -37.359 21.295 -21.203 1.00 39.79 C ANISOU 3530 CA ALA A 510 5612 5466 4041 272 81 -144 C ATOM 3531 C ALA A 510 -37.791 21.753 -19.814 1.00 39.33 C ANISOU 3531 C ALA A 510 5610 5309 4026 304 57 -106 C ATOM 3532 O ALA A 510 -37.223 22.703 -19.258 1.00 38.22 O ANISOU 3532 O ALA A 510 5466 5143 3913 306 47 -80 O ATOM 3533 CB ALA A 510 -38.305 21.870 -22.255 1.00 30.69 C ANISOU 3533 CB ALA A 510 4441 4379 2840 223 97 -83 C ATOM 3534 N ILE A 511 -38.804 21.098 -19.245 1.00 34.50 N ANISOU 3534 N ILE A 511 5044 4645 3419 327 49 -107 N ATOM 3535 CA ILE A 511 -39.397 21.597 -18.011 1.00 35.46 C ANISOU 3535 CA ILE A 511 5212 4691 3568 348 31 -70 C ATOM 3536 C ILE A 511 -38.449 21.410 -16.838 1.00 36.52 C ANISOU 3536 C ILE A 511 5361 4775 3738 386 9 -101 C ATOM 3537 O ILE A 511 -38.296 22.320 -16.016 1.00 35.87 O ANISOU 3537 O ILE A 511 5288 4661 3679 392 -3 -77 O ATOM 3538 CB ILE A 511 -40.768 20.939 -17.768 1.00 37.54 C ANISOU 3538 CB ILE A 511 5518 4924 3822 355 31 -61 C ATOM 3539 CG1 ILE A 511 -41.816 21.737 -18.519 1.00 38.45 C ANISOU 3539 CG1 ILE A 511 5625 5070 3915 318 43 -5 C ATOM 3540 CG2 ILE A 511 -41.124 20.914 -16.316 1.00 30.67 C ANISOU 3540 CG2 ILE A 511 4695 3981 2977 386 11 -53 C ATOM 3541 CD1 ILE A 511 -41.676 23.196 -18.243 1.00 33.97 C ANISOU 3541 CD1 ILE A 511 5045 4488 3373 303 35 47 C ATOM 3542 N VAL A 512 -37.785 20.247 -16.745 1.00 36.88 N ANISOU 3542 N VAL A 512 5404 4816 3794 413 1 -159 N ATOM 3543 CA VAL A 512 -36.841 20.037 -15.648 1.00 35.69 C ANISOU 3543 CA VAL A 512 5263 4620 3676 449 -25 -184 C ATOM 3544 C VAL A 512 -35.697 21.027 -15.743 1.00 35.69 C ANISOU 3544 C VAL A 512 5227 4646 3689 440 -23 -187 C ATOM 3545 O VAL A 512 -35.110 21.414 -14.729 1.00 38.90 O ANISOU 3545 O VAL A 512 5643 5019 4120 462 -44 -188 O ATOM 3546 CB VAL A 512 -36.315 18.578 -15.602 1.00 37.01 C ANISOU 3546 CB VAL A 512 5425 4770 3866 479 -39 -242 C ATOM 3547 CG1 VAL A 512 -37.443 17.599 -15.289 1.00 34.41 C ANISOU 3547 CG1 VAL A 512 5135 4401 3539 490 -45 -233 C ATOM 3548 CG2 VAL A 512 -35.566 18.204 -16.868 1.00 35.55 C ANISOU 3548 CG2 VAL A 512 5183 4647 3677 463 -19 -298 C ATOM 3549 N GLU A 513 -35.375 21.473 -16.945 1.00 38.55 N ANISOU 3549 N GLU A 513 5543 5072 4031 404 0 -186 N ATOM 3550 CA GLU A 513 -34.254 22.387 -17.099 1.00 42.89 C ANISOU 3550 CA GLU A 513 6053 5648 4594 391 3 -187 C ATOM 3551 C GLU A 513 -34.673 23.838 -16.862 1.00 40.31 C ANISOU 3551 C GLU A 513 5729 5307 4281 368 3 -120 C ATOM 3552 O GLU A 513 -33.996 24.574 -16.135 1.00 41.55 O ANISOU 3552 O GLU A 513 5879 5436 4473 379 -10 -120 O ATOM 3553 CB GLU A 513 -33.636 22.198 -18.489 1.00 44.00 C ANISOU 3553 CB GLU A 513 6137 5875 4706 358 28 -215 C ATOM 3554 CG GLU A 513 -32.527 23.176 -18.779 1.00 52.71 C ANISOU 3554 CG GLU A 513 7194 7014 5819 334 35 -208 C ATOM 3555 CD GLU A 513 -31.174 22.520 -18.683 1.00 64.06 C ANISOU 3555 CD GLU A 513 8601 8463 7276 358 30 -287 C ATOM 3556 OE1 GLU A 513 -30.197 23.103 -19.201 1.00 70.75 O ANISOU 3556 OE1 GLU A 513 9399 9360 8123 333 43 -296 O ATOM 3557 OE2 GLU A 513 -31.095 21.418 -18.091 1.00 65.75 O1- ANISOU 3557 OE2 GLU A 513 8837 8633 7510 401 11 -338 O1- ATOM 3558 N ASP A 514 -35.793 24.267 -17.465 1.00 37.79 N ANISOU 3558 N ASP A 514 5414 5003 3942 337 15 -67 N ATOM 3559 CA ASP A 514 -36.240 25.652 -17.331 1.00 35.04 C ANISOU 3559 CA ASP A 514 5058 4635 3621 314 12 -3 C ATOM 3560 C ASP A 514 -37.021 25.896 -16.046 1.00 33.76 C ANISOU 3560 C ASP A 514 4939 4400 3488 341 -7 4 C ATOM 3561 O ASP A 514 -36.952 26.998 -15.490 1.00 31.47 O ANISOU 3561 O ASP A 514 4637 4076 3243 338 -17 25 O ATOM 3562 CB ASP A 514 -37.102 26.067 -18.521 1.00 29.39 C ANISOU 3562 CB ASP A 514 4323 3967 2878 267 27 57 C ATOM 3563 CG ASP A 514 -37.374 27.563 -18.535 1.00 29.50 C ANISOU 3563 CG ASP A 514 4314 3958 2937 239 19 128 C ATOM 3564 OD1 ASP A 514 -36.388 28.333 -18.502 1.00 29.75 O ANISOU 3564 OD1 ASP A 514 4310 3991 3003 229 16 135 O ATOM 3565 OD2 ASP A 514 -38.558 27.974 -18.554 1.00 29.38 O1- ANISOU 3565 OD2 ASP A 514 4312 3918 2932 228 13 175 O1- ATOM 3566 N MET A 515 -37.772 24.908 -15.579 1.00 31.29 N ANISOU 3566 N MET A 515 4670 4065 3154 365 -11 -16 N ATOM 3567 CA MET A 515 -38.497 25.037 -14.326 1.00 32.31 C ANISOU 3567 CA MET A 515 4837 4140 3300 388 -26 -14 C ATOM 3568 C MET A 515 -39.234 26.365 -14.225 1.00 30.05 C ANISOU 3568 C MET A 515 4538 3831 3048 366 -27 29 C ATOM 3569 O MET A 515 -38.863 27.223 -13.421 1.00 31.94 O ANISOU 3569 O MET A 515 4764 4041 3330 374 -40 21 O ATOM 3570 CB MET A 515 -37.530 24.878 -13.150 1.00 34.07 C ANISOU 3570 CB MET A 515 5068 4338 3541 423 -46 -56 C ATOM 3571 CG MET A 515 -38.214 24.447 -11.884 1.00 33.21 C ANISOU 3571 CG MET A 515 5001 4193 3424 447 -62 -65 C ATOM 3572 SD MET A 515 -37.065 23.922 -10.600 1.00 38.20 S ANISOU 3572 SD MET A 515 5642 4812 4062 487 -90 -108 S ATOM 3573 CE MET A 515 -37.175 22.150 -10.847 1.00 30.35 C ANISOU 3573 CE MET A 515 4677 3814 3040 505 -96 -118 C ATOM 3574 N PRO A 516 -40.268 26.592 -15.020 1.00 31.36 N ANISOU 3574 N PRO A 516 4701 4009 3204 339 -17 73 N ATOM 3575 CA PRO A 516 -41.033 27.829 -14.833 1.00 32.12 C ANISOU 3575 CA PRO A 516 4783 4073 3349 322 -25 112 C ATOM 3576 C PRO A 516 -41.916 27.795 -13.594 1.00 30.22 C ANISOU 3576 C PRO A 516 4576 3787 3121 344 -34 88 C ATOM 3577 O PRO A 516 -42.249 28.854 -13.048 1.00 29.94 O ANISOU 3577 O PRO A 516 4521 3716 3140 340 -44 92 O ATOM 3578 CB PRO A 516 -41.847 27.929 -16.130 1.00 30.54 C ANISOU 3578 CB PRO A 516 4568 3906 3128 286 -14 167 C ATOM 3579 CG PRO A 516 -41.961 26.527 -16.603 1.00 30.56 C ANISOU 3579 CG PRO A 516 4597 3948 3065 293 1 140 C ATOM 3580 CD PRO A 516 -40.669 25.873 -16.239 1.00 30.48 C ANISOU 3580 CD PRO A 516 4589 3948 3046 318 0 88 C ATOM 3581 N TYR A 517 -42.304 26.609 -13.143 1.00 29.85 N ANISOU 3581 N TYR A 517 4573 3742 3028 365 -31 61 N ATOM 3582 CA TYR A 517 -43.089 26.415 -11.926 1.00 29.40 C ANISOU 3582 CA TYR A 517 4547 3656 2967 382 -38 38 C ATOM 3583 C TYR A 517 -42.235 25.590 -10.982 1.00 29.44 C ANISOU 3583 C TYR A 517 4575 3664 2949 412 -49 -1 C ATOM 3584 O TYR A 517 -42.148 24.372 -11.150 1.00 33.53 O ANISOU 3584 O TYR A 517 5119 4192 3430 424 -48 -7 O ATOM 3585 CB TYR A 517 -44.419 25.723 -12.204 1.00 27.58 C ANISOU 3585 CB TYR A 517 4349 3427 2704 375 -28 54 C ATOM 3586 CG TYR A 517 -45.252 26.439 -13.255 1.00 32.04 C