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*** ***elNémo ID: 2511261730481320370Job options:ID = 2511261730481320370 JOBID = USERID = unknown PRIVAT = 0 NMODES = 5 DQMIN = -50 DQMAX = 50 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = 0 DORMSD = 0 NRBL = 0 CUTOFF = 0 CAONLY = 0 Input data for this run:ATOM 1 N SER A 1 -5.518 27.819 -4.954 1.00 46.51 N ANISOU 1 N SER A 1 6153 5764 5754 -4 78 196 N ATOM 2 CA SER A 1 -4.783 26.762 -5.718 1.00 45.79 C ANISOU 2 CA SER A 1 6082 5708 5608 -1 20 244 C ATOM 3 C SER A 1 -5.184 25.340 -5.277 1.00 44.26 C ANISOU 3 C SER A 1 5881 5656 5280 -33 -67 282 C ATOM 4 O SER A 1 -5.651 24.555 -6.090 1.00 44.55 O ANISOU 4 O SER A 1 5993 5738 5193 -39 -35 452 O ATOM 5 CB SER A 1 -3.269 27.008 -5.611 1.00 46.22 C ANISOU 5 CB SER A 1 6077 5778 5706 31 24 186 C ATOM 6 OG SER A 1 -2.508 25.865 -5.957 1.00 48.47 O ANISOU 6 OG SER A 1 6579 5711 6125 2 25 -34 O ATOM 7 N THR A 2 -4.996 25.013 -3.997 1.00 41.81 N ANISOU 7 N THR A 2 5493 5492 4900 0 -98 319 N ATOM 8 CA THR A 2 -5.478 23.737 -3.466 1.00 39.68 C ANISOU 8 CA THR A 2 5199 5334 4543 71 -215 251 C ATOM 9 C THR A 2 -6.682 23.912 -2.547 1.00 38.03 C ANISOU 9 C THR A 2 4951 5201 4297 106 -318 246 C ATOM 10 O THR A 2 -7.329 22.913 -2.195 1.00 36.78 O ANISOU 10 O THR A 2 4771 5196 4005 112 -288 327 O ATOM 11 CB THR A 2 -4.385 22.932 -2.693 1.00 40.15 C ANISOU 11 CB THR A 2 5239 5304 4710 60 -139 274 C ATOM 12 CG2 THR A 2 -3.392 22.255 -3.677 1.00 41.22 C ANISOU 12 CG2 THR A 2 5355 5388 4917 141 -47 140 C ATOM 13 OG1 THR A 2 -3.684 23.794 -1.789 1.00 41.21 O ANISOU 13 OG1 THR A 2 5559 5456 4640 200 -269 278 O ATOM 14 N ALA A 3 -6.992 25.161 -2.196 1.00 36.03 N ANISOU 14 N ALA A 3 4755 5133 3800 122 -471 220 N ATOM 15 CA ALA A 3 -8.076 25.459 -1.251 1.00 35.52 C ANISOU 15 CA ALA A 3 4691 4986 3816 170 -459 230 C ATOM 16 C ALA A 3 -9.412 24.995 -1.772 1.00 35.27 C ANISOU 16 C ALA A 3 4686 4925 3787 209 -353 192 C ATOM 17 O ALA A 3 -9.734 25.206 -2.940 1.00 33.63 O ANISOU 17 O ALA A 3 4593 4765 3419 311 -523 321 O ATOM 18 CB ALA A 3 -8.128 26.920 -0.931 1.00 36.00 C ANISOU 18 CB ALA A 3 4749 5043 3884 221 -462 159 C ATOM 19 N GLY A 4 -10.170 24.338 -0.908 1.00 34.93 N ANISOU 19 N GLY A 4 4627 4845 3799 249 -290 229 N ATOM 20 CA GLY A 4 -11.488 23.841 -1.276 1.00 34.03 C ANISOU 20 CA GLY A 4 4545 4674 3710 174 -254 50 C ATOM 21 C GLY A 4 -11.537 22.480 -1.940 1.00 34.45 C ANISOU 21 C GLY A 4 4576 4578 3935 220 -169 87 C ATOM 22 O GLY A 4 -12.641 21.935 -2.152 1.00 34.52 O ANISOU 22 O GLY A 4 4601 4668 3846 369 -294 90 O ATOM 23 N LYS A 5 -10.362 21.917 -2.248 1.00 33.76 N ANISOU 23 N LYS A 5 4676 4359 3791 320 -276 6 N ATOM 24 CA LYS A 5 -10.304 20.599 -2.886 1.00 35.78 C ANISOU 24 CA LYS A 5 4867 4598 4127 271 -94 -81 C ATOM 25 C LYS A 5 -9.420 19.606 -2.185 1.00 35.15 C ANISOU 25 C LYS A 5 4759 4599 3995 276 -99 -103 C ATOM 26 O LYS A 5 -8.561 19.945 -1.330 1.00 36.50 O ANISOU 26 O LYS A 5 4961 4764 4142 262 -4 -238 O ATOM 27 CB LYS A 5 -9.921 20.687 -4.350 1.00 36.34 C ANISOU 27 CB LYS A 5 4904 4605 4297 298 -6 -44 C ATOM 28 CG LYS A 5 -8.924 21.745 -4.669 1.00 38.79 C ANISOU 28 CG LYS A 5 5259 4759 4721 50 -80 -200 C ATOM 29 CD LYS A 5 -9.223 22.308 -6.097 1.00 39.61 C ANISOU 29 CD LYS A 5 5231 4971 4846 218 -41 148 C ATOM 30 CE LYS A 5 -8.217 23.378 -6.430 1.00 40.40 C ANISOU 30 CE LYS A 5 5137 5111 5101 122 -107 -77 C ATOM 31 NZ LYS A 5 -7.682 23.285 -7.820 1.00 38.81 N1+ ANISOU 31 NZ LYS A 5 4798 5324 4622 161 -400 127 N1+ ATOM 32 N VAL A 6 -9.670 18.355 -2.526 1.00 34.86 N ANISOU 32 N VAL A 6 4732 4644 3866 305 -45 -61 N ATOM 33 CA VAL A 6 -8.877 17.261 -2.027 1.00 34.46 C ANISOU 33 CA VAL A 6 4678 4645 3771 245 -114 -30 C ATOM 34 C VAL A 6 -7.420 17.406 -2.439 1.00 33.62 C ANISOU 34 C VAL A 6 4654 4550 3568 247 -34 -95 C ATOM 35 O VAL A 6 -7.106 17.736 -3.601 1.00 33.68 O ANISOU 35 O VAL A 6 4769 4640 3387 339 -92 52 O ATOM 36 CB VAL A 6 -9.427 15.921 -2.518 1.00 34.80 C ANISOU 36 CB VAL A 6 4687 4686 3848 233 -67 -200 C ATOM 37 CG1 VAL A 6 -8.526 14.794 -2.108 1.00 35.79 C ANISOU 37 CG1 VAL A 6 4893 4913 3793 302 -342 62 C ATOM 38 CG2 VAL A 6 -10.825 15.679 -1.982 1.00 35.86 C ANISOU 38 CG2 VAL A 6 4790 4824 4011 91 36 -38 C ATOM 39 N ILE A 7 -6.531 17.169 -1.472 1.00 32.49 N ANISOU 39 N ILE A 7 4524 4497 3321 210 -166 -120 N ATOM 40 CA ILE A 7 -5.089 17.046 -1.738 1.00 33.52 C ANISOU 40 CA ILE A 7 4672 4576 3489 33 -62 -216 C ATOM 41 C ILE A 7 -4.602 15.585 -1.731 1.00 33.49 C ANISOU 41 C ILE A 7 4610 4607 3506 129 45 -221 C ATOM 42 O ILE A 7 -4.802 14.857 -0.760 1.00 34.44 O ANISOU 42 O ILE A 7 4829 4543 3713 103 7 -223 O ATOM 43 CB ILE A 7 -4.267 17.896 -0.714 1.00 33.96 C ANISOU 43 CB ILE A 7 4665 4573 3663 17 -110 -256 C ATOM 44 CG1 ILE A 7 -4.472 19.389 -0.992 1.00 33.32 C ANISOU 44 CG1 ILE A 7 4749 4527 3384 15 -95 -228 C ATOM 45 CG2 ILE A 7 -2.789 17.536 -0.780 1.00 36.45 C ANISOU 45 CG2 ILE A 7 4771 4766 4310 111 -209 -326 C ATOM 46 CD1 ILE A 7 -3.802 20.348 0.073 1.00 34.76 C ANISOU 46 CD1 ILE A 7 4801 4600 3804 -81 -129 -238 C ATOM 47 N LYS A 8 -3.954 15.146 -2.812 1.00 33.50 N ANISOU 47 N LYS A 8 4629 4576 3523 181 25 -377 N ATOM 48 CA LYS A 8 -3.310 13.826 -2.835 1.00 34.72 C ANISOU 48 CA LYS A 8 4707 4706 3778 190 31 -312 C ATOM 49 C LYS A 8 -1.866 14.032 -2.377 1.00 33.27 C ANISOU 49 C LYS A 8 4560 4483 3597 216 42 -289 C ATOM 50 O LYS A 8 -1.136 14.833 -2.966 1.00 33.07 O ANISOU 50 O LYS A 8 4595 4392 3578 378 -29 -105 O ATOM 51 CB LYS A 8 -3.317 13.239 -4.274 1.00 35.37 C ANISOU 51 CB LYS A 8 4795 4837 3805 192 91 -398 C ATOM 52 CG LYS A 8 -4.719 13.095 -4.859 1.00 36.34 C ANISOU 52 CG LYS A 8 4844 5084 3879 187 7 -350 C ATOM 53 CD LYS A 8 -4.829 12.204 -6.109 1.00 38.48 C ANISOU 53 CD LYS A 8 5115 5074 4432 118 -203 -398 C ATOM 54 CE LYS A 8 -6.272 12.159 -6.588 1.00 41.35 C ANISOU 54 CE LYS A 8 5142 5430 5139 -83 -142 -263 C ATOM 55 NZ LYS A 8 -6.428 11.735 -7.995 1.00 44.91 N1+ ANISOU 55 NZ LYS A 8 5834 5768 5458 -8 155 -197 N1+ ATOM 56 N CYS A 9 -1.442 13.308 -1.346 1.00 32.05 N ANISOU 56 N CYS A 9 4414 4276 3485 175 184 -279 N ATOM 57 CA CYS A 9 -0.089 13.437 -0.824 1.00 31.48 C ANISOU 57 CA CYS A 9 4394 4134 3433 65 160 -239 C ATOM 58 C CYS A 9 0.363 12.103 -0.227 1.00 31.65 C ANISOU 58 C CYS A 9 4353 4099 3572 118 163 -306 C ATOM 59 O CYS A 9 -0.384 11.124 -0.247 1.00 32.86 O ANISOU 59 O CYS A 9 4308 4224 3952 48 76 -261 O ATOM 60 CB CYS A 9 -0.032 14.546 0.235 1.00 30.97 C ANISOU 60 CB CYS A 9 4286 4182 3297 86 215 -214 C ATOM 61 SG CYS A 9 -0.905 14.151 1.756 1.00 32.28 S ANISOU 61 SG CYS A 9 4808 4253 3201 -175 368 -553 S ATOM 62 N LYS A 10 1.571 12.068 0.319 1.00 30.26 N ANISOU 62 N LYS A 10 4314 3949 3232 163 91 -273 N ATOM 63 CA LYS A 10 2.040 10.863 1.013 1.00 31.06 C ANISOU 63 CA LYS A 10 4466 4011 3321 84 75 -278 C ATOM 64 C LYS A 10 1.830 10.965 2.526 1.00 30.06 C ANISOU 64 C LYS A 10 4261 3848 3310 69 146 -321 C ATOM 65 O LYS A 10 1.943 12.045 3.116 1.00 29.66 O ANISOU 65 O LYS A 10 4090 3832 3346 -90 -53 -383 O ATOM 66 CB LYS A 10 3.499 10.632 0.729 1.00 32.23 C ANISOU 66 CB LYS A 10 4552 4124 3567 126 83 -265 C ATOM 67 CG LYS A 10 3.808 10.128 -0.704 1.00 34.91 C ANISOU 67 CG LYS A 10 4905 4619 3739 215 248 -154 C ATOM 68 CD LYS A 10 5.304 10.003 -0.880 1.00 40.75 C ANISOU 68 CD LYS A 10 5407 5290 4784 165 282 32 C ATOM 69 CE LYS A 10 5.664 9.193 -2.115 1.00 43.94 C ANISOU 69 CE LYS A 10 6000 5713 4982 120 136 -185 C ATOM 70 NZ LYS A 10 4.685 9.343 -3.233 1.00 46.26 N1+ ANISOU 70 NZ LYS A 10 6064 5850 5661 422 -68 -81 N1+ ATOM 71 N ALA A 11 1.539 9.831 3.141 1.00 29.07 N ANISOU 71 N ALA A 11 4098 3774 3171 125 110 -304 N ATOM 72 CA ALA A 11 1.483 9.757 4.589 1.00 29.08 C ANISOU 72 CA ALA A 11 4104 3700 3244 77 142 -348 C ATOM 73 C ALA A 11 2.017 8.405 5.047 1.00 29.37 C ANISOU 73 C ALA A 11 4174 3703 3279 84 134 -348 C ATOM 74 O ALA A 11 2.102 7.438 4.236 1.00 30.30 O ANISOU 74 O ALA A 11 4220 3792 3500 53 53 -386 O ATOM 75 CB ALA A 11 0.070 9.994 5.092 1.00 28.77 C ANISOU 75 CB ALA A 11 3993 3578 3359 233 47 -439 C ATOM 76 N ALA A 12 2.418 8.347 6.316 1.00 28.88 N ANISOU 76 N ALA A 12 4029 3676 3267 82 104 -341 N ATOM 77 CA ALA A 12 2.779 7.075 6.916 1.00 28.39 C ANISOU 77 CA ALA A 12 3980 3621 3186 -75 122 -317 C ATOM 78 C ALA A 12 1.563 6.525 7.617 1.00 28.88 C ANISOU 78 C ALA A 12 4063 3603 3305 -32 187 -449 C ATOM 79 O ALA A 12 1.128 7.049 8.632 1.00 28.25 O ANISOU 79 O ALA A 12 4239 3488 3006 -32 233 -635 O ATOM 80 CB ALA A 12 3.968 7.238 7.888 1.00 28.35 C ANISOU 80 CB ALA A 12 3931 3674 3167 -174 145 -331 C ATOM 81 N VAL A 13 0.992 5.472 7.034 1.00 28.01 N ANISOU 81 N VAL A 13 3903 3440 3297 -82 159 -582 N ATOM 82 CA VAL A 13 -0.147 4.753 7.598 1.00 29.03 C ANISOU 82 CA VAL A 13 3997 3594 3438 -23 190 -431 C ATOM 83 C VAL A 13 0.269 3.526 8.424 1.00 29.43 C ANISOU 83 C VAL A 13 4068 3585 3526 0 301 -438 C ATOM 84 O VAL A 13 1.121 2.725 8.014 1.00 29.91 O ANISOU 84 O VAL A 13 4096 3597 3672 4 445 -474 O ATOM 85 CB VAL A 13 -1.118 4.280 6.460 1.00 28.09 C ANISOU 85 CB VAL A 13 3905 3419 3347 -109 106 -446 C ATOM 86 CG1 VAL A 13 -2.311 3.529 7.057 1.00 29.87 C ANISOU 86 CG1 VAL A 13 3903 3733 3711 -294 127 -572 C ATOM 87 CG2 VAL A 13 -1.637 5.462 5.635 1.00 29.90 C ANISOU 87 CG2 VAL A 13 4071 3642 3648 52 192 -241 C ATOM 88 N LEU A 14 -0.368 3.361 9.576 1.00 29.13 N ANISOU 88 N LEU A 14 4083 3594 3387 43 382 -400 N ATOM 89 CA LEU A 14 -0.223 2.147 10.374 1.00 30.33 C ANISOU 89 CA LEU A 14 4252 3677 3593 56 322 -464 C ATOM 90 C LEU A 14 -1.498 1.352 10.145 1.00 30.31 C ANISOU 90 C LEU A 14 4223 3596 3695 36 394 -527 C ATOM 91 O LEU A 14 -2.585 1.741 10.598 1.00 29.98 O ANISOU 91 O LEU A 14 4042 3772 3576 -117 474 -553 O ATOM 92 CB LEU A 14 -0.030 2.494 11.858 1.00 30.69 C ANISOU 92 CB LEU A 14 4227 3836 3598 17 309 -397 C ATOM 93 CG LEU A 14 0.358 1.324 12.777 1.00 31.61 C ANISOU 93 CG LEU A 14 4358 3867 3783 -11 322 -391 C ATOM 94 CD1 LEU A 14 1.752 0.706 12.468 1.00 32.63 C ANISOU 94 CD1 LEU A 14 4253 4300 3843 38 228 -524 C ATOM 95 CD2 LEU A 14 0.267 1.742 14.271 1.00 32.30 C ANISOU 95 CD2 LEU A 14 4601 4003 3665 10 339 -391 C ATOM 96 N TRP A 15 -1.385 0.274 9.370 1.00 31.76 N ANISOU 96 N TRP A 15 4464 3750 3850 -20 359 -662 N ATOM 97 CA TRP A 15 -2.580 -0.470 8.983 1.00 32.23 C ANISOU 97 CA TRP A 15 4623 3738 3882 -53 421 -702 C ATOM 98 C TRP A 15 -3.054 -1.380 10.116 1.00 33.98 C ANISOU 98 C TRP A 15 4794 3998 4119 0 482 -665 C ATOM 99 O TRP A 15 -4.224 -1.695 10.202 1.00 36.12 O ANISOU 99 O TRP A 15 4924 4363 4435 91 434 -653 O ATOM 100 CB TRP A 15 -2.273 -1.316 7.737 1.00 32.57 C ANISOU 100 CB TRP A 15 4642 3772 3959 -83 340 -707 C ATOM 101 CG TRP A 15 -2.143 -0.487 6.520 1.00 32.38 C ANISOU 101 CG TRP A 15 4653 3730 3920 -199 224 -777 C ATOM 102 CD1 TRP A 15 -0.998 -0.213 5.838 1.00 34.12 C ANISOU 102 CD1 TRP A 15 4653 4151 4160 -310 106 -514 C ATOM 103 CD2 TRP A 15 -3.204 0.163 5.803 1.00 33.03 C ANISOU 103 CD2 TRP A 15 4683 3798 4068 -247 204 -624 C ATOM 104 CE2 TRP A 15 -2.622 0.805 4.691 1.00 31.96 C ANISOU 104 CE2 TRP A 15 4664 3561 3917 -351 117 -505 C ATOM 105 CE3 TRP A 15 -4.585 0.227 5.966 1.00 32.91 C ANISOU 105 CE3 TRP A 15 4673 3699 4129 -46 -43 -848 C ATOM 106 NE1 TRP A 15 -1.274 0.564 4.740 1.00 34.62 N ANISOU 106 NE1 TRP A 15 4831 4146 4178 -120 97 -530 N ATOM 107 CZ2 TRP A 15 -3.370 1.540 3.776 1.00 33.15 C ANISOU 107 CZ2 TRP A 15 4516 4010 4068 -138 89 -820 C ATOM 108 CZ3 TRP A 15 -5.326 0.970 5.061 1.00 33.56 C ANISOU 108 CZ3 TRP A 15 4886 3966 3898 -135 91 -580 C ATOM 109 CH2 TRP A 15 -4.719 1.605 3.979 1.00 35.38 C ANISOU 109 CH2 TRP A 15 4800 4239 4403 -144 105 -550 C ATOM 110 N GLU A 16 -2.116 -1.818 10.947 1.00 35.45 N ANISOU 110 N GLU A 16 4983 4177 4309 24 454 -526 N ATOM 111 CA GLU A 16 -2.345 -2.842 11.958 1.00 38.09 C ANISOU 111 CA GLU A 16 5253 4496 4723 -21 386 -333 C ATOM 112 C GLU A 16 -1.266 -2.696 13.003 1.00 37.76 C ANISOU 112 C GLU A 16 5254 4436 4655 -68 385 -295 C ATOM 113 O GLU A 16 -0.156 -2.233 12.694 1.00 37.88 O ANISOU 113 O GLU A 16 5268 4502 4622 -158 536 -343 O ATOM 114 CB GLU A 16 -2.245 -4.242 11.326 1.00 39.52 C ANISOU 114 CB GLU A 16 5470 4562 4982 -4 287 -289 C ATOM 115 CG GLU A 16 -3.528 -4.752 10.663 1.00 44.91 C ANISOU 115 CG GLU A 16 5845 5340 5878 -53 147 -182 C ATOM 116 CD GLU A 16 -3.276 -5.380 9.305 1.00 49.11 C ANISOU 116 CD GLU A 16 6445 5915 6300 32 47 -325 C ATOM 117 OE1 GLU A 16 -2.335 -6.216 9.191 1.00 51.39 O ANISOU 117 OE1 GLU A 16 6562 6087 6875 86 -1 -279 O ATOM 118 OE2 GLU A 16 -4.012 -5.032 8.341 1.00 53.38 O1- ANISOU 118 OE2 GLU A 16 6991 6266 7024 211 -99 -24 O1- ATOM 119 N GLU A 17 -1.566 -3.125 14.229 1.00 38.28 N ANISOU 119 N GLU A 17 5387 4448 4709 -37 380 -261 N ATOM 120 CA GLU A 17 -0.581 -3.133 15.324 1.00 38.51 C ANISOU 120 CA GLU A 17 5383 4516 4733 2 350 -98 C ATOM 121 C GLU A 17 0.651 -3.929 14.938 1.00 38.59 C ANISOU 121 C GLU A 17 5484 4447 4731 -20 382 -68 C ATOM 122 O GLU A 17 0.554 -4.860 14.125 1.00 38.01 O ANISOU 122 O GLU A 17 5539 4230 4671 -35 445 -100 O ATOM 123 CB GLU A 17 -1.177 -3.839 16.543 1.00 39.42 C ANISOU 123 CB GLU A 17 5458 4697 4821 -29 356 -55 C ATOM 124 CG GLU A 17 -2.052 -3.035 17.446 1.00 43.05 C ANISOU 124 CG GLU A 17 5720 5062 5572 58 294 -120 C ATOM 125 CD GLU A 17 -2.582 -3.901 18.576 1.00 47.31 C ANISOU 125 CD GLU A 17 6109 5866 6001 -56 319 113 C ATOM 126 OE1 GLU A 17 -1.752 -4.527 19.266 1.00 49.24 O ANISOU 126 OE1 GLU A 17 6263 6076 6370 -48 281 160 O ATOM 127 OE2 GLU A 17 -3.822 -3.985 18.753 1.00 51.29 O1- ANISOU 127 OE2 GLU A 17 6328 6282 6878 -88 405 -37 O1- ATOM 128 N LYS A 18 1.792 -3.574 15.536 1.00 38.18 N ANISOU 128 N LYS A 18 5405 4340 4760 16 422 -82 N ATOM 129 CA LYS A 18 3.033 -4.358 15.433 1.00 39.15 C ANISOU 129 CA LYS A 18 5501 4455 4919 7 426 -46 C ATOM 130 C LYS A 18 3.473 -4.573 13.983 1.00 39.04 C ANISOU 130 C LYS A 18 5567 4408 4859 40 432 -211 C ATOM 131 O LYS A 18 3.938 -5.667 13.601 1.00 40.20 O ANISOU 131 O LYS A 18 5636 4471 5165 111 513 -138 O ATOM 132 CB LYS A 18 2.892 -5.702 16.163 1.00 39.13 C ANISOU 132 CB LYS A 18 5542 4333 4990 -16 387 -53 C ATOM 133 CG LYS A 18 2.572 -5.588 17.650 1.00 41.29 C ANISOU 133 CG LYS A 18 5606 4818 5261 -94 387 69 C ATOM 134 CD LYS A 18 2.121 -6.953 18.190 1.00 44.42 C ANISOU 134 CD LYS A 18 6035 4937 5906 -133 205 209 C ATOM 135 CE LYS A 18 0.727 -7.306 17.654 1.00 47.14 C ANISOU 135 CE LYS A 18 6023 5548 6339 -3 -11 202 C ATOM 136 NZ LYS A 18 0.279 -8.711 17.967 1.00 49.07 N1+ ANISOU 136 NZ LYS A 18 6294 5691 6658 -88 13 250 N1+ ATOM 137 N LYS A 19 3.314 -3.527 13.176 1.00 38.04 N ANISOU 137 N LYS A 19 5471 4332 4649 25 484 -282 N ATOM 138 CA LYS A 19 3.775 -3.510 11.775 1.00 37.04 C ANISOU 138 CA LYS A 19 5276 4323 4472 38 547 -401 C ATOM 139 C LYS A 19 4.591 -2.233 11.549 1.00 36.15 C ANISOU 139 C LYS A 19 5190 4263 4280 35 556 -468 C ATOM 140 O LYS A 19 4.404 -1.238 12.275 1.00 35.63 O ANISOU 140 O LYS A 19 5229 4073 4234 -18 664 -553 O ATOM 141 CB LYS A 19 2.587 -3.518 10.802 1.00 38.17 C ANISOU 141 CB LYS A 19 5396 4564 4544 6 549 -465 C ATOM 142 CG LYS A 19 1.649 -4.735 10.872 1.00 39.52 C ANISOU 142 CG LYS A 19 5467 4654 4894 -29 431 -256 C ATOM 143 CD LYS A 19 2.151 -5.903 10.029 1.00 43.69 C ANISOU 143 CD LYS A 19 6018 5063 5516 2 279 -530 C ATOM 144 CE LYS A 19 1.133 -7.059 10.044 1.00 45.06 C ANISOU 144 CE LYS A 19 6079 5225 5815 -158 243 -471 C ATOM 145 NZ LYS A 19 1.487 -8.116 9.039 1.00 50.34 N1+ ANISOU 145 NZ LYS A 19 6728 5754 6642 386 400 -376 N1+ ATOM 146 N PRO A 20 5.496 -2.233 10.555 1.00 35.17 N ANISOU 146 N PRO A 20 5055 4197 4110 58 586 -579 N ATOM 147 CA PRO A 20 6.144 -0.982 10.171 1.00 34.45 C ANISOU 147 CA PRO A 20 4937 4162 3991 147 556 -472 C ATOM 148 C PRO A 20 5.120 -0.020 9.602 1.00 34.10 C ANISOU 148 C PRO A 20 4742 4275 3936 124 431 -442 C ATOM 149 O PRO A 20 4.049 -0.459 9.157 1.00 34.49 O ANISOU 149 O PRO A 20 4867 4215 4023 106 331 -448 O ATOM 150 CB PRO A 20 7.118 -1.408 9.047 1.00 35.06 C ANISOU 150 CB PRO A 20 4989 4310 4021 28 624 -449 C ATOM 151 CG PRO A 20 6.569 -2.672 8.538 1.00 36.25 C ANISOU 151 CG PRO A 20 5198 4264 4310 -17 626 -483 C ATOM 152 CD PRO A 20 5.975 -3.366 9.732 1.00 35.44 C ANISOU 152 CD PRO A 20 5159 4187 4119 162 588 -516 C ATOM 153 N PHE A 21 5.443 1.276 9.630 1.00 32.63 N ANISOU 153 N PHE A 21 4496 4115 3786 219 339 -343 N ATOM 154 CA PHE A 21 4.624 2.276 8.938 1.00 32.82 C ANISOU 154 CA PHE A 21 4555 4211 3702 212 230 -332 C ATOM 155 C PHE A 21 4.725 2.052 7.441 1.00 32.39 C ANISOU 155 C PHE A 21 4425 4207 3674 202 335 -439 C ATOM 156 O PHE A 21 5.790 1.669 6.898 1.00 33.51 O ANISOU 156 O PHE A 21 4237 4538 3953 185 339 -397 O ATOM 157 CB PHE A 21 5.077 3.696 9.271 1.00 31.95 C ANISOU 157 CB PHE A 21 4353 4101 3684 195 338 -343 C ATOM 158 CG PHE A 21 4.851 4.065 10.720 1.00 31.45 C ANISOU 158 CG PHE A 21 4302 4109 3535 309 153 -293 C ATOM 159 CD1 PHE A 21 3.623 4.539 11.132 1.00 32.04 C ANISOU 159 CD1 PHE A 21 4298 4070 3803 281 122 -185 C ATOM 160 CD2 PHE A 21 5.862 3.870 11.672 1.00 30.62 C ANISOU 160 CD2 PHE A 21 4166 3875 3591 370 38 -248 C ATOM 161 CE1 PHE A 21 3.402 4.833 12.458 1.00 30.46 C ANISOU 161 CE1 PHE A 21 4008 3931 3633 631 96 -178 C ATOM 162 CE2 PHE A 21 5.653 4.175 13.011 1.00 31.65 C ANISOU 162 CE2 PHE A 21 4011 3992 4021 482 305 -366 C ATOM 163 CZ PHE A 21 4.421 4.645 13.412 1.00 30.10 C ANISOU 163 CZ PHE A 21 3759 3781 3894 490 58 -424 C ATOM 164 N SER A 22 3.600 2.244 6.767 1.00 32.43 N ANISOU 164 N SER A 22 4473 4282 3564 163 304 -366 N ATOM 165 CA SER A 22 3.584 2.063 5.314 1.00 33.67 C ANISOU 165 CA SER A 22 4610 4401 3780 35 167 -375 C ATOM 166 C SER A 22 3.473 3.448 4.699 1.00 32.28 C ANISOU 166 C SER A 22 4408 4261 3596 -12 222 -375 C ATOM 167 O SER A 22 2.523 4.190 4.998 1.00 31.67 O ANISOU 167 O SER A 22 4304 4238 3491 -60 284 -405 O ATOM 168 CB SER A 22 2.361 1.225 4.891 1.00 34.82 C ANISOU 168 CB SER A 22 4620 4414 4193 -8 183 -287 C ATOM 169 OG SER A 22 2.306 -0.012 5.587 1.00 39.77 O ANISOU 169 OG SER A 22 5291 4918 4901 13 148 0 O ATOM 170 N ILE A 23 4.417 3.810 3.830 1.00 31.56 N ANISOU 170 N ILE A 23 4350 4234 3407 -6 236 -520 N ATOM 171 CA ILE A 23 4.277 5.067 3.127 1.00 32.17 C ANISOU 171 CA ILE A 23 4369 4353 3500 73 263 -480 C ATOM 172 C ILE A 23 3.234 4.866 2.030 1.00 31.88 C ANISOU 172 C ILE A 23 4379 4271 3462 94 221 -518 C ATOM 173 O ILE A 23 3.430 4.040 1.091 1.00 33.59 O ANISOU 173 O ILE A 23 4807 4372 3580 227 191 -679 O ATOM 174 CB ILE A 23 5.617 5.566 2.519 1.00 32.77 C ANISOU 174 CB ILE A 23 4313 4393 3744 25 222 -467 C ATOM 175 CG1 ILE A 23 6.676 5.815 3.624 1.00 32.62 C ANISOU 175 CG1 ILE A 23 4197 4525 3673 -58 278 -450 C ATOM 176 CG2 ILE A 23 5.399 6.838 1.708 1.00 34.67 C ANISOU 176 CG2 ILE A 23 4526 4710 3935 79 213 -258 C ATOM 177 CD1 ILE A 23 6.270 6.835 4.693 1.00 35.66 C ANISOU 177 CD1 ILE A 23 4620 4865 4062 12 77 -561 C ATOM 178 N GLU A 24 2.166 5.661 2.087 1.00 31.07 N ANISOU 178 N GLU A 24 4320 4188 3296 85 208 -491 N ATOM 179 CA GLU A 24 1.041 5.491 1.132 1.00 31.32 C ANISOU 179 CA GLU A 24 4364 4152 3383 -29 91 -610 C ATOM 180 C GLU A 24 0.646 6.826 0.512 1.00 32.04 C ANISOU 180 C GLU A 24 4432 4305 3434 -64 91 -587 C ATOM 181 O GLU A 24 0.859 7.883 1.122 1.00 31.93 O ANISOU 181 O GLU A 24 4494 4116 3520 -168 170 -584 O ATOM 182 CB GLU A 24 -0.204 4.945 1.837 1.00 31.98 C ANISOU 182 CB GLU A 24 4537 4149 3465 -17 89 -617 C ATOM 183 CG GLU A 24 -0.064 3.649 2.625 1.00 33.31 C ANISOU 183 CG GLU A 24 4893 3953 3808 46 108 -660 C ATOM 184 CD GLU A 24 -0.033 2.378 1.728 1.00 35.28 C ANISOU 184 CD GLU A 24 5239 4029 4136 -16 115 -618 C ATOM 185 OE1 GLU A 24 -0.275 2.464 0.500 1.00 35.77 O ANISOU 185 OE1 GLU A 24 5363 3915 4312 -78 -234 -604 O ATOM 186 OE2 GLU A 24 0.224 1.295 2.289 1.00 34.63 O1- ANISOU 186 OE2 GLU A 24 4912 3633 4613 54 253 -707 O1- ATOM 187 N GLU A 25 0.013 6.770 -0.668 1.00 31.87 N ANISOU 187 N GLU A 25 4303 4411 3393 -62 38 -672 N ATOM 188 CA GLU A 25 -0.666 7.905 -1.258 1.00 34.15 C ANISOU 188 CA GLU A 25 4542 4623 3809 -42 81 -588 C ATOM 189 C GLU A 25 -2.019 7.992 -0.583 1.00 33.41 C ANISOU 189 C GLU A 25 4437 4516 3739 -11 66 -632 C ATOM 190 O GLU A 25 -2.818 7.038 -0.618 1.00 34.21 O ANISOU 190 O GLU A 25 4454 4646 3895 -73 225 -877 O ATOM 191 CB GLU A 25 -0.890 7.696 -2.781 1.00 34.40 C ANISOU 191 CB GLU A 25 4569 4753 3746 44 61 -627 C ATOM 192 CG GLU A 25 0.361 7.704 -3.677 1.00 37.26 C ANISOU 192 CG GLU A 25 4882 4762 4511 -71 168 -514 C ATOM 193 CD GLU A 25 -0.003 7.662 -5.155 1.00 38.63 C ANISOU 193 CD GLU A 25 5045 5111 4520 22 174 -380 C ATOM 194 OE1 GLU A 25 -1.129 8.103 -5.531 1.00 43.35 O ANISOU 194 OE1 GLU A 25 5459 5409 5603 97 -328 -113 O ATOM 195 OE2 GLU A 25 0.826 7.192 -5.960 1.00 44.29 O1- ANISOU 195 OE2 GLU A 25 6052 5255 5519 221 613 -567 O1- ATOM 196 N VAL A 26 -2.277 9.120 0.055 1.00 32.22 N ANISOU 196 N VAL A 26 4290 4476 3474 16 25 -578 N ATOM 197 CA VAL A 26 -3.574 9.341 0.703 1.00 31.48 C ANISOU 197 CA VAL A 26 4259 4412 3287 16 -23 -493 C ATOM 198 C VAL A 26 -4.256 10.556 0.101 1.00 31.29 C ANISOU 198 C VAL A 26 4253 4345 3290 0 -9 -497 C ATOM 199 O VAL A 26 -3.617 11.344 -0.605 1.00 33.00 O ANISOU 199 O VAL A 26 4194 4660 3684 124 71 -424 O ATOM 200 CB VAL A 26 -3.388 9.493 2.233 1.00 31.11 C ANISOU 200 CB VAL A 26 4330 4316 3172 34 -46 -475 C ATOM 201 CG1 VAL A 26 -2.793 8.224 2.844 1.00 31.82 C ANISOU 201 CG1 VAL A 26 4392 4208 3487 -151 57 -531 C ATOM 202 CG2 VAL A 26 -2.507 10.731 2.548 1.00 32.13 C ANISOU 202 CG2 VAL A 26 4526 4304 3376 -52 -56 -395 C ATOM 203 N GLU A 27 -5.558 10.693 0.340 1.00 31.46 N ANISOU 203 N GLU A 27 4384 4378 3191 88 4 -516 N ATOM 204 CA GLU A 27 -6.314 11.857 -0.085 1.00 31.65 C ANISOU 204 CA GLU A 27 4396 4351 3277 75 11 -497 C ATOM 205 C GLU A 27 -6.683 12.560 1.206 1.00 30.21 C ANISOU 205 C GLU A 27 4220 4183 3075 125 28 -446 C ATOM 206 O GLU A 27 -7.180 11.924 2.151 1.00 29.73 O ANISOU 206 O GLU A 27 4100 4178 3017 70 10 -473 O ATOM 207 CB GLU A 27 -7.609 11.474 -0.813 1.00 32.31 C ANISOU 207 CB GLU A 27 4444 4442 3390 101 -44 -350 C ATOM 208 CG GLU A 27 -7.420 10.880 -2.226 1.00 36.13 C ANISOU 208 CG GLU A 27 5018 4819 3891 -53 -197 -693 C ATOM 209 CD GLU A 27 -8.682 11.028 -3.108 1.00 36.99 C ANISOU 209 CD GLU A 27 5041 4890 4122 -29 -128 -398 C ATOM 210 OE1 GLU A 27 -9.746 11.463 -2.618 1.00 45.36 O ANISOU 210 OE1 GLU A 27 5835 5595 5804 -17 118 -339 O ATOM 211 OE2 GLU A 27 -8.623 10.722 -4.302 1.00 44.40 O1- ANISOU 211 OE2 GLU A 27 6291 5494 5084 -294 -153 -634 O1- ATOM 212 N VAL A 28 -6.395 13.846 1.254 1.00 29.42 N ANISOU 212 N VAL A 28 4249 4078 2849 117 27 -399 N ATOM 213 CA VAL A 28 -6.697 14.656 2.437 1.00 29.11 C ANISOU 213 CA VAL A 28 4208 3814 3037 111 -67 -396 C ATOM 214 C VAL A 28 -7.784 15.620 2.034 1.00 29.45 C ANISOU 214 C VAL A 28 4256 3874 3058 102 -18 -305 C ATOM 215 O VAL A 28 -7.574 16.448 1.130 1.00 29.25 O ANISOU 215 O VAL A 28 4236 3760 3117 128 40 -146 O ATOM 216 CB VAL A 28 -5.460 15.409 2.914 1.00 29.18 C ANISOU 216 CB VAL A 28 4206 3824 3054 88 -64 -444 C ATOM 217 CG1 VAL A 28 -5.785 16.176 4.203 1.00 28.13 C ANISOU 217 CG1 VAL A 28 4379 3422 2886 37 -43 -518 C ATOM 218 CG2 VAL A 28 -4.305 14.468 3.179 1.00 28.63 C ANISOU 218 CG2 VAL A 28 4226 3385 3265 123 -215 -172 C ATOM 219 N ALA A 29 -8.960 15.482 2.656 1.00 29.95 N ANISOU 219 N ALA A 29 4181 4045 3151 222 6 -186 N ATOM 220 CA ALA A 29 -10.129 16.326 2.322 1.00 30.73 C ANISOU 220 CA ALA A 29 4186 4258 3231 179 -63 -40 C ATOM 221 C ALA A 29 -9.892 17.790 2.739 1.00 31.13 C ANISOU 221 C ALA A 29 4293 4274 3260 288 -139 -60 C ATOM 222 O ALA A 29 -9.043 18.091 3.591 1.00 32.48 O ANISOU 222 O ALA A 29 4615 4379 3344 224 -324 -185 O ATOM 223 CB ALA A 29 -11.398 15.758 2.997 1.00 31.53 C ANISOU 223 CB ALA A 29 4231 4309 3437 62 -29 -41 C ATOM 224 N PRO A 30 -10.611 18.733 2.126 1.00 31.90 N ANISOU 224 N PRO A 30 4530 4265 3326 315 -254 0 N ATOM 225 CA PRO A 30 -10.476 20.136 2.549 1.00 31.93 C ANISOU 225 CA PRO A 30 4519 4264 3347 371 -269 -39 C ATOM 226 C PRO A 30 -11.101 20.344 3.926 1.00 31.72 C ANISOU 226 C PRO A 30 4336 4296 3420 406 -180 -75 C ATOM 227 O PRO A 30 -11.947 19.558 4.330 1.00 33.08 O ANISOU 227 O PRO A 30 4555 4436 3576 413 -57 -174 O ATOM 228 CB PRO A 30 -11.271 20.920 1.494 1.00 33.01 C ANISOU 228 CB PRO A 30 4624 4356 3561 451 -363 -76 C ATOM 229 CG PRO A 30 -12.150 19.926 0.838 1.00 33.77 C ANISOU 229 CG PRO A 30 4764 4260 3806 310 -418 56 C ATOM 230 CD PRO A 30 -11.576 18.547 1.035 1.00 31.58 C ANISOU 230 CD PRO A 30 4569 4235 3194 353 -335 -36 C ATOM 231 N PRO A 31 -10.671 21.386 4.641 1.00 31.77 N ANISOU 231 N PRO A 31 4374 4242 3452 443 -110 -43 N ATOM 232 CA PRO A 31 -11.210 21.670 5.983 1.00 32.03 C ANISOU 232 CA PRO A 31 4389 4272 3505 414 -54 -163 C ATOM 233 C PRO A 31 -12.646 22.160 5.993 1.00 33.43 C ANISOU 233 C PRO A 31 4509 4448 3744 373 -136 -45 C ATOM 234 O PRO A 31 -13.015 23.049 5.197 1.00 34.41 O ANISOU 234 O PRO A 31 4746 4451 3875 524 -166 35 O ATOM 235 CB PRO A 31 -10.252 22.753 6.520 1.00 32.64 C ANISOU 235 CB PRO A 31 4488 4299 3615 332 -23 -104 C ATOM 236 CG PRO A 31 -9.813 23.449 5.309 1.00 31.42 C ANISOU 236 CG PRO A 31 4548 4099 3289 369 -103 -72 C ATOM 237 CD PRO A 31 -9.624 22.348 4.274 1.00 31.01 C ANISOU 237 CD PRO A 31 4196 4211 3373 424 -19 -105 C ATOM 238 N LYS A 32 -13.445 21.556 6.873 1.00 33.59 N ANISOU 238 N LYS A 32 4416 4503 3842 405 -42 -59 N ATOM 239 CA LYS A 32 -14.834 21.970 7.108 1.00 34.65 C ANISOU 239 CA LYS A 32 4518 4509 4137 464 -30 -154 C ATOM 240 C LYS A 32 -14.841 23.144 8.082 1.00 34.41 C ANISOU 240 C LYS A 32 4445 4575 4053 487 -89 -209 C ATOM 241 O LYS A 32 -13.790 23.730 8.366 1.00 34.80 O ANISOU 241 O LYS A 32 4595 4430 4195 565 -6 -120 O ATOM 242 CB LYS A 32 -15.698 20.819 7.633 1.00 34.38 C ANISOU 242 CB LYS A 32 4444 4573 4046 397 -44 -157 C ATOM 243 CG LYS A 32 -15.761 19.597 6.719 1.00 36.72 C ANISOU 243 CG LYS A 32 4731 4504 4717 572 93 -165 C ATOM 244 CD LYS A 32 -16.807 18.608 7.194 1.00 40.57 C ANISOU 244 CD LYS A 32 5063 4908 5442 357 -40 35 C ATOM 245 CE LYS A 32 -17.097 17.547 6.123 1.00 43.27 C ANISOU 245 CE LYS A 32 5642 5039 5757 361 -1 -96 C ATOM 246 NZ LYS A 32 -18.569 17.224 6.006 1.00 46.81 N1+ ANISOU 246 NZ LYS A 32 6053 5587 6144 139 -85 108 N1+ ATOM 247 N ALA A 33 -16.020 23.531 8.558 1.00 34.00 N ANISOU 247 N ALA A 33 4405 4536 3976 505 -41 -238 N ATOM 248 CA ALA A 33 -16.071 24.707 9.410 1.00 34.31 C ANISOU 248 CA ALA A 33 4445 4582 4008 595 -94 -303 C ATOM 249 C ALA A 33 -15.193 24.475 10.614 1.00 34.20 C ANISOU 249 C ALA A 33 4504 4489 4001 587 -61 -250 C ATOM 250 O ALA A 33 -15.260 23.416 11.238 1.00 35.14 O ANISOU 250 O ALA A 33 4666 4576 4109 633 -32 -320 O ATOM 251 CB ALA A 33 -17.479 25.000 9.857 1.00 34.54 C ANISOU 251 CB ALA A 33 4406 4684 4030 530 -16 -254 C ATOM 252 N HIS A 34 -14.380 25.481 10.933 1.00 34.55 N ANISOU 252 N HIS A 34 4503 4577 4047 622 -131 -213 N ATOM 253 CA HIS A 34 -13.600 25.499 12.170 1.00 33.72 C ANISOU 253 CA HIS A 34 4497 4432 3881 580 -53 -187 C ATOM 254 C HIS A 34 -12.496 24.467 12.132 1.00 32.28 C ANISOU 254 C HIS A 34 4438 4198 3628 617 -72 -180 C ATOM 255 O HIS A 34 -12.005 24.017 13.160 1.00 31.14 O ANISOU 255 O HIS A 34 4504 3926 3400 701 -88 -87 O ATOM 256 CB HIS A 34 -14.504 25.334 13.394 1.00 34.47 C ANISOU 256 CB HIS A 34 4483 4434 4177 638 77 -234 C ATOM 257 CG HIS A 34 -15.500 26.444 13.541 1.00 38.95 C ANISOU 257 CG HIS A 34 4843 4900 5056 642 175 -106 C ATOM 258 CD2 HIS A 34 -15.325 27.774 13.711 1.00 40.81 C ANISOU 258 CD2 HIS A 34 5047 4988 5469 439 136 -187 C ATOM 259 ND1 HIS A 34 -16.859 26.242 13.452 1.00 40.89 N ANISOU 259 ND1 HIS A 34 4976 5076 5483 312 89 99 N ATOM 260 CE1 HIS A 34 -17.486 27.397 13.609 1.00 42.28 C ANISOU 260 CE1 HIS A 34 5110 5231 5724 387 205 -224 C ATOM 261 NE2 HIS A 34 -16.577 28.343 13.767 1.00 43.44 N ANISOU 261 NE2 HIS A 34 5158 5418 5926 477 60 -127 N ATOM 262 N GLU A 35 -12.082 24.119 10.914 1.00 31.35 N ANISOU 262 N GLU A 35 4175 4204 3530 642 3 -148 N ATOM 263 CA GLU A 35 -10.950 23.214 10.709 1.00 31.39 C ANISOU 263 CA GLU A 35 4343 4080 3502 626 94 -129 C ATOM 264 C GLU A 35 -9.865 23.921 9.928 1.00 31.13 C ANISOU 264 C GLU A 35 4367 3989 3471 644 107 -70 C ATOM 265 O GLU A 35 -10.144 24.907 9.221 1.00 31.79 O ANISOU 265 O GLU A 35 4574 3882 3621 796 370 -205 O ATOM 266 CB GLU A 35 -11.400 21.930 10.008 1.00 30.83 C ANISOU 266 CB GLU A 35 4154 4029 3527 597 35 -97 C ATOM 267 CG GLU A 35 -12.501 21.212 10.765 1.00 31.62 C ANISOU 267 CG GLU A 35 4531 4036 3446 360 72 -83 C ATOM 268 CD GLU A 35 -13.010 19.977 10.055 1.00 31.86 C ANISOU 268 CD GLU A 35 4251 4258 3597 280 31 -323 C ATOM 269 OE1 GLU A 35 -12.552 19.719 8.922 1.00 34.36 O ANISOU 269 OE1 GLU A 35 4646 4789 3619 242 130 -332 O ATOM 270 OE2 GLU A 35 -13.866 19.263 10.633 1.00 34.51 O1- ANISOU 270 OE2 GLU A 35 5117 4205 3789 588 372 -424 O1- ATOM 271 N VAL A 36 -8.648 23.382 10.023 1.00 29.47 N ANISOU 271 N VAL A 36 4246 3830 3118 692 311 -198 N ATOM 272 CA VAL A 36 -7.448 24.005 9.494 1.00 29.60 C ANISOU 272 CA VAL A 36 4379 3738 3128 665 93 -178 C ATOM 273 C VAL A 36 -6.659 22.913 8.777 1.00 29.53 C ANISOU 273 C VAL A 36 4595 3695 2928 619 149 -215 C ATOM 274 O VAL A 36 -6.348 21.872 9.384 1.00 29.13 O ANISOU 274 O VAL A 36 4578 3466 3024 776 104 -237 O ATOM 275 CB VAL A 36 -6.582 24.628 10.637 1.00 29.83 C ANISOU 275 CB VAL A 36 4368 3730 3235 640 193 -387 C ATOM 276 CG1 VAL A 36 -5.279 25.211 10.084 1.00 30.33 C ANISOU 276 CG1 VAL A 36 4549 3509 3464 490 31 30 C ATOM 277 CG2 VAL A 36 -7.380 25.702 11.416 1.00 30.07 C ANISOU 277 CG2 VAL A 36 4271 3860 3294 867 229 -226 C ATOM 278 N ARG A 37 -6.319 23.138 7.506 1.00 30.23 N ANISOU 278 N ARG A 37 4635 3918 2931 531 21 -259 N ATOM 279 CA ARG A 37 -5.445 22.176 6.798 1.00 29.09 C ANISOU 279 CA ARG A 37 4578 3827 2647 504 -99 -287 C ATOM 280 C ARG A 37 -3.992 22.690 6.798 1.00 30.76 C ANISOU 280 C ARG A 37 4789 3943 2952 427 -4 -224 C ATOM 281 O ARG A 37 -3.724 23.846 6.479 1.00 32.15 O ANISOU 281 O ARG A 37 5060 3874 3281 517 -103 -84 O ATOM 282 CB ARG A 37 -5.976 21.872 5.381 1.00 29.50 C ANISOU 282 CB ARG A 37 4525 4008 2674 594 -158 -283 C ATOM 283 CG ARG A 37 -5.123 20.853 4.639 1.00 27.97 C ANISOU 283 CG ARG A 37 4519 3754 2354 497 -302 -395 C ATOM 284 CD ARG A 37 -5.945 20.171 3.566 1.00 29.60 C ANISOU 284 CD ARG A 37 4460 4098 2687 275 -410 -245 C ATOM 285 NE ARG A 37 -6.282 21.106 2.499 1.00 31.36 N ANISOU 285 NE ARG A 37 4537 4464 2913 352 -148 28 N ATOM 286 CZ ARG A 37 -6.904 20.769 1.370 1.00 30.67 C ANISOU 286 CZ ARG A 37 4329 3956 3367 139 -392 -94 C ATOM 287 NH1 ARG A 37 -7.313 19.516 1.149 1.00 28.46 N1+ ANISOU 287 NH1 ARG A 37 3957 3792 3062 -41 -255 265 N1+ ATOM 288 NH2 ARG A 37 -7.090 21.691 0.435 1.00 30.21 N ANISOU 288 NH2 ARG A 37 3933 3958 3585 436 -168 133 N ATOM 289 N ILE A 38 -3.054 21.832 7.180 1.00 29.93 N ANISOU 289 N ILE A 38 4684 3959 2728 377 20 -242 N ATOM 290 CA ILE A 38 -1.678 22.237 7.429 1.00 29.59 C ANISOU 290 CA ILE A 38 4646 3962 2633 207 61 -200 C ATOM 291 C ILE A 38 -0.686 21.426 6.575 1.00 29.32 C ANISOU 291 C ILE A 38 4534 3880 2724 170 126 -156 C ATOM 292 O ILE A 38 -0.777 20.183 6.524 1.00 28.91 O ANISOU 292 O ILE A 38 4383 3880 2719 153 121 -250 O ATOM 293 CB ILE A 38 -1.290 21.976 8.942 1.00 29.18 C ANISOU 293 CB ILE A 38 4615 3818 2651 206 105 -232 C ATOM 294 CG1 ILE A 38 -2.290 22.622 9.897 1.00 28.86 C ANISOU 294 CG1 ILE A 38 4744 3856 2363 367 122 -96 C ATOM 295 CG2 ILE A 38 0.199 22.349 9.218 1.00 30.46 C ANISOU 295 CG2 ILE A 38 4663 4152 2757 179 -239 -211 C ATOM 296 CD1 ILE A 38 -2.054 22.195 11.358 1.00 28.88 C ANISOU 296 CD1 ILE A 38 4854 3804 2316 167 109 -91 C ATOM 297 N LYS A 39 0.271 22.117 5.933 1.00 29.45 N ANISOU 297 N LYS A 39 4493 3925 2772 111 144 -100 N ATOM 298 CA LYS A 39 1.379 21.459 5.245 1.00 30.39 C ANISOU 298 CA LYS A 39 4586 3944 3014 95 202 45 C ATOM 299 C LYS A 39 2.494 21.208 6.244 1.00 30.28 C ANISOU 299 C LYS A 39 4453 3936 3113 72 127 -24 C ATOM 300 O LYS A 39 3.038 22.155 6.822 1.00 30.76 O ANISOU 300 O LYS A 39 4525 3856 3307 148 55 -6 O ATOM 301 CB LYS A 39 1.916 22.324 4.096 1.00 30.48 C ANISOU 301 CB LYS A 39 4649 3926 3003 114 278 62 C ATOM 302 CG LYS A 39 3.027 21.604 3.318 1.00 31.22 C ANISOU 302 CG LYS A 39 4674 4226 2960 113 332 177 C ATOM 303 CD LYS A 39 3.654 22.482 2.207 1.00 33.30 C ANISOU 303 CD LYS A 39 4889 4350 3411 32 403 263 C ATOM 304 CE LYS A 39 4.599 21.617 1.368 1.00 38.54 C ANISOU 304 CE LYS A 39 5360 4861 4423 -65 348 -301 C ATOM 305 NZ LYS A 39 3.833 20.511 0.721 1.00 42.39 N1+ ANISOU 305 NZ LYS A 39 5806 5330 4971 42 34 -451 N1+ ATOM 306 N MET A 40 2.808 19.944 6.505 1.00 29.63 N ANISOU 306 N MET A 40 4360 3859 3040 48 58 -5 N ATOM 307 CA MET A 40 3.855 19.650 7.515 1.00 30.16 C ANISOU 307 CA MET A 40 4370 3895 3194 -14 -45 20 C ATOM 308 C MET A 40 5.239 20.056 7.070 1.00 30.62 C ANISOU 308 C MET A 40 4446 3946 3242 -69 11 34 C ATOM 309 O MET A 40 5.594 19.896 5.900 1.00 31.31 O ANISOU 309 O MET A 40 4497 4083 3314 128 59 4 O ATOM 310 CB MET A 40 3.888 18.183 7.921 1.00 31.10 C ANISOU 310 CB MET A 40 4521 3965 3329 -96 -19 0 C ATOM 311 CG MET A 40 4.131 17.991 9.407 1.00 33.26 C ANISOU 311 CG MET A 40 4898 4227 3512 -175 -95 196 C ATOM 312 SD MET A 40 2.607 18.348 10.319 1.00 38.97 S ANISOU 312 SD MET A 40 6208 5161 3437 -379 439 -118 S ATOM 313 CE MET A 40 1.451 17.470 9.245 1.00 41.37 C ANISOU 313 CE MET A 40 6048 5266 4402 7 -283 63 C ATOM 314 N VAL A 41 6.030 20.564 8.021 1.00 29.88 N ANISOU 314 N VAL A 41 4305 3915 3133 -57 -41 120 N ATOM 315 CA VAL A 41 7.423 20.916 7.749 1.00 29.34 C ANISOU 315 CA VAL A 41 4229 3746 3172 -212 38 164 C ATOM 316 C VAL A 41 8.382 20.017 8.505 1.00 29.12 C ANISOU 316 C VAL A 41 4169 3739 3154 -242 135 168 C ATOM 317 O VAL A 41 9.448 19.610 7.984 1.00 29.50 O ANISOU 317 O VAL A 41 4303 3726 3179 -273 185 252 O ATOM 318 CB VAL A 41 7.704 22.432 8.005 1.00 30.36 C ANISOU 318 CB VAL A 41 4229 3838 3467 -77 -42 51 C ATOM 319 CG1 VAL A 41 9.205 22.770 7.905 1.00 28.68 C ANISOU 319 CG1 VAL A 41 4141 3248 3508 -193 272 -20 C ATOM 320 CG2 VAL A 41 6.865 23.334 7.062 1.00 31.24 C ANISOU 320 CG2 VAL A 41 4549 3913 3408 -232 54 467 C ATOM 321 N ALA A 42 8.012 19.700 9.748 1.00 27.69 N ANISOU 321 N ALA A 42 4146 3488 2886 -253 36 230 N ATOM 322 CA ALA A 42 8.821 18.758 10.531 1.00 26.52 C ANISOU 322 CA ALA A 42 3859 3282 2933 -252 166 226 C ATOM 323 C ALA A 42 7.974 18.136 11.589 1.00 25.51 C ANISOU 323 C ALA A 42 3648 3216 2829 -289 291 214 C ATOM 324 O ALA A 42 7.028 18.764 12.129 1.00 27.15 O ANISOU 324 O ALA A 42 3963 3313 3040 -209 289 393 O ATOM 325 CB ALA A 42 10.022 19.443 11.195 1.00 26.90 C ANISOU 325 CB ALA A 42 3894 3271 3055 -322 24 193 C ATOM 326 N THR A 43 8.332 16.915 11.921 1.00 25.58 N ANISOU 326 N THR A 43 3582 3332 2804 -37 458 91 N ATOM 327 CA THR A 43 7.617 16.161 12.988 1.00 26.77 C ANISOU 327 CA THR A 43 3796 3460 2913 -86 350 76 C ATOM 328 C THR A 43 8.589 15.289 13.768 1.00 26.34 C ANISOU 328 C THR A 43 3705 3448 2851 12 316 -30 C ATOM 329 O THR A 43 9.486 14.670 13.190 1.00 27.99 O ANISOU 329 O THR A 43 3979 3633 3023 -144 275 -54 O ATOM 330 CB THR A 43 6.389 15.364 12.442 1.00 27.17 C ANISOU 330 CB THR A 43 3829 3382 3111 -40 384 16 C ATOM 331 CG2 THR A 43 6.809 14.348 11.430 1.00 27.01 C ANISOU 331 CG2 THR A 43 3803 3477 2981 -25 355 -346 C ATOM 332 OG1 THR A 43 5.687 14.694 13.500 1.00 27.35 O ANISOU 332 OG1 THR A 43 3630 3481 3279 -281 390 17 O ATOM 333 N GLY A 44 8.453 15.302 15.095 1.00 27.15 N ANISOU 333 N GLY A 44 3841 3517 2955 66 464 82 N ATOM 334 CA GLY A 44 9.321 14.524 15.971 1.00 27.12 C ANISOU 334 CA GLY A 44 3738 3466 3101 83 332 61 C ATOM 335 C GLY A 44 8.764 13.123 16.164 1.00 28.85 C ANISOU 335 C GLY A 44 3959 3687 3314 101 393 58 C ATOM 336 O GLY A 44 7.550 12.913 16.008 1.00 30.92 O ANISOU 336 O GLY A 44 4218 3838 3691 182 304 117 O ATOM 337 N ILE A 45 9.643 12.160 16.444 1.00 28.29 N ANISOU 337 N ILE A 45 4061 3655 3030 124 418 18 N ATOM 338 CA ILE A 45 9.194 10.808 16.775 1.00 29.11 C ANISOU 338 CA ILE A 45 4063 3757 3239 161 369 -99 C ATOM 339 C ILE A 45 9.186 10.661 18.277 1.00 29.31 C ANISOU 339 C ILE A 45 3972 3910 3252 136 345 -87 C ATOM 340 O ILE A 45 10.247 10.697 18.912 1.00 29.79 O ANISOU 340 O ILE A 45 4043 4063 3212 37 292 -114 O ATOM 341 CB ILE A 45 10.135 9.745 16.131 1.00 29.02 C ANISOU 341 CB ILE A 45 3994 3703 3327 222 343 -94 C ATOM 342 CG1 ILE A 45 9.973 9.789 14.613 1.00 28.56 C ANISOU 342 CG1 ILE A 45 3901 3605 3343 -49 310 -187 C ATOM 343 CG2 ILE A 45 9.841 8.326 16.673 1.00 31.49 C ANISOU 343 CG2 ILE A 45 4339 3897 3727 233 307 11 C ATOM 344 CD1 ILE A 45 11.004 8.968 13.878 1.00 30.37 C ANISOU 344 CD1 ILE A 45 3904 4197 3436 -34 396 -462 C ATOM 345 N CYS A 46 7.980 10.520 18.844 1.00 29.45 N ANISOU 345 N CYS A 46 4017 3946 3225 112 334 -47 N ATOM 346 CA CYS A 46 7.826 10.386 20.294 1.00 29.66 C ANISOU 346 CA CYS A 46 3970 3963 3335 239 327 -104 C ATOM 347 C CYS A 46 7.501 8.953 20.734 1.00 29.44 C ANISOU 347 C CYS A 46 3909 3956 3319 176 243 -122 C ATOM 348 O CYS A 46 6.841 8.214 19.999 1.00 29.05 O ANISOU 348 O CYS A 46 3799 3953 3283 13 -10 63 O ATOM 349 CB CYS A 46 6.724 11.360 20.714 1.00 28.69 C ANISOU 349 CB CYS A 46 3920 3689 3291 246 437 -267 C ATOM 350 SG CYS A 46 6.229 11.227 22.463 1.00 30.96 S ANISOU 350 SG CYS A 46 4283 3902 3575 376 284 -6 S ATOM 351 N ARG A 47 7.950 8.563 21.938 1.00 30.80 N ANISOU 351 N ARG A 47 4069 4077 3555 237 163 -23 N ATOM 352 CA ARG A 47 7.621 7.266 22.549 1.00 33.23 C ANISOU 352 CA ARG A 47 4426 4229 3968 212 78 31 C ATOM 353 C ARG A 47 6.130 6.950 22.409 1.00 31.31 C ANISOU 353 C ARG A 47 4304 3975 3616 252 176 99 C ATOM 354 O ARG A 47 5.745 5.819 22.136 1.00 31.77 O ANISOU 354 O ARG A 47 4415 3936 3721 493 148 67 O ATOM 355 CB ARG A 47 8.017 7.266 24.046 1.00 35.13 C ANISOU 355 CB ARG A 47 4649 4557 4140 149 -9 58 C ATOM 356 CG ARG A 47 8.452 5.915 24.714 1.00 38.26 C ANISOU 356 CG ARG A 47 5278 4609 4647 75 -60 -101 C ATOM 357 CD ARG A 47 8.854 6.128 26.245 1.00 37.97 C ANISOU 357 CD ARG A 47 4993 4818 4614 271 -177 121 C ATOM 358 NE ARG A 47 9.655 5.045 26.836 1.00 43.55 N ANISOU 358 NE ARG A 47 5695 5355 5496 148 -291 336 N ATOM 359 CZ ARG A 47 9.642 4.700 28.123 1.00 45.57 C ANISOU 359 CZ ARG A 47 5903 5707 5702 81 -40 219 C ATOM 360 NH1 ARG A 47 8.832 5.308 28.977 1.00 48.15 N1+ ANISOU 360 NH1 ARG A 47 6291 5779 6224 212 17 -63 N1+ ATOM 361 NH2 ARG A 47 10.416 3.707 28.561 1.00 49.29 N ANISOU 361 NH2 ARG A 47 6346 6043 6336 256 -93 267 N ATOM 362 N SER A 48 5.272 7.952 22.589 1.00 29.84 N ANISOU 362 N SER A 48 4299 3669 3368 254 262 87 N ATOM 363 CA SER A 48 3.847 7.702 22.507 1.00 29.02 C ANISOU 363 CA SER A 48 4098 3592 3334 159 398 57 C ATOM 364 C SER A 48 3.373 7.210 21.139 1.00 28.62 C ANISOU 364 C SER A 48 3952 3605 3314 115 413 -18 C ATOM 365 O SER A 48 2.419 6.419 21.055 1.00 28.37 O ANISOU 365 O SER A 48 3978 3639 3163 171 452 -70 O ATOM 366 CB SER A 48 3.041 8.925 22.923 1.00 29.67 C ANISOU 366 CB SER A 48 4201 3641 3432 273 300 113 C ATOM 367 OG SER A 48 3.296 9.220 24.282 1.00 31.43 O ANISOU 367 OG SER A 48 4845 3524 3571 -53 347 217 O ATOM 368 N ASP A 49 4.044 7.663 20.073 1.00 27.50 N ANISOU 368 N ASP A 49 3766 3476 3205 17 422 43 N ATOM 369 CA ASP A 49 3.766 7.160 18.739 1.00 28.87 C ANISOU 369 CA ASP A 49 4081 3507 3381 35 431 2 C ATOM 370 C ASP A 49 4.084 5.655 18.614 1.00 29.24 C ANISOU 370 C ASP A 49 4119 3488 3501 71 434 -22 C ATOM 371 O ASP A 49 3.328 4.904 17.976 1.00 30.71 O ANISOU 371 O ASP A 49 4391 3539 3740 112 499 -19 O ATOM 372 CB ASP A 49 4.524 7.958 17.665 1.00 28.34 C ANISOU 372 CB ASP A 49 4112 3328 3326 -41 499 -46 C ATOM 373 CG ASP A 49 4.174 9.444 17.683 1.00 29.59 C ANISOU 373 CG ASP A 49 4287 3391 3562 121 265 34 C ATOM 374 OD1 ASP A 49 2.965 9.819 17.535 1.00 28.95 O ANISOU 374 OD1 ASP A 49 4674 2841 3482 243 331 -433 O ATOM 375 OD2 ASP A 49 5.132 10.228 17.848 1.00 30.90 O1- ANISOU 375 OD2 ASP A 49 4338 3761 3641 181 129 178 O1- ATOM 376 N ASP A 50 5.174 5.238 19.263 1.00 29.87 N ANISOU 376 N ASP A 50 4194 3572 3581 226 489 -17 N ATOM 377 CA ASP A 50 5.607 3.836 19.353 1.00 31.68 C ANISOU 377 CA ASP A 50 4417 3694 3923 224 427 -88 C ATOM 378 C ASP A 50 4.604 3.023 20.158 1.00 31.64 C ANISOU 378 C ASP A 50 4512 3676 3830 250 430 -88 C ATOM 379 O ASP A 50 4.329 1.857 19.836 1.00 31.56 O ANISOU 379 O ASP A 50 4535 3543 3913 472 482 -202 O ATOM 380 CB ASP A 50 6.972 3.781 20.027 1.00 32.73 C ANISOU 380 CB ASP A 50 4417 3812 4207 218 437 -18 C ATOM 381 CG ASP A 50 7.661 2.446 19.868 1.00 35.87 C ANISOU 381 CG ASP A 50 4777 4106 4746 117 307 2 C ATOM 382 OD1 ASP A 50 7.689 1.940 18.748 1.00 39.38 O ANISOU 382 OD1 ASP A 50 5480 4579 4901 261 762 -61 O ATOM 383 OD2 ASP A 50 8.188 1.920 20.874 1.00 40.92 O1- ANISOU 383 OD2 ASP A 50 5545 4798 5202 207 240 303 O1- ATOM 384 N HIS A 51 4.009 3.647 21.184 1.00 30.36 N ANISOU 384 N HIS A 51 4301 3543 3691 315 510 -141 N ATOM 385 CA HIS A 51 2.977 2.945 21.968 1.00 31.09 C ANISOU 385 CA HIS A 51 4440 3683 3687 288 519 -110 C ATOM 386 C HIS A 51 1.749 2.590 21.118 1.00 30.79 C ANISOU 386 C HIS A 51 4465 3621 3611 269 606 -238 C ATOM 387 O HIS A 51 1.067 1.609 21.381 1.00 32.41 O ANISOU 387 O HIS A 51 4743 3738 3831 250 636 -141 O ATOM 388 CB HIS A 51 2.588 3.759 23.209 1.00 32.16 C ANISOU 388 CB HIS A 51 4562 3956 3700 209 527 -60 C ATOM 389 CG HIS A 51 3.691 3.907 24.206 1.00 33.51 C ANISOU 389 CG HIS A 51 4724 4111 3898 11 435 157 C ATOM 390 CD2 HIS A 51 4.794 3.155 24.435 1.00 37.31 C ANISOU 390 CD2 HIS A 51 5158 4448 4571 94 211 90 C ATOM 391 ND1 HIS A 51 3.740 4.942 25.116 1.00 33.82 N ANISOU 391 ND1 HIS A 51 4896 4178 3776 -240 274 305 N ATOM 392 CE1 HIS A 51 4.816 4.811 25.871 1.00 37.18 C ANISOU 392 CE1 HIS A 51 5001 4673 4452 67 171 198 C ATOM 393 NE2 HIS A 51 5.469 3.731 25.483 1.00 38.97 N ANISOU 393 NE2 HIS A 51 5333 4687 4784 38 57 42 N ATOM 394 N VAL A 52 1.441 3.398 20.115 1.00 30.60 N ANISOU 394 N VAL A 52 4484 3526 3615 265 494 -253 N ATOM 395 CA VAL A 52 0.363 3.042 19.161 1.00 31.27 C ANISOU 395 CA VAL A 52 4537 3599 3745 240 466 -351 C ATOM 396 C VAL A 52 0.740 1.759 18.398 1.00 31.97 C ANISOU 396 C VAL A 52 4628 3595 3920 220 393 -325 C ATOM 397 O VAL A 52 -0.087 0.828 18.249 1.00 32.34 O ANISOU 397 O VAL A 52 4884 3248 4155 351 504 -595 O ATOM 398 CB VAL A 52 0.024 4.236 18.212 1.00 30.03 C ANISOU 398 CB VAL A 52 4345 3562 3501 145 470 -332 C ATOM 399 CG1 VAL A 52 -1.083 3.873 17.162 1.00 30.49 C ANISOU 399 CG1 VAL A 52 4505 3542 3537 172 336 -307 C ATOM 400 CG2 VAL A 52 -0.459 5.452 19.031 1.00 32.30 C ANISOU 400 CG2 VAL A 52 4779 3808 3685 190 507 -306 C ATOM 401 N VAL A 53 1.969 1.734 17.897 1.00 33.29 N ANISOU 401 N VAL A 53 4785 3815 4049 243 382 -311 N ATOM 402 CA VAL A 53 2.490 0.573 17.171 1.00 33.89 C ANISOU 402 CA VAL A 53 4866 3839 4172 218 413 -239 C ATOM 403 C VAL A 53 2.401 -0.690 18.041 1.00 35.58 C ANISOU 403 C VAL A 53 5126 3996 4394 250 299 -118 C ATOM 404 O VAL A 53 1.902 -1.719 17.575 1.00 35.72 O ANISOU 404 O VAL A 53 5283 3883 4403 144 371 3 O ATOM 405 CB VAL A 53 3.930 0.786 16.676 1.00 33.86 C ANISOU 405 CB VAL A 53 4914 3828 4121 266 432 -342 C ATOM 406 CG1 VAL A 53 4.411 -0.482 15.919 1.00 34.18 C ANISOU 406 CG1 VAL A 53 4986 3904 4096 297 622 -484 C ATOM 407 CG2 VAL A 53 4.016 2.024 15.803 1.00 32.77 C ANISOU 407 CG2 VAL A 53 4700 3914 3835 285 396 -352 C ATOM 408 N SER A 54 2.827 -0.586 19.301 1.00 36.50 N ANISOU 408 N SER A 54 5251 4135 4482 206 353 -92 N ATOM 409 CA SER A 54 2.854 -1.757 20.197 1.00 37.33 C ANISOU 409 CA SER A 54 5321 4243 4619 217 343 -51 C ATOM 410 C SER A 54 1.451 -2.250 20.593 1.00 37.90 C ANISOU 410 C SER A 54 5346 4298 4757 149 274 -17 C ATOM 411 O SER A 54 1.298 -3.373 21.108 1.00 39.06 O ANISOU 411 O SER A 54 5521 4259 5060 247 305 -35 O ATOM 412 CB SER A 54 3.646 -1.445 21.466 1.00 37.60 C ANISOU 412 CB SER A 54 5251 4292 4743 167 260 122 C ATOM 413 OG SER A 54 4.948 -0.995 21.167 1.00 41.81 O ANISOU 413 OG SER A 54 5541 4982 5361 213 430 -141 O ATOM 414 N GLY A 55 0.437 -1.400 20.411 1.00 38.07 N ANISOU 414 N GLY A 55 5364 4400 4702 127 292 -122 N ATOM 415 CA GLY A 55 -0.913 -1.717 20.849 1.00 38.43 C ANISOU 415 CA GLY A 55 5390 4553 4658 85 312 -101 C ATOM 416 C GLY A 55 -1.158 -1.351 22.306 1.00 39.11 C ANISOU 416 C GLY A 55 5449 4708 4702 31 337 -57 C ATOM 417 O GLY A 55 -2.206 -1.674 22.883 1.00 40.26 O ANISOU 417 O GLY A 55 5620 4699 4975 -46 396 -31 O ATOM 418 N THR A 56 -0.200 -0.665 22.904 1.00 38.59 N ANISOU 418 N THR A 56 5414 4619 4630 29 381 -19 N ATOM 419 CA THR A 56 -0.316 -0.311 24.327 1.00 37.73 C ANISOU 419 CA THR A 56 5362 4572 4401 -51 379 105 C ATOM 420 C THR A 56 -1.069 0.997 24.538 1.00 37.06 C ANISOU 420 C THR A 56 5293 4539 4246 -114 474 98 C ATOM 421 O THR A 56 -1.721 1.165 25.573 1.00 37.82 O ANISOU 421 O THR A 56 5472 4633 4265 -102 525 149 O ATOM 422 CB THR A 56 1.042 -0.365 25.084 1.00 38.55 C ANISOU 422 CB THR A 56 5427 4615 4605 -8 394 89 C ATOM 423 CG2 THR A 56 1.674 -1.772 24.982 1.00 38.47 C ANISOU 423 CG2 THR A 56 5471 4524 4620 -15 249 122 C ATOM 424 OG1 THR A 56 1.960 0.600 24.548 1.00 40.93 O ANISOU 424 OG1 THR A 56 5649 4837 5065 -190 60 210 O ATOM 425 N LEU A 57 -0.957 1.943 23.590 1.00 35.15 N ANISOU 425 N LEU A 57 5064 4353 3937 -174 475 97 N ATOM 426 CA LEU A 57 -1.850 3.099 23.546 1.00 35.16 C ANISOU 426 CA LEU A 57 5017 4343 3999 -239 508 135 C ATOM 427 C LEU A 57 -2.929 2.693 22.541 1.00 34.72 C ANISOU 427 C LEU A 57 4890 4289 4012 -171 460 101 C ATOM 428 O LEU A 57 -2.678 2.613 21.336 1.00 35.08 O ANISOU 428 O LEU A 57 4960 4303 4063 -211 479 -22 O ATOM 429 CB LEU A 57 -1.108 4.388 23.121 1.00 35.54 C ANISOU 429 CB LEU A 57 5017 4476 4011 -251 563 119 C ATOM 430 CG LEU A 57 -1.341 5.767 23.770 1.00 37.94 C ANISOU 430 CG LEU A 57 5289 4480 4647 -225 589 176 C ATOM 431 CD1 LEU A 57 -0.965 6.945 22.884 1.00 36.94 C ANISOU 431 CD1 LEU A 57 5166 4190 4676 -225 380 165 C ATOM 432 CD2 LEU A 57 -2.714 6.038 24.481 1.00 38.07 C ANISOU 432 CD2 LEU A 57 5090 4660 4716 -186 432 -198 C ATOM 433 N VAL A 58 -4.114 2.364 23.041 1.00 35.53 N ANISOU 433 N VAL A 58 4935 4285 4278 -173 346 48 N ATOM 434 CA VAL A 58 -5.188 1.869 22.186 1.00 35.59 C ANISOU 434 CA VAL A 58 4927 4365 4228 -75 315 -63 C ATOM 435 C VAL A 58 -5.920 3.019 21.516 1.00 35.12 C ANISOU 435 C VAL A 58 4886 4344 4112 -1 317 -139 C ATOM 436 O VAL A 58 -6.493 3.867 22.194 1.00 36.00 O ANISOU 436 O VAL A 58 5091 4311 4276 42 194 -204 O ATOM 437 CB VAL A 58 -6.185 1.040 22.998 1.00 36.16 C ANISOU 437 CB VAL A 58 4895 4402 4440 -118 233 1 C ATOM 438 CG1 VAL A 58 -7.378 0.613 22.131 1.00 38.43 C ANISOU 438 CG1 VAL A 58 5308 4646 4647 -93 205 -208 C ATOM 439 CG2 VAL A 58 -5.470 -0.152 23.614 1.00 37.94 C ANISOU 439 CG2 VAL A 58 5126 4545 4742 -179 207 158 C ATOM 440 N THR A 59 -5.914 3.030 20.185 1.00 34.64 N ANISOU 440 N THR A 59 4790 4257 4114 -22 268 -363 N ATOM 441 CA THR A 59 -6.603 4.054 19.408 1.00 32.86 C ANISOU 441 CA THR A 59 4597 3980 3906 -2 353 -449 C ATOM 442 C THR A 59 -7.060 3.304 18.145 1.00 32.95 C ANISOU 442 C THR A 59 4523 3976 4019 -20 300 -512 C ATOM 443 O THR A 59 -6.439 2.290 17.795 1.00 32.79 O ANISOU 443 O THR A 59 4559 4019 3879 42 328 -667 O ATOM 444 CB THR A 59 -5.654 5.268 19.092 1.00 33.97 C ANISOU 444 CB THR A 59 4662 4111 4132 55 379 -372 C ATOM 445 CG2 THR A 59 -4.576 4.877 18.041 1.00 34.53 C ANISOU 445 CG2 THR A 59 4893 3997 4230 3 594 -402 C ATOM 446 OG1 THR A 59 -6.407 6.408 18.627 1.00 33.30 O ANISOU 446 OG1 THR A 59 4776 3708 4166 56 673 -803 O ATOM 447 N PRO A 60 -8.164 3.741 17.510 1.00 31.95 N ANISOU 447 N PRO A 60 4408 3833 3897 -27 335 -531 N ATOM 448 CA PRO A 60 -8.640 3.035 16.310 1.00 31.80 C ANISOU 448 CA PRO A 60 4357 3880 3844 -88 300 -471 C ATOM 449 C PRO A 60 -7.620 2.935 15.179 1.00 32.00 C ANISOU 449 C PRO A 60 4386 3828 3943 -83 339 -574 C ATOM 450 O PRO A 60 -6.921 3.917 14.910 1.00 31.85 O ANISOU 450 O PRO A 60 4343 3901 3855 -31 626 -517 O ATOM 451 CB PRO A 60 -9.852 3.871 15.883 1.00 31.96 C ANISOU 451 CB PRO A 60 4381 3755 4005 -22 325 -635 C ATOM 452 CG PRO A 60 -10.414 4.425 17.213 1.00 32.83 C ANISOU 452 CG PRO A 60 4356 4054 4062 33 361 -474 C ATOM 453 CD PRO A 60 -9.123 4.783 17.954 1.00 32.89 C ANISOU 453 CD PRO A 60 4497 3936 4061 -2 218 -621 C ATOM 454 N LEU A 61 -7.520 1.747 14.553 1.00 32.95 N ANISOU 454 N LEU A 61 4516 4028 3974 -26 423 -467 N ATOM 455 CA LEU A 61 -6.666 1.534 13.393 1.00 32.96 C ANISOU 455 CA LEU A 61 4467 3949 4107 -64 308 -513 C ATOM 456 C LEU A 61 -7.559 1.247 12.179 1.00 32.10 C ANISOU 456 C LEU A 61 4379 3810 4004 -175 289 -570 C ATOM 457 O LEU A 61 -8.689 0.745 12.347 1.00 33.44 O ANISOU 457 O LEU A 61 4643 3898 4164 -208 383 -468 O ATOM 458 CB LEU A 61 -5.713 0.341 13.666 1.00 33.12 C ANISOU 458 CB LEU A 61 4513 3871 4197 -94 256 -449 C ATOM 459 CG LEU A 61 -4.800 0.461 14.900 1.00 37.05 C ANISOU 459 CG LEU A 61 4595 4428 5054 -60 50 -300 C ATOM 460 CD1 LEU A 61 -3.725 -0.627 14.935 1.00 40.50 C ANISOU 460 CD1 LEU A 61 5216 4360 5813 -39 -153 -286 C ATOM 461 CD2 LEU A 61 -4.152 1.837 14.989 1.00 37.39 C ANISOU 461 CD2 LEU A 61 4499 4405 5299 -135 83 -262 C ATOM 462 N PRO A 62 -7.050 1.478 10.945 1.00 30.98 N ANISOU 462 N PRO A 62 4327 3636 3808 -249 220 -658 N ATOM 463 CA PRO A 62 -5.722 2.001 10.616 1.00 30.29 C ANISOU 463 CA PRO A 62 4277 3602 3628 -183 312 -707 C ATOM 464 C PRO A 62 -5.643 3.476 10.990 1.00 29.30 C ANISOU 464 C PRO A 62 4118 3478 3535 -167 292 -635 C ATOM 465 O PRO A 62 -6.690 4.125 11.064 1.00 31.03 O ANISOU 465 O PRO A 62 4181 3771 3837 -249 229 -592 O ATOM 466 CB PRO A 62 -5.654 1.817 9.088 1.00 30.93 C ANISOU 466 CB PRO A 62 4278 3888 3582 -129 309 -635 C ATOM 467 CG PRO A 62 -7.048 1.908 8.646 1.00 31.74 C ANISOU 467 CG PRO A 62 4507 3720 3832 -209 104 -676 C ATOM 468 CD PRO A 62 -7.819 1.180 9.708 1.00 31.55 C ANISOU 468 CD PRO A 62 4397 3722 3867 -245 216 -674 C ATOM 469 N VAL A 63 -4.433 4.005 11.160 1.00 28.94 N ANISOU 469 N VAL A 63 4043 3471 3480 -2 380 -613 N ATOM 470 CA VAL A 63 -4.261 5.359 11.699 1.00 27.33 C ANISOU 470 CA VAL A 63 3833 3312 3240 -90 393 -474 C ATOM 471 C VAL A 63 -3.047 6.058 11.098 1.00 27.93 C ANISOU 471 C VAL A 63 3857 3409 3345 -12 417 -442 C ATOM 472 O VAL A 63 -2.047 5.394 10.718 1.00 26.91 O ANISOU 472 O VAL A 63 3440 3347 3437 -134 462 -571 O ATOM 473 CB VAL A 63 -4.101 5.317 13.251 1.00 28.88 C ANISOU 473 CB VAL A 63 4038 3506 3427 11 383 -522 C ATOM 474 CG1 VAL A 63 -2.803 4.671 13.668 1.00 27.89 C ANISOU 474 CG1 VAL A 63 3892 3435 3267 56 526 -353 C ATOM 475 CG2 VAL A 63 -4.232 6.714 13.893 1.00 27.67 C ANISOU 475 CG2 VAL A 63 4129 3155 3226 -22 243 -572 C ATOM 476 N ILE A 64 -3.178 7.376 10.968 1.00 26.73 N ANISOU 476 N ILE A 64 3757 3336 3062 124 397 -318 N ATOM 477 CA ILE A 64 -2.017 8.261 10.743 1.00 26.19 C ANISOU 477 CA ILE A 64 3868 3203 2876 80 130 -312 C ATOM 478 C ILE A 64 -1.607 8.834 12.110 1.00 26.57 C ANISOU 478 C ILE A 64 3894 3230 2971 114 117 -246 C ATOM 479 O ILE A 64 -2.335 9.686 12.672 1.00 25.71 O ANISOU 479 O ILE A 64 3826 3083 2858 373 -10 -290 O ATOM 480 CB ILE A 64 -2.309 9.375 9.688 1.00 26.16 C ANISOU 480 CB ILE A 64 3840 3305 2793 114 122 -383 C ATOM 481 CG1 ILE A 64 -2.566 8.749 8.307 1.00 29.06 C ANISOU 481 CG1 ILE A 64 4278 3821 2942 81 -225 -214 C ATOM 482 CG2 ILE A 64 -1.130 10.328 9.573 1.00 27.65 C ANISOU 482 CG2 ILE A 64 4238 3448 2817 -30 230 -700 C ATOM 483 CD1 ILE A 64 -2.821 9.759 7.234 1.00 30.19 C ANISOU 483 CD1 ILE A 64 4221 3967 3282 435 -197 -117 C ATOM 484 N ALA A 65 -0.507 8.318 12.663 1.00 25.56 N ANISOU 484 N ALA A 65 3732 3322 2658 16 73 -211 N ATOM 485 CA ALA A 65 0.006 8.791 13.965 1.00 25.90 C ANISOU 485 CA ALA A 65 3707 3272 2858 119 -14 -290 C ATOM 486 C ALA A 65 0.823 10.070 13.827 1.00 25.89 C ANISOU 486 C ALA A 65 3592 3472 2773 105 145 -231 C ATOM 487 O ALA A 65 0.716 10.777 12.795 1.00 26.33 O ANISOU 487 O ALA A 65 3786 3463 2752 45 113 -254 O ATOM 488 CB ALA A 65 0.765 7.704 14.705 1.00 26.40 C ANISOU 488 CB ALA A 65 3633 3402 2994 197 14 -208 C ATOM 489 N GLY A 66 1.599 10.398 14.864 1.00 24.51 N ANISOU 489 N GLY A 66 3322 3355 2635 133 248 -343 N ATOM 490 CA GLY A 66 2.339 11.653 14.876 1.00 24.75 C ANISOU 490 CA GLY A 66 3497 3247 2659 231 235 -271 C ATOM 491 C GLY A 66 1.538 12.724 15.600 1.00 24.64 C ANISOU 491 C GLY A 66 3370 3268 2724 272 184 -266 C ATOM 492 O GLY A 66 0.376 13.002 15.269 1.00 26.35 O ANISOU 492 O GLY A 66 3464 3448 3100 226 101 -379 O ATOM 493 N HIS A 67 2.172 13.351 16.576 1.00 24.82 N ANISOU 493 N HIS A 67 3382 3242 2806 256 142 -410 N ATOM 494 CA HIS A 67 1.535 14.383 17.391 1.00 25.22 C ANISOU 494 CA HIS A 67 3662 3119 2798 279 251 -312 C ATOM 495 C HIS A 67 2.444 15.558 17.774 1.00 26.30 C ANISOU 495 C HIS A 67 3859 3130 3001 271 257 -306 C ATOM 496 O HIS A 67 1.954 16.538 18.368 1.00 29.31 O ANISOU 496 O HIS A 67 4275 3303 3555 229 290 -607 O ATOM 497 CB HIS A 67 0.890 13.753 18.641 1.00 24.91 C ANISOU 497 CB HIS A 67 3634 3023 2805 246 174 -192 C ATOM 498 CG HIS A 67 1.879 13.120 19.573 1.00 25.00 C ANISOU 498 CG HIS A 67 3629 3160 2707 422 232 -252 C ATOM 499 CD2 HIS A 67 2.374 13.542 20.763 1.00 25.82 C ANISOU 499 CD2 HIS A 67 3757 2937 3112 334 382 -661 C ATOM 500 ND1 HIS A 67 2.462 11.892 19.328 1.00 26.13 N ANISOU 500 ND1 HIS A 67 3453 3300 3172 81 279 -127 N ATOM 501 CE1 HIS A 67 3.283 11.603 20.321 1.00 26.12 C ANISOU 501 CE1 HIS A 67 3657 3304 2963 355 423 -252 C ATOM 502 NE2 HIS A 67 3.230 12.577 21.216 1.00 26.12 N ANISOU 502 NE2 HIS A 67 3680 3378 2867 -11 62 -379 N ATOM 503 N GLU A 68 3.720 15.499 17.412 1.00 26.44 N ANISOU 503 N GLU A 68 4104 3025 2915 220 193 -126 N ATOM 504 CA GLU A 68 4.721 16.484 17.798 1.00 26.42 C ANISOU 504 CA GLU A 68 4209 3136 2692 136 181 -275 C ATOM 505 C GLU A 68 5.259 17.070 16.505 1.00 27.04 C ANISOU 505 C GLU A 68 4274 3220 2779 48 178 -140 C ATOM 506 O GLU A 68 5.999 16.393 15.787 1.00 27.45 O ANISOU 506 O GLU A 68 4392 3192 2843 -20 332 -110 O ATOM 507 CB GLU A 68 5.859 15.803 18.563 1.00 26.99 C ANISOU 507 CB GLU A 68 4165 3173 2914 71 39 -228 C ATOM 508 CG GLU A 68 7.034 16.725 18.962 1.00 27.65 C ANISOU 508 CG GLU A 68 4206 3025 3275 204 29 -688 C ATOM 509 CD GLU A 68 8.173 15.998 19.672 1.00 29.74 C ANISOU 509 CD GLU A 68 4546 3539 3211 336 154 -345 C ATOM 510 OE1 GLU A 68 9.195 15.712 19.013 1.00 33.75 O ANISOU 510 OE1 GLU A 68 4647 4260 3914 388 532 -327 O ATOM 511 OE2 GLU A 68 8.089 15.715 20.887 1.00 34.72 O1- ANISOU 511 OE2 GLU A 68 5061 4500 3630 691 406 -447 O1- ATOM 512 N ALA A 69 4.787 18.254 16.144 1.00 25.06 N ANISOU 512 N ALA A 69 4304 2879 2336 -113 103 -209 N ATOM 513 CA ALA A 69 5.111 18.766 14.807 1.00 26.10 C ANISOU 513 CA ALA A 69 4258 3174 2482 -122 119 -144 C ATOM 514 C ALA A 69 4.933 20.251 14.650 1.00 27.26 C ANISOU 514 C ALA A 69 4391 3323 2641 -4 202 -80 C ATOM 515 O ALA A 69 4.370 20.936 15.514 1.00 27.71 O ANISOU 515 O ALA A 69 4561 3264 2701 -10 317 -60 O ATOM 516 CB ALA A 69 4.247 18.003 13.724 1.00 26.70 C ANISOU 516 CB ALA A 69 4367 3176 2601 -24 -28 -195 C ATOM 517 N ALA A 70 5.409 20.748 13.509 1.00 28.18 N ANISOU 517 N ALA A 70 4511 3356 2840 -23 267 84 N ATOM 518 CA ALA A 70 5.183 22.100 13.102 1.00 29.34 C ANISOU 518 CA ALA A 70 4660 3550 2935 4 126 192 C ATOM 519 C ALA A 70 4.993 22.160 11.595 1.00 29.72 C ANISOU 519 C ALA A 70 4760 3581 2951 69 226 226 C ATOM 520 O ALA A 70 5.549 21.355 10.839 1.00 28.79 O ANISOU 520 O ALA A 70 4757 3459 2722 119 176 241 O ATOM 521 CB ALA A 70 6.312 22.985 13.551 1.00 29.60 C ANISOU 521 CB ALA A 70 4575 3426 3243 -60 223 322 C ATOM 522 N GLY A 71 4.196 23.122 11.165 1.00 29.54 N ANISOU 522 N GLY A 71 4748 3610 2865 46 115 294 N ATOM 523 CA GLY A 71 3.936 23.257 9.735 1.00 30.28 C ANISOU 523 CA GLY A 71 4898 3565 3041 81 112 294 C ATOM 524 C GLY A 71 3.456 24.644 9.386 1.00 29.74 C ANISOU 524 C GLY A 71 4798 3375 3124 18 126 268 C ATOM 525 O GLY A 71 3.509 25.551 10.213 1.00 28.95 O ANISOU 525 O GLY A 71 4767 3174 3056 -38 93 268 O ATOM 526 N ILE A 72 2.928 24.763 8.174 1.00 29.59 N ANISOU 526 N ILE A 72 4720 3347 3174 117 23 225 N ATOM 527 CA ILE A 72 2.394 26.023 7.648 1.00 29.32 C ANISOU 527 CA ILE A 72 4660 3268 3209 163 94 348 C ATOM 528 C ILE A 72 0.968 25.826 7.190 1.00 29.75 C ANISOU 528 C ILE A 72 4800 3367 3138 193 72 212 C ATOM 529 O ILE A 72 0.675 24.835 6.513 1.00 31.83 O ANISOU 529 O ILE A 72 4996 3709 3388 189 -57 115 O ATOM 530 CB ILE A 72 3.256 26.567 6.463 1.00 30.11 C ANISOU 530 CB ILE A 72 4518 3462 3460 77 74 441 C ATOM 531 CG1 ILE A 72 4.646 27.000 6.918 1.00 33.23 C ANISOU 531 CG1 ILE A 72 4871 3641 4113 89 -88 132 C ATOM 532 CG2 ILE A 72 2.542 27.780 5.837 1.00 30.93 C ANISOU 532 CG2 ILE A 72 4691 2995 4065 228 136 433 C ATOM 533 CD1 ILE A 72 4.758 28.499 7.302 1.00 38.35 C ANISOU 533 CD1 ILE A 72 5357 3779 5434 -101 -141 218 C ATOM 534 N VAL A 73 0.070 26.764 7.543 1.00 29.55 N ANISOU 534 N VAL A 73 4877 3374 2974 271 70 184 N ATOM 535 CA VAL A 73 -1.337 26.670 7.167 1.00 30.07 C ANISOU 535 CA VAL A 73 4907 3506 3013 275 75 77 C ATOM 536 C VAL A 73 -1.538 26.811 5.640 1.00 31.48 C ANISOU 536 C VAL A 73 5087 3708 3165 252 113 123 C ATOM 537 O VAL A 73 -1.138 27.808 5.028 1.00 31.91 O ANISOU 537 O VAL A 73 5262 3725 3136 290 160 172 O ATOM 538 CB VAL A 73 -2.220 27.704 7.925 1.00 30.49 C ANISOU 538 CB VAL A 73 4923 3504 3155 282 57 66 C ATOM 539 CG1 VAL A 73 -3.673 27.618 7.479 1.00 31.39 C ANISOU 539 CG1 VAL A 73 4874 3588 3462 211 42 10 C ATOM 540 CG2 VAL A 73 -2.143 27.447 9.404 1.00 29.89 C ANISOU 540 CG2 VAL A 73 4925 3490 2940 261 -22 114 C ATOM 541 N GLU A 74 -2.123 25.768 5.065 1.00 31.64 N ANISOU 541 N GLU A 74 5085 3841 3093 194 -17 75 N ATOM 542 CA GLU A 74 -2.445 25.722 3.657 1.00 32.13 C ANISOU 542 CA GLU A 74 5178 3936 3094 195 -70 162 C ATOM 543 C GLU A 74 -3.783 26.391 3.391 1.00 32.99 C ANISOU 543 C GLU A 74 5212 4068 3252 250 39 193 C ATOM 544 O GLU A 74 -3.893 27.201 2.458 1.00 34.69 O ANISOU 544 O GLU A 74 5494 4127 3559 443 53 297 O ATOM 545 CB GLU A 74 -2.417 24.269 3.133 1.00 31.05 C ANISOU 545 CB GLU A 74 5020 3806 2971 198 -200 191 C ATOM 546 CG GLU A 74 -2.927 24.091 1.681 1.00 33.80 C ANISOU 546 CG GLU A 74 5284 4172 3385 291 -385 298 C ATOM 547 CD GLU A 74 -4.436 23.966 1.583 1.00 34.76 C ANISOU 547 CD GLU A 74 5179 4542 3485 24 -248 509 C ATOM 548 OE1 GLU A 74 -4.996 24.209 0.473 1.00 37.40 O ANISOU 548 OE1 GLU A 74 5428 5015 3766 338 -558 450 O ATOM 549 OE2 GLU A 74 -5.082 23.612 2.590 1.00 36.45 O1- ANISOU 549 OE2 GLU A 74 5476 5016 3356 164 -317 409 O1- ATOM 550 N SER A 75 -4.806 26.057 4.183 1.00 34.22 N ANISOU 550 N SER A 75 5338 4291 3371 287 -2 109 N ATOM 551 CA SER A 75 -6.096 26.710 4.056 1.00 34.39 C ANISOU 551 CA SER A 75 5183 4521 3361 303 -41 159 C ATOM 552 C SER A 75 -6.906 26.604 5.341 1.00 33.95 C ANISOU 552 C SER A 75 5198 4369 3330 397 -37 178 C ATOM 553 O SER A 75 -6.613 25.760 6.209 1.00 33.14 O ANISOU 553 O SER A 75 5138 4515 2937 478 -202 402 O ATOM 554 CB SER A 75 -6.888 26.135 2.869 1.00 35.47 C ANISOU 554 CB SER A 75 5307 4576 3593 303 -90 81 C ATOM 555 OG SER A 75 -7.382 24.827 3.148 1.00 36.55 O ANISOU 555 OG SER A 75 5398 4767 3722 319 -126 163 O ATOM 556 N ILE A 76 -7.904 27.472 5.478 1.00 34.45 N ANISOU 556 N ILE A 76 5162 4487 3439 392 -81 167 N ATOM 557 CA ILE A 76 -8.767 27.444 6.671 1.00 34.22 C ANISOU 557 CA ILE A 76 5151 4208 3640 450 -46 16 C ATOM 558 C ILE A 76 -10.217 27.226 6.264 1.00 33.72 C ANISOU 558 C ILE A 76 5074 4196 3540 434 -79 21 C ATOM 559 O ILE A 76 -10.676 27.704 5.193 1.00 33.80 O ANISOU 559 O ILE A 76 5202 4145 3495 520 -146 55 O ATOM 560 CB ILE A 76 -8.606 28.735 7.560 1.00 34.38 C ANISOU 560 CB ILE A 76 5100 4334 3626 413 -235 -11 C ATOM 561 CG1 ILE A 76 -8.874 29.997 6.719 1.00 34.20 C ANISOU 561 CG1 ILE A 76 5184 4220 3588 439 8 16 C ATOM 562 CG2 ILE A 76 -7.202 28.779 8.207 1.00 32.62 C ANISOU 562 CG2 ILE A 76 4680 4175 3537 336 -189 -215 C ATOM 563 CD1 ILE A 76 -9.082 31.290 7.551 1.00 35.14 C ANISOU 563 CD1 ILE A 76 5195 4241 3913 514 -43 48 C ATOM 564 N GLY A 77 -10.945 26.491 7.095 1.00 33.65 N ANISOU 564 N GLY A 77 5090 4110 3586 421 -21 -85 N ATOM 565 CA GLY A 77 -12.385 26.338 6.898 1.00 35.40 C ANISOU 565 CA GLY A 77 5158 4427 3863 410 -34 89 C ATOM 566 C GLY A 77 -13.145 27.582 7.338 1.00 36.78 C ANISOU 566 C GLY A 77 5236 4575 4163 396 -54 6 C ATOM 567 O GLY A 77 -12.548 28.510 7.890 1.00 36.85 O ANISOU 567 O GLY A 77 5155 4655 4189 425 -237 127 O ATOM 568 N GLU A 78 -14.457 27.579 7.091 1.00 38.07 N ANISOU 568 N GLU A 78 5263 4773 4426 516 -37 -23 N ATOM 569 CA GLU A 78 -15.361 28.667 7.464 1.00 40.01 C ANISOU 569 CA GLU A 78 5468 4979 4753 459 -22 -59 C ATOM 570 C GLU A 78 -15.249 28.977 8.947 1.00 39.32 C ANISOU 570 C GLU A 78 5409 4938 4591 548 18 -39 C ATOM 571 O GLU A 78 -15.175 28.053 9.775 1.00 39.29 O ANISOU 571 O GLU A 78 5490 4941 4496 578 107 -28 O ATOM 572 CB GLU A 78 -16.817 28.285 7.174 1.00 39.70 C ANISOU 572 CB GLU A 78 5334 4951 4795 496 1 -101 C ATOM 573 CG GLU A 78 -17.173 28.085 5.730 1.00 42.33 C ANISOU 573 CG GLU A 78 5552 5383 5145 423 14 -112 C ATOM 574 CD GLU A 78 -18.667 27.905 5.512 1.00 42.88 C ANISOU 574 CD GLU A 78 5713 5339 5239 243 -71 -116 C ATOM 575 OE1 GLU A 78 -19.067 27.716 4.347 1.00 48.75 O ANISOU 575 OE1 GLU A 78 6602 6144 5776 19 -332 -260 O ATOM 576 OE2 GLU A 78 -19.437 27.949 6.496 1.00 44.88 O1- ANISOU 576 OE2 GLU A 78 5857 5310 5882 228 184 -529 O1- ATOM 577 N GLY A 79 -15.221 30.270 9.270 1.00 39.68 N ANISOU 577 N GLY A 79 5471 4994 4610 556 -109 1 N ATOM 578 CA GLY A 79 -15.295 30.744 10.661 1.00 38.93 C ANISOU 578 CA GLY A 79 5318 4897 4576 631 -32 -40 C ATOM 579 C GLY A 79 -14.025 30.648 11.497 1.00 39.05 C ANISOU 579 C GLY A 79 5421 4913 4503 703 -72 47 C ATOM 580 O GLY A 79 -14.035 30.982 12.675 1.00 38.85 O ANISOU 580 O GLY A 79 5445 4776 4538 829 -196 -15 O ATOM 581 N VAL A 80 -12.925 30.228 10.880 1.00 38.06 N ANISOU 581 N VAL A 80 5268 4789 4403 707 -29 41 N ATOM 582 CA VAL A 80 -11.617 30.181 11.554 1.00 38.01 C ANISOU 582 CA VAL A 80 5336 4696 4407 532 7 104 C ATOM 583 C VAL A 80 -11.063 31.590 11.705 1.00 38.30 C ANISOU 583 C VAL A 80 5439 4701 4412 518 62 73 C ATOM 584 O VAL A 80 -11.018 32.356 10.713 1.00 37.92 O ANISOU 584 O VAL A 80 5637 4405 4365 612 115 214 O ATOM 585 CB VAL A 80 -10.609 29.254 10.786 1.00 37.13 C ANISOU 585 CB VAL A 80 5152 4696 4259 516 104 17 C ATOM 586 CG1 VAL A 80 -9.187 29.378 11.337 1.00 37.84 C ANISOU 586 CG1 VAL A 80 5219 4608 4549 429 -133 204 C ATOM 587 CG2 VAL A 80 -11.020 27.791 10.889 1.00 36.96 C ANISOU 587 CG2 VAL A 80 5255 4846 3941 425 -70 139 C ATOM 588 N THR A 81 -10.702 31.946 12.943 1.00 38.24 N ANISOU 588 N THR A 81 5457 4666 4406 444 141 38 N ATOM 589 CA THR A 81 -10.194 33.279 13.253 1.00 37.77 C ANISOU 589 CA THR A 81 5361 4598 4390 388 159 -21 C ATOM 590 C THR A 81 -8.786 33.347 13.817 1.00 38.08 C ANISOU 590 C THR A 81 5489 4591 4386 271 113 53 C ATOM 591 O THR A 81 -8.199 34.424 13.822 1.00 40.05 O ANISOU 591 O THR A 81 5725 4771 4719 193 29 130 O ATOM 592 CB THR A 81 -11.096 33.999 14.264 1.00 38.00 C ANISOU 592 CB THR A 81 5365 4569 4502 408 140 -100 C ATOM 593 CG2 THR A 81 -12.564 33.924 13.830 1.00 39.71 C ANISOU 593 CG2 THR A 81 5289 4731 5065 516 198 -301 C ATOM 594 OG1 THR A 81 -10.932 33.396 15.550 1.00 36.40 O ANISOU 594 OG1 THR A 81 5033 4282 4514 630 190 -304 O ATOM 595 N THR A 82 -8.244 32.228 14.312 1.00 37.64 N ANISOU 595 N THR A 82 5432 4580 4288 204 45 90 N ATOM 596 CA THR A 82 -7.012 32.283 15.091 1.00 37.23 C ANISOU 596 CA THR A 82 5487 4448 4209 185 23 156 C ATOM 597 C THR A 82 -5.771 32.020 14.277 1.00 36.47 C ANISOU 597 C THR A 82 5444 4332 4080 175 27 106 C ATOM 598 O THR A 82 -4.641 32.252 14.763 1.00 36.19 O ANISOU 598 O THR A 82 5433 4141 4176 158 164 -88 O ATOM 599 CB THR A 82 -7.034 31.292 16.289 1.00 37.19 C ANISOU 599 CB THR A 82 5492 4519 4116 198 30 222 C ATOM 600 CG2 THR A 82 -8.118 31.676 17.324 1.00 37.00 C ANISOU 600 CG2 THR A 82 5443 4400 4215 248 -2 88 C ATOM 601 OG1 THR A 82 -7.254 29.956 15.816 1.00 37.07 O ANISOU 601 OG1 THR A 82 5499 4524 4063 21 -144 356 O ATOM 602 N VAL A 83 -5.969 31.514 13.057 1.00 36.54 N ANISOU 602 N VAL A 83 5548 4235 4098 204 92 68 N ATOM 603 CA VAL A 83 -4.877 31.292 12.106 1.00 36.47 C ANISOU 603 CA VAL A 83 5514 4375 3964 148 49 158 C ATOM 604 C VAL A 83 -5.335 31.630 10.685 1.00 36.75 C ANISOU 604 C VAL A 83 5562 4408 3993 148 94 123 C ATOM 605 O VAL A 83 -6.529 31.676 10.387 1.00 36.27 O ANISOU 605 O VAL A 83 5638 4357 3783 71 291 157 O ATOM 606 CB VAL A 83 -4.363 29.822 12.103 1.00 35.86 C ANISOU 606 CB VAL A 83 5408 4304 3911 237 -38 145 C ATOM 607 CG1 VAL A 83 -3.865 29.356 13.517 1.00 35.76 C ANISOU 607 CG1 VAL A 83 5457 4325 3803 80 -194 173 C ATOM 608 CG2 VAL A 83 -5.423 28.844 11.565 1.00 35.79 C ANISOU 608 CG2 VAL A 83 5374 4293 3930 211 -62 223 C ATOM 609 N ARG A 84 -4.358 31.840 9.809 1.00 37.27 N ANISOU 609 N ARG A 84 5719 4456 3985 59 125 145 N ATOM 610 CA ARG A 84 -4.638 32.262 8.440 1.00 38.83 C ANISOU 610 CA ARG A 84 5818 4619 4315 166 51 163 C ATOM 611 C ARG A 84 -3.680 31.511 7.526 1.00 37.39 C ANISOU 611 C ARG A 84 5699 4449 4056 181 28 167 C ATOM 612 O ARG A 84 -2.606 31.098 7.971 1.00 37.67 O ANISOU 612 O ARG A 84 5852 4437 4023 234 15 189 O ATOM 613 CB ARG A 84 -4.453 33.776 8.283 1.00 39.21 C ANISOU 613 CB ARG A 84 5754 4696 4446 11 55 205 C ATOM 614 CG ARG A 84 -5.534 34.651 8.957 1.00 41.11 C ANISOU 614 CG ARG A 84 5887 4820 4913 10 211 218 C ATOM 615 CD ARG A 84 -5.375 36.149 8.595 1.00 42.08 C ANISOU 615 CD ARG A 84 6079 4801 5109 139 87 205 C ATOM 616 NE ARG A 84 -6.413 37.049 9.143 1.00 45.57 N ANISOU 616 NE ARG A 84 6279 5352 5682 160 197 -6 N ATOM 617 CZ ARG A 84 -7.068 37.974 8.430 1.00 47.49 C ANISOU 617 CZ ARG A 84 6347 5770 5926 71 92 22 C ATOM 618 NH1 ARG A 84 -6.811 38.133 7.140 1.00 48.97 N1+ ANISOU 618 NH1 ARG A 84 6700 5952 5951 -185 129 157 N1+ ATOM 619 NH2 ARG A 84 -7.975 38.761 9.002 1.00 49.45 N ANISOU 619 NH2 ARG A 84 6402 6142 6245 67 190 -6 N ATOM 620 N PRO A 85 -4.058 31.327 6.255 1.00 37.30 N ANISOU 620 N PRO A 85 5711 4414 4047 211 -25 191 N ATOM 621 CA PRO A 85 -3.119 30.725 5.307 1.00 36.50 C ANISOU 621 CA PRO A 85 5671 4335 3862 221 -38 222 C ATOM 622 C PRO A 85 -1.750 31.372 5.363 1.00 36.25 C ANISOU 622 C PRO A 85 5683 4292 3797 178 -13 266 C ATOM 623 O PRO A 85 -1.642 32.610 5.428 1.00 37.54 O ANISOU 623 O PRO A 85 5899 4395 3968 110 85 259 O ATOM 624 CB PRO A 85 -3.786 31.009 3.945 1.00 36.17 C ANISOU 624 CB PRO A 85 5578 4269 3896 177 -117 316 C ATOM 625 CG PRO A 85 -5.214 30.896 4.258 1.00 36.23 C ANISOU 625 CG PRO A 85 5585 4296 3885 281 -7 281 C ATOM 626 CD PRO A 85 -5.356 31.607 5.613 1.00 36.52 C ANISOU 626 CD PRO A 85 5604 4314 3958 311 -44 153 C ATOM 627 N GLY A 86 -0.712 30.546 5.346 1.00 35.64 N ANISOU 627 N GLY A 86 5672 4155 3712 186 124 226 N ATOM 628 CA GLY A 86 0.673 31.006 5.411 1.00 36.16 C ANISOU 628 CA GLY A 86 5593 4217 3926 110 147 234 C ATOM 629 C GLY A 86 1.295 31.143 6.790 1.00 35.78 C ANISOU 629 C GLY A 86 5525 4169 3899 87 174 341 C ATOM 630 O GLY A 86 2.520 31.282 6.930 1.00 36.25 O ANISOU 630 O GLY A 86 5701 4245 3825 66 240 456 O ATOM 631 N ASP A 87 0.473 31.086 7.830 1.00 36.71 N ANISOU 631 N ASP A 87 5553 4303 4089 161 173 145 N ATOM 632 CA ASP A 87 0.979 31.142 9.206 1.00 36.21 C ANISOU 632 CA ASP A 87 5491 4149 4117 180 169 240 C ATOM 633 C ASP A 87 1.734 29.885 9.595 1.00 35.52 C ANISOU 633 C ASP A 87 5431 4024 4041 101 169 264 C ATOM 634 O ASP A 87 1.352 28.790 9.169 1.00 35.84 O ANISOU 634 O ASP A 87 5624 3921 4072 199 127 302 O ATOM 635 CB ASP A 87 -0.178 31.299 10.179 1.00 36.43 C ANISOU 635 CB ASP A 87 5452 4133 4254 84 226 181 C ATOM 636 CG ASP A 87 -0.743 32.677 10.202 1.00 38.27 C ANISOU 636 CG ASP A 87 5555 4403 4583 112 227 203 C ATOM 637 OD1 ASP A 87 -0.134 33.618 9.629 1.00 40.40 O ANISOU 637 OD1 ASP A 87 5908 4445 4995 -4 215 469 O ATOM 638 OD2 ASP A 87 -1.824 32.800 10.809 1.00 40.88 O1- ANISOU 638 OD2 ASP A 87 5814 4713 5005 21 535 26 O1- ATOM 639 N LYS A 88 2.806 30.055 10.366 1.00 34.02 N ANISOU 639 N LYS A 88 5259 3831 3836 134 246 364 N ATOM 640 CA LYS A 88 3.487 28.919 11.007 1.00 33.21 C ANISOU 640 CA LYS A 88 5160 3849 3609 80 255 270 C ATOM 641 C LYS A 88 2.671 28.481 12.215 1.00 31.61 C ANISOU 641 C LYS A 88 5054 3565 3389 61 318 141 C ATOM 642 O LYS A 88 2.109 29.329 12.971 1.00 30.73 O ANISOU 642 O LYS A 88 5282 3260 3134 -20 327 2 O ATOM 643 CB LYS A 88 4.912 29.272 11.413 1.00 33.14 C ANISOU 643 CB LYS A 88 5075 3843 3671 32 347 339 C ATOM 644 CG LYS A 88 5.865 29.405 10.194 1.00 34.66 C ANISOU 644 CG LYS A 88 5104 4355 3710 11 353 234 C ATOM 645 CD LYS A 88 7.285 29.600 10.615 1.00 37.49 C ANISOU 645 CD LYS A 88 5185 4414 4645 22 354 151 C ATOM 646 CE LYS A 88 8.179 29.671 9.389 1.00 37.12 C ANISOU 646 CE LYS A 88 4996 4547 4559 181 189 173 C ATOM 647 NZ LYS A 88 9.482 30.319 9.729 1.00 37.85 N1+ ANISOU 647 NZ LYS A 88 5391 4382 4607 -198 108 92 N1+ ATOM 648 N VAL A 89 2.601 27.159 12.408 1.00 29.69 N ANISOU 648 N VAL A 89 4935 3417 2928 62 140 111 N ATOM 649 CA VAL A 89 1.698 26.588 13.423 1.00 29.82 C ANISOU 649 CA VAL A 89 4734 3422 3173 90 147 12 C ATOM 650 C VAL A 89 2.237 25.320 14.031 1.00 28.90 C ANISOU 650 C VAL A 89 4679 3382 2917 139 177 18 C ATOM 651 O VAL A 89 3.032 24.616 13.404 1.00 28.95 O ANISOU 651 O VAL A 89 4790 3227 2981 246 275 164 O ATOM 652 CB VAL A 89 0.237 26.291 12.898 1.00 29.78 C ANISOU 652 CB VAL A 89 4730 3333 3251 79 -7 -117 C ATOM 653 CG1 VAL A 89 -0.541 27.558 12.598 1.00 30.48 C ANISOU 653 CG1 VAL A 89 4903 3158 3519 -11 -53 -122 C ATOM 654 CG2 VAL A 89 0.228 25.323 11.679 1.00 31.60 C ANISOU 654 CG2 VAL A 89 4942 3849 3213 128 160 -247 C ATOM 655 N ILE A 90 1.759 25.017 15.246 1.00 27.88 N ANISOU 655 N ILE A 90 4579 3260 2754 84 161 -38 N ATOM 656 CA ILE A 90 2.066 23.782 15.932 1.00 27.82 C ANISOU 656 CA ILE A 90 4439 3413 2719 151 -27 -182 C ATOM 657 C ILE A 90 0.731 23.152 16.347 1.00 27.94 C ANISOU 657 C ILE A 90 4444 3444 2726 141 -61 -95 C ATOM 658 O ILE A 90 -0.079 23.798 17.035 1.00 28.95 O ANISOU 658 O ILE A 90 4678 3269 3052 16 53 -256 O ATOM 659 CB ILE A 90 2.944 24.045 17.169 1.00 26.96 C ANISOU 659 CB ILE A 90 4343 3303 2598 133 -39 -260 C ATOM 660 CG1 ILE A 90 4.393 24.349 16.731 1.00 27.51 C ANISOU 660 CG1 ILE A 90 4262 3362 2826 21 -166 -484 C ATOM 661 CG2 ILE A 90 2.870 22.841 18.114 1.00 27.70 C ANISOU 661 CG2 ILE A 90 4578 3291 2652 285 -44 -109 C ATOM 662 CD1 ILE A 90 5.341 24.760 17.891 1.00 28.78 C ANISOU 662 CD1 ILE A 90 4421 3574 2941 138 -159 -239 C ATOM 663 N PRO A 91 0.437 21.940 15.841 1.00 27.64 N ANISOU 663 N PRO A 91 4405 3328 2768 241 -1 -145 N ATOM 664 CA PRO A 91 -0.780 21.206 16.243 1.00 27.39 C ANISOU 664 CA PRO A 91 4337 3382 2685 204 144 -170 C ATOM 665 C PRO A 91 -0.715 20.873 17.720 1.00 28.53 C ANISOU 665 C PRO A 91 4323 3512 3006 185 96 -79 C ATOM 666 O PRO A 91 0.387 20.636 18.275 1.00 28.42 O ANISOU 666 O PRO A 91 4204 3328 3263 333 205 -86 O ATOM 667 CB PRO A 91 -0.733 19.924 15.368 1.00 28.27 C ANISOU 667 CB PRO A 91 4499 3387 2853 229 224 -162 C ATOM 668 CG PRO A 91 0.153 20.316 14.220 1.00 30.46 C ANISOU 668 CG PRO A 91 4567 3685 3320 -10 120 -172 C ATOM 669 CD PRO A 91 1.199 21.189 14.819 1.00 28.14 C ANISOU 669 CD PRO A 91 4369 3576 2744 316 -169 -293 C ATOM 670 N LEU A 92 -1.895 20.908 18.351 1.00 27.42 N ANISOU 670 N LEU A 92 4171 3541 2703 319 213 -60 N ATOM 671 CA LEU A 92 -1.990 20.703 19.809 1.00 28.77 C ANISOU 671 CA LEU A 92 4325 3582 3023 337 304 -148 C ATOM 672 C LEU A 92 -2.660 19.359 20.128 1.00 28.32 C ANISOU 672 C LEU A 92 4195 3521 3044 395 247 -155 C ATOM 673 O LEU A 92 -3.879 19.217 19.964 1.00 28.88 O ANISOU 673 O LEU A 92 4206 3459 3308 446 161 -245 O ATOM 674 CB LEU A 92 -2.737 21.893 20.429 1.00 29.16 C ANISOU 674 CB LEU A 92 4456 3556 3066 426 215 -35 C ATOM 675 CG LEU A 92 -2.195 23.281 20.055 1.00 29.88 C ANISOU 675 CG LEU A 92 4400 3666 3285 400 342 -36 C ATOM 676 CD1 LEU A 92 -3.189 24.335 20.591 1.00 32.23 C ANISOU 676 CD1 LEU A 92 5019 4066 3160 631 537 -153 C ATOM 677 CD2 LEU A 92 -0.770 23.572 20.509 1.00 29.97 C ANISOU 677 CD2 LEU A 92 4710 3150 3524 133 96 -117 C ATOM 678 N PHE A 93 -1.884 18.376 20.605 1.00 27.50 N ANISOU 678 N PHE A 93 4201 3313 2934 351 220 -94 N ATOM 679 CA PHE A 93 -2.494 17.065 20.916 1.00 27.69 C ANISOU 679 CA PHE A 93 4052 3338 3130 313 112 -132 C ATOM 680 C PHE A 93 -3.391 17.134 22.145 1.00 27.94 C ANISOU 680 C PHE A 93 4146 3338 3132 384 94 -109 C ATOM 681 O PHE A 93 -4.290 16.320 22.287 1.00 29.51 O ANISOU 681 O PHE A 93 4289 3432 3490 394 175 -77 O ATOM 682 CB PHE A 93 -1.476 15.917 21.024 1.00 26.93 C ANISOU 682 CB PHE A 93 3856 3351 3023 371 168 -139 C ATOM 683 CG PHE A 93 -0.683 15.916 22.297 1.00 28.45 C ANISOU 683 CG PHE A 93 4002 3496 3311 312 72 -101 C ATOM 684 CD1 PHE A 93 -1.182 15.335 23.460 1.00 29.18 C ANISOU 684 CD1 PHE A 93 3891 3936 3260 96 -61 -54 C ATOM 685 CD2 PHE A 93 0.602 16.453 22.314 1.00 28.65 C ANISOU 685 CD2 PHE A 93 3891 3489 3505 372 -41 -246 C ATOM 686 CE1 PHE A 93 -0.430 15.367 24.663 1.00 27.65 C ANISOU 686 CE1 PHE A 93 3977 3345 3181 397 -231 134 C ATOM 687 CE2 PHE A 93 1.352 16.475 23.469 1.00 28.65 C ANISOU 687 CE2 PHE A 93 4056 3533 3295 564 0 35 C ATOM 688 CZ PHE A 93 0.837 15.919 24.648 1.00 26.12 C ANISOU 688 CZ PHE A 93 3938 2957 3026 384 -46 53 C ATOM 689 N THR A 94 -3.158 18.115 23.011 1.00 28.69 N ANISOU 689 N THR A 94 4362 3424 3114 489 159 -220 N ATOM 690 CA THR A 94 -4.115 18.480 24.061 1.00 29.95 C ANISOU 690 CA THR A 94 4504 3587 3285 484 161 -275 C ATOM 691 C THR A 94 -4.732 19.783 23.605 1.00 30.13 C ANISOU 691 C THR A 94 4622 3604 3222 467 200 -300 C ATOM 692 O THR A 94 -4.039 20.791 23.571 1.00 30.36 O ANISOU 692 O THR A 94 4736 3478 3321 487 114 -334 O ATOM 693 CB THR A 94 -3.420 18.675 25.413 1.00 30.62 C ANISOU 693 CB THR A 94 4707 3664 3262 541 204 -299 C ATOM 694 CG2 THR A 94 -4.453 18.892 26.532 1.00 32.14 C ANISOU 694 CG2 THR A 94 4875 3589 3746 681 342 -514 C ATOM 695 OG1 THR A 94 -2.694 17.493 25.732 1.00 30.74 O ANISOU 695 OG1 THR A 94 4446 3910 3322 709 271 -370 O ATOM 696 N PRO A 95 -6.029 19.763 23.243 1.00 30.16 N ANISOU 696 N PRO A 95 4729 3590 3140 504 85 -317 N ATOM 697 CA PRO A 95 -6.712 20.917 22.665 1.00 29.81 C ANISOU 697 CA PRO A 95 4660 3545 3118 613 134 -375 C ATOM 698 C PRO A 95 -6.908 22.005 23.747 1.00 29.71 C ANISOU 698 C PRO A 95 4815 3501 2971 598 75 -400 C ATOM 699 O PRO A 95 -6.714 21.730 24.942 1.00 29.67 O ANISOU 699 O PRO A 95 4650 3675 2946 691 81 -308 O ATOM 700 CB PRO A 95 -8.073 20.357 22.238 1.00 30.40 C ANISOU 700 CB PRO A 95 4996 3405 3148 527 70 -567 C ATOM 701 CG PRO A 95 -8.104 18.966 22.582 1.00 32.18 C ANISOU 701 CG PRO A 95 4788 3938 3498 502 95 -129 C ATOM 702 CD PRO A 95 -6.951 18.634 23.449 1.00 30.79 C ANISOU 702 CD PRO A 95 4692 3720 3286 484 31 -216 C ATOM 703 N GLN A 96 -7.255 23.227 23.345 1.00 28.95 N ANISOU 703 N GLN A 96 4703 3380 2916 686 138 -465 N ATOM 704 CA GLN A 96 -7.698 24.254 24.334 1.00 29.81 C ANISOU 704 CA GLN A 96 4888 3507 2928 593 85 -395 C ATOM 705 C GLN A 96 -8.946 24.893 23.767 1.00 30.97 C ANISOU 705 C GLN A 96 4944 3637 3186 621 128 -348 C ATOM 706 O GLN A 96 -8.881 25.868 23.015 1.00 32.33 O ANISOU 706 O GLN A 96 5208 3731 3345 629 -51 -173 O ATOM 707 CB GLN A 96 -6.613 25.262 24.655 1.00 28.93 C ANISOU 707 CB GLN A 96 4739 3445 2808 757 61 -524 C ATOM 708 CG GLN A 96 -7.100 26.311 25.676 1.00 28.58 C ANISOU 708 CG GLN A 96 5154 3105 2599 704 -4 -457 C ATOM 709 CD GLN A 96 -6.053 27.284 26.107 1.00 30.16 C ANISOU 709 CD GLN A 96 5160 3432 2867 487 114 -328 C ATOM 710 NE2 GLN A 96 -6.451 28.184 26.998 1.00 33.60 N ANISOU 710 NE2 GLN A 96 5835 3455 3475 402 186 -668 N ATOM 711 OE1 GLN A 96 -4.895 27.216 25.713 1.00 33.00 O ANISOU 711 OE1 GLN A 96 5715 3452 3370 429 34 -422 O ATOM 712 N CYS A 97 -10.090 24.291 24.078 1.00 32.46 N ANISOU 712 N CYS A 97 4800 4096 3437 650 80 -344 N ATOM 713 CA CYS A 97 -11.384 24.798 23.594 1.00 33.42 C ANISOU 713 CA CYS A 97 5012 4205 3479 776 52 -402 C ATOM 714 C CYS A 97 -11.767 26.164 24.166 1.00 33.95 C ANISOU 714 C CYS A 97 5074 4212 3610 763 60 -344 C ATOM 715 O CYS A 97 -12.423 26.935 23.497 1.00 34.42 O ANISOU 715 O CYS A 97 5283 4245 3548 989 94 -486 O ATOM 716 CB CYS A 97 -12.495 23.754 23.813 1.00 33.55 C ANISOU 716 CB CYS A 97 4840 4381 3525 720 133 -396 C ATOM 717 SG CYS A 97 -13.227 23.627 25.464 1.00 36.40 S ANISOU 717 SG CYS A 97 5345 5040 3444 1119 394 -814 S ATOM 718 N GLY A 98 -11.346 26.450 25.396 1.00 33.77 N ANISOU 718 N GLY A 98 5089 4110 3631 763 44 -377 N ATOM 719 CA GLY A 98 -11.644 27.723 26.050 1.00 35.20 C ANISOU 719 CA GLY A 98 5245 4291 3838 714 37 -371 C ATOM 720 C GLY A 98 -12.987 27.765 26.744 1.00 36.73 C ANISOU 720 C GLY A 98 5370 4427 4156 697 93 -326 C ATOM 721 O GLY A 98 -13.286 28.755 27.431 1.00 38.46 O ANISOU 721 O GLY A 98 5702 4535 4374 742 100 -427 O ATOM 722 N LYS A 99 -13.798 26.715 26.604 1.00 37.00 N ANISOU 722 N LYS A 99 5299 4546 4213 704 109 -226 N ATOM 723 CA LYS A 99 -15.193 26.766 27.056 1.00 39.05 C ANISOU 723 CA LYS A 99 5465 4854 4516 649 219 -229 C ATOM 724 C LYS A 99 -15.535 25.805 28.195 1.00 38.61 C ANISOU 724 C LYS A 99 5353 4905 4412 688 335 -245 C ATOM 725 O LYS A 99 -16.427 26.080 29.008 1.00 40.23 O ANISOU 725 O LYS A 99 5571 5163 4550 779 435 -245 O ATOM 726 CB LYS A 99 -16.143 26.495 25.882 1.00 39.39 C ANISOU 726 CB LYS A 99 5460 4883 4623 665 168 -249 C ATOM 727 CG LYS A 99 -16.093 27.505 24.727 1.00 41.85 C ANISOU 727 CG LYS A 99 5883 5068 4950 500 197 -184 C ATOM 728 CD LYS A 99 -17.242 27.216 23.779 1.00 46.44 C ANISOU 728 CD LYS A 99 6148 5644 5852 236 -73 -94 C ATOM 729 CE LYS A 99 -17.166 28.001 22.487 1.00 49.29 C ANISOU 729 CE LYS A 99 6531 6140 6056 165 65 -56 C ATOM 730 NZ LYS A 99 -18.112 27.449 21.467 1.00 51.39 N1+ ANISOU 730 NZ LYS A 99 6595 6357 6570 141 -10 -216 N1+ ATOM 731 N CYS A 100 -14.840 24.677 28.261 1.00 37.71 N ANISOU 731 N CYS A 100 5304 4784 4237 650 362 -290 N ATOM 732 CA CYS A 100 -15.173 23.608 29.190 1.00 36.58 C ANISOU 732 CA CYS A 100 5091 4687 4118 676 353 -368 C ATOM 733 C CYS A 100 -14.684 23.972 30.596 1.00 35.61 C ANISOU 733 C CYS A 100 5034 4479 4017 585 353 -379 C ATOM 734 O CYS A 100 -13.843 24.859 30.751 1.00 35.31 O ANISOU 734 O CYS A 100 5049 4383 3983 669 362 -579 O ATOM 735 CB CYS A 100 -14.548 22.284 28.717 1.00 37.43 C ANISOU 735 CB CYS A 100 5088 4805 4328 653 271 -463 C ATOM 736 SG CYS A 100 -12.757 22.078 28.948 1.00 34.82 S ANISOU 736 SG CYS A 100 4781 4763 3686 1062 647 -335 S ATOM 737 N ARG A 101 -15.166 23.254 31.600 1.00 35.61 N ANISOU 737 N ARG A 101 5030 4387 4109 527 381 -357 N ATOM 738 CA ARG A 101 -14.777 23.526 32.991 1.00 35.40 C ANISOU 738 CA ARG A 101 5060 4383 4004 506 320 -163 C ATOM 739 C ARG A 101 -13.280 23.413 33.278 1.00 34.02 C ANISOU 739 C ARG A 101 5031 4115 3779 616 306 -204 C ATOM 740 O ARG A 101 -12.752 24.149 34.115 1.00 34.14 O ANISOU 740 O ARG A 101 5048 4246 3675 726 287 -101 O ATOM 741 CB ARG A 101 -15.601 22.696 33.986 1.00 37.30 C ANISOU 741 CB ARG A 101 5219 4548 4405 417 270 -51 C ATOM 742 CG ARG A 101 -15.581 21.232 33.716 1.00 41.33 C ANISOU 742 CG ARG A 101 5823 4966 4914 318 220 -122 C ATOM 743 CD ARG A 101 -16.031 20.410 34.920 1.00 44.56 C ANISOU 743 CD ARG A 101 5967 5550 5412 150 125 232 C ATOM 744 NE ARG A 101 -15.409 19.094 34.823 1.00 47.21 N ANISOU 744 NE ARG A 101 6303 5731 5900 161 106 10 N ATOM 745 CZ ARG A 101 -15.925 18.059 34.170 1.00 47.66 C ANISOU 745 CZ ARG A 101 6189 5972 5946 -89 35 109 C ATOM 746 NH1 ARG A 101 -17.111 18.167 33.564 1.00 46.95 N1+ ANISOU 746 NH1 ARG A 101 5766 6132 5939 20 321 111 N1+ ATOM 747 NH2 ARG A 101 -15.241 16.915 34.118 1.00 48.34 N ANISOU 747 NH2 ARG A 101 6301 6182 5885 -114 402 -93 N ATOM 748 N VAL A 102 -12.584 22.555 32.514 1.00 32.15 N ANISOU 748 N VAL A 102 4787 3810 3615 812 282 -102 N ATOM 749 CA VAL A 102 -11.144 22.452 32.664 1.00 31.51 C ANISOU 749 CA VAL A 102 4852 3650 3468 710 218 -273 C ATOM 750 C VAL A 102 -10.437 23.670 32.064 1.00 30.34 C ANISOU 750 C VAL A 102 4846 3388 3292 797 91 -245 C ATOM 751 O VAL A 102 -9.521 24.228 32.682 1.00 29.99 O ANISOU 751 O VAL A 102 4919 3259 3216 990 78 -359 O ATOM 752 CB VAL A 102 -10.601 21.187 31.990 1.00 31.01 C ANISOU 752 CB VAL A 102 4817 3460 3504 676 197 -257 C ATOM 753 CG1 VAL A 102 -9.100 21.144 32.101 1.00 31.33 C ANISOU 753 CG1 VAL A 102 4957 3663 3282 578 126 -319 C ATOM 754 CG2 VAL A 102 -11.252 19.920 32.644 1.00 33.21 C ANISOU 754 CG2 VAL A 102 5153 3717 3745 543 224 -138 C ATOM 755 N CYS A 103 -10.840 24.066 30.851 1.00 30.97 N ANISOU 755 N CYS A 103 5010 3560 3195 886 130 -370 N ATOM 756 CA CYS A 103 -10.224 25.230 30.224 1.00 31.02 C ANISOU 756 CA CYS A 103 5081 3635 3069 873 83 -282 C ATOM 757 C CYS A 103 -10.495 26.507 31.030 1.00 32.97 C ANISOU 757 C CYS A 103 5257 3851 3419 795 72 -308 C ATOM 758 O CYS A 103 -9.670 27.431 31.038 1.00 33.76 O ANISOU 758 O CYS A 103 5512 3664 3650 792 13 -319 O ATOM 759 CB CYS A 103 -10.748 25.409 28.797 1.00 30.32 C ANISOU 759 CB CYS A 103 4814 3686 3019 1064 -30 -352 C ATOM 760 SG CYS A 103 -10.012 24.228 27.634 1.00 31.73 S ANISOU 760 SG CYS A 103 5252 3840 2963 1153 143 -366 S ATOM 761 N LYS A 104 -11.643 26.544 31.698 1.00 34.25 N ANISOU 761 N LYS A 104 5481 4027 3502 741 185 -283 N ATOM 762 CA LYS A 104 -12.017 27.696 32.556 1.00 35.29 C ANISOU 762 CA LYS A 104 5490 4173 3744 656 119 -339 C ATOM 763 C LYS A 104 -11.358 27.654 33.936 1.00 35.21 C ANISOU 763 C LYS A 104 5559 4227 3590 684 181 -277 C ATOM 764 O LYS A 104 -11.477 28.614 34.722 1.00 35.93 O ANISOU 764 O LYS A 104 5850 3998 3803 