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*** ***elNémo ID: 230302160037112688Job options:ID = 230302160037112688 JOBID = USERID = unknown PRIVAT = 0 NMODES = 5 DQMIN = -100 DQMAX = 100 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = 0 DORMSD = on NRBL = 0 CUTOFF = 0 CAONLY = 0 Input data for this run:CRYST1 46.841 97.136 128.119 90.00 90.00 90.00 P 21 21 21 1 MODEL 1 ATOM 1 N LEU B 7 10.251 22.880 41.314 1.00 89.38 N ATOM 2 CA LEU B 7 9.976 21.558 41.871 1.00 92.16 C ATOM 3 C LEU B 7 8.475 21.273 41.870 1.00 90.60 C ATOM 4 O LEU B 7 8.045 20.134 42.067 1.00 86.68 O ATOM 5 CB LEU B 7 10.551 21.439 43.272 1.00 92.82 C ATOM 6 N ASN B 8 7.689 22.329 41.683 1.00101.52 N ATOM 7 CA ASN B 8 6.306 22.211 41.236 1.00 96.09 C ATOM 8 C ASN B 8 6.147 23.133 40.025 1.00 82.83 C ATOM 9 O ASN B 8 7.116 23.772 39.609 1.00 81.83 O ATOM 10 CB ASN B 8 5.309 22.503 42.363 1.00 99.15 C ATOM 11 CG ASN B 8 5.245 21.370 43.385 1.00107.79 C ATOM 12 ND2 ASN B 8 4.113 20.676 43.437 1.00106.21 N ATOM 13 OD1 ASN B 8 6.211 21.121 44.112 1.00112.58 O ATOM 14 N VAL B 9 4.950 23.211 39.457 1.00 52.72 N ATOM 15 CA VAL B 9 4.829 23.653 38.064 1.00 43.83 C ATOM 16 C VAL B 9 4.834 25.160 37.807 1.00 40.59 C ATOM 17 O VAL B 9 3.993 25.906 38.312 1.00 40.91 O ATOM 18 CB VAL B 9 3.635 22.977 37.372 1.00 41.45 C ATOM 19 CG1 VAL B 9 3.521 23.434 35.931 1.00 34.30 C ATOM 20 CG2 VAL B 9 3.808 21.472 37.427 1.00 35.44 C ATOM 21 N ILE B 10 5.791 25.583 36.990 1.00 37.92 N ANISOU 21 N ILE B 10 4714 4345 5346 342 356 -258 N ATOM 22 CA ILE B 10 5.994 26.988 36.657 1.00 42.12 C ANISOU 22 CA ILE B 10 5293 4812 5898 349 363 -262 C ATOM 23 C ILE B 10 5.087 27.463 35.513 1.00 38.30 C ANISOU 23 C ILE B 10 4795 4298 5461 385 343 -213 C ATOM 24 O ILE B 10 4.977 26.808 34.474 1.00 31.79 O ANISOU 24 O ILE B 10 3942 3499 4636 376 305 -174 O ATOM 25 CB ILE B 10 7.481 27.227 36.330 1.00 40.44 C ANISOU 25 CB ILE B 10 5122 4595 5650 289 345 -279 C ATOM 26 CG1 ILE B 10 8.310 27.113 37.617 1.00 42.24 C ANISOU 26 CG1 ILE B 10 5373 4839 5840 260 366 -332 C ATOM 27 CG2 ILE B 10 7.684 28.569 35.664 1.00 38.34 C ANISOU 27 CG2 ILE B 10 4903 4261 5404 288 344 -271 C ATOM 28 CD1 ILE B 10 9.809 26.914 37.390 1.00 51.25 C ANISOU 28 CD1 ILE B 10 6531 5999 6943 198 343 -348 C ATOM 29 N LYS B 11 4.424 28.596 35.730 1.00 36.31 N ANISOU 29 N LYS B 11 4563 3987 5246 429 368 -217 N ATOM 30 CA LYS B 11 3.512 29.181 34.753 1.00 33.25 C ANISOU 30 CA LYS B 11 4164 3563 4908 472 348 -171 C ATOM 31 C LYS B 11 4.276 30.096 33.812 1.00 33.82 C ANISOU 31 C LYS B 11 4292 3583 4974 445 324 -156 C ATOM 32 O LYS B 11 4.694 31.178 34.215 1.00 36.40 O ANISOU 32 O LYS B 11 4674 3853 5302 442 348 -183 O ATOM 33 CB LYS B 11 2.462 30.017 35.484 1.00 38.08 C ANISOU 33 CB LYS B 11 4772 4131 5566 538 390 -184 C ATOM 34 CG LYS B 11 1.027 29.605 35.235 1.00 38.59 C ANISOU 34 CG LYS B 11 4767 4217 5679 594 384 -147 C ATOM 35 CD LYS B 11 0.637 28.402 36.075 1.00 41.84 C ANISOU 35 CD LYS B 11 5125 4697 6075 591 406 -162 C ATOM 36 CE LYS B 11 -0.676 28.654 36.826 1.00 42.13 C ANISOU 36 CE LYS B 11 5118 4728 6160 656 450 -169 C ATOM 37 NZ LYS B 11 -0.466 29.369 38.122 1.00 43.40 N1+ ANISOU 37 NZ LYS B 11 5324 4857 6310 669 512 -227 N1+ ATOM 38 N MET B 12 4.456 29.681 32.566 1.00 26.31 N ANISOU 38 N MET B 12 3332 2651 4015 421 279 -113 N ATOM 39 CA MET B 12 5.196 30.497 31.612 1.00 30.30 C ANISOU 39 CA MET B 12 3893 3111 4511 389 258 -95 C ATOM 40 C MET B 12 4.207 31.196 30.690 1.00 28.54 C ANISOU 40 C MET B 12 3672 2840 4332 435 232 -44 C ATOM 41 O MET B 12 3.032 30.843 30.668 1.00 27.80 O ANISOU 41 O MET B 12 3525 2762 4274 486 224 -20 O ATOM 42 CB MET B 12 6.158 29.618 30.807 1.00 22.67 C ANISOU 42 CB MET B 12 2922 2193 3498 327 228 -84 C ATOM 43 CG MET B 12 7.265 29.016 31.651 1.00 28.43 C ANISOU 43 CG MET B 12 3653 2965 4186 280 248 -133 C ATOM 44 SD MET B 12 8.274 27.888 30.690 1.00 23.89 S ANISOU 44 SD MET B 12 3062 2450 3565 220 216 -120 S ATOM 45 CE MET B 12 9.692 27.688 31.778 1.00 26.22 C ANISOU 45 CE MET B 12 3370 2771 3821 170 241 -182 C ATOM 46 N LYS B 13 4.670 32.194 29.944 1.00 28.75 N ANISOU 46 N LYS B 13 3758 2808 4357 418 219 -26 N ATOM 47 CA LYS B 13 3.796 32.864 28.979 1.00 27.35 C ANISOU 47 CA LYS B 13 3590 2584 4220 460 186 28 C ATOM 48 C LYS B 13 4.354 32.742 27.584 1.00 27.18 C ANISOU 48 C LYS B 13 3595 2566 4166 412 142 71 C ATOM 49 O LYS B 13 5.565 32.686 27.406 1.00 24.97 O ANISOU 49 O LYS B 13 3351 2296 3841 347 148 53 O ATOM 50 CB LYS B 13 3.639 34.347 29.324 1.00 34.51 C ANISOU 50 CB LYS B 13 4553 3398 5160 494 209 18 C ATOM 51 CG LYS B 13 2.636 34.605 30.418 1.00 38.70 C ANISOU 51 CG LYS B 13 5052 3913 5738 565 246 -7 C ATOM 52 CD LYS B 13 3.302 35.225 31.621 1.00 41.46 C ANISOU 52 CD LYS B 13 5448 4230 6074 551 299 -71 C ATOM 53 CE LYS B 13 3.875 36.598 31.285 1.00 43.95 C ANISOU 53 CE LYS B 13 5852 4456 6393 535 299 -70 C ATOM 54 NZ LYS B 13 4.412 37.269 32.504 1.00 50.98 N1+ ANISOU 54 NZ LYS B 13 6789 5308 7272 524 350 -134 N1+ ATOM 55 N SER B 14 3.464 32.723 26.598 1.00 28.59 N ANISOU 55 N SER B 14 3757 2738 4367 444 98 128 N ATOM 56 CA SER B 14 3.853 32.676 25.198 1.00 30.97 C ANISOU 56 CA SER B 14 4092 3039 4638 402 54 174 C ATOM 57 C SER B 14 4.829 33.802 24.869 1.00 31.52 C ANISOU 57 C SER B 14 4246 3044 4686 360 64 171 C ATOM 58 O SER B 14 5.785 33.611 24.110 1.00 27.75 O ANISOU 58 O SER B 14 3802 2582 4160 295 55 178 O ATOM 59 CB SER B 14 2.614 32.764 24.307 1.00 29.61 C ANISOU 59 CB SER B 14 3896 2852 4501 453 2 236 C ATOM 60 OG SER B 14 1.696 31.727 24.624 1.00 32.34 O ANISOU 60 OG SER B 14 4160 3259 4869 487 -7 239 O ATOM 61 N SER B 15 4.607 34.961 25.481 1.00 31.97 N ANISOU 61 N SER B 15 4339 3028 4779 396 88 157 N ATOM 62 CA SER B 15 5.477 36.111 25.251 1.00 30.60 C ANISOU 62 CA SER B 15 4251 2785 4590 356 100 153 C ATOM 63 C SER B 15 6.895 35.920 25.803 1.00 30.95 C ANISOU 63 C SER B 15 4315 2856 4588 281 137 99 C ATOM 64 O SER B 15 7.796 36.695 25.468 1.00 29.72 O ANISOU 64 O SER B 15 4225 2656 4409 229 144 97 O ATOM 65 CB SER B 15 4.840 37.384 25.815 1.00 34.58 C ANISOU 65 CB SER B 15 4792 3200 5149 417 117 148 C ATOM 66 OG SER B 15 4.607 37.271 27.209 1.00 32.94 O ANISOU 66 OG SER B 15 4550 3003 4961 451 162 92 O ATOM 67 N ASP B 16 7.103 34.890 26.629 1.00 26.79 N ANISOU 67 N ASP B 16 3732 2401 4047 274 157 57 N ATOM 68 CA ASP B 16 8.443 34.575 27.139 1.00 25.43 C ANISOU 68 CA ASP B 16 3568 2262 3831 205 185 8 C ATOM 69 C ASP B 16 9.288 33.886 26.070 1.00 25.06 C ANISOU 69 C ASP B 16 3520 2264 3738 141 164 28 C ATOM 70 O ASP B 16 10.479 33.612 26.289 1.00 22.96 O ANISOU 70 O ASP B 16 3259 2031 3436 80 183 -6 O ATOM 71 CB ASP B 16 8.361 33.639 28.356 1.00 27.44 C ANISOU 71 CB ASP B 16 3763 2578 4084 221 209 -39 C ATOM 72 CG ASP B 16 7.766 34.308 29.579 1.00 33.06 C ANISOU 72 CG ASP B 16 4482 3247 4832 272 242 -73 C ATOM 73 OD1 ASP B 16 7.893 35.546 29.698 1.00 33.41 O ANISOU 73 OD1 ASP B 16 4588 3215 4892 274 256 -80 O ATOM 74 OD2 ASP B 16 7.186 33.589 30.429 1.00 34.10 O1- ANISOU 74 OD2 ASP B 16 4561 3420 4973 307 257 -94 O1- ATOM 75 N PHE B 17 8.673 33.612 24.918 1.00 25.72 N ANISOU 75 N PHE B 17 3598 2355 3821 155 125 84 N ATOM 76 CA PHE B 17 9.267 32.727 23.919 1.00 28.64 C ANISOU 76 CA PHE B 17 3957 2780 4145 104 106 102 C ATOM 77 C PHE B 17 9.327 33.307 22.511 1.00 32.64 C ANISOU 77 C PHE B 17 4520 3250 4633 78 77 156 C ATOM 78 O PHE B 17 8.416 34.009 22.070 1.00 33.01 O ANISOU 78 O PHE B 17 4592 3242 4709 121 50 200 O ATOM 79 CB PHE B 17 8.480 31.410 23.837 1.00 28.28 C ANISOU 79 CB PHE B 17 3842 2802 4102 137 82 114 C ATOM 80 CG PHE B 17 8.606 30.541 25.056 1.00 27.50 C ANISOU 80 CG PHE B 17 3688 2755 4006 147 108 63 C ATOM 81 CD1 PHE B 17 9.699 29.696 25.208 1.00 21.38 C ANISOU 81 CD1 PHE B 17 2895 2037 3191 95 122 29 C ATOM 82 CD2 PHE B 17 7.622 30.549 26.034 1.00 20.19 C ANISOU 82 CD2 PHE B 17 2727 1823 3122 208 118 51 C ATOM 83 CE1 PHE B 17 9.817 28.882 26.315 1.00 22.29 C ANISOU 83 CE1 PHE B 17 2964 2198 3306 104 141 -13 C ATOM 84 CE2 PHE B 17 7.729 29.734 27.157 1.00 24.98 C ANISOU 84 CE2 PHE B 17 3289 2479 3725 213 142 8 C ATOM 85 CZ PHE B 17 8.841 28.903 27.303 1.00 19.11 C ANISOU 85 CZ PHE B 17 2534 1788 2940 161 151 -23 C ATOM 86 N LEU B 18 10.409 32.982 21.807 1.00 28.87 N ANISOU 86 N LEU B 18 4061 2803 4106 8 82 154 N ATOM 87 CA LEU B 18 10.483 33.160 20.360 1.00 31.02 C ANISOU 87 CA LEU B 18 4379 3062 4346 -25 54 206 C ATOM 88 C LEU B 18 10.556 31.756 19.779 1.00 31.76 C ANISOU 88 C LEU B 18 4427 3236 4404 -41 39 209 C ATOM 89 O LEU B 18 11.393 30.972 20.196 1.00 32.12 O ANISOU 89 O LEU B 18 4439 3338 4429 -73 65 166 O ATOM 90 CB LEU B 18 11.735 33.955 19.987 1.00 33.11 C ANISOU 90 CB LEU B 18 4706 3297 4578 -99 82 198 C ATOM 91 CG LEU B 18 11.651 35.469 20.190 1.00 33.91 C ANISOU 91 CG LEU B 18 4875 3303 4705 -93 89 209 C ATOM 92 CD1 LEU B 18 12.974 36.136 19.852 1.00 39.28 C ANISOU 92 CD1 LEU B 18 5612 3962 5350 -178 119 198 C ATOM 93 CD2 LEU B 18 10.527 36.040 19.337 1.00 34.70 C ANISOU 93 CD2 LEU B 18 5012 3348 4823 -47 43 276 C ATOM 94 N GLU B 19 9.686 31.420 18.832 1.00 32.17 N ANISOU 94 N GLU B 19 4478 3294 4451 -18 -6 260 N ATOM 95 CA GLU B 19 9.558 30.023 18.411 1.00 32.33 C ANISOU 95 CA GLU B 19 4452 3387 4444 -24 -24 259 C ATOM 96 C GLU B 19 9.965 29.731 16.973 1.00 34.03 C ANISOU 96 C GLU B 19 4709 3620 4603 -76 -43 292 C ATOM 97 O GLU B 19 9.889 30.595 16.097 1.00 34.19 O ANISOU 97 O GLU B 19 4791 3591 4608 -92 -62 336 O ATOM 98 CB GLU B 19 8.122 29.532 18.626 1.00 31.71 C ANISOU 98 CB GLU B 19 4323 3319 4405 44 -63 283 C ATOM 99 CG GLU B 19 7.722 29.420 20.079 1.00 27.99 C ANISOU 99 CG GLU B 19 3798 2854 3982 92 -38 243 C ATOM 100 CD GLU B 19 6.249 29.119 20.246 1.00 32.50 C ANISOU 100 CD GLU B 19 4321 3430 4599 159 -73 270 C ATOM 101 OE1 GLU B 19 5.744 28.203 19.557 1.00 31.69 O ANISOU 101 OE1 GLU B 19 4191 3368 4480 159 -110 296 O ATOM 102 OE2 GLU B 19 5.595 29.807 21.060 1.00 32.70 O1- ANISOU 102 OE2 GLU B 19 4334 3417 4675 211 -62 265 O1- ATOM 103 N SER B 20 10.379 28.490 16.745 1.00 32.60 N ANISOU 103 N SER B 20 4493 3506 4387 -100 -38 270 N ATOM 104 CA SER B 20 10.601 27.980 15.399 1.00 34.60 C ANISOU 104 CA SER B 20 4778 3785 4585 -142 -57 298 C ATOM 105 C SER B 20 9.248 27.677 14.775 1.00 33.41 C ANISOU 105 C SER B 20 4620 3631 4442 -101 -119 349 C ATOM 106 O SER B 20 8.214 27.728 15.453 1.00 33.06 O ANISOU 106 O SER B 20 4535 3575 4451 -41 -141 357 O ATOM 107 CB SER B 20 11.415 26.690 15.461 1.00 33.97 C ANISOU 107 CB SER B 20 4659 3775 4471 -173 -31 253 C ATOM 108 OG SER B 20 10.617 25.602 15.926 1.00 31.60 O ANISOU 108 OG SER B 20 4299 3516 4194 -129 -54 244 O ATOM 109 N ALA B 21 9.253 27.361 13.480 1.00 34.13 N ANISOU 109 N ALA B 21 4751 3735 4481 -135 -147 383 N ATOM 110 CA ALA B 21 8.076 26.817 12.810 1.00 33.54 C ANISOU 110 CA ALA B 21 4666 3672 4405 -107 -210 426 C ATOM 111 C ALA B 21 7.794 25.433 13.380 1.00 32.38 C ANISOU 111 C ALA B 21 4445 3587 4269 -87 -210 391 C ATOM 112 O ALA B 21 8.635 24.868 14.084 1.00 27.63 O ANISOU 112 O ALA B 21 3815 3020 3665 -103 -163 338 O ATOM 113 CB ALA B 21 8.320 26.728 11.311 1.00 37.68 C ANISOU 113 CB ALA B 21 5257 4201 4860 -158 -234 463 C ATOM 114 N GLU B 22 6.617 24.885 13.080 1.00 33.23 N ANISOU 114 N GLU B 22 4526 3708 4391 -55 -266 423 N ATOM 115 CA GLU B 22 6.238 23.557 13.571 1.00 35.26 C ANISOU 115 CA GLU B 22 4718 4021 4659 -39 -271 396 C ATOM 116 C GLU B 22 7.236 22.500 13.130 1.00 37.91 C ANISOU 116 C GLU B 22 5065 4404 4936 -91 -245 360 C ATOM 117 O GLU B 22 7.674 22.502 11.979 1.00 35.25 O ANISOU 117 O GLU B 22 4785 4068 4541 -135 -253 377 O ATOM 118 CB GLU B 22 4.826 23.179 13.098 1.00 38.99 C ANISOU 118 CB GLU B 22 5166 4500 5150 -8 -341 443 C ATOM 119 CG GLU B 22 4.375 21.786 13.542 1.00 39.21 C ANISOU 119 CG GLU B 22 5130 4581 5187 2 -350 418 C ATOM 120 CD GLU B 22 2.890 21.532 13.320 1.00 42.92 C ANISOU 120 CD GLU B 22 5560 5056 5691 38 -416 462 C ATOM 121 OE1 GLU B 22 2.220 22.363 12.665 1.00 45.95 O ANISOU 121 OE1 GLU B 22 5969 5405 6085 54 -462 514 O ATOM 122 OE2 GLU B 22 2.394 20.496 13.813 1.00 43.51 O1- ANISOU 122 OE2 GLU B 22 5578 5170 5784 49 -423 445 O1- ATOM 123 N LEU B 23 7.596 21.611 14.054 1.00 32.07 N ANISOU 123 N LEU B 23 4273 3702 4210 -83 -213 311 N ATOM 124 CA LEU B 23 8.550 20.528 13.786 1.00 37.35 C ANISOU 124 CA LEU B 23 4944 4416 4833 -123 -185 271 C ATOM 125 C LEU B 23 7.905 19.306 13.114 1.00 43.30 C ANISOU 125 C LEU B 23 5689 5203 5560 -128 -228 282 C ATOM 126 O LEU B 23 6.704 19.052 13.280 1.00 36.47 O ANISOU 126 O LEU B 23 4791 4339 4727 -95 -273 309 O ATOM 127 CB LEU B 23 9.228 20.095 15.090 1.00 35.81 C ANISOU 127 CB LEU B 23 4699 4243 4664 -110 -137 215 C ATOM 128 CG LEU B 23 10.532 20.791 15.493 1.00 37.71 C ANISOU 128 CG LEU B 23 4956 4474 4899 -136 -82 181 C ATOM 129 CD1 LEU B 23 10.558 22.241 15.044 1.00 38.77 C ANISOU 129 CD1 LEU B 23 5141 4556 5033 -148 -82 214 C ATOM 130 CD2 LEU B 23 10.780 20.685 16.995 1.00 32.26 C ANISOU 130 CD2 LEU B 23 4213 3792 4251 -108 -51 139 C ATOM 131 N ASP B 24 8.707 18.546 12.369 1.00 58.50 N ANISOU 131 N ASP B 24 7643 7156 7427 -170 -211 261 N ATOM 132 CA ASP B 24 8.210 17.325 11.729 1.00 62.84 C ANISOU 132 CA ASP B 24 8192 7736 7947 -180 -247 264 C ATOM 133 C ASP B 24 8.341 16.126 12.670 1.00 60.96 C ANISOU 133 C ASP B 24 7898 7532 7730 -163 -229 219 C ATOM 134 O ASP B 24 7.965 15.002 12.328 1.00 64.89 O ANISOU 134 O ASP B 24 8392 8055 8210 -169 -255 214 O ATOM 135 CB ASP B 24 8.898 17.066 10.378 1.00 63.79 C ANISOU 135 CB ASP B 24 8380 7866 7991 -233 -241 264 C ATOM 136 CG ASP B 24 10.312 16.525 10.523 1.00 68.72 C ANISOU 136 CG ASP B 24 9005 8517 8589 -259 -176 207 C ATOM 137 OD1 ASP B 24 11.249 17.337 10.682 1.00 72.07 O ANISOU 137 OD1 ASP B 24 9442 8929 9011 -275 -129 193 O ATOM 138 OD2 ASP B 24 10.486 15.288 10.458 1.00 76.27 O1- ANISOU 138 OD2 ASP B 24 9948 9504 9526 -263 -172 176 O1- ATOM 139 N SER B 25 8.873 16.385 13.861 1.00 51.57 N ANISOU 139 N SER B 25 6672 6342 6580 -142 -186 186 N ATOM 140 CA SER B 25 8.923 15.396 14.934 1.00 45.94 C ANISOU 140 CA SER B 25 5906 5656 5894 -120 -171 149 C ATOM 141 C SER B 25 8.440 16.038 16.238 1.00 44.41 C ANISOU 141 C SER B 25 5666 5446 5761 -78 -163 149 C ATOM 142 O SER B 25 8.266 17.256 16.314 1.00 43.15 O ANISOU 142 O SER B 25 5519 5254 5622 -68 -162 171 O ATOM 143 CB SER B 25 10.351 14.894 15.120 1.00 45.76 C ANISOU 143 CB SER B 25 5885 5656 5847 -141 -120 97 C ATOM 144 OG SER B 25 11.187 15.938 15.597 1.00 47.97 O ANISOU 144 OG SER B 25 6167 5920 6139 -145 -79 82 O ATOM 145 N GLY B 26 8.230 15.229 17.271 1.00 37.61 N ANISOU 145 N GLY B 26 4758 4606 4928 -55 -157 125 N ATOM 146 CA GLY B 26 7.883 15.786 18.567 1.00 28.18 C ANISOU 146 CA GLY B 26 3524 3400 3785 -19 -141 119 C ATOM 147 C GLY B 26 6.569 15.271 19.121 1.00 27.74 C ANISOU 147 C GLY B 26 3423 3352 3765 12 -170 137 C ATOM 148 O GLY B 26 6.216 15.572 20.265 1.00 26.87 O ANISOU 148 O GLY B 26 3277 3236 3695 43 -153 128 O ATOM 149 N GLY B 27 5.840 14.513 18.306 1.00 27.86 N ANISOU 149 N GLY B 27 3440 3381 3766 2 -213 162 N ATOM 150 CA GLY B 27 4.632 13.831 18.750 1.00 26.72 C ANISOU 150 CA GLY B 27 3249 3251 3653 22 -242 178 C ATOM 151 C GLY B 27 3.337 14.627 18.694 1.00 30.86 C ANISOU 151 C GLY B 27 3748 3757 4220 52 -275 223 C ATOM 152 O GLY B 27 3.103 15.435 17.784 1.00 29.78 O ANISOU 152 O GLY B 27 3641 3597 4076 49 -302 257 O ATOM 153 N PHE B 28 2.506 14.389 19.703 1.00 27.62 N ANISOU 153 N PHE B 28 3282 3356 3855 81 -271 223 N ATOM 154 CA PHE B 28 1.148 14.929 19.835 1.00 26.25 C ANISOU 154 CA PHE B 28 3067 3173 3732 115 -299 262 C ATOM 155 C PHE B 28 1.113 16.460 19.951 1.00 28.25 C ANISOU 155 C PHE B 28 3332 3387 4015 146 -285 276 C ATOM 156 O PHE B 28 1.949 17.056 20.633 1.00 25.66 O ANISOU 156 O PHE B 28 3021 3043 3687 153 -238 245 O ATOM 157 CB PHE B 28 0.545 14.304 21.097 1.00 26.04 C ANISOU 157 CB PHE B 28 2981 3169 3744 136 -278 246 C ATOM 158 CG PHE B 28 -0.923 14.547 21.287 1.00 27.91 C ANISOU 158 CG PHE B 28 3160 3408 4035 168 -303 281 C ATOM 159 CD1 PHE B 28 -1.854 13.623 20.832 1.00 35.70 C ANISOU 159 CD1 PHE B 28 4116 4422 5028 153 -349 306 C ATOM 160 CD2 PHE B 28 -1.371 15.661 21.984 1.00 30.87 C ANISOU 160 CD2 PHE B 28 3511 3760 4460 214 -279 286 C ATOM 161 CE1 PHE B 28 -3.211 13.825 21.032 1.00 38.01 C ANISOU 161 CE1 PHE B 28 4345 4722 5375 181 -372 338 C ATOM 162 CE2 PHE B 28 -2.720 15.871 22.192 1.00 32.99 C ANISOU 162 CE2 PHE B 28 3718 4033 4783 247 -298 317 C ATOM 163 CZ PHE B 28 -3.644 14.950 21.716 1.00 38.28 C ANISOU 163 CZ PHE B 28 4350 4734 5461 231 -345 344 C ATOM 164 N GLY B 29 0.133 17.092 19.304 1.00 28.90 N ANISOU 164 N GLY B 29 3405 3452 4123 166 -329 323 N ATOM 165 CA GLY B 29 -0.022 18.540 19.386 1.00 24.70 C ANISOU 165 CA GLY B 29 2886 2876 3624 201 -321 341 C ATOM 166 C GLY B 29 0.801 19.294 18.357 1.00 25.92 C ANISOU 166 C GLY B 29 3113 2999 3735 175 -330 354 C ATOM 167 O GLY B 29 1.366 18.688 17.448 1.00 27.88 O ANISOU 167 O GLY B 29 3399 3263 3929 131 -348 354 O ATOM 168 N LYS B 30 0.856 20.622 18.492 1.00 24.45 N ANISOU 168 N LYS B 30 2949 2767 3574 202 -317 365 N ATOM 169 CA LYS B 30 1.682 21.452 17.620 1.00 25.24 C ANISOU 169 CA LYS B 30 3122 2832 3635 174 -318 377 C ATOM 170 C LYS B 30 3.014 21.719 18.299 1.00 25.83 C ANISOU 170 C LYS B 30 3224 2899 3690 153 -255 327 C ATOM 171 O LYS B 30 3.078 22.458 19.294 1.00 25.66 O ANISOU 171 O LYS B 30 3192 2852 3705 183 -218 307 O ATOM 172 CB LYS B 30 0.974 22.768 17.284 1.00 27.13 C ANISOU 172 CB LYS B 30 3378 3020 3913 213 -346 423 C ATOM 173 N VAL B 31 4.074 21.113 17.772 1.00 20.41 N ANISOU 173 N VAL B 31 2572 2236 2946 103 -242 305 N ATOM 174 CA VAL B 31 5.374 21.111 18.449 1.00 25.89 C ANISOU 174 CA VAL B 31 3279 2936 3622 79 -185 254 C ATOM 175 C VAL B 31 6.364 22.053 17.778 1.00 24.90 C ANISOU 175 C VAL B 31 3218 2778 3463 44 -167 257 C ATOM 176 O VAL B 31 6.528 22.028 16.556 1.00 29.35 O ANISOU 176 O VAL B 31 3826 3341 3986 12 -192 284 O ATOM 177 CB VAL B 31 5.980 19.685 18.507 1.00 25.36 C ANISOU 177 CB VAL B 31 3194 2921 3520 50 -173 219 C ATOM 178 CG1 VAL B 31 7.231 19.676 19.351 1.00 23.32 C ANISOU 178 CG1 VAL B 31 2936 2670 3252 35 -119 166 C ATOM 179 CG2 VAL B 31 4.970 18.715 19.100 1.00 25.10 C ANISOU 179 CG2 VAL B 31 3103 2918 3516 78 -193 220 C ATOM 180 N SER B 32 7.017 22.898 18.573 1.00 24.88 N ANISOU 180 N SER B 32 3227 2750 3478 47 -125 230 N ATOM 181 CA SER B 32 8.011 23.816 18.025 1.00 25.99 C ANISOU 181 CA SER B 32 3426 2858 3589 8 -104 230 C ATOM 182 C SER B 32 9.208 23.925 18.953 1.00 25.23 C ANISOU 182 C SER B 32 3326 2771 3491 -13 -49 176 C ATOM 183 O SER B 32 9.099 23.672 20.153 1.00 22.62 O ANISOU 183 O SER B 32 2953 2453 3190 14 -30 144 O ATOM 184 CB SER B 32 7.393 25.202 17.814 1.00 25.64 C ANISOU 184 CB SER B 32 3417 2751 3574 33 -121 271 C ATOM 185 OG SER B 32 6.904 25.719 19.048 1.00 25.55 O ANISOU 185 OG SER B 32 3374 2716 3618 81 -103 254 O ATOM 186 N LEU B 33 10.357 24.292 18.399 1.00 23.95 N ANISOU 186 N LEU B 33 3205 2603 3290 -64 -25 165 N ATOM 187 CA LEU B 33 11.488 24.678 19.228 1.00 22.64 C ANISOU 187 CA LEU B 33 3039 2437 3127 -87 22 119 C ATOM 188 C LEU B 33 11.219 26.097 19.717 1.00 25.09 C ANISOU 188 C LEU B 33 3377 2684 3472 -69 30 129 C ATOM 189 O LEU B 33 10.803 26.955 18.943 1.00 28.81 O ANISOU 189 O LEU B 33 3895 3110 3943 -69 10 172 O ATOM 190 CB LEU B 33 12.776 24.645 18.410 1.00 26.60 C ANISOU 190 CB LEU B 33 3573 2955 3580 -150 47 107 C ATOM 191 CG LEU B 33 13.662 23.422 18.594 1.00 33.30 C ANISOU 191 CG LEU B 33 4383 3865 4405 -171 69 63 C ATOM 192 CD1 LEU B 33 14.714 23.348 17.501 1.00 39.63 C ANISOU 192 CD1 LEU B 33 5217 4683 5157 -229 91 60 C ATOM 193 CD2 LEU B 33 14.319 23.493 19.965 1.00 34.55 C ANISOU 193 CD2 LEU B 33 4505 4032 4589 -165 100 14 C ATOM 194 N ALA B 34 11.459 26.355 20.996 1.00 25.34 N ANISOU 194 N ALA B 34 3387 2710 3532 -54 58 90 N ATOM 195 CA ALA B 34 11.180 27.674 21.538 1.00 27.09 C ANISOU 195 CA ALA B 34 3637 2869 3788 -33 68 94 C ATOM 196 C ALA B 34 12.342 28.192 22.374 1.00 29.84 C ANISOU 196 C ALA B 34 3996 3209 4132 -68 109 46 C ATOM 197 O ALA B 34 12.807 27.525 23.294 1.00 33.10 O ANISOU 197 O ALA B 34 4369 3663 4546 -69 128 3 O ATOM 198 CB ALA B 34 9.891 27.645 22.358 1.00 27.87 C ANISOU 198 CB ALA B 34 3699 2955 3933 35 54 101 C ATOM 199 N PHE B 35 12.802 29.390 22.049 1.00 22.33 N ANISOU 199 N PHE B 35 3101 2205 3178 -98 121 56 N ATOM 200 CA PHE B 35 13.836 30.049 22.820 1.00 26.30 C ANISOU 200 CA PHE B 35 3619 2691 3681 -135 157 13 C ATOM 201 C PHE B 35 13.176 30.963 23.849 1.00 28.21 C ANISOU 201 C PHE B 35 3876 2877 3966 -90 164 3 C ATOM 202 O PHE B 35 12.562 31.976 23.497 1.00 26.90 O ANISOU 202 O PHE B 35 3756 2646 3821 -70 153 36 O ATOM 203 CB PHE B 35 14.768 30.839 21.902 1.00 32.23 C ANISOU 203 CB PHE B 35 4428 3416 4404 -200 170 27 C ATOM 204 CG PHE B 35 16.115 31.085 22.492 1.00 30.59 C ANISOU 204 CG PHE B 35 4217 3220 4184 -256 205 -21 C ATOM 205 CD1 PHE B 35 16.377 32.255 23.192 1.00 32.14 C ANISOU 205 CD1 PHE B 35 4451 3360 4401 -269 223 -39 C ATOM 206 CD2 PHE B 35 17.118 30.136 22.362 1.00 31.27 C ANISOU 206 CD2 PHE B 35 4263 3375 4242 -296 220 -49 C ATOM 207 CE1 PHE B 35 17.623 32.475 23.754 1.00 36.58 C ANISOU 207 CE1 PHE B 35 5009 3937 4953 -325 252 -84 C ATOM 208 CE2 PHE B 35 18.370 30.343 22.920 1.00 34.67 C ANISOU 208 CE2 PHE B 35 4684 3823 4667 -347 250 -93 C ATOM 209 CZ PHE B 35 18.625 31.515 23.617 1.00 34.56 C ANISOU 209 CZ PHE B 35 4705 3754 4671 -364 264 -110 C ATOM 210 N HIS B 36 13.266 30.553 25.115 1.00 23.84 N ANISOU 210 N HIS B 36 3283 2350 3426 -72 181 -42 N ATOM 211 CA HIS B 36 12.792 31.347 26.247 1.00 20.43 C ANISOU 211 CA HIS B 36 2864 1871 3028 -36 196 -65 C ATOM 212 C HIS B 36 13.746 32.522 26.414 1.00 27.97 C ANISOU 212 C HIS B 36 3875 2776 3977 -86 219 -86 C ATOM 213 O HIS B 36 14.968 32.336 26.409 1.00 26.00 O ANISOU 213 O HIS B 36 3622 2558 3699 -147 233 -113 O ATOM 214 CB HIS B 36 12.785 30.486 27.513 1.00 21.26 C ANISOU 214 CB HIS B 36 2916 2025 3136 -15 209 -109 C ATOM 215 CG HIS B 36 12.208 31.172 28.716 1.00 26.05 C ANISOU 215 CG HIS B 36 3534 2591 3774 26 228 -135 C ATOM 216 CD2 HIS B 36 11.035 30.989 29.367 1.00 24.89 C ANISOU 216 CD2 HIS B 36 3361 2440 3656 91 230 -133 C ATOM 217 ND1 HIS B 36 12.871 32.172 29.394 1.00 28.64 N ANISOU 217 ND1 HIS B 36 3906 2875 4102 -1 252 -169 N ATOM 218 CE1 HIS B 36 12.124 32.586 30.405 1.00 27.10 C ANISOU 218 CE1 HIS B 36 3715 2649 3933 47 269 -189 C ATOM 219 NE2 HIS B 36 11.007 31.882 30.411 1.00 29.11 N ANISOU 219 NE2 HIS B 36 3926 2929 4207 104 258 -167 N ATOM 220 N ARG B 37 13.191 33.725 26.563 1.00 24.88 N ANISOU 220 N ARG B 37 3533 2306 3613 -60 223 -74 N ATOM 221 CA ARG B 37 13.994 34.951 26.494 1.00 27.74 C ANISOU 221 CA ARG B 37 3962 2608 3971 -111 240 -83 C ATOM 222 C ARG B 37 15.091 35.056 27.538 1.00 29.35 C ANISOU 222 C ARG B 37 4163 2828 4161 -158 267 -144 C ATOM 223 O ARG B 37 16.042 35.825 27.364 1.00 28.86 O ANISOU 223 O ARG B 37 4143 2736 4085 -221 280 -154 O ATOM 224 CB ARG B 37 13.105 36.194 26.576 1.00 30.98 C ANISOU 224 CB ARG B 37 4428 2926 4419 -66 238 -62 C ATOM 225 CG ARG B 37 12.201 36.371 25.376 1.00 29.15 C ANISOU 225 CG ARG B 37 4214 2664 4198 -32 205 4 C ATOM 226 CD ARG B 37 11.172 37.470 25.617 1.00 29.93 C ANISOU 226 CD ARG B 37 4354 2675 4344 32 201 23 C ATOM 227 NE ARG B 37 10.196 37.514 24.534 1.00 34.72 N ANISOU 227 NE ARG B 37 4965 3261 4964 73 162 88 N ATOM 228 CZ ARG B 37 10.415 38.105 23.364 1.00 35.07 C ANISOU 228 CZ ARG B 37 5068 3265 4991 40 141 136 C ATOM 229 NH1 ARG B 37 11.579 38.697 23.134 1.00 25.52 N1+ ANISOU 229 NH1 ARG B 37 3913 2032 3751 -37 160 124 N1+ ATOM 230 NH2 ARG B 37 9.478 38.102 22.424 1.00 34.07 N ANISOU 230 NH2 ARG B 37 4946 3124 4878 81 99 196 N ATOM 231 N THR B 38 14.963 34.304 28.627 1.00 25.27 N ANISOU 231 N THR B 38 3597 2357 3647 -131 274 -182 N ATOM 232 CA THR B 38 15.995 34.330 29.662 1.00 33.90 C ANISOU 232 CA THR B 38 4685 3470 4725 -175 293 -239 C ATOM 233 C THR B 38 16.546 32.945 30.007 1.00 36.75 C ANISOU 233 C THR B 38 4976 3923 5063 -187 287 -263 C ATOM 234 O THR B 38 17.666 32.826 30.518 1.00 37.88 O ANISOU 234 O THR B 38 5108 4097 5189 -237 295 -302 O ATOM 235 CB THR B 38 15.507 35.039 30.950 1.00 37.10 C ANISOU 235 CB THR B 38 5117 3827 5152 -140 310 -275 C ATOM 236 CG2 THR B 38 14.986 36.437 30.632 1.00 39.15 C ANISOU 236 CG2 THR B 38 5449 3988 5438 -124 316 -253 C ATOM 237 OG1 THR B 38 14.457 34.284 31.562 1.00 31.97 O ANISOU 237 OG1 THR B 38 4424 3206 4518 -70 309 -276 O ATOM 238 N GLN B 39 15.779 31.898 29.721 1.00 31.85 N ANISOU 238 N GLN B 39 4310 3346 4446 -141 272 -239 N ATOM 239 CA GLN B 39 16.158 30.560 30.185 1.00 30.37 C ANISOU 239 CA GLN B 39 4062 3238 4241 -142 266 -262 C ATOM 240 C GLN B 39 16.649 29.628 29.078 1.00 32.00 C ANISOU 240 C GLN B 39 4235 3497 4425 -167 252 -240 C ATOM 241 O GLN B 39 17.125 28.515 29.343 1.00 31.02 O ANISOU 241 O GLN B 39 4064 3437 4286 -173 247 -259 O ATOM 242 CB GLN B 39 15.013 29.928 30.983 1.00 32.70 C ANISOU 242 CB GLN B 39 4325 3547 4551 -75 263 -264 C ATOM 243 CG GLN B 39 14.537 30.792 32.148 1.00 35.32 C ANISOU 243 CG GLN B 39 4688 3829 4902 -47 283 -292 C ATOM 244 CD GLN B 39 13.520 30.088 33.027 1.00 37.35 C ANISOU 244 CD GLN B 39 4910 4110 5170 12 287 -299 C ATOM 245 NE2 GLN B 39 12.775 30.862 33.808 1.00 43.31 N ANISOU 245 NE2 GLN B 39 5692 4817 5948 50 308 -313 N ATOM 246 OE1 GLN B 39 13.406 28.865 33.005 1.00 38.31 O ANISOU 246 OE1 GLN B 39 4983 4293 5282 22 274 -292 O ATOM 247 N GLY B 40 16.545 30.076 27.833 1.00 25.29 N ANISOU 247 N GLY B 40 3416 2620 3572 -183 247 -200 N ATOM 248 CA GLY B 40 17.118 29.317 26.737 1.00 23.74 C ANISOU 248 CA GLY B 40 3200 2470 3349 -215 240 -183 C ATOM 249 C GLY B 40 16.176 28.349 26.039 1.00 26.78 C ANISOU 249 C GLY B 40 3559 2883 3733 -173 216 -147 C ATOM 250 O GLY B 40 14.951 28.415 26.195 1.00 22.99 O ANISOU 250 O GLY B 40 3079 2379 3276 -119 202 -124 O ATOM 251 N LEU B 41 16.763 27.442 25.263 1.00 24.32 N ANISOU 251 N LEU B 41 3223 2623 3394 -200 213 -144 N ATOM 252 CA LEU B 41 16.008 26.568 24.364 1.00 27.65 C ANISOU 252 CA LEU B 41 3631 3068 3806 -174 189 -108 C ATOM 253 C LEU B 41 15.194 25.494 25.097 1.00 25.11 C ANISOU 253 C LEU B 41 3261 2780 3498 -122 173 -115 C ATOM 254 O LEU B 41 15.665 24.890 26.061 1.00 25.53 O ANISOU 254 O LEU B 41 3281 2869 3553 -120 182 -153 O ATOM 255 CB LEU B 41 16.969 25.924 23.364 1.00 33.32 C ANISOU 255 CB LEU B 41 4342 3829 4488 -221 196 -110 C ATOM 256 CG LEU B 41 16.423 25.599 21.977 1.00 33.25 C ANISOU 256 CG LEU B 41 4354 3822 4458 -221 177 -65 C ATOM 257 CD1 LEU B 41 15.443 26.650 21.553 1.00 37.74 C ANISOU 257 CD1 LEU B 41 4971 4328 5042 -201 159 -20 C ATOM 258 CD2 LEU B 41 17.558 25.522 20.968 1.00 39.99 C ANISOU 258 CD2 LEU B 41 5223 4699 5273 -281 198 -68 C ATOM 259 N MET B 42 13.955 25.302 24.648 1.00 23.97 N ANISOU 259 N MET B 42 3117 2625 3367 -81 148 -77 N ATOM 260 CA MET B 42 13.004 24.342 25.225 1.00 18.64 C ANISOU 260 CA MET B 42 2398 1976 2707 -34 133 -75 C ATOM 261 C MET B 42 12.103 23.851 24.094 1.00 21.62 C ANISOU 261 C MET B 42 2775 2360 3080 -18 100 -29 C ATOM 262 O MET B 42 12.085 24.441 23.022 1.00 24.67 O ANISOU 262 O MET B 42 3200 2720 3455 -37 90 3 O ATOM 263 CB MET B 42 12.121 25.007 26.297 1.00 23.40 C ANISOU 263 CB MET B 42 3000 2544 3348 11 140 -80 C ATOM 264 CG MET B 42 12.854 25.829 27.344 1.00 24.74 C ANISOU 264 CG MET B 42 3187 2691 3523 -4 169 -120 C ATOM 265 SD MET B 42 11.757 26.565 28.583 1.00 22.48 S ANISOU 265 SD MET B 42 2904 2361 3276 52 183 -129 S ATOM 266 CE MET B 42 12.954 27.452 29.575 1.00 29.65 C ANISOU 266 CE MET B 42 3844 3247 4175 13 213 -181 C ATOM 267 N ILE B 43 11.336 22.788 24.336 1.00 18.92 N ANISOU 267 N ILE B 43 2393 2050 2745 13 82 -24 N ATOM 268 CA ILE B 43 10.333 22.323 23.380 1.00 16.87 C ANISOU 268 CA ILE B 43 2129 1795 2485 29 46 20 C ATOM 269 C ILE B 43 8.921 22.753 23.787 1.00 20.54 C ANISOU 269 C ILE B 43 2578 2233 2993 81 31 46 C ATOM 270 O ILE B 43 8.502 22.566 24.930 1.00 17.82 O ANISOU 270 O ILE B 43 2201 1896 2674 112 45 26 O ATOM 271 CB ILE B 43 10.382 20.782 23.238 1.00 19.22 C ANISOU 271 CB ILE B 43 2394 2148 2762 24 33 10 C ATOM 272 CG1 ILE B 43 11.759 20.360 22.736 1.00 18.29 C ANISOU 272 CG1 ILE B 43 2288 2056 2603 -23 50 -16 C ATOM 273 CG2 ILE B 43 9.287 20.287 22.285 1.00 23.44 C ANISOU 273 CG2 ILE B 43 2924 2687 3295 37 -8 54 C ATOM 274 CD1 ILE B 43 12.069 20.877 21.337 1.00 22.70 C ANISOU 274 CD1 ILE B 43 2893 2598 3134 -57 43 12 C ATOM 275 N MET B 44 8.192 23.342 22.846 1.00 18.09 N ANISOU 275 N MET B 44 2291 1892 2692 92 2 92 N ATOM 276 CA MET B 44 6.838 23.828 23.080 1.00 16.35 C ANISOU 276 CA MET B 44 2052 1644 2518 145 -16 122 C ATOM 277 C MET B 44 5.843 22.874 22.443 1.00 19.70 C ANISOU 277 C MET B 44 2442 2099 2944 159 -58 156 C ATOM 278 O MET B 44 5.889 22.656 21.235 1.00 23.48 O ANISOU 278 O MET B 44 2945 2583 3393 134 -90 185 O ATOM 279 CB MET B 44 6.703 25.212 22.427 1.00 22.08 C ANISOU 279 CB MET B 44 2828 2307 3254 149 -25 154 C ATOM 280 CG MET B 44 5.302 25.751 22.374 1.00 29.29 C ANISOU 280 CG MET B 44 3725 3189 4216 206 -53 194 C ATOM 281 SD MET B 44 4.894 26.627 23.880 1.00 39.06 S ANISOU 281 SD MET B 44 4947 4389 5507 257 -11 163 S ATOM 282 CE MET B 44 6.144 27.928 23.894 1.00 28.71 C ANISOU 282 CE MET B 44 3711 3021 4177 220 20 142 C ATOM 283 N LYS B 45 4.967 22.275 23.250 1.00 19.31 N ANISOU 283 N LYS B 45 2339 2073 2926 194 -58 150 N ATOM 284 CA LYS B 45 3.904 21.430 22.719 1.00 19.34 C ANISOU 284 CA LYS B 45 2306 2104 2939 207 -100 184 C ATOM 285 C LYS B 45 2.579 22.118 22.985 1.00 19.86 C ANISOU 285 C LYS B 45 2341 2143 3061 261 -114 213 C ATOM 286 O LYS B 45 2.052 22.076 24.099 1.00 17.81 O ANISOU 286 O LYS B 45 2040 1889 2837 295 -87 195 O ATOM 287 CB LYS B 45 3.914 20.045 23.386 1.00 23.12 C ANISOU 287 CB LYS B 45 2742 2634 3407 199 -91 157 C ATOM 288 CG LYS B 45 2.840 19.100 22.859 1.00 20.63 C ANISOU 288 CG LYS B 45 2389 2348 3100 204 -135 189 C ATOM 289 CD LYS B 45 2.832 17.763 23.634 1.00 20.02 C ANISOU 289 CD LYS B 45 2275 2316 3016 196 -122 161 C ATOM 290 CE LYS B 45 4.088 16.925 23.345 1.00 21.18 C ANISOU 290 CE LYS B 45 2452 2487 3110 152 -114 132 C ATOM 291 NZ LYS B 45 4.087 16.307 21.967 1.00 21.99 N1+ ANISOU 291 NZ LYS B 45 2576 2602 3178 122 -156 156 N1+ ATOM 292 N THR B 46 2.047 22.780 21.967 1.00 20.23 N ANISOU 292 N THR B 46 2408 2160 3117 271 -154 260 N ATOM 293 CA THR B 46 0.753 23.440 22.122 1.00 24.31 C ANISOU 293 CA THR B 46 2892 2651 3694 329 -172 292 C ATOM 294 C THR B 46 -0.377 22.457 21.827 1.00 24.47 C ANISOU 294 C THR B 46 2852 2714 3733 340 -214 320 C ATOM 295 O THR B 46 -0.415 21.824 20.775 1.00 24.92 O ANISOU 295 O THR B 46 2920 2792 3757 308 -259 346 O ATOM 296 CB THR B 46 0.688 24.731 21.295 1.00 27.00 C ANISOU 296 CB THR B 46 3283 2932 4043 341 -196 330 C ATOM 297 CG2 THR B 46 -0.699 25.370 21.380 1.00 29.12 C ANISOU 297 CG2 THR B 46 3512 3175 4379 407 -221 366 C ATOM 298 OG1 THR B 46 1.661 25.647 21.824 1.00 25.12 O ANISOU 298 OG1 THR B 46 3093 2654 3797 332 -149 297 O ATOM 299 N VAL B 47 -1.273 22.305 22.794 1.00 17.56 N ANISOU 299 N VAL B 47 1914 1852 2907 381 -195 312 N ATOM 300 CA VAL B 47 -2.299 21.272 22.735 1.00 21.74 C ANISOU 300 CA VAL B 47 2378 2427 3455 386 -226 331 C ATOM 301 C VAL B 47 -3.637 21.844 22.262 1.00 32.61 C ANISOU 301 C VAL B 47 3714 3787 4888 433 -270 382 C ATOM 302 O VAL B 47 -4.403 21.173 21.557 1.00 31.07 O ANISOU 302 O VAL B 47 3484 3622 4697 424 -323 416 O ATOM 303 CB VAL B 47 -2.430 20.586 24.101 1.00 31.14 C ANISOU 303 CB VAL B 47 3522 