ANISOU 3586 CG TYR A 517 4891 3996 3289 345 -20 98 C ATOM 3587 CD1 TYR A 517 -45.025 26.248 -14.633 1.00 29.54 C ANISOU 3587 CD1 TYR A 517 4555 3718 2950 324 -10 129 C ATOM 3588 CD2 TYR A 517 -46.250 27.332 -12.879 1.00 29.76 C ANISOU 3588 CD2 TYR A 517 4592 3677 3040 335 -26 108 C ATOM 3589 CE1 TYR A 517 -45.781 26.921 -15.586 1.00 30.71 C ANISOU 3589 CE1 TYR A 517 4678 3877 3112 293 -8 180 C ATOM 3590 CE2 TYR A 517 -47.004 28.005 -13.835 1.00 32.22 C ANISOU 3590 CE2 TYR A 517 4877 3987 3376 308 -25 156 C ATOM 3591 CZ TYR A 517 -46.771 27.794 -15.180 1.00 31.87 C ANISOU 3591 CZ TYR A 517 4818 3984 3305 286 -18 197 C ATOM 3592 OH TYR A 517 -47.530 28.481 -16.103 1.00 30.98 O ANISOU 3592 OH TYR A 517 4678 3877 3216 257 -22 254 O ATOM 3593 N ILE A 518 -41.619 26.243 -9.998 1.00 28.74 N ANISOU 3593 N ILE A 518 4471 3565 2886 425 -63 -28 N ATOM 3594 CA ILE A 518 -40.690 25.597 -9.062 1.00 31.39 C ANISOU 3594 CA ILE A 518 4819 3906 3201 453 -79 -61 C ATOM 3595 C ILE A 518 -41.451 24.642 -8.148 1.00 29.23 C ANISOU 3595 C ILE A 518 4588 3632 2884 464 -86 -64 C ATOM 3596 O ILE A 518 -42.324 25.067 -7.377 1.00 31.22 O ANISOU 3596 O ILE A 518 4845 3883 3134 457 -85 -70 O ATOM 3597 CB ILE A 518 -39.885 26.643 -8.263 1.00 28.84 C ANISOU 3597 CB ILE A 518 4461 3580 2916 460 -92 -92 C ATOM 3598 CG1 ILE A 518 -39.324 27.708 -9.218 1.00 32.25 C ANISOU 3598 CG1 ILE A 518 4847 4006 3402 441 -85 -78 C ATOM 3599 CG2 ILE A 518 -38.738 26.004 -7.568 1.00 28.73 C ANISOU 3599 CG2 ILE A 518 4453 3579 2884 487 -111 -120 C ATOM 3600 CD1 ILE A 518 -38.691 28.885 -8.553 1.00 33.76 C ANISOU 3600 CD1 ILE A 518 4996 4184 3648 444 -96 -108 C ATOM 3601 N PRO A 519 -41.165 23.344 -8.210 1.00 30.67 N ANISOU 3601 N PRO A 519 4797 3817 3037 479 -93 -59 N ATOM 3602 CA PRO A 519 -41.954 22.369 -7.437 1.00 27.94 C ANISOU 3602 CA PRO A 519 4492 3469 2656 484 -100 -48 C ATOM 3603 C PRO A 519 -41.724 22.504 -5.942 1.00 30.14 C ANISOU 3603 C PRO A 519 4775 3763 2916 494 -121 -62 C ATOM 3604 O PRO A 519 -40.583 22.566 -5.477 1.00 29.86 O ANISOU 3604 O PRO A 519 4723 3735 2886 512 -141 -80 O ATOM 3605 CB PRO A 519 -41.449 21.013 -7.951 1.00 29.73 C ANISOU 3605 CB PRO A 519 4734 3686 2878 499 -108 -42 C ATOM 3606 CG PRO A 519 -40.840 21.321 -9.329 1.00 31.09 C ANISOU 3606 CG PRO A 519 4874 3866 3073 492 -92 -52 C ATOM 3607 CD PRO A 519 -40.293 22.709 -9.217 1.00 30.94 C ANISOU 3607 CD PRO A 519 4821 3856 3078 485 -91 -62 C ATOM 3608 N ILE A 520 -42.824 22.526 -5.184 1.00 34.36 N ANISOU 3608 N ILE A 520 5325 4307 3422 481 -117 -56 N ATOM 3609 CA ILE A 520 -42.760 22.387 -3.729 1.00 28.45 C ANISOU 3609 CA ILE A 520 4583 3590 2636 484 -136 -65 C ATOM 3610 C ILE A 520 -43.033 20.922 -3.439 1.00 28.91 C ANISOU 3610 C ILE A 520 4681 3644 2660 488 -150 -24 C ATOM 3611 O ILE A 520 -42.101 20.123 -3.346 1.00 29.97 O ANISOU 3611 O ILE A 520 4820 3769 2797 508 -175 -11 O ATOM 3612 CB ILE A 520 -43.750 23.322 -2.998 1.00 28.49 C ANISOU 3612 CB ILE A 520 4574 3620 2632 464 -124 -91 C ATOM 3613 CG1 ILE A 520 -43.411 24.788 -3.269 1.00 28.46 C ANISOU 3613 CG1 ILE A 520 4523 3608 2683 462 -116 -132 C ATOM 3614 CG2 ILE A 520 -43.741 23.070 -1.489 1.00 33.42 C ANISOU 3614 CG2 ILE A 520 5201 4296 3201 461 -142 -100 C ATOM 3615 CD1 ILE A 520 -44.473 25.761 -2.854 1.00 28.51 C ANISOU 3615 CD1 ILE A 520 4505 3622 2705 442 -101 -164 C ATOM 3616 N LEU A 521 -44.306 20.546 -3.340 1.00 30.89 N ANISOU 3616 N LEU A 521 4956 3896 2886 468 -136 -3 N ATOM 3617 CA LEU A 521 -44.682 19.174 -3.021 1.00 31.02 C ANISOU 3617 CA LEU A 521 5006 3904 2876 467 -149 41 C ATOM 3618 C LEU A 521 -46.046 18.904 -3.628 1.00 28.46 C ANISOU 3618 C LEU A 521 4702 3563 2550 447 -122 55 C ATOM 3619 O LEU A 521 -46.794 19.826 -3.952 1.00 28.23 O ANISOU 3619 O LEU A 521 4660 3539 2527 432 -97 32 O ATOM 3620 CB LEU A 521 -44.739 18.923 -1.496 1.00 34.03 C ANISOU 3620 CB LEU A 521 5393 4332 3203 458 -172 59 C ATOM 3621 CG LEU A 521 -43.495 18.497 -0.717 1.00 32.22 C ANISOU 3621 CG LEU A 521 5158 4121 2964 478 -212 74 C ATOM 3622 CD1 LEU A 521 -43.854 18.110 0.712 1.00 31.32 C ANISOU 3622 CD1 LEU A 521 5052 4064 2783 458 -232 107 C ATOM 3623 CD2 LEU A 521 -42.793 17.356 -1.434 1.00 33.56 C ANISOU 3623 CD2 LEU A 521 5339 4234 3177 501 -232 102 C ATOM 3624 N THR A 522 -46.374 17.626 -3.749 1.00 29.21 N ANISOU 3624 N THR A 522 4823 3633 2642 446 -130 93 N ATOM 3625 CA THR A 522 -47.715 17.220 -4.164 1.00 32.37 C ANISOU 3625 CA THR A 522 5242 4019 3036 426 -106 108 C ATOM 3626 C THR A 522 -48.705 17.479 -3.043 1.00 30.37 C ANISOU 3626 C THR A 522 4998 3808 2734 399 -99 116 C ATOM 3627 O THR A 522 -48.590 16.897 -1.959 1.00 29.24 O ANISOU 3627 O THR A 522 4865 3690 2554 392 -121 148 O ATOM 3628 CB THR A 522 -47.736 15.741 -4.565 1.00 32.04 C ANISOU 3628 CB THR A 522 5221 3936 3018 433 -118 141 C ATOM 3629 CG2 THR A 522 -49.141 15.306 -4.994 1.00 30.34 C ANISOU 3629 CG2 THR A 522 5023 3706 2798 411 -93 153 C ATOM 3630 OG1 THR A 522 -46.856 15.559 -5.671 1.00 32.43 O ANISOU 3630 OG1 THR A 522 5252 3956 3112 455 -121 118 O ATOM 3631 N GLY A 523 -49.684 18.343 -3.304 1.00 30.89 N ANISOU 3631 N GLY A 523 5054 3884 2798 381 -71 88 N ATOM 3632 CA GLY A 523 -50.693 18.643 -2.291 1.00 31.14 C ANISOU 3632 CA GLY A 523 5087 3961 2786 353 -60 82 C ATOM 3633 C GLY A 523 -51.727 17.532 -2.183 1.00 31.50 C ANISOU 3633 C GLY A 523 5162 3998 2808 333 -53 123 C ATOM 3634 O GLY A 523 -52.184 16.964 -3.181 1.00 32.55 O ANISOU 3634 O GLY A 523 5310 4088 2971 335 -41 135 O ATOM 3635 N GLY A 524 -52.066 17.189 -0.941 1.00 29.92 N ANISOU 3635 N GLY A 524 4969 3847 2553 310 -60 145 N ATOM 3636 CA GLY A 524 -53.127 16.242 -0.678 1.00 32.63 C ANISOU 3636 CA GLY A 524 5336 4191 2870 283 -52 187 C ATOM 3637 C GLY A 524 -54.410 16.936 -0.277 1.00 33.56 C ANISOU 3637 C GLY A 524 5442 4354 2956 251 -21 151 C ATOM 3638 O GLY A 524 -54.458 17.657 0.728 1.00 34.25 O ANISOU 3638 O GLY A 524 5506 4509 3000 234 -20 119 O ATOM 3639 N THR A 525 -55.457 16.740 -1.078 1.00 30.75 N ANISOU 3639 N THR A 525 5097 3963 2624 242 3 147 N ATOM 3640 CA THR A 525 -56.798 17.180 -0.710 1.00 32.24 C ANISOU 3640 CA THR A 525 5276 4188 2786 209 32 116 C ATOM 3641 C THR A 525 -57.345 16.295 0.404 1.00 32.10 C ANISOU 3641 C THR A 525 5273 4220 2705 173 30 162 C ATOM 3642 O THR A 525 -57.309 15.069 0.298 1.00 33.18 O ANISOU 3642 O THR A 525 5437 4323 2846 170 17 