744 112 -353 O ATOM 765 CB LYS A 104 -13.551 27.795 32.687 1.00 34.62 C ANISOU 765 CB LYS A 104 5416 4087 3649 726 213 -362 C ATOM 766 CG LYS A 104 -14.229 28.281 31.396 1.00 38.35 C ANISOU 766 CG LYS A 104 5698 4526 4345 607 16 -170 C ATOM 767 CD LYS A 104 -13.963 29.781 31.161 1.00 42.07 C ANISOU 767 CD LYS A 104 6023 4788 5173 368 0 -116 C ATOM 768 CE LYS A 104 -14.454 30.229 29.786 1.00 44.83 C ANISOU 768 CE LYS A 104 6344 5094 5593 473 -126 23 C ATOM 769 NZ LYS A 104 -15.004 31.634 29.788 1.00 47.19 N1+ ANISOU 769 NZ LYS A 104 6599 5184 6148 462 -290 66 N1+ ATOM 770 N HIS A 105 -10.678 26.560 34.260 1.00 35.45 N ANISOU 770 N HIS A 105 5497 4308 3662 589 196 -346 N ATOM 771 CA HIS A 105 -10.058 26.419 35.594 1.00 34.84 C ANISOU 771 CA HIS A 105 5277 4375 3585 546 242 -266 C ATOM 772 C HIS A 105 -8.626 26.959 35.576 1.00 35.70 C ANISOU 772 C HIS A 105 5347 4436 3780 481 280 -293 C ATOM 773 O HIS A 105 -7.865 26.628 34.667 1.00 34.57 O ANISOU 773 O HIS A 105 5149 4389 3595 691 420 -268 O ATOM 774 CB HIS A 105 -10.077 24.951 36.006 1.00 35.15 C ANISOU 774 CB HIS A 105 5282 4472 3600 503 217 -173 C ATOM 775 CG HIS A 105 -9.735 24.707 37.443 1.00 34.51 C ANISOU 775 CG HIS A 105 5033 4436 3641 451 57 -1 C ATOM 776 CD2 HIS A 105 -10.523 24.360 38.486 1.00 35.04 C ANISOU 776 CD2 HIS A 105 5401 4336 3577 537 31 138 C ATOM 777 ND1 HIS A 105 -8.457 24.814 37.946 1.00 36.31 N ANISOU 777 ND1 HIS A 105 5333 4722 3740 393 83 104 N ATOM 778 CE1 HIS A 105 -8.472 24.537 39.240 1.00 36.35 C ANISOU 778 CE1 HIS A 105 5327 4535 3947 531 -32 260 C ATOM 779 NE2 HIS A 105 -9.713 24.253 39.589 1.00 35.82 N ANISOU 779 NE2 HIS A 105 5424 4624 3561 411 -31 246 N ATOM 780 N PRO A 106 -8.227 27.771 36.582 1.00 36.17 N ANISOU 780 N PRO A 106 5408 4354 3981 395 336 -385 N ATOM 781 CA PRO A 106 -6.846 28.309 36.542 1.00 36.99 C ANISOU 781 CA PRO A 106 5456 4454 4142 373 332 -433 C ATOM 782 C PRO A 106 -5.710 27.272 36.484 1.00 37.70 C ANISOU 782 C PRO A 106 5493 4573 4256 325 293 -434 C ATOM 783 O PRO A 106 -4.638 27.576 35.948 1.00 38.44 O ANISOU 783 O PRO A 106 5668 4707 4230 244 345 -426 O ATOM 784 CB PRO A 106 -6.735 29.169 37.840 1.00 37.47 C ANISOU 784 CB PRO A 106 5604 4390 4241 255 259 -385 C ATOM 785 CG PRO A 106 -7.947 28.899 38.609 1.00 36.61 C ANISOU 785 CG PRO A 106 5465 4361 4081 473 340 -490 C ATOM 786 CD PRO A 106 -8.994 28.293 37.734 1.00 36.30 C ANISOU 786 CD PRO A 106 5315 4414 4062 422 356 -328 C ATOM 787 N GLU A 107 -5.925 26.072 37.013 1.00 37.88 N ANISOU 787 N GLU A 107 5556 4569 4267 385 274 -492 N ATOM 788 CA GLU A 107 -4.833 25.089 37.023 1.00 39.97 C ANISOU 788 CA GLU A 107 5753 4728 4705 295 150 -462 C ATOM 789 C GLU A 107 -5.048 23.864 36.121 1.00 39.15 C ANISOU 789 C GLU A 107 5636 4646 4592 362 164 -524 C ATOM 790 O GLU A 107 -4.152 23.015 36.002 1.00 41.24 O ANISOU 790 O GLU A 107 5889 4767 5013 437 206 -548 O ATOM 791 CB GLU A 107 -4.495 24.666 38.447 1.00 41.18 C ANISOU 791 CB GLU A 107 5848 4924 4872 250 62 -332 C ATOM 792 CG GLU A 107 -3.407 25.529 39.140 1.00 45.95 C ANISOU 792 CG GLU A 107 6357 5478 5620 18 -11 -247 C ATOM 793 CD GLU A 107 -2.007 25.193 38.637 1.00 50.04 C ANISOU 793 CD GLU A 107 6598 6199 6214 79 72 -102 C ATOM 794 OE1 GLU A 107 -1.589 25.738 37.584 1.00 52.92 O ANISOU 794 OE1 GLU A 107 7027 6520 6559 36 352 50 O ATOM 795 OE2 GLU A 107 -1.328 24.370 39.288 1.00 51.19 O1- ANISOU 795 OE2 GLU A 107 6967 6243 6236 -34 -84 -177 O1- ATOM 796 N GLY A 108 -6.205 23.756 35.494 1.00 36.54 N ANISOU 796 N GLY A 108 5456 4312 4115 297 220 -538 N ATOM 797 CA GLY A 108 -6.439 22.607 34.598 1.00 34.53 C ANISOU 797 CA GLY A 108 5288 4013 3817 308 225 -453 C ATOM 798 C GLY A 108 -5.947 22.876 33.189 1.00 33.90 C ANISOU 798 C GLY A 108 5204 3940 3734 320 198 -374 C ATOM 799 O GLY A 108 -5.916 24.019 32.752 1.00 33.85 O ANISOU 799 O GLY A 108 5395 3707 3759 519 231 -662 O ATOM 800 N ASN A 109 -5.573 21.819 32.466 1.00 31.74 N ANISOU 800 N ASN A 109 4931 3774 3353 375 211 -292 N ATOM 801 CA ASN A 109 -5.205 21.973 31.055 1.00 31.39 C ANISOU 801 CA ASN A 109 4733 3842 3352 333 202 -187 C ATOM 802 C ASN A 109 -5.665 20.809 30.201 1.00 30.84 C ANISOU 802 C ASN A 109 4719 3723 3273 296 219 -143 C ATOM 803 O ASN A 109 -5.585 20.876 28.976 1.00 30.75 O ANISOU 803 O ASN A 109 4846 3784 3051 376 378 -273 O ATOM 804 CB ASN A 109 -3.688 22.168 30.865 1.00 31.45 C ANISOU 804 CB ASN A 109 4645 3884 3420 307 133 -99 C ATOM 805 CG ASN A 109 -2.906 20.876 31.045 1.00 31.06 C ANISOU 805 CG ASN A 109 4416 4004 3380 363 186 107 C ATOM 806 ND2 ASN A 109 -1.868 20.663 30.204 1.00 29.22 N ANISOU 806 ND2 ASN A 109 4099 4121 2882 556 28 568 N ATOM 807 OD1 ASN A 109 -3.250 20.056 31.906 1.00 34.13 O ANISOU 807 OD1 ASN A 109 4987 4040 3941 254 230 382 O ATOM 808 N PHE A 110 -6.168 19.755 30.832 1.00 29.92 N ANISOU 808 N PHE A 110 4646 3469 3251 400 196 -112 N ATOM 809 CA PHE A 110 -6.583 18.567 30.086 1.00 29.16 C ANISOU 809 CA PHE A 110 4578 3478 3023 299 255 -106 C ATOM 810 C PHE A 110 -8.013 18.749 29.596 1.00 29.63 C ANISOU 810 C PHE A 110 4628 3509 3119 417 296 -128 C ATOM 811 O PHE A 110 -8.976 18.211 30.163 1.00 29.92 O ANISOU 811 O PHE A 110 4556 3564 3246 439 287 -147 O ATOM 812 CB PHE A 110 -6.410 17.322 30.977 1.00 29.41 C ANISOU 812 CB PHE A 110 4593 3349 3232 261 290 37 C ATOM 813 CG PHE A 110 -6.554 16.008 30.248 1.00 28.46 C ANISOU 813 CG PHE A 110 4548 3406 2857 -50 398 77 C ATOM 814 CD1 PHE A 110 -5.993 15.806 28.994 1.00 30.75 C ANISOU 814 CD1 PHE A 110 4665 3757 3261 358 321 -346 C ATOM 815 CD2 PHE A 110 -7.224 14.932 30.865 1.00 30.04 C ANISOU 815 CD2 PHE A 110 4953 3311 3149 -11 338 172 C ATOM 816 CE1 PHE A 110 -6.145 14.575 28.336 1.00 31.52 C ANISOU 816 CE1 PHE A 110 4559 3628 3787 -60 13 -113 C ATOM 817 CE2 PHE A 110 -7.370 13.694 30.209 1.00 29.67 C ANISOU 817 CE2 PHE A 110 4673 3447 3151 112 32 143 C ATOM 818 CZ PHE A 110 -6.821 13.515 28.960 1.00 30.70 C ANISOU 818 CZ PHE A 110 4751 3551 3360 76 65 -63 C ATOM 819 N CYS A 111 -8.141 19.584 28.566 1.00 29.16 N ANISOU 819 N CYS A 111 4620 3671 2787 494 303 -262 N ATOM 820 CA CYS A 111 -9.421 19.978 28.002 1.00 30.47 C ANISOU 820 CA CYS A 111 4691 3831 3055 503 305 -222 C ATOM 821 C CYS A 111 -10.302 18.767 27.702 1.00 30.12 C ANISOU 821 C CYS A 111 4576 3889 2977 477 200 -280 C ATOM 822 O CYS A 111 -9.798 17.777 27.178 1.00 30.55 O ANISOU 822 O CYS A 111 4799 3583 3224 341 110 -414 O ATOM 823 CB CYS A 111 -9.151 20.802 26.737 1.00 29.73 C ANISOU 823 CB CYS A 111 4600 3831 2864 510 314 -161 C ATOM 824 SG CYS A 111 -10.595 21.101 25.702 1.00 32.26 S ANISOU 824 SG CYS A 111 4924 4171 3161 756 372 -354 S ATOM 825 N LEU A 112 -11.587 18.837 28.064 1.00 31.14 N ANISOU 825 N LEU A 112 4588 4063 3179 454 209 -292 N ATOM 826 CA LEU A 112 -12.559 17.742 27.914 1.00 31.59 C ANISOU 826 CA LEU A 112 4532 4154 3315 443 249 -339 C ATOM 827 C LEU A 112 -12.839 17.319 26.454 1.00 32.00 C ANISOU 827 C LEU A 112 4547 4174 3436 354 140 -306 C ATOM 828 O LEU A 112 -13.406 16.232 26.236 1.00 32.76 O ANISOU 828 O LEU A 112 4615 4212 3619 413 152 -227 O ATOM 829 CB LEU A 112 -13.869 18.011 28.709 1.00 33.50 C ANISOU 829 CB LEU A 112 4667 4416 3644 414 245 -274 C ATOM 830 CG LEU A 112 -13.790 17.985 30.256 1.00 34.87 C ANISOU 830 CG LEU A 112 4807 4607 3834 374 245 -248 C ATOM 831 CD1 LEU A 112 -15.147 18.317 30.875 1.00 37.25 C ANISOU 831 CD1 LEU A 112 5166 4667 4318 274 385 -333 C ATOM 832 CD2 LEU A 112 -13.262 16.662 30.831 1.00 36.74 C ANISOU 832 CD2 LEU A 112 5198 4771 3988 306 443 -227 C ATOM 833 N LYS A 113 -12.420 18.154 25.482 1.00 30.96 N ANISOU 833 N LYS A 113 4362 4145 3254 498 55 -335 N ATOM 834 CA LYS A 113 -12.446 17.810 24.050 1.00 32.09 C ANISOU 834 CA LYS A 113 4467 4293 3432 423 84 -283 C ATOM 835 C LYS A 113 -11.287 16.956 23.571 1.00 31.33 C ANISOU 835 C LYS A 113 4349 4222 3332 366 53 -282 C ATOM 836 O LYS A 113 -11.191 16.631 22.371 1.00 31.87 O ANISOU 836 O LYS A 113 4457 4361 3290 468 159 -217 O ATOM 837 CB LYS A 113 -12.572 19.085 23.194 1.00 31.27 C ANISOU 837 CB LYS A 113 4362 4339 3180 429 -35 -193 C ATOM 838 CG LYS A 113 -13.837 19.888 23.518 1.00 34.51 C ANISOU 838 CG LYS A 113 4692 4510 3908 541 317 -404 C ATOM 839 CD LYS A 113 -15.072 19.096 23.137 1.00 38.83 C ANISOU 839 CD LYS A 113 4811 4855 5085 550 140 -145 C ATOM 840 CE LYS A 113 -16.258 19.997 22.757 1.00 40.94 C ANISOU 840 CE LYS A 113 5079 5034 5442 553 -89 -10 C ATOM 841 NZ LYS A 113 -17.374 19.183 22.140 1.00 43.54 N1+ ANISOU 841 NZ LYS A 113 5485 4871 6186 215 180 -66 N1+ ATOM 842 N ASN A 114 -10.423 16.540 24.488 1.00 30.70 N ANISOU 842 N ASN A 114 4334 4142 3187 357 63 -335 N ATOM 843 CA ASN A 114 -9.269 15.703 24.096 1.00 30.06 C ANISOU 843 CA ASN A 114 4342 3976 3101 301 150 -392 C ATOM 844 C ASN A 114 -9.722 14.349 23.533 1.00 30.64 C ANISOU 844 C ASN A 114 4339 4020 3280 245 197 -330 C ATOM 845 O ASN A 114 -10.822 13.872 23.847 1.00 30.59 O ANISOU 845 O ASN A 114 4199 4080 3340 371 256 -449 O ATOM 846 CB ASN A 114 -8.340 15.469 25.294 1.00 30.50 C ANISOU 846 CB ASN A 114 4433 3990 3164 280 138 -337 C ATOM 847 CG ASN A 114 -8.891 14.441 26.262 1.00 30.00 C ANISOU 847 CG ASN A 114 4628 3703 3065 225 177 -318 C ATOM 848 ND2 ASN A 114 -9.461 14.900 27.390 1.00 30.96 N ANISOU 848 ND2 ASN A 114 4807 3738 3217 410 202 -407 N ATOM 849 OD1 ASN A 114 -8.767 13.240 26.029 1.00 32.05 O ANISOU 849 OD1 ASN A 114 4987 3766 3422 269 189 -168 O ATOM 850 N ASP A 115 -8.871 13.753 22.689 1.00 30.44 N ANISOU 850 N ASP A 115 4365 4013 3184 290 282 -407 N ATOM 851 CA ASP A 115 -9.133 12.419 22.143 1.00 31.68 C ANISOU 851 CA ASP A 115 4564 4030 3439 206 328 -369 C ATOM 852 C ASP A 115 -8.256 11.344 22.786 1.00 32.02 C ANISOU 852 C ASP A 115 4636 3958 3572 208 340 -355 C ATOM 853 O ASP A 115 -7.982 10.287 22.197 1.00 33.23 O ANISOU 853 O ASP A 115 5001 3936 3690 149 312 -419 O ATOM 854 CB ASP A 115 -8.930 12.398 20.611 1.00 31.10 C ANISOU 854 CB ASP A 115 4301 4188 3324 272 446 -374 C ATOM 855 CG ASP A 115 -9.614 11.192 19.945 1.00 32.79 C ANISOU 855 CG ASP A 115 4681 4184 3592 312 492 -404 C ATOM 856 OD1 ASP A 115 -10.758 10.878 20.368 1.00 34.51 O ANISOU 856 OD1 ASP A 115 5120 4147 3845 1 456 -411 O ATOM 857 OD2 ASP A 115 -9.034 10.566 18.990 1.00 32.84 O1- ANISOU 857 OD2 ASP A 115 4833 4236 3406 443 657 -282 O1- ATOM 858 N LEU A 116 -7.754 11.632 23.971 1.00 31.78 N ANISOU 858 N LEU A 116 4571 3893 3608 227 214 -318 N ATOM 859 CA LEU A 116 -6.868 10.731 24.663 1.00 33.12 C ANISOU 859 CA LEU A 116 4850 3825 3909 199 204 -285 C ATOM 860 C LEU A 116 -7.576 9.789 25.612 1.00 35.03 C ANISOU 860 C LEU A 116 5207 3952 4149 194 130 -183 C ATOM 861 O LEU A 116 -7.196 8.630 25.669 1.00 36.16 O ANISOU 861 O LEU A 116 5432 3926 4381 322 126 -185 O ATOM 862 CB LEU A 116 -5.822 11.528 25.436 1.00 32.54 C ANISOU 862 CB LEU A 116 4669 3783 3909 256 52 -311 C ATOM 863 CG LEU A 116 -4.742 10.725 26.142 1.00 34.04 C ANISOU 863 CG LEU A 116 4953 3892 4088 300 -11 -367 C ATOM 864 CD1 LEU A 116 -4.099 9.729 25.160 1.00 31.45 C ANISOU 864 CD1 LEU A 116 4143 3475 4329 577 18 -110 C ATOM 865 CD2 LEU A 116 -3.723 11.701 26.703 1.00 36.53 C ANISOU 865 CD2 LEU A 116 5218 3753 4908 302 -205 -428 C ATOM 866 N SER A 117 -8.567 10.286 26.361 1.00 36.23 N ANISOU 866 N SER A 117 5364 4167 4233 115 241 -86 N ATOM 867 CA SER A 117 -9.220 9.467 27.400 1.00 38.60 C ANISOU 867 CA SER A 117 5656 4429 4581 23 328 -127 C ATOM 868 C SER A 117 -10.000 8.305 26.830 1.00 40.15 C ANISOU 868 C SER A 117 5805 4659 4790 -38 203 -97 C ATOM 869 O SER A 117 -9.888 7.172 27.338 1.00 41.64 O ANISOU 869 O SER A 117 6148 4805 4867 -103 127 -43 O ATOM 870 CB SER A 117 -10.117 10.322 28.292 1.00 39.13 C ANISOU 870 CB SER A 117 5674 4535 4658 23 285 -158 C ATOM 871 OG SER A 117 -9.282 11.160 29.029 1.00 39.34 O ANISOU 871 OG SER A 117 5648 4417 4882 -3 366 -234 O ATOM 872 N MET A 118 -10.790 8.586 25.796 1.00 40.57 N ANISOU 872 N MET A 118 5884 4805 4725 -90 263 -84 N ATOM 873 CA MET A 118 -11.587 7.576 25.113 1.00 42.68 C ANISOU 873 CA MET A 118 6056 5094 5064 -131 267 -99 C ATOM 874 C MET A 118 -11.401 7.798 23.604 1.00 39.52 C ANISOU 874 C MET A 118 5628 4784 4602 -175 329 -119 C ATOM 875 O MET A 118 -12.249 8.394 22.980 1.00 39.41 O ANISOU 875 O MET A 118 5659 4870 4445 -236 491 -180 O ATOM 876 CB MET A 118 -13.070 7.702 25.498 1.00 42.06 C ANISOU 876 CB MET A 118 5964 4977 5036 -144 267 -119 C ATOM 877 CG MET A 118 -13.323 7.648 27.009 1.00 45.86 C ANISOU 877 CG MET A 118 6386 5504 5533 -78 324 -106 C ATOM 878 SD MET A 118 -14.793 6.714 27.473 1.00 50.66 S ANISOU 878 SD MET A 118 6835 5889 6524 -176 320 7 S ATOM 879 CE MET A 118 -14.301 5.051 26.997 1.00 51.25 C ANISOU 879 CE MET A 118 6724 6037 6711 69 294 -146 C ATOM 880 N PRO A 119 -10.260 7.359 23.044 1.00 38.57 N ANISOU 880 N PRO A 119 5478 4733 4443 -176 387 -103 N ATOM 881 CA PRO A 119 -9.970 7.770 21.645 1.00 37.65 C ANISOU 881 CA PRO A 119 5280 4744 4282 -126 361 -155 C ATOM 882 C PRO A 119 -10.984 7.291 20.604 1.00 37.88 C ANISOU 882 C PRO A 119 5241 4816 4334 -104 414 -190 C ATOM 883 O PRO A 119 -11.324 6.100 20.572 1.00 38.62 O ANISOU 883 O PRO A 119 5473 4801 4400 -167 324 -215 O ATOM 884 CB PRO A 119 -8.571 7.184 21.368 1.00 37.85 C ANISOU 884 CB PRO A 119 5248 4772 4359 -112 338 -134 C ATOM 885 CG PRO A 119 -7.948 6.941 22.735 1.00 38.11 C ANISOU 885 CG PRO A 119 5357 4760 4363 -31 399 -187 C ATOM 886 CD PRO A 119 -9.151 6.587 23.633 1.00 38.08 C ANISOU 886 CD PRO A 119 5435 4622 4412 -224 359 -65 C ATOM 887 N ARG A 120 -11.452 8.227 19.780 1.00 35.75 N ANISOU 887 N ARG A 120 4815 4739 4026 -15 518 -243 N ATOM 888 CA ARG A 120 -12.324 7.942 18.646 1.00 35.74 C ANISOU 888 CA ARG A 120 4688 4795 4094 -23 538 -241 C ATOM 889 C ARG A 120 -11.514 7.909 17.338 1.00 34.21 C ANISOU 889 C ARG A 120 4539 4623 3833 -8 585 -292 C ATOM 890 O ARG A 120 -11.913 7.257 16.343 1.00 34.60 O ANISOU 890 O ARG A 120 4586 4726 3834 -41 630 -279 O ATOM 891 CB ARG A 120 -13.365 9.048 18.501 1.00 36.49 C ANISOU 891 CB ARG A 120 4780 4781 4302 -18 429 -257 C ATOM 892 CG ARG A 120 -14.577 8.990 19.373 1.00 40.67 C ANISOU 892 CG ARG A 120 5162 5255 5036 1 311 1 C ATOM 893 CD ARG A 120 -15.590 10.044 18.852 1.00 45.19 C ANISOU 893 CD ARG A 120 5547 5497 6126 124 116 7 C ATOM 894 NE ARG A 120 -15.051 11.416 18.850 1.00 44.13 N ANISOU 894 NE ARG A 120 5281 5460 6024 43 115 -54 N ATOM 895 CZ ARG A 120 -15.751 12.496 18.510 1.00 42.38 C ANISOU 895 CZ ARG A 120 5120 5358 5622 20 186 -177 C ATOM 896 NH1 ARG A 120 -17.015 12.375 18.115 1.00 42.23 N1+ ANISOU 896 NH1 ARG A 120 4910 5475 5661 -62 364 -275 N1+ ATOM 897 NH2 ARG A 120 -15.189 13.700 18.552 1.00 41.28 N ANISOU 897 NH2 ARG A 120 4786 5344 5555 9 358 -53 N ATOM 898 N GLY A 121 -10.395 8.613 17.329 1.00 32.76 N ANISOU 898 N GLY A 121 4272 4523 3650 207 620 -401 N ATOM 899 CA GLY A 121 -9.544 8.675 16.100 1.00 31.91 C ANISOU 899 CA GLY A 121 4034 4512 3577 274 602 -374 C ATOM 900 C GLY A 121 -10.232 9.415 14.971 1.00 32.72 C ANISOU 900 C GLY A 121 4215 4467 3749 243 479 -444 C ATOM 901 O GLY A 121 -10.121 9.049 13.772 1.00 32.55 O ANISOU 901 O GLY A 121 4065 4510 3792 255 541 -677 O ATOM 902 N THR A 122 -10.960 10.466 15.337 1.00 32.57 N ANISOU 902 N THR A 122 4045 4404 3923 327 335 -427 N ATOM 903 CA THR A 122 -11.639 11.315 14.343 1.00 33.25 C ANISOU 903 CA THR A 122 4146 4418 4067 338 289 -409 C ATOM 904 C THR A 122 -11.368 12.805 14.568 1.00 32.44 C ANISOU 904 C THR A 122 4031 4354 3940 379 222 -394 C ATOM 905 O THR A 122 -10.708 13.205 15.521 1.00 32.57 O ANISOU 905 O THR A 122 3962 4467 3943 514 41 -376 O ATOM 906 CB THR A 122 -13.167 11.061 14.359 1.00 33.41 C ANISOU 906 CB THR A 122 4195 4412 4085 273 156 -426 C ATOM 907 CG2 THR A 122 -13.486 9.570 14.104 1.00 35.51 C ANISOU 907 CG2 THR A 122 4408 4511 4574 170 181 -293 C ATOM 908 OG1 THR A 122 -13.685 11.416 15.638 1.00 35.06 O ANISOU 908 OG1 THR A 122 4142 4723 4454 415 523 -403 O ATOM 909 N MET A 123 -11.892 13.627 13.673 1.00 32.01 N ANISOU 909 N MET A 123 4127 4229 3804 384 276 -333 N ATOM 910 CA MET A 123 -12.096 15.054 13.910 1.00 32.88 C ANISOU 910 CA MET A 123 4222 4351 3918 381 387 -309 C ATOM 911 C MET A 123 -13.136 15.239 15.007 1.00 32.81 C ANISOU 911 C MET A 123 4209 4335 3919 349 359 -250 C ATOM 912 O MET A 123 -13.790 14.280 15.410 1.00 32.89 O ANISOU 912 O MET A 123 4265 4255 3973 414 393 -375 O ATOM 913 CB MET A 123 -12.633 15.680 12.627 1.00 32.69 C ANISOU 913 CB MET A 123 4189 4316 3916 441 456 -240 C ATOM 914 CG MET A 123 -11.665 15.512 11.432 1.00 33.97 C ANISOU 914 CG MET A 123 4547 4420 3938 337 699 -340 C ATOM 915 SD MET A 123 -10.099 16.427 11.580 1.00 35.19 S ANISOU 915 SD MET A 123 4569 4509 4290 542 373 -112 S ATOM 916 CE MET A 123 -10.655 18.152 11.624 1.00 37.22 C ANISOU 916 CE MET A 123 4927 4635 4578 388 475 -264 C ATOM 917 N GLN A 124 -13.309 16.476 15.464 1.00 33.25 N ANISOU 917 N GLN A 124 4278 4365 3991 320 306 -216 N ATOM 918 CA GLN A 124 -14.297 16.758 16.516 1.00 33.27 C ANISOU 918 CA GLN A 124 4224 4293 4122 331 348 -191 C ATOM 919 C GLN A 124 -15.707 16.340 16.083 1.00 34.72 C ANISOU 919 C GLN A 124 4325 4547 4320 316 318 -191 C ATOM 920 O GLN A 124 -16.540 15.988 16.925 1.00 36.48 O ANISOU 920 O GLN A 124 4654 4791 4414 227 305 -60 O ATOM 921 CB GLN A 124 -14.251 18.226 16.990 1.00 33.54 C ANISOU 921 CB GLN A 124 4183 4382 4178 279 303 -255 C ATOM 922 CG GLN A 124 -13.047 18.584 17.879 1.00 32.37 C ANISOU 922 CG GLN A 124 4285 4181 3831 353 297 -136 C ATOM 923 CD GLN A 124 -13.059 17.897 19.221 1.00 33.25 C ANISOU 923 CD GLN A 124 4410 4264 3957 328 244 -220 C ATOM 924 NE2 GLN A 124 -11.872 17.615 19.744 1.00 30.03 N ANISOU 924 NE2 GLN A 124 4479 3726 3203 268 168 -513 N ATOM 925 OE1 GLN A 124 -14.123 17.633 19.792 1.00 34.62 O ANISOU 925 OE1 GLN A 124 4433 4524 4195 161 362 132 O ATOM 926 N ASP A 125 -15.969 16.358 14.782 1.00 34.90 N ANISOU 926 N ASP A 125 4301 4608 4350 357 299 -237 N ATOM 927 CA ASP A 125 -17.317 16.077 14.273 1.00 36.25 C ANISOU 927 CA ASP A 125 4440 4820 4512 254 288 -273 C ATOM 928 C ASP A 125 -17.622 14.587 14.087 1.00 36.75 C ANISOU 928 C ASP A 125 4426 4893 4643 211 258 -254 C ATOM 929 O ASP A 125 -18.691 14.227 13.580 1.00 38.52 O ANISOU 929 O ASP A 125 4617 5162 4855 205 245 -355 O ATOM 930 CB ASP A 125 -17.600 16.879 12.985 1.00 36.52 C ANISOU 930 CB ASP A 125 4537 4827 4509 283 334 -234 C ATOM 931 CG ASP A 125 -16.889 16.320 11.763 1.00 38.25 C ANISOU 931 CG ASP A 125 4764 5116 4652 231 284 -247 C ATOM 932 OD1 ASP A 125 -16.097 15.374 11.921 1.00 38.54 O ANISOU 932 OD1 ASP A 125 4988 5233 4420 279 100 -148 O ATOM 933 OD2 ASP A 125 -17.155 16.812 10.636 1.00 40.46 O1- ANISOU 933 OD2 ASP A 125 5166 5333 4873 380 121 -331 O1- ATOM 934 N GLY A 126 -16.672 13.731 14.453 1.00 35.41 N ANISOU 934 N GLY A 126 4304 4706 4442 254 268 -276 N ATOM 935 CA GLY A 126 -16.861 12.277 14.422 1.00 34.94 C ANISOU 935 CA GLY A 126 4280 4657 4335 234 248 -327 C ATOM 936 C GLY A 126 -16.550 11.650 13.083 1.00 34.96 C ANISOU 936 C GLY A 126 4369 4569 4344 237 172 -378 C ATOM 937 O GLY A 126 -16.844 10.465 12.850 1.00 35.04 O ANISOU 937 O GLY A 126 4316 4566 4430 256 255 -503 O ATOM 938 N THR A 127 -15.951 12.434 12.197 1.00 34.19 N ANISOU 938 N THR A 127 4305 4592 4092 293 204 -479 N ATOM 939 CA THR A 127 -15.501 11.880 10.908 1.00 34.38 C ANISOU 939 CA THR A 127 4459 4600 4000 217 136 -484 C ATOM 940 C THR A 127 -14.022 12.059 10.633 1.00 33.71 C ANISOU 940 C THR A 127 4429 4528 3851 172 152 -509 C ATOM 941 O THR A 127 -13.317 12.726 11.391 1.00 34.37 O ANISOU 941 O THR A 127 4495 4724 3837 102 247 -588 O ATOM 942 CB THR A 127 -16.332 12.424 9.740 1.00 34.17 C ANISOU 942 CB THR A 127 4450 4435 4099 273 153 -357 C ATOM 943 CG2 THR A 127 -17.810 12.166 9.997 1.00 36.64 C ANISOU 943 CG2 THR A 127 4610 4815 4495 283 6 -304 C ATOM 944 OG1 THR A 127 -16.023 13.823 9.534 1.00 36.25 O ANISOU 944 OG1 THR A 127 4745 4524 4502 143 50 -504 O ATOM 945 N SER A 128 -13.554 11.442 9.535 1.00 33.62 N ANISOU 945 N SER A 128 4352 4525 3896 225 206 -471 N ATOM 946 CA SER A 128 -12.162 11.451 9.161 1.00 32.64 C ANISOU 946 CA SER A 128 4262 4404 3732 182 85 -364 C ATOM 947 C SER A 128 -11.955 12.243 7.868 1.00 31.65 C ANISOU 947 C SER A 128 4147 4294 3584 163 -56 -290 C ATOM 948 O SER A 128 -12.824 12.207 6.940 1.00 32.27 O ANISOU 948 O SER A 128 4155 4426 3678 119 -246 -324 O ATOM 949 CB SER A 128 -11.683 10.018 8.946 1.00 33.06 C ANISOU 949 CB SER A 128 4294 4428 3838 227 135 -182 C ATOM 950 OG SER A 128 -10.393 10.028 8.334 1.00 33.80 O ANISOU 950 OG SER A 128 4370 4295 4176 529 285 -98 O ATOM 951 N ARG A 129 -10.813 12.938 7.782 1.00 30.13 N ANISOU 951 N ARG A 129 4097 4038 3310 224 -33 -400 N ATOM 952 CA ARG A 129 -10.444 13.692 6.576 1.00 29.43 C ANISOU 952 CA ARG A 129 3990 3830 3362 191 59 -413 C ATOM 953 C ARG A 129 -9.489 12.895 5.682 1.00 29.34 C ANISOU 953 C ARG A 129 3986 3795 3364 302 56 -384 C ATOM 954 O ARG A 129 -9.045 13.399 4.640 1.00 29.79 O ANISOU 954 O ARG A 129 4177 3729 3410 359 130 -368 O ATOM 955 CB ARG A 129 -9.795 15.036 6.948 1.00 28.46 C ANISOU 955 CB ARG A 129 3941 3609 3263 336 122 -418 C ATOM 956 CG ARG A 129 -10.759 15.951 7.692 1.00 28.34 C ANISOU 956 CG ARG A 129 3712 3759 3295 467 179 -271 C ATOM 957 CD ARG A 129 -11.851 16.568 6.807 1.00 29.52 C ANISOU 957 CD ARG A 129 3463 4132 3618 331 51 -333 C ATOM 958 NE ARG A 129 -12.824 17.151 7.742 1.00 31.74 N ANISOU 958 NE ARG A 129 3917 4097 4044 696 283 -311 N ATOM 959 CZ ARG A 129 -13.845 16.493 8.287 1.00 31.41 C ANISOU 959 CZ ARG A 129 3446 4085 4400 549 -97 -286 C ATOM 960 NH1 ARG A 129 -14.123 15.236 7.936 1.00 35.13 N1+ ANISOU 960 NH1 ARG A 129 4450 4295 4603 586 325 -422 N1+ ATOM 961 NH2 ARG A 129 -14.613 17.106 9.189 1.00 33.13 N ANISOU 961 NH2 ARG A 129 4045 4333 4208 111 315 -360 N ATOM 962 N PHE A 130 -9.136 11.681 6.106 1.00 29.95 N ANISOU 962 N PHE A 130 4103 3800 3475 98 87 -469 N ATOM 963 CA PHE A 130 -8.161 10.861 5.368 1.00 30.25 C ANISOU 963 CA PHE A 130 4138 3929 3424 69 12 -424 C ATOM 964 C PHE A 130 -8.750 9.636 4.701 1.00 30.87 C ANISOU 964 C PHE A 130 4248 3973 3506 24 5 -453 C ATOM 965 O PHE A 130 -9.473 8.856 5.328 1.00 30.86 O ANISOU 965 O PHE A 130 4309 3864 3553 -165 29 -574 O ATOM 966 CB PHE A 130 -7.110 10.309 6.335 1.00 29.66 C ANISOU 966 CB PHE A 130 4038 3883 3349 64 -72 -422 C ATOM 967 CG PHE A 130 -6.279 11.351 7.002 1.00 29.51 C ANISOU 967 CG PHE A 130 4140 3897 3175 -137 7 -293 C ATOM 968 CD1 PHE A 130 -5.437 12.205 6.262 1.00 31.68 C ANISOU 968 CD1 PHE A 130 4570 3823 3641 -259 -286 -135 C ATOM 969 CD2 PHE A 130 -6.302 11.459 8.403 1.00 28.62 C ANISOU 969 CD2 PHE A 130 4248 3709 2916 -57 -22 -118 C ATOM 970 CE1 PHE A 130 -4.642 13.154 6.926 1.00 33.20 C ANISOU 970 CE1 PHE A 130 4537 4228 3849 -306 -95 -347 C ATOM 971 CE2 PHE A 130 -5.496 12.389 9.065 1.00 28.62 C ANISOU 971 CE2 PHE A 130 4187 3294 3391 181 259 -574 C ATOM 972 CZ PHE A 130 -4.664 13.241 8.320 1.00 28.34 C ANISOU 972 CZ PHE A 130 4012 3511 3245 19 18 -286 C ATOM 973 N THR A 131 -8.357 9.404 3.457 1.00 31.50 N ANISOU 973 N THR A 131 4306 4061 3599 89 131 -535 N ATOM 974 CA THR A 131 -8.695 8.141 2.799 1.00 33.29 C ANISOU 974 CA THR A 131 4458 4228 3961 15 140 -502 C ATOM 975 C THR A 131 -7.462 7.619 2.086 1.00 32.85 C ANISOU 975 C THR A 131 4432 4126 3920 124 139 -639 C ATOM 976 O THR A 131 -6.607 8.402 1.672 1.00 32.24 O ANISOU 976 O THR A 131 4427 4020 3803 241 189 -725 O ATOM 977 CB THR A 131 -9.857 8.289 1.784 1.00 33.35 C ANISOU 977 CB THR A 131 4466 4153 4052 -9 61 -451 C ATOM 978 CG2 THR A 131 -11.178 8.506 2.513 1.00 35.11 C ANISOU 978 CG2 THR A 131 4529 4445 4365 26 44 -505 C ATOM 979 OG1 THR A 131 -9.607 9.384 0.885 1.00 37.14 O ANISOU 979 OG1 THR A 131 5066 4586 4456 -137 68 -414 O ATOM 980 N CYS A 132 -7.351 6.298 1.993 1.00 34.37 N ANISOU 980 N CYS A 132 4542 4209 4305 89 260 -737 N ATOM 981 CA CYS A 132 -6.268 5.688 1.200 1.00 34.96 C ANISOU 981 CA CYS A 132 4645 4227 4408 -33 180 -843 C ATOM 982 C CYS A 132 -6.968 4.704 0.290 1.00 36.81 C ANISOU 982 C CYS A 132 4923 4431 4629 -147 102 -753 C ATOM 983 O CYS A 132 -7.542 3.735 0.781 1.00 37.60 O ANISOU 983 O CYS A 132 5177 4412 4696 -245 0 -876 O ATOM 984 CB CYS A 132 -5.287 4.965 2.112 1.00 34.76 C ANISOU 984 CB CYS A 132 4593 4169 4443 42 299 -835 C ATOM 985 SG CYS A 132 -3.941 4.168 1.225 1.00 38.34 S ANISOU 985 SG CYS A 132 4825 4531 5210 167 596 -820 S ATOM 986 N ARG A 133 -6.952 4.994 -1.008 1.00 38.10 N ANISOU 986 N ARG A 133 5085 4646 4745 -195 -12 -745 N ATOM 987 CA ARG A 133 -7.703 4.184 -1.990 1.00 40.19 C ANISOU 987 CA ARG A 133 5267 5032 4969 -187 -58 -579 C ATOM 988 C ARG A 133 -9.160 3.968 -1.570 1.00 41.65 C ANISOU 988 C ARG A 133 5418 5217 5189 -198 -74 -461 C ATOM 989 O ARG A 133 -9.726 2.851 -1.692 1.00 43.59 O ANISOU 989 O ARG A 133 5659 5403 5497 -239 -86 -398 O ATOM 990 CB ARG A 133 -6.951 2.885 -2.242 1.00 40.61 C ANISOU 990 CB ARG A 133 5287 5017 5124 -203 -91 -523 C ATOM 991 CG ARG A 133 -5.592 3.162 -2.859 1.00 43.32 C ANISOU 991 CG ARG A 133 5631 5392 5436 -93 60 -395 C ATOM 992 CD ARG A 133 -4.716 1.939 -2.955 1.00 45.91 C ANISOU 992 CD ARG A 133 5858 5642 5943 150 170 -296 C ATOM 993 NE ARG A 133 -3.569 2.232 -3.800 1.00 48.48 N ANISOU 993 NE ARG A 133 6238 6056 6126 121 208 -247 N ATOM 994 CZ ARG A 133 -2.424 2.729 -3.367 1.00 48.57 C ANISOU 994 CZ ARG A 133 6289 6117 6047 73 67 -352 C ATOM 995 NH1 ARG A 133 -2.253 2.981 -2.068 1.00 51.32 N1+ ANISOU 995 NH1 ARG A 133 6600 6562 6335 240 185 -384 N1+ ATOM 996 NH2 ARG A 133 -1.445 2.970 -4.224 1.00 48.25 N ANISOU 996 NH2 ARG A 133 6500 6062 5769 66 108 -519 N ATOM 997 N GLY A 134 -9.765 5.064 -1.106 1.00 41.65 N ANISOU 997 N GLY A 134 5322 5392 5112 -115 6 -432 N ATOM 998 CA GLY A 134 -11.175 5.097 -0.671 1.00 42.24 C ANISOU 998 CA GLY A 134 5385 5456 5206 -107 91 -291 C ATOM 999 C GLY A 134 -11.486 4.443 0.673 1.00 42.07 C ANISOU 999 C GLY A 134 5371 5434 5179 -93 100 -320 C ATOM 1000 O GLY A 134 -12.657 4.361 1.064 1.00 43.97 O ANISOU 1000 O GLY A 134 5484 5720 5499 -82 191 -219 O ATOM 1001 N LYS A 135 -10.466 3.943 1.371 1.00 40.86 N ANISOU 1001 N LYS A 135 5325 5243 4955 -175 98 -373 N ATOM 1002 CA LYS A 135 -10.671 3.334 2.684 1.00 39.14 C ANISOU 1002 CA LYS A 135 5272 4934 4662 -171 -3 -534 C ATOM 1003 C LYS A 135 -10.426 4.437 3.716 1.00 37.40 C ANISOU 1003 C LYS A 135 4954 4770 4486 -170 21 -555 C ATOM 1004 O LYS A 135 -9.428 5.104 3.631 1.00 36.20 O ANISOU 1004 O LYS A 135 5164 4385 4205 -302 210 -628 O ATOM 1005 CB LYS A 135 -9.706 2.154 2.871 1.00 40.44 C ANISOU 1005 CB LYS A 135 5341 5074 4947 -161 -10 -418 C ATOM 1006 CG LYS A 135 -9.816 1.451 4.205 1.00 42.81 C ANISOU 1006 CG LYS A 135 5886 5250 5128 -131 -87 -410 C ATOM 1007 CD LYS A 135 -9.538 -0.052 4.058 1.00 47.76 C ANISOU 1007 CD LYS A 135 6460 5597 6089 196 168 -167 C ATOM 1008 CE LYS A 135 -10.697 -0.861 4.637 1.00 50.02 C ANISOU 1008 CE LYS A 135 6627 6025 6351 31 91 -61 C ATOM 1009 NZ LYS A 135 -10.664 -2.294 4.248 1.00 51.09 N1+ ANISOU 1009 NZ LYS A 135 6849 6197 6365 59 169 -282 N1+ ATOM 1010 N PRO A 136 -11.355 4.641 4.662 1.00 36.09 N ANISOU 1010 N PRO A 136 4801 4634 4276 -188 -16 -552 N ATOM 1011 CA PRO A 136 -11.099 5.694 5.661 1.00 35.27 C ANISOU 1011 CA PRO A 136 4631 4605 4164 -48 57 -563 C ATOM 1012 C PRO A 136 -9.908 5.341 6.553 1.00 33.83 C ANISOU 1012 C PRO A 136 4493 4378 3981 -38 36 -572 C ATOM 1013 O PRO A 136 -9.707 4.162 6.897 1.00 35.17 O ANISOU 1013 O PRO A 136 4701 4577 4085 -87 5 -628 O ATOM 1014 CB PRO A 136 -12.395 5.724 6.494 1.00 35.62 C ANISOU 1014 CB PRO A 136 4626 4663 4245 -3 35 -480 C ATOM 1015 CG PRO A 136 -13.396 4.986 5.680 1.00 37.39 C ANISOU 1015 CG PRO A 136 4831 4825 4551 -53 9 -514 C ATOM 1016 CD PRO A 136 -12.654 3.982 4.867 1.00 37.00 C ANISOU 1016 CD PRO A 136 4811 4818 4427 -93 21 -474 C ATOM 1017 N ILE A 137 -9.149 6.362 6.957 1.00 32.04 N ANISOU 1017 N ILE A 137 4224 4345 3604 -8 110 -565 N ATOM 1018 CA ILE A 137 -8.010 6.188 7.882 1.00 30.30 C ANISOU 1018 CA ILE A 137 4192 4019 3301 85 108 -626 C ATOM 1019 C ILE A 137 -8.260 7.117 9.078 1.00 29.17 C ANISOU 1019 C ILE A 137 4046 3772 3265 240 133 -615 C ATOM 1020 O ILE A 137 -8.667 8.262 8.898 1.00 30.81 O ANISOU 1020 O ILE A 137 4332 3961 3411 172 -56 -648 O ATOM 1021 CB ILE A 137 -6.655 6.561 7.216 1.00 30.46 C ANISOU 1021 CB ILE A 137 4150 4090 3333 105 106 -674 C ATOM 1022 CG1 ILE A 137 -6.473 5.822 5.859 1.00 32.29 C ANISOU 1022 CG1 ILE A 137 4675 4268 3325 -20 58 -688 C ATOM 1023 CG2 ILE A 137 -5.463 6.249 8.150 1.00 31.70 C ANISOU 1023 CG2 ILE A 137 4270 4242 3532 -48 -2 -607 C ATOM 1024 CD1 ILE A 137 -6.300 4.332 5.983 1.00 34.66 C ANISOU 1024 CD1 ILE A 137 4845 4556 3767 141 265 -756 C ATOM 1025 N HIS A 138 -8.002 6.612 10.282 1.00 28.65 N ANISOU 1025 N HIS A 138 3944 3639 3301 356 86 -714 N ATOM 1026 CA HIS A 138 -8.184 7.365 11.515 1.00 28.69 C ANISOU 1026 CA HIS A 138 3902 3585 3413 188 40 -625 C ATOM 1027 C HIS A 138 -7.154 8.459 11.737 1.00 27.94 C ANISOU 1027 C HIS A 138 3810 3522 3283 203 26 -544 C ATOM 1028 O HIS A 138 -5.996 8.381 11.274 1.00 27.46 O ANISOU 1028 O HIS A 138 3831 3268 3334 257 48 -608 O ATOM 1029 CB HIS A 138 -8.210 6.429 12.720 1.00 29.58 C ANISOU 1029 CB HIS A 138 3915 3701 3621 78 111 -617 C ATOM 1030 CG HIS A 138 -9.444 5.598 12.782 1.00 31.71 C ANISOU 1030 CG HIS A 138 4064 3897 4088 -145 209 -463 C ATOM 1031 CD2 HIS A 138 -10.690 5.912 13.214 1.00 31.53 C ANISOU 1031 CD2 HIS A 138 3835 3948 4197 -362 325 -494 C ATOM 1032 ND1 HIS A 138 -9.510 4.304 12.302 1.00 33.78 N ANISOU 1032 ND1 HIS A 138 4306 4297 4231 -252 -13 -382 N ATOM 1033 CE1 HIS A 138 -10.737 3.846 12.481 1.00 34.78 C ANISOU 1033 CE1 HIS A 138 4361 4297 4557 -294 299 -442 C ATOM 1034 NE2 HIS A 138 -11.476 4.809 13.000 1.00 36.51 N ANISOU 1034 NE2 HIS A 138 4727 4101 5043 -495 266 -328 N ATOM 1035 N HIS A 139 -7.627 9.477 12.449 1.00 26.95 N ANISOU 1035 N HIS A 139 3761 3390 3086 236 2 -580 N ATOM 1036 CA HIS A 139 -6.771 10.520 13.015 1.00 26.83 C ANISOU 1036 CA HIS A 139 3684 3436 3073 206 77 -459 C ATOM 1037 C HIS A 139 -6.176 9.993 14.331 1.00 27.63 C ANISOU 1037 C HIS A 139 3791 3537 3168 177 90 -341 C ATOM 1038 O HIS A 139 -6.639 8.975 14.908 1.00 28.42 O ANISOU 1038 O HIS A 139 3882 3828 3087 -14 89 -293 O ATOM 1039 CB HIS A 139 -7.613 11.801 13.258 1.00 26.78 C ANISOU 1039 CB HIS A 139 3777 3274 3121 214 -66 -480 C ATOM 1040 CG HIS A 139 -8.113 12.448 11.997 1.00 27.23 C ANISOU 1040 CG HIS A 139 3576 3405 3364 386 23 -432 C ATOM 1041 CD2 HIS A 139 -9.034 12.048 11.081 1.00 29.61 C ANISOU 1041 CD2 HIS A 139 4190 3540 3520 296 -52 -491 C ATOM 1042 ND1 HIS A 139 -7.621 13.651 11.538 1.00 30.06 N ANISOU 1042 ND1 HIS A 139 4173 3627 3622 243 -69 -177 N ATOM 1043 CE1 HIS A 139 -8.211 13.966 10.396 1.00 29.16 C ANISOU 1043 CE1 HIS A 139 3699 3847 3532 352 54 -635 C ATOM 1044 NE2 HIS A 139 -9.073 13.011 10.096 1.00 29.44 N ANISOU 1044 NE2 HIS A 139 3752 4102 3329 236 31 -458 N ATOM 1045 N PHE A 140 -5.209 10.727 14.858 1.00 26.75 N ANISOU 1045 N PHE A 140 3617 3633 2911 141 193 -260 N ATOM 1046 CA PHE A 140 -4.574 10.394 16.151 1.00 27.28 C ANISOU 1046 CA PHE A 140 3820 3527 3016 238 237 -324 C ATOM 1047 C PHE A 140 -4.449 11.650 16.980 1.00 27.31 C ANISOU 1047 C PHE A 140 3906 3473 2997 222 269 -298 C ATOM 1048 O PHE A 140 -3.735 12.599 16.614 1.00 26.99 O ANISOU 1048 O PHE A 140 4078 3462 2713 236 420 -455 O ATOM 1049 CB PHE A 140 -3.192 9.768 15.924 1.00 27.70 C ANISOU 1049 CB PHE A 140 3789 3627 3106 229 138 -300 C ATOM 1050 CG PHE A 140 -2.445 9.448 17.198 1.00 25.78 C ANISOU 1050 CG PHE A 140 3731 3090 2972 311 91 -330 C ATOM 1051 CD1 PHE A 140 -2.981 8.587 18.159 1.00 28.02 C ANISOU 1051 CD1 PHE A 140 4039 3415 3192 478 245 -465 C ATOM 1052 CD2 PHE A 140 -1.228 10.059 17.444 1.00 25.33 C ANISOU 1052 CD2 PHE A 140 3675 3151 2795 150 208 -399 C ATOM 1053 CE1 PHE A 140 -2.270 8.299 19.336 1.00 27.94 C ANISOU 1053 CE1 PHE A 140 4019 3505 3092 236 327 -352 C ATOM 1054 CE2 PHE A 140 -0.501 9.779 18.624 1.00 28.55 C ANISOU 1054 CE2 PHE A 140 4028 3718 3102 134 109 -15 C ATOM 1055 CZ PHE A 140 -1.031 8.889 19.563 1.00 29.52 C ANISOU 1055 CZ PHE A 140 4280 3632 3302 123 67 -156 C ATOM 1056 N LEU A 141 -5.132 11.638 18.123 1.00 27.27 N ANISOU 1056 N LEU A 141 3891 3353 3115 310 360 -355 N ATOM 1057 CA LEU A 141 -5.118 12.777 19.072 1.00 27.38 C ANISOU 1057 CA LEU A 141 3870 3395 3138 233 265 -318 C ATOM 1058 C LEU A 141 -5.449 14.114 18.397 1.00 27.93 C ANISOU 1058 C LEU A 141 3839 3465 3308 241 257 -249 C ATOM 1059 O LEU A 141 -4.962 15.176 18.814 1.00 27.77 O ANISOU 1059 O LEU A 141 3874 3303 3373 279 46 -233 O ATOM 1060 CB LEU A 141 -3.770 12.883 19.813 1.00 26.94 C ANISOU 1060 CB LEU A 141 3911 3270 3053 389 229 -319 C ATOM 1061 CG LEU A 141 -3.259 11.645 20.540 1.00 29.22 C ANISOU 1061 CG LEU A 141 4228 3473 3400 308 132 -160 C ATOM 1062 CD1 LEU A 141 -1.962 11.973 21.274 1.00 30.77 C ANISOU 1062 CD1 LEU A 141 4446 3362 3882 335 -95 50 C ATOM 1063 CD2 LEU A 141 -4.356 11.042 21.430 1.00 32.89 C ANISOU 1063 CD2 LEU A 141 4366 3825 4305 143 158 141 C ATOM 1064 N GLY A 142 -6.280 14.072 17.358 1.00 28.14 N ANISOU 1064 N GLY A 142 3859 3503 3329 230 262 -283 N ATOM 1065 CA GLY A 142 -6.683 15.273 16.666 1.00 30.50 C ANISOU 1065 CA GLY A 142 4267 3694 3624 229 322 -147 C ATOM 1066 C GLY A 142 -5.529 15.996 15.991 1.00 30.61 C ANISOU 1066 C GLY A 142 4272 3688 3669 284 331 -109 C ATOM 1067 O GLY A 142 -5.628 17.192 15.710 1.00 32.39 O ANISOU 1067 O GLY A 142 4464 3808 4035 566 366 8 O ATOM 1068 N THR A 143 -4.418 15.299 15.765 1.00 28.15 N ANISOU 1068 N THR A 143 4164 3349 3181 405 268 -220 N ATOM 1069 CA THR A 143 -3.246 15.909 15.114 1.00 27.64 C ANISOU 1069 CA THR A 143 4104 3407 2991 310 272 -305 C ATOM 1070 C THR A 143 -2.813 15.207 13.815 1.00 28.48 C ANISOU 1070 C THR A 143 4234 3466 3119 286 345 -190 C ATOM 1071 O THR A 143 -2.887 15.800 12.747 1.00 30.44 O ANISOU 1071 O THR A 143 4732 3584 3249 420 265 -252 O ATOM 1072 CB THR A 143 -2.036 16.089 16.077 1.00 28.22 C ANISOU 1072 CB THR A 143 4108 3473 3140 366 256 -397 C ATOM 1073 CG2 THR A 143 -2.396 17.066 17.218 1.00 28.60 C ANISOU 1073 CG2 THR A 143 4127 3854 2883 456 514 -548 C ATOM 1074 OG1 THR A 143 -1.636 14.822 16.630 1.00 29.56 O ANISOU 1074 OG1 THR A 143 4334 3752 3143 245 270 -267 O ATOM 1075 N SER A 144 -2.348 13.971 13.913 1.00 27.37 N ANISOU 1075 N SER A 144 4071 3353 2972 206 328 -89 N ATOM 1076 CA SER A 144 -1.956 13.166 12.743 1.00 26.22 C ANISOU 1076 CA SER A 144 3836 3426 2699 24 228 -58 C ATOM 1077 C SER A 144 -0.899 13.873 11.920 1.00 26.46 C ANISOU 1077 C SER A 144 3911 3398 2744 33 191 -60 C ATOM 1078 O SER A 144 -1.142 14.323 10.794 1.00 28.83 O ANISOU 1078 O SER A 144 4094 3596 3262 172 129 342 O ATOM 1079 CB SER A 144 -3.181 12.857 11.872 1.00 26.40 C ANISOU 1079 CB SER A 144 3902 3454 2672 58 210 -52 C ATOM 1080 OG SER A 144 -3.960 11.866 12.507 1.00 27.55 O ANISOU 1080 OG SER A 144 3467 3954 3044 -118 77 136 O ATOM 1081 N THR A 145 0.298 13.912 12.445 1.00 25.59 N ANISOU 1081 N THR A 145 3768 3257 2696 42 228 -151 N ATOM 1082 CA THR A 145 1.346 14.693 11.844 1.00 25.35 C ANISOU 1082 CA THR A 145 3784 3118 2730 -46 226 -249 C ATOM 1083 C THR A 145 2.301 13.889 10.957 1.00 25.69 C ANISOU 1083 C THR A 145 3844 3146 2769 65 189 -251 C ATOM 1084 O THR A 145 3.192 14.493 10.345 1.00 26.46 O ANISOU 1084 O THR A 145 4064 3148 2840 45 372 -145 O ATOM 1085 CB THR A 145 2.174 15.442 12.902 1.00 26.00 C ANISOU 1085 CB THR A 145 3739 3194 2944 -10 93 -221 C ATOM 1086 CG2 THR A 145 1.300 16.249 13.797 1.00 27.64 C ANISOU 1086 CG2 THR A 145 3997 3203 3301 -88 189 -471 C ATOM 1087 OG1 THR A 145 2.934 14.526 13.680 1.00 26.55 O ANISOU 1087 OG1 THR A 145 3746 3323 3019 -151 29 -33 O ATOM 1088 N PHE A 146 2.109 12.572 10.848 1.00 26.28 N ANISOU 1088 N PHE A 146 4071 3212 2700 128 177 -256 N ATOM 1089 CA PHE A 146 2.973 11.719 9.964 1.00 26.28 C ANISOU 1089 CA PHE A 146 4026 3325 2631 185 134 -205 C ATOM 1090 C PHE A 146 2.382 11.687 8.550 1.00 27.30 C ANISOU 1090 C PHE A 146 4117 3399 2857 120 89 -284 C ATOM 1091 O PHE A 146 2.110 10.611 7.970 1.00 28.35 O ANISOU 1091 O PHE A 146 4225 3547 2997 61 -113 -292 O ATOM 1092 CB PHE A 146 3.074 10.275 10.508 1.00 26.50 C ANISOU 1092 CB PHE A 146 4108 3313 2647 207 136 -334 C ATOM 1093 CG PHE A 146 3.889 10.126 11.774 1.00 25.74 C ANISOU 1093 CG PHE A 146 3797 3247 2736 308 225 -232 C ATOM 1094 CD1 PHE A 146 4.725 11.145 12.252 1.00 26.91 C ANISOU 1094 CD1 PHE A 146 3829 3467 2927 322 47 -336 C ATOM 1095 CD2 PHE A 146 3.828 8.911 12.489 1.00 25.53 C ANISOU 1095 CD2 PHE A 146 3882 3341 2476 265 503 -164 C ATOM 1096 CE1 PHE A 146 5.510 10.951 13.451 1.00 25.82 C ANISOU 1096 CE1 PHE A 146 3415 3285 3110 72 36 -138 C ATOM 1097 CE2 PHE A 146 4.575 8.714 13.639 1.00 24.46 C ANISOU 1097 CE2 PHE A 146 3598 2900 2793 445 151 -288 C ATOM 1098 CZ PHE A 146 5.428 9.742 14.142 1.00 27.02 C ANISOU 1098 CZ PHE A 146 3837 3357 3069 214 148 -218 C ATOM 1099 N SER A 147 2.190 12.880 8.007 1.00 27.40 N ANISOU 1099 N SER A 147 4176 3489 2744 172 67 -150 N ATOM 1100 CA SER A 147 1.604 13.074 6.687 1.00 28.15 C ANISOU 1100 CA SER A 147 4315 3574 2806 62 117 -194 C ATOM 1101 C SER A 147 2.086 14.396 6.136 1.00 28.09 C ANISOU 1101 C SER A 147 4301 3670 2701 65 160 -133 C ATOM 1102 O SER A 147 2.295 15.356 6.870 1.00 29.17 O ANISOU 1102 O SER A 147 4477 3817 2789 104 120 -5 O ATOM 1103 CB SER A 147 0.078 13.092 6.784 1.00 27.93 C ANISOU 1103 CB SER A 147 4215 3516 2879 186 126 -262 C ATOM 1104 OG SER A 147 -0.565 13.302 5.511 1.00 29.79 O ANISOU 1104 OG SER A 147 4581 3697 3037 -84 142 -470 O ATOM 1105 N GLN A 148 2.241 14.462 4.823 1.00 28.33 N ANISOU 1105 N GLN A 148 4189 3861 2712 152 242 -176 N ATOM 1106 CA GLN A 148 2.609 15.739 4.220 1.00 27.72 C ANISOU 1106 CA GLN A 148 4134 3694 2704 235 307 -179 C ATOM 1107 C GLN A 148 1.595 16.865 4.493 1.00 28.28 C ANISOU 1107 C GLN A 148 4122 3705 2916 252 139 -128 C ATOM 1108 O GLN A 148 2.000 18.034 4.575 1.00 28.09 O ANISOU 1108 O GLN A 148 4097 3619 2957 356 165 -79 O ATOM 1109 CB GLN A 148 2.886 15.568 2.726 1.00 28.97 C ANISOU 1109 CB GLN A 148 4280 3879 2849 213 289 -310 C ATOM 1110 CG GLN A 148 4.138 14.715 2.490 1.00 29.29 C ANISOU 1110 CG GLN A 148 4249 4170 2707 137 208 -405 C ATOM 1111 CD GLN A 148 4.328 14.375 1.004 1.00 32.02 C ANISOU 1111 CD GLN A 148 4735 4711 2718 92 216 -162 C ATOM 1112 NE2 GLN A 148 5.567 14.092 0.628 1.00 37.11 N ANISOU 1112 NE2 GLN A 148 5080 5385 3634 -191 702 -164 N ATOM 1113 OE1 GLN A 148 3.364 14.319 0.231 1.00 32.95 O ANISOU 1113 OE1 GLN A 148 4898 4499 3121 -136 165 -463 O ATOM 1114 N TYR A 149 0.314 16.500 4.619 1.00 27.99 N ANISOU 1114 N TYR A 149 4195 3568 2871 153 177 -116 N ATOM 1115 CA TYR A 149 -0.786 17.427 4.960 1.00 27.91 C ANISOU 1115 CA TYR A 149 4161 3586 2856 171 76 -127 C ATOM 1116 C TYR A 149 -1.714 16.809 5.950 1.00 27.59 C ANISOU 1116 C TYR A 149 4092 3488 2902 122 63 -179 C ATOM 1117 O TYR A 149 -2.005 15.611 5.879 1.00 27.55 O ANISOU 1117 O TYR A 149 4161 3328 2977 214 401 -241 O ATOM 1118 CB TYR A 149 -1.634 17.800 3.742 1.00 29.10 C ANISOU 1118 CB TYR A 149 4392 3703 2958 125 4 -109 C ATOM 1119 CG TYR A 149 -0.915 18.653 2.748 1.00 31.55 C ANISOU 1119 CG TYR A 149 4639 4046 3301 19 31 -5 C ATOM 1120 CD1 TYR A 149 -0.060 18.073 1.794 1.00 30.91 C ANISOU 1120 CD1 TYR A 149 4570 4157 3014 153 30 184 C ATOM 1121 CD2 TYR A 149 -1.086 20.019 2.747 1.00 32.64 C ANISOU 1121 CD2 TYR A 149 4838 4167 3393 -123 -270 20 C ATOM 1122 CE1 TYR A 149 0.623 18.852 0.899 1.00 30.45 C ANISOU 1122 CE1 TYR A 149 4788 4028 2753 117 -148 93 C ATOM 1123 CE2 TYR A 149 -0.433 20.822 1.813 1.00 32.56 C ANISOU 1123 CE2 TYR A 149 4830 4054 3484 -205 -175 156 C ATOM 1124 CZ TYR A 149 0.427 20.228 0.905 1.00 33.26 C ANISOU 1124 CZ TYR A 149 4998 4149 3487 -100 40 232 C ATOM 1125 OH TYR A 149 1.095 20.960 -0.040 1.00 37.01 O ANISOU 1125 OH TYR A 149 5399 4531 4129 -331 141 341 O ATOM 1126 N THR A 150 -2.188 17.627 6.884 1.00 26.17 N ANISOU 1126 N THR A 150 3942 3255 2744 222 114 -110 N ATOM 1127 CA THR A 150 -3.162 17.142 7.868 1.00 26.55 C ANISOU 1127 CA THR A 150 3972 3422 2692 236 -32 -128 C ATOM 1128 C THR A 150 -4.253 18.163 8.044 1.00 26.68 C ANISOU 1128 C THR A 150 4050 3344 2743 230 6 -317 C ATOM 1129 O THR A 150 -4.107 19.294 7.565 1.00 27.94 O ANISOU 1129 O THR A 150 4213 3373 3028 411 11 -350 O ATOM 1130 CB THR A 150 -2.512 16.759 9.215 1.00 25.00 C ANISOU 1130 CB THR A 150 3795 3131 2573 188 -117 -35 C ATOM 1131 CG2 THR A 150 -2.095 17.967 9.971 1.00 27.56 C ANISOU 1131 CG2 THR A 150 4211 3428 2830 177 -304 -64 C ATOM 1132 OG1 THR A 150 -3.485 16.074 10.011 1.00 27.20 O ANISOU 1132 OG1 THR A 150 3943 3433 2960 -24 -87 110 O ATOM 1133 N VAL A 151 -5.369 17.740 8.636 1.00 27.01 N ANISOU 1133 N VAL A 151 4116 3479 2668 359 168 -419 N ATOM 1134 CA VAL A 151 -6.469 18.663 8.947 1.00 26.99 C ANISOU 1134 CA VAL A 151 4094 3430 2729 462 112 -263 C ATOM 1135 C VAL A 151 -6.721 18.498 10.422 1.00 28.23 C ANISOU 1135 C VAL A 151 4224 3619 2881 383 166 -245 C ATOM 1136 O VAL A 151 -6.851 17.359 10.923 1.00 27.65 O ANISOU 1136 O VAL A 151 4215 3610 2679 545 -38 -241 O ATOM 1137 CB VAL A 151 -7.783 18.364 8.137 1.00 27.52 C ANISOU 1137 CB VAL A 151 4131 3326 2996 461 178 -232 C ATOM 1138 CG1 VAL A 151 -8.920 19.335 8.507 1.00 27.66 C ANISOU 1138 CG1 VAL A 151 3941 3123 3445 406 369 -241 C ATOM 1139 CG2 VAL A 151 -7.506 18.435 6.662 1.00 28.23 C ANISOU 1139 CG2 VAL A 151 4266 3530 2929 406 129 -505 C ATOM 1140 N VAL A 152 -6.768 19.643 11.109 1.00 28.20 N ANISOU 1140 N VAL A 152 4239 3713 2762 383 131 -295 N ATOM 1141 CA VAL A 152 -6.986 19.651 12.554 1.00 29.28 C ANISOU 1141 CA VAL A 152 4256 3844 3022 441 162 -225 C ATOM 1142 C VAL A 152 -8.115 20.623 12.893 1.00 28.51 C ANISOU 1142 C VAL A 152 4169 3597 3064 519 121 -177 C ATOM 1143 O VAL A 152 -8.414 21.534 12.133 1.00 29.77 O ANISOU 1143 O VAL A 152 4289 3693 3327 907 295 -215 O ATOM 1144 CB VAL A 152 -5.670 20.020 13.354 1.00 29.64 C ANISOU 1144 CB VAL A 152 4248 3817 3195 345 120 -151 C ATOM 1145 CG1 VAL A 152 -4.513 19.080 13.017 1.00 30.61 C ANISOU 1145 CG1 VAL A 152 4219 4115 3296 366 155 -235 C ATOM 1146 CG2 VAL A 152 -5.257 21.462 13.130 1.00 32.05 C ANISOU 1146 CG2 VAL A 152 4676 3948 3553 275 285 -222 C ATOM 1147 N ASP A 153 -8.737 20.421 14.041 1.00 27.96 N ANISOU 1147 N ASP A 153 4073 3487 3062 673 200 -184 N ATOM 1148 CA ASP A 153 -9.738 21.347 14.542 1.00 27.85 C ANISOU 1148 CA ASP A 153 4125 3370 3085 597 242 -117 C ATOM 1149 C ASP A 153 -9.045 22.633 15.016 1.00 28.67 C ANISOU 1149 C ASP A 153 4157 3484 3251 601 81 -138 C ATOM 1150 O ASP A 153 -7.898 22.604 15.444 1.00 28.86 O ANISOU 1150 O ASP A 153 4421 3314 3228 685 107 -135 O ATOM 1151 CB ASP A 153 -10.534 20.649 15.646 1.00 29.94 C ANISOU 1151 CB ASP A 153 4153 3821 3400 424 297 -203 C ATOM 1152 CG ASP A 153 -11.490 19.607 15.075 1.00 31.60 C ANISOU 1152 CG ASP A 153 4194 4130 3682 336 359 -273 C ATOM 1153 OD1 ASP A 153 -12.499 20.009 14.441 1.00 35.39 O ANISOU 1153 OD1 ASP A 153 4575 4907 3962 350 72 -288 O ATOM 1154 OD2 ASP A 153 -11.212 18.388 15.208 1.00 35.69 O1- ANISOU 1154 OD2 ASP A 153 4818 4654 4087 381 393 -51 O1- ATOM 1155 N GLU A 154 -9.740 23.777 14.904 1.00 29.30 N ANISOU 1155 N GLU A 154 4484 3397 3250 549 15 -50 N ATOM 1156 CA GLU A 154 -9.142 25.057 15.286 1.00 30.32 C ANISOU 1156 CA GLU A 154 4582 3553 3385 588 -109 0 C ATOM 1157 C GLU A 154 -8.656 25.028 16.729 1.00 30.05 C ANISOU 1157 C GLU A 154 4534 3623 3261 532 -116 19 C ATOM 1158 O GLU A 154 -7.613 25.627 17.055 1.00 30.03 O ANISOU 1158 O GLU A 154 4737 3630 3041 637 -203 0 O ATOM 1159 CB GLU A 154 -10.120 26.222 15.057 1.00 31.14 C ANISOU 1159 CB GLU A 154 4642 3547 3641 537 -144 -109 C ATOM 1160 CG GLU A 154 -9.474 27.570 15.356 1.00 32.09 C ANISOU 1160 CG GLU A 154 4548 3482 4162 674 -151 116 C ATOM 1161 CD GLU A 154 -10.385 28.757 15.024 1.00 32.25 C ANISOU 1161 CD GLU A 154 4813 3579 3861 675 -194 66 C ATOM 1162 OE1 GLU A 154 -11.625 28.557 14.877 1.00 33.16 O ANISOU 1162 OE1 GLU A 154 4798 3993 3809 961 -48 14 O ATOM 1163 OE2 GLU A 154 -9.817 29.868 14.957 1.00 33.35 O1- ANISOU 1163 OE2 GLU A 154 5308 3505 3857 712 -158 87 O1- ATOM 1164 N ILE A 155 -9.394 24.310 17.572 1.00 30.02 N ANISOU 1164 N ILE A 155 4566 3745 3094 510 -154 42 N ATOM 1165 CA ILE A 155 -8.993 24.208 19.011 1.00 30.16 C ANISOU 1165 CA ILE A 155 4514 3811 3133 410 -65 97 C ATOM 1166 C ILE A 155 -7.719 23.414 19.243 1.00 29.53 C ANISOU 1166 C ILE A 155 4489 3624 3107 384 -25 5 C ATOM 1167 O ILE A 155 -7.201 23.397 20.360 1.00 29.92 O ANISOU 1167 O ILE A 155 4405 3840 3121 452 -36 -69 O ATOM 1168 CB ILE A 155 -10.122 23.663 19.920 1.00 30.07 C ANISOU 1168 CB ILE A 155 4396 3754 3274 366 -186 197 C ATOM 1169 CG1 ILE A 155 -10.494 22.224 19.527 1.00 30.99 C ANISOU 1169 CG1 ILE A 155 4680 3767 3326 346 37 134 C ATOM 1170 CG2 ILE A 155 -11.325 24.597 19.874 1.00 30.87 C ANISOU 1170 CG2 ILE A 155 4544 3612 3574 544 2 11 C ATOM 1171 CD1 ILE A 155 -11.329 21.473 20.589 1.00 31.91 C ANISOU 1171 CD1 ILE A 155 4736 4011 3375 335 124 211 C ATOM 1172 N SER A 156 -7.226 22.754 18.194 1.00 28.94 N ANISOU 1172 N SER A 156 4461 3367 3168 369 85 -27 N ATOM 1173 CA SER A 156 -6.042 21.923 18.257 1.00 29.47 C ANISOU 1173 CA SER A 156 4465 3411 3320 335 67 5 C ATOM 1174 C SER A 156 -4.882 22.508 17.463 1.00 29.56 C ANISOU 1174 C SER A 156 4516 3412 3303 371 57 44 C ATOM 1175 O SER A 156 -4.028 21.775 17.011 1.00 28.90 O ANISOU 1175 O SER A 156 4453 3363 3162 385 34 -86 O ATOM 1176 CB SER A 156 -6.382 20.503 17.725 1.00 30.16 C ANISOU 1176 CB SER A 156 4502 3366 3588 452 70 37 C ATOM 1177 OG SER A 156 -7.294 19.838 18.611 1.00 32.48 O ANISOU 1177 OG SER A 156 4794 3559 3987 333 203 -26 O ATOM 1178 N VAL A 157 -4.871 23.822 17.237 1.00 29.44 N ANISOU 1178 N VAL A 157 4679 3379 3124 280 61 -83 N ATOM 1179 CA VAL A 157 -3.726 24.417 16.538 1.00 30.71 C ANISOU 1179 CA VAL A 157 4717 3618 3332 250 17 -3 C ATOM 1180 C VAL A 157 -3.414 25.791 17.124 1.00 31.39 C ANISOU 1180 C VAL A 157 4832 3663 3429 215 56 -87 C ATOM 1181 O VAL A 157 -4.334 26.485 17.537 1.00 30.47 O ANISOU 1181 O VAL A 157 4820 3371 3383 299 47 -155 O ATOM 1182 CB VAL A 157 -3.979 24.508 15.017 1.00 31.07 C ANISOU 1182 CB VAL A 157 4650 3819 3333 269 59 -26 C ATOM 1183 CG1 VAL A 157 -5.093 25.548 14.723 1.00 31.87 C ANISOU 1183 CG1 VAL A 157 4657 4018 3433 385 -18 133 C ATOM 1184 CG2 VAL A 157 -2.669 24.782 14.252 1.00 33.31 C ANISOU 1184 CG2 VAL A 157 4837 4214 3603 165 103 90 C ATOM 1185 N ALA A 158 -2.127 26.134 17.198 1.00 32.46 N ANISOU 1185 N ALA A 158 5067 3714 3551 173 17 -79 N ATOM 1186 CA ALA A 158 -1.669 27.417 17.703 1.00 33.43 C ANISOU 1186 CA ALA A 158 5219 3831 3650 105 -69 -49 C ATOM 1187 C ALA A 158 -0.754 28.122 16.695 1.00 33.35 C ANISOU 1187 C ALA A 158 5235 3787 3647 190 37 1 C ATOM 1188 O ALA A 158 0.152 27.506 16.135 1.00 33.06 O ANISOU 1188 O ALA A 158 5194 3828 3536 337 -30 29 O ATOM 1189 CB ALA A 158 -0.949 27.231 19.035 1.00 33.71 C ANISOU 1189 CB ALA A 158 5338 3793 3678 59 -179 -72 C ATOM 1190 N LYS A 159 -1.007 29.407 16.447 1.00 34.77 N ANISOU 1190 N LYS A 159 5376 3921 3913 227 76 -71 N ATOM 1191 CA LYS A 159 -0.143 30.219 15.599 1.00 35.31 C ANISOU 1191 CA LYS A 159 5390 3830 4194 172 62 70 C ATOM 1192 C LYS A 159 1.124 30.597 16.354 1.00 34.94 C ANISOU 1192 C LYS A 159 5403 3784 4087 54 122 29 C ATOM 1193 O LYS A 159 1.065 30.978 17.525 1.00 35.17 O ANISOU 1193 O LYS A 159 5476 3748 4139 -14 81 116 O ATOM 1194 CB LYS A 159 -0.900 31.485 15.139 1.00 35.74 C ANISOU 1194 CB LYS A 159 5458 3918 4203 141 -37 153 C ATOM 1195 CG LYS A 159 -0.046 32.541 14.407 1.00 38.19 C ANISOU 1195 CG LYS A 159 5678 4119 4713 111 159 92 C ATOM 1196 CD LYS A 159 -0.772 33.882 14.396 1.00 38.95 C ANISOU 1196 CD LYS A 159 5728 4189 4883 275 -20 251 C ATOM 1197 CE LYS A 159 -0.056 34.864 13.463 1.00 43.28 C ANISOU 1197 CE LYS A 159 6074 4755 5613 220 243 336 C ATOM 1198 NZ LYS A 159 -0.796 36.158 13.273 1.00 45.50 N1+ ANISOU 1198 NZ LYS A 159 6473 4791 6021 316 -78 344 N1+ ATOM 1199 N ILE A 160 2.273 30.487 15.681 1.00 34.20 N ANISOU 1199 N ILE A 160 5298 3734 3961 -74 110 32 N ATOM 1200 CA ILE A 160 3.550 30.814 16.284 1.00 34.15 C ANISOU 1200 CA ILE A 160 5279 3788 3908 -161 138 72 C ATOM 1201 C ILE A 160 4.285 31.857 15.445 1.00 35.79 C ANISOU 1201 C ILE A 160 5465 3969 4161 -292 114 136 C ATOM 1202 O ILE A 160 3.874 32.162 14.309 1.00 35.69 O ANISOU 1202 O ILE A 160 5525 3759 4274 -459 59 294 O ATOM 1203 CB ILE A 160 4.415 29.546 16.547 1.00 33.64 C ANISOU 1203 CB ILE A 160 5257 3747 3778 -183 0 6 C ATOM 1204 CG1 ILE A 160 4.837 28.864 15.224 1.00 33.58 C ANISOU 1204 CG1 ILE A 160 5139 3864 3755 -110 199 24 C ATOM 1205 CG2 ILE A 160 3.635 28.565 17.444 1.00 33.75 C ANISOU 1205 CG2 ILE A 160 5343 3861 3618 -84 159 -97 C ATOM 1206 CD1 ILE A 160 5.967 27.891 15.347 1.00 33.09 C ANISOU 1206 CD1 ILE A 160 5262 3763 3544 -114 144 0 C ATOM 1207 N ASP A 161 5.348 32.404 16.021 1.00 37.06 N ANISOU 1207 N ASP A 161 5582 4142 4355 -341 142 102 N ATOM 1208 CA ASP A 161 6.186 33.431 15.368 1.00 38.68 C ANISOU 1208 CA ASP A 161 5821 4366 4509 -349 153 169 C ATOM 1209 C ASP A 161 6.602 33.061 13.940 1.00 39.26 C ANISOU 1209 C ASP A 161 5897 4429 4588 -311 140 162 C ATOM 1210 O ASP A 161 7.218 32.027 13.713 1.00 38.94 O ANISOU 1210 O ASP A 161 5933 4378 4484 -282 87 187 O ATOM 1211 CB ASP A 161 7.446 33.657 16.197 1.00 39.82 C ANISOU 1211 CB ASP A 161 5886 4503 4738 -382 123 75 C ATOM 1212 CG ASP A 161 8.246 34.862 15.740 1.00 41.63 C ANISOU 1212 CG ASP A 161 6017 4744 5054 -422 129 64 C ATOM 1213 OD1 ASP A 161 8.791 35.554 16.620 1.00 46.36 O ANISOU 1213 OD1 ASP A 161 6352 5349 5911 -383 -96 -276 O ATOM 1214 OD2 ASP A 161 8.345 35.113 14.525 1.00 43.51 O1- ANISOU 1214 OD2 ASP A 161 6341 4996 5195 -478 18 -32 O1- ATOM 1215 N ALA A 162 6.318 33.946 12.991 1.00 39.76 N ANISOU 1215 N ALA A 162 5986 4489 4631 -292 86 218 N ATOM 1216 CA ALA A 162 6.600 33.636 11.575 1.00 40.16 C ANISOU 1216 CA ALA A 162 6032 4485 4742 -270 132 211 C ATOM 1217 C ALA A 162 8.083 33.380 11.257 1.00 40.59 C ANISOU 1217 C ALA A 162 6054 4530 4837 -326 128 242 C ATOM 1218 O ALA A 162 8.418 32.756 10.243 1.00 39.62 O ANISOU 1218 O ALA A 162 6099 4193 4763 -374 206 248 O ATOM 1219 CB ALA A 162 6.009 34.694 10.668 1.00 40.58 C ANISOU 1219 CB ALA A 162 6050 4526 4840 -273 95 234 C ATOM 1220 N ALA A 163 8.973 33.848 12.125 1.00 41.13 N ANISOU 1220 N ALA A 163 6040 4630 4956 -317 109 171 N ATOM 1221 CA ALA A 163 10.402 33.644 11.922 1.00 41.79 C ANISOU 1221 CA ALA A 163 5960 4791 5126 -273 152 116 C ATOM 1222 C ALA A 163 10.974 32.350 12.536 1.00 41.63 C ANISOU 1222 C ALA A 163 5875 4817 5124 -271 168 129 C ATOM 1223 O ALA A 163 12.186 32.113 12.467 1.00 41.99 O ANISOU 1223 O ALA A 163 5815 4898 5239 -378 243 120 O ATOM 1224 CB ALA A 163 11.182 34.867 12.394 1.00 42.79 C ANISOU 1224 CB ALA A 163 6065 4885 5309 -219 70 83 C ATOM 1225 N SER A 164 10.102 31.501 13.093 1.00 41.34 N ANISOU 1225 N SER A 164 5822 4808 5077 -254 240 154 N ATOM 1226 CA SER A 164 10.511 30.291 13.843 1.00 40.99 C ANISOU 1226 CA SER A 164 5764 4793 5016 -259 210 213 C ATOM 1227 C SER A 164 11.152 29.211 12.968 1.00 39.92 C ANISOU 1227 C SER A 164 5558 4707 4902 -317 197 215 C ATOM 1228 O SER A 164 10.658 28.946 11.880 1.00 39.96 O ANISOU 1228 O SER A 164 5705 4615 4862 -376 270 191 O ATOM 1229 CB SER A 164 9.289 29.656 14.532 1.00 41.08 C ANISOU 1229 CB SER A 164 5767 4826 5014 -231 217 298 C ATOM 1230 OG SER A 164 8.451 30.608 15.153 1.00 43.24 O ANISOU 1230 OG SER A 164 6222 4984 5223 -117 52 401 O ATOM 1231 N PRO A 165 12.252 28.580 13.443 1.00 39.35 N ANISOU 1231 N PRO A 165 5481 4677 4791 -345 203 166 N ATOM 1232 CA PRO A 165 12.798 27.426 12.720 1.00 38.35 C ANISOU 1232 CA PRO A 165 5314 4651 4606 -341 196 130 C ATOM 1233 C PRO A 165 11.951 26.208 13.041 1.00 37.88 C ANISOU 1233 C PRO A 165 5316 4598 4476 -345 167 60 C ATOM 1234 O PRO A 165 12.044 25.658 14.144 1.00 37.60 O ANISOU 1234 O PRO A 165 5382 4620 4282 -334 308 49 O ATOM 1235 CB PRO A 165 14.225 27.303 13.282 1.00 38.50 C ANISOU 1235 CB PRO A 165 5360 4565 4702 -304 179 122 C ATOM 1236 CG PRO A 165 14.145 27.874 14.624 1.00 38.64 C ANISOU 1236 CG PRO A 165 5340 4700 4640 -401 100 178 C ATOM 1237 CD PRO A 165 13.067 28.913 14.628 1.00 38.52 C ANISOU 1237 CD PRO A 165 5364 4633 4639 -382 180 156 C ATOM 1238 N LEU A 166 11.108 25.797 12.094 1.00 37.85 N ANISOU 1238 N LEU A 166 5176 4709 4496 -405 182 108 N ATOM 1239 CA LEU A 166 10.112 24.745 12.381 1.00 37.35 C ANISOU 1239 CA LEU A 166 5124 4697 4367 -400 182 25 C ATOM 1240 C LEU A 166 10.752 23.379 12.684 1.00 37.27 C ANISOU 1240 C LEU A 166 5176 4658 4327 -360 234 -33 C ATOM 1241 O LEU A 166 10.208 22.574 13.466 1.00 36.45 O ANISOU 1241 O LEU A 166 5128 4685 4035 -380 369 -102 O ATOM 1242 CB LEU A 166 9.103 24.634 11.227 1.00 36.30 C ANISOU 1242 CB LEU A 166 4964 4592 4236 -426 135 18 C ATOM 1243 CG LEU A 166 8.222 25.873 11.000 1.00 36.18 C ANISOU 1243 CG LEU A 166 5023 4565 4159 -402 138 -25 C ATOM 1244 CD1 LEU A 166 7.184 25.604 9.932 1.00 36.50 C ANISOU 1244 CD1 LEU A 166 4928 4300 4640 -394 -200 101 C ATOM 1245 CD2 LEU A 166 7.554 26.422 12.287 1.00 35.70 C ANISOU 1245 CD2 LEU A 166 4908 4321 4334 -568 146 -216 C ATOM 1246 N GLU A 167 11.927 23.134 12.103 1.00 37.37 N ANISOU 1246 N GLU A 167 5197 4761 4238 -396 249 -84 N ATOM 1247 CA GLU A 167 12.666 21.903 12.347 1.00 38.71 C ANISOU 1247 CA GLU A 167 5364 4898 4443 -335 160 -143 C ATOM 1248 C GLU A 167 13.164 21.756 13.783 1.00 38.21 C ANISOU 1248 C GLU A 167 5342 4763 4411 -342 110 -97 C ATOM 1249 O GLU A 167 13.575 20.678 14.181 1.00 38.75 O ANISOU 1249 O GLU A 167 5447 4739 4535 -333 57 -280 O ATOM 1250 CB GLU A 167 13.852 21.761 11.371 1.00 40.05 C ANISOU 1250 CB GLU A 167 5462 5098 4656 -322 245 6 C ATOM 1251 CG GLU A 167 14.561 23.076 11.064 1.00 44.94 C ANISOU 1251 CG GLU A 167 6027 5580 5466 -415 257 -46 C ATOM 1252 CD GLU A 167 13.784 23.914 10.046 1.00 48.86 C ANISOU 1252 CD GLU A 167 6568 6000 5996 -185 327 229 C ATOM 1253 OE1 GLU A 167 13.548 23.441 8.906 1.00 52.56 O ANISOU 1253 OE1 GLU A 167 6981 6378 6609 -383 149 -6 O ATOM 1254 OE2 GLU A 167 13.416 25.053 10.381 1.00 50.62 O1- ANISOU 1254 OE2 GLU A 167 6815 6270 6148 -141 733 119 O1- ATOM 1255 N LYS A 168 13.150 22.858 14.531 1.00 37.30 N ANISOU 1255 N LYS A 168 5333 4626 4211 -327 52 -172 N ATOM 1256 CA LYS A 168 13.532 22.853 15.954 1.00 36.71 C ANISOU 1256 CA LYS A 168 5173 4504 4271 -398 -75 -143 C ATOM 1257 C LYS A 168 12.316 22.982 16.853 1.00 35.61 C ANISOU 1257 C LYS A 168 5147 4253 4127 -405 -130 -143 C ATOM 1258 O LYS A 168 12.135 22.204 17.798 1.00 33.99 O ANISOU 1258 O LYS A 168 5102 3757 4054 -443 -298 -37 O ATOM 1259 CB LYS A 168 14.522 23.982 16.249 1.00 38.06 C ANISOU 1259 CB LYS A 168 5332 4696 4433 -395 -81 -189 C ATOM 1260 CG LYS A 168 15.788 23.853 15.396 1.00 39.19 C ANISOU 1260 CG LYS A 168 5254 4851 4784 -355 49 -111 C ATOM 1261 CD LYS A 168 16.942 24.704 15.917 1.00 42.55 C ANISOU 1261 CD LYS A 168 5373 5279 5514 -437 -42 -160 C ATOM 1262 CE LYS A 168 18.172 24.629 14.980 1.00 43.80 C ANISOU 1262 CE LYS A 168 5587 5515 5540 -305 41 -113 C ATOM 1263 NZ LYS A 168 18.090 25.441 13.720 1.00 46.59 N1+ ANISOU 1263 NZ LYS A 168 5901 5477 6322 -87 -184 92 N1+ ATOM 1264 N VAL A 169 11.459 23.951 16.554 1.00 33.94 N ANISOU 1264 N VAL A 169 5016 3924 3956 -392 -86 -235 N ATOM 1265 CA VAL A 169 10.361 24.253 17.480 1.00 34.48 C ANISOU 1265 CA VAL A 169 5142 4045 3913 -325 -32 -148 C ATOM 1266 C VAL A 169 9.243 23.216 17.487 1.00 33.32 C ANISOU 1266 C VAL A 169 5107 3916 3636 -261 -14 -106 C ATOM 1267 O VAL A 169 8.368 23.233 18.363 1.00 33.84 O ANISOU 1267 O VAL A 169 5303 4012 3541 -362 9 -188 O ATOM 1268 CB VAL A 169 9.827 25.710 17.322 1.00 35.21 C ANISOU 1268 CB VAL A 169 5195 4078 4103 -334 -82 -169 C ATOM 1269 CG1 VAL A 169 10.949 26.730 17.566 1.00 36.16 C ANISOU 1269 CG1 VAL A 169 5113 4308 4315 -434 42 -75 C ATOM 1270 CG2 VAL A 169 9.189 25.934 15.977 1.00 35.20 C ANISOU 1270 CG2 VAL A 169 5221 4039 4114 -225 -106 -105 C ATOM 1271 N CYS A 170 9.289 22.266 16.548 1.00 32.32 N ANISOU 1271 N CYS A 170 5109 3685 3483 -291 -66 -15 N ATOM 1272 CA CYS A 170 8.322 21.194 16.582 1.00 32.26 C ANISOU 1272 CA CYS A 170 5065 3782 3410 -209 -126 -20 C ATOM 1273 C CYS A 170 8.388 20.486 17.937 1.00 31.38 C ANISOU 1273 C CYS A 170 4948 3710 3262 -172 -25 -40 C ATOM 1274 O CYS A 170 7.386 19.997 18.379 1.00 31.28 O ANISOU 1274 O CYS A 170 5094 3641 3146 -174 32 -25 O ATOM 1275 CB CYS A 170 8.556 20.204 15.453 1.00 32.93 C ANISOU 1275 CB CYS A 170 5086 3741 3685 -179 -107 -132 C ATOM 1276 SG CYS A 170 10.212 19.566 15.326 1.00 35.00 S ANISOU 1276 SG CYS A 170 5106 4226 3966 -213 -169 -185 S ATOM 1277 N LEU A 171 9.546 20.486 18.591 1.00 31.98 N ANISOU 1277 N LEU A 171 4943 3918 3287 -157 14 -63 N ATOM 1278 CA LEU A 171 9.682 19.840 19.947 1.00 31.17 C ANISOU 1278 CA LEU A 171 4683 3946 3213 -93 73 22 C ATOM 1279 C LEU A 171 8.751 20.448 20.998 1.00 30.70 C ANISOU 1279 C LEU A 171 4542 3910 3212 -168 112 11 C ATOM 1280 O LEU A 171 8.384 19.818 22.004 1.00 31.07 O ANISOU 1280 O LEU A 171 4752 3985 3066 -231 128 39 O ATOM 1281 CB LEU A 171 11.112 19.961 20.485 1.00 32.77 C ANISOU 1281 CB LEU A 171 4809 4241 3400 -101 3 -83 C ATOM 1282 CG LEU A 171 12.167 19.257 19.620 1.00 35.87 C ANISOU 1282 CG LEU A 171 4836 4654 4139 181 -2 -73 C ATOM 1283 CD1 LEU A 171 13.508 19.196 20.312 1.00 38.67 C ANISOU 1283 CD1 LEU A 171 5047 4968 4676 137 -142 -263 C ATOM 1284 CD2 LEU A 171 11.692 17.865 19.248 1.00 39.59 C ANISOU 1284 CD2 LEU A 171 5239 5113 4688 -80 -285 -15 C ATOM 1285 N ILE A 172 8.363 21.680 20.772 1.00 29.58 N ANISOU 1285 N ILE A 172 4370 3793 3074 -189 276 -63 N ATOM 1286 CA ILE A 172 7.411 22.328 21.678 1.00 30.31 C ANISOU 1286 CA ILE A 172 4446 3772 3296 -42 216 -62 C ATOM 1287 C ILE A 172 6.017 21.641 21.596 1.00 29.41 C ANISOU 1287 C ILE A 172 4419 3685 3068 -33 178 0 C ATOM 1288 O ILE A 172 5.196 21.739 22.502 1.00 30.26 O ANISOU 1288 O ILE A 172 4438 3801 3258 -139 152 -5 O ATOM 1289 CB ILE A 172 7.466 23.862 21.464 1.00 30.50 C ANISOU 1289 CB ILE A 172 4426 3839 3322 -110 189 87 C ATOM 1290 CG1 ILE A 172 8.815 24.398 21.994 1.00 31.75 C ANISOU 1290 CG1 ILE A 172 4731 3726 3607 -116 50 25 C ATOM 1291 CG2 ILE A 172 6.309 24.546 22.155 1.00 30.95 C ANISOU 1291 CG2 ILE A 172 4616 3537 3606 -10 260 -66 C ATOM 1292 CD1 ILE A 172 9.169 25.791 21.512 1.00 32.67 C ANISOU 1292 CD1 ILE A 172 4654 3773 3987 -504 -189 -111 C ATOM 1293 N GLY A 173 5.800 20.874 20.527 1.00 28.43 N ANISOU 1293 N GLY A 173 4314 3541 2946 -80 -39 46 N ATOM 1294 CA GLY A 173 4.588 20.129 20.306 1.00 28.50 C ANISOU 1294 CA GLY A 173 4354 3439 3033 13 -43 95 C ATOM 1295 C GLY A 173 4.386 19.005 21.309 1.00 28.17 C ANISOU 1295 C GLY A 173 4281 3380 3042 91 -77 76 C ATOM 1296 O GLY A 173 3.250 18.518 21.483 1.00 29.38 O ANISOU 1296 O GLY A 173 4450 3516 3196 215 41 58 O ATOM 1297 N CYS A 174 5.466 18.552 21.955 1.00 29.25 N ANISOU 1297 N CYS A 174 4529 3525 3058 141 -54 -135 N ATOM 1298 CA CYS A 174 5.278 17.495 22.950 1.00 28.50 C ANISOU 1298 CA CYS A 174 4421 3466 2939 142 -115 -271 C ATOM 1299 C CYS A 174 6.450 17.358 23.902 1.00 28.53 C ANISOU 1299 C CYS A 174 4278 3569 2992 250 -162 -279 C ATOM 1300 O CYS A 174 6.321 17.683 25.095 1.00 29.89 O ANISOU 1300 O CYS A 174 4345 3976 3035 189 -236 -216 O ATOM 1301 CB CYS A 174 4.970 16.095 22.308 1.00 29.73 C ANISOU 1301 CB CYS A 174 4676 3451 3168 97 -166 -237 C ATOM 1302 SG CYS A 174 4.613 14.878 23.720 1.00 29.66 S ANISOU 1302 SG CYS A 174 4509 3782 2979 163 48 -100 S ATOM 1303 N GLY A 175 7.579 16.863 23.420 1.00 29.49 N ANISOU 1303 N GLY A 175 4365 3831 3009 136 -147 -239 N ATOM 1304 CA GLY A 175 8.608 16.394 24.366 1.00 30.09 C ANISOU 1304 CA GLY A 175 4345 3899 3185 226 -145 -308 C ATOM 1305 C GLY A 175 9.209 17.488 25.231 1.00 31.32 C ANISOU 1305 C GLY A 175 4640 3905 3354 124 -33 -195 C ATOM 1306 O GLY A 175 9.325 17.327 26.460 1.00 32.07 O ANISOU 1306 O GLY A 175 4670 4078 3435 118 40 -377 O ATOM 1307 N PHE A 176 9.577 18.606 24.601 1.00 31.67 N ANISOU 1307 N PHE A 176 4707 3988 3335 -5 25 -146 N ATOM 1308 CA PHE A 176 10.189 19.705 25.338 1.00 30.10 C ANISOU 1308 CA PHE A 176 4618 3786 3029 -50 28 -101 C ATOM 1309 C PHE A 176 9.192 20.312 26.325 1.00 30.32 C ANISOU 1309 C PHE A 176 4643 3760 3116 9 -11 -115 C ATOM 1310 O PHE A 176 9.529 20.536 27.503 1.00 30.37 O ANISOU 1310 O PHE A 176 4700 3966 2871 38 -169 70 O ATOM 1311 CB PHE A 176 10.715 20.821 24.433 1.00 31.25 C ANISOU 1311 CB PHE A 176 4723 4029 3120 -109 163 -182 C ATOM 1312 CG PHE A 176 11.117 22.054 25.213 1.00 31.40 C ANISOU 1312 CG PHE A 176 4890 3894 3144 -328 143 75 C ATOM 1313 CD1 PHE A 176 12.335 22.090 25.873 1.00 33.60 C ANISOU 1313 CD1 PHE A 176 5087 4324 3353 -400 108 -90 C ATOM 1314 CD2 PHE A 176 10.243 23.145 25.344 1.00 31.97 C ANISOU 1314 CD2 PHE A 176 5333 3881 2930 -143 294 -322 C ATOM 1315 CE1 PHE A 176 12.699 23.224 26.649 1.00 33.63 C ANISOU 1315 CE1 PHE A 176 5443 3773 3561 -318 445 -21 C ATOM 1316 CE2 PHE A 176 10.617 24.309 26.107 1.00 31.34 C ANISOU 1316 CE2 PHE A 176 5026 3884 2995 -481 172 141 C ATOM 1317 CZ PHE A 176 11.838 24.333 26.732 1.00 32.23 C ANISOU 1317 CZ PHE A 176 4993 4103 3147 -216 265 -135 C ATOM 1318 N SER A 177 7.991 20.638 25.845 1.00 28.62 N ANISOU 1318 N SER A 177 4462 3558 2854 -50 -31 -140 N ATOM 1319 CA SER A 177 6.968 21.281 26.703 1.00 29.50 C ANISOU 1319 CA SER A 177 4653 3624 2929 0 89 6 C ATOM 1320 C SER A 177 6.587 20.406 27.882 1.00 29.00 C ANISOU 1320 C SER A 177 4562 3613 2841 -56 78 -78 C ATOM 1321 O SER A 177 6.345 20.885 29.023 1.00 29.07 O ANISOU 1321 O SER A 177 4796 3480 2767 -53 208 -314 O ATOM 1322 CB SER A 177 5.751 21.619 25.868 1.00 28.05 C ANISOU 1322 CB SER A 177 4258 3519 2881 -15 223 -10 C ATOM 1323 OG SER A 177 6.140 22.562 24.858 1.00 30.05 O ANISOU 1323 OG SER A 177 5088 3223 3107 254 100 129 O ATOM 1324 N THR A 178 6.535 19.116 27.616 1.00 28.81 N ANISOU 1324 N THR A 178 4517 3564 2862 9 -15 4 N ATOM 1325 CA THR A 178 6.121 18.153 28.652 1.00 27.77 C ANISOU 1325 CA THR A 178 4174 3552 2823 -88 17 -8 C ATOM 1326 C THR A 178 7.125 18.155 29.821 1.00 28.68 C ANISOU 1326 C THR A 178 4226 3726 2943 -5 25 -74 C ATOM 1327 O THR A 178 6.733 18.229 30.986 1.00 29.32 O ANISOU 1327 O THR A 178 4062 3978 3098 22 174 -144 O ATOM 1328 CB THR A 178 5.956 16.748 28.051 1.00 27.49 C ANISOU 1328 CB THR A 178 4083 3547 2813 24 -71 -35 C ATOM 1329 CG2 THR A 178 5.737 15.719 29.142 1.00 28.24 C ANISOU 1329 CG2 THR A 178 4215 3663 2850 72 -62 8 C ATOM 1330 OG1 THR A 178 4.811 16.730 27.164 1.00 27.34 O ANISOU 1330 OG1 THR A 178 4015 3282 3091 -223 -275 25 O ATOM 1331 N GLY A 179 8.411 18.048 29.516 1.00 28.65 N ANISOU 1331 N GLY A 179 4069 3763 3052 -136 -83 -9 N ATOM 1332 CA GLY A 179 9.447 18.054 30.571 1.00 29.71 C ANISOU 1332 CA GLY A 179 4250 3958 3079 9 -117 -51 C ATOM 1333 C GLY A 179 9.610 19.437 31.178 1.00 30.39 C ANISOU 1333 C GLY A 179 4419 4071 3056 -55 -84 -1 C ATOM 1334 O GLY A 179 9.597 19.596 32.388 1.00 30.39 O ANISOU 1334 O GLY A 179 4515 4122 2908 7 -234 -37 O ATOM 1335 N TYR A 180 9.723 20.452 30.333 1.00 30.41 N ANISOU 1335 N TYR A 180 4637 4058 2859 -84 -102 61 N ATOM 1336 CA TYR A 180 9.945 21.832 30.787 1.00 30.83 C ANISOU 1336 CA TYR A 180 4745 4125 2843 -191 25 79 C ATOM 1337 C TYR A 180 8.823 22.334 31.709 1.00 30.62 C ANISOU 1337 C TYR A 180 4669 4108 2855 -221 -16 -7 C ATOM 1338 O TYR A 180 9.116 22.842 32.803 1.00 30.86 O ANISOU 1338 O TYR A 180 4762 4298 2664 -315 -42 4 O ATOM 1339 CB TYR A 180 10.087 22.739 29.552 1.00 32.10 C ANISOU 1339 CB TYR A 180 4942 4122 3133 -212 56 169 C ATOM 1340 CG TYR A 180 10.498 24.141 29.851 1.00 34.04 C ANISOU 1340 CG TYR A 180 5148 4329 3454 -249 60 88 C ATOM 1341 CD1 TYR A 180 11.828 24.460 30.109 1.00 35.79 C ANISOU 1341 CD1 TYR A 180 5497 4376 3725 -325 -188 35 C ATOM 1342 CD2 TYR A 180 9.559 25.157 29.832 1.00 33.16 C ANISOU 1342 CD2 TYR A 180 5279 3702 3617 -281 156 -197 C ATOM 1343 CE1 TYR A 180 12.207 25.761 30.360 1.00 35.68 C ANISOU 1343 CE1 TYR A 180 5756 4348 3451 -257 -24 -152 C ATOM 1344 CE2 TYR A 180 9.922 26.465 30.098 1.00 36.61 C ANISOU 1344 CE2 TYR A 180 5660 4159 4089 -549 164 -207 C ATOM 1345 CZ TYR A 180 11.253 26.752 30.352 1.00 35.43 C ANISOU 1345 CZ TYR A 180 5399 4331 3730 -276 -125 -142 C ATOM 1346 OH TYR A 180 11.634 28.052 30.598 1.00 39.70 O ANISOU 1346 OH TYR A 180 6173 4450 4461 -401 -21 74 O ATOM 1347 N GLY A 181 7.562 22.164 31.286 1.00 30.10 N ANISOU 1347 N GLY A 181 4640 4114 2680 3 -11 125 N ATOM 1348 CA GLY A 181 6.389 22.529 32.100 1.00 30.68 C ANISOU 1348 CA GLY A 181 4588 4139 2927 -77 -24 70 C ATOM 1349 C GLY A 181 6.287 21.755 33.400 1.00 30.59 C ANISOU 1349 C GLY A 181 4662 4055 2905 -20 -5 -37 C ATOM 1350 O GLY A 181 5.860 22.300 34.449 1.00 31.87 O ANISOU 1350 O GLY A 181 4879 4178 3050 -27 33 -173 O ATOM 1351 N SER A 182 6.677 20.492 33.375 1.00 29.43 N ANISOU 1351 N SER A 182 4579 3773 2829 -172 9 -158 N ATOM 1352 CA SER A 182 6.620 19.694 34.586 1.00 30.06 C ANISOU 1352 CA SER A 182 4751 3811 2857 -50 -64 -169 C ATOM 1353 C SER A 182 7.430 20.361 35.681 1.00 30.20 C ANISOU 1353 C SER A 182 4618 3845 3011 -167 -63 -88 C ATOM 1354 O SER A 182 7.024 20.355 36.844 1.00 29.95 O ANISOU 1354 O SER A 182 4418 3874 3086 -51 14 -70 O ATOM 1355 CB SER A 182 7.105 18.282 34.319 1.00 30.99 C ANISOU 1355 CB SER A 182 4948 3782 3043 -146 -124 109 C ATOM 1356 OG SER A 182 6.219 17.663 33.429 1.00 32.23 O ANISOU 1356 OG SER A 182 5233 4077 2933 46 -78 -240 O ATOM 1357 N ALA A 183 8.551 20.971 35.307 1.00 30.11 N ANISOU 1357 N ALA A 183 4580 3808 3051 -231 -115 -160 N ATOM 1358 CA ALA A 183 9.361 21.722 36.280 1.00 30.85 C ANISOU 1358 CA ALA A 183 4649 3882 3191 -263 -28 -132 C ATOM 1359 C ALA A 183 8.786 23.105 36.560 1.00 31.93 C ANISOU 1359 C ALA A 183 4794 4046 3289 -191 30 -161 C ATOM 1360 O ALA A 183 8.572 23.470 37.740 1.00 32.15 O ANISOU 1360 O ALA A 183 4957 4124 3135 -92 -17 -112 O ATOM 1361 CB ALA A 183 10.798 21.816 35.780 1.00 31.42 C ANISOU 1361 CB ALA A 183 4687 4031 3217 -254 32 -230 C ATOM 1362 N VAL A 184 8.550 23.889 35.498 1.00 31.40 N ANISOU 1362 N VAL A 184 4621 3966 3341 -183 -53 -121 N ATOM 1363 CA VAL A 184 8.232 25.324 35.652 1.00 34.10 C ANISOU 1363 CA VAL A 184 4952 4191 3813 -203 79 -122 C ATOM 1364 C VAL A 184 6.785 25.590 36.012 1.00 34.56 C ANISOU 1364 C VAL A 184 5016 4179 3933 -127 39 -214 C ATOM 1365 O VAL A 184 6.485 26.575 36.728 1.00 37.06 O ANISOU 1365 O VAL A 184 5374 4270 4435 -169 138 -363 O ATOM 1366 CB VAL A 184 8.691 26.163 34.404 1.00 34.94 C ANISOU 1366 CB VAL A 184 4860 4206 4207 -209 67 16 C ATOM 1367 CG1 VAL A 184 8.291 27.624 34.548 1.00 38.53 C ANISOU 1367 CG1 VAL A 184 5332 4570 4736 -130 111 -78 C ATOM 1368 CG2 VAL A 184 10.188 25.992 34.198 1.00 36.79 C ANISOU 1368 CG2 VAL A 184 4976 4724 4275 -185 -21 -50 C ATOM 1369 N LYS A 185 5.898 24.677 35.615 1.00 34.15 N ANISOU 1369 N LYS A 185 5015 4119 3838 -120 87 -175 N ATOM 1370 CA LYS A 185 4.458 24.868 35.732 1.00 34.10 C ANISOU 1370 CA LYS A 185 4980 4221 3754 -101 124 -139 C ATOM 1371 C LYS A 185 3.791 23.945 36.764 1.00 33.35 C ANISOU 1371 C LYS A 185 4919 4162 3587 -116 183 -173 C ATOM 1372 O LYS A 185 2.978 24.401 37.584 1.00 34.72 O ANISOU 1372 O LYS A 185 5014 4269 3909 -73 351 -149 O ATOM 1373 CB LYS A 185 3.806 24.659 34.363 1.00 35.00 C ANISOU 1373 CB LYS A 185 5055 4280 3960 -151 25 -273 C ATOM 1374 CG LYS A 185 2.307 24.936 34.298 1.00 37.59 C ANISOU 1374 CG LYS A 185 5187 4625 4469 47 139 -146 C ATOM 1375 CD LYS A 185 1.956 26.406 34.476 1.00 41.96 C ANISOU 1375 CD LYS A 185 5580 4935 5427 62 -24 -254 C ATOM 1376 CE LYS A 185 0.523 26.676 34.049 1.00 45.04 C ANISOU 1376 CE LYS A 185 5707 5680 5725 42 -74 6 C ATOM 1377 NZ LYS A 185 -0.474 25.897 34.860 1.00 47.42 N1+ ANISOU 1377 NZ LYS A 185 5972 5974 6069 90 121 6 N1+ ATOM 1378 N VAL A 186 4.138 22.665 36.730 1.00 32.05 N ANISOU 1378 N VAL A 186 4788 4129 3261 -176 167 -152 N ATOM 1379 CA VAL A 186 3.477 21.666 37.577 1.00 31.69 C ANISOU 1379 CA VAL A 186 4825 4135 3080 -157 42 -149 C ATOM 1380 C VAL A 186 4.118 21.649 38.951 1.00 31.84 C ANISOU 1380 C VAL A 186 4775 4284 3039 -110 62 -131 C ATOM 1381 O VAL A 186 3.424 21.924 39.951 1.00 32.99 O ANISOU 1381 O VAL A 186 4806 4579 3147 -30 130 -316 O ATOM 1382 CB VAL A 186 3.471 20.238 36.921 1.00 30.76 C ANISOU 1382 CB VAL A 186 4772 4008 2908 -173 96 -123 C ATOM 1383 CG1 VAL A 186 2.777 19.229 37.843 1.00 31.21 C ANISOU 1383 CG1 VAL A 186 4618 4013 3224 -284 6 120 C ATOM 1384 CG2 VAL A 186 2.756 20.270 35.545 1.00 30.41 C ANISOU 1384 CG2 VAL A 186 4579 4052 2921 -144 -63 33 C ATOM 1385 N ALA A 187 5.417 21.344 39.001 1.00 31.49 N ANISOU 1385 N ALA A 187 4692 4295 2978 -211 -64 -162 N ATOM 1386 CA ALA A 187 6.166 21.374 40.291 1.00 32.67 C ANISOU 1386 CA ALA A 187 4729 4379 3306 -156 -107 -168 C ATOM 1387 C ALA A 187 6.324 22.789 40.831 1.00 33.23 C ANISOU 1387 C ALA A 187 4837 4385 3404 -213 -90 -243 C ATOM 1388 O ALA A 187 6.321 22.993 42.055 1.00 33.60 O ANISOU 1388 O ALA A 187 4892 4371 3501 -157 74 -436 O ATOM 1389 CB ALA A 187 7.530 20.701 40.160 1.00 32.00 C ANISOU 1389 CB ALA A 187 4540 4347 3269 -212 -131 -150 C ATOM 1390 N LYS A 188 6.497 23.752 39.923 1.00 34.23 N ANISOU 1390 N LYS A 188 4934 4348 3723 -287 -54 -321 N ATOM 1391 CA LYS A 188 6.862 25.130 40.301 1.00 35.11 C ANISOU 1391 CA LYS A 188 5228 4335 3775 -171 19 -378 C ATOM 1392 C LYS A 188 8.153 25.152 41.104 1.00 34.83 C ANISOU 1392 C LYS A 188 5231 4284 3719 -181 89 -405 C ATOM 1393 O LYS A 188 8.189 25.638 42.260 1.00 35.75 O ANISOU 1393 O LYS A 188 5500 4418 3666 -248 -119 -478 O ATOM 1394 CB LYS A 188 5.710 25.833 41.052 1.00 36.45 C ANISOU 1394 CB LYS A 188 5305 4456 4086 -116 11 -367 C ATOM 1395 CG LYS A 188 4.527 26.179 40.161 1.00 39.95 C ANISOU 1395 CG LYS A 188 5630 4803 4744 -26 -83 -282 C ATOM 1396 CD LYS A 188 3.300 26.426 41.015 1.00 43.99 C ANISOU 1396 CD LYS A 188 5981 5139 5591 206 -8 -232 C ATOM 1397 CE LYS A 188 2.222 27.139 40.233 1.00 46.15 C ANISOU 1397 CE LYS A 188 6439 5436 5659 126 -235 -56 C ATOM 1398 NZ LYS A 188 2.151 26.631 38.848 1.00 44.68 N1+ ANISOU 1398 NZ LYS A 188 6393 5071 5509 515 33 -256 N1+ ATOM 1399 N VAL A 189 9.209 24.625 40.492 1.00 34.31 N ANISOU 1399 N VAL A 189 5345 4127 3565 -234 118 -305 N ATOM 1400 CA VAL A 189 10.548 24.683 41.055 1.00 33.70 C ANISOU 1400 CA VAL A 189 5326 3951 3524 -376 243 -243 C ATOM 1401 C VAL A 189 10.914 26.108 41.451 1.00 35.11 C ANISOU 1401 C VAL A 189 5608 4059 3671 -365 181 -125 C ATOM 1402 O VAL A 189 10.639 27.076 40.708 1.00 36.39 O ANISOU 1402 O VAL A 189 5990 4204 3629 -453 299 0 O ATOM 1403 CB VAL A 189 11.562 24.102 40.065 1.00 33.90 C ANISOU 1403 CB VAL A 189 5294 3989 3595 -296 258 -165 C ATOM 1404 CG1 VAL A 189 12.985 24.232 40.588 1.00 31.45 C ANISOU 1404 CG1 VAL A 189 5196 3667 3085 -607 201 -122 C ATOM 1405 CG2 VAL A 189 11.233 22.665 39.823 1.00 32.14 C ANISOU 1405 CG2 VAL A 189 4962 3921 3328 -550 358 -340 C ATOM 1406 N THR A 190 11.491 26.217 42.644 1.00 35.07 N ANISOU 1406 N THR A 190 5643 4057 3624 -503 198 -172 N ATOM 1407 CA THR A 190 11.868 27.497 43.234 1.00 35.45 C ANISOU 1407 CA THR A 190 5676 4043 3751 -432 192 -215 C ATOM 1408 C THR A 190 13.386 27.712 43.162 1.00 36.78 C ANISOU 1408 C THR A 190 5685 4265 4025 -390 199 -189 C ATOM 1409 O THR A 190 14.162 26.746 43.119 1.00 37.28 O ANISOU 1409 O THR A 190 5711 4408 4046 -464 255 -106 O ATOM 1410 CB THR A 190 11.419 27.576 44.721 1.00 36.21 C ANISOU 1410 CB THR A 190 5732 4183 3841 -359 221 -212 C ATOM 1411 CG2 THR A 190 9.917 27.694 44.826 1.00 36.01 C ANISOU 1411 CG2 THR A 190 5519 4108 4054 -239 87 -306 C ATOM 1412 OG1 THR A 190 11.826 26.397 45.424 1.00 34.68 O ANISOU 1412 OG1 THR A 190 5959 3659 3557 -414 55 -457 O ATOM 1413 N GLN A 191 13.795 28.983 43.185 1.00 37.59 N ANISOU 1413 N GLN A 191 5680 4320 4281 -498 180 -109 N ATOM 1414 CA GLN A 191 15.210 29.390 43.260 1.00 38.83 C ANISOU 1414 CA GLN A 191 5748 4449 4553 -448 173 -160 C ATOM 1415 C GLN A 191 15.977 28.758 44.423 1.00 37.87 C ANISOU 1415 C GLN A 191 5632 4310 4446 -577 198 -139 C ATOM 1416 O GLN A 191 15.496 28.710 45.576 1.00 39.52 O ANISOU 1416 O GLN A 191 5905 4529 4580 -568 197 -279 O ATOM 1417 CB GLN A 191 15.328 30.925 43.319 1.00 39.08 C ANISOU 1417 CB GLN A 191 5796 4428 4625 -517 226 -97 C ATOM 1418 CG GLN A 191 14.973 31.641 42.011 1.00 43.88 C ANISOU 1418 CG GLN A 191 6247 5112 5313 -153 -67 -64 C ATOM 1419 CD GLN A 191 14.299 32.995 42.223 1.00 48.70 C ANISOU 1419 CD GLN A 191 6770 5645 6087 73 104 -21 C ATOM 1420 NE2 GLN A 191 13.858 33.260 43.449 1.00 50.17 N ANISOU 1420 NE2 GLN A 191 6811 6030 6218 -15 174 -15 N ATOM 1421 OE1 GLN A 191 14.165 33.787 41.282 1.00 52.20 O ANISOU 1421 OE1 GLN A 191 7129 6099 6603 -109 158 204 O ATOM 1422 N GLY A 192 17.152 28.228 44.111 1.00 37.15 N ANISOU 1422 N GLY A 192 5503 4231 4381 -688 130 -108 N ATOM 1423 CA GLY A 192 18.018 27.616 45.106 1.00 36.55 C ANISOU 1423 CA GLY A 192 5353 4221 4312 -784 92 -70 C ATOM 1424 C GLY A 192 17.626 26.229 45.604 1.00 35.81 C ANISOU 1424 C GLY A 192 5192 4220 4193 -821 55 -31 C ATOM 1425 O GLY A 192 18.291 25.687 46.496 1.00 35.34 O ANISOU 1425 O GLY A 192 5170 4187 4069 -996 90 -61 O ATOM 1426 N SER A 193 16.585 25.642 45.008 1.00 34.83 N ANISOU 1426 N SER A 193 5181 4105 3946 -814 58 -144 N ATOM 1427 CA SER A 193 16.096 24.328 45.445 1.00 34.12 C ANISOU 1427 CA SER A 193 4946 4165 3852 -821 67 -148 C ATOM 1428 C SER A 193 16.970 23.203 44.890 1.00 33.65 C ANISOU 1428 C SER A 193 4857 4129 3798 -854 2 -219 C ATOM 1429 O SER A 193 17.812 23.443 44.021 1.00 34.16 O ANISOU 1429 O SER A 193 4961 4199 3819 -934 146 -256 O ATOM 1430 CB SER A 193 14.637 24.145 45.034 1.00 34.56 C ANISOU 1430 CB SER A 193 5063 4177 3890 -829 -47 -164 C ATOM 1431 OG SER A 193 14.526 24.059 43.623 1.00 33.96 O ANISOU 1431 OG SER A 193 5273 4012 3614 -836 -98 123 O ATOM 1432 N THR A 194 16.761 21.988 45.390 1.00 31.56 N ANISOU 1432 N THR A 194 4550 4006 3436 -890 -129 -238 N ATOM 1433 CA THR A 194 17.474 20.799 44.944 1.00 31.97 C ANISOU 1433 CA THR A 194 4371 4087 3686 -947 -144 -243 C ATOM 1434 C THR A 194 16.438 19.932 44.241 1.00 31.07 C ANISOU 1434 C THR A 194 4221 4035 3547 -895 -134 -271 C ATOM 1435 O THR A 194 15.372 19.675 44.794 1.00 30.17 O ANISOU 1435 O THR A 194 4041 3822 3599 -1189 -183 -394 O ATOM 1436 CB THR A 194 18.135 20.018 46.133 1.00 31.92 C ANISOU 1436 CB THR A 194 4334 4077 3717 -944 -172 -254 C ATOM 1437 CG2 THR A 194 18.672 18.668 45.689 1.00 31.90 C ANISOU 1437 CG2 THR A 194 4018 4249 3853 -919 -51 -193 C ATOM 1438 OG1 THR A 194 19.206 20.791 46.702 1.00 35.14 O ANISOU 1438 OG1 THR A 194 4789 4508 4054 -992 -484 -369 O ATOM 1439 N CYS A 195 16.767 19.502 43.033 1.00 30.22 N ANISOU 1439 N CYS A 195 4104 4050 3327 -907 -147 -238 N ATOM 1440 CA CYS A 195 15.871 18.702 42.185 1.00 30.40 C ANISOU 1440 CA CYS A 195 4194 4073 3280 -873 -142 -114 C ATOM 1441 C CYS A 195 16.538 17.385 41.847 1.00 29.92 C ANISOU 1441 C CYS A 195 4014 4169 3184 -732 -162 -118 C ATOM 1442 O CYS A 195 17.765 17.331 41.720 1.00 30.82 O ANISOU 1442 O CYS A 195 4116 4298 3295 -910 -214 -58 O ATOM 1443 CB CYS A 195 15.566 19.448 40.882 1.00 30.92 C ANISOU 1443 CB CYS A 195 4314 4148 3285 -774 -192 -163 C ATOM 1444 SG CYS A 195 14.618 20.952 41.077 1.00 32.91 S ANISOU 1444 SG CYS A 195 4854 4173 3475 -973 97 168 S ATOM 1445 N ALA A 196 15.734 16.325 41.675 1.00 28.34 N ANISOU 1445 N ALA A 196 3687 4135 2945 -730 -69 -166 N ATOM 1446 CA ALA A 196 16.237 15.022 41.216 1.00 28.14 C ANISOU 1446 CA ALA A 196 3586 4143 2963 -646 -320 -105 C ATOM 1447 C ALA A 196 15.391 14.590 40.036 1.00 27.52 C ANISOU 1447 C ALA A 196 3356 4126 2974 -560 -214 -160 C ATOM 1448 O ALA A 196 14.162 14.589 40.140 1.00 28.17 O ANISOU 1448 O ALA A 196 3197 4368 3138 -651 -250 -287 O ATOM 1449 CB ALA A 196 16.136 13.984 42.327 1.00 29.72 C ANISOU 1449 CB ALA A 196 3890 4279 3120 -635 -231 -6 C ATOM 1450 N VAL A 197 16.048 14.196 38.940 1.00 27.31 N ANISOU 1450 N VAL A 197 3286 4047 3042 -537 -222 -173 N ATOM 1451 CA VAL A 197 15.354 13.882 37.701 1.00 28.05 C ANISOU 1451 CA VAL A 197 3395 4168 3094 -338 -197 -81 C ATOM 1452 C VAL A 197 15.673 12.440 37.340 1.00 28.00 C ANISOU 1452 C VAL A 197 3359 4133 3144 -292 -209 -167 C ATOM 1453 O VAL A 197 16.828 12.130 37.037 1.00 28.79 O ANISOU 1453 O VAL A 197 3396 4192 3351 -265 -133 -141 O ATOM 1454 CB VAL A 197 15.790 14.790 36.538 1.00 27.46 C ANISOU 1454 CB VAL A 197 3203 4075 3152 -342 -244 -91 C ATOM 1455 CG1 VAL A 197 15.049 14.361 35.235 1.00 28.25 C ANISOU 1455 CG1 VAL A 197 3494 4095 3145 -598 -286 125 C ATOM 1456 CG2 VAL A 197 15.522 16.207 36.875 1.00 29.73 C ANISOU 1456 CG2 VAL A 197 4064 4037 3194 -472 -85 208 C ATOM 1457 N PHE A 198 14.653 11.576 37.343 1.00 29.28 N ANISOU 1457 N PHE A 198 3448 4314 3363 -196 -74 -127 N ATOM 1458 CA PHE A 198 14.851 10.144 37.084 1.00 29.50 C ANISOU 1458 CA PHE A 198 3474 4486 3248 -128 -73 -214 C ATOM 1459 C PHE A 198 14.507 9.857 35.624 1.00 29.40 C ANISOU 1459 C PHE A 198 3413 4507 3248 -47 -95 -281 C ATOM 1460 O PHE A 198 13.314 9.806 35.245 1.00 30.31 O ANISOU 1460 O PHE A 198 3292 4774 3450 30 78 -415 O ATOM 1461 CB PHE A 198 13.942 9.306 37.992 1.00 30.01 C ANISOU 1461 CB PHE A 198 3378 4623 3399 -17 -133 -100 C ATOM 1462 CG PHE A 198 14.343 9.321 39.443 1.00 30.52 C ANISOU 1462 CG PHE A 198 3576 4654 3363 -129 -36 -135 C ATOM 1463 CD1 PHE A 198 13.967 10.372 40.268 1.00 29.88 C ANISOU 1463 CD1 PHE A 198 3587 4506 3258 -54 -149 -86 C ATOM 1464 CD2 PHE A 198 15.084 8.267 39.973 1.00 30.72 C ANISOU 1464 CD2 PHE A 198 3487 4664 3519 -161 -259 -221 C ATOM 1465 CE1 PHE A 198 14.332 10.401 41.615 1.00 30.68 C ANISOU 1465 CE1 PHE A 198 3709 4689 3258 12 -54 -272 C ATOM 1466 CE2 PHE A 198 15.451 8.269 41.315 1.00 31.05 C ANISOU 1466 CE2 PHE A 198 3712 4722 3363 17 -191 -244 C ATOM 1467 CZ PHE A 198 15.061 9.351 42.138 1.00 31.41 C ANISOU 1467 CZ PHE A 198 3711 4782 3439 -26 -104 -192 C ATOM 1468 N GLY A 199 15.559 9.681 34.830 1.00 29.78 N ANISOU 1468 N GLY A 199 3541 4596 3179 -14 -69 -263 N ATOM 1469 CA GLY A 199 15.484 9.450 33.399 1.00 29.81 C ANISOU 1469 CA GLY A 199 3750 4437 3140 -85 -36 -290 C ATOM 1470 C GLY A 199 16.066 10.618 32.620 1.00 30.78 C ANISOU 1470 C GLY A 199 3862 4448 3384 -91 -22 -274 C ATOM 1471 O GLY A 199 15.635 11.763 32.789 1.00 31.53 O ANISOU 1471 O GLY A 199 4009 4393 3576 -182 203 -216 O ATOM 1472 N LEU A 200 17.049 10.328 31.772 1.00 29.75 N ANISOU 1472 N LEU A 200 3770 4431 3099 -148 -72 -242 N ATOM 1473 CA LEU A 200 17.788 11.367 31.072 1.00 30.82 C ANISOU 1473 CA LEU A 200 3964 4360 3384 -99 -52 -213 C ATOM 1474 C LEU A 200 17.707 11.268 29.540 1.00 30.49 C ANISOU 1474 C LEU A 200 3821 4363 3400 -103 6 -163 C ATOM 1475 O LEU A 200 18.626 11.693 28.813 1.00 31.34 O ANISOU 1475 O LEU A 200 3824 4575 3506 -179 94 -177 O ATOM 1476 CB LEU A 200 19.247 11.422 31.573 1.00 31.00 C ANISOU 1476 CB LEU A 200 4114 4338 3326 -73 -152 -222 C ATOM 1477 CG LEU A 200 19.405 11.650 33.080 1.00 31.61 C ANISOU 1477 CG LEU A 200 4374 4257 3379 187 -156 -175 C ATOM 1478 CD1 LEU A 200 20.894 11.548 33.505 1.00 33.59 C ANISOU 1478 CD1 LEU A 200 4453 4651 3656 24 -132 -225 C ATOM 1479 CD2 LEU A 200 18.815 12.993 33.450 1.00 31.67 C ANISOU 1479 CD2 LEU A 200 4279 4323 3432 304 143 -275 C ATOM 1480 N GLY A 201 16.599 10.699 29.063 1.00 31.27 N ANISOU 1480 N GLY A 201 3958 4426 3497 -136 -70 -164 N ATOM 1481 CA GLY A 201 16.120 10.918 27.697 1.00 31.34 C ANISOU 1481 CA GLY A 201 3921 4397 3589 -94 54 -151 C ATOM 1482 C GLY A 201 15.646 12.341 27.445 1.00 32.06 C ANISOU 1482 C GLY A 201 3981 4522 3678 -16 70 -231 C ATOM 1483 O GLY A 201 15.837 13.234 28.273 1.00 32.50 O ANISOU 1483 O GLY A 201 3839 4520 3988 -23 130 -387 O ATOM 1484 N GLY A 202 15.021 12.540 26.292 1.00 31.27 N ANISOU 1484 N GLY A 202 3892 4402 3586 -4 34 -78 N ATOM 1485 CA GLY A 202 14.656 13.881 25.822 1.00 30.51 C ANISOU 1485 CA GLY A 202 3908 4298 3384 52 111 -112 C ATOM 1486 C GLY A 202 13.742 14.600 26.789 1.00 30.22 C ANISOU 1486 C GLY A 202 3904 4276 3299 -40 83 -74 C ATOM 1487 O GLY A 202 13.920 15.789 27.024 1.00 30.49 O ANISOU 1487 O GLY A 202 3975 4440 3169 -121 81 -113 O ATOM 1488 N VAL A 203 12.774 13.877 27.358 1.00 29.46 N ANISOU 1488 N VAL A 203 3762 4195 3233 -74 42 -95 N ATOM 1489 CA VAL A 203 11.822 14.493 28.282 1.00 29.50 C ANISOU 1489 CA VAL A 203 3903 4160 3144 -165 36 -143 C ATOM 1490 C VAL A 203 12.565 14.867 29.579 1.00 29.18 C ANISOU 1490 C VAL A 203 3787 4245 3054 -114 21 -86 C ATOM 1491 O VAL A 203 12.389 15.998 30.084 1.00 30.41 O ANISOU 1491 O VAL A 203 4048 4383 3122 -196 54 2 O ATOM 1492 CB VAL A 203 10.567 13.647 28.510 1.00 29.58 C ANISOU 1492 CB VAL A 203 3825 4298 3115 -88 123 -209 C ATOM 1493 CG1 VAL A 203 9.607 14.375 29.466 1.00 31.18 C ANISOU 1493 CG1 VAL A 203 3957 4338 3551 36 205 -167 C ATOM 1494 CG2 VAL A 203 9.845 13.328 27.168 1.00 31.47 C ANISOU 1494 CG2 VAL A 203 3916 4362 3678 -136 -76 -150 C ATOM 1495 N GLY A 204 13.449 13.982 30.054 1.00 29.50 N ANISOU 1495 N GLY A 204 4004 4201 3003 -276 35 -16 N ATOM 1496 CA GLY A 204 14.229 14.263 31.280 1.00 29.41 C ANISOU 1496 CA GLY A 204 3842 4256 3074 -266 -11 47 C ATOM 1497 C GLY A 204 15.173 15.447 31.104 1.00 29.68 C ANISOU 1497 C GLY A 204 3872 4361 3043 -333 63 -66 C ATOM 1498 O GLY A 204 15.335 16.289 32.017 1.00 30.52 O ANISOU 1498 O GLY A 204 3943 4438 3214 -318 104 8 O ATOM 1499 N LEU A 205 15.814 15.525 29.937 1.00 29.66 N ANISOU 1499 N LEU A 205 3901 4411 2956 -329 32 -61 N ATOM 1500 CA LEU A 205 16.646 