3651 4660 394 -176 291 C ATOM 304 CG1 VAL B 47 -3.715 19.826 24.203 1.00 33.80 C ANISOU 304 CG1 VAL B 47 3782 4025 5034 410 -200 314 C ATOM 305 CG2 VAL B 47 -1.237 19.668 24.328 1.00 24.73 C ANISOU 305 CG2 VAL B 47 2741 2866 3790 343 -154 252 C ATOM 306 N TYR B 48 -3.887 23.099 22.630 1.00 22.91 N ANISOU 306 N TYR B 48 2492 2511 3703 483 -250 385 N ATOM 307 CA TYR B 48 -5.166 23.745 22.344 1.00 28.11 C ANISOU 307 CA TYR B 48 3105 3149 4426 540 -286 429 C ATOM 308 C TYR B 48 -4.968 25.197 21.911 1.00 30.94 C ANISOU 308 C TYR B 48 3520 3437 4799 570 -294 450 C ATOM 309 O TYR B 48 -4.194 25.943 22.518 1.00 22.84 O ANISOU 309 O TYR B 48 2541 2373 3766 574 -243 416 O ATOM 310 CB TYR B 48 -6.061 23.680 23.590 1.00 26.19 C ANISOU 310 CB TYR B 48 2785 2923 4244 589 -241 408 C ATOM 311 CG TYR B 48 -7.438 24.320 23.464 1.00 28.78 C ANISOU 311 CG TYR B 48 3050 3236 4650 656 -269 448 C ATOM 312 CD1 TYR B 48 -8.567 23.543 23.215 1.00 34.09 C ANISOU 312 CD1 TYR B 48 3641 3956 5355 662 -309 479 C ATOM 313 CD2 TYR B 48 -7.610 25.695 23.627 1.00 33.00 C ANISOU 313 CD2 TYR B 48 3605 3707 5228 714 -253 454 C ATOM 314 CE1 TYR B 48 -9.828 24.118 23.117 1.00 37.74 C ANISOU 314 CE1 TYR B 48 4037 4408 5895 726 -335 515 C ATOM 315 CE2 TYR B 48 -8.865 26.282 23.528 1.00 34.00 C ANISOU 315 CE2 TYR B 48 3670 3818 5430 782 -278 490 C ATOM 316 CZ TYR B 48 -9.971 25.489 23.272 1.00 39.86 C ANISOU 316 CZ TYR B 48 4325 4613 6207 789 -319 520 C ATOM 317 OH TYR B 48 -11.220 26.073 23.180 1.00 39.20 O ANISOU 317 OH TYR B 48 4173 4518 6205 859 -345 556 O ATOM 318 N LYS B 49 -5.677 25.580 20.855 1.00 31.63 N ANISOU 318 N LYS B 49 3605 3507 4905 589 -361 507 N ATOM 319 CA LYS B 49 -5.778 26.976 20.433 1.00 37.20 C ANISOU 319 CA LYS B 49 4355 4141 5637 629 -378 537 C ATOM 320 C LYS B 49 -7.214 27.215 19.975 1.00 35.91 C ANISOU 320 C LYS B 49 4128 3976 5539 686 -438 592 C ATOM 321 O LYS B 49 -7.668 26.589 19.022 1.00 35.85 O ANISOU 321 O LYS B 49 4104 4001 5517 663 -506 633 O ATOM 322 CB LYS B 49 -4.806 27.271 19.289 1.00 38.74 C ANISOU 322 CB LYS B 49 4646 4310 5766 576 -410 558 C ATOM 323 CG LYS B 49 -4.932 28.679 18.712 1.00 48.41 C ANISOU 323 CG LYS B 49 5924 5457 7012 611 -437 599 C ATOM 324 CD LYS B 49 -4.130 28.818 17.416 1.00 55.69 C ANISOU 324 CD LYS B 49 6934 6361 7863 552 -478 630 C ATOM 325 CE LYS B 49 -4.364 30.168 16.731 1.00 57.49 C ANISOU 325 CE LYS B 49 7221 6513 8112 586 -515 680 C ATOM 326 NZ LYS B 49 -5.403 30.117 15.660 1.00 55.24 N1+ ANISOU 326 NZ LYS B 49 6915 6231 7842 607 -606 749 N1+ ATOM 327 N GLY B 50 -7.934 28.096 20.662 1.00 38.82 N ANISOU 327 N GLY B 50 4460 4307 5981 761 -413 591 N ATOM 328 CA GLY B 50 -9.331 28.355 20.336 1.00 38.51 C ANISOU 328 CA GLY B 50 4349 4268 6016 824 -466 640 C ATOM 329 C GLY B 50 -10.012 29.288 21.326 1.00 40.63 C ANISOU 329 C GLY B 50 4574 4497 6367 910 -418 623 C ATOM 330 O GLY B 50 -9.358 30.144 21.915 1.00 37.01 O ANISOU 330 O GLY B 50 4173 3984 5906 925 -362 590 O ATOM 331 N PRO B 51 -11.334 29.130 21.518 1.00 39.75 N ANISOU 331 N PRO B 51 4369 4421 6314 957 -432 637 N ATOM 332 CA PRO B 51 -12.051 30.018 22.438 1.00 38.30 C ANISOU 332 CA PRO B 51 4157 4216 6178 1027 -376 607 C ATOM 333 C PRO B 51 -11.782 29.666 23.892 1.00 41.22 C ANISOU 333 C PRO B 51 4499 4607 6554 1027 -281 541 C ATOM 334 O PRO B 51 -11.262 28.588 24.183 1.00 41.18 O ANISOU 334 O PRO B 51 4479 4646 6522 976 -264 523 O ATOM 335 CB PRO B 51 -13.519 29.754 22.105 1.00 45.70 C ANISOU 335 CB PRO B 51 5008 5207 7149 1054 -420 634 C ATOM 336 CG PRO B 51 -13.536 28.354 21.608 1.00 46.44 C ANISOU 336 CG PRO B 51 5063 5370 7212 989 -462 652 C ATOM 337 CD PRO B 51 -12.233 28.158 20.870 1.00 41.03 C ANISOU 337 CD PRO B 51 4463 4654 6472 933 -494 670 C ATOM 338 N ASN B 52 -12.157 30.571 24.789 1.00 34.20 N ANISOU 338 N ASN B 52 3608 3687 5698 1085 -222 505 N ATOM 339 CA ASN B 52 -11.865 30.428 26.211 1.00 38.28 C ANISOU 339 CA ASN B 52 4115 4214 6214 1088 -128 440 C ATOM 340 C ASN B 52 -12.555 29.209 26.810 1.00 39.73 C ANISOU 340 C ASN B 52 4209 4486 6401 1067 -106 423 C ATOM 341 O ASN B 52 -13.721 28.942 26.513 1.00 42.71 O ANISOU 341 O ASN B 52 4515 4907 6807 1085 -139 449 O ATOM 342 CB ASN B 52 -12.291 31.695 26.958 1.00 38.91 C ANISOU 342 CB ASN B 52 4212 4244 6328 1157 -78 409 C ATOM 343 CG ASN B 52 -11.683 31.794 28.344 1.00 42.37 C ANISOU 343 CG ASN B 52 4676 4672 6752 1153 17 340 C ATOM 344 ND2 ASN B 52 -12.269 32.632 29.190 1.00 40.00 N ANISOU 344 ND2 ASN B 52 4370 4349 6480 1210 68 305 N ATOM 345 OD1 ASN B 52 -10.691 31.129 28.649 1.00 42.95 O ANISOU 345 OD1 ASN B 52 4775 4756 6787 1100 42 317 O ATOM 346 N CYS B 53 -11.832 28.469 27.646 1.00 38.51 N ANISOU 346 N CYS B 53 4060 4356 6217 1026 -51 382 N ATOM 347 CA CYS B 53 -12.409 27.314 28.333 1.00 41.19 C ANISOU 347 CA CYS B 53 4323 4774 6554 1002 -22 363 C ATOM 348 C CYS B 53 -11.759 27.129 29.697 1.00 39.74 C ANISOU 348 C CYS B 53 4160 4593 6346 990 68 301 C ATOM 349 O CYS B 53 -11.228 26.058 30.011 1.00 36.52 O ANISOU 349 O CYS B 53 3745 4226 5905 938 83 286 O ATOM 350 CB CYS B 53 -12.263 26.052 27.481 1.00 32.74 C ANISOU 350 CB CYS B 53 3228 3754 5458 941 -84 399 C ATOM 351 SG CYS B 53 -10.569 25.757 26.892 1.00 35.65 S ANISOU 351 SG CYS B 53 3692 4094 5758 877 -106 398 S ATOM 352 N ILE B 54 -11.827 28.183 30.508 1.00 40.12 N ANISOU 352 N ILE B 54 4237 4599 6409 1037 125 264 N ATOM 353 CA ILE B 54 -11.167 28.238 31.810 1.00 40.55 C ANISOU 353 CA ILE B 54 4327 4645 6437 1028 209 202 C ATOM 354 C ILE B 54 -11.531 27.092 32.736 1.00 41.81 C ANISOU 354 C ILE B 54 4429 4877 6579 998 254 176 C ATOM 355 O ILE B 54 -10.760 26.756 33.644 1.00 35.51 O ANISOU 355 O ILE B 54 3664 4084 5743 969 309 133 O ATOM 356 CB ILE B 54 -11.516 29.535 32.554 1.00 44.87 C ANISOU 356 CB ILE B 54 4901 5143 7006 1088 261 167 C ATOM 357 CG1 ILE B 54 -13.027 29.629 32.773 1.00 51.07 C ANISOU 357 CG1 ILE B 54 5604 5964 7836 1136 266 175 C ATOM 358 CG2 ILE B 54 -11.017 30.736 31.790 1.00 46.36 C ANISOU 358 CG2 ILE B 54 5161 5248 7205 1115 226 185 C ATOM 359 CD1 ILE B 54 -13.406 30.330 34.047 1.00 52.57 C ANISOU 359 CD1 ILE B 54 5799 6140 8034 1178 346 121 C ATOM 360 N GLU B 55 -12.701 26.495 32.508 1.00 44.02 N ANISOU 360 N GLU B 55 4626 5213 6886 1003 229 203 N ATOM 361 CA GLU B 55 -13.212 25.453 33.392 1.00 48.13 C ANISOU 361 CA GLU B 55 5089 5802 7396 976 273 183 C ATOM 362 C GLU B 55 -12.249 24.266 33.485 1.00 46.89 C ANISOU 362 C GLU B 55 4951 5675 7191 908 272 177 C ATOM 363 O GLU B 55 -12.229 23.542 34.489 1.00 47.80 O ANISOU 363 O GLU B 55 5052 5828 7282 882 326 146 O ATOM 364 CB GLU B 55 -14.607 24.992 32.945 1.00 48.42 C ANISOU 364 CB GLU B 55 5033 5892 7472 985 236 219 C ATOM 365 CG GLU B 55 -14.645 24.307 31.579 1.00 49.25 C ANISOU 365 CG GLU B 55 5118 6018 7578 950 144 275 C ATOM 366 CD GLU B 55 -14.958 25.265 30.447 1.00 55.97 C ANISOU 366 CD GLU B 55 5980 6827 8461 992 77 316 C ATOM 367 OE1 GLU B 55 -15.492 24.801 29.413 1.00 55.97 O ANISOU 367 OE1 GLU B 55 5941 6853 8472 975 3 363 O ATOM 368 OE2 GLU B 55 -14.673 26.478 30.593 1.00 58.50 O1- ANISOU 368 OE2 GLU B 55 6350 7085 8793 1039 98 301 O1- ATOM 369 N HIS B 56 -11.433 24.088 32.449 1.00 40.92 N ANISOU 369 N HIS B 56 4231 4898 6420 880 212 206 N ATOM 370 CA HIS B 56 -10.480 22.987 32.415 1.00 35.73 C ANISOU 370 CA HIS B 56 3599 4267 5709 815 203 200 C ATOM 371 C HIS B 56 -9.171 23.290 33.143 1.00 35.35 C ANISOU 371 C HIS B 56 3642 4190 5599 790 248 148 C ATOM 372 O HIS B 56 -8.463 22.359 33.547 1.00 29.36 O ANISOU 372 O HIS B 56 2909 3463 4781 733 258 126 O ATOM 373 CB HIS B 56 -10.170 22.597 30.974 1.00 35.66 C ANISOU 373 CB HIS B 56 3609 4262 5677 776 113 245 C ATOM 374 CG HIS B 56 -11.372 22.174 30.192 1.00 39.52 C ANISOU 374 CG HIS B 56 4013 4785 6217 788 57 297 C ATOM 375 CD2 HIS B 56 -11.824 22.557 28.977 1.00 41.77 C ANISOU 375 CD2 HIS B 56 4285 5054 6531 806 -17 347 C ATOM 376 ND1 HIS B 56 -12.262 21.229 30.655 1.00 41.66 N ANISOU 376 ND1 HIS B 56 4209 5117 6501 772 71 298 N ATOM 377 CE1 HIS B 56 -13.215 21.050 29.755 1.00 44.71 C ANISOU 377 CE1 HIS B 56 4547 5528 6914 773 7 342 C ATOM 378 NE2 HIS B 56 -12.974 21.844 28.727 1.00 43.29 N ANISOU 378 NE2 HIS B 56 4404 5303 6743 794 -49 372 N ATOM 379 N ASN B 57 -8.862 24.579 33.306 1.00 31.35 N ANISOU 379 N ASN B 57 3184 3620 5108 831 272 130 N ATOM 380 CA ASN B 57 -7.576 25.008 33.861 1.00 32.82 C ANISOU 380 CA ASN B 57 3461 3772 5237 805 305 84 C ATOM 381 C ASN B 57 -7.121 24.192 35.061 1.00 36.10 C ANISOU 381 C ASN B 57 3886 4227 5603 766 358 39 C ATOM 382 O ASN B 57 -6.077 23.527 35.010 1.00 33.25 O ANISOU 382 O ASN B 57 3570 3883 5179 707 341 27 O ATOM 383 CB ASN B 57 -7.601 26.503 34.214 1.00 31.97 C ANISOU 383 CB ASN B 57 3391 3593 5164 863 341 63 C ATOM 384 CG ASN B 57 -7.638 27.393 32.982 1.00 34.28 C ANISOU 384 CG ASN B 57 3707 3833 5486 889 283 105 C ATOM 385 ND2 ASN B 57 -7.346 28.676 33.163 1.00 33.31 N ANISOU 385 ND2 ASN B 57 3640 3637 5378 925 306 86 N ATOM 386 OD1 ASN B 57 -7.925 26.927 31.879 1.00 35.64 O ANISOU 386 OD1 ASN B 57 3851 4026 5664 874 216 154 O ATOM 387 N GLU B 58 -7.926 24.221 36.121 1.00 40.26 N ANISOU 387 N GLU B 58 4369 4770 6160 800 421 16 N ATOM 388 CA GLU B 58 -7.639 23.456 37.330 1.00 39.47 C ANISOU 388 CA GLU B 58 4276 4707 6012 767 475 -24 C ATOM 389 C GLU B 58 -7.207 22.038 36.976 1.00 38.16 C ANISOU 389 C GLU B 58 4105 4595 5798 699 432 -6 C ATOM 390 O GLU B 58 -6.064 21.652 37.259 1.00 40.86 O ANISOU 390 O GLU B 58 4508 4940 6077 652 430 -30 O ATOM 391 CB GLU B 58 -8.856 23.444 38.258 1.00 40.46 C ANISOU 391 CB GLU B 58 4333 4856 6183 809 540 -35 C ATOM 392 N ALA B 59 -8.080 21.302 36.280 1.00 27.17 N ANISOU 392 N ALA B 59 2643 3242 4439 696 393 38 N ATOM 393 CA ALA B 59 -7.767 19.919 35.910 1.00 30.58 C ANISOU 393 CA ALA B 59 3070 3721 4829 633 352 56 C ATOM 394 C ALA B 59 -6.397 19.865 35.234 1.00 23.70 C ANISOU 394 C ALA B 59 2275 2829 3902 592 307 52 C ATOM 395 O ALA B 59 -5.488 19.141 35.680 1.00 27.02 O ANISOU 395 O ALA B 59 2736 3267 4264 547 313 28 O ATOM 396 CB ALA B 59 -8.840 19.358 34.981 1.00 26.79 C ANISOU 396 CB ALA B 59 2512 3272 4394 635 301 107 C ATOM 397 N LEU B 60 -6.247 20.698 34.208 1.00 29.54 N ANISOU 397 N LEU B 60 3035 3529 4661 611 266 74 N ATOM 398 CA LEU B 60 -5.019 20.736 33.432 1.00 29.72 C ANISOU 398 CA LEU B 60 3124 3532 4636 573 225 74 C ATOM 399 C LEU B 60 -3.851 20.922 34.379 1.00 32.97 C ANISOU 399 C LEU B 60 3599 3930 4997 552 267 23 C ATOM 400 O LEU B 60 -2.932 20.087 34.418 1.00 29.05 O ANISOU 400 O LEU B 60 3133 3457 4447 503 254 10 O ATOM 401 CB LEU B 60 -5.076 21.861 32.399 1.00 28.52 C ANISOU 401 CB LEU B 60 2991 3330 4513 604 189 102 C ATOM 402 CG LEU B 60 -6.108 21.641 31.293 1.00 27.50 C ANISOU 402 CG LEU B 60 2806 3215 4427 618 131 157 C ATOM 403 CD1 LEU B 60 -6.332 22.912 30.477 1.00 33.03 C ANISOU 403 CD1 LEU B 60 3524 3861 5165 661 102 184 C ATOM 404 CD2 LEU B 60 -5.680 20.484 30.389 1.00 26.19 C ANISOU 404 CD2 LEU B 60 2649 3086 4217 559 74 179 C ATOM 405 N LEU B 61 -3.927 21.962 35.210 1.00 30.68 N ANISOU 405 N LEU B 61 3327 3603 4725 590 319 -7 N ATOM 406 CA LEU B 61 -2.782 22.282 36.044 1.00 31.46 C ANISOU 406 CA LEU B 61 3492 3684 4776 568 353 -55 C ATOM 407 C LEU B 61 -2.493 21.089 36.950 1.00 30.19 C ANISOU 407 C LEU B 61 3327 3573 4570 530 373 -77 C ATOM 408 O LEU B 61 -1.330 20.660 37.072 1.00 34.12 O ANISOU 408 O LEU B 61 3870 4079 5015 486 361 -97 O ATOM 409 CB LEU B 61 -3.012 23.569 36.846 1.00 33.93 C ANISOU 409 CB LEU B 61 3827 3948 5115 614 407 -87 C ATOM 410 CG LEU B 61 -1.795 24.182 37.545 1.00 39.29 C ANISOU 410 CG LEU B 61 4583 4595 5748 592 434 -135 C ATOM 411 CD1 LEU B 61 -0.716 24.515 36.537 1.00 38.76 C ANISOU 411 CD1 LEU B 61 4566 4503 5658 559 386 -124 C ATOM 412 CD2 LEU B 61 -2.181 25.434 38.341 1.00 42.17 C ANISOU 412 CD2 LEU B 61 4970 4910 6142 641 490 -167 C ATOM 413 N GLU B 62 -3.549 20.493 37.508 1.00 29.42 N ANISOU 413 N GLU B 62 3172 3511 4495 544 399 -70 N ATOM 414 CA GLU B 62 -3.322 19.430 38.477 1.00 32.02 C ANISOU 414 CA GLU B 62 3503 3882 4780 509 424 -90 C ATOM 415 C GLU B 62 -2.588 18.319 37.756 1.00 30.18 C ANISOU 415 C GLU B 62 3282 3676 4509 459 368 -72 C ATOM 416 O GLU B 62 -1.576 17.802 38.258 1.00 31.28 O ANISOU 416 O GLU B 62 3464 3826 4595 423 368 -97 O ATOM 417 CB GLU B 62 -4.624 18.910 39.088 1.00 32.68 C ANISOU 417 CB GLU B 62 3522 4002 4895 527 461 -80 C ATOM 418 CG GLU B 62 -4.383 17.990 40.284 1.00 40.74 C ANISOU 418 CG GLU B 62 4557 5058 5866 493 497 -105 C ATOM 419 CD GLU B 62 -4.409 16.505 39.947 1.00 37.72 C ANISOU 419 CD GLU B 62 4151 4719 5460 447 458 -77 C ATOM 420 OE1 GLU B 62 -4.328 15.692 40.901 1.00 41.81 O ANISOU 420 OE1 GLU B 62 4680 5265 5941 420 485 -91 O ATOM 421 OE2 GLU B 62 -4.509 16.145 38.752 1.00 42.03 O1- ANISOU 421 OE2 GLU B 62 4675 5270 6024 437 401 -42 O1- ATOM 422 N GLU B 63 -3.044 18.016 36.544 1.00 25.88 N ANISOU 422 N GLU B 63 2703 3139 3990 457 317 -30 N ATOM 423 CA GLU B 63 -2.450 16.894 35.823 1.00 28.78 C ANISOU 423 CA GLU B 63 3080 3531 4322 411 267 -14 C ATOM 424 C GLU B 63 -0.975 17.169 35.625 1.00 25.62 C ANISOU 424 C GLU B 63 2746 3110 3877 386 253 -38 C ATOM 425 O GLU B 63 -0.133 16.289 35.855 1.00 24.51 O ANISOU 425 O GLU B 63 2630 2990 3691 350 243 -52 O ATOM 426 CB GLU B 63 -3.137 16.653 34.482 1.00 24.08 C ANISOU 426 CB GLU B 63 2447 2943 3759 412 212 33 C ATOM 427 CG GLU B 63 -2.661 15.374 33.782 1.00 21.73 C ANISOU 427 CG GLU B 63 2158 2673 3424 364 165 48 C ATOM 428 CD GLU B 63 -3.537 15.001 32.600 1.00 24.78 C ANISOU 428 CD GLU B 63 2502 3072 3840 361 113 94 C ATOM 429 OE1 GLU B 63 -3.308 15.529 31.490 1.00 23.63 O ANISOU 429 OE1 GLU B 63 2375 2904 3698 364 73 113 O ATOM 430 OE2 GLU B 63 -4.467 14.178 32.780 1.00 26.08 O1- ANISOU 430 OE2 GLU B 63 2616 3270 4022 352 110 112 O1- ATOM 431 N ALA B 64 -0.654 18.407 35.250 1.00 22.25 N ANISOU 431 N ALA B 64 2348 2641 3465 407 254 -43 N ATOM 432 CA ALA B 64 0.745 18.733 35.003 1.00 24.65 C ANISOU 432 CA ALA B 64 2710 2925 3730 380 241 -65 C ATOM 433 C ALA B 64 1.517 18.445 36.277 1.00 30.20 C ANISOU 433 C ALA B 64 3442 3640 4392 361 275 -108 C ATOM 434 O ALA B 64 2.519 17.705 36.278 1.00 25.20 O ANISOU 434 O ALA B 64 2832 3027 3718 324 256 -120 O ATOM 435 CB ALA B 64 0.888 20.180 34.587 1.00 24.36 C ANISOU 435 CB ALA B 64 2702 2837 3717 404 245 -66 C ATOM 436 N LYS B 65 0.995 18.965 37.382 1.00 28.08 N ANISOU 436 N LYS B 65 3171 3363 4136 387 324 -130 N ATOM 437 CA LYS B 65 1.681 18.795 38.644 1.00 30.19 C ANISOU 437 CA LYS B 65 3471 3638 4361 370 356 -172 C ATOM 438 C LYS B 65 1.862 17.307 38.922 1.00 23.97 C ANISOU 438 C LYS B 65 2671 2898 3539 338 339 -166 C ATOM 439 O LYS B 65 2.958 16.862 39.285 1.00 27.49 O ANISOU 439 O LYS B 65 3150 3354 3941 307 328 -187 O ATOM 440 CB LYS B 65 0.941 19.539 39.759 1.00 29.55 C ANISOU 440 CB LYS B 65 3389 3542 4297 405 415 -195 C ATOM 441 CG LYS B 65 0.914 21.058 39.525 1.00 36.28 C ANISOU 441 CG LYS B 65 4266 4339 5181 437 431 -206 C ATOM 442 CD LYS B 65 0.356 21.812 40.733 1.00 45.73 C ANISOU 442 CD LYS B 65 5473 5515 6387 470 495 -240 C ATOM 443 CE LYS B 65 1.262 22.973 41.158 1.00 48.87 C ANISOU 443 CE LYS B 65 5938 5865 6766 466 513 -281 C ATOM 444 NZ LYS B 65 1.063 24.218 40.348 1.00 47.01 N1+ ANISOU 444 NZ LYS B 65 5713 5573 6575 498 506 -270 N1+ ATOM 445 N MET B 66 0.828 16.520 38.644 1.00 22.58 N ANISOU 445 N MET B 66 2446 2748 3386 343 332 -134 N ATOM 446 CA MET B 66 0.917 15.103 38.946 1.00 21.79 C ANISOU 446 CA MET B 66 2338 2686 3255 312 318 -127 C ATOM 447 C MET B 66 2.032 14.511 38.095 1.00 23.14 C ANISOU 447 C MET B 66 2533 2862 3398 281 268 -123 C ATOM 448 O MET B 66 2.938 13.831 38.607 1.00 23.42 O ANISOU 448 O MET B 66 2596 2911 3391 256 260 -142 O ATOM 449 CB MET B 66 -0.420 14.409 38.669 1.00 24.38 C ANISOU 449 CB MET B 66 2608 3040 3617 318 316 -91 C ATOM 450 CG MET B 66 -0.655 13.137 39.458 1.00 31.05 C ANISOU 450 CG MET B 66 3444 3919 4433 292 326 -89 C ATOM 451 SD MET B 66 -0.052 13.136 41.165 1.00 53.04 S ANISOU 451 SD MET B 66 6277 6709 7168 283 374 -132 S ATOM 452 CE MET B 66 -0.830 14.587 41.842 1.00 20.62 C ANISOU 452 CE MET B 66 2161 2580 3096 328 438 -153 C ATOM 453 N MET B 67 2.004 14.820 36.803 1.00 19.91 N ANISOU 453 N MET B 67 2114 2439 3011 284 234 -100 N ATOM 454 CA MET B 67 2.976 14.192 35.914 1.00 19.85 C ANISOU 454 CA MET B 67 2126 2438 2977 255 191 -95 C ATOM 455 C MET B 67 4.376 14.703 36.266 1.00 20.80 C ANISOU 455 C MET B 67 2292 2545 3066 242 197 -132 C ATOM 456 O MET B 67 5.392 14.016 36.031 1.00 16.51 O ANISOU 456 O MET B 67 1767 2015 2492 216 173 -141 O ATOM 457 CB MET B 67 2.619 14.459 34.451 1.00 21.15 C ANISOU 457 CB MET B 67 2277 2591 3167 258 155 -63 C ATOM 458 CG MET B 67 1.344 13.771 33.986 1.00 23.13 C ANISOU 458 CG MET B 67 2481 2862 3446 263 137 -25 C ATOM 459 SD MET B 67 1.323 11.984 34.318 1.00 24.73 S ANISOU 459 SD MET B 67 2675 3103 3619 230 122 -21 S ATOM 460 CE MET B 67 -0.413 11.777 34.734 1.00 31.34 C ANISOU 460 CE MET B 67 3451 3958 4499 246 140 6 C ATOM 461 N ASN B 68 4.436 15.883 36.881 1.00 19.29 N ANISOU 461 N ASN B 68 2119 2328 2884 259 230 -154 N ATOM 462 CA ASN B 68 5.733 16.493 37.157 1.00 19.06 C ANISOU 462 CA ASN B 68 2132 2283 2828 243 233 -187 C ATOM 463 C ASN B 68 6.383 15.814 38.353 1.00 19.01 C ANISOU 463 C ASN B 68 2142 2299 2782 225 242 -216 C ATOM 464 O ASN B 68 7.549 16.077 38.657 1.00 18.08 O ANISOU 464 O ASN B 68 2053 2178 2638 207 237 -244 O ATOM 465 CB ASN B 68 5.576 18.001 37.407 1.00 21.76 C ANISOU 465 CB ASN B 68 2493 2584 3191 264 263 -202 C ATOM 466 CG ASN B 68 6.911 18.733 37.529 1.00 26.83 C ANISOU 466 CG ASN B 68 3179 3206 3810 241 262 -235 C ATOM 467 ND2 ASN B 68 7.087 19.468 38.623 1.00 28.48 N ANISOU 467 ND2 ASN B 68 3415 3397 4009 245 295 -269 N ATOM 468 OD1 ASN B 68 7.766 18.643 36.648 1.00 21.20 O ANISOU 468 OD1 ASN B 68 2473 2494 3087 217 234 -230 O ATOM 469 N ARG B 69 5.633 14.954 39.042 1.00 15.51 N ANISOU 469 N ARG B 69 1680 1879 2333 230 253 -207 N ATOM 470 CA ARG B 69 6.214 14.241 40.173 1.00 22.79 C ANISOU 470 CA ARG B 69 2623 2823 3214 213 257 -230 C ATOM 471 C ARG B 69 7.063 13.063 39.710 1.00 17.12 C ANISOU 471 C ARG B 69 1906 2127 2473 190 215 -223 C ATOM 472 O ARG B 69 7.837 12.503 40.488 1.00 19.73 O ANISOU 472 O ARG B 69 2257 2472 2768 175 206 -241 O ATOM 473 CB ARG B 69 5.129 13.780 41.144 1.00 24.19 C ANISOU 473 CB ARG B 69 2786 3015 3389 223 290 -223 C ATOM 474 CG ARG B 69 4.348 14.937 41.756 1.00 30.88 C ANISOU 474 CG ARG B 69 3635 3842 4258 250 340 -237 C ATOM 475 CD ARG B 69 3.214 14.433 42.628 1.00 38.37 C ANISOU 475 CD ARG B 69 4562 4809 5207 259 377 -229 C ATOM 476 NE ARG B 69 2.917 15.357 43.721 1.00 50.29 N ANISOU 476 NE ARG B 69 6093 6304 6711 276 431 -259 N ATOM 477 CZ ARG B 69 2.036 15.114 44.689 1.00 50.97 C ANISOU 477 CZ ARG B 69 6171 6406 6791 283 477 -262 C ATOM 478 NH1 ARG B 69 1.355 13.974 44.698 1.00 46.03 N1+ ANISOU 478 NH1 ARG B 69 5513 5811 6166 271 473 -233 N1+ ATOM 479 NH2 ARG B 69 1.833 16.011 45.646 1.00 51.17 N ANISOU 479 NH2 ARG B 69 6221 6414 6808 299 528 -295 N ATOM 480 N LEU B 70 6.914 12.692 38.438 1.00 18.42 N ANISOU 480 N LEU B 70 2050 2293 2656 187 187 -197 N ATOM 481 CA LEU B 70 7.744 11.647 37.849 1.00 16.82 C ANISOU 481 CA LEU B 70 1849 2106 2434 168 149 -194 C ATOM 482 C LEU B 70 9.085 12.282 37.462 1.00 18.66 C ANISOU 482 C LEU B 70 2102 2330 2657 157 138 -218 C ATOM 483 O LEU B 70 9.199 12.889 36.405 1.00 16.30 O ANISOU 483 O LEU B 70 1801 2018 2375 155 132 -210 O ATOM 484 CB LEU B 70 7.037 11.045 36.623 1.00 14.16 C ANISOU 484 CB LEU B 70 1488 1773 2118 168 125 -159 C ATOM 485 CG LEU B 70 5.673 10.423 36.963 1.00 14.38 C ANISOU 485 CG LEU B 70 1490 1812 2160 174 135 -134 C ATOM 486 CD1 LEU B 70 4.820 10.119 35.731 1.00 16.19 C ANISOU 486 CD1 LEU B 70 1693 2043 2416 173 111 -99 C ATOM 487 CD2 LEU B 70 5.864 9.173 37.824 1.00 16.37 C ANISOU 487 CD2 LEU B 70 1754 2085 2383 160 129 -137 C ATOM 488 N ARG B 71 10.084 12.165 38.338 1.00 17.84 N ANISOU 488 N ARG B 71 2017 2235 2525 146 136 -247 N ATOM 489 CA ARG B 71 11.362 12.847 38.123 1.00 19.54 C ANISOU 489 CA ARG B 71 2246 2445 2733 132 129 -273 C ATOM 490 C ARG B 71 12.509 11.863 38.312 1.00 16.08 C ANISOU 490 C ARG B 71 1808 2030 2270 119 101 -287 C ATOM 491 O ARG B 71 12.602 11.172 39.349 1.00 17.43 O ANISOU 491 O ARG B 71 1988 2216 2419 120 95 -294 O ATOM 492 CB ARG B 71 11.529 14.029 39.093 1.00 25.88 C ANISOU 492 CB ARG B 71 3071 3230 3530 131 156 -300 C ATOM 493 CG ARG B 71 10.361 15.015 39.098 1.00 25.50 C ANISOU 493 CG ARG B 71 3024 3155 3509 151 189 -290 C ATOM 494 CD ARG B 71 10.659 16.289 39.912 1.00 31.68 C ANISOU 494 CD ARG B 71 3837 3912 4286 149 216 -322 C ATOM 495 NE ARG B 71 11.657 17.143 39.261 1.00 32.12 N ANISOU 495 NE ARG B 71 3906 3951 4347 129 207 -336 N ATOM 496 CZ ARG B 71 11.371 17.996 38.281 1.00 32.00 C ANISOU 496 CZ ARG B 71 3892 3908 4360 134 212 -321 C ATOM 497 NH1 ARG B 71 10.127 18.102 37.846 1.00 32.13 N1+ ANISOU 497 NH1 ARG B 71 3893 3910 4403 162 223 -292 N1+ ATOM 498 NH2 ARG B 71 12.322 18.745 37.736 1.00 32.14 N ANISOU 498 NH2 ARG B 71 3924 3909 4377 111 206 -333 N ATOM 499 N HIS B 72 13.382 11.799 37.312 1.00 14.18 N ANISOU 499 N HIS B 72 1560 1794 2035 108 84 -291 N ATOM 500 CA HIS B 72 14.457 10.816 37.314 1.00 13.41 C ANISOU 500 CA HIS B 72 1456 1719 1921 102 57 -303 C ATOM 501 C HIS B 72 15.411 11.157 36.179 1.00 13.02 C ANISOU 501 C HIS B 72 1396 1671 1880 88 52 -312 C ATOM 502 O HIS B 72 15.025 11.856 35.225 1.00 13.43 O ANISOU 502 O HIS B 72 1449 1706 1946 84 64 -300 O ATOM 503 CB HIS B 72 13.870 9.416 37.123 1.00 14.60 C ANISOU 503 CB HIS B 72 1600 1879 2068 113 39 -280 C ATOM 504 CG HIS B 72 14.868 8.308 37.269 1.00 13.55 C ANISOU 504 CG HIS B 72 1464 1764 1920 115 11 -292 C ATOM 505 CD2 HIS B 72 15.229 7.566 38.348 1.00 14.85 C ANISOU 505 CD2 HIS B 72 1637 1940 2064 120 -6 -299 C ATOM 506 ND1 HIS B 72 15.611 7.835 36.208 1.00 14.56 N ANISOU 506 ND1 HIS B 72 1579 1898 2053 113 -3 -296 N ATOM 507 CE1 HIS B 72 16.399 6.858 36.629 1.00 17.14 C ANISOU 507 CE1 HIS B 72 1904 2239 2369 121 -27 -307 C ATOM 508 NE2 HIS B 72 16.189 6.677 37.924 1.00 14.34 N ANISOU 508 NE2 HIS B 72 1564 1887 1999 125 -32 -307 N ATOM 509 N SER B 73 16.660 10.691 36.270 1.00 10.67 N ANISOU 509 N SER B 73 1088 1393 1573 82 34 -334 N ATOM 510 CA SER B 73 17.655 11.072 35.262 1.00 14.13 C ANISOU 510 CA SER B 73 1514 1837 2019 65 36 -347 C ATOM 511 C SER B 73 17.270 10.584 33.869 1.00 14.93 C ANISOU 511 C SER B 73 1611 1935 2127 67 36 -326 C ATOM 512 O SER B 73 17.710 11.147 32.857 1.00 13.35 O ANISOU 512 O SER B 73 1409 1732 1932 51 48 -328 O ATOM 513 CB SER B 73 19.023 10.503 35.612 1.00 15.14 C ANISOU 513 CB SER B 73 1623 1991 2140 62 17 -373 C ATOM 514 OG SER B 73 18.991 9.092 35.507 1.00 17.75 O ANISOU 514 OG SER B 73 1946 2333 2466 82 -5 -365 O ATOM 515 N ARG B 74 16.441 9.547 33.813 1.00 12.91 N ANISOU 515 N ARG B 74 1357 1679 1868 84 24 -305 N ATOM 516 CA ARG B 74 16.114 8.935 32.515 1.00 10.23 C ANISOU 516 CA ARG B 74 1019 1339 1531 84 18 -287 C ATOM 517 C ARG B 74 14.697 9.223 32.010 1.00 12.86 C ANISOU 517 C ARG B 74 1360 1652 1872 86 22 -255 C ATOM 518 O ARG B 74 14.221 8.533 31.101 1.00 11.46 O ANISOU 518 O ARG B 74 1187 1475 1693 86 11 -237 O ATOM 519 CB ARG B 74 16.309 7.420 32.587 1.00 10.19 C ANISOU 519 CB ARG B 74 1010 1345 1517 98 -4 -289 C ATOM 520 CG ARG B 74 17.625 6.981 33.222 1.00 12.40 C ANISOU 520 CG ARG B 74 1276 1643 1791 104 -15 -318 C ATOM 521 CD ARG B 74 18.839 7.467 32.449 1.00 12.69 C ANISOU 521 CD ARG B 74 1297 1692 1833 91 -4 -342 C ATOM 522 NE ARG B 74 20.023 6.956 33.136 1.00 14.75 N ANISOU 522 NE ARG B 74 1537 1973 2093 101 -19 -368 N ATOM 523 CZ ARG B 74 21.139 7.653 33.313 1.00 21.33 C ANISOU 523 CZ ARG B 74 2350 2823 2933 87 -13 -393 C ATOM 524 NH1 ARG B 74 21.222 8.878 32.813 1.00 17.34 N1+ ANISOU 524 NH1 ARG B 74 1845 2311 2432 61 11 -396 N1+ ATOM 525 NH2 ARG B 74 22.163 7.118 33.987 1.00 19.44 N ANISOU 525 NH2 ARG B 74 2087 2603 2695 99 -34 -415 N ATOM 526 N VAL B 75 14.021 10.208 32.601 1.00 11.80 N ANISOU 526 N VAL B 75 1230 1504 1748 89 38 -247 N ATOM 527 CA VAL B 75 12.762 10.706 32.040 1.00 11.53 C ANISOU 527 CA VAL B 75 1199 1452 1730 93 42 -217 C ATOM 528 C VAL B 75 12.814 12.217 31.838 1.00 11.28 C ANISOU 528 C VAL B 75 1177 1398 1709 87 61 -218 C ATOM 529 O VAL B 75 13.457 12.942 32.614 1.00 15.23 O ANISOU 529 O VAL B 75 1683 1895 2208 82 76 -242 O ATOM 530 CB VAL B 75 11.529 10.287 32.888 1.00 13.05 C ANISOU 530 CB VAL B 75 1384 1643 1929 109 43 -199 C ATOM 531 CG1 VAL B 75 11.489 8.742 33.073 1.00 10.19 C ANISOU 531 CG1 VAL B 75 1019 1299 1555 111 22 -195 C ATOM 532 CG2 VAL B 75 11.510 10.999 34.241 1.00 11.70 C ANISOU 532 CG2 VAL B 75 1218 1468 1760 117 64 -216 C ATOM 533 N VAL B 76 12.172 12.690 30.777 1.00 15.32 N ANISOU 533 N VAL B 76 1694 1895 2232 85 59 -192 N ATOM 534 CA VAL B 76 12.244 14.111 30.437 1.00 15.85 C ANISOU 534 CA VAL B 76 1777 1935 2310 78 74 -190 C ATOM 535 C VAL B 76 11.531 14.952 31.481 1.00 17.56 C ANISOU 535 C VAL B 76 1994 2132 2545 97 92 -191 C ATOM 536 O VAL B 76 10.659 14.451 32.203 1.00 16.70 O ANISOU 536 O VAL B 76 1871 2030 2444 117 93 -183 O ATOM 537 CB VAL B 76 11.657 14.409 29.045 1.00 16.74 C ANISOU 537 CB VAL B 76 1900 2034 2428 73 62 -156 C ATOM 538 CG1 VAL B 76 12.487 13.754 27.955 1.00 19.89 C ANISOU 538 CG1 VAL B 76 2305 2449 2803 50 51 -160 C ATOM 539 CG2 VAL B 76 10.201 13.941 28.955 1.00 17.95 C ANISOU 539 CG2 VAL B 76 2037 2186 2598 95 45 -124 C ATOM 540 N LYS B 77 11.925 16.221 31.577 1.00 13.27 N ANISOU 540 N LYS B 77 1470 1563 2008 90 110 -202 N ATOM 541 CA LYS B 77 11.293 17.152 32.500 1.00 14.04 C ANISOU 541 CA LYS B 77 1576 1636 2124 109 132 -207 C ATOM 542 C LYS B 77 10.302 18.093 31.825 1.00 15.39 C ANISOU 542 C LYS B 77 1755 1771 2323 127 134 -177 C ATOM 543 O LYS B 77 10.550 18.628 30.733 1.00 17.30 O ANISOU 543 O LYS B 77 2013 1996 2565 112 125 -161 O ATOM 544 CB LYS B 77 12.350 17.981 33.231 1.00 16.91 C ANISOU 544 CB LYS B 77 1960 1988 2477 90 149 -244 C ATOM 545 CG LYS B 77 13.061 17.200 34.325 1.00 20.82 C ANISOU 545 CG LYS B 77 2446 2514 2950 84 147 -275 C ATOM 546 CD LYS B 77 14.205 17.986 34.932 1.00 24.00 C ANISOU 546 CD LYS B 77 2868 2910 3343 58 156 -311 C ATOM 547 CE LYS B 77 14.791 17.198 36.087 1.00 21.34 C ANISOU 547 CE LYS B 77 2522 2603 2983 55 148 -337 C ATOM 548 NZ LYS B 77 15.195 15.833 35.629 1.00 19.65 N1+ ANISOU 548 NZ LYS B 77 2282 2425 2758 55 123 -329 N1+ ATOM 549 N LEU B 78 9.173 18.280 32.499 1.00 16.20 N ANISOU 549 N LEU B 78 1845 1863 2447 159 146 -168 N ATOM 550 CA LEU B 78 8.230 19.339 32.165 1.00 17.65 C ANISOU 550 CA LEU B 78 2033 2008 2663 184 153 -145 C ATOM 551 C LEU B 78 8.811 20.620 32.762 1.00 19.66 C ANISOU 551 C LEU B 78 2323 2227 2920 180 180 -173 C ATOM 552 O LEU B 78 9.018 20.693 33.977 1.00 19.68 O ANISOU 552 O LEU B 78 2331 2232 2915 183 203 -206 O ATOM 553 CB LEU B 78 6.873 19.038 32.812 1.00 15.91 C ANISOU 553 CB LEU B 78 1782 1795 2469 221 163 -131 C ATOM 554 CG LEU B 78 5.801 20.121 32.567 1.00 19.76 C ANISOU 554 CG LEU B 78 2267 2243 2998 257 172 -108 C ATOM 555 CD1 LEU B 78 5.377 20.142 31.104 1.00 17.21 C ANISOU 555 CD1 LEU B 78 1938 1913 2688 257 135 -65 C ATOM 556 CD2 LEU B 78 4.599 19.918 33.471 1.00 26.45 C ANISOU 556 CD2 LEU B 78 3079 3099 3872 293 194 -106 C ATOM 557 N LEU B 79 9.098 21.619 31.927 1.00 13.73 N ANISOU 557 N LEU B 79 1601 1439 2176 170 177 -162 N ATOM 558 CA LEU B 79 9.776 22.825 32.419 1.00 18.97 C ANISOU 558 CA LEU B 79 2303 2065 2839 158 200 -190 C ATOM 559 C LEU B 79 8.746 23.866 32.781 1.00 20.80 C ANISOU 559 C LEU B 79 2547 2250 3107 199 219 -183 C ATOM 560 O LEU B 79 8.971 24.712 33.656 1.00 22.50 O ANISOU 560 O LEU B 79 2790 2435 3325 201 246 -214 O ATOM 561 CB LEU B 79 10.720 23.396 31.364 1.00 17.70 C ANISOU 561 CB LEU B 79 2173 1887 2666 119 189 -183 C ATOM 562 CG LEU B 79 11.910 22.498 31.033 1.00 19.98 C ANISOU 562 CG LEU B 79 2449 2220 2921 78 178 -198 C ATOM 563 CD1 LEU B 79 12.802 23.151 29.985 1.00 19.67 C ANISOU 563 CD1 LEU B 79 2440 2164 2870 37 175 -192 C ATOM 564 CD2 LEU B 79 12.686 22.198 32.309 1.00 20.96 C ANISOU 564 CD2 LEU B 79 2567 2367 3028 65 191 -243 C ATOM 565 N GLY B 80 7.607 23.815 32.104 1.00 18.26 N ANISOU 565 N GLY B 80 2203 1920 2814 232 204 -142 N ATOM 566 CA GLY B 80 6.562 24.770 32.450 1.00 20.06 C ANISOU 566 CA GLY B 80 2435 2104 3082 279 223 -134 C ATOM 567 C GLY B 80 5.255 24.479 31.761 1.00 19.30 C ANISOU 567 C GLY B 80 2300 2012 3020 317 201 -88 C ATOM 568 O GLY B 80 5.181 23.565 30.946 1.00 18.80 O ANISOU 568 O GLY B 80 2214 1985 2945 301 168 -62 O ATOM 569 N VAL B 81 4.218 25.240 32.091 1.00 17.44 N ANISOU 569 N VAL B 81 2055 1742 2827 367 217 -80 N ATOM 570 CA VAL B 81 2.986 25.165 31.320 1.00 21.17 C ANISOU 570 CA VAL B 81 2490 2213 3339 404 190 -32 C ATOM 571 C VAL B 81 2.589 26.570 30.890 1.00 23.37 C ANISOU 571 C VAL B 81 2800 2425 3655 438 189 -13 C ATOM 572 O VAL B 81 2.923 27.549 31.557 1.00 24.58 O ANISOU 572 O VAL B 81 2992 2533 3813 447 223 -43 O ATOM 573 CB VAL B 81 1.817 24.547 32.115 1.00 21.64 C ANISOU 573 CB VAL B 81 2491 2305 3427 442 209 -32 C ATOM 574 CG1 VAL B 81 2.139 23.115 32.539 1.00 19.09 C ANISOU 574 CG1 VAL B 81 2141 2044 3068 409 208 -46 C ATOM 575 CG2 VAL B 81 1.460 25.414 33.319 1.00 22.46 C ANISOU 575 CG2 VAL B 81 2603 2375 3555 481 262 -66 C ATOM 576 N ILE B 82 1.901 26.660 29.765 1.00 16.79 N ANISOU 576 N ILE B 82 1952 1582 2845 455 148 38 N ATOM 577 CA ILE B 82 1.301 27.910 29.335 1.00 22.65 C ANISOU 577 CA ILE B 82 2715 2261 3630 498 140 64 C ATOM 578 C ILE B 82 -0.211 27.737 29.395 1.00 20.68 C ANISOU 578 C ILE B 82 2399 2021 3435 559 131 93 C ATOM 579 O ILE B 82 -0.778 26.880 28.707 1.00 19.73 O ANISOU 579 O ILE B 82 2234 1943 3319 555 91 128 O ATOM 580 CB ILE B 82 1.740 28.284 27.918 1.00 21.55 C ANISOU 580 CB ILE B 82 2619 2096 3473 470 93 105 C ATOM 581 CG1 ILE B 82 3.236 28.618 27.924 1.00 23.09 C ANISOU 581 CG1 ILE B 82 2878 2276 3620 411 110 74 C ATOM 582 CG2 ILE B 82 0.937 29.484 27.414 1.00 26.48 C ANISOU 582 CG2 ILE B 82 3261 2655 4147 521 76 142 C ATOM 583 CD1 ILE B 82 3.814 28.854 26.538 1.00 27.40 C ANISOU 583 CD1 ILE B 82 3468 2806 4137 371 72 110 C ATOM 584 N ILE B 83 -0.848 28.538 30.248 1.00 20.01 N ANISOU 584 N ILE B 83 2306 1901 3395 613 170 74 N ATOM 585 CA ILE B 83 -2.293 28.499 30.426 1.00 22.80 C ANISOU 585 CA ILE B 83 2592 2263 3809 676 172 96 C ATOM 586 C ILE B 83 -2.799 29.920 30.212 1.00 24.04 C ANISOU 586 C ILE B 83 2773 2342 4018 735 173 112 C ATOM 587 O ILE B 83 -2.701 30.768 31.102 1.00 21.64 O ANISOU 587 O ILE B 83 2500 1995 3729 762 223 74 O ATOM 588 CB ILE B 83 -2.676 27.959 31.827 1.00 28.25 C ANISOU 588 CB ILE B 83 3238 2990 4505 692 230 53 C ATOM 589 CG1 ILE B 83 -2.173 26.515 31.983 1.00 22.88 C ANISOU 589 CG1 ILE B 83 2538 2382 3774 634 222 43 C ATOM 590 CG2 ILE B 83 -4.187 28.019 32.054 1.00 25.24 C ANISOU 590 CG2 ILE B 83 2782 2617 4193 759 240 73 C ATOM 591 CD1 ILE B 83 -2.676 25.799 33.208 1.00 29.98 C ANISOU 591 CD1 ILE B 83 3391 3325 4676 644 269 13 C ATOM 592 N GLU B 84 -3.284 30.181 29.003 1.00 20.84 N ANISOU 592 N GLU B 84 2362 1918 3636 751 114 169 N ATOM 593 CA GLU B 84 -3.758 31.511 28.622 1.00 24.91 C ANISOU 593 CA GLU B 84 2907 2357 4201 807 103 194 C ATOM 594 C GLU B 84 -5.137 31.392 27.990 1.00 29.05 C ANISOU 594 C GLU B 84 3358 2893 4785 862 57 248 C ATOM 595 O GLU B 84 -5.618 30.280 27.719 1.00 30.02 O ANISOU 595 O GLU B 84 3417 3084 4904 846 30 268 O ATOM 596 CB GLU B 84 -2.776 32.170 27.639 1.00 26.61 C ANISOU 596 CB GLU B 84 3209 2523 4378 764 68 215 C ATOM 597 