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*** CDK2 ***elNémo ID: 23050916240439595Job options:ID = 23050916240439595 JOBID = CDK2 USERID = unknown PRIVAT = 0 NMODES = 5 DQMIN = -100 DQMAX = 100 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = 0 DORMSD = 0 NRBL = 0 CUTOFF = 0 CAONLY = 0 Input data for this run:HEADER CDK2 CRYST1 53.340 71.434 72.406 90.00 90.00 90.00 P 21 21 21 1 HETATM 1 C ACE A 0 40.807 33.635 39.882 1.00 27.76 C HETATM 2 O ACE A 0 39.803 34.163 40.365 1.00 27.43 O HETATM 3 CH3 ACE A 0 42.068 34.466 39.623 1.00 28.59 C ATOM 4 N MET A 1 40.897 32.336 39.600 1.00 28.70 N ANISOU 4 N MET A 1 3196 4258 3449 289 -618 126 N ATOM 5 CA MET A 1 39.768 31.403 39.770 1.00 28.96 C ANISOU 5 CA MET A 1 3249 4277 3477 290 -606 107 C ATOM 6 C MET A 1 39.220 31.283 41.191 1.00 29.04 C ANISOU 6 C MET A 1 3275 4270 3488 288 -609 103 C ATOM 7 O MET A 1 38.068 30.894 41.365 1.00 27.74 O ANISOU 7 O MET A 1 3119 4098 3320 284 -604 97 O ATOM 8 CB MET A 1 40.078 30.012 39.197 1.00 32.84 C ANISOU 8 CB MET A 1 3746 4770 3962 306 -599 99 C ATOM 9 CG MET A 1 39.930 29.911 37.699 1.00 38.78 C ANISOU 9 CG MET A 1 4492 5536 4709 317 -594 97 C ATOM 10 SD MET A 1 38.276 30.329 37.081 1.00 45.92 S ANISOU 10 SD MET A 1 5407 6419 5621 302 -590 88 S ATOM 11 CE MET A 1 38.626 31.924 36.430 1.00 42.63 C ANISOU 11 CE MET A 1 4966 6023 5207 286 -591 94 C ATOM 12 N GLU A 2 40.020 31.620 42.206 1.00 25.36 N ANISOU 12 N GLU A 2 2812 3796 3028 293 -620 111 N ATOM 13 CA GLU A 2 39.543 31.561 43.600 1.00 25.61 C ANISOU 13 CA GLU A 2 2859 3813 3058 299 -624 109 C ATOM 14 C GLU A 2 38.415 32.575 43.860 1.00 28.69 C ANISOU 14 C GLU A 2 3252 4210 3439 300 -633 108 C ATOM 15 O GLU A 2 37.722 32.465 44.872 1.00 28.32 O ANISOU 15 O GLU A 2 3215 4161 3384 311 -632 108 O ATOM 16 CB GLU A 2 40.703 31.746 44.610 1.00 27.08 C ANISOU 16 CB GLU A 2 3055 3979 3256 310 -637 117 C ATOM 17 CG GLU A 2 41.277 33.155 44.696 1.00 35.68 C ANISOU 17 CG GLU A 2 4140 5062 4353 317 -666 134 C ATOM 18 CD GLU A 2 42.275 33.581 43.634 1.00 57.09 C ANISOU 18 CD GLU A 2 6831 7786 7075 310 -675 153 C ATOM 19 OE1 GLU A 2 42.644 32.746 42.776 1.00 42.77 O ANISOU 19 OE1 GLU A 2 5006 5988 5258 304 -653 149 O ATOM 20 OE2 GLU A 2 42.702 34.758 43.672 1.00 54.71 O1- ANISOU 20 OE2 GLU A 2 6522 7481 6784 313 -710 175 O1- ATOM 21 N ASN A 3 38.217 33.549 42.925 1.00 25.59 N ANISOU 21 N ASN A 3 2848 3828 3046 290 -643 108 N ATOM 22 CA ASN A 3 37.173 34.567 43.027 1.00 25.52 C ANISOU 22 CA ASN A 3 2842 3826 3027 288 -659 101 C ATOM 23 C ASN A 3 35.836 34.041 42.511 1.00 27.25 C ANISOU 23 C ASN A 3 3064 4050 3241 276 -636 91 C ATOM 24 O ASN A 3 34.853 34.790 42.525 1.00 27.65 O ANISOU 24 O ASN A 3 3118 4107 3282 272 -644 83 O ATOM 25 CB ASN A 3 37.547 35.794 42.194 1.00 27.15 C ANISOU 25 CB ASN A 3 3035 4042 3239 275 -688 103 C ATOM 26 CG ASN A 3 38.759 36.521 42.701 1.00 36.93 C ANISOU 26 CG ASN A 3 4270 5274 4488 287 -725 123 C ATOM 27 ND2 ASN A 3 39.829 36.458 41.937 1.00 29.13 N ANISOU 27 ND2 ASN A 3 3263 4291 3513 279 -725 140 N ATOM 28 OD1 ASN A 3 38.733 37.175 43.750 1.00 34.99 O ANISOU 28 OD1 ASN A 3 4038 5018 4237 308 -758 127 O ATOM 29 N PHE A 4 35.803 32.795 42.023 1.00 23.51 N ANISOU 29 N PHE A 4 2590 3568 2774 272 -613 93 N ATOM 30 CA PHE A 4 34.591 32.164 41.485 1.00 22.61 C ANISOU 30 CA PHE A 4 2481 3446 2662 264 -599 92 C ATOM 31 C PHE A 4 34.271 30.894 42.229 1.00 28.22 C ANISOU 31 C PHE A 4 3196 4153 3373 271 -593 106 C ATOM 32 O PHE A 4 35.151 30.065 42.469 1.00 30.94 O ANISOU 32 O PHE A 4 3540 4494 3721 277 -596 108 O ATOM 33 CB PHE A 4 34.717 31.867 39.977 1.00 22.66 C ANISOU 33 CB PHE A 4 2487 3443 2680 256 -594 86 C ATOM 34 CG PHE A 4 34.877 33.109 39.148 1.00 21.85 C ANISOU 34 CG PHE A 4 2376 3347 2578 242 -601 74 C ATOM 35 CD1 PHE A 4 33.763 33.796 38.674 1.00 21.22 C ANISOU 35 CD1 PHE A 4 2303 3259 2502 224 -602 62 C ATOM 36 CD2 PHE A 4 36.135 33.648 38.910 1.00 23.80 C ANISOU 36 CD2 PHE A 4 2608 3610 2826 244 -612 79 C ATOM 37 CE1 PHE A 4 33.910 34.982 37.954 1.00 23.53 C ANISOU 37 CE1 PHE A 4 2586 3559 2796 206 -617 49 C ATOM 38 CE2 PHE A 4 36.276 34.834 38.196 1.00 26.42 C ANISOU 38 CE2 PHE A 4 2926 3952 3161 228 -628 74 C ATOM 39 CZ PHE A 4 35.166 35.482 37.703 1.00 23.96 C ANISOU 39 CZ PHE A 4 2621 3632 2851 207 -632 57 C ATOM 40 N GLN A 5 33.021 30.762 42.643 1.00 26.06 N ANISOU 40 N GLN A 5 2925 3882 3096 270 -589 118 N ATOM 41 CA GLN A 5 32.532 29.571 43.308 1.00 26.89 C ANISOU 41 CA GLN A 5 3027 3987 3203 274 -590 141 C ATOM 42 C GLN A 5 31.680 28.826 42.298 1.00 28.66 C ANISOU 42 C GLN A 5 3255 4189 3444 264 -595 154 C ATOM 43 O GLN A 5 30.680 29.369 41.829 1.00 25.98 O ANISOU 43 O GLN A 5 2920 3843 3108 256 -589 157 O ATOM 44 CB GLN A 5 31.685 29.956 44.535 1.00 28.91 C ANISOU 44 CB GLN A 5 3277 4266 3442 284 -586 157 C ATOM 45 CG GLN A 5 31.034 28.762 45.244 1.00 51.34 C ANISOU 45 CG GLN A 5 6107 7114 6286 285 -589 191 C ATOM 46 CD GLN A 5 29.981 29.170 46.247 0.50 73.59 C ANISOU 46 CD GLN A 5 8915 9964 9084 300 -581 215 C ATOM 47 NE2 GLN A 5 30.057 28.601 47.439 0.50 67.50 N ANISOU 47 NE2 GLN A 5 8132 9212 8303 312 -583 236 N ATOM 48 OE1 GLN A 5 29.065 29.952 45.957 0.50 68.88 O ANISOU 48 OE1 GLN A 5 8319 9376 8478 301 -574 217 O ATOM 49 N LYS A 6 32.073 27.591 41.961 1.00 26.67 N ANISOU 49 N LYS A 6 3007 3923 3204 267 -612 161 N ATOM 50 CA ALYS A 6 31.342 26.728 41.036 0.50 26.84 C ANISOU 50 CA ALYS A 6 3037 3915 3245 267 -632 178 C ATOM 51 CA BLYS A 6 31.317 26.766 41.026 0.50 27.06 C ANISOU 51 CA BLYS A 6 3066 3944 3273 267 -631 178 C ATOM 52 C LYS A 6 29.972 26.377 41.643 1.00 30.73 C ANISOU 52 C LYS A 6 3523 4408 3745 260 -639 218 C ATOM 53 O LYS A 6 29.908 25.959 42.804 1.00 32.50 O ANISOU 53 O LYS A 6 3732 4656 3962 260 -643 239 O ATOM 54 CB ALYS A 6 32.163 25.451 40.767 0.50 29.50 C ANISOU 54 CB ALYS A 6 3379 4243 3586 279 -663 176 C ATOM 55 CB BLYS A 6 32.120 25.525 40.604 0.50 30.21 C ANISOU 55 CB BLYS A 6 3471 4331 3678 279 -662 175 C ATOM 56 CG ALYS A 6 31.465 24.409 39.897 0.50 37.74 C ANISOU 56 CG ALYS A 6 4436 5251 4650 288 -702 198 C ATOM 57 CG BLYS A 6 33.259 25.842 39.642 0.50 43.83 C ANISOU 57 CG BLYS A 6 5202 6055 5395 292 -655 143 C ATOM 58 CD ALYS A 6 32.068 23.028 40.116 0.50 49.75 C ANISOU 58 CD ALYS A 6 5958 6771 6172 299 -750 203 C ATOM 59 CD BLYS A 6 34.078 24.607 39.299 0.50 54.58 C