227 O ATOM 3643 CB THR A 525 -57.733 17.127 -1.917 1.00 32.96 C ANISOU 3643 CB THR A 525 5374 4228 2922 211 55 105 C ATOM 3644 CG2 THR A 525 -59.138 17.573 -1.528 1.00 33.83 C ANISOU 3644 CG2 THR A 525 5471 4374 3011 179 83 70 C ATOM 3645 OG1 THR A 525 -57.237 17.995 -2.933 1.00 34.38 O ANISOU 3645 OG1 THR A 525 5536 4373 3155 239 55 72 O ATOM 3646 N THR A 526 -57.849 16.903 1.467 1.00 29.95 N ANISOU 3646 N THR A 526 4976 4028 2377 142 42 129 N ATOM 3647 CA THR A 526 -58.329 16.140 2.605 1.00 37.07 C ANISOU 3647 CA THR A 526 5885 4996 3204 99 40 176 C ATOM 3648 C THR A 526 -59.824 16.345 2.787 1.00 35.63 C ANISOU 3648 C THR A 526 5692 4849 2999 61 76 141 C ATOM 3649 O THR A 526 -60.334 17.461 2.647 1.00 30.60 O ANISOU 3649 O THR A 526 5022 4226 2378 62 98 59 O ATOM 3650 CB THR A 526 -57.574 16.497 3.887 1.00 33.47 C ANISOU 3650 CB THR A 526 5405 4632 2682 87 20 172 C ATOM 3651 CG2 THR A 526 -58.017 15.607 4.996 1.00 35.11 C ANISOU 3651 CG2 THR A 526 5620 4913 2808 38 14 238 C ATOM 3652 OG1 THR A 526 -56.174 16.279 3.676 1.00 36.23 O ANISOU 3652 OG1 THR A 526 5763 4943 3059 124 -15 203 O ATOM 3653 N SER A 527 -60.509 15.236 3.071 1.00 35.73 N ANISOU 3653 N SER A 527 5727 4866 2981 28 80 205 N ATOM 3654 CA SER A 527 -61.946 15.167 3.287 1.00 35.40 C ANISOU 3654 CA SER A 527 5679 4859 2912 -13 114 186 C ATOM 3655 C SER A 527 -62.222 14.353 4.541 1.00 34.95 C ANISOU 3655 C SER A 527 5625 4886 2769 -66 109 253 C ATOM 3656 O SER A 527 -61.562 13.334 4.796 1.00 32.68 O ANISOU 3656 O SER A 527 5362 4581 2474 -67 77 346 O ATOM 3657 CB SER A 527 -62.660 14.502 2.089 1.00 33.99 C ANISOU 3657 CB SER A 527 5529 4588 2798 -2 127 205 C ATOM 3658 OG SER A 527 -62.921 15.440 1.055 1.00 34.87 O ANISOU 3658 OG SER A 527 5627 4653 2970 28 143 133 O ATOM 3659 N GLU A 528 -63.215 14.792 5.308 1.00 35.28 N ANISOU 3659 N GLU A 528 5637 5019 2750 -112 139 206 N ATOM 3660 CA GLU A 528 -63.604 14.115 6.537 1.00 37.49 C ANISOU 3660 CA GLU A 528 5911 5399 2934 -174 139 266 C ATOM 3661 C GLU A 528 -65.073 13.737 6.423 1.00 37.83 C ANISOU 3661 C GLU A 528 5955 5446 2970 -214 176 261 C ATOM 3662 O GLU A 528 -65.909 14.573 6.055 1.00 35.85 O ANISOU 3662 O GLU A 528 5681 5196 2744 -212 209 165 O ATOM 3663 CB GLU A 528 -63.335 14.991 7.768 1.00 34.06 C ANISOU 3663 CB GLU A 528 5427 5102 2412 -201 142 209 C ATOM 3664 CG GLU A 528 -61.931 15.588 7.844 1.00 33.61 C ANISOU 3664 CG GLU A 528 5360 5042 2368 -158 110 189 C ATOM 3665 CD GLU A 528 -61.788 16.836 6.978 1.00 35.45 C ANISOU 3665 CD GLU A 528 5572 5213 2683 -109 123 80 C ATOM 3666 OE1 GLU A 528 -62.821 17.398 6.549 1.00 33.32 O ANISOU 3666 OE1 GLU A 528 5285 4928 2447 -115 156 8 O ATOM 3667 OE2 GLU A 528 -60.644 17.248 6.701 1.00 36.79 O1- ANISOU 3667 OE2 GLU A 528 5742 5347 2890 -66 98 70 O1- ATOM 3668 N TYR A 529 -65.372 12.468 6.710 1.00 41.20 N ANISOU 3668 N TYR A 529 6408 5869 3375 -250 167 367 N ATOM 3669 CA TYR A 529 -66.659 11.869 6.391 1.00 38.75 C ANISOU 3669 CA TYR A 529 6110 5535 3080 -281 197 380 C ATOM 3670 C TYR A 529 -67.101 10.950 7.525 1.00 45.10 C ANISOU 3670 C TYR A 529 6911 6427 3797 -354 196 473 C ATOM 3671 O TYR A 529 -66.293 10.385 8.269 1.00 46.67 O ANISOU 3671 O TYR A 529 7116 6665 3953 -370 160 565 O ATOM 3672 CB TYR A 529 -66.613 11.093 5.056 1.00 40.15 C ANISOU 3672 CB TYR A 529 6327 5565 3365 -238 187 417 C ATOM 3673 CG TYR A 529 -65.433 10.154 4.912 1.00 39.20 C ANISOU 3673 CG TYR A 529 6235 5376 3282 -212 139 515 C ATOM 3674 CD1 TYR A 529 -64.140 10.640 4.762 1.00 40.56 C ANISOU 3674 CD1 TYR A 529 6407 5531 3473 -164 110 500 C ATOM 3675 CD2 TYR A 529 -65.612 8.793 4.924 1.00 37.83 C ANISOU 3675 CD2 TYR A 529 6085 5154 3136 -234 122 618 C ATOM 3676 CE1 TYR A 529 -63.071 9.799 4.638 1.00 39.43 C ANISOU 3676 CE1 TYR A 529 6285 5327 3370 -139 65 581 C ATOM 3677 CE2 TYR A 529 -64.544 7.949 4.804 1.00 41.04 C ANISOU 3677 CE2 TYR A 529 6510 5493 3591 -208 75 701 C ATOM 3678 CZ TYR A 529 -63.280 8.459 4.663 1.00 40.32 C ANISOU 3678 CZ TYR A 529 6417 5389 3514 -160 47 680 C ATOM 3679 OH TYR A 529 -62.214 7.612 4.546 1.00 49.34 O ANISOU 3679 OH TYR A 529 7572 6463 4711 -133 -2 757 O ATOM 3680 N ASN A 530 -68.413 10.788 7.610 1.00 45.61 N ANISOU 3680 N ASN A 530 6966 6522 3842 -399 234 454 N ATOM 3681 CA ASN A 530 -69.107 10.182 8.740 1.00 42.63 C ANISOU 3681 CA ASN A 530 6573 6256 3369 -480 246 518 C ATOM 3682 C ASN A 530 -69.322 8.708 8.419 1.00 43.53 C ANISOU 3682 C ASN A 530 6725 6282 3533 -496 229 645 C ATOM 3683 O ASN A 530 -70.246 8.345 7.683 1.00 39.69 O ANISOU 3683 O ASN A 530 6250 5724 3105 -496 254 629 O ATOM 3684 CB ASN A 530 -70.399 10.963 8.973 1.00 43.60 C ANISOU 3684 CB ASN A 530 6656 6461 3451 -517 300 406 C ATOM 3685 CG ASN A 530 -71.271 10.398 10.067 1.00 41.98 C ANISOU 3685 CG ASN A 530 6428 6381 3142 -608 322 457 C ATOM 3686 ND2 ASN A 530 -72.161 11.240 10.583 1.00 37.30 N ANISOU 3686 ND2 ASN A 530 5784 5899 2488 -646 366 346 N ATOM 3687 OD1 ASN A 530 -71.156 9.236 10.454 1.00 43.81 O ANISOU 3687 OD1 ASN A 530 6682 6612 3353 -645 300 593 O ATOM 3688 N VAL A 531 -68.452 7.865 8.986 1.00 47.07 N ANISOU 3688 N VAL A 531 7187 6735 3963 -509 183 771 N ATOM 3689 CA VAL A 531 -68.472 6.422 8.741 1.00 45.99 C ANISOU 3689 CA VAL A 531 7080 6504 3891 -521 155 902 C ATOM 3690 C VAL A 531 -69.492 5.716 9.618 1.00 42.61 C ANISOU 3690 C VAL A 531 6637 6160 3391 -610 172 982 C ATOM 3691 O VAL A 531 -69.897 4.587 9.320 1.00 41.57 O ANISOU 3691 O VAL A 531 6524 5945 3325 -628 163 1071 O ATOM 3692 CB VAL A 531 -67.070 5.854 8.998 1.00 51.40 C ANISOU 3692 CB VAL A 531 7779 7153 4598 -495 91 1005 C ATOM 3693 CG1 VAL A 531 -66.863 4.530 8.278 1.00 53.85 C ANISOU 3693 CG1 VAL A 531 8118 7311 5031 -474 57 1102 C ATOM 3694 CG2 VAL A 531 -66.059 6.860 8.580 1.00 53.50 C ANISOU 3694 CG2 VAL A 531 8044 7403 4881 -427 81 915 C ATOM 3695 N GLU A 532 -69.898 6.343 10.713 1.00 42.42 N ANISOU 3695 N GLU A 532 6577 6304 3237 -669 198 951 N ATOM 3696 CA GLU A 532 -71.003 5.809 11.493 1.00 45.85 C ANISOU 3696 CA GLU A 532 6992 6835 3596 -759 225 1007 C ATOM 3697 C GLU A 532 -72.279 5.789 10.665 1.00 41.08 C ANISOU 3697 C GLU A 532 6392 6164 3054 -759 274 933 C ATOM 3698 O GLU A 532 -73.026 4.804 10.671 1.00 39.65 O ANISOU 3698 O GLU A 532 6218 5951 2895 -804 281 1015 O ATOM 3699 CB GLU A 532 -71.183 6.655 12.751 1.00 47.74 C ANISOU 3699 CB GLU A 532 7181 7281 3679 -819 