16.688 29.642 1.00 30.08 C ANISOU 1500 CA LEU A 205 3924 4527 2976 -285 199 -85 C ATOM 1501 C LEU A 205 15.813 17.962 29.658 1.00 29.59 C ANISOU 1501 C LEU A 205 3982 4484 2775 -304 99 -76 C ATOM 1502 O LEU A 205 16.291 18.982 30.098 1.00 30.76 O ANISOU 1502 O LEU A 205 4063 4691 2931 -368 162 53 O ATOM 1503 CB LEU A 205 17.339 16.554 28.282 1.00 30.58 C ANISOU 1503 CB LEU A 205 4046 4582 2990 -301 125 -156 C ATOM 1504 CG LEU A 205 18.368 15.428 28.230 1.00 30.73 C ANISOU 1504 CG LEU A 205 4220 4456 3000 -192 135 -262 C ATOM 1505 CD1 LEU A 205 18.896 15.333 26.784 1.00 32.53 C ANISOU 1505 CD1 LEU A 205 4455 4754 3149 -118 268 -391 C ATOM 1506 CD2 LEU A 205 19.517 15.625 29.224 1.00 32.54 C ANISOU 1506 CD2 LEU A 205 4266 4786 3309 -170 80 -145 C ATOM 1507 N SER A 206 14.574 17.892 29.151 1.00 29.62 N ANISOU 1507 N SER A 206 3983 4608 2660 -214 166 7 N ATOM 1508 CA SER A 206 13.681 19.032 29.163 1.00 29.77 C ANISOU 1508 CA SER A 206 4103 4543 2664 -301 94 -23 C ATOM 1509 C SER A 206 13.289 19.432 30.605 1.00 29.49 C ANISOU 1509 C SER A 206 4159 4409 2637 -303 48 -36 C ATOM 1510 O SER A 206 13.130 20.619 30.918 1.00 30.99 O ANISOU 1510 O SER A 206 4532 4481 2762 -473 141 75 O ATOM 1511 CB SER A 206 12.464 18.755 28.263 1.00 29.19 C ANISOU 1511 CB SER A 206 4100 4566 2424 -125 32 -117 C ATOM 1512 OG SER A 206 12.897 18.594 26.908 1.00 32.61 O ANISOU 1512 OG SER A 206 4363 4920 3105 -290 230 76 O ATOM 1513 N VAL A 207 13.112 18.445 31.475 1.00 29.59 N ANISOU 1513 N VAL A 207 4256 4448 2538 -347 46 -32 N ATOM 1514 CA VAL A 207 12.853 18.740 32.896 1.00 28.99 C ANISOU 1514 CA VAL A 207 4141 4339 2533 -457 -108 -77 C ATOM 1515 C VAL A 207 14.066 19.485 33.475 1.00 29.41 C ANISOU 1515 C VAL A 207 4215 4291 2667 -396 -87 -160 C ATOM 1516 O VAL A 207 13.904 20.489 34.178 1.00 29.29 O ANISOU 1516 O VAL A 207 4297 4020 2810 -408 0 -116 O ATOM 1517 CB VAL A 207 12.563 17.454 33.718 1.00 28.42 C ANISOU 1517 CB VAL A 207 4092 4290 2414 -473 -83 -115 C ATOM 1518 CG1 VAL A 207 12.449 17.828 35.211 1.00 29.72 C ANISOU 1518 CG1 VAL A 207 4412 4545 2335 -635 -120 -201 C ATOM 1519 CG2 VAL A 207 11.290 16.783 33.257 1.00 31.12 C ANISOU 1519 CG2 VAL A 207 4167 4644 3011 -490 -55 23 C ATOM 1520 N ILE A 208 15.269 18.996 33.183 1.00 29.41 N ANISOU 1520 N ILE A 208 4168 4234 2772 -379 -66 -236 N ATOM 1521 CA ILE A 208 16.509 19.642 33.659 1.00 30.34 C ANISOU 1521 CA ILE A 208 4271 4279 2975 -431 -15 -236 C ATOM 1522 C ILE A 208 16.557 21.107 33.191 1.00 31.75 C ANISOU 1522 C ILE A 208 4573 4422 3067 -482 47 -159 C ATOM 1523 O ILE A 208 16.811 22.035 33.983 1.00 32.87 O ANISOU 1523 O ILE A 208 4895 4504 3090 -626 154 22 O ATOM 1524 CB ILE A 208 17.767 18.858 33.227 1.00 30.89 C ANISOU 1524 CB ILE A 208 4215 4372 3147 -510 -87 -225 C ATOM 1525 CG1 ILE A 208 17.813 17.513 33.953 1.00 30.90 C ANISOU 1525 CG1 ILE A 208 4437 4383 2918 -336 40 -223 C ATOM 1526 CG2 ILE A 208 19.044 19.672 33.527 1.00 31.48 C ANISOU 1526 CG2 ILE A 208 4070 4654 3236 -635 3 -108 C ATOM 1527 CD1 ILE A 208 18.864 16.514 33.441 1.00 30.87 C ANISOU 1527 CD1 ILE A 208 4221 4165 3343 -441 26 -304 C ATOM 1528 N MET A 209 16.279 21.319 31.909 1.00 32.80 N ANISOU 1528 N MET A 209 4744 4472 3245 -362 25 -59 N ATOM 1529 CA MET A 209 16.172 22.650 31.366 1.00 34.70 C ANISOU 1529 CA MET A 209 5060 4692 3431 -354 55 -54 C ATOM 1530 C MET A 209 15.232 23.553 32.175 1.00 33.75 C ANISOU 1530 C MET A 209 4993 4511 3317 -300 34 -12 C ATOM 1531 O MET A 209 15.584 24.701 32.441 1.00 35.09 O ANISOU 1531 O MET A 209 5113 4756 3463 -374 -12 -103 O ATOM 1532 CB MET A 209 15.757 22.595 29.898 1.00 35.43 C ANISOU 1532 CB MET A 209 5167 4741 3551 -364 37 -76 C ATOM 1533 CG MET A 209 16.899 22.145 29.021 1.00 35.83 C ANISOU 1533 CG MET A 209 5159 4908 3547 -452 2 -168 C ATOM 1534 SD MET A 209 16.370 22.203 27.333 1.00 37.57 S ANISOU 1534 SD MET A 209 5457 5370 3447 -571 265 -83 S ATOM 1535 CE MET A 209 17.809 21.513 26.518 1.00 40.17 C ANISOU 1535 CE MET A 209 5382 5581 4299 -353 330 51 C ATOM 1536 N GLY A 210 14.060 23.032 32.546 1.00 34.39 N ANISOU 1536 N GLY A 210 4981 4515 3567 -207 28 -80 N ATOM 1537 CA GLY A 210 13.046 23.750 33.348 1.00 33.11 C ANISOU 1537 CA GLY A 210 4935 4280 3365 -298 63 -145 C ATOM 1538 C GLY A 210 13.486 24.060 34.764 1.00 33.56 C ANISOU 1538 C GLY A 210 5011 4213 3527 -366 78 -179 C ATOM 1539 O GLY A 210 13.235 25.171 35.292 1.00 33.77 O ANISOU 1539 O GLY A 210 5093 4135 3600 -414 213 -225 O ATOM 1540 N CYS A 211 14.144 23.080 35.379 1.00 32.33 N ANISOU 1540 N CYS A 211 4860 4121 3300 -460 23 -181 N ATOM 1541 CA CYS A 211 14.721 23.255 36.721 1.00 33.38 C ANISOU 1541 CA CYS A 211 4996 4196 3491 -601 29 -183 C ATOM 1542 C CYS A 211 15.783 24.362 36.677 1.00 33.52 C ANISOU 1542 C CYS A 211 5100 4071 3563 -639 236 -69 C ATOM 1543 O CYS A 211 15.870 25.166 37.625 1.00 34.77 O ANISOU 1543 O CYS A 211 5470 4147 3592 -801 128 -4 O ATOM 1544 CB CYS A 211 15.340 21.967 37.208 1.00 31.64 C ANISOU 1544 CB CYS A 211 4744 4024 3251 -676 99 -215 C ATOM 1545 SG CYS A 211 14.132 20.666 37.594 1.00 31.86 S ANISOU 1545 SG CYS A 211 4788 4227 3088 -934 15 -135 S ATOM 1546 N LYS A 212 16.579 24.405 35.598 1.00 35.05 N ANISOU 1546 N LYS A 212 5283 4250 3784 -596 243 -14 N ATOM 1547 CA LYS A 212 17.597 25.439 35.407 1.00 36.64 C ANISOU 1547 CA LYS A 212 5341 4446 4134 -480 400 -8 C ATOM 1548 C LYS A 212 16.945 26.809 35.194 1.00 36.52 C ANISOU 1548 C LYS A 212 5436 4361 4077 -516 432 115 C ATOM 1549 O LYS A 212 17.330 27.772 35.865 1.00 37.21 O ANISOU 1549 O LYS A 212 5452 4388 4299 -629 502 157 O ATOM 1550 CB LYS A 212 18.514 25.083 34.241 1.00 36.16 C ANISOU 1550 CB LYS A 212 5268 4565 3906 -558 406 115 C ATOM 1551 CG LYS A 212 19.563 26.126 33.932 1.00 37.92 C ANISOU 1551 CG LYS A 212 5247 4655 4503 -518 327 187 C ATOM 1552 CD LYS A 212 20.293 25.699 32.681 1.00 39.99 C ANISOU 1552 CD LYS A 212 5296 4936 4960 -330 368 30 C ATOM 1553 CE LYS A 212 21.423 26.668 32.312 1.00 42.30 C ANISOU 1553 CE LYS A 212 5592 5023 5455 -307 438 454 C ATOM 1554 NZ LYS A 212 22.014 26.240 31.017 1.00 44.78 N1+ ANISOU 1554 NZ LYS A 212 5913 5267 5835 -98 491 154 N1+ ATOM 1555 N ALA A 213 15.909 26.857 34.352 1.00 36.29 N ANISOU 1555 N ALA A 213 5445 4289 4053 -465 508 85 N ATOM 1556 CA ALA A 213 15.151 28.093 34.073 1.00 37.02 C ANISOU 1556 CA ALA A 213 5571 4285 4210 -436 433 67 C ATOM 1557 C ALA A 213 14.579 28.696 35.358 1.00 37.71 C ANISOU 1557 C ALA A 213 5712 4245 4369 -423 489 59 C ATOM 1558 O ALA A 213 14.542 29.918 35.530 1.00 38.96 O ANISOU 1558 O ALA A 213 5939 4243 4619 -544 592 100 O ATOM 1559 CB ALA A 213 14.041 27.841 33.047 1.00 36.83 C ANISOU 1559 CB ALA A 213 5473 4192 4326 -471 437 142 C ATOM 1560 N ALA A 214 14.172 27.819 36.271 1.00 36.85 N ANISOU 1560 N ALA A 214 5682 4183 4136 -491 508 55 N ATOM 1561 CA ALA A 214 13.565 28.214 37.536 1.00 37.30 C ANISOU 1561 CA ALA A 214 5808 4182 4180 -388 415 13 C ATOM 1562 C ALA A 214 14.598 28.526 38.592 1.00 37.52 C ANISOU 1562 C ALA A 214 5831 4289 4134 -393 340 -8 C ATOM 1563 O ALA A 214 14.240 28.923 39.722 1.00 38.92 O ANISOU 1563 O ALA A 214 6149 4417 4220 -194 401 -99 O ATOM 1564 CB ALA A 214 12.654 27.111 38.027 1.00 36.01 C ANISOU 1564 CB ALA A 214 5560 4089 4030 -483 439 -9 C ATOM 1565 N GLY A 215 15.867 28.289 38.281 1.00 36.90 N ANISOU 1565 N GLY A 215 5840 4215 3962 -482 280 16 N ATOM 1566 CA GLY A 215 16.969 28.634 39.200 1.00 38.30 C ANISOU 1566 CA GLY A 215 5869 4427 4254 -623 134 10 C ATOM 1567 C GLY A 215 17.312 27.658 40.319 1.00 37.29 C ANISOU 1567 C GLY A 215 5744 4358 4063 -682 98 -78 C ATOM 1568 O GLY A 215 17.850 28.049 41.360 1.00 37.08 O ANISOU 1568 O GLY A 215 5684 4210 4194 -936 84 -155 O ATOM 1569 N ALA A 216 17.028 26.381 40.108 1.00 36.99 N ANISOU 1569 N ALA A 216 5607 4372 4075 -746 118 -158 N ATOM 1570 CA ALA A 216 17.485 25.326 41.016 1.00 35.94 C ANISOU 1570 CA ALA A 216 5307 4403 3942 -731 95 -222 C ATOM 1571 C ALA A 216 18.988 25.406 41.271 1.00 36.21 C ANISOU 1571 C ALA A 216 5233 4563 3960 -749 69 -198 C ATOM 1572 O ALA A 216 19.776 25.683 40.348 1.00 35.89 O ANISOU 1572 O ALA A 216 5219 4575 3841 -987 209 -144 O ATOM 1573 CB ALA A 216 17.069 23.926 40.474 1.00 36.45 C ANISOU 1573 CB ALA A 216 5274 4417 4159 -666 -30 -274 C ATOM 1574 N ALA A 217 19.393 25.275 42.530 1.00 36.47 N ANISOU 1574 N ALA A 217 5087 4690 4077 -753 5 -169 N ATOM 1575 CA ALA A 217 20.822 25.263 42.854 1.00 35.60 C ANISOU 1575 CA ALA A 217 4843 4703 3980 -705 -102 -225 C ATOM 1576 C ALA A 217 21.511 23.919 42.605 1.00 36.09 C ANISOU 1576 C ALA A 217 4782 4776 4154 -736 -150 -185 C ATOM 1577 O ALA A 217 22.726 23.881 42.346 1.00 37.03 O ANISOU 1577 O ALA A 217 4862 4893 4311 -775 1 -192 O ATOM 1578 CB ALA A 217 21.086 25.776 44.308 1.00 36.43 C ANISOU 1578 CB ALA A 217 4926 4842 4073 -510 -158 -267 C ATOM 1579 N ARG A 218 20.742 22.823 42.682 1.00 33.32 N ANISOU 1579 N ARG A 218 4351 4548 3761 -887 -292 -291 N ATOM 1580 CA ARG A 218 21.293 21.478 42.473 1.00 32.69 C ANISOU 1580 CA ARG A 218 4193 4514 3713 -857 -324 -215 C ATOM 1581 C ARG A 218 20.292 20.709 41.659 1.00 31.73 C ANISOU 1581 C ARG A 218 4112 4432 3512 -809 -270 -252 C ATOM 1582 O ARG A 218 19.113 20.776 41.966 1.00 31.91 O ANISOU 1582 O ARG A 218 4013 4674 3434 -907 -252 -256 O ATOM 1583 CB ARG A 218 21.500 20.728 43.795 1.00 33.02 C ANISOU 1583 CB ARG A 218 4351 4499 3694 -863 -380 -316 C ATOM 1584 CG ARG A 218 22.694 21.157 44.601 1.00 35.04 C ANISOU 1584 CG ARG A 218 4448 4746 4120 -771 -436 -190 C ATOM 1585 CD ARG A 218 22.794 20.305 45.836 1.00 36.21 C ANISOU 1585 CD ARG A 218 4702 4744 4312 -778 -280 -1 C ATOM 1586 NE ARG A 218 23.359 18.963 45.598 1.00 36.45 N ANISOU 1586 NE ARG A 218 4617 4869 4363 -579 -378 -146 N ATOM 1587 CZ ARG A 218 23.506 18.045 46.561 1.00 36.61 C ANISOU 1587 CZ ARG A 218 4587 4893 4428 -641 -251 -187 C ATOM 1588 NH1 ARG A 218 23.091 18.302 47.797 1.00 38.25 N1+ ANISOU 1588 NH1 ARG A 218 4753 5388 4392 -811 -147 -194 N1+ ATOM 1589 NH2 ARG A 218 24.024 16.856 46.295 1.00 38.33 N ANISOU 1589 NH2 ARG A 218 4577 5319 4667 -383 -318 -223 N ATOM 1590 N ILE A 219 20.753 20.022 40.625 1.00 30.97 N ANISOU 1590 N ILE A 219 3965 4349 3453 -773 -261 -172 N ATOM 1591 CA ILE A 219 19.872 19.236 39.770 1.00 31.06 C ANISOU 1591 CA ILE A 219 4061 4355 3385 -655 -227 -201 C ATOM 1592 C ILE A 219 20.575 17.932 39.543 1.00 31.13 C ANISOU 1592 C ILE A 219 3978 4375 3476 -625 -204 -227 C ATOM 1593 O ILE A 219 21.577 17.866 38.825 1.00 31.80 O ANISOU 1593 O ILE A 219 4036 4398 3647 -833 55 -149 O ATOM 1594 CB ILE A 219 19.639 19.865 38.403 1.00 31.73 C ANISOU 1594 CB ILE A 219 4218 4408 3429 -633 -201 -157 C ATOM 1595 CG1 ILE A 219 19.018 21.266 38.512 1.00 31.55 C ANISOU 1595 CG1 ILE A 219 4267 4489 3229 -626 -343 -218 C ATOM 1596 CG2 ILE A 219 18.786 18.939 37.568 1.00 31.98 C ANISOU 1596 CG2 ILE A 219 4168 4501 3479 -521 -328 -253 C ATOM 1597 CD1 ILE A 219 19.158 22.074 37.256 1.00 34.39 C ANISOU 1597 CD1 ILE A 219 5008 4898 3159 -727 -137 -85 C ATOM 1598 N ILE A 220 20.052 16.898 40.173 1.00 29.57 N ANISOU 1598 N ILE A 220 3753 4240 3243 -606 -219 -149 N ATOM 1599 CA ILE A 220 20.679 15.592 40.199 1.00 30.69 C ANISOU 1599 CA ILE A 220 3889 4335 3437 -481 -156 -164 C ATOM 1600 C ILE A 220 20.017 14.678 39.161 1.00 30.98 C ANISOU 1600 C ILE A 220 3853 4485 3430 -422 -138 -237 C ATOM 1601 O ILE A 220 18.881 14.260 39.347 1.00 31.55 O ANISOU 1601 O ILE A 220 3935 4698 3355 -470 -97 -260 O ATOM 1602 CB ILE A 220 20.566 14.957 41.619 1.00 30.32 C ANISOU 1602 CB ILE A 220 3885 4201 3434 -409 -168 -144 C ATOM 1603 CG1 ILE A 220 21.126 15.901 42.717 1.00 28.50 C ANISOU 1603 CG1 ILE A 220 3953 3630 3245 -454 -2 20 C ATOM 1604 CG2 ILE A 220 21.291 13.604 41.631 1.00 31.31 C ANISOU 1604 CG2 ILE A 220 4013 4137 3744 -299 -305 -53 C ATOM 1605 CD1 ILE A 220 20.616 15.616 44.165 1.00 31.47 C ANISOU 1605 CD1 ILE A 220 4029 4316 3610 -523 4 -142 C ATOM 1606 N GLY A 221 20.729 14.364 38.079 1.00 31.44 N ANISOU 1606 N GLY A 221 3855 4665 3425 -351 -157 -218 N ATOM 1607 CA GLY A 221 20.204 13.426 37.088 1.00 31.36 C ANISOU 1607 CA GLY A 221 3690 4775 3450 -215 -202 -262 C ATOM 1608 C GLY A 221 20.476 12.000 37.543 1.00 32.47 C ANISOU 1608 C GLY A 221 3731 4948 3658 -78 -233 -213 C ATOM 1609 O GLY A 221 21.583 11.689 38.036 1.00 33.76 O ANISOU 1609 O GLY A 221 3684 5152 3992 -133 -407 -314 O ATOM 1610 N VAL A 222 19.486 11.136 37.375 1.00 31.23 N ANISOU 1610 N VAL A 222 3468 4860 3539 -12 -139 -206 N ATOM 1611 CA VAL A 222 19.538 9.722 37.763 1.00 31.68 C ANISOU 1611 CA VAL A 222 3507 4830 3700 38 -174 -268 C ATOM 1612 C VAL A 222 19.175 8.835 36.565 1.00 31.88 C ANISOU 1612 C VAL A 222 3529 4789 3792 106 -233 -225 C ATOM 1613 O VAL A 222 18.093 8.975 35.971 1.00 30.98 O ANISOU 1613 O VAL A 222 3401 4599 3772 231 -532 -151 O ATOM 1614 CB VAL A 222 18.609 9.395 38.971 1.00 30.72 C ANISOU 1614 CB VAL A 222 3359 4737 3576 32 -203 -320 C ATOM 1615 CG1 VAL A 222 18.804 7.938 39.397 1.00 33.18 C ANISOU 1615 CG1 VAL A 222 3841 4794 3969 -109 -125 -147 C ATOM 1616 CG2 VAL A 222 18.825 10.362 40.150 1.00 32.81 C ANISOU 1616 CG2 VAL A 222 3822 4691 3949 -83 -197 -489 C ATOM 1617 N ASP A 223 20.085 7.937 36.189 1.00 33.32 N ANISOU 1617 N ASP A 223 3903 4832 3923 173 -205 -93 N ATOM 1618 CA ASP A 223 19.847 7.027 35.057 1.00 34.28 C ANISOU 1618 CA ASP A 223 4031 4922 4071 177 -191 -145 C ATOM 1619 C ASP A 223 20.888 5.918 35.089 1.00 35.34 C ANISOU 1619 C ASP A 223 4148 5035 4245 202 -155 -61 C ATOM 1620 O ASP A 223 22.020 6.187 35.506 1.00 35.61 O ANISOU 1620 O ASP A 223 3996 5265 4269 368 -280 -87 O ATOM 1621 CB ASP A 223 19.968 7.833 33.757 1.00 34.56 C ANISOU 1621 CB ASP A 223 4140 4914 4077 106 -176 -59 C ATOM 1622 CG ASP A 223 19.368 7.122 32.550 1.00 36.99 C ANISOU 1622 CG ASP A 223 4406 5029 4617 82 -173 -250 C ATOM 1623 OD1 ASP A 223 19.993 6.155 32.046 1.00 40.08 O ANISOU 1623 OD1 ASP A 223 4927 5091 5210 262 -237 -278 O ATOM 1624 OD2 ASP A 223 18.293 7.563 32.078 1.00 37.11 O1- ANISOU 1624 OD2 ASP A 223 4434 5088 4576 128 -275 -262 O1- ATOM 1625 N ILE A 224 20.527 4.695 34.679 1.00 36.28 N ANISOU 1625 N ILE A 224 4314 5019 4450 345 -100 -97 N ATOM 1626 CA ILE A 224 21.492 3.564 34.695 1.00 38.69 C ANISOU 1626 CA ILE A 224 4704 5111 4883 223 -21 -86 C ATOM 1627 C ILE A 224 22.390 3.545 33.489 1.00 39.49 C ANISOU 1627 C ILE A 224 4774 5208 5021 296 -2 -91 C ATOM 1628 O ILE A 224 23.349 2.761 33.447 1.00 39.99 O ANISOU 1628 O ILE A 224 4698 5312 5182 441 -7 -38 O ATOM 1629 CB ILE A 224 20.819 2.171 34.835 1.00 39.05 C ANISOU 1629 CB ILE A 224 4735 5179 4923 246 0 -59 C ATOM 1630 CG1 ILE A 224 19.927 1.863 33.612 1.00 39.85 C ANISOU 1630 CG1 ILE A 224 4756 5143 5241 122 70 -196 C ATOM 1631 CG2 ILE A 224 20.137 2.057 36.218 1.00 39.76 C ANISOU 1631 CG2 ILE A 224 5106 5186 4815 174 90 -5 C ATOM 1632 CD1 ILE A 224 19.164 0.528 33.706 1.00 40.32 C ANISOU 1632 CD1 ILE A 224 4992 5151 5173 76 -40 -149 C ATOM 1633 N ASN A 225 22.080 4.386 32.502 1.00 39.11 N ANISOU 1633 N ASN A 225 4708 5196 4955 298 -30 -42 N ATOM 1634 CA ASN A 225 22.928 4.524 31.326 1.00 40.59 C ANISOU 1634 CA ASN A 225 4955 5397 5070 234 37 -16 C ATOM 1635 C ASN A 225 23.818 5.763 31.436 1.00 40.41 C ANISOU 1635 C ASN A 225 4908 5441 5006 189 58 -6 C ATOM 1636 O ASN A 225 23.373 6.901 31.224 1.00 39.87 O ANISOU 1636 O ASN A 225 4823 5486 4837 271 39 59 O ATOM 1637 CB ASN A 225 22.088 4.555 30.052 1.00 41.31 C ANISOU 1637 CB ASN A 225 5091 5481 5122 208 12 -13 C ATOM 1638 CG ASN A 225 22.917 4.325 28.788 1.00 43.27 C ANISOU 1638 CG ASN A 225 5312 5762 5365 254 83 -89 C ATOM 1639 ND2 ASN A 225 22.262 3.877 27.735 1.00 46.31 N ANISOU 1639 ND2 ASN A 225 5892 5993 5708 100 34 -295 N ATOM 1640 OD1 ASN A 225 24.118 4.569 28.759 1.00 46.24 O ANISOU 1640 OD1 ASN A 225 5637 6131 5799 63 302 -152 O ATOM 1641 N LYS A 226 25.082 5.530 31.773 1.00 40.62 N ANISOU 1641 N LYS A 226 4907 5446 5077 207 61 65 N ATOM 1642 CA LYS A 226 26.035 6.616 32.049 1.00 41.19 C ANISOU 1642 CA LYS A 226 4916 5515 5217 161 27 49 C ATOM 1643 C LYS A 226 26.439 7.431 30.834 1.00 41.15 C ANISOU 1643 C LYS A 226 4868 5534 5230 122 112 24 C ATOM 1644 O LYS A 226 27.001 8.514 30.970 1.00 40.88 O ANISOU 1644 O LYS A 226 4751 5551 5231 147 215 30 O ATOM 1645 CB LYS A 226 27.278 6.063 32.737 1.00 42.00 C ANISOU 1645 CB LYS A 226 4983 5617 5357 137 -41 80 C ATOM 1646 CG LYS A 226 26.933 5.297 33.980 1.00 43.02 C ANISOU 1646 CG LYS A 226 5080 5659 5606 16 -60 112 C ATOM 1647 CD LYS A 226 28.119 4.461 34.444 1.00 46.02 C ANISOU 1647 CD LYS A 226 5467 5764 6253 204 -290 52 C ATOM 1648 CE LYS A 226 29.003 5.276 35.388 1.00 46.71 C ANISOU 1648 CE LYS A 226 5786 5718 6241 201 -233 -48 C ATOM 1649 NZ LYS A 226 28.472 5.141 36.739 1.00 45.83 N1+ ANISOU 1649 NZ LYS A 226 5378 5567 6466 155 64 -153 N1+ ATOM 1650 N ASP A 227 26.163 6.915 29.645 1.00 41.62 N ANISOU 1650 N ASP A 227 4960 5571 5282 60 168 -2 N ATOM 1651 CA ASP A 227 26.416 7.695 28.435 1.00 42.58 C ANISOU 1651 CA ASP A 227 5171 5637 5370 -21 258 -18 C ATOM 1652 C ASP A 227 25.410 8.859 28.221 1.00 41.47 C ANISOU 1652 C ASP A 227 5064 5544 5148 -73 309 -18 C ATOM 1653 O ASP A 227 25.583 9.686 27.342 1.00 41.90 O ANISOU 1653 O ASP A 227 5175 5635 5109 -59 464 59 O ATOM 1654 CB ASP A 227 26.536 6.764 27.221 1.00 43.71 C ANISOU 1654 CB ASP A 227 5387 5677 5541 -96 193 -87 C ATOM 1655 CG ASP A 227 27.605 5.667 27.429 1.00 47.18 C ANISOU 1655 CG ASP A 227 5702 5939 6283 -17 127 -143 C ATOM 1656 OD1 ASP A 227 28.792 5.991 27.716 1.00 49.64 O ANISOU 1656 OD1 ASP A 227 5760 6135 6965 6 192 -152 O ATOM 1657 OD2 ASP A 227 27.261 4.464 27.322 1.00 51.21 O1- ANISOU 1657 OD2 ASP A 227 6223 6167 7064 -184 186 -200 O1- ATOM 1658 N LYS A 228 24.370 8.934 29.052 1.00 40.06 N ANISOU 1658 N LYS A 228 4821 5472 4928 -107 319 -6 N ATOM 1659 CA LYS A 228 23.442 10.071 29.028 1.00 39.01 C ANISOU 1659 CA LYS A 228 4686 5349 4784 -116 218 22 C ATOM 1660 C LYS A 228 23.888 11.216 29.938 1.00 38.02 C ANISOU 1660 C LYS A 228 4539 5297 4609 -109 188 83 C ATOM 1661 O LYS A 228 23.297 12.315 29.914 1.00 36.43 O ANISOU 1661 O LYS A 228 4422 5132 4285 -151 203 99 O ATOM 1662 CB LYS A 228 22.033 9.634 29.472 1.00 39.25 C ANISOU 1662 CB LYS A 228 4747 5388 4775 -166 291 64 C ATOM 1663 CG LYS A 228 21.445 8.449 28.735 1.00 42.33 C ANISOU 1663 CG LYS A 228 5198 5586 5297 -109 272 -29 C ATOM 1664 CD LYS A 228 21.181 8.713 27.268 1.00 45.96 C ANISOU 1664 CD LYS A 228 5761 5922 5778 -55 62 252 C ATOM 1665 CE LYS A 228 20.546 7.484 26.641 1.00 47.97 C ANISOU 1665 CE LYS A 228 5952 6076 6198 -32 64 129 C ATOM 1666 NZ LYS A 228 19.241 7.175 27.322 1.00 48.24 N1+ ANISOU 1666 NZ LYS A 228 6028 5835 6463 14 134 498 N1+ ATOM 1667 N PHE A 229 24.903 10.956 30.764 1.00 36.70 N ANISOU 1667 N PHE A 229 4313 5199 4430 -126 149 117 N ATOM 1668 CA PHE A 229 25.337 11.949 31.745 1.00 36.69 C ANISOU 1668 CA PHE A 229 4345 5247 4347 -113 168 126 C ATOM 1669 C PHE A 229 25.920 13.208 31.083 1.00 36.39 C ANISOU 1669 C PHE A 229 4296 5292 4238 -136 213 85 C ATOM 1670 O PHE A 229 25.681 14.317 31.537 1.00 36.43 O ANISOU 1670 O PHE A 229 4459 5321 4061 -186 208 79 O ATOM 1671 CB PHE A 229 26.319 11.354 32.773 1.00 36.22 C ANISOU 1671 CB PHE A 229 4282 5148 4332 -114 149 170 C ATOM 1672 CG PHE A 229 25.722 10.281 33.660 1.00 36.60 C ANISOU 1672 CG PHE A 229 4304 5123 4476 18 89 210 C ATOM 1673 CD1 PHE A 229 24.343 10.009 33.656 1.00 37.14 C ANISOU 1673 CD1 PHE A 229 4471 5132 4507 -116 -123 247 C ATOM 1674 CD2 PHE A 229 26.544 9.575 34.550 1.00 34.94 C ANISOU 1674 CD2 PHE A 229 4252 4954 4067 -33 -25 173 C ATOM 1675 CE1 PHE A 229 23.805 9.036 34.492 1.00 36.65 C ANISOU 1675 CE1 PHE A 229 4258 5189 4477 -165 -15 231 C ATOM 1676 CE2 PHE A 229 26.015 8.598 35.383 1.00 36.72 C ANISOU 1676 CE2 PHE A 229 4424 5056 4469 -184 -61 88 C ATOM 1677 CZ PHE A 229 24.641 8.323 35.360 1.00 35.96 C ANISOU 1677 CZ PHE A 229 4166 5039 4457 -63 32 242 C ATOM 1678 N ALA A 230 26.677 13.042 30.001 1.00 36.65 N ANISOU 1678 N ALA A 230 4393 5394 4136 -164 281 -9 N ATOM 1679 CA ALA A 230 27.324 14.204 29.379 1.00 36.58 C ANISOU 1679 CA ALA A 230 4490 5324 4082 -119 389 1 C ATOM 1680 C ALA A 230 26.327 15.297 28.961 1.00 36.19 C ANISOU 1680 C ALA A 230 4477 5265 4007 -141 451 -55 C ATOM 1681 O ALA A 230 26.473 16.454 29.343 1.00 37.72 O ANISOU 1681 O ALA A 230 4724 5391 4215 -178 552 27 O ATOM 1682 CB ALA A 230 28.220 13.775 28.198 1.00 36.47 C ANISOU 1682 CB ALA A 230 4444 5356 4057 -145 432 -36 C ATOM 1683 N LYS A 231 25.290 14.906 28.232 1.00 36.50 N ANISOU 1683 N LYS A 231 4578 5323 3967 -35 365 -41 N ATOM 1684 CA LYS A 231 24.268 15.829 27.767 1.00 36.67 C ANISOU 1684 CA LYS A 231 4547 5334 4052 -68 269 -113 C ATOM 1685 C LYS A 231 23.434 16.405 28.929 1.00 36.03 C ANISOU 1685 C LYS A 231 4509 5229 3951 -136 258 -56 C ATOM 1686 O LYS A 231 23.016 17.553 28.896 1.00 35.24 O ANISOU 1686 O LYS A 231 4460 5152 3774 -165 186 24 O ATOM 1687 CB LYS A 231 23.357 15.110 26.784 1.00 37.13 C ANISOU 1687 CB LYS A 231 4578 5438 4089 -87 258 -126 C ATOM 1688 CG LYS A 231 22.467 16.012 26.003 1.00 40.42 C ANISOU 1688 CG LYS A 231 5003 5752 4603 23 -5 -113 C ATOM 1689 CD LYS A 231 21.778 15.204 24.871 1.00 43.99 C ANISOU 1689 CD LYS A 231 5445 5963 5306 -137 -242 -267 C ATOM 1690 CE LYS A 231 22.738 14.852 23.734 1.00 45.81 C ANISOU 1690 CE LYS A 231 5711 6245 5448 -95 -57 -100 C ATOM 1691 NZ LYS A 231 23.083 16.023 22.881 1.00 44.77 N1+ ANISOU 1691 NZ LYS A 231 5508 6077 5425 -266 -205 -216 N1+ ATOM 1692 N ALA A 232 23.212 15.602 29.961 1.00 35.84 N ANISOU 1692 N ALA A 232 4526 5128 3962 -174 212 -42 N ATOM 1693 CA ALA A 232 22.434 16.056 31.099 1.00 36.05 C ANISOU 1693 CA ALA A 232 4582 5120 3993 -303 259 -34 C ATOM 1694 C ALA A 232 23.162 17.228 31.766 1.00 36.35 C ANISOU 1694 C ALA A 232 4661 5092 4059 -329 244 9 C ATOM 1695 O ALA A 232 22.537 18.220 32.138 1.00 36.12 O ANISOU 1695 O ALA A 232 4668 4993 4060 -524 142 -23 O ATOM 1696 CB ALA A 232 22.218 14.903 32.083 1.00 36.03 C ANISOU 1696 CB ALA A 232 4597 5081 4012 -248 254 23 C ATOM 1697 N LYS A 233 24.486 17.119 31.873 1.00 37.62 N ANISOU 1697 N LYS A 233 4838 5217 4238 -368 297 19 N ATOM 1698 CA LYS A 233 25.284 18.190 32.450 1.00 39.72 C ANISOU 1698 CA LYS A 233 5009 5409 4673 -328 256 24 C ATOM 1699 C LYS A 233 25.308 19.436 31.542 1.00 39.85 C ANISOU 1699 C LYS A 233 5119 5342 4678 -355 346 2 C ATOM 1700 O LYS A 233 25.159 20.553 32.023 1.00 39.69 O ANISOU 1700 O LYS A 233 5100 5278 4702 -508 452 -38 O ATOM 1701 CB LYS A 233 26.695 17.687 32.753 1.00 40.02 C ANISOU 1701 CB LYS A 233 5035 5511 4657 -231 162 -20 C ATOM 1702 CG LYS A 233 26.756 16.600 33.830 1.00 41.12 C ANISOU 1702 CG LYS A 233 5035 5396 5190 -238 151 80 C ATOM 1703 CD LYS A 233 28.139 15.904 33.811 1.00 42.07 C ANISOU 1703 CD LYS A 233 5194 5644 5145 -186 182 -10 C ATOM 1704 CE LYS A 233 28.220 14.760 34.809 1.00 44.15 C ANISOU 1704 CE LYS A 233 5487 5866 5419 -193 -10 121 C ATOM 1705 NZ LYS A 233 28.596 15.205 36.184 1.00 44.89 N1+ ANISOU 1705 NZ LYS A 233 5652 5828 5574 -303 267 -183 N1+ ATOM 1706 N GLU A 234 25.474 19.237 30.230 1.00 39.96 N ANISOU 1706 N GLU A 234 5172 5348 4661 -387 269 28 N ATOM 1707 CA GLU A 234 25.395 20.324 29.247 1.00 40.65 C ANISOU 1707 CA GLU A 234 5262 5414 4766 -373 257 52 C ATOM 1708 C GLU A 234 24.137 21.178 29.430 1.00 40.05 C ANISOU 1708 C GLU A 234 5279 5288 4649 -430 273 24 C ATOM 1709 O GLU A 234 24.192 22.407 29.353 1.00 40.18 O ANISOU 1709 O GLU A 234 5306 5287 4672 -563 377 135 O ATOM 1710 CB GLU A 234 25.440 19.738 27.831 1.00 40.65 C ANISOU 1710 CB GLU A 234 5265 5486 4693 -319 247 82 C ATOM 1711 CG GLU A 234 25.507 20.768 26.699 1.00 42.29 C ANISOU 1711 CG GLU A 234 5506 5530 5031 -258 240 172 C ATOM 1712 CD GLU A 234 25.369 20.125 25.320 1.00 43.12 C ANISOU 1712 CD GLU A 234 5615 5713 5055 -319 121 111 C ATOM 1713 OE1 GLU A 234 25.365 18.877 25.225 1.00 47.25 O ANISOU 1713 OE1 GLU A 234 6252 6037 5663 -343 129 299 O ATOM 1714 OE2 GLU A 234 25.286 20.865 24.315 1.00 46.83 O1- ANISOU 1714 OE2 GLU A 234 5910 6315 5568 -345 -182 324 O1- ATOM 1715 N VAL A 235 23.008 20.532 29.729 1.00 38.41 N ANISOU 1715 N VAL A 235 5095 5188 4308 -478 304 16 N ATOM 1716 CA VAL A 235 21.744 21.255 29.770 1.00 38.21 C ANISOU 1716 CA VAL A 235 5168 5108 4239 -439 236 -12 C ATOM 1717 C VAL A 235 21.355 21.730 31.183 1.00 38.21 C ANISOU 1717 C VAL A 235 5102 5156 4258 -393 232 -11 C ATOM 1718 O VAL A 235 20.341 22.411 31.347 1.00 38.55 O ANISOU 1718 O VAL A 235 5226 5209 4212 -423 274 -43 O ATOM 1719 CB VAL A 235 20.582 20.470 29.074 1.00 38.24 C ANISOU 1719 CB VAL A 235 5218 5122 4188 -465 157 16 C ATOM 1720 CG1 VAL A 235 21.006 20.043 27.664 1.00 38.56 C ANISOU 1720 CG1 VAL A 235 5294 5087 4270 -269 307 3 C ATOM 1721 CG2 VAL A 235 20.151 19.264 29.882 1.00 37.85 C ANISOU 1721 CG2 VAL A 235 5235 4996 4150 -510 280 -61 C ATOM 1722 N GLY A 236 22.165 21.365 32.173 1.00 37.34 N ANISOU 1722 N GLY A 236 4951 5058 4175 -513 218 -52 N ATOM 1723 CA GLY A 236 22.051 21.934 33.514 1.00 37.14 C ANISOU 1723 CA GLY A 236 4827 4998 4286 -473 181 -58 C ATOM 1724 C GLY A 236 22.201 21.056 34.736 1.00 36.24 C ANISOU 1724 C GLY A 236 4618 4903 4247 -505 107 -31 C ATOM 1725 O GLY A 236 22.213 21.587 35.859 1.00 35.99 O ANISOU 1725 O GLY A 236 4687 4749 4238 -643 233 21 O ATOM 1726 N ALA A 237 22.337 19.735 34.559 1.00 35.96 N ANISOU 1726 N ALA A 237 4445 4970 4246 -538 45 31 N ATOM 1727 CA ALA A 237 22.554 18.838 35.704 1.00 35.41 C ANISOU 1727 CA ALA A 237 4293 4970 4191 -524 37 67 C ATOM 1728 C ALA A 237 23.853 19.198 36.409 1.00 35.40 C ANISOU 1728 C ALA A 237 4179 4991 4278 -512 67 77 C ATOM 1729 O ALA A 237 24.884 19.443 35.761 1.00 35.56 O ANISOU 1729 O ALA A 237 4193 5073 4244 -502 55 142 O ATOM 1730 CB ALA A 237 22.567 17.393 35.297 1.00 34.94 C ANISOU 1730 CB ALA A 237 4174 4926 4174 -532 64 155 C ATOM 1731 N THR A 238 23.795 19.260 37.736 1.00 35.85 N ANISOU 1731 N THR A 238 4194 5045 4379 -515 67 -25 N ATOM 1732 CA THR A 238 24.953 19.623 38.521 1.00 36.17 C ANISOU 1732 CA THR A 238 4167 5094 4481 -503 29 -55 C ATOM 1733 C THR A 238 25.763 18.393 38.920 1.00 37.30 C ANISOU 1733 C THR A 238 4300 5210 4661 -429 -34 -21 C ATOM 1734 O THR A 238 26.967 18.489 39.195 1.00 37.35 O ANISOU 1734 O THR A 238 4120 5150 4919 -329 13 -22 O ATOM 1735 CB THR A 238 24.573 20.462 39.746 1.00 36.43 C ANISOU 1735 CB THR A 238 4234 5045 4562 -514 88 -56 C ATOM 1736 CG2 THR A 238 23.925 21.790 39.330 1.00 35.69 C ANISOU 1736 CG2 THR A 238 4079 4975 4504 -551 1 29 C ATOM 1737 OG1 THR A 238 23.659 19.727 40.561 1.00 35.16 O ANISOU 1737 OG1 THR A 238 3858 5282 4217 -708 -79 -259 O ATOM 1738 N GLU A 239 25.083 17.243 38.975 1.00 36.97 N ANISOU 1738 N GLU A 239 4244 5209 4592 -418 -156 -141 N ATOM 1739 CA GLU A 239 25.701 15.945 39.228 1.00 37.90 C ANISOU 1739 CA GLU A 239 4414 5391 4595 -293 -95 -149 C ATOM 1740 C GLU A 239 24.811 14.893 38.607 1.00 38.02 C ANISOU 1740 C GLU A 239 4407 5506 4531 -216 -139 -149 C ATOM 1741 O GLU A 239 23.589 15.119 38.451 1.00 37.56 O ANISOU 1741 O GLU A 239 4121 5707 4442 -279 -166 -261 O ATOM 1742 CB GLU A 239 25.798 15.630 40.733 1.00 38.79 C ANISOU 1742 CB GLU A 239 4701 5371 4664 -189 -290 -94 C ATOM 1743 CG GLU A 239 26.362 16.707 41.653 1.00 42.13 C ANISOU 1743 CG GLU A 239 5135 5513 5357 -172 -105 -163 C ATOM 1744 CD GLU A 239 25.501 16.869 42.891 1.00 45.41 C ANISOU 1744 CD GLU A 239 5599 5931 5722 -121 -5 -104 C ATOM 1745 OE1 GLU A 239 25.546 15.975 43.756 1.00 47.70 O ANISOU 1745 OE1 GLU A 239 5902 6441 5780 -156 -113 68 O ATOM 1746 OE2 GLU A 239 24.758 17.881 42.977 1.00 46.28 O1- ANISOU 1746 OE2 GLU A 239 5327 6261 5996 117 77 -301 O1- ATOM 1747 N CYS A 240 25.399 13.735 38.310 1.00 37.38 N ANISOU 1747 N CYS A 240 4374 5499 4327 -231 -83 -249 N ATOM 1748 CA CYS A 240 24.636 12.592 37.828 1.00 37.96 C ANISOU 1748 CA CYS A 240 4426 5572 4425 -218 -33 -115 C ATOM 1749 C CYS A 240 24.963 11.362 38.626 1.00 37.91 C ANISOU 1749 C CYS A 240 4370 5578 4454 -100 -96 -100 C ATOM 1750 O CYS A 240 26.124 11.141 39.005 1.00 38.60 O ANISOU 1750 O CYS A 240 4270 5698 4696 -112 -145 -5 O ATOM 1751 CB CYS A 240 24.925 12.319 36.359 1.00 37.56 C ANISOU 1751 CB CYS A 240 4422 5501 4345 -222 -7 -198 C ATOM 1752 SG CYS A 240 24.106 13.429 35.264 1.00 41.17 S ANISOU 1752 SG CYS A 240 5266 6062 4313 -356 55 -30 S ATOM 1753 N VAL A 241 23.928 10.562 38.860 1.00 36.80 N ANISOU 1753 N VAL A 241 4201 5474 4305 -33 -103 -72 N ATOM 1754 CA VAL A 241 23.999 9.369 39.667 1.00 37.24 C ANISOU 1754 CA VAL A 241 4307 5392 4449 52 -157 -87 C ATOM 1755 C VAL A 241 23.548 8.151 38.877 1.00 36.55 C ANISOU 1755 C VAL A 241 4199 5287 4400 168 -97 -93 C ATOM 1756 O VAL A 241 22.485 8.183 38.274 1.00 34.73 O ANISOU 1756 O VAL A 241 4019 4983 4191 223 -152 -281 O ATOM 1757 CB VAL A 241 23.102 9.541 40.915 1.00 37.85 C ANISOU 1757 CB VAL A 241 4399 5482 4500 4 -127 -26 C ATOM 1758 CG1 VAL A 241 22.878 8.205 41.612 1.00 39.50 C ANISOU 1758 CG1 VAL A 241 4663 5612 4731 33 -300 157 C ATOM 1759 CG2 VAL A 241 23.712 10.565 41.871 1.00 40.18 C ANISOU 1759 CG2 VAL A 241 5021 5596 4649 0 -195 -5 C ATOM 1760 N ASN A 242 24.369 7.095 38.880 1.00 35.78 N ANISOU 1760 N ASN A 242 4109 5155 4331 276 -37 -24 N ATOM 1761 CA ASN A 242 23.999 5.813 38.302 1.00 36.94 C ANISOU 1761 CA ASN A 242 4165 5274 4595 370 0 -36 C ATOM 1762 C ASN A 242 23.686 4.844 39.432 1.00 37.02 C ANISOU 1762 C ASN A 242 4165 5291 4608 374 -122 5 C ATOM 1763 O ASN A 242 24.574 4.473 40.201 1.00 36.65 O ANISOU 1763 O ASN A 242 3967 5314 4643 528 -159 3 O ATOM 1764 CB ASN A 242 25.119 5.271 37.389 1.00 37.56 C ANISOU 1764 CB ASN A 242 4307 5299 4665 388 37 -26 C ATOM 1765 CG ASN A 242 24.828 3.868 36.850 1.00 37.00 C ANISOU 1765 CG ASN A 242 4246 5148 4663 567 181 -166 C ATOM 1766 ND2 ASN A 242 25.752 3.341 36.052 1.00 39.52 N ANISOU 1766 ND2 ASN A 242 4517 5763 4735 682 428 -377 N ATOM 1767 OD1 ASN A 242 23.805 3.262 37.152 1.00 36.59 O ANISOU 1767 OD1 ASN A 242 4185 4588 5127 775 -167 -126 O ATOM 1768 N PRO A 243 22.411 4.466 39.594 1.00 37.34 N ANISOU 1768 N PRO A 243 4207 5298 4682 329 -243 -39 N ATOM 1769 CA PRO A 243 22.040 3.580 40.697 1.00 37.90 C ANISOU 1769 CA PRO A 243 4362 5276 4760 284 -301 8 C ATOM 1770 C PRO A 243 22.809 2.266 40.737 1.00 39.50 C ANISOU 1770 C PRO A 243 4671 5327 5008 224 -327 38 C ATOM 1771 O PRO A 243 22.920 1.686 41.808 1.00 40.68 O ANISOU 1771 O PRO A 243 4931 5486 5038 217 -459 8 O ATOM 1772 CB PRO A 243 20.559 3.284 40.441 1.00 38.27 C ANISOU 1772 CB PRO A 243 4381 5313 4845 188 -269 23 C ATOM 1773 CG PRO A 243 20.090 4.374 39.612 1.00 38.37 C ANISOU 1773 CG PRO A 243 4425 5320 4833 248 -243 74 C ATOM 1774 CD PRO A 243 21.246 4.854 38.783 1.00 35.81 C ANISOU 1774 CD PRO A 243 3947 5197 4461 434 -242 -90 C ATOM 1775 N GLN A 244 23.305 1.801 39.592 1.00 40.05 N ANISOU 1775 N GLN A 244 4796 5288 5131 223 -375 2 N ATOM 1776 CA GLN A 244 24.064 0.552 39.510 1.00 42.30 C ANISOU 1776 CA GLN A 244 5181 5443 5444 197 -287 -56 C ATOM 1777 C GLN A 244 25.457 0.679 40.121 1.00 42.67 C ANISOU 1777 C GLN A 244 5181 5488 5543 193 -322 26 C ATOM 1778 O GLN A 244 26.106 -0.333 40.401 1.00 43.16 O ANISOU 1778 O GLN A 244 5307 5475 5616 269 -308 71 O ATOM 1779 CB GLN A 244 24.141 0.070 38.057 1.00 42.24 C ANISOU 1779 CB GLN A 244 5167 5422 5459 243 -200 -37 C ATOM 1780 CG GLN A 244 22.804 -0.385 37.535 1.00 43.47 C ANISOU 1780 CG GLN A 244 5567 5461 5485 237 -301 -134 C ATOM 1781 CD GLN A 244 22.852 -0.919 36.104 1.00 43.75 C ANISOU 1781 CD GLN A 244 5598 5404 5618 242 -197 -256 C ATOM 1782 NE2 GLN A 244 23.936 -0.645 35.384 1.00 44.59 N ANISOU 1782 NE2 GLN A 244 5981 5249 5712 402 27 -523 N ATOM 1783 OE1 GLN A 244 21.901 -1.539 35.652 1.00 48.15 O ANISOU 1783 OE1 GLN A 244 6062 5731 6500 224 -197 -494 O ATOM 1784 N ASP A 245 25.910 1.915 40.320 1.00 42.31 N ANISOU 1784 N ASP A 245 5105 5466 5504 138 -345 68 N ATOM 1785 CA ASP A 245 27.185 2.183 40.995 1.00 42.57 C ANISOU 1785 CA ASP A 245 5071 5523 5580 29 -315 79 C ATOM 1786 C ASP A 245 27.133 1.910 42.496 1.00 42.33 C ANISOU 1786 C ASP A 245 5075 5490 5518 3 -348 77 C ATOM 1787 O ASP A 245 28.180 1.908 43.157 1.00 42.27 O ANISOU 1787 O ASP A 245 5004 5499 5554 -20 -411 147 O ATOM 1788 CB ASP A 245 27.597 3.641 40.776 1.00 43.08 C ANISOU 1788 CB ASP A 245 5116 5568 5683 10 -290 73 C ATOM 1789 CG ASP A 245 28.226 3.887 39.407 1.00 44.10 C ANISOU 1789 CG ASP A 245 5244 5701 5809 -3 -270 103 C ATOM 1790 OD1 ASP A 245 28.338 2.947 38.593 1.00 45.64 O ANISOU 1790 OD1 ASP A 245 5158 6139 6043 129 -148 -50 O ATOM 1791 OD2 ASP A 245 28.624 5.043 39.147 1.00 44.95 O1- ANISOU 1791 OD2 ASP A 245 5145 5719 6212 -51 -275 265 O1- ATOM 1792 N TYR A 246 25.933 1.686 43.042 1.00 42.27 N ANISOU 1792 N TYR A 246 5078 5504 5475 -37 -369 32 N ATOM 1793 CA TYR A 246 25.730 1.630 44.505 1.00 42.85 C ANISOU 1793 CA TYR A 246 5216 5548 5518 -56 -357 84 C ATOM 1794 C TYR A 246 25.326 0.296 45.067 1.00 44.33 C ANISOU 1794 C TYR A 246 5480 5705 5655 -96 -362 77 C ATOM 1795 O TYR A 246 24.697 -0.525 44.381 1.00 45.00 O ANISOU 1795 O TYR A 246 5600 5757 5737 -112 -483 121 O ATOM 1796 CB TYR A 246 24.690 2.660 44.941 1.00 42.52 C ANISOU 1796 CB TYR A 246 5169 5516 5469 -118 -221 87 C ATOM 1797 CG TYR A 246 25.157 4.057 44.718 1.00 42.35 C ANISOU 1797 CG TYR A 246 5060 5482 5548 -83 -240 77 C ATOM 1798 CD1 TYR A 246 25.036 4.667 43.474 1.00 41.61 C ANISOU 1798 CD1 TYR A 246 4944 5433 5431 29 -149 54 C ATOM 1799 CD2 TYR A 246 25.763 4.763 45.747 1.00 41.56 C ANISOU 1799 CD2 TYR A 246 5105 5396 5289 -9 -39 -55 C ATOM 1800 CE1 TYR A 246 25.500 5.961 43.281 1.00 41.90 C ANISOU 1800 CE1 TYR A 246 4942 5392 5586 40 -91 221 C ATOM 1801 CE2 TYR A 246 26.218 6.019 45.566 1.00 42.03 C ANISOU 1801 CE2 TYR A 246 5043 5436 5487 57 -161 99 C ATOM 1802 CZ TYR A 246 26.087 6.632 44.346 1.00 42.81 C ANISOU 1802 CZ TYR A 246 5183 5495 5588 -42 -7 103 C ATOM 1803 OH TYR A 246 26.566 7.921 44.238 1.00 43.77 O ANISOU 1803 OH TYR A 246 4962 5565 6103 -103 65 140 O ATOM 1804 N LYS A 247 25.681 0.101 46.337 1.00 45.36 N ANISOU 1804 N LYS A 247 5655 5823 5755 -48 -402 82 N ATOM 1805 CA LYS A 247 25.279 -1.057 47.102 1.00 46.99 C ANISOU 1805 CA LYS A 247 5898 5987 5968 -97 -277 84 C ATOM 1806 C LYS A 247 24.019 -0.810 47.914 1.00 47.88 C ANISOU 1806 C LYS A 247 6056 6070 6064 -90 -199 73 C ATOM 1807 O LYS A 247 23.395 -1.764 48.393 1.00 49.07 O ANISOU 1807 O LYS A 247 6155 6175 6312 -139 -143 32 O ATOM 1808 CB LYS A 247 26.408 -1.489 48.041 1.00 47.33 C ANISOU 1808 CB LYS A 247 5983 5994 6007 -58 -332 132 C ATOM 1809 CG LYS A 247 27.117 -2.738 47.616 1.00 48.29 C ANISOU 1809 CG LYS A 247 6065 6146 6135 44 -317 114 C ATOM 1810 CD LYS A 247 28.287 -3.060 48.552 1.00 50.06 C ANISOU 1810 CD LYS A 247 6325 6227 6467 1 -462 149 C ATOM 1811 CE LYS A 247 29.596 -2.786 47.843 1.00 50.80 C ANISOU 1811 CE LYS A 247 6407 6284 6607 87 -276 163 C ATOM 1812 NZ LYS A 247 30.714 -2.488 48.783 1.00 52.63 N1+ ANISOU 1812 NZ LYS A 247 6875 6395 6725 -6 -397 109 N1+ ATOM 1813 N LYS A 248 23.665 0.456 48.112 1.00 48.59 N ANISOU 1813 N LYS A 248 6183 6151 6126 -96 -132 107 N ATOM 1814 CA LYS A 248 22.422 0.784 48.805 1.00 48.74 C ANISOU 1814 CA LYS A 248 6202 6180 6136 -122 -96 89 C ATOM 1815 C LYS A 248 21.346 1.303 47.861 1.00 48.72 C ANISOU 1815 C LYS A 248 6191 6194 6122 -136 -44 55 C ATOM 1816 O LYS A 248 21.674 1.804 46.774 1.00 48.72 O ANISOU 1816 O LYS A 248 6229 6221 6060 -208 -16 44 O ATOM 1817 CB LYS A 248 22.646 1.751 49.973 1.00 49.27 C ANISOU 1817 CB LYS A 248 6293 6190 6236 -146 -97 94 C ATOM 1818 CG LYS A 248 23.475 3.000 49.702 1.00 49.75 C ANISOU 1818 CG LYS A 248 6388 6134 6379 -145 -58 80 C ATOM 1819 CD LYS A 248 23.788 3.646 51.060 1.00 51.26 C ANISOU 1819 CD LYS A 248 6591 6402 6483 -154 -104 92 C ATOM 1820 CE LYS A 248 23.905 5.160 50.970 1.00 52.40 C ANISOU 1820 CE LYS A 248 6828 6385 6697 -124 7 -1 C ATOM 1821 NZ LYS A 248 25.033 5.553 50.067 1.00 52.81 N1+ ANISOU 1821 NZ LYS A 248 6794 6422 6848 -183 87 37 N1+ ATOM 1822 N PRO A 249 20.058 1.162 48.262 1.00 47.98 N ANISOU 1822 N PRO A 249 6035 6161 6033 -162 -29 50 N ATOM 1823 CA PRO A 249 18.958 1.690 47.470 1.00 47.62 C ANISOU 1823 CA PRO A 249 5955 6139 6000 -162 -6 13 C ATOM 1824 C PRO A 249 19.160 3.147 47.133 1.00 46.38 C ANISOU 1824 C PRO A 249 5727 6076 5817 -156 -19 26 C ATOM 1825 O PRO A 249 19.626 3.950 47.963 1.00 46.13 O ANISOU 1825 O PRO A 249 5633 6137 5754 -180 -38 88 O ATOM 1826 CB PRO A 249 17.743 1.526 48.384 1.00 47.98 C ANISOU 1826 CB PRO A 249 6011 6177 6040 -149 -10 26 C ATOM 1827 CG PRO A 249 18.101 0.423 49.271 1.00 48.67 C ANISOU 1827 CG PRO A 249 6128 6200 6163 -125 -4 46 C ATOM 1828 CD PRO A 249 19.571 0.494 49.486 1.00 48.31 C ANISOU 1828 CD PRO A 249 6059 6184 6110 -144 5 29 C ATOM 1829 N ILE A 250 18.801 3.468 45.908 1.00 45.27 N ANISOU 1829 N ILE A 250 5462 6046 5691 -157 -52 -62 N ATOM 1830 CA ILE A 250 18.931 4.805 45.372 1.00 44.67 C ANISOU 1830 CA ILE A 250 5359 6020 5594 -153 -81 -52 C ATOM 1831 C ILE A 250 18.237 5.888 46.214 1.00 43.37 C ANISOU 1831 C ILE A 250 5138 5947 5393 -176 -53 -77 C ATOM 1832 O ILE A 250 18.776 6.969 46.333 1.00 42.64 O ANISOU 1832 O ILE A 250 4895 5995 5310 -165 -13 -66 O ATOM 1833 CB ILE A 250 18.479 4.861 43.885 1.00 45.31 C ANISOU 1833 CB ILE A 250 5529 6051 5633 -141 -85 -63 C ATOM 1834 CG1 ILE A 250 18.741 6.240 43.263 1.00 46.14 C ANISOU 1834 CG1 ILE A 250 5676 6102 5753 -97 -112 52 C ATOM 1835 CG2 ILE A 250 17.011 4.450 43.733 1.00 46.44 C ANISOU 1835 CG2 ILE A 250 5607 6212 5825 -128 -97 -9 C ATOM 1836 CD1 ILE A 250 20.170 6.516 42.979 1.00 45.32 C ANISOU 1836 CD1 ILE A 250 5660 5932 5625 -183 -290 9 C ATOM 1837 N GLN A 251 17.063 5.624 46.808 1.00 43.23 N ANISOU 1837 N GLN A 251 5114 5900 5409 -260 -85 -108 N ATOM 1838 CA GLN A 251 16.393 6.712 47.539 1.00 42.58 C ANISOU 1838 CA GLN A 251 5009 5846 5324 -276 -99 -162 C ATOM 1839 C GLN A 251 17.215 7.143 48.766 1.00 42.23 C ANISOU 1839 C GLN A 251 5000 5757 5286 -295 -118 -148 C ATOM 1840 O GLN A 251 17.199 8.309 49.166 1.00 42.57 O ANISOU 1840 O GLN A 251 5036 5776 5361 -330 -130 -223 O ATOM 1841 CB GLN A 251 14.952 6.375 47.951 1.00 43.12 C ANISOU 1841 CB GLN A 251 5061 5921 5402 -245 -62 -157 C ATOM 1842 CG GLN A 251 14.823 5.313 49.022 1.00 44.36 C ANISOU 1842 CG GLN A 251 5220 5949 5686 -157 -89 -81 C ATOM 1843 CD GLN A 251 14.421 3.960 48.459 1.00 45.82 C ANISOU 1843 CD GLN A 251 5443 6092 5874 -35 -158 -172 C ATOM 1844 NE2 GLN A 251 13.684 3.185 49.250 1.00 48.09 N ANISOU 1844 NE2 GLN A 251 5833 6129 6308 -174 -19 -152 N ATOM 1845 OE1 GLN A 251 14.768 3.616 47.335 1.00 46.37 O ANISOU 1845 OE1 GLN A 251 5235 6304 6079 78 -59 -361 O ATOM 1846 N GLU A 252 17.918 6.189 49.350 1.00 41.54 N ANISOU 1846 N GLU A 252 4920 5686 5176 -289 -165 -161 N ATOM 1847 CA GLU A 252 18.776 6.464 50.493 1.00 41.50 C ANISOU 1847 CA GLU A 252 5050 5639 5078 -323 -168 -165 C ATOM 1848 C GLU A 252 19.982 7.293 50.067 1.00 40.64 C ANISOU 1848 C GLU A 252 4996 5553 4892 -274 -82 -166 C ATOM 1849 O GLU A 252 20.350 8.268 50.741 1.00 39.61 O ANISOU 1849 O GLU A 252 4929 5470 4649 -333 -145 -203 O ATOM 1850 CB GLU A 252 19.232 5.156 51.120 1.00 42.49 C ANISOU 1850 CB GLU A 252 5160 5673 5309 -297 -186 -173 C ATOM 1851 CG GLU A 252 19.493 5.241 52.603 1.00 45.82 C ANISOU 1851 CG GLU A 252 5711 6042 5657 -174 -175 -88 C ATOM 1852 CD GLU A 252 20.030 3.947 53.163 1.00 49.44 C ANISOU 1852 CD GLU A 252 6233 6224 6328 -134 -205 84 C ATOM 1853 OE1 GLU A 252 19.471 2.878 52.824 1.00 50.65 O ANISOU 1853 OE1 GLU A 252 6357 6406 6481 -162 -155 -149 O ATOM 1854 OE2 GLU A 252 21.014 4.004 53.938 1.00 50.30 O1- ANISOU 1854 OE2 GLU A 252 6488 6184 6436 -316 -436 -24 O1- ATOM 1855 N VAL A 253 20.599 6.903 48.952 1.00 38.99 N ANISOU 1855 N VAL A 253 4800 5414 4598 -317 -71 -134 N ATOM 1856 CA VAL A 253 21.712 7.653 48.378 1.00 38.32 C ANISOU 1856 CA VAL A 253 4614 5368 4578 -210 -50 -106 C ATOM 1857 C VAL A 253 21.281 9.085 48.150 1.00 36.83 C ANISOU 1857 C VAL A 253 4440 5226 4326 -211 -53 -50 C ATOM 1858 O VAL A 253 21.996 10.006 48.499 1.00 36.95 O ANISOU 1858 O VAL A 253 4412 5317 4308 -85 -159 -92 O ATOM 1859 CB VAL A 253 22.149 7.044 47.021 1.00 38.14 C ANISOU 1859 CB VAL A 253 4648 5318 4524 -217 -24 -79 C ATOM 1860 CG1 VAL A 253 23.191 7.939 46.322 1.00 37.61 C ANISOU 1860 CG1 VAL A 253 4290 5371 4628 -215 36 45 C ATOM 1861 CG2 VAL A 253 22.675 5.642 47.205 1.00 38.86 C ANISOU 1861 CG2 VAL A 253 4690 5282 4793 -297 -233 -67 C ATOM 1862 N LEU A 254 20.090 9.294 47.589 1.00 36.04 N ANISOU 1862 N LEU A 254 4290 5174 4226 -279 20 -40 N ATOM 1863 CA LEU A 254 19.654 10.668 47.320 1.00 35.96 C ANISOU 1863 CA LEU A 254 4286 5157 4220 -246 33 -114 C ATOM 1864 C LEU A 254 19.267 11.441 48.568 1.00 36.04 C ANISOU 1864 C LEU A 254 4283 5144 4266 -299 74 -69 C ATOM 1865 O LEU A 254 19.456 12.676 48.641 1.00 35.62 O ANISOU 1865 O LEU A 254 4227 5094 4210 -331 36 -64 O ATOM 1866 CB LEU A 254 18.519 10.672 46.313 1.00 36.11 C ANISOU 1866 CB LEU A 254 4310 5128 4281 -189 60 -52 C ATOM 1867 CG LEU A 254 18.954 10.169 44.928 1.00 37.93 C ANISOU 1867 CG LEU A 254 4771 5320 4320 -240 14 -88 C ATOM 1868 CD1 LEU A 254 17.719 9.840 44.151 1.00 39.93 C ANISOU 1868 CD1 LEU A 254 4879 5403 4886 -113 -167 -12 C ATOM 1869 CD2 LEU A 254 19.846 11.164 44.198 1.00 38.51 C ANISOU 1869 CD2 LEU A 254 5194 5327 4109 -184 206 -308 C ATOM 1870 N THR A 255 18.683 10.735 49.532 1.00 36.27 N ANISOU 1870 N THR A 255 4442 5173 4164 -265 42 -71 N ATOM 1871 CA THR A 255 18.303 11.387 50.777 1.00 37.08 C ANISOU 1871 CA THR A 255 4551 5271 4265 -292 105 -50 C ATOM 1872 C THR A 255 19.549 11.869 51.522 1.00 37.06 C ANISOU 1872 C THR A 255 4657 5228 4197 -359 138 -5 C ATOM 1873 O THR A 255 19.548 12.968 52.075 1.00 38.21 O ANISOU 1873 O THR A 255 4846 5346 4323 -485 277 18 O ATOM 1874 CB THR A 255 17.414 10.467 51.619 1.00 36.79 C ANISOU 1874 CB THR A 255 4520 5261 4195 -311 76 -80 C ATOM 1875 CG2 THR A 255 16.994 11.146 52.933 1.00 37.93 C ANISOU 1875 CG2 THR A 255 4769 5365 4277 -78 112 -22 C ATOM 1876 OG1 THR A 255 16.237 10.175 50.836 1.00 37.19 O ANISOU 1876 OG1 THR A 255 4354 5228 4546 -270 -158 147 O ATOM 1877 N GLU A 256 20.608 11.059 51.500 1.00 38.31 N ANISOU 1877 N GLU A 256 4768 5345 4442 -340 120 -56 N ATOM 1878 CA GLU A 256 21.878 11.391 52.150 1.00 39.94 C ANISOU 1878 CA GLU A 256 4983 5493 4697 -326 -2 -92 C ATOM 1879 C GLU A 256 22.566 12.535 51.387 1.00 39.03 C ANISOU 1879 C GLU A 256 4861 5417 4550 -335 -63 -122 C ATOM 1880 O GLU A 256 23.090 13.478 51.993 1.00 38.70 O ANISOU 1880 O GLU A 256 4797 5449 4457 -384 -158 -146 O ATOM 1881 CB GLU A 256 22.772 10.149 52.185 1.00 40.35 C ANISOU 1881 CB GLU A 256 5098 5492 4741 -268 -39 -29 C ATOM 1882 CG GLU A 256 23.886 10.115 53.231 1.00 43.75 C ANISOU 1882 CG GLU A 256 5340 5735 5545 -265 -118 -103 C ATOM 1883 CD GLU A 256 24.665 8.794 53.208 1.00 44.49 C ANISOU 1883 CD GLU A 256 5441 5783 5680 -230 -92 -68 C ATOM 1884 OE1 GLU A 256 24.033 7.708 53.333 1.00 49.78 O ANISOU 1884 OE1 GLU A 256 6149 5957 6807 -315 52 143 O ATOM 1885 OE2 GLU A 256 25.917 8.834 53.083 1.00 50.87 O1- ANISOU 1885 OE2 GLU A 256 6028 6384 6914 -337 384 -175 O1- ATOM 1886 N MET A 257 22.544 12.461 50.054 1.00 38.24 N ANISOU 1886 N MET A 257 4666 5450 4411 -323 -83 -166 N ATOM 1887 CA MET A 257 23.123 13.509 49.219 1.00 38.32 C ANISOU 1887 CA MET A 257 4675 5478 4405 -384 18 -156 C ATOM 1888 C MET A 257 22.500 14.882 49.430 1.00 37.89 C ANISOU 1888 C MET A 257 4612 5426 4357 -339 -10 -164 C ATOM 1889 O MET A 257 23.183 15.887 49.280 1.00 38.51 O ANISOU 1889 O MET A 257 4688 5425 4519 -394 180 -142 O ATOM 1890 CB MET A 257 22.994 13.173 47.735 1.00 38.98 C ANISOU 1890 CB MET A 257 4836 5486 4487 -343 112 -172 C ATOM 1891 CG MET A 257 24.008 12.208 47.191 1.00 39.21 C ANISOU 1891 CG MET A 257 4834 5453 4610 -331 193 -94 C ATOM 1892 SD MET A 257 23.492 11.839 45.482 1.00 40.85 S ANISOU 1892 SD MET A 257 5006 5864 4648 -657 358 -241 S ATOM 1893 CE MET A 257 24.103 13.302 44.625 1.00 39.67 C ANISOU 1893 CE MET A 257 5252 5842 3978 -388 186 151 C ATOM 1894 N SER A 258 21.207 14.924 49.773 1.00 36.61 N ANISOU 1894 N SER A 258 4430 5301 4179 -356 -85 -119 N ATOM 1895 CA SER A 258 20.448 16.178 49.818 1.00 36.43 C ANISOU 1895 CA SER A 258 4445 5254 4142 -296 -152 -162 C ATOM 1896 C SER A 258 20.133 16.566 51.257 1.00 37.56 C ANISOU 1896 C SER A 258 4730 5282 4257 -206 -122 -126 C ATOM 1897 O SER A 258 19.208 17.350 51.514 1.00 37.43 O ANISOU 1897 O SER A 258 4790 5249 4180 -286 -104 -221 O ATOM 1898 CB SER A 258 19.132 16.007 49.062 1.00 35.88 C ANISOU 1898 CB SER A 258 4389 5200 4043 -302 -238 -35 C ATOM 1899 OG SER A 258 18.418 14.947 49.661 1.00 33.61 O ANISOU 1899 OG SER A 258 3860 4984 3926 -106 -475 -281 O ATOM 1900 N ASN A 259 20.879 15.962 52.182 1.00 38.57 N ANISOU 1900 N ASN A 259 4967 5345 4340 -198 -116 -157 N ATOM 1901 CA ASN A 259 20.767 16.265 53.601 1.00 39.48 C ANISOU 1901 CA ASN A 259 5144 5373 4480 -144 -55 -76 C ATOM 1902 C ASN A 259 19.294 16.201 54.031 1.00 39.10 C ANISOU 1902 C ASN A 259 5114 5302 4439 -68 -73 -52 C ATOM 1903 O ASN A 259 18.743 17.128 54.647 1.00 40.24 O ANISOU 1903 O ASN A 259 5392 5314 4584 0 -5 -126 O ATOM 1904 CB ASN A 259 21.458 17.603 53.906 1.00 40.62 C ANISOU 1904 CB ASN A 259 5266 5430 4738 -107 -79 -143 C ATOM 1905 CG ASN A 259 22.973 17.558 53.630 1.00 43.31 C ANISOU 1905 CG ASN A 259 5499 5763 5193 -226 -36 -15 C ATOM 1906 ND2 ASN A 259 23.685 16.703 54.354 1.00 45.40 N ANISOU 1906 ND2 ASN A 259 5605 5830 5812 -92 -169 -188 N ATOM 1907 OD1 ASN A 259 23.474 18.248 52.741 1.00 49.43 O ANISOU 1907 OD1 ASN A 259 6210 6268 6300 -476 175 138 O ATOM 1908 N GLY A 260 18.658 15.096 53.652 1.00 37.59 N ANISOU 1908 N GLY A 260 4846 5252 4184 -89 -137 48 N ATOM 1909 CA GLY A 260 17.375 14.697 54.202 1.00 36.36 C ANISOU 1909 CA GLY A 260 4637 5201 3975 -133 -132 102 C ATOM 1910 C GLY A 260 16.233 14.778 53.214 1.00 35.89 C ANISOU 1910 C GLY A 260 4512 5141 3983 -221 -112 177 C ATOM 1911 O GLY A 260 15.082 14.903 53.646 1.00 36.87 O ANISOU 1911 O GLY A 260 4587 5288 4131 -301 -101 245 O ATOM 1912 N GLY A 261 16.552 14.748 51.903 1.00 34.75 N ANISOU 1912 N GLY A 261 4415 5033 3756 -288 -263 133 N ATOM 1913 CA GLY A 261 15.542 14.744 50.838 1.00 33.51 C ANISOU 1913 CA GLY A 261 4313 4781 3635 -411 -277 260 C ATOM 1914 C GLY A 261 15.614 15.923 49.863 1.00 33.18 C ANISOU 1914 C GLY A 261 4337 4715 3553 -530 -295 195 C ATOM 1915 O GLY A 261 16.007 17.031 50.239 1.00 33.10 O ANISOU 1915 O GLY A 261 4436 4671 3467 -528 -286 259 O ATOM 1916 N VAL A 262 15.198 15.699 48.614 1.00 31.84 N ANISOU 1916 N VAL A 262 4096 4477 3524 -645 -256 42 N ATOM 1917 CA VAL A 262 15.181 16.771 47.630 1.00 31.69 C ANISOU 1917 CA VAL A 262 4188 4462 3388 -653 -299 -26 C ATOM 1918 C VAL A 262 13.904 17.626 47.738 1.00 30.40 C ANISOU 1918 C VAL A 262 4142 4268 3139 -694 -196 -124 C ATOM 1919 O VAL A 262 12.890 17.190 48.282 1.00 31.35 O ANISOU 1919 O VAL A 262 4323 4489 3098 -778 -171 32 O ATOM 1920 CB VAL A 262 15.391 16.242 46.169 1.00 30.58 C ANISOU 1920 CB VAL A 262 3986 4238 3393 -661 -185 -19 C ATOM 1921 CG1 VAL A 262 16.696 15.428 46.066 1.00 32.30 C ANISOU 1921 CG1 VAL A 262 4244 4484 3542 -441 -560 -9 C ATOM 1922 CG2 VAL A 262 14.192 15.415 45.691 1.00 31.31 C ANISOU 1922 CG2 VAL A 262 3884 4517 3492 -654 -415 127 C ATOM 1923 N ASP A 263 13.950 18.856 47.229 1.00 30.17 N ANISOU 1923 N ASP A 263 4290 4287 2886 -725 -160 -160 N ATOM 1924 CA ASP A 263 12.766 19.683 47.166 1.00 29.69 C ANISOU 1924 CA ASP A 263 4253 4195 2829 -758 -296 -194 C ATOM 1925 C ASP A 263 11.764 19.177 46.127 1.00 29.39 C ANISOU 1925 C ASP A 263 4239 4187 2739 -643 -213 -216 C ATOM 1926 O ASP A 263 10.591 19.166 46.386 1.00 29.82 O ANISOU 1926 O ASP A 263 4316 4383 2630 -743 -85 -249 O ATOM 1927 CB ASP A 263 13.132 21.132 46.873 1.00 31.75 C ANISOU 1927 CB ASP A 263 4618 4330 3115 -724 -326 -178 C ATOM 1928 CG ASP A 263 14.019 21.715 47.960 1.00 32.81 C ANISOU 1928 CG ASP A 263 4601 4628 3235 -731 -243 -465 C ATOM 1929 OD1 ASP A 263 13.499 21.909 49.091 1.00 35.09 O ANISOU 1929 OD1 ASP A 263 4615 5236 3479 -1161 254 -421 O ATOM 1930 OD2 ASP A 263 15.231 21.905 47.721 1.00 35.86 O1- ANISOU 1930 OD2 ASP A 263 5129 5016 3479 -694 18 -248 O1- ATOM 1931 N PHE A 264 12.266 18.817 44.947 1.00 28.39 N ANISOU 1931 N PHE A 264 4086 4014 2685 -539 -110 -226 N ATOM 1932 CA PHE A 264 11.416 18.404 43.826 1.00 27.50 C ANISOU 1932 CA PHE A 264 3991 3789 2668 -492 -65 -227 C ATOM 1933 C PHE A 264 12.017 17.152 43.203 1.00 27.45 C ANISOU 1933 C PHE A 264 3843 3739 2848 -408 -145 -213 C ATOM 1934 O PHE A 264 13.213 17.106 42.922 1.00 28.51 O ANISOU 1934 O PHE A 264 3838 3774 3220 -669 -139 -410 O ATOM 1935 CB PHE A 264 11.377 19.542 42.787 1.00 28.18 C ANISOU 1935 CB PHE A 264 4130 3704 2871 -306 -73 -218 C ATOM 1936 CG PHE A 264 10.842 20.849 43.351 1.00 26.99 C ANISOU 1936 CG PHE A 264 4185 3325 2745 -456 25 -192 C ATOM 1937 CD1 PHE A 264 9.468 21.027 43.506 1.00 27.14 C ANISOU 1937 CD1 PHE A 264 4305 3071 2935 -240 -13 -22 C ATOM 1938 CD2 PHE A 264 11.706 21.828 43.823 1.00 29.59 C ANISOU 1938 CD2 PHE A 264 4593 3551 3099 -380 182 -115 C ATOM 1939 CE1 PHE A 264 8.944 22.163 44.049 1.00 28.92 C ANISOU 1939 CE1 PHE A 264 4446 3283 3258 -119 14 0 C ATOM 1940 CE2 PHE A 264 11.200 22.983 44.394 1.00 29.72 C ANISOU 1940 CE2 PHE A 264 4442 3548 3299 -311 167 -118 C ATOM 1941 CZ PHE A 264 9.829 23.179 44.505 1.00 27.69 C ANISOU 1941 CZ PHE A 264 4174 3434 2912 -284 -152 116 C ATOM 1942 N SER A 265 11.195 16.158 42.909 1.00 26.78 N ANISOU 1942 N SER A 265 3755 3640 2778 -373 -38 -80 N ATOM 1943 CA SER A 265 11.689 15.036 42.123 1.00 26.34 C ANISOU 1943 CA SER A 265 3556 3658 2792 -290 -106 -118 C ATOM 1944 C SER A 265 10.775 14.786 40.952 1.00 26.83 C ANISOU 1944 C SER A 265 3644 3693 2856 -286 -95 -135 C ATOM 1945 O SER A 265 9.589 15.093 41.007 1.00 26.76 O ANISOU 1945 O SER A 265 3612 3687 2869 -227 -70 -127 O ATOM 1946 CB SER A 265 11.829 13.770 42.957 1.00 27.86 C ANISOU 1946 CB SER A 265 3827 3855 2900 -183 67 -45 C ATOM 1947 OG SER A 265 10.584 13.400 43.535 1.00 29.33 O ANISOU 1947 OG SER A 265 3869 3969 3305 -397 -123 86 O ATOM 1948 N PHE A 266 11.323 14.158 39.927 1.00 26.07 N ANISOU 1948 N PHE A 266 3617 3537 2749 -377 -118 -140 N ATOM 1949 CA PHE A 266 10.553 13.938 38.707 1.00 26.93 C ANISOU 1949 CA PHE A 266 3650 3704 2878 -328 -175 -66 C ATOM 1950 C PHE A 266 10.788 12.522 38.222 1.00 28.10 C ANISOU 1950 C PHE A 266 3725 3707 3242 -276 -134 -137 C ATOM 1951 O PHE A 266 11.958 12.126 38.053 1.00 28.75 O ANISOU 1951 O PHE A 266 3812 3773 3336 -340 2 -74 O ATOM 1952 CB PHE A 266 11.045 14.932 37.615 1.00 26.75 C ANISOU 1952 CB PHE A 266 3647 3615 2900 -378 -27 -50 C ATOM 1953 CG PHE A 266 10.872 16.378 38.008 1.00 26.32 C ANISOU 1953 CG PHE A 266 3609 3550 2841 -529 -33 -94 C ATOM 1954 CD1 PHE A 266 11.863 17.009 38.788 1.00 25.88 C ANISOU 1954 CD1 PHE A 266 3590 3747 2495 -271 -199 -304 C ATOM 1955 CD2 PHE A 266 9.696 17.088 37.670 1.00 27.04 C ANISOU 1955 CD2 PHE A 266 3963 3219 3091 -503 54 -43 C ATOM 1956 CE1 PHE A 266 11.687 18.345 39.202 1.00 27.44 C ANISOU 1956 CE1 PHE A 266 3832 3530 3064 -139 86 90 C ATOM 1957 CE2 PHE A 266 9.508 18.418 38.081 1.00 29.05 C ANISOU 1957 CE2 PHE A 266 4330 3738 2970 -158 74 43 C ATOM 1958 CZ PHE A 266 10.501 19.046 38.850 1.00 27.63 C ANISOU 1958 CZ PHE A 266 3918 3734 2844 -184 68 171 C ATOM 1959 N GLU A 267 9.706 11.768 37.935 1.00 28.98 N ANISOU 1959 N GLU A 267 3809 3877 3324 -169 -6 -43 N ATOM 1960 CA GLU A 267 9.876 10.458 37.315 1.00 30.52 C ANISOU 1960 CA GLU A 267 4037 4063 3494 -178 47 -13 C ATOM 1961 C GLU A 267 9.482 10.596 35.876 1.00 31.81 C ANISOU 1961 C GLU A 267 4144 4304 3637 -114 146 -67 C ATOM 1962 O GLU A 267 8.377 10.978 35.558 1.00 29.86 O ANISOU 1962 O GLU A 267 4046 3994 3303 -64 229 -77 O ATOM 1963 CB GLU A 267 9.020 9.382 37.993 1.00 31.21 C ANISOU 1963 CB GLU A 267 4144 4055 3660 -89 108 152 C ATOM 1964 CG GLU A 267 9.582 7.959 37.719 1.00 35.68 C ANISOU 1964 CG GLU A 267 5113 4067 4376 -255 282 2 C ATOM 1965 CD GLU A 267 9.355 7.430 36.323 1.00 37.22 C ANISOU 1965 CD GLU A 267 4980 4192 4969 -329 -17 -55 C ATOM 1966 OE1 GLU A 267 8.474 7.925 35.590 1.00 42.95 O ANISOU 1966 OE1 GLU A 267 5640 4869 5810 -226 -164 -35 O ATOM 1967 OE2 GLU A 267 10.056 6.471 35.956 1.00 39.71 O1- ANISOU 1967 OE2 GLU A 267 5164 4374 5548 -470 -183 -807 O1- ATOM 1968 N VAL A 268 10.423 10.279 34.999 1.00 34.20 N ANISOU 1968 N VAL A 268 4541 4734 3716 -76 276 -113 N ATOM 1969 CA VAL A 268 10.190 10.508 33.593 1.00 38.72 C ANISOU 1969 CA VAL A 268 5052 5197 4464 -82 162 7 C ATOM 1970 C VAL A 268 9.991 9.102 33.002 1.00 41.77 C ANISOU 1970 C VAL A 268 5491 5534 4845 -108 170 -56 C ATOM 1971 O VAL A 268 9.025 8.864 32.325 1.00 43.72 O ANISOU 1971 O VAL A 268 5568 5862 5180 -179 222 64 O ATOM 1972 CB VAL A 268 11.351 11.284 32.948 1.00 38.85 C ANISOU 1972 CB VAL A 268 5011 5225 4522 -14 223 -92 C ATOM 1973 CG1 VAL A 268 11.657 12.592 33.714 1.00 37.95 C ANISOU 1973 CG1 VAL A 268 4563 5294 4563 -350 100 130 C ATOM 1974 CG2 VAL A 268 12.564 10.437 32.868 1.00 42.20 C ANISOU 1974 CG2 VAL A 268 5256 5550 5228 9 43 51 C ATOM 1975 N ILE A 269 10.881 8.176 33.379 1.00 44.58 N ANISOU 1975 N ILE A 269 5900 5730 5305 -50 255 4 N ATOM 1976 CA ILE A 269 11.009 6.828 32.789 1.00 47.11 C ANISOU 1976 CA ILE A 269 6212 5987 5697 -120 164 -11 C ATOM 1977 C ILE A 269 9.681 6.129 32.507 1.00 46.79 C ANISOU 1977 C ILE A 269 6111 5945 5722 -151 192 -6 C ATOM 1978 O ILE A 269 9.488 5.555 31.425 1.00 47.86 O ANISOU 1978 O ILE A 269 6359 6085 5738 -107 297 47 O ATOM 1979 CB ILE A 269 11.927 5.900 33.665 1.00 47.36 C ANISOU 1979 CB ILE A 269 6214 6020 5760 -125 168 41 C ATOM 1980 CG1 ILE A 269 13.049 6.713 34.326 1.00 49.43 C ANISOU 1980 CG1 ILE A 269 6552 6312 5915 -202 23 23 C ATOM 1981 CG2 ILE A 269 12.477 4.733 32.834 1.00 48.14 C ANISOU 1981 CG2 ILE A 269 6462 6086 5742 -156 171 -22 C ATOM 1982 CD1 ILE A 269 13.854 5.985 35.393 1.00 48.84 C ANISOU 1982 CD1 ILE A 269 6423 6194 5937 -129 67 -25 C ATOM 1983 N GLY A 270 8.756 6.193 33.462 1.00 46.38 N ANISOU 1983 N GLY A 270 6020 5867 5733 -181 183 24 N ATOM 1984 CA GLY A 270 7.475 5.523 33.308 1.00 46.12 C ANISOU 1984 CA GLY A 270 5807 5913 5802 -69 89 28 C ATOM 1985 C GLY A 270 7.466 4.229 34.094 1.00 45.51 C ANISOU 1985 C GLY A 270 5628 5827 5834 -91 21 52 C ATOM 1986 O GLY A 270 6.585 3.369 33.917 1.00 45.73 O ANISOU 1986 O GLY A 270 5607 5811 5955 -78 -160 -13 O ATOM 1987 N ARG A 271 8.427 4.099 35.006 1.00 43.60 N ANISOU 1987 N ARG A 271 5399 5735 5430 -121 72 -17 N ATOM 1988 CA ARG A 271 8.641 2.834 35.669 1.00 42.94 C ANISOU 1988 CA ARG A 271 5361 5700 5250 -32 169 -28 C ATOM 1989 C ARG A 271 8.013 2.870 37.056 1.00 42.21 C ANISOU 1989 C ARG A 271 5298 5588 5149 -17 269 -59 C ATOM 1990 O ARG A 271 8.272 3.792 37.827 1.00 41.46 O ANISOU 1990 O ARG A 271 5290 5485 4976 98 261 -55 O ATOM 1991 CB ARG A 271 10.136 2.566 35.785 1.00 43.53 C ANISOU 1991 CB ARG A 271 5397 5783 5356 -73 132 -37 C ATOM 1992 CG ARG A 271 10.764 2.058 34.510 1.00 46.02 C ANISOU 1992 CG ARG A 271 5552 6054 5880 -10 238 -52 C ATOM 1993 CD ARG A 271 11.019 0.558 34.607 1.00 50.50 C ANISOU 1993 CD ARG A 271 6248 6264 6676 85 150 83 C ATOM 1994 NE ARG A 271 11.784 0.212 35.806 1.00 54.23 N ANISOU 1994 NE ARG A 271 6814 6891 6899 98 -36 13 N ATOM 1995 CZ ARG A 271 12.470 -0.920 35.960 1.00 56.43 C ANISOU 1995 CZ ARG A 271 7057 7068 7313 175 -27 13 C ATOM 1996 NH1 ARG A 271 12.502 -1.825 34.987 1.00 58.04 N1+ ANISOU 1996 NH1 ARG A 271 7289 7327 7432 183 123 -38 N1+ ATOM 1997 NH2 ARG A 271 13.126 -1.148 37.089 1.00 57.48 N ANISOU 1997 NH2 ARG A 271 7133 7284 7420 183 -37 38 N ATOM 1998 N LEU A 272 7.259 1.834 37.404 1.00 41.90 N ANISOU 1998 N LEU A 272 5280 5615 5025 -10 340 -90 N ATOM 1999 CA LEU A 272 6.556 1.860 38.704 1.00 42.12 C ANISOU 1999 CA LEU A 272 5473 5517 5013 20 339 -82 C ATOM 2000 C LEU A 272 7.497 1.931 39.899 1.00 42.92 C ANISOU 2000 C LEU A 272 5581 5560 5167 -23 327 -118 C ATOM 2001 O LEU A 272 7.193 2.605 40.914 1.00 44.47 O ANISOU 2001 O LEU A 272 5897 5664 5332 -14 424 -193 O ATOM 2002 CB LEU A 272 5.614 0.664 38.836 1.00 42.05 C ANISOU 2002 CB LEU A 272 5353 5593 5028 -16 354 -67 C ATOM 2003 CG LEU A 272 4.510 0.474 37.790 1.00 42.09 C ANISOU 2003 CG LEU A 272 5444 5595 4950 97 324 -109 C ATOM 2004 CD1 LEU A 272 3.826 -0.830 38.093 1.00 44.19 C ANISOU 2004 CD1 LEU A 272 5657 5817 5315 16 313 -35 C ATOM 2005 CD2 LEU A 272 3.475 1.621 37.724 1.00 43.04 C ANISOU 2005 CD2 LEU A 272 5681 5656 5014 168 482 -28 C ATOM 2006 N ASP A 273 8.628 1.233 39.811 1.00 43.26 N ANISOU 2006 N ASP A 273 5682 5549 5205 8 154 -18 N ATOM 2007 CA ASP A 273 9.634 1.303 40.873 1.00 42.89 C ANISOU 2007 CA ASP A 273 5704 5505 5084 26 93 -1 C ATOM 2008 C ASP A 273 10.229 2.692 41.063 1.00 42.00 C ANISOU 2008 C ASP A 273 5530 5479 4947 0 118 47 C ATOM 2009 O ASP A 273 10.250 3.175 42.201 1.00 41.40 O ANISOU 2009 O ASP A 273 5629 5390 4712 53 236 87 O ATOM 2010 CB ASP A 273 10.718 0.223 40.746 1.00 44.17 C ANISOU 2010 CB ASP A 273 5826 5653 5302 62 -46 41 C ATOM 2011 CG ASP A 273 11.359 0.175 39.375 1.00 45.99 C ANISOU 2011 CG ASP A 273 6152 5735 5586 97 0 -14 C ATOM 2012 OD1 ASP A 273 10.746 0.637 38.385 1.00 48.53 O ANISOU 2012 OD1 ASP A 273 6821 5806 5812 344 -288 31 O ATOM 2013 OD2 ASP A 273 12.486 -0.346 39.279 1.00 50.28 O1- ANISOU 2013 OD2 ASP A 273 6491 6121 6489 100 -268 123 O1- ATOM 2014 N THR A 274 10.684 3.365 39.996 1.00 39.85 N ANISOU 2014 N THR A 274 5232 5292 4616 47 129 42 N ATOM 2015 CA THR A 274 11.238 4.707 40.221 1.00 39.08 C ANISOU 2015 CA THR A 274 4997 5233 4617 0 170 91 C ATOM 2016 C THR A 274 10.165 5.743 40.551 1.00 37.18 C ANISOU 2016 C THR A 274 4759 5018 4347 -68 205 29 C ATOM 2017 O THR A 274 10.490 6.747 41.149 1.00 36.47 O ANISOU 2017 O THR A 274 4471 5186 4200 -220 195 61 O ATOM 2018 CB THR A 274 12.257 5.272 39.147 1.00 39.69 C ANISOU 2018 CB THR A 274 5063 5263 4755 50 141 51 C ATOM 2019 CG2 THR A 274 13.679 4.705 39.369 1.00 41.81 C ANISOU 2019 CG2 THR A 274 5190 5440 5254 -34 159 175 C ATOM 2020 OG1 THR A 274 11.816 4.987 37.829 1.00 41.87 O ANISOU 2020 OG1 THR A 274 5558 5518 4830 -92 236 125 O ATOM 2021 N MET A 275 8.900 5.514 40.177 1.00 35.54 N ANISOU 2021 N MET A 275 4561 4816 4125 -87 208 54 N ATOM 2022 CA MET A 275 7.841 6.439 40.623 1.00 35.17 C ANISOU 2022 CA MET A 275 4478 4828 4057 -150 173 12 C ATOM 2023 C MET A 275 7.845 6.475 42.146 1.00 34.11 C ANISOU 2023 C MET A 275 4430 4622 3908 -209 314 41 C ATOM 2024 O MET A 275 7.818 7.563 42.745 1.00 31.88 O ANISOU 2024 O MET A 275 4038 4397 3675 -393 341 -38 O ATOM 2025 CB MET A 275 6.440 6.086 40.097 1.00 35.80 C ANISOU 2025 CB MET A 275 4572 4858 4171 -174 228 37 C ATOM 2026 CG MET A 275 6.236 6.397 38.607 1.00 37.44 C ANISOU 2026 CG MET A 275 4508 5252 4464 -69 84 64 C ATOM 2027 SD MET A 275 4.684 5.663 38.025 1.00 38.97 S ANISOU 2027 SD MET A 275 4851 5370 4584 -172 -166 -68 S ATOM 2028 CE MET A 275 5.097 5.508 36.298 1.00 37.09 C ANISOU 2028 CE MET A 275 4523 4990 4577 -160 395 65 C ATOM 2029 N VAL A 276 7.898 5.302 42.781 1.00 33.16 N ANISOU 2029 N VAL A 276 4256 4495 3845 -117 232 -7 N ATOM 2030 CA VAL A 276 7.873 5.305 44.255 1.00 32.90 C ANISOU 2030 CA VAL A 276 4336 4379 3784 -230 275 124 C ATOM 2031 C VAL A 276 9.218 5.801 44.844 1.00 32.63 C ANISOU 2031 C VAL A 276 4203 4379 3814 -24 222 160 C ATOM 2032 O VAL A 276 9.235 6.559 45.804 1.00 31.30 O ANISOU 2032 O VAL A 276 3917 4223 3750 -18 309 184 O ATOM 2033 CB VAL A 276 7.392 3.965 44.880 1.00 33.41 C ANISOU 2033 CB VAL A 276 4463 4413 3817 -141 284 128 C ATOM 2034 CG1 VAL A 276 7.072 4.174 46.333 1.00 34.24 C ANISOU 2034 CG1 VAL A 276 4895 4417 3694 -279 130 106 C ATOM 2035 CG2 VAL A 276 6.137 3.455 44.159 1.00 34.68 C ANISOU 2035 CG2 VAL A 276 4584 4508 4082 -350 339 27 C ATOM 2036 N THR A 277 10.329 5.423 44.226 1.00 32.34 N ANISOU 2036 N THR A 277 4168 4222 3896 65 222 192 N ATOM 2037 CA THR A 277 11.631 5.947 44.617 1.00 32.81 C ANISOU 2037 CA THR A 277 4220 4336 3910 177 121 81 C ATOM 2038 C THR A 277 11.680 7.462 44.538 1.00 31.52 C ANISOU 2038 C THR A 277 4082 4266 3627 109 47 94 C ATOM 2039 O THR A 277 12.190 8.132 45.470 1.00 32.00 O ANISOU 2039 O THR A 277 4124 4349 3682 116 -131 112 O ATOM 2040 CB THR A 277 12.751 5.366 43.728 1.00 33.52 C ANISOU 2040 CB THR A 277 4266 4355 4115 150 181 79 C ATOM 2041 CG2 THR A 277 14.073 5.977 44.102 1.00 34.25 C ANISOU 2041 CG2 THR A 277 4108 4633 4272 380 234 77 C ATOM 2042 OG1 THR A 277 12.815 3.960 43.963 1.00 37.80 O ANISOU 2042 OG1 THR A 277 5028 4506 4825 424 138 -130 O ATOM 2043 N ALA A 278 11.119 8.019 43.455 1.00 30.43 N ANISOU 2043 N ALA A 278 3972 4278 3312 59 132 97 N ATOM 2044 CA ALA A 278 11.146 9.470 43.285 1.00 28.95 C ANISOU 2044 CA ALA A 278 3803 4109 3085 22 -9 109 C ATOM 2045 C ALA A 278 10.320 10.161 44.371 1.00 28.39 C ANISOU 2045 C ALA A 278 3702 4043 3041 -77 -11 88 C ATOM 2046 O ALA A 278 10.771 11.148 44.944 1.00 28.93 O ANISOU 2046 O ALA A 278 3586 4079 3327 -114 -148 148 O ATOM 2047 CB ALA A 278 10.684 9.885 41.878 1.00 28.72 C ANISOU 2047 CB ALA A 278 4014 4028 2867 -102 -75 70 C ATOM 2048 N LEU A 279 9.169 9.591 44.720 1.00 28.36 N ANISOU 2048 N LEU A 279 3509 4188 3078 -9 -13 0 N ATOM 2049 CA LEU A 279 8.358 10.131 45.820 1.00 27.84 C ANISOU 2049 CA LEU A 279 3442 4025 3111 -153 -4 10 C ATOM 2050 C LEU A 279 9.117 10.089 47.136 1.00 28.88 C ANISOU 2050 C LEU A 279 3431 4228 3313 -184 -72 -48 C ATOM 2051 O LEU A 279 9.103 11.066 47.887 1.00 28.94 O ANISOU 2051 O LEU A 279 3510 4177 3307 -342 -172 -144 O ATOM 2052 CB LEU A 279 7.028 9.367 45.947 1.00 27.72 C ANISOU 2052 CB LEU A 279 3368 4065 3099 -9 71 0 C ATOM 2053 CG LEU A 279 6.128 9.837 47.094 1.00 26.99 C ANISOU 2053 CG LEU A 279 3364 3608 3281 23 74 91 C ATOM 2054 CD1 LEU A 279 5.673 11.237 46.848 1.00 26.61 C ANISOU 2054 CD1 LEU A 279 3295 3403 3412 272 -58 80 C ATOM 2055 CD2 LEU A 279 4.938 8.870 47.250 1.00 29.94 C ANISOU 2055 CD2 LEU A 279 3622 4214 3539 -296 151 259 C ATOM 2056 N SER A 280 9.706 8.938 47.427 1.00 29.35 N ANISOU 2056 N SER A 280 3359 4452 3339 -159 -246 -10 N ATOM 2057 CA SER A 280 10.384 8.694 48.707 1.00 30.90 C ANISOU 2057 CA SER A 280 3624 4573 3542 -249 -335 64 C ATOM 2058 C SER A 280 11.584 9.621 48.870 1.00 31.71 C ANISOU 2058 C SER A 280 3789 4648 3611 -293 -301 37 C ATOM 2059 O SER A 280 11.926 10.033 49.978 1.00 33.43 O ANISOU 2059 O SER A 280 3953 4893 3853 -408 -247 4 O ATOM 2060 CB SER A 280 10.836 7.233 48.771 1.00 31.76 C ANISOU 2060 CB SER A 280 3662 4678 3727 -320 -577 109 C ATOM 2061 OG SER A 280 9.715 6.348 48.724 1.00 36.70 O ANISOU 2061 OG SER A 280 4338 4913 4693 -355 -210 210 O ATOM 2062 N CYS A 281 12.248 9.953 47.771 1.00 32.16 N ANISOU 2062 N CYS A 281 3871 4696 3650 -352 -241 -63 N ATOM 2063 CA CYS A 281 13.498 10.687 47.908 1.00 33.34 C ANISOU 2063 CA CYS A 281 4053 4792 3820 -400 -157 -176 C ATOM 2064 C CYS A 281 13.284 12.208 48.103 1.00 32.69 C ANISOU 2064 C CYS A 281 4122 4577 3720 -467 -173 -236 C ATOM 2065 O CYS A 281 14.259 12.913 48.430 1.00 33.27 O ANISOU 2065 O CYS A 281 4073 4629 3939 -508 -232 -185 O ATOM 2066 CB CYS A 281 14.456 10.386 46.746 1.00 34.88 C ANISOU 2066 CB CYS A 281 4180 5029 4041 -340 -117 -180 C ATOM 2067 SG CYS A 281 14.148 11.397 45.322 1.00 37.52 S ANISOU 2067 SG CYS A 281 4463 5695 4095 -543 0 -204 S ATOM 2068 N CYS A 282 12.043 12.704 47.974 1.00 31.48 N ANISOU 2068 N CYS A 282 4195 4370 3395 -502 -128 -340 N ATOM 2069 CA CYS A 282 11.786 14.121 48.280 1.00 31.37 C ANISOU 2069 CA CYS A 282 4172 4308 3438 -494 30 -201 C ATOM 2070 C CYS A 282 11.606 14.301 49.781 1.00 31.01 C ANISOU 2070 C CYS A 282 4256 4208 3315 -470 -17 -175 C ATOM 2071 O CYS A 282 11.194 13.373 50.504 1.00 30.97 O ANISOU 2071 O CYS A 282 4186 4160 3421 -601 29 -222 O ATOM 2072 CB CYS A 282 10.662 14.811 47.457 1.00 33.55 C ANISOU 2072 CB CYS A 282 4324 4534 3887 -496 194 -153 C ATOM 2073 SG CYS A 282 8.969 14.225 47.741 1.00 33.98 S ANISOU 2073 SG CYS A 282 4530 4662 3719 -746 302 -129 S ATOM 2074 N GLN A 283 11.906 15.508 50.247 1.00 30.57 N ANISOU 2074 N GLN A 283 4332 4141 3142 -460 -8 -191 N ATOM 2075 CA GLN A 283 11.814 15.799 51.698 1.00 30.65 C ANISOU 2075 CA GLN A 283 4320 4256 3069 -374 -20 -68 C ATOM 2076 C GLN A 283 10.418 15.420 52.255 1.00 30.01 C ANISOU 2076 C GLN A 283 4245 4092 3063 -469 -91 -7 C ATOM 2077 O GLN A 283 9.371 15.736 51.663 1.00 28.95 O ANISOU 2077 O GLN A 283 4072 4046 2880 -536 -62 119 O ATOM 2078 CB GLN A 283 12.172 17.265 51.973 1.00 31.54 C ANISOU 2078 CB GLN A 283 4434 4334 3215 -330 -90 -123 C ATOM 2079 CG GLN A 283 12.666 17.546 53.433 1.00 33.87 C ANISOU 2079 CG GLN A 283 4973 4614 3280 -302 194 14 C ATOM 2080 CD GLN A 283 11.525 17.599 54.454 1.00 34.86 C ANISOU 2080 CD GLN A 283 4680 4514 4050 -158 213 173 C ATOM 2081 NE2 GLN A 283 11.823 17.241 55.690 1.00 35.94 N ANISOU 2081 NE2 GLN A 283 4815 4885 3953 -47 44 -31 N ATOM 2082 OE1 GLN A 283 10.394 17.941 54.122 1.00 34.99 O ANISOU 2082 OE1 GLN A 283 4727 4695 3870 -547 -46 277 O ATOM 2083 N GLU A 284 10.404 14.743 53.392 1.00 30.18 N ANISOU 2083 N GLU A 284 4230 4090 3147 -365 -51 -49 N ATOM 2084 CA GLU A 284 9.170 14.138 53.883 1.00 30.24 C ANISOU 2084 CA GLU A 284 4364 3987 3136 -399 -56 23 C ATOM 2085 C GLU A 284 8.084 15.142 54.276 1.00 28.86 C ANISOU 2085 C GLU A 284 4148 3808 3010 -357 -78 7 C ATOM 2086 O GLU A 284 6.883 14.786 54.298 1.00 29.44 O ANISOU 2086 O GLU A 284 4287 3806 3091 -340 -51 -277 O ATOM 2087 CB GLU A 284 9.478 13.219 55.070 1.00 30.97 C ANISOU 2087 CB GLU A 284 4487 4069 3209 -328 -103 109 C ATOM 2088 CG GLU A 284 9.881 14.021 56.302 1.00 33.30 C ANISOU 2088 CG GLU A 284 4852 4202 3595 -248 -236 -7 C ATOM 2089 CD GLU A 284 10.089 13.200 57.554 1.00 37.69 C ANISOU 2089 CD GLU A 284 5472 4601 4245 -181 -294 220 C ATOM 2090 OE1 GLU A 284 9.681 11.999 57.578 1.00 39.97 O ANISOU 2090 OE1 GLU A 284 5908 4575 4703 -82 -576 585 O ATOM 2091 OE2 GLU A 284 10.651 13.788 58.523 1.00 36.83 O1- ANISOU 2091 OE2 GLU A 284 5240 4389 4362 55 -187 -104 O1- ATOM 2092 N ALA A 285 8.487 16.367 54.643 1.00 29.34 N ANISOU 2092 N ALA A 285 4257 3962 2929 -332 -50 81 N ATOM 2093 CA ALA A 285 7.548 17.404 55.130 1.00 28.91 C ANISOU 2093 CA ALA A 285 4167 3968 2849 -386 77 74 C ATOM 2094 C ALA A 285 7.021 18.353 54.048 1.00 29.84 C ANISOU 2094 C ALA A 285 4222 3986 3130 -381 215 171 C ATOM 2095 O ALA A 285 5.907 18.875 54.164 1.00 31.59 O ANISOU 2095 O ALA A 285 4561 3984 3456 -369 409 306 O ATOM 2096 CB ALA A 285 8.191 18.233 56.330 1.00 29.98 C ANISOU 2096 CB ALA A 285 4247 4204 2938 -344 45 40 C ATOM 2097 N TYR A 286 7.800 18.584 52.992 1.00 28.81 N ANISOU 2097 N TYR A 286 4353 3887 2707 -465 150 11 N ATOM 2098 CA TYR A 286 7.408 19.629 52.028 1.00 28.81 C ANISOU 2098 CA TYR A 286 4323 3845 2779 -392 199 -25 C ATOM 2099 C TYR A 286 7.825 19.287 50.595 1.00 29.16 C ANISOU 2099 C TYR A 286 4300 4024 2755 -347 224 56 C ATOM 2100 O TYR A 286 7.695 20.122 49.676 1.00 30.51 O ANISOU 2100 O TYR A 286 4575 4181 2834 -341 171 91 O ATOM 2101 CB TYR A 286 7.975 20.998 52.468 1.00 30.32 C ANISOU 2101 CB TYR A 286 4403 4013 3102 -436 112 -87 C ATOM 2102 CG TYR A 286 9.481 21.016 52.702 1.00 29.17 C ANISOU 2102 CG TYR A 286 4241 3786 3054 -654 248 -133 C ATOM 2103 CD1 TYR A 286 10.378 21.044 51.629 1.00 29.96 C ANISOU 2103 CD1 TYR A 286 4212 4231 2940 -619 114 30 C ATOM 2104 CD2 TYR A 286 10.016 21.093 53.987 1.00 29.74 C ANISOU 2104 CD2 TYR A 286 4092 3854 3352 -565 167 -14 C ATOM 2105 CE1 TYR A 286 11.729 21.064 51.833 1.00 30.37 C ANISOU 2105 CE1 TYR A 286 4140 4299 3100 -592 -22 -155 C ATOM 2106 CE2 TYR A 286 11.356 21.120 54.197 1.00 31.15 C ANISOU 2106 CE2 TYR A 286 4457 4146 3232 -517 -120 -220 C ATOM 2107 CZ TYR A 286 12.226 21.124 53.124 1.00 32.56 C ANISOU 2107 CZ TYR A 286 4347 4519 3502 -355 37 -148 C ATOM 2108 OH TYR A 286 13.590 21.155 53.308 1.00 34.92 O ANISOU 2108 OH TYR A 286 4592 4503 4172 -869 -13 -146 O ATOM 2109 N GLY A 287 8.328 18.076 50.414 1.00 28.50 N ANISOU 2109 N GLY A 287 4295 3966 2567 -395 253 -48 N ATOM 2110 CA GLY A 287 8.822 17.607 49.080 1.00 29.06 C ANISOU 2110 CA GLY A 287 4288 4174 2576 -404 4 -98 C ATOM 2111 C GLY A 287 7.657 17.459 48.095 1.00 28.67 C ANISOU 2111 C GLY A 287 4097 3958 2839 -406 -63 -64 C ATOM 2112 O GLY A 287 6.533 17.237 48.503 1.00 27.44 O ANISOU 2112 O GLY A 287 3953 3822 2650 -419 56 18 O ATOM 2113 N VAL A 288 7.935 17.662 46.813 1.00 27.60 N ANISOU 2113 N VAL A 288 3900 3919 2667 -348 -165 -251 N ATOM 2114 CA VAL A 288 6.918 17.488 45.758 1.00 27.45 C ANISOU 2114 CA VAL A 288 3815 3799 2815 -281 -192 -233 C ATOM 2115 C VAL A 288 7.496 16.561 44.725 1.00 27.60 C ANISOU 2115 C VAL A 288 3746 3859 2880 -279 -108 -162 C ATOM 2116 O VAL A 288 8.624 16.772 44.274 1.00 29.39 O ANISOU 2116 O VAL A 288 3810 4194 3160 -289 52 -292 O ATOM 2117 CB VAL A 288 6.581 18.843 45.090 1.00 28.01 C ANISOU 2117 CB VAL A 288 3951 3930 2761 -283 -156 -169 C ATOM 2118 CG1 VAL A 288 5.646 18.671 43.914 1.00 28.54 C ANISOU 2118 CG1 VAL A 288 4231 3743 2869 -219 -325 -172 C ATOM 2119 CG2 VAL A 288 5.983 19.814 46.125 1.00 28.80 C ANISOU 2119 CG2 VAL A 288 3869 3817 3257 -188 59 -224 C ATOM 2120 N SER A 289 6.732 15.549 44.327 1.00 25.74 N ANISOU 2120 N SER A 289 3596 3663 2520 -343 -142 -195 N ATOM 2121 CA SER A 289 7.211 14.626 43.297 1.00 25.29 C ANISOU 2121 CA SER A 289 3542 3510 2557 -194 -195 -19 C ATOM 2122 C SER A 289 6.208 14.627 42.143 1.00 25.21 C ANISOU 2122 C SER A 289 3405 3563 2610 -217 -164 -57 C ATOM 2123 O SER A 289 4.996 14.537 42.356 1.00 26.03 O ANISOU 2123 O SER A 289 3667 3589 2632 -212 -246 -86 O ATOM 2124 CB SER A 289 7.378 13.217 43.876 1.00 26.63 C ANISOU 2124 CB SER A 289 3693 3611 2814 -251 -12 0 C ATOM 2125 OG SER A 289 7.954 12.337 42.914 1.00 27.43 O ANISOU 2125 OG SER A 289 4017 3410 2992 -229 -192 110 O ATOM 2126 N VAL A 290 6.731 14.720 40.922 1.00 25.02 N ANISOU 2126 N VAL A 290 3517 3538 2447 -226 -291 -18 N ATOM 2127 CA VAL A 290 5.882 14.828 39.722 1.00 26.43 C ANISOU 2127 CA VAL A 290 3687 3653 2699 -194 -236 3 C ATOM 2128 C VAL A 290 6.129 13.661 38.786 1.00 26.07 C ANISOU 2128 C VAL A 290 3581 3619 2704 -239 -241 -38 C ATOM 2129 O VAL A 290 7.286 13.350 38.454 1.00 27.87 O ANISOU 2129 O VAL A 290 3798 3851 2937 -294 -87 -198 O ATOM 2130 CB VAL A 290 6.165 16.167 38.936 1.00 26.88 C ANISOU 2130 CB VAL A 290 3826 3602 2785 -164 -50 0 C ATOM 2131 CG1 VAL A 290 5.287 16.271 37.656 1.00 27.98 C ANISOU 2131 CG1 VAL A 290 3689 3887 3052 -242 -226 -89 C ATOM 2132 CG2 VAL A 290 5.939 17.431 39.802 1.00 27.07 C ANISOU 2132 CG2 VAL A 290 4172 3565 2547 -407 -5 -73 C ATOM 2133 N ILE A 291 5.034 13.036 38.338 1.00 26.27 N ANISOU 2133 N ILE A 291 3853 3547 2578 -386 -255 22 N ATOM 2134 CA ILE A 291 5.048 11.935 37.388 1.00 29.39 C ANISOU 2134 CA ILE A 291 4319 3872 2976 -319 -161 -27 C ATOM 2135 C ILE A 291 4.871 12.620 36.030 1.00 29.55 C ANISOU 2135 C ILE A 291 4308 3932 2988 -290 -190 -60 C ATOM 2136 O ILE A 291 3.893 13.331 35.819 1.00 29.89 O ANISOU 2136 O ILE A 291 4336 4073 2944 -218 -159 -197 O ATOM 2137 CB ILE A 291 3.839 10.971 37.723 1.00 29.13 C ANISOU 2137 CB ILE A 291 4459 3788 2818 -348 -187 0 C ATOM 2138 CG1 ILE A 291 4.125 10.247 39.077 1.00 32.26 C ANISOU 2138 CG1 ILE A 291 4898 4041 3319 -445 -174 375 C ATOM 2139 CG2 ILE A 291 3.473 10.007 36.563 1.00 32.59 C ANISOU 2139 CG2 ILE A 291 4906 3940 3537 -281 -163 -83 C ATOM 2140 CD1 ILE A 291 3.072 9.202 39.496 1.00 32.27 C ANISOU 2140 CD1 ILE A 291 4516 4206 3539 -444 -56 39 C ATOM 2141 N VAL A 292 5.829 12.413 35.130 1.00 29.53 N ANISOU 2141 N VAL A 292 4252 4068 2900 -319 -192 0 N ATOM 2142 CA VAL A 292 5.864 13.139 33.860 1.00 31.33 C ANISOU 2142 CA VAL A 292 4414 4204 3282 -276 -161 88 C ATOM 2143 C VAL A 292 5.283 12.232 32.772 1.00 32.59 C ANISOU 2143 C VAL A 292 4547 4414 3421 -262 -195 95 C ATOM 2144 O VAL A 292 4.735 12.697 31.757 1.00 35.29 O ANISOU 2144 O VAL A 292 4802 4834 3772 -227 -238 215 O ATOM 2145 CB VAL A 292 7.291 13.621 33.548 1.00 31.17 C ANISOU 2145 CB VAL A 292 4359 4308 3174 -240 -130 83 C ATOM 2146 CG1 VAL A 292 7.345 14.365 32.221 1.00 28.58 C ANISOU 2146 CG1 VAL A 292 4062 3703 3094 -261 -36 144 C ATOM 2147 CG2 VAL A 292 7.813 14.529 34.692 1.00 30.69 C ANISOU 2147 CG2 VAL A 292 4113 4184 3360 -116 -116 47 C ATOM 2148 N GLY A 293 5.337 10.931 32.997 1.00 34.21 N ANISOU 2148 N GLY A 293 4716 4511 3771 -243 -117 -30 N ATOM 2149 CA GLY A 293 4.716 10.014 32.032 1.00 35.55 C ANISOU 2149 CA GLY A 293 4768 4606 4130 -314 21 -2 C ATOM 2150 C GLY A 293 4.377 8.720 32.719 1.00 36.56 C ANISOU 2150 C GLY A 293 4896 4740 4253 -277 98 14 C ATOM 2151 O GLY A 293 4.985 8.378 33.725 1.00 36.70 O ANISOU 2151 O GLY A 293 4876 4754 4312 -338 160 86 O ATOM 2152 N VAL A 294 3.409 8.014 32.154 1.00 37.34 N ANISOU 2152 N VAL A 294 4880 4897 4407 -289 83 -1 N ATOM 2153 CA VAL A 294 3.057 6.661 32.559 1.00 38.49 C ANISOU 2153 CA VAL A 294 5093 4996 4533 -300 93 -47 C ATOM 2154 C VAL A 294 2.881 5.816 31.302 1.00 38.95 C ANISOU 2154 C VAL A 294 5149 5038 4611 -369 70 1 C ATOM 2155 O VAL A 294 2.081 6.190 30.450 1.00 40.05 O ANISOU 2155 O VAL A 294 5271 5282 4664 -507 75 -2 O ATOM 2156 CB VAL A 294 1.740 6.642 33.357 1.00 38.99 C ANISOU 2156 CB VAL A 294 5180 5085 4548 -298 84 -77 C ATOM 2157 CG1 VAL A 294 1.489 5.260 33.947 1.00 39.03 C ANISOU 2157 CG1 VAL A 294 5199 5002 4625 -226 192 -327 C ATOM 2158 CG2 VAL A 294 1.791 7.685 34.486 1.00 39.84 C ANISOU 2158 CG2 VAL A 294 5201 5181 4753 -291 86 -304 C ATOM 2159 N PRO A 295 3.585 4.667 31.197 1.00 39.95 N ANISOU 2159 N PRO A 295 5268 5196 4714 -327 42 -62 N ATOM 2160 CA PRO A 295 3.298 3.824 30.038 1.00 40.37 C ANISOU 2160 CA PRO A 295 5431 5213 4694 -290 42 -12 C ATOM 2161 C PRO A 295 1.811 3.496 30.046 1.00 40.69 C ANISOU 2161 C PRO A 295 5551 5287 4621 -297 0 37 C ATOM 2162 O PRO A 295 1.254 3.242 31.117 1.00 39.88 O ANISOU 2162 O PRO A 295 5598 5179 4375 -437 79 152 O ATOM 2163 CB PRO A 295 4.144 2.566 30.297 1.00 40.63 C ANISOU 2163 CB PRO A 295 5480 5195 4760 -246 -32 -132 C ATOM 2164 CG PRO A 295 5.288 3.054 31.170 1.00 41.68 C ANISOU 2164 CG PRO A 295 5472 5341 5022 -251 41 -116 C ATOM 2165 CD PRO A 295 4.583 4.042 32.087 1.00 40.39 C ANISOU 2165 CD PRO A 295 5336 5231 4778 -298 47 -126 C ATOM 2166 N PRO A 296 1.158 3.543 28.871 1.00 40.74 N ANISOU 2166 N PRO A 296 5582 5298 4598 -228 -52 183 N ATOM 2167 CA PRO A 296 -0.290 3.385 28.746 1.00 41.21 C ANISOU 2167 CA PRO A 296 5633 5294 4729 -250 -25 195 C ATOM 2168 C PRO A 296 -0.838 2.016 29.149 1.00 41.53 C ANISOU 2168 C PRO A 296 5667 5290 4822 -231 -27 172 C ATOM 2169 O PRO A 296 -2.041 1.901 29.394 1.00 41.79 O ANISOU 2169 O PRO A 296 5633 5302 4942 -205 -82 119 O ATOM 2170 CB PRO A 296 -0.559 3.659 27.262 1.00 41.08 C ANISOU 2170 CB PRO A 296 5630 5342 4634 -174 -99 190 C ATOM 2171 CG PRO A 296 0.723 3.506 26.575 1.00 40.32 C ANISOU 2171 CG PRO A 296 5425 5284 4611 -233 -109 293 C ATOM 2172 CD PRO A 296 1.801 3.831 27.574 1.00 40.19 C ANISOU 2172 CD PRO A 296 5555 5176 4539 -298 -3 185 C ATOM 2173 N ASP A 297 0.034 1.013 29.228 1.00 42.17 N ANISOU 2173 N ASP A 297 5751 5304 4968 -223 6 129 N ATOM 2174 CA ASP A 297 -0.333 -0.305 29.746 1.00 43.38 C ANISOU 2174 CA ASP A 297 5967 5359 5155 -166 -53 76 C ATOM 2175 C ASP A 297 0.154 -0.558 31.173 1.00 43.28 C ANISOU 2175 C ASP A 297 5924 5302 5217 -174 -65 90 C ATOM 2176 O ASP A 297 0.314 -1.707 31.565 1.00 43.67 O ANISOU 2176 O ASP A 297 6052 5291 5247 -137 -153 160 O ATOM 2177 CB ASP A 297 0.170 -1.420 28.805 1.00 44.00 C ANISOU 2177 CB ASP A 297 5983 5407 5327 -113 -36 27 C ATOM 2178 CG ASP A 297 1.695 -1.489 28.710 1.00 46.33 C ANISOU 2178 CG ASP A 297 6263 5721 5618 -51 -9 -22 C ATOM 2179 OD1 ASP A 297 2.395 -0.490 29.015 1.00 47.94 O ANISOU 2179 OD1 ASP A 297 6573 6033 5609 -187 -135 -221 O ATOM 2180 OD2 ASP A 297 2.195 -2.561 28.299 1.00 48.94 O1- ANISOU 2180 OD2 ASP A 297 6819 5621 6155 42 -107 -206 O1- ATOM 2181 N SER A 298 0.381 0.506 31.945 1.00 42.14 N ANISOU 2181 N SER A 298 5729 5236 5045 -143 -23 16 N ATOM 2182 CA SER A 298 0.954 0.356 33.284 1.00 41.81 C ANISOU 2182 CA SER A 298 5707 5158 5018 -144 37 103 C ATOM 2183 C SER A 298 0.016 -0.443 34.161 1.00 40.61 C ANISOU 2183 C SER A 298 5531 5024 4876 -119 -2 28 C ATOM 2184 O SER A 298 -1.191 -0.224 34.141 1.00 39.20 O ANISOU 2184 O SER A 298 5477 4819 4596 -175 32 -26 O ATOM 2185 CB SER A 298 1.192 1.717 33.955 1.00 43.03 C ANISOU 2185 CB SER A 298 5768 5309 5270 -67 65 56 C ATOM 2186 OG SER A 298 -0.043 2.353 34.286 1.00 46.62 O ANISOU 2186 OG SER A 298 6218 5646 5848 -66 253 146 O ATOM 2187 N GLN A 299 0.590 -1.366 34.929 1.00 40.12 N ANISOU 2187 N GLN A 299 5492 4863 4887 -99 12 -22 N ATOM 2188 CA GLN A 299 -0.136 -1.978 36.030 1.00 39.49 C ANISOU 2188 CA GLN A 299 5443 4787 4772 21 37 -56 C ATOM 2189 C GLN A 299 -0.163 -1.058 37.271 1.00 38.50 C ANISOU 2189 C GLN A 299 5208 4641 4776 23 119 -73 C ATOM 2190 O GLN A 299 0.374 0.045 37.268 1.00 38.29 O ANISOU 2190 O GLN A 299 5274 4528 4745 199 129 123 O ATOM 2191 CB GLN A 299 0.504 -3.319 36.381 1.00 41.16 C ANISOU 2191 CB GLN A 299 5637 4921 5078 85 15 -120 C ATOM 2192 CG GLN A 299 0.403 -4.351 35.258 1.00 43.76 C ANISOU 2192 CG GLN A 299 6062 5201 5364 -3 -58 -194 C ATOM 2193 CD GLN A 299 -0.863 -5.171 35.368 1.00 48.32 C ANISOU 2193 CD GLN A 299 6362 5714 6282 -120 -142 -94 C ATOM 2194 NE2 GLN A 299 -0.718 -6.418 35.816 1.00 50.87 N ANISOU 2194 NE2 GLN A 299 6875 5936 6516 -62 -185 84 N ATOM 2195 OE1 GLN A 299 -1.961 -4.694 35.071 1.00 49.23 O ANISOU 2195 OE1 GLN A 299 6608 5764 6333 -33 -294 -149 O ATOM 2196 N ASN A 300 -0.757 -1.542 38.352 1.00 36.59 N ANISOU 2196 N ASN A 300 4940 4447 4516 63 193 -143 N ATOM 2197 CA ASN A 300 -0.802 -0.749 39.573 1.00 36.46 C ANISOU 2197 CA ASN A 300 4813 4514 4526 -73 212 -171 C ATOM 2198 C ASN A 300 0.546 -0.727 40.224 1.00 35.86 C ANISOU 2198 C ASN A 300 4691 4446 4488 -54 267 -102 C ATOM 2199 O ASN A 300 1.331 -1.686 40.095 1.00 36.32 O ANISOU 2199 O ASN A 300 4640 4452 4705 -106 190 -228 O ATOM 2200 CB ASN A 300 -1.773 -1.354 40.574 1.00 36.00 C ANISOU 2200 CB ASN A 300 4855 4347 4473 -34 332 -233 C ATOM 2201 CG ASN A 300 -3.220 -0.995 40.304 1.00 38.68 C ANISOU 2201 CG ASN A 300 5018 4842 4835 -244 97 -216 C ATOM 2202 ND2 ASN A 300 -3.506 -0.349 39.178 1.00 39.53 N ANISOU 2202 ND2 ASN A 300 5097 5032 4890 -437 204 -89 N ATOM 2203 OD1 ASN A 300 -4.080 -1.306 41.125 1.00 44.37 O ANISOU 2203 OD1 ASN A 300 5761 5731 5364 -237 458 72 O ATOM 2204 N LEU A 301 0.820 0.360 40.920 1.00 34.79 N ANISOU 2204 N LEU A 301 4533 4433 4251 -22 306 -129 N ATOM 2205 CA LEU A 301 2.008 0.446 41.759 1.00 35.74 C ANISOU 2205 CA LEU A 301 4728 4497 4353 -22 220 -36 C ATOM 2206 C LEU A 301 1.592 0.179 43.180 1.00 35.36 C ANISOU 2206 C LEU A 301 4686 4432 4314 88 188 -26 C ATOM 2207 O LEU A 301 0.382 0.228 43.513 1.00 36.13 O ANISOU 2207 O LEU A 301 4711 4621 4396 19 205 37 O ATOM 2208 CB LEU A 301 2.706 1.816 41.625 1.00 35.79 C ANISOU 2208 CB LEU A 301 4738 4513 4346 -86 166 -73 C ATOM 2209 CG LEU A 301 2.030 3.140 41.995 1.00 35.74 C ANISOU 2209 CG LEU A 301 4844 4549 4186 -127 312 -36 C ATOM 2210 CD1 LEU A 301 2.065 3.388 43.502 1.00 37.17 C ANISOU 2210 CD1 LEU A 301 5244 4732 4144 -119 51 -103 C ATOM 2211 CD2 LEU A 301 2.715 4.290 41.270 1.00 36.45 C ANISOU 2211 CD2 LEU A 301 4876 4519 4453 -136 184 0 C ATOM 2212 N SER A 302 2.585 -0.138 44.008 1.00 35.15 N ANISOU 2212 N SER A 302 4799 4385 4170 119 187 -33 N ATOM 2213 CA SER A 302 2.355 -0.384 45.409 1.00 34.55 C ANISOU 2213 CA SER A 302 4809 4140 4177 185 175 103 C ATOM 2214 C SER A 302 3.180 0.619 46.186 1.00 33.31 C ANISOU 2214 C SER A 302 4540 4117 3997 168 203 52 C ATOM 2215 O SER A 302 4.396 0.743 45.960 1.00 32.54 O ANISOU 2215 O SER A 302 4371 4082 3908 155 230 88 O ATOM 2216 CB SER A 302 2.787 -1.801 45.765 1.00 35.56 C ANISOU 2216 CB SER A 302 4988 4195 4328 252 163 121 C ATOM 2217 OG SER A 302 2.766 -1.941 47.155 1.00 38.94 O ANISOU 2217 OG SER A 302 5690 4403 4699 392 179 216 O ATOM 2218 N MET A 303 2.532 1.333 47.102 1.00 32.28 N ANISOU 2218 N MET A 303 4425 3965 3874 75 281 100 N ATOM 2219 CA MET A 303 3.243 2.337 47.893 1.00 31.48 C ANISOU 2219 CA MET A 303 4282 3961 3715 99 254 45 C ATOM 2220 C MET A 303 2.608 2.456 49.251 1.00 30.80 C ANISOU 2220 C MET A 303 4051 3876 3772 135 310 12 C ATOM 2221 O MET A 303 1.443 2.098 49.414 1.00 30.61 O ANISOU 2221 O MET A 303 4052 3813 3762 202 355 -1 O ATOM 2222 CB MET A 303 3.231 3.704 47.186 1.00 32.41 C ANISOU 2222 CB MET A 303 4356 3987 3969 101 275 59 C ATOM 2223 CG MET A 303 1.854 4.306 46.991 1.00 33.20 C ANISOU 2223 CG MET A 303 4316 4253 4046 83 32 -56 C ATOM 2224 SD MET A 303 1.134 5.270 48.346 1.00 33.76 S ANISOU 2224 SD MET A 303 4570 4138 4116 -203 327 -96 S ATOM 2225 CE MET A 303 2.189 6.709 48.500 1.00 35.36 C ANISOU 2225 CE MET A 303 4842 4205 4385 -151 22 -111 C ATOM 2226 N ASN A 304 3.387 2.945 50.221 1.00 30.51 N ANISOU 2226 N ASN A 304 4009 3956 3626 53 369 16 N ATOM 2227 CA ASN A 304 2.881 3.104 51.577 1.00 31.66 C ANISOU 2227 CA ASN A 304 4046 4083 3900 3 248 50 C ATOM 2228 C ASN A 304 2.385 4.557 51.727 1.00 31.02 C ANISOU 2228 C ASN A 304 3894 3964 3925 -78 275 63 C ATOM 2229 O ASN A 304 3.192 5.512 51.526 1.00 29.49 O ANISOU 2229 O ASN A 304 3663 3855 3684 -97 218 -33 O ATOM 2230 CB ASN A 304 4.008 2.765 52.564 1.00 32.61 C ANISOU 2230 CB ASN A 304 4324 4111 3955 24 101 167 C ATOM 2231 CG ASN A 304 3.570 2.779 53.992 1.00 35.83 C ANISOU 2231 CG ASN A 304 4608 4668 4338 196 158 281 C ATOM 2232 ND2 ASN A 304 4.402 2.207 54.850 1.00 41.73 N ANISOU 2232 ND2 ASN A 304 5364 5376 5115 234 -358 333 N ATOM 2233 