CG GLU B 84 -1.413 32.453 28.257 1.00 29.40 C ANISOU 597 CG GLU B 84 3632 2858 4680 710 112 162 C ATOM 598 CD GLU B 84 -0.324 32.740 27.236 1.00 25.24 C ANISOU 598 CD GLU B 84 3179 2308 4103 648 79 182 C ATOM 599 OE1 GLU B 84 -0.521 32.456 26.034 1.00 28.88 O ANISOU 599 OE1 GLU B 84 3636 2781 4554 634 23 234 O ATOM 600 OE2 GLU B 84 0.741 33.239 27.656 1.00 28.61 O1- ANISOU 600 OE2 GLU B 84 3666 2706 4498 609 112 144 O1- ATOM 601 N GLU B 85 -5.775 32.533 27.745 1.00 30.44 N ANISOU 601 N GLU B 85 3544 3003 5018 928 47 272 N ATOM 602 CA GLU B 85 -7.107 32.519 27.138 1.00 27.45 C ANISOU 602 CA GLU B 85 3093 2632 4704 987 -1 326 C ATOM 603 C GLU B 85 -7.113 31.788 25.813 1.00 28.13 C ANISOU 603 C GLU B 85 3171 2757 4759 943 -82 382 C ATOM 604 O GLU B 85 -6.539 32.251 24.831 1.00 34.85 O ANISOU 604 O GLU B 85 4092 3570 5580 915 -127 414 O ATOM 605 CB GLU B 85 -7.649 33.934 26.951 1.00 30.18 C ANISOU 605 CB GLU B 85 3465 2891 5113 1063 -9 348 C ATOM 606 CG GLU B 85 -8.088 34.577 28.251 1.00 39.49 C ANISOU 606 CG GLU B 85 4632 4048 6324 1119 67 293 C ATOM 607 CD GLU B 85 -9.186 35.599 28.039 1.00 41.12 C ANISOU 607 CD GLU B 85 4828 4222 6573 1191 46 313 C ATOM 608 OE1 GLU B 85 -10.060 35.716 28.928 1.00 43.53 O ANISOU 608 OE1 GLU B 85 5082 4554 6904 1237 89 280 O ATOM 609 OE2 GLU B 85 -9.176 36.268 26.977 1.00 38.10 O1- ANISOU 609 OE2 GLU B 85 4489 3788 6197 1202 -15 363 O1- ATOM 610 N GLY B 86 -7.757 30.628 25.797 1.00 33.56 N ANISOU 610 N GLY B 86 3777 3521 5454 932 -100 393 N ATOM 611 CA GLY B 86 -7.852 29.843 24.581 1.00 32.58 C ANISOU 611 CA GLY B 86 3641 3437 5299 890 -177 443 C ATOM 612 C GLY B 86 -6.512 29.393 24.026 1.00 34.67 C ANISOU 612 C GLY B 86 3984 3713 5477 804 -188 433 C ATOM 613 O GLY B 86 -6.384 29.144 22.820 1.00 30.60 O ANISOU 613 O GLY B 86 3492 3204 4929 770 -253 477 O ATOM 614 N LYS B 87 -5.505 29.284 24.890 1.00 31.62 N ANISOU 614 N LYS B 87 3635 3329 5050 769 -126 376 N ATOM 615 CA LYS B 87 -4.214 28.786 24.408 1.00 30.12 C ANISOU 615 CA LYS B 87 3508 3156 4780 689 -133 364 C ATOM 616 C LYS B 87 -3.514 27.998 25.501 1.00 27.53 C ANISOU 616 C LYS B 87 3172 2872 4418 653 -74 304 C ATOM 617 O LYS B 87 -3.251 28.533 26.589 1.00 23.65 O ANISOU 617 O LYS B 87 2693 2355 3938 672 -15 259 O ATOM 618 CB LYS B 87 -3.329 29.937 23.917 1.00 30.51 C ANISOU 618 CB LYS B 87 3652 3134 4807 674 -134 369 C ATOM 619 CG LYS B 87 -2.201 29.516 22.974 1.00 31.99 C ANISOU 619 CG LYS B 87 3900 3337 4918 596 -160 377 C ATOM 620 CD LYS B 87 -0.911 29.190 23.720 1.00 32.25 C ANISOU 620 CD LYS B 87 3964 3387 4901 543 -105 317 C ATOM 621 CE LYS B 87 0.278 29.088 22.763 1.00 30.85 C ANISOU 621 CE LYS B 87 3855 3211 4657 471 -122 324 C ATOM 622 NZ LYS B 87 1.583 29.008 23.480 1.00 34.11 N1+ ANISOU 622 NZ LYS B 87 4300 3631 5029 424 -70 268 N1+ ATOM 623 N TYR B 88 -3.222 26.728 25.215 1.00 21.54 N ANISOU 623 N TYR B 88 2394 2175 3616 602 -92 303 N ATOM 624 CA TYR B 88 -2.643 25.833 26.224 1.00 21.39 C ANISOU 624 CA TYR B 88 2361 2201 3565 570 -45 251 C ATOM 625 C TYR B 88 -1.440 25.068 25.697 1.00 21.80 C ANISOU 625 C TYR B 88 2456 2282 3547 498 -58 240 C ATOM 626 O TYR B 88 -1.526 24.437 24.651 1.00 19.68 O ANISOU 626 O TYR B 88 2185 2038 3256 470 -108 273 O ATOM 627 CB TYR B 88 -3.696 24.837 26.713 1.00 21.88 C ANISOU 627 CB TYR B 88 2337 2319 3656 588 -43 255 C ATOM 628 CG TYR B 88 -4.859 25.498 27.415 1.00 27.82 C ANISOU 628 CG TYR B 88 3037 3053 4481 659 -17 257 C ATOM 629 CD1 TYR B 88 -4.827 25.712 28.789 1.00 27.79 C ANISOU 629 CD1 TYR B 88 3025 3045 4489 681 53 208 C ATOM 630 CD2 TYR B 88 -5.979 25.925 26.705 1.00 31.30 C ANISOU 630 CD2 TYR B 88 3437 3479 4977 706 -62 307 C ATOM 631 CE1 TYR B 88 -5.889 26.323 29.442 1.00 30.01 C ANISOU 631 CE1 TYR B 88 3258 3308 4835 749 85 207 C ATOM 632 CE2 TYR B 88 -7.048 26.537 27.353 1.00 30.44 C ANISOU 632 CE2 TYR B 88 3274 3353 4939 777 -34 307 C ATOM 633 CZ TYR B 88 -6.991 26.731 28.723 1.00 36.69 C ANISOU 633 CZ TYR B 88 4059 4142 5742 798 42 255 C ATOM 634 OH TYR B 88 -8.033 27.338 29.399 1.00 37.39 O ANISOU 634 OH TYR B 88 4094 4214 5900 870 78 250 O ATOM 635 N SER B 89 -0.336 25.095 26.440 1.00 20.76 N ANISOU 635 N SER B 89 2360 2148 3379 469 -12 191 N ATOM 636 CA SER B 89 0.891 24.428 25.997 1.00 19.19 C ANISOU 636 CA SER B 89 2199 1975 3119 405 -19 176 C ATOM 637 C SER B 89 1.580 23.772 27.172 1.00 17.89 C ANISOU 637 C SER B 89 2025 1842 2929 384 26 123 C ATOM 638 O SER B 89 1.474 24.258 28.296 1.00 20.18 O ANISOU 638 O SER B 89 2312 2117 3241 411 69 92 O ATOM 639 CB SER B 89 1.865 25.439 25.381 1.00 21.51 C ANISOU 639 CB SER B 89 2566 2220 3388 379 -20 178 C ATOM 640 OG SER B 89 1.300 26.158 24.298 1.00 23.38 O ANISOU 640 OG SER B 89 2822 2419 3642 397 -63 229 O ATOM 641 N LEU B 90 2.299 22.679 26.904 1.00 16.96 N ANISOU 641 N LEU B 90 1909 1768 2766 338 15 113 N ATOM 642 CA LEU B 90 3.253 22.108 27.839 1.00 16.74 C ANISOU 642 CA LEU B 90 1888 1767 2707 310 50 64 C ATOM 643 C LEU B 90 4.635 22.474 27.320 1.00 17.71 C ANISOU 643 C LEU B 90 2065 1876 2789 266 52 49 C ATOM 644 O LEU B 90 4.857 22.486 26.117 1.00 18.10 O ANISOU 644 O LEU B 90 2138 1921 2820 243 21 77 O ATOM 645 CB LEU B 90 3.129 20.577 27.867 1.00 17.99 C ANISOU 645 CB LEU B 90 2009 1982 2844 291 35 64 C ATOM 646 CG LEU B 90 1.778 20.017 28.310 1.00 18.94 C ANISOU 646 CG LEU B 90 2070 2125 3000 323 31 81 C ATOM 647 CD1 LEU B 90 1.632 18.542 27.933 1.00 20.70 C ANISOU 647 CD1 LEU B 90 2266 2396 3201 296 3 91 C ATOM 648 CD2 LEU B 90 1.603 20.190 29.797 1.00 21.09 C ANISOU 648 CD2 LEU B 90 2326 2398 3288 347 81 46 C ATOM 649 N VAL B 91 5.549 22.777 28.231 1.00 15.29 N ANISOU 649 N VAL B 91 1780 1563 2468 252 88 5 N ATOM 650 CA VAL B 91 6.917 23.136 27.885 1.00 15.43 C ANISOU 650 CA VAL B 91 1841 1570 2450 206 95 -14 C ATOM 651 C VAL B 91 7.872 22.103 28.485 1.00 12.34 C ANISOU 651 C VAL B 91 1437 1226 2025 176 107 -52 C ATOM 652 O VAL B 91 7.899 21.889 29.716 1.00 16.96 O ANISOU 652 O VAL B 91 2007 1824 2614 187 132 -84 O ATOM 653 CB VAL B 91 7.278 24.542 28.395 1.00 19.50 C ANISOU 653 CB VAL B 91 2398 2033 2980 211 124 -33 C ATOM 654 CG1 VAL B 91 8.665 24.935 27.906 1.00 22.17 C ANISOU 654 CG1 VAL B 91 2778 2361 3283 158 129 -48 C ATOM 655 CG2 VAL B 91 6.245 25.546 27.925 1.00 19.84 C ANISOU 655 CG2 VAL B 91 2452 2024 3062 252 112 4 C ATOM 656 N MET B 92 8.653 21.486 27.592 1.00 17.13 N ANISOU 656 N MET B 92 2052 1857 2599 138 90 -48 N ATOM 657 CA MET B 92 9.478 20.317 27.904 1.00 16.54 C ANISOU 657 CA MET B 92 1960 1830 2495 114 93 -76 C ATOM 658 C MET B 92 10.951 20.627 27.673 1.00 17.74 C ANISOU 658 C MET B 92 2139 1983 2620 71 106 -103 C ATOM 659 O MET B 92 11.291 21.481 26.854 1.00 15.65 O ANISOU 659 O MET B 92 1906 1690 2350 51 106 -89 O ATOM 660 CB MET B 92 9.053 19.150 26.992 1.00 15.53 C ANISOU 660 CB MET B 92 1813 1733 2353 110 61 -50 C ATOM 661 CG MET B 92 9.672 17.792 27.321 1.00 22.08 C ANISOU 661 CG MET B 92 2623 2609 3159 95 60 -75 C ATOM 662 SD MET B 92 9.188 16.571 26.055 1.00 23.59 S ANISOU 662 SD MET B 92 2805 2825 3332 85 22 -45 S ATOM 663 CE MET B 92 10.354 16.976 24.747 1.00 22.70 C ANISOU 663 CE MET B 92 2733 2706 3185 44 23 -46 C ATOM 664 N GLU B 93 11.845 19.935 28.366 1.00 16.41 N ANISOU 664 N GLU B 93 1956 1848 2433 55 116 -139 N ATOM 665 CA GLU B 93 13.266 20.153 28.086 1.00 18.26 C ANISOU 665 CA GLU B 93 2204 2089 2644 13 128 -164 C ATOM 666 C GLU B 93 13.640 19.669 26.678 1.00 20.34 C ANISOU 666 C GLU B 93 2475 2369 2885 -12 115 -145 C ATOM 667 O GLU B 93 12.984 18.799 26.098 1.00 17.80 O ANISOU 667 O GLU B 93 2141 2064 2559 1 93 -123 O ATOM 668 CB GLU B 93 14.136 19.501 29.143 1.00 22.86 C ANISOU 668 CB GLU B 93 2765 2705 3215 6 136 -205 C ATOM 669 CG GLU B 93 14.118 18.018 29.087 1.00 21.67 C ANISOU 669 CG GLU B 93 2585 2596 3052 14 120 -206 C ATOM 670 CD GLU B 93 15.028 17.399 30.124 1.00 21.91 C ANISOU 670 CD GLU B 93 2596 2657 3071 8 124 -244 C ATOM 671 OE1 GLU B 93 16.236 17.744 30.157 1.00 30.73 O ANISOU 671 OE1 GLU B 93 3715 3782 4180 -21 133 -270 O ATOM 672 OE2 GLU B 93 14.531 16.569 30.906 1.00 18.52 O1- ANISOU 672 OE2 GLU B 93 2150 2245 2644 32 115 -246 O1- ATOM 673 N TYR B 94 14.708 20.248 26.142 1.00 17.06 N ATOM 674 CA TYR B 94 15.109 20.040 24.761 1.00 20.27 C ATOM 675 C TYR B 94 16.269 19.061 24.739 1.00 21.50 C ATOM 676 O TYR B 94 17.278 19.266 25.430 1.00 21.31 O ATOM 677 CB TYR B 94 15.513 21.394 24.173 1.00 19.03 C ATOM 678 CG TYR B 94 16.191 21.381 22.814 1.00 26.41 C ATOM 679 CD1 TYR B 94 15.652 20.688 21.736 1.00 25.96 C ATOM 680 CD2 TYR B 94 17.350 22.113 22.610 1.00 27.50 C ATOM 681 CE1 TYR B 94 16.278 20.709 20.490 1.00 28.82 C ATOM 682 CE2 TYR B 94 17.977 22.143 21.384 1.00 31.24 C ATOM 683 CZ TYR B 94 17.439 21.444 20.327 1.00 33.48 C ATOM 684 OH TYR B 94 18.076 21.486 19.104 1.00 31.49 O ATOM 685 N MET B 95 16.106 17.980 23.979 1.00 18.09 N ATOM 686 CA MET B 95 17.159 16.976 23.827 1.00 20.31 C ATOM 687 C MET B 95 17.736 17.169 22.435 1.00 23.38 C ATOM 688 O MET B 95 17.076 16.902 21.428 1.00 24.24 O ATOM 689 CB MET B 95 16.607 15.550 23.990 1.00 22.37 C ATOM 690 CG MET B 95 15.894 15.291 25.317 1.00 20.99 C ATOM 691 SD MET B 95 16.968 15.469 26.754 1.00 29.12 S ATOM 692 CE MET B 95 18.012 14.033 26.560 1.00 30.21 C ATOM 693 N GLU B 96 18.970 17.647 22.384 1.00 31.51 N ATOM 694 CA GLU B 96 19.520 18.196 21.149 1.00 28.90 C ATOM 695 C GLU B 96 19.702 17.186 20.010 1.00 31.39 C ATOM 696 O GLU B 96 19.661 17.564 18.836 1.00 37.89 O ATOM 697 CB GLU B 96 20.830 18.926 21.438 1.00 37.40 C ATOM 698 CG GLU B 96 20.678 20.168 22.326 1.00 39.77 C ATOM 699 CD GLU B 96 20.830 19.878 23.816 1.00 47.96 C ATOM 700 OE1 GLU B 96 21.067 20.843 24.580 1.00 55.99 O ATOM 701 OE2 GLU B 96 20.712 18.696 24.227 1.00 46.57 O1- ATOM 702 N LYS B 97 19.877 15.910 20.342 1.00 29.46 N ATOM 703 CA LYS B 97 20.062 14.895 19.292 1.00 22.77 C ATOM 704 C LYS B 97 18.767 14.277 18.764 1.00 28.18 C ATOM 705 O LYS B 97 18.790 13.404 17.885 1.00 28.12 O ATOM 706 CB LYS B 97 21.040 13.810 19.743 1.00 23.58 C ATOM 707 CG LYS B 97 22.480 14.295 19.748 1.00 33.11 C ATOM 708 CD LYS B 97 23.476 13.147 19.783 1.00 35.06 C ATOM 709 CE LYS B 97 24.893 13.672 19.568 1.00 43.05 C ATOM 710 NZ LYS B 97 25.075 14.265 18.208 1.00 44.62 N1+ ATOM 711 N GLY B 98 17.634 14.741 19.273 1.00 22.80 N ATOM 712 CA GLY B 98 16.359 14.256 18.774 1.00 15.55 C ATOM 713 C GLY B 98 16.090 12.871 19.332 1.00 20.95 C ATOM 714 O GLY B 98 16.578 12.527 20.404 1.00 17.29 O ATOM 715 N ASN B 99 15.324 12.067 18.613 1.00 19.12 N ATOM 716 CA ASN B 99 14.968 10.751 19.135 1.00 18.69 C ATOM 717 C ASN B 99 15.964 9.641 18.749 1.00 18.90 C ATOM 718 O ASN B 99 16.855 9.827 17.898 1.00 19.38 O ATOM 719 CB ASN B 99 13.510 10.399 18.772 1.00 15.36 C ATOM 720 CG ASN B 99 13.312 10.140 17.283 1.00 17.89 C ATOM 721 ND2 ASN B 99 12.237 10.689 16.724 1.00 18.17 N ATOM 722 OD1 ASN B 99 14.113 9.456 16.646 1.00 19.16 O ATOM 723 N LEU B 100 15.808 8.488 19.386 1.00 14.43 N ATOM 724 CA LEU B 100 16.730 7.365 19.212 1.00 13.82 C ATOM 725 C LEU B 100 16.857 6.878 17.770 1.00 14.71 C ATOM 726 O LEU B 100 17.957 6.561 17.316 1.00 17.19 O ATOM 727 CB LEU B 100 16.324 6.210 20.136 1.00 13.71 C ATOM 728 CG LEU B 100 17.132 4.919 20.019 1.00 12.90 C ATOM 729 CD1 LEU B 100 18.580 5.204 20.388 1.00 13.44 C ATOM 730 CD2 LEU B 100 16.545 3.839 20.928 1.00 18.60 C ATOM 731 N MET B 101 15.758 6.807 17.035 1.00 15.37 N ATOM 732 CA MET B 101 15.864 6.302 15.663 1.00 20.35 C ATOM 733 C MET B 101 16.627 7.305 14.807 1.00 23.59 C ATOM 734 O MET B 101 17.384 6.920 13.910 1.00 19.48 O ATOM 735 CB MET B 101 14.494 6.021 15.055 1.00 18.33 C ATOM 736 CG MET B 101 14.554 5.384 13.639 1.00 23.12 C ATOM 737 SD MET B 101 15.392 3.777 13.581 1.00 21.27 S ATOM 738 CE MET B 101 14.248 2.798 14.558 1.00 20.98 C ATOM 739 N HIS B 102 16.438 8.588 15.098 1.00 19.93 N ATOM 740 CA HIS B 102 17.169 9.626 14.377 1.00 21.60 C ATOM 741 C HIS B 102 18.672 9.508 14.652 1.00 23.51 C ATOM 742 O HIS B 102 19.499 9.713 13.764 1.00 23.38 O ATOM 743 CB HIS B 102 16.636 11.015 14.747 1.00 25.63 C ATOM 744 CG HIS B 102 17.295 12.127 13.998 1.00 30.77 C ATOM 745 CD2 HIS B 102 17.087 12.611 12.750 1.00 35.37 C ATOM 746 ND1 HIS B 102 18.333 12.867 14.527 1.00 39.16 N ATOM 747 CE1 HIS B 102 18.727 13.764 13.641 1.00 36.52 C ATOM 748 NE2 HIS B 102 17.986 13.631 12.554 1.00 39.11 N ATOM 749 N VAL B 103 19.027 9.139 15.877 1.00 18.90 N ATOM 750 CA VAL B 103 20.431 8.910 16.209 1.00 22.59 C ATOM 751 C VAL B 103 20.982 7.649 15.520 1.00 22.52 C ATOM 752 O VAL B 103 22.112 7.652 15.013 1.00 24.51 O ATOM 753 CB VAL B 103 20.653 8.848 17.740 1.00 18.38 C ATOM 754 CG1 VAL B 103 22.065 8.353 18.067 1.00 21.81 C ATOM 755 CG2 VAL B 103 20.418 10.235 18.371 1.00 18.23 C ATOM 756 N LEU B 104 20.183 6.584 15.490 1.00 20.54 N ATOM 757 CA LEU B 104 20.624 5.290 14.958 1.00 20.31 C ATOM 758 C LEU B 104 20.846 5.352 13.452 1.00 24.18 C ATOM 759 O LEU B 104 21.656 4.603 12.900 1.00 24.13 O ATOM 760 CB LEU B 104 19.589 4.205 15.258 1.00 20.96 C ATOM 761 CG LEU B 104 19.466 3.802 16.728 1.00 19.78 C ATOM 762 CD1 LEU B 104 18.212 2.939 16.967 1.00 18.54 C ATOM 763 CD2 LEU B 104 20.738 3.093 17.189 1.00 19.01 C ATOM 764 N LYS B 105 20.116 6.248 12.799 1.00 25.02 N ATOM 765 CA LYS B 105 20.194 6.392 11.344 1.00 30.42 C ATOM 766 C LYS B 105 21.189 7.449 10.884 1.00 34.21 C ATOM 767 O LYS B 105 21.407 7.620 9.684 1.00 38.70 O ATOM 768 CB LYS B 105 18.811 6.699 10.778 1.00 31.00 C ATOM 769 CG LYS B 105 17.921 5.478 10.714 1.00 29.65 C ATOM 770 CD LYS B 105 16.578 5.817 10.115 1.00 37.26 C ATOM 771 CE LYS B 105 15.851 4.551 9.697 1.00 36.56 C ATOM 772 NZ LYS B 105 14.468 4.854 9.232 1.00 40.39 N1+ ATOM 773 N ALA B 106 21.793 8.151 11.838 1.00 29.17 N ATOM 774 CA ALA B 106 22.758 9.206 11.531 1.00 32.66 C ATOM 775 C ALA B 106 23.975 8.692 10.762 1.00 38.83 C ATOM 776 O ALA B 106 24.201 7.482 10.656 1.00 33.62 O ATOM 777 CB ALA B 106 23.199 9.906 12.801 1.00 33.68 C ATOM 778 N GLU B 107 24.763 9.630 10.240 1.00 46.96 N ATOM 779 CA GLU B 107 25.941 9.289 9.447 1.00 52.20 C ATOM 780 C GLU B 107 27.027 8.651 10.306 1.00 50.33 C ATOM 781 O GLU B 107 27.609 7.628 9.931 1.00 50.95 O ATOM 782 CB GLU B 107 26.496 10.531 8.745 1.00 52.38 C ATOM 783 N MET B 108 27.298 9.267 11.452 1.00 41.42 N ATOM 784 CA MET B 108 28.308 8.764 12.379 1.00 47.71 C ATOM 785 C MET B 108 27.803 7.527 13.121 1.00 43.39 C ATOM 786 O MET B 108 26.733 7.550 13.739 1.00 40.09 O ATOM 787 CB MET B 108 28.705 9.858 13.376 1.00 43.60 C ATOM 788 N SER B 109 28.569 6.444 13.048 1.00 45.94 N ATOM 789 CA SER B 109 28.194 5.199 13.706 1.00 42.30 C ATOM 790 C SER B 109 28.153 5.375 15.224 1.00 39.68 C ATOM 791 O SER B 109 28.929 6.143 15.793 1.00 39.69 O ATOM 792 CB SER B 109 29.182 4.090 13.329 1.00 40.53 C ATOM 793 OG SER B 109 28.719 2.821 13.756 1.00 47.36 O ATOM 794 N THR B 110 27.228 4.673 15.873 1.00 33.65 N ATOM 795 CA THR B 110 27.137 4.683 17.328 1.00 28.93 C ATOM 796 C THR B 110 27.832 3.426 17.831 1.00 29.35 C ATOM 797 O THR B 110 27.410 2.321 17.499 1.00 25.53 O ATOM 798 CB THR B 110 25.666 4.674 17.779 1.00 28.83 C ATOM 799 CG2 THR B 110 25.569 4.757 19.293 1.00 21.68 C ATOM 800 OG1 THR B 110 24.989 5.797 17.204 1.00 28.38 O ATOM 801 N PRO B 111 28.915 3.585 18.614 1.00 27.49 N ATOM 802 CA PRO B 111 29.719 2.435 19.060 1.00 22.39 C ATOM 803 C PRO B 111 28.919 1.442 19.897 1.00 22.81 C ATOM 804 O PRO B 111 27.937 1.835 20.541 1.00 19.88 O ATOM 805 CB PRO B 111 30.799 3.077 19.946 1.00 28.04 C ATOM 806 CG PRO B 111 30.850 4.522 19.532 1.00 27.03 C ATOM 807 CD PRO B 111 29.445 4.867 19.110 1.00 28.10 C ATOM 808 N LEU B 112 29.338 0.179 19.908 1.00 19.13 N ANISOU 808 N LEU B 112 1994 2713 2562 9 278 -700 N ATOM 809 CA LEU B 112 28.673 -0.821 20.754 1.00 17.40 C ANISOU 809 CA LEU B 112 1794 2470 2349 66 191 -674 C ATOM 810 C LEU B 112 28.576 -0.391 22.220 1.00 19.96 C ANISOU 810 C LEU B 112 2111 2770 2702 93 149 -655 C ATOM 811 O LEU B 112 27.535 -0.566 22.836 1.00 15.98 O ANISOU 811 O LEU B 112 1650 2243 2179 111 106 -589 O ATOM 812 CB LEU B 112 29.344 -2.200 20.652 1.00 20.98 C ANISOU 812 CB LEU B 112 2214 2929 2828 107 148 -750 C ATOM 813 CG LEU B 112 28.811 -3.309 21.577 1.00 19.81 C ANISOU 813 CG LEU B 112 2090 2749 2689 165 55 -729 C ATOM 814 CD1 LEU B 112 27.342 -3.631 21.312 1.00 20.96 C ANISOU 814 CD1 LEU B 112 2304 2877 2782 159 35 -638 C ATOM 815 CD2 LEU B 112 29.643 -4.585 21.496 1.00 24.27 C ANISOU 815 CD2 LEU B 112 2618 3314 3290 208 9 -814 C ATOM 816 N SER B 113 29.648 0.174 22.777 1.00 18.98 N ANISOU 816 N SER B 113 1932 2655 2625 92 165 -718 N ATOM 817 CA SER B 113 29.635 0.602 24.187 1.00 22.48 C ANISOU 817 CA SER B 113 2367 3079 3094 118 125 -708 C ATOM 818 C SER B 113 28.505 1.587 24.480 1.00 19.91 C ANISOU 818 C SER B 113 2089 2736 2739 92 143 -617 C ATOM 819 O SER B 113 27.865 1.545 25.556 1.00 19.29 O ANISOU 819 O SER B 113 2035 2637 2658 117 95 -578 O ATOM 820 CB SER B 113 30.971 1.246 24.570 1.00 26.67 C ANISOU 820 CB SER B 113 2829 3624 3680 111 150 -792 C ATOM 821 OG SER B 113 31.252 2.361 23.733 1.00 31.01 O ANISOU 821 OG SER B 113 3373 4187 4224 47 236 -788 O ATOM 822 N VAL B 114 28.269 2.479 23.520 1.00 17.85 N ANISOU 822 N VAL B 114 1844 2482 2456 42 211 -586 N ATOM 823 CA VAL B 114 27.232 3.482 23.668 1.00 18.60 C ANISOU 823 CA VAL B 114 1980 2557 2530 19 227 -506 C ATOM 824 C VAL B 114 25.851 2.858 23.508 1.00 16.07 C ANISOU 824 C VAL B 114 1714 2222 2168 34 188 -434 C ATOM 825 O VAL B 114 24.937 3.191 24.257 1.00 14.10 O ANISOU 825 O VAL B 114 1489 1953 1915 42 164 -383 O ATOM 826 CB VAL B 114 27.440 4.671 22.707 1.00 21.51 C ANISOU 826 CB VAL B 114 2355 2929 2888 -39 306 -494 C ATOM 827 CG1 VAL B 114 26.267 5.644 22.784 1.00 25.07 C ANISOU 827 CG1 VAL B 114 2853 3352 3319 -56 311 -409 C ATOM 828 CG2 VAL B 114 28.738 5.400 23.053 1.00 22.62 C ANISOU 828 CG2 VAL B 114 2436 3080 3077 -59 348 -567 C ATOM 829 N LYS B 115 25.688 1.954 22.548 1.00 16.19 N ANISOU 829 N LYS B 115 1748 2249 2155 35 182 -435 N ATOM 830 CA LYS B 115 24.422 1.236 22.439 1.00 13.96 C ANISOU 830 CA LYS B 115 1511 1952 1840 51 140 -377 C ATOM 831 C LYS B 115 24.092 0.472 23.724 1.00 16.00 C ANISOU 831 C LYS B 115 1773 2194 2114 92 76 -374 C ATOM 832 O LYS B 115 22.934 0.438 24.153 1.00 12.60 O ANISOU 832 O LYS B 115 1375 1746 1668 96 52 -318 O ATOM 833 CB LYS B 115 24.417 0.288 21.235 1.00 14.36 C ANISOU 833 CB LYS B 115 1576 2019 1861 49 141 -390 C ATOM 834 CG LYS B 115 24.512 0.999 19.921 1.00 14.52 C ANISOU 834 CG LYS B 115 1612 2054 1849 3 202 -379 C ATOM 835 CD LYS B 115 24.322 0.033 18.723 1.00 17.31 C ANISOU 835 CD LYS B 115 1988 2425 2163 0 199 -388 C ATOM 836 CE LYS B 115 24.211 0.823 17.428 1.00 20.79 C ANISOU 836 CE LYS B 115 2465 2878 2558 -49 255 -361 C ATOM 837 NZ LYS B 115 23.732 -0.015 16.281 1.00 17.30 N1+ ANISOU 837 NZ LYS B 115 2056 2450 2067 -53 245 -355 N1+ ATOM 838 N GLY B 116 25.111 -0.139 24.330 1.00 14.16 N ANISOU 838 N GLY B 116 1506 1964 1910 121 48 -437 N ATOM 839 CA GLY B 116 24.937 -0.851 25.581 1.00 15.59 C ANISOU 839 CA GLY B 116 1699 2124 2100 159 -16 -435 C ATOM 840 C GLY B 116 24.491 0.102 26.673 1.00 15.32 C ANISOU 840 C GLY B 116 1672 2079 2070 152 -13 -402 C ATOM 841 O GLY B 116 23.562 -0.213 27.450 1.00 14.34 O ANISOU 841 O GLY B 116 1583 1936 1928 161 -46 -359 O ATOM 842 N ARG B 117 25.139 1.269 26.735 1.00 16.70 N ANISOU 842 N ARG B 117 1811 2264 2268 132 30 -426 N ATOM 843 CA ARG B 117 24.724 2.258 27.744 1.00 14.14 C ANISOU 843 CA ARG B 117 1490 1929 1952 124 35 -399 C ATOM 844 C ARG B 117 23.294 2.780 27.519 1.00 14.96 C ANISOU 844 C ARG B 117 1631 2020 2031 102 53 -325 C ATOM 845 O ARG B 117 22.526 2.925 28.470 1.00 14.04 O ANISOU 845 O ARG B 117 1533 1891 1910 107 34 -296 O ATOM 846 CB ARG B 117 25.710 3.419 27.828 1.00 16.28 C ANISOU 846 CB ARG B 117 1716 2211 2259 106 78 -443 C ATOM 847 CG ARG B 117 25.586 4.239 29.123 1.00 20.98 C ANISOU 847 CG ARG B 117 2305 2797 2870 109 70 -440 C ATOM 848 CD ARG B 117 26.471 5.494 29.071 1.00 21.68 C ANISOU 848 CD ARG B 117 2348 2893 2997 83 120 -480 C ATOM 849 NE ARG B 117 26.065 6.352 27.958 1.00 20.62 N ANISOU 849 NE ARG B 117 2226 2752 2855 41 181 -441 N ATOM 850 CZ ARG B 117 26.744 7.411 27.520 1.00 32.10 C ANISOU 850 CZ ARG B 117 3654 4208 4335 6 238 -465 C ATOM 851 NH1 ARG B 117 27.885 7.765 28.103 1.00 32.29 N1+ ANISOU 851 NH1 ARG B 117 3626 4242 4400 7 245 -535 N1+ ATOM 852 NH2 ARG B 117 26.287 8.113 26.490 1.00 29.99 N ANISOU 852 NH2 ARG B 117 3414 3930 4051 -32 285 -420 N ATOM 853 N ILE B 118 22.939 3.046 26.265 1.00 13.41 N ANISOU 853 N ILE B 118 1447 1829 1820 78 87 -299 N ATOM 854 CA ILE B 118 21.582 3.447 25.912 1.00 15.04 C ANISOU 854 CA ILE B 118 1687 2021 2007 63 93 -234 C ATOM 855 C ILE B 118 20.581 2.412 26.410 1.00 13.57 C ANISOU 855 C ILE B 118 1528 1825 1802 82 47 -207 C ATOM 856 O ILE B 118 19.566 2.772 27.025 1.00 12.91 O ANISOU 856 O ILE B 118 1457 1728 1719 78 41 -172 O ATOM 857 CB ILE B 118 21.433 3.666 24.389 1.00 14.95 C ANISOU 857 CB ILE B 118 1693 2016 1973 39 124 -213 C ATOM 858 CG1 ILE B 118 22.148 4.959 23.974 1.00 12.45 C ANISOU 858 CG1 ILE B 118 1361 1700 1671 7 178 -223 C ATOM 859 CG2 ILE B 118 19.948 3.748 23.986 1.00 15.72 C ANISOU 859 CG2 ILE B 118 1826 2098 2050 35 109 -151 C ATOM 860 CD1 ILE B 118 22.326 5.101 22.455 1.00 14.52 C ANISOU 860 CD1 ILE B 118 1645 1969 1901 -22 214 -213 C ATOM 861 N ILE B 119 20.853 1.135 26.135 1.00 11.88 N ANISOU 861 N ILE B 119 1323 1617 1576 100 17 -226 N ATOM 862 CA ILE B 119 19.974 0.065 26.633 1.00 11.30 C ANISOU 862 CA ILE B 119 1280 1529 1485 114 -26 -203 C ATOM 863 C ILE B 119 19.854 0.069 28.151 1.00 14.31 C ANISOU 863 C ILE B 119 1668 1897 1871 123 -48 -203 C ATOM 864 O ILE B 119 18.738 -0.041 28.704 1.00 10.79 O ANISOU 864 O ILE B 119 1246 1440 1414 115 -56 -168 O ATOM 865 CB ILE B 119 20.444 -1.315 26.143 1.00 11.30 C ANISOU 865 CB ILE B 119 1287 1529 1475 134 -57 -231 C ATOM 866 CG1 ILE B 119 20.318 -1.346 24.621 1.00 14.81 C ANISOU 866 CG1 ILE B 119 1734 1989 1905 119 -33 -225 C ATOM 867 CG2 ILE B 119 19.617 -2.438 26.784 1.00 12.11 C ANISOU 867 CG2 ILE B 119 1427 1611 1563 145 -102 -208 C ATOM 868 CD1 ILE B 119 21.180 -2.435 23.963 1.00 16.40 C ANISOU 868 CD1 ILE B 119 1926 2199 2105 136 -49 -274 C ATOM 869 N LEU B 120 20.980 0.225 28.842 1.00 12.46 N ANISOU 869 N LEU B 120 1412 1667 1654 139 -57 -246 N ATOM 870 CA LEU B 120 20.914 0.266 30.308 1.00 12.07 C ANISOU 870 CA LEU B 120 1377 1608 1602 147 -82 -248 C ATOM 871 C LEU B 120 20.084 1.439 30.831 1.00 11.29 C ANISOU 871 C LEU B 120 1274 1508 1507 123 -49 -219 C ATOM 872 O LEU B 120 19.329 1.282 31.801 1.00 13.10 O ANISOU 872 O LEU B 120 1530 1728 1720 118 -60 -199 O ATOM 873 CB LEU B 120 22.332 0.325 30.913 1.00 11.40 C ANISOU 873 CB LEU B 120 1264 1529 1537 172 -103 -306 C ATOM 874 CG LEU B 120 22.412 0.386 32.438 1.00 15.93 C ANISOU 874 CG LEU B 120 1855 2093 2102 183 -134 -313 C ATOM 875 CD1 LEU B 120 21.853 -0.868 33.090 1.00 14.97 C ANISOU 875 CD1 LEU B 120 1792 1949 1945 194 -185 -288 C ATOM 876 CD2 LEU B 120 23.867 0.627 32.858 1.00 16.85 C ANISOU 876 CD2 LEU B 120 1934 2220 2248 208 -155 -378 C ATOM 877 N GLU B 121 20.219 2.603 30.200 1.00 12.60 N ANISOU 877 N GLU B 121 1411 1682 1695 107 -6 -219 N ATOM 878 CA GLU B 121 19.477 3.785 30.632 1.00 12.14 C ANISOU 878 CA GLU B 121 1345 1618 1650 88 23 -197 C ATOM 879 C GLU B 121 17.986 3.654 30.349 1.00 10.24 C ANISOU 879 C GLU B 121 1126 1367 1397 75 25 -151 C ATOM 880 O GLU B 121 17.154 4.106 31.147 1.00 11.44 O ANISOU 880 O GLU B 121 1279 1513 1554 65 33 -139 O ATOM 881 CB GLU B 121 20.054 5.045 29.978 1.00 12.02 C ANISOU 881 CB GLU B 121 1298 1605 1663 73 65 -208 C ATOM 882 CG GLU B 121 21.424 5.403 30.565 1.00 15.15 C ANISOU 882 CG GLU B 121 1664 2012 2083 81 68 -263 C ATOM 883 CD GLU B 121 22.097 6.559 29.882 1.00 15.06 C ANISOU 883 CD GLU B 121 1623 2001 2100 60 115 -278 C ATOM 884 OE1 GLU B 121 21.497 7.170 28.968 1.00 18.66 O ANISOU 884 OE1 GLU B 121 2091 2446 2555 39 143 -240 O ATOM 885 OE2 GLU B 121 23.260 6.840 30.255 1.00 20.49 O1- ANISOU 885 OE2 GLU B 121 2276 2697 2810 63 121 -330 O1- ATOM 886 N ILE B 122 17.643 3.047 29.220 1.00 10.94 N ANISOU 886 N ILE B 122 1228 1457 1474 75 20 -131 N ATOM 887 CA ILE B 122 16.230 2.796 28.941 1.00 11.32 C ANISOU 887 CA ILE B 122 1292 1496 1513 65 14 -95 C ATOM 888 C ILE B 122 15.690 1.863 30.026 1.00 12.29 C ANISOU 888 C ILE B 122 1438 1613 1619 65 -8 -94 C ATOM 889 O ILE B 122 14.592 2.081 30.559 1.00 10.02 O ANISOU 889 O ILE B 122 1152 1320 1335 50 0 -79 O ATOM 890 CB ILE B 122 16.030 2.144 27.563 1.00 11.98 C ANISOU 890 CB ILE B 122 1388 1582 1581 67 5 -80 C ATOM 891 CG1 ILE B 122 16.347 3.129 26.436 1.00 13.54 C ANISOU 891 CG1 ILE B 122 1576 1782 1785 59 31 -72 C ATOM 892 CG2 ILE B 122 14.612 1.577 27.421 1.00 11.00 C ANISOU 892 CG2 ILE B 122 1279 1450 1449 60 -11 -53 C ATOM 893 CD1 ILE B 122 16.566 2.409 25.082 1.00 12.23 C ANISOU 893 CD1 ILE B 122 1425 1626 1594 60 24 -70 C ATOM 894 N ILE B 123 16.456 0.824 30.367 1.00 9.12 N ANISOU 894 N ILE B 123 1055 1211 1199 80 -37 -113 N ATOM 895 CA ILE B 123 16.032 -0.049 31.464 1.00 9.31 C ANISOU 895 CA ILE B 123 1114 1223 1199 76 -60 -108 C ATOM 896 C ILE B 123 15.843 0.723 32.777 1.00 13.21 C ANISOU 896 C ILE B 123 1606 1719 1694 64 -44 -114 C ATOM 897 O ILE B 123 14.848 0.540 33.470 1.00 12.84 O ANISOU 897 O ILE B 123 1580 1666 1634 42 -36 -100 O ATOM 898 CB ILE B 123 17.020 -1.211 31.672 1.00 9.92 C ANISOU 898 CB ILE B 123 1218 1293 1260 100 -103 -128 C ATOM 899 CG1 ILE B 123 16.975 -2.170 30.474 1.00 11.54 C ANISOU 899 CG1 ILE B 123 1429 1494 1462 109 -119 -124 C ATOM 900 CG2 ILE B 123 16.678 -2.018 32.922 1.00 11.82 C ANISOU 900 CG2 ILE B 123 1507 1514 1469 94 -130 -119 C ATOM 901 CD1 ILE B 123 18.270 -3.014 30.365 1.00 12.76 C ANISOU 901 CD1 ILE B 123 1587 1643 1616 141 -158 -160 C ATOM 902 N GLU B 124 16.791 1.591 33.118 1.00 11.95 N ANISOU 902 N GLU B 124 1421 1568 1550 74 -36 -141 N ATOM 903 CA GLU B 124 16.699 2.383 34.353 1.00 12.19 C ANISOU 903 CA GLU B 124 1448 1602 1582 64 -22 -153 C ATOM 904 C GLU B 124 15.441 3.244 34.381 1.00 10.45 C ANISOU 904 C GLU B 124 1210 1382 1380 39 16 -136 C ATOM 905 O GLU B 124 14.753 3.319 35.409 1.00 12.23 O ANISOU 905 O GLU B 124 1447 1607 1592 20 28 -138 O ATOM 906 CB GLU B 124 17.910 3.298 34.488 1.00 10.94 C ANISOU 906 CB GLU B 124 1255 1453 1448 78 -16 -188 C ATOM 907 CG GLU B 124 19.205 2.571 34.868 1.00 12.19 C ANISOU 907 CG GLU B 124 1424 1613 1594 106 -59 -221 C ATOM 908 CD GLU B 124 20.388 3.526 34.937 1.00 19.36 C ANISOU 908 CD GLU B 124 2287 2532 2535 116 -49 -265 C ATOM 909 OE1 GLU B 124 20.357 4.543 34.223 1.00 19.95 O ANISOU 909 OE1 GLU B 124 2328 2611 2642 103 -7 -263 O ATOM 910 OE2 GLU B 124 21.342 3.253 35.708 1.00 22.72 O1- ANISOU 910 OE2 GLU B 124 2716 2961 2956 138 -85 -302 O1- ATOM 911 N GLY B 125 15.143 3.864 33.247 1.00 8.74 N ANISOU 911 N GLY B 125 965 1163 1193 39 34 -123 N ATOM 912 CA GLY B 125 13.987 4.740 33.147 1.00 11.38 C ANISOU 912 CA GLY B 125 1278 1493 1555 24 60 -111 C ATOM 913 C GLY B 125 12.686 3.967 33.266 1.00 10.39 C ANISOU 913 C GLY B 125 1168 1364 1417 7 58 -95 C ATOM 914 O GLY B 125 11.740 4.408 33.957 1.00 10.88 O ANISOU 914 O GLY B 125 1217 1425 1491 -11 80 -102 O ATOM 915 N MET B 126 12.623 2.811 32.597 1.00 9.44 N ANISOU 915 N MET B 126 1072 1241 1274 11 35 -79 N ATOM 916 CA MET B 126 11.392 2.019 32.674 1.00 12.01 C ANISOU 916 CA MET B 126 1411 1561 1590 -9 34 -67 C ATOM 917 C MET B 126 11.200 1.417 34.050 1.00 12.63 C ANISOU 917 C MET B 126 1523 1639 1637 -32 40 -76 C ATOM 918 O MET B 126 10.079 1.360 34.547 1.00 13.32 O ANISOU 918 O MET B 126 1608 1727 1728 -60 62 -79 O ATOM 919 CB MET B 126 11.342 0.939 31.596 1.00 10.20 C ANISOU 919 CB MET B 126 1200 1328 1348 -1 8 -50 C ATOM 920 CG MET B 126 11.218 1.524 30.171 1.00 9.74 C ANISOU 920 CG MET B 126 1116 1270 1313 13 4 -38 C ATOM 921 SD MET B 126 9.760 2.607 29.949 1.00 12.76 S ANISOU 921 SD MET B 126 1460 1648 1740 4 21 -35 S ATOM 922 CE MET B 126 8.464 1.469 30.485 1.00 12.07 C ANISOU 922 CE MET B 126 1382 1559 1646 -24 22 -40 C ATOM 923 N ALA B 127 12.284 0.958 34.665 1.00 10.18 N ANISOU 923 N ALA B 127 1244 1327 1295 -20 18 -82 N ATOM 924 CA ALA B 127 12.220 0.520 36.055 1.00 12.56 C ANISOU 924 CA ALA B 127 1588 1625 1558 -41 20 -88 C ATOM 925 C ALA B 127 11.722 1.646 36.963 1.00 15.40 C ANISOU 925 C ALA B 127 1922 1998 1930 -62 60 -108 C ATOM 926 O ALA B 127 10.945 1.394 37.906 1.00 16.22 O ANISOU 926 O ALA B 127 2050 2103 2009 -97 82 -112 O ATOM 927 CB ALA B 127 13.579 0.024 36.541 1.00 12.33 C ANISOU 927 CB ALA B 127 1594 1591 1499 -15 -21 -97 C ATOM 928 N TYR B 128 12.169 2.876 36.713 1.00 12.76 N ANISOU 928 N TYR B 128 1542 1672 1633 -44 71 -124 N ATOM 929 CA TYR B 128 11.660 3.990 37.517 1.00 11.96 C ANISOU 929 CA TYR B 128 1412 1580 1552 -61 108 -148 C ATOM 930 C TYR B 128 10.143 4.157 37.351 1.00 14.82 C ANISOU 930 C TYR B 128 1748 1942 1942 -87 139 -149 C ATOM 931 O TYR B 128 9.389 4.223 38.355 1.00 15.04 O ANISOU 931 O TYR B 128 1779 1977 1958 -121 171 -168 O ATOM 932 CB TYR B 128 12.377 5.311 37.192 1.00 10.93 C ANISOU 932 CB TYR B 128 1236 1451 1465 -38 114 -164 C ATOM 933 CG TYR B 128 11.725 6.484 37.889 1.00 11.54 C ANISOU 933 CG TYR B 128 1278 1534 1574 -54 151 -191 C ATOM 934 CD1 TYR B 128 11.979 6.752 39.228 1.00 16.11 C ANISOU 934 CD1 TYR B 128 1870 2125 2128 -68 164 -220 C ATOM 935 CD2 TYR B 128 10.812 7.291 37.222 1.00 12.36 C ANISOU 935 CD2 TYR B 128 1338 1628 1732 -54 169 -191 C ATOM 936 CE1 TYR B 128 11.366 7.816 39.876 1.00 13.96 C ANISOU 936 CE1 TYR B 128 1561 1857 1885 -84 201 -252 C ATOM 937 CE2 TYR B 128 10.195 8.352 37.861 1.00 15.23 C ANISOU 937 CE2 TYR B 128 1664 1993 2131 -65 200 -222 C ATOM 938 CZ TYR B 128 10.471 8.601 39.182 1.00 16.83 C ANISOU 938 CZ TYR B 128 1875 2209 2310 -81 219 -254 C ATOM 939 OH TYR B 128 9.838 9.651 39.799 1.00 17.25 O ANISOU 939 OH TYR B 128 1889 2265 2402 -93 252 -292 O ATOM 940 N LEU B 129 9.699 4.256 36.096 1.00 11.41 N ANISOU 940 N LEU B 129 1287 1502 1546 -73 131 -132 N ATOM 941 CA LEU B 129 8.266 4.444 35.824 1.00 13.60 C ANISOU 941 CA LEU B 129 1531 1777 1859 -91 151 -139 C ATOM 942 C LEU B 129 7.414 3.318 36.424 1.00 14.64 C ANISOU 942 C LEU B 129 1691 1912 1958 -130 166 -142 C ATOM 943 O LEU B 129 6.419 3.576 37.123 1.00 15.37 O ANISOU 943 O LEU B 129 1763 2012 2065 -162 203 -169 O ATOM 944 CB LEU B 129 8.007 4.569 34.313 1.00 9.49 C ANISOU 944 CB LEU B 129 987 1246 1373 -66 126 -118 C ATOM 945 CG LEU B 129 8.557 5.855 33.676 1.00 13.36 C ANISOU 945 CG LEU B 129 1448 1727 1900 -37 120 -115 C ATOM 946 CD1 LEU B 129 8.369 5.853 32.173 1.00 13.35 C ANISOU 946 CD1 LEU B 129 1442 1715 1916 -16 92 -89 C ATOM 947 CD2 LEU B 129 7.886 7.087 34.289 1.00 12.45 C ANISOU 947 CD2 LEU B 129 1289 1608 1833 -43 147 -146 C ATOM 948 N HIS B 130 7.794 2.069 36.167 1.00 12.43 N ANISOU 948 N HIS B 130 1460 1625 1638 -130 140 -117 N ATOM 949 CA HIS B 130 7.030 0.949 36.727 1.00 12.97 C ANISOU 949 CA HIS B 130 1565 1689 1672 -172 154 -115 C ATOM 950 C HIS B 130 7.078 0.957 38.255 1.00 14.23 C ANISOU 950 C HIS B 130 1762 1857 1789 -208 185 -131 C ATOM 951 O HIS B 130 6.114 0.573 38.926 1.00 15.65 O ANISOU 951 O HIS B 130 1953 2039 1955 -256 223 -145 O ATOM 952 CB HIS B 130 7.547 -0.381 36.190 1.00 13.39 C ANISOU 952 CB HIS B 130 1669 1726 1691 -163 115 -85 C ATOM 953 CG HIS B 130 7.151 -0.636 34.771 1.00 9.38 C ANISOU 953 CG HIS B 130 1133 1213 1217 -144 94 -74 C ATOM 954 CD2 HIS B 130 6.559 0.177 33.864 1.00 10.99 C ANISOU 954 CD2 HIS B 130 1280 1423 1472 -128 95 -81 C ATOM 955 ND1 HIS B 130 7.314 -1.853 34.166 1.00 10.61 N ANISOU 955 ND1 HIS B 130 1325 1356 1353 -140 64 -55 N ATOM 956 CE1 HIS B 130 6.874 -1.775 32.913 1.00 9.17 C ANISOU 956 CE1 HIS B 130 1105 1174 1203 -123 49 -51 C ATOM 957 NE2 HIS B 130 6.398 -0.564 32.717 1.00 11.35 N ANISOU 957 NE2 HIS B 130 1330 1462 1522 -116 66 -65 N ATOM 958 N GLY B 131 8.196 1.403 38.800 1.00 12.72 N ANISOU 958 N GLY B 131 1588 1670 1576 -186 170 -133 N ATOM 959 CA GLY B 131 8.322 1.515 40.245 1.00 17.53 C ANISOU 959 CA GLY B 131 2235 2288 2139 -215 193 -151 C ATOM 960 C GLY B 131 7.391 2.579 40.810 1.00 18.35 C ANISOU 960 C GLY B 131 2287 2410 2277 -243 248 -191 C ATOM 961 O GLY B 131 7.045 2.523 41.994 1.00 19.17 O ANISOU 961 O GLY B 131 2420 2525 2340 -286 284 -210 O ATOM 962 N LYS B 132 6.995 3.549 39.983 1.00 14.30 N ANISOU 962 N LYS B 132 1700 1899 1836 -219 254 -205 N ATOM 963 CA LYS B 132 5.966 4.526 40.399 1.00 18.63 C ANISOU 963 CA LYS B 132 2189 2459 2430 -241 302 -249 C ATOM 964 C LYS B 132 4.551 4.117 39.997 1.00 20.24 C ANISOU 964 C LYS B 132 2361 2663 2667 -270 327 -263 C ATOM 965 O LYS B 132 3.616 4.920 40.080 1.00 18.48 O ANISOU 965 O LYS B 132 2075 2448 2500 -280 359 -305 O ATOM 966 CB LYS B 132 6.244 5.910 39.809 1.00 15.11 C ANISOU 966 CB LYS B 132 1680 2009 2051 -199 292 -263 C ATOM 967 CG LYS B 132 7.544 6.535 40.286 1.00 19.27 C ANISOU 967 CG LYS B 132 2223 2540 2560 -176 277 -265 C ATOM 968 CD LYS B 132 7.467 6.818 41.775 1.00 26.21 C ANISOU 968 CD LYS B 132 3118 3438 3405 -210 315 -303 C ATOM 969 CE LYS B 132 8.809 7.285 42.316 1.00 23.42 C ANISOU 969 CE LYS B 132 2785 3089 3027 -187 294 -308 C ATOM 970 NZ LYS B 132 8.693 7.791 43.729 1.00 34.81 N1+ ANISOU 970 NZ LYS B 132 4234 4551 4441 -218 331 -352 N1+ ATOM 971 N GLY B 133 4.402 2.882 39.531 1.00 16.96 N ANISOU 971 N GLY B 133 1984 2237 2223 -282 309 -232 N ATOM 972 CA GLY B 133 3.115 2.381 39.081 1.00 18.13 C ANISOU 972 CA GLY B 133 2102 2384 2404 -310 328 -246 C ATOM 973 C GLY B 133 2.616 3.025 37.801 1.00 21.54 C ANISOU 973 C GLY B 133 2463 2809 2913 -269 301 -252 C ATOM 974 O GLY B 133 1.405 3.054 37.527 1.00 19.78 O ANISOU 974 O GLY B 133 2189 2588 2739 -287 319 -283 O ATOM 975 N VAL B 134 3.542 3.543 37.001 1.00 16.69 N ANISOU 975 N VAL B 134 1846 2185 2309 -217 257 -223 N ATOM 976 CA VAL B 134 3.165 4.122 35.719 1.00 17.35 C ANISOU 976 CA VAL B 134 1880 2257 2454 -177 224 -219 C ATOM 977 C VAL B 134 3.426 3.099 34.618 1.00 19.25 C ANISOU 977 C VAL B 134 2153 2489 2673 -162 182 -180 C ATOM 978 O VAL B 134 4.536 2.570 34.513 1.00 17.11 O ANISOU 978 O VAL B 134 1932 2214 2354 -149 161 -147 O ATOM 979 CB VAL B 134 3.954 5.433 35.433 1.00 17.62 C ANISOU 979 CB VAL B 134 1894 2284 2516 -135 207 -214 C ATOM 980 CG1 VAL B 134 3.731 5.906 33.999 1.00 18.36 C ANISOU 980 CG1 VAL B 134 1959 2361 2656 -95 164 -195 C ATOM 981 CG2 VAL B 134 3.538 6.550 36.410 1.00 16.76 C ANISOU 981 CG2 VAL B 134 1742 2182 2444 -147 245 -261 C ATOM 982 N ILE B 135 2.407 2.801 33.815 1.00 13.07 N ANISOU 982 N ILE B 135 1337 1701 1926 -162 169 -188 N ATOM 983 CA ILE B 135 2.619 2.036 32.583 1.00 12.05 C ANISOU 983 CA ILE B 135 1230 1564 1785 -140 124 -155 C ATOM 984 C ILE B 135 2.755 3.018 31.426 1.00 14.36 C ANISOU 984 C ILE B 135 1493 1847 2115 -92 85 -142 C ATOM 985 O ILE B 135 1.909 3.917 31.255 1.00 14.44 O ANISOU 985 O ILE B 135 1451 1853 2184 -81 82 -167 O ATOM 986 CB ILE B 135 1.473 1.048 32.333 1.00 14.76 C ANISOU 986 CB ILE B 135 1561 1908 2141 -170 127 -172 C ATOM 987 CG1 ILE B 135 1.367 0.092 33.527 1.00 17.23 C ANISOU 987 CG1 ILE B 135 1914 2224 2410 -225 171 -180 C ATOM 988 CG2 ILE B 135 1.724 0.243 31.060 1.00 13.80 C ANISOU 988 CG2 ILE B 135 1462 1777 2004 -147 80 -141 C ATOM 989 CD1 ILE B 135 0.076 -0.749 33.560 1.00 24.25 C ANISOU 989 CD1 ILE B 135 2782 3112 3318 -271 194 -210 C ATOM 990 N HIS B 136 3.827 2.887 30.648 1.00 13.53 N ANISOU 990 N HIS B 136 1425 1738 1978 -65 55 -105 N ATOM 991 CA HIS B 136 4.069 3.864 29.597 1.00 13.73 C ANISOU 991 CA HIS B 136 1437 1752 2028 -27 24 -87 C ATOM 992 C HIS B 136 2.999 3.758 28.512 1.00 14.75 C ANISOU 992 C HIS B 136 1540 1874 2189 -13 -12 -90 C ATOM 993 O HIS B 136 2.383 4.769 28.152 1.00 16.29 O ANISOU 993 O HIS B 136 1700 2057 2434 8 -30 -100 O ATOM 994 CB HIS B 136 5.467 3.721 28.987 1.00 12.20 C ANISOU 994 CB HIS B 136 1287 1559 1791 -8 9 -53 C ATOM 995 CG HIS B 136 5.847 4.870 28.110 1.00 14.00 C ANISOU 995 CG HIS B 136 1510 1773 2036 21 -9 -35 C ATOM 996 CD2 HIS B 136 6.714 5.897 28.295 1.00 13.24 C ANISOU 996 CD2 HIS B 136 1417 1670 1946 30 4 -29 C ATOM 997 ND1 HIS B 136 5.255 5.089 26.880 1.00 15.10 N ANISOU 997 ND1 HIS B 136 1645 1901 2191 40 -47 -20 N ATOM 998 CE1 HIS B 136 5.763 6.179 26.334 1.00 16.51 C ANISOU 998 CE1 HIS B 136 1831 2063 2377 59 -55 -1 C ATOM 999 NE2 HIS B 136 6.649 6.691 27.171 1.00 15.27 N ANISOU 999 NE2 HIS B 136 1676 1908 2218 52 -22 -7 N ATOM 1000 N LYS B 137 2.816 2.536 27.997 1.00 14.15 N ANISOU 1000 N LYS B 137 1485 1804 2087 -22 -28 -83 N ATOM 1001 CA LYS B 137 1.803 2.175 26.979 1.00 14.57 C ANISOU 1001 CA LYS B 137 1517 1854 2164 -13 -67 -90 C ATOM 1002 C LYS B 137 2.241 2.420 25.529 1.00 17.77 C ANISOU 1002 C LYS B 137 1947 2253 2551 23 -115 -57 C ATOM 1003 O LYS B 137 1.647 1.872 24.592 1.00 18.45 O ANISOU 1003 O LYS B 137 2032 2340 2639 31 -152 -57 O ATOM 1004 CB LYS B 137 0.437 2.847 27.239 1.00 15.89 C ANISOU 1004 CB LYS B 137 1620 2017 2402 -14 -67 -132 C ATOM 1005 CG LYS B 137 -0.146 2.603 28.627 1.00 16.93 C ANISOU 1005 CG LYS B 137 1723 2158 2550 -57 -12 -173 C ATOM 1006 CD LYS B 137 -1.342 3.545 28.905 1.00 23.69 C ANISOU 1006 CD LYS B 137 2506 3010 3485 -52 -9 -224 C ATOM 1007 CE LYS B 137 -0.892 5.004 29.058 1.00 25.10 C ANISOU 1007 CE LYS B 137 2673 3175 3688 -21 -13 -218 C ATOM 1008 NZ LYS B 137 -0.198 5.262 30.372 1.00 23.07 N1+ ANISOU 1008 NZ LYS B 137 2431 2928 3408 -47 44 -224 N1+ ATOM 1009 N ASP B 138 3.264 3.243 25.333 1.00 12.09 N ANISOU 1009 N ASP B 138 1251 1527 1814 40 -113 -30 N ATOM 1010 CA ASP B 138 3.719 3.542 23.971 1.00 14.41 C ANISOU 1010 CA ASP B 138 1577 1815 2084 66 -150 3 C ATOM 1011 C ASP B 138 5.218 3.754 23.890 1.00 15.74 C ANISOU 1011 C ASP B 138 1785 1986 2208 67 -129 28 C ATOM 1012 O ASP B 138 5.690 4.751 23.314 1.00 14.26 O ANISOU 1012 O ASP B 138 1614 1786 2019 81 -136 50 O ATOM 1013 CB ASP B 138 2.983 4.744 23.389 1.00 20.09 C ANISOU 1013 CB ASP B 138 2276 2511 2845 93 -187 7 C ATOM 1014 CG ASP B 138 2.980 4.730 21.861 1.00 21.70 C ANISOU 1014 CG ASP B 138 2516 2709 3020 115 -238 36 C ATOM 1015 OD1 ASP B 138 2.665 5.765 21.254 1.00 23.10 O ANISOU 1015 OD1 ASP B 138 2698 2863 3218 139 -273 52 O ATOM 1016 OD2 ASP B 138 3.296 3.673 21.266 1.00 24.20 O1- ANISOU 1016 OD2 ASP B 138 2861 3044 3292 107 -245 43 O1- ATOM 1017 N LEU B 139 5.963 2.808 24.464 1.00 13.57 N ANISOU 1017 N LEU B 139 1527 1726 1901 50 -104 22 N ATOM 1018 CA LEU B 139 7.415 2.850 24.402 1.00 14.16 C ANISOU 1018 CA LEU B 139 1632 1808 1941 51 -86 33 C ATOM 1019 C LEU B 139 7.813 2.508 22.968 1.00 12.92 C ANISOU 1019 C LEU B 139 1507 1657 1747 61 -110 52 C ATOM 1020 O LEU B 139 7.263 1.580 22.365 1.00 12.98 O ANISOU 1020 O LEU B 139 1521 1670 1742 61 -136 49 O ATOM 1021 CB LEU B 139 8.014 1.853 25.400 1.00 11.72 C ANISOU 1021 CB LEU B 139 1333 1509 1610 36 -66 17 C ATOM 1022 CG LEU B 139 9.545 1.876 25.464 1.00 12.65 C ANISOU 1022 CG LEU B 139 1472 1635 1701 41 -51 18 C ATOM 1023 CD1 LEU B 139 10.071 3.250 25.931 1.00 14.26 C ANISOU 1023 CD1 LEU B 139 1661 1832 1926 44 -27 17 C ATOM 1024 CD2 LEU B 139 9.985 0.783 26.420 1.00 12.83 C ANISOU 1024 CD2 LEU B 139 1509 1661 1705 33 -46 2 C ATOM 1025 N LYS B 140 8.722 3.298 22.408 1.00 10.35 N ANISOU 1025 N LYS B 140 1200 1327 1404 66 -100 68 N ATOM 1026 CA LYS B 140 9.157 3.159 21.011 1.00 12.06 C ANISOU 1026 CA LYS B 140 1452 1551 1579 69 -115 86 C ATOM 1027 C LYS B 140 10.272 4.174 20.817 1.00 13.82 C ANISOU 1027 C LYS B 140 1691 1768 1791 63 -85 97 C ATOM 1028 O LYS B 140 10.409 5.087 21.637 1.00 13.63 O ANISOU 1028 O LYS B 140 1648 1731 1799 61 -64 95 O ATOM 1029 CB LYS B 140 7.987 3.462 20.051 1.00 14.02 C ANISOU 1029 CB LYS B 140 1708 1787 1833 81 -159 104 C ATOM 1030 CG LYS B 140 7.384 4.864 20.232 1.00 15.51 C ANISOU 1030 CG LYS B 140 1883 1947 2062 92 -170 119 C ATOM 1031 CD LYS B 140 6.116 5.020 19.372 1.00 18.34 C ANISOU 1031 CD LYS B 140 2244 2292 2434 112 -227 129 C ATOM 1032 CE LYS B 140 5.450 6.373 19.603 1.00 24.30 C ANISOU 1032 CE LYS B 140 2981 3012 3239 129 -246 137 C ATOM 1033 NZ LYS B 140 4.113 6.489 18.915 1.00 22.11 N1+ ANISOU 1033 NZ LYS B 140 2694 2720 2988 154 -312 137 N1+ ATOM 1034 N PRO B 141 11.080 4.033 19.747 1.00 15.06 N ANISOU 1034 N PRO B 141 1882 1936 1903 55 -77 105 N ATOM 1035 CA PRO B 141 12.231 4.931 19.574 1.00 15.43 C ANISOU 1035 CA PRO B 141 1943 1979 1939 40 -38 109 C ATOM 1036 C PRO B 141 11.881 6.424 19.508 1.00 14.46 C ANISOU 1036 C PRO B 141 1830 1825 1840 40 -38 139 C ATOM 1037 O PRO B 141 12.707 7.233 19.942 1.00 14.10 O ANISOU 1037 O PRO B 141 1778 1770 1808 27 -2 134 O ATOM 1038 CB PRO B 141 12.846 4.449 18.251 1.00 14.81 C ANISOU 1038 CB PRO B 141 1903 1920 1804 28 -33 111 C ATOM 1039 CG PRO B 141 12.533 2.967 18.253 1.00 14.68 C ANISOU 1039 CG PRO B 141 1876 1924 1778 39 -57 88 C ATOM 1040 CD PRO B 141 11.096 2.946 18.752 1.00 16.42 C ANISOU 1040 CD PRO B 141 2078 2129 2034 55 -96 100 C ATOM 1041 N GLU B 142 10.701 6.789 19.004 1.00 16.30 N ANISOU 1041 N GLU B 142 2075 2037 2081 54 -82 165 N ATOM 1042 CA GLU B 142 10.301 8.203 18.984 1.00 18.27 C ANISOU 1042 CA GLU B 142 2334 2247 2361 60 -92 191 C ATOM 1043 C GLU B 142 10.069 8.817 20.371 1.00 14.52 C ANISOU 1043 C GLU B 142 1810 1758 1950 67 -77 170 C ATOM 1044 O GLU B 142 10.055 10.053 20.510 1.00 15.33 O ANISOU 1044 O GLU B 142 1916 1827 2082 68 -73 184 O ATOM 1045 CB GLU B 142 9.067 8.421 18.085 1.00 20.61 C ANISOU 1045 CB GLU B 142 2654 2522 2656 81 -155 219 C ATOM 1046 CG GLU B 142 9.354 8.157 16.609 1.00 23.52 C ANISOU 1046 CG GLU B 142 3086 2896 2953 71 -170 246 C ATOM 1047 CD GLU B 142 8.215 8.549 15.672 1.00 36.74 C ANISOU 1047 CD GLU B 142 4794 4544 4621 95 -240 277 C ATOM 1048 OE1 GLU B 142 7.089 8.805 16.150 1.00 39.55 O ANISOU 1048 OE1 GLU B 142 5112 4880 5034 123 -282 269 O ATOM 1049 OE2 GLU B 142 8.460 8.604 14.445 1.00 38.27 O1- ANISOU 1049 OE2 GLU B 142 5054 4736 4751 84 -254 307 O1- ATOM 1050 N ASN B 143 9.898 7.960 21.378 1.00 13.19 N ANISOU 1050 N ASN B 143 1600 1613 1798 69 -69 137 N ATOM 1051 CA ASN B 143 9.737 8.374 22.779 1.00 11.64 C ANISOU 1051 CA ASN B 143 1360 1411 1651 70 -49 111 C ATOM 1052 C ASN B 143 11.006 8.172 23.609 1.00 12.37 C ANISOU 1052 C ASN B 143 1443 1523 1734 55 -4 87 C ATOM 1053 O ASN B 143 10.981 8.258 24.845 1.00 13.55 O ANISOU 1053 O ASN B 143 1561 1676 1910 54 12 62 O ATOM 1054 CB ASN B 143 8.547 7.637 23.426 1.00 11.22 C ANISOU 1054 CB ASN B 143 1272 1368 1623 78 -69 90 C ATOM 1055 CG ASN B 143 7.220 8.327 23.168 1.00 16.81 C ANISOU 1055 CG ASN B 143 1962 2050 2376 97 -107 95 C ATOM 1056 ND2 ASN B 143 6.138 7.550 23.162 1.00 13.90 N ANISOU 1056 ND2 ASN B 143 1571 1691 2019 103 -134 79 N ATOM 1057 OD1 ASN B 143 7.166 9.553 22.986 1.00 15.79 O ANISOU 1057 OD1 ASN B 143 1838 1889 2274 107 -115 109 O ATOM 1058 N ILE B 144 12.121 7.912 22.934 1.00 11.42 N ANISOU 1058 N ILE B 144 1348 1415 1574 43 14 91 N ATOM 1059 CA ILE B 144 13.406 7.825 23.627 1.00 10.69 C ANISOU 1059 CA ILE B 144 1243 1339 1479 32 51 61 C ATOM 1060 C ILE B 144 14.271 8.937 23.049 1.00 14.91 C ANISOU 1060 C ILE B 144 1795 1859 2013 15 81 72 C ATOM 1061 O ILE B 144 14.661 8.885 21.876 1.00 15.45 O ANISOU 1061 O ILE B 144 1898 1929 2044 2 87 89 O ATOM 1062 CB ILE B 144 14.057 6.449 23.433 1.00 10.29 C ANISOU 1062 CB ILE B 144 1199 1320 1393 32 49 41 C ATOM 1063 CG1 ILE B 144 13.110 5.361 23.972 1.00 11.09 C ANISOU 1063 CG1 ILE B 144 1290 1428 1494 44 20 36 C ATOM 1064 CG2 ILE B 144 15.425 6.399 24.136 1.00 11.04 C ANISOU 1064 CG2 ILE B 144 1275 1429 1491 26 79 4 C ATOM 1065 CD1 ILE B 144 13.434 3.950 23.519 1.00 11.68 C ANISOU 1065 CD1 ILE B 144 1380 1524 1535 47 6 24 C ATOM 1066 N LEU B 145 14.532 9.964 23.860 1.00 11.67 N ANISOU 1066 N LEU B 145 1363 1430 1641 10 103 61 N ATOM 1067 CA LEU B 145 15.218 11.166 23.390 1.00 14.45 C ANISOU 1067 CA LEU B 145 1733 1757 2001 -10 133 73 C ATOM 1068 C LEU B 145 16.675 11.165 23.843 1.00 16.67 C ANISOU 1068 C LEU B 145 1992 2058 2283 -29 176 32 C ATOM 1069 O LEU B 145 17.006 10.591 24.871 1.00 14.66 O ANISOU 1069 O LEU B 145 1704 1825 2040 -18 176 -5 O ATOM 1070 CB LEU B 145 14.501 12.415 23.911 1.00 15.91 C ANISOU 1070 CB LEU B 145 1906 1902 2236 -3 125 85 C ATOM 1071 CG LEU B 145 12.995 12.480 23.614 1.00 18.72 C ANISOU 1071 CG LEU B 145 2269 2237 2606 21 76 112 C ATOM 1072 CD1 LEU B 145 12.384 13.745 24.181 1.00 19.44 C ANISOU 1072 CD1 LEU B 145 2343 2288 2757 31 70 113 C ATOM 1073 CD2 LEU B 145 12.713 12.377 22.114 1.00 22.01 C ANISOU 1073 CD2 LEU B 145 2740 2643 2981 19 51 155 C ATOM 1074 N VAL B 146 17.543 11.811 23.079 1.00 16.67 N ANISOU 1074 N VAL B 146 2014 2048 2272 -57 212 37 N ATOM 1075 CA VAL B 146 18.985 11.682 23.276 1.00 15.39 C ANISOU 1075 CA VAL B 146 1829 1910 2111 -78 255 -10 C ATOM 1076 C VAL B 146 19.632 13.065 23.402 1.00 17.28 C ANISOU 1076 C VAL B 146 2065 2120 2383 -106 297 -15 C ATOM 1077 O VAL B 146 19.340 13.964 22.605 1.00 19.78 O ANISOU 1077 O VAL B 146 2424 2400 2693 -126 306 27 O ATOM 1078 CB VAL B 146 19.609 10.949 22.067 1.00 14.40 C ANISOU 1078 CB VAL B 146 1728 1808 1934 -96 272 -12 C ATOM 1079 CG1 VAL B 146 21.088 10.666 22.306 1.00 16.96 C ANISOU 1079 CG1 VAL B 146 2016 2161 2267 -113 312 -75 C ATOM 1080 CG2 VAL B 146 18.844 9.665 21.775 1.00 13.14 C ANISOU 1080 CG2 VAL B 146 1580 1669 1743 -70 228 -1 C ATOM 1081 N ASP B 147 20.486 13.244 24.407 1.00 19.94 N ANISOU 1081 N ASP B 147 2355 2469 2754 -108 318 -67 N ATOM 1082 CA ASP B 147 21.190 14.521 24.563 1.00 25.76 C ANISOU 1082 CA ASP B 147 3082 3178 3527 -139 362 -81 C ATOM 1083 C ASP B 147 22.524 14.514 23.824 1.00 29.01 C ANISOU 1083 C ASP B 147 3493 3606 3924 -180 416 -113 C ATOM 1084 O ASP B 147 22.859 13.536 23.161 1.00 23.44 O ANISOU 1084 O ASP B 147 2794 2932 3179 -181 418 -124 O ATOM 1085 CB ASP B 147 21.320 14.969 26.037 1.00 23.17 C ANISOU 1085 CB ASP B 147 2704 2849 3250 -124 358 -122 C ATOM 1086 CG ASP B 147 22.152 14.019 26.899 1.00 26.84 C ANISOU 1086 CG ASP B 147 3124 3359 3717 -106 350 -184 C ATOM 1087 OD1 ASP B 147 21.941 14.039 28.140 1.00 29.58 O ANISOU 1087 OD1 ASP B 147 3441 3710 4087 -84 328 -208 O ATOM 1088 OD2 ASP B 147 23.026 13.286 26.368 1.00 30.28 O1- ANISOU 1088 OD2 ASP B 147 3552 3822 4131 -115 364 -212 O1- ATOM 1089 N ASN B 148 23.275 15.609 23.913 1.00 40.36 N ANISOU 1089 N ASN B 148 4920 5020 5393 -216 463 -132 N ATOM 1090 CA ASN B 148 24.551 15.691 23.204 1.00 43.76 C ANISOU 1090 CA ASN B 148 5346 5465 5814 -263 525 -169 C ATOM 1091 C ASN B 148 25.573 14.684 23.715 1.00 37.72 C ANISOU 1091 C ASN B 148 4520 4754 5060 -249 528 -248 C ATOM 1092 O ASN B 148 26.461 14.265 22.967 1.00 45.48 O ANISOU 1092 O ASN B 148 5495 5761 6023 -278 567 -282 O ATOM 1093 CB ASN B 148 25.124 17.111 23.258 1.00 50.74 C ANISOU 1093 CB ASN B 148 6232 6310 6738 -309 578 -177 C ATOM 1094 CG ASN B 148 24.612 17.993 22.127 1.00 56.04 C ANISOU 1094 CG ASN B 148 6984 6930 7379 -346 597 -104 C ATOM 1095 ND2 ASN B 148 25.091 17.740 20.911 1.00 57.78 N ANISOU 1095 ND2 ASN B 148 7246 7161 7547 -389 638 -94 N ATOM 1096 OD1 ASN B 148 23.802 18.895 22.347 1.00 62.32 O ANISOU 1096 OD1 ASN B 148 7807 7675 8198 -337 574 -59 O ATOM 1097 N ASP B 149 25.445 14.295 24.983 1.00 34.73 N ANISOU 1097 N ASP B 149 4097 4389 4711 -206 484 -278 N ATOM 1098 CA ASP B 149 26.349 13.316 25.584 1.00 31.29 C ANISOU 1098 CA ASP B 149 3606 3996 4286 -182 469 -351 C ATOM 1099 C ASP B 149 25.906 11.879 25.278 1.00 31.08 C ANISOU 1099 C ASP B 149 3596 3997 4217 -148 425 -338 C ATOM 1100 O ASP B 149 26.477 10.925 25.809 1.00 30.91 O ANISOU 1100 O ASP B 149 3538 4005 4203 -119 396 -389 O ATOM 1101 CB ASP B 149 26.441 13.516 27.106 1.00 36.34 C ANISOU 1101 CB ASP B 149 4203 4638 4969 -152 438 -388 C ATOM 1102 CG ASP B 149 27.206 14.770 27.492 1.00 44.00 C ANISOU 1102 CG ASP B 149 5139 5589 5989 -184 483 -427 C ATOM 1103 OD1 ASP B 149 27.977 15.280 26.650 1.00 48.53 O ANISOU 1103 OD1 ASP B 149 5711 6157 6570 -232 542 -444 O ATOM 1104 OD2 ASP B 149 27.037 15.240 28.641 1.00 43.88 O1- ANISOU 1104 OD2 ASP B 149 5101 5565 6006 -166 461 -443 O1- ATOM 1105 N PHE B 150 24.889 11.751 24.425 1.00 22.54 N ANISOU 1105 N PHE B 150 2570 2901 3094 -150 414 -270 N ATOM 1106 CA PHE B 150 24.246 10.467 24.093 1.00 21.98 C ANISOU 1106 CA PHE B 150 2519 2848 2983 -120 370 -249 C ATOM 1107 C PHE B 150 23.588 9.767 25.273 1.00 22.51 C ANISOU 1107 C PHE B 150 2574 2921 3059 -73 311 -248 C ATOM 1108 O PHE B 150 23.363 8.554 25.223 1.00 20.55 O ANISOU 1108 O PHE B 150 2331 2690 2786 -48 275 -251 O ATOM 1109 CB PHE B 150 25.222 9.495 23.420 1.00 21.51 C ANISOU 1109 CB PHE B 150 2443 2825 2906 -126 385 -300 C ATOM 1110 CG PHE B 150 25.638 9.911 22.045 1.00 29.61 C ANISOU 1110 CG PHE B 150 3496 3851 3903 -176 444 -292 C ATOM 1111 CD1 PHE B 150 24.936 9.467 20.930 1.00 29.60 C ANISOU 1111 CD1 PHE B 150 3549 3850 3846 -182 437 -244 C ATOM 1112 CD2 PHE B 150 26.740 10.735 21.865 1.00 34.41 C ANISOU 1112 CD2 PHE B 150 4080 4459 4536 -220 508 -335 C ATOM 1113 CE1 PHE B 150 25.324 9.843 19.647 1.00 35.65 C ANISOU 1113 CE1 PHE B 150 4351 4618 4575 -233 492 -235 C ATOM 1114 CE2 PHE B 150 27.137 11.119 20.593 1.00 37.93 C ANISOU 1114 CE2 PHE B 150 4560 4905 4947 -275 570 -328 C ATOM 1115 CZ PHE B 150 26.429 10.670 19.479 1.00 42.11 C ANISOU 1115 CZ PHE B 150 5150 5436 5414 -282 562 -276 C ATOM 1116 N HIS B 151 23.288 10.507 26.336 1.00 19.78 N ANISOU 1116 N HIS B 151 2212 2558 2744 -65 303 -247 N ATOM 1117 CA HIS B 151 22.478 9.943 27.410 1.00 17.41 C ANISOU 1117 CA HIS B 151 1911 2259 2443 -30 253 -238 C ATOM 1118 C HIS B 151 21.015 10.048 26.974 1.00 14.85 C ANISOU 1118 C HIS B 151 1627 1916 2101 -28 237 -173 C ATOM 1119 O HIS B 151 20.677 10.903 26.150 1.00 17.69 O ANISOU 1119 O HIS B 151 2009 2251 2461 -49 259 -137 O ATOM 1120 CB HIS B 151 22.730 10.689 28.719 1.00 18.18 C ANISOU 1120 CB HIS B 151 1979 2352 2579 -26 254 -269 C ATOM 1121 CG HIS B 151 24.084 10.428 29.304 1.00 19.48 C ANISOU 1121 CG HIS B 151 2100 2537 2762 -19 254 -339 C ATOM 1122 CD2 HIS B 151 25.152 11.242 29.484 1.00 21.87 C ANISOU 1122 CD2 HIS B 151 2366 2842 3103 -38 288 -389 C ATOM 1123 ND1 HIS B 151 24.455 9.195 29.795 1.00 21.18 N ANISOU 1123 ND1 HIS B 151 2310 2776 2963 13 211 -370 N ATOM 1124 CE1 HIS B 151 25.694 9.260 30.253 1.00 22.79 C ANISOU 1124 CE1 HIS B 151 2471 2993 3194 17 212 -437 C ATOM 1125 NE2 HIS B 151 26.139 10.492 30.079 1.00 21.02 N ANISOU 1125 NE2 HIS B 151 2224 2759 3004 -15 261 -452 N ATOM 1126 N ILE B 152 20.142 9.184 27.488 1.00 15.65 N ANISOU 1126 N ILE B 152 1738 2023 2187 -3 196 -158 N ATOM 1127 CA ILE B 152 18.758 9.194 26.997 1.00 14.37 C ANISOU 1127 CA ILE B 152 1604 1845 2012 0 179 -106 C ATOM 1128 C ILE B 152 17.730 9.545 28.061 1.00 15.97 C ANISOU 1128 C ILE B 152 1797 2034 2236 10 163 -97 C ATOM 1129 O ILE B 152 17.979 9.418 29.265 1.00 12.81 O ANISOU 1129 O ILE B 152 1377 1644 1846 18 158 -128 O ATOM 1130 CB ILE B 152 18.349 7.854 26.291 1.00 15.77 C ANISOU 1130 CB ILE B 152 1805 2037 2150 11 151 -90 C ATOM 1131 CG1 ILE B 152 18.314 6.680 27.279 1.00 15.08 C ANISOU 1131 CG1 ILE B 152 1711 1966 2054 32 119 -113 C ATOM 1132 CG2 ILE B 152 19.272 7.588 25.115 1.00 16.23 C ANISOU 1132 CG2 ILE B 152 1873 2109 2186 -3 171 -101 C ATOM 1133 CD1 ILE B 152 16.900 6.418 27.898 1.00 14.14 C ANISOU 1133 CD1 ILE B 152 1601 1837 1934 39 95 -87 C ATOM 1134 N LYS B 153 16.557 9.963 27.603 1.00 13.32 N ANISOU 1134 N LYS B 153 1476 1678 1907 11 153 -59 N ATOM 1135 CA LYS B 153 15.440 10.209 28.515 1.00 14.74 C ANISOU 1135 CA LYS B 153 1642 1849 2111 20 140 -58 C ATOM 1136 C LYS B 153 14.169 9.736 27.838 1.00 13.38 C ANISOU 1136 C LYS B 153 1486 1670 1929 28 113 -25 C ATOM 1137 O LYS B 153 13.933 10.014 26.661 1.00 15.69 O ANISOU 1137 O LYS B 153 1800 1947 2214 27 105 6 O ATOM 1138 CB LYS B 153 15.346 11.701 28.848 1.00 16.30 C ANISOU 1138 CB LYS B 153 1822 2017 2354 13 160 -61 C ATOM 1139 CG LYS B 153 16.503 12.193 29.743 1.00 15.53 C ANISOU 1139 CG LYS B 153 1700 1927 2273 5 186 -103 C ATOM 1140 CD LYS B 153 16.369 13.686 30.036 1.00 23.30 C ANISOU 1140 CD LYS B 153 2667 2878 3306 -2 205 -108 C ATOM 1141 CE LYS B 153 17.622 14.254 30.688 1.00 27.63 C ANISOU 1141 CE LYS B 153 3193 3432 3874 -14 233 -151 C ATOM 1142 NZ LYS B 153 17.709 13.957 32.149 1.00 25.69 N1+ ANISOU 1142 NZ LYS B 153 2921 3210 3628 -5 227 -193 N1+ ATOM 1143 N ILE B 154 13.367 8.981 28.572 1.00 13.10 N ANISOU 1143 N ILE B 154 1442 1646 1889 33 97 -33 N ATOM 1144 CA ILE B 154 12.098 8.499 28.030 1.00 12.22 C ANISOU 1144 CA ILE B 154 1337 1530 1776 39 72 -12 C ATOM 1145 C ILE B 154 11.061 9.606 28.141 1.00 12.50 C ANISOU 1145 C ILE B 154 1351 1539 1859 44 68 -8 C ATOM 1146 O ILE B 154 11.029 10.332 29.137 1.00 13.82 O ANISOU 1146 O ILE B 154 1493 1701 2057 41 87 -32 O ATOM 1147 CB ILE B 154 11.634 7.271 28.802 1.00 10.09 C ANISOU 1147 CB ILE B 154 1067 1279 1486 36 63 -26 C ATOM 1148 CG1 ILE B 154 12.702 6.175 28.722 1.00 13.01 C ANISOU 1148 CG1 ILE B 154 1460 1669 1816 37 58 -33 C ATOM 1149 CG2 ILE B 154 10.328 6.756 28.261 1.00 10.73 C ANISOU 1149 CG2 ILE B 154 1148 1357 1572 38 39 -12 C ATOM 1150 CD1 ILE B 154 12.506 5.061 29.736 1.00 12.85 C ANISOU 1150 CD1 ILE B 154 1449 1660 1774 32 50 -47 C ATOM 1151 N ALA B 155 10.219 9.738 27.116 1.00 11.45 N ANISOU 1151 N ALA B 155 1227 1389 1733 54 40 18 N ATOM 1152 CA ALA B 155 9.173 10.759 27.096 1.00 11.68 C ANISOU 1152 CA ALA B 155 1235 1388 1814 66 24 20 C ATOM 1153 C ALA B 155 7.832 10.133 26.773 1.00 14.98 C ANISOU 1153 C ALA B 155 1641 1809 2242 77 -9 19 C ATOM 1154 O ALA B 155 7.765 9.025 26.256 1.00 11.43 O ANISOU 1154 O ALA B 155 1209 1378 1755 74 -23 29 O ATOM 1155 CB ALA B 155 9.509 11.832 26.056 1.00 16.52 C ANISOU 1155 CB ALA B 155 1876 1966 2434 73 14 53 C ATOM 1156 N ASP B 156 6.763 10.870 27.064 1.00 12.16 N ANISOU 1156 N ASP B 156 1249 1431 1941 89 -23 2 N ATOM 1157 CA ASP B 156 5.420 10.495 26.631 1.00 13.76 C ANISOU 1157 CA ASP B 156 1431 1630 2168 102 -60 -5 C ATOM 1158 C ASP B 156 4.940 11.528 25.608 1.00 17.33 C ANISOU 1158 C ASP B 156 1893 2040 2651 131 -108 20 C ATOM 1159 O ASP B 156 4.011 12.292 25.869 1.00 17.87 O ANISOU 1159 O ASP B 156 1923 2083 2783 149 -127 -4 O ATOM 1160 CB ASP B 156 4.491 10.462 27.849 1.00 13.38 C ANISOU 1160 CB ASP B 156 1327 1592 2164 93 -39 -55 C ATOM 1161 CG ASP B 156 3.053 10.146 27.488 1.00 19.02 C ANISOU 1161 CG ASP B 156 2007 2304 2917 104 -74 -76 C ATOM 1162 OD1 ASP B 156 2.813 9.450 26.468 1.00 18.70 O ANISOU 1162 OD1 ASP B 156 1989 2267 2851 113 -110 -53 O ATOM 1163 OD2 ASP B 156 2.159 10.604 28.230 1.00 17.95 O1- ANISOU 1163 OD2 ASP B 156 1818 2164 2840 104 -65 -121 O1- ATOM 1164 N LEU B 157 5.572 11.556 24.437 1.00 11.01 N ANISOU 1164 N LEU B 157 1148 1229 1807 134 -127 65 N ATOM 1165 CA LEU B 157 5.304 12.626 23.480 1.00 15.85 C ANISOU 1165 CA LEU B 157 1788 1795 2438 157 -171 97 C ATOM 1166 C LEU B 157 3.895 12.550 22.905 1.00 19.68 C ANISOU 1166 C LEU B 157 2255 2265 2958 188 -236 90 C ATOM 1167 O LEU B 157 3.378 13.547 22.390 1.00 20.30 O ANISOU 1167 O LEU B 157 2343 2297 3073 215 -283 104 O ATOM 1168 CB LEU B 157 6.325 12.619 22.342 1.00 15.30 C ANISOU 1168 CB LEU B 157 1790 1721 2302 146 -171 147 C ATOM 1169 CG LEU B 157 7.783 12.834 22.743 1.00 16.98 C ANISOU 1169 CG LEU B 157 2020 1944 2487 117 -110 149 C ATOM 1170 CD1 LEU B 157 8.652 12.867 21.507 1.00 18.72 C ANISOU 1170 CD1 LEU B 157 2307 2159 2645 102 -108 192 C ATOM 1171 CD2 LEU B 157 7.941 14.134 23.543 1.00 18.84 C ANISOU 1171 CD2 LEU B 157 2233 2146 2779 118 -90 136 C ATOM 1172 N GLY B 158 3.266 11.378 22.999 1.00 15.45 N ANISOU 1172 N GLY B 158 1692 1764 2413 183 -242 66 N ATOM 1173 CA GLY B 158 1.925 11.211 22.472 1.00 21.35 C ANISOU 1173 CA GLY B 158 2413 2502 3197 210 -303 49 C ATOM 1174 C GLY B 158 0.881 11.559 23.507 1.00 19.71 C ANISOU 1174 C GLY B 158 2126 2289 3072 218 -297 -10 C ATOM 1175 O GLY B 158 -0.318 11.426 23.254 1.00 18.64 O ANISOU 1175 O GLY B 158 1950 2148 2983 239 -343 -40 O ATOM 1176 N LEU B 159 1.353 12.000 24.672 1.00 18.84 N ANISOU 1176 N LEU B 159 1993 2184 2982 199 -240 -32 N ATOM 1177 CA LEU B 159 0.521 12.315 25.830 1.00 21.02 C ANISOU 1177 CA LEU B 159 2195 2463 3329 196 -217 -95 C ATOM 1178 C LEU B 159 -0.431 11.173 26.180 1.00 21.71 C ANISOU 1178 C LEU B 159 2236 2586 3425 179 -207 -140 C ATOM 1179 O LEU B 159 -1.565 11.404 26.609 1.00 16.70 O ANISOU 1179 O LEU B 159 1535 1948 2861 186 -215 -196 O ATOM 1180 CB LEU B 159 -0.243 13.636 25.639 1.00 21.35 C ANISOU 1180 CB LEU B 159 2206 2455 3452 237 -265 -113 C ATOM 1181 CG LEU B 159 0.564 14.903 25.326 1.00 23.90 C ANISOU 1181 CG LEU B 159 2573 2730 3777 253 -276 -72 C ATOM 1182 CD1 LEU B 159 -0.351 16.117 25.418 1.00 25.22 C ANISOU 1182 CD1 LEU B 159 2696 2846 4040 292 -322 -105 C ATOM 1183 CD2 LEU B 159 1.774 15.072 26.245 1.00 19.30 C ANISOU 1183 CD2 LEU B 159 2004 2165 3164 219 -203 -69 C ATOM 1184 N ALA B 160 0.040 9.936 26.021 1.00 19.51 N ANISOU 1184 N ALA B 160 1993 2342 3080 153 -188 -119 N ATOM 1185 CA ALA B 160 -0.764 8.765 26.402 1.00 21.71 C ANISOU 1185 CA ALA B 160 2236 2650 3361 127 -172 -158 C ATOM 1186 C ALA B 160 -1.087 8.721 27.901 1.00 21.71 C ANISOU 1186 C ALA B 160 2190 2671 3390 92 -107 -212 C ATOM 1187 O ALA B 160 -2.075 8.100 28.310 1.00 22.60 O ANISOU 1187 O ALA B 160 2257 2801 3531 70 -91 -259 O ATOM 1188 CB ALA B 160 -0.070 7.485 25.977 1.00 21.01 C ANISOU 1188 CB ALA B 160 2200 2587 3195 106 -163 -123 C ATOM 1189 N SER B 161 -0.256 9.364 28.716 1.00 17.19 N ANISOU 1189 N SER B 161 1629 2097 2806 83 -66 -207 N ATOM 1190 CA SER B 161 -0.510 9.426 30.158 1.00 16.74 C ANISOU 1190 CA SER B 161 1534 2058 2767 49 -4 -259 C ATOM 1191 C SER B 161 -1.125 10.746 30.639 1.00 19.40 C ANISOU 1191 C SER B 161 1812 2374 3186 68 -3 -306 C ATOM 1192 O SER B 161 -1.509 10.847 31.801 1.00 23.17 O ANISOU 1192 O SER B 161 2250 2869 3686 39 49 -360 O ATOM 1193 CB SER B 161 0.773 9.140 30.946 1.00 17.67 C ANISOU 1193 CB SER B 161 1702 2195 2819 22 42 -234 C ATOM 1194 OG SER B 161 1.228 7.823 30.700 1.00 20.68 O ANISOU 1194 OG SER B 161 2129 2595 3132 3 44 -204 O ATOM 1195 N PHE B 162 -1.192 11.756 29.770 1.00 21.93 N ANISOU 1195 N PHE B 162 2130 2654 3548 114 -59 -288 N ATOM 1196 CA PHE B 162 -1.784 13.044 30.140 1.00 21.88 C ANISOU 1196 CA PHE B 162 2068 2619 3628 139 -69 -334 C ATOM 1197 C PHE B 162 -3.234 13.076 29.654 1.00 24.81 C ANISOU 1197 C PHE B 162 2375 2977 4074 165 -117 -381 C ATOM 1198 O PHE B 162 -3.554 13.741 28.659 1.00 27.32 O ANISOU 1198 O PHE B 162 2696 3254 4432 213 -191 -363 O ATOM 1199 CB PHE B 162 -1.024 14.209 29.497 1.00 20.59 C ANISOU 1199 CB PHE B 162 1945 2409 3472 176 -107 -287 C ATOM 1200 CG PHE B 162 0.368 14.445 30.042 1.00 23.01 C ANISOU 1200 CG PHE B 162 2297 2722 3725 154 -60 -256 C ATOM 1201 CD1 PHE B 162 0.678 15.644 30.673 1.00 21.76 C ANISOU 1201 CD1 PHE B 162 2121 2538 3608 161 -42 -277 C ATOM 1202 CD2 PHE B 162 1.384 13.511 29.852 1.00 22.42 C ANISOU 1202 CD2 PHE B 162 2281 2675 3562 130 -40 -209 C ATOM 1203 CE1 PHE B 162 1.962 15.904 31.145 1.00 21.47 C ANISOU 1203 CE1 PHE B 162 2122 2507 3528 142 -3 -254 C ATOM 1204 CE2 PHE B 162 2.679 13.763 30.317 1.00 19.48 C ANISOU 1204 CE2 PHE B 162 1945 2308 3149 114 -3 -188 C ATOM 1205 CZ PHE B 162 2.964 14.960 30.966 1.00 20.71 C ANISOU 1205 CZ PHE B 162 2081 2441 3348 119 16 -211 C ATOM 1206 N LYS B 163 -4.101 12.346 30.348 1.00 22.88 N ANISOU 1206 N LYS B 163 2086 2767 3842 129 -77 -440 N ATOM 1207 CA LYS B 163 -5.481 12.154 29.895 1.00 24.93 C ANISOU 1207 CA LYS B 163 2308 3020 4145 140 -115 -483 C ATOM 1208 C LYS B 163 -6.234 13.468 29.706 1.00 27.02 C ANISOU 1208 C LYS B 163 2548 3239 4480 180 -162 -517 C ATOM 1209 O LYS B 163 -6.893 13.669 28.682 1.00 26.14 O ANISOU 1209 O LYS B 163 2431 3099 4403 221 -238 -514 O ATOM 1210 CB LYS B 163 -6.224 11.198 30.843 1.00 30.65 C ANISOU 1210 CB LYS B 163 3006 3784 4855 82 -47 -540 C ATOM 1211 CG LYS B 163 -7.629 11.620 31.243 1.00 33.65 C ANISOU 1211 CG LYS B 163 3335 4154 5295 79 -43 -620 C ATOM 1212 CD LYS B 163 -8.332 10.481 31.968 1.00 37.75 C ANISOU 1212 CD LYS B 163 3837 4712 5793 20 21 -667 C ATOM 1213 CE LYS B 163 -8.797 10.878 33.367 1.00 40.01 C ANISOU 1213 CE LYS B 163 4105 5010 6088 -19 92 -733 C ATOM 1214 NZ LYS B 163 -7.696 11.167 34.336 1.00 41.34 N1+ ANISOU 1214 NZ LYS B 163 4311 5192 6204 -43 145 -707 N1+ ATOM 1215 N MET B 164 -6.111 14.372 30.671 1.00 25.51 N ANISOU 1215 N MET B 164 2346 3039 4309 170 -123 -548 N ATOM 1216 CA MET B 164 -6.807 15.649 30.585 1.00 27.70 C ANISOU 1216 CA MET B 164 2597 3270 4658 205 -166 -586 C ATOM 1217 C MET B 164 -6.267 16.571 29.488 1.00 28.73 C ANISOU 1217 C MET B 164 2763 3347 4806 261 -245 -525 C ATOM 1218 O MET B 164 -7.037 17.279 28.833 1.00 29.15 O ANISOU 1218 O MET B 164 2805 3358 4913 301 -315 -540 O ATOM 1219 CB MET B 164 -6.784 16.357 31.943 1.00 29.75 C ANISOU 1219 CB MET B 164 2837 3535 4933 176 -102 -638 C ATOM 1220 CG MET B 164 -8.166 16.732 32.438 1.00 39.88 C ANISOU 1220 CG MET B 164 4064 4810 6280 171 -99 -728 C ATOM 1221 SD MET B 164 -9.317 15.347 32.357 1.00 40.80 S ANISOU 1221 SD MET B 164 4148 4964 6390 141 -82 -773 S ATOM 1222 CE MET B 164 -9.008 14.604 33.951 1.00 37.45 C ANISOU 1222 CE MET B 164 3733 4594 5901 65 36 -802 C ATOM 1223 N TRP B 165 -4.951 16.581 29.280 1.00 29.70 N ANISOU 1223 N TRP B 165 2933 3467 4883 264 -235 -457 N ATOM 1224 CA TRP B 165 -4.403 17.413 28.210 1.00 25.69 C ANISOU 1224 CA TRP B 165 2473 2905 4384 312 -306 -393 C ATOM 1225 C TRP B 165 -4.797 16.865 26.825 1.00 28.92 C ANISOU 1225 C TRP B 165 2910 3303 4776 344 -386 -353 C ATOM 1226 O TRP B 165 -5.112 17.639 25.909 1.00 28.19 O ANISOU 1226 O TRP B 165 2846 3159 4707 386 -464 -329 O ATOM 1227 CB TRP B 165 -2.876 17.627 28.364 1.00 20.84 C ANISOU 1227 CB TRP B 165 1904 2286 3730 305 -271 -335 C ATOM 1228 CG TRP B 165 -2.520 18.634 29.445 1.00 20.51 C ANISOU 1228 CG TRP B 165 1845 2232 3716 290 -222 -369 C ATOM 1229 CD1 TRP B 165 -2.495 18.421 30.789 1.00 22.12 C ANISOU 1229 CD1 TRP B 165 2018 2479 3908 245 -143 -422 C ATOM 1230 CD2 TRP B 165 -2.142 20.013 29.248 1.00 20.57 C ANISOU 1230 CD2 TRP B 165 1875 2178 3763 318 -252 -350 C ATOM 1231 CE2 TRP B 165 -1.904 20.569 30.520 1.00 21.82 C ANISOU 1231 CE2 TRP B 165 2004 2349 3937 289 -188 -399 C ATOM 1232 CE3 TRP B 165 -1.987 20.823 28.119 1.00 23.43 C ANISOU 1232 CE3 TRP B 165 2286 2473 4142 362 -327 -295 C ATOM 1233 NE1 TRP B 165 -2.126 19.586 31.449 1.00 21.04 N ANISOU 1233 NE1 TRP B 165 1878 2315 3802 245 -123 -441 N ATOM 1234 CZ2 TRP B 165 -1.520 21.902 30.690 1.00 24.10 C ANISOU 1234 CZ2 TRP B 165 2302 2586 4267 304 -197 -399 C ATOM 1235 CZ3 TRP B 165 -1.604 22.143 28.289 1.00 21.13 C ANISOU 1235 CZ3 TRP B 165 2010 2127 3889 374 -334 -290 C ATOM 1236 CH2 TRP B 165 -1.380 22.667 29.564 1.00 20.75 C ANISOU 1236 CH2 TRP B 165 1922 2094 3866 346 -269 -344 C ATOM 1237 N SER B 166 -4.832 15.539 26.686 1.00 28.05 N ANISOU 1237 N SER B 166 2796 3239 4623 321 -367 -349 N ATOM 1238 CA SER B 166 -5.291 14.907 25.443 1.00 30.84 C ANISOU 1238 CA SER B 166 3172 3589 4957 345 -439 -321 C ATOM 1239 C SER B 166 -6.760 15.236 25.186 1.00 33.21 C ANISOU 1239 C SER B 166 3430 3871 5316 366 -490 -381 C ATOM 1240 O SER B 166 -7.169 15.567 24.055 1.00 34.85 