248 956 C ATOM 3700 CG GLU A 532 -71.454 5.888 14.020 1.00 47.30 C ANISOU 3700 CG GLU A 532 7102 7362 3507 -918 239 1090 C ATOM 3701 CD GLU A 532 -71.983 6.813 15.114 1.00 54.55 C ANISOU 3701 CD GLU A 532 7960 8496 4270 -984 281 998 C ATOM 3702 OE1 GLU A 532 -71.163 7.335 15.906 1.00 56.05 O ANISOU 3702 OE1 GLU A 532 8122 8802 4371 -990 260 990 O ATOM 3703 OE2 GLU A 532 -73.220 7.024 15.180 1.00 54.51 O1- ANISOU 3703 OE2 GLU A 532 7929 8548 4234 -1029 335 926 O1- ATOM 3704 N LYS A 533 -72.505 6.847 9.897 1.00 42.51 N ANISOU 3704 N LYS A 533 6567 6311 3273 -705 304 782 N ATOM 3705 CA LYS A 533 -73.781 7.073 9.240 1.00 42.97 C ANISOU 3705 CA LYS A 533 6619 6337 3372 -709 353 692 C ATOM 3706 C LYS A 533 -73.850 6.487 7.834 1.00 40.47 C ANISOU 3706 C LYS A 533 6341 5841 3196 -650 344 697 C ATOM 3707 O LYS A 533 -74.934 6.090 7.401 1.00 44.26 O ANISOU 3707 O LYS A 533 6821 6283 3712 -670 375 682 O ATOM 3708 CB LYS A 533 -74.062 8.578 9.195 1.00 40.95 C ANISOU 3708 CB LYS A 533 6326 6146 3086 -686 387 526 C ATOM 3709 CG LYS A 533 -75.518 8.975 9.259 1.00 37.37 C ANISOU 3709 CG LYS A 533 5838 5751 2608 -728 442 432 C ATOM 3710 CD LYS A 533 -75.640 10.486 9.135 1.00 36.87 C ANISOU 3710 CD LYS A 533 5735 5730 2545 -695 465 268 C ATOM 3711 CE LYS A 533 -77.082 10.896 8.976 1.00 36.86 C ANISOU 3711 CE LYS A 533 5700 5756 2549 -723 515 164 C ATOM 3712 NZ LYS A 533 -77.182 12.298 8.510 1.00 36.23 N1+ ANISOU 3712 NZ LYS A 533 5586 5664 2517 -673 527 10 N1+ ATOM 3713 N PHE A 534 -72.736 6.409 7.110 1.00 41.12 N ANISOU 3713 N PHE A 534 6451 5819 3356 -580 305 713 N ATOM 3714 CA PHE A 534 -72.772 5.948 5.727 1.00 44.35 C ANISOU 3714 CA PHE A 534 6887 6071 3891 -523 299 699 C ATOM 3715 C PHE A 534 -71.575 5.066 5.407 1.00 44.06 C ANISOU 3715 C PHE A 534 6877 5935 3928 -485 245 795 C ATOM 3716 O PHE A 534 -70.451 5.326 5.852 1.00 41.01 O ANISOU 3716 O PHE A 534 6492 5578 3512 -466 211 824 O ATOM 3717 CB PHE A 534 -72.819 7.126 4.726 1.00 39.53 C ANISOU 3717 CB PHE A 534 6272 5425 3323 -460 319 560 C ATOM 3718 CG PHE A 534 -74.044 7.993 4.859 1.00 39.60 C ANISOU 3718 CG PHE A 534 6249 5507 3290 -488 369 455 C ATOM 3719 CD1 PHE A 534 -75.305 7.478 4.605 1.00 38.97 C ANISOU 3719 CD1 PHE A 534 6166 5410 3230 -522 401 448 C ATOM 3720 CD2 PHE A 534 -73.937 9.324 5.228 1.00 39.24 C ANISOU 3720 CD2 PHE A 534 6172 5544 3193 -479 382 356 C ATOM 3721 CE1 PHE A 534 -76.427 8.270 4.726 1.00 38.37 C ANISOU 3721 CE1 PHE A 534 6057 5400 3121 -547 444 346 C ATOM 3722 CE2 PHE A 534 -75.071 10.115 5.360 1.00 36.35 C ANISOU 3722 CE2 PHE A 534 5770 5241 2802 -504 424 252 C ATOM 3723 CZ PHE A 534 -76.307 9.586 5.106 1.00 37.11 C ANISOU 3723 CZ PHE A 534 5864 5320 2915 -537 455 248 C ATOM 3724 N SER A 535 -71.830 4.037 4.605 1.00 48.34 N ANISOU 3724 N SER A 535 7436 6358 4572 -473 237 835 N ATOM 3725 CA SER A 535 -70.799 3.149 4.106 1.00 47.39 C ANISOU 3725 CA SER A 535 7335 6124 4549 -431 187 906 C ATOM 3726 C SER A 535 -70.738 3.249 2.588 1.00 44.81 C ANISOU 3726 C SER A 535 7017 5683 4327 -363 194 818 C ATOM 3727 O SER A 535 -71.720 3.603 1.932 1.00 46.05 O ANISOU 3727 O SER A 535 7168 5832 4496 -361 235 735 O ATOM 3728 CB SER A 535 -71.064 1.706 4.540 1.00 47.73 C ANISOU 3728 CB SER A 535 7378 6122 4634 -480 164 1039 C ATOM 3729 OG SER A 535 -69.846 0.998 4.706 1.00 58.74 O ANISOU 3729 OG SER A 535 8780 7457 6082 -458 104 1135 O ATOM 3730 N GLY A 536 -69.568 2.945 2.043 1.00 40.78 N ANISOU 3730 N GLY A 536 6516 5092 3888 -309 154 834 N ATOM 3731 CA GLY A 536 -69.355 2.972 0.617 1.00 38.09 C ANISOU 3731 CA GLY A 536 6177 4654 3640 -247 156 757 C ATOM 3732 C GLY A 536 -68.538 4.134 0.098 1.00 40.19 C ANISOU 3732 C GLY A 536 6444 4937 3888 -192 155 673 C ATOM 3733 O GLY A 536 -68.654 4.465 -1.086 1.00 34.68 O ANISOU 3733 O GLY A 536 5744 4193 3240 -151 171 592 O ATOM 3734 N TRP A 537 -67.731 4.772 0.938 1.00 41.11 N ANISOU 3734 N TRP A 537 6560 5125 3936 -192 137 692 N ATOM 3735 CA TRP A 537 -66.977 5.932 0.491 1.00 36.96 C ANISOU 3735 CA TRP A 537 6031 4616 3395 -144 137 614 C ATOM 3736 C TRP A 537 -65.794 5.505 -0.370 1.00 35.15 C ANISOU 3736 C TRP A 537 5807 4296 3252 -87 102 618 C ATOM 3737 O TRP A 537 -65.383 4.343 -0.345 1.00 38.70 O ANISOU 3737 O TRP A 537 6259 4679 3764 -87 70 689 O ATOM 3738 CB TRP A 537 -66.474 6.733 1.688 1.00 34.53 C ANISOU 3738 CB TRP A 537 5715 4415 2990 -163 129 625 C ATOM 3739 CG TRP A 537 -67.515 7.113 2.690 1.00 39.08 C ANISOU 3739 CG TRP A 537 6277 5098 3474 -224 161 620 C ATOM 3740 CD1 TRP A 537 -67.952 6.367 3.764 1.00 41.42 C ANISOU 3740 CD1 TRP A 537 6571 5449 3717 -287 157 709 C ATOM 3741 CD2 TRP A 537 -68.237 8.344 2.742 1.00 38.74 C ANISOU 3741 CD2 TRP A 537 6213 5124 3381 -231 201 520 C ATOM 3742 CE2 TRP A 537 -69.099 8.279 3.863 1.00 35.68 C ANISOU 3742 CE2 TRP A 537 5810 4838 2909 -299 222 542 C ATOM 3743 CE3 TRP A 537 -68.251 9.491 1.942 1.00 36.88 C ANISOU 3743 CE3 TRP A 537 5967 4875 3170 -189 217 416 C ATOM 3744 NE1 TRP A 537 -68.908 7.064 4.466 1.00 37.35 N ANISOU 3744 NE1 TRP A 537 6035 5044 3114 -334 196 662 N ATOM 3745 CZ2 TRP A 537 -69.952 9.315 4.202 1.00 36.23 C ANISOU 3745 CZ2 TRP A 537 5851 4993 2922 -322 261 450 C ATOM 3746 CZ3 TRP A 537 -69.101 10.525 2.284 1.00 36.29 C ANISOU 3746 CZ3 TRP A 537 5865 4876 3048 -211 252 334 C ATOM 3747 CH2 TRP A 537 -69.937 10.432 3.407 1.00 38.35 C ANISOU 3747 CH2 TRP A 537 6107 5235 3230 -276 274 345 C ATOM 3748 N PRO A 538 -65.221 6.427 -1.141 1.00 32.58 N ANISOU 3748 N PRO A 538 5478 3966 2936 -40 106 541 N ATOM 3749 CA PRO A 538 -63.985 6.104 -1.869 1.00 33.58 C ANISOU 3749 CA PRO A 538 5603 4023 3131 10 74 540 C ATOM 3750 C PRO A 538 -62.847 5.805 -0.911 1.00 38.12 C ANISOU 3750 C PRO A 538 6181 4613 3691 11 30 614 C ATOM 3751 O PRO A 538 -62.488 6.634 -0.076 1.00 42.98 O ANISOU 3751 O PRO A 538 6794 5307 4229 2 27 614 O ATOM 3752 CB PRO A 538 -63.710 7.369 -2.687 1.00 35.48 C ANISOU 3752 CB PRO A 538 5835 4283 3361 47 91 449 C ATOM 3753 CG PRO A 538 -65.033 8.070 -2.785 1.00 36.47 C ANISOU 3753 CG PRO A 538 5957 4452 3450 22 134 397 C ATOM 3754 CD PRO A 538 -65.768 7.740 -1.517 1.00 33.23 C ANISOU 3754 CD PRO A 538 5550 4097 2981 -33 141 450 C ATOM 3755 N THR A 539 -62.274 4.612 -1.035 1.00 39.92 N ANISOU 3755 N THR A 539 6409 4763 3997 22 -8 673 N ATOM 3756 CA THR A 539 -61.053 4.282 -0.313 1.00 40.06 C ANISOU 3756 CA THR A 539 6425 4778 