OD1 ASN A 304 2.539 3.316 54.346 1.00 35.00 O ANISOU 2233 OD1 ASN A 304 4456 4386 4455 224 18 729 O ATOM 2234 N PRO A 305 1.075 4.735 52.061 1.00 30.19 N ANISOU 2234 N PRO A 305 3697 3897 3876 -223 306 61 N ATOM 2235 CA PRO A 305 0.521 6.088 52.157 1.00 30.45 C ANISOU 2235 CA PRO A 305 3668 4088 3811 -216 365 65 C ATOM 2236 C PRO A 305 1.196 6.895 53.255 1.00 29.44 C ANISOU 2236 C PRO A 305 3534 4066 3585 -240 282 147 C ATOM 2237 O PRO A 305 1.036 8.094 53.277 1.00 29.53 O ANISOU 2237 O PRO A 305 3639 4244 3337 -205 399 119 O ATOM 2238 CB PRO A 305 -0.971 5.868 52.500 1.00 30.95 C ANISOU 2238 CB PRO A 305 3679 4093 3987 -140 382 191 C ATOM 2239 CG PRO A 305 -1.026 4.473 53.059 1.00 30.98 C ANISOU 2239 CG PRO A 305 3795 3981 3992 -202 456 219 C ATOM 2240 CD PRO A 305 0.041 3.704 52.329 1.00 31.72 C ANISOU 2240 CD PRO A 305 3893 4116 4040 -187 476 56 C ATOM 2241 N MET A 306 1.959 6.252 54.143 1.00 29.73 N ANISOU 2241 N MET A 306 3646 4135 3515 -292 297 263 N ATOM 2242 CA MET A 306 2.717 7.046 55.097 1.00 31.30 C ANISOU 2242 CA MET A 306 3915 4249 3726 -157 97 212 C ATOM 2243 C MET A 306 3.695 8.014 54.430 1.00 30.63 C ANISOU 2243 C MET A 306 3807 4261 3567 -139 104 155 C ATOM 2244 O MET A 306 4.104 8.991 55.045 1.00 30.78 O ANISOU 2244 O MET A 306 3861 4359 3473 -170 98 131 O ATOM 2245 CB MET A 306 3.499 6.191 56.073 1.00 32.53 C ANISOU 2245 CB MET A 306 4077 4397 3886 -145 10 254 C ATOM 2246 CG MET A 306 3.592 6.837 57.375 1.00 38.17 C ANISOU 2246 CG MET A 306 4954 4856 4692 11 -19 297 C ATOM 2247 SD MET A 306 2.033 6.394 58.134 1.00 45.29 S ANISOU 2247 SD MET A 306 5536 5920 5752 -35 311 649 S ATOM 2248 CE MET A 306 2.541 4.740 58.687 1.00 45.83 C ANISOU 2248 CE MET A 306 6019 6093 5302 80 -391 841 C ATOM 2249 N LEU A 307 4.096 7.730 53.189 1.00 29.84 N ANISOU 2249 N LEU A 307 3654 4286 3396 -92 16 187 N ATOM 2250 CA LEU A 307 4.957 8.651 52.456 1.00 29.39 C ANISOU 2250 CA LEU A 307 3609 4132 3424 -65 43 151 C ATOM 2251 C LEU A 307 4.308 10.028 52.275 1.00 29.64 C ANISOU 2251 C LEU A 307 3694 4110 3457 -124 57 62 C ATOM 2252 O LEU A 307 4.988 11.051 52.220 1.00 30.09 O ANISOU 2252 O LEU A 307 3582 4418 3430 -218 -106 90 O ATOM 2253 CB LEU A 307 5.265 8.075 51.070 1.00 29.75 C ANISOU 2253 CB LEU A 307 3651 4135 3516 -36 108 84 C ATOM 2254 CG LEU A 307 6.249 6.892 51.106 1.00 30.70 C ANISOU 2254 CG LEU A 307 3768 4034 3861 139 151 83 C ATOM 2255 CD1 LEU A 307 6.421 6.329 49.688 1.00 32.46 C ANISOU 2255 CD1 LEU A 307 3880 4388 4064 187 73 -100 C ATOM 2256 CD2 LEU A 307 7.606 7.274 51.728 1.00 32.32 C ANISOU 2256 CD2 LEU A 307 4227 3814 4239 250 -15 -53 C ATOM 2257 N LEU A 308 2.985 10.040 52.159 1.00 28.94 N ANISOU 2257 N LEU A 308 3527 4042 3426 -56 17 77 N ATOM 2258 CA LEU A 308 2.252 11.282 51.961 1.00 28.56 C ANISOU 2258 CA LEU A 308 3692 3761 3398 -182 101 68 C ATOM 2259 C LEU A 308 1.864 11.963 53.274 1.00 30.33 C ANISOU 2259 C LEU A 308 4044 3923 3556 -138 103 91 C ATOM 2260 O LEU A 308 1.785 13.181 53.337 1.00 30.80 O ANISOU 2260 O LEU A 308 4212 3890 3599 -39 20 61 O ATOM 2261 CB LEU A 308 0.993 11.031 51.144 1.00 28.02 C ANISOU 2261 CB LEU A 308 3485 3737 3422 -116 117 148 C ATOM 2262 CG LEU A 308 1.236 10.563 49.718 1.00 26.32 C ANISOU 2262 CG LEU A 308 3313 3471 3215 -411 -113 105 C ATOM 2263 CD1 LEU A 308 -0.051 10.221 49.030 1.00 29.37 C ANISOU 2263 CD1 LEU A 308 3684 3585 3889 -267 -478 399 C ATOM 2264 CD2 LEU A 308 2.036 11.613 48.931 1.00 29.65 C ANISOU 2264 CD2 LEU A 308 3984 3921 3358 -395 36 479 C ATOM 2265 N LEU A 309 1.619 11.169 54.316 1.00 30.95 N ANISOU 2265 N LEU A 309 4219 4003 3535 -153 359 160 N ATOM 2266 CA LEU A 309 1.082 11.725 55.566 1.00 32.47 C ANISOU 2266 CA LEU A 309 4541 4063 3732 -190 280 138 C ATOM 2267 C LEU A 309 1.995 12.735 56.238 1.00 32.63 C ANISOU 2267 C LEU A 309 4547 4198 3650 -163 236 133 C ATOM 2268 O LEU A 309 1.500 13.635 56.893 1.00 33.85 O ANISOU 2268 O LEU A 309 4637 4181 4043 -226 176 36 O ATOM 2269 CB LEU A 309 0.671 10.621 56.533 1.00 32.66 C ANISOU 2269 CB LEU A 309 4647 4024 3735 -86 353 252 C ATOM 2270 CG LEU A 309 -0.206 11.121 57.692 1.00 33.92 C ANISOU 2270 CG LEU A 309 4759 4183 3944 -253 230 16 C ATOM 2271 CD1 LEU A 309 -1.615 11.579 57.251 1.00 38.04 C ANISOU 2271 CD1 LEU A 309 5140 4457 4857 99 413 23 C ATOM 2272 CD2 LEU A 309 -0.254 10.072 58.778 1.00 37.48 C ANISOU 2272 CD2 LEU A 309 5319 4506 4414 -163 -53 277 C ATOM 2273 N SER A 310 3.300 12.641 55.992 1.00 32.15 N ANISOU 2273 N SER A 310 4532 4213 3468 -167 123 250 N ATOM 2274 CA SER A 310 4.258 13.561 56.577 1.00 32.41 C ANISOU 2274 CA SER A 310 4565 4162 3585 -240 196 295 C ATOM 2275 C SER A 310 4.180 14.974 55.925 1.00 32.17 C ANISOU 2275 C SER A 310 4679 4197 3345 -167 59 248 C ATOM 2276 O SER A 310 4.588 15.952 56.507 1.00 31.13 O ANISOU 2276 O SER A 310 4687 4042 3097 -191 249 228 O ATOM 2277 CB SER A 310 5.691 12.961 56.533 1.00 33.02 C ANISOU 2277 CB SER A 310 4564 4350 3629 -198 170 276 C ATOM 2278 OG SER A 310 6.009 12.414 55.237 1.00 32.51 O ANISOU 2278 OG SER A 310 4038 4334 3979 -337 214 -154 O ATOM 2279 N GLY A 311 3.639 15.066 54.718 1.00 31.67 N ANISOU 2279 N GLY A 311 4713 4174 3146 -141 41 269 N ATOM 2280 CA GLY A 311 3.523 16.373 54.091 1.00 30.13 C ANISOU 2280 CA GLY A 311 4657 4008 2783 -54 98 123 C ATOM 2281 C GLY A 311 3.954 16.390 52.651 1.00 30.99 C ANISOU 2281 C GLY A 311 4663 4102 3007 -11 231 92 C ATOM 2282 O GLY A 311 3.925 17.463 52.040 1.00 32.19 O ANISOU 2282 O GLY A 311 5141 4108 2981 111 381 -16 O ATOM 2283 N ARG A 312 4.300 15.217 52.088 1.00 28.93 N ANISOU 2283 N ARG A 312 4278 3869 2843 -94 24 64 N ATOM 2284 CA ARG A 312 4.653 15.163 50.650 1.00 28.88 C ANISOU 2284 CA ARG A 312 3992 4076 2903 -147 -30 130 C ATOM 2285 C ARG A 312 3.449 15.424 49.744 1.00 28.33 C ANISOU 2285 C ARG A 312 3846 4046 2871 -182 -33 196 C ATOM 2286 O ARG A 312 2.293 15.236 50.152 1.00 28.89 O ANISOU 2286 O ARG A 312 3916 4223 2838 -238 -87 127 O ATOM 2287 CB ARG A 312 5.270 13.809 50.255 1.00 27.96 C ANISOU 2287 CB ARG A 312 3754 3957 2912 -122 -42 171 C ATOM 2288 CG ARG A 312 6.664 13.556 50.880 1.00 28.01 C ANISOU 2288 CG ARG A 312 3549 3945 3145 -116 -141 305 C ATOM 2289 CD ARG A 312 7.294 12.260 50.284 1.00 27.96 C ANISOU 2289 CD ARG A 312 3598 4178 2847 -148 -52 202 C ATOM 2290 NE ARG A 312 8.605 11.953 50.848 1.00 30.01 N ANISOU 2290 NE ARG A 312 3581 4652 3170 -466 -233 -6 N ATOM 2291 CZ ARG A 312 8.816 11.234 51.944 1.00 28.35 C ANISOU 2291 CZ ARG A 312 3330 3953 3486 -263 -176 113 C ATOM 2292 NH1 ARG A 312 7.796 10.769 52.686 1.00 30.72 N1+ ANISOU 2292 NH1 ARG A 312 3817 4257 3596 -195 29 497 N1+ ATOM 2293 NH2 ARG A 312 10.075 11.023 52.335 1.00 31.65 N ANISOU 2293 NH2 ARG A 312 3429 4651 3942 -157 -51 2 N ATOM 2294 N THR A 313 3.738 15.879 48.513 1.00 26.68 N ANISOU 2294 N THR A 313 3816 3849 2471 -241 -100 54 N ATOM 2295 CA THR A 313 2.715 16.108 47.502 1.00 27.15 C ANISOU 2295 CA THR A 313 3772 3873 2670 -206 -109 -51 C ATOM 2296 C THR A 313 3.107 15.295 46.290 1.00 26.96 C ANISOU 2296 C THR A 313 3707 3808 2725 -216 -164 -173 C ATOM 2297 O THR A 313 4.262 15.348 45.894 1.00 27.77 O ANISOU 2297 O THR A 313 3921 4069 2561 -317 -36 -340 O ATOM 2298 CB THR A 313 2.728 17.609 47.046 1.00 27.76 C ANISOU 2298 CB THR A 313 3974 3821 2749 -217 -135 -45 C ATOM 2299 CG2 THR A 313 1.743 17.843 45.946 1.00 30.78 C ANISOU 2299 CG2 THR A 313 4279 4063 3351 -144 -438 78 C ATOM 2300 OG1 THR A 313 2.385 18.484 48.131 1.00 30.82 O ANISOU 2300 OG1 THR A 313 4500 3886 3324 -196 -121 -331 O ATOM 2301 N TRP A 314 2.158 14.565 45.685 1.00 26.42 N ANISOU 2301 N TRP A 314 3630 3871 2537 -114 -183 -50 N ATOM 2302 CA TRP A 314 2.445 13.754 44.513 1.00 27.41 C ANISOU 2302 CA TRP A 314 3787 3898 2728 -48 -193 -31 C ATOM 2303 C TRP A 314 1.505 14.215 43.424 1.00 27.88 C ANISOU 2303 C TRP A 314 3770 4054 2768 30 -178 68 C ATOM 2304 O TRP A 314 0.303 14.291 43.638 1.00 28.26 O ANISOU 2304 O TRP A 314 3926 4144 2666 48 -124 -134 O ATOM 2305 CB TRP A 314 2.100 12.307 44.804 1.00 28.42 C ANISOU 2305 CB TRP A 314 3874 3844 3079 -100 -56 -37 C ATOM 2306 CG TRP A 314 2.896 11.284 44.066 1.00 27.57 C ANISOU 2306 CG TRP A 314 4089 3685 2700 -177 55 53 C ATOM 2307 CD1 TRP A 314 3.878 11.492 43.119 1.00 27.19 C ANISOU 2307 CD1 TRP A 314 3628 3766 2935 -39 -151 -45 C ATOM 2308 CD2 TRP A 314 2.725 9.870 44.166 1.00 27.58 C ANISOU 2308 CD2 TRP A 314 3915 3836 2728 -75 -174 51 C ATOM 2309 CE2 TRP A 314 3.667 9.274 43.318 1.00 28.92 C ANISOU 2309 CE2 TRP A 314 4103 3662 3221 -131 65 -112 C ATOM 2310 CE3 TRP A 314 1.896 9.049 44.950 1.00 28.75 C ANISOU 2310 CE3 TRP A 314 4052 3699 3170 -369 -171 29 C ATOM 2311 NE1 TRP A 314 4.340 10.281 42.662 1.00 28.87 N ANISOU 2311 NE1 TRP A 314 4080 3731 3159 -105 -231 70 N ATOM 2312 CZ2 TRP A 314 3.769 7.883 43.187 1.00 29.94 C ANISOU 2312 CZ2 TRP A 314 4250 3547 3575 -208 119 19 C ATOM 2313 CZ3 TRP A 314 2.007 7.681 44.835 1.00 29.68 C ANISOU 2313 CZ3 TRP A 314 4079 3808 3388 -229 -131 -20 C ATOM 2314 CH2 TRP A 314 2.944 7.110 43.982 1.00 31.51 C ANISOU 2314 CH2 TRP A 314 4555 3845 3570 -188 94 -47 C ATOM 2315 N LYS A 315 2.053 14.533 42.258 1.00 26.67 N ANISOU 2315 N LYS A 315 3779 3951 2403 68 -284 -54 N ATOM 2316 CA LYS A 315 1.174 14.964 41.188 1.00 28.19 C ANISOU 2316 CA LYS A 315 3897 4018 2794 80 -177 87 C ATOM 2317 C LYS A 315 1.624 14.505 39.833 1.00 27.10 C ANISOU 2317 C LYS A 315 3855 3818 2623 -31 -184 -32 C ATOM 2318 O LYS A 315 2.742 14.091 39.654 1.00 27.78 O ANISOU 2318 O LYS A 315 3963 3828 2764 -262 -172 2 O ATOM 2319 CB LYS A 315 0.999 16.479 41.189 1.00 29.86 C ANISOU 2319 CB LYS A 315 4211 4000 3133 -33 -210 5 C ATOM 2320 CG LYS A 315 2.240 17.295 41.037 1.00 32.02 C ANISOU 2320 CG LYS A 315 4001 4597 3566 219 -67 17 C ATOM 2321 CD LYS A 315 2.021 18.631 41.750 1.00 35.43 C ANISOU 2321 CD LYS A 315 4925 4613 3923 130 167 -324 C ATOM 2322 CE LYS A 315 0.983 19.476 41.005 1.00 38.58 C ANISOU 2322 CE LYS A 315 5146 4837 4674 47 220 -245 C ATOM 2323 NZ LYS A 315 0.409 20.590 41.820 1.00 43.46 N1+ ANISOU 2323 NZ LYS A 315 6124 4917 5471 0 302 -516 N1+ ATOM 2324 N GLY A 316 0.708 14.567 38.869 1.00 27.12 N ANISOU 2324 N GLY A 316 3879 3992 2432 84 -102 109 N ATOM 2325 CA GLY A 316 1.092 14.272 37.493 1.00 27.27 C ANISOU 2325 CA GLY A 316 3993 3899 2467 234 57 54 C ATOM 2326 C GLY A 316 0.461 15.318 36.618 1.00 29.20 C ANISOU 2326 C GLY A 316 4368 4011 2717 244 97 51 C ATOM 2327 O GLY A 316 -0.318 16.165 37.096 1.00 29.62 O ANISOU 2327 O GLY A 316 4464 3880 2909 309 -12 58 O ATOM 2328 N ALA A 317 0.799 15.258 35.337 1.00 28.83 N ANISOU 2328 N ALA A 317 4623 3844 2487 176 -13 47 N ATOM 2329 CA ALA A 317 0.236 16.182 34.371 1.00 29.32 C ANISOU 2329 CA ALA A 317 4716 3820 2604 91 50 74 C ATOM 2330 C ALA A 317 0.457 15.689 32.946 1.00 29.49 C ANISOU 2330 C ALA A 317 4721 3763 2722 180 42 10 C ATOM 2331 O ALA A 317 1.345 14.881 32.680 1.00 31.30 O ANISOU 2331 O ALA A 317 4878 4146 2866 233 20 161 O ATOM 2332 CB ALA A 317 0.855 17.551 34.566 1.00 30.23 C ANISOU 2332 CB ALA A 317 4953 3745 2788 43 -50 94 C ATOM 2333 N ILE A 318 -0.373 16.209 32.046 1.00 28.91 N ANISOU 2333 N ILE A 318 4684 3671 2628 243 47 48 N ATOM 2334 CA ILE A 318 -0.204 16.024 30.616 1.00 29.35 C ANISOU 2334 CA ILE A 318 4577 3744 2828 230 64 32 C ATOM 2335 C ILE A 318 0.320 17.356 30.021 1.00 27.68 C ANISOU 2335 C ILE A 318 4338 3501 2678 314 75 1 C ATOM 2336 O ILE A 318 -0.042 18.453 30.460 1.00 28.07 O ANISOU 2336 O ILE A 318 4316 3491 2858 566 72 124 O ATOM 2337 CB ILE A 318 -1.567 15.514 29.947 1.00 29.91 C ANISOU 2337 CB ILE A 318 4611 3817 2936 166 114 62 C ATOM 2338 CG1 ILE A 318 -1.966 14.130 30.513 1.00 31.62 C ANISOU 2338 CG1 ILE A 318 4583 4210 3220 -22 26 50 C ATOM 2339 CG2 ILE A 318 -1.457 15.461 28.427 1.00 31.27 C ANISOU 2339 CG2 ILE A 318 4571 4218 3090 218 64 -115 C ATOM 2340 CD1 ILE A 318 -3.347 13.567 30.062 1.00 33.35 C ANISOU 2340 CD1 ILE A 318 4872 4155 3642 64 -36 81 C ATOM 2341 N PHE A 319 1.223 17.266 29.061 1.00 26.58 N ANISOU 2341 N PHE A 319 4032 3291 2775 325 56 87 N ATOM 2342 CA PHE A 319 1.720 18.434 28.339 1.00 27.24 C ANISOU 2342 CA PHE A 319 4185 3389 2774 317 83 -4 C ATOM 2343 C PHE A 319 2.272 19.475 29.275 1.00 27.18 C ANISOU 2343 C PHE A 319 4088 3418 2821 215 118 -5 C ATOM 2344 O PHE A 319 2.041 20.683 29.082 1.00 27.78 O ANISOU 2344 O PHE A 319 4503 3418 2632 290 77 -163 O ATOM 2345 CB PHE A 319 0.650 19.074 27.452 1.00 27.14 C ANISOU 2345 CB PHE A 319 4100 3348 2864 342 117 58 C ATOM 2346 CG PHE A 319 1.243 19.976 26.379 1.00 27.03 C ANISOU 2346 CG PHE A 319 4379 3257 2631 399 212 81 C ATOM 2347 CD1 PHE A 319 2.258 19.506 25.511 1.00 28.04 C ANISOU 2347 CD1 PHE A 319 4449 3221 2982 433 461 301 C ATOM 2348 CD2 PHE A 319 0.782 21.278 26.216 1.00 27.40 C ANISOU 2348 CD2 PHE A 319 4260 3087 3063 244 132 283 C ATOM 2349 CE1 PHE A 319 2.799 20.350 24.496 1.00 27.14 C ANISOU 2349 CE1 PHE A 319 4347 3097 2866 517 383 248 C ATOM 2350 CE2 PHE A 319 1.322 22.120 25.209 1.00 29.94 C ANISOU 2350 CE2 PHE A 319 4395 3652 3327 322 546 175 C ATOM 2351 CZ PHE A 319 2.308 21.658 24.352 1.00 27.76 C ANISOU 2351 CZ PHE A 319 4256 3330 2960 476 430 116 C ATOM 2352 N GLY A 320 2.945 18.997 30.313 1.00 27.59 N ANISOU 2352 N GLY A 320 4050 3612 2818 134 187 14 N ATOM 2353 CA GLY A 320 3.627 19.889 31.241 1.00 27.80 C ANISOU 2353 CA GLY A 320 4156 3542 2862 242 201 -111 C ATOM 2354 C GLY A 320 2.758 20.842 32.022 1.00 27.79 C ANISOU 2354 C GLY A 320 4222 3498 2836 246 223 -55 C ATOM 2355 O GLY A 320 3.285 21.823 32.570 1.00 29.30 O ANISOU 2355 O GLY A 320 4505 3607 3020 230 190 -85 O ATOM 2356 N GLY A 321 1.450 20.547 32.074 1.00 28.05 N ANISOU 2356 N GLY A 321 4280 3608 2770 368 275 -178 N ATOM 2357 CA GLY A 321 0.460 21.378 32.765 1.00 28.27 C ANISOU 2357 CA GLY A 321 4260 3594 2886 443 380 -4 C ATOM 2358 C GLY A 321 0.087 22.664 32.030 1.00 28.51 C ANISOU 2358 C GLY A 321 4355 3677 2799 495 288 -44 C ATOM 2359 O GLY A 321 -0.751 23.463 32.517 1.00 30.34 O ANISOU 2359 O GLY A 321 4602 3902 3023 614 336 -152 O ATOM 2360 N PHE A 322 0.658 22.846 30.838 1.00 29.10 N ANISOU 2360 N PHE A 322 4521 3610 2924 233 301 -15 N ATOM 2361 CA PHE A 322 0.366 23.994 30.004 1.00 29.35 C ANISOU 2361 CA PHE A 322 4552 3651 2947 268 155 1 C ATOM 2362 C PHE A 322 -1.012 23.947 29.339 1.00 29.78 C ANISOU 2362 C PHE A 322 4703 3562 3047 219 167 35 C ATOM 2363 O PHE A 322 -1.380 22.966 28.680 1.00 30.38 O ANISOU 2363 O PHE A 322 4866 3614 3063 204 1 2 O ATOM 2364 CB PHE A 322 1.438 24.136 28.894 1.00 30.08 C ANISOU 2364 CB PHE A 322 4626 3761 3040 94 193 213 C ATOM 2365 CG PHE A 322 2.818 24.557 29.375 1.00 30.87 C ANISOU 2365 CG PHE A 322 4632 3867 3229 123 136 216 C ATOM 2366 CD1 PHE A 322 3.025 25.747 30.085 1.00 30.60 C ANISOU 2366 CD1 PHE A 322 4504 3676 3446 140 1 258 C ATOM 2367 CD2 PHE A 322 3.929 23.794 29.046 1.00 30.23 C ANISOU 2367 CD2 PHE A 322 4626 3555 3305 122 180 170 C ATOM 2368 CE1 PHE A 322 4.301 26.147 30.497 1.00 30.01 C ANISOU 2368 CE1 PHE A 322 4414 3213 3774 18 285 169 C ATOM 2369 CE2 PHE A 322 5.218 24.179 29.447 1.00 29.78 C ANISOU 2369 CE2 PHE A 322 4528 3389 3395 -69 243 333 C ATOM 2370 CZ PHE A 322 5.402 25.369 30.187 1.00 30.18 C ANISOU 2370 CZ PHE A 322 4365 3639 3463 55 201 295 C ATOM 2371 N LYS A 323 -1.757 25.023 29.509 1.00 30.43 N ANISOU 2371 N LYS A 323 4692 3761 3109 295 199 59 N ATOM 2372 CA LYS A 323 -2.898 25.323 28.637 1.00 29.86 C ANISOU 2372 CA LYS A 323 4728 3540 3075 295 161 -79 C ATOM 2373 C LYS A 323 -2.303 25.511 27.253 1.00 30.23 C ANISOU 2373 C LYS A 323 4769 3536 3177 230 198 -185 C ATOM 2374 O LYS A 323 -1.485 26.399 27.012 1.00 30.71 O ANISOU 2374 O LYS A 323 4892 3516 3258 243 181 -212 O ATOM 2375 CB LYS A 323 -3.575 26.591 29.142 1.00 30.67 C ANISOU 2375 CB LYS A 323 4831 3628 3190 296 245 -110 C ATOM 2376 CG LYS A 323 -4.323 26.343 30.462 1.00 31.34 C ANISOU 2376 CG LYS A 323 4939 3860 3107 448 243 -39 C ATOM 2377 CD LYS A 323 -5.146 27.532 30.830 1.00 32.68 C ANISOU 2377 CD LYS A 323 5232 3860 3324 471 320 -185 C ATOM 2378 CE LYS A 323 -5.834 27.356 32.147 1.00 34.56 C ANISOU 2378 CE LYS A 323 5345 4180 3605 38 453 86 C ATOM 2379 NZ LYS A 323 -7.020 26.463 32.061 1.00 35.47 N1+ ANISOU 2379 NZ LYS A 323 5354 4567 3553 36 199 -37 N1+ ATOM 2380 N SER A 324 -2.686 24.653 26.326 1.00 29.56 N ANISOU 2380 N SER A 324 4745 3395 3092 275 128 -180 N ATOM 2381 CA SER A 324 -1.809 24.481 25.155 1.00 28.92 C ANISOU 2381 CA SER A 324 4737 3255 2996 201 159 -102 C ATOM 2382 C SER A 324 -1.806 25.652 24.163 1.00 29.98 C ANISOU 2382 C SER A 324 4885 3290 3215 100 98 -127 C ATOM 2383 O SER A 324 -0.722 26.068 23.706 1.00 30.67 O ANISOU 2383 O SER A 324 4915 3564 3174 -106 55 -19 O ATOM 2384 CB SER A 324 -2.191 23.227 24.419 1.00 30.41 C ANISOU 2384 CB SER A 324 4786 3361 3405 170 99 -152 C ATOM 2385 OG SER A 324 -3.565 23.268 24.146 1.00 28.83 O ANISOU 2385 OG SER A 324 4613 3091 3251 452 218 -296 O ATOM 2386 N LYS A 325 -2.985 26.148 23.800 1.00 30.64 N ANISOU 2386 N LYS A 325 5052 3260 3329 93 68 -50 N ATOM 2387 CA LYS A 325 -3.039 27.230 22.791 1.00 30.97 C ANISOU 2387 CA LYS A 325 5061 3156 3547 89 71 73 C ATOM 2388 C LYS A 325 -2.451 28.551 23.350 1.00 31.22 C ANISOU 2388 C LYS A 325 5103 3130 3626 93 -18 80 C ATOM 2389 O LYS A 325 -1.850 29.317 22.612 1.00 32.75 O ANISOU 2389 O LYS A 325 5142 3358 3942 -11 74 -5 O ATOM 2390 CB LYS A 325 -4.438 27.400 22.216 1.00 31.11 C ANISOU 2390 CB LYS A 325 5113 3179 3526 104 128 145 C ATOM 2391 CG LYS A 325 -4.555 28.367 20.998 1.00 32.03 C ANISOU 2391 CG LYS A 325 5180 3320 3667 217 -12 42 C ATOM 2392 CD LYS A 325 -5.725 27.975 20.162 1.00 34.82 C ANISOU 2392 CD LYS A 325 5035 3761 4434 299 -121 73 C ATOM 2393 CE LYS A 325 -5.813 28.766 18.879 1.00 35.49 C ANISOU 2393 CE LYS A 325 5383 3826 4274 266 -205 -24 C ATOM 2394 NZ LYS A 325 -6.739 28.117 17.903 1.00 33.62 N1+ ANISOU 2394 NZ LYS A 325 5091 3523 4159 264 -214 116 N1+ ATOM 2395 N ASP A 326 -2.644 28.820 24.630 1.00 32.04 N ANISOU 2395 N ASP A 326 5233 3151 3787 108 31 43 N ATOM 2396 CA ASP A 326 -1.947 29.919 25.326 1.00 32.79 C ANISOU 2396 CA ASP A 326 5279 3273 3906 55 -35 -40 C ATOM 2397 C ASP A 326 -0.436 29.798 25.388 1.00 32.69 C ANISOU 2397 C ASP A 326 5304 3394 3723 57 44 -136 C ATOM 2398 O ASP A 326 0.308 30.786 25.190 1.00 33.67 O ANISOU 2398 O ASP A 326 5476 3418 3899 -6 -10 -95 O ATOM 2399 CB ASP A 326 -2.411 30.019 26.780 1.00 34.14 C ANISOU 2399 CB ASP A 326 5328 3533 4109 129 33 -126 C ATOM 2400 CG ASP A 326 -3.855 30.482 26.927 1.00 35.58 C ANISOU 2400 CG ASP A 326 5358 3547 4612 85 68 -198 C ATOM 2401 OD1 ASP A 326 -4.416 31.023 25.962 1.00 39.28 O ANISOU 2401 OD1 ASP A 326 5709 4014 5199 233 -140 -299 O ATOM 2402 OD2 ASP A 326 -4.417 30.291 28.028 1.00 39.37 O1- ANISOU 2402 OD2 ASP A 326 5838 3896 5223 173 383 -569 O1- ATOM 2403 N SER A 327 0.033 28.595 25.702 1.00 31.86 N ANISOU 2403 N SER A 327 5179 3395 3529 35 -22 -281 N ATOM 2404 CA SER A 327 1.403 28.410 26.116 1.00 32.53 C ANISOU 2404 CA SER A 327 5158 3642 3559 40 6 -311 C ATOM 2405 C SER A 327 2.335 28.179 24.943 1.00 32.40 C ANISOU 2405 C SER A 327 5171 3691 3446 -93 -16 -390 C ATOM 2406 O SER A 327 3.459 28.667 24.937 1.00 33.36 O ANISOU 2406 O SER A 327 5196 3990 3488 -178 -56 -359 O ATOM 2407 CB SER A 327 1.473 27.220 27.046 1.00 31.88 C ANISOU 2407 CB SER A 327 5020 3718 3375 60 -19 -216 C ATOM 2408 OG SER A 327 0.813 27.504 28.263 1.00 33.87 O ANISOU 2408 OG SER A 327 5338 3817 3714 427 18 -455 O ATOM 2409 N VAL A 328 1.890 27.435 23.930 1.00 32.71 N ANISOU 2409 N VAL A 328 5236 3683 3509 -113 -78 -322 N ATOM 2410 CA VAL A 328 2.803 27.126 22.847 1.00 31.82 C ANISOU 2410 CA VAL A 328 5309 3514 3266 -197 23 -299 C ATOM 2411 C VAL A 328 3.407 28.385 22.171 1.00 31.90 C ANISOU 2411 C VAL A 328 5239 3582 3299 -169 50 -285 C ATOM 2412 O VAL A 328 4.614 28.445 21.973 1.00 31.88 O ANISOU 2412 O VAL A 328 5392 3420 3298 -281 93 -309 O ATOM 2413 CB VAL A 328 2.148 26.106 21.847 1.00 31.28 C ANISOU 2413 CB VAL A 328 5302 3341 3242 -158 21 -358 C ATOM 2414 CG1 VAL A 328 2.876 26.096 20.507 1.00 32.76 C ANISOU 2414 CG1 VAL A 328 5305 3828 3312 74 163 -68 C ATOM 2415 CG2 VAL A 328 2.145 24.703 22.498 1.00 31.98 C ANISOU 2415 CG2 VAL A 328 5550 3458 3143 -210 56 -172 C ATOM 2416 N PRO A 329 2.580 29.388 21.841 1.00 32.02 N ANISOU 2416 N PRO A 329 5210 3596 3359 -199 142 -164 N ATOM 2417 CA PRO A 329 3.222 30.555 21.258 1.00 33.22 C ANISOU 2417 CA PRO A 329 5251 3688 3682 -164 85 -169 C ATOM 2418 C PRO A 329 4.205 31.233 22.202 1.00 34.04 C ANISOU 2418 C PRO A 329 5262 3723 3946 -181 174 -209 C ATOM 2419 O PRO A 329 5.222 31.753 21.734 1.00 35.53 O ANISOU 2419 O PRO A 329 5300 3903 4296 -168 154 -200 O ATOM 2420 CB PRO A 329 2.035 31.441 20.884 1.00 33.59 C ANISOU 2420 CB PRO A 329 5216 3743 3800 -150 118 -148 C ATOM 2421 CG PRO A 329 0.882 30.475 20.705 1.00 33.09 C ANISOU 2421 CG PRO A 329 5332 3621 3620 -126 75 -88 C ATOM 2422 CD PRO A 329 1.118 29.552 21.865 1.00 32.85 C ANISOU 2422 CD PRO A 329 5244 3763 3471 -71 99 -52 C ATOM 2423 N LYS A 330 3.917 31.229 23.505 1.00 34.37 N ANISOU 2423 N LYS A 330 5329 3807 3920 -195 6 -103 N ATOM 2424 CA LYS A 330 4.822 31.809 24.501 1.00 35.17 C ANISOU 2424 CA LYS A 330 5435 3834 4093 -246 76 -219 C ATOM 2425 C LYS A 330 6.119 31.052 24.585 1.00 34.56 C ANISOU 2425 C LYS A 330 5361 3849 3921 -327 -69 -208 C ATOM 2426 O LYS A 330 7.190 31.646 24.698 1.00 34.95 O ANISOU 2426 O LYS A 330 5569 3690 4020 -468 18 -164 O ATOM 2427 CB LYS A 330 4.158 31.838 25.864 1.00 35.43 C ANISOU 2427 CB LYS A 330 5350 3965 4146 -237 73 -228 C ATOM 2428 CG LYS A 330 3.042 32.847 25.959 1.00 38.35 C ANISOU 2428 CG LYS A 330 5407 4338 4825 -59 89 -41 C ATOM 2429 CD LYS A 330 2.440 32.782 27.361 1.00 42.76 C ANISOU 2429 CD LYS A 330 5851 5305 5088 -12 30 -120 C ATOM 2430 CE LYS A 330 1.967 34.144 27.808 1.00 46.32 C ANISOU 2430 CE LYS A 330 6044 5521 6035 154 -8 23 C ATOM 2431 NZ LYS A 330 0.796 34.558 26.981 1.00 48.38 N1+ ANISOU 2431 NZ LYS A 330 5982 6027 6370 60 -216 185 N1+ ATOM 2432 N LEU A 331 6.038 29.724 24.518 1.00 34.12 N ANISOU 2432 N LEU A 331 5418 3787 3759 -377 15 -217 N ATOM 2433 CA LEU A 331 7.242 28.906 24.507 1.00 34.70 C ANISOU 2433 CA LEU A 331 5355 4017 3811 -372 33 -253 C ATOM 2434 C LEU A 331 8.084 29.144 23.251 1.00 34.71 C ANISOU 2434 C LEU A 331 5330 4045 3813 -331 19 -273 C ATOM 2435 O LEU A 331 9.317 29.172 23.313 1.00 34.91 O ANISOU 2435 O LEU A 331 5439 4055 3768 -406 -207 -406 O ATOM 2436 CB LEU A 331 6.890 27.428 24.669 1.00 34.03 C ANISOU 2436 CB LEU A 331 5388 3869 3672 -272 114 -320 C ATOM 2437 CG LEU A 331 6.238 27.099 26.028 1.00 36.63 C ANISOU 2437 CG LEU A 331 5584 4443 3891 -297 102 -135 C ATOM 2438 CD1 LEU A 331 5.523 25.757 26.010 1.00 36.21 C ANISOU 2438 CD1 LEU A 331 5582 4396 3778 -261 130 50 C ATOM 2439 CD2 LEU A 331 7.221 27.236 27.219 1.00 38.37 C ANISOU 2439 CD2 LEU A 331 5568 4678 4330 -88 -55 -426 C ATOM 2440 N VAL A 332 7.435 29.337 22.109 1.00 36.04 N ANISOU 2440 N VAL A 332 5357 4273 4062 -367 -8 -286 N ATOM 2441 CA VAL A 332 8.192 29.623 20.888 1.00 37.04 C ANISOU 2441 CA VAL A 332 5418 4415 4241 -369 36 -243 C ATOM 2442 C VAL A 332 8.877 30.983 21.009 1.00 38.30 C ANISOU 2442 C VAL A 332 5513 4513 4524 -374 9 -305 C ATOM 2443 O VAL A 332 10.030 31.128 20.622 1.00 38.38 O ANISOU 2443 O VAL A 332 5434 4571 4574 -412 -86 -471 O ATOM 2444 CB VAL A 332 7.315 29.549 19.626 1.00 37.07 C ANISOU 2444 CB VAL A 332 5445 4525 4114 -361 98 -121 C ATOM 2445 CG1 VAL A 332 8.055 30.112 18.402 1.00 35.39 C ANISOU 2445 CG1 VAL A 332 5206 4237 4004 -179 215 -37 C ATOM 2446 CG2 VAL A 332 6.937 28.130 19.366 1.00 37.03 C ANISOU 2446 CG2 VAL A 332 5405 4500 4163 -332 324 -107 C ATOM 2447 N ALA A 333 8.152 31.967 21.541 1.00 39.82 N ANISOU 2447 N ALA A 333 5771 4551 4808 -336 -25 -308 N ATOM 2448 CA ALA A 333 8.711 33.316 21.751 1.00 41.13 C ANISOU 2448 CA ALA A 333 5791 4716 5118 -310 -54 -264 C ATOM 2449 C ALA A 333 9.879 33.278 22.725 1.00 41.80 C ANISOU 2449 C ALA A 333 5870 4777 5233 -282 -39 -266 C ATOM 2450 O ALA A 333 10.877 33.974 22.527 1.00 42.04 O ANISOU 2450 O ALA A 333 5872 4712 5389 -206 48 -142 O ATOM 2451 CB ALA A 333 7.627 34.256 22.243 1.00 41.41 C ANISOU 2451 CB ALA A 333 5939 4678 5117 -279 -10 -321 C ATOM 2452 N ASP A 334 9.769 32.439 23.762 1.00 42.17 N ANISOU 2452 N ASP A 334 5945 4843 5233 -282 -86 -287 N ATOM 2453 CA ASP A 334 10.880 32.236 24.693 1.00 42.59 C ANISOU 2453 CA ASP A 334 5949 4861 5369 -297 -85 -434 C ATOM 2454 C ASP A 334 12.089 31.680 23.939 1.00 42.23 C ANISOU 2454 C ASP A 334 5882 4858 5302 -383 -112 -506 C ATOM 2455 O ASP A 334 13.225 32.044 24.206 1.00 42.74 O ANISOU 2455 O ASP A 334 5964 4867 5405 -447 -154 -659 O ATOM 2456 CB ASP A 334 10.473 31.304 25.847 1.00 43.45 C ANISOU 2456 CB ASP A 334 6095 5046 5368 -254 -51 -357 C ATOM 2457 CG ASP A 334 9.514 31.968 26.848 1.00 45.60 C ANISOU 2457 CG ASP A 334 6273 5272 5780 -156 134 -217 C ATOM 2458 OD1 ASP A 334 9.396 33.211 26.860 1.00 48.18 O ANISOU 2458 OD1 ASP A 334 6717 5446 6140 -213 56 34 O ATOM 2459 OD2 ASP A 334 8.869 31.240 27.644 1.00 48.86 O1- ANISOU 2459 OD2 ASP A 334 6949 5593 6021 -155 255 -34 O1- ATOM 2460 N PHE A 335 11.841 30.779 22.986 1.00 40.54 N ANISOU 2460 N PHE A 335 5736 4591 5075 -446 -186 -652 N ATOM 2461 CA PHE A 335 12.936 30.241 22.187 1.00 41.37 C ANISOU 2461 CA PHE A 335 5726 4710 5282 -412 -130 -532 C ATOM 2462 C PHE A 335 13.497 31.322 21.270 1.00 42.17 C ANISOU 2462 C PHE A 335 5801 4822 5398 -415 -123 -529 C ATOM 2463 O PHE A 335 14.698 31.411 21.065 1.00 42.59 O ANISOU 2463 O PHE A 335 5876 4833 5472 -360 -34 -601 O ATOM 2464 CB PHE A 335 12.462 29.029 21.354 1.00 40.24 C ANISOU 2464 CB PHE A 335 5588 4636 5064 -459 -145 -579 C ATOM 2465 CG PHE A 335 13.535 28.441 20.455 1.00 39.62 C ANISOU 2465 CG PHE A 335 5423 4477 5153 -307 -126 -330 C ATOM 2466 CD1 PHE A 335 14.514 27.598 20.966 1.00 40.98 C ANISOU 2466 CD1 PHE A 335 5474 4679 5415 -206 71 -263 C ATOM 2467 CD2 PHE A 335 13.557 28.736 19.098 1.00 37.57 C ANISOU 2467 CD2 PHE A 335 5210 4028 5036 -589 -148 -652 C ATOM 2468 CE1 PHE A 335 15.513 27.070 20.136 1.00 39.98 C ANISOU 2468 CE1 PHE A 335 5565 4397 5226 -237 27 -354 C ATOM 2469 CE2 PHE A 335 14.542 28.215 18.259 1.00 35.59 C ANISOU 2469 CE2 PHE A 335 4847 3757 4919 -682 -66 -315 C ATOM 2470 CZ PHE A 335 15.513 27.372 18.771 1.00 37.97 C ANISOU 2470 CZ PHE A 335 5134 4120 5171 -417 -49 -257 C ATOM 2471 N MET A 336 12.623 32.164 20.736 1.00 44.05 N ANISOU 2471 N MET A 336 6021 5033 5681 -368 -118 -397 N ATOM 2472 CA MET A 336 13.057 33.185 19.784 1.00 45.97 C ANISOU 2472 CA MET A 336 6181 5283 6001 -466 -66 -281 C ATOM 2473 C MET A 336 13.783 34.310 20.510 1.00 47.44 C ANISOU 2473 C MET A 336 6312 5505 6208 -440 -74 -284 C ATOM 2474 O MET A 336 14.594 35.018 19.912 1.00 49.06 O ANISOU 2474 O MET A 336 6420 5733 6485 -480 -58 -253 O ATOM 2475 CB MET A 336 11.874 33.733 18.995 1.00 46.14 C ANISOU 2475 CB MET A 336 6269 5266 5995 -448 -66 -205 C ATOM 2476 CG MET A 336 11.249 32.741 18.005 1.00 46.67 C ANISOU 2476 CG MET A 336 6488 5039 6202 -676 -2 -113 C ATOM 2477 SD MET A 336 12.389 32.106 16.757 1.00 47.86 S ANISOU 2477 SD MET A 336 7049 4682 6452 -1182 225 -12 S ATOM 2478 CE MET A 336 12.602 33.547 15.709 1.00 47.17 C ANISOU 2478 CE MET A 336 6658 5108 6154 -821 219 220 C ATOM 2479 N ALA A 337 13.501 34.438 21.801 1.00 48.34 N ANISOU 2479 N ALA A 337 6379 5672 6313 -427 -99 -351 N ATOM 2480 CA ALA A 337 14.163 35.406 22.680 1.00 48.95 C ANISOU 2480 CA ALA A 337 6399 5762 6437 -425 -146 -374 C ATOM 2481 C ALA A 337 15.468 34.843 23.222 1.00 49.81 C ANISOU 2481 C ALA A 337 6490 5904 6530 -367 -160 -370 C ATOM 2482 O ALA A 337 16.142 35.489 24.040 1.00 50.43 O ANISOU 2482 O ALA A 337 6597 5929 6634 -422 -198 -462 O ATOM 2483 CB ALA A 337 13.242 35.780 23.824 1.00 48.94 C ANISOU 2483 CB ALA A 337 6370 5802 6421 -447 -124 -393 C ATOM 2484 N LYS A 338 15.818 33.646 22.746 1.00 50.19 N ANISOU 2484 N LYS A 338 6523 5959 6587 -299 -132 -329 N ATOM 2485 CA LYS A 338 17.000 32.881 23.162 1.00 50.34 C ANISOU 2485 CA LYS A 338 6502 6042 6582 -250 -131 -299 C ATOM 2486 C LYS A 338 17.040 32.551 24.661 1.00 50.17 C ANISOU 2486 C LYS A 338 6476 6023 6564 -244 -154 -361 C ATOM 2487 O LYS A 338 18.103 32.435 25.250 1.00 51.00 O ANISOU 2487 O LYS A 338 6524 6158 6694 -245 -175 -381 O ATOM 2488 CB LYS A 338 18.302 33.522 22.632 1.00 50.30 C ANISOU 2488 CB LYS A 338 6488 6068 6552 -234 -143 -282 C ATOM 2489 CG LYS A 338 18.311 33.656 21.106 1.00 50.36 C ANISOU 2489 CG LYS A 338 6502 6049 6581 -119 -19 -157 C ATOM 2490 CD LYS A 338 19.391 34.601 20.573 1.00 50.74 C ANISOU 2490 CD LYS A 338 6573 6131 6574 -203 -134 -195 C ATOM 2491 CE LYS A 338 19.041 35.067 19.159 1.00 51.69 C ANISOU 2491 CE LYS A 338 6849 6380 6408 -181 129 -201 C ATOM 2492 NZ LYS A 338 19.895 36.216 18.674 1.00 52.21 N1+ ANISOU 2492 NZ LYS A 338 7159 6188 6487 -158 -110 -203 N1+ ATOM 2493 N LYS A 339 15.867 32.364 25.260 1.00 50.03 N ANISOU 2493 N LYS A 339 6515 5990 6505 -258 -162 -446 N ATOM 2494 CA LYS A 339 15.762 31.959 26.665 1.00 50.03 C ANISOU 2494 CA LYS A 339 6499 6011 6498 -213 -180 -408 C ATOM 2495 C LYS A 339 16.245 30.542 26.927 1.00 48.94 C ANISOU 2495 C LYS A 339 6419 5879 6296 -235 -237 -469 C ATOM 2496 O LYS A 339 16.722 30.236 28.015 1.00 49.09 O ANISOU 2496 O LYS A 339 6553 5821 6278 -246 -258 -491 O ATOM 2497 CB LYS A 339 14.329 32.125 27.187 1.00 50.35 C ANISOU 2497 CB LYS A 339 6448 6121 6560 -260 -199 -431 C ATOM 2498 CG LYS A 339 14.047 33.454 27.885 1.00 51.72 C ANISOU 2498 CG LYS A 339 6604 6213 6831 -96 -123 -353 C ATOM 2499 CD LYS A 339 12.539 33.696 28.024 1.00 51.93 C ANISOU 2499 CD LYS A 339 6626 6299 6804 -152 -52 -342 C ATOM 2500 CE LYS A 339 12.221 35.135 28.437 1.00 54.15 C ANISOU 2500 CE LYS A 339 6815 6432 7327 -12 10 -135 C ATOM 2501 NZ LYS A 339 10.802 35.504 28.130 1.00 55.28 N1+ ANISOU 2501 NZ LYS A 339 6784 6737 7483 -134 69 14 N1+ ATOM 2502 N PHE A 340 16.094 29.662 25.939 1.00 47.38 N ANISOU 2502 N PHE A 340 6272 5671 6059 -228 -246 -480 N ATOM 2503 CA PHE A 340 16.578 28.286 26.080 1.00 46.19 C ANISOU 2503 CA PHE A 340 6058 5583 5908 -252 -263 -422 C ATOM 2504 C PHE A 340 16.995 27.740 24.720 1.00 45.45 C ANISOU 2504 C PHE A 340 6026 5461 5779 -283 -316 -449 C ATOM 2505 O PHE A 340 16.629 28.308 23.689 1.00 45.75 O ANISOU 2505 O PHE A 340 6115 5364 5904 -343 -389 -546 O ATOM 2506 CB PHE A 340 15.524 27.377 26.739 1.00 45.88 C ANISOU 2506 CB PHE A 340 6057 5557 5818 -249 -277 -348 C ATOM 2507 CG PHE A 340 14.169 27.403 26.057 1.00 43.83 C ANISOU 2507 CG PHE A 340 5788 5207 5659 -297 -203 -350 C ATOM 2508 CD1 PHE A 340 13.940 26.666 24.892 1.00 42.41 C ANISOU 2508 CD1 PHE A 340 5752 5067 5295 -232 -200 -157 C ATOM 2509 CD2 PHE A 340 13.124 28.137 26.600 1.00 43.16 C ANISOU 2509 CD2 PHE A 340 5747 5047 5604 -309 -315 -335 C ATOM 2510 CE1 PHE A 340 12.686 26.692 24.268 1.00 43.35 C ANISOU 2510 CE1 PHE A 340 5759 5039 5672 -233 -103 -144 C ATOM 2511 CE2 PHE A 340 11.880 28.167 26.010 1.00 44.02 C ANISOU 2511 CE2 PHE A 340 5835 5278 5610 -164 -242 -140 C ATOM 2512 CZ PHE A 340 11.653 27.440 24.823 1.00 44.03 C ANISOU 2512 CZ PHE A 340 5802 5225 5700 -295 -95 -276 C ATOM 2513 N ALA A 341 17.803 26.676 24.748 1.00 44.88 N ANISOU 2513 N ALA A 341 5948 5438 5666 -270 -312 -452 N ATOM 2514 CA ALA A 341 18.298 25.989 23.557 1.00 43.89 C ANISOU 2514 CA ALA A 341 5708 5414 5552 -321 -198 -326 C ATOM 2515 C ALA A 341 17.494 24.712 23.266 1.00 42.94 C ANISOU 2515 C ALA A 341 5658 5333 5322 -325 -174 -267 C ATOM 2516 O ALA A 341 17.079 24.000 24.181 1.00 42.72 O ANISOU 2516 O ALA A 341 5680 5282 5270 -411 -252 -256 O ATOM 2517 CB ALA A 341 19.780 25.652 23.725 1.00 44.61 C ANISOU 2517 CB ALA A 341 5865 5378 5707 -228 -259 -341 C ATOM 2518 N LEU A 342 17.263 24.431 21.991 1.00 41.02 N ANISOU 2518 N LEU A 342 5317 5226 5040 -322 -145 -207 N ATOM 2519 CA LEU A 342 16.624 23.160 21.605 1.00 39.57 C ANISOU 2519 CA LEU A 342 5088 5123 4821 -371 -65 -73 C ATOM 2520 C LEU A 342 17.573 22.176 20.922 1.00 39.56 C ANISOU 2520 C LEU A 342 5089 5227 4714 -366 -91 -81 C ATOM 2521 O LEU A 342 17.331 20.978 20.925 1.00 39.33 O ANISOU 2521 O LEU A 342 5047 5276 4618 -502 -26 -19 O ATOM 2522 CB LEU A 342 15.398 23.411 20.721 1.00 38.96 C ANISOU 2522 CB LEU A 342 5007 5079 4716 -327 -9 -66 C ATOM 2523 CG LEU A 342 14.156 23.960 21.430 1.00 37.51 C ANISOU 2523 CG LEU A 342 4998 4645 4608 -299 123 -17 C ATOM 2524 CD1 LEU A 342 13.095 24.284 20.402 1.00 36.66 C ANISOU 2524 CD1 LEU A 342 4776 4627 4526 -414 375 148 C ATOM 2525 CD2 LEU A 342 13.623 22.974 22.507 1.00 36.71 C ANISOU 2525 CD2 LEU A 342 4720 4633 4594 -220 531 -217 C ATOM 2526 N ASP A 343 18.662 22.678 20.338 1.00 39.96 N ANISOU 2526 N ASP A 343 5068 5300 4813 -402 -34 -115 N ATOM 2527 CA ASP A 343 19.647 21.807 19.665 1.00 40.92 C ANISOU 2527 CA ASP A 343 5181 5429 4937 -296 -11 -65 C ATOM 2528 C ASP A 343 20.196 20.580 20.439 1.00 40.25 C ANISOU 2528 C ASP A 343 5145 5374 4771 -285 -16 -123 C ATOM 2529 O ASP A 343 20.316 19.498 19.855 1.00 39.98 O ANISOU 2529 O ASP A 343 5133 5359 4697 -396 9 -122 O ATOM 2530 CB ASP A 343 20.797 22.647 19.082 1.00 41.53 C ANISOU 2530 CB ASP A 343 5174 5532 5074 -293 0 -41 C ATOM 2531 CG ASP A 343 20.406 23.350 17.802 1.00 44.98 C ANISOU 2531 CG ASP A 343 5705 5848 5537 -223 -40 117 C ATOM 2532 OD1 ASP A 343 19.359 22.993 17.239 1.00 47.78 O ANISOU 2532 OD1 ASP A 343 5912 6218 6021 -168 -200 357 O ATOM 2533 OD2 ASP A 343 21.152 24.236 17.334 1.00 49.19 O1- ANISOU 2533 OD2 ASP A 343 6195 6148 6347 -284 -31 214 O1- ATOM 2534 N PRO A 344 20.572 20.737 21.738 1.00 39.95 N ANISOU 2534 N PRO A 344 5116 5320 4740 -221 -74 -149 N ATOM 2535 CA PRO A 344 21.024 19.559 22.494 1.00 39.05 C ANISOU 2535 CA PRO A 344 5007 5226 4603 -218 -101 -156 C ATOM 2536 C PRO A 344 20.039 18.382 22.502 1.00 37.60 C ANISOU 2536 C PRO A 344 4838 5074 4372 -231 -159 -180 C ATOM 2537 O PRO A 344 20.458 17.254 22.693 1.00 38.04 O ANISOU 2537 O PRO A 344 4767 5191 4495 -283 -297 -205 O ATOM 2538 CB PRO A 344 21.202 20.074 23.936 1.00 39.43 C ANISOU 2538 CB PRO A 344 5024 5260 4695 -177 -140 -160 C ATOM 2539 CG PRO A 344 20.845 21.529 23.910 1.00 39.89 C ANISOU 2539 CG PRO A 344 5097 5275 4783 -57 -31 -150 C ATOM 2540 CD PRO A 344 20.699 21.986 22.508 1.00 40.13 C ANISOU 2540 CD PRO A 344 5210 5326 4712 -210 -53 -207 C ATOM 2541 N LEU A 345 18.752 18.641 22.297 1.00 36.13 N ANISOU 2541 N LEU A 345 4728 4931 4066 -232 -99 -137 N ATOM 2542 CA LEU A 345 17.768 17.559 22.274 1.00 34.48 C ANISOU 2542 CA LEU A 345 4652 4671 3776 -217 -88 -162 C ATOM 2543 C LEU A 345 17.689 16.821 20.923 1.00 34.18 C ANISOU 2543 C LEU A 345 4636 4562 3786 -257 -75 -127 C ATOM 2544 O LEU A 345 17.153 15.710 20.847 1.00 33.94 O ANISOU 2544 O LEU A 345 4736 4411 3746 -334 -63 -71 O ATOM 2545 CB LEU A 345 16.377 18.088 22.649 1.00 33.90 C ANISOU 2545 CB LEU A 345 4590 4590 3700 -220 -22 -104 C ATOM 2546 CG LEU A 345 16.219 18.886 23.949 1.00 35.31 C ANISOU 2546 CG LEU A 345 4731 4846 3839 -86 -44 -46 C ATOM 2547 CD1 LEU A 345 14.788 19.398 24.036 1.00 33.55 C ANISOU 2547 CD1 LEU A 345 4286 4673 3787 -92 285 147 C ATOM 2548 CD2 LEU A 345 16.467 17.953 25.109 1.00 35.98 C ANISOU 2548 CD2 LEU A 345 4942 5058 3668 -160 -245 51 C ATOM 2549 N ILE A 346 18.206 17.439 19.870 1.00 32.80 N ANISOU 2549 N ILE A 346 4389 4430 3642 -212 -27 -155 N ATOM 2550 CA ILE A 346 18.106 16.865 18.530 1.00 32.81 C ANISOU 2550 CA ILE A 346 4489 4332 3643 -132 -65 -162 C ATOM 2551 C ILE A 346 19.370 16.095 18.155 1.00 33.71 C ANISOU 2551 C ILE A 346 4409 4576 3822 -178 65 -116 C ATOM 2552 O ILE A 346 20.445 16.699 17.929 1.00 35.56 O ANISOU 2552 O ILE A 346 4539 4687 4285 -198 183 -68 O ATOM 2553 CB ILE A 346 17.733 17.940 17.478 1.00 32.55 C ANISOU 2553 CB ILE A 346 4501 4324 3540 -141 -149 -211 C ATOM 2554 CG1 ILE A 346 16.412 18.593 17.913 1.00 32.05 C ANISOU 2554 CG1 ILE A 346 4829 3816 3530 63 -48 -258 C ATOM 2555 CG2 ILE A 346 17.525 17.270 16.096 1.00 32.60 C ANISOU 2555 CG2 ILE A 346 4818 4181 3385 -231 -144 -385 C ATOM 2556 CD1 ILE A 346 16.123 19.915 17.275 1.00 33.73 C ANISOU 2556 CD1 ILE A 346 5092 4144 3577 1 -262 225 C ATOM 2557 N THR A 347 19.248 14.773 18.104 1.00 32.60 N ANISOU 2557 N THR A 347 4177 4572 3634 -143 95 -119 N ATOM 2558 CA THR A 347 20.405 13.931 17.823 1.00 33.42 C ANISOU 2558 CA THR A 347 4231 4680 3785 -136 29 -22 C ATOM 2559 C THR A 347 20.417 13.339 16.429 1.00 33.15 C ANISOU 2559 C THR A 347 4109 4664 3819 -83 49 -82 C ATOM 2560 O THR A 347 21.479 12.897 15.935 1.00 34.24 O ANISOU 2560 O THR A 347 4187 4769 4053 -71 99 -122 O ATOM 2561 CB THR A 347 20.547 12.826 18.871 1.00 33.62 C ANISOU 2561 CB THR A 347 4297 4622 3855 -239 -79 20 C ATOM 2562 CG2 THR A 347 20.838 13.448 20.264 1.00 34.24 C ANISOU 2562 CG2 THR A 347 4315 5055 3638 -113 54 -77 C ATOM 2563 OG1 THR A 347 19.333 12.052 18.928 1.00 32.83 O ANISOU 2563 OG1 THR A 347 3854 4838 3781 -198 -29 235 O ATOM 2564 N HIS A 348 19.246 13.310 15.788 1.00 32.15 N ANISOU 2564 N HIS A 348 4015 4518 3680 -56 116 -77 N ATOM 2565 CA HIS A 348 19.115 12.706 14.463 1.00 31.45 C ANISOU 2565 CA HIS A 348 3955 4486 3508 11 204 -5 C ATOM 2566 C HIS A 348 18.077 13.447 13.649 1.00 30.63 C ANISOU 2566 C HIS A 348 3878 4438 3319 -11 234 -39 C ATOM 2567 O HIS A 348 17.037 13.862 14.169 1.00 31.07 O ANISOU 2567 O HIS A 348 3975 4407 3423 68 187 24 O ATOM 2568 CB HIS A 348 18.745 11.223 14.581 1.00 30.92 C ANISOU 2568 CB HIS A 348 3677 4467 3604 40 276 44 C ATOM 2569 CG HIS A 348 19.770 10.398 15.299 1.00 34.12 C ANISOU 2569 CG HIS A 348 4277 4626 4061 109 131 133 C ATOM 2570 CD2 HIS A 348 20.692 9.521 14.835 1.00 35.13 C ANISOU 2570 CD2 HIS A 348 4266 4678 4403 240 100 108 C ATOM 2571 ND1 HIS A 348 19.962 10.471 16.658 1.00 35.35 N ANISOU 2571 ND1 HIS A 348 4342 4807 4282 177 320 251 N ATOM 2572 CE1 HIS A 348 20.942 9.658 17.010 1.00 36.39 C ANISOU 2572 CE1 HIS A 348 4687 4770 4368 260 247 351 C ATOM 2573 NE2 HIS A 348 21.395 9.059 15.923 1.00 36.20 N ANISOU 2573 NE2 HIS A 348 4905 4686 4162 298 207 201 N ATOM 2574 N VAL A 349 18.367 13.647 12.366 1.00 30.56 N ANISOU 2574 N VAL A 349 3999 4370 3241 -40 204 -75 N ATOM 2575 CA VAL A 349 17.349 14.195 11.461 1.00 30.86 C ANISOU 2575 CA VAL A 349 4056 4370 3296 -76 199 -154 C ATOM 2576 C VAL A 349 17.287 13.314 10.227 1.00 30.30 C ANISOU 2576 C VAL A 349 3914 4358 3239 -43 308 -195 C ATOM 2577 O VAL A 349 18.327 12.977 9.648 1.00 32.59 O ANISOU 2577 O VAL A 349 4013 4683 3683 -59 324 -326 O ATOM 2578 CB VAL A 349 17.697 15.649 11.059 1.00 30.57 C ANISOU 2578 CB VAL A 349 3999 4277 3338 -129 223 -149 C ATOM 2579 CG1 VAL A 349 16.737 16.220 10.027 1.00 33.18 C ANISOU 2579 CG1 VAL A 349 4543 4446 3616 -289 240 110 C ATOM 2580 CG2 VAL A 349 17.791 16.559 12.309 1.00 30.37 C ANISOU 2580 CG2 VAL A 349 4180 4114 3243 -236 218 -107 C ATOM 2581 N LEU A 350 16.072 12.947 9.831 1.00 30.30 N ANISOU 2581 N LEU A 350 4027 4378 3106 -24 290 -166 N ATOM 2582 CA LEU A 350 15.862 12.078 8.672 1.00 29.90 C ANISOU 2582 CA LEU A 350 3930 4271 3160 47 341 -160 C ATOM 2583 C LEU A 350 14.762 12.635 7.804 1.00 29.62 C ANISOU 2583 C LEU A 350 3883 4290 3080 75 352 -177 C ATOM 2584 O LEU A 350 13.861 13.288 8.322 1.00 30.11 O ANISOU 2584 O LEU A 350 3896 4520 3024 114 392 -223 O ATOM 2585 CB LEU A 350 15.477 10.675 9.116 1.00 30.48 C ANISOU 2585 CB LEU A 350 4099 4235 3247 87 337 -183 C ATOM 2586 CG LEU A 350 16.542 9.849 9.822 1.00 30.82 C ANISOU 2586 CG LEU A 350 3898 4359 3452 64 563 46 C ATOM 2587 CD1 LEU A 350 15.882 8.634 10.434 1.00 33.41 C ANISOU 2587 CD1 LEU A 350 4547 4364 3782 -69 207 324 C ATOM 2588 CD2 LEU A 350 17.658 9.466 8.832 1.00 34.02 C ANISOU 2588 CD2 LEU A 350 4397 4621 3907 -144 897 104 C ATOM 2589 N PRO A 351 14.805 12.372 6.478 1.00 28.65 N ANISOU 2589 N PRO A 351 3717 4158 3011 -1 383 -124 N ATOM 2590 CA PRO A 351 13.656 12.732 5.652 1.00 28.95 C ANISOU 2590 CA PRO A 351 3855 4163 2978 95 421 -47 C ATOM 2591 C PRO A 351 12.457 11.867 6.105 1.00 29.25 C ANISOU 2591 C PRO A 351 3915 4043 3153 59 313 -40 C ATOM 2592 O PRO A 351 12.655 10.762 6.605 1.00 29.91 O ANISOU 2592 O PRO A 351 4068 3996 3300 83 515 -47 O ATOM 2593 CB PRO A 351 14.102 12.333 4.236 1.00 28.23 C ANISOU 2593 CB PRO A 351 3834 4146 2745 103 341 -74 C ATOM 2594 CG PRO A 351 15.149 11.288 4.460 1.00 28.82 C ANISOU 2594 CG PRO A 351 3979 4100 2871 78 380 -84 C ATOM 2595 CD PRO A 351 15.860 11.683 5.717 1.00 29.42 C ANISOU 2595 CD PRO A 351 3917 4208 3054 -13 418 -199 C ATOM 2596 N PHE A 352 11.242 12.374 5.927 1.00 29.43 N ANISOU 2596 N PHE A 352 3931 3937 3313 93 489 -81 N ATOM 2597 CA PHE A 352 10.009 11.710 6.348 1.00 30.56 C ANISOU 2597 CA PHE A 352 4114 4071 3425 78 271 -138 C ATOM 2598 C PHE A 352 9.920 10.239 5.869 1.00 29.85 C ANISOU 2598 C PHE A 352 4054 3984 3301 106 348 -215 C ATOM 2599 O PHE A 352 9.476 9.355 6.600 1.00 29.83 O ANISOU 2599 O PHE A 352 4166 3974 3193 83 449 -430 O ATOM 2600 CB PHE A 352 8.840 12.523 5.826 1.00 31.90 C ANISOU 2600 CB PHE A 352 4300 4111 3707 171 352 -82 C ATOM 2601 CG PHE A 352 7.521 11.840 5.938 1.00 32.64 C ANISOU 2601 CG PHE A 352 4215 4137 4047 145 240 -137 C ATOM 2602 CD1 PHE A 352 7.005 11.475 7.186 1.00 36.26 C ANISOU 2602 CD1 PHE A 352 4775 4420 4582 41 156 175 C ATOM 2603 CD2 PHE A 352 6.754 11.618 4.808 1.00 35.79 C ANISOU 2603 CD2 PHE A 352 4524 4457 4614 124 74 -118 C ATOM 2604 CE1 PHE A 352 5.759 10.850 7.273 1.00 37.18 C ANISOU 2604 CE1 PHE A 352 4638 4662 4827 163 90 86 C ATOM 2605 CE2 PHE A 352 5.526 10.998 4.895 1.00 37.14 C ANISOU 2605 CE2 PHE A 352 4705 4548 4857 70 230 -149 C ATOM 2606 CZ PHE A 352 5.027 10.616 6.123 1.00 36.61 C ANISOU 2606 CZ PHE A 352 4677 4514 4716 -17 207 -88 C ATOM 2607 N GLU A 353 10.415 9.959 4.667 1.00 31.63 N ANISOU 2607 N GLU A 353 4387 4232 3397 87 144 -206 N ATOM 2608 CA GLU A 353 10.232 8.641 4.105 1.00 31.36 C ANISOU 2608 CA GLU A 353 4353 4164 3396 71 169 -165 C ATOM 2609 C GLU A 353 11.044 7.557 4.814 1.00 30.66 C ANISOU 2609 C GLU A 353 4238 4090 3320 85 324 -198 C ATOM 2610 O GLU A 353 10.806 6.358 4.603 1.00 31.89 O ANISOU 2610 O GLU A 353 4429 4206 3482 89 419 -203 O ATOM 2611 CB GLU A 353 10.565 8.662 2.619 1.00 32.10 C ANISOU 2611 CB GLU A 353 4552 4220 3423 -15 205 -104 C ATOM 2612 CG GLU A 353 9.604 9.564 1.830 1.00 35.93 C ANISOU 2612 CG GLU A 353 5029 4605 4017 0 -231 -107 C ATOM 2613 CD GLU A 353 9.967 11.076 1.813 1.00 38.76 C ANISOU 2613 CD GLU A 353 5495 4941 4288 -265 -109 315 C ATOM 2614 OE1 GLU A 353 10.997 11.537 2.413 1.00 36.19 O ANISOU 2614 OE1 GLU A 353 5208 5160 3379 -285 -86 473 O ATOM 2615 OE2 GLU A 353 9.167 11.813 1.179 1.00 45.02 O1- ANISOU 2615 OE2 GLU A 353 6248 5600 5257 5 -350 222 O1- ATOM 2616 N LYS A 354 11.996 8.007 5.633 1.00 28.94 N ANISOU 2616 N LYS A 354 3803 4132 3061 35 640 -243 N ATOM 2617 CA LYS A 354 12.810 7.140 6.448 1.00 29.16 C ANISOU 2617 CA LYS A 354 3769 4155 3154 53 642 -281 C ATOM 2618 C LYS A 354 12.240 6.992 7.893 1.00 29.24 C ANISOU 2618 C LYS A 354 3770 4120 3220 89 638 -224 C ATOM 2619 O LYS A 354 12.948 6.683 8.861 1.00 28.72 O ANISOU 2619 O LYS A 354 3563 4084 3265 81 703 -208 O ATOM 2620 CB LYS A 354 14.247 7.650 6.462 1.00 29.66 C ANISOU 2620 CB LYS A 354 3855 4249 3164 88 773 -267 C ATOM 2621 CG LYS A 354 14.966 7.495 5.107 1.00 31.30 C ANISOU 2621 CG LYS A 354 3927 4621 3345 53 795 -273 C ATOM 2622 CD LYS A 354 16.436 7.783 5.305 1.00 34.01 C ANISOU 2622 CD LYS A 354 4125 4902 3895 -39 754 -359 C ATOM 2623 CE LYS A 354 17.198 7.527 3.994 1.00 36.27 C ANISOU 2623 CE LYS A 354 4374 5145 4261 231 807 -159 C ATOM 2624 NZ LYS A 354 18.646 7.643 4.261 1.00 38.67 N1+ ANISOU 2624 NZ LYS A 354 4396 5148 5147 -83 647 -254 N1+ ATOM 2625 N ILE A 355 10.933 7.176 8.015 1.00 29.25 N ANISOU 2625 N ILE A 355 3718 4105 3288 82 684 -262 N ATOM 2626 CA ILE A 355 10.251 7.121 9.330 1.00 27.70 C ANISOU 2626 CA ILE A 355 3593 3686 3244 174 705 -266 C ATOM 2627 C ILE A 355 10.554 5.799 10.050 1.00 28.50 C ANISOU 2627 C ILE A 355 3650 3706 3471 208 581 -233 C ATOM 2628 O ILE A 355 10.804 5.778 11.263 1.00 27.73 O ANISOU 2628 O ILE A 355 3590 3373 3572 449 474 -324 O ATOM 2629 CB ILE A 355 8.734 7.378 9.189 1.00 28.48 C ANISOU 2629 CB ILE A 355 3729 3859 3233 14 686 -228 C ATOM 2630 CG1 ILE A 355 8.034 7.295 10.572 1.00 28.12 C ANISOU 2630 CG1 ILE A 355 3526 3899 3257 196 882 -342 C ATOM 2631 CG2 ILE A 355 8.078 6.419 8.170 1.00 28.98 C ANISOU 2631 CG2 ILE A 355 3689 3938 3382 -66 660 -363 C ATOM 2632 CD1 ILE A 355 6.618 7.858 10.532 1.00 26.81 C ANISOU 2632 CD1 ILE A 355 3520 3376 3290 545 841 87 C ATOM 2633 N ASN A 356 10.560 4.680 9.318 1.00 28.64 N ANISOU 2633 N ASN A 356 3612 3580 3687 215 539 -181 N ATOM 2634 CA ASN A 356 10.876 3.431 10.035 1.00 30.55 C ANISOU 2634 CA ASN A 356 3952 3738 3915 128 487 -100 C ATOM 2635 C ASN A 356 12.269 3.346 10.675 1.00 30.89 C ANISOU 2635 C ASN A 356 4016 3810 3908 34 476 -11 C ATOM 2636 O ASN A 356 12.400 2.879 11.809 1.00 30.83 O ANISOU 2636 O ASN A 356 4212 3570 3929 63 423 39 O ATOM 2637 CB ASN A 356 10.554 2.201 9.189 1.00 30.77 C ANISOU 2637 CB ASN A 356 3982 3730 3977 101 406 -271 C ATOM 2638 CG ASN A 356 9.059 2.034 8.972 1.00 33.17 C ANISOU 2638 CG ASN A 356 4089 4335 4177 133 534 -145 C ATOM 2639 ND2 ASN A 356 8.641 1.942 7.706 1.00 35.69 N ANISOU 2639 ND2 ASN A 356 4687 4341 4530 180 303 -349 N ATOM 2640 OD1 ASN A 356 8.281 1.995 9.942 1.00 34.11 O ANISOU 2640 OD1 ASN A 356 4652 4621 3686 64 730 -425 O ATOM 2641 N GLU A 357 13.299 3.825 9.967 1.00 31.87 N ANISOU 2641 N GLU A 357 4044 3946 4116 -10 553 89 N ATOM 2642 CA GLU A 357 14.629 3.969 10.550 1.00 32.32 C ANISOU 2642 CA GLU A 357 4161 4106 4013 -16 460 98 C ATOM 2643 C GLU A 357 14.591 4.843 11.801 1.00 31.93 C ANISOU 2643 C GLU A 357 4089 3996 4046 -43 440 143 C ATOM 2644 O GLU A 357 15.315 4.576 12.777 1.00 31.65 O ANISOU 2644 O GLU A 357 4015 4174 3834 3 336 198 O ATOM 2645 CB GLU A 357 15.631 4.535 9.509 1.00 33.47 C ANISOU 2645 CB GLU A 357 4219 4164 4332 -52 532 129 C ATOM 2646 CG GLU A 357 16.752 5.378 10.118 1.00 38.88 C ANISOU 2646 CG GLU A 357 4836 5007 4930 -2 256 -56 C ATOM 2647 CD GLU A 357 18.044 5.380 9.343 1.00 43.03 C ANISOU 2647 CD GLU A 357 5296 5669 5383 -16 331 150 C ATOM 2648 OE1 GLU A 357 17.980 5.514 8.107 1.00 42.23 O ANISOU 2648 OE1 GLU A 357 5553 5529 4961 175 630 31 O ATOM 2649 OE2 GLU A 357 19.122 5.249 9.996 1.00 46.81 O1- ANISOU 2649 OE2 GLU A 357 5336 6186 6261 42 151 106 O1- ATOM 2650 N GLY A 358 13.751 5.874 11.791 1.00 30.95 N ANISOU 2650 N GLY A 358 3945 3928 3886 -48 406 114 N ATOM 2651 CA GLY A 358 13.672 6.767 12.955 1.00 30.75 C ANISOU 2651 CA GLY A 358 4020 3859 3802 135 433 60 C ATOM 2652 C GLY A 358 13.103 6.058 14.167 1.00 30.02 C ANISOU 2652 C GLY A 358 3915 3675 3817 247 400 0 C ATOM 2653 O GLY A 358 13.532 6.313 15.302 1.00 30.99 O ANISOU 2653 O GLY A 358 4015 3745 4012 230 415 -109 O ATOM 2654 N PHE A 359 12.129 5.181 13.929 1.00 29.02 N ANISOU 2654 N PHE A 359 3836 3548 3641 287 374 -53 N ATOM 2655 CA PHE A 359 11.556 4.346 15.010 1.00 29.15 C ANISOU 2655 CA PHE A 359 3935 3527 3610 408 334 -99 C ATOM 2656 C PHE A 359 12.537 3.273 15.480 1.00 29.93 C ANISOU 2656 C PHE A 359 4088 3600 3682 462 336 -111 C ATOM 2657 O PHE A 359 12.630 2.999 16.670 1.00 31.80 O ANISOU 2657 O PHE A 359 4481 3760 3840 430 465 -125 O ATOM 2658 CB PHE A 359 10.212 3.760 14.589 1.00 29.94 C ANISOU 2658 CB PHE A 359 3889 3720 3764 496 349 -103 C ATOM 2659 CG PHE A 359 9.063 4.721 14.823 1.00 26.59 C ANISOU 2659 CG PHE A 359 3548 3435 3118 409 625 -245 C ATOM 2660 CD1 PHE A 359 8.792 5.752 13.917 1.00 29.21 C ANISOU 2660 CD1 PHE A 359 3484 4005 3609 585 309 16 C ATOM 2661 CD2 PHE A 359 8.298 4.619 15.976 1.00 29.09 C ANISOU 2661 CD2 PHE A 359 4050 3969 3033 273 563 -136 C ATOM 2662 CE1 PHE A 359 7.772 6.655 14.151 1.00 28.96 C ANISOU 2662 CE1 PHE A 359 3707 3732 3564 326 765 -104 C ATOM 2663 CE2 PHE A 359 7.289 5.511 16.202 1.00 28.61 C ANISOU 2663 CE2 PHE A 359 3942 3649 3278 279 599 -195 C ATOM 2664 CZ PHE A 359 7.008 6.526 15.292 1.00 28.33 C ANISOU 2664 CZ PHE A 359 3975 3778 3012 309 510 -199 C ATOM 2665 N ASP A 360 13.330 2.710 14.573 1.00 30.70 N ANISOU 2665 N ASP A 360 4183 3788 3690 387 392 -149 N ATOM 2666 CA ASP A 360 14.429 1.868 15.055 1.00 31.27 C ANISOU 2666 CA ASP A 360 4234 3885 3760 510 280 -112 C ATOM 2667 C ASP A 360 15.402 2.571 16.006 1.00 31.96 C ANISOU 2667 C ASP A 360 4332 4060 3748 518 325 -109 C ATOM 2668 O ASP A 360 15.821 1.970 17.006 1.00 33.34 O ANISOU 2668 O ASP A 360 4595 4183 3888 657 193 44 O ATOM 2669 CB ASP A 360 15.242 1.259 13.894 1.00 32.15 C ANISOU 2669 CB ASP A 360 4326 4018 3868 474 329 -215 C ATOM 2670 CG ASP A 360 14.403 0.364 13.010 1.00 34.47 C ANISOU 2670 CG ASP A 360 4512 4137 4444 280 153 -163 C ATOM 2671 OD1 ASP A 360 14.813 0.109 11.853 1.00 39.52 O ANISOU 2671 OD1 ASP A 360 4975 4741 5299 184 373 -272 O ATOM 2672 OD2 ASP A 360 13.349 -0.100 13.479 1.00 37.53 O1- ANISOU 2672 OD2 ASP A 360 4660 4204 5396 215 139 -221 O1- ATOM 2673 N LEU A 361 15.806 3.795 15.659 1.00 31.96 N ANISOU 2673 N LEU A 361 4284 4037 3821 554 296 -187 N ATOM 2674 CA LEU A 361 16.625 4.662 16.517 1.00 32.87 C ANISOU 2674 CA LEU A 361 4362 4255 3870 425 379 -166 C ATOM 2675 C LEU A 361 15.996 4.906 17.884 1.00 33.35 C ANISOU 2675 C LEU A 361 4482 4285 3901 365 336 -220 C ATOM 2676 O LEU A 361 16.701 4.966 18.898 1.00 34.40 O ANISOU 2676 O LEU A 361 4484 4561 4023 507 386 -197 O ATOM 2677 CB LEU A 361 16.892 6.005 15.829 1.00 32.79 C ANISOU 2677 CB LEU A 361 4403 4293 3760 459 423 -200 C ATOM 2678 CG LEU A 361 17.894 5.984 14.651 1.00 33.63 C ANISOU 2678 CG LEU A 361 4402 4470 3904 361 585 -118 C ATOM 2679 CD1 LEU A 361 17.797 7.317 13.919 1.00 36.15 C ANISOU 2679 CD1 LEU A 361 4741 4677 4317 347 644 -57 C ATOM 2680 CD2 LEU A 361 19.335 5.692 15.103 1.00 35.80 C ANISOU 2680 CD2 LEU A 361 4718 4325 4557 241 303 -368 C ATOM 2681 N LEU A 362 14.680 5.075 17.899 1.00 33.35 N ANISOU 2681 N LEU A 362 4459 4374 3838 363 300 -250 N ATOM 2682 CA LEU A 362 13.920 5.323 19.135 1.00 34.42 C ANISOU 2682 CA LEU A 362 4591 4431 4054 247 332 -174 C ATOM 2683 C LEU A 362 13.969 4.074 19.987 1.00 35.04 C ANISOU 2683 C LEU A 362 4755 4485 4072 188 219 -94 C ATOM 2684 O LEU A 362 14.251 4.142 21.178 1.00 36.27 O ANISOU 2684 O LEU A 362 4933 4653 4192 209 264 -51 O ATOM 2685 CB LEU A 362 12.458 5.639 18.808 1.00 33.81 C ANISOU 2685 CB LEU A 362 4516 4409 3921 314 311 -182 C ATOM 2686 CG LEU A 362 11.462 5.676 19.997 1.00 34.47 C ANISOU 2686 CG LEU A 362 4430 4395 4269 210 396 -229 C ATOM 2687 CD1 LEU A 362 11.452 7.019 20.657 1.00 36.51 C ANISOU 2687 CD1 LEU A 362 4866 4626 4377 230 521 -386 C ATOM 2688 CD2 LEU A 362 10.046 5.355 19.507 1.00 35.18 C ANISOU 2688 CD2 LEU A 362 4395 4287 4684 464 315 -376 C ATOM 2689 N ARG A 363 13.707 2.924 19.351 1.00 35.07 N ANISOU 2689 N ARG A 363 4798 4429 4098 197 195 -94 N ATOM 2690 CA ARG A 363 13.539 1.661 20.073 1.00 36.20 C ANISOU 2690 CA ARG A 363 4856 4504 4393 183 83 51 C ATOM 2691 C ARG A 363 14.850 1.116 20.635 1.00 36.83 C ANISOU 2691 C ARG A 363 4878 4593 4520 192 83 62 C ATOM 2692 O ARG A 363 14.845 0.367 21.617 1.00 39.19 O ANISOU 2692 O ARG A 363 5245 4843 4800 161 50 100 O ATOM 2693 CB ARG A 363 12.866 0.615 19.192 1.00 35.49 C ANISOU 2693 CB ARG A 363 4778 4371 4335 207 141 48 C ATOM 2694 CG ARG A 363 11.384 0.915 18.899 1.00 35.91 C ANISOU 2694 CG ARG A 363 4852 4473 4319 169 -69 145 C ATOM 2695 CD ARG A 363 10.830 0.047 17.788 1.00 37.36 C ANISOU 2695 CD ARG A 363 4964 4518 4712 106 -151 136 C ATOM 2696 NE ARG A 363 9.520 0.532 17.358 1.00 37.76 N ANISOU 2696 NE ARG A 363 4837 4717 4791 171 119 -121 N ATOM 2697 CZ ARG A 363 9.024 0.436 16.129 1.00 35.19 C ANISOU 2697 CZ ARG A 363 4640 4249 4479 282 198 -99 C ATOM 2698 NH1 ARG A 363 9.739 -0.101 15.131 1.00 36.95 N1+ ANISOU 2698 NH1 ARG A 363 4844 4464 4731 260 395 -257 N1+ ATOM 2699 NH2 ARG A 363 7.801 0.914 15.891 1.00 34.19 N ANISOU 2699 NH2 ARG A 363 4545 4256 4190 41 -115 -464 N ATOM 2700 N SER A 364 15.963 1.492 20.012 1.00 37.50 N ANISOU 2700 N SER A 364 4762 4659 4826 221 -29 -31 N ATOM 2701 CA SER A 364 17.268 0.966 20.386 1.00 38.66 C ANISOU 2701 CA SER A 364 4896 4809 4981 245 -62 49 C ATOM 2702 C SER A 364 17.869 1.796 21.509 1.00 39.43 C ANISOU 2702 C SER A 364 4978 4921 5081 187 -127 30 C ATOM 2703 O SER A 364 18.835 1.370 22.150 1.00 40.54 O ANISOU 2703 O SER A 364 5124 5005 5274 226 -130 145 O ATOM 2704 CB SER A 364 18.193 1.010 19.174 1.00 38.21 C ANISOU 2704 CB SER A 364 4783 4743 4990 269 -45 29 C ATOM 2705 OG SER A 364 18.526 2.348 18.852 1.00 38.84 O ANISOU 2705 OG SER A 364 4677 4824 5253 334 158 -118 O ATOM 2706 N GLY A 365 17.286 2.970 21.754 1.00 40.24 N ANISOU 2706 N GLY A 365 5116 5009 5162 190 -151 79 N ATOM 2707 CA GLY A 365 17.820 3.957 22.720 1.00 40.74 C ANISOU 2707 CA GLY A 365 5180 5155 5141 132 -183 -12 C ATOM 2708 C GLY A 365 18.913 4.877 22.167 1.00 41.36 C ANISOU 2708 C GLY A 365 5226 5264 5222 115 -108 -44 C ATOM 2709 O GLY A 365 19.463 5.718 22.884 1.00 42.00 O ANISOU 2709 O GLY A 365 5306 5390 5261 152 -190 -43 O ATOM 2710 N GLU A 366 19.206 4.752 20.879 1.00 41.23 N ANISOU 2710 N GLU A 366 5175 5276 5213 116 -53 -1 N ATOM 2711 CA GLU A 366 20.339 5.443 20.248 1.00 42.04 C ANISOU 2711 CA GLU A 366 5282 5311 5380 71 15 -21 C ATOM 2712 C GLU A 366 20.112 6.956 20.090 1.00 40.92 C ANISOU 2712 C GLU A 366 5127 5187 5232 66 17 -16 C ATOM 2713 O GLU A 366 21.060 7.749 20.165 1.00 42.09 O ANISOU 2713 O GLU A 366 5223 5297 5473 71 -52 -43 O ATOM 2714 CB GLU A 366 20.595 4.798 18.880 1.00 42.27 C ANISOU 2714 CB GLU A 366 5304 5434 5322 17 43 -38 C ATOM 2715 CG GLU A 366 21.930 5.106 18.222 1.00 44.45 C ANISOU 2715 CG GLU A 366 5498 5648 5742 -51 105 -64 C ATOM 2716 CD GLU A 366 22.061 4.423 16.861 1.00 44.31 C ANISOU 2716 CD GLU A 366 5492 5597 5747 89 143 -82 C ATOM 2717 OE1 GLU A 366 21.448 3.334 16.656 1.00 48.66 O ANISOU 2717 OE1 GLU A 366 5820 6016 6649 -41 120 -271 O ATOM 2718 OE2 GLU A 366 22.751 4.985 15.990 1.00 48.46 O1- ANISOU 2718 OE2 GLU A 366 5582 6327 6502 -104 288 -33 O1- ATOM 2719 N SER A 367 18.857 7.341 19.848 1.00 39.23 N ANISOU 2719 N SER A 367 5021 4960 4923 98 73 14 N ATOM 2720 CA SER A 367 18.485 8.743 19.685 1.00 37.31 C ANISOU 2720 CA SER A 367 4823 4757 4596 148 133 -92 C ATOM 2721 C SER A 367 17.916 9.357 20.968 1.00 36.47 C ANISOU 2721 C SER A 367 4767 4665 4425 59 240 -30 C ATOM 2722 O SER A 367 17.171 8.691 21.701 1.00 36.99 O ANISOU 2722 O SER A 367 4979 4560 4513 70 453 -153 O ATOM 2723 CB SER A 367 17.431 8.848 18.574 1.00 36.67 C ANISOU 2723 CB SER A 367 4711 4724 4495 163 87 -42 C ATOM 2724 OG SER A 367 16.277 8.050 18.895 1.00 38.35 O ANISOU 2724 OG SER A 367 4986 4690 4892 271 78 -147 O ATOM 2725 N ILE A 368 18.265 10.618 21.242 1.00 34.16 N ANISOU 2725 N ILE A 368 4440 4511 4028 104 202 4 N ATOM 2726 CA ILE A 368 17.469 11.437 22.177 1.00 32.53 C ANISOU 2726 CA ILE A 368 4208 4456 3694 47 183 39 C ATOM 2727 C ILE A 368 16.157 11.844 21.485 1.00 32.57 C ANISOU 2727 C ILE A 368 4166 4516 3691 74 254 201 C ATOM 2728 O ILE A 368 15.038 11.559 21.965 1.00 32.84 O ANISOU 2728 O ILE A 368 4167 4672 3638 55 209 296 O ATOM 2729 CB ILE A 368 18.273 12.672 22.667 1.00 33.42 C ANISOU 2729 CB ILE A 368 4382 4476 3837 119 211 5 C ATOM 2730 CG1 ILE A 368 19.444 12.212 23.540 1.00 34.48 C ANISOU 2730 CG1 ILE A 368 4400 4738 3962 -24 119 18 C ATOM 2731 CG2 ILE A 368 17.360 13.656 23.424 1.00 32.45 C ANISOU 2731 CG2 ILE A 368 4256 4274 3799 -1 286 -137 C ATOM 2732 CD1 ILE A 368 19.003 11.601 24.905 1.00 34.06 C ANISOU 2732 CD1 ILE A 368 4457 4441 4040 -318 236 -37 C ATOM 2733 N ARG A 369 16.294 12.502 20.344 1.00 31.09 N ANISOU 2733 N ARG A 369 3923 4524 3363 21 211 233 N ATOM 2734 CA ARG A 369 15.150 12.777 19.483 1.00 31.08 C ANISOU 2734 CA ARG A 369 3957 4479 3372 -6 223 158 C ATOM 2735 C ARG A 369 15.542 12.793 18.051 1.00 30.73 C ANISOU 2735 C ARG A 369 3927 4475 3273 8 234 100 C ATOM 2736 O ARG A 369 16.587 13.373 17.695 1.00 31.08 O ANISOU 2736 O ARG A 369 3906 4666 3236 -66 195 139 O ATOM 2737 CB ARG A 369 14.610 14.159 19.759 1.00 31.83 C ANISOU 2737 CB ARG A 369 4244 4489 3357 61 251 72 C ATOM 2738 CG ARG A 369 13.374 14.133 20.483 1.00 36.21 C ANISOU 2738 CG ARG A 369 4552 4570 4634 -96 191 -133 C ATOM 2739 CD ARG A 369 12.191 13.877 19.539 1.00 40.62 C ANISOU 2739 CD ARG A 369 4940 5194 5299 51 -30 -174 C ATOM 2740 NE ARG A 369 10.983 14.069 20.317 1.00 40.13 N ANISOU 2740 NE ARG A 369 4878 4987 5380 -115 165 -298 N ATOM 2741 CZ ARG A 369 10.643 13.332 21.368 1.00 39.81 C ANISOU 2741 CZ ARG A 369 4883 4981 5260 104 -56 -172 C ATOM 2742 NH1 ARG A 369 11.416 12.330 21.773 1.00 38.63 N1+ ANISOU 2742 NH1 ARG A 369 4102 5004 5571 348 -25 -307 N1+ ATOM 2743 NH2 ARG A 369 9.523 13.601 22.022 1.00 39.99 N ANISOU 2743 NH2 ARG A 369 4930 5154 5109 22 221 -232 N ATOM 2744 N THR A 370 14.687 12.184 17.243 1.00 30.53 N ANISOU 2744 N THR A 370 3810 4492 3296 30 232 133 N ATOM 2745 CA THR A 370 14.787 12.255 15.794 1.00 31.43 C ANISOU 2745 CA THR A 370 4117 4403 3422 30 174 -72 C ATOM 2746 C THR A 370 13.676 13.153 15.282 1.00 30.85 C ANISOU 2746 C THR A 370 4004 4346 3370 -23 142 -87 C ATOM 2747 O THR A 370 12.514 13.014 15.694 1.00 30.53 O ANISOU 2747 O THR A 370 4010 4290 3300 -59 141 -120 O ATOM 2748 CB THR A 370 14.649 10.866 15.149 1.00 32.44 C ANISOU 2748 CB THR A 370 4231 4403 3691 -52 135 20 C ATOM 2749 CG2 THR A 370 14.770 10.945 13.633 1.00 31.54 C ANISOU 2749 CG2 THR A 370 4355 4098 3529 -53 182 -372 C ATOM 2750 OG1 THR A 370 15.686 10.015 15.638 1.00 34.19 O ANISOU 2750 OG1 THR A 370 4222 4606 4162 164 236 23 O ATOM 2751 N ILE A 371 14.065 14.107 14.420 1.00 29.55 N ANISOU 2751 N ILE A 371 3957 4199 3070 45 186 -165 N ATOM 2752 CA ILE A 371 13.135 14.945 13.689 1.00 29.47 C ANISOU 2752 CA ILE A 371 3991 4176 3027 6 101 -278 C ATOM 2753 C ILE A 371 13.033 14.466 12.246 1.00 29.57 C ANISOU 2753 C ILE A 371 3940 4240 3054 0 172 -335 C ATOM 2754 O ILE A 371 14.051 14.197 11.602 1.00 30.47 O ANISOU 2754 O ILE A 371 3875 4513 3187 5 237 -362 O ATOM 2755 CB ILE A 371 13.575 16.429 13.726 1.00 30.44 C ANISOU 2755 CB ILE A 371 4159 4228 3179 -17 -14 -239 C ATOM 2756 CG1 ILE A 371 13.800 16.883 15.190 1.00 30.49 C ANISOU 2756 CG1 ILE A 371 4209 4173 3201 81 -54 -301 C ATOM 2757 CG2 ILE A 371 12.591 17.342 12.983 1.00 29.25 C ANISOU 2757 CG2 ILE A 371 4133 3887 3091 -93 54 -314 C ATOM 2758 CD1 ILE A 371 12.583 16.836 16.034 1.00 32.20 C ANISOU 2758 CD1 ILE A 371 4807 4081 3347 -236 265 -356 C ATOM 2759 N LEU A 372 11.810 14.365 11.750 1.00 29.12 N ANISOU 2759 N LEU A 372 4003 4125 2936 89 179 -271 N ATOM 2760 CA LEU A 372 11.579 14.002 10.359 1.00 28.66 C ANISOU 2760 CA LEU A 372 4027 3879 2982 -35 118 -159 C ATOM 2761 C LEU A 372 11.217 15.246 9.591 1.00 29.55 C ANISOU 2761 C LEU A 372 4090 3923 3211 -29 171 -135 C ATOM 2762 O LEU A 372 10.368 16.040 10.016 1.00 29.19 O ANISOU 2762 O LEU A 372 4217 3899 2974 -144 231 -116 O ATOM 2763 CB LEU A 372 10.432 12.975 10.244 1.00 29.19 C ANISOU 2763 CB LEU A 372 4035 3759 3295 0 77 -179 C ATOM 2764 CG LEU A 372 10.561 11.587 10.915 1.00 28.21 C ANISOU 2764 CG LEU A 372 3662 3562 3495 196 210 -166 C ATOM 2765 CD1 LEU A 372 9.309 10.769 10.695 1.00 29.37 C ANISOU 2765 CD1 LEU A 372 3592 3776 3789 238 679 -223 C ATOM 2766 CD2 LEU A 372 11.792 10.845 10.376 1.00 29.07 C ANISOU 2766 CD2 LEU A 372 3736 3280 4030 367 407 -394 C ATOM 2767 N THR A 373 11.860 15.406 8.434 1.00 29.01 N ANISOU 2767 N THR A 373 4186 3850 2984 22 153 -120 N ATOM 2768 CA THR A 373 11.664 16.618 7.659 1.00 31.11 C ANISOU 2768 CA THR A 373 4287 4090 3443 -29 67 -88 C ATOM 2769 C THR A 373 10.939 16.307 6.343 1.00 31.97 C ANISOU 2769 C THR A 373 4505 4167 3473 57 -83 -88 C ATOM 2770 O THR A 373 11.094 15.237 5.742 1.00 31.38 O ANISOU 2770 O THR A 373 4380 4206 3334 150 -99 82 O ATOM 2771 CB THR A 373 13.001 17.377 7.465 1.00 31.58 C ANISOU 2771 CB THR A 373 4389 4019 3588 -12 181 -178 C ATOM 2772 CG2 THR A 373 13.505 17.982 8.818 1.00 33.21 C ANISOU 2772 CG2 THR A 373 4533 4203 3879 -93 -10 -17 C ATOM 2773 OG1 THR A 373 13.974 16.487 6.930 1.00 33.37 O ANISOU 2773 OG1 THR A 373 4127 4517 4034 -27 535 90 O ATOM 2774 N PHE A 374 10.125 17.251 5.905 1.00 34.40 N ANISOU 2774 N PHE A 374 4689 4487 3894 170 -253 -226 N ATOM 2775 CA PHE A 374 9.368 17.073 4.668 1.00 37.50 C ANISOU 2775 CA PHE A 374 5006 4898 4344 150 -314 -246 C ATOM 2776 C PHE A 374 10.017 17.725 3.453 1.00 39.00 C ANISOU 2776 C PHE A 374 5147 5053 4614 116 -335 -226 C ATOM 2777 O PHE A 374 11.142 18.236 3.508 1.00 41.39 O ANISOU 2777 O PHE A 374 5458 5232 5036 -13 -243 -203 O ATOM 2778 CB PHE A 374 7.903 17.484 4.880 1.00 37.72 C ANISOU 2778 CB PHE A 374 5053 4948 4330 220 -276 -224 C ATOM 2779 CG PHE A 374 7.172 16.639 5.890 1.00 37.66 C ANISOU 2779 CG PHE A 374 5061 4937 4311 238 -278 -268 C ATOM 2780 CD1 PHE A 374 7.307 16.884 7.267 1.00 38.16 C ANISOU 2780 CD1 PHE A 374 5244 4988 4264 354 -21 -171 C ATOM 2781 CD2 PHE A 374 6.359 15.585 5.474 1.00 37.02 C ANISOU 2781 CD2 PHE A 374 4654 5025 4384 294 -271 -117 C ATOM 2782 CE1 PHE A 374 6.618 16.098 8.191 1.00 38.34 C ANISOU 2782 CE1 PHE A 374 5344 4828 4395 199 -211 -32 C ATOM 2783 CE2 PHE A 374 5.671 14.806 6.374 1.00 37.85 C ANISOU 2783 CE2 PHE A 374 5207 4919 4254 360 -477 -53 C ATOM 2784 CZ PHE A 374 5.799 15.058 7.750 1.00 39.15 C ANISOU 2784 CZ PHE A 374 5512 5114 4247 215 -207 -96 C ATOM 2785 OXT PHE A 374 9.505 17.718 2.328 1.00 40.97 O1- ANISOU 2785 OXT PHE A 374 5440 5311 4813 91 -383 -245 O1- TER HETATM 2786 ZN ZN A 375 4.483 12.864 22.813 1.00 30.69 ZN ANISOU 2786 ZN ZN A 375 4563 3867 3228 403 -80 -269 ZN HETATM 2787 ZN ZN A 376 -11.700 22.745 26.935 1.00 35.56 ZN ANISOU 2787 ZN ZN A 376 5536 4797 3177 1674 111 -394 ZN HETATM 2788 O HOH A 401 -11.002 23.183 41.910 1.00 35.36 O HETATM 2789 O HOH A 402 7.029 10.055 41.460 1.00 30.48 O HETATM 2790 O HOH A 403 -2.780 17.576 32.982 1.00 37.57 O HETATM 2791 O HOH A 404 0.714 6.207 11.254 1.00 28.57 O HETATM 2792 O HOH A 405 -7.038 24.159 28.866 1.00 35.44 O HETATM 2793 O HOH A 406 -2.759 1.021 19.193 1.00 36.13 O HETATM 2794 O HOH A 407 -11.487 11.274 24.865 1.00 38.43 O HETATM 2795 O HOH A 408 25.145 12.307 26.686 1.00 34.20 O HETATM 2796 O HOH A 409 -5.042 22.885 27.125 1.00 31.09 O HETATM 2797 O HOH A 410 4.615 18.573 3.666 1.00 30.88 O HETATM 2798 O HOH A 411 -13.988 5.729 16.023 1.00 40.90 O HETATM 2799 O HOH A 412 10.772 4.345 6.375 1.00 33.37 O HETATM 2800 O HOH A 413 -16.120 21.080 11.228 1.00 46.53 O HETATM 2801 O HOH A 414 12.867 13.308 54.126 1.00 38.86 O HETATM 2802 O HOH A 415 -5.173 19.178 33.774 1.00 36.33 O HETATM 2803 O HOH A 416 6.264 2.832 49.672 1.00 36.74 O HETATM 2804 O HOH A 417 9.173 21.222 47.692 1.00 31.03 O HETATM 2805 O HOH A 418 21.172 12.376 27.934 1.00 35.29 O HETATM 2806 O HOH A 419 4.548 18.742 49.792 1.00 29.37 O HETATM 2807 O HOH A 420 11.142 14.533 2.910 1.00 34.61 O HETATM 2808 O HOH A 421 12.900 10.225 18.566 1.00 30.55 O HETATM 2809 O HOH A 422 -8.156 18.127 15.633 1.00 32.42 O HETATM 2810 O HOH A 423 -5.939 15.595 12.642 1.00 30.82 O HETATM 2811 O HOH A 424 -9.793 24.699 1.854 1.00 36.38 O HETATM 2812 O HOH A 425 10.103 16.705 58.374 1.00 35.67 O HETATM 2813 O HOH A 426 3.488 16.571 31.735 1.00 35.89 O HETATM 2814 O HOH A 427 -13.804 25.701 35.912 1.00 44.82 O HETATM 2815 O HOH A 428 4.946 12.748 16.995 1.00 27.52 O HETATM 2816 O HOH A 429 -0.681 19.974 23.070 1.00 30.96 O HETATM 2817 O HOH A 430 -14.169 18.131 3.545 1.00 43.14 O HETATM 2818 O HOH A 431 -8.263 12.029 16.782 1.00 31.09 O HETATM 2819 O HOH A 432 0.975 19.449 20.774 1.00 30.32 O HETATM 2820 O HOH A 433 -12.301 9.522 5.598 1.00 34.67 O HETATM 2821 O HOH A 434 -14.632 18.627 13.260 1.00 35.87 O HETATM 2822 O HOH A 435 2.682 19.177 17.781 1.00 29.41 O HETATM 2823 O HOH A 436 17.199 22.560 49.427 1.00 57.23 O HETATM 2824 O HOH A 437 5.224 32.368 18.929 1.00 37.61 O HETATM 2825 O HOH A 438 -7.002 29.921 0.813 1.00 44.81 O HETATM 2826 O HOH A 439 17.841 3.456 12.212 1.00 48.34 O HETATM 2827 O HOH A 440 -5.980 17.800 19.784 1.00 30.35 O HETATM 2828 O HOH A 441 -9.029 26.811 -4.902 1.00 36.54 O HETATM 2829 O HOH A 442 -6.821 24.267 -11.602 1.00 37.00 O HETATM 2830 O HOH A 443 -5.114 24.757 -13.507 1.00 38.02 O HETATM 2831 O HOH A 444 -5.972 20.010 -4.430 1.00 52.76 O HETATM 2832 O HOH A 445 -3.389 16.901 -5.146 1.00 38.78 O HETATM 2833 O HOH A 446 -11.085 13.481 0.124 1.00 37.79 O HETATM 2834 O HOH A 447 -10.059 11.889 2.152 1.00 34.25 O HETATM 2835 O HOH A 448 -12.512 12.125 3.853 1.00 39.14 O HETATM 2836 O HOH A 449 -13.827 14.175 5.021 1.00 35.77 O HETATM 2837 O HOH A 450 -8.104 8.095 -1.243 1.00 48.71 O HETATM 2838 O HOH A 451 -14.651 10.653 2.445 1.00 48.67 O HETATM 2839 O HOH A 452 1.286 -0.360 8.366 1.00 39.91 O HETATM 2840 O HOH A 453 -13.394 22.192 14.731 1.00 36.65 O HETATM 2841 O HOH A 454 -9.447 18.334 18.299 1.00 32.31 O HETATM 2842 O HOH A 455 -12.395 23.876 16.775 1.00 36.69 O HETATM 2843 O HOH A 456 -8.773 15.924 19.747 1.00 40.79 O HETATM 2844 O HOH A 457 -6.790 15.158 21.555 1.00 30.71 O HETATM 2845 O HOH A 458 -14.700 15.772 21.897 1.00 44.41 O HETATM 2846 O HOH A 459 7.005 21.444 3.846 1.00 37.25 O HETATM 2847 O HOH A 460 9.341 26.586 7.303 1.00 44.02 O HETATM 2848 O HOH A 461 11.449 26.551 9.223 1.00 44.00 O HETATM 2849 O HOH A 462 14.310 8.325 17.045 1.00 34.79 O HETATM 2850 O HOH A 463 3.422 11.891 24.353 1.00 30.95 O HETATM 2851 O HOH A 464 2.072 7.028 25.674 1.00 38.95 O HETATM 2852 O HOH A 465 6.196 0.804 22.672 1.00 42.87 O HETATM 2853 O HOH A 466 -4.717 2.403 25.882 1.00 41.67 O HETATM 2854 O HOH A 467 -6.618 9.270 18.956 1.00 30.53 O HETATM 2855 O HOH A 468 -7.113 6.489 16.008 1.00 33.63 O HETATM 2856 O HOH A 469 -12.976 30.803 15.594 1.00 49.12 O HETATM 2857 O HOH A 470 25.553 13.158 15.156 1.00 57.74 O HETATM 2858 O HOH A 471 12.815 8.573 23.234 1.00 44.58 O HETATM 2859 O HOH A 472 23.796 12.993 17.153 1.00 45.68 O HETATM 2860 O HOH A 473 6.841 32.717 7.954 1.00 44.51 O HETATM 2861 O HOH A 474 -8.884 28.810 28.390 1.00 46.72 O HETATM 2862 O HOH A 475 -17.306 21.516 30.969 1.00 41.21 O HETATM 2863 O HOH A 476 -13.445 14.141 27.919 1.00 41.30 O HETATM 2864 O HOH A 477 -10.875 13.542 29.483 1.00 36.44 O HETATM 2865 O HOH A 478 -8.475 15.966 14.162 1.00 41.72 O HETATM 2866 O HOH A 479 15.971 19.640 13.401 1.00 47.55 O HETATM 2867 O HOH A 480 2.604 14.962 27.923 1.00 31.32 O HETATM 2868 O HOH A 481 3.775 16.246 34.430 1.00 43.07 O HETATM 2869 O HOH A 482 2.852 14.166 30.749 1.00 42.86 O HETATM 2870 O HOH A 483 -0.834 27.292 31.085 1.00 42.03 O HETATM 2871 O HOH A 484 -0.931 18.031 38.748 1.00 39.54 O HETATM 2872 O HOH A 485 7.149 22.913 47.127 1.00 49.75 O HETATM 2873 O HOH A 486 7.759 25.555 46.846 1.00 43.47 O HETATM 2874 O HOH A 487 11.893 30.876 43.346 1.00 55.40 O HETATM 2875 O HOH A 488 16.420 6.709 36.793 1.00 47.74 O HETATM 2876 O HOH A 489 14.751 10.343 24.396 1.00 36.32 O HETATM 2877 O HOH A 490 10.137 10.299 23.495 1.00 44.14 O HETATM 2878 O HOH A 491 14.036 9.458 30.317 1.00 40.04 O HETATM 2879 O HOH A 492 22.570 11.675 25.747 1.00 34.52 O HETATM 2880 O HOH A 493 26.873 17.246 25.896 1.00 42.36 O HETATM 2881 O HOH A 494 27.011 6.887 39.922 1.00 45.28 O HETATM 2882 O HOH A 495 12.361 10.589 27.652 1.00 33.34 O HETATM 2883 O HOH A 496 13.668 11.720 51.706 1.00 39.73 O HETATM 2884 O HOH A 497 10.405 25.591 47.522 1.00 37.88 O HETATM 2885 O HOH A 498 7.015 9.894 55.335 1.00 41.34 O HETATM 2886 O HOH A 499 13.223 3.609 7.005 1.00 40.98 O HETATM 2887 O HOH A 500 16.196 18.412 6.885 1.00 36.69 O HETATM 2888 O HOH A 501 -12.630 23.893 2.682 1.00 36.99 O HETATM 2889 O HOH A 502 -8.321 29.245 3.150 1.00 34.87 O HETATM 2890 O HOH A 503 -7.662 16.776 -5.936 1.00 45.28 O HETATM 2891 O HOH A 504 -14.038 20.256 -4.139 1.00 40.35 O HETATM 2892 O HOH A 505 -9.248 18.382 -7.765 1.00 41.68 O HETATM 2893 O HOH A 506 -0.302 4.238 -1.778 1.00 41.91 O HETATM 2894 O HOH A 507 -1.998 0.800 -1.031 1.00 60.41 O HETATM 2895 O HOH A 508 6.623 -0.422 5.294 1.00 45.40 O HETATM 2896 O HOH A 509 -5.101 6.827 -1.778 1.00 51.42 O HETATM 2897 O HOH A 510 -11.281 9.947 -1.782 1.00 55.79 O HETATM 2898 O HOH A 511 -15.156 25.205 5.313 1.00 42.96 O HETATM 2899 O HOH A 512 -17.715 23.798 4.873 1.00 58.42 O HETATM 2900 O HOH A 513 -12.994 26.578 16.777 1.00 38.34 O HETATM 2901 O HOH A 514 -11.991 28.033 18.835 1.00 42.58 O HETATM 2902 O HOH A 515 -13.318 27.185 21.050 1.00 39.72 O HETATM 2903 O HOH A 516 5.654 18.035 1.417 1.00 42.14 O HETATM 2904 O HOH A 517 16.050 19.241 4.484 1.00 36.24 O HETATM 2905 O HOH A 518 -1.141 24.936 -1.627 1.00 47.48 O HETATM 2906 O HOH A 519 6.805 13.406 -2.003 1.00 46.77 O HETATM 2907 O HOH A 520 -12.198 36.306 17.160 1.00 45.42 O HETATM 2908 O HOH A 521 -8.845 17.209 -10.033 1.00 50.46 O HETATM 2909 O HOH A 522 -12.665 11.301 22.188 1.00 43.48 O HETATM 2910 O HOH A 523 -15.167 10.166 7.686 1.00 52.51 O HETATM 2911 O HOH A 524 3.316 32.365 11.626 1.00 40.90 O HETATM 2912 O HOH A 525 9.601 10.013 27.736 1.00 49.10 O HETATM 2913 O HOH A 526 18.698 4.198 30.337 1.00 50.63 O HETATM 2914 O HOH A 527 28.103 10.575 29.260 1.00 41.46 O HETATM 2915 O HOH A 528 4.725 36.524 13.943 1.00 50.73 O HETATM 2916 O HOH A 529 -6.282 30.158 23.485 1.00 52.50 O HETATM 2917 O HOH A 530 -16.284 20.908 14.066 1.00 58.70 O HETATM 2918 O HOH A 531 -9.082 28.052 19.155 1.00 39.90 O HETATM 2919 O HOH A 532 -1.187 4.961 -7.178 1.00 49.86 O HETATM 2920 O HOH A 533 -8.542 -0.745 15.902 1.00 43.44 O HETATM 2921 O HOH A 534 28.909 17.759 29.769 1.00 50.37 O HETATM 2922 O HOH A 535 -5.653 -3.691 6.392 1.00 46.99 O HETATM 2923 O HOH A 536 -6.341 -1.854 8.200 1.00 44.80 O HETATM 2924 O HOH A 537 -4.191 -4.327 14.918 1.00 47.73 O HETATM 2925 O HOH A 538 5.946 0.815 13.018 1.00 47.04 O HETATM 2926 O HOH A 539 5.321 2.144 0.683 1.00 53.10 O HETATM 2927 O HOH A 540 9.834 29.780 29.854 1.00 53.28 O HETATM 2928 O HOH A 541 0.564 23.629 -0.161 1.00 52.68 O HETATM 2929 O HOH A 542 -14.131 22.659 18.894 1.00 46.45 O HETATM 2930 O HOH A 543 -16.387 18.940 19.798 1.00 44.45 O HETATM 2931 O HOH A 544 7.892 14.677 2.148 1.00 45.26 O HETATM 2932 O HOH A 545 22.594 17.147 19.730 1.00 44.65 O HETATM 2933 O HOH A 546 28.315 13.462 38.630 1.00 44.19 O HETATM 2934 O HOH A 547 -14.704 23.816 1.124 1.00 49.65 O HETATM 2935 O HOH A 548 3.715 21.750 43.134 1.00 54.47 O HETATM 2936 O HOH A 549 11.989 -1.773 14.969 1.00 48.44 O HETATM 2937 O HOH A 550 26.626 13.224 24.607 1.00 44.44 O HETATM 2938 O HOH A 551 13.124 10.030 21.372 1.00 44.04 O HETATM 2939 O HOH A 552 -15.646 12.260 6.014 1.00 44.57 O HETATM 2940 O HOH A 553 10.528 9.349 54.527 1.00 51.26 O HETATM 2941 O HOH A 554 6.602 2.079 3.055 1.00 46.42 O HETATM 2942 O HOH A 555 -17.488 14.293 6.161 1.00 51.30 O HETATM 2943 O HOH A 556 4.191 31.225 4.824 1.00 42.43 O HETATM 2944 O HOH A 557 -6.729 17.554 -11.597 1.00 63.47 O HETATM 2945 O HOH A 558 -14.685 34.461 17.489 1.00 56.40 O HETATM 2946 O HOH A 559 -17.806 28.366 28.758 1.00 51.24 O HETATM 2947 O HOH A 560 19.746 27.511 48.085 1.00 49.80 O HETATM 2948 O HOH A 561 16.563 26.095 30.509 1.00 51.29 O HETATM 2949 O HOH A 562 23.824 7.458 15.978 1.00 48.69 O HETATM 2950 O HOH A 563 5.172 -0.484 42.800 1.00 49.47 O HETATM 2951 O HOH A 564 3.696 29.556 2.625 1.00 48.34 O HETATM 2952 O HOH A 565 -13.330 32.113 8.046 1.00 58.44 O HETATM 2953 O HOH A 566 10.538 36.062 21.128 1.00 59.52 O HETATM 2954 O HOH A 567 -4.625 15.159 24.981 1.00 39.84 O HETATM 2955 O HOH A 568 24.428 15.055 18.720 1.00 54.12 O HETATM 2956 O HOH A 569 3.156 15.954 -2.163 1.00 49.90 O HETATM 2957 O HOH A 570 0.699 16.873 -2.531 1.00 50.19 O HETATM 2958 O HOH A 571 -8.714 30.445 -1.051 1.00 52.06 O HETATM 2959 O HOH A 572 -10.128 31.307 3.513 1.00 53.18 O HETATM 2960 O HOH A 573 -18.605 19.104 10.604 1.00 44.00 O HETATM 2961 O HOH A 574 13.394 14.112 57.610 1.00 45.92 O HETATM 2962 O HOH A 575 21.601 10.282 21.253 1.00 46.14 O HETATM 2963 O HOH A 576 8.046 15.929 -1.627 1.00 55.25 O HETATM 2964 O HOH A 577 -0.717 10.724 -5.063 1.00 53.35 O HETATM 2965 O HOH A 578 16.023 18.541 52.884 1.00 50.41 O HETATM 2966 O HOH A 579 13.010 11.127 0.710 1.00 45.11 O HETATM 2967 O HOH A 580 -3.363 19.194 -4.920 1.00 55.90 O HETATM 2968 O HOH A 581 -16.171 32.845 13.244 1.00 48.76 O HETATM 2969 O HOH A 582 6.519 14.023 25.992 1.00 37.95 O HETATM 2970 O HOH A 583 -3.069 -0.656 27.073 1.00 46.93 O HETATM 2971 O HOH A 584 2.181 34.769 10.435 1.00 43.98 O HETATM 2972 O HOH A 585 25.689 21.847 34.285 1.00 56.56 O HETATM 2973 O HOH A 586 -2.934 35.002 11.735 1.00 46.09 O HETATM 2974 O HOH A 587 27.808 10.934 41.219 1.00 58.33 O HETATM 2975 O HOH A 588 -10.545 27.422 2.213 1.00 45.59 O HETATM 2976 O HOH A 589 -7.460 20.295 -8.075 1.00 58.31 O HETATM 2977 O HOH A 590 0.118 33.354 18.460 1.00 44.42 O HETATM 2978 O HOH A 591 18.453 38.329 19.503 1.00 47.22 O HETATM 2979 O HOH A 592 -12.238 14.553 20.822 1.00 48.26 O HETATM 2980 O HOH A 593 19.894 24.292 29.479 1.00 62.56 O HETATM 2981 O HOH A 594 22.800 4.651 13.505 1.00 56.68 O HETATM 2982 O HOH A 595 14.116 2.792 42.124 1.00 47.12 O HETATM 2983 O HOH A 596 14.054 0.059 9.735 1.00 58.34 O HETATM 2984 O HOH A 597 6.453 4.559 54.352 1.00 47.45 O HETATM 2985 O HOH A 598 7.431 0.793 48.841 1.00 52.53 O HETATM 2986 O HOH A 599 10.129 24.721 4.938 1.00 50.63 O HETATM 2987 O HOH A 600 -14.404 26.871 3.363 1.00 52.81 O HETATM 2988 CM MPD A2001 1.621 10.460 27.590 1.00 63.45 C HETATM 2989 C1 MPD A2001 -0.624 11.315 28.245 1.00 63.95 C HETATM 2990 C2 MPD A2001 0.129 10.425 27.265 1.00 64.11 C HETATM 2991 O2 MPD A2001 -0.048 10.968 25.931 1.00 64.54 O HETATM 2992 C3 MPD A2001 -0.473 9.015 27.262 1.00 63.68 C HETATM 2993 C4 MPD A2001 0.091 8.077 28.330 1.00 63.22 C HETATM 2994 O4 MPD A2001 0.846 7.075 27.688 1.00 62.31 O HETATM 2995 C5 MPD A2001 -1.017 7.420 29.144 1.00 62.30 C ATOM 2996 N SER B 1 5.518 27.819 95.579 1.00 46.51 A N ANISOU 2996 N SER B 1 6153 5764 5754 -4 78 196 A N ATOM 2997 CA SER B 1 4.783 26.762 96.343 1.00 45.79 A C ANISOU 2997 CA SER B 1 6082 5708 5608 -1 20 244 A C ATOM 2998 C SER B 1 5.184 25.340 95.902 1.00 44.26 A C ANISOU 2998 C SER B 1 5881 5656 5280 -33 -67 282 A C ATOM 2999 O SER B 1 5.651 24.555 96.715 1.00 44.55 A O ANISOU 2999 O SER B 1 5993 5738 5193 -39 -35 452 A O ATOM 3000 CB SER B 1 3.269 27.008 96.236 1.00 46.22 A C ANISOU 3000 CB SER B 1 6077 5778 5706 31 24 186 A C ATOM 3001 OG SER B 1 2.508 25.865 96.582 1.00 48.47 A O ANISOU 3001 OG SER B 1 6579 5711 6125 2 25 -34 A O ATOM 3002 N THR B 2 4.996 25.013 94.622 1.00 41.81 A N ANISOU 3002 N THR B 2 5493 5492 4900 0 -98 319 A N ATOM 3003 CA THR B 2 5.478 23.737 94.091 1.00 39.68 A C ANISOU 3003 CA THR B 2 5199 5334 4543 71 -215 251 A C ATOM 3004 C THR B 2 6.682 23.912 93.172 1.00 38.03 A C ANISOU 3004 C THR B 2 4951 5201 4297 106 -318 246 A C ATOM 3005 O THR B 2 7.329 22.913 92.820 1.00 36.78 A O ANISOU 3005 O THR B 2 4771 5196 4005 112 -288 327 A O ATOM 3006 CB THR B 2 4.385 22.932 93.318 1.00 40.15 A C ANISOU 3006 CB THR B 2 5239 5304 4710 60 -139 274 A C ATOM 3007 CG2 THR B 2 3.392 22.255 94.302 1.00 41.22 A C ANISOU 3007 CG2 THR B 2 5355 5388 4917 141 -47 140 A C ATOM 3008 OG1 THR B 2 3.684 23.794 92.414 1.00 41.21 A O ANISOU 3008 OG1 THR B 2 5559 5456 4640 200 -269 278 A O ATOM 3009 N ALA B 3 6.992 25.161 92.821 1.00 36.03 A N ANISOU 3009 N ALA B 3 4755 5133 3800 122 -471 220 A N ATOM 3010 CA ALA B 3 8.076 25.459 91.876 1.00 35.52 A C ANISOU 3010 CA ALA B 3 4691 4986 3816 170 -459 230 A C ATOM 3011 C ALA B 3 9.412 24.995 92.397 1.00 35.27 A C ANISOU 3011 C ALA B 3 4686 4925 3787 209 -353 192 A C ATOM 3012 O ALA B 3 9.734 25.206 93.565 1.00 33.63 A O ANISOU 3012 O ALA B 3 4593 4765 3419 311 -523 321 A O ATOM 3013 CB ALA B 3 8.128 26.920 91.556 1.00 36.00 A C ANISOU 3013 CB ALA B 3 4749 5043 3884 221 -462 159 A C ATOM 3014 N GLY B 4 10.170 24.338 91.533 1.00 34.93 A N ANISOU 3014 N GLY B 4 4627 4845 3799 249 -290 229 A N ATOM 3015 CA GLY B 4 11.488 23.841 91.901 1.00 34.03 A C ANISOU 3015 CA GLY B 4 4545 4674 3710 174 -254 50 A C ATOM 3016 C GLY B 4 11.537 22.480 92.565 1.00 34.45 A C ANISOU 3016 C GLY B 4 4576 4578 3935 220 -169 87 A C ATOM 3017 O GLY B 4 12.641 21.935 92.777 1.00 34.52 A O ANISOU 3017 O GLY B 4 4601 4668 3846 369 -294 90 A O ATOM 3018 N LYS B 5 10.362 21.917 92.873 1.00 33.76 A N ANISOU 3018 N LYS B 5 4676 4359 3791 320 -276 6 A N ATOM 3019 CA LYS B 5 10.304 20.599 93.511 1.00 35.78 A C ANISOU 3019 CA LYS B 5 4867 4598 4127 271 -94 -81 A C ATOM 3020 C LYS B 5 9.420 19.606 92.810 1.00 35.15 A C ANISOU 3020 C LYS B 5 4759 4599 3995 276 -99 -103 A C ATOM 3021 O LYS B 5 8.561 19.945 91.955 1.00 36.50 A O ANISOU 3021 O LYS B 5 4961 4764 4142 262 -4 -238 A O ATOM 3022 CB LYS B 5 9.921 20.687 94.975 1.00 36.34 A C ANISOU 3022 CB LYS B 5 4904 4605 4297 298 -6 -44 A C ATOM 3023 CG LYS B 5 8.924 21.745 95.294 1.00 38.79 A C ANISOU 3023 CG LYS B 5 5259 4759 4721 50 -80 -200 A C ATOM 3024 CD LYS B 5 9.223 22.308 96.722 1.00 39.61 A C ANISOU 3024 CD LYS B 5 5231 4971 4846 218 -41 148 A C ATOM 3025 CE LYS B 5 8.217 23.378 97.055 1.00 40.40 A C ANISOU 3025 CE LYS B 5 5137 5111 5101 122 -107 -77 A C ATOM 3026 NZ LYS B 5 7.682 23.285 98.445 1.00 38.81 A N1+ ANISOU 3026 NZ LYS B 5 4798 5324 4622 161 -400 127 A N1+ ATOM 3027 N VAL B 6 9.670 18.355 93.151 1.00 34.86 A N ANISOU 3027 N VAL B 6 4732 4644 3866 305 -45 -61 A N ATOM 3028 CA VAL B 6 8.877 17.261 92.652 1.00 34.46 A C ANISOU 3028 CA VAL B 6 4678 4645 3771 245 -114 -30 A C ATOM 3029 C VAL B 6 7.420 17.406 93.064 1.00 33.62 A C ANISOU 3029 C VAL B 6 4654 4550 3568 247 -34 -95 A C ATOM 3030 O VAL B 6 7.106 17.736 94.226 1.00 33.68 A O ANISOU 3030 O VAL B 6 4769 4640 3387 339 -92 52 A O ATOM 3031 CB VAL B 6 9.427 15.921 93.143 1.00 34.80 A C ANISOU 3031 CB VAL B 6 4687 4686 3848 233 -67 -200 A C ATOM 3032 CG1 VAL B 6 8.526 14.794 92.733 1.00 35.79 A C ANISOU 3032 CG1 VAL B 6 4893 4913 3793 302 -342 62 A C ATOM 3033 CG2 VAL B 6 10.825 15.679 92.607 1.00 35.86 A C ANISOU 3033 CG2 VAL B 6 4790 4824 4011 91 36 -38 A C ATOM 3034 N ILE B 7 6.531 17.169 92.097 1.00 32.49 A N ANISOU 3034 N ILE B 7 4524 4497 3321 210 -166 -120 A N ATOM 3035 CA ILE B 7 5.089 17.046 92.363 1.00 33.52 A C ANISOU 3035 CA ILE B 7 4672 4576 3489 33 -62 -216 A C ATOM 3036 C ILE B 7 4.602 15.585 92.356 1.00 33.49 A C ANISOU 3036 C ILE B 7 4610 4607 3506 129 45 -221 A C ATOM 3037 O ILE B 7 4.802 14.857 91.385 1.00 34.44 A O ANISOU 3037 O ILE B 7 4829 4543 3713 103 7 -223 A O ATOM 3038 CB ILE B 7 4.267 17.896 91.339 1.00 33.96 A C ANISOU 3038 CB ILE B 7 4665 4573 3663 17 -110 -256 A C ATOM 3039 CG1 ILE B 7 4.472 19.389 91.617 1.00 33.32 A C ANISOU 3039 CG1 ILE B 7 4749 4527 3384 15 -95 -228 A C ATOM 3040 CG2 ILE B 7 2.789 17.536 91.405 1.00 36.45 A C ANISOU 3040 CG2 ILE B 7 4771 4766 4310 111 -209 -326 A C ATOM 3041 CD1 ILE B 7 3.802 20.348 90.552 1.00 34.76 A C ANISOU 3041 CD1 ILE B 7 4801 4600 3804 -81 -129 -238 A C ATOM 3042 N LYS B 8 3.954 15.146 93.437 1.00 33.50 A N ANISOU 3042 N LYS B 8 4629 4576 3523 181 25 -377 A N ATOM 3043 CA LYS B 8 3.310 13.826 93.460 1.00 34.72 A C ANISOU 3043 CA LYS B 8 4707 4706 3778 190 31 -312 A C ATOM 3044 C LYS B 8 1.866 14.032 93.002 1.00 33.27 A C ANISOU 3044 C LYS B 8 4560 4483 3597 216 42 -289 A C ATOM 3045 O LYS B 8 1.136 14.833 93.591 1.00 33.07 A O ANISOU 3045 O LYS B 8 4595 4392 3578 378 -29 -105 A O ATOM 3046 CB LYS B 8 3.317 13.239 94.899 1.00 35.37 A C ANISOU 3046 CB LYS B 8 4795 4837 3805 192 91 -398 A C ATOM 3047 CG LYS B 8 4.719 13.095 95.484 1.00 36.34 A C ANISOU 3047 CG LYS B 8 4844 5084 3879 187 7 -350 A C ATOM 3048 CD LYS B 8 4.829 12.204 96.734 1.00 38.48 A C ANISOU 3048 CD LYS B 8 5115 5074 4432 118 -203 -398 A C ATOM 3049 CE LYS B 8 6.272 12.159 97.213 1.00 41.35 A C ANISOU 3049 CE LYS B 8 5142 5430 5139 -83 -142 -263 A C ATOM 3050 NZ LYS B 8 6.428 11.735 98.620 1.00 44.91 A N1+ ANISOU 3050 NZ LYS B 8 5834 5768 5458 -8 155 -197 A N1+ ATOM 3051 N CYS B 9 1.442 13.308 91.971 1.00 32.05 A N ANISOU 3051 N CYS B 9 4414 4276 3485 175 184 -279 A N ATOM 3052 CA CYS B 9 0.089 13.437 91.449 1.00 31.48 A C ANISOU 3052 CA CYS B 9 4394 4134 3433 65 160 -239 A C ATOM 3053 C CYS B 9 -0.363 12.103 90.852 1.00 31.65 A C ANISOU 3053 C CYS B 9 4353 4099 3572 118 163 -306 A C ATOM 3054 O CYS B 9 0.384 11.124 90.872 1.00 32.86 A O ANISOU 3054 O CYS B 9 4308 4224 3952 48 76 -261 A O ATOM 3055 CB CYS B 9 0.032 14.546 90.390 1.00 30.97 A C ANISOU 3055 CB CYS B 9 4286 4182 3297 86 215 -214 A C ATOM 3056 SG CYS B 9 0.905 14.151 88.869 1.00 32.28 A S ANISOU 3056 SG CYS B 9 4808 4253 3201 -175 368 -553 A S ATOM 3057 N LYS B 10 -1.571 12.068 90.306 1.00 30.26 A N ANISOU 3057 N LYS B 10 4314 3949 3232 163 91 -273 A N ATOM 3058 CA LYS B 10 -2.040 10.863 89.612 1.00 31.06 A C ANISOU 3058 CA LYS B 10 4466 4011 3321 84 75 -278 A C ATOM 3059 C LYS B 10 -1.830 10.965 88.099 1.00 30.06 A C ANISOU 3059 C LYS B 10 4261 3848 3310 69 146 -321 A C ATOM 3060 O LYS B 10 -1.943 12.045 87.509 1.00 29.66 A O ANISOU 3060 O LYS B 10 4090 3832 3346 -90 -53 -383 A O ATOM 3061 CB LYS B 10 -3.499 10.632 89.896 1.00 32.23 A C ANISOU 3061 CB LYS B 10 4552 4124 3567 126 83 -265 A C ATOM 3062 CG LYS B 10 -3.808 10.128 91.329 1.00 34.91 A C ANISOU 3062 CG LYS B 10 4905 4619 3739 215 248 -154 A C ATOM 3063 CD LYS B 10 -5.304 10.003 91.505 1.00 40.75 A C ANISOU 3063 CD LYS B 10 5407 5290 4784 165 282 32 A C ATOM 3064 CE LYS B 10 -5.664 9.193 92.740 1.00 43.94 A C ANISOU 3064 CE LYS B 10 6000 5713 4982 120 136 -185 A C ATOM 3065 NZ LYS B 10 -4.685 9.343 93.858 1.00 46.26 A N1+ ANISOU 3065 NZ LYS B 10 6064 5850 5661 422 -68 -81 A N1+ ATOM 3066 N ALA B 11 -1.539 9.831 87.484 1.00 29.07 A N ANISOU 