ANISOU 59 CD BLYS A 6 6571 7413 6754 312 -690 137 C ATOM 60 CE ALYS A 6 31.148 21.923 39.660 0.50 62.54 C ANISOU 60 CE ALYS A 6 7590 8358 7816 308 -806 240 C ATOM 61 CE BLYS A 6 35.383 24.979 38.640 0.50 65.58 C ANISOU 61 CE BLYS A 6 7963 8823 8132 327 -677 110 C ATOM 62 NZ ALYS A 6 31.684 20.583 40.016 0.50 72.51 N1+ ANISOU 62 NZ ALYS A 6 8851 9623 9078 314 -866 245 N1+ ATOM 63 NZ BLYS A 6 36.170 23.777 38.260 0.50 74.08 N1+ ANISOU 63 NZ BLYS A 6 9048 9900 9199 353 -713 101 N1+ ATOM 64 N VAL A 7 28.891 26.558 40.879 1.00 23.21 N ANISOU 64 N VAL A 7 3261 2605 2952 302 541 134 N ATOM 65 CA VAL A 7 27.536 26.237 41.318 1.00 22.68 C ANISOU 65 CA VAL A 7 3179 2580 2857 246 568 171 C ATOM 66 C VAL A 7 27.231 24.844 40.786 1.00 27.18 C ANISOU 66 C VAL A 7 3832 3078 3419 151 637 194 C ATOM 67 O VAL A 7 26.942 23.938 41.574 1.00 27.54 O ANISOU 67 O VAL A 7 3937 3096 3433 149 695 236 O ATOM 68 CB VAL A 7 26.487 27.293 40.865 1.00 24.93 C ANISOU 68 CB VAL A 7 3376 2946 3150 195 507 145 C ATOM 69 CG1 VAL A 7 25.061 26.830 41.194 1.00 25.42 C ANISOU 69 CG1 VAL A 7 3421 3062 3176 120 542 147 C ATOM 70 CG2 VAL A 7 26.765 28.664 41.475 1.00 24.70 C ANISOU 70 CG2 VAL A 7 3260 2987 3139 296 419 123 C ATOM 71 N GLU A 8 27.307 24.668 39.452 1.00 24.11 N ANISOU 71 N GLU A 8 3446 2657 3058 77 629 167 N ATOM 72 CA GLU A 8 27.070 23.396 38.781 1.00 25.41 C ANISOU 72 CA GLU A 8 3663 2757 3235 -3 676 172 C ATOM 73 C GLU A 8 27.619 23.369 37.362 1.00 27.81 C ANISOU 73 C GLU A 8 3952 3042 3571 -35 644 132 C ATOM 74 O GLU A 8 27.826 24.419 36.742 1.00 23.04 O ANISOU 74 O GLU A 8 3299 2480 2974 -27 599 106 O ATOM 75 CB GLU A 8 25.569 23.032 38.781 1.00 27.71 C ANISOU 75 CB GLU A 8 3926 3073 3528 -94 727 175 C ATOM 76 CG GLU A 8 24.668 24.039 38.082 1.00 34.54 C ANISOU 76 CG GLU A 8 4705 4018 4400 -127 687 118 C ATOM 77 CD GLU A 8 23.180 23.829 38.283 1.00 53.79 C ANISOU 77 CD GLU A 8 7105 6507 6826 -200 731 81 C ATOM 78 OE1 GLU A 8 22.768 23.431 39.399 1.00 55.10 O ANISOU 78 OE1 GLU A 8 7287 6689 6961 -215 780 115 O ATOM 79 OE2 GLU A 8 22.418 24.099 37.327 1.00 39.05 O1- ANISOU 79 OE2 GLU A 8 5191 4673 4974 -238 716 4 O1- ATOM 80 N LYS A 9 27.830 22.168 36.837 1.00 26.69 N ANISOU 80 N LYS A 9 3852 2843 3448 -72 662 127 N ATOM 81 CA LYS A 9 28.250 21.983 35.456 1.00 24.77 C ANISOU 81 CA LYS A 9 3576 2602 3234 -102 628 84 C ATOM 82 C LYS A 9 27.004 22.230 34.614 1.00 29.33 C ANISOU 82 C LYS A 9 4084 3218 3841 -161 645 65 C ATOM 83 O LYS A 9 25.925 21.710 34.936 1.00 30.66 O ANISOU 83 O LYS A 9 4248 3377 4023 -205 696 68 O ATOM 84 CB LYS A 9 28.759 20.545 35.230 1.00 27.14 C ANISOU 84 CB LYS A 9 3927 2836 3549 -112 622 72 C ATOM 85 CG LYS A 9 29.223 20.300 33.794 1.00 29.47 C ANISOU 85 CG LYS A 9 4164 3158 3874 -134 571 19 C ATOM 86 CD LYS A 9 29.791 18.914 33.599 1.00 32.91 C ANISOU 86 CD LYS A 9 4639 3542 4325 -132 533 -9 C ATOM 87 CE LYS A 9 29.630 18.497 32.160 1.00 40.01 C ANISOU 87 CE LYS A 9 5442 4482 5278 -164 496 -55 C ATOM 88 NZ LYS A 9 30.266 17.179 31.893 1.00 49.08 N1+ ANISOU 88 NZ LYS A 9 6609 5594 6445 -153 427 -98 N1+ ATOM 89 N ILE A 10 27.117 23.084 33.594 1.00 24.62 N ANISOU 89 N ILE A 10 3441 2669 3247 -159 606 34 N ATOM 90 CA ILE A 10 25.958 23.381 32.755 1.00 25.93 C ANISOU 90 CA ILE A 10 3551 2872 3427 -186 613 -8 C ATOM 91 C ILE A 10 26.073 22.812 31.352 1.00 31.74 C ANISOU 91 C ILE A 10 4243 3616 4201 -195 602 -49 C ATOM 92 O ILE A 10 25.067 22.703 30.656 1.00 34.16 O ANISOU 92 O ILE A 10 4501 3946 4533 -201 619 -103 O ATOM 93 CB ILE A 10 25.418 24.836 32.872 1.00 29.03 C ANISOU 93 CB ILE A 10 3931 3318 3782 -166 577 -21 C ATOM 94 CG1 ILE A 10 26.517 25.860 32.540 1.00 28.60 C ANISOU 94 CG1 ILE A 10 3892 3270 3706 -136 525 1 C ATOM 95 CG2 ILE A 10 24.840 25.047 34.284 1.00 30.26 C ANISOU 95 CG2 ILE A 10 4093 3489 3914 -161 591 -2 C ATOM 96 CD1 ILE A 10 26.112 27.370 32.470 1.00 27.90 C ANISOU 96 CD1 ILE A 10 3801 3215 3582 -114 468 -9 C ATOM 97 N GLY A 11 27.274 22.384 30.970 1.00 26.44 N ANISOU 97 N GLY A 11 3579 2935 3532 -186 570 -41 N ATOM 98 CA GLY A 11 27.462 21.757 29.670 1.00 26.87 C ANISOU 98 CA GLY A 11 3571 3015 3621 -185 545 -84 C ATOM 99 C GLY A 11 28.891 21.470 29.288 1.00 28.15 C ANISOU 99 C GLY A 11 3734 3195 3766 -177 490 -94 C ATOM 100 O GLY A 11 29.829 21.740 30.044 1.00 23.77 O ANISOU 100 O GLY A 11 3236 2624 3171 -168 477 -81 O ATOM 101 N GLU A 12 29.036 20.876 28.105 1.00 26.63 N ANISOU 101 N GLU A 12 3466 3048 3605 -171 455 -138 N ATOM 102 CA GLU A 12 30.304 20.534 27.480 1.00 25.67 C ANISOU 102 CA GLU A 12 3313 2979 3463 -168 387 -177 C ATOM 103 C GLU A 12 30.306 21.308 26.186 1.00 27.96 C ANISOU 103 C GLU A 12 3538 3353 3732 -162 377 -190 C ATOM 104 O GLU A 12 29.473 21.065 25.306 1.00 27.37 O ANISOU 104 O GLU A 12 3390 3310 3700 -134 383 -213 O ATOM 105 CB GLU A 12 30.414 19.021 27.219 1.00 27.56 C ANISOU 105 CB GLU A 12 3504 3209 3759 -157 335 -224 C ATOM 106 CG GLU A 12 30.437 18.187 28.492 1.00 36.88 C ANISOU 106 CG GLU A 12 4777 4288 4948 -161 343 -204 C ATOM 107 CD GLU A 12 29.830 16.804 28.380 1.00 59.05 C ANISOU 107 CD GLU A 12 7553 7044 7839 -163 329 -221 C ATOM 108 OE1 GLU A 12 29.615 16.327 27.241 1.00 43.19 O ANISOU 108 OE1 GLU A 12 5426 5093 5891 -147 287 -272 O ATOM 109 OE2 GLU A 12 29.578 16.191 29.442 1.00 52.49 O1- ANISOU 109 OE2 GLU A 12 6815 6113 7014 -178 359 -185 O1- ATOM 110 N GLY A 13 31.181 22.304 26.109 1.00 21.44 N ANISOU 110 N GLY A 13 2746 2559 2841 -184 372 -177 N ATOM 111 CA GLY A 13 31.292 23.140 24.931 1.00 21.89 C ANISOU 111 CA GLY A 13 2770 2688 2859 -189 371 -173 C ATOM 112 C GLY A 13 32.207 22.527 23.900 1.00 24.38 C ANISOU 112 C GLY A 13 2997 3105 3161 -194 312 -230 C ATOM 113 O GLY A 13 32.657 21.384 24.045 1.00 24.33 O ANISOU 113 O GLY A 13 2946 3113 3184 -185 256 -285 O ATOM 114 N THR A 14 32.479 23.280 22.853 1.00 22.94 N ANISOU 114 N THR A 14 2791 2997 2929 -207 315 -221 N ATOM 115 CA THR A 14 33.366 22.830 21.803 1.00 22.15 C ANISOU 115 CA THR A 14 2593 3023 2801 -217 258 -279 C ATOM 116 C THR A 14 34.796 22.712 22.350 1.00 21.75 C ANISOU 116 C THR A 14 2559 3000 2703 -276 224 -338 C ATOM 117 O THR A 14 35.519 21.763 22.029 1.00 20.97 O ANISOU 117 O THR A 14 2378 2987 2601 -272 143 -427 O ATOM 118 CB THR A 14 33.340 23.836 20.637 1.00 34.96 C ANISOU 118 CB THR A 14 4211 4712 4359 -225 288 -241 C ATOM 119 CG2 THR A 14 34.036 23.313 