4018 32 -57 742 C ATOM 3757 C THR A 539 -59.853 4.450 -1.236 1.00 41.54 C ANISOU 3757 C THR A 539 6603 4912 4269 92 -77 688 C ATOM 3758 O THR A 539 -59.992 4.602 -2.453 1.00 42.52 O ANISOU 3758 O THR A 539 6720 4995 4441 121 -54 611 O ATOM 3759 CB THR A 539 -61.112 2.859 0.257 1.00 42.74 C ANISOU 3759 CB THR A 539 6764 5064 4413 4 -95 852 C ATOM 3760 CG2 THR A 539 -62.404 2.641 1.048 1.00 39.82 C ANISOU 3760 CG2 THR A 539 6400 4748 3983 -61 -70 904 C ATOM 3761 OG1 THR A 539 -61.032 1.905 -0.801 1.00 44.15 O ANISOU 3761 OG1 THR A 539 6931 5127 4718 33 -106 834 O ATOM 3762 N GLU A 540 -58.656 4.455 -0.636 1.00 43.53 N ANISOU 3762 N GLU A 540 6852 5173 4515 109 -119 729 N ATOM 3763 CA GLU A 540 -57.443 4.604 -1.439 1.00 46.79 C ANISOU 3763 CA GLU A 540 7252 5540 4985 163 -138 679 C ATOM 3764 C GLU A 540 -57.266 3.431 -2.390 1.00 45.10 C ANISOU 3764 C GLU A 540 7022 5217 4896 187 -156 671 C ATOM 3765 O GLU A 540 -56.703 3.592 -3.479 1.00 45.34 O ANISOU 3765 O GLU A 540 7037 5214 4977 227 -150 594 O ATOM 3766 CB GLU A 540 -56.192 4.733 -0.565 1.00 48.81 C ANISOU 3766 CB GLU A 540 7504 5823 5218 176 -184 727 C ATOM 3767 CG GLU A 540 -56.323 5.563 0.686 1.00 55.89 C ANISOU 3767 CG GLU A 540 8408 6831 5996 142 -179 756 C ATOM 3768 CD GLU A 540 -56.987 4.817 1.845 1.00 54.77 C ANISOU 3768 CD GLU A 540 8273 6722 5815 87 -195 862 C ATOM 3769 OE1 GLU A 540 -58.037 4.170 1.630 1.00 53.79 O ANISOU 3769 OE1 GLU A 540 8154 6565 5718 59 -176 883 O ATOM 3770 OE2 GLU A 540 -56.432 4.872 2.967 1.00 59.94 O1- ANISOU 3770 OE2 GLU A 540 8925 7440 6411 69 -228 927 O1- ATOM 3771 N ASP A 541 -57.747 2.250 -1.999 1.00 43.05 N ANISOU 3771 N ASP A 541 6761 4905 4691 161 -177 746 N ATOM 3772 CA ASP A 541 -57.671 1.094 -2.879 1.00 44.22 C ANISOU 3772 CA ASP A 541 6886 4944 4972 181 -193 731 C ATOM 3773 C ASP A 541 -58.653 1.219 -4.038 1.00 42.07 C ANISOU 3773 C ASP A 541 6609 4660 4716 183 -142 641 C ATOM 3774 O ASP A 541 -58.297 0.938 -5.189 1.00 43.43 O ANISOU 3774 O ASP A 541 6756 4780 4965 217 -140 565 O ATOM 3775 CB ASP A 541 -57.914 -0.179 -2.073 1.00 43.87 C ANISOU 3775 CB ASP A 541 6837 4842 4990 149 -234 845 C ATOM 3776 CG ASP A 541 -56.890 -0.375 -0.990 1.00 45.60 C ANISOU 3776 CG ASP A 541 7055 5071 5199 149 -292 941 C ATOM 3777 OD1 ASP A 541 -55.725 0.034 -1.193 1.00 49.96 O ANISOU 3777 OD1 ASP A 541 7598 5625 5758 190 -313 903 O ATOM 3778 OD2 ASP A 541 -57.247 -0.914 0.077 1.00 54.60 O1- ANISOU 3778 OD2 ASP A 541 8202 6225 6319 104 -317 1056 O1- ATOM 3779 N ASP A 542 -59.881 1.657 -3.758 1.00 38.07 N ANISOU 3779 N ASP A 542 6122 4208 4135 144 -102 645 N ATOM 3780 CA ASP A 542 -60.913 1.864 -4.773 1.00 38.01 C ANISOU 3780 CA ASP A 542 6110 4200 4131 142 -55 565 C ATOM 3781 C ASP A 542 -61.303 3.337 -4.782 1.00 37.95 C ANISOU 3781 C ASP A 542 6118 4287 4014 137 -15 514 C ATOM 3782 O ASP A 542 -62.334 3.719 -4.230 1.00 37.71 O ANISOU 3782 O ASP A 542 6102 4307 3918 100 12 529 O ATOM 3783 CB ASP A 542 -62.133 1.007 -4.536 1.00 41.14 C ANISOU 3783 CB ASP A 542 6508 4565 4557 101 -43 606 C ATOM 3784 CG ASP A 542 -63.182 1.200 -5.620 1.00 40.74 C ANISOU 3784 CG ASP A 542 6450 4515 4513 100 4 519 C ATOM 3785 OD1 ASP A 542 -62.798 1.672 -6.707 1.00 42.97 O ANISOU 3785 OD1 ASP A 542 6719 4801 4808 137 17 433 O ATOM 3786 OD2 ASP A 542 -64.379 0.931 -5.396 1.00 45.39 O1- ANISOU 3786 OD2 ASP A 542 7046 5109 5091 63 29 537 O1- ATOM 3787 N LEU A 543 -60.500 4.162 -5.449 1.00 38.31 N ANISOU 3787 N LEU A 543 6156 4352 4048 174 -12 451 N ATOM 3788 CA LEU A 543 -60.799 5.589 -5.561 1.00 35.75 C ANISOU 3788 CA LEU A 543 5840 4105 3640 174 20 402 C ATOM 3789 C LEU A 543 -61.717 5.822 -6.760 1.00 35.64 C ANISOU 3789 C LEU A 543 5815 4087 3639 176 58 330 C ATOM 3790 O LEU A 543 -61.363 6.461 -7.754 1.00 37.01 O ANISOU 3790 O LEU A 543 5975 4273 3815 202 68 269 O ATOM 3791 CB LEU A 543 -59.510 6.389 -5.660 1.00 33.57 C ANISOU 3791 CB LEU A 543 5557 3851 3347 208 4 378 C ATOM 3792 CG LEU A 543 -59.633 7.878 -5.416 1.00 30.65 C ANISOU 3792 CG LEU A 543 5191 3556 2897 204 26 347 C ATOM 3793 CD1 LEU A 543 -60.034 8.122 -3.998 1.00 33.90 C ANISOU 3793 CD1 LEU A 543 5617 4023 3241 168 24 396 C ATOM 3794 CD2 LEU A 543 -58.304 8.529 -5.712 1.00 34.89 C ANISOU 3794 CD2 LEU A 543 5717 4102 3438 239 8 320 C ATOM 3795 N TYR A 544 -62.937 5.287 -6.632 1.00 35.87 N ANISOU 3795 N TYR A 544 5850 4105 3674 144 77 344 N ATOM 3796 CA TYR A 544 -63.898 5.244 -7.730 1.00 30.23 C ANISOU 3796 CA TYR A 544 5123 3381 2982 143 108 283 C ATOM 3797 C TYR A 544 -64.339 6.621 -8.206 1.00 32.10 C ANISOU 3797 C TYR A 544 5358 3679 3158 146 137 229 C ATOM 3798 O TYR A 544 -64.945 6.716 -9.275 1.00 33.38 O ANISOU 3798 O TYR A 544 5505 3840 3337 152 157 175 O ATOM 3799 CB TYR A 544 -65.118 4.412 -7.313 1.00 31.27 C ANISOU 3799 CB TYR A 544 5261 3491 3130 104 122 315 C ATOM 3800 CG TYR A 544 -65.965 4.924 -6.146 1.00 34.84 C ANISOU 3800 CG TYR A 544 5733 4003 3504 62 139 355 C ATOM 3801 CD1 TYR A 544 -66.822 6.015 -6.301 1.00 32.73 C ANISOU 3801 CD1 TYR A 544 5466 3793 3178 52 173 305 C ATOM 3802 CD2 TYR A 544 -65.951 4.273 -4.893 1.00 36.61 C ANISOU 3802 CD2 TYR A 544 5968 4227 3714 28 121 441 C ATOM 3803 CE1 TYR A 544 -67.609 6.476 -5.245 1.00 34.05 C ANISOU 3803 CE1 TYR A 544 5640 4019 3277 12 190 326 C ATOM 3804 CE2 TYR A 544 -66.743 4.719 -3.823 1.00 31.25 C ANISOU 3804 CE2 TYR A 544 5300 3618 2955 -16 139 471 C ATOM 3805 CZ TYR A 544 -67.571 5.821 -4.013 1.00 35.64 C ANISOU 3805 CZ TYR A 544 5852 4232 3456 -24 176 405 C ATOM 3806 OH TYR A 544 -68.368 6.276 -2.985 1.00 36.47 O ANISOU 3806 OH TYR A 544 5960 4412 3487 -68 197 419 O ATOM 3807 N ALA A 545 -64.052 7.670 -7.437 1.00 36.94 N ANISOU 3807 N ALA A 545 5981 4345 3709 143 135 241 N ATOM 3808 CA ALA A 545 -64.414 9.057 -7.701 1.00 31.94 C ANISOU 3808 CA ALA A 545 5342 3764 3031 145 156 197 C ATOM 3809 C ALA A 545 -63.503 9.912 -6.836 1.00 29.15 C ANISOU 3809 C ALA A 545 4991 3449 2635 152 139 213 C ATOM 3810 O ALA A 545 -62.924 9.422 -5.871 1.00 34.09 O ANISOU 3810 O ALA A 545 5628 4075 3251 145 118 262 O ATOM 3811 CB ALA A 545 -65.885 9.330 -7.387 1.00 28.90 C ANISOU 3811 CB ALA A 545 4958 3406 2615 111 185 185 C ATOM 3812 N PHE A 546 -63.359 11.185 -7.192 1.00 33.16 N ANISOU 3812 N PHE A 546 5486 3990 3124 165 147 173 N ATOM 3813 CA PHE A 546 -62.486 12.071 -6.420 1.00 28.71 C ANISOU 3813 CA PHE A 546 4919 