3066 N ALA B 11 4098 3774 3171 125 110 -304 A N ATOM 3067 CA ALA B 11 -1.483 9.757 86.036 1.00 29.08 A C ANISOU 3067 CA ALA B 11 4104 3700 3244 77 142 -348 A C ATOM 3068 C ALA B 11 -2.017 8.405 85.578 1.00 29.37 A C ANISOU 3068 C ALA B 11 4174 3703 3279 84 134 -348 A C ATOM 3069 O ALA B 11 -2.102 7.438 86.389 1.00 30.30 A O ANISOU 3069 O ALA B 11 4220 3792 3500 53 53 -386 A O ATOM 3070 CB ALA B 11 -0.070 9.994 85.533 1.00 28.77 A C ANISOU 3070 CB ALA B 11 3993 3578 3359 233 47 -439 A C ATOM 3071 N ALA B 12 -2.418 8.347 84.309 1.00 28.88 A N ANISOU 3071 N ALA B 12 4029 3676 3267 82 104 -341 A N ATOM 3072 CA ALA B 12 -2.779 7.075 83.709 1.00 28.39 A C ANISOU 3072 CA ALA B 12 3980 3621 3186 -75 122 -317 A C ATOM 3073 C ALA B 12 -1.563 6.525 83.008 1.00 28.88 A C ANISOU 3073 C ALA B 12 4063 3603 3305 -32 187 -449 A C ATOM 3074 O ALA B 12 -1.128 7.049 81.993 1.00 28.25 A O ANISOU 3074 O ALA B 12 4239 3488 3006 -32 233 -635 A O ATOM 3075 CB ALA B 12 -3.968 7.238 82.737 1.00 28.35 A C ANISOU 3075 CB ALA B 12 3931 3674 3167 -174 145 -331 A C ATOM 3076 N VAL B 13 -0.992 5.472 83.591 1.00 28.01 A N ANISOU 3076 N VAL B 13 3903 3440 3297 -82 159 -582 A N ATOM 3077 CA VAL B 13 0.147 4.753 83.027 1.00 29.03 A C ANISOU 3077 CA VAL B 13 3997 3594 3438 -23 190 -431 A C ATOM 3078 C VAL B 13 -0.269 3.526 82.201 1.00 29.43 A C ANISOU 3078 C VAL B 13 4068 3585 3526 0 301 -438 A C ATOM 3079 O VAL B 13 -1.121 2.725 82.611 1.00 29.91 A O ANISOU 3079 O VAL B 13 4096 3597 3672 4 445 -474 A O ATOM 3080 CB VAL B 13 1.118 4.280 84.165 1.00 28.09 A C ANISOU 3080 CB VAL B 13 3905 3419 3347 -109 106 -446 A C ATOM 3081 CG1 VAL B 13 2.311 3.529 83.568 1.00 29.87 A C ANISOU 3081 CG1 VAL B 13 3903 3733 3711 -294 127 -572 A C ATOM 3082 CG2 VAL B 13 1.637 5.462 84.990 1.00 29.90 A C ANISOU 3082 CG2 VAL B 13 4071 3642 3648 52 192 -241 A C ATOM 3083 N LEU B 14 0.368 3.361 81.049 1.00 29.13 A N ANISOU 3083 N LEU B 14 4083 3594 3387 43 382 -400 A N ATOM 3084 CA LEU B 14 0.223 2.147 80.251 1.00 30.33 A C ANISOU 3084 CA LEU B 14 4252 3677 3593 56 322 -464 A C ATOM 3085 C LEU B 14 1.498 1.352 80.480 1.00 30.31 A C ANISOU 3085 C LEU B 14 4223 3596 3695 36 394 -527 A C ATOM 3086 O LEU B 14 2.585 1.741 80.027 1.00 29.98 A O ANISOU 3086 O LEU B 14 4042 3772 3576 -117 474 -553 A O ATOM 3087 CB LEU B 14 0.030 2.494 78.767 1.00 30.69 A C ANISOU 3087 CB LEU B 14 4227 3836 3598 17 309 -397 A C ATOM 3088 CG LEU B 14 -0.358 1.324 77.848 1.00 31.61 A C ANISOU 3088 CG LEU B 14 4358 3867 3783 -11 322 -391 A C ATOM 3089 CD1 LEU B 14 -1.752 0.706 78.157 1.00 32.63 A C ANISOU 3089 CD1 LEU B 14 4253 4300 3843 38 228 -524 A C ATOM 3090 CD2 LEU B 14 -0.267 1.742 76.354 1.00 32.30 A C ANISOU 3090 CD2 LEU B 14 4601 4003 3665 10 339 -391 A C ATOM 3091 N TRP B 15 1.385 0.274 81.255 1.00 31.76 A N ANISOU 3091 N TRP B 15 4464 3750 3850 -20 359 -662 A N ATOM 3092 CA TRP B 15 2.580 -0.470 81.642 1.00 32.23 A C ANISOU 3092 CA TRP B 15 4623 3738 3882 -53 421 -702 A C ATOM 3093 C TRP B 15 3.054 -1.380 80.509 1.00 33.98 A C ANISOU 3093 C TRP B 15 4794 3998 4119 0 482 -665 A C ATOM 3094 O TRP B 15 4.224 -1.695 80.423 1.00 36.12 A O ANISOU 3094 O TRP B 15 4924 4363 4435 91 434 -653 A O ATOM 3095 CB TRP B 15 2.273 -1.316 82.888 1.00 32.57 A C ANISOU 3095 CB TRP B 15 4642 3772 3959 -83 340 -707 A C ATOM 3096 CG TRP B 15 2.143 -0.487 84.105 1.00 32.38 A C ANISOU 3096 CG TRP B 15 4653 3730 3920 -199 224 -777 A C ATOM 3097 CD1 TRP B 15 0.998 -0.213 84.787 1.00 34.12 A C ANISOU 3097 CD1 TRP B 15 4653 4151 4160 -310 106 -514 A C ATOM 3098 CD2 TRP B 15 3.204 0.163 84.822 1.00 33.03 A C ANISOU 3098 CD2 TRP B 15 4683 3798 4068 -247 204 -624 A C ATOM 3099 CE2 TRP B 15 2.622 0.805 85.934 1.00 31.96 A C ANISOU 3099 CE2 TRP B 15 4664 3561 3917 -351 117 -505 A C ATOM 3100 CE3 TRP B 15 4.585 0.227 84.659 1.00 32.91 A C ANISOU 3100 CE3 TRP B 15 4673 3699 4129 -46 -43 -848 A C ATOM 3101 NE1 TRP B 15 1.274 0.564 85.885 1.00 34.62 A N ANISOU 3101 NE1 TRP B 15 4831 4146 4178 -120 97 -530 A N ATOM 3102 CZ2 TRP B 15 3.370 1.540 86.849 1.00 33.15 A C ANISOU 3102 CZ2 TRP B 15 4516 4010 4068 -138 89 -820 A C ATOM 3103 CZ3 TRP B 15 5.326 0.970 85.564 1.00 33.56 A C ANISOU 3103 CZ3 TRP B 15 4886 3966 3898 -135 91 -580 A C ATOM 3104 CH2 TRP B 15 4.719 1.605 86.646 1.00 35.38 A C ANISOU 3104 CH2 TRP B 15 4800 4239 4403 -144 105 -550 A C ATOM 3105 N GLU B 16 2.116 -1.818 79.678 1.00 35.45 A N ANISOU 3105 N GLU B 16 4983 4177 4309 24 454 -526 A N ATOM 3106 CA GLU B 16 2.345 -2.842 78.667 1.00 38.09 A C ANISOU 3106 CA GLU B 16 5253 4496 4723 -21 386 -333 A C ATOM 3107 C GLU B 16 1.266 -2.696 77.622 1.00 37.76 A C ANISOU 3107 C GLU B 16 5254 4436 4655 -68 385 -295 A C ATOM 3108 O GLU B 16 0.156 -2.233 77.931 1.00 37.88 A O ANISOU 3108 O GLU B 16 5268 4502 4622 -158 536 -343 A O ATOM 3109 CB GLU B 16 2.245 -4.242 79.299 1.00 39.52 A C ANISOU 3109 CB GLU B 16 5470 4562 4982 -4 287 -289 A C ATOM 3110 CG GLU B 16 3.528 -4.752 79.962 1.00 44.91 A C ANISOU 3110 CG GLU B 16 5845 5340 5878 -53 147 -182 A C ATOM 3111 CD GLU B 16 3.276 -5.380 81.320 1.00 49.11 A C ANISOU 3111 CD GLU B 16 6445 5915 6300 32 47 -325 A C ATOM 3112 OE1 GLU B 16 2.335 -6.216 81.434 1.00 51.39 A O ANISOU 3112 OE1 GLU B 16 6562 6087 6875 86 -1 -279 A O ATOM 3113 OE2 GLU B 16 4.012 -5.032 82.284 1.00 53.38 A O1- ANISOU 3113 OE2 GLU B 16 6991 6266 7024 211 -99 -24 A O1- ATOM 3114 N GLU B 17 1.566 -3.125 76.396 1.00 38.28 A N ANISOU 3114 N GLU B 17 5387 4448 4709 -37 380 -261 A N ATOM 3115 CA GLU B 17 0.581 -3.133 75.301 1.00 38.51 A C ANISOU 3115 CA GLU B 17 5383 4516 4733 2 350 -98 A C ATOM 3116 C GLU B 17 -0.651 -3.929 75.687 1.00 38.59 A C ANISOU 3116 C GLU B 17 5484 4447 4731 -20 382 -68 A C ATOM 3117 O GLU B 17 -0.554 -4.860 76.500 1.00 38.01 A O ANISOU 3117 O GLU B 17 5539 4230 4671 -35 445 -100 A O ATOM 3118 CB GLU B 17 1.177 -3.839 74.082 1.00 39.42 A C ANISOU 3118 CB GLU B 17 5458 4697 4821 -29 356 -55 A C ATOM 3119 CG GLU B 17 2.052 -3.035 73.179 1.00 43.05 A C ANISOU 3119 CG GLU B 17 5720 5062 5572 58 294 -120 A C ATOM 3120 CD GLU B 17 2.582 -3.901 72.049 1.00 47.31 A C ANISOU 3120 CD GLU B 17 6109 5866 6001 -56 319 113 A C ATOM 3121 OE1 GLU B 17 1.752 -4.527 71.359 1.00 49.24 A O ANISOU 3121 OE1 GLU B 17 6263 6076 6370 -48 281 160 A O ATOM 3122 OE2 GLU B 17 3.822 -3.985 71.872 1.00 51.29 A O1- ANISOU 3122 OE2 GLU B 17 6328 6282 6878 -88 405 -37 A O1- ATOM 3123 N LYS B 18 -1.792 -3.574 75.089 1.00 38.18 A N ANISOU 3123 N LYS B 18 5405 4340 4760 16 422 -82 A N ATOM 3124 CA LYS B 18 -3.033 -4.358 75.192 1.00 39.15 A C ANISOU 3124 CA LYS B 18 5501 4455 4919 7 426 -46 A C ATOM 3125 C LYS B 18 -3.473 -4.573 76.642 1.00 39.04 A C ANISOU 3125 C LYS B 18 5567 4408 4859 40 432 -211 A C ATOM 3126 O LYS B 18 -3.938 -5.667 77.024 1.00 40.20 A O ANISOU 3126 O LYS B 18 5636 4471 5165 111 513 -138 A O ATOM 3127 CB LYS B 18 -2.892 -5.702 74.462 1.00 39.13 A C ANISOU 3127 CB LYS B 18 5542 4333 4990 -16 387 -53 A C ATOM 3128 CG LYS B 18 -2.572 -5.588 72.975 1.00 41.29 A C ANISOU 3128 CG LYS B 18 5606 4818 5261 -94 387 69 A C ATOM 3129 CD LYS B 18 -2.121 -6.953 72.435 1.00 44.42 A C ANISOU 3129 CD LYS B 18 6035 4937 5906 -133 205 209 A C ATOM 3130 CE LYS B 18 -0.727 -7.306 72.971 1.00 47.14 A C ANISOU 3130 CE LYS B 18 6023 5548 6339 -3 -11 202 A C ATOM 3131 NZ LYS B 18 -0.279 -8.711 72.658 1.00 49.07 A N1+ ANISOU 3131 NZ LYS B 18 6294 5691 6658 -88 13 250 A N1+ ATOM 3132 N LYS B 19 -3.314 -3.527 77.449 1.00 38.04 A N ANISOU 3132 N LYS B 19 5471 4332 4649 25 484 -282 A N ATOM 3133 CA LYS B 19 -3.775 -3.510 78.850 1.00 37.04 A C ANISOU 3133 CA LYS B 19 5276 4323 4472 38 547 -401 A C ATOM 3134 C LYS B 19 -4.591 -2.233 79.076 1.00 36.15 A C ANISOU 3134 C LYS B 19 5190 4263 4280 35 556 -468 A C ATOM 3135 O LYS B 19 -4.404 -1.238 78.350 1.00 35.63 A O ANISOU 3135 O LYS B 19 5229 4073 4234 -18 664 -553 A O ATOM 3136 CB LYS B 19 -2.587 -3.518 79.823 1.00 38.17 A C ANISOU 3136 CB LYS B 19 5396 4564 4544 6 549 -465 A C ATOM 3137 CG LYS B 19 -1.649 -4.735 79.753 1.00 39.52 A C ANISOU 3137 CG LYS B 19 5467 4654 4894 -29 431 -256 A C ATOM 3138 CD LYS B 19 -2.151 -5.903 80.596 1.00 43.69 A C ANISOU 3138 CD LYS B 19 6018 5063 5516 2 279 -530 A C ATOM 3139 CE LYS B 19 -1.133 -7.059 80.581 1.00 45.06 A C ANISOU 3139 CE LYS B 19 6079 5225 5815 -158 243 -471 A C ATOM 3140 NZ LYS B 19 -1.487 -8.116 81.586 1.00 50.34 A N1+ ANISOU 3140 NZ LYS B 19 6728 5754 6642 386 400 -376 A N1+ ATOM 3141 N PRO B 20 -5.496 -2.233 80.070 1.00 35.17 A N ANISOU 3141 N PRO B 20 5055 4197 4110 58 586 -579 A N ATOM 3142 CA PRO B 20 -6.144 -0.982 80.454 1.00 34.45 A C ANISOU 3142 CA PRO B 20 4937 4162 3991 147 556 -472 A C ATOM 3143 C PRO B 20 -5.120 -0.020 81.023 1.00 34.10 A C ANISOU 3143 C PRO B 20 4742 4275 3936 124 431 -442 A C ATOM 3144 O PRO B 20 -4.049 -0.459 81.468 1.00 34.49 A O ANISOU 3144 O PRO B 20 4867 4215 4023 106 331 -448 A O ATOM 3145 CB PRO B 20 -7.118 -1.408 81.578 1.00 35.06 A C ANISOU 3145 CB PRO B 20 4989 4310 4021 28 624 -449 A C ATOM 3146 CG PRO B 20 -6.569 -2.672 82.087 1.00 36.25 A C ANISOU 3146 CG PRO B 20 5198 4264 4310 -17 626 -483 A C ATOM 3147 CD PRO B 20 -5.975 -3.366 80.893 1.00 35.44 A C ANISOU 3147 CD PRO B 20 5159 4187 4119 162 588 -516 A C ATOM 3148 N PHE B 21 -5.443 1.276 80.995 1.00 32.63 A N ANISOU 3148 N PHE B 21 4496 4115 3786 219 339 -343 A N ATOM 3149 CA PHE B 21 -4.624 2.276 81.687 1.00 32.82 A C ANISOU 3149 CA PHE B 21 4555 4211 3702 212 230 -332 A C ATOM 3150 C PHE B 21 -4.725 2.052 83.184 1.00 32.39 A C ANISOU 3150 C PHE B 21 4425 4207 3674 202 335 -439 A C ATOM 3151 O PHE B 21 -5.790 1.669 83.727 1.00 33.51 A O ANISOU 3151 O PHE B 21 4237 4538 3953 185 339 -397 A O ATOM 3152 CB PHE B 21 -5.077 3.696 81.354 1.00 31.95 A C ANISOU 3152 CB PHE B 21 4353 4101 3684 195 338 -343 A C ATOM 3153 CG PHE B 21 -4.851 4.065 79.905 1.00 31.45 A C ANISOU 3153 CG PHE B 21 4302 4109 3535 309 153 -293 A C ATOM 3154 CD1 PHE B 21 -3.623 4.539 79.493 1.00 32.04 A C ANISOU 3154 CD1 PHE B 21 4298 4070 3803 281 122 -185 A C ATOM 3155 CD2 PHE B 21 -5.862 3.870 78.953 1.00 30.62 A C ANISOU 3155 CD2 PHE B 21 4166 3875 3591 370 38 -248 A C ATOM 3156 CE1 PHE B 21 -3.402 4.833 78.167 1.00 30.46 A C ANISOU 3156 CE1 PHE B 21 4008 3931 3633 631 96 -178 A C ATOM 3157 CE2 PHE B 21 -5.653 4.175 77.614 1.00 31.65 A C ANISOU 3157 CE2 PHE B 21 4011 3992 4021 482 305 -366 A C ATOM 3158 CZ PHE B 21 -4.421 4.645 77.213 1.00 30.10 A C ANISOU 3158 CZ PHE B 21 3759 3781 3894 490 58 -424 A C ATOM 3159 N SER B 22 -3.600 2.244 83.858 1.00 32.43 A N ANISOU 3159 N SER B 22 4473 4282 3564 163 304 -366 A N ATOM 3160 CA SER B 22 -3.584 2.063 85.311 1.00 33.67 A C ANISOU 3160 CA SER B 22 4610 4401 3780 35 167 -375 A C ATOM 3161 C SER B 22 -3.473 3.448 85.926 1.00 32.28 A C ANISOU 3161 C SER B 22 4408 4261 3596 -12 222 -375 A C ATOM 3162 O SER B 22 -2.523 4.190 85.627 1.00 31.67 A O ANISOU 3162 O SER B 22 4304 4238 3491 -60 284 -405 A O ATOM 3163 CB SER B 22 -2.361 1.225 85.734 1.00 34.82 A C ANISOU 3163 CB SER B 22 4620 4414 4193 -8 183 -287 A C ATOM 3164 OG SER B 22 -2.306 -0.012 85.038 1.00 39.77 A O ANISOU 3164 OG SER B 22 5291 4918 4901 13 148 0 A O ATOM 3165 N ILE B 23 -4.417 3.810 86.795 1.00 31.56 A N ANISOU 3165 N ILE B 23 4350 4234 3407 -6 236 -520 A N ATOM 3166 CA ILE B 23 -4.277 5.067 87.498 1.00 32.17 A C ANISOU 3166 CA ILE B 23 4369 4353 3500 73 263 -480 A C ATOM 3167 C ILE B 23 -3.234 4.866 88.595 1.00 31.88 A C ANISOU 3167 C ILE B 23 4379 4271 3462 94 221 -518 A C ATOM 3168 O ILE B 23 -3.430 4.040 89.534 1.00 33.59 A O ANISOU 3168 O ILE B 23 4807 4372 3580 227 191 -679 A O ATOM 3169 CB ILE B 23 -5.617 5.566 88.106 1.00 32.77 A C ANISOU 3169 CB ILE B 23 4313 4393 3744 25 222 -467 A C ATOM 3170 CG1 ILE B 23 -6.676 5.815 87.001 1.00 32.62 A C ANISOU 3170 CG1 ILE B 23 4197 4525 3673 -58 278 -450 A C ATOM 3171 CG2 ILE B 23 -5.399 6.838 88.917 1.00 34.67 A C ANISOU 3171 CG2 ILE B 23 4526 4710 3935 79 213 -258 A C ATOM 3172 CD1 ILE B 23 -6.270 6.835 85.932 1.00 35.66 A C ANISOU 3172 CD1 ILE B 23 4620 4865 4062 12 77 -561 A C ATOM 3173 N GLU B 24 -2.166 5.661 88.538 1.00 31.07 A N ANISOU 3173 N GLU B 24 4320 4188 3296 85 208 -491 A N ATOM 3174 CA GLU B 24 -1.041 5.491 89.493 1.00 31.32 A C ANISOU 3174 CA GLU B 24 4364 4152 3383 -29 91 -610 A C ATOM 3175 C GLU B 24 -0.646 6.826 90.113 1.00 32.04 A C ANISOU 3175 C GLU B 24 4432 4305 3434 -64 91 -587 A C ATOM 3176 O GLU B 24 -0.859 7.883 89.503 1.00 31.93 A O ANISOU 3176 O GLU B 24 4494 4116 3520 -168 170 -584 A O ATOM 3177 CB GLU B 24 0.204 4.945 88.788 1.00 31.98 A C ANISOU 3177 CB GLU B 24 4537 4149 3465 -17 89 -617 A C ATOM 3178 CG GLU B 24 0.064 3.649 88.000 1.00 33.31 A C ANISOU 3178 CG GLU B 24 4893 3953 3808 46 108 -660 A C ATOM 3179 CD GLU B 24 0.033 2.378 88.897 1.00 35.28 A C ANISOU 3179 CD GLU B 24 5239 4029 4136 -16 115 -618 A C ATOM 3180 OE1 GLU B 24 0.275 2.464 90.125 1.00 35.77 A O ANISOU 3180 OE1 GLU B 24 5363 3915 4312 -78 -234 -604 A O ATOM 3181 OE2 GLU B 24 -0.224 1.295 88.336 1.00 34.63 A O1- ANISOU 3181 OE2 GLU B 24 4912 3633 4613 54 253 -707 A O1- ATOM 3182 N GLU B 25 -0.013 6.770 91.293 1.00 31.87 A N ANISOU 3182 N GLU B 25 4303 4411 3393 -62 38 -672 A N ATOM 3183 CA GLU B 25 0.666 7.905 91.883 1.00 34.15 A C ANISOU 3183 CA GLU B 25 4542 4623 3809 -42 81 -588 A C ATOM 3184 C GLU B 25 2.019 7.992 91.208 1.00 33.41 A C ANISOU 3184 C GLU B 25 4437 4516 3739 -11 66 -632 A C ATOM 3185 O GLU B 25 2.818 7.038 91.243 1.00 34.21 A O ANISOU 3185 O GLU B 25 4454 4646 3895 -73 225 -877 A O ATOM 3186 CB GLU B 25 0.890 7.696 93.406 1.00 34.40 A C ANISOU 3186 CB GLU B 25 4569 4753 3746 44 61 -627 A C ATOM 3187 CG GLU B 25 -0.361 7.704 94.302 1.00 37.26 A C ANISOU 3187 CG GLU B 25 4882 4762 4511 -71 168 -514 A C ATOM 3188 CD GLU B 25 0.003 7.662 95.780 1.00 38.63 A C ANISOU 3188 CD GLU B 25 5045 5111 4520 22 174 -380 A C ATOM 3189 OE1 GLU B 25 1.129 8.103 96.156 1.00 43.35 A O ANISOU 3189 OE1 GLU B 25 5459 5409 5603 97 -328 -113 A O ATOM 3190 OE2 GLU B 25 -0.826 7.192 96.585 1.00 44.29 A O1- ANISOU 3190 OE2 GLU B 25 6052 5255 5519 221 613 -567 A O1- ATOM 3191 N VAL B 26 2.277 9.120 90.570 1.00 32.22 A N ANISOU 3191 N VAL B 26 4290 4476 3474 16 25 -578 A N ATOM 3192 CA VAL B 26 3.574 9.341 89.922 1.00 31.48 A C ANISOU 3192 CA VAL B 26 4259 4412 3287 16 -23 -493 A C ATOM 3193 C VAL B 26 4.256 10.556 90.524 1.00 31.29 A C ANISOU 3193 C VAL B 26 4253 4345 3290 0 -9 -497 A C ATOM 3194 O VAL B 26 3.617 11.344 91.230 1.00 33.00 A O ANISOU 3194 O VAL B 26 4194 4660 3684 124 71 -424 A O ATOM 3195 CB VAL B 26 3.388 9.493 88.392 1.00 31.11 A C ANISOU 3195 CB VAL B 26 4330 4316 3172 34 -46 -475 A C ATOM 3196 CG1 VAL B 26 2.793 8.224 87.781 1.00 31.82 A C ANISOU 3196 CG1 VAL B 26 4392 4208 3487 -151 57 -531 A C ATOM 3197 CG2 VAL B 26 2.507 10.731 88.077 1.00 32.13 A C ANISOU 3197 CG2 VAL B 26 4526 4304 3376 -52 -56 -395 A C ATOM 3198 N GLU B 27 5.558 10.693 90.285 1.00 31.46 A N ANISOU 3198 N GLU B 27 4384 4378 3191 88 4 -516 A N ATOM 3199 CA GLU B 27 6.314 11.857 90.710 1.00 31.65 A C ANISOU 3199 CA GLU B 27 4396 4351 3277 75 11 -497 A C ATOM 3200 C GLU B 27 6.683 12.560 89.419 1.00 30.21 A C ANISOU 3200 C GLU B 27 4220 4183 3075 125 28 -446 A C ATOM 3201 O GLU B 27 7.180 11.924 88.474 1.00 29.73 A O ANISOU 3201 O GLU B 27 4100 4178 3017 70 10 -473 A O ATOM 3202 CB GLU B 27 7.609 11.474 91.438 1.00 32.31 A C ANISOU 3202 CB GLU B 27 4444 4442 3390 101 -44 -350 A C ATOM 3203 CG GLU B 27 7.420 10.880 92.851 1.00 36.13 A C ANISOU 3203 CG GLU B 27 5018 4819 3891 -53 -197 -693 A C ATOM 3204 CD GLU B 27 8.682 11.028 93.733 1.00 36.99 A C ANISOU 3204 CD GLU B 27 5041 4890 4122 -29 -128 -398 A C ATOM 3205 OE1 GLU B 27 9.746 11.463 93.243 1.00 45.36 A O ANISOU 3205 OE1 GLU B 27 5835 5595 5804 -17 118 -339 A O ATOM 3206 OE2 GLU B 27 8.623 10.722 94.927 1.00 44.40 A O1- ANISOU 3206 OE2 GLU B 27 6291 5494 5084 -294 -153 -634 A O1- ATOM 3207 N VAL B 28 6.395 13.846 89.371 1.00 29.42 A N ANISOU 3207 N VAL B 28 4249 4078 2849 117 27 -399 A N ATOM 3208 CA VAL B 28 6.697 14.656 88.188 1.00 29.11 A C ANISOU 3208 CA VAL B 28 4208 3814 3037 111 -67 -396 A C ATOM 3209 C VAL B 28 7.784 15.620 88.591 1.00 29.45 A C ANISOU 3209 C VAL B 28 4256 3874 3058 102 -18 -305 A C ATOM 3210 O VAL B 28 7.574 16.448 89.495 1.00 29.25 A O ANISOU 3210 O VAL B 28 4236 3760 3117 128 40 -146 A O ATOM 3211 CB VAL B 28 5.460 15.409 87.711 1.00 29.18 A C ANISOU 3211 CB VAL B 28 4206 3824 3054 88 -64 -444 A C ATOM 3212 CG1 VAL B 28 5.785 16.176 86.422 1.00 28.13 A C ANISOU 3212 CG1 VAL B 28 4379 3422 2886 37 -43 -518 A C ATOM 3213 CG2 VAL B 28 4.305 14.468 87.446 1.00 28.63 A C ANISOU 3213 CG2 VAL B 28 4226 3385 3265 123 -215 -172 A C ATOM 3214 N ALA B 29 8.960 15.482 87.969 1.00 29.95 A N ANISOU 3214 N ALA B 29 4181 4045 3151 222 6 -186 A N ATOM 3215 CA ALA B 29 10.129 16.326 88.303 1.00 30.73 A C ANISOU 3215 CA ALA B 29 4186 4258 3231 179 -63 -40 A C ATOM 3216 C ALA B 29 9.892 17.790 87.886 1.00 31.13 A C ANISOU 3216 C ALA B 29 4293 4274 3260 288 -139 -60 A C ATOM 3217 O ALA B 29 9.043 18.091 87.034 1.00 32.48 A O ANISOU 3217 O ALA B 29 4615 4379 3344 224 -324 -185 A O ATOM 3218 CB ALA B 29 11.398 15.758 87.628 1.00 31.53 A C ANISOU 3218 CB ALA B 29 4231 4309 3437 62 -29 -41 A C ATOM 3219 N PRO B 30 10.611 18.733 88.499 1.00 31.90 A N ANISOU 3219 N PRO B 30 4530 4265 3326 315 -254 0 A N ATOM 3220 CA PRO B 30 10.476 20.136 88.076 1.00 31.93 A C ANISOU 3220 CA PRO B 30 4519 4264 3347 371 -269 -39 A C ATOM 3221 C PRO B 30 11.101 20.344 86.699 1.00 31.72 A C ANISOU 3221 C PRO B 30 4336 4296 3420 406 -180 -75 A C ATOM 3222 O PRO B 30 11.947 19.558 86.295 1.00 33.08 A O ANISOU 3222 O PRO B 30 4555 4436 3576 413 -57 -174 A O ATOM 3223 CB PRO B 30 11.271 20.920 89.131 1.00 33.01 A C ANISOU 3223 CB PRO B 30 4624 4356 3561 451 -363 -76 A C ATOM 3224 CG PRO B 30 12.150 19.926 89.787 1.00 33.77 A C ANISOU 3224 CG PRO B 30 4764 4260 3806 310 -418 56 A C ATOM 3225 CD PRO B 30 11.576 18.547 89.590 1.00 31.58 A C ANISOU 3225 CD PRO B 30 4569 4235 3194 353 -335 -36 A C ATOM 3226 N PRO B 31 10.671 21.386 85.984 1.00 31.77 A N ANISOU 3226 N PRO B 31 4374 4242 3452 443 -110 -43 A N ATOM 3227 CA PRO B 31 11.210 21.670 84.642 1.00 32.03 A C ANISOU 3227 CA PRO B 31 4389 4272 3505 414 -54 -163 A C ATOM 3228 C PRO B 31 12.646 22.160 84.632 1.00 33.43 A C ANISOU 3228 C PRO B 31 4509 4448 3744 373 -136 -45 A C ATOM 3229 O PRO B 31 13.015 23.049 85.428 1.00 34.41 A O ANISOU 3229 O PRO B 31 4746 4451 3875 524 -166 35 A O ATOM 3230 CB PRO B 31 10.252 22.753 84.105 1.00 32.64 A C ANISOU 3230 CB PRO B 31 4488 4299 3615 332 -23 -104 A C ATOM 3231 CG PRO B 31 9.813 23.449 85.316 1.00 31.42 A C ANISOU 3231 CG PRO B 31 4548 4099 3289 369 -103 -72 A C ATOM 3232 CD PRO B 31 9.624 22.348 86.351 1.00 31.01 A C ANISOU 3232 CD PRO B 31 4196 4211 3373 424 -19 -105 A C ATOM 3233 N LYS B 32 13.445 21.556 83.752 1.00 33.59 A N ANISOU 3233 N LYS B 32 4416 4503 3842 405 -42 -59 A N ATOM 3234 CA LYS B 32 14.834 21.970 83.517 1.00 34.65 A C ANISOU 3234 CA LYS B 32 4518 4509 4137 464 -30 -154 A C ATOM 3235 C LYS B 32 14.841 23.144 82.543 1.00 34.41 A C ANISOU 3235 C LYS B 32 4445 4575 4053 487 -89 -209 A C ATOM 3236 O LYS B 32 13.790 23.730 82.259 1.00 34.80 A O ANISOU 3236 O LYS B 32 4595 4430 4195 565 -6 -120 A O ATOM 3237 CB LYS B 32 15.698 20.819 82.992 1.00 34.38 A C ANISOU 3237 CB LYS B 32 4444 4573 4046 397 -44 -157 A C ATOM 3238 CG LYS B 32 15.761 19.597 83.906 1.00 36.72 A C ANISOU 3238 CG LYS B 32 4731 4504 4717 572 93 -165 A C ATOM 3239 CD LYS B 32 16.807 18.608 83.431 1.00 40.57 A C ANISOU 3239 CD LYS B 32 5063 4908 5442 357 -40 35 A C ATOM 3240 CE LYS B 32 17.097 17.547 84.502 1.00 43.27 A C ANISOU 3240 CE LYS B 32 5642 5039 5757 361 -1 -96 A C ATOM 3241 NZ LYS B 32 18.569 17.224 84.619 1.00 46.81 A N1+ ANISOU 3241 NZ LYS B 32 6053 5587 6144 139 -85 108 A N1+ ATOM 3242 N ALA B 33 16.020 23.531 82.067 1.00 34.00 A N ANISOU 3242 N ALA B 33 4405 4536 3976 505 -41 -238 A N ATOM 3243 CA ALA B 33 16.071 24.707 81.215 1.00 34.31 A C ANISOU 3243 CA ALA B 33 4445 4582 4008 595 -94 -303 A C ATOM 3244 C ALA B 33 15.193 24.475 80.011 1.00 34.20 A C ANISOU 3244 C ALA B 33 4504 4489 4001 587 -61 -250 A C ATOM 3245 O ALA B 33 15.260 23.416 79.387 1.00 35.14 A O ANISOU 3245 O ALA B 33 4666 4576 4109 633 -32 -320 A O ATOM 3246 CB ALA B 33 17.479 25.000 80.768 1.00 34.54 A C ANISOU 3246 CB ALA B 33 4406 4684 4030 530 -16 -254 A C ATOM 3247 N HIS B 34 14.380 25.481 79.692 1.00 34.55 A N ANISOU 3247 N HIS B 34 4503 4577 4047 622 -131 -213 A N ATOM 3248 CA HIS B 34 13.600 25.499 78.455 1.00 33.72 A C ANISOU 3248 CA HIS B 34 4497 4432 3881 580 -53 -187 A C ATOM 3249 C HIS B 34 12.496 24.467 78.493 1.00 32.28 A C ANISOU 3249 C HIS B 34 4438 4198 3628 617 -72 -180 A C ATOM 3250 O HIS B 34 12.005 24.017 77.465 1.00 31.14 A O ANISOU 3250 O HIS B 34 4504 3926 3400 701 -88 -87 A O ATOM 3251 CB HIS B 34 14.504 25.334 77.231 1.00 34.47 A C ANISOU 3251 CB HIS B 34 4483 4434 4177 638 77 -234 A C ATOM 3252 CG HIS B 34 15.500 26.444 77.084 1.00 38.95 A C ANISOU 3252 CG HIS B 34 4843 4900 5056 642 175 -106 A C ATOM 3253 CD2 HIS B 34 15.325 27.774 76.914 1.00 40.81 A C ANISOU 3253 CD2 HIS B 34 5047 4988 5469 439 136 -187 A C ATOM 3254 ND1 HIS B 34 16.859 26.242 77.173 1.00 40.89 A N ANISOU 3254 ND1 HIS B 34 4976 5076 5483 312 89 99 A N ATOM 3255 CE1 HIS B 34 17.486 27.397 77.016 1.00 42.28 A C ANISOU 3255 CE1 HIS B 34 5110 5231 5724 387 205 -224 A C ATOM 3256 NE2 HIS B 34 16.577 28.343 76.858 1.00 43.44 A N ANISOU 3256 NE2 HIS B 34 5158 5418 5926 477 60 -127 A N ATOM 3257 N GLU B 35 12.082 24.119 79.711 1.00 31.35 A N ANISOU 3257 N GLU B 35 4175 4204 3530 642 3 -148 A N ATOM 3258 CA GLU B 35 10.950 23.214 79.916 1.00 31.39 A C ANISOU 3258 CA GLU B 35 4343 4080 3502 626 94 -129 A C ATOM 3259 C GLU B 35 9.865 23.921 80.697 1.00 31.13 A C ANISOU 3259 C GLU B 35 4367 3989 3471 644 107 -70 A C ATOM 3260 O GLU B 35 10.144 24.907 81.404 1.00 31.79 A O ANISOU 3260 O GLU B 35 4574 3882 3621 796 370 -205 A O ATOM 3261 CB GLU B 35 11.400 21.930 80.617 1.00 30.83 A C ANISOU 3261 CB GLU B 35 4154 4029 3527 597 35 -97 A C ATOM 3262 CG GLU B 35 12.501 21.212 79.860 1.00 31.62 A C ANISOU 3262 CG GLU B 35 4531 4036 3446 360 72 -83 A C ATOM 3263 CD GLU B 35 13.010 19.977 80.570 1.00 31.86 A C ANISOU 3263 CD GLU B 35 4251 4258 3597 280 31 -323 A C ATOM 3264 OE1 GLU B 35 12.552 19.719 81.703 1.00 34.36 A O ANISOU 3264 OE1 GLU B 35 4646 4789 3619 242 130 -332 A O ATOM 3265 OE2 GLU B 35 13.866 19.263 79.992 1.00 34.51 A O1- ANISOU 3265 OE2 GLU B 35 5117 4205 3789 588 372 -424 A O1- ATOM 3266 N VAL B 36 8.648 23.382 80.602 1.00 29.47 A N ANISOU 3266 N VAL B 36 4246 3830 3118 692 311 -198 A N ATOM 3267 CA VAL B 36 7.448 24.005 81.131 1.00 29.60 A C ANISOU 3267 CA VAL B 36 4379 3738 3128 665 93 -178 A C ATOM 3268 C VAL B 36 6.659 22.913 81.848 1.00 29.53 A C ANISOU 3268 C VAL B 36 4595 3695 2928 619 149 -215 A C ATOM 3269 O VAL B 36 6.348 21.872 81.241 1.00 29.13 A O ANISOU 3269 O VAL B 36 4578 3466 3024 776 104 -237 A O ATOM 3270 CB VAL B 36 6.582 24.628 79.988 1.00 29.83 A C ANISOU 3270 CB VAL B 36 4368 3730 3235 640 193 -387 A C ATOM 3271 CG1 VAL B 36 5.279 25.211 80.541 1.00 30.33 A C ANISOU 3271 CG1 VAL B 36 4549 3509 3464 490 31 30 A C ATOM 3272 CG2 VAL B 36 7.380 25.702 79.209 1.00 30.07 A C ANISOU 3272 CG2 VAL B 36 4271 3860 3294 867 229 -226 A C ATOM 3273 N ARG B 37 6.319 23.138 83.119 1.00 30.23 A N ANISOU 3273 N ARG B 37 4635 3918 2931 531 21 -259 A N ATOM 3274 CA ARG B 37 5.445 22.176 83.827 1.00 29.09 A C ANISOU 3274 CA ARG B 37 4578 3827 2647 504 -99 -287 A C ATOM 3275 C ARG B 37 3.992 22.690 83.827 1.00 30.76 A C ANISOU 3275 C ARG B 37 4789 3943 2952 427 -4 -224 A C ATOM 3276 O ARG B 37 3.724 23.846 84.146 1.00 32.15 A O ANISOU 3276 O ARG B 37 5060 3874 3281 517 -103 -84 A O ATOM 3277 CB ARG B 37 5.976 21.872 85.244 1.00 29.50 A C ANISOU 3277 CB ARG B 37 4525 4008 2674 594 -158 -283 A C ATOM 3278 CG ARG B 37 5.123 20.853 85.986 1.00 27.97 A C ANISOU 3278 CG ARG B 37 4519 3754 2354 497 -302 -395 A C ATOM 3279 CD ARG B 37 5.945 20.171 87.059 1.00 29.60 A C ANISOU 3279 CD ARG B 37 4460 4098 2687 275 -410 -245 A C ATOM 3280 NE ARG B 37 6.282 21.106 88.126 1.00 31.36 A N ANISOU 3280 NE ARG B 37 4537 4464 2913 352 -148 28 A N ATOM 3281 CZ ARG B 37 6.904 20.769 89.255 1.00 30.67 A C ANISOU 3281 CZ ARG B 37 4329 3956 3367 139 -392 -94 A C ATOM 3282 NH1 ARG B 37 7.313 19.516 89.476 1.00 28.46 A N1+ ANISOU 3282 NH1 ARG B 37 3957 3792 3062 -41 -255 265 A N1+ ATOM 3283 NH2 ARG B 37 7.090 21.691 90.190 1.00 30.21 A N ANISOU 3283 NH2 ARG B 37 3933 3958 3585 436 -168 133 A N ATOM 3284 N ILE B 38 3.054 21.832 83.445 1.00 29.93 A N ANISOU 3284 N ILE B 38 4684 3959 2728 377 20 -242 A N ATOM 3285 CA ILE B 38 1.678 22.237 83.196 1.00 29.59 A C ANISOU 3285 CA ILE B 38 4646 3962 2633 207 61 -200 A C ATOM 3286 C ILE B 38 0.686 21.426 84.050 1.00 29.32 A C ANISOU 3286 C ILE B 38 4534 3880 2724 170 126 -156 A C ATOM 3287 O ILE B 38 0.777 20.183 84.101 1.00 28.91 A O ANISOU 3287 O ILE B 38 4383 3880 2719 153 121 -250 A O ATOM 3288 CB ILE B 38 1.290 21.976 81.683 1.00 29.18 A C ANISOU 3288 CB ILE B 38 4615 3818 2651 206 105 -232 A C ATOM 3289 CG1 ILE B 38 2.290 22.622 80.728 1.00 28.86 A C ANISOU 3289 CG1 ILE B 38 4744 3856 2363 367 122 -96 A C ATOM 3290 CG2 ILE B 38 -0.199 22.349 81.407 1.00 30.46 A C ANISOU 3290 CG2 ILE B 38 4663 4152 2757 179 -239 -211 A C ATOM 3291 CD1 ILE B 38 2.054 22.195 79.267 1.00 28.88 A C ANISOU 3291 CD1 ILE B 38 4854 3804 2316 167 109 -91 A C ATOM 3292 N LYS B 39 -0.271 22.117 84.692 1.00 29.45 A N ANISOU 3292 N LYS B 39 4493 3925 2772 111 144 -100 A N ATOM 3293 CA LYS B 39 -1.379 21.459 85.380 1.00 30.39 A C ANISOU 3293 CA LYS B 39 4586 3944 3014 95 202 45 A C ATOM 3294 C LYS B 39 -2.494 21.208 84.381 1.00 30.28 A C ANISOU 3294 C LYS B 39 4453 3936 3113 72 127 -24 A C ATOM 3295 O LYS B 39 -3.038 22.155 83.803 1.00 30.76 A O ANISOU 3295 O LYS B 39 4525 3856 3307 148 55 -6 A O ATOM 3296 CB LYS B 39 -1.916 22.324 86.529 1.00 30.48 A C ANISOU 3296 CB LYS B 39 4649 3926 3003 114 278 62 A C ATOM 3297 CG LYS B 39 -3.027 21.604 87.307 1.00 31.22 A C ANISOU 3297 CG LYS B 39 4674 4226 2960 113 332 177 A C ATOM 3298 CD LYS B 39 -3.654 22.482 88.418 1.00 33.30 A C ANISOU 3298 CD LYS B 39 4889 4350 3411 32 403 263 A C ATOM 3299 CE LYS B 39 -4.599 21.617 89.257 1.00 38.54 A C ANISOU 3299 CE LYS B 39 5360 4861 4423 -65 348 -301 A C ATOM 3300 NZ LYS B 39 -3.833 20.511 89.904 1.00 42.39 A N1+ ANISOU 3300 NZ LYS B 39 5806 5330 4971 42 34 -451 A N1+ ATOM 3301 N MET B 40 -2.808 19.944 84.120 1.00 29.63 A N ANISOU 3301 N MET B 40 4360 3859 3040 48 58 -5 A N ATOM 3302 CA MET B 40 -3.855 19.650 83.110 1.00 30.16 A C ANISOU 3302 CA MET B 40 4370 3895 3194 -14 -45 20 A C ATOM 3303 C MET B 40 -5.239 20.056 83.555 1.00 30.62 A C ANISOU 3303 C MET B 40 4446 3946 3242 -69 11 34 A C ATOM 3304 O MET B 40 -5.594 19.896 84.725 1.00 31.31 A O ANISOU 3304 O MET B 40 4497 4083 3314 128 59 4 A O ATOM 3305 CB MET B 40 -3.888 18.183 82.704 1.00 31.10 A C ANISOU 3305 CB MET B 40 4521 3965 3329 -96 -19 0 A C ATOM 3306 CG MET B 40 -4.131 17.991 81.218 1.00 33.26 A C ANISOU 3306 CG MET B 40 4898 4227 3512 -175 -95 196 A C ATOM 3307 SD MET B 40 -2.607 18.348 80.306 1.00 38.97 A S ANISOU 3307 SD MET B 40 6208 5161 3437 -379 439 -118 A S ATOM 3308 CE MET B 40 -1.451 17.470 81.380 1.00 41.37 A C ANISOU 3308 CE MET B 40 6048 5266 4402 7 -283 63 A C ATOM 3309 N VAL B 41 -6.030 20.564 82.604 1.00 29.88 A N ANISOU 3309 N VAL B 41 4305 3915 3133 -57 -41 120 A N ATOM 3310 CA VAL B 41 -7.423 20.916 82.876 1.00 29.34 A C ANISOU 3310 CA VAL B 41 4229 3746 3172 -212 38 164 A C ATOM 3311 C VAL B 41 -8.382 20.017 82.120 1.00 29.12 A C ANISOU 3311 C VAL B 41 4169 3739 3154 -242 135 168 A C ATOM 3312 O VAL B 41 -9.448 19.610 82.641 1.00 29.50 A O ANISOU 3312 O VAL B 41 4303 3726 3179 -273 185 252 A O ATOM 3313 CB VAL B 41 -7.704 22.432 82.620 1.00 30.36 A C ANISOU 3313 CB VAL B 41 4229 3838 3467 -77 -42 51 A C ATOM 3314 CG1 VAL B 41 -9.205 22.770 82.720 1.00 28.68 A C ANISOU 3314 CG1 VAL B 41 4141 3248 3508 -193 272 -20 A C ATOM 3315 CG2 VAL B 41 -6.865 23.334 83.563 1.00 31.24 A C ANISOU 3315 CG2 VAL B 41 4549 3913 3408 -232 54 467 A C ATOM 3316 N ALA B 42 -8.012 19.700 80.877 1.00 27.69 A N ANISOU 3316 N ALA B 42 4146 3488 2886 -253 36 230 A N ATOM 3317 CA ALA B 42 -8.821 18.758 80.094 1.00 26.52 A C ANISOU 3317 CA ALA B 42 3859 3282 2933 -252 166 226 A C ATOM 3318 C ALA B 42 -7.974 18.136 79.036 1.00 25.51 A C ANISOU 3318 C ALA B 42 3648 3216 2829 -289 291 214 A C ATOM 3319 O ALA B 42 -7.028 18.764 78.496 1.00 27.15 A O ANISOU 3319 O ALA B 42 3963 3313 3040 -209 289 393 A O ATOM 3320 CB ALA B 42 -10.022 19.443 79.430 1.00 26.90 A C ANISOU 3320 CB ALA B 42 3894 3271 3055 -322 24 193 A C ATOM 3321 N THR B 43 -8.332 16.915 78.704 1.00 25.58 A N ANISOU 3321 N THR B 43 3582 3332 2804 -37 458 91 A N ATOM 3322 CA THR B 43 -7.617 16.161 77.637 1.00 26.77 A C ANISOU 3322 CA THR B 43 3796 3460 2913 -86 350 76 A C ATOM 3323 C THR B 43 -8.589 15.289 76.857 1.00 26.34 A C ANISOU 3323 C THR B 43 3705 3448 2851 12 316 -30 A C ATOM 3324 O THR B 43 -9.486 14.670 77.435 1.00 27.99 A O ANISOU 3324 O THR B 43 3979 3633 3023 -144 275 -54 A O ATOM 3325 CB THR B 43 -6.389 15.364 78.183 1.00 27.17 A C ANISOU 3325 CB THR B 43 3829 3382 3111 -40 384 16 A C ATOM 3326 CG2 THR B 43 -6.809 14.348 79.195 1.00 27.01 A C ANISOU 3326 CG2 THR B 43 3803 3477 2981 -25 355 -346 A C ATOM 3327 OG1 THR B 43 -5.687 14.694 77.125 1.00 27.35 A O ANISOU 3327 OG1 THR B 43 3630 3481 3279 -281 390 17 A O ATOM 3328 N GLY B 44 -8.453 15.302 75.530 1.00 27.15 A N ANISOU 3328 N GLY B 44 3841 3517 2955 66 464 82 A N ATOM 3329 CA GLY B 44 -9.321 14.524 74.654 1.00 27.12 A C ANISOU 3329 CA GLY B 44 3738 3466 3101 83 332 61 A C ATOM 3330 C GLY B 44 -8.764 13.123 74.461 1.00 28.85 A C ANISOU 3330 C GLY B 44 3959 3687 3314 101 393 58 A C ATOM 3331 O GLY B 44 -7.550 12.913 74.617 1.00 30.92 A O ANISOU 3331 O GLY B 44 4218 3838 3691 182 304 117 A O ATOM 3332 N ILE B 45 -9.643 12.160 74.181 1.00 28.29 A N ANISOU 3332 N ILE B 45 4061 3655 3030 124 418 18 A N ATOM 3333 CA ILE B 45 -9.194 10.808 73.850 1.00 29.11 A C ANISOU 3333 CA ILE B 45 4063 3757 3239 161 369 -99 A C ATOM 3334 C ILE B 45 -9.186 10.661 72.348 1.00 29.31 A C ANISOU 3334 C ILE B 45 3972 3910 3252 136 345 -87 A C ATOM 3335 O ILE B 45 -10.247 10.697 71.713 1.00 29.79 A O ANISOU 3335 O ILE B 45 4043 4063 3212 37 292 -114 A O ATOM 3336 CB ILE B 45 -10.135 9.745 74.494 1.00 29.02 A C ANISOU 3336 CB ILE B 45 3994 3703 3327 222 343 -94 A C ATOM 3337 CG1 ILE B 45 -9.973 9.789 76.012 1.00 28.56 A C ANISOU 3337 CG1 ILE B 45 3901 3605 3343 -49 310 -187 A C ATOM 3338 CG2 ILE B 45 -9.841 8.326 73.952 1.00 31.49 A C ANISOU 3338 CG2 ILE B 45 4339 3897 3727 233 307 11 A C ATOM 3339 CD1 ILE B 45 -11.004 8.968 76.747 1.00 30.37 A C ANISOU 3339 CD1 ILE B 45 3904 4197 3436 -34 396 -462 A C ATOM 3340 N CYS B 46 -7.980 10.520 71.781 1.00 29.45 A N ANISOU 3340 N CYS B 46 4017 3946 3225 112 334 -47 A N ATOM 3341 CA CYS B 46 -7.826 10.386 70.331 1.00 29.66 A C ANISOU 3341 CA CYS B 46 3970 3963 3335 239 327 -104 A C ATOM 3342 C CYS B 46 -7.501 8.953 69.891 1.00 29.44 A C ANISOU 3342 C CYS B 46 3909 3956 3319 176 243 -122 A C ATOM 3343 O CYS B 46 -6.841 8.214 70.626 1.00 29.05 A O ANISOU 3343 O CYS B 46 3799 3953 3283 13 -10 63 A O ATOM 3344 CB CYS B 46 -6.724 11.360 69.911 1.00 28.69 A C ANISOU 3344 CB CYS B 46 3920 3689 3291 246 437 -267 A C ATOM 3345 SG CYS B 46 -6.229 11.227 68.162 1.00 30.96 A S ANISOU 3345 SG CYS B 46 4283 3902 3575 376 284 -6 A S ATOM 3346 N ARG B 47 -7.950 8.563 68.687 1.00 30.80 A N ANISOU 3346 N ARG B 47 4069 4077 3555 237 163 -23 A N ATOM 3347 CA ARG B 47 -7.621 7.266 68.076 1.00 33.23 A C ANISOU 3347 CA ARG B 47 4426 4229 3968 212 78 31 A C ATOM 3348 C ARG B 47 -6.130 6.950 68.216 1.00 31.31 A C ANISOU 3348 C ARG B 47 4304 3975 3616 252 176 99 A C ATOM 3349 O ARG B 47 -5.745 5.819 68.489 1.00 31.77 A O ANISOU 3349 O ARG B 47 4415 3936 3721 493 148 67 A O ATOM 3350 CB ARG B 47 -8.017 7.266 66.579 1.00 35.13 A C ANISOU 3350 CB ARG B 47 4649 4557 4140 149 -9 58 A C ATOM 3351 CG ARG B 47 -8.452 5.915 65.911 1.00 38.26 A C ANISOU 3351 CG ARG B 47 5278 4609 4647 75 -60 -101 A C ATOM 3352 CD ARG B 47 -8.854 6.128 64.380 1.00 37.97 A C ANISOU 3352 CD ARG B 47 4993 4818 4614 271 -177 121 A C ATOM 3353 NE ARG B 47 -9.655 5.045 63.789 1.00 43.55 A N ANISOU 3353 NE ARG B 47 5695 5355 5496 148 -291 336 A N ATOM 3354 CZ ARG B 47 -9.642 4.700 62.502 1.00 45.57 A C ANISOU 3354 CZ ARG B 47 5903 5707 5702 81 -40 219 A C ATOM 3355 NH1 ARG B 47 -8.832 5.308 61.648 1.00 48.15 A N1+ ANISOU 3355 NH1 ARG B 47 6291 5779 6224 212 17 -63 A N1+ ATOM 3356 NH2 ARG B 47 -10.416 3.707 62.064 1.00 49.29 A N ANISOU 3356 NH2 ARG B 47 6346 6043 6336 256 -93 267 A N ATOM 3357 N SER B 48 -5.272 7.952 68.036 1.00 29.84 A N ANISOU 3357 N SER B 48 4299 3669 3368 254 262 87 A N ATOM 3358 CA SER B 48 -3.847 7.702 68.118 1.00 29.02 A C ANISOU 3358 CA SER B 48 4098 3592 3334 159 398 57 A C ATOM 3359 C SER B 48 -3.373 7.210 69.486 1.00 28.62 A C ANISOU 3359 C SER B 48 3952 3605 3314 115 413 -18 A C ATOM 3360 O SER B 48 -2.419 6.419 69.570 1.00 28.37 A O ANISOU 3360 O SER B 48 3978 3639 3163 171 452 -70 A O ATOM 3361 CB SER B 48 -3.041 8.925 67.702 1.00 29.67 A C ANISOU 3361 CB SER B 48 4201 3641 3432 273 300 113 A C ATOM 3362 OG SER B 48 -3.296 9.220 66.343 1.00 31.43 A O ANISOU 3362 OG SER B 48 4845 3524 3571 -53 347 217 A O ATOM 3363 N ASP B 49 -4.044 7.663 70.552 1.00 27.50 A N ANISOU 3363 N ASP B 49 3766 3476 3205 17 422 43 A N ATOM 3364 CA ASP B 49 -3.766 7.160 71.886 1.00 28.87 A C ANISOU 3364 CA ASP B 49 4081 3507 3381 35 431 2 A C ATOM 3365 C ASP B 49 -4.084 5.655 72.011 1.00 29.24 A C ANISOU 3365 C ASP B 49 4119 3488 3501 71 434 -22 A C ATOM 3366 O ASP B 49 -3.328 4.904 72.649 1.00 30.71 A O ANISOU 3366 O ASP B 49 4391 3539 3740 112 499 -19 A O ATOM 3367 CB ASP B 49 -4.524 7.958 72.960 1.00 28.34 A C ANISOU 3367 CB ASP B 49 4112 3328 3326 -41 499 -46 A C ATOM 3368 CG ASP B 49 -4.174 9.444 72.942 1.00 29.59 A C ANISOU 3368 CG ASP B 49 4287 3391 3562 121 265 34 A C ATOM 3369 OD1 ASP B 49 -2.965 9.819 73.090 1.00 28.95 A O ANISOU 3369 OD1 ASP B 49 4674 2841 3482 243 331 -433 A O ATOM 3370 OD2 ASP B 49 -5.132 10.228 72.777 1.00 30.90 A O1- ANISOU 3370 OD2 ASP B 49 4338 3761 3641 181 129 178 A O1- ATOM 3371 N ASP B 50 -5.174 5.238 71.362 1.00 29.87 A N ANISOU 3371 N ASP B 50 4194 3572 3581 226 489 -17 A N ATOM 3372 CA ASP B 50 -5.607 3.836 71.272 1.00 31.68 A C ANISOU 3372 CA ASP B 50 4417 3694 3923 224 427 -88 A C ATOM 3373 C ASP B 50 -4.604 3.023 70.467 1.00 31.64 A C ANISOU 3373 C ASP B 50 4512 3676 3830 250 430 -88 A C ATOM 3374 O ASP B 50 -4.329 1.857 70.789 1.00 31.56 A O ANISOU 3374 O ASP B 50 4535 3543 3913 472 482 -202 A O ATOM 3375 CB ASP B 50 -6.972 3.781 70.598 1.00 32.73 A C ANISOU 3375 CB ASP B 50 4417 3812 4207 218 437 -18 A C ATOM 3376 CG ASP B 50 -7.661 2.446 70.757 1.00 35.87 A C ANISOU 3376 CG ASP B 50 4777 4106 4746 117 307 2 A C ATOM 3377 OD1 ASP B 50 -7.689 1.940 71.877 1.00 39.38 A O ANISOU 3377 OD1 ASP B 50 5480 4579 4901 261 762 -61 A O ATOM 3378 OD2 ASP B 50 -8.188 1.920 69.751 1.00 40.92 A O1- ANISOU 3378 OD2 ASP B 50 5545 4798 5202 207 240 303 A O1- ATOM 3379 N HIS B 51 -4.009 3.647 69.441 1.00 30.36 A N ANISOU 3379 N HIS B 51 4301 3543 3691 315 510 -141 A N ATOM 3380 CA HIS B 51 -2.977 2.945 68.657 1.00 31.09 A C ANISOU 3380 CA HIS B 51 4440 3683 3687 288 519 -110 A C ATOM 3381 C HIS B 51 -1.749 2.590 69.507 1.00 30.79 A C ANISOU 3381 C HIS B 51 4465 3621 3611 269 606 -238 A C ATOM 3382 O HIS B 51 -1.067 1.609 69.244 1.00 32.41 A O ANISOU 3382 O HIS B 51 4743 3738 3831 250 636 -141 A O ATOM 3383 CB HIS B 51 -2.588 3.759 67.416 1.00 32.16 A C ANISOU 3383 CB HIS B 51 4562 3956 3700 209 527 -60 A C ATOM 3384 CG HIS B 51 -3.691 3.907 66.419 1.00 33.51 A C ANISOU 3384 CG HIS B 51 4724 4111 3898 11 435 157 A C ATOM 3385 CD2 HIS B 51 -4.794 3.155 66.190 1.00 37.31 A C ANISOU 3385 CD2 HIS B 51 5158 4448 4571 94 211 90 A C ATOM 3386 ND1 HIS B 51 -3.740 4.942 65.509 1.00 33.82 A N ANISOU 3386 ND1 HIS B 51 4896 4178 3776 -240 274 305 A N ATOM 3387 CE1 HIS B 51 -4.816 4.811 64.754 1.00 37.18 A C ANISOU 3387 CE1 HIS B 51 5001 4673 4452 67 171 198 A C ATOM 3388 NE2 HIS B 51 -5.469 3.731 65.142 1.00 38.97 A N ANISOU 3388 NE2 HIS B 51 5333 4687 4784 38 57 42 A N ATOM 3389 N VAL B 52 -1.441 3.398 70.510 1.00 30.60 A N ANISOU 3389 N VAL B 52 4484 3526 3615 265 494 -253 A N ATOM 3390 CA VAL B 52 -0.363 3.042 71.464 1.00 31.27 A C ANISOU 3390 CA VAL B 52 4537 3599 3745 240 466 -351 A C ATOM 3391 C VAL B 52 -0.740 1.759 72.227 1.00 31.97 A C ANISOU 3391 C VAL B 52 4628 3595 3920 220 393 -325 A C ATOM 3392 O VAL B 52 0.087 0.828 72.376 1.00 32.34 A O ANISOU 3392 O VAL B 52 4884 3248 4155 351 504 -595 A O ATOM 3393 CB VAL B 52 -0.024 4.236 72.413 1.00 30.03 A C ANISOU 3393 CB VAL B 52 4345 3562 3501 145 470 -332 A C ATOM 3394 CG1 VAL B 52 1.083 3.873 73.463 1.00 30.49 A C ANISOU 3394 CG1 VAL B 52 4505 3542 3537 172 336 -307 A C ATOM 3395 CG2 VAL B 52 0.459 5.452 71.594 1.00 32.30 A C ANISOU 3395 CG2 VAL B 52 4779 3808 3685 190 507 -306 A C ATOM 3396 N VAL B 53 -1.969 1.734 72.728 1.00 33.29 A N ANISOU 3396 N VAL B 53 4785 3815 4049 243 382 -311 A N ATOM 3397 CA VAL B 53 -2.490 0.573 73.454 1.00 33.89 A C ANISOU 3397 CA VAL B 53 4866 3839 4172 218 413 -239 A C ATOM 3398 C VAL B 53 -2.401 -0.690 72.584 1.00 35.58 A C ANISOU 3398 C VAL B 53 5126 3996 4394 250 299 -118 A C ATOM 3399 O VAL B 53 -1.902 -1.719 73.050 1.00 35.72 A O ANISOU 3399 O VAL B 53 5283 3883 4403 144 371 3 A O ATOM 3400 CB VAL B 53 -3.930 0.786 73.949 1.00 33.86 A C ANISOU 3400 CB VAL B 53 4914 3828 4121 266 432 -342 A C ATOM 3401 CG1 VAL B 53 -4.411 -0.482 74.706 1.00 34.18 A C ANISOU 3401 CG1 VAL B 53 4986 3904 4096 297 622 -484 A C ATOM 3402 CG2 VAL B 53 -4.016 2.024 74.822 1.00 32.77 A C ANISOU 3402 CG2 VAL B 53 4700 3914 3835 285 396 -352 A C ATOM 3403 N SER B 54 -2.827 -0.586 71.324 1.00 36.50 A N ANISOU 3403 N SER B 54 5251 4135 4482 206 353 -92 A N ATOM 3404 CA SER B 54 -2.854 -1.757 70.428 1.00 37.33 A C ANISOU 3404 CA SER B 54 5321 4243 4619 217 343 -51 A C ATOM 3405 C SER B 54 -1.451 -2.250 70.032 1.00 37.90 A C ANISOU 3405 C SER B 54 5346 4298 4757 149 274 -17 A C ATOM 3406 O SER B 54 -1.298 -3.373 69.517 1.00 39.06 A O ANISOU 3406 O SER B 54 5521 4259 5060 247 305 -35 A O ATOM 3407 CB SER B 54 -3.646 -1.445 69.159 1.00 37.60 A C ANISOU 3407 CB SER B 54 5251 4292 4743 167 260 122 A C ATOM 3408 OG SER B 54 -4.948 -0.995 69.458 1.00 41.81 A O ANISOU 3408 OG SER B 54 5541 4982 5361 213 430 -141 A O ATOM 3409 N GLY B 55 -0.437 -1.400 70.214 1.00 38.07 A N ANISOU 3409 N GLY B 55 5364 4400 4702 127 292 -122 A N ATOM 3410 CA GLY B 55 0.913 -1.717 69.776 1.00 38.43 A C ANISOU 3410 CA GLY B 55 5390 4553 4658 85 312 -101 A C ATOM 3411 C GLY B 55 1.158 -1.351 68.319 1.00 39.11 A C ANISOU 3411 C GLY B 55 5449 4708 4702 31 337 -57 A C ATOM 3412 O GLY B 55 2.206 -1.674 67.742 1.00 40.26 A O ANISOU 3412 O GLY B 55 5620 4699 4975 -46 396 -31 A O ATOM 3413 N THR B 56 0.200 -0.665 67.721 1.00 38.59 A N ANISOU 3413 N THR B 56 5414 4619 4630 29 381 -19 A N ATOM 3414 CA THR B 56 0.316 -0.311 66.298 1.00 37.73 A C ANISOU 3414 CA THR B 56 5362 4572 4401 -51 379 105 A C ATOM 3415 C THR B 56 1.069 0.997 66.087 1.00 37.06 A C ANISOU 3415 C THR B 56 5293 4539 4246 -114 474 98 A C ATOM 3416 O THR B 56 1.721 1.165 65.052 1.00 37.82 A O ANISOU 3416 O THR B 56 5472 4633 4265 -102 525 149 A O ATOM 3417 CB THR B 56 -1.042 -0.365 65.541 1.00 38.55 A C ANISOU 3417 CB THR B 56 5427 4615 4605 -8 394 89 A C ATOM 3418 CG2 THR B 56 -1.674 -1.772 65.643 1.00 38.47 A C ANISOU 3418 CG2 THR B 56 5471 4524 4620 -15 249 122 A C ATOM 3419 OG1 THR B 56 -1.960 0.600 66.077 1.00 40.93 A O ANISOU 3419 OG1 THR B 56 5649 4837 5065 -190 60 210 A O ATOM 3420 N LEU B 57 0.957 1.943 67.035 1.00 35.15 A N ANISOU 3420 N LEU B 57 5064 4353 3937 -174 475 97 A N ATOM 3421 CA LEU B 57 1.850 3.099 67.079 1.00 35.16 A C ANISOU 3421 CA LEU B 57 5017 4343 3999 -239 508 135 A C ATOM 3422 C LEU B 57 2.929 2.693 68.084 1.00 34.72 A C ANISOU 3422 C LEU B 57 4890 4289 4012 -171 460 101 A C ATOM 3423 O LEU B 57 2.678 2.613 69.289 1.00 35.08 A O ANISOU 3423 O LEU B 57 4960 4303 4063 -211 479 -22 A O ATOM 3424 CB LEU B 57 1.108 4.388 67.504 1.00 35.54 A C ANISOU 3424 CB LEU B 57 5017 4476 4011 -251 563 119 A C ATOM 3425 CG LEU B 57 1.341 5.767 66.855 1.00 37.94 A C ANISOU 3425 CG LEU B 57 5289 4480 4647 -225 589 176 A C ATOM 3426 CD1 LEU B 57 0.965 6.945 67.741 1.00 36.94 A C ANISOU 3426 CD1 LEU B 57 5166 4190 4676 -225 380 165 A C ATOM 3427 CD2 LEU B 57 2.714 6.038 66.144 1.00 38.07 A C ANISOU 3427 CD2 LEU B 57 5090 4660 4716 -186 432 -198 A C ATOM 3428 N VAL B 58 4.114 2.364 67.584 1.00 35.53 A N ANISOU 3428 N VAL B 58 4935 4285 4278 -173 346 48 A N ATOM 3429 CA VAL B 58 5.188 1.869 68.439 1.00 35.59 A C ANISOU 3429 CA VAL B 58 4927 4365 4228 -75 315 -63 A C ATOM 3430 C VAL B 58 5.920 3.019 69.109 1.00 35.12 A C ANISOU 3430 C VAL B 58 4886 4344 4112 -1 317 -139 A C ATOM 3431 O VAL B 58 6.493 3.867 68.431 1.00 36.00 A O ANISOU 3431 O VAL B 58 5091 4311 4276 42 194 -204 A O ATOM 3432 CB VAL B 58 6.185 1.040 67.627 1.00 36.16 A C ANISOU 3432 CB VAL B 58 4895 4402 4440 -118 233 1 A C ATOM 3433 CG1 VAL B 58 7.378 0.613 68.494 1.00 38.43 A C ANISOU 3433 CG1 VAL B 58 5308 4646 4647 -93 205 -208 A C ATOM 3434 CG2 VAL B 58 5.470 -0.152 67.011 1.00 37.94 A C ANISOU 3434 CG2 VAL B 58 5126 4545 4742 -179 207 158 A C ATOM 3435 N THR B 59 5.914 3.030 70.440 1.00 34.64 A N ANISOU 3435 N THR B 59 4790 4257 4114 -22 268 -363 A N ATOM 3436 CA THR B 59 6.603 4.054 71.217 1.00 32.86 A C ANISOU 3436 CA THR B 59 4597 3980 3906 -2 353 -449 A C ATOM 3437 C THR B 59 7.060 3.304 72.480 1.00 32.95 A C ANISOU 3437 C THR B 59 4523 3976 4019 -20 300 -512 A C ATOM 3438 O THR B 59 6.439 2.290 72.830 1.00 32.79 A O ANISOU 3438 O THR B 59 4559 4019 3879 42 328 -667 A O ATOM 3439 CB THR B 59 5.654 5.268 71.533 1.00 33.97 A C ANISOU 3439 CB THR B 59 4662 4111 4132 55 379 -372 A C ATOM 3440 CG2 THR B 59 4.576 4.877 72.584 1.00 34.53 A C ANISOU 3440 CG2 THR B 59 4893 3997 4230 3 594 -402 A C ATOM 3441 OG1 THR B 59 6.407 6.408 71.998 1.00 33.30 A O ANISOU 3441 OG1 THR B 59 4776 3708 4166 56 673 -803 A O ATOM 3442 N PRO B 60 8.164 3.741 73.115 1.00 31.95 A N ANISOU 3442 N PRO B 60 4408 3833 3897 -27 335 -531 A N ATOM 3443 CA PRO B 60 8.640 3.035 74.315 1.00 31.80 A C ANISOU 3443 CA PRO B 60 4357 3880 3844 -88 300 -471 A C ATOM 3444 C PRO B 60 7.620 2.935 75.446 1.00 32.00 A C ANISOU 3444 C PRO B 60 4386 3828 3943 -83 339 -574 A C ATOM 3445 O PRO B 60 6.921 3.917 75.715 1.00 31.85 A O ANISOU 3445 O PRO B 60 4343 3901 3855 -31 626 -517 A O ATOM 3446 CB PRO B 60 9.852 3.871 74.742 1.00 31.96 A C ANISOU 3446 CB PRO B 60 4381 3755 4005 -22 325 -635 A C ATOM 3447 CG PRO B 60 10.414 4.425 73.412 1.00 32.83 A C ANISOU 3447 CG PRO B 60 4356 4054 4062 33 361 -474 A C ATOM 3448 CD PRO B 60 9.123 4.783 72.671 1.00 32.89 A C ANISOU 3448 CD PRO B 60 4497 3936 4061 -2 218 -621 A C ATOM 3449 N LEU B 61 7.520 1.747 76.072 1.00 32.95 A N ANISOU 3449 N LEU B 61 4516 4028 3974 -26 423 -467 A N ATOM 3450 CA LEU B 61 6.666 1.534 77.232 1.00 32.96 A C ANISOU 3450 CA LEU B 61 4467 3949 4107 -64 308 -513 A C ATOM 3451 C LEU B 61 7.559 1.247 78.446 1.00 32.10 A C ANISOU 3451 C LEU B 61 4379 3810 4004 -175 289 -570 A C ATOM 3452 O LEU B 61 8.689 0.745 78.278 1.00 33.44 A O ANISOU 3452 O LEU B 61 4643 3898 4164 -208 383 -468 A O ATOM 3453 CB LEU B 61 5.713 0.341 76.959 1.00 33.12 A C ANISOU 3453 CB LEU B 61 4513 3871 4197 -94 256 -449 A C ATOM 3454 CG LEU B 61 4.800 0.461 75.725 1.00 37.05 A C ANISOU 3454 CG LEU B 61 4595 4428 5054 -60 50 -300 A C ATOM 3455 CD1 LEU B 61 3.725 -0.627 75.690 1.00 40.50 A C ANISOU 3455 CD1 LEU B 61 5216 4360 5813 -39 -153 -286 A C ATOM 3456 CD2 LEU B 61 4.152 1.837 75.636 1.00 37.39 A C ANISOU 3456 CD2 LEU B 61 4499 4405 5299 -135 83 -262 A C ATOM 3457 N PRO B 62 7.050 1.478 79.680 1.00 30.98 A N ANISOU 3457 N PRO B 62 4327 3636 3808 -249 220 -658 A N ATOM 3458 CA PRO B 62 5.722 2.001 80.009 1.00 30.29 A C ANISOU 3458 CA PRO B 62 4277 3602 3628 -183 312 -707 A C ATOM 3459 C PRO B 62 5.643 3.476 79.635 1.00 29.30 A C ANISOU 3459 C PRO B 62 4118 3478 3535 -167 292 -635 A C ATOM 3460 O PRO B 62 6.690 4.125 79.561 1.00 31.03 A O ANISOU 3460 O PRO B 62 4181 3771 3837 -249 229 -592 A O ATOM 3461 CB PRO B 62 5.654 1.817 81.537 1.00 30.93 A C ANISOU 3461 CB PRO B 62 4278 3888 3582 -129 309 -635 A C ATOM 3462 CG PRO B 62 7.048 1.908 81.979 1.00 31.74 A C ANISOU 3462 CG PRO B 62 4507 3720 3832 -209 104 -676 A C ATOM 3463 CD PRO B 62 7.819 1.180 80.917 1.00 31.55 A C ANISOU 3463 CD PRO B 62 4397 3722 3867 -245 216 -674 A C ATOM 3464 N VAL B 63 4.433 4.005 79.465 1.00 28.94 A N ANISOU 3464 N VAL B 63 4043 3471 3480 -2 380 -613 A N ATOM 3465 CA VAL B 63 4.261 5.359 78.926 1.00 27.33 A C ANISOU 3465 CA VAL B 63 3833 3312 3240 -90 393 -474 A C ATOM 3466 C VAL B 63 3.047 6.058 79.527 1.00 27.93 A C ANISOU 3466 C VAL B 63 3857 3409 3345 -12 417 -442 A C ATOM 3467 O VAL B 63 2.047 5.394 79.907 1.00 26.91 A O ANISOU 3467 O VAL B 63 3440 3347 3437 -134 462 -571 A O ATOM 3468 CB VAL B 63 4.101 5.317 77.374 1.00 28.88 A C ANISOU 3468 CB VAL B 63 4038 3506 3427 11 383 -522 A C ATOM 3469 CG1 VAL B 63 2.803 4.671 76.957 1.00 27.89 A C ANISOU 3469 CG1 VAL B 63 3892 3435 3267 56 526 -353 A C ATOM 3470 CG2 VAL B 63 4.232 6.714 76.732 1.00 27.67 A C ANISOU 3470 CG2 VAL B 63 4129 3155 3226 -22 243 -572 A C ATOM 3471 N ILE B 64 3.178 7.376 79.657 1.00 26.73 A N ANISOU 3471 N ILE B 64 3757 3336 3062 124 397 -318 A N ATOM 3472 CA ILE B 64 2.017 8.261 79.882 1.00 26.19 A C ANISOU 3472 CA ILE B 64 3868 3203 2876 80 130 -312 A C ATOM 3473 C ILE B 64 1.607 8.834 78.515 1.00 26.57 A C ANISOU 3473 C ILE B 64 3894 3230 2971 114 117 -246 A C ATOM 3474 O ILE B 64 2.335 9.686 77.953 1.00 25.71 A O ANISOU 3474 O ILE B 64 3826 3083 2858 373 -10 -290 A O ATOM 3475 CB ILE B 64 2.309 9.375 80.937 1.00 26.16 A C ANISOU 3475 CB ILE B 64 3840 3305 2793 114 122 -383 A C ATOM 3476 CG1 ILE B 64 2.566 8.749 82.318 1.00 29.06 A C ANISOU 3476 CG1 ILE B 64 4278 3821 2942 81 -225 -214 A C ATOM 3477 CG2 ILE B 64 1.130 10.328 81.052 1.00 27.65 A C ANISOU 3477 CG2 ILE B 64 4238 3448 2817 -30 230 -700 A C ATOM 3478 CD1 ILE B 64 2.821 9.759 83.391 1.00 30.19 A C ANISOU 3478 CD1 ILE B 64 4221 3967 3282 435 -197 -117 A C ATOM 3479 N ALA B 65 0.507 8.318 77.962 1.00 25.56 A N ANISOU 3479 N ALA B 65 3732 3322 2658 16 73 -211 A N ATOM 3480 CA ALA B 65 -0.006 8.791 76.660 1.00 25.90 A C ANISOU 3480 CA ALA B 65 3707 3272 2858 119 -14 -290 A C ATOM 3481 C ALA B 65 -0.823 10.070 76.798 1.00 25.89 A C ANISOU 3481 C ALA B 65 3592 3472 2773 105 145 -231 A C ATOM 3482 O ALA B 65 -0.716 10.777 77.830 1.00 26.33 A O ANISOU 3482 O ALA B 65 3786 3463 2752 45 113 -254 A O ATOM 3483 CB ALA B 65 -0.765 7.704 75.920 1.00 26.40 A C ANISOU 3483 CB ALA B 65 3633 3402 2994 197 14 -208 A C ATOM 3484 N GLY B 66 -1.599 10.398 75.761 1.00 24.51 A N ANISOU 3484 N GLY B 66 3322 3355 2635 133 248 -343 A N ATOM 3485 CA GLY B 66 -2.339 11.653 75.749 1.00 24.75 A C ANISOU 3485 CA GLY B 66 3497 3247 2659 231 235 -271 A C ATOM 3486 C GLY B 66 -1.538 12.724 75.025 1.00 24.64 A C ANISOU 3486 C GLY B 66 3370 3268 2724 272 184 -266 A C ATOM 3487 O GLY B 66 -0.376 13.002 75.356 1.00 26.35 A O ANISOU 3487 O GLY B 66 3464 3448 3100 226 101 -379 A O ATOM 3488 N HIS B 67 -2.172 13.351 74.049 1.00 24.82 A N ANISOU 3488 N HIS B 67 3382 3242 2806 256 142 -410 A N ATOM 3489 CA HIS B 67 -1.535 14.383 73.234 1.00 25.22 A C ANISOU 3489 CA HIS B 67 3662 3119 2798 279 251 -312 A C ATOM 3490 C HIS B 67 -2.444 15.558 72.851 1.00 26.30 A C ANISOU 3490 C HIS B 67 3859 3130 3001 271 257 -306 A C ATOM 3491 O HIS B 67 -1.954 16.538 72.257 1.00 29.31 A O ANISOU 3491 O HIS B 67 4275 3303 3555 229 290 -607 A O ATOM 3492 CB HIS B 67 -0.890 13.753 71.984 1.00 24.91 A C ANISOU 3492 CB HIS B 67 3634 3023 2805 246 174 -192 A C ATOM 3493 CG HIS B 67 -1.879 13.120 71.052 1.00 25.00 A C ANISOU 3493 CG HIS B 67 3629 3160 2707 422 232 -252 A C ATOM 3494 CD2 HIS B 67 -2.374 13.542 69.862 1.00 25.82 A C ANISOU 3494 CD2 HIS B 67 3757 2937 3112 334 382 -661 A C ATOM 3495 ND1 HIS B 67 -2.462 11.892 71.297 1.00 26.13 A N ANISOU 3495 ND1 HIS B 67 3453 3300 3172 81 279 -127 A N ATOM 3496 CE1 HIS B 67 -3.283 11.603 70.304 1.00 26.12 A C ANISOU 3496 CE1 HIS B 67 3657 3304 2963 355 423 -252 A C ATOM 3497 NE2 HIS B 67 -3.230 12.577 69.409 1.00 26.12 A N ANISOU 3497 NE2 HIS B 67 3680 3378 2867 -11 62 -379 A N ATOM 3498 N GLU B 68 -3.720 15.499 73.213 1.00 26.44 A N ANISOU 3498 N GLU B 68 4104 3025 2915 220 193 -126 A N ATOM 3499 CA GLU B 68 -4.721 16.484 72.827 1.00 26.42 A C ANISOU 3499 CA GLU B 68 4209 3136 2692 136 181 -275 A C ATOM 3500 C GLU B 68 -5.259 17.070 74.120 1.00 27.04 A C ANISOU 3500 C GLU B 68 4274 3220 2779 48 178 -140 A C ATOM 3501 O GLU B 68 -5.999 16.393 74.838 1.00 27.45 A O ANISOU 3501 O GLU B 68 4392 3192 2843 -20 332 -110 A O ATOM 3502 CB GLU B 68 -5.859 15.803 72.062 1.00 26.99 A C ANISOU 3502 CB GLU B 68 4165 3173 2914 71 39 -228 A C ATOM 3503 CG GLU B 68 -7.034 16.725 71.663 1.00 27.65 A C ANISOU 3503 CG GLU B 68 4206 3025 3275 204 29 -688 A C ATOM 3504 CD GLU B 68 -8.173 15.998 70.953 1.00 29.74 A C ANISOU 3504 CD GLU B 68 4546 3539 3211 336 154 -345 A C ATOM 3505 OE1 GLU B 68 -9.195 15.712 71.612 1.00 33.75 A O ANISOU 3505 OE1 GLU B 68 4647 4260 3914 388 532 -327 A O ATOM 3506 OE2 GLU B 68 -8.089 15.715 69.738 1.00 34.72 A O1- ANISOU 3506 OE2 GLU B 68 5061 4500 3630 691 406 -447 A O1- ATOM 3507 N ALA B 69 -4.787 18.254 74.481 1.00 25.06 A N ANISOU 3507 N ALA B 69 4304 2879 2336 -113 103 -209 A N ATOM 3508 CA ALA B 69 -5.111 18.766 75.818 1.00 26.10 A C ANISOU 3508 CA ALA B 69 4258 3174 2482 -122 119 -144 A C ATOM 3509 C ALA B 69 -4.933 20.251 75.975 1.00 27.26 A C ANISOU 3509 C ALA B 69 4391 3323 2641 -4 202 -80 A C ATOM 3510 O ALA B 69 -4.370 20.936 75.111 1.00 27.71 A O ANISOU 3510 O ALA B 69 4561 3264 2701 -10 317 -60 A O ATOM 3511 CB ALA B 69 -4.247 18.003 76.901 1.00 26.70 A C ANISOU 3511 CB ALA B 69 4367 3176 2601 -24 -28 -195 A C ATOM 3512 N ALA B 70 -5.409 20.748 77.116 1.00 28.18 A N ANISOU 3512 N ALA B 70 4511 3356 2840 -23 267 84 A N ATOM 3513 CA ALA B 70 -5.183 22.100 77.523 1.00 29.34 A C ANISOU 3513 CA ALA B 70 4660 3550 2935 4 126 192 A C ATOM 3514 C ALA B 70 -4.993 22.160 79.030 1.00 29.72 A C ANISOU 3514 C ALA B 70 4760 3581 2951 69 226 226 A C ATOM 3515 O ALA B 70 -5.549 21.355 79.786 1.00 28.79 A O ANISOU 3515 O ALA B 70 4757 3459 2722 119 176 241 A O ATOM 3516 CB ALA B 70 -6.312 22.985 77.074 1.00 29.60 A C ANISOU 3516 CB ALA B 70 4575 3426 3243 -60 223 322 A C ATOM 3517 N GLY B 71 -4.196 23.122 79.460 1.00 29.54 A N ANISOU 3517 N GLY B 71 4748 3610 2865 46 115 294 A N ATOM 3518 CA GLY B 71 -3.936 23.257 80.890 1.00 30.28 A C ANISOU 3518 CA GLY B 71 4898 3565 3041 81 112 294 A C ATOM 3519 C GLY B 71 -3.456 24.644 81.239 1.00 29.74 A C ANISOU 3519 C GLY B 71 4798 3375 3124 18 126 268 A C ATOM 3520 O GLY B 71 -3.509 25.551 80.412 1.00 28.95 A O ANISOU 3520 O GLY B 71 4767 3174 3056 -38 93 268 A O ATOM 3521 N ILE B 72 -2.928 24.763 82.451 1.00 29.59 A N ANISOU 3521 N ILE B 72 4720 3347 3174 117 23 225 A N ATOM 3522 CA ILE B 72 -2.394 26.023 82.977 1.00 29.32 A C ANISOU 3522 CA ILE B 72 4660 3268 3209 163 94 348 A C ATOM 3523 C ILE B 72 -0.968 25.826 83.435 1.00 29.75 A C ANISOU 3523 C ILE B 72 4800 3367 3138 193 72 212 A C ATOM 3524 O ILE B 72 -0.675 24.835 84.112 1.00 31.83 A O ANISOU 3524 O ILE B 72 4996 3709 3388 189 -57 115 A O ATOM 3525 CB ILE B 72 -3.256 26.567 84.162 1.00 30.11 A C ANISOU 3525 CB ILE B 72 4518 3462 3460 77 74 441 A C ATOM 3526 CG1 ILE B 72 -4.646 27.000 83.707 1.00 33.23 A C ANISOU 3526 CG1 ILE B 72 4871 3641 4113 89 -88 132 A C ATOM 3527 CG2 ILE B 72 -2.542 27.780 84.788 1.00 30.93 A C ANISOU 3527 CG2 ILE B 72 4691 2995 4065 228 136 433 A C ATOM 3528 CD1 ILE B 72 -4.758 28.499 83.323 1.00 38.35 A C ANISOU 3528 CD1 ILE B 72 5357 3779 5434 -101 -141 218 A C ATOM 3529 N VAL B 73 -0.070 26.764 83.082 1.00 29.55 A N ANISOU 3529 N VAL B 73 4877 3374 2974 271 70 184 A N ATOM 3530 CA VAL B 73 1.337 26.670 83.458 1.00 30.07 A C ANISOU 3530 CA VAL B 73 4907 3506 3013 275 75 77 A C ATOM 3531 C VAL B 73 1.538 26.811 84.985 1.00 31.48 A C ANISOU 3531 C VAL B 73 5087 3708 3165 252 113 123 A C ATOM 3532 O VAL B 73 1.138 27.808 85.597 1.00 31.91 A O ANISOU 3532 O VAL B 73 5262 3725 3136 290 160 172 A O ATOM 3533 CB VAL B 73 2.220 27.704 82.700 1.00 30.49 A C ANISOU 3533 CB VAL B 73 4923 3504 3155 282 57 66 A C ATOM 3534 CG1 VAL B 73 3.673 27.618 83.146 1.00 31.39 A C ANISOU 3534 CG1 VAL B 73 4874 3588 3462 211 42 10 A C ATOM 3535 CG2 VAL B 73 2.143 27.447 81.221 1.00 29.89 A C ANISOU 3535 CG2 VAL B 73 4925 3490 2940 261 -22 114 A C ATOM 3536 N GLU B 74 2.123 25.768 85.560 1.00 31.64 A N ANISOU 3536 N GLU B 74 5085 3841 3093 194 -17 75 A N ATOM 3537 CA GLU B 74 2.445 25.722 86.968 1.00 32.13 A C ANISOU 3537 CA GLU B 74 5178 3936 3094 195 -70 162 A C ATOM 3538 C GLU B 74 3.783 26.391 87.234 1.00 32.99 A C ANISOU 3538 C GLU B 74 5212 4068 3252 250 39 193 A C ATOM 3539 O GLU B 74 3.893 27.201 88.167 1.00 34.69 A O ANISOU 3539 O GLU B 74 5494 4127 3559 443 53 297 A O ATOM 3540 CB GLU B 74 2.417 24.269 87.492 1.00 31.05 A C ANISOU 3540 CB GLU B 74 5020 3806 2971 198 -200 191 A C ATOM 3541 CG GLU B 74 2.927 24.091 88.944 1.00 33.80 A C ANISOU 3541 CG GLU B 74 5284 4172 3385 291 -385 298 A C ATOM 3542 CD GLU B 74 4.436 23.966 89.042 1.00 34.76 A C ANISOU 3542 CD GLU B 74 5179 4542 3485 24 -248 509 A C ATOM 3543 OE1 GLU B 74 4.996 24.209 90.152 1.00 37.40 A O ANISOU 3543 OE1 GLU B 74 5428 5015 3766 338 -558 450 A O ATOM 3544 OE2 GLU B 74 5.082 23.612 88.035 1.00 36.45 A O1- ANISOU 3544 OE2 GLU B 74 5476 5016 3356 164 -317 409 A O1- ATOM 3545 N SER B 75 4.806 26.057 86.442 1.00 34.22 A N ANISOU 3545 N SER B 75 5338 4291 3371 287 -2 109 A N ATOM 3546 CA SER B 75 6.096 26.710 86.569 1.00 34.39 A C ANISOU 3546 CA SER B 75 5183 4521 3361 303 -41 159 A C ATOM 3547 C SER B 75 6.906 26.604 85.284 1.00 33.95 A C ANISOU 3547 C SER B 75 5198 4369 3330 397 -37 178 A C ATOM 3548 O SER B 75 6.613 25.760 84.416 1.00 33.14 A O ANISOU 3548 O SER B 75 5138 4515 2937 478 -202 402 A O ATOM 3549 CB SER B 75 6.888 26.135 87.756 1.00 35.47 A C ANISOU 3549 CB SER B 75 5307 4576 3593 303 -90 81 A C ATOM 3550 OG SER B 75 7.382 24.827 87.477 1.00 36.55 A O ANISOU 3550 OG SER B 75 5398 4767 3722 319 -126 163 A O ATOM 3551 N ILE B 76 7.904 27.472 85.147 1.00 34.45 A N ANISOU 3551 N ILE B 76 5162 4487 3439 392 -81 167 A N ATOM 3552 CA ILE B 76 8.767 27.444 83.954 1.00 34.22 A C ANISOU 3552 CA ILE B 76 5151 4208 3640 450 -46 16 A C ATOM 3553 C ILE B 76 10.217 27.226 84.361 1.00 33.72 A C ANISOU 3553 C ILE B 76 5074 4196 3540 434 -79 21 A C ATOM 3554 O ILE B 76 10.676 27.704 85.432 1.00 33.80 A O ANISOU 3554 O ILE B 76 5202 4145 3495 520 -146 55 A O ATOM 3555 CB ILE B 76 8.606 28.735 83.065 1.00 34.38 A C ANISOU 3555 CB ILE B 76 5100 4334 3626 413 -235 -11 A C ATOM 3556 CG1 ILE B 76 8.874 29.997 83.906 1.00 34.20 A C ANISOU 3556 CG1 ILE B 76 5184 4220 3588 439 8 16 A C ATOM 3557 CG2 ILE B 76 7.202 28.779 82.418 1.00 32.62 A C ANISOU 3557 CG2 ILE B 76 4680 4175 3537 336 -189 -215 A C ATOM 3558 CD1 ILE B 76 9.082 31.290 83.074 1.00 35.14 A C ANISOU 3558 CD1 ILE B 76 5195 4241 3913 514 -43 48 A C ATOM 3559 N GLY B 77 10.945 26.491 83.530 1.00 33.65 A N ANISOU 3559 N GLY B 77 5090 4110 3586 421 -21 -85 A N ATOM 3560 CA GLY B 77 12.385 26.338 83.727 1.00 35.40 A C ANISOU 3560 CA GLY B 77 5158 4427 3863 410 -34 89 A C ATOM 3561 C GLY B 77 13.145 27.582 83.287 1.00 36.78 A C ANISOU 3561 C GLY B 77 5236 4575 4163 396 -54 6 A C ATOM 3562 O GLY B 77 12.548 28.510 82.735 1.00 36.85 A O ANISOU 3562 O GLY B 77 5155 4655 4189 425 -237 127 A O ATOM 3563 N GLU B 78 14.457 27.579 83.534 1.00 38.07 A N ANISOU 3563 N GLU B 78 5263 4773 4426 516 -37 -23 A N ATOM 3564 CA GLU B 78 15.361 28.667 83.161 1.00 40.01 A C ANISOU 3564 CA GLU B 78 5468 4979 4753 459 -22 -59 A C ATOM 3565 C GLU B 78 15.249 28.977 81.678 1.00 39.32 A C ANISOU 3565 C GLU B 78 5409 4938 4591 548 18 -39 A C ATOM 3566 O GLU B 78 15.175 28.053 80.850 1.00 39.29 A O ANISOU 3566 O GLU B 78 5490 4941 4496 578 107 -28 A O ATOM 3567 CB GLU B 78 16.817 28.285 83.451 1.00 39.70 A C ANISOU 3567 CB GLU B 78 5334 4951 4795 496 1 -101 A C ATOM 3568 CG GLU B 78 17.173 28.085 84.895 1.00 42.33 A C ANISOU 3568 CG GLU B 78 5552 5383 5145 423 14 -112 A C ATOM 3569 CD GLU B 78 18.667 27.905 85.113 1.00 42.88 A C ANISOU 3569 CD GLU B 78 5713 5339 5239 243 -71 -116 A C ATOM 3570 OE1 GLU B 78 19.067 27.716 86.278 1.00 48.75 A O ANISOU 3570 OE1 GLU B 78 6602 6144 5776 19 -332 -260 A O ATOM 3571 OE2 GLU B 78 19.437 27.949 84.129 1.00 44.88 A O1- ANISOU 3571 OE2 GLU B 78 5857 5310 5882 228 184 -529 A O1- ATOM 3572 N GLY B 79 15.221 30.270 81.355 1.00 39.68 A N ANISOU 3572 N GLY B 79 5471 4994 4610 556 -109 1 A N ATOM 3573 CA GLY B 79 15.295 30.744 79.964 1.00 38.93 A C ANISOU 3573 CA GLY B 79 5318 4897 4576 631 -32 -40 A C ATOM 3574 C GLY B 79 14.025 30.648 79.128 1.00 39.05 A C ANISOU 3574 C GLY B 79 5421 4913 4503 703 -72 47 A C ATOM 3575 O GLY B 79 14.035 30.982 77.950 1.00 38.85 A O ANISOU 3575 O GLY B 79 5445 4776 4538 829 -196 -15 A O ATOM 3576 N VAL B 80 12.925 30.228 79.745 1.00 38.06 A N ANISOU 3576 N VAL B 80 5268 4789 4403 707 -29 41 A N ATOM 3577 CA VAL B 80 11.617 30.181 79.071 1.00 38.01 A C ANISOU 3577 CA VAL B 80 5336 4696 4407 532 7 104 A C ATOM 3578 C VAL B 80 11.063 31.590 78.920 1.00 38.30 A C ANISOU 3578 C VAL B 80 5439 4701 4412 518 62 73 A C ATOM 3579 O VAL B 80 11.018 32.356 79.912 1.00 37.92 A O ANISOU 3579 O VAL B 80 5637 4405 4365 612 115 214 A O ATOM 3580 CB VAL B 80 10.609 29.254 79.839 1.00 37.13 A C ANISOU 3580 CB VAL B 80 5152 4696 4259 516 104 17 A C ATOM 3581 CG1 VAL B 80 9.187 29.378 79.288 1.00 37.84 A C ANISOU 3581 CG1 VAL B 80 5219 4608 4549 429 -133 204 A C ATOM 3582 CG2 VAL B 80 11.020 27.791 79.736 1.00 36.96 A C ANISOU 3582 CG2 VAL B 80 5255 4846 3941 425 -70 139 A C ATOM 3583 N THR B 81 10.702 31.946 77.682 1.00 38.24 A N ANISOU 3583 N THR B 81 5457 4666 4406 444 141 38 A N ATOM 3584 CA THR B 81 10.194 33.279 77.372 1.00 37.77 A C ANISOU 3584 CA THR B 81 5361 4598 4390 388 159 -21 A C ATOM 3585 C THR B 81 8.786 33.347 76.808 1.00 38.08 A C ANISOU 3585 C THR B 81 5489 4591 4386 271 113 53 A C ATOM 3586 O THR B 81 8.199 34.424 76.803 1.00 40.05 A O ANISOU 3586 O THR B 81 5725 4771 4719 193 29 130 A O ATOM 3587 CB THR B 81 11.096 33.999 76.361 1.00 38.00 A C ANISOU 3587 CB THR B 81 5365 4569 4502 408 140 -100 A C ATOM 3588 CG2 THR B 81 12.564 33.924 76.795 1.00 39.71 A C ANISOU 3588 CG2 THR B 81 5289 4731 5065 516 198 -301 A C ATOM 3589 OG1 THR B 81 10.932 33.396 75.075 1.00 36.40 A O ANISOU 3589 OG1 THR B 81 5033 4282 4514 630 190 -304 A O ATOM 3590 N THR B 82 8.244 32.228 76.313 1.00 37.64 A N ANISOU 3590 N THR B 82 5432 4580 4288 204 45 90 A N ATOM 3591 CA THR B 82 7.012 32.283 75.534 1.00 37.23 A C ANISOU 3591 CA THR B 82 5487 4448 4209 185 23 156 A C ATOM 3592 C THR B 82 5.771 32.020 76.348 1.00 36.47 A C ANISOU 3592 C THR B 82 5444 4332 4080 175 27 106 A C ATOM 3593 O THR B 82 4.641 32.252 75.862 1.00 36.19 A O ANISOU 3593 O THR B 82 5433 4141 4176 158 164 -88 A O ATOM 3594 CB THR B 82 7.034 31.292 74.336 1.00 37.19 A C ANISOU 3594 CB THR B 82 5492 4519 4116 198 30 222 A C ATOM 3595 CG2 THR B 82 8.118 31.676 73.301 1.00 37.00 A C ANISOU 3595 CG2 THR B 82 5443 4400 4215 248 -2 88 A C ATOM 3596 OG1 THR B 82 7.254 29.956 74.809 1.00 37.07 A O ANISOU 3596 OG1 THR B 82 5499 4524 4063 21 -144 356 A O ATOM 3597 N VAL B 83 5.969 31.514 77.568 1.00 36.54 A N ANISOU 3597 N VAL B 83 5548 4235 4098 204 92 68 A N ATOM 3598 CA VAL B 83 4.877 31.292 78.519 1.00 36.47 A C ANISOU 3598 CA VAL B 83 5514 4375 3964 148 49 158 A C ATOM 3599 C VAL B 83 5.335 31.630 79.940 1.00 36.75 A C ANISOU 3599 C VAL B 83 5562 4408 3993 148 94 123 A C ATOM 3600 O VAL B 83 6.529 31.676 80.238 1.00 36.27 A O ANISOU 3600 O VAL B 83 5638 4357 3783 71 291 157 A O ATOM 3601 CB VAL B 83 4.363 29.822 78.522 1.00 35.86 A C ANISOU 3601 CB VAL B 83 5408 4304 3911 237 -38 145 A C ATOM 3602 CG1 VAL B 83 3.865 29.356 77.108 1.00 35.76 A C ANISOU 3602 CG1 VAL B 83 5457 4325 3803 80 -194 173 A C ATOM 3603 CG2 VAL B 83 5.423 28.844 79.060 1.00 35.79 A C ANISOU 3603 CG2 VAL B 83 5374 4293 3930 211 -62 223 A C ATOM 3604 N ARG B 84 4.358 31.840 80.816 1.00 37.27 A N ANISOU 3604 N ARG B 84 5719 4456 3985 59 125 145 A N ATOM 3605 CA ARG B 84 4.638 32.262 82.185 1.00 38.83 A C ANISOU 3605 CA ARG B 84 5818 4619 4315 166 51 163 A C ATOM 3606 C ARG B 84 3.680 31.511 83.099 1.00 37.39 A C ANISOU 3606 C ARG B 84 5699 4449 4056 181 28 167 A C ATOM 3607 O ARG B 84 2.606 31.098 82.654 1.00 37.67 A O ANISOU 3607 O ARG B 84 5852 4437 4023 234 15 189 A O ATOM 3608 CB ARG B 84 4.453 33.776 82.342 1.00 39.21 A C ANISOU 3608 CB ARG B 84 5754 4696 4446 11 55 205 A C ATOM 3609 CG ARG B 84 5.534 34.651 81.668 1.00 41.11 A C ANISOU 3609 CG ARG B 84 5887 4820 4913 10 211 218 A C ATOM 3610 CD ARG B 84 5.375 36.149 82.030 1.00 42.08 A C ANISOU 3610 CD ARG B 84 6079 4801 5109 139 87 205 A C ATOM 3611 NE ARG B 84 6.413 37.049 81.482 1.00 45.57 A N ANISOU 3611 NE ARG B 84 6279 5352 5682 160 197 -6 A N ATOM 3612 CZ ARG B 84 7.068 37.974 82.195 1.00 47.49 A C ANISOU 3612 CZ ARG B 84 6347 5770 5926 71 92 22 A C ATOM 3613 NH1 ARG B 84 6.811 38.133 83.485 1.00 48.97 A N1+ ANISOU 3613 NH1 ARG B 84 6700 5952 5951 -185 129 157 A N1+ ATOM 3614 NH2 ARG B 84 7.975 38.761 81.623 1.00 49.45 A N ANISOU 3614 NH2 ARG B 84 6402 6142 6245 67 190 -6 A N ATOM 3615 N PRO B 85 4.058 31.327 84.370 1.00 37.30 A N ANISOU 3615 N PRO B 85 5711 4414 4047 211 -25 191 A N ATOM 3616 CA PRO B 85 3.119 30.725 85.318 1.00 36.50 A C ANISOU 3616 CA PRO B 85 5671 4335 3862 221 -38 222 A C ATOM 3617 C PRO B 85 1.750 31.372 85.262 1.00 36.25 A C ANISOU 3617 C PRO B 85 5683 4292 3797 178 -13 266 A C ATOM 3618 O PRO B 85 1.642 32.610 85.197 1.00 37.54 A O ANISOU 3618 O PRO B 85 5899 4395 3968 110 85 259 A O ATOM 3619 CB PRO B 85 3.786 31.009 86.680 1.00 36.17 A C ANISOU 3619 CB PRO B 85 5578 4269 3896 177 -117 316 A C ATOM 3620 CG PRO B 85 5.214 30.896 86.367 1.00 36.23 A C ANISOU 3620 CG PRO B 85 5585 4296 3885 281 -7 281 A C ATOM 3621 CD PRO B 85 5.356 31.607 85.012 1.00 36.52 A C ANISOU 3621 CD PRO B 85 5604 4314 3958 311 -44 153 A C ATOM 3622 N GLY B 86 0.712 30.546 85.279 1.00 35.64 A N ANISOU 3622 N GLY B 86 5672 4155 3712 186 124 226 A N ATOM 3623 CA GLY B 86 -0.673 31.006 85.214 1.00 36.16 A C ANISOU 3623 CA GLY B 86 5593 4217 3926 110 147 234 A C ATOM 3624 C GLY B 86 -1.295 31.143 83.835 1.00 35.78 A C ANISOU 3624 C GLY B 86 5525 4169 3899 87 174 341 A C ATOM 3625 O GLY B 86 -2.520 31.282 83.695 1.00 36.25 A O ANISOU 3625 O GLY B 86 5701 4245 3825 66 240 456 A O ATOM 3626 N ASP B 87 -0.473 31.086 82.795 1.00 36.71 A N ANISOU 3626 N ASP B 87 5553 4303 4089 161 173 145 A N ATOM 3627 CA ASP B 87 -0.979 31.142 81.419 1.00 36.21 A C ANISOU 3627 CA ASP B 87 5491 4149 4117 180 169 240 A C ATOM 3628 C ASP B 87 -1.734 29.885 81.030 1.00 35.52 A C ANISOU 3628 C ASP B 87 5431 4024 4041 101 169 264 A C ATOM 3629 O ASP B 87 -1.352 28.790 81.456 1.00 35.84 A O ANISOU 3629 O ASP B 87 5624 3921 4072 199 127 302 A O ATOM 3630 CB ASP B 87 0.178 31.299 80.446 1.00 36.43 A C ANISOU 3630 CB ASP B 87 5452 4133 4254 84 226 181 A C ATOM 3631 CG ASP B 87 0.743 32.677 80.423 1.00 38.27 A C ANISOU 3631 CG ASP B 87 5555 4403 4583 112 227 203 A C ATOM 3632 OD1 ASP B 87 0.134 33.618 80.996 1.00 40.40 A O ANISOU 3632 OD1 ASP B 87 5908 4445 4995 -4 215 469 A O ATOM 3633 OD2 ASP B 87 1.824 32.800 79.816 1.00 40.88 A O1- ANISOU 3633 OD2 ASP B 87 5814 4713 5005 21 535 26 A O1- ATOM 3634 N LYS B 88 -2.806 30.055 80.259 1.00 34.02 A N ANISOU 3634 N LYS B 88 5259 3831 3836 134 246 364 A N ATOM 3635 CA LYS B 88 -3.487 28.919 79.618 1.00 33.21 A C ANISOU 3635 CA LYS B 88 5160 3849 3609 80 255 270 A C ATOM 3636 C LYS B 88 -2.671 28.481 78.410 1.00 31.61 A C ANISOU 3636 C LYS B 88 5054 3565 3389 61 318 141 A C ATOM 3637 O LYS B 88 -2.109 29.329 77.654 1.00 30.73 A O ANISOU 3637 O LYS B 88 5282 3260 3134 -20 327 2 A O ATOM 3638 CB LYS B 88 -4.912 29.272 79.212 1.00 33.14 A C ANISOU 3638 CB LYS B 88 5075 3843 3671 32 347 339 A C ATOM 3639 CG LYS B 88 -5.865 29.405 80.431 1.00 34.66 A C ANISOU 3639 CG LYS B 88 5104 4355 3710 11 353 234 A C ATOM 3640 CD LYS B 88 -7.285 29.600 80.010 1.00 37.49 A C ANISOU 3640 CD LYS B 88 5185 4414 4645 22 354 151 A C ATOM 3641 CE LYS B 88 -8.179 29.671 81.236 1.00 37.12 A C ANISOU 3641 CE LYS B 88 4996 4547 4559 181 189 173 A C ATOM 3642 NZ LYS B 88 -9.482 30.319 80.896 1.00 37.85 A N1+ ANISOU 3642 NZ LYS B 88 5391 4382 4607 -198 108 92 A N1+ ATOM 3643 N VAL B 89 -2.601 27.159 78.217 1.00 29.69 A N ANISOU 3643 N VAL B 89 4935 3417 2928 62 140 111 A N ATOM 3644 CA VAL B 89 -1.698 26.588 77.202 1.00 29.82 A C ANISOU 3644 CA VAL B 89 4734 3422 3173 90 147 12 A C ATOM 3645 C VAL B 89 -2.237 25.320 76.594 1.00 28.90 A C ANISOU 3645 C VAL B 89 4679 3382 2917 139 177 18 A C ATOM 3646 O VAL B 89 -3.032 24.616 77.221 1.00 28.95 A O ANISOU 3646 O VAL B 89 4790 3227 2981 246 275 164 A O ATOM 3647 CB VAL B 89 -0.237 26.291 77.727 1.00 29.78 A C ANISOU 3647 CB VAL B 89 4730 3333 3251 79 -7 -117 A C ATOM 3648 CG1 VAL B 89 0.541 27.558 78.027 1.00 30.48 A C ANISOU 3648 CG1 VAL B 89 4903 3158 3519 -11 -53 -122 A C ATOM 3649 CG2 VAL B 89 -0.228 25.323 78.946 1.00 31.60 A C ANISOU 3649 CG2 VAL B 89 4942 3849 3213 128 160 -247 A C ATOM 3650 N ILE B 90 -1.759 25.017 75.379 1.00 27.88 A N ANISOU 3650 N ILE B 90 4579 3260 2754 84 161 -38 A N ATOM 3651 CA ILE B 90 -2.066 23.782 74.693 1.00 27.82 A C ANISOU 3651 CA ILE B 90 4439 3413 2719 151 -27 -182 A C ATOM 3652 C ILE B 90 -0.731 23.152 74.278 1.00 27.94 A C ANISOU 3652 C ILE B 90 4444 3444 2726 141 -61 -95 A C ATOM 3653 O ILE B 90 0.079 23.798 73.590 1.00 28.95 A O ANISOU 3653 O ILE B 90 4678 3269 3052 16 53 -256 A O ATOM 3654 CB ILE B 90 -2.944 24.045 73.456 1.00 26.96 A C ANISOU 3654 CB ILE B 90 4343 3303 2598 133 -39 -260 A C ATOM 3655 CG1 ILE B 90 -4.393 24.349 73.894 1.00 27.51 A C ANISOU 3655 CG1 ILE B 90 4262 3362 2826 21 -166 -484 A C ATOM 3656 CG2 ILE B 90 -2.870 22.841 72.511 1.00 27.70 A C ANISOU 3656 CG2 ILE B 90 4578 3291 2652 285 -44 -109 A C ATOM 3657 CD1 ILE B 90 -5.341 24.760 72.734 1.00 28.78 A C ANISOU 3657 CD1 ILE B 90 4421 3574 2941 138 -159 -239 A C ATOM 3658 N PRO B 91 -0.437 21.940 74.784 1.00 27.64 A N ANISOU 3658 N PRO B 91 4405 3328 2768 241 -1 -145 A N ATOM 3659 CA PRO B 91 0.780 21.206 74.382 1.00 27.39 A C ANISOU 3659 CA PRO B 91 4337 3382 2685 204 144 -170 A C ATOM 3660 C PRO B 91 0.715 20.873 72.905 1.00 28.53 A C ANISOU 3660 C PRO B 91 4323 3512 3006 185 96 -79 A C ATOM 3661 O PRO B 91 -0.387 20.636 72.350 1.00 28.42 A O ANISOU 3661 O PRO B 91 4204 3328 3263 333 205 -86 A O ATOM 3662 CB PRO B 91 0.733 19.924 75.257 1.00 28.27 A C ANISOU 3662 CB PRO B 91 4499 3387 2853 229 224 -162 A C ATOM 3663 CG PRO B 91 -0.153 20.316 76.405 1.00 30.46 A C ANISOU 3663 CG PRO B 91 4567 3685 3320 -10 120 -172 A C ATOM 3664 CD PRO B 91 -1.199 21.189 75.806 1.00 28.14 A C ANISOU 3664 CD PRO B 91 4369 3576 2744 316 -169 -293 A C ATOM 3665 N LEU B 92 1.895 20.908 72.274 1.00 27.42 A N ANISOU 3665 N LEU B 92 4171 3541 2703 319 213 -60 A N ATOM 3666 CA LEU B 92 1.990 20.703 70.816 1.00 28.77 A C ANISOU 3666 CA LEU B 92 4325 3582 3023 337 304 -148 A C ATOM 3667 C LEU B 92 2.660 19.359 70.497 1.00 28.32 A C ANISOU 3667 C LEU B 92 4195 3521 3044 395 247 -155 A C ATOM 3668 O LEU B 92 3.879 19.217 70.661 1.00 28.88 A O ANISOU 3668 O LEU B 92 4206 3459 3308 446 161 -245 A O ATOM 3669 CB LEU B 92 2.737 21.893 70.196 1.00 29.16 A C ANISOU 3669 CB LEU B 92 4456 3556 3066 426 215 -35 A C ATOM 3670 CG LEU B 92 2.195 23.281 70.570 1.00 29.88 A C ANISOU 3670 CG LEU B 92 4400 3666 3285 400 342 -36 A C ATOM 3671 CD1 LEU B 92 3.189 24.335 70.034 1.00 32.23 A C ANISOU 3671 CD1 LEU B 92 5019 4066 3160 631 537 -153 A C ATOM 3672 CD2 LEU B 92 0.770 23.572 70.116 1.00 29.97 A C ANISOU 3672 CD2 LEU B 92 4710 3150 3524 133 96 -117 A C ATOM 3673 N PHE B 93 1.884 18.376 70.020 1.00 27.50 A N ANISOU 3673 N PHE B 93 4201 3313 2934 351 220 -94 A N ATOM 3674 CA PHE B 93 2.494 17.065 69.709 1.00 27.69 A C ANISOU 3674 CA PHE B 93 4052 3338 3130 313 112 -132 A C ATOM 3675 C PHE B 93 3.391 17.134 68.480 1.00 27.94 A C ANISOU 3675 C PHE B 93 4146 3338 3132 384 94 -109 A C ATOM 3676 O PHE B 93 4.290 16.320 68.338 1.00 29.51 A O ANISOU 3676 O PHE B 93 4289 3432 3490 394 175 -77 A O ATOM 3677 CB PHE B 93 1.476 15.917 69.601 1.00 26.93 A C ANISOU 3677 CB PHE B 93 3856 3351 3023 371 168 -139 A C ATOM 3678 CG PHE B 93 0.683 15.916 68.328 1.00 28.45 A C ANISOU 3678 CG PHE B 93 4002 3496 3311 312 72 -101 A C ATOM 3679 CD1 PHE B 93 1.182 15.335 67.165 1.00 29.18 A C ANISOU 3679 CD1 PHE B 93 3891 3936 3260 96 -61 -54 A C ATOM 3680 CD2 PHE B 93 -0.602 16.453 68.311 1.00 28.65 A C ANISOU 3680 CD2 PHE B 93 3891 3489 3505 372 -41 -246 A C ATOM 3681 CE1 PHE B 93 0.430 15.367 65.962 1.00 27.65 A C ANISOU 3681 CE1 PHE B 93 3977 3345 3181 397 -231 134 A C ATOM 3682 CE2 PHE B 93 -1.352 16.475 67.156 1.00 28.65 A C ANISOU 3682 CE2 PHE B 93 4056 3533 3295 564 0 35 A C ATOM 3683 CZ PHE B 93 -0.837 15.919 65.977 1.00 26.12 A C ANISOU 3683 CZ PHE B 93 3938 2957 3026 384 -46 53 A C ATOM 3684 N THR B 94 3.158 18.115 67.614 1.00 28.69 A N ANISOU 3684 N THR B 94 4362 3424 3114 489 159 -220 A N ATOM 3685 CA THR B 94 4.115 18.480 66.564 1.00 29.95 A C ANISOU 3685 CA THR B 94 4504 3587 3285 484 161 -275 A C ATOM 3686 C THR B 94 4.732 19.783 67.020 1.00 30.13 A C ANISOU 3686 C THR B 94 4622 3604 3222 467 200 -300 A C ATOM 3687 O THR B 94 4.039 20.791 67.054 1.00 30.36 A O ANISOU 3687 O THR B 94 4736 3478 3321 487 114 -334 A O ATOM 3688 CB THR B 94 3.420 18.675 65.212 1.00 30.62 A C ANISOU 3688 CB THR B 94 4707 3664 3262 541 204 -299 A C ATOM 3689 CG2 THR B 94 4.453 18.892 64.093 1.00 32.14 A C ANISOU 3689 CG2 THR B 94 4875 3589 3746 681 342 -514 A C ATOM 3690 OG1 THR B 94 2.694 17.493 64.893 1.00 30.74 A O ANISOU 3690 OG1 THR B 94 4446 3910 3322 709 271 -370 A O ATOM 3691 N PRO B 95 6.029 19.763 67.382 1.00 30.16 A N ANISOU 3691 N PRO B 95 4729 3590 3140 504 85 -317 A N ATOM 3692 CA PRO B 95 6.712 20.917 67.960 1.00 29.81 A C ANISOU 3692 CA PRO B 95 4660 3545 3118 613 134 -375 A C ATOM 3693 C PRO B 95 6.908 22.005 66.878 1.00 29.71 A C ANISOU 3693 C PRO B 95 4815 3501 2971 598 75 -400 A C ATOM 3694 O PRO B 95 6.714 21.730 65.683 1.00 29.67 A O ANISOU 3694 O PRO B 95 4650 3675 2946 691 81 -308 A O ATOM 3695 CB PRO B 95 8.073 20.357 68.387 1.00 30.40 A C ANISOU 3695 CB PRO B 95 4996 3405 3148 527 70 -567 A C ATOM 3696 CG PRO B 95 8.104 18.966 68.043 1.00 32.18 A C ANISOU 3696 CG PRO B 95 4788 3938 3498 502 95 -129 A C ATOM 3697 CD PRO B 95 6.951 18.634 67.176 1.00 30.79 A C ANISOU 3697 CD PRO B 95 4692 3720 3286 484 31 -216 A C ATOM 3698 N GLN B 96 7.255 23.227 67.280 1.00 28.95 A N ANISOU 3698 N GLN B 96 4703 3380 2916 686 138 -465 A N ATOM 3699 CA GLN B 96 7.698 24.254 66.291 1.00 29.81 A C ANISOU 3699 CA GLN B 96 4888 3507 2928 593 85 -395 A C ATOM 3700 C GLN B 96 8.946 24.893 66.858 1.00 30.97 A C ANISOU 3700 C GLN B 96 4944 3637 3186 621 128 -348 A C ATOM 3701 O GLN B 96 8.881 25.868 67.610 1.00 32.33 A O ANISOU 3701 O GLN B 96 5208 3731 3345 629 -51 -173 A O ATOM 3702 CB GLN B 96 6.613 25.262 65.970 1.00 28.93 A C ANISOU 3702 CB GLN B 96 4739 3445 2808 757 61 -524 A C ATOM 3703 CG GLN B 96 7.100 26.311 64.949 1.00 28.58 A C ANISOU 3703 CG GLN B 96 5154 3105 2599 704 -4 -457 A C ATOM 3704 CD GLN B 96 6.053 27.284 64.518 1.00 30.16 A C ANISOU 3704 CD GLN B 96 5160 3432 2867 487 114 -328 A C ATOM 3705 NE2 GLN B 96 6.451 28.184 63.627 1.00 33.60 A N ANISOU 3705 NE2 GLN B 96 5835 3455 3475 402 186 -668 A N ATOM 3706 OE1 GLN B 96 4.895 27.216 64.912 1.00 33.00 A O ANISOU 3706 OE1 GLN B 96 5715 3452 3370 429 34 -422 A O ATOM 3707 N CYS B 97 10.090 24.291 66.547 1.00 32.46 A N ANISOU 3707 N CYS B 97 4800 4096 3437 650 80 -344 A N ATOM 3708 CA CYS B 97 11.384 24.798 67.031 1.00 33.42 A C ANISOU 3708 CA CYS B 97 5012 4205 3479 776 52 -402 A C ATOM 3709 C CYS B 97 11.767 26.164 66.459 1.00 33.95 A C ANISOU 3709 C CYS B 97 5074 4212 3610 763 60 -344 A C ATOM 3710 O CYS B 97 12.423 26.935 67.128 1.00 34.42 A O ANISOU 3710 O CYS B 97 5283 4245 3548 989 94 -486 A O ATOM 3711 CB CYS B 97 12.495 23.754 66.812 1.00 33.55 A C ANISOU 3711 CB CYS B 97 4840 4381 3525 720 133 -396 A C ATOM 3712 SG CYS B 97 13.227 23.627 65.161 1.00 36.40 A S ANISOU 3712 SG CYS B 97 5345 5040 3444 1119 394 -814 A S ATOM 3713 N GLY B 98 11.346 26.450 65.229 1.00 33.77 A N ANISOU 3713 N GLY B 98 5089 4110 3631 763 44 -377 A N ATOM 3714 CA GLY B 98 11.644 27.723 64.575 1.00 35.20 A C ANISOU 3714 CA GLY B 98 5245 4291 3838 714 37 -371 A C ATOM 3715 C GLY B 98 12.987 27.765 63.881 1.00 36.73 A C ANISOU 3715 C GLY B 98 5370 4427 4156 697 93 -326 A C ATOM 3716 O GLY B 98 13.286 28.755 63.194 1.00 38.46 A O ANISOU 3716 O GLY B 98 5702 4535 4374 742 100 -427 A O ATOM 3717 N LYS B 99 13.798 26.715 64.021 1.00 37.00 A N ANISOU 3717 N LYS B 99 5299 4546 4213 704 109 -226 A N ATOM 3718 CA LYS B 99 15.193 26.766 63.569 1.00 39.05 A C ANISOU 3718 CA LYS B 99 5465 4854 4516 649 219 -229 A C ATOM 3719 C LYS B 99 15.535 25.805 62.430 1.00 38.61 A C ANISOU 3719 C LYS B 99 5353 4905 4412 688 335 -245 A C ATOM 3720 O LYS B 99 16.427 26.080 61.617 1.00 40.23 A O ANISOU 3720 O LYS B 99 5571 5163 4550 779 435 -245 A O ATOM 3721 CB LYS B 99 16.143 26.495 64.743 1.00 39.39 A C ANISOU 3721 CB LYS B 99 5460 4883 4623 665 168 -249 A C ATOM 3722 CG LYS B 99 16.093 27.505 65.898 1.00 41.85 A C ANISOU 3722 CG LYS B 99 5883 5068 4950 500 197 -184 A C ATOM 3723 CD LYS B 99 17.242 27.216 66.846 1.00 46.44 A C ANISOU 3723 CD LYS B 99 6148 5644 5852 236 -73 -94 A C ATOM 3724 CE LYS B 99 17.166 28.001 68.138 1.00 49.29 A C ANISOU 3724 CE LYS B 99 6531 6140 6056 165 65 -56 A C ATOM 3725 NZ LYS B 99 18.112 27.449 69.158 1.00 51.39 A N1+ ANISOU 3725 NZ LYS B 99 6595 6357 6570 141 -10 -216 A N1+ ATOM 3726 N CYS B 100 14.840 24.677 62.364 1.00 37.71 A N ANISOU 3726 N CYS B 100 5304 4784 4237 650 362 -290 A N ATOM 3727 CA CYS B 100 15.173 23.608 61.435 1.00 36.58 A C ANISOU 3727 CA CYS B 100 5091 4687 4118 676 353 -368 A C ATOM 3728 C CYS B 100 14.684 23.972 60.029 1.00 35.61 A C ANISOU 3728 C CYS B 100 5034 4479 4017 585 353 -379 A C ATOM 3729 O CYS B 100 13.843 24.859 59.874 1.00 35.31 A O ANISOU 3729 O CYS B 100 5049 4383 3983 669 362 -579 A O ATOM 3730 CB CYS B 100 14.548 22.284 61.908 1.00 37.43 A C ANISOU 3730 CB CYS B 100 5088 4805 4328 653 271 -463 A C ATOM 3731 SG CYS B 100 12.757 22.078 61.677 1.00 34.82 A S ANISOU 3731 SG CYS B 100 4781 4763 3686 1062 647 -335 A S ATOM 3732 N ARG B 101 15.166 23.254 59.025 1.00 35.61 A N ANISOU 3732 N ARG B 101 5030 4387 4109 527 381 -357 A N ATOM 3733 CA ARG B 101 14.777 23.526 57.634 1.00 35.40 A C ANISOU 3733 CA ARG B 101 5060 4383 4004 506 320 -163 A C ATOM 3734 C ARG B 101 13.280 23.413 57.347 1.00 34.02 A C ANISOU 3734 C ARG B 101 5031 4115 3779 616 306 -204 A C ATOM 3735 O ARG B 101 12.752 24.149 56.510 1.00 34.14 A O ANISOU 3735 O ARG B 101 5048 4246 3675 726 287 -101 A O ATOM 3736 CB ARG B 101 15.601 22.696 56.639 1.00 37.30 A C ANISOU 3736 CB ARG B 101 5219 4548 4405 417 270 -51 A C ATOM 3737 CG ARG B 101 15.581 21.232 56.909 1.00 41.33 A C ANISOU 3737 CG ARG B 101 5823 4966 4914 318 220 -122 A C ATOM 3738 CD ARG B 101 16.031 20.410 55.705 1.00 44.56 A C ANISOU 3738 CD ARG B 101 5967 5550 5412 150 125 232 A C ATOM 3739 NE ARG B 101 15.409 19.094 55.802 1.00 47.21 A N ANISOU 3739 NE ARG B 101 6303 5731 5900 161 106 10 A N ATOM 3740 CZ ARG B 101 15.925 18.059 56.455 1.00 47.66 A C ANISOU 3740 CZ ARG B 101 6189 5972 5946 -89 35 109 A C ATOM 3741 NH1 ARG B 101 17.111 18.167 57.061 1.00 46.95 A N1+ ANISOU 3741 NH1 ARG B 101 5766 6132 5939 20 321 111 A N1+ ATOM 3742 NH2 ARG B 101 15.241 16.915 56.507 1.00 48.34 A N ANISOU 3742 NH2 ARG B 101 6301 6182 5885 -114 402 -93 A N ATOM 3743 N VAL B 102 12.584 22.555 58.111 1.00 32.15 A N ANISOU 3743 N VAL B 102 4787 3810 3615 812 282 -102 A N ATOM 3744 CA VAL B 102 11.144 22.452 57.961 1.00 31.51 A C ANISOU 3744 CA VAL B 102 4852 3650 3468 710 218 -273 A C ATOM 3745 C VAL B 102 10.437 23.670 58.561 1.00 30.34 A C ANISOU 3745 C VAL B 102 4846 3388 3292 797 91 -245 A C ATOM 3746 O VAL B 102 9.521 24.228 57.943 1.00 29.99 A O ANISOU 3746 O VAL B 102 4919 3259 3216 990 78 -359 A O ATOM 3747 CB VAL B 102 10.601 21.187 58.635 1.00 31.01 A C ANISOU 3747 CB VAL B 102 4817 3460 3504 676 197 -257 A C ATOM 3748 CG1 VAL B 102 9.100 21.144 58.524 1.00 31.33 A C ANISOU 3748 CG1 VAL B 102 4957 3663 3282 578 126 -319 A C ATOM 3749 CG2 VAL B 102 11.252 19.920 57.981 1.00 33.21 A C ANISOU 3749 CG2 VAL B 102 5153 3717 3745 543 224 -138 A C ATOM 3750 N CYS B 103 10.840 24.066 59.774 1.00 30.97 A N ANISOU 3750 N CYS B 103 5010 3560 3195 886 130 -370 A N ATOM 3751 CA CYS B 103 10.224 25.230 60.401 1.00 31.02 A C ANISOU 3751 CA CYS B 103 5081 3635 3069 873 83 -282 A C ATOM 3752 C CYS B 103 10.495 26.507 59.595 1.00 32.97 A C ANISOU 3752 C CYS B 103 5257 3851 3419 795 72 -308 A C ATOM 3753 O CYS B 103 9.670 27.431 59.587 1.00 33.76 A O ANISOU 3753 O CYS B 103 5512 3664 3650 792 13 -319 A O ATOM 3754 CB CYS B 103 10.748 25.409 61.828 1.00 30.32 A C ANISOU 3754 CB CYS B 103 4814 3686 3019 1064 -30 -352 A C ATOM 3755 SG CYS B 103 10.012 24.228 62.991 1.00 31.73 A S ANISOU 3755 SG CYS B 103 5252 3840 2963 1153 143 -366 A S ATOM 3756 N LYS B 104 11.643 26.544 58.927 1.00 34.25 A N ANISOU 3756 N LYS B 104 5481 4027 3502 741 185 -283 A N ATOM 3757 CA LYS B 104 12.017 27.696 58.069 1.00 35.29 A C ANISOU 3757 CA LYS B 104 5490 4173 3744 656 119 -339 A C ATOM 3758 C LYS B 104 11.358 27.654 56.689 1.00 35.21 A C ANISOU 3758 C LYS B 104 5559 4227 3590 684 181 -277 A C ATOM 3759 O LYS B 104 11.477 28.614 55.903 1.00 35.93 A O ANISOU 3759 O LYS B 104 5850 3998 3803 744 112 -353 A O ATOM 3760 CB LYS B 104 13.551 27.795 57.938 1.00 34.62 A C ANISOU 3760 CB LYS B 104 5416 4087 3649 726 213 -362 A C ATOM 3761 CG LYS B 104 14.229 28.281 59.229 1.00 38.35 A C ANISOU 3761 CG LYS B 104 5698 4526 4345 607 16 -170 A C ATOM 3762 CD LYS B 104 13.963 29.781 59.464 1.00 42.07 A C ANISOU 3762 CD LYS B 104 6023 4788 5173 368 0 -116 A C ATOM 3763 CE LYS B 104 14.454 30.229 60.839 1.00 44.83 A C ANISOU 3763 CE LYS B 104 6344 5094 5593 473 -126 23 A C ATOM 3764 NZ LYS B 104 15.004 31.634 60.837 1.00 47.19 A N1+ ANISOU 3764 NZ LYS B 104 6599 5184 6148 462 -290 66 A N1+ ATOM 3765 N HIS B 105 10.678 26.560 56.365 1.00 35.45 A N ANISOU 3765 N HIS B 105 5497 4308 3662 589 196 -346 A N ATOM 3766 CA HIS B 105 10.058 26.419 55.031 1.00 34.84 A C ANISOU 3766 CA HIS B 105 5277 4375 3585 546 242 -266 A C ATOM 3767 C HIS B 105 8.626 26.959 55.049 1.00 35.70 A C ANISOU 3767 C HIS B 105 5347 4436 3780 481 280 -293 A C ATOM 3768 O HIS B 105 7.865 26.628 55.958 1.00 34.57 A O ANISOU 3768 O HIS B 105 5149 4389 3595 691 420 -268 A O ATOM 3769 CB HIS B 105 10.077 24.951 54.619 1.00 35.15 A C ANISOU 3769 CB HIS B 105 5282 4472 3600 503 217 -173 A C ATOM 3770 CG HIS B 105 9.735 24.707 53.182 1.00 34.51 A C ANISOU 3770 CG HIS B 105 5033 4436 3641 451 57 -1 A C ATOM 3771 CD2 HIS B 105 10.523 24.360 52.139 1.00 35.04 A C ANISOU 3771 CD2 HIS B 105 5401 4336 3577 537 31 138 A C ATOM 3772 ND1 HIS B 105 8.457 24.814 52.679 1.00 36.31 A N ANISOU 3772 ND1 HIS B 105 5333 4722 3740 393 83 104 A N ATOM 3773 CE1 HIS B 105 8.472 24.537 51.385 1.00 36.35 A C ANISOU 3773 CE1 HIS B 105 5327 4535 3947 531 -32 260 A C ATOM 3774 NE2 HIS B 105 9.713 24.253 51.036 1.00 35.82 A N ANISOU 3774 NE2 HIS B 105 5424 4624 3561 411 -31 246 A N ATOM 3775 N PRO B 106 8.227 27.771 54.043 1.00 36.17 A N ANISOU 3775 N PRO B 106 5408 4354 3981 395 336 -385 A N ATOM 3776 CA PRO B 106 6.846 28.309 54.083 1.00 36.99 A C ANISOU 3776 CA PRO B 106 5456 4454 4142 373 332 -433 A C ATOM 3777 C PRO B 106 5.710 27.272 54.141 1.00 37.70 A C ANISOU 3777 C PRO B 106 5493 4573 4256 325 293 -434 A C ATOM 3778 O PRO B 106 4.638 27.576 54.677 1.00 38.44 A O ANISOU 3778 O PRO B 106 5668 4707 4230 244 345 -426 A O ATOM 3779 CB PRO B 106 6.735 29.169 52.785 1.00 37.47 A C ANISOU 3779 CB PRO B 106 5604 4390 4241 255 259 -385 A C ATOM 3780 CG PRO B 106 7.947 28.899 52.016 1.00 36.61 A C ANISOU 3780 CG PRO B 106 5465 4361 4081 473 340 -490 A C ATOM 3781 CD PRO B 106 8.994 28.293 52.891 1.00 36.30 A C ANISOU 3781 CD PRO B 106 5315 4414 4062 422 356 -328 A C ATOM 3782 N GLU B 107 5.925 26.072 53.612 1.00 37.88 A N ANISOU 3782 N GLU B 107 5556 4569 4267 385 274 -492 A N ATOM 3783 CA GLU B 107 4.833 25.089 53.602 1.00 39.97 A C ANISOU 3783 CA GLU B 107 5753 4728 4705 295 150 -462 A C ATOM 3784 C GLU B 107 5.048 23.864 54.504 1.00 39.15 A C ANISOU 3784 C GLU B 107 5636 4646 4592 362 164 -524 A C ATOM 3785 O GLU B 107 4.152 23.015 54.623 1.00 41.24 A O ANISOU 3785 O GLU B 107 5889 4767 5013 437 206 -548 A O ATOM 3786 CB GLU B 107 4.495 24.666 52.178 1.00 41.18 A C ANISOU 3786 CB GLU B 107 5848 4924 4872 250 62 -332 A C ATOM 3787 CG GLU B 107 3.407 25.529 51.485 1.00 45.95 A C ANISOU 3787 CG GLU B 107 6357 5478 5620 18 -11 -247 A C ATOM 3788 CD GLU B 107 2.007 25.193 51.988 1.00 50.04 A C ANISOU 3788 CD GLU B 107 6598 6199 6214 79 72 -102 A C ATOM 3789 OE1 GLU B 107 1.589 25.738 53.041 1.00 52.92 A O ANISOU 3789 OE1 GLU B 107 7027 6520 6559 36 352 50 A O ATOM 3790 OE2 GLU B 107 1.328 24.370 51.337 1.00 51.19 A O1- ANISOU 3790 OE2 GLU B 107 6967 6243 6236 -34 -84 -177 A O1- ATOM 3791 N GLY B 108 6.205 23.756 55.131 1.00 36.54 A N ANISOU 3791 N GLY B 108 5456 4312 4115 297 220 -538 A N ATOM 3792 CA GLY B 108 6.439 22.607 56.027 1.00 34.53 A C ANISOU 3792 CA GLY B 108 5288 4013 3817 308 225 -453 A C ATOM 3793 C GLY B 108 5.947 22.876 57.436 1.00 33.90 A C ANISOU 3793 C GLY B 108 5204 3940 3734 320 198 -374 A C ATOM 3794 O GLY B 108 5.916 24.019 57.873 1.00 33.85 A O ANISOU 3794 O GLY B 108 5395 3707 3759 519 231 -662 A O ATOM 3795 N ASN B 109 5.573 21.819 58.159 1.00 31.74 A N ANISOU 3795 N ASN B 109 4931 3774 3353 375 211 -292 A N ATOM 3796 CA ASN B 109 5.205 21.973 59.570 1.00 31.39 A C ANISOU 3796 CA ASN B 109 4733 3842 3352 333 202 -187 A C ATOM 3797 C ASN B 109 5.665 20.809 60.424 1.00 30.84 A C ANISOU 3797 C ASN B 109 4719 3723 3273 296 219 -143 A C ATOM 3798 O ASN B 109 5.585 20.876 61.649 1.00 30.75 A O ANISOU 3798 O ASN B 109 4846 3784 3051 376 378 -273 A O ATOM 3799 CB ASN B 109 3.688 22.168 59.760 1.00 31.45 A C ANISOU 3799 CB ASN B 109 4645 3884 3420 307 133 -99 A C ATOM 3800 CG ASN B 109 2.906 20.876 59.580 1.00 31.06 A C ANISOU 3800 CG ASN B 109 4416 4004 3380 363 186 107 A C ATOM 3801 ND2 ASN B 109 1.868 20.663 60.421 1.00 29.22 A N ANISOU 3801 ND2 ASN B 109 4099 4121 2882 556 28 568 A N ATOM 3802 OD1 ASN B 109 3.250 20.056 58.719 1.00 34.13 A O ANISOU 3802 OD1 ASN B 109 4987 4040 3941 254 230 382 A O ATOM 3803 N PHE B 110 6.168 19.755 59.793 1.00 29.92 A N ANISOU 3803 N PHE B 110 4646 3469 3251 400 196 -112 A N ATOM 3804 CA PHE B 110 6.583 18.567 60.539 1.00 29.16 A C ANISOU 3804 CA PHE B 110 4578 3478 3023 299 255 -106 A C ATOM 3805 C PHE B 110 8.013 18.749 61.029 1.00 29.63 A C ANISOU 3805 C PHE B 110 4628 3509 3119 417 296 -128 A C ATOM 3806 O PHE B 110 8.976 18.211 60.462 1.00 29.92 A O ANISOU 3806 O PHE B 110 4556 3564 3246 439 287 -147 A O ATOM 3807 CB PHE B 110 6.410 17.322 59.648 1.00 29.41 A C ANISOU 3807 CB PHE B 110 4593 3349 3232 261 290 37 A C ATOM 3808 CG PHE B 110 6.554 16.008 60.377 1.00 28.46 A C ANISOU 3808 CG PHE B 110 4548 3406 2857 -50 398 77 A C ATOM 3809 CD1 PHE B 110 5.993 15.806 61.631 1.00 30.75 A C ANISOU 3809 CD1 PHE B 110 4665 3757 3261 358 321 -346 A C ATOM 3810 CD2 PHE B 110 7.224 14.932 59.760 1.00 30.04 A C ANISOU 3810 CD2 PHE B 110 4953 3311 3149 -11 338 172 A C ATOM 3811 CE1 PHE B 110 6.145 14.575 62.289 1.00 31.52 A C ANISOU 3811 CE1 PHE B 110 4559 3628 3787 -60 13 -113 A C ATOM 3812 CE2 PHE B 110 7.370 13.694 60.416 1.00 29.67 A C ANISOU 3812 CE2 PHE B 110 4673 3447 3151 112 32 143 A C ATOM 3813 CZ PHE B 110 6.821 13.515 61.665 1.00 30.70 A C ANISOU 3813 CZ PHE B 110 4751 3551 3360 76 65 -63 A C ATOM 3814 N CYS B 111 8.141 19.584 62.059 1.00 29.16 A N ANISOU 3814 N CYS B 111 4620 3671 2787 494 303 -262 A N ATOM 3815 CA CYS B 111 9.421 19.978 62.623 1.00 30.47 A C ANISOU 3815 CA CYS B 111 4691 3831 3055 503 305 -222 A C ATOM 3816 C CYS B 111 10.302 18.767 62.923 1.00 30.12 A C ANISOU 3816 C CYS B 111 4576 3889 2977 477 200 -280 A C ATOM 3817 O CYS B 111 9.798 17.777 63.447 1.00 30.55 A O ANISOU 3817 O CYS B 111 4799 3583 3224 341 110 -414 A O ATOM 3818 CB CYS B 111 9.151 20.802 63.888 1.00 29.73 A C ANISOU 3818 CB CYS B 111 4600 3831 2864 510 314 -161 A C ATOM 3819 SG CYS B 111 10.595 21.101 64.923 1.00 32.26 A S ANISOU 3819 SG CYS B 111 4924 4171 3161 756 372 -354 A S ATOM 3820 N LEU B 112 11.587 18.837 62.561 1.00 31.14 A N ANISOU 3820 N LEU B 112 4588 4063 3179 454 209 -292 A N ATOM 3821 CA LEU B 112 12.559 17.742 62.711 1.00 31.59 A C ANISOU 3821 CA LEU B 112 4532 4154 3315 443 249 -339 A C ATOM 3822 C LEU B 112 12.839 17.319 64.171 1.00 32.00 A C ANISOU 3822 C LEU B 112 4547 4174 3436 354 140 -306 A C ATOM 3823 O LEU B 112 13.406 16.232 64.389 1.00 32.76 A O ANISOU 3823 O LEU B 112 4615 4212 3619 413 152 -227 A O ATOM 3824 CB LEU B 112 13.869 18.011 61.916 1.00 33.50 A C ANISOU 3824 CB LEU B 112 4667 4416 3644 414 245 -274 A C ATOM 3825 CG LEU B 112 13.790 17.985 60.369 1.00 34.87 A C ANISOU 3825 CG LEU B 112 4807 4607 3834 374 245 -248 A C ATOM 3826 CD1 LEU B 112 15.147 18.317 59.750 1.00 37.25 A C ANISOU 3826 CD1 LEU B 112 5166 4667 4318 274 385 -333 A C ATOM 3827 CD2 LEU B 112 13.262 16.662 59.794 1.00 36.74 A C ANISOU 3827 CD2 LEU B 112 5198 4771 3988 306 443 -227 A C ATOM 3828 N LYS B 113 12.420 18.154 65.143 1.00 30.96 A N ANISOU 3828 N LYS B 113 4362 4145 3254 498 55 -335 A N ATOM 3829 CA LYS B 113 12.446 17.810 66.575 1.00 32.09 A C ANISOU 3829 CA LYS B 113 4467 4293 3432 423 84 -283 A C ATOM 3830 C LYS B 113 11.287 16.956 67.054 1.00 31.33 A C ANISOU 3830 C LYS B 113 4349 4222 3332 366 53 -282 A C ATOM 3831 O LYS B 113 11.191 16.631 68.254 1.00 31.87 A O ANISOU 3831 O LYS B 113 4457 4361 3290 468 159 -217 A O ATOM 3832 CB LYS B 113 12.572 19.085 67.431 1.00 31.27 A C ANISOU 3832 CB LYS B 113 4362 4339 3180 429 -35 -193 A C ATOM 3833 CG LYS B 113 13.837 19.888 67.107 1.00 34.51 A C ANISOU 3833 CG LYS B 113 4692 4510 3908 541 317 -404 A C ATOM 3834 CD LYS B 113 15.072 19.096 67.488 1.00 38.83 A C ANISOU 3834 CD LYS B 113 4811 4855 5085 550 140 -145 A C ATOM 3835 CE LYS B 113 16.258 19.997 67.868 1.00 40.94 A C ANISOU 3835 CE LYS B 113 5079 5034 5442 553 -89 -10 A C ATOM 3836 NZ LYS B 113 17.374 19.183 68.485 1.00 43.54 A N1+ ANISOU 3836 NZ LYS B 113 5485 4871 6186 215 180 -66 A N1+ ATOM 3837 N ASN B 114 10.423 16.540 66.137 1.00 30.70 A N ANISOU 3837 N ASN B 114 4334 4142 3187 357 63 -335 A N ATOM 3838 CA ASN B 114 9.269 15.703 66.529 1.00 30.06 A C ANISOU 3838 CA ASN B 114 4342 3976 3101 301 150 -392 A C ATOM 3839 C ASN B 114 9.722 14.349 67.092 1.00 30.64 A C ANISOU 3839 C ASN B 114 4339 4020 3280 245 197 -330 A C ATOM 3840 O ASN B 114 10.822 13.872 66.778 1.00 30.59 A O ANISOU 3840 O ASN B 114 4199 4080 3340 371 256 -449 A O ATOM 3841 CB ASN B 114 8.340 15.469 65.331 1.00 30.50 A C ANISOU 3841 CB ASN B 114 4433 3990 3164 280 138 -337 A C ATOM 3842 CG ASN B 114 8.891 14.441 64.363 1.00 30.00 A C ANISOU 3842 CG ASN B 114 4628 3703 3065 225 177 -318 A C ATOM 3843 ND2 ASN B 114 9.461 14.900 63.235 1.00 30.96 A N ANISOU 3843 ND2 ASN B 114 4807 3738 3217 410 202 -407 A N ATOM 3844 OD1 ASN B 114 8.767 13.240 64.596 1.00 32.05 A O ANISOU 3844 OD1 ASN B 114 4987 3766 3422 269 189 -168 A O ATOM 3845 N ASP B 115 8.871 13.753 67.936 1.00 30.44 A N ANISOU 3845 N ASP B 115 4365 4013 3184 290 282 -407 A N ATOM 3846 CA ASP B 115 9.133 12.419 68.482 1.00 31.68 A C ANISOU 3846 CA ASP B 115 4564 4030 3439 206 328 -369 A C ATOM 3847 C ASP B 115 8.256 11.344 67.839 1.00 32.02 A C ANISOU 3847 C ASP B 115 4636 3958 3572 208 340 -355 A C ATOM 3848 O ASP B 115 7.982 10.287 68.428 1.00 33.23 A O ANISOU 3848 O ASP B 115 5001 3936 3690 149 312 -419 A O ATOM 3849 CB ASP B 115 8.930 12.398 70.014 1.00 31.10 A C ANISOU 3849 CB ASP B 115 4301 4188 3324 272 446 -374 A C ATOM 3850 CG ASP B 115 9.614 11.192 70.680 1.00 32.79 A C ANISOU 3850 CG ASP B 115 4681 4184 3592 312 492 -404 A C ATOM 3851 OD1 ASP B 115 10.758 10.878 70.257 1.00 34.51 A O ANISOU 3851 OD1 ASP B 115 5120 4147 3845 1 456 -411 A O ATOM 3852 OD2 ASP B 115 9.034 10.566 71.635 1.00 32.84 A O1- ANISOU 3852 OD2 ASP B 115 4833 4236 3406 443 657 -282 A O1- ATOM 3853 N LEU B 116 7.754 11.632 66.654 1.00 31.78 A N ANISOU 3853 N LEU B 116 4571 3893 3608 227 214 -318 A N ATOM 3854 CA LEU B 116 6.868 10.731 65.962 1.00 33.12 A C ANISOU 3854 CA LEU B 116 4850 3825 3909 199 204 -285 A C ATOM 3855 C LEU B 116 7.576 9.789 65.013 1.00 35.03 A C ANISOU 3855 C LEU B 116 5207 3952 4149 194 130 -183 A C ATOM 3856 O LEU B 116 7.196 8.630 64.956 1.00 36.16 A O ANISOU 3856 O LEU B 116 5432 3926 4381 322 126 -185 A O ATOM 3857 CB LEU B 116 5.822 11.528 65.189 1.00 32.54 A C ANISOU 3857 CB LEU B 116 4669 3783 3909 256 52 -311 A C ATOM 3858 CG LEU B 116 4.742 10.725 64.483 1.00 34.04 A C ANISOU 3858 CG LEU B 116 4953 3892 4088 300 -11 -367 A C ATOM 3859 CD1 LEU B 116 4.099 9.729 65.465 1.00 31.45 A C ANISOU 3859 CD1 LEU B 116 4143 3475 4329 577 18 -110 A C ATOM 3860 CD2 LEU B 116 3.723 11.701 63.922 1.00 36.53 A C ANISOU 3860 CD2 LEU B 116 5218 3753 4908 302 -205 -428 A C ATOM 3861 N SER B 117 8.567 10.286 64.264 1.00 36.23 A N ANISOU 3861 N SER B 117 5364 4167 4233 115 241 -86 A N ATOM 3862 CA SER B 117 9.220 9.467 63.225 1.00 38.60 A C ANISOU 3862 CA SER B 117 5656 4429 4581 23 328 -127 A C ATOM 3863 C SER B 117 10.000 8.305 63.795 1.00 40.15 A C ANISOU 3863 C SER B 117 5805 4659 4790 -38 203 -97 A C ATOM 3864 O SER B 117 9.888 7.172 63.287 1.00 41.64 A O ANISOU 3864 O SER B 117 6148 4805 4867 -103 127 -43 A O ATOM 3865 CB SER B 117 10.117 10.322 62.333 1.00 39.13 A C ANISOU 3865 CB SER B 117 5674 4535 4658 23 285 -158 A C ATOM 3866 OG SER B 117 9.282 11.160 61.596 1.00 39.34 A O ANISOU 3866 OG SER B 117 5648 4417 4882 -3 366 -234 A O ATOM 3867 N MET B 118 10.790 8.586 64.829 1.00 40.57 A N ANISOU 3867 N MET B 118 5884 4805 4725 -90 263 -84 A N ATOM 3868 CA MET B 118 11.587 7.576 65.512 1.00 42.68 A C ANISOU 3868 CA MET B 118 6056 5094 5064 -131 267 -99 A C ATOM 3869 C MET B 118 11.401 7.798 67.021 1.00 39.52 A C ANISOU 3869 C MET B 118 5628 4784 4602 -175 329 -119 A C ATOM 3870 O MET B 118 12.249 8.394 67.645 1.00 39.41 A O ANISOU 3870 O MET B 118 5659 4870 4445 -236 491 -180 A O ATOM 3871 CB MET B 118 13.070 7.702 65.127 1.00 42.06 A C ANISOU 3871 CB MET B 118 5964 4977 5036 -144 267 -119 A C ATOM 3872 CG MET B 118 13.323 7.648 63.616 1.00 45.86 A C ANISOU 3872 CG MET B 118 6386 5504 5533 -78 324 -106 A C ATOM 3873 SD MET B 118 14.793 6.714 63.152 1.00 50.66 A S ANISOU 3873 SD MET B 118 6835 5889 6524 -176 320 7 A S ATOM 3874 CE MET B 118 14.301 5.051 63.628 1.00 51.25 A C ANISOU 3874 CE MET B 118 6724 6037 6711 69 294 -146 A C ATOM 3875 N PRO B 119 10.260 7.359 67.581 1.00 38.57 A N ANISOU 3875 N PRO B 119 5478 4733 4443 -176 387 -103 A N ATOM 3876 CA PRO B 119 9.970 7.770 68.980 1.00 37.65 A C ANISOU 3876 CA PRO B 119 5280 4744 4282 -126 361 -155 A C ATOM 3877 C PRO B 119 10.984 7.291 70.021 1.00 37.88 A C ANISOU 3877 C PRO B 119 5241 4816 4334 -104 414 -190 A C ATOM 3878 O PRO B 119 11.324 6.100 70.053 1.00 38.62 A O ANISOU 3878 O PRO B 119 5473 4801 4400 -167 324 -215 A O ATOM 3879 CB PRO B 119 8.571 7.184 69.257 1.00 37.85 A C ANISOU 3879 CB PRO B 119 5248 4772 4359 -112 338 -134 A C ATOM 3880 CG PRO B 119 7.948 6.941 67.890 1.00 38.11 A C ANISOU 3880 CG PRO B 119 5357 4760 4363 -31 399 -187 A C ATOM 3881 CD PRO B 119 9.151 6.587 66.992 1.00 38.08 A C ANISOU 3881 CD PRO B 119 5435 4622 4412 -224 359 -65 A C ATOM 3882 N ARG B 120 11.452 8.227 70.845 1.00 35.75 A N ANISOU 3882 N ARG B 120 4815 4739 4026 -15 518 -243 A N ATOM 3883 CA ARG B 120 12.324 7.942 71.979 1.00 35.74 A C ANISOU 3883 CA ARG B 120 4688 4795 4094 -23 538 -241 A C ATOM 3884 C ARG B 120 11.514 7.909 73.287 1.00 34.21 A C ANISOU 3884 C ARG B 120 4539 4623 3833 -8 585 -292 A C ATOM 3885 O ARG B 120 11.913 7.257 74.282 1.00 34.60 A O ANISOU 3885 O ARG B 120 4586 4726 3834 -41 630 -279 A O ATOM 3886 CB ARG B 120 13.365 9.048 72.124 1.00 36.49 A C ANISOU 3886 CB ARG B 120 4780 4781 4302 -18 429 -257 A C ATOM 3887 CG ARG B 120 14.577 8.990 71.252 1.00 40.67 A C ANISOU 3887 CG ARG B 120 5162 5255 5036 1 311 1 A C ATOM 3888 CD ARG B 120 15.590 10.044 71.773 1.00 45.19 A C ANISOU 3888 CD ARG B 120 5547 5497 6126 124 116 7 A C ATOM 3889 NE ARG B 120 15.051 11.416 71.775 1.00 44.13 A N ANISOU 3889 NE ARG B 120 5281 5460 6024 43 115 -54 A N ATOM 3890 CZ ARG B 120 15.751 12.496 72.115 1.00 42.38 A C ANISOU 3890 CZ ARG B 120 5120 5358 5622 20 186 -177 A C ATOM 3891 NH1 ARG B 120 17.015 12.375 72.510 1.00 42.23 A N1+ ANISOU 3891 NH1 ARG B 120 4910 5475 5661 -62 364 -275 A N1+ ATOM 3892 NH2 ARG B 120 15.189 13.700 72.073 1.00 41.28 A N ANISOU 3892 NH2 ARG B 120 4786 5344 5555 9 358 -53 A N ATOM 3893 N GLY B 121 10.395 8.613 73.296 1.00 32.76 A N ANISOU 3893 N GLY B 121 4272 4523 3650 207 620 -401 A N ATOM 3894 CA GLY B 121 9.544 8.675 74.525 1.00 31.91 A C ANISOU 3894 CA GLY B 121 4034 4512 3577 274 602 -374 A C ATOM 3895 C GLY B 121 10.232 9.415 75.654 1.00 32.72 A C ANISOU 3895 C GLY B 121 4215 4467 3749 243 479 -444 A C ATOM 3896 O GLY B 121 10.121 9.049 76.853 1.00 32.55 A O ANISOU 3896 O GLY B 121 4065 4510 3792 255 541 -677 A O ATOM 3897 N THR B 122 10.960 10.466 75.288 1.00 32.57 A N ANISOU 3897 N THR B 122 4045 4404 3923 327 335 -427 A N ATOM 3898 CA THR B 122 11.639 11.315 76.282 1.00 33.25 A C ANISOU 3898 CA THR B 122 4146 4418 4067 338 289 -409 A C ATOM 3899 C THR B 122 11.368 12.805 76.057 1.00 32.44 A C ANISOU 3899 C THR B 122 4031 4354 3940 379 222 -394 A C ATOM 3900 O THR B 122 10.708 13.205 75.104 1.00 32.57 A O ANISOU 3900 O THR B 122 3962 4467 3943 514 41 -376 A O ATOM 3901 CB THR B 122 13.167 11.061 76.266 1.00 33.41 A C ANISOU 3901 CB THR B 122 4195 4412 4085 273 156 -426 A C ATOM 3902 CG2 THR B 122 13.486 9.570 76.521 1.00 35.51 A C ANISOU 3902 CG2 THR B 122 4408 4511 4574 170 181 -293 A C ATOM 3903 OG1 THR B 122 13.685 11.416 74.987 1.00 35.06 A O ANISOU 3903 OG1 THR B 122 4142 4723 4454 415 523 -403 A O ATOM 3904 N MET B 123 11.892 13.627 76.952 1.00 32.01 A N ANISOU 3904 N MET B 123 4127 4229 3804 384 276 -333 A N ATOM 3905 CA MET B 123 12.096 15.054 76.715 1.00 32.88 A C ANISOU 3905 CA MET B 123 4222 4351 3918 381 387 -309 A C ATOM 3906 C MET B 123 13.136 15.239 75.618 1.00 32.81 A C ANISOU 3906 C MET B 123 4209 4335 3919 349 359 -250 A C ATOM 3907 O MET B 123 13.790 14.280 75.215 1.00 32.89 A O ANISOU 3907 O MET B 123 4265 4255 3973 414 393 -375 A O ATOM 3908 CB MET B 123 12.633 15.680 77.998 1.00 32.69 A C ANISOU 3908 CB MET B 123 4189 4316 3916 441 456 -240 A C ATOM 3909 CG MET B 123 11.665 15.512 79.193 1.00 33.97 A C ANISOU 3909 CG MET B 123 4547 4420 3938 337 699 -340 A C ATOM 3910 SD MET B 123 10.099 16.427 79.045 1.00 35.19 A S ANISOU 3910 SD MET B 123 4569 4509 4290 542 373 -112 A S ATOM 3911 CE MET B 123 10.655 18.152 79.001 1.00 37.22 A C ANISOU 3911 CE MET B 123 4927 4635 4578 388 475 -264 A C ATOM 3912 N GLN B 124 13.309 16.476 75.161 1.00 33.25 A N ANISOU 3912 N GLN B 124 4278 4365 3991 320 306 -216 A N ATOM 3913 CA GLN B 124 14.297 16.758 74.109 1.00 33.27 A C ANISOU 3913 CA GLN B 124 4224 4293 4122 331 348 -191 A C ATOM 3914 C GLN B 124 15.707 16.340 74.542 1.00 34.72 A C ANISOU 3914 C GLN B 124 4325 4547 4320 316 318 -191 A C ATOM 3915 O GLN B 124 16.540 15.988 73.700 1.00 36.48 A O ANISOU 3915 O GLN B 124 4654 4791 4414 227 305 -60 A O ATOM 3916 CB GLN B 124 14.251 18.226 73.635 1.00 33.54 A C ANISOU 3916 CB GLN B 124 4183 4382 4178 279 303 -255 A C ATOM 3917 CG GLN B 124 13.047 18.584 72.746 1.00 32.37 A C ANISOU 3917 CG GLN B 124 4285 4181 3831 353 297 -136 A C ATOM 3918 CD GLN B 124 13.059 17.897 71.404 1.00 33.25 A C ANISOU 3918 CD GLN B 124 4410 4264 3957 328 244 -220 A C ATOM 3919 NE2 GLN B 124 11.872 17.615 70.881 1.00 30.03 A N ANISOU 3919 NE2 GLN B 124 4479 3726 3203 268 168 -513 A N ATOM 3920 OE1 GLN B 124 14.123 17.633 70.833 1.00 34.62 A O ANISOU 3920 OE1 GLN B 124 4433 4524 4195 161 362 132 A O ATOM 3921 N ASP B 125 15.969 16.358 75.843 1.00 34.90 A N ANISOU 3921 N ASP B 125 4301 4608 4350 357 299 -237 A N ATOM 3922 CA ASP B 125 17.317 16.077 76.352 1.00 36.25 A C ANISOU 3922 CA ASP B 125 4440 4820 4512 254 288 -273 A C ATOM 3923 C ASP B 125 17.622 14.587 76.538 1.00 36.75 A C ANISOU 3923 C ASP B 125 4426 4893 4643 211 258 -254 A C ATOM 3924 O ASP B 125 18.691 14.227 77.045 1.00 38.52 A O ANISOU 3924 O ASP B 125 4617 5162 4855 205 245 -355 A O ATOM 3925 CB ASP B 125 17.600 16.879 77.640 1.00 36.52 A C ANISOU 3925 CB ASP B 125 4537 4827 4509 283 334 -234 A C ATOM 3926 CG ASP B 125 16.889 16.320 78.862 1.00 38.25 A C ANISOU 3926 CG ASP B 125 4764 5116 4652 231 284 -247 A C ATOM 3927 OD1 ASP B 125 16.097 15.374 78.704 1.00 38.54 A O ANISOU 3927 OD1 ASP B 125 4988 5233 4420 279 100 -148 A O ATOM 3928 OD2 ASP B 125 17.155 16.812 79.989 1.00 40.46 A O1- ANISOU 3928 OD2 ASP B 125 5166 5333 4873 380 121 -331 A O1- ATOM 3929 N GLY B 126 16.672 13.731 76.172 1.00 35.41 A N ANISOU 3929 N GLY B 126 4304 4706 4442 254 268 -276 A N ATOM 3930 CA GLY B 126 16.861 12.277 76.203 1.00 34.94 A C ANISOU 3930 CA GLY B 126 4280 4657 4335 234 248 -327 A C ATOM 3931 C GLY B 126 16.550 11.650 77.542 1.00 34.96 A C ANISOU 3931 C GLY B 126 4369 4569 4344 237 172 -378 A C ATOM 3932 O GLY B 126 16.844 10.465 77.775 1.00 35.04 A O ANISOU 3932 O GLY B 126 4316 4566 4430 256 255 -503 A O ATOM 3933 N THR B 127 15.951 12.434 78.428 1.00 34.19 A N ANISOU 3933 N THR B 127 4305 4592 4092 293 204 -479 A N ATOM 3934 CA THR B 127 15.501 11.880 79.717 1.00 34.38 A C ANISOU 3934 CA THR B 127 4459 4600 4000 217 136 -484 A C ATOM 3935 C THR B 127 14.022 12.059 79.992 1.00 33.71 A C ANISOU 3935 C THR B 127 4429 4528 3851 172 152 -509 A C ATOM 3936 O THR B 127 13.317 12.726 79.234 1.00 34.37 A O ANISOU 3936 O THR B 127 4495 4724 3837 102 247 -588 A O ATOM 3937 CB THR B 127 16.332 12.424 80.885 1.00 34.17 A C ANISOU 3937 CB THR B 127 4450 4435 4099 273 153 -357 A C ATOM 3938 CG2 THR B 127 17.810 12.166 80.628 1.00 36.64 A C ANISOU 3938 CG2 THR B 127 4610 4815 4495 283 6 -304 A C ATOM 3939 OG1 THR B 127 16.023 13.823 81.091 1.00 36.25 A O ANISOU 3939 OG1 THR B 127 4745 4524 4502 143 50 -504 A O ATOM 3940 N SER B 128 13.554 11.442 81.090 1.00 33.62 A N ANISOU 3940 N SER B 128 4352 4525 3896 225 206 -471 A N ATOM 3941 CA SER B 128 12.162 11.451 81.464 1.00 32.64 A C ANISOU 3941 CA SER B 128 4262 4404 3732 182 85 -364 A C ATOM 3942 C SER B 128 11.955 12.243 82.757 1.00 31.65 A C ANISOU 3942 C SER B 128 4147 4294 3584 163 -56 -290 A C ATOM 3943 O SER B 128 12.824 12.207 83.685 1.00 32.27 A O ANISOU 3943 O SER B 128 4155 4426 3678 119 -246 -324 A O ATOM 3944 CB SER B 128 11.683 10.018 81.679 1.00 33.06 A C ANISOU 3944 CB SER B 128 4294 4428 3838 227 135 -182 A C ATOM 3945 OG SER B 128 10.393 10.028 82.291 1.00 33.80 A O ANISOU 3945 OG SER B 128 4370 4295 4176 529 285 -98 A O ATOM 3946 N ARG B 129 10.813 12.938 82.843 1.00 30.13 A N ANISOU 3946 N ARG B 129 4097 4038 3310 224 -33 -400 A N ATOM 3947 CA ARG B 129 10.444 13.692 84.049 1.00 29.43 A C ANISOU 3947 CA ARG B 129 3990 3830 3362 191 59 -413 A C ATOM 3948 C ARG B 129 9.489 12.895 84.943 1.00 29.34 A C ANISOU 3948 C ARG B 129 3986 3795 3364 302 56 -384 A C ATOM 3949 O ARG B 129 9.045 13.399 85.985 1.00 29.79 A O ANISOU 3949 O ARG B 129 4177 3729 3410 359 130 -368 A O ATOM 3950 CB ARG B 129 9.795 15.036 83.677 1.00 28.46 A C ANISOU 3950 CB ARG B 129 3941 3609 3263 336 122 -418 A C ATOM 3951 CG ARG B 129 10.759 15.951 82.933 1.00 28.34 A C ANISOU 3951 CG ARG B 129 3712 3759 3295 467 179 -271 A C ATOM 3952 CD ARG B 129 11.851 16.568 83.818 1.00 29.52 A C ANISOU 3952 CD ARG B 129 3463 4132 3618 331 51 -333 A C ATOM 3953 NE ARG B 129 12.824 17.151 82.883 1.00 31.74 A N ANISOU 3953 NE ARG B 129 3917 4097 4044 696 283 -311 A N ATOM 3954 CZ ARG B 129 13.845 16.493 82.338 1.00 31.41 A C ANISOU 3954 CZ ARG B 129 3446 4085 4400 549 -97 -286 A C ATOM 3955 NH1 ARG B 129 14.123 15.236 82.689 1.00 35.13 A N1+ ANISOU 3955 NH1 ARG B 129 4450 4295 4603 586 325 -422 A N1+ ATOM 3956 NH2 ARG B 129 14.613 17.106 81.436 1.00 33.13 A N ANISOU 3956 NH2 ARG B 129 4045 4333 4208 111 315 -360 A N ATOM 3957 N PHE B 130 9.136 11.681 84.519 1.00 29.95 A N ANISOU 3957 N PHE B 130 4103 3800 3475 98 87 -469 A N ATOM 3958 CA PHE B 130 8.161 10.861 85.257 1.00 30.25 A C ANISOU 3958 CA PHE B 130 4138 3929 3424 69 12 -424 A C ATOM 3959 C PHE B 130 8.750 9.636 85.924 1.00 30.87 A C ANISOU 3959 C PHE B 130 4248 3973 3506 24 5 -453 A C ATOM 3960 O PHE B 130 9.473 8.856 85.297 1.00 30.86 A O ANISOU 3960 O PHE B 130 4309 3864 3553 -165 29 -574 A O ATOM 3961 CB PHE B 130 7.110 10.309 84.290 1.00 29.66 A C ANISOU 3961 CB PHE B 130 4038 3883 3349 64 -72 -422 A C ATOM 3962 CG PHE B 130 6.279 11.351 83.623 1.00 29.51 A C ANISOU 3962 CG PHE B 130 4140 3897 3175 -137 7 -293 A C ATOM 3963 CD1 PHE B 130 5.437 12.205 84.363 1.00 31.68 A C ANISOU 3963 CD1 PHE B 130 4570 3823 3641 -259 -286 -135 A C ATOM 3964 CD2 PHE B 130 6.302 11.459 82.222 1.00 28.62 A C ANISOU 3964 CD2 PHE B 130 4248 3709 2916 -57 -22 -118 A C ATOM 3965 CE1 PHE B 130 4.642 13.154 83.699 1.00 33.20 A C ANISOU 3965 CE1 PHE B 130 4537 4228 3849 -306 -95 -347 A C ATOM 3966 CE2 PHE B 130 5.496 12.389 81.560 1.00 28.62 A C ANISOU 3966 CE2 PHE B 130 4187 3294 3391 181 259 -574 A C ATOM 3967 CZ PHE B 130 4.664 13.241 82.305 1.00 28.34 A C ANISOU 3967 CZ PHE B 130 4012 3511 3245 19 18 -286 A C ATOM 3968 N THR B 131 8.357 9.404 87.168 1.00 31.50 A N ANISOU 3968 N THR B 131 4306 4061 3599 89 131 -535 A N ATOM 3969 CA THR B 131 8.695 8.141 87.826 1.00 33.29 A C ANISOU 3969 CA THR B 131 4458 4228 3961 15 140 -502 A C ATOM 3970 C THR B 131 7.462 7.619 88.539 1.00 32.85 A C ANISOU 3970 C THR B 131 4432 4126 3920 124 139 -639 A C ATOM 3971 O THR B 131 6.607 8.402 88.953 1.00 32.24 A O ANISOU 3971 O THR B 131 4427 4020 3803 241 189 -725 A O ATOM 3972 CB THR B 131 9.857 8.289 88.841 1.00 33.35 A C ANISOU 3972 CB THR B 131 4466 4153 4052 -9 61 -451 A C ATOM 3973 CG2 THR B 131 11.178 8.506 88.112 1.00 35.11 A C ANISOU 3973 CG2 THR B 131 4529 4445 4365 26 44 -505 A C ATOM 3974 OG1 THR B 131 9.607 9.384 89.740 1.00 37.14 A O ANISOU 3974 OG1 THR B 131 5066 4586 4456 -137 68 -414 A O ATOM 3975 N CYS B 132 7.351 6.298 88.632 1.00 34.37 A N ANISOU 3975 N CYS B 132 4542 4209 4305 89 260 -737 A N ATOM 3976 CA CYS B 132 6.268 5.688 89.425 1.00 34.96 A C ANISOU 3976 CA CYS B 132 4645 4227 4408 -33 180 -843 A C ATOM 3977 C CYS B 132 6.968 4.704 90.335 1.00 36.81 A C ANISOU 3977 C CYS B 132 4923 4431 4629 -147 102 -753 A C ATOM 3978 O CYS B 132 7.542 3.735 89.844 1.00 37.60 A O ANISOU 3978 O CYS B 132 5177 4412 4696 -245 0 -876 A O ATOM 3979 CB CYS B 132 5.287 4.965 88.513 1.00 34.76 A C ANISOU 3979 CB CYS B 132 4593 4169 4443 42 299 -835 A C ATOM 3980 SG CYS B 132 3.941 4.168 89.400 1.00 38.34 A S ANISOU 3980 SG CYS B 132 4825 4531 5210 167 596 -820 A S ATOM 3981 N ARG B 133 6.952 4.994 91.633 1.00 38.10 A N ANISOU 3981 N ARG B 133 5085 4646 4745 -195 -12 -745 A N ATOM 3982 CA ARG B 133 7.703 4.184 92.615 1.00 40.19 A C ANISOU 3982 CA ARG B 133 5267 5032 4969 -187 -58 -579 A C ATOM 3983 C ARG B 133 9.160 3.968 92.195 1.00 41.65 A C ANISOU 3983 C ARG B 133 5418 5217 5189 -198 -74 -461 A C ATOM 3984 O ARG B 133 9.726 2.851 92.317 1.00 43.59 A O ANISOU 3984 O ARG B 133 5659 5403 5497 -239 -86 -398 A O ATOM 3985 CB ARG B 133 6.951 2.885 92.867 1.00 40.61 A C ANISOU 3985 CB ARG B 133 5287 5017 5124 -203 -91 -523 A C ATOM 3986 CG ARG B 133 5.592 3.162 93.484 1.00 43.32 A C ANISOU 3986 CG ARG B 133 5631 5392 5436 -93 60 -395 A C ATOM 3987 CD ARG B 133 4.716 1.939 93.580 1.00 45.91 A C ANISOU 3987 CD ARG B 133 5858 5642 5943 150 170 -296 A C ATOM 3988 NE ARG B 133 3.569 2.232 94.425 1.00 48.48 A N ANISOU 3988 NE ARG B 133 6238 6056 6126 121 208 -247 A N ATOM 3989 CZ ARG B 133 2.424 2.729 93.992 1.00 48.57 A C ANISOU 3989 CZ ARG B 133 6289 6117 6047 73 67 -352 A C ATOM 3990 NH1 ARG B 133 2.253 2.981 92.693 1.00 51.32 A N1+ ANISOU 3990 NH1 ARG B 133 6600 6562 6335 240 185 -384 A N1+ ATOM 3991 NH2 ARG B 133 1.445 2.970 94.849 1.00 48.25 A N ANISOU 3991 NH2 ARG B 133 6500 6062 5769 66 108 -519 A N ATOM 3992 N GLY B 134 9.765 5.064 91.731 1.00 41.65 A N ANISOU 3992 N GLY B 134 5322 5392 5112 -115 6 -432 A N ATOM 3993 CA GLY B 134 11.175 5.097 91.296 1.00 42.24 A C ANISOU 3993 CA GLY B 134 5385 5456 5206 -107 91 -291 A C ATOM 3994 C GLY B 134 11.486 4.443 89.952 1.00 42.07 A C ANISOU 3994 C GLY B 134 5371 5434 5179 -93 100 -320 A C ATOM 3995 O GLY B 134 12.657 4.361 89.561 1.00 43.97 A O ANISOU 3995 O GLY B 134 5484 5720 5499 -82 191 -219 A O ATOM 3996 N LYS B 135 10.466 3.943 89.254 1.00 40.86 A N ANISOU 3996 N LYS B 135 5325 5243 4955 -175 98 -373 A N ATOM 3997 CA LYS B 135 10.671 3.334 87.941 1.00 39.14 A C ANISOU 3997 CA LYS B 135 5272 4934 4662 -171 -3 -534 A C ATOM 3998 C LYS B 135 10.426 4.437 86.909 1.00 37.40 A C ANISOU 3998 C LYS B 135 4954 4770 4486 -170 21 -555 A C ATOM 3999 O LYS B 135 9.428 5.104 86.994 1.00 36.20 A O ANISOU 3999 O LYS B 135 5164 4385 4205 -302 210 -628 A O ATOM 4000 CB LYS B 135 9.706 2.154 87.754 1.00 40.44 A C ANISOU 4000 CB LYS B 135 5341 5074 4947 -161 -10 -418 A C ATOM 4001 CG LYS B 135 9.816 1.451 86.420 1.00 42.81 A C ANISOU 4001 CG LYS B 135 5886 5250 5128 -131 -87 -410 A C ATOM 4002 CD LYS B 135 9.538 -0.052 86.567 1.00 47.76 A C ANISOU 4002 CD LYS B 135 6460 5597 6089 196 168 -167 A C ATOM 4003 CE LYS B 135 10.697 -0.861 85.988 1.00 50.02 A C ANISOU 4003 CE LYS B 135 6627 6025 6351 31 91 -61 A C ATOM 4004 NZ LYS B 135 10.664 -2.294 86.377 1.00 51.09 A N1+ ANISOU 4004 NZ LYS B 135 6849 6197 6365 59 169 -282 A N1+ ATOM 4005 N PRO B 136 11.355 4.641 85.963 1.00 36.09 A N ANISOU 4005 N PRO B 136 4801 4634 4276 -188 -16 -552 A N ATOM 4006 CA PRO B 136 11.099 5.694 84.964 1.00 35.27 A C ANISOU 4006 CA PRO B 136 4631 4605 4164 -48 57 -563 A C ATOM 4007 C PRO B 136 9.908 5.341 84.072 1.00 33.83 A C ANISOU 4007 C PRO B 136 4493 4378 3981 -38 36 -572 A C ATOM 4008 O PRO B 136 9.707 4.162 83.728 1.00 35.17 A O ANISOU 4008 O PRO B 136 4701 4577 4085 -87 5 -628 A O ATOM 4009 CB PRO B 136 12.395 5.724 84.131 1.00 35.62 A C ANISOU 4009 CB PRO B 136 4626 4663 4245 -3 35 -480 A C ATOM 4010 CG PRO B 136 13.396 4.986 84.945 1.00 37.39 A C ANISOU 4010 CG PRO B 136 4831 4825 4551 -53 9 -514 A C ATOM 4011 CD PRO B 136 12.654 3.982 85.758 1.00 37.00 A C ANISOU 4011 CD PRO B 136 4811 4818 4427 -93 21 -474 A C ATOM 4012 N ILE B 137 9.149 6.362 83.668 1.00 32.04 A N ANISOU 4012 N ILE B 137 4224 4345 3604 -8 110 -565 A N ATOM 4013 CA ILE B 137 8.010 6.188 82.743 1.00 30.30 A C ANISOU 4013 CA ILE B 137 4192 4019 3301 85 108 -626 A C ATOM 4014 C ILE B 137 8.260 7.117 81.547 1.00 29.17 A C ANISOU 4014 C ILE B 137 4046 3772 3265 240 133 -615 A C ATOM 4015 O ILE B 137 8.667 8.262 81.727 1.00 30.81 A O ANISOU 4015 O ILE B 137 4332 3961 3411 172 -56 -648 A O ATOM 4016 CB ILE B 137 6.655 6.561 83.409 1.00 30.46 A C ANISOU 4016 CB ILE B 137 4150 4090 3333 105 106 -674 A C ATOM 4017 CG1 ILE B 137 6.473 5.822 84.766 1.00 32.29 A C ANISOU 4017 CG1 ILE B 137 4675 4268 3325 -20 58 -688 A C ATOM 4018 CG2 ILE B 137 5.463 6.249 82.475 1.00 31.70 A C ANISOU 4018 CG2 ILE B 137 4270 4242 3532 -48 -2 -607 A C ATOM 4019 CD1 ILE B 137 6.300 4.332 84.642 1.00 34.66 A C ANISOU 4019 CD1 ILE B 137 4845 4556 3767 141 265 -756 A C ATOM 4020 N HIS B 138 8.002 6.612 80.343 1.00 28.65 A N ANISOU 4020 N HIS B 138 3944 3639 3301 356 86 -714 A N ATOM 4021 CA HIS B 138 8.184 7.365 79.110 1.00 28.69 A C ANISOU 4021 CA HIS B 138 3902 3585 3413 188 40 -625 A C ATOM 4022 C HIS B 138 7.154 8.459 78.888 1.00 27.94 A C ANISOU 4022 C HIS B 138 3810 3522 3283 203 26 -544 A C ATOM 4023 O HIS B 138 5.996 8.381 79.351 1.00 27.46 A O ANISOU 4023 O HIS B 138 3831 3268 3334 257 48 -608 A O ATOM 4024 CB HIS B 138 8.210 6.429 77.905 1.00 29.58 A C ANISOU 4024 CB HIS B 138 3915 3701 3621 78 111 -617 A C ATOM 4025 CG HIS B 138 9.444 5.598 77.843 1.00 31.71 A C ANISOU 4025 CG HIS B 138 4064 3897 4088 -145 209 -463 A C ATOM 4026 CD2 HIS B 138 10.690 5.912 77.411 1.00 31.53 A C ANISOU 4026 CD2 HIS B 138 3835 3948 4197 -362 325 -494 A C ATOM 4027 ND1 HIS B 138 9.510 4.304 78.323 1.00 33.78 A N ANISOU 4027 ND1 HIS B 138 4306 4297 4231 -252 -13 -382 A N ATOM 4028 CE1 HIS B 138 10.737 3.846 78.144 1.00 34.78 A C ANISOU 4028 CE1 HIS B 138 4361 4297 4557 -294 299 -442 A C ATOM 4029 NE2 HIS B 138 11.476 4.809 77.625 1.00 36.51 A N ANISOU 4029 NE2 HIS B 138 4727 4101 5043 -495 266 -328 A N ATOM 4030 N HIS B 139 7.627 9.477 78.176 1.00 26.95 A N ANISOU 4030 N HIS B 139 3761 3390 3086 236 2 -580 A N ATOM 4031 CA HIS B 139 6.771 10.520 77.610 1.00 26.83 A C ANISOU 4031 CA HIS B 139 3684 3436 3073 206 77 -459 A C ATOM 4032 C HIS B 139 6.176 9.993 76.294 1.00 27.63 A C ANISOU 4032 C HIS B 139 3791 3537 3168 177 90 -341 A C ATOM 4033 O HIS B 139 6.639 8.975 75.717 1.00 28.42 A O ANISOU 4033 O HIS B 139 3882 3828 3087 -14 89 -293 A O ATOM 4034 CB HIS B 139 7.613 11.801 77.367 1.00 26.78 A C ANISOU 4034 CB HIS B 139 3777 3274 3121 214 -66 -480 A C ATOM 4035 CG HIS B 139 8.113 12.448 78.628 1.00 27.23 A C ANISOU 4035 CG HIS B 139 3576 3405 3364 386 23 -432 A C ATOM 4036 CD2 HIS B 139 9.034 12.048 79.544 1.00 29.61 A C ANISOU 4036 CD2 HIS B 139 4190 3540 3520 296 -52 -491 A C ATOM 4037 ND1 HIS B 139 7.621 13.651 79.087 1.00 30.06 A N ANISOU 4037 ND1 HIS B 139 4173 3627 3622 243 -69 -177 A N ATOM 4038 CE1 HIS B 139 8.211 13.966 80.229 1.00 29.16 A C ANISOU 4038 CE1 HIS B 139 3699 3847 3532 352 54 -635 A C ATOM 4039 NE2 HIS B 139 9.073 13.011 80.529 1.00 29.44 A N ANISOU 4039 NE2 HIS B 139 3752 4102 3329 236 31 -458 A N ATOM 4040 N PHE B 140 5.209 10.727 75.767 1.00 26.75 A N ANISOU 4040 N PHE B 140 3617 3633 2911 141 193 -260 A N ATOM 4041 CA PHE B 140 4.574 10.394 74.474 1.00 27.28 A C ANISOU 4041 CA PHE B 140 3820 3527 3016 238 237 -324 A C ATOM 4042 C PHE B 140 4.449 11.650 73.645 1.00 27.31 A C ANISOU 4042 C PHE B 140 3906 3473 2997 222 269 -298 A C ATOM 4043 O PHE B 140 3.735 12.599 74.011 1.00 26.99 A O ANISOU 4043 O PHE B 140 4078 3462 2713 236 420 -455 A O ATOM 4044 CB PHE B 140 3.192 9.768 74.701 1.00 27.70 A C ANISOU 4044 CB PHE B 140 3789 3627 3106 229 138 -300 A C ATOM 4045 CG PHE B 140 2.445 9.448 73.427 1.00 25.78 A C ANISOU 4045 CG PHE B 140 3731 3090 2972 311 91 -330 A C ATOM 4046 CD1 PHE B 140 2.981 8.587 72.466 1.00 28.02 A C ANISOU 4046 CD1 PHE B 140 4039 3415 3192 478 245 -465 A C ATOM 4047 CD2 PHE B 140 1.228 10.059 73.181 1.00 25.33 A C ANISOU 4047 CD2 PHE B 140 3675 3151 2795 150 208 -399 A C ATOM 4048 CE1 PHE B 140 2.270 8.299 71.289 1.00 27.94 A C ANISOU 4048 CE1 PHE B 140 4019 3505 3092 236 327 -352 A C ATOM 4049 CE2 PHE B 140 0.501 9.779 72.001 1.00 28.55 A C ANISOU 4049 CE2 PHE B 140 4028 3718 3102 134 109 -15 A C ATOM 4050 CZ PHE B 140 1.031 8.889 71.062 1.00 29.52 A C ANISOU 4050 CZ PHE B 140 4280 3632 3302 123 67 -156 A C ATOM 4051 N LEU B 141 5.132 11.638 72.502 1.00 27.27 A N ANISOU 4051 N LEU B 141 3891 3353 3115 310 360 -355 A N ATOM 4052 CA LEU B 141 5.118 12.777 71.553 1.00 27.38 A C ANISOU 4052 CA LEU B 141 3870 3395 3138 233 265 -318 A C ATOM 4053 C LEU B 141 5.449 14.114 72.228 1.00 27.93 A C ANISOU 4053 C LEU B 141 3839 3465 3308 241 257 -249 A C ATOM 4054 O LEU B 141 4.962 15.176 71.811 1.00 27.77 A O ANISOU 4054 O LEU B 141 3874 3303 3373 279 46 -233 A O ATOM 4055 CB LEU B 141 3.770 12.883 70.812 1.00 26.94 A C ANISOU 4055 CB LEU B 141 3911 3270 3053 389 229 -319 A C ATOM 4056 CG LEU B 141 3.259 11.645 70.085 1.00 29.22 A C ANISOU 4056 CG LEU B 141 4228 3473 3400 308 132 -160 A C ATOM 4057 CD1 LEU B 141 1.962 11.973 69.351 1.00 30.77 A C ANISOU 4057 CD1 LEU B 141 4446 3362 3882 335 -95 50 A C ATOM 4058 CD2 LEU B 141 4.356 11.042 69.195 1.00 32.89 A C ANISOU 4058 CD2 LEU B 141 4366 3825 4305 143 158 141 A C ATOM 4059 N GLY B 142 6.280 14.072 73.267 1.00 28.14 A N ANISOU 4059 N GLY B 142 3859 3503 3329 230 262 -283 A N ATOM 4060 CA GLY B 142 6.683 15.273 73.959 1.00 30.50 A C ANISOU 4060 CA GLY B 142 4267 3694 3624 229 322 -147 A C ATOM 4061 C GLY B 142 5.529 15.996 74.634 1.00 30.61 A C ANISOU 4061 C GLY B 142 4272 3688 3669 284 331 -109 A C ATOM 4062 O GLY B 142 5.628 17.192 74.915 1.00 32.39 A O ANISOU 4062 O GLY B 142 4464 3808 4035 566 366 8 A O ATOM 4063 N THR B 143 4.418 15.299 74.860 1.00 28.15 A N ANISOU 4063 N THR B 143 4164 3349 3181 405 268 -220 A N ATOM 4064 CA THR B 143 3.246 15.909 75.511 1.00 27.64 A C ANISOU 4064 CA THR B 143 4104 3407 2991 310 272 -305 A C ATOM 4065 C THR B 143 2.813 15.207 76.810 1.00 28.48 A C ANISOU 4065 C THR B 143 4234 3466 3119 286 345 -190 A C ATOM 4066 O THR B 143 2.887 15.800 77.878 1.00 30.44 A O ANISOU 4066 O THR B 143 4732 3584 3249 420 265 -252 A O ATOM 4067 CB THR B 143 2.036 16.089 74.548 1.00 28.22 A C ANISOU 4067 CB THR B 143 4108 3473 3140 366 256 -397 A C ATOM 4068 CG2 THR B 143 2.396 17.066 73.407 1.00 28.60 A C ANISOU 4068 CG2 THR B 143 4127 3854 2883 456 514 -548 A C ATOM 4069 OG1 THR B 143 1.636 14.822 73.995 1.00 29.56 A O ANISOU 4069 OG1 THR B 143 4334 3752 3143 245 270 -267 A O ATOM 4070 N SER B 144 2.348 13.971 76.712 1.00 27.37 A N ANISOU 4070 N SER B 144 4071 3353 2972 206 328 -89 A N ATOM 4071 CA SER B 144 1.956 13.166 77.882 1.00 26.22 A C ANISOU 4071 CA SER B 144 3836 3426 2699 24 228 -58 A C ATOM 4072 C SER B 144 0.899 13.873 78.705 1.00 26.46 A C ANISOU 4072 C SER B 144 3911 3398 2744 33 191 -60 A C ATOM 4073 O SER B 144 1.142 14.323 79.831 1.00 28.83 A O ANISOU 4073 O SER B 144 4094 3596 3262 172 129 342 A O ATOM 4074 CB SER B 144 3.181 12.857 78.753 1.00 26.40 A C ANISOU 4074 CB SER B 144 3902 3454 2672 58 210 -52 A C ATOM 4075 OG SER B 144 3.960 11.866 78.118 1.00 27.55 A O ANISOU 4075 OG SER B 144 3467 3954 3044 -118 77 136 A O ATOM 4076 N THR B 145 -0.298 13.912 78.180 1.00 25.59 A N ANISOU 4076 N THR B 145 3768 3257 2696 42 228 -151 A N ATOM 4077 CA THR B 145 -1.346 14.693 78.781 1.00 25.35 A C ANISOU 4077 CA THR B 145 3784 3118 2730 -46 226 -249 A C ATOM 4078 C THR B 145 -2.301 13.889 79.668 1.00 25.69 A C ANISOU 4078 C THR B 145 3844 3146 2769 65 189 -251 A C ATOM 4079 O THR B 145 -3.192 14.493 80.280 1.00 26.46 A O ANISOU 4079 O THR B 145 4064 3148 2840 45 372 -145 A O ATOM 4080 CB THR B 145 -2.174 15.442 77.723 1.00 26.00 A C ANISOU 4080 CB THR B 145 3739 3194 2944 -10 93 -221 A C ATOM 4081 CG2 THR B 145 -1.300 16.249 76.828 1.00 27.64 A C ANISOU 4081 CG2 THR B 145 3997 3203 3301 -88 189 -471 A C ATOM 4082 OG1 THR B 145 -2.934 14.526 76.945 1.00 26.55 A O ANISOU 4082 OG1 THR B 145 3746 3323 3019 -151 29 -33 A O ATOM 4083 N PHE B 146 -2.109 12.572 79.777 1.00 26.28 A N ANISOU 4083 N PHE B 146 4071 3212 2700 128 177 -256 A N ATOM 4084 CA PHE B 146 -2.973 11.719 80.661 1.00 26.28 A C ANISOU 4084 CA PHE B 146 4026 3325 2631 185 134 -205 A C ATOM 4085 C PHE B 146 -2.382 11.687 82.075 1.00 27.30 A C ANISOU 4085 C PHE B 146 4117 3399 2857 120 89 -284 A C ATOM 4086 O PHE B 146 -2.110 10.611 82.655 1.00 28.35 A O ANISOU 4086 O PHE B 146 4225 3547 2997 61 -113 -292 A O ATOM 4087 CB PHE B 146 -3.074 10.275 80.117 1.00 26.50 A C ANISOU 4087 CB PHE B 146 4108 3313 2647 207 136 -334 A C ATOM 4088 CG PHE B 146 -3.889 10.126 78.851 1.00 25.74 A C ANISOU 4088 CG PHE B 146 3797 3247 2736 308 225 -232 A C ATOM 4089 CD1 PHE B 146 -4.725 11.145 78.373 1.00 26.91 A C ANISOU 4089 CD1 PHE B 146 3829 3467 2927 322 47 -336 A C ATOM 4090 CD2 PHE B 146 -3.828 8.911 78.136 1.00 25.53 A C ANISOU 4090 CD2 PHE B 146 3882 3341 2476 265 503 -164 A C ATOM 4091 CE1 PHE B 146 -5.510 10.951 77.174 1.00 25.82 A C ANISOU 4091 CE1 PHE B 146 3415 3285 3110 72 36 -138 A C ATOM 4092 CE2 PHE B 146 -4.575 8.714 76.986 1.00 24.46 A C ANISOU 4092 CE2 PHE B 146 3598 2900 2793 445 151 -288 A C ATOM 4093 CZ PHE B 146 -5.428 9.742 76.483 1.00 27.02 A C ANISOU 4093 CZ PHE B 146 3837 3357 3069 214 148 -218 A C ATOM 4094 N SER B 147 -2.190 12.880 82.618 1.00 27.40 A N ANISOU 4094 N SER B 147 4176 3489 2744 172 67 -150 A N ATOM 4095 CA SER B 147 -1.604 13.074 83.938 1.00 28.15 A C ANISOU 4095 CA SER B 147 4315 3574 2806 62 117 -194 A C ATOM 4096 C SER B 147 -2.086 14.396 84.489 1.00 28.09 A C ANISOU 4096 C SER B 147 4301 3670 2701 65 160 -133 A C ATOM 4097 O SER B 147 -2.295 15.356 83.755 1.00 29.17 A O ANISOU 4097 O SER B 147 4477 3817 2789 104 120 -5 A O ATOM 4098 CB SER B 147 -0.078 13.092 83.841 1.00 27.93 A C ANISOU 4098 CB SER B 147 4215 3516 2879 186 126 -262 A C ATOM 4099 OG SER B 147 0.565 13.302 85.114 1.00 29.79 A O ANISOU 4099 OG SER B 147 4581 3697 3037 -84 142 -470 A O ATOM 4100 N GLN B 148 -2.241 14.462 85.802 1.00 28.33 A N ANISOU 4100 N GLN B 148 4189 3861 2712 152 242 -176 A N ATOM 4101 CA GLN B 148 -2.609 15.739 86.405 1.00 27.72 A C ANISOU 4101 CA GLN B 148 4134 3694 2704 235 307 -179 A C ATOM 4102 C GLN B 148 -1.595 16.865 86.132 1.00 28.28 A C ANISOU 4102 C GLN B 148 4122 3705 2916 252 139 -128 A C ATOM 4103 O GLN B 148 -2.000 18.034 86.050 1.00 28.09 A O ANISOU 4103 O GLN B 148 4097 3619 2957 356 165 -79 A O ATOM 4104 CB GLN B 148 -2.886 15.568 87.899 1.00 28.97 A C ANISOU 4104 CB GLN B 148 4280 3879 2849 213 289 -310 A C ATOM 4105 CG GLN B 148 -4.138 14.715 88.135 1.00 29.29 A C ANISOU 4105 CG GLN B 148 4249 4170 2707 137 208 -405 A C ATOM 4106 CD GLN B 148 -4.328 14.375 89.621 1.00 32.02 A C ANISOU 4106 CD GLN B 148 4735 4711 2718 92 216 -162 A C ATOM 4107 NE2 GLN B 148 -5.567 14.092 89.997 1.00 37.11 A N ANISOU 4107 NE2 GLN B 148 5080 5385 3634 -191 702 -164 A N ATOM 4108 OE1 GLN B 148 -3.364 14.319 90.394 1.00 32.95 A O ANISOU 4108 OE1 GLN B 148 4898 4499 3121 -136 165 -463 A O ATOM 4109 N TYR B 149 -0.314 16.500 86.006 1.00 27.99 A N ANISOU 4109 N TYR B 149 4195 3568 2871 153 177 -116 A N ATOM 4110 CA TYR B 149 0.786 17.427 85.665 1.00 27.91 A C ANISOU 4110 CA TYR B 149 4161 3586 2856 171 76 -127 A C ATOM 4111 C TYR B 149 1.714 16.809 84.675 1.00 27.59 A C ANISOU 4111 C TYR B 149 4092 3488 2902 122 63 -179 A C ATOM 4112 O TYR B 149 2.005 15.611 84.746 1.00 27.55 A O ANISOU 4112 O TYR B 149 4161 3328 2977 214 401 -241 A O ATOM 4113 CB TYR B 149 1.634 17.800 86.883 1.00 29.10 A C ANISOU 4113 CB TYR B 149 4392 3703 2958 125 4 -109 A C ATOM 4114 CG TYR B 149 0.915 18.653 87.877 1.00 31.55 A C ANISOU 4114 CG TYR B 149 4639 4046 3301 19 31 -5 A C ATOM 4115 CD1 TYR B 149 0.060 18.073 88.831 1.00 30.91 A C ANISOU 4115 CD1 TYR B 149 4570 4157 3014 153 30 184 A C ATOM 4116 CD2 TYR B 149 1.086 20.019 87.878 1.00 32.64 A C ANISOU 4116 CD2 TYR B 149 4838 4167 3393 -123 -270 20 A C ATOM 4117 CE1 TYR B 149 -0.623 18.852 89.726 1.00 30.45 A C ANISOU 4117 CE1 TYR B 149 4788 4028 2753 117 -148 93 A C ATOM 4118 CE2 TYR B 149 0.433 20.822 88.812 1.00 32.56 A C ANISOU 4118 CE2 TYR B 149 4830 4054 3484 -205 -175 156 A C ATOM 4119 CZ TYR B 149 -0.427 20.228 89.720 1.00 33.26 A C ANISOU 4119 CZ TYR B 149 4998 4149 3487 -100 40 232 A C ATOM 4120 OH TYR B 149 -1.095 20.960 90.665 1.00 37.01 A O ANISOU 4120 OH TYR B 149 5399 4531 4129 -331 141 341 A O ATOM 4121 N THR B 150 2.188 17.627 83.741 1.00 26.17 A N ANISOU 4121 N THR B 150 3942 3255 2744 222 114 -110 A N ATOM 4122 CA THR B 150 3.162 17.142 82.757 1.00 26.55 A C ANISOU 4122 CA THR B 150 3972 3422 2692 236 -32 -128 A C ATOM 4123 C THR B 150 4.253 18.163 82.581 1.00 26.68 A C ANISOU 4123 C THR B 150 4050 3344 2743 230 6 -317 A C ATOM 4124 O THR B 150 4.107 19.294 83.060 1.00 27.94 A O ANISOU 4124 O THR B 150 4213 3373 3028 411 11 -350 A O ATOM 4125 CB THR B 150 2.512 16.759 81.410 1.00 25.00 A C ANISOU 4125 CB THR B 150 3795 3131 2573 188 -117 -35 A C ATOM 4126 CG2 THR B 150 2.095 17.967 80.654 1.00 27.56 A C ANISOU 4126 CG2 THR B 150 4211 3428 2830 177 -304 -64 A C ATOM 4127 OG1 THR B 150 3.485 16.074 80.614 1.00 27.20 A O ANISOU 4127 OG1 THR B 150 3943 3433 2960 -24 -87 110 A O ATOM 4128 N VAL B 151 5.369 17.740 81.989 1.00 27.01 A N ANISOU 4128 N VAL B 151 4116 3479 2668 359 168 -419 A N ATOM 4129 CA VAL B 151 6.469 18.663 81.678 1.00 26.99 A C ANISOU 4129 CA VAL B 151 4094 3430 2729 462 112 -263 A C ATOM 4130 C VAL B 151 6.721 18.498 80.203 1.00 28.23 A C ANISOU 4130 C VAL B 151 4224 3619 2881 383 166 -245 A C ATOM 4131 O VAL B 151 6.851 17.359 79.702 1.00 27.65 A O ANISOU 4131 O VAL B 151 4215 3610 2679 545 -38 -241 A O ATOM 4132 CB VAL B 151 7.783 18.364 82.488 1.00 27.52 A C ANISOU 4132 CB VAL B 151 4131 3326 2996 461 178 -232 A C ATOM 4133 CG1 VAL B 151 8.920 19.335 82.118 1.00 27.66 A C ANISOU 4133 CG1 VAL B 151 3941 3123 3445 406 369 -241 A C ATOM 4134 CG2 VAL B 151 7.506 18.435 83.963 1.00 28.23 A C ANISOU 4134 CG2 VAL B 151 4266 3530 2929 406 129 -505 A C ATOM 4135 N VAL B 152 6.768 19.643 79.516 1.00 28.20 A N ANISOU 4135 N VAL B 152 4239 3713 2762 383 131 -295 A N ATOM 4136 CA VAL B 152 6.986 19.651 78.071 1.00 29.28 A C ANISOU 4136 CA VAL B 152 4256 3844 3022 441 162 -225 A C ATOM 4137 C VAL B 152 8.115 20.623 77.732 1.00 28.51 A C ANISOU 4137 C VAL B 152 4169 3597 3064 519 121 -177 A C ATOM 4138 O VAL B 152 8.414 21.534 78.492 1.00 29.77 A O ANISOU 4138 O VAL B 152 4289 3693 3327 907 295 -215 A O ATOM 4139 CB VAL B 152 5.670 20.020 77.271 1.00 29.64 A C ANISOU 4139 CB VAL B 152 4248 3817 3195 345 120 -151 A C ATOM 4140 CG1 VAL B 152 4.513 19.080 77.608 1.00 30.61 A C ANISOU 4140 CG1 VAL B 152 4219 4115 3296 366 155 -235 A C ATOM 4141 CG2 VAL B 152 5.257 21.462 77.495 1.00 32.05 A C ANISOU 4141 CG2 VAL B 152 4676 3948 3553 275 285 -222 A C ATOM 4142 N ASP B 153 8.737 20.421 76.584 1.00 27.96 A N ANISOU 4142 N ASP B 153 4073 3487 3062 673 200 -184 A N ATOM 4143 CA ASP B 153 9.738 21.347 76.083 1.00 27.85 A C ANISOU 4143 CA ASP B 153 4125 3370 3085 597 242 -117 A C ATOM 4144 C ASP B 153 9.045 22.633 75.609 1.00 28.67 A C ANISOU 4144 C ASP B 153 4157 3484 3251 601 81 -138 A C ATOM 4145 O ASP B 153 7.898 22.604 75.181 1.00 28.86 A O ANISOU 4145 O ASP B 153 4421 3314 3228 685 107 -135 A O ATOM 4146 CB ASP B 153 10.534 20.649 74.979 1.00 29.94 A C ANISOU 4146 CB ASP B 153 4153 3821 3400 424 297 -203 A C ATOM 4147 CG ASP B 153 11.490 19.607 75.550 1.00 31.60 A C ANISOU 4147 CG ASP B 153 4194 4130 3682 336 359 -273 A C ATOM 4148 OD1 ASP B 153 12.499 20.009 76.184 1.00 35.39 A O ANISOU 4148 OD1 ASP B 153 4575 4907 3962 350 72 -288 A O ATOM 4149 OD2 ASP B 153 11.212 18.388 75.417 1.00 35.69 A O1- ANISOU 4149 OD2 ASP B 153 4818 4654 4087 381 393 -51 A O1- ATOM 4150 N GLU B 154 9.740 23.777 75.721 1.00 29.30 A N ANISOU 4150 N GLU B 154 4484 3397 3250 549 15 -50 A N ATOM 4151 CA GLU B 154 9.142 25.057 75.339 1.00 30.32 A C ANISOU 4151 CA GLU B 154 4582 3553 3385 588 -109 0 A C ATOM 4152 C GLU B 154 8.656 25.028 73.896 1.00 30.05 A C ANISOU 4152 C GLU B 154 4534 3623 3261 532 -116 19 A C ATOM 4153 O GLU B 154 7.613 25.627 73.570 1.00 30.03 A O ANISOU 4153 O GLU B 154 4737 3630 3041 637 -203 0 A O ATOM 4154 CB GLU B 154 10.120 26.222 75.568 1.00 31.14 A C ANISOU 4154 CB GLU B 154 4642 3547 3641 537 -144 -109 A C ATOM 4155 CG GLU B 154 9.474 27.570 75.269 1.00 32.09 A C ANISOU 4155 CG GLU B 154 4548 3482 4162 674 -151 116 A C ATOM 4156 CD GLU B 154 10.385 28.757 75.601 1.00 32.25 A C ANISOU 4156 CD GLU B 154 4813 3579 3861 675 -194 66 A C ATOM 4157 OE1 GLU B 154 11.625 28.557 75.748 1.00 33.16 A O ANISOU 4157 OE1 GLU B 154 4798 3993 3809 961 -48 14 A O ATOM 4158 OE2 GLU B 154 9.817 29.868 75.668 1.00 33.35 A O1- ANISOU 4158 OE2 GLU B 154 5308 3505 3857 712 -158 87 A O1- ATOM 4159 N ILE B 155 9.394 24.310 73.053 1.00 30.02 A N ANISOU 4159 N ILE B 155 4566 3745 3094 510 -154 42 A N ATOM 4160 CA ILE B 155 8.993 24.208 71.614 1.00 30.16 A C ANISOU 4160 CA ILE B 155 4514 3811 3133 410 -65 97 A C ATOM 4161 C ILE B 155 7.719 23.414 71.382 1.00 29.53 A C ANISOU 4161 C ILE B 155 4489 3624 3107 384 -25 5 A C ATOM 4162 O ILE B 155 7.201 23.397 70.265 1.00 29.92 A O ANISOU 4162 O ILE B 155 4405 3840 3121 452 -36 -69 A O ATOM 4163 CB ILE B 155 10.122 23.663 70.705 1.00 30.07 A C ANISOU 4163 CB ILE B 155 4396 3754 3274 366 -186 197 A C ATOM 4164 CG1 ILE B 155 10.494 22.224 71.098 1.00 30.99 A C ANISOU 4164 CG1 ILE B 155 4680 3767 3326 346 37 134 A C ATOM 4165 CG2 ILE B 155 11.325 24.597 70.751 1.00 30.87 A C ANISOU 4165 CG2 ILE B 155 4544 3612 3574 544 2 11 A C ATOM 4166 CD1 ILE B 155 11.329 21.473 70.036 1.00 31.91 A C ANISOU 4166 CD1 ILE B 155 4736 4011 3375 335 124 211 A C ATOM 4167 N SER B 156 7.226 22.754 72.431 1.00 28.94 A N ANISOU 4167 N SER B 156 4461 3367 3168 369 85 -27 A N ATOM 4168 CA SER B 156 6.042 21.923 72.368 1.00 29.47 A C ANISOU 4168 CA SER B 156 4465 3411 3320 335 67 5 A C ATOM 4169 C SER B 156 4.882 22.508 73.162 1.00 29.56 A C ANISOU 4169 C SER B 156 4516 3412 3303 371 57 44 A C ATOM 4170 O SER B 156 4.028 21.775 73.614 1.00 28.90 A O ANISOU 4170 O SER B 156 4453 3363 3162 385 34 -86 A O ATOM 4171 CB SER B 156 6.382 20.503 72.900 1.00 30.16 A C ANISOU 4171 CB SER B 156 4502 3366 3588 452 70 37 A C ATOM 4172 OG SER B 156 7.294 19.838 72.014 1.00 32.48 A O ANISOU 4172 OG SER B 156 4794 3559 3987 333 203 -26 A O ATOM 4173 N VAL B 157 4.871 23.822 73.388 1.00 29.44 A N ANISOU 4173 N VAL B 157 4679 3379 3124 280 61 -83 A N ATOM 4174 CA VAL B 157 3.726 24.417 74.087 1.00 30.71 A C ANISOU 4174 CA VAL B 157 4717 3618 3332 250 17 -3 A C ATOM 4175 C VAL B 157 3.414 25.791 73.501 1.00 31.39 A C ANISOU 4175 C VAL B 157 4832 3663 3429 215 56 -87 A C ATOM 4176 O VAL B 157 4.334 26.485 73.088 1.00 30.47 A O ANISOU 4176 O VAL B 157 4820 3371 3383 299 47 -155 A O ATOM 4177 CB VAL B 157 3.979 24.508 75.608 1.00 31.07 A C ANISOU 4177 CB VAL B 157 4650 3819 3333 269 59 -26 A C ATOM 4178 CG1 VAL B 157 5.093 25.548 75.902 1.00 31.87 A C ANISOU 4178 CG1 VAL B 157 4657 4018 3433 385 -18 133 A C ATOM 4179 CG2 VAL B 157 2.669 24.782 76.373 1.00 33.31 A C ANISOU 4179 CG2 VAL B 157 4837 4214 3603 165 103 90 A C ATOM 4180 N ALA B 158 2.127 26.134 73.427 1.00 32.46 A N ANISOU 4180 N ALA B 158 5067 3714 3551 173 17 -79 A N ATOM 4181 CA ALA B 158 1.669 27.417 72.922 1.00 33.43 A C ANISOU 4181 CA ALA B 158 5219 3831 3650 105 -69 -49 A C ATOM 4182 C ALA B 158 0.754 28.122 73.930 1.00 33.35 A C ANISOU 4182 C ALA B 158 5235 3787 3647 190 37 1 A C ATOM 4183 O ALA B 158 -0.152 27.506 74.490 1.00 33.06 A O ANISOU 4183 O ALA B 158 5194 3828 3536 337 -30 29 A O ATOM 4184 CB ALA B 158 0.949 27.231 71.590 1.00 33.71 A C ANISOU 4184 CB ALA B 158 5338 3793 3678 59 -179 -72 A C ATOM 4185 N LYS B 159 1.007 29.407 74.178 1.00 34.77 A N ANISOU 4185 N LYS B 159 5376 3921 3913 227 76 -71 A N ATOM 4186 CA LYS B 159 0.143 30.219 75.026 1.00 35.31 A C ANISOU 4186 CA LYS B 159 5390 3830 4194 172 62 70 A C ATOM 4187 C LYS B 159 -1.124 30.597 74.271 1.00 34.94 A C ANISOU 4187 C LYS B 159 5403 3784 4087 54 122 29 A C ATOM 4188 O LYS B 159 -1.065 30.978 73.100 1.00 35.17 A O ANISOU 4188 O LYS B 159 5476 3748 4139 -14 81 116 A O ATOM 4189 CB LYS B 159 0.900 31.485 75.486 1.00 35.74 A C ANISOU 4189 CB LYS B 159 5458 3918 4203 141 -37 153 A C ATOM 4190 CG LYS B 159 0.046 32.541 76.218 1.00 38.19 A C ANISOU 4190 CG LYS B 159 5678 4119 4713 111 159 92 A C ATOM 4191 CD LYS B 159 0.772 33.882 76.229 1.00 38.95 A C ANISOU 4191 CD LYS B 159 5728 4189 4883 275 -20 251 A C ATOM 4192 CE LYS B 159 0.056 34.864 77.162 1.00 43.28 A C ANISOU 4192 CE LYS B 159 6074 4755 5613 220 243 336 A C ATOM 4193 NZ LYS B 159 0.796 36.158 77.352 1.00 45.50 A N1+ ANISOU 4193 NZ LYS B 159 6473 4791 6021 316 -78 344 A N1+ ATOM 4194 N ILE B 160 -2.273 30.487 74.944 1.00 34.20 A N ANISOU 4194 N ILE B 160 5298 3734 3961 -74 110 32 A N ATOM 4195 CA ILE B 160 -3.550 30.814 74.341 1.00 34.15 A C ANISOU 4195 CA ILE B 160 5279 3788 3908 -161 138 72 A C ATOM 4196 C ILE B 160 -4.285 31.857 75.180 1.00 35.79 A C ANISOU 4196 C ILE B 160 5465 3969 4161 -292 114 136 A C ATOM 4197 O ILE B 160 -3.874 32.162 76.316 1.00 35.69 A O ANISOU 4197 O ILE B 160 5525 3759 4274 -459 59 294 A O ATOM 4198 CB ILE B 160 -4.415 29.546 74.078 1.00 33.64 A C ANISOU 4198 CB ILE B 160 5257 3747 3778 -183 0 6 A C ATOM 4199 CG1 ILE B 160 -4.837 28.864 75.401 1.00 33.58 A C ANISOU 4199 CG1 ILE B 160 5139 3864 3755 -110 199 24 A C ATOM 4200 CG2 ILE B 160 -3.635 28.565 73.181 1.00 33.75 A C ANISOU 4200 CG2 ILE B 160 5343 3861 3618 -84 159 -97 A C ATOM 4201 CD1 ILE B 160 -5.967 27.891 75.278 1.00 33.09 A C ANISOU 4201 CD1 ILE B 160 5262 3763 3544 -114 144 0 A C ATOM 4202 N ASP B 161 -5.348 32.404 74.604 1.00 37.06 A N ANISOU 4202 N ASP B 161 5582 4142 4355 -341 142 102 A N ATOM 4203 CA ASP B 161 -6.186 33.431 75.257 1.00 38.68 A C ANISOU 4203 CA ASP B 161 5821 4366 4509 -349 153 169 A C ATOM 4204 C ASP B 161 -6.602 33.061 76.685 1.00 39.26 A C ANISOU 4204 C ASP B 161 5897 4429 4588 -311 140 162 A C ATOM 4205 O ASP B 161 -7.218 32.027 76.912 1.00 38.94 A O ANISOU 4205 O ASP B 161 5933 4378 4484 -282 87 187 A O ATOM 4206 CB ASP B 161 -7.446 33.657 74.428 1.00 39.82 A C ANISOU 4206 CB ASP B 161 5886 4503 4738 -382 123 75 A C ATOM 4207 CG ASP B 161 -8.246 34.862 74.885 1.00 41.63 A C ANISOU 4207 CG ASP B 161 6017 4744 5054 -422 129 64 A C ATOM 4208 OD1 ASP B 161 -8.791 35.554 74.005 1.00 46.36 A O ANISOU 4208 OD1 ASP B 161 6352 5349 5911 -383 -96 -276 A O ATOM 4209 OD2 ASP B 161 -8.345 35.113 76.100 1.00 43.51 A O1- ANISOU 4209 OD2 ASP B 161 6341 4996 5195 -478 18 -32 A O1- ATOM 4210 N ALA B 162 -6.318 33.946 77.634 1.00 39.76 A N ANISOU 4210 N ALA B 162 5986 4489 4631 -292 86 218 A N ATOM 4211 CA ALA B 162 -6.600 33.636 79.050 1.00 40.16 A C ANISOU 4211 CA ALA B 162 6032 4485 4742 -270 132 211 A C ATOM 4212 C ALA B 162 -8.083 33.380 79.368 1.00 40.59 A C ANISOU 4212 C ALA B 162 6054 4530 4837 -326 128 242 A C ATOM 4213 O ALA B 162 -8.418 32.756 80.382 1.00 39.62 A O ANISOU 4213 O ALA B 162 6099 4193 4763 -374 206 248 A O ATOM 4214 CB ALA B 162 -6.009 34.694 79.957 1.00 40.58 A C ANISOU 4214 CB ALA B 162 6050 4526 4840 -273 95 234 A C ATOM 4215 N ALA B 163 -8.973 33.848 78.500 1.00 41.13 A N ANISOU 4215 N ALA B 163 6040 4630 4956 -317 109 171 A N ATOM 4216 CA ALA B 163 -10.402 33.644 78.703 1.00 41.79 A C ANISOU 4216 CA ALA B 163 5960 4791 5126 -273 152 116 A C ATOM 4217 C ALA B 163 -10.974 32.350 78.089 1.00 41.63 A C ANISOU 4217 C ALA B 163 5875 4817 5124 -271 168 129 A C ATOM 4218 O ALA B 163 -12.186 32.113 78.158 1.00 41.99 A O ANISOU 4218 O ALA B 163 5815 4898 5239 -378 243 120 A O ATOM 4219 CB ALA B 163 -11.182 34.867 78.231 1.00 42.79 A C ANISOU 4219 CB ALA B 163 6065 4885 5309 -219 70 83 A C ATOM 4220 N SER B 164 -10.102 31.501 77.532 1.00 41.34 A N ANISOU 4220 N SER B 164 5822 4808 5077 -254 240 154 A N ATOM 4221 CA SER B 164 -10.511 30.291 76.782 1.00 40.99 A C ANISOU 4221 CA SER B 164 5764 4793 5016 -259 210 213 A C ATOM 4222 C SER B 164 -11.152 29.211 77.657 1.00 39.92 A C ANISOU 4222 C SER B 164 5558 4707 4902 -317 197 215 A C ATOM 4223 O SER B 164 -10.658 28.946 78.745 1.00 39.96 A O ANISOU 4223 O SER B 164 5705 4615 4862 -376 270 191 A O ATOM 4224 CB SER B 164 -9.289 29.656 76.093 1.00 41.08 A C ANISOU 4224 CB SER B 164 5767 4826 5014 -231 217 298 A C ATOM 4225 OG SER B 164 -8.451 30.608 75.472 1.00 43.24 A O ANISOU 4225 OG SER B 164 6222 4984 5223 -117 52 401 A O ATOM 4226 N PRO B 165 -12.252 28.580 77.182 1.00 39.35 A N ANISOU 4226 N PRO B 165 5481 4677 4791 -345 203 166 A N ATOM 4227 CA PRO B 165 -12.798 27.426 77.905 1.00 38.35 A C ANISOU 4227 CA PRO B 165 5314 4651 4606 -341 196 130 A C ATOM 4228 C PRO B 165 -11.951 26.208 77.584 1.00 37.88 A C ANISOU 4228 C PRO B 165 5316 4598 4476 -345 167 60 A C ATOM 4229 O PRO B 165 -12.044 25.658 76.481 1.00 37.60 A O ANISOU 4229 O PRO B 165 5382 4620 4282 -334 308 49 A O ATOM 4230 CB PRO B 165 -14.225 27.303 77.343 1.00 38.50 A C ANISOU 4230 CB PRO B 165 5360 4565 4702 -304 179 122 A C ATOM 4231 CG PRO B 165 -14.145 27.874 76.001 1.00 38.64 A C ANISOU 4231 CG PRO B 165 5340 4700 4640 -401 100 178 A C ATOM 4232 CD PRO B 165 -13.067 28.913 75.997 1.00 38.52 A C ANISOU 4232 CD PRO B 165 5364 4633 4639 -382 180 156 A C ATOM 4233 N LEU B 166 -11.108 25.797 78.531 1.00 37.85 A N ANISOU 4233 N LEU B 166 5176 4709 4496 -405 182 108 A N ATOM 4234 CA LEU B 166 -10.112 24.745 78.244 1.00 37.35 A C ANISOU 4234 CA LEU B 166 5124 4697 4367 -400 182 25 A C ATOM 4235 C LEU B 166 -10.752 23.379 77.941 1.00 37.27 A C ANISOU 4235 C LEU B 166 5176 4658 4327 -360 234 -33 A C ATOM 4236 O LEU B 166 -10.208 22.574 77.159 1.00 36.45 A O ANISOU 4236 O LEU B 166 5128 4685 4035 -380 369 -102 A O ATOM 4237 CB LEU B 166 -9.103 24.634 79.398 1.00 36.30 A C ANISOU 4237 CB LEU B 166 4964 4592 4236 -426 135 18 A C ATOM 4238 CG LEU B 166 -8.222 25.873 79.625 1.00 36.18 A C ANISOU 4238 CG LEU B 166 5023 4565 4159 -402 138 -25 A C ATOM 4239 CD1 LEU B 166 -7.184 25.604 80.693 1.00 36.50 A C ANISOU 4239 CD1 LEU B 166 4928 4300 4640 -394 -200 101 A C ATOM 4240 CD2 LEU B 166 -7.554 26.422 78.338 1.00 35.70 A C ANISOU 4240 CD2 LEU B 166 4908 4321 4334 -568 146 -216 A C ATOM 4241 N GLU B 167 -11.927 23.134 78.522 1.00 37.37 A N ANISOU 4241 N GLU B 167 5197 4761 4238 -396 249 -84 A N ATOM 4242 CA GLU B 167 -12.666 21.903 78.278 1.00 38.71 A C ANISOU 4242 CA GLU B 167 5364 4898 4443 -335 160 -143 A C ATOM 4243 C GLU B 167 -13.164 21.756 76.842 1.00 38.21 A C ANISOU 4243 C GLU B 167 5342 4763 4411 -342 110 -97 A C ATOM 4244 O GLU B 167 -13.575 20.678 76.444 1.00 38.75 A O ANISOU 4244 O GLU B 167 5447 4739 4535 -333 57 -280 A O ATOM 4245 CB GLU B 167 -13.852 21.761 79.254 1.00 40.05 A C ANISOU 4245 CB GLU B 167 5462 5098 4656 -322 245 6 A C ATOM 4246 CG GLU B 167 -14.561 23.076 79.561 1.00 44.94 A C ANISOU 4246 CG GLU B 167 6027 5580 5466 -415 257 -46 A C ATOM 4247 CD GLU B 167 -13.784 23.914 80.579 1.00 48.86 A C ANISOU 4247 CD GLU B 167 6568 6000 5996 -185 327 229 A C ATOM 4248 OE1 GLU B 167 -13.548 23.441 81.719 1.00 52.56 A O ANISOU 4248 OE1 GLU B 167 6981 6378 6609 -383 149 -6 A O ATOM 4249 OE2 GLU B 167 -13.416 25.053 80.244 1.00 50.62 A O1- ANISOU 4249 OE2 GLU B 167 6815 6270 6148 -141 733 119 A O1- ATOM 4250 N LYS B 168 -13.150 22.858 76.094 1.00 37.30 A N ANISOU 4250 N LYS B 168 5333 4626 4211 -327 52 -172 A N ATOM 4251 CA LYS B 168 -13.532 22.853 74.671 1.00 36.71 A C ANISOU 4251 CA LYS B 168 5173 4504 4271 -398 -75 -143 A C ATOM 4252 C LYS B 168 -12.316 22.982 73.772 1.00 35.61 A C ANISOU 4252 C LYS B 168 5147 4253 4127 -405 -130 -143 A C ATOM 4253 O LYS B 168 -12.135 22.204 72.827 1.00 33.99 A O ANISOU 4253 O LYS B 168 5102 3757 4054 -443 -298 -37 A O ATOM 4254 CB LYS B 168 -14.522 23.982 74.376 1.00 38.06 A C ANISOU 4254 CB LYS B 168 5332 4696 4433 -395 -81 -189 A C ATOM 4255 CG LYS B 168 -15.788 23.853 75.229 1.00 39.19 A C ANISOU 4255 CG LYS B 168 5254 4851 4784 -355 49 -111 A C ATOM 4256 CD LYS B 168 -16.942 24.704 74.708 1.00 42.55 A C ANISOU 4256 CD LYS B 168 5373 5279 5514 -437 -42 -160 A C ATOM 4257 CE LYS B 168 -18.172 24.629 75.645 1.00 43.80 A C ANISOU 4257 CE LYS B 168 5587 5515 5540 -305 41 -113 A C ATOM 4258 NZ LYS B 168 -18.090 25.441 76.905 1.00 46.59 A N1+ ANISOU 4258 NZ LYS B 168 5901 5477 6322 -87 -184 92 A N1+ ATOM 4259 N VAL B 169 -11.459 23.951 74.071 1.00 33.94 A N ANISOU 4259 N VAL B 169 5016 3924 3956 -392 -86 -235 A N ATOM 4260 CA VAL B 169 -10.361 24.253 73.145 1.00 34.48 A C ANISOU 4260 CA VAL B 169 5142 4045 3913 -325 -32 -148 A C ATOM 4261 C VAL B 169 -9.243 23.216 73.138 1.00 33.32 A C ANISOU 4261 C VAL B 169 5107 3916 3636 -261 -14 -106 A C ATOM 4262 O VAL B 169 -8.368 23.233 72.262 1.00 33.84 A O ANISOU 4262 O VAL B 169 5303 4012 3541 -362 9 -188 A O ATOM 4263 CB VAL B 169 -9.827 25.710 73.303 1.00 35.21 A C ANISOU 4263 CB VAL B 169 5195 4078 4103 -334 -82 -169 A C ATOM 4264 CG1 VAL B 169 -10.949 26.730 73.059 1.00 36.16 A C ANISOU 4264 CG1 VAL B 169 5113 4308 4315 -434 42 -75 A C ATOM 4265 CG2 VAL B 169 -9.189 25.934 74.648 1.00 35.20 A C ANISOU 4265 CG2 VAL B 169 5221 4039 4114 -225 -106 -105 A C ATOM 4266 N CYS B 170 -9.289 22.266 74.077 1.00 32.32 A N ANISOU 4266 N CYS B 170 5109 3685 3483 -291 -66 -15 A N ATOM 4267 CA CYS B 170 -8.322 21.194 74.043 1.00 32.26 A C ANISOU 4267 CA CYS B 170 5065 3782 3410 -209 -126 -20 A C ATOM 4268 C CYS B 170 -8.388 20.486 72.688 1.00 31.38 A C ANISOU 4268 C CYS B 170 4948 3710 3262 -172 -25 -40 A C ATOM 4269 O CYS B 170 -7.386 19.997 72.246 1.00 31.28 A O ANISOU 4269 O CYS B 170 5094 3641 3146 -174 32 -25 A O ATOM 4270 CB CYS B 170 -8.556 20.204 75.172 1.00 32.93 A C ANISOU 4270 CB CYS B 170 5086 3741 3685 -179 -107 -132 A C ATOM 4271 SG CYS B 170 -10.212 19.566 75.299 1.00 35.00 A S ANISOU 4271 SG CYS B 170 5106 4226 3966 -213 -169 -185 A S ATOM 4272 N LEU B 171 -9.546 20.486 72.034 1.00 31.98 A N ANISOU 4272 N LEU B 171 4943 3918 3287 -157 14 -63 A N ATOM 4273 CA LEU B 171 -9.682 19.840 70.678 1.00 31.17 A C ANISOU 4273 CA LEU B 171 4683 3946 3213 -93 73 22 A C ATOM 4274 C LEU B 171 -8.751 20.448 69.627 1.00 30.70 A C ANISOU 4274 C LEU B 171 4542 3910 3212 -168 112 11 A C ATOM 4275 O LEU B 171 -8.384 19.818 68.621 1.00 31.07 A O ANISOU 4275 O LEU B 171 4752 3985 3066 -231 128 39 A O ATOM 4276 CB LEU B 171 -11.112 19.961 70.140 1.00 32.77 A C ANISOU 4276 CB LEU B 171 4809 4241 3400 -101 3 -83 A C ATOM 4277 CG LEU B 171 -12.167 19.257 71.005 1.00 35.87 A C ANISOU 4277 CG LEU B 171 4836 4654 4139 181 -2 -73 A C ATOM 4278 CD1 LEU B 171 -13.508 19.196 70.313 1.00 38.67 A C ANISOU 4278 CD1 LEU B 171 5047 4968 4676 137 -142 -263 A C ATOM 4279 CD2 LEU B 171 -11.692 17.865 71.377 1.00 39.59 A C ANISOU 4279 CD2 LEU B 171 5239 5113 4688 -80 -285 -15 A C ATOM 4280 N ILE B 172 -8.363 21.680 69.853 1.00 29.58 A N ANISOU 4280 N ILE B 172 4370 3793 3074 -189 276 -63 A N ATOM 4281 CA ILE B 172 -7.411 22.328 68.947 1.00 30.31 A C ANISOU 4281 CA ILE B 172 4446 3772 3296 -42 216 -62 A C ATOM 4282 C ILE B 172 -6.017 21.641 69.029 1.00 29.41 A C ANISOU 4282 C ILE B 172 4419 3685 3068 -33 178 0 A C ATOM 4283 O ILE B 172 -5.196 21.739 68.123 1.00 30.26 A O ANISOU 4283 O ILE B 172 4438 3801 3258 -139 152 -5 A O ATOM 4284 CB ILE B 172 -7.466 23.862 69.161 1.00 30.50 A C ANISOU 4284 CB ILE B 172 4426 3839 3322 -110 189 87 A C ATOM 4285 CG1 ILE B 172 -8.815 24.398 68.631 1.00 31.75 A C ANISOU 4285 CG1 ILE B 172 4731 3726 3607 -116 50 25 A C ATOM 4286 CG2 ILE B 172 -6.309 24.546 68.470 1.00 30.95 A C ANISOU 4286 CG2 ILE B 172 4616 3537 3606 -10 260 -66 A C ATOM 4287 CD1 ILE B 172 -9.169 25.791 69.113 1.00 32.67 A C ANISOU 4287 CD1 ILE B 172 4654 3773 3987 -504 -189 -111 A C ATOM 4288 N GLY B 173 -5.800 20.874 70.098 1.00 28.43 A N ANISOU 4288 N GLY B 173 4314 3541 2946 -80 -39 46 A N ATOM 4289 CA GLY B 173 -4.588 20.129 70.319 1.00 28.50 A C ANISOU 4289 CA GLY B 173 4354 3439 3033 13 -43 95 A C ATOM 4290 C GLY B 173 -4.386 19.005 69.316 1.00 28.17 A C ANISOU 4290 C GLY B 173 4281 3380 3042 91 -77 76 A C ATOM 4291 O GLY B 173 -3.250 18.518 69.142 1.00 29.38 A O ANISOU 4291 O GLY B 173 4450 3516 3196 215 41 58 A O ATOM 4292 N CYS B 174 -5.466 18.552 68.670 1.00 29.25 A N ANISOU 4292 N CYS B 174 4529 3525 3058 141 -54 -135 A N ATOM 4293 CA CYS B 174 -5.278 17.495 67.675 1.00 28.50 A C ANISOU 4293 CA CYS B 174 4421 3466 2939 142 -115 -271 A C ATOM 4294 C CYS B 174 -6.450 17.358 66.723 1.00 28.53 A C ANISOU 4294 C CYS B 174 4278 3569 2992 250 -162 -279 A C ATOM 4295 O CYS B 174 -6.321 17.683 65.530 1.00 29.89 A O ANISOU 4295 O CYS B 174 4345 3976 3035 189 -236 -216 A O ATOM 4296 CB CYS B 174 -4.970 16.095 68.317 1.00 29.73 A C ANISOU 4296 CB CYS B 174 4676 3451 3168 97 -166 -237 A C ATOM 4297 SG CYS B 174 -4.613 14.878 66.905 1.00 29.66 A S ANISOU 4297 SG CYS B 174 4509 3782 2979 163 48 -100 A S ATOM 4298 N GLY B 175 -7.579 16.863 67.205 1.00 29.49 A N ANISOU 4298 N GLY B 175 4365 3831 3009 136 -147 -239 A N ATOM 4299 CA GLY B 175 -8.608 16.394 66.259 1.00 30.09 A C ANISOU 4299 CA GLY B 175 4345 3899 3185 226 -145 -308 A C ATOM 4300 C GLY B 175 -9.209 17.488 65.394 1.00 31.32 A C ANISOU 4300 C GLY B 175 4640 3905 3354 124 -33 -195 A C ATOM 4301 O GLY B 175 -9.325 17.327 64.165 1.00 32.07 A O ANISOU 4301 O GLY B 175 4670 4078 3435 118 40 -377 A O ATOM 4302 N PHE B 176 -9.577 18.606 66.024 1.00 31.67 A N ANISOU 4302 N PHE B 176 4707 3988 3335 -5 25 -146 A N ATOM 4303 CA PHE B 176 -10.189 19.705 65.287 1.00 30.10 A C ANISOU 4303 CA PHE B 176 4618 3786 3029 -50 28 -101 A C ATOM 4304 C PHE B 176 -9.192 20.312 64.300 1.00 30.32 A C ANISOU 4304 C PHE B 176 4643 3760 3116 9 -11 -115 A C ATOM 4305 O PHE B 176 -9.529 20.536 63.122 1.00 30.37 A O ANISOU 4305 O PHE B 176 4700 3966 2871 38 -169 70 A O ATOM 4306 CB PHE B 176 -10.715 20.821 66.192 1.00 31.25 A C ANISOU 4306 CB PHE B 176 4723 4029 3120 -109 163 -182 A C ATOM 4307 CG PHE B 176 -11.117 22.054 65.412 1.00 31.40 A C ANISOU 4307 CG PHE B 176 4890 3894 3144 -328 143 75 A C ATOM 4308 CD1 PHE B 176 -12.335 22.090 64.752 1.00 33.60 A C ANISOU 4308 CD1 PHE B 176 5087 4324 3353 -400 108 -90 A C ATOM 4309 CD2 PHE B 176 -10.243 23.145 65.281 1.00 31.97 A C ANISOU 4309 CD2 PHE B 176 5333 3881 2930 -143 294 -322 A C ATOM 4310 CE1 PHE B 176 -12.699 23.224 63.976 1.00 33.63 A C ANISOU 4310 CE1 PHE B 176 5443 3773 3561 -318 445 -21 A C ATOM 4311 CE2 PHE B 176 -10.617 24.309 64.518 1.00 31.34 A C ANISOU 4311 CE2 PHE B 176 5026 3884 2995 -481 172 141 A C ATOM 4312 CZ PHE B 176 -11.838 24.333 63.893 1.00 32.23 A C ANISOU 4312 CZ PHE B 176 4993 4103 3147 -216 265 -135 A C ATOM 4313 N SER B 177 -7.991 20.638 64.780 1.00 28.62 A N ANISOU 4313 N SER B 177 4462 3558 2854 -50 -31 -140 A N ATOM 4314 CA SER B 177 -6.968 21.281 63.922 1.00 29.50 A C ANISOU 4314 CA SER B 177 4653 3624 2929 0 89 6 A C ATOM 4315 C SER B 177 -6.587 20.406 62.743 1.00 29.00 A C ANISOU 4315 C SER B 177 4562 3613 2841 -56 78 -78 A C ATOM 4316 O SER B 177 -6.345 20.885 61.602 1.00 29.07 A O ANISOU 4316 O SER B 177 4796 3480 2767 -53 208 -314 A O ATOM 4317 CB SER B 177 -5.751 21.619 64.757 1.00 28.05 A C ANISOU 4317 CB SER B 177 4258 3519 2881 -15 223 -10 A C ATOM 4318 OG SER B 177 -6.140 22.562 65.767 1.00 30.05 A O ANISOU 4318 OG SER B 177 5088 3223 3107 254 100 129 A O ATOM 4319 N THR B 178 -6.535 19.116 63.009 1.00 28.81 A N ANISOU 4319 N THR B 178 4517 3564 2862 9 -15 4 A N ATOM 4320 CA THR B 178 -6.121 18.153 61.973 1.00 27.77 A C ANISOU 4320 CA THR B 178 4174 3552 2823 -88 17 -8 A C ATOM 4321 C THR B 178 -7.125 18.155 60.804 1.00 28.68 A C ANISOU 4321 C THR B 178 4226 3726 2943 -5 25 -74 A C ATOM 4322 O THR B 178 -6.733 18.229 59.639 1.00 29.32 A O ANISOU 4322 O THR B 178 4062 3978 3098 22 174 -144 A O ATOM 4323 CB THR B 178 -5.956 16.748 62.574 1.00 27.49 A C ANISOU 4323 CB THR B 178 4083 3547 2813 24 -71 -35 A C ATOM 4324 CG2 THR B 178 -5.737 15.719 61.483 1.00 28.24 A C ANISOU 4324 CG2 THR B 178 4215 3663 2850 72 -62 8 A C ATOM 4325 OG1 THR B 178 -4.811 16.730 63.461 1.00 27.34 A O ANISOU 4325 OG1 THR B 178 4015 3282 3091 -223 -275 25 A O ATOM 4326 N GLY B 179 -8.411 18.048 61.109 1.00 28.65 A N ANISOU 4326 N GLY B 179 4069 3763 3052 -136 -83 -9 A N ATOM 4327 CA GLY B 179 -9.447 18.054 60.054 1.00 29.71 A C ANISOU 4327 CA GLY B 179 4250 3958 3079 9 -117 -51 A C ATOM 4328 C GLY B 179 -9.610 19.437 59.447 1.00 30.39 A C ANISOU 4328 C GLY B 179 4419 4071 3056 -55 -84 -1 A C ATOM 4329 O GLY B 179 -9.597 19.596 58.237 1.00 30.39 A O ANISOU 4329 O GLY B 179 4515 4122 2908 7 -234 -37 A O ATOM 4330 N TYR B 180 -9.723 20.452 60.292 1.00 30.41 A N ANISOU 4330 N TYR B 180 4637 4058 2859 -84 -102 61 A N ATOM 4331 CA TYR B 180 -9.945 21.832 59.838 1.00 30.83 A C ANISOU 4331 CA TYR B 180 4745 4125 2843 -191 25 79 A C ATOM 4332 C TYR B 180 -8.823 22.334 58.916 1.00 30.62 A C ANISOU 4332 C TYR B 180 4669 4108 2855 -221 -16 -7 A C ATOM 4333 O TYR B 180 -9.116 22.842 57.822 1.00 30.86 A O ANISOU 4333 O TYR B 180 4762 4298 2664 -315 -42 4 A O ATOM 4334 CB TYR B 180 -10.087 22.739 61.073 1.00 32.10 A C ANISOU 4334 CB TYR B 180 4942 4122 3133 -212 56 169 A C ATOM 4335 CG TYR B 180 -10.498 24.141 60.774 1.00 34.04 A C ANISOU 4335 CG TYR B 180 5148 4329 3454 -249 60 88 A C ATOM 4336 CD1 TYR B 180 -11.828 24.460 60.516 1.00 35.79 A C ANISOU 4336 CD1 TYR B 180 5497 4376 3725 -325 -188 35 A C ATOM 4337 CD2 TYR B 180 -9.559 25.157 60.793 1.00 33.16 A C ANISOU 4337 CD2 TYR B 180 5279 3702 3617 -281 156 -197 A C ATOM 4338 CE1 TYR B 180 -12.207 25.761 60.265 1.00 35.68 A C ANISOU 4338 CE1 TYR B 180 5756 4348 3451 -257 -24 -152 A C ATOM 4339 CE2 TYR B 180 -9.922 26.465 60.527 1.00 36.61 A C ANISOU 4339 CE2 TYR B 180 5660 4159 4089 -549 164 -207 A C ATOM 4340 CZ TYR B 180 -11.253 26.752 60.273 1.00 35.43 A C ANISOU 4340 CZ TYR B 180 5399 4331 3730 -276 -125 -142 A C ATOM 4341 OH TYR B 180 -11.634 28.052 60.027 1.00 39.70 A O ANISOU 4341 OH TYR B 180 6173 4450 4461 -401 -21 74 A O ATOM 4342 N GLY B 181 -7.562 22.164 59.339 1.00 30.10 A N ANISOU 4342 N GLY B 181 4640 4114 2680 3 -11 125 A N ATOM 4343 CA GLY B 181 -6.389 22.529 58.525 1.00 30.68 A C ANISOU 4343 CA GLY B 181 4588 4139 2927 -77 -24 70 A C ATOM 4344 C GLY B 181 -6.287 21.755 57.225 1.00 30.59 A C ANISOU 4344 C GLY B 181 4662 4055 2905 -20 -5 -37 A C ATOM 4345 O GLY B 181 -5.860 22.300 56.176 1.00 31.87 A O ANISOU 4345 O GLY B 181 4879 4178 3050 -27 33 -173 A O ATOM 4346 N SER B 182 -6.677 20.492 57.250 1.00 29.43 A N ANISOU 4346 N SER B 182 4579 3773 2829 -172 9 -158 A N ATOM 4347 CA SER B 182 -6.620 19.694 56.039 1.00 30.06 A C ANISOU 4347 CA SER B 182 4751 3811 2857 -50 -64 -169 A C ATOM 4348 C SER B 182 -7.430 20.361 54.944 1.00 30.20 A C ANISOU 4348 C SER B 182 4618 3845 3011 -167 -63 -88 A C ATOM 4349 O SER B 182 -7.024 20.355 53.781 1.00 29.95 A O ANISOU 4349 O SER B 182 4418 3874 3086 -51 14 -70 A O ATOM 4350 CB SER B 182 -7.105 18.282 56.306 1.00 30.99 A C ANISOU 4350 CB SER B 182 4948 3782 3043 -146 -124 109 A C ATOM 4351 OG SER B 182 -6.219 17.663 57.196 1.00 32.23 A O ANISOU 4351 OG SER B 182 5233 4077 2933 46 -78 -240 A O ATOM 4352 N ALA B 183 -8.551 20.971 55.318 1.00 30.11 A N ANISOU 4352 N ALA B 183 4580 3808 3051 -231 -115 -160 A N ATOM 4353 CA ALA B 183 -9.361 21.722 54.345 1.00 30.85 A C ANISOU 4353 CA ALA B 183 4649 3882 3191 -263 -28 -132 A C ATOM 4354 C ALA B 183 -8.786 23.105 54.065 1.00 31.93 A C ANISOU 4354 C ALA B 183 4794 4046 3289 -191 30 -161 A C ATOM 4355 O ALA B 183 -8.572 23.470 52.885 1.00 32.15 A O ANISOU 4355 O ALA B 183 4957 4124 3135 -92 -17 -112 A O ATOM 4356 CB ALA B 183 -10.798 21.816 54.845 1.00 31.42 A C ANISOU 4356 CB ALA B 183 4687 4031 3217 -254 32 -230 A C ATOM 4357 N VAL B 184 -8.550 23.889 55.127 1.00 31.40 A N ANISOU 4357 N VAL B 184 4621 3966 3341 -183 -53 -121 A N ATOM 4358 CA VAL B 184 -8.232 25.324 54.973 1.00 34.10 A C ANISOU 4358 CA VAL B 184 4952 4191 3813 -203 79 -122 A C ATOM 4359 C VAL B 184 -6.785 25.590 54.613 1.00 34.56 A C ANISOU 4359 C VAL B 184 5016 4179 3933 -127 39 -214 A C ATOM 4360 O VAL B 184 -6.485 26.575 53.897 1.00 37.06 A O ANISOU 4360 O VAL B 184 5374 4270 4435 -169 138 -363 A O ATOM 4361 CB VAL B 184 -8.691 26.163 56.221 1.00 34.94 A C ANISOU 4361 CB VAL B 184 4860 4206 4207 -209 67 16 A C ATOM 4362 CG1 VAL B 184 -8.291 27.624 56.077 1.00 38.53 A C ANISOU 4362 CG1 VAL B 184 5332 4570 4736 -130 111 -78 A C ATOM 4363 CG2 VAL B 184 -10.188 25.992 56.427 1.00 36.79 A C ANISOU 4363 CG2 VAL B 184 4976 4724 4275 -185 -21 -50 A C ATOM 4364 N LYS B 185 -5.898 24.677 55.010 1.00 34.15 A N ANISOU 4364 N LYS B 185 5015 4119 3838 -120 87 -175 A N ATOM 4365 CA LYS B 185 -4.458 24.868 54.893 1.00 34.10 A C ANISOU 4365 CA LYS B 185 4980 4221 3754 -101 124 -139 A C ATOM 4366 C LYS B 185 -3.791 23.945 53.861 1.00 33.35 A C ANISOU 4366 C LYS B 185 4919 4162 3587 -116 183 -173 A C ATOM 4367 O LYS B 185 -2.978 24.401 53.041 1.00 34.72 A O ANISOU 4367 O LYS B 185 5014 4269 3909 -73 351 -149 A O ATOM 4368 CB LYS B 185 -3.806 24.659 56.262 1.00 35.00 A C ANISOU 4368 CB LYS B 185 5055 4280 3960 -151 25 -273 A C ATOM 4369 CG LYS B 185 -2.307 24.936 56.327 1.00 37.59 A C ANISOU 4369 CG LYS B 185 5187 4625 4469 47 139 -146 A C ATOM 4370 CD LYS B 185 -1.956 26.406 56.149 1.00 41.96 A C ANISOU 4370 CD LYS B 185 5580 4935 5427 62 -24 -254 A C ATOM 4371 CE LYS B 185 -0.523 26.676 56.576 1.00 45.04 A C ANISOU 4371 CE LYS B 185 5707 5680 5725 42 -74 6 A C ATOM 4372 NZ LYS B 185 0.474 25.897 55.765 1.00 47.42 A N1+ ANISOU 4372 NZ LYS B 185 5972 5974 6069 90 121 6 A N1+ ATOM 4373 N VAL B 186 -4.138 22.665 53.895 1.00 32.05 A N ANISOU 4373 N VAL B 186 4788 4129 3261 -176 167 -152 A N ATOM 4374 CA VAL B 186 -3.477 21.666 53.048 1.00 31.69 A C ANISOU 4374 CA VAL B 186 4825 4135 3080 -157 42 -149 A C ATOM 4375 C VAL B 186 -4.118 21.649 51.674 1.00 31.84 A C ANISOU 4375 C VAL B 186 4775 4284 3039 -110 62 -131 A C ATOM 4376 O VAL B 186 -3.424 21.924 50.674 1.00 32.99 A O ANISOU 4376 O VAL B 186 4806 4579 3147 -30 130 -316 A O ATOM 4377 CB VAL B 186 -3.471 20.238 53.704 1.00 30.76 A C ANISOU 4377 CB VAL B 186 4772 4008 2908 -173 96 -123 A C ATOM 4378 CG1 VAL B 186 -2.777 19.229 52.782 1.00 31.21 A C ANISOU 4378 CG1 VAL B 186 4618 4013 3224 -284 6 120 A C ATOM 4379 CG2 VAL B 186 -2.756 20.270 55.080 1.00 30.41 A C ANISOU 4379 CG2 VAL B 186 4579 4052 2921 -144 -63 33 A C ATOM 4380 N ALA B 187 -5.417 21.344 51.624 1.00 31.49 A N ANISOU 4380 N ALA B 187 4692 4295 2978 -211 -64 -162 A N ATOM 4381 CA ALA B 187 -6.166 21.374 50.334 1.00 32.67 A C ANISOU 4381 CA ALA B 187 4729 4379 3306 -156 -107 -168 A C ATOM 4382 C ALA B 187 -6.324 22.789 49.794 1.00 33.23 A C ANISOU 4382 C ALA B 187 4837 4385 3404 -213 -90 -243 A C ATOM 4383 O ALA B 187 -6.321 22.993 48.570 1.00 33.60 A O ANISOU 4383 O ALA B 187 4892 4371 3501 -157 74 -436 A O ATOM 4384 CB ALA B 187 -7.530 20.701 50.465 1.00 32.00 A C ANISOU 4384 CB ALA B 187 4540 4347 3269 -212 -131 -150 A C ATOM 4385 N LYS B 188 -6.497 23.752 50.702 1.00 34.23 A N ANISOU 4385 N LYS B 188 4934 4348 3723 -287 -54 -321 A N ATOM 4386 CA LYS B 188 -6.862 25.130 50.324 1.00 35.11 A C ANISOU 4386 CA LYS B 188 5228 4335 3775 -171 19 -378 A C ATOM 4387 C LYS B 188 -8.153 25.152 49.521 1.00 34.83 A C ANISOU 4387 C LYS B 188 5231 4284 3719 -181 89 -405 A C ATOM 4388 O LYS B 188 -8.189 25.638 48.365 1.00 35.75 A O ANISOU 4388 O LYS B 188 5500 4418 3666 -248 -119 -478 A O ATOM 4389 CB LYS B 188 -5.710 25.833 49.573 1.00 36.45 A C ANISOU 4389 CB LYS B 188 5305 4456 4086 -116 11 -367 A C ATOM 4390 CG LYS B 188 -4.527 26.179 50.464 1.00 39.95 A C ANISOU 4390 CG LYS B 188 5630 4803 4744 -26 -83 -282 A C ATOM 4391 CD LYS B 188 -3.300 26.426 49.610 1.00 43.99 A C ANISOU 4391 CD LYS B 188 5981 5139 5591 206 -8 -232 A C ATOM 4392 CE LYS B 188 -2.222 27.139 50.392 1.00 46.15 A C ANISOU 4392 CE LYS B 188 6439 5436 5659 126 -235 -56 A C ATOM 4393 NZ LYS B 188 -2.151 26.631 51.777 1.00 44.68 A N1+ ANISOU 4393 NZ LYS B 188 6393 5071 5509 515 33 -256 A N1+ ATOM 4394 N VAL B 189 -9.209 24.625 50.133 1.00 34.31 A N ANISOU 4394 N VAL B 189 5345 4127 3565 -234 118 -305 A N ATOM 4395 CA VAL B 189 -10.548 24.683 49.570 1.00 33.70 A C ANISOU 4395 CA VAL B 189 5326 3951 3524 -376 243 -243 A C ATOM 4396 C VAL B 189 -10.914 26.108 49.174 1.00 35.11 A C ANISOU 4396 C VAL B 189 5608 4059 3671 -365 181 -125 A C ATOM 4397 O VAL B 189 -10.639 27.076 49.917 1.00 36.39 A O ANISOU 4397 O VAL B 189 5990 4204 3629 -453 299 0 A O ATOM 4398 CB VAL B 189 -11.562 24.102 50.560 1.00 33.90 A C ANISOU 4398 CB VAL B 189 5294 3989 3595 -296 258 -165 A C ATOM 4399 CG1 VAL B 189 -12.985 24.232 50.037 1.00 31.45 A C ANISOU 4399 CG1 VAL B 189 5196 3667 3085 -607 201 -122 A C ATOM 4400 CG2 VAL B 189 -11.233 22.665 50.802 1.00 32.14 A C ANISOU 4400 CG2 VAL B 189 4962 3921 3328 -550 358 -340 A C ATOM 4401 N THR B 190 -11.491 26.217 47.981 1.00 35.07 A N ANISOU 4401 N THR B 190 5643 4057 3624 -503 198 -172 A N ATOM 4402 CA THR B 190 -11.868 27.497 47.391 1.00 35.45 A C ANISOU 4402 CA THR B 190 5676 4043 3751 -432 192 -215 A C ATOM 4403 C THR B 190 -13.386 27.712 47.463 1.00 36.78 A C ANISOU 4403 C THR B 190 5685 4265 4025 -390 199 -189 A C ATOM 4404 O THR B 190 -14.162 26.746 47.506 1.00 37.28 A O ANISOU 4404 O THR B 190 5711 4408 4046 -464 255 -106 A O ATOM 4405 CB THR B 190 -11.419 27.576 45.904 1.00 36.21 A C ANISOU 4405 CB THR B 190 5732 4183 3841 -359 221 -212 A C ATOM 4406 CG2 THR B 190 -9.917 27.694 45.799 1.00 36.01 A C ANISOU 4406 CG2 THR B 190 5519 4108 4054 -239 87 -306 A C ATOM 4407 OG1 THR B 190 -11.826 26.397 45.201 1.00 34.68 A O ANISOU 4407 OG1 THR B 190 5959 3659 3557 -414 55 -457 A O ATOM 4408 N GLN B 191 -13.795 28.983 47.440 1.00 37.59 A N ANISOU 4408 N GLN B 191 5680 4320 4281 -498 180 -109 A N ATOM 4409 CA GLN B 191 -15.210 29.390 47.365 1.00 38.83 A C ANISOU 4409 CA GLN B 191 5748 4449 4553 -448 173 -160 A C ATOM 4410 C GLN B 191 -15.977 28.758 46.202 1.00 37.87 A C ANISOU 4410 C GLN B 191 5632 4310 4446 -577 198 -139 A C ATOM 4411 O GLN B 191 -15.496 28.710 45.049 1.00 39.52 A O ANISOU 4411 O GLN B 191 5905 4529 4580 -568 197 -279 A O ATOM 4412 CB GLN B 191 -15.328 30.925 47.306 1.00 39.08 A C ANISOU 4412 CB GLN B 191 5796 4428 4625 -517 226 -97 A C ATOM 4413 CG GLN B 191 -14.973 31.641 48.614 1.00 43.88 A C ANISOU 4413 CG GLN B 191 6247 5112 5313 -153 -67 -64 A C ATOM 4414 CD GLN B 191 -14.299 32.995 48.402 1.00 48.70 A C ANISOU 4414 CD GLN B 191 6770 5645 6087 73 104 -21 A C ATOM 4415 NE2 GLN B 191 -13.858 33.260 47.176 1.00 50.17 A N ANISOU 4415 NE2 GLN B 191 6811 6030 6218 -15 174 -15 A N ATOM 4416 OE1 GLN B 191 -14.165 33.787 49.343 1.00 52.20 A O ANISOU 4416 OE1 GLN B 191 7129 6099 6603 -109 158 204 A O ATOM 4417 N GLY B 192 -17.152 28.228 46.514 1.00 37.15 A N ANISOU 4417 N GLY B 192 5503 4231 4381 -688 130 -108 A N ATOM 4418 CA GLY B 192 -18.018 27.616 45.519 1.00 36.55 A C ANISOU 4418 CA GLY B 192 5353 4221 4312 -784 92 -70 A C ATOM 4419 C GLY B 192 -17.626 26.229 45.021 1.00 35.81 A C ANISOU 4419 C GLY B 192 5192 4220 4193 -821 55 -31 A C ATOM 4420 O GLY B 192 -18.291 25.687 44.129 1.00 35.34 A O ANISOU 4420 O GLY B 192 5170 4187 4069 -996 90 -61 A O ATOM 4421 N SER B 193 -16.585 25.642 45.617 1.00 34.83 A N ANISOU 4421 N SER B 193 5181 4105 3946 -814 58 -144 A N ATOM 4422 CA SER B 193 -16.096 24.328 45.180 1.00 34.12 A C ANISOU 4422 CA SER B 193 4946 4165 3852 -821 67 -148 A C ATOM 4423 C SER B 193 -16.970 23.203 45.735 1.00 33.65 A C ANISOU 4423 C SER B 193 4857 4129 3798 -854 2 -219 A C ATOM 4424 O SER B 193 -17.812 23.443 46.604 1.00 34.16 A O ANISOU 4424 O SER B 193 4961 4199 3819 -934 146 -256 A O ATOM 4425 CB SER B 193 -14.637 24.145 45.591 1.00 34.56 A C ANISOU 4425 CB SER B 193 5063 4177 3890 -829 -47 -164 A C ATOM 4426 OG SER B 193 -14.526 24.059 47.002 1.00 33.96 A O ANISOU 4426 OG SER B 193 5273 4012 3614 -836 -98 123 A O ATOM 4427 N THR B 194 -16.761 21.988 45.235 1.00 31.56 A N ANISOU 4427 N THR B 194 4550 4006 3436 -890 -129 -238 A N ATOM 4428 CA THR B 194 -17.474 20.799 45.681 1.00 31.97 A C ANISOU 4428 CA THR B 194 4371 4087 3686 -947 -144 -243 A C ATOM 4429 C THR B 194 -16.438 19.932 46.384 1.00 31.07 A C ANISOU 4429 C THR B 194 4221 4035 3547 -895 -134 -271 A C ATOM 4430 O THR B 194 -15.372 19.675 45.831 1.00 30.17 A O ANISOU 4430 O THR B 194 4041 3822 3599 -1189 -183 -394 A O ATOM 4431 CB THR B 194 -18.135 20.018 44.492 1.00 31.92 A C ANISOU 4431 CB THR B 194 4334 4077 3717 -944 -172 -254 A C ATOM 4432 CG2 THR B 194 -18.672 18.668 44.936 1.00 31.90 A C ANISOU 4432 CG2 THR B 194 4018 4249 3853 -919 -51 -193 A C ATOM 4433 OG1 THR B 194 -19.206 20.791 43.923 1.00 35.14 A O ANISOU 4433 OG1 THR B 194 4789 4508 4054 -992 -484 -369 A O ATOM 4434 N CYS B 195 -16.767 19.502 47.592 1.00 30.22 A N ANISOU 4434 N CYS B 195 4104 4050 3327 -907 -147 -238 A N ATOM 4435 CA CYS B 195 -15.871 18.702 48.440 1.00 30.40 A C ANISOU 4435 CA CYS B 195 4194 4073 3280 -873 -142 -114 A C ATOM 4436 C CYS B 195 -16.538 17.385 48.778 1.00 29.92 A C ANISOU 4436 C CYS B 195 4014 4169 3184 -732 -162 -118 A C ATOM 4437 O CYS B 195 -17.765 17.331 48.905 1.00 30.82 A O ANISOU 4437 O CYS B 195 4116 4298 3295 -910 -214 -58 A O ATOM 4438 CB CYS B 195 -15.566 19.448 49.743 1.00 30.92 A C ANISOU 4438 CB CYS B 195 4314 4148 3285 -774 -192 -163 A C ATOM 4439 SG CYS B 195 -14.618 20.952 49.548 1.00 32.91 A S ANISOU 4439 SG CYS B 195 4854 4173 3475 -973 97 168 A S ATOM 4440 N ALA B 196 -15.734 16.325 48.950 1.00 28.34 A N ANISOU 4440 N ALA B 196 3687 4135 2945 -730 -69 -166 A N ATOM 4441 CA ALA B 196 -16.237 15.022 49.409 1.00 28.14 A C ANISOU 4441 CA ALA B 196 3586 4143 2963 -646 -320 -105 A C ATOM 4442 C ALA B 196 -15.391 14.590 50.589 1.00 27.52 A C ANISOU 4442 C ALA B 196 3356 4126 2974 -560 -214 -160 A C ATOM 4443 O ALA B 196 -14.162 14.589 50.485 1.00 28.17 A O ANISOU 4443 O ALA B 196 3197 4368 3138 -651 -250 -287 A O ATOM 4444 CB ALA B 196 -16.136 13.984 48.298 1.00 29.72 A C ANISOU 4444 CB ALA B 196 3890 4279 3120 -635 -231 -6 A C ATOM 4445 N VAL B 197 -16.048 14.196 51.685 1.00 27.31 A N ANISOU 4445 N VAL B 197 3286 4047 3042 -537 -222 -173 A N ATOM 4446 CA VAL B 197 -15.354 13.882 52.924 1.00 28.05 A C ANISOU 4446 CA VAL B 197 3395 4168 3094 -338 -197 -81 A C ATOM 4447 C VAL B 197 -15.673 12.440 53.285 1.00 28.00 A C ANISOU 4447 C VAL B 197 3359 4133 3144 -292 -209 -167 A C ATOM 4448 O VAL B 197 -16.828 12.130 53.588 1.00 28.79 A O ANISOU 4448 O VAL B 197 3396 4192 3351 -265 -133 -141 A O ATOM 4449 CB VAL B 197 -15.790 14.790 54.087 1.00 27.46 A C ANISOU 4449 CB VAL B 197 3203 4075 3152 -342 -244 -91 A C ATOM 4450 CG1 VAL B 197 -15.049 14.361 55.390 1.00 28.25 A C ANISOU 4450 CG1 VAL B 197 3494 4095 3145 -598 -286 125 A C ATOM 4451 CG2 VAL B 197 -15.522 16.207 53.750 1.00 29.73 A C ANISOU 4451 CG2 VAL B 197 4064 4037 3194 -472 -85 208 A C ATOM 4452 N PHE B 198 -14.653 11.576 53.282 1.00 29.28 A N ANISOU 4452 N PHE B 198 3448 4314 3363 -196 -74 -127 A N ATOM 4453 CA PHE B 198 -14.851 10.144 53.541 1.00 29.50 A C ANISOU 4453 CA PHE B 198 3474 4486 3248 -128 -73 -214 A C ATOM 4454 C PHE B 198 -14.507 9.857 55.001 1.00 29.40 A C ANISOU 4454 C PHE B 198 3413 4507 3248 -47 -95 -281 A C ATOM 4455 O PHE B 198 -13.314 9.806 55.380 1.00 30.31 A O ANISOU 4455 O PHE B 198 3292 4774 3450 30 78 -415 A O ATOM 4456 CB PHE B 198 -13.942 9.306 52.633 1.00 30.01 A C ANISOU 4456 CB PHE B 198 3378 4623 3399 -17 -133 -100 A C ATOM 4457 CG PHE B 198 -14.343 9.321 51.182 1.00 30.52 A C ANISOU 4457 CG PHE B 198 3576 4654 3363 -129 -36 -135 A C ATOM 4458 CD1 PHE B 198 -13.967 10.372 50.357 1.00 29.88 A C ANISOU 4458 CD1 PHE B 198 3587 4506 3258 -54 -149 -86 A C ATOM 4459 CD2 PHE B 198 -15.084 8.267 50.652 1.00 30.72 A C ANISOU 4459 CD2 PHE B 198 3487 4664 3519 -161 -259 -221 A C ATOM 4460 CE1 PHE B 198 -14.332 10.401 49.010 1.00 30.68 A C ANISOU 4460 CE1 PHE B 198 3709 4689 3258 12 -54 -272 A C ATOM 4461 CE2 PHE B 198 -15.451 8.269 49.310 1.00 31.05 A C ANISOU 4461 CE2 PHE B 198 3712 4722 3363 17 -191 -244 A C ATOM 4462 CZ PHE B 198 -15.061 9.351 48.487 1.00 31.41 A C ANISOU 4462 CZ PHE B 198 3711 4782 3439 -26 -104 -192 A C ATOM 4463 N GLY B 199 -15.559 9.681 55.795 1.00 29.78 A N ANISOU 4463 N GLY B 199 3541 4596 3179 -14 -69 -263 A N ATOM 4464 CA GLY B 199 -15.484 9.450 57.226 1.00 29.81 A C ANISOU 4464 CA GLY B 199 3750 4437 3140 -85 -36 -290 A C ATOM 4465 C GLY B 199 -16.066 10.618 58.005 1.00 30.78 A C ANISOU 4465 C GLY B 199 3862 4448 3384 -91 -22 -274 A C ATOM 4466 O GLY B 199 -15.635 11.763 57.836 1.00 31.53 A O ANISOU 4466 O GLY B 199 4009 4393 3576 -182 203 -216 A O ATOM 4467 N LEU B 200 -17.049 10.328 58.853 1.00 29.75 A N ANISOU 4467 N LEU B 200 3770 4431 3099 -148 -72 -242 A N ATOM 4468 CA LEU B 200 -17.788 11.367 59.553 1.00 30.82 A C ANISOU 4468 CA LEU B 200 3964 4360 3384 -99 -52 -213 A C ATOM 4469 C LEU B 200 -17.707 11.268 61.085 1.00 30.49 A C ANISOU 4469 C LEU B 200 3821 4363 3400 -103 6 -163 A C ATOM 4470 O LEU B 200 -18.626 11.693 61.812 1.00 31.34 A O ANISOU 4470 O LEU B 200 3824 4575 3506 -179 94 -177 A O ATOM 4471 CB LEU B 200 -19.247 11.422 59.052 1.00 31.00 A C ANISOU 4471 CB LEU B 200 4114 4338 3326 -73 -152 -222 A C ATOM 4472 CG LEU B 200 -19.405 11.650 57.545 1.00 31.61 A C ANISOU 4472 CG LEU B 200 4374 4257 3379 187 -156 -175 A C ATOM 4473 CD1 LEU B 200 -20.894 11.548 57.120 1.00 33.59 A C ANISOU 4473 CD1 LEU B 200 4453 4651 3656 24 -132 -225 A C ATOM 4474 CD2 LEU B 200 -18.815 12.993 57.175 1.00 31.67 A C ANISOU 4474 CD2 LEU B 200 4279 4323 3432 304 143 -275 A C ATOM 4475 N GLY B 201 -16.599 10.699 61.562 1.00 31.27 A N ANISOU 4475 N GLY B 201 3958 4426 3497 -136 -70 -164 A N ATOM 4476 CA GLY B 201 -16.120 10.918 62.928 1.00 31.34 A C ANISOU 4476 CA GLY B 201 3921 4397 3589 -94 54 -151 A C ATOM 4477 C GLY B 201 -15.646 12.341 63.180 1.00 32.06 A C ANISOU 4477 C GLY B 201 3981 4522 3678 -16 70 -231 A C ATOM 4478 O GLY B 201 -15.837 13.234 62.352 1.00 32.50 A O ANISOU 4478 O GLY B 201 3839 4520 3988 -23 130 -387 A O ATOM 4479 N GLY B 202 -15.021 12.540 64.333 1.00 31.27 A N ANISOU 4479 N GLY B 202 3892 4402 3586 -4 34 -78 A N ATOM 4480 CA GLY B 202 -14.656 13.881 64.803 1.00 30.51 A C ANISOU 4480 CA GLY B 202 3908 4298 3384 52 111 -112 A C ATOM 4481 C GLY B 202 -13.742 14.600 63.836 1.00 30.22 A C ANISOU 4481 C GLY B 202 3904 4276 3299 -40 83 -74 A C ATOM 4482 O GLY B 202 -13.920 15.789 63.601 1.00 30.49 A O ANISOU 4482 O GLY B 202 3975 4440 3169 -121 81 -113 A O ATOM 4483 N VAL B 203 -12.774 13.877 63.267 1.00 29.46 A N ANISOU 4483 N VAL B 203 3762 4195 3233 -74 42 -95 A N ATOM 4484 CA VAL B 203 -11.822 14.493 62.343 1.00 29.50 A C ANISOU 4484 CA VAL B 203 3903 4160 3144 -165 36 -143 A C ATOM 4485 C VAL B 203 -12.565 14.867 61.046 1.00 29.18 A C ANISOU 4485 C VAL B 203 3787 4245 3054 -114 21 -86 A C ATOM 4486 O VAL B 203 -12.389 15.998 60.541 1.00 30.41 A O ANISOU 4486 O VAL B 203 4048 4383 3122 -196 54 2 A O ATOM 4487 CB VAL B 203 -10.567 13.647 62.115 1.00 29.58 A C ANISOU 4487 CB VAL B 203 3825 4298 3115 -88 123 -209 A C ATOM 4488 CG1 VAL B 203 -9.607 14.375 61.159 1.00 31.18 A C ANISOU 4488 CG1 VAL B 203 3957 4338 3551 36 205 -167 A C ATOM 4489 CG2 VAL B 203 -9.845 13.328 63.457 1.00 31.47 A C ANISOU 4489 CG2 VAL B 203 3916 4362 3678 -136 -76 -150 A C ATOM 4490 N GLY B 204 -13.449 13.982 60.571 1.00 29.50 A N ANISOU 4490 N GLY B 204 4004 4201 3003 -276 35 -16 A N ATOM 4491 CA GLY B 204 -14.229 14.263 59.345 1.00 29.41 A C ANISOU 4491 CA GLY B 204 3842 4256 3074 -266 -11 47 A C ATOM 4492 C GLY B 204 -15.173 15.447 59.521 1.00 29.68 A C ANISOU 4492 C GLY B 204 3872 4361 3043 -333 63 -66 A C ATOM 4493 