O ANISOU 1240 O SER B 166 3669 4043 5528 407 -577 -356 O ATOM 1241 CB SER B 166 -5.147 13.381 25.523 1.00 29.73 C ANISOU 1241 CB SER B 166 3022 3505 4768 309 -401 -320 C ATOM 1242 OG SER B 166 -3.828 12.990 25.847 1.00 33.57 O ANISOU 1242 OG SER B 166 3570 4015 5170 272 -339 -268 O ATOM 1243 N LYS B 167 -7.550 15.118 26.251 1.00 26.49 N ANISOU 1243 N LYS B 167 2514 3044 4506 335 -435 -461 N ATOM 1244 CA LYS B 167 -8.977 15.401 26.182 1.00 31.93 C ANISOU 1244 CA LYS B 167 3154 3718 5261 350 -472 -533 C ATOM 1245 C LYS B 167 -9.161 16.833 25.715 1.00 36.28 C ANISOU 1245 C LYS B 167 3720 4206 5860 398 -543 -525 C ATOM 1246 O LYS B 167 -9.969 17.109 24.823 1.00 35.51 O ANISOU 1246 O LYS B 167 3624 4077 5792 436 -626 -534 O ATOM 1247 CB LYS B 167 -9.623 15.215 27.554 1.00 33.18 C ANISOU 1247 CB LYS B 167 3249 3907 5451 304 -388 -619 C ATOM 1248 CG LYS B 167 -11.154 15.261 27.541 1.00 41.55 C ANISOU 1248 CG LYS B 167 4249 4957 6579 311 -415 -705 C ATOM 1249 CD LYS B 167 -11.714 15.072 28.952 1.00 44.72 C ANISOU 1249 CD LYS B 167 4599 5390 7002 260 -323 -788 C ATOM 1250 CE LYS B 167 -13.220 14.831 28.945 1.00 51.76 C ANISOU 1250 CE LYS B 167 5430 6281 7956 258 -336 -879 C ATOM 1251 NZ LYS B 167 -13.990 16.029 28.500 1.00 57.71 N1+ ANISOU 1251 NZ LYS B 167 6156 6980 8790 309 -416 -919 N1+ ATOM 1252 N LEU B 168 -8.387 17.740 26.308 1.00 35.10 N ANISOU 1252 N LEU B 168 3585 4036 5716 396 -513 -508 N ATOM 1253 CA LEU B 168 -8.417 19.143 25.914 1.00 34.18 C ANISOU 1253 CA LEU B 168 3490 3856 5642 438 -576 -494 C ATOM 1254 C LEU B 168 -8.100 19.290 24.433 1.00 37.67 C ANISOU 1254 C LEU B 168 4007 4259 6045 480 -666 -413 C ATOM 1255 O LEU B 168 -8.744 20.075 23.732 1.00 37.33 O ANISOU 1255 O LEU B 168 3977 4168 6038 520 -748 -415 O ATOM 1256 CB LEU B 168 -7.435 19.969 26.744 1.00 33.35 C ANISOU 1256 CB LEU B 168 3396 3738 5538 424 -522 -480 C ATOM 1257 CG LEU B 168 -7.250 21.401 26.249 1.00 35.86 C ANISOU 1257 CG LEU B 168 3750 3985 5891 464 -586 -449 C ATOM 1258 CD1 LEU B 168 -8.500 22.219 26.527 1.00 33.88 C ANISOU 1258 CD1 LEU B 168 3442 3705 5726 483 -624 -530 C ATOM 1259 CD2 LEU B 168 -6.026 22.040 26.890 1.00 28.13 C ANISOU 1259 CD2 LEU B 168 2797 2994 4899 448 -531 -418 C ATOM 1260 N ASN B 169 -7.121 18.532 23.942 1.00 32.77 N ANISOU 1260 N ASN B 169 3442 3661 5350 470 -652 -341 N ATOM 1261 CA ASN B 169 -6.853 18.569 22.505 1.00 36.14 C ANISOU 1261 CA ASN B 169 3950 4056 5726 502 -733 -264 C ATOM 1262 C ASN B 169 -8.086 18.146 21.717 1.00 41.34 C ANISOU 1262 C ASN B 169 4592 4716 6400 525 -804 -297 C ATOM 1263 O ASN B 169 -8.329 18.619 20.600 1.00 41.13 O ANISOU 1263 O ASN B 169 4621 4647 6358 562 -890 -260 O ATOM 1264 CB ASN B 169 -5.678 17.661 22.137 1.00 33.27 C ANISOU 1264 CB ASN B 169 3643 3721 5277 482 -703 -193 C ATOM 1265 CG ASN B 169 -5.343 17.710 20.653 1.00 43.32 C ANISOU 1265 CG ASN B 169 5012 4962 6485 508 -780 -112 C ATOM 1266 ND2 ASN B 169 -4.569 18.715 20.252 1.00 39.52 N ANISOU 1266 ND2 ASN B 169 4605 4428 5983 520 -799 -50 N ATOM 1267 OD1 ASN B 169 -5.782 16.859 19.877 1.00 46.48 O ANISOU 1267 OD1 ASN B 169 5424 5386 6849 513 -818 -107 O ATOM 1268 N ASN B 170 -8.864 17.249 22.311 1.00 43.41 N ANISOU 1268 N ASN B 170 4780 5025 6688 500 -765 -369 N ATOM 1269 CA ASN B 170 -10.031 16.702 21.622 1.00 48.60 C ANISOU 1269 CA ASN B 170 5413 5689 7363 517 -824 -408 C ATOM 1270 C ASN B 170 -11.244 17.638 21.495 1.00 53.48 C ANISOU 1270 C ASN B 170 5994 6262 8062 552 -889 -471 C ATOM 1271 O ASN B 170 -12.067 17.450 20.590 1.00 55.81 O ANISOU 1271 O ASN B 170 6294 6545 8366 581 -965 -484 O ATOM 1272 CB ASN B 170 -10.457 15.380 22.269 1.00 52.32 C ANISOU 1272 CB ASN B 170 5823 6222 7835 474 -756 -464 C ATOM 1273 CG ASN B 170 -11.097 14.431 21.278 1.00 56.40 C ANISOU 1273 CG ASN B 170 6346 6755 8330 485 -810 -467 C ATOM 1274 ND2 ASN B 170 -11.934 13.530 21.776 1.00 57.28 N ANISOU 1274 ND2 ASN B 170 6390 6904 8471 455 -770 -539 N ATOM 1275 OD1 ASN B 170 -10.840 14.506 20.074 1.00 59.44 O ANISOU 1275 OD1 ASN B 170 6799 7118 8668 516 -883 -406 O ATOM 1276 N GLU B 171 -11.355 18.629 22.387 1.00 45.93 N ANISOU 1276 N GLU B 171 5001 5283 7168 551 -863 -512 N ATOM 1277 CA GLU B 171 -12.539 19.501 22.442 1.00 49.01 C ANISOU 1277 CA GLU B 171 5343 5633 7646 581 -918 -586 C ATOM 1278 C GLU B 171 -12.940 20.053 21.064 1.00 51.76 C ANISOU 1278 C GLU B 171 5748 5928 7992 636 -1040 -550 C ATOM 1279 O GLU B 171 -12.080 20.396 20.247 1.00 54.80 O ANISOU 1279 O GLU B 171 6222 6285 8313 653 -1078 -457 O ATOM 1280 CB GLU B 171 -12.342 20.652 23.442 1.00 51.88 C ANISOU 1280 CB GLU B 171 5679 5970 8063 576 -882 -616 C ATOM 1281 CG GLU B 171 -11.627 20.276 24.748 1.00 47.36 C ANISOU 1281 CG GLU B 171 5078 5445 7473 522 -763 -629 C ATOM 1282 CD GLU B 171 -12.533 19.652 25.802 1.00 54.02 C ANISOU 1282 CD GLU B 171 5836 6331 8358 482 -694 -731 C ATOM 1283 OE1 GLU B 171 -13.756 19.576 25.559 1.00 59.18 O ANISOU 1283 OE1 GLU B 171 6443 6975 9067 498 -737 -800 O ATOM 1284 OE2 GLU B 171 -12.021 19.242 26.880 1.00 46.73 O1- ANISOU 1284 OE2 GLU B 171 4895 5450 7410 434 -596 -744 O1- ATOM 1285 N GLU B 172 -14.245 20.121 20.814 1.00 54.45 N ANISOU 1285 N GLU B 172 6038 6253 8397 660 -1099 -625 N ATOM 1286 CA GLU B 172 -14.773 20.464 19.488 1.00 58.63 C ANISOU 1286 CA GLU B 172 6616 6737 8922 711 -1218 -601 C ATOM 1287 C GLU B 172 -14.278 21.806 18.940 1.00 55.12 C ANISOU 1287 C GLU B 172 6248 6224 8469 748 -1285 -536 C ATOM 1288 O GLU B 172 -13.924 21.915 17.764 1.00 53.11 O ANISOU 1288 O GLU B 172 6086 5944 8151 773 -1354 -457 O ATOM 1289 CB GLU B 172 -16.306 20.444 19.500 1.00 59.79 C ANISOU 1289 CB GLU B 172 6684 6875 9160 732 -1267 -710 C ATOM 1290 N HIS B 173 -14.254 22.821 19.799 1.00 43.15 N ANISOU 1290 N HIS B 173 4698 4681 7017 748 -1263 -569 N ATOM 1291 CA HIS B 173 -13.869 24.170 19.389 1.00 43.92 C ANISOU 1291 CA HIS B 173 4860 4708 7120 781 -1324 -517 C ATOM 1292 C HIS B 173 -12.353 24.356 19.199 1.00 43.06 C ANISOU 1292 C HIS B 173 4845 4594 6924 763 -1284 -406 C ATOM 1293 O HIS B 173 -11.893 25.439 18.833 1.00 39.24 O ANISOU 1293 O HIS B 173 4427 4050 6433 784 -1325 -351 O ATOM 1294 CB HIS B 173 -14.410 25.192 20.395 1.00 41.63 C ANISOU 1294 CB HIS B 173 4494 4389 6934 787 -1315 -600 C ATOM 1295 N ASN B 174 -11.577 23.302 19.446 1.00 45.22 N ANISOU 1295 N ASN B 174 5125 4925 7132 723 -1204 -373 N ATOM 1296 CA ASN B 174 -10.126 23.393 19.298 1.00 45.38 C ANISOU 1296 CA ASN B 174 5228 4942 7072 704 -1161 -276 C ATOM 1297 C ASN B 174 -9.657 23.350 17.847 1.00 47.72 C ANISOU 1297 C ASN B 174 5643 5212 7278 721 -1227 -179 C ATOM 1298 O ASN B 174 -9.896 22.372 17.139 1.00 47.87 O ANISOU 1298 O ASN B 174 5678 5264 7248 721 -1249 -168 O ATOM 1299 CB ASN B 174 -9.424 22.290 20.086 1.00 41.34 C ANISOU 1299 CB ASN B 174 4683 4500 6524 656 -1055 -278 C ATOM 1300 CG ASN B 174 -7.914 22.382 19.979 1.00 41.02 C ANISOU 1300 CG ASN B 174 4722 4453 6409 635 -1010 -186 C ATOM 1301 ND2 ASN B 174 -7.244 21.236 20.009 1.00 38.17 N ANISOU 1301 ND2 ASN B 174 4372 4146 5985 604 -956 -158 N ATOM 1302 OD1 ASN B 174 -7.356 23.476 19.857 1.00 40.54 O ANISOU 1302 OD1 ASN B 174 4716 4338 6350 646 -1025 -143 O ATOM 1303 N GLU B 175 -8.959 24.401 17.421 1.00 51.80 N ANISOU 1303 N GLU B 175 6244 5669 7768 732 -1252 -109 N ATOM 1304 CA GLU B 175 -8.441 24.479 16.060 1.00 55.33 C ANISOU 1304 CA GLU B 175 6816 6087 8120 741 -1306 -13 C ATOM 1305 C GLU B 175 -7.372 23.419 15.807 1.00 58.60 C ANISOU 1305 C GLU B 175 7279 6551 8437 701 -1243 48 C ATOM 1306 O GLU B 175 -7.053 23.111 14.659 1.00 61.20 O ANISOU 1306 O GLU B 175 7700 6877 8677 700 -1279 114 O ATOM 1307 CB GLU B 175 -7.832 25.857 15.789 1.00 59.47 C ANISOU 1307 CB GLU B 175 7424 6535 8638 750 -1329 48 C ATOM 1308 CG GLU B 175 -8.707 27.055 16.138 1.00 62.21 C ANISOU 1308 CG GLU B 175 7728 6825 9085 787 -1388 -8 C ATOM 1309 CD GLU B 175 -7.917 28.348 16.088 1.00 67.65 C ANISOU 1309 CD GLU B 175 8493 7443 9769 787 -1387 53 C ATOM 1310 OE1 GLU B 175 -6.774 28.305 15.581 1.00 66.96 O ANISOU 1310 OE1 GLU B 175 8503 7347 9590 758 -1352 142 O ATOM 1311 OE2 GLU B 175 -8.419 29.394 16.553 1.00 69.39 O1- ANISOU 1311 OE2 GLU B 175 8676 7615 10073 812 -1419 9 O1- ATOM 1312 N LEU B 176 -6.694 23.020 16.858 1.00 83.16 N ANISOU 1312 N LEU B 176 10328 9706 11561 668 -1149 23 N ATOM 1313 CA LEU B 176 -5.549 22.146 16.700 1.00 83.39 C ANISOU 1313 CA LEU B 176 10400 9778 11506 630 -1086 78 C ATOM 1314 C LEU B 176 -5.987 20.697 16.716 1.00 82.14 C ANISOU 1314 C LEU B 176 10200 9686 11323 623 -1083 46 C ATOM 1315 O LEU B 176 -5.201 19.818 17.034 1.00 83.28 O ANISOU 1315 O LEU B 176 10334 9880 11427 591 -1019 58 O ATOM 1316 CB LEU B 176 -4.501 22.433 17.782 1.00 20.00 C ATOM 1317 CG LEU B 176 -3.808 23.782 17.612 1.00 20.00 C ATOM 1318 CD1 LEU B 176 -2.923 24.192 18.786 1.00 20.00 C ATOM 1319 CD2 LEU B 176 -3.041 23.787 16.309 1.00 20.00 C ATOM 1320 N THR B 189 2.774 3.276 15.543 1.00 53.46 N ANISOU 1320 N THR B 189 6729 6748 6836 169 -446 127 N ATOM 1321 CA THR B 189 2.971 2.606 16.832 1.00 43.50 C ANISOU 1321 CA THR B 189 5422 5501 5605 147 -392 97 C ATOM 1322 C THR B 189 2.842 1.085 16.694 1.00 35.98 C ANISOU 1322 C THR B 189 4463 4573 4635 133 -391 70 C ATOM 1323 O THR B 189 3.216 0.328 17.606 1.00 40.95 O ANISOU 1323 O THR B 189 5075 5213 5271 112 -348 52 O ATOM 1324 CB THR B 189 2.049 3.223 17.951 1.00 45.28 C ANISOU 1324 CB THR B 189 5585 5708 5910 153 -388 72 C ATOM 1325 CG2 THR B 189 1.621 2.213 19.009 1.00 46.73 C ANISOU 1325 CG2 THR B 189 5721 5908 6125 130 -355 31 C ATOM 1326 OG1 THR B 189 2.751 4.277 18.618 1.00 35.74 O ANISOU 1326 OG1 THR B 189 4381 4485 4714 151 -351 89 O ATOM 1327 N LEU B 190 2.396 0.614 15.531 1.00 32.24 N ANISOU 1327 N LEU B 190 4010 4107 4132 144 -441 70 N ATOM 1328 CA LEU B 190 2.153 -0.822 15.371 1.00 26.14 C ANISOU 1328 CA LEU B 190 3227 3354 3350 131 -446 39 C ATOM 1329 C LEU B 190 3.360 -1.726 15.668 1.00 18.68 C ANISOU 1329 C LEU B 190 2305 2425 2367 109 -395 36 C ATOM 1330 O LEU B 190 3.192 -2.811 16.232 1.00 21.27 O ANISOU 1330 O LEU B 190 2612 2758 2712 93 -381 10 O ATOM 1331 CB LEU B 190 1.573 -1.149 13.988 1.00 36.23 C ANISOU 1331 CB LEU B 190 4528 4639 4597 148 -510 37 C ATOM 1332 CG LEU B 190 0.091 -1.525 14.068 1.00 39.08 C ANISOU 1332 CG LEU B 190 4836 4996 5018 156 -555 -2 C ATOM 1333 CD1 LEU B 190 -0.691 -0.376 14.686 1.00 44.42 C ANISOU 1333 CD1 LEU B 190 5470 5649 5760 174 -569 -4 C ATOM 1334 CD2 LEU B 190 -0.509 -1.923 12.725 1.00 40.57 C ANISOU 1334 CD2 LEU B 190 5044 5194 5177 174 -625 -11 C ATOM 1335 N TYR B 191 4.563 -1.284 15.297 1.00 15.90 N ANISOU 1335 N TYR B 191 1994 2079 1968 107 -370 61 N ATOM 1336 CA TYR B 191 5.731 -2.165 15.325 1.00 15.53 C ANISOU 1336 CA TYR B 191 1967 2050 1885 93 -333 49 C ATOM 1337 C TYR B 191 6.176 -2.528 16.735 1.00 15.14 C ANISOU 1337 C TYR B 191 1892 1995 1868 80 -290 36 C ATOM 1338 O TYR B 191 6.862 -3.521 16.918 1.00 13.20 O ANISOU 1338 O TYR B 191 1652 1756 1606 73 -274 17 O ATOM 1339 CB TYR B 191 6.929 -1.505 14.638 1.00 13.91 C ANISOU 1339 CB TYR B 191 1805 1853 1628 89 -309 71 C ATOM 1340 CG TYR B 191 6.793 -1.208 13.156 1.00 17.34 C ANISOU 1340 CG TYR B 191 2285 2295 2007 94 -343 88 C ATOM 1341 CD1 TYR B 191 5.843 -1.840 12.376 1.00 20.18 C ANISOU 1341 CD1 TYR B 191 2648 2661 2358 104 -396 77 C ATOM 1342 CD2 TYR B 191 7.646 -0.289 12.549 1.00 21.83 C ANISOU 1342 CD2 TYR B 191 2898 2865 2531 85 -320 116 C ATOM 1343 CE1 TYR B 191 5.742 -1.561 11.009 1.00 21.97 C ANISOU 1343 CE1 TYR B 191 2926 2897 2526 108 -431 94 C ATOM 1344 CE2 TYR B 191 7.555 -0.001 11.193 1.00 23.54 C ANISOU 1344 CE2 TYR B 191 3170 3087 2686 84 -349 136 C ATOM 1345 CZ TYR B 191 6.600 -0.642 10.434 1.00 26.19 C ANISOU 1345 CZ TYR B 191 3512 3430 3008 97 -407 126 C ATOM 1346 OH TYR B 191 6.506 -0.353 9.090 1.00 28.57 O ANISOU 1346 OH TYR B 191 3875 3737 3242 97 -440 146 O ATOM 1347 N TYR B 192 5.814 -1.711 17.720 1.00 16.30 N ANISOU 1347 N TYR B 192 2010 2126 2056 80 -276 43 N ATOM 1348 CA TYR B 192 6.303 -1.910 19.093 1.00 17.45 C ANISOU 1348 CA TYR B 192 2140 2267 2223 67 -235 33 C ATOM 1349 C TYR B 192 5.188 -2.304 20.043 1.00 17.25 C ANISOU 1349 C TYR B 192 2080 2232 2243 55 -236 14 C ATOM 1350 O TYR B 192 5.399 -2.416 21.251 1.00 16.31 O ANISOU 1350 O TYR B 192 1952 2108 2139 41 -204 7 O ATOM 1351 CB TYR B 192 7.034 -0.644 19.611 1.00 18.05 C ANISOU 1351 CB TYR B 192 2216 2337 2305 70 -205 50 C ATOM 1352 CG TYR B 192 8.136 -0.225 18.686 1.00 15.07 C ANISOU 1352 CG TYR B 192 1872 1969 1884 73 -195 64 C ATOM 1353 CD1 TYR B 192 9.445 -0.646 18.902 1.00 13.96 C ANISOU 1353 CD1 TYR B 192 1743 1840 1721 67 -164 51 C ATOM 1354 CD2 TYR B 192 7.868 0.550 17.558 1.00 17.81 C ANISOU 1354 CD2 TYR B 192 2244 2313 2211 81 -219 88 C ATOM 1355 CE1 TYR B 192 10.449 -0.307 18.042 1.00 14.77 C ANISOU 1355 CE1 TYR B 192 1872 1955 1787 63 -148 55 C ATOM 1356 CE2 TYR B 192 8.873 0.893 16.684 1.00 11.84 C ANISOU 1356 CE2 TYR B 192 1526 1566 1408 74 -202 101 C ATOM 1357 CZ TYR B 192 10.163 0.452 16.931 1.00 18.06 C ANISOU 1357 CZ TYR B 192 2316 2369 2177 63 -162 81 C ATOM 1358 OH TYR B 192 11.175 0.790 16.077 1.00 21.68 O ANISOU 1358 OH TYR B 192 2806 2840 2592 51 -137 85 O ATOM 1359 N MET B 193 3.997 -2.530 19.492 1.00 16.55 N ANISOU 1359 N MET B 193 1972 2141 2174 58 -271 3 N ATOM 1360 CA MET B 193 2.833 -2.904 20.289 1.00 16.01 C ANISOU 1360 CA MET B 193 1865 2066 2153 40 -267 -23 C ATOM 1361 C MET B 193 2.768 -4.406 20.533 1.00 13.71 C ANISOU 1361 C MET B 193 1583 1774 1853 17 -261 -42 C ATOM 1362 O MET B 193 2.898 -5.189 19.605 1.00 13.57 O ANISOU 1362 O MET B 193 1585 1762 1810 22 -287 -46 O ATOM 1363 CB MET B 193 1.550 -2.443 19.588 1.00 18.78 C ANISOU 1363 CB MET B 193 2183 2414 2539 55 -312 -36 C ATOM 1364 CG MET B 193 0.301 -2.709 20.403 1.00 24.82 C ANISOU 1364 CG MET B 193 2895 3173 3362 34 -302 -73 C ATOM 1365 SD MET B 193 -1.149 -2.142 19.492 1.00 40.31 S ANISOU 1365 SD MET B 193 4811 5132 5373 60 -366 -97 S ATOM 1366 CE MET B 193 -0.540 -0.534 19.017 1.00 25.51 C ANISOU 1366 CE MET B 193 2961 3246 3484 98 -387 -56 C ATOM 1367 N ALA B 194 2.570 -4.802 21.790 1.00 14.83 N ANISOU 1367 N ALA B 194 1716 1905 2013 -11 -226 -54 N ATOM 1368 CA ALA B 194 2.487 -6.212 22.133 1.00 17.34 C ANISOU 1368 CA ALA B 194 2052 2213 2324 -38 -218 -68 C ATOM 1369 C ALA B 194 1.304 -6.819 21.393 1.00 19.20 C ANISOU 1369 C ALA B 194 2262 2450 2585 -46 -248 -94 C ATOM 1370 O ALA B 194 0.275 -6.154 21.201 1.00 17.07 O ANISOU 1370 O ALA B 194 1947 2184 2354 -42 -262 -110 O ATOM 1371 CB ALA B 194 2.340 -6.391 23.638 1.00 16.25 C ANISOU 1371 CB ALA B 194 1915 2063 2198 -73 -174 -73 C ATOM 1372 N PRO B 195 1.448 -8.077 20.971 1.00 18.83 N ANISOU 1372 N PRO B 195 2239 2395 2519 -55 -262 -103 N ATOM 1373 CA PRO B 195 0.448 -8.702 20.099 1.00 18.99 C ANISOU 1373 CA PRO B 195 2237 2418 2561 -60 -296 -132 C ATOM 1374 C PRO B 195 -0.917 -8.819 20.762 1.00 23.68 C ANISOU 1374 C PRO B 195 2784 3005 3210 -95 -279 -164 C ATOM 1375 O PRO B 195 -1.934 -8.823 20.058 1.00 22.75 O ANISOU 1375 O PRO B 195 2627 2894 3124 -91 -312 -193 O ATOM 1376 CB PRO B 195 1.027 -10.097 19.833 1.00 23.41 C ANISOU 1376 CB PRO B 195 2837 2965 3093 -69 -303 -136 C ATOM 1377 CG PRO B 195 2.004 -10.347 20.937 1.00 18.85 C ANISOU 1377 CG PRO B 195 2297 2371 2494 -80 -268 -116 C ATOM 1378 CD PRO B 195 2.575 -8.982 21.263 1.00 21.13 C ANISOU 1378 CD PRO B 195 2579 2675 2776 -58 -252 -92 C ATOM 1379 N GLU B 196 -0.949 -8.903 22.091 1.00 20.21 N ANISOU 1379 N GLU B 196 2348 2552 2779 -130 -229 -163 N ATOM 1380 CA GLU B 196 -2.227 -8.981 22.802 1.00 23.36 C ANISOU 1380 CA GLU B 196 2702 2946 3229 -172 -200 -200 C ATOM 1381 C GLU B 196 -3.066 -7.714 22.604 1.00 26.56 C ANISOU 1381 C GLU B 196 3042 3368 3681 -151 -213 -221 C ATOM 1382 O GLU B 196 -4.277 -7.718 22.850 1.00 28.93 O ANISOU 1382 O GLU B 196 3286 3669 4036 -177 -203 -266 O ATOM 1383 CB GLU B 196 -2.023 -9.264 24.299 1.00 26.21 C ANISOU 1383 CB GLU B 196 3089 3290 3579 -218 -139 -192 C ATOM 1384 CG GLU B 196 -1.183 -8.223 25.046 1.00 23.16 C ANISOU 1384 CG GLU B 196 2718 2911 3170 -201 -117 -163 C ATOM 1385 CD GLU B 196 0.282 -8.615 25.141 1.00 17.86 C ANISOU 1385 CD GLU B 196 2113 2230 2442 -182 -124 -124 C ATOM 1386 OE1 GLU B 196 0.954 -8.194 26.114 1.00 15.31 O ANISOU 1386 OE1 GLU B 196 1815 1905 2098 -185 -96 -105 O ATOM 1387 OE2 GLU B 196 0.773 -9.325 24.246 1.00 18.26 O1- ANISOU 1387 OE2 GLU B 196 2189 2277 2473 -161 -159 -117 O1- ATOM 1388 N HIS B 197 -2.424 -6.631 22.163 1.00 18.12 N ANISOU 1388 N HIS B 197 1980 2309 2596 -105 -237 -192 N ATOM 1389 CA HIS B 197 -3.130 -5.370 21.932 1.00 20.60 C ANISOU 1389 CA HIS B 197 2242 2631 2955 -78 -259 -208 C ATOM 1390 C HIS B 197 -3.473 -5.165 20.463 1.00 23.08 C ANISOU 1390 C HIS B 197 2546 2952 3271 -36 -331 -210 C ATOM 1391 O HIS B 197 -4.294 -4.308 20.125 1.00 25.16 O ANISOU 1391 O HIS B 197 2763 3216 3580 -11 -366 -231 O ATOM 1392 CB HIS B 197 -2.307 -4.189 22.441 1.00 18.57 C ANISOU 1392 CB HIS B 197 1999 2374 2682 -57 -240 -175 C ATOM 1393 CG HIS B 197 -1.920 -4.318 23.877 1.00 19.34 C ANISOU 1393 CG HIS B 197 2110 2467 2770 -95 -175 -172 C ATOM 1394 CD2 HIS B 197 -0.724 -4.194 24.495 1.00 18.97 C ANISOU 1394 CD2 HIS B 197 2111 2419 2680 -95 -148 -139 C ATOM 1395 ND1 HIS B 197 -2.829 -4.646 24.861 1.00 26.25 N ANISOU 1395 ND1 HIS B 197 2951 3340 3681 -142 -131 -211 N ATOM 1396 CE1 HIS B 197 -2.211 -4.700 26.028 1.00 26.81 C ANISOU 1396 CE1 HIS B 197 3055 3407 3724 -169 -81 -196 C ATOM 1397 NE2 HIS B 197 -0.933 -4.429 25.834 1.00 23.61 N ANISOU 1397 NE2 HIS B 197 2697 3002 3273 -138 -94 -153 N ATOM 1398 N LEU B 198 -2.847 -5.943 19.588 1.00 19.75 N ANISOU 1398 N LEU B 198 2170 2533 2800 -26 -357 -192 N ATOM 1399 CA LEU B 198 -3.119 -5.813 18.152 1.00 21.93 C ANISOU 1399 CA LEU B 198 2448 2818 3065 10 -426 -193 C ATOM 1400 C LEU B 198 -4.527 -6.320 17.840 1.00 24.94 C ANISOU 1400 C LEU B 198 2773 3201 3503 0 -458 -249 C ATOM 1401 O LEU B 198 -4.977 -7.328 18.399 1.00 21.60 O ANISOU 1401 O LEU B 198 2332 2772 3103 -42 -426 -280 O ATOM 1402 CB LEU B 198 -2.085 -6.574 17.329 1.00 17.61 C ANISOU 1402 CB LEU B 198 1963 2278 2451 18 -438 -168 C ATOM 1403 CG LEU B 198 -0.644 -6.066 17.410 1.00 17.26 C ANISOU 1403 CG LEU B 198 1970 2236 2352 31 -413 -122 C ATOM 1404 CD1 LEU B 198 0.274 -6.990 16.627 1.00 14.88 C ANISOU 1404 CD1 LEU B 198 1718 1943 1994 34 -421 -114 C ATOM 1405 CD2 LEU B 198 -0.572 -4.644 16.862 1.00 17.41 C ANISOU 1405 CD2 LEU B 198 1993 2257 2364 66 -441 -96 C ATOM 1406 N ASN B 199 -5.223 -5.608 16.961 1.00 28.20 N ANISOU 1406 N ASN B 199 3159 3617 3938 39 -523 -262 N ATOM 1407 CA ASN B 199 -6.629 -5.916 16.663 1.00 37.11 C ANISOU 1407 CA ASN B 199 4220 4747 5131 36 -562 -324 C ATOM 1408 C ASN B 199 -7.508 -6.064 17.910 1.00 41.81 C ANISOU 1408 C ASN B 199 4748 5337 5800 -8 -506 -373 C ATOM 1409 O ASN B 199 -8.493 -6.806 17.899 1.00 43.05 O ANISOU 1409 O ASN B 199 4856 5496 6006 -35 -510 -430 O ATOM 1410 CB ASN B 199 -6.750 -7.172 15.789 1.00 34.98 C ANISOU 1410 CB ASN B 199 3968 4485 4838 26 -593 -343 C ATOM 1411 CG ASN B 199 -6.603 -6.875 14.303 1.00 41.36 C ANISOU 1411 CG ASN B 199 4811 5303 5601 75 -675 -326 C ATOM 1412 ND2 ASN B 199 -6.459 -7.931 13.501 1.00 39.48 N ANISOU 1412 ND2 ASN B 199 4600 5075 5328 69 -697 -336 N ATOM 1413 OD1 ASN B 199 -6.633 -5.719 13.878 1.00 40.38 O ANISOU 1413 OD1 ASN B 199 4693 5177 5473 117 -718 -303 O ATOM 1414 N ASP B 200 -7.134 -5.385 18.991 1.00 36.23 N ANISOU 1414 N ASP B 200 4041 4625 5099 -21 -450 -356 N ATOM 1415 CA ASP B 200 -7.962 -5.354 20.188 1.00 46.00 C ANISOU 1415 CA ASP B 200 5216 5860 6400 -64 -393 -405 C ATOM 1416 C ASP B 200 -8.266 -3.892 20.479 1.00 53.46 C ANISOU 1416 C ASP B 200 6120 6803 7391 -31 -405 -413 C ATOM 1417 O ASP B 200 -7.553 -3.240 21.241 1.00 49.93 O ANISOU 1417 O ASP B 200 5697 6352 6923 -33 -362 -380 O ATOM 1418 CB ASP B 200 -7.248 -6.005 21.374 1.00 43.86 C ANISOU 1418 CB ASP B 200 4989 5585 6093 -119 -308 -382 C ATOM 1419 CG ASP B 200 -8.163 -6.211 22.565 1.00 55.93 C ANISOU 1419 CG ASP B 200 6462 7112 7676 -178 -242 -436 C ATOM 1420 OD1 ASP B 200 -8.537 -5.206 23.208 1.00 58.86 O ANISOU 1420 OD1 ASP B 200 6788 7487 8090 -174 -220 -458 O ATOM 1421 OD2 ASP B 200 -8.498 -7.379 22.864 1.00 56.76 O1- ANISOU 1421 OD2 ASP B 200 6572 7211 7783 -231 -207 -459 O1- ATOM 1422 N VAL B 201 -9.328 -3.392 19.849 1.00 81.50 N ANISOU 1422 N VAL B 201 9607 10354 11007 3 -468 -460 N ATOM 1423 CA VAL B 201 -9.732 -1.983 19.905 1.00 83.72 C ANISOU 1423 CA VAL B 201 9844 10625 11339 47 -502 -473 C ATOM 1424 C VAL B 201 -9.769 -1.397 21.311 1.00 80.38 C ANISOU 1424 C VAL B 201 9388 10201 10952 16 -424 -493 C ATOM 1425 O VAL B 201 -9.758 -0.176 21.487 1.00 84.74 O ANISOU 1425 O VAL B 201 9923 10742 11534 52 -440 -490 O ATOM 1426 CB VAL B 201 -11.144 -1.801 19.304 1.00 86.69 C ANISOU 1426 CB VAL B 201 10143 10998 11796 75 -568 -544 C ATOM 1427 CG1 VAL B 201 -11.134 -0.757 18.198 1.00 89.76 C ANISOU 1427 CG1 VAL B 201 10566 11368 12171 150 -659 -511 C ATOM 1428 CG2 VAL B 201 -11.683 -3.137 18.794 1.00 87.24 C ANISOU 1428 CG2 VAL B 201 10206 11079 11863 46 -575 -578 C ATOM 1429 N ASN B 202 -9.817 -2.277 22.306 1.00 59.22 N ANISOU 1429 N ASN B 202 6703 7531 8267 -51 -340 -514 N ATOM 1430 CA ASN B 202 -9.989 -1.886 23.694 1.00 59.61 C ANISOU 1430 CA ASN B 202 6719 7584 8346 -92 -259 -543 C ATOM 1431 C ASN B 202 -8.864 -2.478 24.545 1.00 57.98 C ANISOU 1431 C ASN B 202 6592 7379 8059 -137 -187 -488 C ATOM 1432 O ASN B 202 -9.105 -3.015 25.627 1.00 57.36 O ANISOU 1432 O ASN B 202 6506 7306 7983 -201 -110 -515 O ATOM 1433 CB ASN B 202 -11.343 -2.398 24.182 1.00 59.70 C ANISOU 1433 CB ASN B 202 6650 7604 8430 -140 -222 -631 C ATOM 1434 CG ASN B 202 -11.882 -1.616 25.366 1.00 61.22 C ANISOU 1434 CG ASN B 202 6809 7796 8655 -158 -153 -670 C ATOM 1435 ND2 ASN B 202 -12.449 -2.333 26.334 1.00 53.14 N ANISOU 1435 ND2 ASN B 202 5776 6781 7633 -227 -68 -710 N ATOM 1436 OD1 ASN B 202 -11.796 -0.384 25.409 1.00 65.77 O ANISOU 1436 OD1 ASN B 202 7373 8363 9252 -111 -177 -665 O ATOM 1437 N ALA B 203 -7.638 -2.385 24.035 1.00 56.10 N ANISOU 1437 N ALA B 203 6432 7135 7749 -104 -213 -415 N ATOM 1438 CA ALA B 203 -6.471 -3.015 24.655 1.00 47.83 C ANISOU 1438 CA ALA B 203 5463 6087 6625 -135 -163 -363 C ATOM 1439 C ALA B 203 -6.211 -2.506 26.067 1.00 38.05 C ANISOU 1439 C ALA B 203 4224 4850 5384 -167 -91 -367 C ATOM 1440 O ALA B 203 -6.284 -1.298 26.314 1.00 41.52 O ANISOU 1440 O ALA B 203 4630 5289 5856 -140 -94 -376 O ATOM 1441 CB ALA B 203 -5.243 -2.792 23.788 1.00 34.53 C ANISOU 1441 CB ALA B 203 3846 4398 4877 -88 -207 -296 C ATOM 1442 N LYS B 204 -5.897 -3.426 26.979 1.00 31.19 N ANISOU 1442 N LYS B 204 3396 3980 4474 -223 -31 -359 N ATOM 1443 CA LYS B 204 -5.630 -3.077 28.381 1.00 32.87 C ANISOU 1443 CA LYS B 204 3621 4197 4672 -260 39 -362 C ATOM 1444 C LYS B 204 -4.156 -3.283 28.756 1.00 23.38 C ANISOU 1444 C LYS B 204 2506 2988 3389 -255 48 -297 C ATOM 1445 O LYS B 204 -3.759 -4.359 29.219 1.00 26.53 O ANISOU 1445 O LYS B 204 2963 3378 3739 -293 74 -277 O ATOM 1446 CB LYS B 204 -6.521 -3.896 29.314 1.00 38.48 C ANISOU 1446 CB LYS B 204 4313 4910 5398 -338 106 -409 C ATOM 1447 N PRO B 205 -3.340 -2.243 28.565 1.00 26.77 N ANISOU 1447 N PRO B 205 2946 3419 3808 -206 25 -266 N ATOM 1448 CA PRO B 205 -1.886 -2.393 28.717 1.00 24.94 C ANISOU 1448 CA PRO B 205 2787 3182 3507 -192 23 -211 C ATOM 1449 C PRO B 205 -1.473 -2.718 30.151 1.00 23.76 C ANISOU 1449 C PRO B 205 2677 3031 3318 -238 81 -208 C ATOM 1450 O PRO B 205 -2.135 -2.294 31.109 1.00 23.44 O ANISOU 1450 O PRO B 205 2604 2999 3303 -272 130 -245 O ATOM 1451 CB PRO B 205 -1.350 -1.014 28.309 1.00 26.69 C ANISOU 1451 CB PRO B 205 2994 3405 3743 -140 -4 -194 C ATOM 1452 CG PRO B 205 -2.460 -0.389 27.494 1.00 35.75 C ANISOU 1452 CG PRO B 205 4075 4551 4956 -114 -42 -227 C ATOM 1453 CD PRO B 205 -3.722 -0.893 28.121 1.00 30.58 C ANISOU 1453 CD PRO B 205 3371 3902 4345 -161 -6 -284 C ATOM 1454 N THR B 206 -0.395 -3.489 30.290 1.00 17.86 N ANISOU 1454 N THR B 206 2001 2275 2509 -239 75 -168 N ATOM 1455 CA THR B 206 0.188 -3.800 31.589 1.00 17.82 C ANISOU 1455 CA THR B 206 2050 2265 2456 -273 115 -156 C ATOM 1456 C THR B 206 1.676 -3.503 31.485 1.00 14.19 C ANISOU 1456 C THR B 206 1632 1803 1955 -230 87 -117 C ATOM 1457 O THR B 206 2.175 -3.174 30.399 1.00 12.56 O ANISOU 1457 O THR B 206 1416 1599 1757 -183 46 -101 O ATOM 1458 CB THR B 206 0.061 -5.294 31.933 1.00 18.40 C ANISOU 1458 CB THR B 206 2179 2319 2492 -320 128 -148 C ATOM 1459 CG2 THR B 206 -1.400 -5.767 31.805 1.00 23.36 C ANISOU 1459 CG2 THR B 206 2762 2947 3165 -365 153 -190 C ATOM 1460 OG1 THR B 206 0.869 -6.046 31.026 1.00 17.01 O ANISOU 1460 OG1 THR B 206 2042 2130 2291 -286 77 -116 O ATOM 1461 N GLU B 207 2.392 -3.664 32.591 1.00 17.36 N ANISOU 1461 N GLU B 207 2084 2200 2311 -248 109 -105 N ATOM 1462 CA GLU B 207 3.853 -3.558 32.570 1.00 12.10 C ANISOU 1462 CA GLU B 207 1459 1531 1608 -209 80 -75 C ATOM 1463 C GLU B 207 4.475 -4.467 31.480 1.00 12.39 C ANISOU 1463 C GLU B 207 1523 1555 1629 -180 33 -53 C ATOM 1464 O GLU B 207 5.494 -4.121 30.841 1.00 11.77 O ANISOU 1464 O GLU B 207 1447 1482 1545 -137 4 -39 O ATOM 1465 CB GLU B 207 4.417 -3.910 33.951 1.00 12.56 C ANISOU 1465 CB GLU B 207 1576 1581 1614 -237 101 -68 C ATOM 1466 CG GLU B 207 3.997 -2.892 35.033 1.00 18.87 C ANISOU 1466 CG GLU B 207 2350 2397 2423 -261 149 -93 C ATOM 1467 CD GLU B 207 4.589 -3.171 36.400 1.00 22.80 C ANISOU 1467 CD GLU B 207 2913 2890 2861 -288 166 -86 C ATOM 1468 OE1 GLU B 207 4.967 -4.334 36.672 1.00 26.49 O ANISOU 1468 OE1 GLU B 207 3450 3334 3280 -302 148 -62 O ATOM 1469 OE2 GLU B 207 4.678 -2.217 37.216 1.00 25.91 O1- ANISOU 1469 OE2 GLU B 207 3291 3300 3254 -293 194 -104 O1- ATOM 1470 N LYS B 208 3.845 -5.624 31.263 1.00 13.08 N ANISOU 1470 N LYS B 208 1629 1627 1713 -208 29 -55 N ATOM 1471 CA LYS B 208 4.353 -6.592 30.286 1.00 14.14 C ANISOU 1471 CA LYS B 208 1790 1748 1835 -184 -14 -41 C ATOM 1472 C LYS B 208 4.238 -6.090 28.832 1.00 12.69 C ANISOU 1472 C LYS B 208 1559 1581 1681 -146 -44 -44 C ATOM 1473 O LYS B 208 5.056 -6.466 27.966 1.00 12.77 O ANISOU 1473 O LYS B 208 1587 1590 1675 -114 -78 -34 O ATOM 1474 CB LYS B 208 3.663 -7.963 30.457 1.00 13.71 C ANISOU 1474 CB LYS B 208 1769 1669 1772 -227 -10 -43 C ATOM 1475 CG LYS B 208 3.855 -8.608 31.843 1.00 12.84 C ANISOU 1475 CG LYS B 208 1725 1534 1619 -269 13 -31 C ATOM 1476 CD LYS B 208 5.346 -8.794 32.183 1.00 14.10 C ANISOU 1476 CD LYS B 208 1939 1680 1737 -232 -21 -8 C ATOM 1477 CE LYS B 208 5.516 -9.468 33.540 1.00 19.09 C ANISOU 1477 CE LYS B 208 2648 2283 2320 -270 -9 7 C ATOM 1478 NZ LYS B 208 6.933 -9.421 34.029 1.00 18.00 N1+ ANISOU 1478 NZ LYS B 208 2555 2137 2148 -231 -46 22 N1+ ATOM 1479 N SER B 209 3.253 -5.224 28.571 1.00 13.14 N ANISOU 1479 N SER B 209 1560 1652 1779 -149 -32 -62 N ATOM 1480 CA SER B 209 3.146 -4.538 27.278 1.00 14.08 C ANISOU 1480 CA SER B 209 1643 1784 1922 -111 -64 -61 C ATOM 1481 C SER B 209 4.398 -3.695 26.995 1.00 12.24 C ANISOU 1481 C SER B 209 1421 1559 1670 -73 -74 -41 C ATOM 1482 O SER B 209 4.937 -3.668 25.855 1.00 12.27 O ANISOU 1482 O SER B 209 1433 1568 1662 -43 -104 -29 O ATOM 1483 CB SER B 209 1.908 -3.627 27.265 1.00 17.82 C ANISOU 1483 CB SER B 209 2056 2267 2449 -117 -54 -87 C ATOM 1484 OG SER B 209 0.768 -4.337 27.733 1.00 20.58 O ANISOU 1484 OG SER B 209 2388 2611 2820 -160 -32 -115 O ATOM 1485 N ASP B 210 4.854 -2.991 28.034 1.00 11.73 N ANISOU 1485 N ASP B 210 1359 1496 1602 -77 -46 -40 N ATOM 1486 CA ASP B 210 6.035 -2.141 27.901 1.00 12.22 C ANISOU 1486 CA ASP B 210 1427 1565 1652 -47 -49 -26 C ATOM 1487 C ASP B 210 7.271 -2.999 27.712 1.00 10.73 C ANISOU 1487 C ASP B 210 1281 1372 1424 -34 -67 -16 C ATOM 1488 O ASP B 210 8.201 -2.616 26.979 1.00 9.10 O ANISOU 1488 O ASP B 210 1076 1173 1209 -7 -79 -10 O ATOM 1489 CB ASP B 210 6.268 -1.277 29.155 1.00 8.84 C ANISOU 1489 CB ASP B 210 991 1139 1229 -57 -16 -34 C ATOM 1490 CG ASP B 210 5.288 -0.133 29.283 1.00 11.65 C ANISOU 1490 CG ASP B 210 1297 1499 1632 -60 0 -49 C ATOM 1491 OD1 ASP B 210 4.635 0.211 28.280 1.00 12.34 O ANISOU 1491 OD1 ASP B 210 1357 1585 1748 -45 -22 -49 O ATOM 1492 OD2 ASP B 210 5.177 0.441 30.401 1.00 13.86 O1- ANISOU 1492 OD2 ASP B 210 1566 1781 1921 -77 32 -65 O1- ATOM 1493 N VAL B 211 7.317 -4.129 28.420 1.00 10.16 N ANISOU 1493 N VAL B 211 1244 1286 1330 -53 -67 -18 N ATOM 1494 CA VAL B 211 8.449 -5.050 28.209 1.00 11.04 C ANISOU 1494 CA VAL B 211 1394 1389 1412 -35 -94 -15 C ATOM 1495 C VAL B 211 8.531 -5.543 26.749 1.00 9.84 C ANISOU 1495 C VAL B 211 1237 1241 1260 -16 -121 -16 C ATOM 1496 O VAL B 211 9.622 -5.577 26.132 1.00 10.21 O ANISOU 1496 O VAL B 211 1291 1295 1293 10 -136 -20 O ATOM 1497 CB VAL B 211 8.401 -6.234 29.211 1.00 10.95 C ANISOU 1497 CB VAL B 211 1431 1352 1377 -59 -97 -13 C ATOM 1498 CG1 VAL B 211 9.508 -7.250 28.909 1.00 10.55 C ANISOU 1498 CG1 VAL B 211 1418 1285 1304 -34 -135 -14 C ATOM 1499 CG2 VAL B 211 8.546 -5.684 30.630 1.00 11.37 C ANISOU 1499 CG2 VAL B 211 1498 1405 1418 -76 -72 -12 C ATOM 1500 N TYR B 212 7.384 -5.893 26.174 1.00 7.78 N ANISOU 1500 N TYR B 212 962 979 1014 -31 -127 -19 N ATOM 1501 CA TYR B 212 7.384 -6.234 24.734 1.00 8.99 C ANISOU 1501 CA TYR B 212 1111 1141 1164 -13 -154 -22 C ATOM 1502 C TYR B 212 7.944 -5.088 23.841 1.00 9.05 C ANISOU 1502 C TYR B 212 1101 1169 1169 13 -155 -15 C ATOM 1503 O TYR B 212 8.823 -5.297 22.927 1.00 11.30 O ANISOU 1503 O TYR B 212 1398 1463 1431 32 -168 -19 O ATOM 1504 CB TYR B 212 5.972 -6.639 24.276 1.00 9.44 C ANISOU 1504 CB TYR B 212 1148 1194 1243 -32 -164 -31 C ATOM 1505 CG TYR B 212 5.945 -7.060 22.817 1.00 11.20 C ANISOU 1505 CG TYR B 212 1371 1427 1457 -14 -196 -36 C ATOM 1506 CD1 TYR B 212 5.972 -8.408 22.466 1.00 11.77 C ANISOU 1506 CD1 TYR B 212 1467 1487 1519 -20 -216 -49 C ATOM 1507 CD2 TYR B 212 5.937 -6.103 21.793 1.00 11.03 C ANISOU 1507 CD2 TYR B 212 1333 1424 1433 7 -209 -29 C ATOM 1508 CE1 TYR B 212 5.981 -8.793 21.142 1.00 14.22 C ANISOU 1508 CE1 TYR B 212 1777 1809 1818 -5 -245 -59 C ATOM 1509 CE2 TYR B 212 5.948 -6.475 20.470 1.00 11.68 C ANISOU 1509 CE2 TYR B 212 1423 1517 1496 21 -238 -34 C ATOM 1510 CZ TYR B 212 5.967 -7.821 20.152 1.00 14.92 C ANISOU 1510 CZ TYR B 212 1850 1920 1897 15 -255 -52 C ATOM 1511 OH TYR B 212 5.988 -8.215 18.826 1.00 17.94 O ANISOU 1511 OH TYR B 212 2241 2317 2259 27 -283 -63 O ATOM 1512 N SER B 213 7.421 -3.878 24.090 1.00 10.01 N ANISOU 1512 N SER B 213 1195 1295 1312 11 -140 -7 N ATOM 1513 CA SER B 213 7.903 -2.747 23.280 1.00 9.32 C ANISOU 1513 CA SER B 213 1100 1219 1221 31 -140 5 C ATOM 1514 C SER B 213 9.424 -2.626 23.374 1.00 11.26 C ANISOU 1514 C SER B 213 1362 1472 1444 42 -127 2 C ATOM 1515 O SER B 213 10.115 -2.391 22.368 1.00 10.71 O ANISOU 1515 O SER B 213 1301 1412 1354 54 -130 4 O ATOM 1516 CB SER B 213 7.250 -1.431 23.727 1.00 10.47 C ANISOU 1516 CB SER B 213 1216 1362 1401 30 -127 11 C ATOM 1517 OG SER B 213 5.833 -1.553 23.687 1.00 14.08 O ANISOU 1517 OG SER B 213 1648 1814 1887 20 -140 2 O ATOM 1518 N PHE B 214 9.928 -2.790 24.601 1.00 10.67 N ANISOU 1518 N PHE B 214 1292 1390 1372 37 -112 -5 N ATOM 1519 CA PHE B 214 11.371 -2.725 24.859 1.00 12.43 C ANISOU 1519 CA PHE B 214 1524 1617 1581 50 -104 -17 C ATOM 1520 C PHE B 214 12.117 -3.773 24.035 1.00 11.03 C ANISOU 1520 C PHE B 214 1363 1444 1382 62 -124 -33 C ATOM 1521 O PHE B 214 13.203 -3.494 23.501 1.00 10.67 O ANISOU 1521 O PHE B 214 1314 1411 1327 74 -116 -47 O ATOM 1522 CB PHE B 214 11.646 -2.941 26.358 1.00 10.40 C ANISOU 1522 CB PHE B 214 1276 1349 1325 44 -98 -24 C ATOM 1523 CG PHE B 