3461 2528 173 132 177 C ATOM 3814 C PHE A 546 -63.193 12.452 -5.126 1.00 33.94 C ANISOU 3814 C PHE A 546 5583 4174 3137 139 143 185 C ATOM 3815 O PHE A 546 -64.244 13.101 -5.174 1.00 36.13 O ANISOU 3815 O PHE A 546 5850 4475 3403 122 166 150 O ATOM 3816 CB PHE A 546 -62.124 13.312 -7.216 1.00 31.75 C ANISOU 3816 CB PHE A 546 5283 3859 2923 195 135 135 C ATOM 3817 CG PHE A 546 -60.978 14.122 -6.630 1.00 31.07 C ANISOU 3817 CG PHE A 546 5188 3796 2820 210 116 135 C ATOM 3818 CD1 PHE A 546 -59.750 13.530 -6.366 1.00 27.96 C ANISOU 3818 CD1 PHE A 546 4803 3387 2434 228 90 163 C ATOM 3819 CD2 PHE A 546 -61.123 15.484 -6.385 1.00 29.67 C ANISOU 3819 CD2 PHE A 546 4990 3651 2631 208 122 102 C ATOM 3820 CE1 PHE A 546 -58.711 14.261 -5.857 1.00 27.96 C ANISOU 3820 CE1 PHE A 546 4794 3410 2421 242 74 160 C ATOM 3821 CE2 PHE A 546 -60.072 16.227 -5.866 1.00 28.90 C ANISOU 3821 CE2 PHE A 546 4881 3573 2526 222 105 96 C ATOM 3822 CZ PHE A 546 -58.872 15.615 -5.596 1.00 28.54 C ANISOU 3822 CZ PHE A 546 4846 3518 2479 238 82 125 C ATOM 3823 N PRO A 547 -62.674 12.054 -3.953 1.00 35.80 N ANISOU 3823 N PRO A 547 5829 4433 3340 126 125 230 N ATOM 3824 CA PRO A 547 -63.411 12.194 -2.693 1.00 34.53 C ANISOU 3824 CA PRO A 547 5667 4334 3119 84 137 242 C ATOM 3825 C PRO A 547 -63.433 13.613 -2.116 1.00 36.98 C ANISOU 3825 C PRO A 547 5952 4708 3391 80 147 188 C ATOM 3826 O PRO A 547 -63.152 13.828 -0.939 1.00 32.49 O ANISOU 3826 O PRO A 547 5376 4201 2769 60 140 198 O ATOM 3827 CB PRO A 547 -62.674 11.218 -1.768 1.00 34.04 C ANISOU 3827 CB PRO A 547 5619 4276 3037 73 108 317 C ATOM 3828 CG PRO A 547 -61.286 11.258 -2.248 1.00 35.01 C ANISOU 3828 CG PRO A 547 5743 4364 3198 116 79 320 C ATOM 3829 CD PRO A 547 -61.354 11.426 -3.751 1.00 33.31 C ANISOU 3829 CD PRO A 547 5522 4094 3041 147 91 273 C ATOM 3830 N ALA A 548 -63.791 14.589 -2.957 1.00 34.06 N ANISOU 3830 N ALA A 548 5563 4325 3053 97 161 128 N ATOM 3831 CA ALA A 548 -63.953 15.971 -2.530 1.00 31.59 C ANISOU 3831 CA ALA A 548 5218 4057 2728 93 169 68 C ATOM 3832 C ALA A 548 -65.403 16.389 -2.726 1.00 32.68 C ANISOU 3832 C ALA A 548 5339 4205 2874 72 198 23 C ATOM 3833 O ALA A 548 -65.969 16.200 -3.804 1.00 33.43 O ANISOU 3833 O ALA A 548 5439 4253 3009 81 206 19 O ATOM 3834 CB ALA A 548 -63.021 16.895 -3.300 1.00 33.91 C ANISOU 3834 CB ALA A 548 5496 4323 3066 132 154 43 C ATOM 3835 N VAL A 549 -65.999 16.969 -1.684 1.00 36.30 N ANISOU 3835 N VAL A 549 5772 4729 3294 42 212 -18 N ATOM 3836 CA VAL A 549 -67.434 17.244 -1.679 1.00 34.81 C ANISOU 3836 CA VAL A 549 5562 4555 3107 15 240 -64 C ATOM 3837 C VAL A 549 -67.818 18.246 -2.762 1.00 31.63 C ANISOU 3837 C VAL A 549 5135 4108 2776 41 240 -114 C ATOM 3838 O VAL A 549 -68.989 18.326 -3.154 1.00 28.59 O ANISOU 3838 O VAL A 549 4738 3712 2411 29 258 -142 O ATOM 3839 CB VAL A 549 -67.854 17.739 -0.270 1.00 30.99 C ANISOU 3839 CB VAL A 549 5046 4163 2566 -23 254 -110 C ATOM 3840 CG1 VAL A 549 -67.611 19.212 -0.152 1.00 29.54 C ANISOU 3840 CG1 VAL A 549 4813 3994 2416 -6 249 -189 C ATOM 3841 CG2 VAL A 549 -69.309 17.381 0.035 1.00 31.69 C ANISOU 3841 CG2 VAL A 549 5127 4284 2631 -65 285 -130 C ATOM 3842 N TRP A 550 -66.849 19.001 -3.272 1.00 31.94 N ANISOU 3842 N TRP A 550 5163 4119 2855 75 219 -119 N ATOM 3843 CA TRP A 550 -67.100 20.057 -4.239 1.00 30.03 C ANISOU 3843 CA TRP A 550 4890 3837 2683 96 213 -154 C ATOM 3844 C TRP A 550 -66.629 19.697 -5.642 1.00 30.57 C ANISOU 3844 C TRP A 550 4981 3850 2786 124 200 -109 C ATOM 3845 O TRP A 550 -66.596 20.576 -6.508 1.00 28.82 O ANISOU 3845 O TRP A 550 4733 3600 2618 142 188 -120 O ATOM 3846 CB TRP A 550 -66.419 21.346 -3.782 1.00 28.19 C ANISOU 3846 CB TRP A 550 4615 3617 2478 109 198 -199 C ATOM 3847 CG TRP A 550 -65.019 21.120 -3.248 1.00 31.92 C ANISOU 3847 CG TRP A 550 5103 4108 2917 121 182 -170 C ATOM 3848 CD1 TRP A 550 -64.613 21.182 -1.940 1.00 31.40 C ANISOU 3848 CD1 TRP A 550 5026 4104 2799 105 182 -190 C ATOM 3849 CD2 TRP A 550 -63.842 20.800 -4.015 1.00 30.73 C ANISOU 3849 CD2 TRP A 550 4978 3919 2781 151 162 -119 C ATOM 3850 CE2 TRP A 550 -62.769 20.685 -3.110 1.00 31.92 C ANISOU 3850 CE2 TRP A 550 5132 4102 2892 154 149 -110 C ATOM 3851 CE3 TRP A 550 -63.596 20.590 -5.378 1.00 33.87 C ANISOU 3851 CE3 TRP A 550 5389 4264 3215 172 154 -84 C ATOM 3852 NE1 TRP A 550 -63.260 20.925 -1.852 1.00 31.56 N ANISOU 3852 NE1 TRP A 550 5066 4121 2805 126 161 -151 N ATOM 3853 CZ2 TRP A 550 -61.472 20.377 -3.527 1.00 35.78 C ANISOU 3853 CZ2 TRP A 550 5641 4567 3388 181 129 -69 C ATOM 3854 CZ3 TRP A 550 -62.302 20.288 -5.791 1.00 31.26 C ANISOU 3854 CZ3 TRP A 550 5076 3917 2886 196 136 -47 C ATOM 3855 CH2 TRP A 550 -61.264 20.179 -4.870 1.00 32.02 C ANISOU 3855 CH2 TRP A 550 5176 4038 2951 201 124 -41 C ATOM 3856 N ALA A 551 -66.211 18.446 -5.871 1.00 35.26 N ANISOU 3856 N ALA A 551 5615 4431 3352 127 199 -58 N ATOM 3857 CA ALA A 551 -65.877 17.931 -7.208 1.00 27.33 C ANISOU 3857 CA ALA A 551 4625 3385 2374 148 191 -26 C ATOM 3858 C ALA A 551 -67.149 17.395 -7.826 1.00 27.29 C ANISOU 3858 C ALA A 551 4625 3367 2377 133 209 -32 C ATOM 3859 O ALA A 551 -67.644 16.333 -7.427 1.00 34.30 O ANISOU 3859 O ALA A 551 5535 4257 3239 115 223 -17 O ATOM 3860 CB ALA A 551 -64.815 16.836 -7.139 1.00 27.38 C ANISOU 3860 CB ALA A 551 4662 3379 2360 159 180 18 C ATOM 3861 N SER A 552 -67.716 18.157 -8.766 1.00 28.88 N ANISOU 3861 N SER A 552 4801 3556 2616 140 208 -52 N ATOM 3862 CA SER A 552 -68.795 17.521 -9.524 1.00 27.67 C ANISOU 3862 CA SER A 552 4652 3391 2470 130 222 -55 C ATOM 3863 C SER A 552 -68.248 16.935 -10.817 1.00 30.39 C ANISOU 3863 C SER A 552 5005 3718 2825 148 213 -29 C ATOM 3864 O SER A 552 -67.288 17.466 -11.392 1.00 33.97 O ANISOU 3864 O SER A 552 5447 4170 3291 168 196 -16 O ATOM 3865 CB SER A 552 -69.919 18.504 -9.830 1.00 27.93 C ANISOU 3865 CB SER A 552 4650 3425 2536 123 224 -90 C ATOM 3866 OG SER A 552 -70.368 19.221 -8.678 1.00 27.68 O ANISOU 3866 OG SER A 552 4598 3414 2504 107 231 -130 O ATOM 3867 N PRO A 553 -68.840 15.836 -11.282 1.00 29.13 N ANISOU 3867 N PRO A 553 4859 3548 2660 140 227 -27 N ATOM 3868 CA PRO A 553 -69.922 15.083 -10.657 1.00 29.53 C ANISOU 3868 CA PRO A 553 4923 3597 2698 115 248 -37 C ATOM 3869 C PRO A 553 -69.423 13.964 -9.763 1.00 30.30 C ANISOU 3869 C PRO A 553 5052 3687 2775 106 251 -8 C ATOM 3870 O PRO A 553 -70.248 13.117 -9.405 