O GLY B 204 -15.335 16.289 58.608 1.00 30.52 A O ANISOU 4493 O GLY B 204 3943 4438 3214 -318 104 8 A O ATOM 4494 N LEU B 205 -15.814 15.525 60.688 1.00 29.66 A N ANISOU 4494 N LEU B 205 3901 4411 2956 -329 32 -61 A N ATOM 4495 CA LEU B 205 -16.646 16.688 60.983 1.00 30.08 A C ANISOU 4495 CA LEU B 205 3924 4527 2976 -285 199 -85 A C ATOM 4496 C LEU B 205 -15.813 17.962 60.967 1.00 29.59 A C ANISOU 4496 C LEU B 205 3982 4484 2775 -304 99 -76 A C ATOM 4497 O LEU B 205 -16.291 18.982 60.527 1.00 30.76 A O ANISOU 4497 O LEU B 205 4063 4691 2931 -368 162 53 A O ATOM 4498 CB LEU B 205 -17.339 16.554 62.343 1.00 30.58 A C ANISOU 4498 CB LEU B 205 4046 4582 2990 -301 125 -156 A C ATOM 4499 CG LEU B 205 -18.368 15.428 62.395 1.00 30.73 A C ANISOU 4499 CG LEU B 205 4220 4456 3000 -192 135 -262 A C ATOM 4500 CD1 LEU B 205 -18.896 15.333 63.841 1.00 32.53 A C ANISOU 4500 CD1 LEU B 205 4455 4754 3149 -118 268 -391 A C ATOM 4501 CD2 LEU B 205 -19.517 15.625 61.401 1.00 32.54 A C ANISOU 4501 CD2 LEU B 205 4266 4786 3309 -170 80 -145 A C ATOM 4502 N SER B 206 -14.574 17.892 61.474 1.00 29.62 A N ANISOU 4502 N SER B 206 3983 4608 2660 -214 166 7 A N ATOM 4503 CA SER B 206 -13.681 19.032 61.462 1.00 29.77 A C ANISOU 4503 CA SER B 206 4103 4543 2664 -301 94 -23 A C ATOM 4504 C SER B 206 -13.289 19.432 60.020 1.00 29.49 A C ANISOU 4504 C SER B 206 4159 4409 2637 -303 48 -36 A C ATOM 4505 O SER B 206 -13.130 20.619 59.707 1.00 30.99 A O ANISOU 4505 O SER B 206 4532 4481 2762 -473 141 75 A O ATOM 4506 CB SER B 206 -12.464 18.755 62.362 1.00 29.19 A C ANISOU 4506 CB SER B 206 4100 4566 2424 -125 32 -117 A C ATOM 4507 OG SER B 206 -12.897 18.594 63.717 1.00 32.61 A O ANISOU 4507 OG SER B 206 4363 4920 3105 -290 230 76 A O ATOM 4508 N VAL B 207 -13.112 18.445 59.150 1.00 29.59 A N ANISOU 4508 N VAL B 207 4256 4448 2538 -347 46 -32 A N ATOM 4509 CA VAL B 207 -12.853 18.740 57.729 1.00 28.99 A C ANISOU 4509 CA VAL B 207 4141 4339 2533 -457 -108 -77 A C ATOM 4510 C VAL B 207 -14.066 19.485 57.150 1.00 29.41 A C ANISOU 4510 C VAL B 207 4215 4291 2667 -396 -87 -160 A C ATOM 4511 O VAL B 207 -13.904 20.489 56.447 1.00 29.29 A O ANISOU 4511 O VAL B 207 4297 4020 2810 -408 0 -116 A O ATOM 4512 CB VAL B 207 -12.563 17.454 56.907 1.00 28.42 A C ANISOU 4512 CB VAL B 207 4092 4290 2414 -473 -83 -115 A C ATOM 4513 CG1 VAL B 207 -12.449 17.828 55.414 1.00 29.72 A C ANISOU 4513 CG1 VAL B 207 4412 4545 2335 -635 -120 -201 A C ATOM 4514 CG2 VAL B 207 -11.290 16.783 57.368 1.00 31.12 A C ANISOU 4514 CG2 VAL B 207 4167 4644 3011 -490 -55 23 A C ATOM 4515 N ILE B 208 -15.269 18.996 57.442 1.00 29.41 A N ANISOU 4515 N ILE B 208 4168 4234 2772 -379 -66 -236 A N ATOM 4516 CA ILE B 208 -16.509 19.642 56.966 1.00 30.34 A C ANISOU 4516 CA ILE B 208 4271 4279 2975 -431 -15 -236 A C ATOM 4517 C ILE B 208 -16.557 21.107 57.434 1.00 31.75 A C ANISOU 4517 C ILE B 208 4573 4422 3067 -482 47 -159 A C ATOM 4518 O ILE B 208 -16.811 22.035 56.642 1.00 32.87 A O ANISOU 4518 O ILE B 208 4895 4504 3090 -626 154 22 A O ATOM 4519 CB ILE B 208 -17.767 18.858 57.398 1.00 30.89 A C ANISOU 4519 CB ILE B 208 4215 4372 3147 -510 -87 -225 A C ATOM 4520 CG1 ILE B 208 -17.813 17.513 56.672 1.00 30.90 A C ANISOU 4520 CG1 ILE B 208 4437 4383 2918 -336 40 -223 A C ATOM 4521 CG2 ILE B 208 -19.044 19.672 57.098 1.00 31.48 A C ANISOU 4521 CG2 ILE B 208 4070 4654 3236 -635 3 -108 A C ATOM 4522 CD1 ILE B 208 -18.864 16.514 57.184 1.00 30.87 A C ANISOU 4522 CD1 ILE B 208 4221 4165 3343 -441 26 -304 A C ATOM 4523 N MET B 209 -16.279 21.319 58.716 1.00 32.80 A N ANISOU 4523 N MET B 209 4744 4472 3245 -362 25 -59 A N ATOM 4524 CA MET B 209 -16.172 22.650 59.259 1.00 34.70 A C ANISOU 4524 CA MET B 209 5060 4692 3431 -354 55 -54 A C ATOM 4525 C MET B 209 -15.232 23.553 58.450 1.00 33.75 A C ANISOU 4525 C MET B 209 4993 4511 3317 -300 34 -12 A C ATOM 4526 O MET B 209 -15.584 24.701 58.184 1.00 35.09 A O ANISOU 4526 O MET B 209 5113 4756 3463 -374 -12 -103 A O ATOM 4527 CB MET B 209 -15.757 22.595 60.727 1.00 35.43 A C ANISOU 4527 CB MET B 209 5167 4741 3551 -364 37 -76 A C ATOM 4528 CG MET B 209 -16.899 22.145 61.604 1.00 35.83 A C ANISOU 4528 CG MET B 209 5159 4908 3547 -452 2 -168 A C ATOM 4529 SD MET B 209 -16.370 22.203 63.292 1.00 37.57 A S ANISOU 4529 SD MET B 209 5457 5370 3447 -571 265 -83 A S ATOM 4530 CE MET B 209 -17.809 21.513 64.107 1.00 40.17 A C ANISOU 4530 CE MET B 209 5382 5581 4299 -353 330 51 A C ATOM 4531 N GLY B 210 -14.060 23.032 58.079 1.00 34.39 A N ANISOU 4531 N GLY B 210 4981 4515 3567 -207 28 -80 A N ATOM 4532 CA GLY B 210 -13.046 23.750 57.277 1.00 33.11 A C ANISOU 4532 CA GLY B 210 4935 4280 3365 -298 63 -145 A C ATOM 4533 C GLY B 210 -13.486 24.060 55.861 1.00 33.56 A C ANISOU 4533 C GLY B 210 5011 4213 3527 -366 78 -179 A C ATOM 4534 O GLY B 210 -13.235 25.171 55.333 1.00 33.77 A O ANISOU 4534 O GLY B 210 5093 4135 3600 -414 213 -225 A O ATOM 4535 N CYS B 211 -14.144 23.080 55.246 1.00 32.33 A N ANISOU 4535 N CYS B 211 4860 4121 3300 -460 23 -181 A N ATOM 4536 CA CYS B 211 -14.721 23.255 53.904 1.00 33.38 A C ANISOU 4536 CA CYS B 211 4996 4196 3491 -601 29 -183 A C ATOM 4537 C CYS B 211 -15.783 24.362 53.948 1.00 33.52 A C ANISOU 4537 C CYS B 211 5100 4071 3563 -639 236 -69 A C ATOM 4538 O CYS B 211 -15.870 25.166 53.000 1.00 34.77 A O ANISOU 4538 O CYS B 211 5470 4147 3592 -801 128 -4 A O ATOM 4539 CB CYS B 211 -15.340 21.967 53.417 1.00 31.64 A C ANISOU 4539 CB CYS B 211 4744 4024 3251 -676 99 -215 A C ATOM 4540 SG CYS B 211 -14.132 20.666 53.031 1.00 31.86 A S ANISOU 4540 SG CYS B 211 4788 4227 3088 -934 15 -135 A S ATOM 4541 N LYS B 212 -16.579 24.405 55.027 1.00 35.05 A N ANISOU 4541 N LYS B 212 5283 4250 3784 -596 243 -14 A N ATOM 4542 CA LYS B 212 -17.597 25.439 55.218 1.00 36.64 A C ANISOU 4542 CA LYS B 212 5341 4446 4134 -480 400 -8 A C ATOM 4543 C LYS B 212 -16.945 26.809 55.431 1.00 36.52 A C ANISOU 4543 C LYS B 212 5436 4361 4077 -516 432 115 A C ATOM 4544 O LYS B 212 -17.330 27.772 54.760 1.00 37.21 A O ANISOU 4544 O LYS B 212 5452 4388 4299 -629 502 157 A O ATOM 4545 CB LYS B 212 -18.514 25.083 56.384 1.00 36.16 A C ANISOU 4545 CB LYS B 212 5268 4565 3906 -558 406 115 A C ATOM 4546 CG LYS B 212 -19.563 26.126 56.693 1.00 37.92 A C ANISOU 4546 CG LYS B 212 5247 4655 4503 -518 327 187 A C ATOM 4547 CD LYS B 212 -20.293 25.699 57.944 1.00 39.99 A C ANISOU 4547 CD LYS B 212 5296 4936 4960 -330 368 30 A C ATOM 4548 CE LYS B 212 -21.423 26.668 58.313 1.00 42.30 A C ANISOU 4548 CE LYS B 212 5592 5023 5455 -307 438 454 A C ATOM 4549 NZ LYS B 212 -22.014 26.240 59.608 1.00 44.78 A N1+ ANISOU 4549 NZ LYS B 212 5913 5267 5835 -98 491 154 A N1+ ATOM 4550 N ALA B 213 -15.909 26.857 56.273 1.00 36.29 A N ANISOU 4550 N ALA B 213 5445 4289 4053 -465 508 85 A N ATOM 4551 CA ALA B 213 -15.151 28.093 56.552 1.00 37.02 A C ANISOU 4551 CA ALA B 213 5571 4285 4210 -436 433 67 A C ATOM 4552 C ALA B 213 -14.579 28.696 55.267 1.00 37.71 A C ANISOU 4552 C ALA B 213 5712 4245 4369 -423 489 59 A C ATOM 4553 O ALA B 213 -14.542 29.918 55.095 1.00 38.96 A O ANISOU 4553 O ALA B 213 5939 4243 4619 -544 592 100 A O ATOM 4554 CB ALA B 213 -14.041 27.841 57.578 1.00 36.83 A C ANISOU 4554 CB ALA B 213 5473 4192 4326 -471 437 142 A C ATOM 4555 N ALA B 214 -14.172 27.819 54.354 1.00 36.85 A N ANISOU 4555 N ALA B 214 5682 4183 4136 -491 508 55 A N ATOM 4556 CA ALA B 214 -13.565 28.214 53.089 1.00 37.30 A C ANISOU 4556 CA ALA B 214 5808 4182 4180 -388 415 13 A C ATOM 4557 C ALA B 214 -14.598 28.526 52.033 1.00 37.52 A C ANISOU 4557 C ALA B 214 5831 4289 4134 -393 340 -8 A C ATOM 4558 O ALA B 214 -14.240 28.923 50.903 1.00 38.92 A O ANISOU 4558 O ALA B 214 6149 4417 4220 -194 401 -99 A O ATOM 4559 CB ALA B 214 -12.654 27.111 52.598 1.00 36.01 A C ANISOU 4559 CB ALA B 214 5560 4089 4030 -483 439 -9 A C ATOM 4560 N GLY B 215 -15.867 28.289 52.344 1.00 36.90 A N ANISOU 4560 N GLY B 215 5840 4215 3962 -482 280 16 A N ATOM 4561 CA GLY B 215 -16.969 28.634 51.425 1.00 38.30 A C ANISOU 4561 CA GLY B 215 5869 4427 4254 -623 134 10 A C ATOM 4562 C GLY B 215 -17.312 27.658 50.306 1.00 37.29 A C ANISOU 4562 C GLY B 215 5744 4358 4063 -682 98 -78 A C ATOM 4563 O GLY B 215 -17.850 28.049 49.265 1.00 37.08 A O ANISOU 4563 O GLY B 215 5684 4210 4194 -936 84 -155 A O ATOM 4564 N ALA B 216 -17.028 26.381 50.517 1.00 36.99 A N ANISOU 4564 N ALA B 216 5607 4372 4075 -746 118 -158 A N ATOM 4565 CA ALA B 216 -17.485 25.326 49.609 1.00 35.94 A C ANISOU 4565 CA ALA B 216 5307 4403 3942 -731 95 -222 A C ATOM 4566 C ALA B 216 -18.988 25.406 49.354 1.00 36.21 A C ANISOU 4566 C ALA B 216 5233 4563 3960 -749 69 -198 A C ATOM 4567 O ALA B 216 -19.776 25.683 50.277 1.00 35.89 A O ANISOU 4567 O ALA B 216 5219 4575 3841 -987 209 -144 A O ATOM 4568 CB ALA B 216 -17.069 23.926 50.151 1.00 36.45 A C ANISOU 4568 CB ALA B 216 5274 4417 4159 -666 -30 -274 A C ATOM 4569 N ALA B 217 -19.393 25.275 48.095 1.00 36.47 A N ANISOU 4569 N ALA B 217 5087 4690 4077 -753 5 -169 A N ATOM 4570 CA ALA B 217 -20.822 25.263 47.771 1.00 35.60 A C ANISOU 4570 CA ALA B 217 4843 4703 3980 -705 -102 -225 A C ATOM 4571 C ALA B 217 -21.511 23.919 48.020 1.00 36.09 A C ANISOU 4571 C ALA B 217 4782 4776 4154 -736 -150 -185 A C ATOM 4572 O ALA B 217 -22.726 23.881 48.279 1.00 37.03 A O ANISOU 4572 O ALA B 217 4862 4893 4311 -775 1 -192 A O ATOM 4573 CB ALA B 217 -21.086 25.776 46.317 1.00 36.43 A C ANISOU 4573 CB ALA B 217 4926 4842 4073 -510 -158 -267 A C ATOM 4574 N ARG B 218 -20.742 22.823 47.943 1.00 33.32 A N ANISOU 4574 N ARG B 218 4351 4548 3761 -887 -292 -291 A N ATOM 4575 CA ARG B 218 -21.293 21.478 48.152 1.00 32.69 A C ANISOU 4575 CA ARG B 218 4193 4514 3713 -857 -324 -215 A C ATOM 4576 C ARG B 218 -20.292 20.709 48.966 1.00 31.73 A C ANISOU 4576 C ARG B 218 4112 4432 3512 -809 -270 -252 A C ATOM 4577 O ARG B 218 -19.113 20.776 48.659 1.00 31.91 A O ANISOU 4577 O ARG B 218 4013 4674 3434 -907 -252 -256 A O ATOM 4578 CB ARG B 218 -21.500 20.728 46.830 1.00 33.02 A C ANISOU 4578 CB ARG B 218 4351 4499 3694 -863 -380 -316 A C ATOM 4579 CG ARG B 218 -22.694 21.157 46.024 1.00 35.04 A C ANISOU 4579 CG ARG B 218 4448 4746 4120 -771 -436 -190 A C ATOM 4580 CD ARG B 218 -22.794 20.305 44.789 1.00 36.21 A C ANISOU 4580 CD ARG B 218 4702 4744 4312 -778 -280 -1 A C ATOM 4581 NE ARG B 218 -23.359 18.963 45.027 1.00 36.45 A N ANISOU 4581 NE ARG B 218 4617 4869 4363 -579 -378 -146 A N ATOM 4582 CZ ARG B 218 -23.506 18.045 44.064 1.00 36.61 A C ANISOU 4582 CZ ARG B 218 4587 4893 4428 -641 -251 -187 A C ATOM 4583 NH1 ARG B 218 -23.091 18.302 42.828 1.00 38.25 A N1+ ANISOU 4583 NH1 ARG B 218 4753 5388 4392 -811 -147 -194 A N1+ ATOM 4584 NH2 ARG B 218 -24.024 16.856 44.330 1.00 38.33 A N ANISOU 4584 NH2 ARG B 218 4577 5319 4667 -383 -318 -223 A N ATOM 4585 N ILE B 219 -20.753 20.022 50.000 1.00 30.97 A N ANISOU 4585 N ILE B 219 3965 4349 3453 -773 -261 -172 A N ATOM 4586 CA ILE B 219 -19.872 19.236 50.855 1.00 31.06 A C ANISOU 4586 CA ILE B 219 4061 4355 3385 -655 -227 -201 A C ATOM 4587 C ILE B 219 -20.575 17.932 51.082 1.00 31.13 A C ANISOU 4587 C ILE B 219 3978 4375 3476 -625 -204 -227 A C ATOM 4588 O ILE B 219 -21.577 17.866 51.800 1.00 31.80 A O ANISOU 4588 O ILE B 219 4036 4398 3647 -833 55 -149 A O ATOM 4589 CB ILE B 219 -19.639 19.865 52.222 1.00 31.73 A C ANISOU 4589 CB ILE B 219 4218 4408 3429 -633 -201 -157 A C ATOM 4590 CG1 ILE B 219 -19.018 21.266 52.113 1.00 31.55 A C ANISOU 4590 CG1 ILE B 219 4267 4489 3229 -626 -343 -218 A C ATOM 4591 CG2 ILE B 219 -18.786 18.939 53.057 1.00 31.98 A C ANISOU 4591 CG2 ILE B 219 4168 4501 3479 -521 -328 -253 A C ATOM 4592 CD1 ILE B 219 -19.158 22.074 53.369 1.00 34.39 A C ANISOU 4592 CD1 ILE B 219 5008 4898 3159 -727 -137 -85 A C ATOM 4593 N ILE B 220 -20.052 16.898 50.452 1.00 29.57 A N ANISOU 4593 N ILE B 220 3753 4240 3243 -606 -219 -149 A N ATOM 4594 CA ILE B 220 -20.679 15.592 50.426 1.00 30.69 A C ANISOU 4594 CA ILE B 220 3889 4335 3437 -481 -156 -164 A C ATOM 4595 C ILE B 220 -20.017 14.678 51.464 1.00 30.98 A C ANISOU 4595 C ILE B 220 3853 4485 3430 -422 -138 -237 A C ATOM 4596 O ILE B 220 -18.881 14.260 51.278 1.00 31.55 A O ANISOU 4596 O ILE B 220 3935 4698 3355 -470 -97 -260 A O ATOM 4597 CB ILE B 220 -20.566 14.957 49.006 1.00 30.32 A C ANISOU 4597 CB ILE B 220 3885 4201 3434 -409 -168 -144 A C ATOM 4598 CG1 ILE B 220 -21.126 15.901 47.908 1.00 28.50 A C ANISOU 4598 CG1 ILE B 220 3953 3630 3245 -454 -2 20 A C ATOM 4599 CG2 ILE B 220 -21.291 13.604 48.994 1.00 31.31 A C ANISOU 4599 CG2 ILE B 220 4013 4137 3744 -299 -305 -53 A C ATOM 4600 CD1 ILE B 220 -20.616 15.616 46.460 1.00 31.47 A C ANISOU 4600 CD1 ILE B 220 4029 4316 3610 -523 4 -142 A C ATOM 4601 N GLY B 221 -20.729 14.364 52.546 1.00 31.44 A N ANISOU 4601 N GLY B 221 3855 4665 3425 -351 -157 -218 A N ATOM 4602 CA GLY B 221 -20.204 13.426 53.537 1.00 31.36 A C ANISOU 4602 CA GLY B 221 3690 4775 3450 -215 -202 -262 A C ATOM 4603 C GLY B 221 -20.476 12.000 53.082 1.00 32.47 A C ANISOU 4603 C GLY B 221 3731 4948 3658 -78 -233 -213 A C ATOM 4604 O GLY B 221 -21.583 11.689 52.589 1.00 33.76 A O ANISOU 4604 O GLY B 221 3684 5152 3992 -133 -407 -314 A O ATOM 4605 N VAL B 222 -19.486 11.136 53.250 1.00 31.23 A N ANISOU 4605 N VAL B 222 3468 4860 3539 -12 -139 -206 A N ATOM 4606 CA VAL B 222 -19.538 9.722 52.862 1.00 31.68 A C ANISOU 4606 CA VAL B 222 3507 4830 3700 38 -174 -268 A C ATOM 4607 C VAL B 222 -19.175 8.835 54.060 1.00 31.88 A C ANISOU 4607 C VAL B 222 3529 4789 3792 106 -233 -225 A C ATOM 4608 O VAL B 222 -18.093 8.975 54.654 1.00 30.98 A O ANISOU 4608 O VAL B 222 3401 4599 3772 231 -532 -151 A O ATOM 4609 CB VAL B 222 -18.609 9.395 51.654 1.00 30.72 A C ANISOU 4609 CB VAL B 222 3359 4737 3576 32 -203 -320 A C ATOM 4610 CG1 VAL B 222 -18.804 7.938 51.228 1.00 33.18 A C ANISOU 4610 CG1 VAL B 222 3841 4794 3969 -109 -125 -147 A C ATOM 4611 CG2 VAL B 222 -18.825 10.362 50.475 1.00 32.81 A C ANISOU 4611 CG2 VAL B 222 3822 4691 3949 -83 -197 -489 A C ATOM 4612 N ASP B 223 -20.085 7.937 54.436 1.00 33.32 A N ANISOU 4612 N ASP B 223 3903 4832 3923 173 -205 -93 A N ATOM 4613 CA ASP B 223 -19.847 7.027 55.568 1.00 34.28 A C ANISOU 4613 CA ASP B 223 4031 4922 4071 177 -191 -145 A C ATOM 4614 C ASP B 223 -20.888 5.918 55.536 1.00 35.34 A C ANISOU 4614 C ASP B 223 4148 5035 4245 202 -155 -61 A C ATOM 4615 O ASP B 223 -22.020 6.187 55.119 1.00 35.61 A O ANISOU 4615 O ASP B 223 3996 5265 4269 368 -280 -87 A O ATOM 4616 CB ASP B 223 -19.968 7.833 56.868 1.00 34.56 A C ANISOU 4616 CB ASP B 223 4140 4914 4077 106 -176 -59 A C ATOM 4617 CG ASP B 223 -19.368 7.122 58.075 1.00 36.99 A C ANISOU 4617 CG ASP B 223 4406 5029 4617 82 -173 -250 A C ATOM 4618 OD1 ASP B 223 -19.993 6.155 58.579 1.00 40.08 A O ANISOU 4618 OD1 ASP B 223 4927 5091 5210 262 -237 -278 A O ATOM 4619 OD2 ASP B 223 -18.293 7.563 58.547 1.00 37.11 A O1- ANISOU 4619 OD2 ASP B 223 4434 5088 4576 128 -275 -262 A O1- ATOM 4620 N ILE B 224 -20.527 4.695 55.946 1.00 36.28 A N ANISOU 4620 N ILE B 224 4314 5019 4450 345 -100 -97 A N ATOM 4621 CA ILE B 224 -21.492 3.564 55.930 1.00 38.69 A C ANISOU 4621 CA ILE B 224 4704 5111 4883 223 -21 -86 A C ATOM 4622 C ILE B 224 -22.390 3.545 57.136 1.00 39.49 A C ANISOU 4622 C ILE B 224 4774 5208 5021 296 -2 -91 A C ATOM 4623 O ILE B 224 -23.349 2.761 57.178 1.00 39.99 A O ANISOU 4623 O ILE B 224 4698 5312 5182 441 -7 -38 A O ATOM 4624 CB ILE B 224 -20.819 2.171 55.790 1.00 39.05 A C ANISOU 4624 CB ILE B 224 4735 5179 4923 246 0 -59 A C ATOM 4625 CG1 ILE B 224 -19.927 1.863 57.013 1.00 39.85 A C ANISOU 4625 CG1 ILE B 224 4756 5143 5241 122 70 -196 A C ATOM 4626 CG2 ILE B 224 -20.137 2.057 54.407 1.00 39.76 A C ANISOU 4626 CG2 ILE B 224 5106 5186 4815 174 90 -5 A C ATOM 4627 CD1 ILE B 224 -19.164 0.528 56.919 1.00 40.32 A C ANISOU 4627 CD1 ILE B 224 4992 5151 5173 76 -40 -149 A C ATOM 4628 N ASN B 225 -22.080 4.386 58.123 1.00 39.11 A N ANISOU 4628 N ASN B 225 4708 5196 4955 298 -30 -42 A N ATOM 4629 CA ASN B 225 -22.928 4.524 59.299 1.00 40.59 A C ANISOU 4629 CA ASN B 225 4955 5397 5070 234 37 -16 A C ATOM 4630 C ASN B 225 -23.818 5.763 59.189 1.00 40.41 A C ANISOU 4630 C ASN B 225 4908 5441 5006 189 58 -6 A C ATOM 4631 O ASN B 225 -23.373 6.901 59.401 1.00 39.87 A O ANISOU 4631 O ASN B 225 4823 5486 4837 271 39 59 A O ATOM 4632 CB ASN B 225 -22.088 4.555 60.573 1.00 41.31 A C ANISOU 4632 CB ASN B 225 5091 5481 5122 208 12 -13 A C ATOM 4633 CG ASN B 225 -22.917 4.325 61.837 1.00 43.27 A C ANISOU 4633 CG ASN B 225 5312 5762 5365 254 83 -89 A C ATOM 4634 ND2 ASN B 225 -22.262 3.877 62.890 1.00 46.31 A N ANISOU 4634 ND2 ASN B 225 5892 5993 5708 100 34 -295 A N ATOM 4635 OD1 ASN B 225 -24.118 4.569 61.866 1.00 46.24 A O ANISOU 4635 OD1 ASN B 225 5637 6131 5799 63 302 -152 A O ATOM 4636 N LYS B 226 -25.082 5.530 58.852 1.00 40.62 A N ANISOU 4636 N LYS B 226 4907 5446 5077 207 61 65 A N ATOM 4637 CA LYS B 226 -26.035 6.616 58.576 1.00 41.19 A C ANISOU 4637 CA LYS B 226 4916 5515 5217 161 27 49 A C ATOM 4638 C LYS B 226 -26.439 7.431 59.791 1.00 41.15 A C ANISOU 4638 C LYS B 226 4868 5534 5230 122 112 24 A C ATOM 4639 O LYS B 226 -27.001 8.514 59.655 1.00 40.88 A O ANISOU 4639 O LYS B 226 4751 5551 5231 147 215 30 A O ATOM 4640 CB LYS B 226 -27.278 6.063 57.888 1.00 42.00 A C ANISOU 4640 CB LYS B 226 4983 5617 5357 137 -41 80 A C ATOM 4641 CG LYS B 226 -26.933 5.297 56.645 1.00 43.02 A C ANISOU 4641 CG LYS B 226 5080 5659 5606 16 -60 112 A C ATOM 4642 CD LYS B 226 -28.119 4.461 56.181 1.00 46.02 A C ANISOU 4642 CD LYS B 226 5467 5764 6253 204 -290 52 A C ATOM 4643 CE LYS B 226 -29.003 5.276 55.237 1.00 46.71 A C ANISOU 4643 CE LYS B 226 5786 5718 6241 201 -233 -48 A C ATOM 4644 NZ LYS B 226 -28.472 5.141 53.886 1.00 45.83 A N1+ ANISOU 4644 NZ LYS B 226 5378 5567 6466 155 64 -153 A N1+ ATOM 4645 N ASP B 227 -26.163 6.915 60.980 1.00 41.62 A N ANISOU 4645 N ASP B 227 4960 5571 5282 60 168 -2 A N ATOM 4646 CA ASP B 227 -26.416 7.695 62.190 1.00 42.58 A C ANISOU 4646 CA ASP B 227 5171 5637 5370 -21 258 -18 A C ATOM 4647 C ASP B 227 -25.410 8.859 62.404 1.00 41.47 A C ANISOU 4647 C ASP B 227 5064 5544 5148 -73 309 -18 A C ATOM 4648 O ASP B 227 -25.583 9.686 63.283 1.00 41.90 A O ANISOU 4648 O ASP B 227 5175 5635 5109 -59 464 59 A O ATOM 4649 CB ASP B 227 -26.536 6.764 63.404 1.00 43.71 A C ANISOU 4649 CB ASP B 227 5387 5677 5541 -96 193 -87 A C ATOM 4650 CG ASP B 227 -27.605 5.667 63.196 1.00 47.18 A C ANISOU 4650 CG ASP B 227 5702 5939 6283 -17 127 -143 A C ATOM 4651 OD1 ASP B 227 -28.792 5.991 62.909 1.00 49.64 A O ANISOU 4651 OD1 ASP B 227 5760 6135 6965 6 192 -152 A O ATOM 4652 OD2 ASP B 227 -27.261 4.464 63.303 1.00 51.21 A O1- ANISOU 4652 OD2 ASP B 227 6223 6167 7064 -184 186 -200 A O1- ATOM 4653 N LYS B 228 -24.370 8.934 61.573 1.00 40.06 A N ANISOU 4653 N LYS B 228 4821 5472 4928 -107 319 -6 A N ATOM 4654 CA LYS B 228 -23.442 10.071 61.597 1.00 39.01 A C ANISOU 4654 CA LYS B 228 4686 5349 4784 -116 218 22 A C ATOM 4655 C LYS B 228 -23.888 11.216 60.687 1.00 38.02 A C ANISOU 4655 C LYS B 228 4539 5297 4609 -109 188 83 A C ATOM 4656 O LYS B 228 -23.297 12.315 60.711 1.00 36.43 A O ANISOU 4656 O LYS B 228 4422 5132 4285 -151 203 99 A O ATOM 4657 CB LYS B 228 -22.033 9.634 61.153 1.00 39.25 A C ANISOU 4657 CB LYS B 228 4747 5388 4775 -166 291 64 A C ATOM 4658 CG LYS B 228 -21.445 8.449 61.890 1.00 42.33 A C ANISOU 4658 CG LYS B 228 5198 5586 5297 -109 272 -29 A C ATOM 4659 CD LYS B 228 -21.181 8.713 63.357 1.00 45.96 A C ANISOU 4659 CD LYS B 228 5761 5922 5778 -55 62 252 A C ATOM 4660 CE LYS B 228 -20.546 7.484 63.984 1.00 47.97 A C ANISOU 4660 CE LYS B 228 5952 6076 6198 -32 64 129 A C ATOM 4661 NZ LYS B 228 -19.241 7.175 63.303 1.00 48.24 A N1+ ANISOU 4661 NZ LYS B 228 6028 5835 6463 14 134 498 A N1+ ATOM 4662 N PHE B 229 -24.903 10.956 59.861 1.00 36.70 A N ANISOU 4662 N PHE B 229 4313 5199 4430 -126 149 117 A N ATOM 4663 CA PHE B 229 -25.337 11.949 58.880 1.00 36.69 A C ANISOU 4663 CA PHE B 229 4345 5247 4347 -113 168 126 A C ATOM 4664 C PHE B 229 -25.920 13.208 59.542 1.00 36.39 A C ANISOU 4664 C PHE B 229 4296 5292 4238 -136 213 85 A C ATOM 4665 O PHE B 229 -25.681 14.317 59.088 1.00 36.43 A O ANISOU 4665 O PHE B 229 4459 5321 4061 -186 208 79 A O ATOM 4666 CB PHE B 229 -26.319 11.354 57.852 1.00 36.22 A C ANISOU 4666 CB PHE B 229 4282 5148 4332 -114 149 170 A C ATOM 4667 CG PHE B 229 -25.722 10.281 56.965 1.00 36.60 A C ANISOU 4667 CG PHE B 229 4304 5123 4476 18 89 210 A C ATOM 4668 CD1 PHE B 229 -24.343 10.009 56.969 1.00 37.14 A C ANISOU 4668 CD1 PHE B 229 4471 5132 4507 -116 -123 247 A C ATOM 4669 CD2 PHE B 229 -26.544 9.575 56.075 1.00 34.94 A C ANISOU 4669 CD2 PHE B 229 4252 4954 4067 -33 -25 173 A C ATOM 4670 CE1 PHE B 229 -23.805 9.036 56.133 1.00 36.65 A C ANISOU 4670 CE1 PHE B 229 4258 5189 4477 -165 -15 231 A C ATOM 4671 CE2 PHE B 229 -26.015 8.598 55.242 1.00 36.72 A C ANISOU 4671 CE2 PHE B 229 4424 5056 4469 -184 -61 88 A C ATOM 4672 CZ PHE B 229 -24.641 8.323 55.265 1.00 35.96 A C ANISOU 4672 CZ PHE B 229 4166 5039 4457 -63 32 242 A C ATOM 4673 N ALA B 230 -26.677 13.042 60.624 1.00 36.65 A N ANISOU 4673 N ALA B 230 4393 5394 4136 -164 281 -9 A N ATOM 4674 CA ALA B 230 -27.324 14.204 61.246 1.00 36.58 A C ANISOU 4674 CA ALA B 230 4490 5324 4082 -119 389 1 A C ATOM 4675 C ALA B 230 -26.327 15.297 61.664 1.00 36.19 A C ANISOU 4675 C ALA B 230 4477 5265 4007 -141 451 -55 A C ATOM 4676 O ALA B 230 -26.473 16.454 61.282 1.00 37.72 A O ANISOU 4676 O ALA B 230 4724 5391 4215 -178 552 27 A O ATOM 4677 CB ALA B 230 -28.220 13.775 62.427 1.00 36.47 A C ANISOU 4677 CB ALA B 230 4444 5356 4057 -145 432 -36 A C ATOM 4678 N LYS B 231 -25.290 14.906 62.393 1.00 36.50 A N ANISOU 4678 N LYS B 231 4578 5323 3967 -35 365 -41 A N ATOM 4679 CA LYS B 231 -24.268 15.829 62.858 1.00 36.67 A C ANISOU 4679 CA LYS B 231 4547 5334 4052 -68 269 -113 A C ATOM 4680 C LYS B 231 -23.434 16.405 61.696 1.00 36.03 A C ANISOU 4680 C LYS B 231 4509 5229 3951 -136 258 -56 A C ATOM 4681 O LYS B 231 -23.016 17.553 61.729 1.00 35.24 A O ANISOU 4681 O LYS B 231 4460 5152 3774 -165 186 24 A O ATOM 4682 CB LYS B 231 -23.357 15.110 63.841 1.00 37.13 A C ANISOU 4682 CB LYS B 231 4578 5438 4089 -87 258 -126 A C ATOM 4683 CG LYS B 231 -22.467 16.012 64.622 1.00 40.42 A C ANISOU 4683 CG LYS B 231 5003 5752 4603 23 -5 -113 A C ATOM 4684 CD LYS B 231 -21.778 15.204 65.754 1.00 43.99 A C ANISOU 4684 CD LYS B 231 5445 5963 5306 -137 -242 -267 A C ATOM 4685 CE LYS B 231 -22.738 14.852 66.891 1.00 45.81 A C ANISOU 4685 CE LYS B 231 5711 6245 5448 -95 -57 -100 A C ATOM 4686 NZ LYS B 231 -23.083 16.023 67.744 1.00 44.77 A N1+ ANISOU 4686 NZ LYS B 231 5508 6077 5425 -266 -205 -216 A N1+ ATOM 4687 N ALA B 232 -23.212 15.602 60.664 1.00 35.84 A N ANISOU 4687 N ALA B 232 4526 5128 3962 -174 212 -42 A N ATOM 4688 CA ALA B 232 -22.434 16.056 59.526 1.00 36.05 A C ANISOU 4688 CA ALA B 232 4582 5120 3993 -303 259 -34 A C ATOM 4689 C ALA B 232 -23.162 17.228 58.859 1.00 36.35 A C ANISOU 4689 C ALA B 232 4661 5092 4059 -329 244 9 A C ATOM 4690 O ALA B 232 -22.537 18.220 58.487 1.00 36.12 A O ANISOU 4690 O ALA B 232 4668 4993 4060 -524 142 -23 A O ATOM 4691 CB ALA B 232 -22.218 14.903 58.542 1.00 36.03 A C ANISOU 4691 CB ALA B 232 4597 5081 4012 -248 254 23 A C ATOM 4692 N LYS B 233 -24.486 17.119 58.752 1.00 37.62 A N ANISOU 4692 N LYS B 233 4838 5217 4238 -368 297 19 A N ATOM 4693 CA LYS B 233 -25.284 18.190 58.175 1.00 39.72 A C ANISOU 4693 CA LYS B 233 5009 5409 4673 -328 256 24 A C ATOM 4694 C LYS B 233 -25.308 19.436 59.083 1.00 39.85 A C ANISOU 4694 C LYS B 233 5119 5342 4678 -355 346 2 A C ATOM 4695 O LYS B 233 -25.159 20.553 58.602 1.00 39.69 A O ANISOU 4695 O LYS B 233 5100 5278 4702 -508 452 -38 A O ATOM 4696 CB LYS B 233 -26.695 17.687 57.872 1.00 40.02 A C ANISOU 4696 CB LYS B 233 5035 5511 4657 -231 162 -20 A C ATOM 4697 CG LYS B 233 -26.756 16.600 56.795 1.00 41.12 A C ANISOU 4697 CG LYS B 233 5035 5396 5190 -238 151 80 A C ATOM 4698 CD LYS B 233 -28.139 15.904 56.814 1.00 42.07 A C ANISOU 4698 CD LYS B 233 5194 5644 5145 -186 182 -10 A C ATOM 4699 CE LYS B 233 -28.220 14.760 55.816 1.00 44.15 A C ANISOU 4699 CE LYS B 233 5487 5866 5419 -193 -10 121 A C ATOM 4700 NZ LYS B 233 -28.596 15.205 54.441 1.00 44.89 A N1+ ANISOU 4700 NZ LYS B 233 5652 5828 5574 -303 267 -183 A N1+ ATOM 4701 N GLU B 234 -25.474 19.237 60.395 1.00 39.96 A N ANISOU 4701 N GLU B 234 5172 5348 4661 -387 269 28 A N ATOM 4702 CA GLU B 234 -25.395 20.324 61.378 1.00 40.65 A C ANISOU 4702 CA GLU B 234 5262 5414 4766 -373 257 52 A C ATOM 4703 C GLU B 234 -24.137 21.178 61.195 1.00 40.05 A C ANISOU 4703 C GLU B 234 5279 5288 4649 -430 273 24 A C ATOM 4704 O GLU B 234 -24.192 22.407 61.272 1.00 40.18 A O ANISOU 4704 O GLU B 234 5306 5287 4672 -563 377 135 A O ATOM 4705 CB GLU B 234 -25.440 19.738 62.794 1.00 40.65 A C ANISOU 4705 CB GLU B 234 5265 5486 4693 -319 247 82 A C ATOM 4706 CG GLU B 234 -25.507 20.768 63.926 1.00 42.29 A C ANISOU 4706 CG GLU B 234 5506 5530 5031 -258 240 172 A C ATOM 4707 CD GLU B 234 -25.369 20.125 65.305 1.00 43.12 A C ANISOU 4707 CD GLU B 234 5615 5713 5055 -319 121 111 A C ATOM 4708 OE1 GLU B 234 -25.365 18.877 65.400 1.00 47.25 A O ANISOU 4708 OE1 GLU B 234 6252 6037 5663 -343 129 299 A O ATOM 4709 OE2 GLU B 234 -25.286 20.865 66.310 1.00 46.83 A O1- ANISOU 4709 OE2 GLU B 234 5910 6315 5568 -345 -182 324 A O1- ATOM 4710 N VAL B 235 -23.008 20.532 60.896 1.00 38.41 A N ANISOU 4710 N VAL B 235 5095 5188 4308 -478 304 16 A N ATOM 4711 CA VAL B 235 -21.744 21.255 60.855 1.00 38.21 A C ANISOU 4711 CA VAL B 235 5168 5108 4239 -439 236 -12 A C ATOM 4712 C VAL B 235 -21.355 21.730 59.442 1.00 38.21 A C ANISOU 4712 C VAL B 235 5102 5156 4258 -393 232 -11 A C ATOM 4713 O VAL B 235 -20.341 22.411 59.278 1.00 38.55 A O ANISOU 4713 O VAL B 235 5226 5209 4212 -423 274 -43 A O ATOM 4714 CB VAL B 235 -20.582 20.470 61.551 1.00 38.24 A C ANISOU 4714 CB VAL B 235 5218 5122 4188 -465 157 16 A C ATOM 4715 CG1 VAL B 235 -21.006 20.043 62.961 1.00 38.56 A C ANISOU 4715 CG1 VAL B 235 5294 5087 4270 -269 307 3 A C ATOM 4716 CG2 VAL B 235 -20.151 19.264 60.743 1.00 37.85 A C ANISOU 4716 CG2 VAL B 235 5235 4996 4150 -510 280 -61 A C ATOM 4717 N GLY B 236 -22.165 21.365 58.452 1.00 37.34 A N ANISOU 4717 N GLY B 236 4951 5058 4175 -513 218 -52 A N ATOM 4718 CA GLY B 236 -22.051 21.934 57.111 1.00 37.14 A C ANISOU 4718 CA GLY B 236 4827 4998 4286 -473 181 -58 A C ATOM 4719 C GLY B 236 -22.201 21.056 55.889 1.00 36.24 A C ANISOU 4719 C GLY B 236 4618 4903 4247 -505 107 -31 A C ATOM 4720 O GLY B 236 -22.213 21.587 54.766 1.00 35.99 A O ANISOU 4720 O GLY B 236 4687 4749 4238 -643 233 21 A O ATOM 4721 N ALA B 237 -22.337 19.735 56.066 1.00 35.96 A N ANISOU 4721 N ALA B 237 4445 4970 4246 -538 45 31 A N ATOM 4722 CA ALA B 237 -22.554 18.838 54.921 1.00 35.41 A C ANISOU 4722 CA ALA B 237 4293 4970 4191 -524 37 67 A C ATOM 4723 C ALA B 237 -23.853 19.198 54.216 1.00 35.40 A C ANISOU 4723 C ALA B 237 4179 4991 4278 -512 67 77 A C ATOM 4724 O ALA B 237 -24.884 19.443 54.864 1.00 35.56 A O ANISOU 4724 O ALA B 237 4193 5073 4244 -502 55 142 A O ATOM 4725 CB ALA B 237 -22.567 17.393 55.328 1.00 34.94 A C ANISOU 4725 CB ALA B 237 4174 4926 4174 -532 64 155 A C ATOM 4726 N THR B 238 -23.795 19.260 52.889 1.00 35.85 A N ANISOU 4726 N THR B 238 4194 5045 4379 -515 67 -25 A N ATOM 4727 CA THR B 238 -24.953 19.623 52.104 1.00 36.17 A C ANISOU 4727 CA THR B 238 4167 5094 4481 -503 29 -55 A C ATOM 4728 C THR B 238 -25.763 18.393 51.705 1.00 37.30 A C ANISOU 4728 C THR B 238 4300 5210 4661 -429 -34 -21 A C ATOM 4729 O THR B 238 -26.967 18.489 51.430 1.00 37.35 A O ANISOU 4729 O THR B 238 4120 5150 4919 -329 13 -22 A O ATOM 4730 CB THR B 238 -24.573 20.462 50.879 1.00 36.43 A C ANISOU 4730 CB THR B 238 4234 5045 4562 -514 88 -56 A C ATOM 4731 CG2 THR B 238 -23.925 21.790 51.295 1.00 35.69 A C ANISOU 4731 CG2 THR B 238 4079 4975 4504 -551 1 29 A C ATOM 4732 OG1 THR B 238 -23.659 19.727 50.064 1.00 35.16 A O ANISOU 4732 OG1 THR B 238 3858 5282 4217 -708 -79 -259 A O ATOM 4733 N GLU B 239 -25.083 17.243 51.650 1.00 36.97 A N ANISOU 4733 N GLU B 239 4244 5209 4592 -418 -156 -141 A N ATOM 4734 CA GLU B 239 -25.701 15.945 51.397 1.00 37.90 A C ANISOU 4734 CA GLU B 239 4414 5391 4595 -293 -95 -149 A C ATOM 4735 C GLU B 239 -24.811 14.893 52.018 1.00 38.02 A C ANISOU 4735 C GLU B 239 4407 5506 4531 -216 -139 -149 A C ATOM 4736 O GLU B 239 -23.589 15.119 52.174 1.00 37.56 A O ANISOU 4736 O GLU B 239 4121 5707 4442 -279 -166 -261 A O ATOM 4737 CB GLU B 239 -25.798 15.630 49.892 1.00 38.79 A C ANISOU 4737 CB GLU B 239 4701 5371 4664 -189 -290 -94 A C ATOM 4738 CG GLU B 239 -26.362 16.707 48.972 1.00 42.13 A C ANISOU 4738 CG GLU B 239 5135 5513 5357 -172 -105 -163 A C ATOM 4739 CD GLU B 239 -25.501 16.869 47.734 1.00 45.41 A C ANISOU 4739 CD GLU B 239 5599 5931 5722 -121 -5 -104 A C ATOM 4740 OE1 GLU B 239 -25.546 15.975 46.869 1.00 47.70 A O ANISOU 4740 OE1 GLU B 239 5902 6441 5780 -156 -113 68 A O ATOM 4741 OE2 GLU B 239 -24.758 17.881 47.648 1.00 46.28 A O1- ANISOU 4741 OE2 GLU B 239 5327 6261 5996 117 77 -301 A O1- ATOM 4742 N CYS B 240 -25.399 13.735 52.315 1.00 37.38 A N ANISOU 4742 N CYS B 240 4374 5499 4327 -231 -83 -249 A N ATOM 4743 CA CYS B 240 -24.636 12.592 52.797 1.00 37.96 A C ANISOU 4743 CA CYS B 240 4426 5572 4425 -218 -33 -115 A C ATOM 4744 C CYS B 240 -24.963 11.362 51.999 1.00 37.91 A C ANISOU 4744 C CYS B 240 4370 5578 4454 -100 -96 -100 A C ATOM 4745 O CYS B 240 -26.124 11.141 51.620 1.00 38.60 A O ANISOU 4745 O CYS B 240 4270 5698 4696 -112 -145 -5 A O ATOM 4746 CB CYS B 240 -24.925 12.319 54.266 1.00 37.56 A C ANISOU 4746 CB CYS B 240 4422 5501 4345 -222 -7 -198 A C ATOM 4747 SG CYS B 240 -24.106 13.429 55.361 1.00 41.17 A S ANISOU 4747 SG CYS B 240 5266 6062 4313 -356 55 -30 A S ATOM 4748 N VAL B 241 -23.928 10.562 51.765 1.00 36.80 A N ANISOU 4748 N VAL B 241 4201 5474 4305 -33 -103 -72 A N ATOM 4749 CA VAL B 241 -23.999 9.369 50.958 1.00 37.24 A C ANISOU 4749 CA VAL B 241 4307 5392 4449 52 -157 -87 A C ATOM 4750 C VAL B 241 -23.548 8.151 51.748 1.00 36.55 A C ANISOU 4750 C VAL B 241 4199 5287 4400 168 -97 -93 A C ATOM 4751 O VAL B 241 -22.485 8.183 52.351 1.00 34.73 A O ANISOU 4751 O VAL B 241 4019 4983 4191 223 -152 -281 A O ATOM 4752 CB VAL B 241 -23.102 9.541 49.710 1.00 37.85 A C ANISOU 4752 CB VAL B 241 4399 5482 4500 4 -127 -26 A C ATOM 4753 CG1 VAL B 241 -22.878 8.205 49.013 1.00 39.50 A C ANISOU 4753 CG1 VAL B 241 4663 5612 4731 33 -300 157 A C ATOM 4754 CG2 VAL B 241 -23.712 10.565 48.754 1.00 40.18 A C ANISOU 4754 CG2 VAL B 241 5021 5596 4649 0 -195 -5 A C ATOM 4755 N ASN B 242 -24.369 7.095 51.745 1.00 35.78 A N ANISOU 4755 N ASN B 242 4109 5155 4331 276 -37 -24 A N ATOM 4756 CA ASN B 242 -23.999 5.813 52.323 1.00 36.94 A C ANISOU 4756 CA ASN B 242 4165 5274 4595 370 0 -36 A C ATOM 4757 C ASN B 242 -23.686 4.844 51.193 1.00 37.02 A C ANISOU 4757 C ASN B 242 4165 5291 4608 374 -122 5 A C ATOM 4758 O ASN B 242 -24.574 4.473 50.424 1.00 36.65 A O ANISOU 4758 O ASN B 242 3967 5314 4643 528 -159 3 A O ATOM 4759 CB ASN B 242 -25.119 5.271 53.236 1.00 37.56 A C ANISOU 4759 CB ASN B 242 4307 5299 4665 388 37 -26 A C ATOM 4760 CG ASN B 242 -24.828 3.868 53.775 1.00 37.00 A C ANISOU 4760 CG ASN B 242 4246 5148 4663 567 181 -166 A C ATOM 4761 ND2 ASN B 242 -25.752 3.341 54.573 1.00 39.52 A N ANISOU 4761 ND2 ASN B 242 4517 5763 4735 682 428 -377 A N ATOM 4762 OD1 ASN B 242 -23.805 3.262 53.473 1.00 36.59 A O ANISOU 4762 OD1 ASN B 242 4185 4588 5127 775 -167 -126 A O ATOM 4763 N PRO B 243 -22.411 4.466 51.031 1.00 37.34 A N ANISOU 4763 N PRO B 243 4207 5298 4682 329 -243 -39 A N ATOM 4764 CA PRO B 243 -22.040 3.580 49.928 1.00 37.90 A C ANISOU 4764 CA PRO B 243 4362 5276 4760 284 -301 8 A C ATOM 4765 C PRO B 243 -22.809 2.266 49.888 1.00 39.50 A C ANISOU 4765 C PRO B 243 4671 5327 5008 224 -327 38 A C ATOM 4766 O PRO B 243 -22.920 1.686 48.817 1.00 40.68 A O ANISOU 4766 O PRO B 243 4931 5486 5038 217 -459 8 A O ATOM 4767 CB PRO B 243 -20.559 3.284 50.184 1.00 38.27 A C ANISOU 4767 CB PRO B 243 4381 5313 4845 188 -269 23 A C ATOM 4768 CG PRO B 243 -20.090 4.374 51.013 1.00 38.37 A C ANISOU 4768 CG PRO B 243 4425 5320 4833 248 -243 74 A C ATOM 4769 CD PRO B 243 -21.246 4.854 51.842 1.00 35.81 A C ANISOU 4769 CD PRO B 243 3947 5197 4461 434 -242 -90 A C ATOM 4770 N GLN B 244 -23.305 1.801 51.033 1.00 40.05 A N ANISOU 4770 N GLN B 244 4796 5288 5131 223 -375 2 A N ATOM 4771 CA GLN B 244 -24.064 0.552 51.115 1.00 42.30 A C ANISOU 4771 CA GLN B 244 5181 5443 5444 197 -287 -56 A C ATOM 4772 C GLN B 244 -25.457 0.679 50.504 1.00 42.67 A C ANISOU 4772 C GLN B 244 5181 5488 5543 193 -322 26 A C ATOM 4773 O GLN B 244 -26.106 -0.333 50.224 1.00 43.16 A O ANISOU 4773 O GLN B 244 5307 5475 5616 269 -308 71 A O ATOM 4774 CB GLN B 244 -24.141 0.070 52.568 1.00 42.24 A C ANISOU 4774 CB GLN B 244 5167 5422 5459 243 -200 -37 A C ATOM 4775 CG GLN B 244 -22.804 -0.385 53.090 1.00 43.47 A C ANISOU 4775 CG GLN B 244 5567 5461 5485 237 -301 -134 A C ATOM 4776 CD GLN B 244 -22.852 -0.919 54.521 1.00 43.75 A C ANISOU 4776 CD GLN B 244 5598 5404 5618 242 -197 -256 A C ATOM 4777 NE2 GLN B 244 -23.936 -0.645 55.241 1.00 44.59 A N ANISOU 4777 NE2 GLN B 244 5981 5249 5712 402 27 -523 A N ATOM 4778 OE1 GLN B 244 -21.901 -1.539 54.973 1.00 48.15 A O ANISOU 4778 OE1 GLN B 244 6062 5731 6500 224 -197 -494 A O ATOM 4779 N ASP B 245 -25.910 1.915 50.305 1.00 42.31 A N ANISOU 4779 N ASP B 245 5105 5466 5504 138 -345 68 A N ATOM 4780 CA ASP B 245 -27.185 2.183 49.630 1.00 42.57 A C ANISOU 4780 CA ASP B 245 5071 5523 5580 29 -315 79 A C ATOM 4781 C ASP B 245 -27.133 1.910 48.129 1.00 42.33 A C ANISOU 4781 C ASP B 245 5075 5490 5518 3 -348 77 A C ATOM 4782 O ASP B 245 -28.180 1.908 47.468 1.00 42.27 A O ANISOU 4782 O ASP B 245 5004 5499 5554 -20 -411 147 A O ATOM 4783 CB ASP B 245 -27.597 3.641 49.849 1.00 43.08 A C ANISOU 4783 CB ASP B 245 5116 5568 5683 10 -290 73 A C ATOM 4784 CG ASP B 245 -28.226 3.887 51.218 1.00 44.10 A C ANISOU 4784 CG ASP B 245 5244 5701 5809 -3 -270 103 A C ATOM 4785 OD1 ASP B 245 -28.338 2.947 52.032 1.00 45.64 A O ANISOU 4785 OD1 ASP B 245 5158 6139 6043 129 -148 -50 A O ATOM 4786 OD2 ASP B 245 -28.624 5.043 51.478 1.00 44.95 A O1- ANISOU 4786 OD2 ASP B 245 5145 5719 6212 -51 -275 265 A O1- ATOM 4787 N TYR B 246 -25.933 1.686 47.583 1.00 42.27 A N ANISOU 4787 N TYR B 246 5078 5504 5475 -37 -369 32 A N ATOM 4788 CA TYR B 246 -25.730 1.630 46.120 1.00 42.85 A C ANISOU 4788 CA TYR B 246 5216 5548 5518 -56 -357 84 A C ATOM 4789 C TYR B 246 -25.326 0.296 45.558 1.00 44.33 A C ANISOU 4789 C TYR B 246 5480 5705 5655 -96 -362 77 A C ATOM 4790 O TYR B 246 -24.697 -0.525 46.244 1.00 45.00 A O ANISOU 4790 O TYR B 246 5600 5757 5737 -112 -483 121 A O ATOM 4791 CB TYR B 246 -24.690 2.660 45.684 1.00 42.52 A C ANISOU 4791 CB TYR B 246 5169 5516 5469 -118 -221 87 A C ATOM 4792 CG TYR B 246 -25.157 4.057 45.907 1.00 42.35 A C ANISOU 4792 CG TYR B 246 5060 5482 5548 -83 -240 77 A C ATOM 4793 CD1 TYR B 246 -25.036 4.667 47.151 1.00 41.61 A C ANISOU 4793 CD1 TYR B 246 4944 5433 5431 29 -149 54 A C ATOM 4794 CD2 TYR B 246 -25.763 4.763 44.878 1.00 41.56 A C ANISOU 4794 CD2 TYR B 246 5105 5396 5289 -9 -39 -55 A C ATOM 4795 CE1 TYR B 246 -25.500 5.961 47.344 1.00 41.90 A C ANISOU 4795 CE1 TYR B 246 4942 5392 5586 40 -91 221 A C ATOM 4796 CE2 TYR B 246 -26.218 6.019 45.059 1.00 42.03 A C ANISOU 4796 CE2 TYR B 246 5043 5436 5487 57 -161 99 A C ATOM 4797 CZ TYR B 246 -26.087 6.632 46.279 1.00 42.81 A C ANISOU 4797 CZ TYR B 246 5183 5495 5588 -42 -7 103 A C ATOM 4798 OH TYR B 246 -26.566 7.921 46.387 1.00 43.77 A O ANISOU 4798 OH TYR B 246 4962 5565 6103 -103 65 140 A O ATOM 4799 N LYS B 247 -25.681 0.101 44.288 1.00 45.36 A N ANISOU 4799 N LYS B 247 5655 5823 5755 -48 -402 82 A N ATOM 4800 CA LYS B 247 -25.279 -1.057 43.523 1.00 46.99 A C ANISOU 4800 CA LYS B 247 5898 5987 5968 -97 -277 84 A C ATOM 4801 C LYS B 247 -24.019 -0.810 42.711 1.00 47.88 A C ANISOU 4801 C LYS B 247 6056 6070 6064 -90 -199 73 A C ATOM 4802 O LYS B 247 -23.395 -1.764 42.232 1.00 49.07 A O ANISOU 4802 O LYS B 247 6155 6175 6312 -139 -143 32 A O ATOM 4803 CB LYS B 247 -26.408 -1.489 42.584 1.00 47.33 A C ANISOU 4803 CB LYS B 247 5983 5994 6007 -58 -332 132 A C ATOM 4804 CG LYS B 247 -27.117 -2.738 43.009 1.00 48.29 A C ANISOU 4804 CG LYS B 247 6065 6146 6135 44 -317 114 A C ATOM 4805 CD LYS B 247 -28.287 -3.060 42.073 1.00 50.06 A C ANISOU 4805 CD LYS B 247 6325 6227 6467 1 -462 149 A C ATOM 4806 CE LYS B 247 -29.596 -2.786 42.782 1.00 50.80 A C ANISOU 4806 CE LYS B 247 6407 6284 6607 87 -276 163 A C ATOM 4807 NZ LYS B 247 -30.714 -2.488 41.842 1.00 52.63 A N1+ ANISOU 4807 NZ LYS B 247 6875 6395 6725 -6 -397 109 A N1+ ATOM 4808 N LYS B 248 -23.665 0.456 42.513 1.00 48.59 A N ANISOU 4808 N LYS B 248 6183 6151 6126 -96 -132 107 A N ATOM 4809 CA LYS B 248 -22.422 0.784 41.820 1.00 48.74 A C ANISOU 4809 CA LYS B 248 6202 6180 6136 -122 -96 89 A C ATOM 4810 C LYS B 248 -21.346 1.303 42.764 1.00 48.72 A C ANISOU 4810 C LYS B 248 6191 6194 6122 -136 -44 55 A C ATOM 4811 O LYS B 248 -21.674 1.804 43.851 1.00 48.72 A O ANISOU 4811 O LYS B 248 6229 6221 6060 -208 -16 44 A O ATOM 4812 CB LYS B 248 -22.646 1.751 40.652 1.00 49.27 A C ANISOU 4812 CB LYS B 248 6293 6190 6236 -146 -97 94 A C ATOM 4813 CG LYS B 248 -23.475 3.000 40.923 1.00 49.75 A C ANISOU 4813 CG LYS B 248 6388 6134 6379 -145 -58 80 A C ATOM 4814 CD LYS B 248 -23.788 3.646 39.565 1.00 51.26 A C ANISOU 4814 CD LYS B 248 6591 6402 6483 -154 -104 92 A C ATOM 4815 CE LYS B 248 -23.905 5.160 39.655 1.00 52.40 A C ANISOU 4815 CE LYS B 248 6828 6385 6697 -124 7 -1 A C ATOM 4816 NZ LYS B 248 -25.033 5.553 40.558 1.00 52.81 A N1+ ANISOU 4816 NZ LYS B 248 6794 6422 6848 -183 87 37 A N1+ ATOM 4817 N PRO B 249 -20.058 1.162 42.363 1.00 47.98 A N ANISOU 4817 N PRO B 249 6035 6161 6033 -162 -29 50 A N ATOM 4818 CA PRO B 249 -18.958 1.690 43.155 1.00 47.62 A C ANISOU 4818 CA PRO B 249 5955 6139 6000 -162 -6 13 A C ATOM 4819 C PRO B 249 -19.160 3.147 43.492 1.00 46.38 A C ANISOU 4819 C PRO B 249 5727 6076 5817 -156 -19 26 A C ATOM 4820 O PRO B 249 -19.626 3.950 42.662 1.00 46.13 A O ANISOU 4820 O PRO B 249 5633 6137 5754 -180 -38 88 A O ATOM 4821 CB PRO B 249 -17.743 1.526 42.241 1.00 47.98 A C ANISOU 4821 CB PRO B 249 6011 6177 6040 -149 -10 26 A C ATOM 4822 CG PRO B 249 -18.101 0.423 41.354 1.00 48.67 A C ANISOU 4822 CG PRO B 249 6128 6200 6163 -125 -4 46 A C ATOM 4823 CD PRO B 249 -19.571 0.494 41.139 1.00 48.31 A C ANISOU 4823 CD PRO B 249 6059 6184 6110 -144 5 29 A C ATOM 4824 N ILE B 250 -18.801 3.468 44.717 1.00 45.27 A N ANISOU 4824 N ILE B 250 5462 6046 5691 -157 -52 -62 A N ATOM 4825 CA ILE B 250 -18.931 4.805 45.253 1.00 44.67 A C ANISOU 4825 CA ILE B 250 5359 6020 5594 -153 -81 -52 A C ATOM 4826 C ILE B 250 -18.237 5.888 44.411 1.00 43.37 A C ANISOU 4826 C ILE B 250 5138 5947 5393 -176 -53 -77 A C ATOM 4827 O ILE B 250 -18.776 6.969 44.292 1.00 42.64 A O ANISOU 4827 O ILE B 250 4895 5995 5310 -165 -13 -66 A O ATOM 4828 CB ILE B 250 -18.479 4.861 46.740 1.00 45.31 A C ANISOU 4828 CB ILE B 250 5529 6051 5633 -141 -85 -63 A C ATOM 4829 CG1 ILE B 250 -18.741 6.240 47.362 1.00 46.14 A C ANISOU 4829 CG1 ILE B 250 5676 6102 5753 -97 -112 52 A C ATOM 4830 CG2 ILE B 250 -17.011 4.450 46.892 1.00 46.44 A C ANISOU 4830 CG2 ILE B 250 5607 6212 5825 -128 -97 -9 A C ATOM 4831 CD1 ILE B 250 -20.170 6.516 47.646 1.00 45.32 A C ANISOU 4831 CD1 ILE B 250 5660 5932 5625 -183 -290 9 A C ATOM 4832 N GLN B 251 -17.063 5.624 43.817 1.00 43.23 A N ANISOU 4832 N GLN B 251 5114 5900 5409 -260 -85 -108 A N ATOM 4833 CA GLN B 251 -16.393 6.712 43.086 1.00 42.58 A C ANISOU 4833 CA GLN B 251 5009 5846 5324 -276 -99 -162 A C ATOM 4834 C GLN B 251 -17.215 7.143 41.859 1.00 42.23 A C ANISOU 4834 C GLN B 251 5000 5757 5286 -295 -118 -148 A C ATOM 4835 O GLN B 251 -17.199 8.309 41.459 1.00 42.57 A O ANISOU 4835 O GLN B 251 5036 5776 5361 -330 -130 -223 A O ATOM 4836 CB GLN B 251 -14.952 6.375 42.674 1.00 43.12 A C ANISOU 4836 CB GLN B 251 5061 5921 5402 -245 -62 -157 A C ATOM 4837 CG GLN B 251 -14.823 5.313 41.603 1.00 44.36 A C ANISOU 4837 CG GLN B 251 5220 5949 5686 -157 -89 -81 A C ATOM 4838 CD GLN B 251 -14.421 3.960 42.166 1.00 45.82 A C ANISOU 4838 CD GLN B 251 5443 6092 5874 -35 -158 -172 A C ATOM 4839 NE2 GLN B 251 -13.684 3.185 41.375 1.00 48.09 A N ANISOU 4839 NE2 GLN B 251 5833 6129 6308 -174 -19 -152 A N ATOM 4840 OE1 GLN B 251 -14.768 3.616 43.290 1.00 46.37 A O ANISOU 4840 OE1 GLN B 251 5235 6304 6079 78 -59 -361 A O ATOM 4841 N GLU B 252 -17.918 6.189 41.275 1.00 41.54 A N ANISOU 4841 N GLU B 252 4920 5686 5176 -289 -165 -161 A N ATOM 4842 CA GLU B 252 -18.776 6.464 40.132 1.00 41.50 A C ANISOU 4842 CA GLU B 252 5050 5639 5078 -323 -168 -165 A C ATOM 4843 C GLU B 252 -19.982 7.293 40.558 1.00 40.64 A C ANISOU 4843 C GLU B 252 4996 5553 4892 -274 -82 -166 A C ATOM 4844 O GLU B 252 -20.350 8.268 39.884 1.00 39.61 A O ANISOU 4844 O GLU B 252 4929 5470 4649 -333 -145 -203 A O ATOM 4845 CB GLU B 252 -19.232 5.156 39.505 1.00 42.49 A C ANISOU 4845 CB GLU B 252 5160 5673 5309 -297 -186 -173 A C ATOM 4846 CG GLU B 252 -19.493 5.241 38.022 1.00 45.82 A C ANISOU 4846 CG GLU B 252 5711 6042 5657 -174 -175 -88 A C ATOM 4847 CD GLU B 252 -20.030 3.947 37.462 1.00 49.44 A C ANISOU 4847 CD GLU B 252 6233 6224 6328 -134 -205 84 A C ATOM 4848 OE1 GLU B 252 -19.471 2.878 37.801 1.00 50.65 A O ANISOU 4848 OE1 GLU B 252 6357 6406 6481 -162 -155 -149 A O ATOM 4849 OE2 GLU B 252 -21.014 4.004 36.687 1.00 50.30 A O1- ANISOU 4849 OE2 GLU B 252 6488 6184 6436 -316 -436 -24 A O1- ATOM 4850 N VAL B 253 -20.599 6.903 41.673 1.00 38.99 A N ANISOU 4850 N VAL B 253 4800 5414 4598 -317 -71 -134 A N ATOM 4851 CA VAL B 253 -21.712 7.653 42.247 1.00 38.32 A C ANISOU 4851 CA VAL B 253 4614 5368 4578 -210 -50 -106 A C ATOM 4852 C VAL B 253 -21.281 9.085 42.475 1.00 36.83 A C ANISOU 4852 C VAL B 253 4440 5226 4326 -211 -53 -50 A C ATOM 4853 O VAL B 253 -21.996 10.006 42.126 1.00 36.95 A O ANISOU 4853 O VAL B 253 4412 5317 4308 -85 -159 -92 A O ATOM 4854 CB VAL B 253 -22.149 7.044 43.604 1.00 38.14 A C ANISOU 4854 CB VAL B 253 4648 5318 4524 -217 -24 -79 A C ATOM 4855 CG1 VAL B 253 -23.191 7.939 44.303 1.00 37.61 A C ANISOU 4855 CG1 VAL B 253 4290 5371 4628 -215 36 45 A C ATOM 4856 CG2 VAL B 253 -22.675 5.642 43.420 1.00 38.86 A C ANISOU 4856 CG2 VAL B 253 4690 5282 4793 -297 -233 -67 A C ATOM 4857 N LEU B 254 -20.090 9.294 43.036 1.00 36.04 A N ANISOU 4857 N LEU B 254 4290 5174 4226 -279 20 -40 A N ATOM 4858 CA LEU B 254 -19.654 10.668 43.305 1.00 35.96 A C ANISOU 4858 CA LEU B 254 4286 5157 4220 -246 33 -114 A C ATOM 4859 C LEU B 254 -19.267 11.441 42.057 1.00 36.04 A C ANISOU 4859 C LEU B 254 4283 5144 4266 -299 74 -69 A C ATOM 4860 O LEU B 254 -19.456 12.676 41.984 1.00 35.62 A O ANISOU 4860 O LEU B 254 4227 5094 4210 -331 36 -64 A O ATOM 4861 CB LEU B 254 -18.519 10.672 44.312 1.00 36.11 A C ANISOU 4861 CB LEU B 254 4310 5128 4281 -189 60 -52 A C ATOM 4862 CG LEU B 254 -18.954 10.169 45.697 1.00 37.93 A C ANISOU 4862 CG LEU B 254 4771 5320 4320 -240 14 -88 A C ATOM 4863 CD1 LEU B 254 -17.719 9.840 46.474 1.00 39.93 A C ANISOU 4863 CD1 LEU B 254 4879 5403 4886 -113 -167 -12 A C ATOM 4864 CD2 LEU B 254 -19.846 11.164 46.427 1.00 38.51 A C ANISOU 4864 CD2 LEU B 254 5194 5327 4109 -184 206 -308 A C ATOM 4865 N THR B 255 -18.683 10.735 41.093 1.00 36.27 A N ANISOU 4865 N THR B 255 4442 5173 4164 -265 42 -71 A N ATOM 4866 CA THR B 255 -18.303 11.387 39.848 1.00 37.08 A C ANISOU 4866 CA THR B 255 4551 5271 4265 -292 105 -50 A C ATOM 4867 C THR B 255 -19.549 11.869 39.103 1.00 37.06 A C ANISOU 4867 C THR B 255 4657 5228 4197 -359 138 -5 A C ATOM 4868 O THR B 255 -19.548 12.968 38.550 1.00 38.21 A O ANISOU 4868 O THR B 255 4846 5346 4323 -485 277 18 A O ATOM 4869 CB THR B 255 -17.414 10.467 39.006 1.00 36.79 A C ANISOU 4869 CB THR B 255 4520 5261 4195 -311 76 -80 A C ATOM 4870 CG2 THR B 255 -16.994 11.146 37.692 1.00 37.93 A C ANISOU 4870 CG2 THR B 255 4769 5365 4277 -78 112 -22 A C ATOM 4871 OG1 THR B 255 -16.237 10.175 39.789 1.00 37.19 A O ANISOU 4871 OG1 THR B 255 4354 5228 4546 -270 -158 147 A O ATOM 4872 N GLU B 256 -20.608 11.059 39.125 1.00 38.31 A N ANISOU 4872 N GLU B 256 4768 5345 4442 -340 120 -56 A N ATOM 4873 CA GLU B 256 -21.878 11.391 38.475 1.00 39.94 A C ANISOU 4873 CA GLU B 256 4983 5493 4697 -326 -2 -92 A C ATOM 4874 C GLU B 256 -22.566 12.535 39.238 1.00 39.03 A C ANISOU 4874 C GLU B 256 4861 5417 4550 -335 -63 -122 A C ATOM 4875 O GLU B 256 -23.090 13.478 38.632 1.00 38.70 A O ANISOU 4875 O GLU B 256 4797 5449 4457 -384 -158 -146 A O ATOM 4876 CB GLU B 256 -22.772 10.149 38.440 1.00 40.35 A C ANISOU 4876 CB GLU B 256 5098 5492 4741 -268 -39 -29 A C ATOM 4877 CG GLU B 256 -23.886 10.115 37.394 1.00 43.75 A C ANISOU 4877 CG GLU B 256 5340 5735 5545 -265 -118 -103 A C ATOM 4878 CD GLU B 256 -24.665 8.794 37.417 1.00 44.49 A C ANISOU 4878 CD GLU B 256 5441 5783 5680 -230 -92 -68 A C ATOM 4879 OE1 GLU B 256 -24.033 7.708 37.292 1.00 49.78 A O ANISOU 4879 OE1 GLU B 256 6149 5957 6807 -315 52 143 A O ATOM 4880 OE2 GLU B 256 -25.917 8.834 37.542 1.00 50.87 A O1- ANISOU 4880 OE2 GLU B 256 6028 6384 6914 -337 384 -175 A O1- ATOM 4881 N MET B 257 -22.544 12.461 40.571 1.00 38.24 A N ANISOU 4881 N MET B 257 4666 5450 4411 -323 -83 -166 A N ATOM 4882 CA MET B 257 -23.123 13.509 41.406 1.00 38.32 A C ANISOU 4882 CA MET B 257 4675 5478 4405 -384 18 -156 A C ATOM 4883 C MET B 257 -22.500 14.882 41.195 1.00 37.89 A C ANISOU 4883 C MET B 257 4612 5426 4357 -339 -10 -164 A C ATOM 4884 O MET B 257 -23.183 15.887 41.345 1.00 38.51 A O ANISOU 4884 O MET B 257 4688 5425 4519 -394 180 -142 A O ATOM 4885 CB MET B 257 -22.994 13.173 42.890 1.00 38.98 A C ANISOU 4885 CB MET B 257 4836 5486 4487 -343 112 -172 A C ATOM 4886 CG MET B 257 -24.008 12.208 43.434 1.00 39.21 A C ANISOU 4886 CG MET B 257 4834 5453 4610 -331 193 -94 A C ATOM 4887 SD MET B 257 -23.492 11.839 45.143 1.00 40.85 A S ANISOU 4887 SD MET B 257 5006 5864 4648 -657 358 -241 A S ATOM 4888 CE MET B 257 -24.103 13.302 46.000 1.00 39.67 A C ANISOU 4888 CE MET B 257 5252 5842 3978 -388 186 151 A C ATOM 4889 N SER B 258 -21.207 14.924 40.852 1.00 36.61 A N ANISOU 4889 N SER B 258 4430 5301 4179 -356 -85 -119 A N ATOM 4890 CA SER B 258 -20.448 16.178 40.807 1.00 36.43 A C ANISOU 4890 CA SER B 258 4445 5254 4142 -296 -152 -162 A C ATOM 4891 C SER B 258 -20.133 16.566 39.368 1.00 37.56 A C ANISOU 4891 C SER B 258 4730 5282 4257 -206 -122 -126 A C ATOM 4892 O SER B 258 -19.208 17.350 39.111 1.00 37.43 A O ANISOU 4892 O SER B 258 4790 5249 4180 -286 -104 -221 A O ATOM 4893 CB SER B 258 -19.132 16.007 41.563 1.00 35.88 A C ANISOU 4893 CB SER B 258 4389 5200 4043 -302 -238 -35 A C ATOM 4894 OG SER B 258 -18.418 14.947 40.964 1.00 33.61 A O ANISOU 4894 OG SER B 258 3860 4984 3926 -106 -475 -281 A O ATOM 4895 N ASN B 259 -20.879 15.962 38.443 1.00 38.57 A N ANISOU 4895 N ASN B 259 4967 5345 4340 -198 -116 -157 A N ATOM 4896 CA ASN B 259 -20.767 16.265 37.024 1.00 39.48 A C ANISOU 4896 CA ASN B 259 5144 5373 4480 -144 -55 -76 A C ATOM 4897 C ASN B 259 -19.294 16.201 36.594 1.00 39.10 A C ANISOU 4897 C ASN B 259 5114 5302 4439 -68 -73 -52 A C ATOM 4898 O ASN B 259 -18.743 17.128 35.978 1.00 40.24 A O ANISOU 4898 O ASN B 259 5392 5314 4584 0 -5 -126 A O ATOM 4899 CB ASN B 259 -21.458 17.603 36.719 1.00 40.62 A C ANISOU 4899 CB ASN B 259 5266 5430 4738 -107 -79 -143 A C ATOM 4900 CG ASN B 259 -22.973 17.558 36.995 1.00 43.31 A C ANISOU 4900 CG ASN B 259 5499 5763 5193 -226 -36 -15 A C ATOM 4901 ND2 ASN B 259 -23.685 16.703 36.271 1.00 45.40 A N ANISOU 4901 ND2 ASN B 259 5605 5830 5812 -92 -169 -188 A N ATOM 4902 OD1 ASN B 259 -23.474 18.248 37.884 1.00 49.43 A O ANISOU 4902 OD1 ASN B 259 6210 6268 6300 -476 175 138 A O ATOM 4903 N GLY B 260 -18.658 15.096 36.973 1.00 37.59 A N ANISOU 4903 N GLY B 260 4846 5252 4184 -89 -137 48 A N ATOM 4904 CA GLY B 260 -17.375 14.697 36.423 1.00 36.36 A C ANISOU 4904 CA GLY B 260 4637 5201 3975 -133 -132 102 A C ATOM 4905 C GLY B 260 -16.233 14.778 37.411 1.00 35.89 A C ANISOU 4905 C GLY B 260 4512 5141 3983 -221 -112 177 A C ATOM 4906 O GLY B 260 -15.082 14.903 36.979 1.00 36.87 A O ANISOU 4906 O GLY B 260 4587 5288 4131 -301 -101 245 A O ATOM 4907 N GLY B 261 -16.552 14.748 38.722 1.00 34.75 A N ANISOU 4907 N GLY B 261 4415 5033 3756 -288 -263 133 A N ATOM 4908 CA GLY B 261 -15.542 14.744 39.787 1.00 33.51 A C ANISOU 4908 CA GLY B 261 4313 4781 3635 -411 -277 260 A C ATOM 4909 C GLY B 261 -15.614 15.923 40.762 1.00 33.18 A C ANISOU 4909 C GLY B 261 4337 4715 3553 -530 -295 195 A C ATOM 4910 O GLY B 261 -16.007 17.031 40.386 1.00 33.10 A O ANISOU 4910 O GLY B 261 4436 4671 3467 -528 -286 259 A O ATOM 4911 N VAL B 262 -15.198 15.699 42.011 1.00 31.84 A N ANISOU 4911 N VAL B 262 4096 4477 3524 -645 -256 42 A N ATOM 4912 CA VAL B 262 -15.181 16.771 42.995 1.00 31.69 A C ANISOU 4912 CA VAL B 262 4188 4462 3388 -653 -299 -26 A C ATOM 4913 C VAL B 262 -13.904 17.626 42.887 1.00 30.40 A C ANISOU 4913 C VAL B 262 4142 4268 3139 -694 -196 -124 A C ATOM 4914 O VAL B 262 -12.890 17.190 42.343 1.00 31.35 A O ANISOU 4914 O VAL B 262 4323 4489 3098 -778 -171 32 A O ATOM 4915 CB VAL B 262 -15.391 16.242 44.456 1.00 30.58 A C ANISOU 4915 CB VAL B 262 3986 4238 3393 -661 -185 -19 A C ATOM 4916 CG1 VAL B 262 -16.696 15.428 44.559 1.00 32.30 A C ANISOU 4916 CG1 VAL B 262 4244 4484 3542 -441 -560 -9 A C ATOM 4917 CG2 VAL B 262 -14.192 15.415 44.934 1.00 31.31 A C ANISOU 4917 CG2 VAL B 262 3884 4517 3492 -654 -415 127 A C ATOM 4918 N ASP B 263 -13.950 18.856 43.396 1.00 30.17 A N ANISOU 4918 N ASP B 263 4290 4287 2886 -725 -160 -160 A N ATOM 4919 CA ASP B 263 -12.766 19.683 43.459 1.00 29.69 A C ANISOU 4919 CA ASP B 263 4253 4195 2829 -758 -296 -194 A C ATOM 4920 C ASP B 263 -11.764 19.177 44.498 1.00 29.39 A C ANISOU 4920 C ASP B 263 4239 4187 2739 -643 -213 -216 A C ATOM 4921 O ASP B 263 -10.591 19.166 44.239 1.00 29.82 A O ANISOU 4921 O ASP B 263 4316 4383 2630 -743 -85 -249 A O ATOM 4922 CB ASP B 263 -13.132 21.132 43.752 1.00 31.75 A C ANISOU 4922 CB ASP B 263 4618 4330 3115 -724 -326 -178 A C ATOM 4923 CG ASP B 263 -14.019 21.715 42.665 1.00 32.81 A C ANISOU 4923 CG ASP B 263 4601 4628 3235 -731 -243 -465 A C ATOM 4924 OD1 ASP B 263 -13.499 21.909 41.534 1.00 35.09 A O ANISOU 4924 OD1 ASP B 263 4615 5236 3479 -1161 254 -421 A O ATOM 4925 OD2 ASP B 263 -15.231 21.905 42.904 1.00 35.86 A O1- ANISOU 4925 OD2 ASP B 263 5129 5016 3479 -694 18 -248 A O1- ATOM 4926 N PHE B 264 -12.266 18.817 45.678 1.00 28.39 A N ANISOU 4926 N PHE B 264 4086 4014 2685 -539 -110 -226 A N ATOM 4927 CA PHE B 264 -11.416 18.404 46.799 1.00 27.50 A C ANISOU 4927 CA PHE B 264 3991 3789 2668 -492 -65 -227 A C ATOM 4928 C PHE B 264 -12.017 17.152 47.422 1.00 27.45 A C ANISOU 4928 C PHE B 264 3843 3739 2848 -408 -145 -213 A C ATOM 4929 O PHE B 264 -13.213 17.106 47.703 1.00 28.51 A O ANISOU 4929 O PHE B 264 3838 3774 3220 -669 -139 -410 A O ATOM 4930 CB PHE B 264 -11.377 19.542 47.838 1.00 28.18 A C ANISOU 4930 CB PHE B 264 4130 3704 2871 -306 -73 -218 A C ATOM 4931 CG PHE B 264 -10.842 20.849 47.274 1.00 26.99 A C ANISOU 4931 CG PHE B 264 4185 3325 2745 -456 25 -192 A C ATOM 4932 CD1 PHE B 264 -9.468 21.027 47.119 1.00 27.14 A C ANISOU 4932 CD1 PHE B 264 4305 3071 2935 -240 -13 -22 A C ATOM 4933 CD2 PHE B 264 -11.706 21.828 46.802 1.00 29.59 A C ANISOU 4933 CD2 PHE B 264 4593 3551 3099 -380 182 -115 A C ATOM 4934 CE1 PHE B 264 -8.944 22.163 46.576 1.00 28.92 A C ANISOU 4934 CE1 PHE B 264 4446 3283 3258 -119 14 0 A C ATOM 4935 CE2 PHE B 264 -11.200 22.983 46.231 1.00 29.72 A C ANISOU 4935 CE2 PHE B 264 4442 3548 3299 -311 167 -118 A C ATOM 4936 CZ PHE B 264 -9.829 23.179 46.120 1.00 27.69 A C ANISOU 4936 CZ PHE B 264 4174 3434 2912 -284 -152 116 A C ATOM 4937 N SER B 265 -11.195 16.158 47.716 1.00 26.78 A N ANISOU 4937 N SER B 265 3755 3640 2778 -373 -38 -80 A N ATOM 4938 CA SER B 265 -11.689 15.036 48.502 1.00 26.34 A C ANISOU 4938 CA SER B 265 3556 3658 2792 -290 -106 -118 A C ATOM 4939 C SER B 265 -10.775 14.786 49.673 1.00 26.83 A C ANISOU 4939 C SER B 265 3644 3693 2856 -286 -95 -135 A C ATOM 4940 O SER B 265 -9.589 15.093 49.618 1.00 26.76 A O ANISOU 4940 O SER B 265 3612 3687 2869 -227 -70 -127 A O ATOM 4941 CB SER B 265 -11.829 13.770 47.668 1.00 27.86 A C ANISOU 4941 CB SER B 265 3827 3855 2900 -183 67 -45 A C ATOM 4942 OG SER B 265 -10.584 13.400 47.090 1.00 29.33 A O ANISOU 4942 OG SER B 265 3869 3969 3305 -397 -123 86 A O ATOM 4943 N PHE B 266 -11.323 14.158 50.698 1.00 26.07 A N ANISOU 4943 N PHE B 266 3617 3537 2749 -377 -118 -140 A N ATOM 4944 CA PHE B 266 -10.553 13.938 51.918 1.00 26.93 A C ANISOU 4944 CA PHE B 266 3650 3704 2878 -328 -175 -66 A C ATOM 4945 C PHE B 266 -10.788 12.522 52.403 1.00 28.10 A C ANISOU 4945 C PHE B 266 3725 3707 3242 -276 -134 -137 A C ATOM 4946 O PHE B 266 -11.958 12.126 52.572 1.00 28.75 A O ANISOU 4946 O PHE B 266 3812 3773 3336 -340 2 -74 A O ATOM 4947 CB PHE B 266 -11.045 14.932 53.010 1.00 26.75 A C ANISOU 4947 CB PHE B 266 3647 3615 2900 -378 -27 -50 A C ATOM 4948 CG PHE B 266 -10.872 16.378 52.617 1.00 26.32 A C ANISOU 4948 CG PHE B 266 3609 3550 2841 -529 -33 -94 A C ATOM 4949 CD1 PHE B 266 -11.863 17.009 51.837 1.00 25.88 A C ANISOU 4949 CD1 PHE B 266 3590 3747 2495 -271 -199 -304 A C ATOM 4950 CD2 PHE B 266 -9.696 17.088 52.955 1.00 27.04 A C ANISOU 4950 CD2 PHE B 266 3963 3219 3091 -503 54 -43 A C ATOM 4951 CE1 PHE B 266 -11.687 18.345 51.423 1.00 27.44 A C ANISOU 4951 CE1 PHE B 266 3832 3530 3064 -139 86 90 A C ATOM 4952 CE2 PHE B 266 -9.508 18.418 52.544 1.00 29.05 A C ANISOU 4952 CE2 PHE B 266 4330 3738 2970 -158 74 43 A C ATOM 4953 CZ PHE B 266 -10.501 19.046 51.775 1.00 27.63 A C ANISOU 4953 CZ PHE B 266 3918 3734 2844 -184 68 171 A C ATOM 4954 N GLU B 267 -9.706 11.768 52.690 1.00 28.98 A N ANISOU 4954 N GLU B 267 3809 3877 3324 -169 -6 -43 A N ATOM 4955 CA GLU B 267 -9.876 10.458 53.310 1.00 30.52 A C ANISOU 4955 CA GLU B 267 4037 4063 3494 -178 47 -13 A C ATOM 4956 C GLU B 267 -9.482 10.596 54.749 1.00 31.81 A C ANISOU 4956 C GLU B 267 4144 4304 3637 -114 146 -67 A C ATOM 4957 O GLU B 267 -8.377 10.978 55.067 1.00 29.86 A O ANISOU 4957 O GLU B 267 4046 3994 3303 -64 229 -77 A O ATOM 4958 CB GLU B 267 -9.020 9.382 52.632 1.00 31.21 A C ANISOU 4958 CB GLU B 267 4144 4055 3660 -89 108 152 A C ATOM 4959 CG GLU B 267 -9.582 7.959 52.906 1.00 35.68 A C ANISOU 4959 CG GLU B 267 5113 4067 4376 -255 282 2 A C ATOM 4960 CD GLU B 267 -9.355 7.430 54.302 1.00 37.22 A C ANISOU 4960 CD GLU B 267 4980 4192 4969 -329 -17 -55 A C ATOM 4961 OE1 GLU B 267 -8.474 7.925 55.035 1.00 42.95 A O ANISOU 4961 OE1 GLU B 267 5640 4869 5810 -226 -164 -35 A O ATOM 4962 OE2 GLU B 267 -10.056 6.471 54.669 1.00 39.71 A O1- ANISOU 4962 OE2 GLU B 267 5164 4374 5548 -470 -183 -807 A O1- ATOM 4963 N VAL B 268 -10.423 10.279 55.626 1.00 34.20 A N ANISOU 4963 N VAL B 268 4541 4734 3716 -76 276 -113 A N ATOM 4964 CA VAL B 268 -10.190 10.508 57.032 1.00 38.72 A C ANISOU 4964 CA VAL B 268 5052 5197 4464 -82 162 7 A C ATOM 4965 C VAL B 268 -9.991 9.102 57.623 1.00 41.77 A C ANISOU 4965 C VAL B 268 5491 5534 4845 -108 170 -56 A C ATOM 4966 O VAL B 268 -9.025 8.864 58.300 1.00 43.72 A O ANISOU 4966 O VAL B 268 5568 5862 5180 -179 222 64 A O ATOM 4967 CB VAL B 268 -11.351 11.284 57.677 1.00 38.85 A C ANISOU 4967 CB VAL B 268 5011 5225 4522 -14 223 -92 A C ATOM 4968 CG1 VAL B 268 -11.657 12.592 56.911 1.00 37.95 A C ANISOU 4968 CG1 VAL B 268 4563 5294 4563 -350 100 130 A C ATOM 4969 CG2 VAL B 268 -12.564 10.437 57.757 1.00 42.20 A C ANISOU 4969 CG2 VAL B 268 5256 5550 5228 9 43 51 A C ATOM 4970 N ILE B 269 -10.881 8.176 57.246 1.00 44.58 A N ANISOU 4970 N ILE B 269 5900 5730 5305 -50 255 4 A N ATOM 4971 CA ILE B 269 -11.009 6.828 57.836 1.00 47.11 A C ANISOU 4971 CA ILE B 269 6212 5987 5697 -120 164 -11 A C ATOM 4972 C ILE B 269 -9.681 6.129 58.118 1.00 46.79 A C ANISOU 4972 C ILE B 269 6111 5945 5722 -151 192 -6 A C ATOM 4973 O ILE B 269 -9.488 5.555 59.200 1.00 47.86 A O ANISOU 4973 O ILE B 269 6359 6085 5738 -107 297 47 A O ATOM 4974 CB ILE B 269 -11.927 5.900 56.960 1.00 47.36 A C ANISOU 4974 CB ILE B 269 6214 6020 5760 -125 168 41 A C ATOM 4975 CG1 ILE B 269 -13.049 6.713 56.299 1.00 49.43 A C ANISOU 4975 CG1 ILE B 269 6552 6312 5915 -202 23 23 A C ATOM 4976 CG2 ILE B 269 -12.477 4.733 57.791 1.00 48.14 A C ANISOU 4976 CG2 ILE B 269 6462 6086 5742 -156 171 -22 A C ATOM 4977 CD1 ILE B 269 -13.854 5.985 55.232 1.00 48.84 A C ANISOU 4977 CD1 ILE B 269 6423 6194 5937 -129 67 -25 A C ATOM 4978 N GLY B 270 -8.756 6.193 57.163 1.00 46.38 A N ANISOU 4978 N GLY B 270 6020 5867 5733 -181 183 24 A N ATOM 4979 CA GLY B 270 -7.475 5.523 57.317 1.00 46.12 A C ANISOU 4979 CA GLY B 270 5807 5913 5802 -69 89 28 A C ATOM 4980 C GLY B 270 -7.466 4.229 56.531 1.00 45.51 A C ANISOU 4980 C GLY B 270 5628 5827 5834 -91 21 52 A C ATOM 4981 O GLY B 270 -6.585 3.369 56.708 1.00 45.73 A O ANISOU 4981 O GLY B 270 5607 5811 5955 -78 -160 -13 A O ATOM 4982 N ARG B 271 -8.427 4.099 55.619 1.00 43.60 A N ANISOU 4982 N ARG B 271 5399 5735 5430 -121 72 -17 A N ATOM 4983 CA ARG B 271 -8.641 2.834 54.956 1.00 42.94 A C ANISOU 4983 CA ARG B 271 5361 5700 5250 -32 169 -28 A C ATOM 4984 C ARG B 271 -8.013 2.870 53.569 1.00 42.21 A C ANISOU 4984 C ARG B 271 5298 5588 5149 -17 269 -59 A C ATOM 4985 O ARG B 271 -8.272 3.792 52.798 1.00 41.46 A O ANISOU 4985 O ARG B 271 5290 5485 4976 98 261 -55 A O ATOM 4986 CB ARG B 271 -10.136 2.566 54.840 1.00 43.53 A C ANISOU 4986 CB ARG B 271 5397 5783 5356 -73 132 -37 A C ATOM 4987 CG ARG B 271 -10.764 2.058 56.115 1.00 46.02 A C ANISOU 4987 CG ARG B 271 5552 6054 5880 -10 238 -52 A C ATOM 4988 CD ARG B 271 -11.019 0.558 56.018 1.00 50.50 A C ANISOU 4988 CD ARG B 271 6248 6264 6676 85 150 83 A C ATOM 4989 NE ARG B 271 -11.784 0.212 54.819 1.00 54.23 A N ANISOU 4989 NE ARG B 271 6814 6891 6899 98 -36 13 A N ATOM 4990 CZ ARG B 271 -12.470 -0.920 54.665 1.00 56.43 A C ANISOU 4990 CZ ARG B 271 7057 7068 7313 175 -27 13 A C ATOM 4991 NH1 ARG B 271 -12.502 -1.825 55.638 1.00 58.04 A N1+ ANISOU 4991 NH1 ARG B 271 7289 7327 7432 183 123 -38 A N1+ ATOM 4992 NH2 ARG B 271 -13.126 -1.148 53.536 1.00 57.48 A N ANISOU 4992 NH2 ARG B 271 7133 7284 7420 183 -37 38 A N ATOM 4993 N LEU B 272 -7.259 1.834 53.221 1.00 41.90 A N ANISOU 4993 N LEU B 272 5280 5615 5025 -10 340 -90 A N ATOM 4994 CA LEU B 272 -6.556 1.860 51.921 1.00 42.12 A C ANISOU 4994 CA LEU B 272 5473 5517 5013 20 339 -82 A C ATOM 4995 C LEU B 272 -7.497 1.931 50.726 1.00 42.92 A C ANISOU 4995 C LEU B 272 5581 5560 5167 -23 327 -118 A C ATOM 4996 O LEU B 272 -7.193 2.605 49.711 1.00 44.47 A O ANISOU 4996 O LEU B 272 5897 5664 5332 -14 424 -193 A O ATOM 4997 CB LEU B 272 -5.614 0.664 51.789 1.00 42.05 A C ANISOU 4997 CB LEU B 272 5353 5593 5028 -16 354 -67 A C ATOM 4998 CG LEU B 272 -4.510 0.474 52.835 1.00 42.09 A C ANISOU 4998 CG LEU B 272 5444 5595 4950 97 324 -109 A C ATOM 4999 CD1 LEU B 272 -3.826 -0.830 52.532 1.00 44.19 A C ANISOU 4999 CD1 LEU B 272 5657 5817 5315 16 313 -35 A C ATOM 5000 CD2 LEU B 272 -3.475 1.621 52.901 1.00 43.04 A C ANISOU 5000 CD2 LEU B 272 5681 5656 5014 168 482 -28 A C ATOM 5001 N ASP B 273 -8.628 1.233 50.814 1.00 43.26 A N ANISOU 5001 N ASP B 273 5682 5549 5205 8 154 -18 A N ATOM 5002 CA ASP B 273 -9.634 1.303 49.752 1.00 42.89 A C ANISOU 5002 CA ASP B 273 5704 5505 5084 26 93 -1 A C ATOM 5003 C ASP B 273 -10.229 2.692 49.562 1.00 42.00 A C ANISOU 5003 C ASP B 273 5530 5479 4947 0 118 47 A C ATOM 5004 O ASP B 273 -10.250 3.175 48.424 1.00 41.40 A O ANISOU 5004 O ASP B 273 5629 5390 4712 53 236 87 A O ATOM 5005 CB ASP B 273 -10.718 0.223 49.879 1.00 44.17 A C ANISOU 5005 CB ASP B 273 5826 5653 5302 62 -46 41 A C ATOM 5006 CG ASP B 273 -11.359 0.175 51.250 1.00 45.99 A C ANISOU 5006 CG ASP B 273 6152 5735 5586 97 0 -14 A C ATOM 5007 OD1 ASP B 273 -10.746 0.637 52.240 1.00 48.53 A O ANISOU 5007 OD1 ASP B 273 6821 5806 5812 344 -288 31 A O ATOM 5008 OD2 ASP B 273 -12.486 -0.346 51.346 1.00 50.28 A O1- ANISOU 5008 OD2 ASP B 273 6491 6121 6489 100 -268 123 A O1- ATOM 5009 N THR B 274 -10.684 3.365 50.629 1.00 39.85 A N ANISOU 5009 N THR B 274 5232 5292 4616 47 129 42 A N ATOM 5010 CA THR B 274 -11.238 4.707 50.404 1.00 39.08 A C ANISOU 5010 CA THR B 274 4997 5233 4617 0 170 91 A C ATOM 5011 C THR B 274 -10.165 5.743 50.074 1.00 37.18 A C ANISOU 5011 C THR B 274 4759 5018 4347 -68 205 29 A C ATOM 5012 O THR B 274 -10.490 6.747 49.476 1.00 36.47 A O ANISOU 5012 O THR B 274 4471 5186 4200 -220 195 61 A O ATOM 5013 CB THR B 274 -12.257 5.272 51.478 1.00 39.69 A C ANISOU 5013 CB THR B 274 5063 5263 4755 50 141 51 A C ATOM 5014 CG2 THR B 274 -13.679 4.705 51.256 1.00 41.81 A C ANISOU 5014 CG2 THR B 274 5190 5440 5254 -34 159 175 A C ATOM 5015 OG1 THR B 274 -11.816 4.987 52.796 1.00 41.87 A O ANISOU 5015 OG1 THR B 274 5558 5518 4830 -92 236 125 A O ATOM 5016 N MET B 275 -8.900 5.514 50.448 1.00 35.54 A N ANISOU 5016 N MET B 275 4561 4816 4125 -87 208 54 A N ATOM 5017 CA MET B 275 -7.841 6.439 50.002 1.00 35.17 A C ANISOU 5017 CA MET B 275 4478 4828 4057 -150 173 12 A C ATOM 5018 C MET B 275 -7.845 6.475 48.479 1.00 34.11 A C ANISOU 5018 C MET B 275 4430 4622 3908 -209 314 41 A C ATOM 5019 O MET B 275 -7.818 7.563 47.880 1.00 31.88 A O ANISOU 5019 O MET B 275 4038 4397 3675 -393 341 -38 A O ATOM 5020 CB MET B 275 -6.440 6.086 50.528 1.00 35.80 A C ANISOU 5020 CB MET B 275 4572 4858 4171 -174 228 37 A C ATOM 5021 CG MET B 275 -6.236 6.397 52.018 1.00 37.44 A C ANISOU 5021 CG MET B 275 4508 5252 4464 -69 84 64 A C ATOM 5022 SD MET B 275 -4.684 5.663 52.600 1.00 38.97 A S ANISOU 5022 SD MET B 275 4851 5370 4584 -172 -166 -68 A S ATOM 5023 CE MET B 275 -5.097 5.508 54.327 1.00 37.09 A C ANISOU 5023 CE MET B 275 4523 4990 4577 -160 395 65 A C ATOM 5024 N VAL B 276 -7.898 5.302 47.844 1.00 33.16 A N ANISOU 5024 N VAL B 276 4256 4495 3845 -117 232 -7 A N ATOM 5025 CA VAL B 276 -7.873 5.305 46.370 1.00 32.90 A C ANISOU 5025 CA VAL B 276 4336 4379 3784 -230 275 124 A C ATOM 5026 C VAL B 276 -9.218 5.801 45.781 1.00 32.63 A C ANISOU 5026 C VAL B 276 4203 4379 3814 -24 222 160 A C ATOM 5027 O VAL B 276 -9.235 6.559 44.821 1.00 31.30 A O ANISOU 5027 O VAL B 276 3917 4223 3750 -18 309 184 A O ATOM 5028 CB VAL B 276 -7.392 3.965 45.745 1.00 33.41 A C ANISOU 5028 CB VAL B 276 4463 4413 3817 -141 284 128 A C ATOM 5029 CG1 VAL B 276 -7.072 4.174 44.292 1.00 34.24 A C ANISOU 5029 CG1 VAL B 276 4895 4417 3694 -279 130 106 A C ATOM 5030 CG2 VAL B 276 -6.137 3.455 46.466 1.00 34.68 A C ANISOU 5030 CG2 VAL B 276 4584 4508 4082 -350 339 27 A C ATOM 5031 N THR B 277 -10.329 5.423 46.399 1.00 32.34 A N ANISOU 5031 N THR B 277 4168 4222 3896 65 222 192 A N ATOM 5032 CA THR B 277 -11.631 5.947 46.008 1.00 32.81 A C ANISOU 5032 CA THR B 277 4220 4336 3910 177 121 81 A C ATOM 5033 C THR B 277 -11.680 7.462 46.087 1.00 31.52 A C ANISOU 5033 C THR B 277 4082 4266 3627 109 47 94 A C ATOM 5034 O THR B 277 -12.190 8.132 45.155 1.00 32.00 A O ANISOU 5034 O THR B 277 4124 4349 3682 116 -131 112 A O ATOM 5035 CB THR B 277 -12.751 5.366 46.897 1.00 33.52 A C ANISOU 5035 CB THR B 277 4266 4355 4115 150 181 79 A C ATOM 5036 CG2 THR B 277 -14.073 5.977 46.523 1.00 34.25 A C ANISOU 5036 CG2 THR B 277 4108 4633 4272 380 234 77 A C ATOM 5037 OG1 THR B 277 -12.815 3.960 46.662 1.00 37.80 A O ANISOU 5037 OG1 THR B 277 5028 4506 4825 424 138 -130 A O ATOM 5038 N ALA B 278 -11.119 8.019 47.170 1.00 30.43 A N ANISOU 5038 N ALA B 278 3972 4278 3312 59 132 97 A N ATOM 5039 CA ALA B 278 -11.146 9.470 47.340 1.00 28.95 A C ANISOU 5039 CA ALA B 278 3803 4109 3085 22 -9 109 A C ATOM 5040 C ALA B 278 -10.320 10.161 46.254 1.00 28.39 A C ANISOU 5040 C ALA B 278 3702 4043 3041 -77 -11 88 A C ATOM 5041 O ALA B 278 -10.771 11.148 45.681 1.00 28.93 A O ANISOU 5041 O ALA B 278 3586 4079 3327 -114 -148 148 A O ATOM 5042 CB ALA B 278 -10.684 9.885 48.747 1.00 28.72 A C ANISOU 5042 CB ALA B 278 4014 4028 2867 -102 -75 70 A C ATOM 5043 N LEU B 279 -9.169 9.591 45.905 1.00 28.36 A N ANISOU 5043 N LEU B 279 3509 4188 3078 -9 -13 0 A N ATOM 5044 CA LEU B 279 -8.358 10.131 44.805 1.00 27.84 A C ANISOU 5044 CA LEU B 279 3442 4025 3111 -153 -4 10 A C ATOM 5045 C LEU B 279 -9.117 10.089 43.489 1.00 28.88 A C ANISOU 5045 C LEU B 279 3431 4228 3313 -184 -72 -48 A C ATOM 5046 O LEU B 279 -9.103 11.066 42.738 1.00 28.94 A O ANISOU 5046 O LEU B 279 3510 4177 3307 -342 -172 -144 A O ATOM 5047 CB LEU B 279 -7.028 9.367 44.678 1.00 27.72 A C ANISOU 5047 CB LEU B 279 3368 4065 3099 -9 71 0 A C ATOM 5048 CG LEU B 279 -6.128 9.837 43.531 1.00 26.99 A C ANISOU 5048 CG LEU B 279 3364 3608 3281 23 74 91 A C ATOM 5049 CD1 LEU B 279 -5.673 11.237 43.777 1.00 26.61 A C ANISOU 5049 CD1 LEU B 279 3295 3403 3412 272 -58 80 A C ATOM 5050 CD2 LEU B 279 -4.938 8.870 43.375 1.00 29.94 A C ANISOU 5050 CD2 LEU B 279 3622 4214 3539 -296 151 259 A C ATOM 5051 N SER B 280 -9.706 8.938 43.198 1.00 29.35 A N ANISOU 5051 N SER B 280 3359 4452 3339 -159 -246 -10 A N ATOM 5052 CA SER B 280 -10.384 8.694 41.918 1.00 30.90 A C ANISOU 5052 CA SER B 280 3624 4573 3542 -249 -335 64 A C ATOM 5053 C SER B 280 -11.584 9.621 41.755 1.00 31.71 A C ANISOU 5053 C SER B 280 3789 4648 3611 -293 -301 37 A C ATOM 5054 O SER B 280 -11.926 10.033 40.647 1.00 33.43 A O ANISOU 5054 O SER B 280 3953 4893 3853 -408 -247 4 A O ATOM 5055 CB SER B 280 -10.836 7.233 41.854 1.00 31.76 A C ANISOU 5055 CB SER B 280 3662 4678 3727 -320 -577 109 A C ATOM 5056 OG SER B 280 -9.715 6.348 41.901 1.00 36.70 A O ANISOU 5056 OG SER B 280 4338 4913 4693 -355 -210 210 A O ATOM 5057 N CYS B 281 -12.248 9.953 42.854 1.00 32.16 A N ANISOU 5057 N CYS B 281 3871 4696 3650 -352 -241 -63 A N ATOM 5058 CA CYS B 281 -13.498 10.687 42.717 1.00 33.34 A C ANISOU 5058 CA CYS B 281 4053 4792 3820 -400 -157 -176 A C ATOM 5059 C CYS B 281 -13.284 12.208 42.522 1.00 32.69 A C ANISOU 5059 C CYS B 281 4122 4577 3720 -467 -173 -236 A C ATOM 5060 O CYS B 281 -14.259 12.913 42.195 1.00 33.27 A O ANISOU 5060 O CYS B 281 4073 4629 3939 -508 -232 -185 A O ATOM 5061 CB CYS B 281 -14.456 10.386 43.879 1.00 34.88 A C ANISOU 5061 CB CYS B 281 4180 5029 4041 -340 -117 -180 A C ATOM 5062 SG CYS B 281 -14.148 11.397 45.303 1.00 37.52 A S ANISOU 5062 SG CYS B 281 4463 5695 4095 -543 0 -204 A S ATOM 5063 N CYS B 282 -12.043 12.704 42.651 1.00 31.48 A N ANISOU 5063 N CYS B 282 4195 4370 3395 -502 -128 -340 A N ATOM 5064 CA CYS B 282 -11.786 14.121 42.345 1.00 31.37 A C ANISOU 5064 CA CYS B 282 4172 4308 3438 -494 30 -201 A C ATOM 5065 C CYS B 282 -11.606 14.301 40.844 1.00 31.01 A C ANISOU 5065 C CYS B 282 4256 4208 3315 -470 -17 -175 A C ATOM 5066 O CYS B 282 -11.194 13.373 40.121 1.00 30.97 A O ANISOU 5066 O CYS B 282 4186 4160 3421 -601 29 -222 A O ATOM 5067 CB CYS B 282 -10.662 14.811 43.168 1.00 33.55 A C ANISOU 5067 CB CYS B 282 4324 4534 3887 -496 194 -153 A C ATOM 5068 SG CYS B 282 -8.969 14.225 42.884 1.00 33.98 A S ANISOU 5068 SG CYS B 282 4530 4662 3719 -746 302 -129 A S ATOM 5069 N GLN B 283 -11.906 15.508 40.378 1.00 30.57 A N ANISOU 5069 N GLN B 283 4332 4141 3142 -460 -8 -191 A N ATOM 5070 CA GLN B 283 -11.814 15.799 38.927 1.00 30.65 A C ANISOU 5070 CA GLN B 283 4320 4256 3069 -374 -20 -68 A C ATOM 5071 C GLN B 283 -10.418 15.420 38.370 1.00 30.01 A C ANISOU 5071 C GLN B 283 4245 4092 3063 -469 -91 -7 A C ATOM 5072 O GLN B 283 -9.371 15.736 38.962 1.00 28.95 A O ANISOU 5072 O GLN B 283 4072 4046 2880 -536 -62 119 A O ATOM 5073 CB GLN B 283 -12.172 17.265 38.652 1.00 31.54 A C ANISOU 5073 CB GLN B 283 4434 4334 3215 -330 -90 -123 A C ATOM 5074 CG GLN B 283 -12.666 17.546 37.192 1.00 33.87 A C ANISOU 5074 CG GLN B 283 4973 4614 3280 -302 194 14 A C ATOM 5075 CD GLN B 283 -11.525 17.599 36.171 1.00 34.86 A C ANISOU 5075 CD GLN B 283 4680 4514 4050 -158 213 173 A C ATOM 5076 NE2 GLN B 283 -11.823 17.241 34.935 1.00 35.94 A N ANISOU 5076 NE2 GLN B 283 4815 4885 3953 -47 44 -31 A N ATOM 5077 OE1 GLN B 283 -10.394 17.941 36.503 1.00 34.99 A O ANISOU 5077 OE1 GLN B 283 4727 4695 3870 -547 -46 277 A O ATOM 5078 N GLU B 284 -10.404 14.743 37.233 1.00 30.18 A N ANISOU 5078 N GLU B 284 4230 4090 3147 -365 -51 -49 A N ATOM 5079 CA GLU B 284 -9.170 14.138 36.742 1.00 30.24 A C ANISOU 5079 CA GLU B 284 4364 3987 3136 -399 -56 23 A C ATOM 5080 C GLU B 284 -8.084 15.142 36.349 1.00 28.86 A C ANISOU 5080 C GLU B 284 4148 3808 3010 -357 -78 7 A C ATOM 5081 O GLU B 284 -6.883 14.786 36.327 1.00 29.44 A O ANISOU 5081 O GLU B 284 4287 3806 3091 -340 -51 -277 A O ATOM 5082 CB GLU B 284 -9.478 13.219 35.555 1.00 30.97 A C ANISOU 5082 CB GLU B 284 4487 4069 3209 -328 -103 109 A C ATOM 5083 CG GLU B 284 -9.881 14.021 34.323 1.00 33.30 A C ANISOU 5083 CG GLU B 284 4852 4202 3595 -248 -236 -7 A C ATOM 5084 CD GLU B 284 -10.089 13.200 33.071 1.00 37.69 A C ANISOU 5084 CD GLU B 284 5472 4601 4245 -181 -294 220 A C ATOM 5085 OE1 GLU B 284 -9.681 11.999 33.047 1.00 39.97 A O ANISOU 5085 OE1 GLU B 284 5908 4575 4703 -82 -576 585 A O ATOM 5086 OE2 GLU B 284 -10.651 13.788 32.102 1.00 36.83 A O1- ANISOU 5086 OE2 GLU B 284 5240 4389 4362 55 -187 -104 A O1- ATOM 5087 N ALA B 285 -8.487 16.367 35.982 1.00 29.34 A N ANISOU 5087 N ALA B 285 4257 3962 2929 -332 -50 81 A N ATOM 5088 CA ALA B 285 -7.548 17.404 35.495 1.00 28.91 A C ANISOU 5088 CA ALA B 285 4167 3968 2849 -386 77 74 A C ATOM 5089 C ALA B 285 -7.021 18.353 36.577 1.00 29.84 A C ANISOU 5089 C ALA B 285 4222 3986 3130 -381 215 171 A C ATOM 5090 O ALA B 285 -5.907 18.875 36.461 1.00 31.59 A O ANISOU 5090 O ALA B 285 4561 3984 3456 -369 409 306 A O ATOM 5091 CB ALA B 285 -8.191 18.233 34.295 1.00 29.98 A C ANISOU 5091 CB ALA B 285 4247 4204 2938 -344 45 40 A C ATOM 5092 N TYR B 286 -7.800 18.584 37.633 1.00 28.81 A N ANISOU 5092 N TYR B 286 4353 3887 2707 -465 150 11 A N ATOM 5093 CA TYR B 286 -7.408 19.629 38.597 1.00 28.81 A C ANISOU 5093 CA TYR B 286 4323 3845 2779 -392 199 -25 A C ATOM 5094 C TYR B 286 -7.825 19.287 40.030 1.00 29.16 A C ANISOU 5094 C TYR B 286 4300 4024 2755 -347 224 56 A C ATOM 5095 O TYR B 286 -7.695 20.122 40.949 1.00 30.51 A O ANISOU 5095 O TYR B 286 4575 4181 2834 -341 171 91 A O ATOM 5096 CB TYR B 286 -7.975 20.998 38.157 1.00 30.32 A C ANISOU 5096 CB TYR B 286 4403 4013 3102 -436 112 -87 A C ATOM 5097 CG TYR B 286 -9.481 21.016 37.923 1.00 29.17 A C ANISOU 5097 CG TYR B 286 4241 3786 3054 -654 248 -133 A C ATOM 5098 CD1 TYR B 286 -10.378 21.044 38.996 1.00 29.96 A C ANISOU 5098 CD1 TYR B 286 4212 4231 2940 -619 114 30 A C ATOM 5099 CD2 TYR B 286 -10.016 21.093 36.638 1.00 29.74 A C ANISOU 5099 CD2 TYR B 286 4092 3854 3352 -565 167 -14 A C ATOM 5100 CE1 TYR B 286 -11.729 21.064 38.792 1.00 30.37 A C ANISOU 5100 CE1 TYR B 286 4140 4299 3100 -592 -22 -155 A C ATOM 5101 CE2 TYR B 286 -11.356 21.120 36.428 1.00 31.15 A C ANISOU 5101 CE2 TYR B 286 4457 4146 3232 -517 -120 -220 A C ATOM 5102 CZ TYR B 286 -12.226 21.124 37.501 1.00 32.56 A C ANISOU 5102 CZ TYR B 286 4347 4519 3502 -355 37 -148 A C ATOM 5103 OH TYR B 286 -13.590 21.155 37.317 1.00 34.92 A O ANISOU 5103 OH TYR B 286 4592 4503 4172 -869 -13 -146 A O ATOM 5104 N GLY B 287 -8.328 18.076 40.211 1.00 28.50 A N ANISOU 5104 N GLY B 287 4295 3966 2567 -395 253 -48 A N ATOM 5105 CA GLY B 287 -8.822 17.607 41.545 1.00 29.06 A C ANISOU 5105 CA GLY B 287 4288 4174 2576 -404 4 -98 A C ATOM 5106 C GLY B 287 -7.657 17.459 42.530 1.00 28.67 A C ANISOU 5106 C GLY B 287 4097 3958 2839 -406 -63 -64 A C ATOM 5107 O GLY B 287 -6.533 17.237 42.122 1.00 27.44 A O ANISOU 5107 O GLY B 287 3953 3822 2650 -419 56 18 A O ATOM 5108 N VAL B 288 -7.935 17.662 43.812 1.00 27.60 A N ANISOU 5108 N VAL B 288 3900 3919 2667 -348 -165 -251 A N ATOM 5109 CA VAL B 288 -6.918 17.488 44.867 1.00 27.45 A C ANISOU 5109 CA VAL B 288 3815 3799 2815 -281 -192 -233 A C ATOM 5110 C VAL B 288 -7.496 16.561 45.900 1.00 27.60 A C ANISOU 5110 C VAL B 288 3746 3859 2880 -279 -108 -162 A C ATOM 5111 O VAL B 288 -8.624 16.772 46.351 1.00 29.39 A O ANISOU 5111 O VAL B 288 3810 4194 3160 -289 52 -292 A O ATOM 5112 CB VAL B 288 -6.581 18.843 45.535 1.00 28.01 A C ANISOU 5112 CB VAL B 288 3951 3930 2761 -283 -156 -169 A C ATOM 5113 CG1 VAL B 288 -5.646 18.671 46.711 1.00 28.54 A C ANISOU 5113 CG1 VAL B 288 4231 3743 2869 -219 -325 -172 A C ATOM 5114 CG2 VAL B 288 -5.983 19.814 44.500 1.00 28.80 A C ANISOU 5114 CG2 VAL B 288 3869 3817 3257 -188 59 -224 A C ATOM 5115 N SER B 289 -6.732 15.549 46.298 1.00 25.74 A N ANISOU 5115 N SER B 289 3596 3663 2520 -343 -142 -195 A N ATOM 5116 CA SER B 289 -7.211 14.626 47.328 1.00 25.29 A C ANISOU 5116 CA SER B 289 3542 3510 2557 -194 -195 -19 A C ATOM 5117 C SER B 289 -6.208 14.627 48.482 1.00 25.21 A C ANISOU 5117 C SER B 289 3405 3563 2610 -217 -164 -57 A C ATOM 5118 O SER B 289 -4.996 14.537 48.269 1.00 26.03 A O ANISOU 5118 O SER B 289 3667 3589 2632 -212 -246 -86 A O ATOM 5119 CB SER B 289 -7.378 13.217 46.749 1.00 26.63 A C ANISOU 5119 CB SER B 289 3693 3611 2814 -251 -12 0 A C ATOM 5120 OG SER B 289 -7.954 12.337 47.711 1.00 27.43 A O ANISOU 5120 OG SER B 289 4017 3410 2992 -229 -192 110 A O ATOM 5121 N VAL B 290 -6.731 14.720 49.703 1.00 25.02 A N ANISOU 5121 N VAL B 290 3517 3538 2447 -226 -291 -18 A N ATOM 5122 CA VAL B 290 -5.882 14.828 50.903 1.00 26.43 A C ANISOU 5122 CA VAL B 290 3687 3653 2699 -194 -236 3 A C ATOM 5123 C VAL B 290 -6.129 13.661 51.839 1.00 26.07 A C ANISOU 5123 C VAL B 290 3581 3619 2704 -239 -241 -38 A C ATOM 5124 O VAL B 290 -7.286 13.350 52.171 1.00 27.87 A O ANISOU 5124 O VAL B 290 3798 3851 2937 -294 -87 -198 A O ATOM 5125 CB VAL B 290 -6.165 16.167 51.689 1.00 26.88 A C ANISOU 5125 CB VAL B 290 3826 3602 2785 -164 -50 0 A C ATOM 5126 CG1 VAL B 290 -5.287 16.271 52.969 1.00 27.98 A C ANISOU 5126 CG1 VAL B 290 3689 3887 3052 -242 -226 -89 A C ATOM 5127 CG2 VAL B 290 -5.939 17.431 50.823 1.00 27.07 A C ANISOU 5127 CG2 VAL B 290 4172 3565 2547 -407 -5 -73 A C ATOM 5128 N ILE B 291 -5.034 13.036 52.287 1.00 26.27 A N ANISOU 5128 N ILE B 291 3853 3547 2578 -386 -255 22 A N ATOM 5129 CA ILE B 291 -5.048 11.935 53.237 1.00 29.39 A C ANISOU 5129 CA ILE B 291 4319 3872 2976 -319 -161 -27 A C ATOM 5130 C ILE B 291 -4.871 12.620 54.595 1.00 29.55 A C ANISOU 5130 C ILE B 291 4308 3932 2988 -290 -190 -60 A C ATOM 5131 O ILE B 291 -3.893 13.331 54.806 1.00 29.89 A O ANISOU 5131 O ILE B 291 4336 4073 2944 -218 -159 -197 A O ATOM 5132 CB ILE B 291 -3.839 10.971 52.902 1.00 29.13 A C ANISOU 5132 CB ILE B 291 4459 3788 2818 -348 -187 0 A C ATOM 5133 CG1 ILE B 291 -4.125 10.247 51.548 1.00 32.26 A C ANISOU 5133 CG1 ILE B 291 4898 4041 3319 -445 -174 375 A C ATOM 5134 CG2 ILE B 291 -3.473 10.007 54.062 1.00 32.59 A C ANISOU 5134 CG2 ILE B 291 4906 3940 3537 -281 -163 -83 A C ATOM 5135 CD1 ILE B 291 -3.072 9.202 51.129 1.00 32.27 A C ANISOU 5135 CD1 ILE B 291 4516 4206 3539 -444 -56 39 A C ATOM 5136 N VAL B 292 -5.829 12.413 55.495 1.00 29.53 A N ANISOU 5136 N VAL B 292 4252 4068 2900 -319 -192 0 A N ATOM 5137 CA VAL B 292 -5.864 13.139 56.765 1.00 31.33 A C ANISOU 5137 CA VAL B 292 4414 4204 3282 -276 -161 88 A C ATOM 5138 C VAL B 292 -5.283 12.232 57.853 1.00 32.59 A C ANISOU 5138 C VAL B 292 4547 4414 3421 -262 -195 95 A C ATOM 5139 O VAL B 292 -4.735 12.697 58.868 1.00 35.29 A O ANISOU 5139 O VAL B 292 4802 4834 3772 -227 -238 215 A O ATOM 5140 CB VAL B 292 -7.291 13.621 57.077 1.00 31.17 A C ANISOU 5140 CB VAL B 292 4359 4308 3174 -240 -130 83 A C ATOM 5141 CG1 VAL B 292 -7.345 14.365 58.404 1.00 28.58 A C ANISOU 5141 CG1 VAL B 292 4062 3703 3094 -261 -36 144 A C ATOM 5142 CG2 VAL B 292 -7.813 14.529 55.933 1.00 30.69 A C ANISOU 5142 CG2 VAL B 292 4113 4184 3360 -116 -116 47 A C ATOM 5143 N GLY B 293 -5.337 10.931 57.628 1.00 34.21 A N ANISOU 5143 N GLY B 293 4716 4511 3771 -243 -117 -30 A N ATOM 5144 CA GLY B 293 -4.716 10.014 58.593 1.00 35.55 A C ANISOU 5144 CA GLY B 293 4768 4606 4130 -314 21 -2 A C ATOM 5145 C GLY B 293 -4.377 8.720 57.906 1.00 36.56 A C ANISOU 5145 C GLY B 293 4896 4740 4253 -277 98 14 A C ATOM 5146 O GLY B 293 -4.985 8.378 56.900 1.00 36.70 A O ANISOU 5146 O GLY B 293 4876 4754 4312 -338 160 86 A O ATOM 5147 N VAL B 294 -3.409 8.014 58.471 1.00 37.34 A N ANISOU 5147 N VAL B 294 4880 4897 4407 -289 83 -1 A N ATOM 5148 CA VAL B 294 -3.057 6.661 58.066 1.00 38.49 A C ANISOU 5148 CA VAL B 294 5093 4996 4533 -300 93 -47 A C ATOM 5149 C VAL B 294 -2.881 5.816 59.323 1.00 38.95 A C ANISOU 5149 C VAL B 294 5149 5038 4611 -369 70 1 A C ATOM 5150 O VAL B 294 -2.081 6.190 60.175 1.00 40.05 A O ANISOU 5150 O VAL B 294 5271 5282 4664 -507 75 -2 A O ATOM 5151 CB VAL B 294 -1.740 6.642 57.268 1.00 38.99 A C ANISOU 5151 CB VAL B 294 5180 5085 4548 -298 84 -77 A C ATOM 5152 CG1 VAL B 294 -1.489 5.260 56.678 1.00 39.03 A C ANISOU 5152 CG1 VAL B 294 5199 5002 4625 -226 192 -327 A C ATOM 5153 CG2 VAL B 294 -1.791 7.685 56.139 1.00 39.84 A C ANISOU 5153 CG2 VAL B 294 5201 5181 4753 -291 86 -304 A C ATOM 5154 N PRO B 295 -3.585 4.667 59.428 1.00 39.95 A N ANISOU 5154 N PRO B 295 5268 5196 4714 -327 42 -62 A N ATOM 5155 CA PRO B 295 -3.298 3.824 60.587 1.00 40.37 A C ANISOU 5155 CA PRO B 295 5431 5213 4694 -290 42 -12 A C ATOM 5156 C PRO B 295 -1.811 3.496 60.579 1.00 40.69 A C ANISOU 5156 C PRO B 295 5551 5287 4621 -297 0 37 A C ATOM 5157 O PRO B 295 -1.254 3.242 59.508 1.00 39.88 A O ANISOU 5157 O PRO B 295 5598 5179 4375 -437 79 152 A O ATOM 5158 CB PRO B 295 -4.144 2.566 60.328 1.00 40.63 A C ANISOU 5158 CB PRO B 295 5480 5195 4760 -246 -32 -132 A C ATOM 5159 CG PRO B 295 -5.288 3.054 59.455 1.00 41.68 A C ANISOU 5159 CG PRO B 295 5472 5341 5022 -251 41 -116 A C ATOM 5160 CD PRO B 295 -4.583 4.042 58.538 1.00 40.39 A C ANISOU 5160 CD PRO B 295 5336 5231 4778 -298 47 -126 A C ATOM 5161 N PRO B 296 -1.158 3.543 61.754 1.00 40.74 A N ANISOU 5161 N PRO B 296 5582 5298 4598 -228 -52 183 A N ATOM 5162 CA PRO B 296 0.290 3.385 61.879 1.00 41.21 A C ANISOU 5162 CA PRO B 296 5633 5294 4729 -250 -25 195 A C ATOM 5163 C PRO B 296 0.838 2.016 61.476 1.00 41.53 A C ANISOU 5163 C PRO B 296 5667 5290 4822 -231 -27 172 A C ATOM 5164 O PRO B 296 2.041 1.901 61.231 1.00 41.79 A O ANISOU 5164 O PRO B 296 5633 5302 4942 -205 -82 119 A O ATOM 5165 CB PRO B 296 0.559 3.659 63.363 1.00 41.08 A C ANISOU 5165 CB PRO B 296 5630 5342 4634 -174 -99 190 A C ATOM 5166 CG PRO B 296 -0.723 3.506 64.050 1.00 40.32 A C ANISOU 5166 CG PRO B 296 5425 5284 4611 -233 -109 293 A C ATOM 5167 CD PRO B 296 -1.801 3.831 63.051 1.00 40.19 A C ANISOU 5167 CD PRO B 296 5555 5176 4539 -298 -3 185 A C ATOM 5168 N ASP B 297 -0.034 1.013 61.397 1.00 42.17 A N ANISOU 5168 N ASP B 297 5751 5304 4968 -223 6 129 A N ATOM 5169 CA ASP B 297 0.333 -0.305 60.879 1.00 43.38 A C ANISOU 5169 CA ASP B 297 5967 5359 5155 -166 -53 76 A C ATOM 5170 C ASP B 297 -0.154 -0.558 59.452 1.00 43.28 A C ANISOU 5170 C ASP B 297 5924 5302 5217 -174 -65 90 A C ATOM 5171 O ASP B 297 -0.314 -1.707 59.060 1.00 43.67 A O ANISOU 5171 O ASP B 297 6052 5291 5247 -137 -153 160 A O ATOM 5172 CB ASP B 297 -0.170 -1.420 61.820 1.00 44.00 A C ANISOU 5172 CB ASP B 297 5983 5407 5327 -113 -36 27 A C ATOM 5173 CG ASP B 297 -1.695 -1.489 61.915 1.00 46.33 A C ANISOU 5173 CG ASP B 297 6263 5721 5618 -51 -9 -22 A C ATOM 5174 OD1 ASP B 297 -2.395 -0.490 61.610 1.00 47.94 A O ANISOU 5174 OD1 ASP B 297 6573 6033 5609 -187 -135 -221 A O ATOM 5175 OD2 ASP B 297 -2.195 -2.561 62.326 1.00 48.94 A O1- ANISOU 5175 OD2 ASP B 297 6819 5621 6155 42 -107 -206 A O1- ATOM 5176 N SER B 298 -0.381 0.506 58.680 1.00 42.14 A N ANISOU 5176 N SER B 298 5729 5236 5045 -143 -23 16 A N ATOM 5177 CA SER B 298 -0.954 0.356 57.341 1.00 41.81 A C ANISOU 5177 CA SER B 298 5707 5158 5018 -144 37 103 A C ATOM 5178 C SER B 298 -0.016 -0.443 56.464 1.00 40.61 A C ANISOU 5178 C SER B 298 5531 5024 4876 -119 -2 28 A C ATOM 5179 O SER B 298 1.191 -0.224 56.484 1.00 39.20 A O ANISOU 5179 O SER B 298 5477 4819 4596 -175 32 -26 A O ATOM 5180 CB SER B 298 -1.192 1.717 56.670 1.00 43.03 A C ANISOU 5180 CB SER B 298 5768 5309 5270 -67 65 56 A C ATOM 5181 OG SER B 298 0.043 2.353 56.339 1.00 46.62 A O ANISOU 5181 OG SER B 298 6218 5646 5848 -66 253 146 A O ATOM 5182 N GLN B 299 -0.590 -1.366 55.696 1.00 40.12 A N ANISOU 5182 N GLN B 299 5492 4863 4887 -99 12 -22 A N ATOM 5183 CA GLN B 299 0.136 -1.978 54.595 1.00 39.49 A C ANISOU 5183 CA GLN B 299 5443 4787 4772 21 37 -56 A C ATOM 5184 C GLN B 299 0.163 -1.058 53.354 1.00 38.50 A C ANISOU 5184 C GLN B 299 5208 4641 4776 23 119 -73 A C ATOM 5185 O GLN B 299 -0.374 0.045 53.357 1.00 38.29 A O ANISOU 5185 O GLN B 299 5274 4528 4745 199 129 123 A O ATOM 5186 CB GLN B 299 -0.504 -3.319 54.244 1.00 41.16 A C ANISOU 5186 CB GLN B 299 5637 4921 5078 85 15 -120 A C ATOM 5187 CG GLN B 299 -0.403 -4.351 55.367 1.00 43.76 A C ANISOU 5187 CG GLN B 299 6062 5201 5364 -3 -58 -194 A C ATOM 5188 CD GLN B 299 0.863 -5.171 55.257 1.00 48.32 A C ANISOU 5188 CD GLN B 299 6362 5714 6282 -120 -142 -94 A C ATOM 5189 NE2 GLN B 299 0.718 -6.418 54.809 1.00 50.87 A N ANISOU 5189 NE2 GLN B 299 6875 5936 6516 -62 -185 84 A N ATOM 5190 OE1 GLN B 299 1.961 -4.694 55.554 1.00 49.23 A O ANISOU 5190 OE1 GLN B 299 6608 5764 6333 -33 -294 -149 A O ATOM 5191 N ASN B 300 0.757 -1.542 52.273 1.00 36.59 A N ANISOU 5191 N ASN B 300 4940 4447 4516 63 193 -143 A N ATOM 5192 CA ASN B 300 0.802 -0.749 51.052 1.00 36.46 A C ANISOU 5192 CA ASN B 300 4813 4514 4526 -73 212 -171 A C ATOM 5193 C ASN B 300 -0.546 -0.727 50.401 1.00 35.86 A C ANISOU 5193 C ASN B 300 4691 4446 4488 -54 267 -102 A C ATOM 5194 O ASN B 300 -1.331 -1.686 50.530 1.00 36.32 A O ANISOU 5194 O ASN B 300 4640 4452 4705 -106 190 -228 A O ATOM 5195 CB ASN B 300 1.773 -1.354 50.051 1.00 36.00 A C ANISOU 5195 CB ASN B 300 4855 4347 4473 -34 332 -233 A C ATOM 5196 CG ASN B 300 3.220 -0.995 50.321 1.00 38.68 A C ANISOU 5196 CG ASN B 300 5018 4842 4835 -244 97 -216 A C ATOM 5197 ND2 ASN B 300 3.506 -0.349 51.447 1.00 39.53 A N ANISOU 5197 ND2 ASN B 300 5097 5032 4890 -437 204 -89 A N ATOM 5198 OD1 ASN B 300 4.080 -1.306 49.500 1.00 44.37 A O ANISOU 5198 OD1 ASN B 300 5761 5731 5364 -237 458 72 A O ATOM 5199 N LEU B 301 -0.820 0.360 49.705 1.00 34.79 A N ANISOU 5199 N LEU B 301 4533 4433 4251 -22 306 -129 A N ATOM 5200 CA LEU B 301 -2.008 0.446 48.866 1.00 35.74 A C ANISOU 5200 CA LEU B 301 4728 4497 4353 -22 220 -36 A C ATOM 5201 C LEU B 301 -1.592 0.179 47.445 1.00 35.36 A C ANISOU 5201 C LEU B 301 4686 4432 4314 88 188 -26 A C ATOM 5202 O LEU B 301 -0.382 0.228 47.112 1.00 36.13 A O ANISOU 5202 O LEU B 301 4711 4621 4396 19 205 37 A O ATOM 5203 CB LEU B 301 -2.706 1.816 49.000 1.00 35.79 A C ANISOU 5203 CB LEU B 301 4738 4513 4346 -86 166 -73 A C ATOM 5204 CG LEU B 301 -2.030 3.140 48.630 1.00 35.74 A C ANISOU 5204 CG LEU B 301 4844 4549 4186 -127 312 -36 A C ATOM 5205 CD1 LEU B 301 -2.065 3.388 47.123 1.00 37.17 A C ANISOU 5205 CD1 LEU B 301 5244 4732 4144 -119 51 -103 A C ATOM 5206 CD2 LEU B 301 -2.715 4.290 49.355 1.00 36.45 A C ANISOU 5206 CD2 LEU B 301 4876 4519 4453 -136 184 0 A C ATOM 5207 N SER B 302 -2.585 -0.138 46.617 1.00 35.15 A N ANISOU 5207 N SER B 302 4799 4385 4170 119 187 -33 A N ATOM 5208 CA SER B 302 -2.355 -0.384 45.216 1.00 34.55 A C ANISOU 5208 CA SER B 302 4809 4140 4177 185 175 103 A C ATOM 5209 C SER B 302 -3.180 0.619 44.439 1.00 33.31 A C ANISOU 5209 C SER B 302 4540 4117 3997 168 203 52 A C ATOM 5210 O SER B 302 -4.396 0.743 44.665 1.00 32.54 A O ANISOU 5210 O SER B 302 4371 4082 3908 155 230 88 A O ATOM 5211 CB SER B 302 -2.787 -1.801 44.860 1.00 35.56 A C ANISOU 5211 CB SER B 302 4988 4195 4328 252 163 121 A C ATOM 5212 OG SER B 302 -2.766 -1.941 43.470 1.00 38.94 A O ANISOU 5212 OG SER B 302 5690 4403 4699 392 179 216 A O ATOM 5213 N MET B 303 -2.532 1.333 43.523 1.00 32.28 A N ANISOU 5213 N MET B 303 4425 3965 3874 75 281 100 A N ATOM 5214 CA MET B 303 -3.243 2.337 42.732 1.00 31.48 A C ANISOU 5214 CA MET B 303 4282 3961 3715 99 254 45 A C ATOM 5215 C MET B 303 -2.608 2.456 41.374 1.00 30.80 A C ANISOU 5215 C MET B 303 4051 3876 3772 135 310 12 A C ATOM 5216 O MET B 303 -1.443 2.098 41.211 1.00 30.61 A O ANISOU 5216 O MET B 303 4052 3813 3762 202 355 -1 A O ATOM 5217 CB MET B 303 -3.231 3.704 43.439 1.00 32.41 A C ANISOU 5217 CB MET B 303 4356 3987 3969 101 275 59 A C ATOM 5218 CG MET B 303 -1.854 4.306 43.634 1.00 33.20 A C ANISOU 5218 CG MET B 303 4316 4253 4046 83 32 -56 A C ATOM 5219 SD MET B 303 -1.134 5.270 42.279 1.00 33.76 A S ANISOU 5219 SD MET B 303 4570 4138 4116 -203 327 -96 A S ATOM 5220 CE MET B 303 -2.189 6.709 42.125 1.00 35.36 A C ANISOU 5220 CE MET B 303 4842 4205 4385 -151 22 -111 A C ATOM 5221 N ASN B 304 -3.387 2.945 40.404 1.00 30.51 A N ANISOU 5221 N ASN B 304 4009 3956 3626 53 369 16 A N ATOM 5222 CA ASN B 304 -2.881 3.104 39.048 1.00 31.66 A C ANISOU 5222 CA ASN B 304 4046 4083 3900 3 248 50 A C ATOM 5223 C ASN B 304 -2.385 4.557 38.898 1.00 31.02 A C ANISOU 5223 C ASN B 304 3894 3964 3925 -78 275 63 A C ATOM 5224 O ASN B 304 -3.192 5.512 39.099 1.00 29.49 A O ANISOU 5224 O ASN B 304 3663 3855 3684 -97 218 -33 A O ATOM 5225 CB ASN B 304 -4.008 2.765 38.061 1.00 32.61 A C ANISOU 5225 CB ASN B 304 4324 4111 3955 24 101 167 A C ATOM 5226 CG ASN B 304 -3.570 2.779 36.633 1.00 35.83 A C ANISOU 5226 CG ASN B 304 4608 4668 4338 196 158 281 A C ATOM 5227 ND2 ASN B 304 -4.402 2.207 35.775 1.00 41.73 A N ANISOU 5227 ND2 ASN B 304 5364 5376 5115 234 -358 333 A N ATOM 5228 OD1 ASN B 304 -2.539 3.316 36.279 1.00 35.00 A O ANISOU 5228 OD1 ASN B 304 4456 4386 4455 224 18 729 A O ATOM 5229 N PRO B 305 -1.075 4.735 38.564 1.00 30.19 A N ANISOU 5229 N PRO B 305 3697 3897 3876 -223 306 61 A N ATOM 5230 CA PRO B 305 -0.521 6.088 38.468 1.00 30.45 A C ANISOU 5230 CA PRO B 305 3668 4088 3811 -216 365 65 A C ATOM 5231 C PRO B 305 -1.196 6.895 37.370 1.00 29.44 A C ANISOU 5231 C PRO B 305 3534 4066 3585 -240 282 147 A C ATOM 5232 O PRO B 305 -1.036 8.094 37.348 1.00 29.53 A O ANISOU 5232 O PRO B 305 3639 4244 3337 -205 399 119 A O ATOM 5233 CB PRO B 305 0.971 5.868 38.125 1.00 30.95 A C ANISOU 5233 CB PRO B 305 3679 4093 3987 -140 382 191 A C ATOM 5234 CG PRO B 305 1.026 4.473 37.566 1.00 30.98 A C ANISOU 5234 CG PRO B 305 3795 3981 3992 -202 456 219 A C ATOM 5235 CD PRO B 305 -0.041 3.704 38.296 1.00 31.72 A C ANISOU 5235 CD PRO B 305 3893 4116 4040 -187 476 56 A C ATOM 5236 N MET B 306 -1.959 6.252 36.482 1.00 29.73 A N ANISOU 5236 N MET B 306 3646 4135 3515 -292 297 263 A N ATOM 5237 CA MET B 306 -2.717 7.046 35.528 1.00 31.30 A C ANISOU 5237 CA MET B 306 3915 4249 3726 -157 97 212 A C ATOM 5238 C MET B 306 -3.695 8.014 36.195 1.00 30.63 A C ANISOU 5238 C MET B 306 3807 4261 3567 -139 104 155 A C ATOM 5239 O MET B 306 -4.104 8.991 35.580 1.00 30.78 A O ANISOU 5239 O MET B 306 3861 4359 3473 -170 98 131 A O ATOM 5240 CB MET B 306 -3.499 6.191 34.552 1.00 32.53 A C ANISOU 5240 CB MET B 306 4077 4397 3886 -145 10 254 A C ATOM 5241 CG MET B 306 -3.592 6.837 33.250 1.00 38.17 A C ANISOU 5241 CG MET B 306 4954 4856 4692 11 -19 297 A C ATOM 5242 SD MET B 306 -2.033 6.394 32.491 1.00 45.29 A S ANISOU 5242 SD MET B 306 5536 5920 5752 -35 311 649 A S ATOM 5243 CE MET B 306 -2.541 4.740 31.938 1.00 45.83 A C ANISOU 5243 CE MET B 306 6019 6093 5302 80 -391 841 A C ATOM 5244 N LEU B 307 -4.096 7.730 37.436 1.00 29.84 A N ANISOU 5244 N LEU B 307 3654 4286 3396 -92 16 187 A N ATOM 5245 CA LEU B 307 -4.957 8.651 38.169 1.00 29.39 A C ANISOU 5245 CA LEU B 307 3609 4132 3424 -65 43 151 A C ATOM 5246 C LEU B 307 -4.308 10.028 38.350 1.00 29.64 A C ANISOU 5246 C LEU B 307 3694 4110 3457 -124 57 62 A C ATOM 5247 O LEU B 307 -4.988 11.051 38.405 1.00 30.09 A O ANISOU 5247 O LEU B 307 3582 4418 3430 -218 -106 90 A O ATOM 5248 CB LEU B 307 -5.265 8.075 39.555 1.00 29.75 A C ANISOU 5248 CB LEU B 307 3651 4135 3516 -36 108 84 A C ATOM 5249 CG LEU B 307 -6.249 6.892 39.519 1.00 30.70 A C ANISOU 5249 CG LEU B 307 3768 4034 3861 139 151 83 A C ATOM 5250 CD1 LEU B 307 -6.421 6.329 40.937 1.00 32.46 A C ANISOU 5250 CD1 LEU B 307 3880 4388 4064 187 73 -100 A C ATOM 5251 CD2 LEU B 307 -7.606 7.274 38.897 1.00 32.32 A C ANISOU 5251 CD2 LEU B 307 4227 3814 4239 250 -15 -53 A C ATOM 5252 N LEU B 308 -2.985 10.040 38.466 1.00 28.94 A N ANISOU 5252 N LEU B 308 3527 4042 3426 -56 17 77 A N ATOM 5253 CA LEU B 308 -2.252 11.282 38.664 1.00 28.56 A C ANISOU 5253 CA LEU B 308 3692 3761 3398 -182 101 68 A C ATOM 5254 C LEU B 308 -1.864 11.963 37.351 1.00 30.33 A C ANISOU 5254 C LEU B 308 4044 3923 3556 -138 103 91 A C ATOM 5255 O LEU B 308 -1.785 13.181 37.288 1.00 30.80 A O ANISOU 5255 O LEU B 308 4212 3890 3599 -39 20 61 A O ATOM 5256 CB LEU B 308 -0.993 11.031 39.481 1.00 28.02 A C ANISOU 5256 CB LEU B 308 3485 3737 3422 -116 117 148 A C ATOM 5257 CG LEU B 308 -1.236 10.563 40.907 1.00 26.32 A C ANISOU 5257 CG LEU B 308 3313 3471 3215 -411 -113 105 A C ATOM 5258 CD1 LEU B 308 0.051 10.221 41.595 1.00 29.37 A C ANISOU 5258 CD1 LEU B 308 3684 3585 3889 -267 -478 399 A C ATOM 5259 CD2 LEU B 308 -2.036 11.613 41.694 1.00 29.65 A C ANISOU 5259 CD2 LEU B 308 3984 3921 3358 -395 36 479 A C ATOM 5260 N LEU B 309 -1.619 11.169 36.309 1.00 30.95 A N ANISOU 5260 N LEU B 309 4219 4003 3535 -153 359 160 A N ATOM 5261 CA LEU B 309 -1.082 11.725 35.059 1.00 32.47 A C ANISOU 5261 CA LEU B 309 4541 4063 3732 -190 280 138 A C ATOM 5262 C LEU B 309 -1.995 12.735 34.387 1.00 32.63 A C ANISOU 5262 C LEU B 309 4547 4198 3650 -163 236 133 A C ATOM 5263 O LEU B 309 -1.500 13.635 33.732 1.00 33.85 A O ANISOU 5263 O LEU B 309 4637 4181 4043 -226 176 36 A O ATOM 5264 CB LEU B 309 -0.671 10.621 34.092 1.00 32.66 A C ANISOU 5264 CB LEU B 309 4647 4024 3735 -86 353 252 A C ATOM 5265 CG LEU B 309 0.206 11.121 32.933 1.00 33.92 A C ANISOU 5265 CG LEU B 309 4759 4183 3944 -253 230 16 A C ATOM 5266 CD1 LEU B 309 1.615 11.579 33.374 1.00 38.04 A C ANISOU 5266 CD1 LEU B 309 5140 4457 4857 99 413 23 A C ATOM 5267 CD2 LEU B 309 0.254 10.072 31.847 1.00 37.48 A C ANISOU 5267 CD2 LEU B 309 5319 4506 4414 -163 -53 277 A C ATOM 5268 N SER B 310 -3.300 12.641 34.633 1.00 32.15 A N ANISOU 5268 N SER B 310 4532 4213 3468 -167 123 250 A N ATOM 5269 CA SER B 310 -4.258 13.561 34.048 1.00 32.41 A C ANISOU 5269 CA SER B 310 4565 4162 3585 -240 196 295 A C ATOM 5270 C SER B 310 -4.180 14.974 34.700 1.00 32.17 A C ANISOU 5270 C SER B 310 4679 4197 3345 -167 59 248 A C ATOM 5271 O SER B 310 -4.588 15.952 34.118 1.00 31.13 A O ANISOU 5271 O SER B 310 4687 4042 3097 -191 249 228 A O ATOM 5272 CB SER B 310 -5.691 12.961 34.092 1.00 33.02 A C ANISOU 5272 CB SER B 310 4564 4350 3629 -198 170 276 A C ATOM 5273 OG SER B 310 -6.009 12.414 35.388 1.00 32.51 A O ANISOU 5273 OG SER B 310 4038 4334 3979 -337 214 -154 A O ATOM 5274 N GLY B 311 -3.639 15.066 35.907 1.00 31.67 A N ANISOU 5274 N GLY B 311 4713 4174 3146 -141 41 269 A N ATOM 5275 CA GLY B 311 -3.523 16.373 36.534 1.00 30.13 A C ANISOU 5275 CA GLY B 311 4657 4008 2783 -54 98 123 A C ATOM 5276 C GLY B 311 -3.954 16.390 37.974 1.00 30.99 A C ANISOU 5276 C GLY B 311 4663 4102 3007 -11 231 92 A C ATOM 5277 O GLY B 311 -3.925 17.463 38.585 1.00 32.19 A O ANISOU 5277 O GLY B 311 5141 4108 2981 111 381 -16 A O ATOM 5278 N ARG B 312 -4.300 15.217 38.537 1.00 28.93 A N ANISOU 5278 N ARG B 312 4278 3869 2843 -94 24 64 A N ATOM 5279 CA ARG B 312 -4.653 15.163 39.975 1.00 28.88 A C ANISOU 5279 CA ARG B 312 3992 4076 2903 -147 -30 130 A C ATOM 5280 C ARG B 312 -3.449 15.424 40.881 1.00 28.33 A C ANISOU 5280 C ARG B 312 3846 4046 2871 -182 -33 196 A C ATOM 5281 O ARG B 312 -2.293 15.236 40.473 1.00 28.89 A O ANISOU 5281 O ARG B 312 3916 4223 2838 -238 -87 127 A O ATOM 5282 CB ARG B 312 -5.270 13.809 40.370 1.00 27.96 A C ANISOU 5282 CB ARG B 312 3754 3957 2912 -122 -42 171 A C ATOM 5283 CG ARG B 312 -6.664 13.556 39.745 1.00 28.01 A C ANISOU 5283 CG ARG B 312 3549 3945 3145 -116 -141 305 A C ATOM 5284 CD ARG B 312 -7.294 12.260 40.341 1.00 27.96 A C ANISOU 5284 CD ARG B 312 3598 4178 2847 -148 -52 202 A C ATOM 5285 NE ARG B 312 -8.605 11.953 39.777 1.00 30.01 A N ANISOU 5285 NE ARG B 312 3581 4652 3170 -466 -233 -6 A N ATOM 5286 CZ ARG B 312 -8.816 11.234 38.681 1.00 28.35 A C ANISOU 5286 CZ ARG B 312 3330 3953 3486 -263 -176 113 A C ATOM 5287 NH1 ARG B 312 -7.796 10.769 37.939 1.00 30.72 A N1+ ANISOU 5287 NH1 ARG B 312 3817 4257 3596 -195 29 497 A N1+ ATOM 5288 NH2 ARG B 312 -10.075 11.023 38.290 1.00 31.65 A N ANISOU 5288 NH2 ARG B 312 3429 4651 3942 -157 -51 2 A N ATOM 5289 N THR B 313 -3.738 15.879 42.112 1.00 26.68 A N ANISOU 5289 N THR B 313 3816 3849 2471 -241 -100 54 A N ATOM 5290 CA THR B 313 -2.715 16.108 43.123 1.00 27.15 A C ANISOU 5290 CA THR B 313 3772 3873 2670 -206 -109 -51 A C ATOM 5291 C THR B 313 -3.107 15.295 44.335 1.00 26.96 A C ANISOU 5291 C THR B 313 3707 3808 2725 -216 -164 -173 A C ATOM 5292 O THR B 313 -4.262 15.348 44.731 1.00 27.77 A O ANISOU 5292 O THR B 313 3921 4069 2561 -317 -36 -340 A O ATOM 5293 CB THR B 313 -2.728 17.609 43.579 1.00 27.76 A C ANISOU 5293 CB THR B 313 3974 3821 2749 -217 -135 -45 A C ATOM 5294 CG2 THR B 313 -1.743 17.843 44.679 1.00 30.78 A C ANISOU 5294 CG2 THR B 313 4279 4063 3351 -144 -438 78 A C ATOM 5295 OG1 THR B 313 -2.385 18.484 42.494 1.00 30.82 A O ANISOU 5295 OG1 THR B 313 4500 3886 3324 -196 -121 -331 A O ATOM 5296 N TRP B 314 -2.158 14.565 44.940 1.00 26.42 A N ANISOU 5296 N TRP B 314 3630 3871 2537 -114 -183 -50 A N ATOM 5297 CA TRP B 314 -2.445 13.754 46.112 1.00 27.41 A C ANISOU 5297 CA TRP B 314 3787 3898 2728 -48 -193 -31 A C ATOM 5298 C TRP B 314 -1.505 14.215 47.201 1.00 27.88 A C ANISOU 5298 C TRP B 314 3770 4054 2768 30 -178 68 A C ATOM 5299 O TRP B 314 -0.303 14.291 46.987 1.00 28.26 A O ANISOU 5299 O TRP B 314 3926 4144 2666 48 -124 -134 A O ATOM 5300 CB TRP B 314 -2.100 12.307 45.821 1.00 28.42 A C ANISOU 5300 CB TRP B 314 3874 3844 3079 -100 -56 -37 A C ATOM 5301 CG TRP B 314 -2.896 11.284 46.559 1.00 27.57 A C ANISOU 5301 CG TRP B 314 4089 3685 2700 -177 55 53 A C ATOM 5302 CD1 TRP B 314 -3.878 11.492 47.506 1.00 27.19 A C ANISOU 5302 CD1 TRP B 314 3628 3766 2935 -39 -151 -45 A C ATOM 5303 CD2 TRP B 314 -2.725 9.870 46.459 1.00 27.58 A C ANISOU 5303 CD2 TRP B 314 3915 3836 2728 -75 -174 51 A C ATOM 5304 CE2 TRP B 314 -3.667 9.274 47.307 1.00 28.92 A C ANISOU 5304 CE2 TRP B 314 4103 3662 3221 -131 65 -112 A C ATOM 5305 CE3 TRP B 314 -1.896 9.049 45.675 1.00 28.75 A C ANISOU 5305 CE3 TRP B 314 4052 3699 3170 -369 -171 29 A C ATOM 5306 NE1 TRP B 314 -4.340 10.281 47.963 1.00 28.87 A N ANISOU 5306 NE1 TRP B 314 4080 3731 3159 -105 -231 70 A N ATOM 5307 CZ2 TRP B 314 -3.769 7.883 47.438 1.00 29.94 A C ANISOU 5307 CZ2 TRP B 314 4250 3547 3575 -208 119 19 A C ATOM 5308 CZ3 TRP B 314 -2.007 7.681 45.790 1.00 29.68 A C ANISOU 5308 CZ3 TRP B 314 4079 3808 3388 -229 -131 -20 A C ATOM 5309 CH2 TRP B 314 -2.944 7.110 46.643 1.00 31.51 A C ANISOU 5309 CH2 TRP B 314 4555 3845 3570 -188 94 -47 A C ATOM 5310 N LYS B 315 -2.053 14.533 48.367 1.00 26.67 A N ANISOU 5310 N LYS B 315 3779 3951 2403 68 -284 -54 A N ATOM 5311 CA LYS B 315 -1.174 14.964 49.437 1.00 28.19 A C ANISOU 5311 CA LYS B 315 3897 4018 2794 80 -177 87 A C ATOM 5312 C LYS B 315 -1.624 14.505 50.792 1.00 27.10 A C ANISOU 5312 C LYS B 315 3855 3818 2623 -31 -184 -32 A C ATOM 5313 O LYS B 315 -2.742 14.091 50.971 1.00 27.78 A O ANISOU 5313 O LYS B 315 3963 3828 2764 -262 -172 2 A O ATOM 5314 CB LYS B 315 -0.999 16.479 49.436 1.00 29.86 A C ANISOU 5314 CB LYS B 315 4211 4000 3133 -33 -210 5 A C ATOM 5315 CG LYS B 315 -2.240 17.295 49.588 1.00 32.02 A C ANISOU 5315 CG LYS B 315 4001 4597 3566 219 -67 17 A C ATOM 5316 CD LYS B 315 -2.021 18.631 48.875 1.00 35.43 A C ANISOU 5316 CD LYS B 315 4925 4613 3923 130 167 -324 A C ATOM 5317 CE LYS B 315 -0.983 19.476 49.620 1.00 38.58 A C ANISOU 5317 CE LYS B 315 5146 4837 4674 47 220 -245 A C ATOM 5318 NZ LYS B 315 -0.409 20.590 48.805 1.00 43.46 A N1+ ANISOU 5318 NZ LYS B 315 6124 4917 5471 0 302 -516 A N1+ ATOM 5319 N GLY B 316 -0.708 14.567 51.756 1.00 27.12 A N ANISOU 5319 N GLY B 316 3879 3992 2432 84 -102 109 A N ATOM 5320 CA GLY B 316 -1.092 14.272 53.132 1.00 27.27 A C ANISOU 5320 CA GLY B 316 3993 3899 2467 234 57 54 A C ATOM 5321 C GLY B 316 -0.461 15.318 54.007 1.00 29.20 A C ANISOU 5321 C GLY B 316 4368 4011 2717 244 97 51 A C ATOM 5322 O GLY B 316 0.318 16.165 53.529 1.00 29.62 A O ANISOU 5322 O GLY B 316 4464 3880 2909 309 -12 58 A O ATOM 5323 N ALA B 317 -0.799 15.258 55.288 1.00 28.83 A N ANISOU 5323 N ALA B 317 4623 3844 2487 176 -13 47 A N ATOM 5324 CA ALA B 317 -0.236 16.182 56.254 1.00 29.32 A C ANISOU 5324 CA ALA B 317 4716 3820 2604 91 50 74 A C ATOM 5325 C ALA B 317 -0.457 15.689 57.679 1.00 29.49 A C ANISOU 5325 C ALA B 317 4721 3763 2722 180 42 10 A C ATOM 5326 O ALA B 317 -1.345 14.881 57.945 1.00 31.30 A O ANISOU 5326 O ALA B 317 4878 4146 2866 233 20 161 A O ATOM 5327 CB ALA B 317 -0.855 17.551 56.059 1.00 30.23 A C ANISOU 5327 CB ALA B 317 4953 3745 2788 43 -50 94 A C ATOM 5328 N ILE B 318 0.373 16.209 58.579 1.00 28.91 A N ANISOU 5328 N ILE B 318 4684 3671 2628 243 47 48 A N ATOM 5329 CA ILE B 318 0.204 16.024 60.009 1.00 29.35 A C ANISOU 5329 CA ILE B 318 4577 3744 2828 230 64 32 A C ATOM 5330 C ILE B 318 -0.320 17.356 60.604 1.00 27.68 A C ANISOU 5330 C ILE B 318 4338 3501 2678 314 75 1 A C ATOM 5331 O ILE B 318 0.042 18.453 60.165 1.00 28.07 A O ANISOU 5331 O ILE B 318 4316 3491 2858 566 72 124 A O ATOM 5332 CB ILE B 318 1.567 15.514 60.678 1.00 29.91 A C ANISOU 5332 CB ILE B 318 4611 3817 2936 166 114 62 A C ATOM 5333 CG1 ILE B 318 1.966 14.130 60.112 1.00 31.62 A C ANISOU 5333 CG1 ILE B 318 4583 4210 3220 -22 26 50 A C ATOM 5334 CG2 ILE B 318 1.457 15.461 62.198 1.00 31.27 A C ANISOU 5334 CG2 ILE B 318 4571 4218 3090 218 64 -115 A C ATOM 5335 CD1 ILE B 318 3.347 13.567 60.563 1.00 33.35 A C ANISOU 5335 CD1 ILE B 318 4872 4155 3642 64 -36 81 A C ATOM 5336 N PHE B 319 -1.223 17.266 61.564 1.00 26.58 A N ANISOU 5336 N PHE B 319 4032 3291 2775 325 56 87 A N ATOM 5337 CA PHE B 319 -1.720 18.434 62.286 1.00 27.24 A C ANISOU 5337 CA PHE B 319 4185 3389 2774 317 83 -4 A C ATOM 5338 C PHE B 319 -2.272 19.475 61.350 1.00 27.18 A C ANISOU 5338 C PHE B 319 4088 3418 2821 215 118 -5 A C ATOM 5339 O PHE B 319 -2.041 20.683 61.543 1.00 27.78 A O ANISOU 5339 O PHE B 319 4503 3418 2632 290 77 -163 A O ATOM 5340 CB PHE B 319 -0.650 19.074 63.173 1.00 27.14 A C ANISOU 5340 CB PHE B 319 4100 3348 2864 342 117 58 A C ATOM 5341 CG PHE B 319 -1.243 19.976 64.246 1.00 27.03 A C ANISOU 5341 CG PHE B 319 4379 3257 2631 399 212 81 A C ATOM 5342 CD1 PHE B 319 -2.258 19.506 65.114 1.00 28.04 A C ANISOU 5342 CD1 PHE B 319 4449 3221 2982 433 461 301 A C ATOM 5343 CD2 PHE B 319 -0.782 21.278 64.409 1.00 27.40 A C ANISOU 5343 CD2 PHE B 319 4260 3087 3063 244 132 283 A C ATOM 5344 CE1 PHE B 319 -2.799 20.350 66.129 1.00 27.14 A C ANISOU 5344 CE1 PHE B 319 4347 3097 2866 517 383 248 A C ATOM 5345 CE2 PHE B 319 -1.322 22.120 65.416 1.00 29.94 A C ANISOU 5345 CE2 PHE B 319 4395 3652 3327 322 546 175 A C ATOM 5346 CZ PHE B 319 -2.308 21.658 66.273 1.00 27.76 A C ANISOU 5346 CZ PHE B 319 4256 3330 2960 476 430 116 A C ATOM 5347 N GLY B 320 -2.945 18.997 60.312 1.00 27.59 A N ANISOU 5347 N GLY B 320 4050 3612 2818 134 187 14 A N ATOM 5348 CA GLY B 320 -3.627 19.889 59.384 1.00 27.80 A C ANISOU 5348 CA GLY B 320 4156 3542 2862 242 201 -111 A C ATOM 5349 C GLY B 320 -2.758 20.842 58.603 1.00 27.79 A C ANISOU 5349 C GLY B 320 4222 3498 2836 246 223 -55 A C ATOM 5350 O GLY B 320 -3.285 21.823 58.055 1.00 29.30 A O ANISOU 5350 O GLY B 320 4505 3607 3020 230 190 -85 A O ATOM 5351 N GLY B 321 -1.450 20.547 58.551 1.00 28.05 A N ANISOU 5351 N GLY B 321 4280 3608 2770 368 275 -178 A N ATOM 5352 CA GLY B 321 -0.460 21.378 57.860 1.00 28.27 A C ANISOU 5352 CA GLY B 321 4260 3594 2886 443 380 -4 A C ATOM 5353 C GLY B 321 -0.087 22.664 58.595 1.00 28.51 A C ANISOU 5353 C GLY B 321 4355 3677 2799 495 288 -44 A C ATOM 5354 O GLY B 321 0.751 23.463 58.108 1.00 30.34 A O ANISOU 5354 O GLY B 321 4602 3902 3023 614 336 -152 A O ATOM 5355 N PHE B 322 -0.658 22.846 59.787 1.00 29.10 A N ANISOU 5355 N PHE B 322 4521 3610 2924 233 301 -15 A N ATOM 5356 CA PHE B 322 -0.366 23.994 60.621 1.00 29.35 A C ANISOU 5356 CA PHE B 322 4552 3651 2947 268 155 1 A C ATOM 5357 C PHE B 322 1.012 23.947 61.286 1.00 29.78 A C ANISOU 5357 C PHE B 322 4703 3562 3047 219 167 35 A C ATOM 5358 O PHE B 322 1.380 22.966 61.945 1.00 30.38 A O ANISOU 5358 O PHE B 322 4866 3614 3063 204 1 2 A O ATOM 5359 CB PHE B 322 -1.438 24.136 61.731 1.00 30.08 A C ANISOU 5359 CB PHE B 322 4626 3761 3040 94 193 213 A C ATOM 5360 CG PHE B 322 -2.818 24.557 61.250 1.00 30.87 A C ANISOU 5360 CG PHE B 322 4632 3867 3229 123 136 216 A C ATOM 5361 CD1 PHE B 322 -3.025 25.747 60.540 1.00 30.60 A C ANISOU 5361 CD1 PHE B 322 4504 3676 3446 140 1 258 A C ATOM 5362 CD2 PHE B 322 -3.929 23.794 61.579 1.00 30.23 A C ANISOU 5362 CD2 PHE B 322 4626 3555 3305 122 180 170 A C ATOM 5363 CE1 PHE B 322 -4.301 26.147 60.128 1.00 30.01 A C ANISOU 5363 CE1 PHE B 322 4414 3213 3774 18 285 169 A C ATOM 5364 CE2 PHE B 322 -5.218 24.179 61.178 1.00 29.78 A C ANISOU 5364 CE2 PHE B 322 4528 3389 3395 -69 243 333 A C ATOM 5365 CZ PHE B 322 -5.402 25.369 60.438 1.00 30.18 A C ANISOU 5365 CZ PHE B 322 4365 3639 3463 55 201 295 A C ATOM 5366 N LYS B 323 1.757 25.023 61.116 1.00 30.43 A N ANISOU 5366 N LYS B 323 4692 3761 3109 295 199 59 A N ATOM 5367 CA LYS B 323 2.898 25.323 61.988 1.00 29.86 A C ANISOU 5367 CA LYS B 323 4728 3540 3075 295 161 -79 A C ATOM 5368 C LYS B 323 2.303 25.511 63.372 1.00 30.23 A C ANISOU 5368 C LYS B 323 4769 3536 3177 230 198 -185 A C ATOM 5369 O LYS B 323 1.485 26.399 63.613 1.00 30.71 A O ANISOU 5369 O LYS B 323 4892 3516 3258 243 181 -212 A O ATOM 5370 CB LYS B 323 3.575 26.591 61.483 1.00 30.67 A C ANISOU 5370 CB LYS B 323 4831 3628 3190 296 245 -110 A C ATOM 5371 CG LYS B 323 4.323 26.343 60.163 1.00 31.34 A C ANISOU 5371 CG LYS B 323 4939 3860 3107 448 243 -39 A C ATOM 5372 CD LYS B 323 5.146 27.532 59.795 1.00 32.68 A C ANISOU 5372 CD LYS B 323 5232 3860 3324 471 320 -185 A C ATOM 5373 CE LYS B 323 5.834 27.356 58.478 1.00 34.56 A C ANISOU 5373 CE LYS B 323 5345 4180 3605 38 453 86 A C ATOM 5374 NZ LYS B 323 7.020 26.463 58.564 1.00 35.47 A N1+ ANISOU 5374 NZ LYS B 323 5354 4567 3553 36 199 -37 A N1+ ATOM 5375 N SER B 324 2.686 24.653 64.299 1.00 29.56 A N ANISOU 5375 N SER B 324 4745 3395 3092 275 128 -180 A N ATOM 5376 CA SER B 324 1.809 24.481 65.470 1.00 28.92 A C ANISOU 5376 CA SER B 324 4737 3255 2996 201 159 -102 A C ATOM 5377 C SER B 324 1.806 25.652 66.462 1.00 29.98 A C ANISOU 5377 C SER B 324 4885 3290 3215 100 98 -127 A C ATOM 5378 O SER B 324 0.722 26.068 66.919 1.00 30.67 A O ANISOU 5378 O SER B 324 4915 3564 3174 -106 55 -19 A O ATOM 5379 CB SER B 324 2.191 23.227 66.206 1.00 30.41 A C ANISOU 5379 CB SER B 324 4786 3361 3405 170 99 -152 A C ATOM 5380 OG SER B 324 3.565 23.268 66.479 1.00 28.83 A O ANISOU 5380 OG SER B 324 4613 3091 3251 452 218 -296 A O ATOM 5381 N LYS B 325 2.985 26.148 66.825 1.00 30.64 A N ANISOU 5381 N LYS B 325 5052 3260 3329 93 68 -50 A N ATOM 5382 CA LYS B 325 3.039 27.230 67.834 1.00 30.97 A C ANISOU 5382 CA LYS B 325 5061 3156 3547 89 71 73 A C ATOM 5383 C LYS B 325 2.451 28.551 67.275 1.00 31.22 A C ANISOU 5383 C LYS B 325 5103 3130 3626 93 -18 80 A C ATOM 5384 O LYS B 325 1.850 29.317 68.013 1.00 32.75 A O ANISOU 5384 O LYS B 325 5142 3358 3942 -11 74 -5 A O ATOM 5385 CB LYS B 325 4.438 27.400 68.409 1.00 31.11 A C ANISOU 5385 CB LYS B 325 5113 3179 3526 104 128 145 A C ATOM 5386 CG LYS B 325 4.555 28.367 69.627 1.00 32.03 A C ANISOU 5386 CG LYS B 325 5180 3320 3667 217 -12 42 A C ATOM 5387 CD LYS B 325 5.725 27.975 70.463 1.00 34.82 A C ANISOU 5387 CD LYS B 325 5035 3761 4434 299 -121 73 A C ATOM 5388 CE LYS B 325 5.813 28.766 71.746 1.00 35.49 A C ANISOU 5388 CE LYS B 325 5383 3826 4274 266 -205 -24 A C ATOM 5389 NZ LYS B 325 6.739 28.117 72.722 1.00 33.62 A N1+ ANISOU 5389 NZ LYS B 325 5091 3523 4159 264 -214 116 A N1+ ATOM 5390 N ASP B 326 2.644 28.820 65.995 1.00 32.04 A N ANISOU 5390 N ASP B 326 5233 3151 3787 108 31 43 A N ATOM 5391 CA ASP B 326 1.947 29.919 65.299 1.00 32.79 A C ANISOU 5391 CA ASP B 326 5279 3273 3906 55 -35 -40 A C ATOM 5392 C ASP B 326 0.436 29.798 65.237 1.00 32.69 A C ANISOU 5392 C ASP B 326 5304 3394 3723 57 44 -136 A C ATOM 5393 O ASP B 326 -0.308 30.786 65.435 1.00 33.67 A O ANISOU 5393 O ASP B 326 5476 3418 3899 -6 -10 -95 A O ATOM 5394 CB ASP B 326 2.411 30.019 63.845 1.00 34.14 A C ANISOU 5394 CB ASP B 326 5328 3533 4109 129 33 -126 A C ATOM 5395 CG ASP B 326 3.855 30.482 63.698 1.00 35.58 A C ANISOU 5395 CG ASP B 326 5358 3547 4612 85 68 -198 A C ATOM 5396 OD1 ASP B 326 4.416 31.023 64.663 1.00 39.28 A O ANISOU 5396 OD1 ASP B 326 5709 4014 5199 233 -140 -299 A O ATOM 5397 OD2 ASP B 326 4.417 30.291 62.597 1.00 39.37 A O1- ANISOU 5397 OD2 ASP B 326 5838 3896 5223 173 383 -569 A O1- ATOM 5398 N SER B 327 -0.033 28.595 64.923 1.00 31.86 A N ANISOU 5398 N SER B 327 5179 3395 3529 35 -22 -281 A N ATOM 5399 CA SER B 327 -1.403 28.410 64.509 1.00 32.53 A C ANISOU 5399 CA SER B 327 5158 3642 3559 40 6 -311 A C ATOM 5400 C SER B 327 -2.335 28.179 65.682 1.00 32.40 A C ANISOU 5400 C SER B 327 5171 3691 3446 -93 -16 -390 A C ATOM 5401 O SER B 327 -3.459 28.667 65.688 1.00 33.36 A O ANISOU 5401 O SER B 327 5196 3990 3488 -178 -56 -359 A O ATOM 5402 CB SER B 327 -1.473 27.220 63.579 1.00 31.88 A C ANISOU 5402 CB SER B 327 5020 3718 3375 60 -19 -216 A C ATOM 5403 OG SER B 327 -0.813 27.504 62.362 1.00 33.87 A O ANISOU 5403 OG SER B 327 5338 3817 3714 427 18 -455 A O ATOM 5404 N VAL B 328 -1.890 27.435 66.695 1.00 32.71 A N ANISOU 5404 N VAL B 328 5236 3683 3509 -113 -78 -322 A N ATOM 5405 CA VAL B 328 -2.803 27.126 67.778 1.00 31.82 A C ANISOU 5405 CA VAL B 328 5309 3514 3266 -197 23 -299 A C ATOM 5406 C VAL B 328 -3.407 28.385 68.454 1.00 31.90 A C ANISOU 5406 C VAL B 328 5239 3582 3299 -169 50 -285 A C ATOM 5407 O VAL B 328 -4.614 28.445 68.652 1.00 31.88 A O ANISOU 5407 O VAL B 328 5392 3420 3298 -281 93 -309 A O ATOM 5408 CB VAL B 328 -2.148 26.106 68.778 1.00 31.28 A C ANISOU 5408 CB VAL B 328 5302 3341 3242 -158 21 -358 A C ATOM 5409 CG1 VAL B 328 -2.876 26.096 70.118 1.00 32.76 A C ANISOU 5409 CG1 VAL B 328 5305 3828 3312 74 163 -68 A C ATOM 5410 CG2 VAL B 328 -2.145 24.703 68.127 1.00 31.98 A C ANISOU 5410 CG2 VAL B 328 5550 3458 3143 -210 56 -172 A C ATOM 5411 N PRO B 329 -2.580 29.388 68.784 1.00 32.02 A N ANISOU 5411 N PRO B 329 5210 3596 3359 -199 142 -164 A N ATOM 5412 CA PRO B 329 -3.222 30.555 69.367 1.00 33.22 A C ANISOU 5412 CA PRO B 329 5251 3688 3682 -164 85 -169 A C ATOM 5413 C PRO B 329 -4.205 31.233 68.423 1.00 34.04 A C ANISOU 5413 C PRO B 329 5262 3723 3946 -181 174 -209 A C ATOM 5414 O PRO B 329 -5.222 31.753 68.891 1.00 35.53 A O ANISOU 5414 O PRO B 329 5300 3903 4296 -168 154 -200 A O ATOM 5415 CB PRO B 329 -2.035 31.441 69.741 1.00 33.59 A C ANISOU 5415 CB PRO B 329 5216 3743 3800 -150 118 -148 A C ATOM 5416 CG PRO B 329 -0.882 30.475 69.920 1.00 33.09 A C ANISOU 5416 CG PRO B 329 5332 3621 3620 -126 75 -88 A C ATOM 5417 CD PRO B 329 -1.118 29.552 68.760 1.00 32.85 A C ANISOU 5417 CD PRO B 329 5244 3763 3471 -71 99 -52 A C ATOM 5418 N LYS B 330 -3.917 31.229 67.120 1.00 34.37 A N ANISOU 5418 N LYS B 330 5329 3807 3920 -195 6 -103 A N ATOM 5419 CA LYS B 330 -4.822 31.809 66.124 1.00 35.17 A C ANISOU 5419 CA LYS B 330 5435 3834 4093 -246 76 -219 A C ATOM 5420 C LYS B 330 -6.119 31.052 66.040 1.00 34.56 A C ANISOU 5420 C LYS B 330 5361 3849 3921 -327 -69 -208 A C ATOM 5421 O LYS B 330 -7.190 31.646 65.927 1.00 34.95 A O ANISOU 5421 O LYS B 330 5569 3690 4020 -468 18 -164 A O ATOM 5422 CB LYS B 330 -4.158 31.838 64.761 1.00 35.43 A C ANISOU 5422 CB LYS B 330 5350 3965 4146 -237 73 -228 A C ATOM 5423 CG LYS B 330 -3.042 32.847 64.666 1.00 38.35 A C ANISOU 5423 CG LYS B 330 5407 4338 4825 -59 89 -41 A C ATOM 5424 CD LYS B 330 -2.440 32.782 63.264 1.00 42.76 A C ANISOU 5424 CD LYS B 330 5851 5305 5088 -12 30 -120 A C ATOM 5425 CE LYS B 330 -1.967 34.144 62.817 1.00 46.32 A C ANISOU 5425 CE LYS B 330 6044 5521 6035 154 -8 23 A C ATOM 5426 NZ LYS B 330 -0.796 34.558 63.644 1.00 48.38 A N1+ ANISOU 5426 NZ LYS B 330 5982 6027 6370 60 -216 185 A N1+ ATOM 5427 N LEU B 331 -6.038 29.724 66.107 1.00 34.12 A N ANISOU 5427 N LEU B 331 5418 3787 3759 -377 15 -217 A N ATOM 5428 CA LEU B 331 -7.242 28.906 66.118 1.00 34.70 A C ANISOU 5428 CA LEU B 331 5355 4017 3811 -372 33 -253 A C ATOM 5429 C LEU B 331 -8.084 29.144 67.374 1.00 34.71 A C ANISOU 5429 C LEU B 331 5330 4045 3813 -331 19 -273 A C ATOM 5430 O LEU B 331 -9.317 29.172 67.312 1.00 34.91 A O ANISOU 5430 O LEU B 331 5439 4055 3768 -406 -207 -406 A O ATOM 5431 CB LEU B 331 -6.890 27.428 65.956 1.00 34.03 A C ANISOU 5431 CB LEU B 331 5388 3869 3672 -272 114 -320 A C ATOM 5432 CG LEU B 331 -6.238 27.099 64.597 1.00 36.63 A C ANISOU 5432 CG LEU B 331 5584 4443 3891 -297 102 -135 A C ATOM 5433 CD1 LEU B 331 -5.523 25.757 64.615 1.00 36.21 A C ANISOU 5433 CD1 LEU B 331 5582 4396 3778 -261 130 50 A C ATOM 5434 CD2 LEU B 331 -7.221 27.236 63.406 1.00 38.37 A C ANISOU 5434 CD2 LEU B 331 5568 4678 4330 -88 -55 -426 A C ATOM 5435 N VAL B 332 -7.435 29.337 68.516 1.00 36.04 A N ANISOU 5435 N VAL B 332 5357 4273 4062 -367 -8 -286 A N ATOM 5436 CA VAL B 332 -8.192 29.623 69.737 1.00 37.04 A C ANISOU 5436 CA VAL B 332 5418 4415 4241 -369 36 -243 A C ATOM 5437 C VAL B 332 -8.877 30.983 69.616 1.00 38.30 A C ANISOU 5437 C VAL B 332 5513 4513 4524 -374 9 -305 A C ATOM 5438 O VAL B 332 -10.030 31.128 70.003 1.00 38.38 A O ANISOU 5438 O VAL B 332 5434 4571 4574 -412 -86 -471 A O ATOM 5439 CB VAL B 332 -7.315 29.549 70.999 1.00 37.07 A C ANISOU 5439 CB VAL B 332 5445 4525 4114 -361 98 -121 A C ATOM 5440 CG1 VAL B 332 -8.055 30.112 72.223 1.00 35.39 A C ANISOU 5440 CG1 VAL B 332 5206 4237 4004 -179 215 -37 A C ATOM 5441 CG2 VAL B 332 -6.937 28.130 71.259 1.00 37.03 A C ANISOU 5441 CG2 VAL B 332 5405 4500 4163 -332 324 -107 A C ATOM 5442 N ALA B 333 -8.152 31.967 69.084 1.00 39.82 A N ANISOU 5442 N ALA B 333 5771 4551 4808 -336 -25 -308 A N ATOM 5443 CA ALA B 333 -8.711 33.316 68.874 1.00 41.13 A C ANISOU 5443 CA ALA B 333 5791 4716 5118 -310 -54 -264 A C ATOM 5444 C ALA B 333 -9.879 33.278 67.900 1.00 41.80 A C ANISOU 5444 C ALA B 333 5870 4777 5233 -282 -39 -266 A C ATOM 5445 O ALA B 333 -10.877 33.974 68.098 1.00 42.04 A O ANISOU 5445 O ALA B 333 5872 4712 5389 -206 48 -142 A O ATOM 5446 CB ALA B 333 -7.627 34.256 68.382 1.00 41.41 A C ANISOU 5446 CB ALA B 333 5939 4678 5117 -279 -10 -321 A C ATOM 5447 N ASP B 334 -9.769 32.439 66.863 1.00 42.17 A N ANISOU 5447 N ASP B 334 5945 4843 5233 -282 -86 -287 A N ATOM 5448 CA ASP B 334 -10.880 32.236 65.932 1.00 42.59 A C ANISOU 5448 CA ASP B 334 5949 4861 5369 -297 -85 -434 A C ATOM 5449 C ASP B 334 -12.089 31.680 66.686 1.00 42.23 A C ANISOU 5449 C ASP B 334 5882 4858 5302 -383 -112 -506 A C ATOM 5450 O ASP B 334 -13.225 32.044 66.419 1.00 42.74 A O ANISOU 5450 O ASP B 334 5964 4867 5405 -447 -154 -659 A O ATOM 5451 CB ASP B 334 -10.473 31.304 64.778 1.00 43.45 A C ANISOU 5451 CB ASP B 334 6095 5046 5368 -254 -51 -357 A C ATOM 5452 CG ASP B 334 -9.514 31.968 63.777 1.00 45.60 A C ANISOU 5452 CG ASP B 334 6273 5272 5780 -156 134 -217 A C ATOM 5453 OD1 ASP B 334 -9.396 33.211 63.765 1.00 48.18 A O ANISOU 5453 OD1 ASP B 334 6717 5446 6140 -213 56 34 A O ATOM 5454 OD2 ASP B 334 -8.869 31.240 62.981 1.00 48.86 A O1- ANISOU 5454 OD2 ASP B 334 6949 5593 6021 -155 255 -34 A O1- ATOM 5455 N PHE B 335 -11.841 30.779 67.639 1.00 40.54 A N ANISOU 5455 N PHE B 335 5736 4591 5075 -446 -186 -652 A N ATOM 5456 CA PHE B 335 -12.936 30.241 68.438 1.00 41.37 A C ANISOU 5456 CA PHE B 335 5726 4710 5282 -412 -130 -532 A C ATOM 5457 C PHE B 335 -13.497 31.322 69.355 1.00 42.17 A C ANISOU 5457 C PHE B 335 5801 4822 5398 -415 -123 -529 A C ATOM 5458 O PHE B 335 -14.698 31.411 69.560 1.00 42.59 A O ANISOU 5458 O PHE B 335 5876 4833 5472 -360 -34 -601 A O ATOM 5459 CB PHE B 335 -12.462 29.029 69.271 1.00 40.24 A C ANISOU 5459 CB PHE B 335 5588 4636 5064 -459 -145 -579 A C ATOM 5460 CG PHE B 335 -13.535 28.441 70.170 1.00 39.62 A C ANISOU 5460 CG PHE B 335 5423 4477 5153 -307 -126 -330 A C ATOM 5461 CD1 PHE B 335 -14.514 27.598 69.659 1.00 40.98 A C ANISOU 5461 CD1 PHE B 335 5474 4679 5415 -206 71 -263 A C ATOM 5462 CD2 PHE B 335 -13.557 28.736 71.527 1.00 37.57 A C ANISOU 5462 CD2 PHE B 335 5210 4028 5036 -589 -148 -652 A C ATOM 5463 CE1 PHE B 335 -15.513 27.070 70.489 1.00 39.98 A C ANISOU 5463 CE1 PHE B 335 5565 4397 5226 -237 27 -354 A C ATOM 5464 CE2 PHE B 335 -14.542 28.215 72.366 1.00 35.59 A C ANISOU 5464 CE2 PHE B 335 4847 3757 4919 -682 -66 -315 A C ATOM 5465 CZ PHE B 335 -15.513 27.372 71.854 1.00 37.97 A C ANISOU 5465 CZ PHE B 335 5134 4120 5171 -417 -49 -257 A C ATOM 5466 N MET B 336 -12.623 32.164 69.889 1.00 44.05 A N ANISOU 5466 N MET B 336 6021 5033 5681 -368 -118 -397 A N ATOM 5467 CA MET B 336 -13.057 33.185 70.841 1.00 45.97 A C ANISOU 5467 CA MET B 336 6181 5283 6001 -466 -66 -281 A C ATOM 5468 C MET B 336 -13.783 34.310 70.115 1.00 47.44 A C ANISOU 5468 C MET B 336 6312 5505 6208 -440 -74 -284 A C ATOM 5469 O MET B 336 -14.594 35.018 70.713 1.00 49.06 A O ANISOU 5469 O MET B 336 6420 5733 6485 -480 -58 -253 A O ATOM 5470 CB MET B 336 -11.874 33.733 71.630 1.00 46.14 A C ANISOU 5470 CB MET B 336 6269 5266 5995 -448 -66 -205 A C ATOM 5471 CG MET B 336 -11.249 32.741 72.620 1.00 46.67 A C ANISOU 5471 CG MET B 336 6488 5039 6202 -676 -2 -113 A C ATOM 5472 SD MET B 336 -12.389 32.106 73.868 1.00 47.86 A S ANISOU 5472 SD MET B 336 7049 4682 6452 -1182 225 -12 A S ATOM 5473 CE MET B 336 -12.602 33.547 74.916 1.00 47.17 A C ANISOU 5473 CE MET B 336 6658 5108 6154 -821 219 220 A C ATOM 5474 N ALA B 337 -13.501 34.438 68.824 1.00 48.34 A N ANISOU 5474 N ALA B 337 6379 5672 6313 -427 -99 -351 A N ATOM 5475 CA ALA B 337 -14.163 35.406 67.945 1.00 48.95 A C ANISOU 5475 CA ALA B 337 6399 5762 6437 -425 -146 -374 A C ATOM 5476 C ALA B 337 -15.468 34.843 67.403 1.00 49.81 A C ANISOU 5476 C ALA B 337 6490 5904 6530 -367 -160 -370 A C ATOM 5477 O ALA B 337 -16.142 35.489 66.585 1.00 50.43 A O ANISOU 5477 O ALA B 337 6597 5929 6634 -422 -198 -462 A O ATOM 5478 CB ALA B 337 -13.242 35.780 66.801 1.00 48.94 A C ANISOU 5478 CB ALA B 337 6370 5802 6421 -447 -124 -393 A C ATOM 5479 N LYS B 338 -15.818 33.646 67.879 1.00 50.19 A N ANISOU 5479 N LYS B 338 6523 5959 6587 -299 -132 -329 A N ATOM 5480 CA LYS B 338 -17.000 32.881 67.463 1.00 50.34 A C ANISOU 5480 CA LYS B 338 6502 6042 6582 -250 -131 -299 A C ATOM 5481 C LYS B 338 -17.040 32.551 65.964 1.00 50.17 A C ANISOU 5481 C LYS B 338 6476 6023 6564 -244 -154 -361 A C ATOM 5482 O LYS B 338 -18.103 32.435 65.375 1.00 51.00 A O ANISOU 5482 O LYS B 338 6524 6158 6694 -245 -175 -381 A O ATOM 5483 CB LYS B 338 -18.302 33.522 67.993 1.00 50.30 A C ANISOU 5483 CB LYS B 338 6488 6068 6552 -234 -143 -282 A C ATOM 5484 CG LYS B 338 -18.311 33.656 69.519 1.00 50.36 A C ANISOU 5484 CG LYS B 338 6502 6049 6581 -119 -19 -157 A C ATOM 5485 CD LYS B 338 -19.391 34.601 70.052 1.00 50.74 A C ANISOU 5485 CD LYS B 338 6573 6131 6574 -203 -134 -195 A C ATOM 5486 CE LYS B 338 -19.041 35.067 71.466 1.00 51.69 A C ANISOU 5486 CE LYS B 338 6849 6380 6408 -181 129 -201 A C ATOM 5487 NZ LYS B 338 -19.895 36.216 71.951 1.00 52.21 A N1+ ANISOU 5487 NZ LYS B 338 7159 6188 6487 -158 -110 -203 A N1+ ATOM 5488 N LYS B 339 -15.867 32.364 65.365 1.00 50.03 A N ANISOU 5488 N LYS B 339 6515 5990 6505 -258 -162 -446 A N ATOM 5489 CA LYS B 339 -15.762 31.959 63.960 1.00 50.03 A C ANISOU 5489 CA LYS B 339 6499 6011 6498 -213 -180 -408 A C ATOM 5490 C LYS B 339 -16.245 30.542 63.698 1.00 48.94 A C ANISOU 5490 C LYS B 339 6419 5879 6296 -235 -237 -469 A C ATOM 5491 O LYS B 339 -16.722 30.236 62.610 1.00 49.09 A O ANISOU 5491 O LYS B 339 6553 5821 6278 -246 -258 -491 A O ATOM 5492 CB LYS B 339 -14.329 32.125 63.438 1.00 50.35 A C ANISOU 5492 CB LYS B 339 6448 6121 6560 -260 -199 -431 A C ATOM 5493 CG LYS B 339 -14.047 33.454 62.740 1.00 51.72 A C ANISOU 5493 CG LYS B 339 6604 6213 6831 -96 -123 -353 A C ATOM 5494 CD LYS B 339 -12.539 33.696 62.601 1.00 51.93 A C ANISOU 5494 CD LYS B 339 6626 6299 6804 -152 -52 -342 A C ATOM 5495 CE LYS B 339 -12.221 35.135 62.188 1.00 54.15 A C ANISOU 5495 CE LYS B 339 6815 6432 7327 -12 10 -135 A C ATOM 5496 NZ LYS B 339 -10.802 35.504 62.495 1.00 55.28 A N1+ ANISOU 5496 NZ LYS B 339 6784 6737 7483 -134 69 14 A N1+ ATOM 5497 N PHE B 340 -16.094 29.662 64.686 1.00 47.38 A N ANISOU 5497 N PHE B 340 6272 5671 6059 -228 -246 -480 A N ATOM 5498 CA PHE B 340 -16.578 28.286 64.545 1.00 46.19 A C ANISOU 5498 CA PHE B 340 6058 5583 5908 -252 -263 -422 A C ATOM 5499 C PHE B 340 -16.995 27.740 65.905 1.00 45.45 A C ANISOU 5499 C PHE B 340 6026 5461 5779 -283 -316 -449 A C ATOM 5500 O PHE B 340 -16.629 28.308 66.936 1.00 45.75 A O ANISOU 5500 O PHE B 340 6115 5364 5904 -343 -389 -546 A O ATOM 5501 CB PHE B 340 -15.524 27.377 63.886 1.00 45.88 A C ANISOU 5501 CB PHE B 340 6057 5557 5818 -249 -277 -348 A C ATOM 5502 CG PHE B 340 -14.169 27.403 64.568 1.00 43.83 A C ANISOU 5502 CG PHE B 340 5788 5207 5659 -297 -203 -350 A C ATOM 5503 CD1 PHE B 340 -13.940 26.666 65.733 1.00 42.41 A C ANISOU 5503 CD1 PHE B 340 5752 5067 5295 -232 -200 -157 A C ATOM 5504 CD2 PHE B 340 -13.124 28.137 64.025 1.00 43.16 A C ANISOU 5504 CD2 PHE B 340 5747 5047 5604 -309 -315 -335 A C ATOM 5505 CE1 PHE B 340 -12.686 26.692 66.357 1.00 43.35 A C ANISOU 5505 CE1 PHE B 340 5759 5039 5672 -233 -103 -144 A C ATOM 5506 CE2 PHE B 340 -11.880 28.167 64.615 1.00 44.02 A C ANISOU 5506 CE2 PHE B 340 5835 5278 5610 -164 -242 -140 A C ATOM 5507 CZ PHE B 340 -11.653 27.440 65.802 1.00 44.03 A C ANISOU 5507 CZ PHE B 340 5802 5225 5700 -295 -95 -276 A C ATOM 5508 N ALA B 341 -17.803 26.676 65.877 1.00 44.88 A N ANISOU 5508 N ALA B 341 5948 5438 5666 -270 -312 -452 A N ATOM 5509 CA ALA B 341 -18.298 25.989 67.068 1.00 43.89 A C ANISOU 5509 CA ALA B 341 5708 5414 5552 -321 -198 -326 A C ATOM 5510 C ALA B 341 -17.494 24.712 67.359 1.00 42.94 A C ANISOU 5510 C ALA B 341 5658 5333 5322 -325 -174 -267 A C ATOM 5511 O ALA B 341 -17.079 24.000 66.444 1.00 42.72 A O ANISOU 5511 O ALA B 341 5680 5282 5270 -411 -252 -256 A O ATOM 5512 CB ALA B 341 -19.780 25.652 66.900 1.00 44.61 A C ANISOU 5512 CB ALA B 341 5865 5378 5707 -228 -259 -341 A C ATOM 5513 N LEU B 342 -17.263 24.431 68.634 1.00 41.02 A N ANISOU 5513 N LEU B 342 5317 5226 5040 -322 -145 -207 A N ATOM 5514 CA LEU B 342 -16.624 23.160 69.020 1.00 39.57 A C ANISOU 5514 CA LEU B 342 5088 5123 4821 -371 -65 -73 A C ATOM 5515 C LEU B 342 -17.573 22.176 69.703 1.00 39.56 A C ANISOU 5515 C LEU B 342 5089 5227 4714 -366 -91 -81 A C ATOM 5516 O LEU B 342 -17.331 20.978 69.700 1.00 39.33 A O ANISOU 5516 O LEU B 342 5047 5276 4618 -502 -26 -19 A O ATOM 5517 CB LEU B 342 -15.398 23.411 69.904 1.00 38.96 A C ANISOU 5517 CB LEU B 342 5007 5079 4716 -327 -9 -66 A C ATOM 5518 CG LEU B 342 -14.156 23.960 69.195 1.00 37.51 A C ANISOU 5518 CG LEU B 342 4998 4645 4608 -299 123 -17 A C ATOM 5519 CD1 LEU B 342 -13.095 24.284 70.223 1.00 36.66 A C ANISOU 5519 CD1 LEU B 342 4776 4627 4526 -414 375 148 A C ATOM 5520 CD2 LEU B 342 -13.623 22.974 68.118 1.00 36.71 A C ANISOU 5520 CD2 LEU B 342 4720 4633 4594 -220 531 -217 A C ATOM 5521 N ASP B 343 -18.662 22.678 70.287 1.00 39.96 A N ANISOU 5521 N ASP B 343 5068 5300 4813 -402 -34 -115 A N ATOM 5522 CA ASP B 343 -19.647 21.807 70.960 1.00 40.92 A C ANISOU 5522 CA ASP B 343 5181 5429 4937 -296 -11 -65 A C ATOM 5523 C ASP B 343 -20.196 20.580 70.186 1.00 40.25 A C ANISOU 5523 C ASP B 343 5145 5374 4771 -285 -16 -123 A C ATOM 5524 O ASP B 343 -20.316 19.498 70.770 1.00 39.98 A O ANISOU 5524 O ASP B 343 5133 5359 4697 -396 9 -122 A O ATOM 5525 CB ASP B 343 -20.797 22.647 71.543 1.00 41.53 A C ANISOU 5525 CB ASP B 343 5174 5532 5074 -293 0 -41 A C ATOM 5526 CG ASP B 343 -20.406 23.350 72.823 1.00 44.98 A C ANISOU 5526 CG ASP B 343 5705 5848 5537 -223 -40 117 A C ATOM 5527 OD1 ASP B 343 -19.359 22.993 73.386 1.00 47.78 A O ANISOU 5527 OD1 ASP B 343 5912 6218 6021 -168 -200 357 A O ATOM 5528 OD2 ASP B 343 -21.152 24.236 73.291 1.00 49.19 A O1- ANISOU 5528 OD2 ASP B 343 6195 6148 6347 -284 -31 214 A O1- ATOM 5529 N PRO B 344 -20.572 20.737 68.887 1.00 39.95 A N ANISOU 5529 N PRO B 344 5116 5320 4740 -221 -74 -149 A N ATOM 5530 CA PRO B 344 -21.024 19.559 68.131 1.00 39.05 A C ANISOU 5530 CA PRO B 344 5007 5226 4603 -218 -101 -156 A C ATOM 5531 C PRO B 344 -20.039 18.382 68.123 1.00 37.60 A C ANISOU 5531 C PRO B 344 4838 5074 4372 -231 -159 -180 A C ATOM 5532 O PRO B 344 -20.458 17.254 67.932 1.00 38.04 A O ANISOU 5532 O PRO B 344 4767 5191 4495 -283 -297 -205 A O ATOM 5533 CB PRO B 344 -21.202 20.074 66.689 1.00 39.43 A C ANISOU 5533 CB PRO B 344 5024 5260 4695 -177 -140 -160 A C ATOM 5534 CG PRO B 344 -20.845 21.529 66.715 1.00 39.89 A C ANISOU 5534 CG PRO B 344 5097 5275 4783 -57 -31 -150 A C ATOM 5535 CD PRO B 344 -20.699 21.986 68.117 1.00 40.13 A C ANISOU 5535 CD PRO B 344 5210 5326 4712 -210 -53 -207 A C ATOM 5536 N LEU B 345 -18.752 18.641 68.328 1.00 36.13 A N ANISOU 5536 N LEU B 345 4728 4931 4066 -232 -99 -137 A N ATOM 5537 CA LEU B 345 -17.768 17.559 68.351 1.00 34.48 A C ANISOU 5537 CA LEU B 345 4652 4671 3776 -217 -88 -162 A C ATOM 5538 C LEU B 345 -17.689 16.821 69.702 1.00 34.18 A C ANISOU 5538 C LEU B 345 4636 4562 3786 -257 -75 -127 A C ATOM 5539 O LEU B 345 -17.153 15.710 69.778 1.00 33.94 A O ANISOU 5539 O LEU B 345 4736 4411 3746 -334 -63 -71 A O ATOM 5540 CB LEU B 345 -16.377 18.088 67.976 1.00 33.90 A C ANISOU 5540 CB LEU B 345 4590 4590 3700 -220 -22 -104 A C ATOM 5541 CG LEU B 345 -16.219 18.886 66.676 1.00 35.31 A C ANISOU 5541 CG LEU B 345 4731 4846 3839 -86 -44 -46 A C ATOM 5542 CD1 LEU B 345 -14.788 19.398 66.589 1.00 33.55 A C ANISOU 5542 CD1 LEU B 345 4286 4673 3787 -92 285 147 A C ATOM 5543 CD2 LEU B 345 -16.467 17.953 65.516 1.00 35.98 A C ANISOU 5543 CD2 LEU B 345 4942 5058 3668 -160 -245 51 A C ATOM 5544 N ILE B 346 -18.206 17.439 70.755 1.00 32.80 A N ANISOU 5544 N ILE B 346 4389 4430 3642 -212 -27 -155 A N ATOM 5545 CA ILE B 346 -18.106 16.865 72.095 1.00 32.81 A C ANISOU 5545 CA ILE B 346 4489 4332 3643 -132 -65 -162 A C ATOM 5546 C ILE B 346 -19.370 16.095 72.470 1.00 33.71 A C ANISOU 5546 C ILE B 346 4409 4576 3822 -178 65 -116 A C ATOM 5547 O ILE B 346 -20.445 16.699 72.696 1.00 35.56 A O ANISOU 5547 O ILE B 346 4539 4687 4285 -198 183 -68 A O ATOM 5548 CB ILE B 346 -17.733 17.940 73.147 1.00 32.55 A C ANISOU 5548 CB ILE B 346 4501 4324 3540 -141 -149 -211 A C ATOM 5549 CG1 ILE B 346 -16.412 18.593 72.712 1.00 32.05 A C ANISOU 5549 CG1 ILE B 346 4829 3816 3530 63 -48 -258 A C ATOM 5550 CG2 ILE B 346 -17.525 17.270 74.529 1.00 32.60 A C ANISOU 5550 CG2 ILE B 346 4818 4181 3385 -231 -144 -385 A C ATOM 5551 CD1 ILE B 346 -16.123 19.915 73.350 1.00 33.73 A C ANISOU 5551 CD1 ILE B 346 5092 4144 3577 1 -262 225 A C ATOM 5552 N THR B 347 -19.248 14.773 72.521 1.00 32.60 A N ANISOU 5552 N THR B 347 4177 4572 3634 -143 95 -119 A N ATOM 5553 CA THR B 347 -20.405 13.931 72.802 1.00 33.42 A C ANISOU 5553 CA THR B 347 4231 4680 3785 -136 29 -22 A C ATOM 5554 C THR B 347 -20.417 13.339 74.196 1.00 33.15 A C ANISOU 5554 C THR B 347 4109 4664 3819 -83 49 -82 A C ATOM 5555 O THR B 347 -21.479 12.897 74.690 1.00 34.24 A O ANISOU 5555 O THR B 347 4187 4769 4053 -71 99 -122 A O ATOM 5556 CB THR B 347 -20.547 12.826 71.754 1.00 33.62 A C ANISOU 5556 CB THR B 347 4297 4622 3855 -239 -79 20 A C ATOM 5557 CG2 THR B 347 -20.838 13.448 70.361 1.00 34.24 A C ANISOU 5557 CG2 THR B 347 4315 5055 3638 -113 54 -77 A C ATOM 5558 OG1 THR B 347 -19.333 12.052 71.697 1.00 32.83 A O ANISOU 5558 OG1 THR B 347 3854 4838 3781 -198 -29 235 A O ATOM 5559 N HIS B 348 -19.246 13.310 74.837 1.00 32.15 A N ANISOU 5559 N HIS B 348 4015 4518 3680 -56 116 -77 A N ATOM 5560 CA HIS B 348 -19.115 12.706 76.162 1.00 31.45 A C ANISOU 5560 CA HIS B 348 3955 4486 3508 11 204 -5 A C ATOM 5561 C HIS B 348 -18.077 13.447 76.976 1.00 30.63 A C ANISOU 5561 C HIS B 348 3878 4438 3319 -11 234 -39 A C ATOM 5562 O HIS B 348 -17.037 13.862 76.456 1.00 31.07 A O ANISOU 5562 O HIS B 348 3975 4407 3423 68 187 24 A O ATOM 5563 CB HIS B 348 -18.745 11.223 76.044 1.00 30.92 A C ANISOU 5563 CB HIS B 348 3677 4467 3604 40 276 44 A C ATOM 5564 CG HIS B 348 -19.770 10.398 75.326 1.00 34.12 A C ANISOU 5564 CG HIS B 348 4277 4626 4061 109 131 133 A C ATOM 5565 CD2 HIS B 348 -20.692 9.521 75.790 1.00 35.13 A C ANISOU 5565 CD2 HIS B 348 4266 4678 4403 240 100 108 A C ATOM 5566 ND1 HIS B 348 -19.962 10.471 73.967 1.00 35.35 A N ANISOU 5566 ND1 HIS B 348 4342 4807 4282 177 320 251 A N ATOM 5567 CE1 HIS B 348 -20.942 9.658 73.615 1.00 36.39 A C ANISOU 5567 CE1 HIS B 348 4687 4770 4368 260 247 351 A C ATOM 5568 NE2 HIS B 348 -21.395 9.059 74.702 1.00 36.20 A N ANISOU 5568 NE2 HIS B 348 4905 4686 4162 298 207 201 A N ATOM 5569 N VAL B 349 -18.367 13.647 78.259 1.00 30.56 A N ANISOU 5569 N VAL B 349 3999 4370 3241 -40 204 -75 A N ATOM 5570 CA VAL B 349 -17.349 14.195 79.164 1.00 30.86 A C ANISOU 5570 CA VAL B 349 4056 4370 3296 -76 199 -154 A C ATOM 5571 C VAL B 349 -17.287 13.314 80.398 1.00 30.30 A C ANISOU 5571 C VAL B 349 3914 4358 3239 -43 308 -195 A C ATOM 5572 O VAL B 349 -18.327 12.977 80.977 1.00 32.59 A O ANISOU 5572 O VAL B 349 4013 4683 3683 -59 324 -326 A O ATOM 5573 CB VAL B 349 -17.697 15.649 79.566 1.00 30.57 A C ANISOU 5573 CB VAL B 349 3999 4277 3338 -129 223 -149 A C ATOM 5574 CG1 VAL B 349 -16.737 16.220 80.598 1.00 33.18 A C ANISOU 5574 CG1 VAL B 349 4543 4446 3616 -289 240 110 A C ATOM 5575 CG2 VAL B 349 -17.791 16.559 78.316 1.00 30.37 A C ANISOU 5575 CG2 VAL B 349 4180 4114 3243 -236 218 -107 A C ATOM 5576 N LEU B 350 -16.072 12.947 80.794 1.00 30.30 A N ANISOU 5576 N LEU B 350 4027 4378 3106 -24 290 -166 A N ATOM 5577 CA LEU B 350 -15.862 12.078 81.953 1.00 29.90 A C ANISOU 5577 CA LEU B 350 3930 4271 3160 47 341 -160 A C ATOM 5578 C LEU B 350 -14.762 12.635 82.821 1.00 29.62 A C ANISOU 5578 C LEU B 350 3883 4290 3080 75 352 -177 A C ATOM 5579 O LEU B 350 -13.861 13.288 82.303 1.00 30.11 A O ANISOU 5579 O LEU B 350 3896 4520 3024 114 392 -223 A O ATOM 5580 CB LEU B 350 -15.477 10.675 81.509 1.00 30.48 A C ANISOU 5580 CB LEU B 350 4099 4235 3247 87 337 -183 A C ATOM 5581 CG LEU B 350 -16.542 9.849 80.803 1.00 30.82 A C ANISOU 5581 CG LEU B 350 3898 4359 3452 64 563 46 A C ATOM 5582 CD1 LEU B 350 -15.882 8.634 80.191 1.00 33.41 A C ANISOU 5582 CD1 LEU B 350 4547 4364 3782 -69 207 324 A C ATOM 5583 CD2 LEU B 350 -17.658 9.466 81.793 1.00 34.02 A C ANISOU 5583 CD2 LEU B 350 4397 4621 3907 -144 897 104 A C ATOM 5584 N PRO B 351 -14.805 12.372 84.147 1.00 28.65 A N ANISOU 5584 N PRO B 351 3717 4158 3011 -1 383 -124 A N ATOM 5585 CA PRO B 351 -13.656 12.732 84.973 1.00 28.95 A C ANISOU 5585 CA PRO B 351 3855 4163 2978 95 421 -47 A C ATOM 5586 C PRO B 351 -12.457 11.867 84.520 1.00 29.25 A C ANISOU 5586 C PRO B 351 3915 4043 3153 59 313 -40 A C ATOM 5587 O PRO B 351 -12.655 10.762 84.020 1.00 29.91 A O ANISOU 5587 O PRO B 351 4068 3996 3300 83 515 -47 A O ATOM 5588 CB PRO B 351 -14.102 12.333 86.389 1.00 28.23 A C ANISOU 5588 CB PRO B 351 3834 4146 2745 103 341 -74 A C ATOM 5589 CG PRO B 351 -15.149 11.288 86.165 1.00 28.82 A C ANISOU 5589 CG PRO B 351 3979 4100 2871 78 380 -84 A C ATOM 5590 CD PRO B 351 -15.860 11.683 84.908 1.00 29.42 A C ANISOU 5590 CD PRO B 351 3917 4208 3054 -13 418 -199 A C ATOM 5591 N PHE B 352 -11.242 12.374 84.698 1.00 29.43 A N ANISOU 5591 N PHE B 352 3931 3937 3313 93 489 -81 A N ATOM 5592 CA PHE B 352 -10.009 11.710 84.277 1.00 30.56 A C ANISOU 5592 CA PHE B 352 4114 4071 3425 78 271 -138 A C ATOM 5593 C PHE B 352 -9.920 10.239 84.756 1.00 29.85 A C ANISOU 5593 C PHE B 352 4054 3984 3301 106 348 -215 A C ATOM 5594 O PHE B 352 -9.476 9.355 84.025 1.00 29.83 A O ANISOU 5594 O PHE B 352 4166 3974 3193 83 449 -430 A O ATOM 5595 CB PHE B 352 -8.840 12.523 84.799 1.00 31.90 A C ANISOU 5595 CB PHE B 352 4300 4111 3707 171 352 -82 A C ATOM 5596 CG PHE B 352 -7.521 11.840 84.687 1.00 32.64 A C ANISOU 5596 CG PHE B 352 4215 4137 4047 145 240 -137 A C ATOM 5597 CD1 PHE B 352 -7.005 11.475 83.439 1.00 36.26 A C ANISOU 5597 CD1 PHE B 352 4775 4420 4582 41 156 175 A C ATOM 5598 CD2 PHE B 352 -6.754 11.618 85.817 1.00 35.79 A C ANISOU 5598 CD2 PHE B 352 4524 4457 4614 124 74 -118 A C ATOM 5599 CE1 PHE B 352 -5.759 10.850 83.352 1.00 37.18 A C ANISOU 5599 CE1 PHE B 352 4638 4662 4827 163 90 86 A C ATOM 5600 CE2 PHE B 352 -5.526 10.998 85.730 1.00 37.14 A C ANISOU 5600 CE2 PHE B 352 4705 4548 4857 70 230 -149 A C ATOM 5601 CZ PHE B 352 -5.027 10.616 84.502 1.00 36.61 A C ANISOU 5601 CZ PHE B 352 4677 4514 4716 -17 207 -88 A C ATOM 5602 N GLU B 353 -10.415 9.959 85.958 1.00 31.63 A N ANISOU 5602 N GLU B 353 4387 4232 3397 87 144 -206 A N ATOM 5603 CA GLU B 353 -10.232 8.641 86.520 1.00 31.36 A C ANISOU 5603 CA GLU B 353 4353 4164 3396 71 169 -165 A C ATOM 5604 C GLU B 353 -11.044 7.557 85.811 1.00 30.66 A C ANISOU 5604 C GLU B 353 4238 4090 3320 85 324 -198 A C ATOM 5605 O GLU B 353 -10.806 6.358 86.022 1.00 31.89 A O ANISOU 5605 O GLU B 353 4429 4206 3482 89 419 -203 A O ATOM 5606 CB GLU B 353 -10.565 8.662 88.006 1.00 32.10 A C ANISOU 5606 CB GLU B 353 4552 4220 3423 -15 205 -104 A C ATOM 5607 CG GLU B 353 -9.604 9.564 88.795 1.00 35.93 A C ANISOU 5607 CG GLU B 353 5029 4605 4017 0 -231 -107 A C ATOM 5608 CD GLU B 353 -9.967 11.076 88.812 1.00 38.76 A C ANISOU 5608 CD GLU B 353 5495 4941 4288 -265 -109 315 A C ATOM 5609 OE1 GLU B 353 -10.997 11.537 88.212 1.00 36.19 A O ANISOU 5609 OE1 GLU B 353 5208 5160 3379 -285 -86 473 A O ATOM 5610 OE2 GLU B 353 -9.167 11.813 89.446 1.00 45.02 A O1- ANISOU 5610 OE2 GLU B 353 6248 5600 5257 5 -350 222 A O1- ATOM 5611 N LYS B 354 -11.996 8.007 84.992 1.00 28.94 A N ANISOU 5611 N LYS B 354 3803 4132 3061 35 640 -243 A N ATOM 5612 CA LYS B 354 -12.810 7.140 84.177 1.00 29.16 A C ANISOU 5612 CA LYS B 354 3769 4155 3154 53 642 -281 A C ATOM 5613 C LYS B 354 -12.240 6.992 82.732 1.00 29.24 A C ANISOU 5613 C LYS B 354 3770 4120 3220 89 638 -224 A C ATOM 5614 O LYS B 354 -12.948 6.683 81.764 1.00 28.72 A O ANISOU 5614 O LYS B 354 3563 4084 3265 81 703 -208 A O ATOM 5615 CB LYS B 354 -14.247 7.650 84.163 1.00 29.66 A C ANISOU 5615 CB LYS B 354 3855 4249 3164 88 773 -267 A C ATOM 5616 CG LYS B 354 -14.966 7.495 85.518 1.00 31.30 A C ANISOU 5616 CG LYS B 354 3927 4621 3345 53 795 -273 A C ATOM 5617 CD LYS B 354 -16.436 7.783 85.320 1.00 34.01 A C ANISOU 5617 CD LYS B 354 4125 4902 3895 -39 754 -359 A C ATOM 5618 CE LYS B 354 -17.198 7.527 86.631 1.00 36.27 A C ANISOU 5618 CE LYS B 354 4374 5145 4261 231 807 -159 A C ATOM 5619 NZ LYS B 354 -18.646 7.643 86.364 1.00 38.67 A N1+ ANISOU 5619 NZ LYS B 354 4396 5148 5147 -83 647 -254 A N1+ ATOM 5620 N ILE B 355 -10.933 7.176 82.610 1.00 29.25 A N ANISOU 5620 N ILE B 355 3718 4105 3288 82 684 -262 A N ATOM 5621 CA ILE B 355 -10.251 7.121 81.295 1.00 27.70 A C ANISOU 5621 CA ILE B 355 3593 3686 3244 174 705 -266 A C ATOM 5622 C ILE B 355 -10.554 5.799 80.575 1.00 28.50 A C ANISOU 5622 C ILE B 355 3650 3706 3471 208 581 -233 A C ATOM 5623 O ILE B 355 -10.804 5.778 79.362 1.00 27.73 A O ANISOU 5623 O ILE B 355 3590 3373 3572 449 474 -324 A O ATOM 5624 CB ILE B 355 -8.734 7.378 81.436 1.00 28.48 A C ANISOU 5624 CB ILE B 355 3729 3859 3233 14 686 -228 A C ATOM 5625 CG1 ILE B 355 -8.034 7.295 80.053 1.00 28.12 A C ANISOU 5625 CG1 ILE B 355 3526 3899 3257 196 882 -342 A C ATOM 5626 CG2 ILE B 355 -8.078 6.419 82.455 1.00 28.98 A C ANISOU 5626 CG2 ILE B 355 3689 3938 3382 -66 660 -363 A C ATOM 5627 CD1 ILE B 355 -6.618 7.858 80.093 1.00 26.81 A C ANISOU 5627 CD1 ILE B 355 3520 3376 3290 545 841 87 A C ATOM 5628 N ASN B 356 -10.560 4.680 81.307 1.00 28.64 A N ANISOU 5628 N ASN B 356 3612 3580 3687 215 539 -181 A N ATOM 5629 CA ASN B 356 -10.876 3.431 80.590 1.00 30.55 A C ANISOU 5629 CA ASN B 356 3952 3738 3915 128 487 -100 A C ATOM 5630 C ASN B 356 -12.269 3.346 79.950 1.00 30.89 A C ANISOU 5630 C ASN B 356 4016 3810 3908 34 476 -11 A C ATOM 5631 O ASN B 356 -12.400 2.879 78.816 1.00 30.83 A O ANISOU 5631 O ASN B 356 4212 3570 3929 63 423 39 A O ATOM 5632 CB ASN B 356 -10.554 2.201 81.436 1.00 30.77 A C ANISOU 5632 CB ASN B 356 3982 3730 3977 101 406 -271 A C ATOM 5633 CG ASN B 356 -9.059 2.034 81.653 1.00 33.17 A C ANISOU 5633 CG ASN B 356 4089 4335 4177 133 534 -145 A C ATOM 5634 ND2 ASN B 356 -8.641 1.942 82.919 1.00 35.69 A N ANISOU 5634 ND2 ASN B 356 4687 4341 4530 180 303 -349 A N ATOM 5635 OD1 ASN B 356 -8.281 1.995 80.683 1.00 34.11 A O ANISOU 5635 OD1 ASN B 356 4652 4621 3686 64 730 -425 A O ATOM 5636 N GLU B 357 -13.299 3.825 80.658 1.00 31.87 A N ANISOU 5636 N GLU B 357 4044 3946 4116 -10 553 89 A N ATOM 5637 CA GLU B 357 -14.629 3.969 80.075 1.00 32.32 A C ANISOU 5637 CA GLU B 357 4161 4106 4013 -16 460 98 A C ATOM 5638 C GLU B 357 -14.591 4.843 78.824 1.00 31.93 A C ANISOU 5638 C GLU B 357 4089 3996 4046 -43 440 143 A C ATOM 5639 O GLU B 357 -15.315 4.576 77.848 1.00 31.65 A O ANISOU 5639 O GLU B 357 4015 4174 3834 3 336 198 A O ATOM 5640 CB GLU B 357 -15.631 4.535 81.116 1.00 33.47 A C ANISOU 5640 CB GLU B 357 4219 4164 4332 -52 532 129 A C ATOM 5641 CG GLU B 357 -16.752 5.378 80.507 1.00 38.88 A C ANISOU 5641 CG GLU B 357 4836 5007 4930 -2 256 -56 A C ATOM 5642 CD GLU B 357 -18.044 5.380 81.282 1.00 43.03 A C ANISOU 5642 CD GLU B 357 5296 5669 5383 -16 331 150 A C ATOM 5643 OE1 GLU B 357 -17.980 5.514 82.518 1.00 42.23 A O ANISOU 5643 OE1 GLU B 357 5553 5529 4961 175 630 31 A O ATOM 5644 OE2 GLU B 357 -19.122 5.249 80.629 1.00 46.81 A O1- ANISOU 5644 OE2 GLU B 357 5336 6186 6261 42 151 106 A O1- ATOM 5645 N GLY B 358 -13.751 5.874 78.834 1.00 30.95 A N ANISOU 5645 N GLY B 358 3945 3928 3886 -48 406 114 A N ATOM 5646 CA GLY B 358 -13.672 6.767 77.670 1.00 30.75 A C ANISOU 5646 CA GLY B 358 4020 3859 3802 135 433 60 A C ATOM 5647 C GLY B 358 -13.103 6.058 76.458 1.00 30.02 A C ANISOU 5647 C GLY B 358 3915 3675 3817 247 400 0 A C ATOM 5648 O GLY B 358 -13.532 6.313 75.323 1.00 30.99 A O ANISOU 5648 O GLY B 358 4015 3745 4012 230 415 -109 A O ATOM 5649 N PHE B 359 -12.129 5.181 76.696 1.00 29.02 A N ANISOU 5649 N PHE B 359 3836 3548 3641 287 374 -53 A N ATOM 5650 CA PHE B 359 -11.556 4.346 75.615 1.00 29.15 A C ANISOU 5650 CA PHE B 359 3935 3527 3610 408 334 -99 A C ATOM 5651 C PHE B 359 -12.537 3.273 75.145 1.00 29.93 A C ANISOU 5651 C PHE B 359 4088 3600 3682 462 336 -111 A C ATOM 5652 O PHE B 359 -12.630 2.999 73.955 1.00 31.80 A O ANISOU 5652 O PHE B 359 4481 3760 3840 430 465 -125 A O ATOM 5653 CB PHE B 359 -10.212 3.760 76.036 1.00 29.94 A C ANISOU 5653 CB PHE B 359 3889 3720 3764 496 349 -103 A C ATOM 5654 CG PHE B 359 -9.063 4.721 75.802 1.00 26.59 A C ANISOU 5654 CG PHE B 359 3548 3435 3118 409 625 -245 A C ATOM 5655 CD1 PHE B 359 -8.792 5.752 76.708 1.00 29.21 A C ANISOU 5655 CD1 PHE B 359 3484 4005 3609 585 309 16 A C ATOM 5656 CD2 PHE B 359 -8.298 4.619 74.649 1.00 29.09 A C ANISOU 5656 CD2 PHE B 359 4050 3969 3033 273 563 -136 A C ATOM 5657 CE1 PHE B 359 -7.772 6.655 76.474 1.00 28.96 A C ANISOU 5657 CE1 PHE B 359 3707 3732 3564 326 765 -104 A C ATOM 5658 CE2 PHE B 359 -7.289 5.511 74.423 1.00 28.61 A C ANISOU 5658 CE2 PHE B 359 3942 3649 3278 279 599 -195 A C ATOM 5659 CZ PHE B 359 -7.008 6.526 75.333 1.00 28.33 A C ANISOU 5659 CZ PHE B 359 3975 3778 3012 309 510 -199 A C ATOM 5660 N ASP B 360 -13.330 2.710 76.052 1.00 30.70 A N ANISOU 5660 N ASP B 360 4183 3788 3690 387 392 -149 A N ATOM 5661 CA ASP B 360 -14.429 1.868 75.570 1.00 31.27 A C ANISOU 5661 CA ASP B 360 4234 3885 3760 510 280 -112 A C ATOM 5662 C ASP B 360 -15.402 2.571 74.619 1.00 31.96 A C ANISOU 5662 C ASP B 360 4332 4060 3748 518 325 -109 A C ATOM 5663 O ASP B 360 -15.821 1.970 73.619 1.00 33.34 A O ANISOU 5663 O ASP B 360 4595 4183 3888 657 193 44 A O ATOM 5664 CB ASP B 360 -15.242 1.259 76.731 1.00 32.15 A C ANISOU 5664 CB ASP B 360 4326 4018 3868 474 329 -215 A C ATOM 5665 CG ASP B 360 -14.403 0.364 77.615 1.00 34.47 A C ANISOU 5665 CG ASP B 360 4512 4137 4444 280 153 -163 A C ATOM 5666 OD1 ASP B 360 -14.813 0.109 78.772 1.00 39.52 A O ANISOU 5666 OD1 ASP B 360 4975 4741 5299 184 373 -272 A O ATOM 5667 OD2 ASP B 360 -13.349 -0.100 77.146 1.00 37.53 A O1- ANISOU 5667 OD2 ASP B 360 4660 4204 5396 215 139 -221 A O1- ATOM 5668 N LEU B 361 -15.806 3.795 74.966 1.00 31.96 A N ANISOU 5668 N LEU B 361 4284 4037 3821 554 296 -187 A N ATOM 5669 CA LEU B 361 -16.625 4.662 74.108 1.00 32.87 A C ANISOU 5669 CA LEU B 361 4362 4255 3870 425 379 -166 A C ATOM 5670 C LEU B 361 -15.996 4.906 72.741 1.00 33.35 A C ANISOU 5670 C LEU B 361 4482 4285 3901 365 336 -220 A C ATOM 5671 O LEU B 361 -16.701 4.966 71.727 1.00 34.40 A O ANISOU 5671 O LEU B 361 4484 4561 4023 507 386 -197 A O ATOM 5672 CB LEU B 361 -16.892 6.005 74.796 1.00 32.79 A C ANISOU 5672 CB LEU B 361 4403 4293 3760 459 423 -200 A C ATOM 5673 CG LEU B 361 -17.894 5.984 75.974 1.00 33.63 A C ANISOU 5673 CG LEU B 361 4402 4470 3904 361 585 -118 A C ATOM 5674 CD1 LEU B 361 -17.797 7.317 76.706 1.00 36.15 A C ANISOU 5674 CD1 LEU B 361 4741 4677 4317 347 644 -57 A C ATOM 5675 CD2 LEU B 361 -19.335 5.692 75.522 1.00 35.80 A C ANISOU 5675 CD2 LEU B 361 4718 4325 4557 241 303 -368 A C ATOM 5676 N LEU B 362 -14.680 5.075 72.726 1.00 33.35 A N ANISOU 5676 N LEU B 362 4459 4374 3838 363 300 -250 A N ATOM 5677 CA LEU B 362 -13.920 5.323 71.490 1.00 34.42 A C ANISOU 5677 CA LEU B 362 4591 4431 4054 247 332 -174 A C ATOM 5678 C LEU B 362 -13.969 4.074 70.638 1.00 35.04 A C ANISOU 5678 C LEU B 362 4755 4485 4072 188 219 -94 A C ATOM 5679 O LEU B 362 -14.251 4.142 69.447 1.00 36.27 A O ANISOU 5679 O LEU B 362 4933 4653 4192 209 264 -51 A O ATOM 5680 CB LEU B 362 -12.458 5.639 71.817 1.00 33.81 A C ANISOU 5680 CB LEU B 362 4516 4409 3921 314 311 -182 A C ATOM 5681 CG LEU B 362 -11.462 5.676 70.628 1.00 34.47 A C ANISOU 5681 CG LEU B 362 4430 4395 4269 210 396 -229 A C ATOM 5682 CD1 LEU B 362 -11.452 7.019 69.968 1.00 36.51 A C ANISOU 5682 CD1 LEU B 362 4866 4626 4377 230 521 -386 A C ATOM 5683 CD2 LEU B 362 -10.046 5.355 71.118 1.00 35.18 A C ANISOU 5683 CD2 LEU B 362 4395 4287 4684 464 315 -376 A C ATOM 5684 N ARG B 363 -13.707 2.924 71.274 1.00 35.07 A N ANISOU 5684 N ARG B 363 4798 4429 4098 197 195 -94 A N ATOM 5685 CA ARG B 363 -13.539 1.661 70.552 1.00 36.20 A C ANISOU 5685 CA ARG B 363 4856 4504 4393 183 83 51 A C ATOM 5686 C ARG B 363 -14.850 1.116 69.990 1.00 36.83 A C ANISOU 5686 C ARG B 363 4878 4593 4520 192 83 62 A C ATOM 5687 O ARG B 363 -14.845 0.367 69.008 1.00 39.19 A O ANISOU 5687 O ARG B 363 5245 4843 4800 161 50 100 A O ATOM 5688 CB ARG B 363 -12.866 0.615 71.433 1.00 35.49 A C ANISOU 5688 CB ARG B 363 4778 4371 4335 207 141 48 A C ATOM 5689 CG ARG B 363 -11.384 0.915 71.726 1.00 35.91 A C ANISOU 5689 CG ARG B 363 4852 4473 4319 169 -69 145 A C ATOM 5690 CD ARG B 363 -10.830 0.047 72.837 1.00 37.36 A C ANISOU 5690 CD ARG B 363 4964 4518 4712 106 -151 136 A C ATOM 5691 NE ARG B 363 -9.520 0.532 73.267 1.00 37.76 A N ANISOU 5691 NE ARG B 363 4837 4717 4791 171 119 -121 A N ATOM 5692 CZ ARG B 363 -9.024 0.436 74.496 1.00 35.19 A C ANISOU 5692 CZ ARG B 363 4640 4249 4479 282 198 -99 A C ATOM 5693 NH1 ARG B 363 -9.739 -0.101 75.494 1.00 36.95 A N1+ ANISOU 5693 NH1 ARG B 363 4844 4464 4731 260 395 -257 A N1+ ATOM 5694 NH2 ARG B 363 -7.801 0.914 74.734 1.00 34.19 A N ANISOU 5694 NH2 ARG B 363 4545 4256 4190 41 -115 -464 A N ATOM 5695 N SER B 364 -15.963 1.492 70.613 1.00 37.50 A N ANISOU 5695 N SER B 364 4762 4659 4826 221 -29 -31 A N ATOM 5696 CA SER B 364 -17.268 0.966 70.239 1.00 38.66 A C ANISOU 5696 CA SER B 364 4896 4809 4981 245 -62 49 A C ATOM 5697 C SER B 364 -17.869 1.796 69.116 1.00 39.43 A C ANISOU 5697 C SER B 364 4978 4921 5081 187 -127 30 A C ATOM 5698 O SER B 364 -18.835 1.370 68.475 1.00 40.54 A O ANISOU 5698 O SER B 364 5124 5005 5274 226 -130 145 A O ATOM 5699 CB SER B 364 -18.193 1.010 71.451 1.00 38.21 A C ANISOU 5699 CB SER B 364 4783 4743 4990 269 -45 29 A C ATOM 5700 OG SER B 364 -18.526 2.348 71.773 1.00 38.84 A O ANISOU 5700 OG SER B 364 4677 4824 5253 334 158 -118 A O ATOM 5701 N GLY B 365 -17.286 2.970 68.871 1.00 40.24 A N ANISOU 5701 N GLY B 365 5116 5009 5162 190 -151 79 A N ATOM 5702 CA GLY B 365 -17.820 3.957 67.905 1.00 40.74 A C ANISOU 5702 CA GLY B 365 5180 5155 5141 132 -183 -12 A C ATOM 5703 C GLY B 365 -18.913 4.877 68.458 1.00 41.36 A C ANISOU 5703 C GLY B 365 5226 5264 5222 115 -108 -44 A C ATOM 5704 O GLY B 365 -19.463 5.718 67.741 1.00 42.00 A O ANISOU 5704 O GLY B 365 5306 5390 5261 152 -190 -43 A O ATOM 5705 N GLU B 366 -19.206 4.752 69.746 1.00 41.23 A N ANISOU 5705 N GLU B 366 5175 5276 5213 116 -53 -1 A N ATOM 5706 CA GLU B 366 -20.339 5.443 70.377 1.00 42.04 A C ANISOU 5706 CA GLU B 366 5282 5311 5380 71 15 -21 A C ATOM 5707 C GLU B 366 -20.112 6.956 70.535 1.00 40.92 A C ANISOU 5707 C GLU B 366 5127 5187 5232 66 17 -16 A C ATOM 5708 O GLU B 366 -21.060 7.749 70.460 1.00 42.09 A O ANISOU 5708 O GLU B 366 5223 5297 5473 71 -52 -43 A O ATOM 5709 CB GLU B 366 -20.595 4.798 71.745 1.00 42.27 A C ANISOU 5709 CB GLU B 366 5304 5434 5322 17 43 -38 A C ATOM 5710 CG GLU B 366 -21.930 5.106 72.403 1.00 44.45 A C ANISOU 5710 CG GLU B 366 5498 5648 5742 -51 105 -64 A C ATOM 5711 CD GLU B 366 -22.061 4.423 73.764 1.00 44.31 A C ANISOU 5711 CD GLU B 366 5492 5597 5747 89 143 -82 A C ATOM 5712 OE1 GLU B 366 -21.448 3.334 73.969 1.00 48.66 A O ANISOU 5712 OE1 GLU B 366 5820 6016 6649 -41 120 -271 A O ATOM 5713 OE2 GLU B 366 -22.751 4.985 74.635 1.00 48.46 A O1- ANISOU 5713 OE2 GLU B 366 5582 6327 6502 -104 288 -33 A O1- ATOM 5714 N SER B 367 -18.857 7.341 70.777 1.00 39.23 A N ANISOU 5714 N SER B 367 5021 4960 4923 98 73 14 A N ATOM 5715 CA SER B 367 -18.485 8.743 70.940 1.00 37.31 A C ANISOU 5715 CA SER B 367 4823 4757 4596 148 133 -92 A C ATOM 5716 C SER B 367 -17.916 9.357 69.657 1.00 36.47 A C ANISOU 5716 C SER B 367 4767 4665 4425 59 240 -30 A C ATOM 5717 O SER B 367 -17.171 8.691 68.924 1.00 36.99 A O ANISOU 5717 O SER B 367 4979 4560 4513 70 453 -153 A O ATOM 5718 CB SER B 367 -17.431 8.848 72.051 1.00 36.67 A C ANISOU 5718 CB SER B 367 4711 4724 4495 163 87 -42 A C ATOM 5719 OG SER B 367 -16.277 8.050 71.730 1.00 38.35 A O ANISOU 5719 OG SER B 367 4986 4690 4892 271 78 -147 A O ATOM 5720 N ILE B 368 -18.265 10.618 69.383 1.00 34.16 A N ANISOU 5720 N ILE B 368 4440 4511 4028 104 202 4 A N ATOM 5721 CA ILE B 368 -17.469 11.437 68.448 1.00 32.53 A C ANISOU 5721 CA ILE B 368 4208 4456 3694 47 183 39 A C ATOM 5722 C ILE B 368 -16.157 11.844 69.140 1.00 32.57 A C ANISOU 5722 C ILE B 368 4166 4516 3691 74 254 201 A C ATOM 5723 O ILE B 368 -15.038 11.559 68.660 1.00 32.84 A O ANISOU 5723 O ILE B 368 4167 4672 3638 55 209 296 A O ATOM 5724 CB ILE B 368 -18.273 12.672 67.958 1.00 33.42 A C ANISOU 5724 CB ILE B 368 4382 4476 3837 119 211 5 A C ATOM 5725 CG1 ILE B 368 -19.444 12.212 67.085 1.00 34.48 A C ANISOU 5725 CG1 ILE B 368 4400 4738 3962 -24 119 18 A C ATOM 5726 CG2 ILE B 368 -17.360 13.656 67.201 1.00 32.45 A C ANISOU 5726 CG2 ILE B 368 4256 4274 3799 -1 286 -137 A C ATOM 5727 CD1 ILE B 368 -19.003 11.601 65.720 1.00 34.06 A C ANISOU 5727 CD1 ILE B 368 4457 4441 4040 -318 236 -37 A C ATOM 5728 N ARG B 369 -16.294 12.502 70.281 1.00 31.09 A N ANISOU 5728 N ARG B 369 3923 4524 3363 21 211 233 A N ATOM 5729 CA ARG B 369 -15.150 12.777 71.142 1.00 31.08 A C ANISOU 5729 CA ARG B 369 3957 4479 3372 -6 223 158 A C ATOM 5730 C ARG B 369 -15.542 12.793 72.574 1.00 30.73 A C ANISOU 5730 C ARG B 369 3927 4475 3273 8 234 100 A C ATOM 5731 O ARG B 369 -16.587 13.373 72.930 1.00 31.08 A O ANISOU 5731 O ARG B 369 3906 4666 3236 -66 195 139 A O ATOM 5732 CB ARG B 369 -14.610 14.159 70.866 1.00 31.83 A C ANISOU 5732 CB ARG B 369 4244 4489 3357 61 251 72 A C ATOM 5733 CG ARG B 369 -13.374 14.133 70.142 1.00 36.21 A C ANISOU 5733 CG ARG B 369 4552 4570 4634 -96 191 -133 A C ATOM 5734 CD ARG B 369 -12.191 13.877 71.086 1.00 40.62 A C ANISOU 5734 CD ARG B 369 4940 5194 5299 51 -30 -174 A C ATOM 5735 NE ARG B 369 -10.983 14.069 70.308 1.00 40.13 A N ANISOU 5735 NE ARG B 369 4878 4987 5380 -115 165 -298 A N ATOM 5736 CZ ARG B 369 -10.643 13.332 69.257 1.00 39.81 A C ANISOU 5736 CZ ARG B 369 4883 4981 5260 104 -56 -172 A C ATOM 5737 NH1 ARG B 369 -11.416 12.330 68.852 1.00 38.63 A N1+ ANISOU 5737 NH1 ARG B 369 4102 5004 5571 348 -25 -307 A N1+ ATOM 5738 NH2 ARG B 369 -9.523 13.601 68.603 1.00 39.99 A N ANISOU 5738 NH2 ARG B 369 4930 5154 5109 22 221 -232 A N ATOM 5739 N THR B 370 -14.687 12.184 73.382 1.00 30.53 A N ANISOU 5739 N THR B 370 3810 4492 3296 30 232 133 A N ATOM 5740 CA THR B 370 -14.787 12.255 74.831 1.00 31.43 A C ANISOU 5740 CA THR B 370 4117 4403 3422 30 174 -72 A C ATOM 5741 C THR B 370 -13.676 13.153 75.343 1.00 30.85 A C ANISOU 5741 C THR B 370 4004 4346 3370 -23 142 -87 A C ATOM 5742 O THR B 370 -12.514 13.014 74.931 1.00 30.53 A O ANISOU 5742 O THR B 370 4010 4290 3300 -59 141 -120 A O ATOM 5743 CB THR B 370 -14.649 10.866 75.476 1.00 32.44 A C ANISOU 5743 CB THR B 370 4231 4403 3691 -52 135 20 A C ATOM 5744 CG2 THR B 370 -14.770 10.945 76.992 1.00 31.54 A C ANISOU 5744 CG2 THR B 370 4355 4098 3529 -53 182 -372 A C ATOM 5745 OG1 THR B 370 -15.686 10.015 74.987 1.00 34.19 A O ANISOU 5745 OG1 THR B 370 4222 4606 4162 164 236 23 A O ATOM 5746 N ILE B 371 -14.065 14.107 76.205 1.00 29.55 A N ANISOU 5746 N ILE B 371 3957 4199 3070 45 186 -165 A N ATOM 5747 CA ILE B 371 -13.135 14.945 76.936 1.00 29.47 A C ANISOU 5747 CA ILE B 371 3991 4176 3027 6 101 -278 A C ATOM 5748 C ILE B 371 -13.033 14.466 78.379 1.00 29.57 A C ANISOU 5748 C ILE B 371 3940 4240 3054 0 172 -335 A C ATOM 5749 O ILE B 371 -14.051 14.197 79.023 1.00 30.47 A O ANISOU 5749 O ILE B 371 3875 4513 3187 5 237 -362 A O ATOM 5750 CB ILE B 371 -13.575 16.429 76.899 1.00 30.44 A C ANISOU 5750 CB ILE B 371 4159 4228 3179 -17 -14 -239 A C ATOM 5751 CG1 ILE B 371 -13.800 16.883 75.435 1.00 30.49 A C ANISOU 5751 CG1 ILE B 371 4209 4173 3201 81 -54 -301 A C ATOM 5752 CG2 ILE B 371 -12.591 17.342 77.642 1.00 29.25 A C ANISOU 5752 CG2 ILE B 371 4133 3887 3091 -93 54 -314 A C ATOM 5753 CD1 ILE B 371 -12.583 16.836 74.591 1.00 32.20 A C ANISOU 5753 CD1 ILE B 371 4807 4081 3347 -236 265 -356 A C ATOM 5754 N LEU B 372 -11.810 14.365 78.875 1.00 29.12 A N ANISOU 5754 N LEU B 372 4003 4125 2936 89 179 -271 A N ATOM 5755 CA LEU B 372 -11.579 14.002 80.266 1.00 28.66 A C ANISOU 5755 CA LEU B 372 4027 3879 2982 -35 118 -159 A C ATOM 5756 C LEU B 372 -11.217 15.246 81.034 1.00 29.55 A C ANISOU 5756 C LEU B 372 4090 3923 3211 -29 171 -135 A C ATOM 5757 O LEU B 372 -10.368 16.040 80.609 1.00 29.19 A O ANISOU 5757 O LEU B 372 4217 3899 2974 -144 231 -116 A O ATOM 5758 CB LEU B 372 -10.432 12.975 80.381 1.00 29.19 A C ANISOU 5758 CB LEU B 372 4035 3759 3295 0 77 -179 A C ATOM 5759 CG LEU B 372 -10.561 11.587 79.710 1.00 28.21 A C ANISOU 5759 CG LEU B 372 3662 3562 3495 196 210 -166 A C ATOM 5760 CD1 LEU B 372 -9.309 10.769 79.930 1.00 29.37 A C ANISOU 5760 CD1 LEU B 372 3592 3776 3789 238 679 -223 A C ATOM 5761 CD2 LEU B 372 -11.792 10.845 80.249 1.00 29.07 A C ANISOU 5761 CD2 LEU B 372 3736 3280 4030 367 407 -394 A C ATOM 5762 N THR B 373 -11.860 15.406 82.191 1.00 29.01 A N ANISOU 5762 N THR B 373 4186 3850 2984 22 153 -120 A N ATOM 5763 CA THR B 373 -11.664 16.618 82.966 1.00 31.11 A C ANISOU 5763 CA THR B 373 4287 4090 3443 -29 67 -88 A C ATOM 5764 C THR B 373 -10.939 16.307 84.282 1.00 31.97 A C ANISOU 5764 C THR B 373 4505 4167 3473 57 -83 -88 A C ATOM 5765 O THR B 373 -11.094 15.237 84.883 1.00 31.38 A O ANISOU 5765 O THR B 373 4380 4206 3334 150 -99 82 A O ATOM 5766 CB THR B 373 -13.001 17.377 83.160 1.00 31.58 A C ANISOU 5766 CB THR B 373 4389 4019 3588 -12 181 -178 A C ATOM 5767 CG2 THR B 373 -13.505 17.982 81.807 1.00 33.21 A C ANISOU 5767 CG2 THR B 373 4533 4203 3879 -93 -10 -17 A C ATOM 5768 OG1 THR B 373 -13.974 16.487 83.695 1.00 33.37 A O ANISOU 5768 OG1 THR B 373 4127 4517 4034 -27 535 90 A O ATOM 5769 N PHE B 374 -10.125 17.251 84.720 1.00 34.40 A N ANISOU 5769 N PHE B 374 4689 4487 3894 170 -253 -226 A N ATOM 5770 CA PHE B 374 -9.368 17.073 85.957 1.00 37.50 A C ANISOU 5770 CA PHE B 374 5006 4898 4344 150 -314 -246 A C ATOM 5771 C PHE B 374 -10.017 17.725 87.172 1.00 39.00 A C ANISOU 5771 C PHE B 374 5147 5053 4614 116 -335 -226 A C ATOM 5772 O PHE B 374 -11.142 18.236 87.117 1.00 41.39 A O ANISOU 5772 O PHE B 374 5458 5232 5036 -13 -243 -203 A O ATOM 5773 CB PHE B 374 -7.903 17.484 85.745 1.00 37.72 A C ANISOU 5773 CB PHE B 374 5053 4948 4330 220 -276 -224 A C ATOM 5774 CG PHE B 374 -7.172 16.639 84.735 1.00 37.66 A C ANISOU 5774 CG PHE B 374 5061 4937 4311 238 -278 -268 A C ATOM 5775 CD1 PHE B 374 -7.307 16.884 83.358 1.00 38.16 A C ANISOU 5775 CD1 PHE B 374 5244 4988 4264 354 -21 -171 A C ATOM 5776 CD2 PHE B 374 -6.359 15.585 85.151 1.00 37.02 A C ANISOU 5776 CD2 PHE B 374 4654 5025 4384 294 -271 -117 A C ATOM 5777 CE1 PHE B 374 -6.618 16.098 82.434 1.00 38.34 A C ANISOU 5777 CE1 PHE B 374 5344 4828 4395 199 -211 -32 A C ATOM 5778 CE2 PHE B 374 -5.671 14.806 84.251 1.00 37.85 A C ANISOU 5778 CE2 PHE B 374 5207 4919 4254 360 -477 -53 A C ATOM 5779 CZ PHE B 374 -5.799 15.058 82.875 1.00 39.15 A C ANISOU 5779 CZ PHE B 374 5512 5114 4247 215 -207 -96 A C ATOM 5780 OXT PHE B 374 -9.505 17.718 88.297 1.00 40.97 A O1- ANISOU 5780 OXT PHE B 374 5440 5311 4813 91 -383 -245 A O1- TER HETATM 5781 ZN ZN B 375 -4.483 12.864 67.812 1.00 30.69 A ZN ANISOU 5781 ZN ZN B 375 4563 3867 3228 403 -80 -269 A ZN HETATM 5782 ZN ZN B 376 11.700 22.745 63.690 1.00 35.56 A ZN ANISOU 5782 ZN ZN B 376 5536 4797 3177 1674 111 -394 A ZN HETATM 5783 O HOH B 401 11.002 23.183 48.715 1.00 35.36 A O HETATM 5784 O HOH B 402 -7.029 10.055 49.165 1.00 30.48 A O HETATM 5785 O HOH B 403 2.780 17.576 57.643 1.00 37.57 A O HETATM 5786 O HOH B 404 -0.714 6.207 79.371 1.00 28.57 A O HETATM 5787 O HOH B 405 7.038 24.159 61.759 1.00 35.44 A O HETATM 5788 O HOH B 406 2.759 1.021 71.432 1.00 36.13 A O HETATM 5789 O HOH B 407 11.487 11.274 65.760 1.00 38.43 A O HETATM 5790 O HOH B 408 -25.145 12.307 63.939 1.00 34.20 A O HETATM 5791 O HOH B 409 5.042 22.885 63.500 1.00 31.09 A O HETATM 5792 O HOH B 410 -4.615 18.573 86.959 1.00 30.88 A O HETATM 5793 O HOH B 411 13.988 5.729 74.602 1.00 40.90 A O HETATM 5794 O HOH B 412 -10.772 4.345 84.250 1.00 33.37 A O HETATM 5795 O HOH B 413 16.120 21.080 79.397 1.00 46.53 A O HETATM 5796 O HOH B 414 -12.867 13.308 36.499 1.00 38.86 A O HETATM 5797 O HOH B 415 5.173 19.178 56.851 1.00 36.33 A O HETATM 5798 O HOH B 416 -6.264 2.832 40.953 1.00 36.74 A O HETATM 5799 O HOH B 417 -9.173 21.222 42.933 1.00 31.03 A O HETATM 5800 O HOH B 418 -21.172 12.376 62.691 1.00 35.29 A O HETATM 5801 O HOH B 419 -4.548 18.742 40.833 1.00 29.37 A O HETATM 5802 O HOH B 420 -11.142 14.533 87.715 1.00 34.61 A O HETATM 5803 O HOH B 421 -12.900 10.225 72.059 1.00 30.55 A O HETATM 5804 O HOH B 422 8.156 18.127 74.992 1.00 32.42 A O HETATM 5805 O HOH B 423 5.939 15.595 77.983 1.00 30.82 A O HETATM 5806 O HOH B 424 9.793 24.699 88.771 1.00 36.38 A O HETATM 5807 O HOH B 425 -10.103 16.705 32.251 1.00 35.67 A O HETATM 5808 O HOH B 426 -3.488 16.571 58.890 1.00 35.89 A O HETATM 5809 O HOH B 427 13.804 25.701 54.713 1.00 44.82 A O HETATM 5810 O HOH B 428 -4.946 12.748 73.630 1.00 27.52 A O HETATM 5811 O HOH B 429 0.681 19.974 67.555 1.00 30.96 A O HETATM 5812 O HOH B 430 14.169 18.131 87.080 1.00 43.14 A O HETATM 5813 O HOH B 431 8.263 12.029 73.843 1.00 31.09 A O HETATM 5814 O HOH B 432 -0.975 19.449 69.851 1.00 30.32 A O HETATM 5815 O HOH B 433 12.301 9.522 85.027 1.00 34.67 A O HETATM 5816 O HOH B 434 14.632 18.627 77.365 1.00 35.87 A O HETATM 5817 O HOH B 435 -2.682 19.177 72.844 1.00 29.41 A O HETATM 5818 O HOH B 436 -17.199 22.560 41.198 1.00 57.23 A O HETATM 5819 O HOH B 437 -5.224 32.368 71.696 1.00 37.61 A O HETATM 5820 O HOH B 438 7.002 29.921 89.812 1.00 44.81 A O HETATM 5821 O HOH B 439 -17.841 3.456 78.413 1.00 48.34 A O HETATM 5822 O HOH B 440 5.980 17.800 70.841 1.00 30.35 A O HETATM 5823 O HOH B 441 9.029 26.811 95.527 1.00 36.54 A O HETATM 5824 O HOH B 442 6.821 24.267 102.227 1.00 37.00 A O HETATM 5825 O HOH B 443 5.114 24.757 104.132 1.00 38.02 A O HETATM 5826 O HOH B 444 5.972 20.010 95.055 1.00 52.76 A O HETATM 5827 O HOH B 445 3.389 16.901 95.771 1.00 38.78 A O HETATM 5828 O HOH B 446 11.085 13.481 90.501 1.00 37.79 A O HETATM 5829 O HOH B 447 10.059 11.889 88.473 1.00 34.25 A O HETATM 5830 O HOH B 448 12.512 12.125 86.772 1.00 39.14 A O HETATM 5831 O HOH B 449 13.827 14.175 85.604 1.00 35.77 A O HETATM 5832 O HOH B 450 8.104 8.095 91.868 1.00 48.71 A O HETATM 5833 O HOH B 451 14.651 10.653 88.180 1.00 48.67 A O HETATM 5834 O HOH B 452 -1.286 -0.360 82.259 1.00 39.91 A O HETATM 5835 O HOH B 453 13.394 22.192 75.894 1.00 36.65 A O HETATM 5836 O HOH B 454 9.447 18.334 72.326 1.00 32.31 A O HETATM 5837 O HOH B 455 12.395 23.876 73.850 1.00 36.69 A O HETATM 5838 O HOH B 456 8.773 15.924 70.878 1.00 40.79 A O HETATM 5839 O HOH B 457 6.790 15.158 69.070 1.00 30.71 A O HETATM 5840 O HOH B 458 14.700 15.772 68.728 1.00 44.41 A O HETATM 5841 O HOH B 459 -7.005 21.444 86.779 1.00 37.25 A O HETATM 5842 O HOH B 460 -9.341 26.586 83.322 1.00 44.02 A O HETATM 5843 O HOH B 461 -11.449 26.551 81.402 1.00 44.00 A O HETATM 5844 O HOH B 462 -14.310 8.325 73.580 1.00 34.79 A O HETATM 5845 O HOH B 463 -3.422 11.891 66.272 1.00 30.95 A O HETATM 5846 O HOH B 464 -2.072 7.028 64.951 1.00 38.95 A O HETATM 5847 O HOH B 465 -6.196 0.804 67.953 1.00 42.87 A O HETATM 5848 O HOH B 466 4.717 2.403 64.743 1.00 41.67 A O HETATM 5849 O HOH B 467 6.618 9.270 71.669 1.00 30.53 A O HETATM 5850 O HOH B 468 7.113 6.489 74.617 1.00 33.63 A O HETATM 5851 O HOH B 469 12.976 30.803 75.031 1.00 49.12 A O HETATM 5852 O HOH B 470 -25.553 13.158 75.469 1.00 57.74 A O HETATM 5853 O HOH B 471 -12.815 8.573 67.391 1.00 44.58 A O HETATM 5854 O HOH B 472 -23.796 12.993 73.472 1.00 45.68 A O HETATM 5855 O HOH B 473 -6.841 32.717 82.671 1.00 44.51 A O HETATM 5856 O HOH B 474 8.884 28.810 62.235 1.00 46.72 A O HETATM 5857 O HOH B 475 17.306 21.516 59.656 1.00 41.21 A O HETATM 5858 O HOH B 476 13.445 14.141 62.706 1.00 41.30 A O HETATM 5859 O HOH B 477 10.875 13.542 61.142 1.00 36.44 A O HETATM 5860 O HOH B 478 8.475 15.966 76.463 1.00 41.72 A O HETATM 5861 O HOH B 479 -15.971 19.640 77.224 1.00 47.55 A O HETATM 5862 O HOH B 480 -2.604 14.962 62.702 1.00 31.32 A O HETATM 5863 O HOH B 481 -3.775 16.246 56.195 1.00 43.07 A O HETATM 5864 O HOH B 482 -2.852 14.166 59.876 1.00 42.86 A O HETATM 5865 O HOH B 483 0.834 27.292 59.540 1.00 42.03 A O HETATM 5866 O HOH B 484 0.931 18.031 51.877 1.00 39.54 A O HETATM 5867 O HOH B 485 -7.149 22.913 43.498 1.00 49.75 A O HETATM 5868 O HOH B 486 -7.759 25.555 43.779 1.00 43.47 A O HETATM 5869 O HOH B 487 -11.893 30.876 47.279 1.00 55.40 A O HETATM 5870 O HOH B 488 -16.420 6.709 53.832 1.00 47.74 A O HETATM 5871 O HOH B 489 -14.751 10.343 66.229 1.00 36.32 A O HETATM 5872 O HOH B 490 -10.137 10.299 67.130 1.00 44.14 A O HETATM 5873 O HOH B 491 -14.036 9.458 60.308 1.00 40.04 A O HETATM 5874 O HOH B 492 -22.570 11.675 64.878 1.00 34.52 A O HETATM 5875 O HOH B 493 -26.873 17.246 64.729 1.00 42.36 A O HETATM 5876 O HOH B 494 -27.011 6.887 50.703 1.00 45.28 A O HETATM 5877 O HOH B 495 -12.361 10.589 62.973 1.00 33.34 A O HETATM 5878 O HOH B 496 -13.668 11.720 38.919 1.00 39.73 A O HETATM 5879 O HOH B 497 -10.405 25.591 43.103 1.00 37.88 A O HETATM 5880 O HOH B 498 -7.015 9.894 35.290 1.00 41.34 A O HETATM 5881 O HOH B 499 -13.223 3.609 83.620 1.00 40.98 A O HETATM 5882 O HOH B 500 -16.196 18.412 83.740 1.00 36.69 A O HETATM 5883 O HOH B 501 12.630 23.893 87.943 1.00 36.99 A O HETATM 5884 O HOH B 502 8.321 29.245 87.475 1.00 34.87 A O HETATM 5885 O HOH B 503 7.662 16.776 96.561 1.00 45.28 A O HETATM 5886 O HOH B 504 14.038 20.256 94.764 1.00 40.35 A O HETATM 5887 O HOH B 505 9.248 18.382 98.390 1.00 41.68 A O HETATM 5888 O HOH B 506 0.302 4.238 92.403 1.00 41.91 A O HETATM 5889 O HOH B 507 1.998 0.800 91.656 1.00 60.41 A O HETATM 5890 O HOH B 508 -6.623 -0.422 85.331 1.00 45.40 A O HETATM 5891 O HOH B 509 5.101 6.827 92.403 1.00 51.42 A O HETATM 5892 O HOH B 510 11.281 9.947 92.407 1.00 55.79 A O HETATM 5893 O HOH B 511 15.156 25.205 85.312 1.00 42.96 A O HETATM 5894 O HOH B 512 17.715 23.798 85.752 1.00 58.42 A O HETATM 5895 O HOH B 513 12.994 26.578 73.848 1.00 38.34 A O HETATM 5896 O HOH B 514 11.991 28.033 71.790 1.00 42.58 A O HETATM 5897 O HOH B 515 13.318 27.185 69.575 1.00 39.72 A O HETATM 5898 O HOH B 516 -5.654 18.035 89.208 1.00 42.14 A O HETATM 5899 O HOH B 517 -16.050 19.241 86.141 1.00 36.24 A O HETATM 5900 O HOH B 518 1.141 24.936 92.252 1.00 47.48 A O HETATM 5901 O HOH B 519 -6.805 13.406 92.628 1.00 46.77 A O HETATM 5902 O HOH B 520 12.198 36.306 73.465 1.00 45.42 A O HETATM 5903 O HOH B 521 8.845 17.209 100.658 1.00 50.46 A O HETATM 5904 O HOH B 522 12.665 11.301 68.437 1.00 43.48 A O HETATM 5905 O HOH B 523 15.167 10.166 82.939 1.00 52.51 A O HETATM 5906 O HOH B 524 -3.316 32.365 78.999 1.00 40.90 A O HETATM 5907 O HOH B 525 -9.601 10.013 62.889 1.00 49.10 A O HETATM 5908 O HOH B 526 -18.698 4.198 60.288 1.00 50.63 A O HETATM 5909 O HOH B 527 -28.103 10.575 61.365 1.00 41.46 A O HETATM 5910 O HOH B 528 -4.725 36.524 76.682 1.00 50.73 A O HETATM 5911 O HOH B 529 6.282 30.158 67.140 1.00 52.50 A O HETATM 5912 O HOH B 530 16.284 20.908 76.559 1.00 58.70 A O HETATM 5913 O HOH B 531 9.082 28.052 71.470 1.00 39.90 A O HETATM 5914 O HOH B 532 1.187 4.961 97.803 1.00 49.86 A O HETATM 5915 O HOH B 533 8.542 -0.745 74.723 1.00 43.44 A O HETATM 5916 O HOH B 534 -28.909 17.759 60.856 1.00 50.37 A O HETATM 5917 O HOH B 535 5.653 -3.691 84.233 1.00 46.99 A O HETATM 5918 O HOH B 536 6.341 -1.854 82.425 1.00 44.80 A O HETATM 5919 O HOH B 537 4.191 -4.327 75.707 1.00 47.73 A O HETATM 5920 O HOH B 538 -5.946 0.815 77.607 1.00 47.04 A O HETATM 5921 O HOH B 539 -5.321 2.144 89.942 1.00 53.10 A O HETATM 5922 O HOH B 540 -9.834 29.780 60.771 1.00 53.28 A O HETATM 5923 O HOH B 541 -0.564 23.629 90.786 1.00 52.68 A O HETATM 5924 O HOH B 542 14.131 22.659 71.731 1.00 46.45 A O HETATM 5925 O HOH B 543 16.387 18.940 70.827 1.00 44.45 A O HETATM 5926 O HOH B 544 -7.892 14.677 88.477 1.00 45.26 A O HETATM 5927 O HOH B 545 -22.594 17.147 70.895 1.00 44.65 A O HETATM 5928 O HOH B 546 -28.315 13.462 51.995 1.00 44.19 A O HETATM 5929 O HOH B 547 14.704 23.816 89.501 1.00 49.65 A O HETATM 5930 O HOH B 548 -3.715 21.750 47.491 1.00 54.47 A O HETATM 5931 O HOH B 549 -11.989 -1.773 75.656 1.00 48.44 A O HETATM 5932 O HOH B 550 -26.626 13.224 66.018 1.00 44.44 A O HETATM 5933 O HOH B 551 -13.124 10.030 69.253 1.00 44.04 A O HETATM 5934 O HOH B 552 15.646 12.260 84.611 1.00 44.57 A O HETATM 5935 O HOH B 553 -10.528 9.349 36.098 1.00 51.26 A O HETATM 5936 O HOH B 554 -6.602 2.079 87.570 1.00 46.42 A O HETATM 5937 O HOH B 555 17.488 14.293 84.464 1.00 51.30 A O HETATM 5938 O HOH B 556 -4.191 31.225 85.801 1.00 42.43 A O HETATM 5939 O HOH B 557 6.729 17.554 102.222 1.00 63.47 A O HETATM 5940 O HOH B 558 14.685 34.461 73.136 1.00 56.40 A O HETATM 5941 O HOH B 559 17.806 28.366 61.867 1.00 51.24 A O HETATM 5942 O HOH B 560 -19.746 27.511 42.540 1.00 49.80 A O HETATM 5943 O HOH B 561 -16.563 26.095 60.116 1.00 51.29 A O HETATM 5944 O HOH B 562 -23.824 7.458 74.647 1.00 48.69 A O HETATM 5945 O HOH B 563 -5.172 -0.484 47.825 1.00 49.47 A O HETATM 5946 O HOH B 564 -3.696 29.556 88.000 1.00 48.34 A O HETATM 5947 O HOH B 565 13.330 32.113 82.579 1.00 58.44 A O HETATM 5948 O HOH B 566 -10.538 36.062 69.497 1.00 59.52 A O HETATM 5949 O HOH B 567 4.625 15.159 65.644 1.00 39.84 A O HETATM 5950 O HOH B 568 -24.428 15.055 71.905 1.00 54.12 A O HETATM 5951 O HOH B 569 -3.156 15.954 92.788 1.00 49.90 A O HETATM 5952 O HOH B 570 -0.699 16.873 93.156 1.00 50.19 A O HETATM 5953 O HOH B 571 8.714 30.445 91.676 1.00 52.06 A O HETATM 5954 O HOH B 572 10.128 31.307 87.112 1.00 53.18 A O HETATM 5955 O HOH B 573 18.605 19.104 80.021 1.00 44.00 A O HETATM 5956 O HOH B 574 -13.394 14.112 33.015 1.00 45.92 A O HETATM 5957 O HOH B 575 -21.601 10.282 69.372 1.00 46.14 A O HETATM 5958 O HOH B 576 -8.046 15.929 92.252 1.00 55.25 A O HETATM 5959 O HOH B 577 0.717 10.724 95.688 1.00 53.35 A O HETATM 5960 O HOH B 578 -16.023 18.541 37.741 1.00 50.41 A O HETATM 5961 O HOH B 579 -13.010 11.127 89.915 1.00 45.11 A O HETATM 5962 O HOH B 580 3.363 19.194 95.545 1.00 55.90 A O HETATM 5963 O HOH B 581 16.171 32.845 77.381 1.00 48.76 A O HETATM 5964 O HOH B 582 -6.519 14.023 64.633 1.00 37.95 A O HETATM 5965 O HOH B 583 3.069 -0.656 63.552 1.00 46.93 A O HETATM 5966 O HOH B 584 -2.181 34.769 80.190 1.00 43.98 A O HETATM 5967 O HOH B 585 -25.689 21.847 56.340 1.00 56.56 A O HETATM 5968 O HOH B 586 2.934 35.002 78.890 1.00 46.09 A O HETATM 5969 O HOH B 587 -27.808 10.934 49.406 1.00 58.33 A O HETATM 5970 O HOH B 588 10.545 27.422 88.412 1.00 45.59 A O HETATM 5971 O HOH B 589 7.460 20.295 98.700 1.00 58.31 A O HETATM 5972 O HOH B 590 -0.118 33.354 72.165 1.00 44.42 A O HETATM 5973 O HOH B 591 -18.453 38.329 71.122 1.00 47.22 A O HETATM 5974 O HOH B 592 12.238 14.553 69.803 1.00 48.26 A O HETATM 5975 O HOH B 593 -19.894 24.292 61.146 1.00 62.56 A O HETATM 5976 O HOH B 594 -22.800 4.651 77.120 1.00 56.68 A O HETATM 5977 O HOH B 595 -14.116 2.792 48.501 1.00 47.12 A O HETATM 5978 O HOH B 596 -14.054 0.059 80.890 1.00 58.34 A O HETATM 5979 O HOH B 597 -6.453 4.559 36.273 1.00 47.45 A O HETATM 5980 O HOH B 598 -7.431 0.793 41.784 1.00 52.53 A O HETATM 5981 O HOH B 599 -10.129 24.721 85.687 1.00 50.63 A O HETATM 5982 O HOH B 600 14.404 26.871 87.262 1.00 52.81 A O HETATM 5983 CM MPD B2001 -1.621 10.460 63.035 1.00 63.45 A C HETATM 5984 C1 MPD B2001 0.624 11.315 62.380 1.00 63.95 A C HETATM 5985 C2 MPD B2001 -0.129 10.425 63.360 1.00 64.11 A C HETATM 5986 O2 MPD B2001 0.048 10.968 64.694 1.00 64.54 A O HETATM 5987 C3 MPD B2001 0.473 9.015 63.363 1.00 63.68 A C HETATM 5988 C4 MPD B2001 -0.091 8.077 62.295 1.00 63.22 A C HETATM 5989 O4 MPD B2001 -0.846 7.075 62.937 1.00 62.31 A O HETATM 5990 C5 MPD B2001 1.017 7.420 61.481 1.00 62.30 A C CONECT 350 2786 CONECT 502 2786 CONECT 717 2787 CONECT 736 2787 CONECT 760 2787 CONECT 824 2787 CONECT 1302 2786 CONECT 2786 350 502 1302 2850 CONECT 2787 717 736 760 824 CONECT 2850 2786 CONECT 2988 2990 CONECT 2989 2990 CONECT 2990 2989 2988 2991 2992 CONECT 2991 2990 CONECT 2992 2990 2993 CONECT 2993 2992 2994 2995 CONECT 2994 2993 CONECT 2995 2993 CONECT 5983 5985 CONECT 5984 5985 CONECT 5985 5984 5983 5986 5987 CONECT 5986 5985 CONECT 5987 5985 5988 CONECT 5988 5987 5989 5990 CONECT 5989 5988 CONECT 5990 5988 END If you find results from this site helpful for your research, please cite one of our papers:
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