19.401 1.00 33.55 C ANISOU 119 CG2 THR A 14 3906 4690 4151 -221 229 -299 C ATOM 120 OG1 THR A 14 31.990 24.191 20.327 1.00 38.98 O ANISOU 120 OG1 THR A 14 4743 5174 4893 -156 324 -202 O ATOM 121 N TYR A 15 35.194 23.662 23.207 1.00 19.28 N ANISOU 121 N TYR A 15 2348 2620 2357 -318 277 -309 N ATOM 122 CA TYR A 15 36.575 23.766 23.678 1.00 18.81 C ANISOU 122 CA TYR A 15 2305 2592 2248 -365 261 -390 C ATOM 123 C TYR A 15 36.851 23.304 25.075 1.00 19.75 C ANISOU 123 C TYR A 15 2487 2628 2389 -330 249 -432 C ATOM 124 O TYR A 15 38.020 23.204 25.461 1.00 20.60 O ANISOU 124 O TYR A 15 2602 2770 2455 -343 222 -538 O ATOM 125 CB TYR A 15 37.088 25.208 23.528 1.00 20.88 C ANISOU 125 CB TYR A 15 2620 2855 2458 -435 328 -356 C ATOM 126 CG TYR A 15 36.803 25.805 22.172 1.00 23.11 C ANISOU 126 CG TYR A 15 2876 3205 2701 -468 350 -298 C ATOM 127 CD1 TYR A 15 37.497 25.383 21.043 1.00 25.56 C ANISOU 127 CD1 TYR A 15 3087 3662 2961 -501 310 -361 C ATOM 128 CD2 TYR A 15 35.805 26.759 22.008 1.00 25.68 C ANISOU 128 CD2 TYR A 15 3272 3454 3030 -453 401 -188 C ATOM 129 CE1 TYR A 15 37.207 25.897 19.783 1.00 28.27 C ANISOU 129 CE1 TYR A 15 3408 4072 3259 -514 333 -301 C ATOM 130 CE2 TYR A 15 35.520 27.297 20.754 1.00 27.94 C ANISOU 130 CE2 TYR A 15 3556 3793 3267 -462 418 -137 C ATOM 131 CZ TYR A 15 36.217 26.855 19.645 1.00 34.26 C ANISOU 131 CZ TYR A 15 4261 4737 4019 -490 391 -187 C ATOM 132 OH TYR A 15 35.945 27.394 18.413 1.00 36.34 O ANISOU 132 OH TYR A 15 4527 5057 4223 -487 413 -131 O ATOM 133 N GLY A 16 35.812 23.187 25.884 1.00 17.85 N ANISOU 133 N GLY A 16 2299 2281 2201 -285 280 -358 N ATOM 134 CA GLY A 16 35.996 22.797 27.271 1.00 18.09 C ANISOU 134 CA GLY A 16 2401 2228 2243 -241 279 -381 C ATOM 135 C GLY A 16 34.705 22.819 28.042 1.00 20.59 C ANISOU 135 C GLY A 16 2766 2447 2610 -209 326 -284 C ATOM 136 O GLY A 16 33.640 23.086 27.483 1.00 19.73 O ANISOU 136 O GLY A 16 2633 2336 2530 -217 352 -220 O ATOM 137 N VAL A 17 34.788 22.477 29.314 1.00 20.06 N ANISOU 137 N VAL A 17 2767 2309 2548 -164 332 -290 N ATOM 138 CA VAL A 17 33.616 22.412 30.184 1.00 19.81 C ANISOU 138 CA VAL A 17 2778 2196 2552 -140 378 -208 C ATOM 139 C VAL A 17 33.049 23.814 30.455 1.00 20.23 C ANISOU 139 C VAL A 17 2841 2239 2605 -147 427 -143 C ATOM 140 O VAL A 17 33.784 24.806 30.431 1.00 18.81 O ANISOU 140 O VAL A 17 2664 2082 2402 -155 431 -160 O ATOM 141 CB VAL A 17 33.972 21.624 31.473 1.00 24.70 C ANISOU 141 CB VAL A 17 3477 2749 3161 -83 369 -231 C ATOM 142 CG1 VAL A 17 34.974 22.384 32.354 1.00 25.60 C ANISOU 142 CG1 VAL A 17 3631 2860 3235 -32 377 -280 C ATOM 143 CG2 VAL A 17 32.728 21.230 32.265 1.00 25.23 C ANISOU 143 CG2 VAL A 17 3582 2743 3260 -75 417 -148 C ATOM 144 N VAL A 18 31.733 23.875 30.692 1.00 17.26 N ANISOU 144 N VAL A 18 2467 1832 2257 -146 457 -83 N ATOM 145 CA VAL A 18 31.029 25.123 31.011 1.00 16.28 C ANISOU 145 CA VAL A 18 2352 1705 2130 -143 476 -37 C ATOM 146 C VAL A 18 30.378 24.959 32.384 1.00 17.07 C ANISOU 146 C VAL A 18 2482 1764 2239 -108 500 -6 C ATOM 147 O VAL A 18 29.659 23.975 32.634 1.00 17.26 O ANISOU 147 O VAL A 18 2513 1764 2282 -117 523 3 O ATOM 148 CB VAL A 18 29.962 25.500 29.961 1.00 19.84 C ANISOU 148 CB VAL A 18 2772 2182 2584 -165 477 -24 C ATOM 149 CG1 VAL A 18 29.338 26.852 30.298 1.00 19.82 C ANISOU 149 CG1 VAL A 18 2791 2176 2563 -154 468 4 C ATOM 150 CG2 VAL A 18 30.527 25.512 28.543 1.00 20.16 C ANISOU 150 CG2 VAL A 18 2777 2272 2609 -190 458 -47 C ATOM 151 N TYR A 19 30.636 25.897 33.285 1.00 16.09 N ANISOU 151 N TYR A 19 1894 1692 2528 206 208 6 N ATOM 152 CA TYR A 19 30.035 25.870 34.616 1.00 16.09 C ANISOU 152 CA TYR A 19 2004 1656 2453 244 197 122 C ATOM 153 C TYR A 19 29.222 27.110 34.846 1.00 17.16 C ANISOU 153 C TYR A 19 2185 1908 2427 231 155 107 C ATOM 154 O TYR A 19 29.541 28.181 34.340 1.00 16.00 O ANISOU 154 O TYR A 19 2011 1836 2232 232 91 75 O ATOM 155 CB TYR A 19 31.117 25.893 35.712 1.00 20.32 C ANISOU 155 CB TYR A 19 2587 2151 2981 326 95 256 C ATOM 156 CG TYR A 19 32.032 24.695 35.737 1.00 28.12 C ANISOU 156 CG TYR A 19 3531 3000 4154 372 106 310 C ATOM 157 CD1 TYR A 19 31.570 23.452 36.150 1.00 31.80 C ANISOU 157 CD1 TYR A 19 4017 3327 4740 376 199 393 C ATOM 158 CD2 TYR A 19 33.373 24.812 35.387 1.00 30.34 C ANISOU 158 CD2 TYR A 19 3745 3273 4512 414 29 275 C ATOM 159 CE1 TYR A 19 32.416 22.338 36.179 1.00 33.70 C ANISOU 159 CE1 TYR A 19 4201 3401 5202 432 212 456 C ATOM 160 CE2 TYR A 19 34.234 23.716 35.444 1.00 33.08 C ANISOU 160 CE2 TYR A 19 4031 3476 5061 471 29 315 C ATOM 161 CZ TYR A 19 33.747 22.479 35.829 1.00 42.65 C ANISOU 161 CZ TYR A 19 5254 4530 6419 486 118 414 C ATOM 162 OH TYR A 19 34.591 21.397 35.873 1.00 48.46 O ANISOU 162 OH TYR A 19 5916 5091 7405 553 120 466 O ATOM 163 N LYS A 20 28.198 26.977 35.674 1.00 15.55 N ANISOU 163 N LYS A 20 2045 1708 2156 214 196 132 N ATOM 164 CA LYS A 20 27.501 28.111 36.253 1.00 15.03 C ANISOU 164 CA LYS A 20 2014 1734 1964 207 148 114 C ATOM 165 C LYS A 20 28.355 28.406 37.516 1.00 16.56 C ANISOU 165 C LYS A 20 2252 1941 2098 248 62 216 C ATOM 166 O LYS A 20 28.739 27.473 38.255 1.00 17.39 O ANISOU 166 O LYS A 20 2396 1997 2216 267 71 327 O ATOM 167 CB LYS A 20 26.062 27.744 36.641 1.00 16.98 C ANISOU 167 CB LYS A 20 2293 1996 2163 152 238 60 C ATOM 168 CG LYS A 20 25.318 28.966 37.186 1.00 15.89 C ANISOU 168 CG LYS A 20 2160 1950 1926 138 188 1 C ATOM 169 CD LYS A 20 23.875 28.624 37.466 1.00 17.80 C ANISOU 169 CD LYS A 20 2418 2220 2124 74 279 -93 C ATOM 170 CE LYS A 20 23.068 29.846 37.781 1.00 17.91 C ANISOU 170 CE LYS A 20 2402 2316 2088 61 233 -195 C ATOM 171 NZ LYS A 20 21.678 29.489 38.174 1.00 21.71 N1+ ANISOU 171 NZ LYS A 20 2894 2835 2520 -11 321 -316 N1+ ATOM 172 N ALA A 21 28.697 29.682 37.733 1.00 15.79 N ANISOU 172 N ALA A 21 2134 1918 1949 262 -15 182 N ATOM 173 CA ALA A 21 29.517 30.063 38.877 1.00 16.23 C ANISOU 173 CA ALA A 21 2194 2038 1934 290 -88 233 C ATOM 174 C ALA A 21 29.101 31.371 39.459 1.00 17.99 C ANISOU 174 C ALA A 21 2385 2355 2094 259 -112 142 C ATOM 175 O ALA A 21 28.371 32.116 38.821 1.00 16.66 O ANISOU 175 O ALA A 21 2190 2169 1970 240 -93 58 O ATOM 176 CB ALA A 21 30.983 30.154 38.460 1.00 17.70 C ANISOU 176 CB ALA A 21 2342 2203 2182 346 -149 250 C ATOM 177 N ARG A 22 29.552 31.654 40.697 1.00 17.62 N ANISOU 177 N ARG A 22 2321 2423 1951 253 -154 153 N ATOM 