214 13.102 -3.182 26.691 1.00 9.31 C ANISOU 1523 CG PHE B 214 1147 1212 1176 62 -104 -44 C ATOM 1524 CD1 PHE B 214 14.022 -2.150 26.670 1.00 11.26 C ANISOU 1524 CD1 PHE B 214 1375 1473 1432 71 -85 -55 C ATOM 1525 CD2 PHE B 214 13.532 -4.448 27.039 1.00 12.30 C ANISOU 1525 CD2 PHE B 214 1556 1578 1542 70 -132 -57 C ATOM 1526 CE1 PHE B 214 15.387 -2.388 26.992 1.00 13.17 C ANISOU 1526 CE1 PHE B 214 1616 1717 1671 89 -93 -84 C ATOM 1527 CE2 PHE B 214 14.876 -4.696 27.358 1.00 11.96 C ANISOU 1527 CE2 PHE B 214 1516 1533 1496 93 -147 -83 C ATOM 1528 CZ PHE B 214 15.799 -3.660 27.330 1.00 11.97 C ANISOU 1528 CZ PHE B 214 1489 1552 1508 103 -127 -99 C ATOM 1529 N ALA B 215 11.550 -4.976 23.930 1.00 11.34 N ANISOU 1529 N ALA B 215 1419 1472 1416 58 -147 -36 N ATOM 1530 CA ALA B 215 12.190 -6.002 23.076 1.00 11.55 C ANISOU 1530 CA ALA B 215 1460 1501 1427 71 -167 -56 C ATOM 1531 C ALA B 215 12.410 -5.511 21.643 1.00 12.43 C ANISOU 1531 C ALA B 215 1564 1637 1524 76 -161 -59 C ATOM 1532 O ALA B 215 13.541 -5.656 21.030 1.00 12.71 O ANISOU 1532 O ALA B 215 1599 1685 1545 88 -156 -83 O ATOM 1533 CB ALA B 215 11.369 -7.285 23.070 1.00 10.95 C ANISOU 1533 CB ALA B 215 1403 1406 1352 61 -192 -58 C ATOM 1534 N VAL B 216 11.344 -4.925 21.089 1.00 9.99 N ANISOU 1534 N VAL B 216 1249 1332 1217 67 -163 -37 N ATOM 1535 CA VAL B 216 11.508 -4.447 19.702 1.00 11.86 C ANISOU 1535 CA VAL B 216 1490 1587 1428 70 -162 -33 C ATOM 1536 C VAL B 216 12.477 -3.271 19.578 1.00 13.13 C ANISOU 1536 C VAL B 216 1647 1759 1581 69 -130 -29 C ATOM 1537 O VAL B 216 13.231 -3.174 18.589 1.00 12.68 O ANISOU 1537 O VAL B 216 1601 1720 1496 68 -118 -40 O ATOM 1538 CB VAL B 216 10.171 -4.099 19.070 1.00 9.00 C ANISOU 1538 CB VAL B 216 1126 1224 1068 65 -182 -12 C ATOM 1539 CG1 VAL B 216 10.367 -3.734 17.574 1.00 10.47 C ANISOU 1539 CG1 VAL B 216 1332 1428 1216 67 -189 -6 C ATOM 1540 CG2 VAL B 216 9.234 -5.305 19.216 1.00 13.67 C ANISOU 1540 CG2 VAL B 216 1716 1805 1672 60 -209 -24 C ATOM 1541 N VAL B 217 12.478 -2.393 20.585 1.00 9.47 N ANISOU 1541 N VAL B 217 1169 1286 1142 67 -113 -17 N ATOM 1542 CA VAL B 217 13.486 -1.334 20.653 1.00 10.64 C ANISOU 1542 CA VAL B 217 1311 1441 1291 64 -80 -19 C ATOM 1543 C VAL B 217 14.929 -1.877 20.655 1.00 13.37 C ANISOU 1543 C VAL B 217 1652 1799 1628 70 -66 -58 C ATOM 1544 O VAL B 217 15.795 -1.350 19.946 1.00 14.70 O ANISOU 1544 O VAL B 217 1821 1982 1782 62 -39 -69 O ATOM 1545 CB VAL B 217 13.260 -0.410 21.883 1.00 9.46 C ANISOU 1545 CB VAL B 217 1143 1278 1174 62 -66 -8 C ATOM 1546 CG1 VAL B 217 14.490 0.507 22.097 1.00 11.45 C ANISOU 1546 CG1 VAL B 217 1385 1535 1431 59 -32 -20 C ATOM 1547 CG2 VAL B 217 12.015 0.427 21.676 1.00 8.80 C ANISOU 1547 CG2 VAL B 217 1057 1183 1105 59 -75 23 C ATOM 1548 N LEU B 218 15.186 -2.934 21.421 1.00 12.86 N ANISOU 1548 N LEU B 218 1585 1726 1574 82 -85 -81 N ATOM 1549 CA LEU B 218 16.502 -3.595 21.369 1.00 12.19 C ANISOU 1549 CA LEU B 218 1493 1651 1489 95 -84 -126 C ATOM 1550 C LEU B 218 16.873 -3.997 19.950 1.00 13.55 C ANISOU 1550 C LEU B 218 1671 1843 1635 91 -78 -146 C ATOM 1551 O LEU B 218 18.030 -3.735 19.436 1.00 14.22 O ANISOU 1551 O LEU B 218 1741 1947 1714 88 -49 -181 O ATOM 1552 CB LEU B 218 16.499 -4.859 22.225 1.00 13.07 C ANISOU 1552 CB LEU B 218 1613 1742 1611 112 -121 -141 C ATOM 1553 CG LEU B 218 16.388 -4.701 23.733 1.00 14.36 C ANISOU 1553 CG LEU B 218 1779 1887 1792 115 -130 -131 C ATOM 1554 CD1 LEU B 218 16.483 -6.079 24.393 1.00 17.98 C ANISOU 1554 CD1 LEU B 218 2261 2321 2252 130 -171 -145 C ATOM 1555 CD2 LEU B 218 17.522 -3.795 24.235 1.00 16.44 C ANISOU 1555 CD2 LEU B 218 2018 2161 2069 121 -108 -153 C ATOM 1556 N TRP B 219 15.890 -4.646 19.307 1.00 11.17 N ANISOU 1556 N TRP B 219 1388 1539 1317 89 -102 -130 N ATOM 1557 CA TRP B 219 16.124 -5.036 17.922 1.00 11.80 C ANISOU 1557 CA TRP B 219 1478 1639 1364 84 -97 -149 C ATOM 1558 C TRP B 219 16.496 -3.822 17.060 1.00 14.54 C ANISOU 1558 C TRP B 219 1833 2007 1685 62 -57 -137 C ATOM 1559 O TRP B 219 17.505 -3.852 16.362 1.00 15.69 O ANISOU 1559 O TRP B 219 1975 2175 1813 54 -28 -173 O ATOM 1560 CB TRP B 219 14.936 -5.827 17.349 1.00 12.63 C ANISOU 1560 CB TRP B 219 1603 1739 1456 84 -132 -134 C ATOM 1561 CG TRP B 219 15.187 -6.359 15.955 1.00 13.47 C ANISOU 1561 CG TRP B 219 1722 1868 1526 79 -131 -160 C ATOM 1562 CD1 TRP B 219 15.581 -7.630 15.608 1.00 12.81 C ANISOU 1562 CD1 TRP B 219 1637 1788 1443 90 -148 -205 C ATOM 1563 CD2 TRP B 219 15.008 -5.641 14.723 1.00 14.59 C ANISOU 1563 CD2 TRP B 219 1886 2032 1624 61 -115 -144 C ATOM 1564 CE2 TRP B 219 15.334 -6.531 13.672 1.00 14.23 C ANISOU 1564 CE2 TRP B 219 1851 2008 1549 60 -119 -182 C ATOM 1565 CE3 TRP B 219 14.620 -4.332 14.412 1.00 14.10 C ANISOU 1565 CE3 TRP B 219 1842 1971 1543 47 -101 -100 C ATOM 1566 NE1 TRP B 219 15.684 -7.728 14.231 1.00 15.63 N ANISOU 1566 NE1 TRP B 219 2009 2173 1758 79 -138 -222 N ATOM 1567 CZ2 TRP B 219 15.282 -6.137 12.324 1.00 18.90 C ANISOU 1567 CZ2 TRP B 219 2473 2624 2083 40 -105 -177 C ATOM 1568 CZ3 TRP B 219 14.575 -3.944 13.081 1.00 15.62 C ANISOU 1568 CZ3 TRP B 219 2069 2183 1682 29 -93 -90 C ATOM 1569 CH2 TRP B 219 14.895 -4.851 12.049 1.00 18.30 C ANISOU 1569 CH2 TRP B 219 2422 2547 1984 25 -94 -128 C ATOM 1570 N ALA B 220 15.732 -2.733 17.160 1.00 10.20 N ANISOU 1570 N ALA B 220 1294 1447 1135 53 -53 -90 N ATOM 1571 CA ALA B 220 15.991 -1.556 16.333 1.00 12.53 C ANISOU 1571 CA ALA B 220 1608 1751 1402 31 -21 -70 C ATOM 1572 C ALA B 220 17.344 -0.921 16.617 1.00 15.36 C ANISOU 1572 C ALA B 220 1946 2118 1770 18 28 -98 C ATOM 1573 O ALA B 220 17.986 -0.377 15.723 1.00 15.02 O ANISOU 1573 O ALA B 220 1920 2091 1697 -7 66 -104 O ATOM 1574 CB ALA B 220 14.879 -0.526 16.526 1.00 10.87 C ANISOU 1574 CB ALA B 220 1410 1520 1201 29 -36 -17 C ATOM 1575 N ILE B 221 17.768 -0.976 17.877 1.00 11.77 N ANISOU 1575 N ILE B 221 1460 1654 1359 33 27 -117 N ATOM 1576 CA ILE B 221 19.055 -0.426 18.266 1.00 11.17 C ANISOU 1576 CA ILE B 221 1357 1586 1302 24 66 -152 C ATOM 1577 C ILE B 221 20.149 -1.168 17.538 1.00 15.54 C ANISOU 1577 C ILE B 221 1897 2165 1842 20 86 -211 C ATOM 1578 O ILE B 221 21.126 -0.545 17.112 1.00 16.38 O ANISOU 1578 O ILE B 221 1992 2287 1943 -4 136 -239 O ATOM 1579 CB ILE B 221 19.268 -0.551 19.782 1.00 14.05 C ANISOU 1579 CB ILE B 221 1692 1936 1711 47 48 -167 C ATOM 1580 CG1 ILE B 221 18.432 0.512 20.478 1.00 11.03 C ANISOU 1580 CG1 ILE B 221 1314 1533 1344 42 48 -120 C ATOM 1581 CG2 ILE B 221 20.761 -0.382 20.150 1.00 13.04 C ANISOU 1581 CG2 ILE B 221 1527 1821 1608 47 77 -224 C ATOM 1582 CD1 ILE B 221 18.339 0.339 21.997 1.00 10.79 C ANISOU 1582 CD1 ILE B 221 1265 1488 1346 61 26 -126 C ATOM 1583 N PHE B 222 20.007 -2.486 17.381 1.00 12.00 N ANISOU 1583 N PHE B 222 1448 1720 1391 41 52 -236 N ATOM 1584 CA PHE B 222 21.058 -3.141 16.574 1.00 14.80 C ANISOU 1584 CA PHE B 222 1787 2101 1734 37 74 -300 C ATOM 1585 C PHE B 222 20.874 -3.155 15.049 1.00 20.22 C ANISOU 1585 C PHE B 222 2507 2812 2366 8 98 -296 C ATOM 1586 O PHE B 222 21.854 -3.241 14.289 1.00 19.79 O ANISOU 1586 O PHE B 222 2440 2784 2295 -11 141 -349 O ATOM 1587 CB PHE B 222 21.413 -4.513 17.129 1.00 13.86 C ANISOU 1587 CB PHE B 222 1644 1973 1647 73 31 -348 C ATOM 1588 CG PHE B 222 22.185 -4.421 18.401 1.00 17.84 C ANISOU 1588 CG PHE B 222 2114 2465 2200 96 20 -376 C ATOM 1589 CD1 PHE B 222 23.571 -4.395 18.375 1.00 19.09 C ANISOU 1589 CD1 PHE B 222 2229 2641 2384 98 47 -448 C ATOM 1590 CD2 PHE B 222 21.526 -4.260 19.609 1.00 14.10 C ANISOU 1590 CD2 PHE B 222 1649 1964 1744 111 -12 -335 C ATOM 1591 CE1 PHE B 222 24.305 -4.272 19.546 1.00 18.15 C ANISOU 1591 CE1 PHE B 222 2076 2510 2309 121 30 -479 C ATOM 1592 CE2 PHE B 222 22.245 -4.136 20.794 1.00 13.04 C ANISOU 1592 CE2 PHE B 222 1489 1819 1647 131 -26 -360 C ATOM 1593 CZ PHE B 222 23.640 -4.145 20.760 1.00 19.14 C ANISOU 1593 CZ PHE B 222 2218 2607 2446 139 -9 -432 C ATOM 1594 N ALA B 223 19.636 -3.053 14.588 1.00 16.23 N ANISOU 1594 N ALA B 223 2042 2296 1828 5 72 -239 N ATOM 1595 CA ALA B 223 19.401 -3.053 13.143 1.00 21.72 C ANISOU 1595 CA ALA B 223 2777 3014 2463 -20 87 -232 C ATOM 1596 C ALA B 223 19.605 -1.682 12.510 1.00 20.51 C ANISOU 1596 C ALA B 223 2657 2865 2271 -60 135 -200 C ATOM 1597 O ALA B 223 19.777 -1.579 11.283 1.00 19.21 O ANISOU 1597 O ALA B 223 2529 2722 2047 -91 163 -203 O ATOM 1598 CB ALA B 223 18.001 -3.572 12.827 1.00 18.59 C ANISOU 1598 CB ALA B 223 2410 2605 2048 -6 32 -192 C ATOM 1599 N ASN B 224 19.577 -0.636 13.340 1.00 15.89 N ANISOU 1599 N ASN B 224 2063 2257 1717 -62 145 -167 N ATOM 1600 CA ASN B 224 19.610 0.750 12.868 1.00 17.69 C ANISOU 1600 CA ASN B 224 2329 2477 1916 -98 183 -125 C ATOM 1601 C ASN B 224 18.457 1.114 11.929 1.00 18.05 C ANISOU 1601 C ASN B 224 2438 2511 1908 -105 152 -63 C ATOM 1602 O ASN B 224 18.603 2.000 11.076 1.00 18.92 O ANISOU 1602 O ASN B 224 2599 2620 1971 -142 183 -34 O ATOM 1603 CB ASN B 224 20.960 1.087 12.198 1.00 19.04 C ANISOU 1603 CB ASN B 224 2498 2674 2063 -142 258 -172 C ATOM 1604 CG ASN B 224 22.159 0.699 13.054 1.00 22.92 C ANISOU 1604 CG ASN B 224 2919 3178 2611 -132 283 -245 C ATOM 1605 ND2 ASN B 224 22.944 -0.272 12.581 1.00 23.28 N ANISOU 1605 ND2 ASN B 224 2939 3255 2652 -133 301 -316 N ATOM 1606 OD1 ASN B 224 22.389 1.279 14.122 1.00 22.97 O ANISOU 1606 OD1 ASN B 224 2894 3166 2668 -122 285 -243 O ATOM 1607 N LYS B 225 17.320 0.431 12.078 1.00 15.57 N ANISOU 1607 N LYS B 225 2124 2188 1603 -72 89 -43 N ATOM 1608 CA LYS B 225 16.135 0.727 11.273 1.00 18.76 C ANISOU 1608 CA LYS B 225 2581 2580 1967 -70 45 10 C ATOM 1609 C LYS B 225 14.874 0.163 11.915 1.00 16.09 C ANISOU 1609 C LYS B 225 2220 2224 1668 -32 -20 25 C ATOM 1610 O LYS B 225 14.951 -0.519 12.942 1.00 17.55 O ANISOU 1610 O LYS B 225 2357 2407 1903 -12 -27 -2 O ATOM 1611 CB LYS B 225 16.288 0.153 9.859 1.00 19.50 C ANISOU 1611 CB LYS B 225 2718 2704 1987 -91 51 -6 C ATOM 1612 CG LYS B 225 16.502 -1.356 9.848 1.00 21.30 C ANISOU 1612 CG LYS B 225 2911 2958 2226 -73 39 -66 C ATOM 1613 CD LYS B 225 16.672 -1.891 8.418 1.00 22.86 C ANISOU 1613 CD LYS B 225 3150 3187 2348 -95 48 -88 C ATOM 1614 CE LYS B 225 16.917 -3.397 8.453 1.00 30.87 C ANISOU 1614 CE LYS B 225 4125 4222 3381 -75 35 -153 C ATOM 1615 NZ LYS B 225 17.231 -3.989 7.108 1.00 26.70 N1+ ANISOU 1615 NZ LYS B 225 3629 3730 2784 -99 52 -191 N1+ ATOM 1616 N GLU B 226 13.716 0.448 11.315 1.00 16.61 N ANISOU 1616 N GLU B 226 2321 2277 1712 -23 -68 67 N ATOM 1617 CA GLU B 226 12.452 -0.158 11.745 1.00 18.35 C ANISOU 1617 CA GLU B 226 2518 2485 1968 8 -128 72 C ATOM 1618 C GLU B 226 12.374 -1.625 11.314 1.00 15.10 C ANISOU 1618 C GLU B 226 2098 2097 1541 15 -147 32 C ATOM 1619 O GLU B 226 12.918 -2.001 10.265 1.00 19.67 O ANISOU 1619 O GLU B 226 2707 2702 2065 -2 -132 12 O ATOM 1620 CB GLU B 226 11.254 0.609 11.153 1.00 20.17 C ANISOU 1620 CB GLU B 226 2785 2695 2185 17 -180 120 C ATOM 1621 CG GLU B 226 11.167 2.090 11.540 1.00 25.35 C ANISOU 1621 CG GLU B 226 3453 3318 2862 15 -172 162 C ATOM 1622 CD GLU B 226 10.818 2.315 12.995 1.00 24.31 C ANISOU 1622 CD GLU B 226 3263 3167 2809 33 -172 157 C ATOM 1623 OE1 GLU B 226 10.546 1.329 13.722 1.00 25.73 O ANISOU 1623 OE1 GLU B 226 3399 3356 3023 45 -180 127 O ATOM 1624 OE2 GLU B 226 10.803 3.492 13.410 1.00 29.57 O1- ANISOU 1624 OE2 GLU B 226 3931 3805 3499 32 -162 184 O1- ATOM 1625 N PRO B 227 11.689 -2.466 12.114 1.00 15.07 N ANISOU 1625 N PRO B 227 2056 2085 1586 36 -178 17 N ATOM 1626 CA PRO B 227 11.498 -3.874 11.738 1.00 16.30 C ANISOU 1626 CA PRO B 227 2204 2254 1734 42 -202 -20 C ATOM 1627 C PRO B 227 10.449 -3.992 10.640 1.00 16.75 C ANISOU 1627 C PRO B 227 2292 2317 1756 46 -251 -6 C ATOM 1628 O PRO B 227 9.800 -2.985 10.300 1.00 15.81 O ANISOU 1628 O PRO B 227 2197 2185 1624 49 -274 34 O ATOM 1629 CB PRO B 227 10.947 -4.499 13.027 1.00 12.64 C ANISOU 1629 CB PRO B 227 1699 1769 1334 57 -219 -29 C ATOM 1630 CG PRO B 227 10.120 -3.335 13.629 1.00 12.32 C ANISOU 1630 CG PRO B 227 1650 1707 1325 62 -229 12 C ATOM 1631 CD PRO B 227 11.026 -2.143 13.391 1.00 12.77 C ANISOU 1631 CD PRO B 227 1728 1767 1358 50 -190 32 C ATOM 1632 N TYR B 228 10.305 -5.200 10.095 1.00 17.39 N ANISOU 1632 N TYR B 228 2373 2413 1822 49 -272 -42 N ATOM 1633 CA TYR B 228 9.177 -5.558 9.228 1.00 18.08 C ANISOU 1633 CA TYR B 228 2477 2504 1888 57 -328 -40 C ATOM 1634 C TYR B 228 9.137 -4.832 7.881 1.00 19.19 C ANISOU 1634 C TYR B 228 2678 2661 1954 48 -342 -16 C ATOM 1635 O TYR B 228 8.046 -4.636 7.329 1.00 17.70 O ANISOU 1635 O TYR B 228 2506 2467 1754 60 -399 3 O ATOM 1636 CB TYR B 228 7.845 -5.337 9.949 1.00 16.74 C ANISOU 1636 CB TYR B 228 2277 2308 1776 74 -371 -20 C ATOM 1637 CG TYR B 228 7.730 -5.990 11.316 1.00 14.90 C ANISOU 1637 CG TYR B 228 1995 2057 1611 76 -357 -38 C ATOM 1638 CD1 TYR B 228 8.039 -7.337 11.507 1.00 15.54 C ANISOU 1638 CD1 TYR B 228 2062 2139 1703 74 -353 -78 C ATOM 1639 CD2 TYR B 228 7.311 -5.248 12.419 1.00 16.16 C ANISOU 1639 CD2 TYR B 228 2127 2193 1820 80 -350 -14 C ATOM 1640 CE1 TYR B 228 7.918 -7.931 12.771 1.00 15.37 C ANISOU 1640 CE1 TYR B 228 2009 2095 1736 73 -344 -88 C ATOM 1641 CE2 TYR B 228 7.196 -5.824 13.674 1.00 14.36 C ANISOU 1641 CE2 TYR B 228 1864 1948 1643 77 -335 -28 C ATOM 1642 CZ TYR B 228 7.495 -7.160 13.844 1.00 13.36 C ANISOU 1642 CZ TYR B 228 1733 1822 1522 72 -333 -62 C ATOM 1643 OH TYR B 228 7.361 -7.719 15.100 1.00 12.21 O ANISOU 1643 OH TYR B 228 1565 1654 1420 66 -321 -70 O ATOM 1644 N GLU B 229 10.299 -4.461 7.347 1.00 15.98 N ANISOU 1644 N GLU B 229 2304 2273 1494 24 -291 -18 N ATOM 1645 CA GLU B 229 10.359 -3.739 6.060 1.00 21.85 C ANISOU 1645 CA GLU B 229 3118 3031 2153 6 -295 9 C ATOM 1646 C GLU B 229 9.698 -4.481 4.896 1.00 23.24 C ANISOU 1646 C GLU B 229 3325 3227 2277 11 -346 -9 C ATOM 1647 O GLU B 229 9.285 -3.852 3.916 1.00 21.61 O ANISOU 1647 O GLU B 229 3181 3023 2006 5 -378 23 O ATOM 1648 CB GLU B 229 11.806 -3.381 5.678 1.00 20.75 C ANISOU 1648 CB GLU B 229 3006 2914 1966 -30 -218 -4 C ATOM 1649 CG GLU B 229 12.699 -4.575 5.326 1.00 24.60 C ANISOU 1649 CG GLU B 229 3474 3436 2436 -42 -182 -73 C ATOM 1650 CD GLU B 229 14.167 -4.192 5.324 1.00 30.52 C ANISOU 1650 CD GLU B 229 4224 4203 3168 -74 -99 -98 C ATOM 1651 OE1 GLU B 229 14.887 -4.556 4.369 1.00 35.83 O ANISOU 1651 OE1 GLU B 229 4922 4911 3781 -102 -62 -137 O ATOM 1652 OE2 GLU B 229 14.596 -3.517 6.280 1.00 27.92 O1- ANISOU 1652 OE2 GLU B 229 3867 3855 2888 -74 -70 -82 O1- ATOM 1653 N ASN B 230 9.589 -5.804 4.988 1.00 19.12 N ANISOU 1653 N ASN B 230 2766 2719 1781 20 -357 -61 N ATOM 1654 CA ASN B 230 8.982 -6.554 3.879 1.00 21.26 C ANISOU 1654 CA ASN B 230 3063 3011 2004 23 -405 -86 C ATOM 1655 C ASN B 230 7.464 -6.698 3.972 1.00 22.64 C ANISOU 1655 C ASN B 230 3219 3165 2217 52 -485 -74 C ATOM 1656 O ASN B 230 6.826 -7.230 3.049 1.00 21.32 O ANISOU 1656 O ASN B 230 3073 3014 2014 57 -536 -93 O ATOM 1657 CB ASN B 230 9.644 -7.925 3.698 1.00 22.56 C ANISOU 1657 CB ASN B 230 3203 3200 2169 17 -379 -155 C ATOM 1658 CG ASN B 230 11.076 -7.819 3.214 1.00 22.27 C ANISOU 1658 CG ASN B 230 3189 3192 2079 -14 -306 -181 C ATOM 1659 ND2 ASN B 230 11.945 -8.677 3.731 1.00 23.07 N ANISOU 1659 ND2 ASN B 230 3244 3299 2221 -13 -267 -235 N ATOM 1660 OD1 ASN B 230 11.402 -6.960 2.395 1.00 27.24 O ANISOU 1660 OD1 ASN B 230 3879 3838 2634 -39 -285 -154 O ATOM 1661 N ALA B 231 6.875 -6.212 5.060 1.00 17.00 N ANISOU 1661 N ALA B 231 2464 2419 1578 68 -497 -48 N ATOM 1662 CA ALA B 231 5.418 -6.286 5.214 1.00 21.69 C ANISOU 1662 CA ALA B 231 3030 2994 2218 93 -569 -45 C ATOM 1663 C ALA B 231 4.728 -5.482 4.108 1.00 19.39 C ANISOU 1663 C ALA B 231 2794 2703 1869 104 -632 -13 C ATOM 1664 O ALA B 231 5.197 -4.399 3.733 1.00 21.60 O ANISOU 1664 O ALA B 231 3130 2979 2099 96 -618 31 O ATOM 1665 CB ALA B 231 4.998 -5.772 6.577 1.00 20.85 C ANISOU 1665 CB ALA B 231 2871 2855 2196 103 -560 -25 C ATOM 1666 N ILE B 232 3.618 -6.009 3.596 1.00 18.86 N ANISOU 1666 N ILE B 232 2717 2639 1810 123 -704 -36 N ATOM 1667 CA ILE B 232 2.913 -5.389 2.475 1.00 20.84 C ANISOU 1667 CA ILE B 232 3024 2891 2003 139 -780 -12 C ATOM 1668 C ILE B 232 1.583 -4.764 2.892 1.00 24.82 C ANISOU 1668 C ILE B 232 3492 3363 2577 173 -851 1 C ATOM 1669 O ILE B 232 1.211 -3.684 2.411 1.00 26.75 O ANISOU 1669 O ILE B 232 3782 3588 2793 191 -902 44 O ATOM 1670 CB ILE B 232 2.680 -6.413 1.325 1.00 20.21 C ANISOU 1670 CB ILE B 232 2969 2844 1866 137 -819 -56 C ATOM 1671 CG1 ILE B 232 4.000 -6.752 0.636 1.00 19.32 C ANISOU 1671 CG1 ILE B 232 2909 2765 1665 103 -754 -67 C ATOM 1672 CG2 ILE B 232 1.686 -5.863 0.295 1.00 18.91 C ANISOU 1672 CG2 ILE B 232 2851 2676 1659 161 -913 -37 C ATOM 1673 CD1 ILE B 232 4.679 -5.534 -0.002 1.00 28.88 C ANISOU 1673 CD1 ILE B 232 4208 3978 2789 85 -733 -11 C ATOM 1674 N ALA B 233 0.860 -5.439 3.784 1.00 23.34 N ANISOU 1674 N ALA B 233 3221 3166 2482 181 -857 -37 N ATOM 1675 CA ALA B 233 -0.446 -4.958 4.227 1.00 25.68 C ANISOU 1675 CA ALA B 233 3467 3435 2857 211 -919 -41 C ATOM 1676 C ALA B 233 -0.515 -4.926 5.741 1.00 25.95 C ANISOU 1676 C ALA B 233 3427 3449 2984 203 -865 -48 C ATOM 1677 O ALA B 233 0.078 -5.770 6.417 1.00 21.81 O ANISOU 1677 O ALA B 233 2876 2932 2477 178 -801 -69 O ATOM 1678 CB ALA B 233 -1.562 -5.842 3.675 1.00 23.45 C ANISOU 1678 CB ALA B 233 3151 3164 2596 225 -991 -94 C ATOM 1679 N GLU B 234 -1.257 -3.963 6.273 1.00 23.95 N ANISOU 1679 N GLU B 234 3144 3168 2790 225 -894 -33 N ATOM 1680 CA GLU B 234 -1.385 -3.831 7.718 1.00 27.33 C ANISOU 1680 CA GLU B 234 3505 3578 3302 215 -843 -41 C ATOM 1681 C GLU B 234 -1.971 -5.084 8.367 1.00 21.92 C ANISOU 1681 C GLU B 234 2751 2899 2679 197 -827 -98 C ATOM 1682 O GLU B 234 -1.448 -5.550 9.373 1.00 19.98 O ANISOU 1682 O GLU B 234 2482 2651 2459 171 -757 -103 O ATOM 1683 CB GLU B 234 -2.202 -2.587 8.083 1.00 28.67 C ANISOU 1683 CB GLU B 234 3647 3716 3528 245 -885 -26 C ATOM 1684 CG GLU B 234 -2.390 -2.398 9.586 1.00 26.38 C ANISOU 1684 CG GLU B 234 3288 3411 3324 233 -830 -41 C ATOM 1685 CD GLU B 234 -2.992 -1.045 9.944 1.00 36.92 C ANISOU 1685 CD GLU B 234 4602 4715 4712 262 -862 -26 C ATOM 1686 OE1 GLU B 234 -4.166 -1.008 10.378 1.00 38.29 O ANISOU 1686 OE1 GLU B 234 4704 4879 4968 276 -896 -69 O ATOM 1687 OE2 GLU B 234 -2.285 -0.023 9.804 1.00 40.94 O1- ANISOU 1687 OE2 GLU B 234 5163 5208 5184 269 -852 25 O1- ATOM 1688 N GLN B 235 -3.040 -5.650 7.805 1.00 23.32 N ANISOU 1688 N GLN B 235 2898 3081 2879 209 -891 -141 N ATOM 1689 CA AGLN B 235 -3.624 -6.858 8.395 0.51 25.69 C ANISOU 1689 CA AGLN B 235 3136 3384 3240 185 -872 -196 C ATOM 1690 CA BGLN B 235 -3.621 -6.859 8.390 0.49 25.69 C ANISOU 1690 CA BGLN B 235 3137 3384 3240 185 -872 -196 C ATOM 1691 C GLN B 235 -2.682 -8.058 8.257 1.00 22.14 C ANISOU 1691 C GLN B 235 2718 2951 2745 157 -825 -205 C ATOM 1692 O GLN B 235 -2.680 -8.948 9.103 1.00 22.44 O ANISOU 1692 O GLN B 235 2722 2981 2825 129 -779 -230 O ATOM 1693 CB AGLN B 235 -5.004 -7.179 7.797 0.51 28.45 C ANISOU 1693 CB AGLN B 235 3442 3736 3632 203 -953 -248 C ATOM 1694 CB BGLN B 235 -4.996 -7.178 7.788 0.49 28.45 C ANISOU 1694 CB BGLN B 235 3443 3737 3631 203 -953 -247 C ATOM 1695 CG AGLN B 235 -6.192 -6.735 8.654 0.51 31.40 C ANISOU 1695 CG AGLN B 235 3731 4090 4108 209 -966 -281 C ATOM 1696 CG BGLN B 235 -6.156 -6.509 8.516 0.49 31.24 C ANISOU 1696 CG BGLN B 235 3720 4070 4079 216 -976 -273 C ATOM 1697 CD AGLN B 235 -6.413 -7.622 9.875 0.51 33.95 C ANISOU 1697 CD AGLN B 235 3996 4408 4497 164 -894 -318 C ATOM 1698 CD BGLN B 235 -6.125 -6.745 10.022 0.49 30.36 C ANISOU 1698 CD BGLN B 235 3556 3946 4032 180 -891 -285 C ATOM 1699 NE2AGLN B 235 -7.288 -8.615 9.735 0.51 33.83 N ANISOU 1699 NE2AGLN B 235 3932 4396 4525 147 -914 -379 N ATOM 1700 NE2BGLN B 235 -6.170 -5.662 10.790 0.49 30.28 N ANISOU 1700 NE2BGLN B 235 3527 3920 4058 189 -871 -264 N ATOM 1701 OE1AGLN B 235 -5.804 -7.415 10.928 0.51 32.51 O ANISOU 1701 OE1AGLN B 235 3814 4215 4323 142 -821 -292 O ATOM 1702 OE1BGLN B 235 -6.057 -7.886 10.487 0.49 33.55 O ANISOU 1702 OE1BGLN B 235 3943 4353 4451 142 -845 -312 O ATOM 1703 N GLN B 236 -1.883 -8.082 7.196 1.00 19.37 N ANISOU 1703 N GLN B 236 2433 2619 2307 164 -836 -186 N ATOM 1704 CA GLN B 236 -0.894 -9.151 7.054 1.00 16.59 C ANISOU 1704 CA GLN B 236 2107 2282 1915 140 -790 -199 C ATOM 1705 C GLN B 236 0.054 -9.069 8.262 1.00 17.77 C ANISOU 1705 C GLN B 236 2250 2417 2083 122 -710 -177 C ATOM 1706 O GLN B 236 0.310 -10.075 8.939 1.00 16.41 O ANISOU 1706 O GLN B 236 2058 2236 1940 101 -672 -201 O ATOM 1707 CB GLN B 236 -0.108 -9.014 5.748 1.00 16.74 C ANISOU 1707 CB GLN B 236 2199 2327 1834 147 -805 -184 C ATOM 1708 CG GLN B 236 1.119 -9.952 5.628 1.00 18.48 C ANISOU 1708 CG GLN B 236 2445 2564 2014 125 -749 -201 C ATOM 1709 CD GLN B 236 2.238 -9.373 4.759 1.00 14.84 C ANISOU 1709 CD GLN B 236 2053 2126 1459 123 -727 -173 C ATOM 1710 NE2 GLN B 236 3.199 -10.225 4.372 1.00 13.30 N ANISOU 1710 NE2 GLN B 236 1878 1952 1225 107 -690 -202 N ATOM 1711 OE1 GLN B 236 2.247 -8.177 4.441 1.00 17.24 O ANISOU 1711 OE1 GLN B 236 2394 2429 1729 132 -741 -128 O ATOM 1712 N LEU B 237 0.554 -7.864 8.523 1.00 18.16 N ANISOU 1712 N LEU B 237 2321 2461 2117 130 -689 -131 N ATOM 1713 CA LEU B 237 1.496 -7.633 9.631 1.00 18.19 C ANISOU 1713 CA LEU B 237 2322 2455 2136 116 -619 -109 C ATOM 1714 C LEU B 237 0.903 -7.953 10.991 1.00 15.78 C ANISOU 1714 C LEU B 237 1959 2127 1909 102 -594 -125 C ATOM 1715 O LEU B 237 1.532 -8.635 11.808 1.00 16.41 O ANISOU 1715 O LEU B 237 2035 2198 2000 83 -546 -132 O ATOM 1716 CB LEU B 237 1.993 -6.182 9.620 1.00 19.46 C ANISOU 1716 CB LEU B 237 2511 2611 2271 127 -607 -61 C ATOM 1717 CG LEU B 237 3.018 -5.819 10.697 1.00 17.45 C ANISOU 1717 CG LEU B 237 2254 2348 2029 114 -538 -41 C ATOM 1718 CD1 LEU B 237 4.228 -6.733 10.617 1.00 19.02 C ANISOU 1718 CD1 LEU B 237 2473 2561 2191 98 -495 -58 C ATOM 1719 CD2 LEU B 237 3.443 -4.376 10.514 1.00 24.67 C ANISOU 1719 CD2 LEU B 237 3199 3256 2917 122 -531 4 C ATOM 1720 N ILE B 238 -0.306 -7.457 11.247 1.00 19.79 N ANISOU 1720 N ILE B 238 2424 2623 2470 110 -627 -134 N ATOM 1721 CA ILE B 238 -0.965 -7.690 12.518 1.00 19.90 C ANISOU 1721 CA ILE B 238 2384 2619 2557 90 -597 -154 C ATOM 1722 C ILE B 238 -1.184 -9.168 12.733 1.00 21.38 C ANISOU 1722 C ILE B 238 2557 2802 2763 63 -585 -193 C ATOM 1723 O ILE B 238 -0.828 -9.710 13.788 1.00 17.86 O ANISOU 1723 O ILE B 238 2107 2342 2337 37 -535 -193 O ATOM 1724 CB ILE B 238 -2.320 -6.931 12.607 1.00 19.22 C ANISOU 1724 CB ILE B 238 2246 2525 2531 105 -639 -171 C ATOM 1725 CG1 ILE B 238 -2.079 -5.422 12.753 1.00 22.74 C ANISOU 1725 CG1 ILE B 238 2703 2963 2974 129 -641 -131 C ATOM 1726 CG2 ILE B 238 -3.129 -7.440 13.766 1.00 22.01 C ANISOU 1726 CG2 ILE B 238 2539 2864 2958 74 -606 -207 C ATOM 1727 CD1 ILE B 238 -3.359 -4.561 12.621 1.00 25.31 C ANISOU 1727 CD1 ILE B 238 2981 3277 3357 155 -699 -149 C ATOM 1728 N MET B 239 -1.761 -9.837 11.733 1.00 19.67 N ANISOU 1728 N MET B 239 2339 2597 2540 68 -635 -225 N ATOM 1729 CA MET B 239 -2.027 -11.259 11.886 1.00 18.08 C ANISOU 1729 CA MET B 239 2123 2386 2360 40 -626 -265 C ATOM 1730 C MET B 239 -0.736 -12.047 12.079 1.00 16.83 C ANISOU 1730 C MET B 239 2009 2222 2162 29 -585 -254 C ATOM 1731 O MET B 239 -0.685 -13.007 12.853 1.00 16.90 O ANISOU 1731 O MET B 239 2013 2209 2199 1 -554 -269 O ATOM 1732 CB MET B 239 -2.823 -11.788 10.693 1.00 19.18 C ANISOU 1732 CB MET B 239 2252 2539 2496 51 -691 -305 C ATOM 1733 CG MET B 239 -4.174 -11.112 10.568 1.00 25.39 C ANISOU 1733 CG MET B 239 2985 3326 3334 65 -739 -327 C ATOM 1734 SD MET B 239 -5.132 -11.214 12.092 1.00 35.98 S ANISOU 1734 SD MET B 239 4255 4643 4772 27 -692 -355 S ATOM 1735 CE MET B 239 -5.626 -12.922 12.018 1.00 32.74 C ANISOU 1735 CE MET B 239 3827 4222 4390 -13 -688 -411 C ATOM 1736 N ALA B 240 0.311 -11.614 11.389 1.00 16.04 N ANISOU 1736 N ALA B 240 1953 2142 1999 50 -585 -229 N ATOM 1737 CA ALA B 240 1.600 -12.288 11.449 1.00 16.13 C ANISOU 1737 CA ALA B 240 2000 2152 1976 45 -551 -227 C ATOM 1738 C ALA B 240 2.186 -12.179 12.855 1.00 14.81 C ANISOU 1738 C ALA B 240 1830 1962 1834 32 -499 -205 C ATOM 1739 O ALA B 240 2.637 -13.176 13.432 1.00 18.49 O ANISOU 1739 O ALA B 240 2307 2408 2312 18 -478 -218 O ATOM 1740 CB ALA B 240 2.540 -11.700 10.431 1.00 17.81 C ANISOU 1740 CB ALA B 240 2254 2394 2119 65 -555 -211 C ATOM 1741 N ILE B 241 2.157 -10.977 13.414 1.00 14.25 N ANISOU 1741 N ILE B 241 1750 1892 1772 38 -482 -173 N ATOM 1742 CA ILE B 241 2.728 -10.788 14.755 1.00 12.88 C ANISOU 1742 CA ILE B 241 1577 1701 1618 26 -434 -153 C ATOM 1743 C ILE B 241 1.901 -11.536 15.796 1.00 15.18 C ANISOU 1743 C ILE B 241 1843 1964 1959 -4 -420 -170 C ATOM 1744 O ILE B 241 2.455 -12.184 16.697 1.00 13.32 O ANISOU 1744 O ILE B 241 1626 1706 1728 -20 -391 -167 O ATOM 1745 CB ILE B 241 2.833 -9.285 15.107 1.00 13.92 C ANISOU 1745 CB ILE B 241 1700 1839 1749 38 -419 -119 C ATOM 1746 CG1 ILE B 241 3.819 -8.599 14.161 1.00 14.72 C ANISOU 1746 CG1 ILE B 241 1836 1963 1795 59 -422 -100 C ATOM 1747 CG2 ILE B 241 3.250 -9.082 16.582 1.00 10.73 C ANISOU 1747 CG2 ILE B 241 1291 1416 1368 24 -373 -104 C ATOM 1748 CD1 ILE B 241 3.738 -7.079 14.204 1.00 16.22 C ANISOU 1748 CD1 ILE B 241 2023 2155 1984 72 -420 -66 C ATOM 1749 N LYS B 242 0.576 -11.466 15.668 1.00 17.53 N ANISOU 1749 N LYS B 242 2102 2261 2296 -14 -441 -190 N ATOM 1750 CA LYS B 242 -0.287 -12.207 16.588 1.00 19.48 C ANISOU 1750 CA LYS B 242 2325 2484 2592 -53 -421 -213 C ATOM 1751 C LYS B 242 -0.064 -13.717 16.495 1.00 19.28 C ANISOU 1751 C LYS B 242 2325 2437 2562 -73 -423 -234 C ATOM 1752 O LYS B 242 -0.246 -14.438 17.482 1.00 23.80 O ANISOU 1752 O LYS B 242 2905 2979 3158 -108 -392 -238 O ATOM 1753 CB LYS B 242 -1.755 -11.849 16.351 1.00 19.58 C ANISOU 1753 CB LYS B 242 2282 2504 2654 -59 -445 -243 C ATOM 1754 CG LYS B 242 -2.078 -10.395 16.688 1.00 20.73 C ANISOU 1754 CG LYS B 242 2398 2660 2818 -43 -441 -226 C ATOM 1755 CD LYS B 242 -3.559 -10.075 16.461 1.00 24.19 C ANISOU 1755 CD LYS B 242 2773 3103 3316 -44 -472 -266 C ATOM 1756 CE LYS B 242 -4.433 -10.685 17.546 1.00 27.27 C ANISOU 1756 CE LYS B 242 3124 3476 3762 -95 -429 -302 C ATOM 1757 NZ LYS B 242 -4.107 -10.129 18.910 1.00 27.57 N1+ ANISOU 1757 NZ LYS B 242 3165 3504 3806 -116 -368 -279 N1+ ATOM 1758 N SER B 243 0.352 -14.188 15.322 1.00 18.07 N ANISOU 1758 N SER B 243 2191 2297 2377 -51 -457 -248 N ATOM 1759 CA SER B 243 0.662 -15.612 15.139 1.00 18.16 C ANISOU 1759 CA SER B 243 2227 2286 2387 -63 -464 -273 C ATOM 1760 C SER B 243 2.065 -15.988 15.628 1.00 20.14 C ANISOU 1760 C SER B 243 2523 2521 2610 -54 -442 -254 C ATOM 1761 O SER B 243 2.394 -17.171 15.693 1.00 21.45 O ANISOU 1761 O SER B 243 2712 2657 2780 -63 -447 -272 O ATOM 1762 CB SER B 243 0.526 -16.018 13.663 1.00 22.07 C ANISOU 1762 CB SER B 243 2722 2804 2860 -44 -510 -305 C ATOM 1763 OG SER B 243 1.727 -15.743 12.953 1.00 20.97 O ANISOU 1763 OG SER B 243 2615 2688 2666 -13 -514 -294 O ATOM 1764 N GLY B 244 2.896 -14.995 15.945 1.00 17.70 N ANISOU 1764 N GLY B 244 2223 2227 2276 -34 -422 -222 N ATOM 1765 CA GLY B 244 4.225 -15.273 16.487 1.00 17.65 C ANISOU 1765 CA GLY B 244 2251 2206 2251 -22 -404 -211 C ATOM 1766 C GLY B 244 5.399 -14.691 15.718 1.00 17.73 C ANISOU 1766 C GLY B 244 2271 2247 2218 11 -405 -208 C ATOM 1767 O GLY B 244 6.561 -14.844 16.138 1.00 12.99 O ANISOU 1767 O GLY B 244 1691 1638 1607 24 -392 -206 O ATOM 1768 N ASN B 245 5.116 -14.053 14.576 1.00 14.82 N ANISOU 1768 N ASN B 245 1892 1914 1825 24 -422 -211 N ATOM 1769 CA ASN B 245 6.153 -13.407 13.785 1.00 19.05 C ANISOU 1769 CA ASN B 245 2442 2482 2315 46 -415 -208 C ATOM 1770 C ASN B 245 6.795 -12.314 14.629 1.00 17.94 C ANISOU 1770 C ASN B 245 2301 2343 2173 50 -382 -174 C ATOM 1771 O ASN B 245 6.100 -11.624 15.374 1.00 16.57 O ANISOU 1771 O ASN B 245 2110 2161 2024 41 -373 -149 O ATOM 1772 CB ASN B 245 5.529 -12.750 12.561 1.00 20.02 C ANISOU 1772 CB ASN B 245 2562 2636 2407 52 -441 -206 C ATOM 1773 CG ASN B 245 6.352 -12.926 11.299 1.00 30.57 C ANISOU 1773 CG ASN B 245 3924 4003 3689 64 -446 -228 C ATOM 1774 ND2 ASN B 245 7.569 -13.441 11.436 1.00 34.27 N ANISOU 1774 ND2 ASN B 245 4402 4469 4148 69 -422 -248 N ATOM 1775 OD1 ASN B 245 5.884 -12.611 10.209 1.00 32.14 O ANISOU 1775 OD1 ASN B 245 4132 4225 3853 68 -473 -230 O ATOM 1776 N ARG B 246 8.109 -12.143 14.484 1.00 17.68 N ANISOU 1776 N ARG B 246 2282 2322 2115 64 -361 -180 N ATOM 1777 CA ARG B 246 8.862 -11.148 15.262 1.00 14.75 C ANISOU 1777 CA ARG B 246 1907 1952 1743 68 -329 -155 C ATOM 1778 C ARG B 246 9.886 -10.503 14.335 1.00 14.62 C ANISOU 1778 C ARG B 246 1902 1969 1685 77 -310 -161 C ATOM 1779 O ARG B 246 10.101 -10.987 13.217 1.00 17.93 O ANISOU 1779 O ARG B 246 2333 2408 2074 79 -320 -188 O ATOM 1780 CB ARG B 246 9.547 -11.820 16.472 1.00 14.20 C ANISOU 1780 CB ARG B 246 1843 1853 1700 70 -319 -163 C ATOM 1781 CG ARG B 246 8.568 -12.370 17.522 1.00 15.27 C ANISOU 1781 CG ARG B 246 1978 1953 1870 52 -327 -151 C ATOM 1782 CD ARG B 246 7.814 -11.248 18.234 1.00 12.59 C ANISOU 1782 CD ARG B 246 1621 1617 1546 39 -309 -118 C ATOM 1783 NE ARG B 246 7.003 -11.779 19.324 1.00 14.57 N ANISOU 1783 NE ARG B 246 1873 1836 1826 14 -305 -112 N ATOM 1784 CZ ARG B 246 5.725 -12.121 19.211 1.00 18.60 C ANISOU 1784 CZ ARG B 246 2369 2339 2358 -8 -315 -118 C ATOM 1785 NH1 ARG B 246 5.104 -12.010 18.036 1.00 15.93 N1+ ANISOU 1785 NH1 ARG B 246 2014 2022 2017 -2 -338 -131 N1+ ATOM 1786 NH2 ARG B 246 5.071 -12.596 20.266 1.00 14.81 N ANISOU 1786 NH2 ARG B 246 1894 1832 1903 -39 -301 -115 N ATOM 1787 N PRO B 247 10.526 -9.401 14.768 1.00 14.09 N ANISOU 1787 N PRO B 247 1831 1908 1614 78 -280 -140 N ATOM 1788 CA PRO B 247 11.543 -8.835 13.868 1.00 13.74 C ANISOU 1788 CA PRO B 247 1799 1894 1529 78 -254 -150 C ATOM 1789 C PRO B 247 12.633 -9.839 13.473 1.00 19.02 C ANISOU 1789 C PRO B 247 2467 2572 2188 85 -247 -203 C ATOM 1790 O PRO B 247 12.952 -10.750 14.245 1.00 16.04 O ANISOU 1790 O PRO B 247 2080 2171 1844 96 -258 -226 O ATOM 1791 CB PRO B 247 12.131 -7.674 14.685 1.00 12.59 C ANISOU 1791 CB PRO B 247 1643 1745 1395 76 -220 -126 C ATOM 1792 CG PRO B 247 11.025 -7.271 15.637 1.00 12.05 C ANISOU 1792 CG PRO B 247 1564 1654 1362 75 -234 -92 C ATOM 1793 CD PRO B 247 10.328 -8.583 15.985 1.00 13.16 C ANISOU 1793 CD PRO B 247 1700 1775 1526 75 -264 -109 C ATOM 1794 N ASP B 248 13.172 -9.688 12.265 1.00 15.24 N ANISOU 1794 N ASP B 248 2002 2125 1663 78 -230 -224 N ATOM 1795 CA ASP B 248 14.116 -10.664 11.725 1.00 20.42 C ANISOU 1795 CA ASP B 248 2653 2794 2311 84 -223 -285 C ATOM 1796 C ASP B 248 15.505 -10.522 12.342 1.00 14.75 C ANISOU 1796 C ASP B 248 1911 2077 1615 91 -189 -316 C ATOM 1797 O ASP B 248 16.248 -9.623 11.983 1.00 18.28 O ANISOU 1797 O ASP B 248 2358 2549 2038 77 -147 -318 O ATOM 1798 CB ASP B 248 14.221 -10.488 10.212 1.00 19.38 C ANISOU 1798 CB ASP B 248 2546 2702 2117 67 -209 -301 C ATOM 1799 CG ASP B 248 14.971 -11.622 9.539 1.00 25.17 C ANISOU 1799 CG ASP B 248 3271 3451 2843 72 -206 -372 C ATOM 1800 OD1 ASP B 248 15.561 -12.463 10.245 1.00 25.12 O ANISOU 1800 OD1 ASP B 248 3238 3422 2883 91 -213 -410 O ATOM 1801 OD2 ASP B 248 14.955 -11.664 8.292 1.00 28.91 O1- ANISOU 1801 OD2 ASP B 248 3767 3956 3260 56 -198 -391 O1- ATOM 1802 N VAL B 249 15.852 -11.432 13.247 1.00 19.66 N ANISOU 1802 N VAL B 249 2516 2670 2284 113 -211 -341 N ATOM 1803 CA VAL B 249 17.147 -11.396 13.935 1.00 21.13 C ANISOU 1803 CA VAL B 249 2677 2852 2500 128 -193 -377 C ATOM 1804 C VAL B 249 18.324 -11.570 12.970 1.00 23.63 C ANISOU 1804 C VAL B 249 2976 3203 2800 125 -160 -445 C ATOM 1805 O VAL B 249 19.392 -10.967 13.145 