1.00 29.66 O ANISOU 3870 O PRO A 553 4982 3600 2688 83 267 -5 O ATOM 3871 CB PRO A 553 -70.668 14.493 -11.872 1.00 27.92 C ANISOU 3871 CB PRO A 553 4713 3383 2512 115 256 -49 C ATOM 3872 CG PRO A 553 -69.566 14.180 -12.831 1.00 26.97 C ANISOU 3872 CG PRO A 553 4591 3257 2399 138 241 -35 C ATOM 3873 CD PRO A 553 -68.530 15.302 -12.628 1.00 30.05 C ANISOU 3873 CD PRO A 553 4972 3659 2788 154 222 -21 C ATOM 3874 N ASP A 554 -68.124 13.901 -9.430 1.00 29.32 N ANISOU 3874 N ASP A 554 4937 3559 2643 122 233 18 N ATOM 3875 CA ASP A 554 -67.635 12.816 -8.575 1.00 33.00 C ANISOU 3875 CA ASP A 554 5428 4014 3095 113 228 56 C ATOM 3876 C ASP A 554 -68.421 12.726 -7.270 1.00 29.30 C ANISOU 3876 C ASP A 554 4967 3575 2590 78 242 64 C ATOM 3877 O ASP A 554 -68.712 11.625 -6.792 1.00 28.32 O ANISOU 3877 O ASP A 554 4860 3439 2461 56 247 97 O ATOM 3878 CB ASP A 554 -66.146 12.983 -8.260 1.00 33.54 C ANISOU 3878 CB ASP A 554 5502 4083 3159 136 204 79 C ATOM 3879 CG ASP A 554 -65.340 13.353 -9.464 1.00 30.86 C ANISOU 3879 CG ASP A 554 5149 3732 2847 166 192 65 C ATOM 3880 OD1 ASP A 554 -65.809 14.228 -10.198 1.00 34.74 O ANISOU 3880 OD1 ASP A 554 5618 4234 3345 169 197 39 O ATOM 3881 OD2 ASP A 554 -64.242 12.798 -9.663 1.00 32.18 O1- ANISOU 3881 OD2 ASP A 554 5321 3880 3027 186 175 82 O1- ATOM 3882 N ASN A 555 -68.780 13.874 -6.685 1.00 28.37 N ANISOU 3882 N ASN A 555 4830 3497 2451 68 249 32 N ATOM 3883 CA ASN A 555 -69.602 13.838 -5.474 1.00 32.55 C ANISOU 3883 CA ASN A 555 5358 4070 2939 29 267 27 C ATOM 3884 C ASN A 555 -70.908 13.085 -5.720 1.00 30.93 C ANISOU 3884 C ASN A 555 5157 3854 2742 3 291 22 C ATOM 3885 O ASN A 555 -71.357 12.309 -4.861 1.00 30.37 O ANISOU 3885 O ASN A 555 5097 3802 2640 -33 303 51 O ATOM 3886 CB ASN A 555 -69.875 15.255 -4.952 1.00 28.32 C ANISOU 3886 CB ASN A 555 4789 3579 2393 24 272 -28 C ATOM 3887 CG ASN A 555 -70.546 16.158 -5.993 1.00 31.77 C ANISOU 3887 CG ASN A 555 5199 3994 2879 40 275 -75 C ATOM 3888 ND2 ASN A 555 -70.770 17.430 -5.618 1.00 28.60 N ANISOU 3888 ND2 ASN A 555 4761 3617 2490 39 275 -127 N ATOM 3889 OD1 ASN A 555 -70.866 15.719 -7.118 1.00 28.68 O ANISOU 3889 OD1 ASN A 555 4814 3565 2517 52 276 -67 O ATOM 3890 N ALA A 556 -71.525 13.287 -6.892 1.00 31.75 N ANISOU 3890 N ALA A 556 5250 3930 2885 17 297 -10 N ATOM 3891 CA ALA A 556 -72.762 12.568 -7.186 1.00 28.76 C ANISOU 3891 CA ALA A 556 4872 3539 2517 -6 319 -19 C ATOM 3892 C ALA A 556 -72.511 11.084 -7.316 1.00 28.48 C ANISOU 3892 C ALA A 556 4861 3465 2496 -10 317 28 C ATOM 3893 O ALA A 556 -73.378 10.276 -6.983 1.00 30.60 O ANISOU 3893 O ALA A 556 5136 3730 2763 -42 334 39 O ATOM 3894 CB ALA A 556 -73.420 13.097 -8.456 1.00 27.94 C ANISOU 3894 CB ALA A 556 4748 3419 2451 12 322 -62 C ATOM 3895 N GLU A 557 -71.340 10.706 -7.809 1.00 29.38 N ANISOU 3895 N GLU A 557 4985 3547 2632 19 294 53 N ATOM 3896 CA GLU A 557 -70.997 9.297 -7.894 1.00 29.35 C ANISOU 3896 CA GLU A 557 4996 3497 2657 18 285 94 C ATOM 3897 C GLU A 557 -70.854 8.698 -6.521 1.00 29.47 C ANISOU 3897 C GLU A 557 5028 3525 2644 -14 281 153 C ATOM 3898 O GLU A 557 -71.087 7.499 -6.332 1.00 31.49 O ANISOU 3898 O GLU A 557 5293 3745 2926 -33 280 192 O ATOM 3899 CB GLU A 557 -69.702 9.131 -8.655 1.00 29.12 C ANISOU 3899 CB GLU A 557 4966 3437 2660 57 260 98 C ATOM 3900 CG GLU A 557 -69.897 9.248 -10.114 1.00 34.24 C ANISOU 3900 CG GLU A 557 5596 4074 3340 79 265 51 C ATOM 3901 CD GLU A 557 -70.771 8.143 -10.601 1.00 33.96 C ANISOU 3901 CD GLU A 557 5556 4006 3342 65 279 39 C ATOM 3902 OE1 GLU A 557 -70.620 7.033 -10.055 1.00 37.43 O ANISOU 3902 OE1 GLU A 557 6006 4407 3808 53 273 76 O ATOM 3903 OE2 GLU A 557 -71.577 8.359 -11.530 1.00 31.69 O1- ANISOU 3903 OE2 GLU A 557 5251 3728 3063 66 294 -5 O1- ATOM 3904 N VAL A 558 -70.430 9.516 -5.564 1.00 32.97 N ANISOU 3904 N VAL A 558 5472 4021 3036 -21 276 161 N ATOM 3905 CA VAL A 558 -70.367 9.063 -4.193 1.00 29.75 C ANISOU 3905 CA VAL A 558 5075 3647 2584 -58 272 217 C ATOM 3906 C VAL A 558 -71.777 8.960 -3.632 1.00 31.02 C ANISOU 3906 C VAL A 558 5228 3845 2713 -106 304 207 C ATOM 3907 O VAL A 558 -72.152 7.938 -3.043 1.00 30.58 O ANISOU 3907 O VAL A 558 5181 3784 2653 -143 307 263 O ATOM 3908 CB VAL A 558 -69.460 10.019 -3.404 1.00 30.89 C ANISOU 3908 CB VAL A 558 5213 3844 2678 -49 257 216 C ATOM 3909 CG1 VAL A 558 -69.402 9.627 -1.946 1.00 31.95 C ANISOU 3909 CG1 VAL A 558 5353 4035 2753 -92 253 274 C ATOM 3910 CG2 VAL A 558 -68.069 10.017 -4.026 1.00 29.47 C ANISOU 3910 CG2 VAL A 558 5039 3622 2535 -2 226 227 C ATOM 3911 N PHE A 559 -72.603 9.977 -3.890 1.00 29.75 N ANISOU 3911 N PHE A 559 5047 3716 2542 -107 327 136 N ATOM 3912 CA PHE A 559 -73.986 9.974 -3.421 1.00 31.53 C ANISOU 3912 CA PHE A 559 5259 3980 2741 -152 359 111 C ATOM 3913 C PHE A 559 -74.724 8.704 -3.825 1.00 30.25 C ANISOU 3913 C PHE A 559 5108 3769 2617 -171 370 141 C ATOM 3914 O PHE A 559 -75.434 8.100 -3.014 1.00 31.26 O ANISOU 3914 O PHE A 559 5236 3925 2716 -220 387 173 O ATOM 3915 CB PHE A 559 -74.723 11.210 -3.945 1.00 31.18 C ANISOU 3915 CB PHE A 559 5186 3953 2706 -138 375 25 C ATOM 3916 CG PHE A 559 -74.207 12.509 -3.378 1.00 33.04 C ANISOU 3916 CG PHE A 559 5401 4241 2913 -128 367 -14 C ATOM 3917 CD1 PHE A 559 -73.524 12.528 -2.169 1.00 31.73 C ANISOU 3917 CD1 PHE A 559 5237 4129 2690 -148 360 18 C ATOM 3918 CD2 PHE A 559 -74.414 13.708 -4.046 1.00 31.30 C ANISOU 3918 CD2 PHE A 559 5153 4013 2726 -101 366 -80 C ATOM 3919 CE1 PHE A 559 -73.051 13.714 -1.633 1.00 32.10 C ANISOU 3919 CE1 PHE A 559 5258 4225 2715 -140 353 -27 C ATOM 3920 CE2 PHE A 559 -73.946 14.897 -3.515 1.00 32.77 C ANISOU 3920 CE2 PHE A 559 5313 4238 2901 -92 357 -119 C ATOM 3921 CZ PHE A 559 -73.263 14.900 -2.299 1.00 31.29 C ANISOU 3921 CZ PHE A 559 5126 4106 2656 -111 353 -98 C ATOM 3922 N LYS A 560 -74.565 8.286 -5.078 1.00 31.75 N ANISOU 3922 N LYS A 560 5302 3891 2872 -135 362 128 N ATOM 3923 CA LYS A 560 -75.202 7.065 -5.556 1.00 30.15 C ANISOU 3923 CA LYS A 560 5103 3634 2718 -149 370 145 C ATOM 3924 C LYS A 560 -74.573 5.826 -4.933 1.00 30.77 C ANISOU 3924 C LYS A 560 5198 3678 2815 -166 350 232 C ATOM 3925 O LYS A 560 -75.253 4.806 -4.772 1.00 33.84 O ANISOU 3925 O LYS A 560 5587 4038 3231 -199 360 265 O ATOM 3926 CB LYS A 560 -75.095 7.012 -7.081 1.00 34.13 C ANISOU 3926 CB LYS A 560 5599 4086 3282 -106 365 98 C ATOM 3927 CG LYS A 560 -75.745 