178 CA AARG A 22 29.268 32.924 41.353 0.50 18.29 C ANISOU 178 CA AARG A 22 2337 2610 2002 209 -163 22 C ATOM 179 CA BARG A 22 29.263 32.921 41.354 0.50 18.34 C ANISOU 179 CA BARG A 22 2344 2617 2009 208 -162 23 C ATOM 180 C ARG A 22 30.566 33.686 41.522 1.00 21.67 C ANISOU 180 C ARG A 22 2694 3092 2446 243 -213 -21 C ATOM 181 O ARG A 22 31.539 33.129 42.051 1.00 23.46 O ANISOU 181 O ARG A 22 2920 3393 2602 282 -260 56 O ATOM 182 CB AARG A 22 28.600 32.727 42.727 0.50 20.00 C ANISOU 182 CB AARG A 22 2550 2976 2071 133 -146 9 C ATOM 183 CB BARG A 22 28.553 32.711 42.713 0.50 20.28 C ANISOU 183 CB BARG A 22 2589 3010 2108 131 -144 9 C ATOM 184 CG AARG A 22 28.273 34.064 43.403 0.50 24.49 C ANISOU 184 CG AARG A 22 3008 3662 2636 66 -139 -180 C ATOM 185 CG BARG A 22 27.142 32.166 42.552 0.50 24.69 C ANISOU 185 CG BARG A 22 3205 3516 2660 75 -74 -5 C ATOM 186 CD AARG A 22 27.474 33.925 44.676 0.50 25.35 C ANISOU 186 CD AARG A 22 3093 3948 2593 -44 -110 -237 C ATOM 187 CD BARG A 22 26.262 32.269 43.786 0.50 29.97 C ANISOU 187 CD BARG A 22 3853 4339 3195 -35 -41 -82 C ATOM 188 NE AARG A 22 26.286 33.099 44.480 0.50 26.44 N ANISOU 188 NE AARG A 22 3321 4016 2709 -85 -55 -197 N ATOM 189 NE BARG A 22 25.050 31.458 43.621 0.50 30.52 N ANISOU 189 NE BARG A 22 3995 4350 3250 -89 38 -79 N ATOM 190 CZ AARG A 22 25.162 33.509 43.902 0.50 34.32 C ANISOU 190 CZ AARG A 22 4307 4927 3808 -110 -10 -325 C ATOM 191 CZ BARG A 22 24.894 30.237 44.122 0.50 42.91 C ANISOU 191 CZ BARG A 22 5652 5925 4726 -123 81 63 C ATOM 192 NH1AARG A 22 25.054 34.754 43.449 0.50 21.92 N1+ ANISOU 192 NH1AARG A 22 2640 3303 2385 -89 -22 -468 N1+ ATOM 193 NH1BARG A 22 25.852 29.688 44.860 0.50 36.23 N1+ ANISOU 193 NH1BARG A 22 4830 5152 3785 -98 33 242 N1+ ATOM 194 NH2AARG A 22 24.139 32.679 43.771 0.50 23.54 N ANISOU 194 NH2AARG A 22 3015 3522 2408 -152 50 -309 N ATOM 195 NH2BARG A 22 23.776 29.558 43.899 0.50 22.76 N ANISOU 195 NH2BARG A 22 3158 3309 2183 -181 176 30 N ATOM 196 N ASN A 23 30.576 34.953 41.081 1.00 19.46 N ANISOU 196 N ASN A 23 2349 2774 2273 233 -199 -144 N ATOM 197 CA ASN A 23 31.705 35.869 41.210 1.00 21.11 C ANISOU 197 CA ASN A 23 2475 3021 2525 246 -214 -233 C ATOM 198 C ASN A 23 31.606 36.368 42.650 1.00 27.46 C ANISOU 198 C ASN A 23 3183 4018 3234 185 -205 -353 C ATOM 199 O ASN A 23 30.633 37.034 43.010 1.00 27.39 O ANISOU 199 O ASN A 23 3118 4024 3264 121 -161 -468 O ATOM 200 CB ASN A 23 31.546 37.023 40.207 1.00 24.55 C ANISOU 200 CB ASN A 23 2877 3316 3134 244 -178 -299 C ATOM 201 CG ASN A 23 32.676 38.016 40.234 1.00 33.19 C ANISOU 201 CG ASN A 23 3890 4415 4308 243 -163 -403 C ATOM 202 ND2 ASN A 23 33.080 38.475 39.063 1.00 27.05 N ANISOU 202 ND2 ASN A 23 3130 3502 3646 259 -148 -371 N ATOM 203 OD1 ASN A 23 33.182 38.397 41.291 1.00 28.32 O ANISOU 203 OD1 ASN A 23 3181 3938 3640 217 -155 -524 O ATOM 204 N LYS A 24 32.557 35.991 43.491 1.00 25.46 N ANISOU 204 N LYS A 24 2892 3933 2848 200 -248 -334 N ATOM 205 CA LYS A 24 32.562 36.387 44.905 1.00 27.66 C ANISOU 205 CA LYS A 24 3052 4469 2989 128 -243 -453 C ATOM 206 C LYS A 24 32.696 37.896 45.155 1.00 33.85 C ANISOU 206 C LYS A 24 3674 5297 3891 65 -176 -712 C ATOM 207 O LYS A 24 32.217 38.388 46.179 1.00 35.89 O ANISOU 207 O LYS A 24 3811 5739 4086 -33 -138 -869 O ATOM 208 CB LYS A 24 33.646 35.620 45.668 1.00 30.22 C ANISOU 208 CB LYS A 24 3358 4992 3132 175 -319 -349 C ATOM 209 CG LYS A 24 33.371 34.124 45.747 1.00 39.78 C ANISOU 209 CG LYS A 24 4703 6172 4241 220 -369 -89 C ATOM 210 CD LYS A 24 34.567 33.371 46.297 1.00 46.31 C ANISOU 210 CD LYS A 24 5508 7142 4944 304 -462 49 C ATOM 211 CE LYS A 24 34.291 31.898 46.440 1.00 55.80 C ANISOU 211 CE LYS A 24 6830 8282 6088 352 -500 327 C ATOM 212 NZ LYS A 24 35.515 31.145 46.816 1.00 65.69 N1+ ANISOU 212 NZ LYS A 24 8056 9625 7278 465 -603 487 N1+ ATOM 213 N LEU A 25 33.314 38.627 44.212 1.00 30.43 N ANISOU 213 N LEU A 25 3228 4690 3642 106 -148 -767 N ATOM 214 CA LEU A 25 33.545 40.067 44.355 1.00 30.63 C ANISOU 214 CA LEU A 25 3099 4706 3835 52 -62 -1005 C ATOM 215 C LEU A 25 32.319 40.909 44.022 1.00 34.77 C ANISOU 215 C LEU A 25 3591 5059 4561 8 3 -1083 C ATOM 216 O LEU A 25 32.009 41.847 44.758 1.00 36.19 O ANISOU 216 O LEU A 25 3605 5312 4834 -75 77 -1310 O ATOM 217 CB LEU A 25 34.764 40.530 43.535 0.50 29.95 C ANISOU 217 CB LEU A 25 3010 4503 3867 101 -44 -1029 C ATOM 218 CG LEU A 25 36.129 39.942 43.919 0.50 34.59 C ANISOU 218 CG LEU A 25 3576 5271 4294 146 -102 -1025 C ATOM 219 CD1 LEU A 25 37.141 40.188 42.826 0.50 33.78 C ANISOU 219 CD1 LEU A 25 3514 5006 4314 190 -88 -1022 C ATOM 220 CD2 LEU A 25 36.638 40.521 45.228 0.50 38.07 C ANISOU 220 CD2 LEU A 25 3817 6005 4641 82 -64 -1257 C ATOM 221 N THR A 26 31.638 40.588 42.916 1.00 29.42 N ANISOU 221 N THR A 26 3047 4168 3962 63 -22 -915 N ATOM 222 CA THR A 26 30.468 41.346 42.457 1.00 27.97 C ANISOU 222 CA THR A 26 2835 3813 3978 50 19 -956 C ATOM 223 C THR A 26 29.135 40.706 42.883 1.00 30.12 C ANISOU 223 C THR A 26 3143 4150 4151 15 -2 -943 C ATOM 224 O THR A 26 28.102 41.377 42.849 1.00 29.86 O ANISOU 224 O THR A 26 3041 4032 4274 -11 31 -1043 O ATOM 225 CB THR A 26 30.495 41.480 40.932 1.00 33.44 C ANISOU 225 CB THR A 26 3628 4274 4803 126 3 -785 C ATOM 226 CG2 THR A 26 31.773 42.161 40.409 1.00 34.13 C ANISOU 226 CG2 THR A 26 3689 4280 4999 141 39 -799 C ATOM 227 OG1 THR A 26 30.343 40.179 40.365 1.00 29.65 O ANISOU 227 OG1 THR A 26 3296 3810 4159 170 -63 -597 O ATOM 228 N GLY A 27 29.160 39.404 43.183 1.00 24.38 N ANISOU 228 N GLY A 27 2525 3546 3192 20 -52 -812 N ATOM 229 CA GLY A 27 27.979 38.627 43.548 1.00 22.56 C ANISOU 229 CA GLY A 27 2352 3373 2847 -23 -57 -784 C ATOM 230 C GLY A 27 27.232 38.115 42.331 1.00 24.41 C ANISOU 230 C GLY A 27 2704 3432 3139 40 -71 -646 C ATOM 231 O GLY A 27 26.228 37.409 42.470 1.00 23.29 O ANISOU 231 O GLY A 27 2616 3316 2915 8 -61 -630 O ATOM 232 N GLU A 28 27.706 38.452 41.128 1.00 21.68 N ANISOU 232 N GLU A 28 2388 2929 2920 117 -86 -557 N ATOM 233 CA AGLU A 28 27.000 38.026 39.929 0.50 20.31 C ANISOU 233 CA AGLU A 28 2293 2642 2782 166 -98 -443 C ATOM 234 CA BGLU A 28 27.028 38.034 39.905 0.50 19.86 C ANISOU 234 CA BGLU A 28 2236 2583 2726 167 -99 -440 C ATOM 235 C GLU A 28 27.184 36.538 39.605 1.00 20.56 C ANISOU 235 C GLU A 28 2442 2704 2666 183 -111 -305 C ATOM 236 O GLU A 28 28.213 35.947 39.930 