1.00 26.25 O ANISOU 1805 O VAL B 249 3283 3550 3139 123 -123 -471 O ATOM 1806 CB VAL B 249 17.193 -12.455 15.053 1.00 23.01 C ANISOU 1806 CB VAL B 249 2911 3045 2787 155 -236 -389 C ATOM 1807 CG1 VAL B 249 18.618 -12.649 15.582 1.00 29.04 C ANISOU 1807 CG1 VAL B 249 3647 3805 3584 179 -232 -442 C ATOM 1808 CG2 VAL B 249 16.240 -12.052 16.179 1.00 17.63 C ANISOU 1808 CG2 VAL B 249 2244 2334 2120 149 -251 -326 C ATOM 1809 N ASP B 250 18.117 -12.365 11.924 1.00 32.17 N ANISOU 1809 N ASP B 250 4068 4299 3858 122 -170 -478 N ATOM 1810 CA ASP B 250 19.166 -12.578 10.928 1.00 36.15 C ANISOU 1810 CA ASP B 250 4554 4840 4341 114 -134 -549 C ATOM 1811 C ASP B 250 19.427 -11.298 10.145 1.00 37.58 C ANISOU 1811 C ASP B 250 4751 5063 4466 76 -75 -531 C ATOM 1812 O ASP B 250 20.488 -11.134 9.535 1.00 39.66 O ANISOU 1812 O ASP B 250 4996 5359 4714 60 -25 -587 O ATOM 1813 CB ASP B 250 18.802 -13.739 9.990 1.00 36.52 C ANISOU 1813 CB ASP B 250 4612 4892 4373 118 -159 -591 C ATOM 1814 CG ASP B 250 18.671 -15.056 10.728 1.00 43.62 C ANISOU 1814 CG ASP B 250 5500 5743 5330 153 -215 -615 C ATOM 1815 OD1 ASP B 250 19.518 -15.327 11.611 1.00 52.22 O ANISOU 1815 OD1 ASP B 250 6563 6808 6470 180 -225 -644 O ATOM 1816 OD2 ASP B 250 17.713 -15.810 10.446 1.00 48.02 O1- ANISOU 1816 OD2 ASP B 250 6077 6283 5883 154 -253 -604 O1- ATOM 1817 N ASP B 251 18.472 -10.374 10.200 1.00 27.94 N ANISOU 1817 N ASP B 251 3562 3837 3218 61 -78 -454 N ATOM 1818 CA ASP B 251 18.570 -9.133 9.445 1.00 33.80 C ANISOU 1818 CA ASP B 251 4332 4609 3903 24 -31 -424 C ATOM 1819 C ASP B 251 19.412 -8.073 10.155 1.00 35.54 C ANISOU 1819 C ASP B 251 4531 4828 4145 14 13 -416 C ATOM 1820 O ASP B 251 19.576 -6.966 9.646 1.00 39.77 O ANISOU 1820 O ASP B 251 5091 5380 4638 -19 56 -389 O ATOM 1821 CB ASP B 251 17.173 -8.587 9.135 1.00 31.73 C ANISOU 1821 CB ASP B 251 4114 4338 3606 17 -64 -350 C ATOM 1822 CG ASP B 251 17.181 -7.556 8.033 1.00 39.46 C ANISOU 1822 CG ASP B 251 5139 5345 4511 -20 -28 -322 C ATOM 1823 OD1 ASP B 251 17.880 -7.778 7.014 1.00 35.41 O ANISOU 1823 OD1 ASP B 251 4638 4866 3950 -44 9 -369 O ATOM 1824 OD2 ASP B 251 16.490 -6.524 8.190 1.00 34.20 O1- ANISOU 1824 OD2 ASP B 251 4499 4663 3833 -26 -38 -255 O1- ATOM 1825 N ILE B 252 19.940 -8.398 11.332 1.00 30.75 N ANISOU 1825 N ILE B 252 3884 4198 3602 42 -1 -439 N ATOM 1826 CA ILE B 252 20.920 -7.512 11.955 1.00 32.70 C ANISOU 1826 CA ILE B 252 4102 4448 3874 34 41 -451 C ATOM 1827 C ILE B 252 22.291 -7.741 11.302 1.00 36.54 C ANISOU 1827 C ILE B 252 4556 4969 4358 20 92 -538 C ATOM 1828 O ILE B 252 22.794 -8.866 11.284 1.00 36.09 O ANISOU 1828 O ILE B 252 4468 4912 4331 45 72 -605 O ATOM 1829 CB ILE B 252 20.982 -7.717 13.492 1.00 25.45 C ANISOU 1829 CB ILE B 252 3155 3493 3021 70 4 -444 C ATOM 1830 CG1 ILE B 252 19.676 -7.225 14.127 1.00 23.56 C ANISOU 1830 CG1 ILE B 252 2944 3227 2780 72 -28 -361 C ATOM 1831 CG2 ILE B 252 22.155 -6.948 14.099 1.00 25.79 C ANISOU 1831 CG2 ILE B 252 3160 3543 3095 65 43 -475 C ATOM 1832 CD1 ILE B 252 19.431 -7.758 15.519 1.00 23.34 C ANISOU 1832 CD1 ILE B 252 2904 3162 2802 103 -73 -352 C ATOM 1833 N THR B 253 22.862 -6.671 10.745 1.00 34.15 N ANISOU 1833 N THR B 253 4262 4693 4023 -23 159 -538 N ATOM 1834 CA THR B 253 24.167 -6.711 10.073 1.00 41.96 C ANISOU 1834 CA THR B 253 5218 5720 5007 -50 223 -624 C ATOM 1835 C THR B 253 25.295 -6.655 11.085 1.00 40.42 C ANISOU 1835 C THR B 253 4956 5518 4885 -29 233 -682 C ATOM 1836 O THR B 253 26.255 -7.429 11.019 1.00 39.58 O ANISOU 1836 O THR B 253 4798 5425 4816 -13 239 -774 O ATOM 1837 CB THR B 253 24.372 -5.477 9.178 1.00 39.85 C ANISOU 1837 CB THR B 253 4989 5477 4673 -112 298 -598 C ATOM 1838 CG2 THR B 253 25.614 -5.645 8.302 1.00 43.80 C ANISOU 1838 CG2 THR B 253 5462 6023 5158 -150 372 -693 C ATOM 1839 OG1 THR B 253 23.219 -5.267 8.360 1.00 46.01 O ANISOU 1839 OG1 THR B 253 5842 6257 5382 -129 278 -527 O ATOM 1840 N GLU B 254 25.179 -5.693 11.997 1.00 35.74 N ANISOU 1840 N GLU B 254 4363 4903 4314 -29 233 -631 N ATOM 1841 CA GLU B 254 26.162 -5.480 13.046 1.00 35.58 C ANISOU 1841 CA GLU B 254 4283 4874 4361 -10 236 -678 C ATOM 1842 C GLU B 254 26.303 -6.689 13.935 1.00 34.54 C ANISOU 1842 C GLU B 254 4118 4717 4289 51 164 -716 C ATOM 1843 O GLU B 254 25.388 -7.508 14.072 1.00 30.76 O ANISOU 1843 O GLU B 254 3669 4215 3804 79 105 -681 O ATOM 1844 CB GLU B 254 25.737 -4.324 13.954 1.00 36.00 C ANISOU 1844 CB GLU B 254 4352 4903 4425 -15 234 -605 C ATOM 1845 CG GLU B 254 26.106 -2.944 13.463 1.00 41.59 C ANISOU 1845 CG GLU B 254 5073 5627 5103 -72 311 -588 C ATOM 1846 CD GLU B 254 25.525 -1.864 14.346 1.00 37.40 C ANISOU 1846 CD GLU B 254 4560 5066 4584 -72 299 -514 C ATOM 1847 OE1 GLU B 254 25.565 -2.014 15.596 1.00 36.10 O ANISOU 1847 OE1 GLU B 254 4364 4879 4472 -33 256 -517 O ATOM 1848 OE2 GLU B 254 25.016 -0.867 13.789 1.00 36.76 O1- ANISOU 1848 OE2 GLU B 254 4527 4981 4458 -110 331 -453 O1- ATOM 1849 N TYR B 255 27.454 -6.770 14.576 1.00 28.15 N ANISOU 1849 N TYR B 255 3247 3909 3539 71 166 -790 N ATOM 1850 CA TYR B 255 27.624 -7.688 15.672 1.00 30.60 C ANISOU 1850 CA TYR B 255 3534 4185 3908 132 88 -815 C ATOM 1851 C TYR B 255 26.596 -7.309 16.736 1.00 24.81 C ANISOU 1851 C TYR B 255 2842 3415 3169 146 44 -720 C ATOM 1852 O TYR B 255 26.478 -6.143 17.101 1.00 27.53 O ANISOU 1852 O TYR B 255 3193 3762 3506 121 75 -676 O ATOM 1853 CB TYR B 255 29.044 -7.560 16.225 1.00 30.87 C ANISOU 1853 CB TYR B 255 3495 4228 4007 150 98 -907 C ATOM 1854 CG TYR B 255 29.229 -8.213 17.564 1.00 29.84 C ANISOU 1854 CG TYR B 255 3350 4056 3933 212 12 -918 C ATOM 1855 CD1 TYR B 255 29.338 -7.449 18.723 1.00 33.21 C ANISOU 1855 CD1 TYR B 255 3770 4466 4382 221 -3 -889 C ATOM 1856 CD2 TYR B 255 29.270 -9.594 17.677 1.00 30.30 C ANISOU 1856 CD2 TYR B 255 3406 4088 4019 261 -57 -956 C ATOM 1857 CE1 TYR B 255 29.507 -8.049 19.954 1.00 30.42 C ANISOU 1857 CE1 TYR B 255 3414 4075 4071 277 -85 -897 C ATOM 1858 CE2 TYR B 255 29.433 -10.202 18.894 1.00 32.80 C ANISOU 1858 CE2 TYR B 255 3721 4360 4380 317 -140 -961 C ATOM 1859 CZ TYR B 255 29.553 -9.429 20.029 1.00 29.41 C ANISOU 1859 CZ TYR B 255 3291 3919 3965 324 -154 -931 C ATOM 1860 OH TYR B 255 29.713 -10.060 21.241 1.00 36.78 O ANISOU 1860 OH TYR B 255 4233 4807 4933 378 -241 -932 O ATOM 1861 N CYS B 256 25.827 -8.290 17.184 1.00 26.77 N ANISOU 1861 N CYS B 256 3120 3630 3422 180 -24 -689 N ATOM 1862 CA CYS B 256 24.970 -8.120 18.351 1.00 23.39 C ANISOU 1862 CA CYS B 256 2725 3165 2997 195 -69 -615 C ATOM 1863 C CYS B 256 25.251 -9.264 19.307 1.00 29.05 C ANISOU 1863 C CYS B 256 3438 3844 3757 247 -144 -644 C ATOM 1864 O CYS B 256 25.122 -10.435 18.940 1.00 29.28 O ANISOU 1864 O CYS B 256 3477 3857 3791 268 -181 -669 O ATOM 1865 CB CYS B 256 23.489 -8.087 17.956 1.00 25.49 C ANISOU 1865 CB CYS B 256 3045 3423 3216 174 -73 -533 C ATOM 1866 SG CYS B 256 22.333 -7.889 19.349 1.00 21.49 S ANISOU 1866 SG CYS B 256 2576 2876 2714 184 -117 -450 S ATOM 1867 N PRO B 257 25.663 -8.930 20.536 1.00 21.79 N ANISOU 1867 N PRO B 257 2507 2905 2867 269 -170 -644 N ATOM 1868 CA PRO B 257 25.974 -9.954 21.537 1.00 23.33 C ANISOU 1868 CA PRO B 257 2709 3058 3097 320 -250 -667 C ATOM 1869 C PRO B 257 24.854 -10.977 21.625 1.00 24.58 C ANISOU 1869 C PRO B 257 2925 3178 3235 327 -296 -615 C ATOM 1870 O PRO B 257 23.678 -10.606 21.577 1.00 20.72 O ANISOU 1870 O PRO B 257 2474 2689 2708 296 -277 -542 O ATOM 1871 CB PRO B 257 26.064 -9.151 22.834 1.00 23.68 C ANISOU 1871 CB PRO B 257 2757 3091 3151 325 -262 -637 C ATOM 1872 CG PRO B 257 26.515 -7.784 22.388 1.00 21.27 C ANISOU 1872 CG PRO B 257 2411 2828 2842 288 -186 -649 C ATOM 1873 CD PRO B 257 25.850 -7.560 21.052 1.00 19.67 C ANISOU 1873 CD PRO B 257 2224 2651 2598 246 -130 -621 C ATOM 1874 N ARG B 258 25.194 -12.256 21.715 1.00 23.99 N ANISOU 1874 N ARG B 258 2856 3071 3187 366 -356 -657 N ATOM 1875 CA ARG B 258 24.151 -13.263 21.805 1.00 27.40 C ANISOU 1875 CA ARG B 258 3346 3463 3603 368 -398 -610 C ATOM 1876 C ARG B 258 23.258 -13.048 23.022 1.00 23.67 C ANISOU 1876 C ARG B 258 2926 2957 3108 358 -421 -530 C ATOM 1877 O ARG B 258 22.074 -13.390 22.986 1.00 22.52 O ANISOU 1877 O ARG B 258 2826 2795 2937 335 -423 -474 O ATOM 1878 CB ARG B 258 24.752 -14.661 21.833 1.00 33.43 C ANISOU 1878 CB ARG B 258 4110 4186 4406 415 -466 -669 C ATOM 1879 CG ARG B 258 25.860 -14.815 22.840 1.00 40.15 C ANISOU 1879 CG ARG B 258 4943 5011 5300 464 -522 -716 C ATOM 1880 CD ARG B 258 25.971 -16.263 23.270 1.00 50.93 C ANISOU 1880 CD ARG B 258 6347 6311 6694 510 -611 -734 C ATOM 1881 NE ARG B 258 27.349 -16.741 23.267 1.00 63.04 N ANISOU 1881 NE ARG B 258 7827 7837 8287 563 -656 -831 N ATOM 1882 CZ ARG B 258 27.680 -18.024 23.167 1.00 64.98 C ANISOU 1882 CZ ARG B 258 8076 8049 8563 593 -718 -853 C ATOM 1883 NH1 ARG B 258 26.728 -18.945 23.058 1.00 58.15 N1+ ANISOU 1883 NH1 ARG B 258 7276 7135 7682 591 -748 -816 N1+ ATOM 1884 NH2 ARG B 258 28.956 -18.387 23.174 1.00 66.98 N ANISOU 1884 NH2 ARG B 258 8269 8318 8864 620 -753 -916 N ATOM 1885 N GLU B 259 23.825 -12.492 24.096 1.00 19.98 N ANISOU 1885 N GLU B 259 2454 2484 2654 374 -436 -531 N ATOM 1886 CA GLU B 259 23.054 -12.176 25.300 1.00 21.27 C ANISOU 1886 CA GLU B 259 2666 2623 2793 360 -450 -462 C ATOM 1887 C GLU B 259 21.900 -11.238 24.994 1.00 18.55 C ANISOU 1887 C GLU B 259 2329 2305 2413 310 -388 -399 C ATOM 1888 O GLU B 259 20.814 -11.350 25.581 1.00 19.78 O ANISOU 1888 O GLU B 259 2531 2440 2546 288 -393 -340 O ATOM 1889 CB GLU B 259 23.936 -11.492 26.350 1.00 25.89 C ANISOU 1889 CB GLU B 259 3233 3209 3393 381 -466 -482 C ATOM 1890 CG GLU B 259 24.951 -12.418 27.005 1.00 25.47 C ANISOU 1890 CG GLU B 259 3186 3118 3375 437 -547 -534 C ATOM 1891 CD GLU B 259 26.227 -12.529 26.197 1.00 30.40 C ANISOU 1891 CD GLU B 259 3737 3766 4047 467 -546 -629 C ATOM 1892 OE1 GLU B 259 27.208 -13.122 26.704 1.00 41.10 O ANISOU 1892 OE1 GLU B 259 5080 5095 5441 519 -614 -687 O ATOM 1893 OE2 GLU B 259 26.254 -12.007 25.061 1.00 30.99 O1- ANISOU 1893 OE2 GLU B 259 3768 3888 4121 438 -478 -649 O1- ATOM 1894 N ILE B 260 22.154 -10.292 24.099 1.00 18.48 N ANISOU 1894 N ILE B 260 2275 2343 2402 291 -330 -415 N ATOM 1895 CA ILE B 260 21.136 -9.308 23.752 1.00 18.74 C ANISOU 1895 CA ILE B 260 2314 2399 2407 249 -277 -360 C ATOM 1896 C ILE B 260 20.087 -9.924 22.802 1.00 20.59 C ANISOU 1896 C ILE B 260 2571 2633 2620 230 -274 -335 C ATOM 1897 O ILE B 260 18.894 -9.663 22.943 1.00 13.93 O ANISOU 1897 O ILE B 260 1752 1784 1758 205 -264 -281 O ATOM 1898 CB ILE B 260 21.758 -7.991 23.226 1.00 17.61 C ANISOU 1898 CB ILE B 260 2126 2298 2266 232 -219 -378 C ATOM 1899 CG1 ILE B 260 22.524 -7.280 24.363 1.00 15.84 C ANISOU 1899 CG1 ILE B 260 1883 2073 2064 244 -223 -393 C ATOM 1900 CG2 ILE B 260 20.683 -7.069 22.697 1.00 17.39 C ANISOU 1900 CG2 ILE B 260 2110 2287 2210 194 -175 -322 C ATOM 1901 CD1 ILE B 260 23.337 -6.028 23.927 1.00 16.28 C ANISOU 1901 CD1 ILE B 260 1891 2164 2130 227 -166 -422 C ATOM 1902 N ILE B 261 20.515 -10.782 21.876 1.00 18.08 N ANISOU 1902 N ILE B 261 2242 2318 2308 244 -286 -380 N ATOM 1903 CA ILE B 261 19.539 -11.572 21.102 1.00 15.59 C ANISOU 1903 CA ILE B 261 1953 1995 1976 231 -296 -363 C ATOM 1904 C ILE B 261 18.605 -12.388 22.022 1.00 15.64 C ANISOU 1904 C ILE B 261 2006 1953 1983 230 -338 -321 C ATOM 1905 O ILE B 261 17.362 -12.379 21.869 1.00 15.68 O ANISOU 1905 O ILE B 261 2032 1955 1971 203 -328 -278 O ATOM 1906 CB ILE B 261 20.248 -12.491 20.072 1.00 19.66 C ANISOU 1906 CB ILE B 261 2449 2517 2502 250 -307 -428 C ATOM 1907 CG1 ILE B 261 21.060 -11.633 19.095 1.00 24.07 C ANISOU 1907 CG1 ILE B 261 2966 3128 3052 238 -252 -468 C ATOM 1908 CG2 ILE B 261 19.232 -13.319 19.303 1.00 19.11 C ANISOU 1908 CG2 ILE B 261 2406 2439 2416 237 -320 -414 C ATOM 1909 CD1 ILE B 261 21.837 -12.423 18.049 1.00 34.76 C ANISOU 1909 CD1 ILE B 261 4295 4498 4414 251 -251 -543 C ATOM 1910 N SER B 262 19.201 -13.088 22.991 1.00 16.92 N ANISOU 1910 N SER B 262 2187 2077 2165 259 -384 -337 N ATOM 1911 CA SER B 262 18.426 -13.864 23.946 1.00 17.57 C ANISOU 1911 CA SER B 262 2325 2109 2243 252 -421 -297 C ATOM 1912 C SER B 262 17.479 -12.961 24.703 1.00 14.36 C ANISOU 1912 C SER B 262 1932 1708 1814 218 -390 -239 C ATOM 1913 O SER B 262 16.326 -13.324 24.948 1.00 16.77 O ANISOU 1913 O SER B 262 2271 1994 2108 189 -388 -200 O ATOM 1914 CB SER B 262 19.341 -14.593 24.939 1.00 22.52 C ANISOU 1914 CB SER B 262 2977 2691 2889 291 -481 -321 C ATOM 1915 OG SER B 262 20.073 -15.599 24.268 1.00 24.55 O ANISOU 1915 OG SER B 262 3222 2933 3173 325 -518 -378 O ATOM 1916 N LEU B 263 17.975 -11.792 25.099 1.00 14.66 N ANISOU 1916 N LEU B 263 1944 1775 1852 219 -363 -239 N ATOM 1917 CA LEU B 263 17.137 -10.879 25.879 1.00 16.50 C ANISOU 1917 CA LEU B 263 2185 2013 2069 188 -333 -191 C ATOM 1918 C LEU B 263 15.929 -10.414 25.072 1.00 13.03 C ANISOU 1918 C LEU B 263 1734 1597 1620 155 -295 -162 C ATOM 1919 O LEU B 263 14.794 -10.421 25.570 1.00 13.53 O ANISOU 1919 O LEU B 263 1818 1647 1675 127 -286 -126 O ATOM 1920 CB LEU B 263 17.947 -9.675 26.357 1.00 14.00 C ANISOU 1920 CB LEU B 263 1837 1722 1758 197 -311 -202 C ATOM 1921 CG LEU B 263 17.157 -8.626 27.145 1.00 15.28 C ANISOU 1921 CG LEU B 263 2003 1894 1909 168 -277 -161 C ATOM 1922 CD1 LEU B 263 16.518 -9.228 28.402 1.00 17.46 C ANISOU 1922 CD1 LEU B 263 2332 2133 2168 154 -300 -131 C ATOM 1923 CD2 LEU B 263 18.076 -7.476 27.529 1.00 15.70 C ANISOU 1923 CD2 LEU B 263 2023 1971 1974 179 -258 -181 C ATOM 1924 N MET B 264 16.149 -10.018 23.819 1.00 14.34 N ANISOU 1924 N MET B 264 1867 1796 1786 158 -273 -180 N ATOM 1925 CA MET B 264 15.001 -9.553 23.057 1.00 13.92 C ANISOU 1925 CA MET B 264 1807 1761 1723 131 -249 -152 C ATOM 1926 C MET B 264 14.011 -10.696 22.879 1.00 13.84 C ANISOU 1926 C MET B 264 1823 1725 1711 119 -273 -143 C ATOM 1927 O MET B 264 12.801 -10.485 23.010 1.00 13.97 O ANISOU 1927 O MET B 264 1842 1739 1727 93 -262 -114 O ATOM 1928 CB MET B 264 15.379 -8.862 21.730 1.00 16.72 C ANISOU 1928 CB MET B 264 2134 2154 2067 132 -222 -168 C ATOM 1929 CG MET B 264 16.122 -9.715 20.713 1.00 17.96 C ANISOU 1929 CG MET B 264 2285 2319 2219 148 -235 -213 C ATOM 1930 SD MET B 264 16.600 -8.758 19.245 1.00 17.89 S ANISOU 1930 SD MET B 264 2255 2358 2186 137 -192 -228 S ATOM 1931 CE MET B 264 18.001 -7.840 19.854 1.00 17.71 C ANISOU 1931 CE MET B 264 2203 2347 2179 146 -163 -253 C ATOM 1932 N LYS B 265 14.502 -11.911 22.640 1.00 12.20 N ANISOU 1932 N LYS B 265 1631 1496 1509 137 -306 -173 N ATOM 1933 CA LYS B 265 13.565 -13.036 22.551 1.00 15.11 C ANISOU 1933 CA LYS B 265 2027 1834 1880 121 -329 -165 C ATOM 1934 C LYS B 265 12.765 -13.270 23.843 1.00 16.39 C ANISOU 1934 C LYS B 265 2224 1961 2043 96 -332 -130 C ATOM 1935 O LYS B 265 11.557 -13.559 23.793 1.00 17.32 O ANISOU 1935 O LYS B 265 2350 2069 2162 65 -324 -112 O ATOM 1936 CB LYS B 265 14.284 -14.311 22.100 1.00 15.50 C ANISOU 1936 CB LYS B 265 2090 1861 1940 147 -368 -206 C ATOM 1937 CG LYS B 265 14.750 -14.226 20.658 1.00 19.39 C ANISOU 1937 CG LYS B 265 2549 2390 2427 160 -358 -244 C ATOM 1938 CD LYS B 265 15.534 -15.483 20.280 1.00 24.31 C ANISOU 1938 CD LYS B 265 3179 2990 3067 188 -395 -295 C ATOM 1939 CE LYS B 265 16.141 -15.368 18.898 1.00 30.15 C ANISOU 1939 CE LYS B 265 3885 3772 3798 198 -378 -343 C ATOM 1940 NZ LYS B 265 16.800 -16.651 18.513 1.00 37.31 N1+ ANISOU 1940 NZ LYS B 265 4793 4654 4727 226 -415 -400 N1+ ATOM 1941 N LEU B 266 13.420 -13.142 24.998 1.00 13.79 N ANISOU 1941 N LEU B 266 1917 1614 1711 106 -340 -123 N ATOM 1942 CA LEU B 266 12.713 -13.244 26.273 1.00 17.74 C ANISOU 1942 CA LEU B 266 2455 2085 2200 76 -335 -89 C ATOM 1943 C LEU B 266 11.629 -12.180 26.404 1.00 14.72 C ANISOU 1943 C LEU B 266 2046 1731 1817 41 -288 -65 C ATOM 1944 O LEU B 266 10.501 -12.448 26.876 1.00 15.82 O ANISOU 1944 O LEU B 266 2203 1854 1955 3 -273 -46 O ATOM 1945 CB LEU B 266 13.691 -13.080 27.439 1.00 19.93 C ANISOU 1945 CB LEU B 266 2758 2346 2468 96 -354 -88 C ATOM 1946 CG LEU B 266 14.590 -14.273 27.727 1.00 29.76 C ANISOU 1946 CG LEU B 266 4045 3545 3716 127 -412 -107 C ATOM 1947 CD1 LEU B 266 15.386 -14.039 29.000 1.00 31.51 C ANISOU 1947 CD1 LEU B 266 4298 3751 3924 145 -436 -102 C ATOM 1948 CD2 LEU B 266 13.712 -15.493 27.851 1.00 31.93 C ANISOU 1948 CD2 LEU B 266 4373 3773 3986 99 -429 -89 C ATOM 1949 N CYS B 267 11.964 -10.975 25.965 1.00 13.96 N ANISOU 1949 N CYS B 267 1906 1675 1725 55 -265 -70 N ATOM 1950 CA CYS B 267 11.077 -9.852 26.191 1.00 12.02 C ANISOU 1950 CA CYS B 267 1634 1452 1484 30 -228 -50 C ATOM 1951 C CYS B 267 9.941 -9.796 25.190 1.00 16.33 C ANISOU 1951 C CYS B 267 2153 2011 2040 14 -220 -48 C ATOM 1952 O CYS B 267 8.934 -9.177 25.483 1.00 12.00 O ANISOU 1952 O CYS B 267 1587 1470 1504 -10 -196 -36 O ATOM 1953 CB CYS B 267 11.858 -8.531 26.212 1.00 12.69 C ANISOU 1953 CB CYS B 267 1686 1565 1569 49 -208 -53 C ATOM 1954 SG CYS B 267 12.910 -8.393 27.649 1.00 13.33 S ANISOU 1954 SG CYS B 267 1791 1632 1640 62 -216 -57 S ATOM 1955 N TRP B 268 10.080 -10.447 24.029 1.00 11.68 N ANISOU 1955 N TRP B 268 1562 1426 1451 28 -241 -65 N ATOM 1956 CA TRP B 268 8.956 -10.459 23.082 1.00 14.99 C ANISOU 1956 CA TRP B 268 1960 1857 1879 14 -242 -66 C ATOM 1957 C TRP B 268 8.157 -11.770 23.023 1.00 16.06 C ANISOU 1957 C TRP B 268 2115 1965 2023 -7 -260 -74 C ATOM 1958 O TRP B 268 7.391 -12.019 22.077 1.00 15.25 O ANISOU 1958 O TRP B 268 1996 1871 1928 -13 -271 -85 O ATOM 1959 CB TRP B 268 9.375 -9.951 21.697 1.00 13.18 C ANISOU 1959 CB TRP B 268 1710 1660 1638 37 -248 -76 C ATOM 1960 CG TRP B 268 10.280 -10.817 20.852 1.00 16.08 C ANISOU 1960 CG TRP B 268 2089 2029 1992 58 -269 -104 C ATOM 1961 CD1 TRP B 268 10.268 -12.193 20.721 1.00 16.53 C ANISOU 1961 CD1 TRP B 268 2168 2060 2053 58 -296 -124 C ATOM 1962 CD2 TRP B 268 11.290 -10.337 19.955 1.00 14.52 C ANISOU 1962 CD2 TRP B 268 1881 1860 1776 79 -262 -120 C ATOM 1963 CE2 TRP B 268 11.871 -11.466 19.328 1.00 17.44 C ANISOU 1963 CE2 TRP B 268 2263 2224 2141 92 -284 -155 C ATOM 1964 CE3 TRP B 268 11.776 -9.061 19.642 1.00 13.82 C ANISOU 1964 CE3 TRP B 268 1776 1798 1675 83 -236 -111 C ATOM 1965 NE1 TRP B 268 11.234 -12.582 19.805 1.00 17.12 N ANISOU 1965 NE1 TRP B 268 2241 2148 2116 82 -307 -156 N ATOM 1966 CZ2 TRP B 268 12.910 -11.344 18.384 1.00 13.50 C ANISOU 1966 CZ2 TRP B 268 1754 1752 1624 109 -276 -186 C ATOM 1967 CZ3 TRP B 268 12.814 -8.942 18.711 1.00 14.50 C ANISOU 1967 CZ3 TRP B 268 1859 1909 1741 96 -227 -136 C ATOM 1968 CH2 TRP B 268 13.367 -10.081 18.097 1.00 14.76 C ANISOU 1968 CH2 TRP B 268 1900 1941 1769 107 -245 -176 C ATOM 1969 N GLU B 269 8.315 -12.574 24.068 1.00 13.34 N ANISOU 1969 N GLU B 269 1809 1583 1675 -21 -264 -68 N ATOM 1970 CA GLU B 269 7.577 -13.830 24.224 1.00 18.26 C ANISOU 1970 CA GLU B 269 2462 2170 2307 -50 -275 -72 C ATOM 1971 C GLU B 269 6.069 -13.584 24.134 1.00 16.62 C ANISOU 1971 C GLU B 269 2224 1972 2121 -89 -252 -73 C ATOM 1972 O GLU B 269 5.564 -12.617 24.680 1.00 14.68 O ANISOU 1972 O GLU B 269 1954 1743 1882 -103 -222 -62 O ATOM 1973 CB GLU B 269 7.941 -14.464 25.577 1.00 17.02 C ANISOU 1973 CB GLU B 269 2360 1968 2136 -65 -278 -56 C ATOM 1974 CG GLU B 269 7.467 -15.904 25.782 1.00 22.43 C ANISOU 1974 CG GLU B 269 3093 2604 2826 -94 -295 -57 C ATOM 1975 CD GLU B 269 7.967 -16.869 24.708 1.00 18.72 C ANISOU 1975 CD GLU B 269 2626 2120 2365 -64 -336 -84 C ATOM 1976 OE1 GLU B 269 9.197 -16.946 24.467 1.00 25.35 O ANISOU 1976 OE1 GLU B 269 3472 2962 3200 -19 -364 -98 O ATOM 1977 OE2 GLU B 269 7.110 -17.540 24.089 1.00 26.58 O1- ANISOU 1977 OE2 GLU B 269 3615 3106 3378 -87 -339 -98 O1- ATOM 1978 N ALA B 270 5.347 -14.451 23.430 1.00 18.37 N ANISOU 1978 N ALA B 270 2441 2182 2357 -103 -268 -91 N ATOM 1979 CA ALA B 270 3.896 -14.294 23.289 1.00 20.83 C ANISOU 1979 CA ALA B 270 2716 2503 2697 -139 -250 -102 C ATOM 1980 C ALA B 270 3.151 -14.175 24.629 1.00 14.83 C ANISOU 1980 C ALA B 270 1964 1725 1945 -188 -208 -92 C ATOM 1981 O ALA B 270 2.373 -13.236 24.818 1.00 18.89 O ANISOU 1981 O ALA B 270 2434 2264 2479 -201 -183 -97 O ATOM 1982 CB ALA B 270 3.313 -15.433 22.431 1.00 20.95 C ANISOU 1982 CB ALA B 270 2731 2502 2728 -150 -275 -128 C ATOM 1983 N ASN B 271 3.381 -15.117 25.537 1.00 18.25 N ANISOU 1983 N ASN B 271 2457 2115 2364 -216 -202 -79 N ATOM 1984 CA ASN B 271 2.797 -15.076 26.881 1.00 18.66 C ANISOU 1984 CA ASN B 271 2531 2149 2410 -269 -158 -67 C ATOM 1985 C ASN B 271 3.331 -13.880 27.653 1.00 17.46 C ANISOU 1985 C ASN B 271 2373 2021 2240 -253 -137 -50 C ATOM 1986 O ASN B 271 4.512 -13.862 28.012 1.00 16.04 O ANISOU 1986 O ASN B 271 2232 1832 2031 -222 -157 -32 O ATOM 1987 CB ASN B 271 3.148 -16.368 27.637 1.00 19.33 C ANISOU 1987 CB ASN B 271 2700 2176 2471 -296 -166 -50 C ATOM 1988 CG ASN B 271 2.591 -16.405 29.063 1.00 21.19 C ANISOU 1988 CG ASN B 271 2975 2389 2687 -359 -117 -34 C ATOM 1989 ND2 ASN B 271 2.917 -17.466 29.798 1.00 24.20 N ANISOU 1989 ND2 ASN B 271 3442 2714 3038 -385 -126 -12 N ATOM 1990 OD1 ASN B 271 1.877 -15.499 29.496 1.00 21.53 O ANISOU 1990 OD1 ASN B 271 2976 2464 2741 -385 -72 -44 O ATOM 1991 N PRO B 272 2.470 -12.883 27.923 1.00 18.10 N ANISOU 1991 N PRO B 272 2403 2132 2343 -273 -99 -61 N ATOM 1992 CA PRO B 272 2.993 -11.678 28.573 1.00 18.42 C ANISOU 1992 CA PRO B 272 2432 2195 2370 -255 -81 -49 C ATOM 1993 C PRO B 272 3.574 -11.990 29.945 1.00 20.73 C ANISOU 1993 C PRO B 272 2794 2463 2622 -278 -65 -27 C ATOM 1994 O PRO B 272 4.574 -11.387 30.336 1.00 16.98 O ANISOU 1994 O PRO B 272 2331 1996 2124 -245 -75 -13 O ATOM 1995 CB PRO B 272 1.752 -10.782 28.706 1.00 18.75 C ANISOU 1995 CB PRO B 272 2409 2264 2451 -282 -43 -74 C ATOM 1996 CG PRO B 272 0.810 -11.267 27.630 1.00 21.89 C ANISOU 1996 CG PRO B 272 2766 2664 2886 -288 -60 -100 C ATOM 1997 CD PRO B 272 1.031 -12.763 27.613 1.00 20.95 C ANISOU 1997 CD PRO B 272 2707 2506 2747 -309 -76 -93 C ATOM 1998 N GLU B 273 2.968 -12.931 30.664 1.00 18.97 N ANISOU 1998 N GLU B 273 2617 2205 2386 -335 -43 -24 N ATOM 1999 CA GLU B 273 3.450 -13.253 32.008 1.00 18.62 C ANISOU 1999 CA GLU B 273 2651 2132 2293 -361 -30 2 C ATOM 2000 C GLU B 273 4.787 -13.988 32.026 1.00 18.72 C ANISOU 2000 C GLU B 273 2730 2111 2273 -319 -88 25 C ATOM 2001 O GLU B 273 5.403 -14.129 33.084 1.00 24.55 O ANISOU 2001 O GLU B 273 3534 2826 2967 -324 -94 48 O ATOM 2002 CB GLU B 273 2.403 -14.032 32.807 1.00 21.07 C ANISOU 2002 CB GLU B 273 3001 2412 2592 -443 16 0 C ATOM 2003 CG GLU B 273 1.305 -13.161 33.390 1.00 29.42 C ANISOU 2003 CG GLU B 273 4008 3503 3669 -492 84 -26 C ATOM 2004 CD GLU B 273 0.558 -12.380 32.328 1.00 34.01 C ANISOU 2004 CD GLU B 273 4483 4126 4314 -469 87 -63 C ATOM 2005 OE1 GLU B 273 0.092 -12.995 31.340 1.00 29.35 O ANISOU 2005 OE1 GLU B 273 3867 3528 3756 -466 65 -78 O ATOM 2006 OE2 GLU B 273 0.451 -11.144 32.467 1.00 37.59 O1- ANISOU 2006 OE2 GLU B 273 4881 4616 4784 -452 105 -77 O1- ATOM 2007 N ALA B 274 5.240 -14.453 30.869 1.00 17.26 N ANISOU 2007 N ALA B 274 2527 1922 2108 -275 -133 17 N ATOM 2008 CA ALA B 274 6.565 -15.068 30.765 1.00 21.56 C ANISOU 2008 CA ALA B 274 3120 2439 2634 -226 -191 27 C ATOM 2009 C ALA B 274 7.662 -14.036 30.500 1.00 17.22 C ANISOU 2009 C ALA B 274 2532 1927 2085 -166 -208 20 C ATOM 2010 O ALA B 274 8.852 -14.341 30.625 1.00 19.22 O ANISOU 2010 O ALA B 274 2816 2162 2323 -125 -252 22 O ATOM 2011 CB ALA B 274 6.581 -16.151 29.690 1.00 20.82 C ANISOU 2011 CB ALA B 274 3028 2321 2562 -211 -228 13 C ATOM 2012 N ARG B 275 7.270 -12.811 30.152 1.00 14.05 N ANISOU 2012 N ARG B 275 2062 1574 1703 -163 -176 10 N ATOM 2013 CA ARG B 275 8.266 -11.758 29.921 1.00 13.63 C ANISOU 2013 CA ARG B 275 1974 1555 1652 -115 -185 5 C ATOM 2014 C ARG B 275 8.820 -11.289 31.257 1.00 14.90 C ANISOU 2014 C ARG B 275 2168 1711 1783 -118 -176 17 C ATOM 2015 O ARG B 275 8.083 -11.216 32.239 1.00 14.77 O ANISOU 2015 O ARG B 275 2175 1687 1751 -164 -142 27 O ATOM 2016 CB ARG B 275 7.653 -10.574 29.165 1.00 10.90 C ANISOU 2016 CB ARG B 275 1554 1252 1335 -111 -157 -6 C ATOM 2017 CG ARG B 275 7.060 -10.942 27.803 1.00 12.84 C ANISOU 2017 CG ARG B 275 1767 1507 1605 -106 -170 -20 C ATOM 2018 CD ARG B 275 6.278 -9.757 27.198 1.00 11.12 C ANISOU 2018 CD ARG B 275 1485 1325 1414 -105 -148 -27 C ATOM 2019 NE ARG B 275 5.402 -10.222 26.111 1.00 10.96 N ANISOU 2019 NE ARG B 275 1440 1309 1415 -111 -162 -41 N ATOM 2020 CZ ARG B 275 4.221 -9.690 25.803 1.00 11.95 C ANISOU 2020 CZ ARG B 275 1520 1450 1571 -127 -149 -53 C ATOM 2021 NH1 ARG B 275 3.753 -8.623 26.449 1.00 10.57 N1+ ANISOU 2021 NH1 ARG B 275 1314 1289 1412 -138 -118 -54 N1+ ATOM 2022 NH2 ARG B 275 3.500 -10.226 24.831 1.00 14.89 N ANISOU 2022 NH2 ARG B 275 1873 1823 1961 -130 -169 -69 N ATOM 2023 N PRO B 276 10.123 -10.949 31.299 1.00 14.49 N ANISOU 2023 N PRO B 276 2116 1665 1724 -71 -206 11 N ATOM 2024 CA PRO B 276 10.702 -10.527 32.578 1.00 14.35 C ANISOU 2024 CA PRO B 276 2131 1644 1678 -71 -206 18 C ATOM 2025 C PRO B 276 10.212 -9.147 33.025 1.00 17.27 C ANISOU 2025 C PRO B 276 2457 2051 2055 -90 -155 16 C ATOM 2026 O PRO B 276 9.606 -8.431 32.237 1.00 17.21 O ANISOU 2026 O PRO B 276 2389 2071 2078 -92 -129 7 O ATOM 2027 CB PRO B 276 12.205 -10.492 32.280 1.00 18.98 C ANISOU 2027 CB PRO B 276 2711 2232 2269 -12 -252 0 C ATOM 2028 CG PRO B 276 12.303 -10.228 30.795 1.00 14.60 C ANISOU 2028 CG PRO B 276 2095 1705 1749 12 -249 -18 C ATOM 2029 CD PRO B 276 11.118 -10.978 30.207 1.00 17.26 C ANISOU 2029 CD PRO B 276 2438 2029 2093 -20 -239 -9 C ATOM 2030 N THR B 277 10.452 -8.782 34.283 1.00 14.48 N ANISOU 2030 N THR B 277 2136 1695 1671 -103 -146 21 N ATOM 2031 CA THR B 277 10.170 -7.426 34.731 1.00 13.30 C ANISOU 2031 CA THR B 277 1942 1580 1532 -114 -103 11 C ATOM 2032 C THR B 277 11.386 -6.552 34.451 1.00 15.53 C ANISOU 2032 C THR B 277 2187 1883 1828 -64 -122 -5 C ATOM 2033 O THR B 277 12.497 -7.056 34.242 1.00 12.62 O ANISOU 2033 O THR B 277 1837 1502 1455 -25 -168 -11 O ATOM 2034 CB THR B 277 9.915 -7.366 36.230 1.00 15.96 C ANISOU 2034 CB THR B 277 2330 1909 1825 -153 -80 19 C ATOM 2035 CG2 THR B 277 8.814 -8.349 36.622 1.00 22.59 C ANISOU 2035 CG2 THR B 277 3219 2723 2643 -211 -57 34 C ATOM 2036 OG1 THR B 277 11.125 -7.692 36.923 1.00 16.54 O ANISOU 2036 OG1 THR B 277 2457 1964 1863 -123 -128 23 O ATOM 2037 N PHE B 278 11.188 -5.242 34.445 1.00 14.15 N ANISOU 2037 N PHE B 278 1959 1740 1678 -65 -86 -16 N ATOM 2038 CA PHE B 278 12.328 -4.359 34.235 1.00 10.83 C ANISOU 2038 CA PHE B 278 1504 1337 1273 -25 -97 -33 C ATOM 2039 C PHE B 278 13.402 -4.461 35.330 1.00 13.54 C ANISOU 2039 C PHE B 278 1886 1672 1586 -8 -127 -42 C ATOM 2040 O PHE B 278 14.583 -4.413 35.016 1.00 15.93 O ANISOU 2040 O PHE B 278 2177 1978 1899 31 -158 -60 O ATOM 2041 CB PHE B 278 11.899 -2.910 33.960 1.00 11.32 C ANISOU 2041 CB PHE B 278 1504 1426 1370 -29 -56 -41 C ATOM 2042 CG PHE B 278 11.498 -2.677 32.525 1.00 11.61 C ANISOU 2042 CG PHE B 278 1499 1472 1440 -19 -52 -37 C ATOM 2043 CD1 PHE B 278 12.457 -2.715 31.512 1.00 12.88 C ANISOU 2043 CD1 PHE B 278 1647 1638 1610 14 -74 -43 C ATOM 2044 CD2 PHE B 278 10.170 -2.437 32.185 1.00 10.31 C ANISOU 2044 CD2 PHE B 278 1309 1311 1297 -43 -28 -32 C ATOM 2045 CE1 PHE B 278 12.094 -2.509 30.170 1.00 13.22 C ANISOU 2045 CE1 PHE B 278 1661 1689 1672 20 -71 -37 C ATOM 2046 CE2 PHE B 278 9.793 -2.218 30.853 1.00 10.47 C ANISOU 2046 CE2 PHE B 278 1298 1338 1344 -31 -33 -27 C ATOM 2047 CZ PHE B 278 10.755 -2.262 29.841 1.00 12.96 C ANISOU 2047 CZ PHE B 278 1610 1657 1657 0 -55 -26 C ATOM 2048 N PRO B 279 13.003 -4.600 36.606 1.00 15.35 N ANISOU 2048 N PRO B 279 2163 1892 1778 -39 -117 -34 N ATOM 2049 CA PRO B 279 14.060 -4.889 37.590 1.00 15.91 C ANISOU 2049 CA PRO B 279 2284 1950 1813 -19 -160 -41 C ATOM 2050 C PRO B 279 14.827 -6.178 37.283 1.00 15.43 C ANISOU 2050 C PRO B 279 2267 1855 1740 13 -225 -36 C ATOM 2051 O PRO B 279 16.064 -6.199 37.416 1.00 16.89 O ANISOU 2051 O PRO B 279 2452 2036 1928 57 -272 -59 O ATOM 2052 CB PRO B 279 13.288 -5.036 38.905 1.00 21.02 C ANISOU 2052 CB PRO B 279 2990 2588 2409 -68 -136 -26 C ATOM 2053 CG PRO B 279 12.075 -4.165 38.721 1.00 20.69 C ANISOU 2053 CG PRO B 279 2894 2573 2395 -106 -67 -31 C ATOM 2054 CD PRO B 279 11.713 -4.279 37.250 1.00 13.48 C ANISOU 2054 CD PRO B 279 1929 1662 1530 -92 -64 -27 C ATOM 2055 N GLY B 280 14.129 -7.234 36.867 1.00 14.05 N ANISOU 2055 N GLY B 280 2126 1655 1558 -6 -229 -14 N ATOM 2056 CA GLY B 280 14.811 -8.477 36.520 1.00 17.10 C ANISOU 2056 CA GLY B 280 2552 2004 1940 26 -292 -13 C ATOM 2057 C GLY B 280 15.796 -8.313 35.364 1.00 14.88 C ANISOU 2057 C GLY B 280 2209 1738 1705 77 -315 -45 C ATOM 2058 O GLY B 280 16.965 -8.809 35.377 1.00 17.32 O ANISOU 2058 O GLY B 280 2530 2031 2020 123 -374 -68 O ATOM 2059 N ILE B 281 15.316 -7.591 34.353 1.00 13.31 N ANISOU 2059 N ILE B 281 1944 1572 1539 69 -269 -50 N ATOM 2060 CA ILE B 281 16.132 -7.287 33.194 1.00 14.66 C ANISOU 2060 CA ILE B 281 2058 1764 1748 105 -275 -79 C ATOM 2061 C ILE B 281 17.362 -6.511 33.640 1.00 17.93 C ANISOU 2061 C ILE B 281 2445 2195 2172 136 -289 -111 C ATOM 2062 O ILE B 281 18.466 -6.811 33.203 1.00 15.04 O ANISOU 2062 O ILE B 281 2061 1828 1827 175 -323 -145 O ATOM 2063 CB ILE B 281 15.365 -6.455 32.148 1.00 12.91 C ANISOU 2063 CB ILE B 281 1780 1573 1551 86 -224 -73 C ATOM 2064 CG1 ILE B 281 14.209 -7.275 31.545 1.00 13.86 C ANISOU 2064 CG1 ILE B 281 1917 1680 1669 61 -217 -51 C ATOM 2065 CG2 ILE B 281 16.314 -6.011 31.040 1.00 15.84 C ANISOU 2065 CG2 ILE B 281 2099 1967 1951 117 -223 -102 C ATOM 2066 CD1 ILE B 281 13.202 -6.428 30.724 1.00 13.81 C ANISOU 2066 CD1 ILE B 281 1863 1700 1684 39 -173 -41 C ATOM 2067 N GLU B 282 17.166 -5.516 34.500 1.00 13.31 N ANISOU 2067 N GLU B 282 1853 1625 1578 119 -260 -107 N ATOM 2068 CA GLU B 282 18.263 -4.669 34.973 1.00 13.73 C ANISOU 2068 CA GLU B 282 1877 1697 1645 144 -268 -141 C ATOM 2069 C GLU B 282 19.303 -5.495 35.709 1.00 16.31 C ANISOU 2069 C GLU B 282 2245 1998 1956 180 -339 -162 C ATOM 2070 O GLU B 282 20.511 -5.281 35.548 1.00 17.05 O ANISOU 2070 O GLU B 282 2302 2101 2077 218 -365 -206 O ATOM 2071 CB GLU B 282 17.755 -3.567 35.919 1.00 13.41 C ANISOU 2071 CB GLU B 282 1831 1673 1593 115 -229 -133 C ATOM 2072 CG GLU B 282 18.848 -2.528 36.212 1.00 19.46 C ANISOU 2072 CG GLU B 282 2553 2461 2382 138 -229 -173 C ATOM 2073 CD GLU B 282 18.396 -1.400 37.135 1.00 25.57 C ANISOU 2073 CD GLU B 282 3316 3249 3148 112 -190 -172 C ATOM 2074 OE1 GLU B 282 19.267 -0.593 37.533 1.00 21.79 O ANISOU 2074 OE1 GLU B 282 2807 2785 2686 129 -194 -207 O ATOM 2075 OE2 GLU B 282 17.185 -1.313 37.465 1.00 21.76 O1- ANISOU 2075 OE2 GLU B 282 2854 2767 2648 75 -156 -144 O1- ATOM 2076 N GLU B 283 18.836 -6.434 36.524 1.00 13.66 N ANISOU 2076 N GLU B 283 1987 1628 1577 168 -370 -133 N ATOM 2077 CA GLU B 283 19.751 -7.212 37.347 1.00 16.02 C ANISOU 2077 CA GLU B 283 2338 1895 1854 203 -448 -147 C ATOM 2078 C GLU B 283 20.591 -8.129 36.498 1.00 21.68 C ANISOU 2078 C GLU B 283 3042 2592 2603 249 -500 -176 C ATOM 2079 O GLU B 283 21.752 -8.421 36.850 1.00 24.08 O ANISOU 2079 O GLU B 283 3348 2882 2919 297 -565 -214 O ATOM 2080 CB GLU B 283 18.993 -8.006 38.413 1.00 17.71 C ANISOU 2080 CB GLU B 283 2652 2071 2006 172 -466 -103 C ATOM 2081 CG GLU B 283 18.421 -7.138 39.523 1.00 25.87 C ANISOU 2081 CG GLU B 283 3705 3124 3001 132 -425 -88 C ATOM 2082 CD GLU B 283 17.488 -7.921 40.437 1.00 37.45 C ANISOU 2082 CD GLU B 283 5270 4556 4402 84 -424 -42 C ATOM 2083 OE1 GLU B 283 16.689 -7.285 41.167 1.00 44.68 O ANISOU 2083 OE1 GLU B 283 6199 5492 5287 36 -369 -29 O ATOM 2084 OE2 GLU B 283 17.556 -9.172 40.413 1.00 40.56 O1- ANISOU 