8.191 -7.821 1.00 29.22 C ANISOU 3927 CG LYS A 560 4957 3494 2652 -89 378 24 C ATOM 3928 CD LYS A 560 -75.683 8.000 -9.316 1.00 28.91 C ANISOU 3928 CD LYS A 560 4906 3417 2662 -55 371 -12 C ATOM 3929 CE LYS A 560 -74.246 8.025 -9.775 1.00 28.73 C ANISOU 3929 CE LYS A 560 4888 3375 2653 -17 343 5 C ATOM 3930 NZ LYS A 560 -74.168 7.776 -11.236 1.00 30.84 N1+ ANISOU 3930 NZ LYS A 560 5138 3620 2961 11 339 -34 N1+ ATOM 3931 N ALA A 561 -73.290 5.904 -4.542 1.00 32.08 N ANISOU 3931 N ALA A 561 5376 3845 2970 -147 319 274 N ATOM 3932 CA ALA A 561 -72.597 4.769 -3.931 1.00 31.74 C ANISOU 3932 CA ALA A 561 5344 3765 2952 -160 291 364 C ATOM 3933 C ALA A 561 -72.901 4.597 -2.439 1.00 35.37 C ANISOU 3933 C ALA A 561 5808 4289 3343 -218 295 434 C ATOM 3934 O ALA A 561 -72.890 3.465 -1.938 1.00 38.92 O ANISOU 3934 O ALA A 561 6262 4706 3819 -248 280 517 O ATOM 3935 CB ALA A 561 -71.089 4.919 -4.119 1.00 31.15 C ANISOU 3935 CB ALA A 561 5275 3667 2893 -115 255 379 C ATOM 3936 N LEU A 562 -73.133 5.681 -1.702 1.00 34.30 N ANISOU 3936 N LEU A 562 5666 4246 3122 -236 312 404 N ATOM 3937 CA LEU A 562 -73.261 5.575 -0.252 1.00 35.51 C ANISOU 3937 CA LEU A 562 5816 4480 3195 -293 313 467 C ATOM 3938 C LEU A 562 -74.513 4.792 0.147 1.00 38.68 C ANISOU 3938 C LEU A 562 6212 4893 3591 -353 340 500 C ATOM 3939 O LEU A 562 -75.530 4.807 -0.551 1.00 38.26 O ANISOU 3939 O LEU A 562 6151 4815 3570 -354 369 440 O ATOM 3940 CB LEU A 562 -73.283 6.966 0.372 1.00 33.40 C ANISOU 3940 CB LEU A 562 5532 4314 2843 -298 329 405 C ATOM 3941 CG LEU A 562 -71.934 7.636 0.131 1.00 34.67 C ANISOU 3941 CG LEU A 562 5698 4464 3012 -245 299 390 C ATOM 3942 CD1 LEU A 562 -71.862 8.915 0.908 1.00 35.29 C ANISOU 3942 CD1 LEU A 562 5754 4641 3013 -255 310 335 C ATOM 3943 CD2 LEU A 562 -70.794 6.724 0.532 1.00 34.48 C ANISOU 3943 CD2 LEU A 562 5691 4407 3002 -240 257 488 C ATOM 3944 N GLU A 563 -74.413 4.077 1.276 1.00 39.92 N ANISOU 3944 N GLU A 563 6371 5089 3708 -406 327 601 N ATOM 3945 CA GLU A 563 -75.527 3.338 1.862 1.00 39.88 C ANISOU 3945 CA GLU A 563 6358 5111 3684 -475 350 649 C ATOM 3946 C GLU A 563 -75.634 3.707 3.337 1.00 39.20 C ANISOU 3946 C GLU A 563 6257 5162 3476 -538 359 691 C ATOM 3947 O GLU A 563 -74.605 3.762 4.033 1.00 43.03 O ANISOU 3947 O GLU A 563 6746 5684 3918 -537 325 751 O ATOM 3948 CB GLU A 563 -75.356 1.809 1.694 1.00 39.32 C ANISOU 3948 CB GLU A 563 6296 4939 3705 -486 321 753 C ATOM 3949 CG GLU A 563 -75.953 1.285 0.383 1.00 40.79 C ANISOU 3949 CG GLU A 563 6481 5017 4000 -455 335 697 C ATOM 3950 CD GLU A 563 -76.726 -0.015 0.519 1.00 39.53 C ANISOU 3950 CD GLU A 563 6314 4804 3900 -504 338 770 C ATOM 3951 OE1 GLU A 563 -77.984 0.005 0.630 1.00 35.75 O ANISOU 3951 OE1 GLU A 563 5825 4363 3397 -548 380 740 O ATOM 3952 OE2 GLU A 563 -76.067 -1.071 0.479 1.00 41.88 O1- ANISOU 3952 OE2 GLU A 563 6615 5017 4282 -498 298 854 O1- ATOM 3953 N PRO A 564 -76.837 3.997 3.840 1.00 39.75 N ANISOU 3953 N PRO A 564 6306 5316 3483 -594 402 653 N ATOM 3954 CA PRO A 564 -77.006 4.238 5.281 1.00 44.33 C ANISOU 3954 CA PRO A 564 6864 6042 3939 -664 413 692 C ATOM 3955 C PRO A 564 -76.790 2.976 6.099 1.00 45.82 C ANISOU 3955 C PRO A 564 7059 6236 4115 -722 386 851 C ATOM 3956 O PRO A 564 -77.215 1.887 5.716 1.00 48.61 O ANISOU 3956 O PRO A 564 7422 6501 4548 -737 381 914 O ATOM 3957 CB PRO A 564 -78.459 4.718 5.399 1.00 40.33 C ANISOU 3957 CB PRO A 564 6329 5605 3391 -707 469 603 C ATOM 3958 CG PRO A 564 -78.810 5.206 4.068 1.00 43.62 C ANISOU 3958 CG PRO A 564 6750 5929 3894 -643 483 495 C ATOM 3959 CD PRO A 564 -78.034 4.383 3.083 1.00 40.17 C ANISOU 3959 CD PRO A 564 6346 5351 3565 -588 445 549 C ATOM 3960 N THR A 565 -76.141 3.134 7.248 1.00 45.58 N ANISOU 3960 N THR A 565 7018 6313 3987 -758 365 916 N ATOM 3961 CA THR A 565 -75.856 1.999 8.122 1.00 57.35 C ANISOU 3961 CA THR A 565 8511 7822 5458 -817 331 1082 C ATOM 3962 C THR A 565 -77.055 1.716 9.020 1.00 64.56 C ANISOU 3962 C THR A 565 9396 8850 6283 -916 370 1119 C ATOM 3963 O THR A 565 -77.384 2.509 9.905 1.00 66.48 O ANISOU 3963 O THR A 565 9609 9253 6399 -962 399 1070 O ATOM 3964 CB THR A 565 -74.597 2.263 8.940 1.00 52.56 C ANISOU 3964 CB THR A 565 7903 7286 4782 -813 288 1143 C ATOM 3965 CG2 THR A 565 -73.402 2.430 8.016 1.00 50.73 C ANISOU 3965 CG2 THR A 565 7697 6932 4645 -718 249 1113 C ATOM 3966 OG1 THR A 565 -74.777 3.461 9.714 1.00 48.49 O ANISOU 3966 OG1 THR A 565 7356 6932 4134 -839 319 1053 O ATOM 3967 N GLY A 566 -77.705 0.581 8.796 1.00 87.97 N ANISOU 3967 N GLY A 566 12367 11738 9320 -950 371 1200 N ATOM 3968 CA GLY A 566 -78.824 0.172 9.623 1.00 90.69 C ANISOU 3968 CA GLY A 566 12685 12183 9591 -1049 405 1251 C ATOM 3969 C GLY A 566 -78.361 -0.512 10.897 1.00 99.37 C ANISOU 3969 C GLY A 566 13772 13374 10609 -1126 369 1424 C ATOM 3970 O GLY A 566 -77.289 -1.111 10.946 1.00100.03 O ANISOU 3970 O GLY A 566 13874 13389 10744 -1101 308 1535 O ATOM 3971 N LYS A 567 -79.189 -0.407 11.935 1.00 90.95 N ANISOU 3971 N LYS A 567 12671 12473 9414 -1221 405 1446 N ATOM 3972 CA LYS A 567 -78.928 -1.055 13.223 1.00 92.29 C ANISOU 3972 CA LYS A 567 12822 12759 9486 -1312 376 1618 C ATOM 3973 C LYS A 567 -80.190 -1.731 13.756 1.00 93.07 C ANISOU 3973 C LYS A 567 12893 12925 9543 -1417 412 1687 C ATOM 3974 O LYS A 567 -80.273 -2.082 14.938 1.00 88.28 O ANISOU 3974 O LYS A 567 12258 12463 8820 -1513 405 1810 O ATOM 3975 CB LYS A 567 -78.414 -0.050 14.258 1.00 88.66 C ANISOU 3975 CB LYS A 567 12334 12495 8859 -1337 379 1579 C ATOM 3976 CG LYS A 567 -77.152 0.685 13.858 1.00 87.83 C ANISOU 3976 CG LYS A 567 12249 12341 8782 -1242 344 1513 C ATOM 3977 CD LYS A 567 -75.956 -0.245 13.759 1.00 87.00 C ANISOU 3977 CD LYS A 567 12173 12119 8762 -1210 266 1668 C ATOM 3978 CE LYS A 567 -74.691 0.547 13.458 1.00 83.32 C ANISOU 3978 CE LYS A 567 11722 11626 8308 -1122 235 1598 C ATOM 3979 NZ LYS A 567 -74.846 1.415 12.252 1.00 67.08 N1+ ANISOU 3979 NZ LYS A 567 9683 9474 6331 -1033 269 1416 N1+ ATOM 3980 OXT LYS A 567 -81.153 -1.932 13.014 1.00 93.93 O1- ANISOU 3980 OXT LYS A 567 13006 12951 9733 -1409 451 1620 O1- TER HETATM 3981 MG MG C 1 -70.636 14.648 -21.200 1.00 33.93 Mg HETATM 3982 MG MG C 2 -49.801 16.153 -14.601 1.00 42.61 Mg END If you find results from this site helpful for your research, please cite one of our papers:
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