1.00 20.43 O ANISOU 236 O GLU A 28 2458 2737 2567 194 -131 -243 O ATOM 237 CB AGLU A 28 27.320 38.947 38.729 0.50 22.08 C ANISOU 237 CB AGLU A 28 2492 2719 3177 222 -107 -384 C ATOM 238 CB BGLU A 28 27.507 38.891 38.704 0.50 21.17 C ANISOU 238 CB BGLU A 28 2384 2607 3052 224 -108 -373 C ATOM 239 CG AGLU A 28 28.646 38.671 38.051 0.50 26.50 C ANISOU 239 CG AGLU A 28 3105 3258 3708 251 -124 -278 C ATOM 240 CG BGLU A 28 26.663 38.819 37.426 0.50 21.51 C ANISOU 240 CG BGLU A 28 2457 2573 3143 269 -125 -271 C ATOM 241 CD AGLU A 28 29.191 39.742 37.129 0.50 40.66 C ANISOU 241 CD AGLU A 28 4863 4929 5656 275 -115 -235 C ATOM 242 CD BGLU A 28 25.157 38.992 37.527 0.50 22.36 C ANISOU 242 CD BGLU A 28 2522 2679 3295 268 -122 -344 C ATOM 243 OE1AGLU A 28 28.479 40.158 36.187 0.50 35.60 O ANISOU 243 OE1AGLU A 28 4217 4207 5101 303 -124 -152 O ATOM 244 OE1BGLU A 28 24.638 40.043 37.086 0.50 20.67 O ANISOU 244 OE1BGLU A 28 2231 2368 3255 306 -133 -349 O ATOM 245 OE2AGLU A 28 30.373 40.107 37.307 0.50 24.19 O1- ANISOU 245 OE2AGLU A 28 2756 2842 3594 263 -99 -274 O1- ATOM 246 OE2BGLU A 28 24.488 38.011 37.906 0.50 12.98 O1- ANISOU 246 OE2BGLU A 28 1379 1576 1977 235 -107 -379 O1- ATOM 247 N VAL A 29 26.165 35.953 38.997 1.00 17.47 N ANISOU 247 N VAL A 29 2092 2283 2261 186 -94 -275 N ATOM 248 CA AVAL A 29 26.134 34.581 38.526 0.50 15.92 C ANISOU 248 CA AVAL A 29 1981 2087 1983 194 -76 -178 C ATOM 249 CA BVAL A 29 26.202 34.568 38.514 0.50 16.55 C ANISOU 249 CA BVAL A 29 2061 2164 2061 195 -77 -174 C ATOM 250 C VAL A 29 26.599 34.648 37.058 1.00 16.85 C ANISOU 250 C VAL A 29 2095 2138 2168 241 -92 -102 C ATOM 251 O VAL A 29 26.091 35.508 36.309 1.00 17.21 O ANISOU 251 O VAL A 29 2093 2154 2293 261 -105 -113 O ATOM 252 CB AVAL A 29 24.676 34.096 38.689 0.50 19.22 C ANISOU 252 CB AVAL A 29 2411 2532 2359 150 -26 -247 C ATOM 253 CB BVAL A 29 24.949 33.674 38.766 0.50 21.24 C ANISOU 253 CB BVAL A 29 2694 2791 2587 149 -20 -210 C ATOM 254 CG1AVAL A 29 24.386 32.909 37.797 0.50 18.25 C ANISOU 254 CG1AVAL A 29 2337 2384 2214 157 21 -191 C ATOM 255 CG1BVAL A 29 24.719 33.444 40.253 0.50 21.84 C ANISOU 255 CG1BVAL A 29 2783 2960 2556 79 -2 -254 C ATOM 256 CG2AVAL A 29 24.362 33.772 40.151 0.50 19.80 C ANISOU 256 CG2AVAL A 29 2500 2697 2324 75 0 -301 C ATOM 257 CG2BVAL A 29 23.687 34.209 38.099 0.50 20.89 C ANISOU 257 CG2BVAL A 29 2599 2734 2605 153 -7 -299 C ATOM 258 N VAL A 30 27.538 33.799 36.665 1.00 15.50 N ANISOU 258 N VAL A 30 1960 1956 1974 253 -93 -28 N ATOM 259 CA VAL A 30 28.119 33.809 35.328 1.00 14.60 C ANISOU 259 CA VAL A 30 1827 1817 1904 267 -102 19 C ATOM 260 C VAL A 30 28.194 32.414 34.741 1.00 15.53 C ANISOU 260 C VAL A 30 1960 1938 2004 252 -58 39 C ATOM 261 O VAL A 30 28.018 31.419 35.453 1.00 15.14 O ANISOU 261 O VAL A 30 1949 1872 1930 244 -23 46 O ATOM 262 CB VAL A 30 29.571 34.387 35.417 1.00 16.55 C ANISOU 262 CB VAL A 30 2062 2042 2185 283 -142 33 C ATOM 263 CG1 VAL A 30 29.569 35.803 35.997 1.00 17.35 C ANISOU 263 CG1 VAL A 30 2122 2126 2343 287 -157 -18 C ATOM 264 CG2 VAL A 30 30.499 33.470 36.247 1.00 17.02 C ANISOU 264 CG2 VAL A 30 2149 2116 2201 297 -156 49 C ATOM 265 N ALA A 31 28.504 32.348 33.445 1.00 13.98 N ANISOU 265 N ALA A 31 1719 1763 1831 236 -52 47 N ATOM 266 CA ALA A 31 28.857 31.101 32.771 1.00 14.60 C ANISOU 266 CA ALA A 31 1769 1847 1933 205 -1 25 C ATOM 267 C ALA A 31 30.390 31.133 32.630 1.00 17.05 C ANISOU 267 C ALA A 31 2068 2125 2287 211 -41 38 C ATOM 268 O ALA A 31 30.960 32.082 32.074 1.00 18.99 O ANISOU 268 O ALA A 31 2291 2395 2528 200 -79 48 O ATOM 269 CB ALA A 31 28.188 31.032 31.409 1.00 16.24 C ANISOU 269 CB ALA A 31 1898 2158 2116 159 38 -15 C ATOM 270 N LEU A 32 31.064 30.137 33.164 1.00 14.54 N ANISOU 270 N LEU A 32 1761 1743 2020 231 -33 42 N ATOM 271 CA ALEU A 32 32.507 30.106 33.104 0.50 14.28 C ANISOU 271 CA ALEU A 32 1704 1685 2039 246 -78 30 C ATOM 272 CA BLEU A 32 32.534 30.038 33.127 0.50 15.29 C ANISOU 272 CA BLEU A 32 1830 1808 2170 248 -77 30 C ATOM 273 C LEU A 32 32.924 28.983 32.132 1.00 16.24 C ANISOU 273 C LEU A 32 1869 1915 2387 201 -23 -42 C ATOM 274 O LEU A 32 32.531 27.835 32.304 1.00 15.96 O ANISOU 274 O LEU A 32 1821 1815 2428 204 38 -46 O ATOM 275 CB ALEU A 32 33.000 29.898 34.554 0.50 15.90 C ANISOU 275 CB ALEU A 32 1959 1850 2231 318 -128 93 C ATOM 276 CB BLEU A 32 33.085 29.573 34.495 0.50 17.48 C ANISOU 276 CB BLEU A 32 2153 2034 2455 319 -121 94 C ATOM 277 CG ALEU A 32 34.490 29.785 34.806 0.50 18.96 C ANISOU 277 CG ALEU A 32 2315 2223 2665 361 -190 79 C ATOM 278 CG BLEU A 32 33.318 30.586 35.596 0.50 21.48 C ANISOU 278 CG BLEU A 32 2695 2593 2875 356 -184 119 C ATOM 279 CD1ALEU A 32 35.207 31.095 34.494 0.50 18.60 C ANISOU 279 CD1ALEU A 32 2248 2232 2586 340 -225 12 C ATOM 280 CD1BLEU A 32 34.158 29.968 36.676 0.50 21.33 C ANISOU 280 CD1BLEU A 32 2681 2574 2849 423 -238 180 C ATOM 281 CD2ALEU A 32 34.751 29.378 36.242 0.50 21.51 C ANISOU 281 CD2ALEU A 32 2674 2550 2949 436 -240 172 C ATOM 282 CD2BLEU A 32 34.032 31.827 35.093 0.50 20.85 C ANISOU 282 CD2BLEU A 32 2581 2546 2795 337 -212 52 C ATOM 283 N LYS A 33 33.707 29.326 31.113 1.00 14.37 N ANISOU 283 N LYS A 33 1562 1733 2163 144 -32 -114 N ATOM 284 CA LYS A 33 34.121 28.371 30.109 1.00 15.54 C ANISOU 284 CA LYS A 33 1597 1898 2409 72 28 -230 C ATOM 285 C LYS A 33 35.610 28.113 30.173 1.00 19.76 C ANISOU 285 C LYS A 33 2086 2378 3044 85 -15 -294 C ATOM 286 O LYS A 33 36.408 29.059 30.076 1.00 20.55 O ANISOU 286 O LYS A 33 2200 2522 3088 75 -71 -307 O ATOM 287 CB LYS A 33 33.715 28.844 28.697 1.00 16.82 C ANISOU 287 CB LYS A 33 1678 2226 2485 -41 67 -290 C ATOM 288 CG LYS A 33 32.230 29.157 28.566 1.00 18.83 C ANISOU 288 CG LYS A 33 1958 2559 2639 -41 95 -234 C ATOM 289 CD LYS A 33 31.714 29.061 27.128 1.00 19.20 C ANISOU 289 CD LYS A 33 1876 2806 2614 -153 154 -313 C ATOM 290 CE LYS A 33 30.213 29.230 27.117 1.00 19.94 C ANISOU 290 CE LYS A 33 1980 2977 2620 -131 178 -275 C ATOM 291 NZ LYS A 33 29.684 28.873 25.755 1.00 24.30 N1+ ANISOU 291 NZ LYS A 33 2372 3766 3095 -242 248 -381 N1+ ATOM 292 N LYS A 34 36.004 26.853 30.377 1.00 19.70 N ANISOU 292 N LYS A 34 2018 2261 3204 113 14 -339 N ATOM 293 CA LYS A 34 37.421 26.471 30.356 1.00 22.96 C ANISOU 293 CA LYS A 34 2356 2619 3750 132 -30 -428 C ATOM 294 C LYS A 34 37.801 26.240 28.876 1.00 28.18 C ANISOU 294 C LYS A 34 2863 