2084 OE2 GLU B 283 5730 4903 4777 93 -474 -22 O1- ATOM 2085 N LYS B 284 20.020 -8.589 35.386 1.00 24.33 N ANISOU 2085 N LYS B 284 3361 2927 2957 237 -475 -164 N ATOM 2086 CA LYS B 284 20.867 -9.323 34.435 1.00 27.60 C ANISOU 2086 CA LYS B 284 3747 3331 3409 280 -515 -203 C ATOM 2087 C LYS B 284 21.779 -8.456 33.535 1.00 25.35 C ANISOU 2087 C LYS B 284 3370 3089 3171 301 -487 -256 C ATOM 2088 O LYS B 284 22.956 -8.767 33.323 1.00 22.49 O ANISOU 2088 O LYS B 284 2980 2724 2842 346 -530 -311 O ATOM 2089 CB LYS B 284 20.016 -10.267 33.576 1.00 31.25 C ANISOU 2089 CB LYS B 284 4231 3773 3870 261 -506 -178 C ATOM 2090 CG LYS B 284 19.696 -11.580 34.274 1.00 38.14 C ANISOU 2090 CG LYS B 284 5195 4585 4710 260 -562 -148 C ATOM 2091 CD LYS B 284 20.971 -12.200 34.856 1.00 46.71 C ANISOU 2091 CD LYS B 284 6308 5637 5804 318 -651 -183 C ATOM 2092 CE LYS B 284 20.666 -13.458 35.651 1.00 49.43 C ANISOU 2092 CE LYS B 284 6758 5912 6110 316 -713 -146 C ATOM 2093 NZ LYS B 284 19.722 -13.158 36.769 1.00 58.22 N1+ ANISOU 2093 NZ LYS B 284 7939 7020 7162 261 -682 -91 N1+ ATOM 2094 N PHE B 285 21.236 -7.370 33.000 1.00 19.07 N ANISOU 2094 N PHE B 285 2530 2333 2384 268 -415 -244 N ATOM 2095 CA PHE B 285 21.927 -6.606 31.976 1.00 16.96 C ANISOU 2095 CA PHE B 285 2187 2102 2155 276 -378 -284 C ATOM 2096 C PHE B 285 23.029 -5.743 32.551 1.00 16.86 C ANISOU 2096 C PHE B 285 2134 2108 2164 296 -383 -330 C ATOM 2097 O PHE B 285 24.052 -5.535 31.896 1.00 17.90 O ANISOU 2097 O PHE B 285 2209 2258 2333 316 -379 -385 O ATOM 2098 CB PHE B 285 20.947 -5.727 31.191 1.00 15.97 C ANISOU 2098 CB PHE B 285 2036 2004 2027 234 -306 -251 C ATOM 2099 CG PHE B 285 21.559 -5.075 29.977 1.00 15.89 C ANISOU 2099 CG PHE B 285 1965 2026 2046 235 -266 -284 C ATOM 2100 CD1 PHE B 285 21.991 -3.755 30.027 1.00 14.78 C ANISOU 2100 CD1 PHE B 285 1782 1911 1923 224 -225 -299 C ATOM 2101 CD2 PHE B 285 21.721 -5.789 28.791 1.00 17.69 C ANISOU 2101 CD2 PHE B 285 2182 2257 2282 243 -268 -302 C ATOM 2102 CE1 PHE B 285 22.555 -3.146 28.921 1.00 16.26 C ANISOU 2102 CE1 PHE B 285 1922 2125 2131 216 -183 -327 C ATOM 2103 CE2 PHE B 285 22.290 -5.191 27.681 1.00 18.19 C ANISOU 2103 CE2 PHE B 285 2197 2351 2363 236 -226 -332 C ATOM 2104 CZ PHE B 285 22.713 -3.868 27.741 1.00 17.86 C ANISOU 2104 CZ PHE B 285 2118 2333 2335 221 -182 -343 C ATOM 2105 N ARG B 286 22.817 -5.206 33.744 1.00 14.32 N ANISOU 2105 N ARG B 286 1838 1784 1821 286 -387 -312 N ATOM 2106 CA ARG B 286 23.820 -4.269 34.278 1.00 15.31 C ANISOU 2106 CA ARG B 286 1918 1929 1969 302 -387 -358 C ATOM 2107 C ARG B 286 25.216 -4.897 34.369 1.00 15.19 C ANISOU 2107 C ARG B 286 1882 1904 1984 355 -454 -424 C ATOM 2108 O ARG B 286 26.173 -4.350 33.805 1.00 18.48 O ANISOU 2108 O ARG B 286 2229 2346 2446 367 -435 -482 O ATOM 2109 CB ARG B 286 23.381 -3.657 35.612 1.00 16.81 C ANISOU 2109 CB ARG B 286 2143 2118 2127 285 -386 -334 C ATOM 2110 CG ARG B 286 24.441 -2.720 36.218 1.00 14.30 C ANISOU 2110 CG ARG B 286 1780 1820 1835 303 -393 -387 C ATOM 2111 CD ARG B 286 23.931 -2.044 37.514 1.00 14.98 C ANISOU 2111 CD ARG B 286 1900 1908 1885 281 -385 -365 C ATOM 2112 NE ARG B 286 22.720 -1.265 37.251 1.00 14.41 N ANISOU 2112 NE ARG B 286 1821 1849 1804 233 -311 -320 N ATOM 2113 CZ ARG B 286 22.709 -0.013 36.801 1.00 14.54 C ANISOU 2113 CZ ARG B 286 1780 1891 1855 214 -252 -332 C ATOM 2114 NH1 ARG B 286 23.848 0.643 36.589 1.00 14.55 N1+ ANISOU 2114 NH1 ARG B 286 1723 1908 1899 232 -249 -385 N1+ ATOM 2115 NH2 ARG B 286 21.554 0.592 36.574 1.00 15.56 N ANISOU 2115 NH2 ARG B 286 1908 2025 1979 177 -196 -292 N ATOM 2116 N PRO B 287 25.341 -6.051 35.052 1.00 17.17 N ANISOU 2116 N PRO B 287 2194 2115 2214 386 -532 -420 N ATOM 2117 CA PRO B 287 26.697 -6.610 35.125 1.00 20.50 C ANISOU 2117 CA PRO B 287 2590 2525 2674 443 -604 -491 C ATOM 2118 C PRO B 287 27.229 -7.083 33.780 1.00 23.46 C ANISOU 2118 C PRO B 287 2908 2909 3095 459 -593 -537 C ATOM 2119 O PRO B 287 28.445 -7.065 33.584 1.00 21.18 O ANISOU 2119 O PRO B 287 2560 2632 2856 496 -619 -615 O ATOM 2120 CB PRO B 287 26.545 -7.800 36.082 1.00 23.34 C ANISOU 2120 CB PRO B 287 3041 2831 2995 470 -693 -463 C ATOM 2121 CG PRO B 287 25.090 -8.132 36.080 1.00 24.15 C ANISOU 2121 CG PRO B 287 3211 2919 3047 422 -657 -382 C ATOM 2122 CD PRO B 287 24.380 -6.832 35.856 1.00 18.46 C ANISOU 2122 CD PRO B 287 2452 2241 2322 371 -563 -357 C ATOM 2123 N PHE B 288 26.350 -7.505 32.874 1.00 19.16 N ANISOU 2123 N PHE B 288 2381 2363 2536 432 -555 -496 N ATOM 2124 CA PHE B 288 26.799 -7.863 31.538 1.00 19.58 C ANISOU 2124 CA PHE B 288 2382 2431 2626 440 -534 -541 C ATOM 2125 C PHE B 288 27.340 -6.638 30.811 1.00 20.84 C ANISOU 2125 C PHE B 288 2462 2641 2817 417 -459 -581 C ATOM 2126 O PHE B 288 28.385 -6.699 30.156 1.00 20.04 O ANISOU 2126 O PHE B 288 2297 2557 2759 436 -456 -655 O ATOM 2127 CB PHE B 288 25.653 -8.471 30.730 1.00 18.51 C ANISOU 2127 CB PHE B 288 2283 2285 2463 411 -507 -487 C ATOM 2128 CG PHE B 288 25.939 -8.540 29.263 1.00 18.42 C ANISOU 2128 CG PHE B 288 2219 2302 2477 404 -465 -525 C ATOM 2129 CD1 PHE B 288 25.419 -7.587 28.397 1.00 21.67 C ANISOU 2129 CD1 PHE B 288 2604 2752 2878 359 -382 -501 C ATOM 2130 CD2 PHE B 288 26.748 -9.544 28.747 1.00 28.66 C ANISOU 2130 CD2 PHE B 288 3495 3585 3809 444 -508 -588 C ATOM 2131 CE1 PHE B 288 25.691 -7.634 27.045 1.00 20.60 C ANISOU 2131 CE1 PHE B 288 2429 2643 2756 348 -342 -535 C ATOM 2132 CE2 PHE B 288 27.018 -9.604 27.386 1.00 28.26 C ANISOU 2132 CE2 PHE B 288 3396 3564 3776 433 -463 -628 C ATOM 2133 CZ PHE B 288 26.489 -8.652 26.535 1.00 28.25 C ANISOU 2133 CZ PHE B 288 3375 3603 3754 383 -378 -600 C ATOM 2134 N TYR B 289 26.616 -5.523 30.909 1.00 19.62 N ANISOU 2134 N TYR B 289 2309 2508 2639 373 -396 -533 N ATOM 2135 CA TYR B 289 27.048 -4.288 30.268 1.00 17.11 C ANISOU 2135 CA TYR B 289 1926 2228 2345 345 -323 -560 C ATOM 2136 C TYR B 289 28.416 -3.909 30.807 1.00 20.11 C ANISOU 2136 C TYR B 289 2251 2619 2769 373 -347 -639 C ATOM 2137 O TYR B 289 29.333 -3.558 30.048 1.00 21.63 O ANISOU 2137 O TYR B 289 2377 2838 3002 370 -311 -704 O ATOM 2138 CB TYR B 289 26.058 -3.157 30.573 1.00 16.32 C ANISOU 2138 CB TYR B 289 1845 2138 2218 301 -270 -497 C ATOM 2139 CG TYR B 289 26.629 -1.782 30.310 1.00 18.37 C ANISOU 2139 CG TYR B 289 2047 2427 2505 277 -208 -526 C ATOM 2140 CD1 TYR B 289 26.862 -1.342 29.011 1.00 20.28 C ANISOU 2140 CD1 TYR B 289 2253 2692 2760 250 -147 -542 C ATOM 2141 CD2 TYR B 289 26.936 -0.920 31.362 1.00 19.00 C ANISOU 2141 CD2 TYR B 289 2114 2509 2595 278 -211 -538 C ATOM 2142 CE1 TYR B 289 27.394 -0.076 28.762 1.00 21.06 C ANISOU 2142 CE1 TYR B 289 2307 2812 2883 221 -87 -566 C ATOM 2143 CE2 TYR B 289 27.467 0.340 31.124 1.00 19.71 C ANISOU 2143 CE2 TYR B 289 2152 2622 2715 253 -154 -567 C ATOM 2144 CZ TYR B 289 27.690 0.755 29.824 1.00 22.66 C ANISOU 2144 CZ TYR B 289 2494 3014 3102 223 -91 -579 C ATOM 2145 OH TYR B 289 28.227 2.009 29.588 1.00 24.33 O ANISOU 2145 OH TYR B 289 2661 3242 3342 192 -31 -605 O ATOM 2146 N LEU B 290 28.547 -3.981 32.130 1.00 19.05 N ANISOU 2146 N LEU B 290 2146 2466 2627 399 -406 -637 N ATOM 2147 CA LEU B 290 29.773 -3.552 32.787 1.00 23.79 C ANISOU 2147 CA LEU B 290 2696 3075 3268 428 -436 -712 C ATOM 2148 C LEU B 290 30.967 -4.412 32.359 1.00 25.40 C ANISOU 2148 C LEU B 290 2852 3276 3523 476 -486 -800 C ATOM 2149 O LEU B 290 32.046 -3.891 32.073 1.00 28.29 O ANISOU 2149 O LEU B 290 3146 3669 3935 469 -463 -872 O ATOM 2150 CB LEU B 290 29.593 -3.579 34.310 1.00 21.87 C ANISOU 2150 CB LEU B 290 2506 2809 2994 449 -500 -688 C ATOM 2151 CG LEU B 290 28.635 -2.516 34.862 1.00 26.53 C ANISOU 2151 CG LEU B 290 3123 3409 3547 403 -446 -625 C ATOM 2152 CD1 LEU B 290 28.455 -2.687 36.353 1.00 27.48 C ANISOU 2152 CD1 LEU B 290 3305 3508 3628 420 -510 -605 C ATOM 2153 CD2 LEU B 290 29.139 -1.101 34.545 1.00 27.62 C ANISOU 2153 CD2 LEU B 290 3187 3583 3724 375 -376 -663 C ATOM 2154 N SER B 291 30.772 -5.724 32.291 1.00 22.53 N ANISOU 2154 N SER B 291 2533 2878 3148 509 -549 -790 N ATOM 2155 CA SER B 291 31.904 -6.617 32.037 1.00 23.00 C ANISOU 2155 CA SER B 291 2559 2929 3251 546 -606 -868 C ATOM 2156 C SER B 291 32.291 -6.747 30.572 1.00 26.94 C ANISOU 2156 C SER B 291 3000 3460 3776 515 -546 -904 C ATOM 2157 O SER B 291 33.456 -7.019 30.267 1.00 29.14 O ANISOU 2157 O SER B 291 3225 3753 4093 516 -564 -974 O ATOM 2158 CB SER B 291 31.646 -8.006 32.638 1.00 31.12 C ANISOU 2158 CB SER B 291 3666 3899 4258 592 -705 -845 C ATOM 2159 OG SER B 291 30.465 -8.587 32.117 1.00 37.85 O ANISOU 2159 OG SER B 291 4570 4735 5077 581 -690 -776 O ATOM 2160 N GLN B 292 31.341 -6.520 29.663 1.00 26.60 N ANISOU 2160 N GLN B 292 2967 3428 3710 487 -474 -861 N ATOM 2161 CA AGLN B 292 31.531 -6.809 28.239 0.44 30.87 C ANISOU 2161 CA AGLN B 292 3473 3995 4262 460 -422 -887 C ATOM 2162 CA BGLN B 292 31.577 -6.793 28.240 0.56 30.89 C ANISOU 2162 CA BGLN B 292 3473 3998 4266 460 -422 -889 C ATOM 2163 C GLN B 292 31.481 -5.596 27.310 1.00 33.42 C ANISOU 2163 C GLN B 292 3755 4362 4580 401 -312 -885 C ATOM 2164 O GLN B 292 32.200 -5.532 26.313 1.00 33.51 O ANISOU 2164 O GLN B 292 3718 4403 4611 371 -267 -930 O ATOM 2165 CB AGLN B 292 30.444 -7.776 27.781 0.44 31.16 C ANISOU 2165 CB AGLN B 292 3569 4002 4267 474 -437 -840 C ATOM 2166 CB BGLN B 292 30.596 -7.838 27.719 0.56 31.15 C ANISOU 2166 CB BGLN B 292 3561 4003 4273 477 -440 -852 C ATOM 2167 CG AGLN B 292 30.455 -9.117 28.485 0.44 33.73 C ANISOU 2167 CG AGLN B 292 3944 4276 4597 528 -543 -839 C ATOM 2168 CG BGLN B 292 30.822 -9.246 28.213 0.56 34.89 C ANISOU 2168 CG BGLN B 292 4069 4431 4756 526 -541 -863 C ATOM 2169 CD AGLN B 292 30.933 -10.221 27.569 0.44 37.35 C ANISOU 2169 CD AGLN B 292 4380 4733 5078 537 -563 -883 C ATOM 2170 CD BGLN B 292 30.222 -10.271 27.264 0.56 38.55 C ANISOU 2170 CD BGLN B 292 4559 4879 5209 529 -542 -852 C ATOM 2171 NE2AGLN B 292 32.195 -10.602 27.714 0.44 37.23 N ANISOU 2171 NE2AGLN B 292 4317 4725 5105 554 -610 -950 N ATOM 2172 NE2BGLN B 292 29.656 -11.336 27.823 0.56 39.33 N ANISOU 2172 NE2BGLN B 292 4729 4923 5293 562 -617 -815 N ATOM 2173 OE1AGLN B 292 30.180 -10.712 26.725 0.44 39.39 O ANISOU 2173 OE1AGLN B 292 4663 4986 5319 528 -539 -861 O ATOM 2174 OE1BGLN B 292 30.257 -10.100 26.039 0.56 37.89 O ANISOU 2174 OE1BGLN B 292 4438 4832 5128 498 -474 -874 O ATOM 2175 N LEU B 293 30.590 -4.660 27.613 1.00 27.55 N ANISOU 2175 N LEU B 293 3042 3621 3806 376 -270 -823 N ATOM 2176 CA LEU B 293 30.265 -3.602 26.661 1.00 29.09 C ANISOU 2176 CA LEU B 293 3223 3847 3983 316 -172 -797 C ATOM 2177 C LEU B 293 30.891 -2.249 26.959 1.00 28.97 C ANISOU 2177 C LEU B 293 3161 3854 3993 289 -122 -826 C ATOM 2178 O LEU B 293 31.344 -1.557 26.047 1.00 30.20 O ANISOU 2178 O LEU B 293 3284 4036 4156 241 -49 -845 O ATOM 2179 CB LEU B 293 28.737 -3.444 26.570 1.00 25.98 C ANISOU 2179 CB LEU B 293 2900 3440 3531 287 -156 -690 C ATOM 2180 CG LEU B 293 27.929 -4.289 25.587 1.00 33.46 C ANISOU 2180 CG LEU B 293 3884 4383 4445 279 -153 -654 C ATOM 2181 CD1 LEU B 293 28.527 -5.680 25.318 1.00 31.53 C ANISOU 2181 CD1 LEU B 293 3629 4127 4224 321 -207 -714 C ATOM 2182 CD2 LEU B 293 26.471 -4.384 26.033 1.00 23.76 C ANISOU 2182 CD2 LEU B 293 2724 3131 3173 269 -170 -560 C ATOM 2183 N GLU B 294 30.896 -1.861 28.231 1.00 21.20 N ATOM 2184 CA GLU B 294 31.317 -0.522 28.641 1.00 25.00 C ATOM 2185 C GLU B 294 32.735 -0.164 28.200 1.00 28.51 C ATOM 2186 O GLU B 294 33.647 -0.984 28.323 1.00 31.36 O ATOM 2187 CB GLU B 294 31.218 -0.395 30.165 1.00 23.34 C ATOM 2188 CG GLU B 294 31.746 0.926 30.715 1.00 29.41 C ATOM 2189 CD GLU B 294 31.531 1.048 32.218 1.00 28.18 C ATOM 2190 OE1 GLU B 294 30.651 1.832 32.640 1.00 38.86 O ATOM 2191 OE2 GLU B 294 32.238 0.354 32.977 1.00 31.47 O1- TER HETATM 2192 CL2 1HX B 301 8.186 9.279 30.274 1.00 17.42 CL HETATM 2193 C1 1HX B 301 4.322 9.018 31.446 1.00 15.17 C HETATM 2194 C2 1HX B 301 4.127 10.261 32.056 1.00 14.16 C HETATM 2195 C3 1HX B 301 5.159 11.187 32.104 1.00 13.92 C HETATM 2196 C4 1HX B 301 6.403 10.906 31.572 1.00 13.15 C HETATM 2197 C5 1HX B 301 6.591 9.666 30.979 1.00 15.55 C HETATM 2198 C6 1HX B 301 5.574 8.729 30.912 1.00 15.41 C HETATM 2199 C7 1HX B 301 7.490 11.922 31.651 1.00 12.53 C HETATM 2200 N8 1HX B 301 7.002 13.258 31.298 1.00 15.38 N HETATM 2201 C9 1HX B 301 6.917 13.631 30.015 1.00 14.07 C HETATM 2202 C10 1HX B 301 8.054 11.999 33.073 1.00 13.56 C HETATM 2203 O11 1HX B 301 7.053 12.797 29.120 1.00 15.61 O HETATM 2204 C12 1HX B 301 6.670 15.060 29.606 1.00 13.61 C HETATM 2205 N13 1HX B 301 6.082 15.424 28.450 1.00 13.59 N HETATM 2206 C14 1HX B 301 6.075 16.767 28.447 1.00 15.59 C HETATM 2207 C15 1HX B 301 6.632 17.339 29.550 1.00 17.56 C HETATM 2208 C16 1HX B 301 7.020 16.237 30.311 1.00 16.13 C HETATM 2209 C17 1HX B 301 5.549 14.586 27.341 1.00 16.16 C HETATM 2210 C18 1HX B 301 5.561 17.440 27.408 1.00 17.02 C HETATM 2211 N19 1HX B 301 5.204 17.996 26.446 1.00 17.28 N HETATM 2212 F20 1HX B 301 4.999 12.381 32.684 1.00 17.11 F HETATM 2213 I IOD B 302 21.084 -3.918 39.396 0.55 17.83 I HETATM 2214 I IOD B 303 21.562 -9.790 29.618 0.55 20.73 I HETATM 2215 I IOD B 304 11.189 16.595 21.069 0.38 32.56 I HETATM 2216 I IOD B 305 -4.861 28.808 36.206 0.52 33.29 I HETATM 2217 O HOH B 401 4.719 0.303 25.428 1.00 13.01 O HETATM 2218 O HOH B 402 6.140 -6.192 16.935 1.00 12.57 O HETATM 2219 O HOH B 403 2.931 7.333 28.804 0.86 15.49 O HETATM 2220 O HOH B 404 19.723 10.763 31.012 1.00 16.35 O HETATM 2221 O HOH B 405 10.390 14.659 34.974 1.00 15.96 O HETATM 2222 O HOH B 406 10.736 -7.568 6.997 1.00 22.12 O HETATM 2223 O HOH B 407 6.543 15.132 33.647 0.86 12.31 O HETATM 2224 O HOH B 408 3.588 8.787 24.098 0.91 14.85 O HETATM 2225 O HOH B 409 2.845 -2.818 23.966 1.00 13.03 O HETATM 2226 O HOH B 410 4.738 1.329 21.473 1.00 20.94 O HETATM 2227 O HOH B 411 13.016 13.968 35.279 1.00 15.31 O HETATM 2228 O HOH B 412 10.686 -1.128 38.975 1.00 21.27 O HETATM 2229 O HOH B 413 0.057 -7.400 28.412 0.95 21.94 O HETATM 2230 O HOH B 414 8.432 -4.236 35.153 1.00 13.92 O HETATM 2231 O HOH B 415 8.577 16.702 34.869 0.96 15.52 O HETATM 2232 O HOH B 416 13.076 -4.112 8.510 1.00 18.75 O HETATM 2233 O HOH B 417 5.421 -9.586 2.767 1.00 20.63 O HETATM 2234 O HOH B 418 15.704 22.579 27.654 0.99 20.58 O HETATM 2235 O HOH B 419 -0.509 -12.571 7.970 0.85 15.19 O HETATM 2236 O HOH B 420 9.240 5.035 17.081 1.00 18.53 O HETATM 2237 O HOH B 421 23.418 6.358 27.030 0.84 18.99 O HETATM 2238 O HOH B 422 -11.837 37.695 28.158 1.00 23.15 O HETATM 2239 O HOH B 423 2.544 -13.604 19.440 1.00 20.00 O HETATM 2240 O HOH B 424 13.491 2.425 8.922 1.00 23.65 O HETATM 2241 O HOH B 425 13.883 -6.634 8.915 0.88 19.50 O HETATM 2242 O HOH B 426 14.315 3.926 40.089 0.92 23.58 O HETATM 2243 O HOH B 427 9.008 -1.373 8.096 1.00 27.35 O HETATM 2244 O HOH B 428 28.979 3.557 31.432 0.99 28.21 O HETATM 2245 O HOH B 429 14.277 9.695 41.072 1.00 22.45 O HETATM 2246 O HOH B 430 10.444 4.066 40.983 1.00 22.12 O HETATM 2247 O HOH B 431 7.937 -4.410 37.758 0.94 23.89 O HETATM 2248 O HOH B 432 30.083 -6.849 35.737 0.90 21.94 O HETATM 2249 O HOH B 433 4.653 -6.880 35.941 1.00 22.77 O HETATM 2250 O HOH B 434 27.520 -11.126 33.177 1.00 26.62 O HETATM 2251 O HOH B 435 10.368 11.935 18.647 1.00 22.07 O HETATM 2252 O HOH B 436 13.090 -0.576 7.897 1.00 20.93 O HETATM 2253 O HOH B 437 3.529 0.108 36.805 1.00 23.41 O HETATM 2254 O HOH B 438 11.651 -15.122 18.178 1.00 26.75 O HETATM 2255 O HOH B 439 24.537 5.663 32.346 1.00 23.70 O HETATM 2256 O HOH B 440 15.101 15.011 32.750 0.77 16.26 O HETATM 2257 O HOH B 441 6.770 -11.182 36.234 0.94 22.28 O HETATM 2258 O HOH B 442 14.257 13.379 16.127 1.00 24.51 O HETATM 2259 O HOH B 443 3.636 -5.363 17.142 1.00 16.79 O HETATM 2260 O HOH B 444 32.264 0.467 35.422 0.97 27.56 O HETATM 2261 O HOH B 445 15.901 -16.067 24.968 1.00 22.66 O HETATM 2262 O HOH B 446 32.042 -2.154 23.593 1.00 32.02 O HETATM 2263 O HOH B 447 32.356 -0.059 21.559 1.00 22.77 O HETATM 2264 O HOH B 448 21.802 12.654 31.448 1.00 23.49 O HETATM 2265 O HOH B 449 0.235 -11.940 23.821 0.82 20.31 O HETATM 2266 O HOH B 450 11.024 5.115 15.296 0.87 18.97 O HETATM 2267 O HOH B 451 2.752 -0.278 22.919 0.83 21.00 O HETATM 2268 O HOH B 452 24.299 -10.942 33.356 0.86 24.04 O HETATM 2269 O HOH B 453 16.889 -11.260 36.645 1.00 34.79 O HETATM 2270 O HOH B 454 10.448 10.431 42.227 0.77 21.33 O HETATM 2271 O HOH B 455 15.715 3.121 37.825 0.83 20.77 O HETATM 2272 O HOH B 456 9.936 -14.277 13.437 1.00 25.43 O HETATM 2273 O HOH B 457 10.077 -6.308 0.196 1.00 21.43 O HETATM 2274 O HOH B 458 6.848 -6.497 34.339 0.80 15.46 O HETATM 2275 O HOH B 459 -3.361 12.943 37.166 1.00 27.68 O HETATM 2276 O HOH B 460 10.245 -15.292 22.299 0.81 18.53 O HETATM 2277 O HOH B 461 4.274 25.029 19.202 1.00 29.44 O HETATM 2278 O HOH B 462 13.328 17.311 23.559 0.74 20.00 O HETATM 2279 O HOH B 463 -7.049 30.503 30.840 1.00 28.70 O HETATM 2280 O HOH B 464 19.578 27.269 25.539 1.00 32.29 O HETATM 2281 O HOH B 465 7.547 -7.291 0.384 0.76 21.48 O HETATM 2282 O HOH B 466 -0.235 31.995 38.957 1.00 30.40 O HETATM 2283 O HOH B 467 14.537 17.169 20.497 1.00 38.22 O HETATM 2284 O HOH B 468 -1.686 8.887 33.729 0.82 24.21 O HETATM 2285 O HOH B 469 22.681 -4.181 11.753 0.96 28.62 O HETATM 2286 O HOH B 470 4.886 -17.689 24.868 1.00 26.03 O HETATM 2287 O HOH B 471 18.800 0.964 39.634 0.76 22.33 O HETATM 2288 O HOH B 472 0.510 3.374 14.787 1.00 41.57 O HETATM 2289 O HOH B 473 3.537 19.460 15.686 0.89 36.42 O HETATM 2290 O HOH B 474 0.018 7.385 34.549 1.00 38.87 O HETATM 2291 O HOH B 475 12.274 -13.408 14.501 1.00 29.05 O HETATM 2292 O HOH B 476 22.637 -17.880 22.069 1.00 38.80 O HETATM 2293 O HOH B 477 12.014 14.191 19.242 1.00 43.15 O HETATM 2294 O HOH B 478 8.412 -2.456 39.359 1.00 25.28 O HETATM 2295 O HOH B 479 10.148 -14.855 28.102 0.80 23.74 O HETATM 2296 O HOH B 480 10.937 -14.053 32.623 0.88 28.84 O HETATM 2297 O HOH B 481 26.229 -10.790 15.796 0.73 28.18 O HETATM 2298 O HOH B 482 1.560 7.692 22.405 0.80 26.12 O HETATM 2299 O HOH B 483 29.828 -8.929 23.437 1.00 39.39 O HETATM 2300 O HOH B 484 -4.716 13.495 40.902 1.00 44.70 O HETATM 2301 O HOH B 485 -9.249 29.395 28.347 1.00 29.96 O HETATM 2302 O HOH B 486 27.180 -3.184 17.556 1.00 28.62 O HETATM 2303 O HOH B 487 10.994 7.446 13.830 1.00 28.62 O HETATM 2304 O HOH B 488 31.924 -0.495 18.737 0.89 32.69 O HETATM 2305 O HOH B 489 5.376 -2.112 39.770 0.64 25.85 O HETATM 2306 O HOH B 490 24.400 6.222 14.791 0.94 26.89 O HETATM 2307 O HOH B 491 23.875 3.224 14.803 0.74 23.56 O HETATM 2308 O HOH B 492 23.066 20.635 20.183 1.00 45.21 O HETATM 2309 O HOH B 493 16.616 25.862 28.581 0.78 26.85 O HETATM 2310 O HOH B 494 1.648 35.488 26.200 0.94 34.92 O HETATM 2311 O HOH B 495 2.240 -16.708 19.002 1.00 31.98 O HETATM 2312 O HOH B 496 10.956 -8.112 39.514 1.00 31.01 O HETATM 2313 O HOH B 497 19.195 34.993 25.716 1.00 40.17 O HETATM 2314 O HOH B 498 33.532 -1.726 32.534 1.00 31.00 O HETATM 2315 O HOH B 499 10.601 -0.111 7.040 0.74 29.43 O HETATM 2316 O HOH B 500 -9.044 32.308 30.155 1.00 40.15 O HETATM 2317 O HOH B 501 15.398 -2.431 39.041 0.69 27.09 O HETATM 2318 O HOH B 502 -10.709 25.578 36.215 0.86 22.48 O HETATM 2319 O HOH B 503 5.110 1.707 13.979 0.88 32.92 O HETATM 2320 O HOH B 504 13.376 12.549 14.012 1.00 34.34 O HETATM 2321 O HOH B 505 3.303 29.303 21.265 0.78 28.87 O HETATM 2322 O HOH B 506 4.590 29.922 38.135 1.00 37.74 O HETATM 2323 O HOH B 507 29.398 3.438 27.195 0.54 23.81 O HETATM 2324 O HOH B 508 6.444 10.798 18.080 1.00 42.91 O HETATM 2325 O HOH B 509 11.208 8.933 43.642 0.62 25.63 O HETATM 2326 O HOH B 510 16.553 0.618 38.951 0.77 24.10 O HETATM 2327 O HOH B 511 4.605 18.744 40.456 1.00 42.50 O HETATM 2328 O HOH B 512 -8.389 29.600 36.210 1.00 38.99 O HETATM 2329 O HOH B 513 2.583 26.970 19.835 0.76 23.45 O HETATM 2330 O HOH B 514 27.992 -12.847 21.438 0.75 30.74 O HETATM 2331 O HOH B 515 4.940 -12.724 35.520 0.92 25.21 O HETATM 2332 O HOH B 516 13.220 -14.732 16.588 0.80 24.96 O HETATM 2333 O HOH B 517 3.486 8.815 20.015 0.75 23.67 O HETATM 2334 O HOH B 518 -2.015 15.858 17.761 1.00 41.19 O HETATM 2335 O HOH B 519 33.671 -3.705 29.552 0.81 26.89 O HETATM 2336 O HOH B 520 9.093 21.954 38.650 0.97 46.79 O HETATM 2337 O HOH B 521 -6.533 16.313 36.872 0.76 23.43 O HETATM 2338 O HOH B 522 11.945 -1.296 41.083 0.74 28.76 O HETATM 2339 O HOH B 523 29.628 -5.458 13.631 0.94 41.57 O HETATM 2340 O HOH B 524 5.977 38.473 22.107 1.00 55.87 O HETATM 2341 O HOH B 525 -9.393 18.814 29.924 1.00 33.84 O HETATM 2342 O HOH B 526 20.365 -3.432 9.378 0.92 38.08 O HETATM 2343 O HOH B 527 21.407 -15.785 21.313 1.00 28.22 O HETATM 2344 O HOH B 528 3.659 -17.423 12.562 1.00 36.55 O HETATM 2345 O HOH B 529 19.234 10.492 11.074 0.76 26.98 O HETATM 2346 O HOH B 530 0.449 30.319 31.784 1.00 33.25 O HETATM 2347 O HOH B 531 13.517 -14.580 10.631 0.47 28.48 O HETATM 2348 O HOH B 532 29.274 10.330 26.918 1.00 38.96 O HETATM 2349 O HOH B 533 13.723 -16.996 24.395 0.62 27.07 O HETATM 2350 O HOH B 534 7.285 35.675 21.122 0.70 40.54 O HETATM 2351 O HOH B 535 14.369 -0.631 5.500 1.00 37.70 O HETATM 2352 O HOH B 536 6.201 9.741 20.277 0.66 19.98 O HETATM 2353 O HOH B 537 18.392 21.455 26.575 1.00 45.14 O HETATM 2354 O HOH B 538 30.494 3.435 34.964 0.71 27.53 O HETATM 2355 O HOH B 539 12.321 -10.745 38.746 1.00 41.52 O HETATM 2356 O HOH B 540 -6.329 -10.782 20.696 1.00 40.74 O HETATM 2357 O HOH B 541 14.544 -14.029 13.049 0.74 25.02 O HETATM 2358 O HOH B 542 8.529 12.776 16.912 1.00 43.35 O HETATM 2359 O HOH B 543 13.450 -7.993 6.726 1.00 35.04 O HETATM 2360 O HOH B 544 0.891 -2.274 37.203 0.73 38.39 O HETATM 2361 O HOH B 545 19.742 31.308 27.085 1.00 51.33 O HETATM 2362 O HOH B 546 0.794 -4.313 35.209 0.85 26.47 O HETATM 2363 O HOH B 547 20.484 12.715 16.191 0.73 31.27 O HETATM 2364 O HOH B 548 4.560 29.217 17.670 0.85 32.92 O HETATM 2365 O HOH B 549 17.930 33.018 27.109 0.95 33.84 O HETATM 2366 O HOH B 550 7.137 10.139 41.981 1.00 41.01 O HETATM 2367 O HOH B 551 11.424 25.472 34.513 0.85 25.04 O HETATM 2368 O HOH B 552 0.759 -0.060 37.073 0.72 23.49 O HETATM 2369 O HOH B 553 26.724 -13.055 30.605 1.00 59.59 O HETATM 2370 O HOH B 554 -2.476 -12.379 20.107 1.00 16.85 O HETATM 2371 O HOH B 555 12.744 23.338 36.261 1.00 47.83 O HETATM 2372 O HOH B 556 -9.459 27.314 38.025 1.00 35.51 O HETATM 2373 O HOH B 557 -1.811 10.552 38.047 0.98 45.54 O HETATM 2374 O HOH B 558 -14.258 36.268 28.915 1.00 34.48 O HETATM 2375 O HOH B 559 -4.242 -2.954 15.950 1.00 33.28 O HETATM 2376 O HOH B 560 4.211 9.573 40.946 0.86 36.80 O HETATM 2377 O HOH B 561 -11.218 19.327 31.983 0.82 35.09 O HETATM 2378 O HOH B 562 19.018 -16.588 21.069 1.00 31.83 O HETATM 2379 O HOH B 563 -0.005 -13.087 21.167 0.58 19.33 O HETATM 2380 O HOH B 564 -3.446 8.995 36.216 1.00 42.61 O HETATM 2381 O HOH B 565 4.101 16.368 15.238 1.00 48.47 O HETATM 2382 O HOH B 566 10.539 -17.073 26.394 1.00 34.04 O HETATM 2383 O HOH B 567 -1.734 33.214 23.687 1.00 50.01 O HETATM 2384 O HOH B 568 26.370 -4.974 38.171 0.67 18.98 O HETATM 2385 O HOH B 569 5.516 27.579 15.476 0.58 29.68 O HETATM 2386 O HOH B 570 17.423 16.680 33.261 0.60 32.27 O HETATM 2387 O HOH B 571 -5.788 25.447 40.336 0.79 31.65 O HETATM 2388 O HOH B 572 5.532 13.173 15.831 1.00 38.88 O HETATM 2389 O HOH B 573 -4.087 26.614 41.261 1.00 48.84 O HETATM 2390 O HOH B 574 -8.306 11.586 27.562 0.78 27.81 O HETATM 2391 O HOH B 575 23.134 -1.747 10.137 1.00 38.11 O HETATM 2392 O HOH B 576 16.945 -3.720 40.419 1.00 54.06 O HETATM 2393 O HOH B 577 20.466 14.627 32.592 0.68 21.77 O HETATM 2394 O HOH B 578 16.992 -6.223 4.580 1.00 37.83 O HETATM 2395 O HOH B 579 10.959 20.573 36.186 0.60 29.77 O HETATM 2396 O HOH B 580 4.515 6.335 15.979 0.94 37.14 O HETATM 2397 O HOH B 581 2.438 10.713 39.477 1.00 36.70 O HETATM 2398 O HOH B 582 2.117 -7.063 34.793 0.56 27.99 O HETATM 2399 O HOH B 583 13.904 -10.238 6.089 0.66 31.59 O HETATM 2400 O HOH B 584 0.596 35.921 24.170 1.00 35.50 O HETATM 2401 O HOH B 585 -5.786 -9.481 23.625 1.00 37.47 O HETATM 2402 O HOH B 586 25.975 2.694 14.248 0.80 32.42 O HETATM 2403 O HOH B 587 16.325 22.477 30.055 0.62 25.58 O HETATM 2404 O HOH B 588 32.649 -5.431 23.783 1.00 39.28 O HETATM 2405 O HOH B 589 23.512 12.218 16.297 1.00 41.92 O HETATM 2406 O HOH B 590 16.202 20.671 32.584 0.84 31.38 O HETATM 2407 O HOH B 591 -5.040 -1.855 13.658 0.72 36.65 O HETATM 2408 O HOH B 592 9.153 2.223 8.078 0.71 45.08 O HETATM 2409 O HOH B 593 23.066 -8.158 39.238 0.72 32.55 O HETATM 2410 O HOH B 594 -3.692 6.615 26.633 0.62 27.81 O HETATM 2411 O HOH B 595 17.707 -17.394 23.133 0.92 32.91 O HETATM 2412 O HOH B 596 -3.518 2.007 25.528 0.68 34.42 O HETATM 2413 O HOH B 597 23.561 4.525 34.631 0.61 28.21 O HETATM 2414 O HOH B 598 -4.110 10.071 27.280 0.71 25.80 O HETATM 2415 O HOH B 599 30.531 -9.053 36.929 1.00 48.28 O HETATM 2416 O HOH B 600 6.809 5.672 15.982 1.00 41.26 O HETATM 2417 O HOH B 601 -2.918 4.812 25.175 0.61 32.58 O HETATM 2418 O HOH B 602 12.659 15.250 17.261 0.67 37.79 O HETATM 2419 O HOH B 603 6.987 37.688 28.631 1.00 40.32 O HETATM 2420 O HOH B 604 13.734 26.145 33.291 0.69 36.61 O HETATM 2421 O HOH B 605 6.444 -16.138 21.395 0.91 27.80 O HETATM 2422 O HOH B 606 -0.260 4.072 34.235 0.82 27.61 O HETATM 2423 O HOH B 607 -0.543 -15.722 30.711 0.92 28.57 O HETATM 2424 O HOH B 608 2.348 33.437 34.910 0.89 29.49 O HETATM 2425 O HOH B 609 -14.741 22.331 26.775 1.00 41.66 O HETATM 2426 O HOH B 610 4.649 1.003 18.898 0.36 22.91 O HETATM 2427 O HOH B 611 13.640 -5.480 1.791 0.74 28.60 O HETATM 2428 O HOH B 612 33.706 1.959 22.313 1.00 35.25 O HETATM 2429 O HOH B 613 8.739 32.125 32.072 1.00 41.51 O HETATM 2430 O HOH B 614 -2.976 -11.450 27.008 1.00 44.38 O HETATM 2431 O HOH B 615 2.003 11.586 18.970 1.00 49.27 O HETATM 2432 O HOH B 616 22.548 3.619 8.719 1.00 46.24 O HETATM 2433 O HOH B 617 11.629 2.835 7.725 0.66 34.40 O HETATM 2434 O HOH B 618 -0.435 5.652 36.376 0.68 25.64 O HETATM 2435 O HOH B 619 23.662 -12.045 30.785 1.00 51.33 O HETATM 2436 O HOH B 620 24.400 14.746 29.313 0.85 39.51 O HETATM 2437 O HOH B 621 -1.991 -13.041 25.377 0.62 26.50 O HETATM 2438 O HOH B 622 23.442 4.703 10.987 1.00 39.99 O HETATM 2439 O HOH B 623 11.820 -4.447 42.284 0.86 34.79 O HETATM 2440 O HOH B 624 -3.086 10.959 23.829 0.60 26.45 O HETATM 2441 O HOH B 625 31.792 -5.050 17.672 0.93 35.78 O HETATM 2442 O HOH B 626 -13.816 24.843 23.884 0.73 38.01 O HETATM 2443 O HOH B 627 11.502 5.323 11.408 0.63 29.52 O HETATM 2444 O HOH B 628 29.092 -10.814 35.602 0.74 31.92 O HETATM 2445 O HOH B 629 3.285 7.039 41.865 0.60 29.82 O HETATM 2446 O HOH B 630 23.469 12.306 9.620 1.00 44.53 O HETATM 2447 O HOH B 631 3.984 25.380 16.213 1.00 54.74 O HETATM 2448 O HOH B 632 -4.833 -6.515 30.600 0.56 28.28 O HETATM 2449 O HOH B 633 29.617 8.428 24.815 1.00 39.93 O HETATM 2450 O HOH B 634 20.518 16.187 29.704 0.67 34.23 O HETATM 2451 O HOH B 635 -2.635 -1.722 4.604 0.97 36.20 O HETATM 2452 O HOH B 636 -1.170 1.342 36.366 1.00 46.14 O HETATM 2453 O HOH B 637 -2.992 -6.903 28.359 0.63 34.89 O HETATM 2454 O HOH B 638 0.899 30.996 20.291 1.00 55.39 O HETATM 2455 O HOH B 639 1.602 33.073 37.322 0.66 28.40 O HETATM 2456 O HOH B 640 19.392 31.457 32.655 1.00 51.59 O HETATM 2457 O HOH B 641 19.799 37.228 26.508 0.63 32.04 O HETATM 2458 O HOH B 642 17.967 27.350 31.668 1.00 47.65 O HETATM 2459 O HOH B 643 7.872 -6.175 39.316 0.59 38.40 O HETATM 2460 O HOH B 644 5.022 -8.631 37.926 0.67 32.88 O HETATM 2461 O HOH B 645 0.926 -0.843 24.647 0.59 31.42 O HETATM 2462 O HOH B 646 0.875 26.282 42.070 1.00 62.37 O HETATM 2463 O HOH B 647 35.848 -7.734 31.605 1.00 46.99 O HETATM 2464 O HOH B 648 1.866 12.140 16.298 1.00 53.44 O HETATM 2465 O HOH B 649 -14.396 30.956 29.518 1.00 54.45 O HETATM 2466 O HOH B 650 29.292 -3.474 16.859 0.69 31.71 O HETATM 2467 O HOH B 651 14.130 -17.179 15.264 0.93 50.88 O HETATM 2468 O HOH B 652 20.038 34.227 30.399 1.00 50.57 O HETATM 2469 O HOH B 653 20.489 -6.252 6.173 0.90 51.80 O HETATM 2470 O HOH B 654 28.327 0.032 16.052 1.00 44.43 O HETATM 2471 O HOH B 655 20.581 39.112 24.475 0.79 36.53 O HETATM 2472 O HOH B 656 5.542 32.443 21.469 0.98 32.98 O HETATM 2473 O HOH B 657 -3.175 21.611 41.358 1.00 36.44 O HETATM 2474 O HOH B 658 23.006 -15.905 25.746 1.00 42.27 O HETATM 2475 O HOH B 659 -10.516 -0.959 28.578 1.00 45.21 O HETATM 2476 O HOH B 660 -6.497 15.652 14.510 1.00 56.17 O HETATM 2477 O HOH B 661 22.137 -10.829 13.790 1.00 52.55 O HETATM 2478 O HOH B 662 -2.362 2.882 32.665 1.00 52.29 O HETATM 2479 O HOH B 663 23.634 17.865 27.272 0.78 44.86 O HETATM 2480 O HOH B 664 15.550 1.978 6.965 1.00 60.34 O HETATM 2481 O HOH B 665 20.018 -17.017 27.598 0.76 38.83 O HETATM 2482 O HOH B 666 8.800 13.328 42.748 0.69 29.60 O HETATM 2483 O HOH B 667 25.500 3.541 11.244 0.75 31.99 O HETATM 2484 O HOH B 668 3.538 34.073 20.840 1.00 45.99 O HETATM 2485 O HOH B 669 29.003 -11.299 31.340 1.00 55.82 O HETATM 2486 O HOH B 670 31.816 3.534 27.611 0.59 33.84 O HETATM 2487 O HOH B 671 31.300 4.435 25.427 0.62 29.13 O HETATM 2488 O HOH B 672 4.222 5.863 43.804 0.67 36.01 O HETATM 2489 O HOH B 673 25.442 6.044 11.958 1.00 58.39 O HETATM 2490 O HOH B 674 6.883 23.906 9.525 0.78 28.91 O HETATM 2491 O HOH B 675 9.648 -4.798 41.484 0.67 30.42 O HETATM 2492 O HOH B 676 0.640 9.508 37.580 1.00 45.91 O HETATM 2493 O HOH B 677 1.105 11.808 43.850 0.85 46.24 O HETATM 2494 O HOH B 678 21.266 -4.531 7.627 0.68 50.35 O HETATM 2495 O HOH B 679 0.292 6.671 38.526 0.73 39.46 O HETATM 2496 O HOH B 680 16.274 15.414 15.390 0.79 36.28 O HETATM 2497 O HOH B 681 12.043 16.676 13.194 0.88 45.24 O HETATM 2498 O HOH B 682 -2.269 3.115 13.489 1.00 64.35 O HETATM 2499 O HOH B 683 -5.147 12.410 34.858 0.76 33.26 O HETATM 2500 O HOH B 684 19.908 2.511 8.645 1.00 45.29 O HETATM 2501 O HOH B 685 28.990 -11.487 24.234 0.65 34.67 O HETATM 2502 O HOH B 686 7.482 23.369 36.034 0.80 39.09 O HETATM 2503 O HOH B 687 30.350 -2.525 14.256 0.98 46.31 O HETATM 2504 O HOH B 688 4.656 -17.732 19.052 1.00 48.46 O HETATM 2505 O HOH B 689 12.861 -0.427 3.279 0.73 33.41 O HETATM 2506 O HOH B 690 -0.558 32.490 21.280 0.73 43.71 O HETATM 2507 O HOH B 691 -5.158 22.532 39.993 0.69 34.44 O HETATM 2508 O HOH B 692 10.340 30.764 35.433 1.00 44.98 O HETATM 2509 O HOH B 693 -4.204 0.303 5.685 0.86 47.96 O HETATM 2510 O HOH B 694 29.757 -3.619 12.208 0.83 55.59 O HETATM 2511 O HOH B 695 21.643 -14.963 28.255 0.59 32.13 O HETATM 2512 O HOH B 696 24.647 10.343 15.965 0.79 51.01 O HETATM 2513 O HOH B 697 24.704 -10.323 13.673 1.00 45.52 O HETATM 2514 O HOH B 698 14.547 8.917 11.884 1.00 27.04 O HETATM 2515 O HOH B 699 -3.581 -14.556 18.736 1.00 44.99 O HETATM 2516 O HOH B 700 2.107 -2.364 7.282 1.00 40.11 O HETATM 2517 O HOH B 701 1.809 -1.841 0.713 1.00 29.21 O HETATM 2518 O HOH B 702 -4.499 -4.365 5.574 1.00 28.47 O HETATM 2519 O HOH B 703 16.345 -11.314 31.886 1.00 25.16 O HETATM 2520 O HOH B 704 20.284 -12.393 27.940 1.00 28.37 O ENDMDL CONECT 2192 2197 CONECT 2193 2194 2198 CONECT 2194 2193 2195 CONECT 2195 2194 2212 2196 CONECT 2196 2195 2197 2199 CONECT 2197 2196 2192 2198 CONECT 2198 2193 2197 CONECT 2199 2196 2200 2202 CONECT 2200 2199 2201 CONECT 2201 2200 2203 2204 CONECT 2202 2199 CONECT 2203 2201 CONECT 2204 2201 2205 2208 CONECT 2205 2204 2209 2206 CONECT 2206 2205 2210 2207 CONECT 2207 2206 2208 CONECT 2208 2204 2207 CONECT 2209 2205 CONECT 2210 2206 2211 CONECT 2211 2210 CONECT 2212 2195 END A second structure was input as follows:FoldX generated pdb file Output generated by If you find results from this site helpful for your research, please cite one of our papers:
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