3374 4469 -17 38 -629 C ATOM 295 O LYS A 34 37.037 25.604 28.131 1.00 27.52 O ANISOU 295 O LYS A 34 2693 3334 4428 -101 139 -707 O ATOM 296 CB LYS A 34 37.639 25.165 31.130 1.00 28.93 C ANISOU 296 CB LYS A 34 3089 3199 4703 229 -25 -378 C ATOM 297 CG LYS A 34 37.584 25.315 32.641 0.50 44.37 C ANISOU 297 CG LYS A 34 5171 5101 6587 366 -109 -178 C ATOM 298 CD LYS A 34 38.242 24.121 33.322 0.50 56.38 C ANISOU 298 CD LYS A 34 6649 6462 8312 473 -138 -106 C ATOM 299 CE LYS A 34 37.995 24.106 34.809 0.50 67.69 C ANISOU 299 CE LYS A 34 8198 7878 9645 590 -209 125 C ATOM 300 NZ LYS A 34 38.662 22.951 35.465 0.50 77.96 N1+ ANISOU 300 NZ LYS A 34 9453 9025 11143 709 -251 245 N1+ ATOM 301 N ILE A 35 38.956 26.761 28.432 1.00 25.54 N ANISOU 301 N ILE A 35 2479 3099 4125 -67 -6 -738 N ATOM 302 CA ILE A 35 39.383 26.585 27.031 1.00 26.84 C ANISOU 302 CA ILE A 35 2486 3393 4320 -237 59 -945 C ATOM 303 C ILE A 35 40.549 25.627 26.983 1.00 35.21 C ANISOU 303 C ILE A 35 3407 4353 5619 -235 57 -1126 C ATOM 304 O ILE A 35 41.559 25.877 27.634 1.00 36.99 O ANISOU 304 O ILE A 35 3665 4511 5880 -148 -32 -1125 O ATOM 305 CB ILE A 35 39.713 27.924 26.300 1.00 29.75 C ANISOU 305 CB ILE A 35 2883 3932 4488 -346 37 -952 C ATOM 306 CG1 ILE A 35 38.552 28.953 26.402 1.00 29.40 C ANISOU 306 CG1 ILE A 35 2969 3954 4247 -324 27 -750 C ATOM 307 CG2 ILE A 35 40.176 27.685 24.831 1.00 32.11 C ANISOU 307 CG2 ILE A 35 3003 4409 4787 -553 108 -1169 C ATOM 308 CD1 ILE A 35 37.234 28.549 25.666 1.00 28.89 C ANISOU 308 CD1 ILE A 35 2846 4010 4122 -391 104 -736 C ATOM 309 N ARG A 36 40.312 24.428 26.444 1.00 33.93 N ANISOU 309 N ARG A 36 3088 4150 5654 -296 155 -1268 N ATOM 310 N PRO A 45 48.308 30.281 23.488 1.00 49.77 N ANISOU 310 N PRO A 45 4967 6855 7087 -1035 16 -2272 N ATOM 311 CA PRO A 45 48.901 31.050 22.383 1.00 49.55 C ANISOU 311 CA PRO A 45 4903 7009 6916 -1288 93 -2410 C ATOM 312 C PRO A 45 48.539 32.528 22.460 1.00 49.21 C ANISOU 312 C PRO A 45 5047 6980 6670 -1303 118 -2168 C ATOM 313 O PRO A 45 47.382 32.879 22.712 1.00 47.75 O ANISOU 313 O PRO A 45 4979 6759 6403 -1213 107 -1881 O ATOM 314 CB PRO A 45 48.337 30.375 21.131 1.00 52.19 C ANISOU 314 CB PRO A 45 5087 7526 7215 -1487 165 -2484 C ATOM 315 CG PRO A 45 48.007 28.993 21.564 1.00 57.19 C ANISOU 315 CG PRO A 45 5610 8034 8085 -1352 136 -2549 C ATOM 316 CD PRO A 45 47.574 29.099 23.000 1.00 51.69 C ANISOU 316 CD PRO A 45 5085 7116 7438 -1064 47 -2298 C ATOM 317 N SER A 46 49.544 33.388 22.246 1.00 43.68 N ANISOU 317 N SER A 46 4365 6320 5913 -1421 161 -2302 N ATOM 318 CA SER A 46 49.446 34.846 22.307 1.00 41.57 C ANISOU 318 CA SER A 46 4254 6030 5511 -1453 212 -2119 C ATOM 319 C SER A 46 48.466 35.453 21.309 1.00 42.02 C ANISOU 319 C SER A 46 4368 6209 5387 -1593 267 -1856 C ATOM 320 O SER A 46 47.768 36.408 21.662 1.00 39.85 O ANISOU 320 O SER A 46 4236 5844 5061 -1509 273 -1582 O ATOM 321 CB SER A 46 50.825 35.474 22.158 1.00 46.40 C ANISOU 321 CB SER A 46 4839 6667 6123 -1585 273 -2375 C ATOM 322 OG SER A 46 51.674 35.040 23.208 1.00 58.24 O ANISOU 322 OG SER A 46 6288 8064 7776 -1419 206 -2590 O ATOM 323 N THR A 47 48.380 34.877 20.078 1.00 36.86 N ANISOU 323 N THR A 47 3583 5776 4647 -1803 305 -1944 N ATOM 324 CA THR A 47 47.465 35.357 19.042 1.00 37.48 C ANISOU 324 CA THR A 47 3682 6038 4521 -1945 345 -1694 C ATOM 325 C THR A 47 46.020 35.227 19.513 1.00 37.49 C ANISOU 325 C THR A 47 3758 5966 4519 -1748 286 -1405 C ATOM 326 O THR A 47 45.231 36.144 19.296 1.00 37.26 O ANISOU 326 O THR A 47 3836 5949 4372 -1738 292 -1101 O ATOM 327 CB THR A 47 47.731 34.667 17.699 1.00 50.08 C ANISOU 327 CB THR A 47 5079 7936 6012 -2221 399 -1901 C ATOM 328 CG2 THR A 47 49.014 35.157 17.032 1.00 49.31 C ANISOU 328 CG2 THR A 47 4934 7954 5848 -2471 478 -2124 C ATOM 329 OG1 THR A 47 47.783 33.252 17.894 1.00 56.67 O ANISOU 329 OG1 THR A 47 5750 8762 7021 -2166 371 -2156 O ATOM 330 N ALA A 48 45.687 34.114 20.202 1.00 33.49 N ANISOU 330 N ALA A 48 3198 5365 4160 -1587 232 -1495 N ATOM 331 CA ALA A 48 44.347 33.897 20.751 1.00 32.12 C ANISOU 331 CA ALA A 48 3093 5114 3997 -1404 185 -1263 C ATOM 332 C ALA A 48 44.036 34.898 21.859 1.00 30.48 C ANISOU 332 C ALA A 48 3070 4690 3819 -1213 146 -1047 C ATOM 333 O ALA A 48 42.931 35.426 21.886 1.00 28.03 O ANISOU 333 O ALA A 48 2840 4370 3438 -1146 132 -790 O ATOM 334 CB ALA A 48 44.196 32.479 21.271 1.00 32.82 C ANISOU 334 CB ALA A 48 3084 5128 4258 -1293 156 -1419 C ATOM 335 N ILE A 49 45.000 35.187 22.753 1.00 27.64 N ANISOU 335 N ILE A 49 2755 4179 3568 -1132 133 -1170 N ATOM 336 CA ILE A 49 44.774 36.158 23.839 1.00 26.57 C ANISOU 336 CA ILE A 49 2758 3867 3472 -973 115 -1019 C ATOM 337 C ILE A 49 44.378 37.528 23.291 1.00 27.81 C ANISOU 337 C ILE A 49 3003 4027 3538 -1055 172 -797 C ATOM 338 O ILE A 49 43.404 38.112 23.783 1.00 25.11 O ANISOU 338 O ILE A 49 2745 3584 3210 -934 153 -577 O ATOM 339 CB ILE A 49 45.996 36.249 24.802 1.00 29.38 C ANISOU 339 CB ILE A 49 3107 4120 3936 -900 104 -1235 C ATOM 340 CG1 ILE A 49 46.425 34.860 25.352 1.00 31.58 C ANISOU 340 CG1 ILE A 49 3289 4384 4328 -799 31 -1418 C ATOM 341 CG2 ILE A 49 45.804 37.308 25.915 1.00 30.14 C ANISOU 341 CG2 ILE A 49 3308 4073 4070 -765 108 -1127 C ATOM 342 CD1 ILE A 49 45.436 34.127 26.332 1.00 41.75 C ANISOU 342 CD1 ILE A 49 4613 5580 5670 -596 -42 -1268 C ATOM 343 N ARG A 50 45.105 38.017 22.265 1.00 28.45 N ANISOU 343 N ARG A 50 3055 4218 3536 -1263 243 -850 N ATOM 344 CA AARG A 50 44.833 39.314 21.649 0.50 29.89 C ANISOU 344 CA AARG A 50 3318 4394 3645 -1356 306 -610 C ATOM 345 CA BARG A 50 44.836 39.315 21.635 0.50 30.17 C ANISOU 345 CA BARG A 50 3353 4431 3678 -1358 306 -610 C ATOM 346 C ARG A 50 43.444 39.329 20.996 1.00 33.87 C ANISOU 346 C ARG A 50 3829 5004 4036 -1343 268 -313 C ATOM 347 O ARG A 50 42.669 40.261 21.242 1.00 33.67 O ANISOU 347 O ARG A 50 3892 4855 4045 -1249 265 -52 O ATOM 348 CB AARG A 50 45.942 39.696 20.653 0.50 30.80 C ANISOU 348 CB AARG A 50 3394 4633 3674 -1607 395 -735 C ATOM 349 CB BARG A 50 45.930 39.667 20.605 0.50 32.38 C ANISOU 349 CB BARG A 50 3591 4844 3868 -1613 395 -734 C ATOM 350 CG AARG A 50 47.335 39.689 21.287 0.50 30.90 C ANISOU 350 CG AARG A 50 3384 4557 3799 -1618 435 -1066 C ATOM 351 CG BARG A 50 45.655 40.912 19.746 0.50 41.25 C ANISOU 351 CG BARG A 50 4789 5991 4894 -1744 466 -440 C ATOM 352 CD AARG A 50 48.428 40.245 20.400 0.50 31.21 C ANISOU 352 CD AARG A 50 3402 4692 3766 -1873 543 -1201 C ATOM 353 CD BARG A 50 46.055 42.222 20.406 0.50 41.53 C ANISOU 353 CD BARG A 50 4933 5770 5076 -1694 549 -379 C ATOM 354 NE AARG A 50 49.748 40.084 21.018 0.50 32.77 N ANISOU 354 NE AARG A 50 3549 4830 4070 -1873 571 -1569 N ATOM 355 NE BARG A 50 45.735 43.368 19.551 0.50 39.93 N ANISOU 355 NE BARG A 50 4799 5560 4815 -1810 619 -55 N ATOM 356 CZ AARG A 50 50.690 39.253 20.577 0.50 45.86 C ANISOU 356 CZ AARG A 50 5078 6633 5713 -2005 570 -1896 C ATOM 357 CZ BARG A 50 45.171 44.495 19.975 0.50 50.37 C ANISOU 357 CZ BARG A 50 6212 6648 6280 -1699 655 200 C ATOM 358 NH1AARG A 50 50.467 38.488 19.514 0.50 40.03 N1+ ANISOU 358 NH1AARG A 50 4235 6111 4862 -2164 555 -1921 N1+ ATOM 359 NH1BARG A 50 44.855 44.648 21.256 0.50 34.32 N1+ ANISOU 359 NH1BARG A 50 4204 4397 4441 -1485 633 136 N1+ ATOM 360 NH2AARG A 50 51.865 39.184 21.192 0.50 30.37 N ANISOU 360 NH2AARG A 50 3066 4615 3857 -1983 586 -2224 N ATOM 361 NH2BARG A 50 44.916 45.477 19.123 0.50 35.79 N ANISOU 361 NH2BARG A 50 4418 4788 4394 -1805 716 521 N ATOM 362 N GLU A 51 43.119 38.271 20.209 1.00 28.75 N ANISOU 362 N GLU A 51 2572 3409 4944 -252 -190 790 N ATOM 363 CA AGLU A 51 41.831 38.147 19.517 0.50 27.42 C ANISOU 363 CA AGLU A 51 2552 3279 4586 -185 -104 707 C ATOM 364 CA BGLU A 51 41.832 38.118 19.520 0.50 27.43 C ANISOU 364 CA BGLU A 51 2554 3282 4587 -183 -104 706 C ATOM 365 C GLU A 51 40.664 38.093 20.511 1.00 27.95 C ANISOU 365 C GLU A 51 2754 3349 4517 -228 -221 551 C ATOM 366 O GLU A 51 39.648 38.779 20.313 1.00 26.63 O ANISOU 366 O GLU A 51 2678 3169 4270 -232 -215 488 O ATOM 367 CB AGLU A 51 41.820 36.918 18.584 0.50 28.97 C ANISOU 367 CB AGLU A 51 2782 3542 4683 -61 36 736 C ATOM 368 CB BGLU A 51 41.830 36.821 18.697 0.50 28.97 C ANISOU 368 CB BGLU A 51 2782 3544 4680 -64 25 729 C ATOM 369 CG AGLU A 51 42.691 37.056 17.341 0.50 41.57 C ANISOU 369 CG AGLU A 51 4290 5139 6366 22 199 890 C ATOM 370 CG BGLU A 51 42.563 36.910 17.372 0.50 42.32 C ANISOU 370 CG BGLU A 51 4403 5240 6435 28 195 872 C ATOM 371 CD AGLU A 51 42.084 37.712 16.113 0.50 56.99 C ANISOU 371 CD AGLU A 51 6317 7090 8248 91 320 911 C ATOM 372 CD BGLU A 51 42.358 35.689 16.502 0.50 61.84 C ANISOU 372 CD BGLU A 51 6962 7768 8767 162 316 870 C ATOM 373 OE1AGLU A 51 41.156 38.540 16.260 0.50 38.39 O ANISOU 373 OE1AGLU A 51 4036 4712 5840 41 262 831 O ATOM 374 OE1BGLU A 51 41.196 35.424 16.121 0.50 59.08 O ANISOU 374 OE1BGLU A 51 6759 7439 8248 204 323 768 O ATOM 375 OE2AGLU A 51 42.570 37.423 14.996 0.50 56.27 O1- ANISOU 375 OE2AGLU A 51 6211 7017 8153 205 478 1017 O1- ATOM 376 OE2BGLU A 51 43.354 34.988 16.211 0.50 55.84 O1- ANISOU 376 OE2BGLU A 51 6123 7024 8069 229 397 972 O1- ATOM 377 N ILE A 52 40.809 37.293 21.589 1.00 25.24 N ANISOU 377 N ILE A 52 2422 3020 4150 -253 -320 498 N ATOM 378 CA ILE A 52 39.768 37.156 22.613 1.00 25.77 C ANISOU 378 CA ILE A 52 2614 3088 4090 -280 -415 367 C ATOM 379 C ILE A 52 39.584 38.458 23.366 1.00 28.69 C ANISOU 379 C ILE A 52 3013 3386 4501 -360 -530 326 C ATOM 380 O ILE A 52 38.458 38.857 23.645 1.00 27.14 O ANISOU 380 O ILE A 52 2931 3183 4197 -360 -545 239 O ATOM 381 CB ILE A 52 40.036 35.933 23.551 1.00 30.59 C ANISOU 381 CB ILE A 52 3234 3728 4661 -272 -479 335 C ATOM 382 CG1 ILE A 52 40.117 34.610 22.768 1.00 32.43 C ANISOU 382 CG1 ILE A 52 3460 4022 4840 -184 -363 367 C ATOM 383 CG2 ILE A 52 39.006 35.828 24.662 1.00 32.47 C ANISOU 383 CG2 ILE A 52 3600 3962 4774 -290 -564 218 C ATOM 384 CD1 ILE A 52 38.897 34.264 21.954 1.00 41.08 C ANISOU 384 CD1 ILE A 52 4662 5150 5798 -124 -271 311 C ATOM 385 N SER A 53 40.695 39.150 23.662 1.00 29.26 N ANISOU 385 N SER A 53 2980 3397 4740 -427 -612 394 N ATOM 386 CA SER A 53 40.661 40.448 24.332 1.00 30.24 C ANISOU 386 CA SER A 53 3134 3433 4923 -507 -738 359 C ATOM 387 C SER A 53 39.860 41.476 23.539 1.00 34.29 C ANISOU 387 C SER A 53 3698 3923 5406 -498 -658 351 C ATOM 388 O SER A 53 39.066 42.208 24.136 1.00 36.46 O ANISOU 388 O SER A 53 4087 4155 5610 -521 -726 265 O ATOM 389 CB SER A 53 42.071 40.930 24.627 1.00 36.78 C ANISOU 389 CB SER A 53 3818 4192 5965 -583 -843 451 C ATOM 390 OG SER A 53 42.675 40.027 25.538 1.00 43.23 O ANISOU 390 OG SER A 53 4610 5025 6789 -590 -945 439 O ATOM 391 N LEU A 54 39.985 41.470 22.191 1.00 30.82 N ANISOU 391 N LEU A 54 3194 3516 4999 -446 -504 440 N ATOM 392 CA LEU A 54 39.227 42.344 21.293 1.00 30.71 C ANISOU 392 CA LEU A 54 3230 3491 4947 -420 -412 443 C ATOM 393 C LEU A 54 37.702 42.084 21.421 1.00 28.75 C ANISOU 393 C LEU A 54 3134 3287 4502 -373 -394 324 C ATOM 394 O LEU A 54 36.893 42.993 21.257 1.00 26.59 O ANISOU 394 O LEU A 54 2932 2984 4186 -375 -385 287 O ATOM 395 CB LEU A 54 39.668 42.149 19.828 1.00 32.40 C ANISOU 395 CB LEU A 54 3365 3742 5204 -347 -243 562 C ATOM 396 CG LEU A 54 41.041 42.707 19.445 1.00 40.94 C ANISOU 396 CG LEU A 54 4283 4770 6504 -383 -219 712 C ATOM 397 CD1 LEU A 54 41.710 41.836 18.401 1.00 42.79 C ANISOU 397 CD1 LEU A 54 4438 5064 6758 -288 -61 826 C ATOM 398 CD2 LEU A 54 40.935 44.131 18.936 1.00 45.64 C ANISOU 398 CD2 LEU A 54 4868 5292 7180 -415 -192 759 C ATOM 399 N LEU A 55 37.308 40.841 21.733 1.00 23.60 N ANISOU 399 N LEU A 55 2526 2700 3741 -332 -388 270 N ATOM 400 CA LEU A 55 35.894 40.502 21.889 1.00 21.22 C ANISOU 400 CA LEU A 55 2345 2437 3282 -292 -372 174 C ATOM 401 C LEU A 55 35.233 41.144 23.118 1.00 23.08 C ANISOU 401 C LEU A 55 2674 2625 3469 -333 -475 87 C ATOM 402 O LEU A 55 34.017 41.316 23.116 1.00 20.85 O ANISOU 402 O LEU A 55 2478 2356 3086 -302 -447 30 O ATOM 403 CB LEU A 55 35.681 38.968 21.862 1.00 20.70 C ANISOU 403 CB LEU A 55 2293 2440 3132 -240 -337 152 C ATOM 404 CG LEU A 55 36.141 38.266 20.585 1.00 25.27 C ANISOU 404 CG LEU A 55 2820 3061 3719 -174 -225 224 C ATOM 405 CD1 LEU A 55 36.225 36.769 20.808 1.00 25.24 C ANISOU 405 CD1 LEU A 55 2826 3105 3661 -137 -220 205 C ATOM 406 CD2 LEU A 55 35.237 38.592 19.394 1.00 27.56 C ANISOU 406 CD2 LEU A 55 3167 3368 3936 -115 -137 220 C ATOM 407 N LYS A 56 36.010 41.539 24.141 1.00 20.90 N ANISOU 407 N LYS A 56 2386 2290 3266 -395 -597 81 N ATOM 408 CA ALYS A 56 35.460 42.184 25.340 0.50 21.36 C ANISOU 408 CA ALYS A 56 2559 2292 3264 -418 -701 -3 C ATOM 409 CA BLYS A 56 35.488 42.197 25.352 0.50 21.08 C ANISOU 409 CA BLYS A 56 2523 2255 3231 -420 -704 -2 C ATOM 410 C LYS A 56 34.826 43.539 25.024 1.00 23.53 C ANISOU 410 C LYS A 56 2891 2511 3539 -425 -686 -18 C ATOM 411 O LYS A 56 34.014 44.030 25.805 1.00 25.15 O ANISOU 411 O LYS A 56 3217 2683 3657 -412 -727 -91 O ATOM 412 CB ALYS A 56 36.524 42.339 26.430 0.50 25.14 C ANISOU 412 CB ALYS A 56 3024 2706 3821 -479 -857 -7 C ATOM 413 CB BLYS A 56 36.598 42.438 26.391 0.50 24.24 C ANISOU 413 CB BLYS A 56 2903 2586 3721 -485 -861 -2 C ATOM 414 CG ALYS A 56 36.307 41.411 27.627 0.50 34.63 C ANISOU 414 CG ALYS A 56 4308 3933 4916 -453 -922 -72 C ATOM 415 CG BLYS A 56 37.234 41.169 26.971 0.50 25.30 C ANISOU 415 CG BLYS A 56 2998 2765 3849 -477 -903 5 C ATOM 416 CD ALYS A 56 37.446 41.509 28.662 0.50 44.83 C ANISOU 416 CD ALYS A 56 5586 5161 6285 -508 -1096 -73 C ATOM 417 CD BLYS A 56 38.201 41.491 28.120 0.50 27.62 C ANISOU 417 CD BLYS A 56 3295 2982 4216 -537 -1087 -8 C ATOM 418 CE ALYS A 56 37.456 42.778 29.491 0.50 53.27 C ANISOU 418 CE ALYS A 56 6761 6118 7363 -549 -1238 -129 C ATOM 419 CE BLYS A 56 39.572 41.920 27.660 0.50 26.36 C ANISOU 419 CE BLYS A 56 2975 2776 4266 -606 -1140 91 C ATOM 420 NZ ALYS A 56 36.345 42.823 30.475 0.50 60.84 N1+ ANISOU 420 NZ ALYS A 56 7909 7068 8138 -487 -1252 -228 N1+ ATOM 421 NZ BLYS A 56 40.435 42.311 28.809 0.50 29.92 N1+ ANISOU 421 NZ BLYS A 56 3435 3137 4796 -672 -1351 71 N1+ ATOM 422 N GLU A 57 35.211 44.143 23.896 1.00 18.80 N ANISOU 422 N GLU A 57 2210 1898 3034 -435 -618 58 N ATOM 423 CA AGLU A 57 34.666 45.432 23.497 0.70 19.34 C ANISOU 423 CA AGLU A 57 2325 1912 3111 -439 -595 55 C ATOM 424 CA BGLU A 57 34.720 45.440 23.428 0.30 18.52 C ANISOU 424 CA BGLU A 57 2214 1808 3015 -439 -591 61 C ATOM 425 C GLU A 57 33.551 45.305 22.464 1.00 19.99 C ANISOU 425 C GLU A 57 2436 2059 3099 -365 -463 55 C ATOM 426 O GLU A 57 32.904 46.307 22.160 1.00 21.33 O ANISOU 426 O GLU A 57 2658 2193 3253 -353 -437 46 O ATOM 427 CB AGLU A 57 35.784 46.355 22.994 0.70 22.24 C ANISOU 427 CB AGLU A 57 2591 2203 3656 -500 -616 145 C ATOM 428 CB BGLU A 57 35.843 46.190 22.696 0.30 20.75 C ANISOU 428 CB BGLU A 57 2379 2033 3473 -489 -583 166 C ATOM 429 CG AGLU A 57 36.776 46.776 24.072 0.70 33.79 C ANISOU 429 CG AGLU A 57 4036 3572 5232 -586 -784 138 C ATOM 430 CG BGLU A 57 37.037 46.549 23.564 0.30 28.51 C ANISOU 430 CG BGLU A 57 3307 2929 4598 -578 -733 185 C ATOM 431 CD AGLU A 57 36.170 47.386 25.323 0.70 62.45 C ANISOU 431 CD AGLU A 57 7824 7130 8774 -599 -910 26 C ATOM 432 CD BGLU A 57 38.011 47.535 22.949 0.30 49.54 C ANISOU 432 CD BGLU A 57 5855 5509 7459 -639 -736 292 C ATOM 433 OE1AGLU A 57 35.727 48.556 25.261 0.70 65.88 O ANISOU 433 OE1AGLU A 57 8329 7489 9214 -608 -921 6 O ATOM 434 OE1BGLU A 57 38.473 47.298 21.809 0.30 38.85 O ANISOU 434 OE1BGLU A 57 4388 4198 6177 -610 -606 401 O ATOM 435 OE2AGLU A 57 36.110 46.682 26.358 0.70 59.39 O1- ANISOU 435 OE2AGLU A 57 7501 6760 8304 -588 -990 -39 O1- ATOM 436 OE2BGLU A 57 38.336 48.536 23.626 0.30 47.84 O1- ANISOU 436 OE2BGLU A 57 5667 5180 7332 -713 -870 272 O1- ATOM 437 N LEU A 58 33.299 44.081 21.942 1.00 16.73 N ANISOU 437 N LEU A 58 1997 1736 2622 -313 -390 62 N ATOM 438 CA LEU A 58 32.276 43.812 20.929 1.00 17.45 C ANISOU 438 CA LEU A 58 2117 1887 2627 -242 -289 59 C ATOM 439 C LEU A 58 30.920 43.579 21.632 1.00 15.49 C ANISOU 439 C LEU A 58 1962 1660 2263 -215 -305 -24 C ATOM 440 O LEU A 58 30.411 42.481 21.720 1.00 16.05 O ANISOU 440 O LEU A 58 2042 1788 2270 -184 -289 -51 O ATOM 441 CB LEU A 58 32.744 42.603 20.076 1.00 18.80 C ANISOU 441 CB LEU A 58 2226 2124 2793 -200 -222 106 C ATOM 442 CG LEU A 58 31.961 42.288 18.800 1.00 22.06 C ANISOU 442 CG LEU A 58 2667 2587 3129 -123 -131 115 C ATOM 443 CD1 LEU A 58 32.190 43.341 17.725 1.00 22.63 C ANISOU 443 CD1 LEU A 58 2722 2630 3246 -100 -63 185 C ATOM 444 CD2 LEU A 58 32.349 40.925 18.308 1.00 23.87 C ANISOU 444 CD2 LEU A 58 2870 2870 3329 -79 -94 134 C ATOM 445 N ASN A 59 30.379 44.671 22.174 1.00 14.27 N ANISOU 445 N ASN A 59 1877 1450 2096 -224 -336 -58 N ATOM 446 CA ASN A 59 29.197 44.640 23.016 1.00 12.49 C ANISOU 446 CA ASN A 59 1741 1229 1776 -193 -345 -123 C ATOM 447 C ASN A 59 27.953 45.028 22.302 1.00 11.76 C ANISOU 447 C ASN A 59 1674 1159 1634 -139 -275 -124 C ATOM 448 O ASN A 59 27.888 46.066 21.643 1.00 13.25 O ANISOU 448 O ASN A 59 1868 1314 1853 -134 -249 -98 O ATOM 449 CB ASN A 59 29.418 45.542 24.240 1.00 13.01 C ANISOU 449 CB ASN A 59 1889 1209 1844 -222 -431 -164 C ATOM 450 CG ASN A 59 30.534 45.098 25.126 1.00 14.64 C ANISOU 450 CG ASN A 59 2082 1390 2089 -272 -528 -174 C ATOM 451 ND2 ASN A 59 31.326 46.045 25.589 1.00 16.35 N ANISOU 451 ND2 ASN A 59 2321 1516 2376 -324 -621 -177 N ATOM 452 OD1 ASN A 59 30.724 43.901 25.363 1.00 15.61 O ANISOU 452 OD1 ASN A 59 2173 1569 2189 -264 -527 -175 O ATOM 453 N HIS A 60 26.921 44.209 22.450 1.00 10.92 N ANISOU 453 N HIS A 60 1581 1106 1461 -97 -246 -148 N ATOM 454 CA HIS A 60 25.615 44.498 21.830 1.00 11.49 C ANISOU 454 CA HIS A 60 1667 1202 1497 -44 -192 -145 C ATOM 455 C HIS A 60 24.559 43.738 22.599 1.00 11.10 C ANISOU 455 C HIS A 60 1637 1184 1398 -13 -180 -171 C ATOM 456 O HIS A 60 24.843 42.662 23.119 1.00 11.42 O ANISOU 456 O HIS A 60 1660 1249 1430 -27 -199 -181 O ATOM 457 CB HIS A 60 25.656 44.039 20.350 1.00 11.38 C ANISOU 457 CB HIS A 60 1596 1235 1494 -24 -156 -109 C ATOM 458 CG HIS A 60 24.404 44.333 19.581 1.00 11.50 C ANISOU 458 CG HIS A 60 1620 1271 1480 30 -122 -103 C ATOM 459 CD2 HIS A 60 24.087 45.407 18.825 1.00 12.78 C ANISOU 459 CD2 HIS A 60 1799 1412 1644 58 -94 -80 C ATOM 460 ND1 HIS A 60 23.324 43.469 19.609 1.00 11.22 N ANISOU 460 ND1 HIS A 60 1569 1277 1417 57 -123 -118 N ATOM 461 CE1 HIS A 60 22.386 44.039 18.879 1.00 12.08 C ANISOU 461 CE1 HIS A 60 1682 1390 1516 100 -105 -104 C ATOM 462 NE2 HIS A 60 22.797 45.201 18.370 1.00 12.75 N ANISOU 462 NE2 HIS A 60 1791 1442 1610 107 -84 -82 N ATOM 463 N PRO A 61 23.296 44.221 22.653 1.00 11.97 N ANISOU 463 N PRO A 61 1773 1293 1482 35 -142 -170 N ATOM 464 CA PRO A 61 22.273 43.507 23.438 1.00 11.69 C ANISOU 464 CA PRO A 61 1742 1283 1419 69 -116 -174 C ATOM 465 C PRO A 61 21.943 42.104 22.948 1.00 12.27 C ANISOU 465 C PRO A 61 1739 1412 1510 63 -117 -162 C ATOM 466 O PRO A 61 21.411 41.312 23.736 1.00 13.43 O ANISOU 466 O PRO A 61 1880 1572 1650 76 -102 -158 O ATOM 467 CB PRO A 61 21.021 44.384 23.325 1.00 15.00 C ANISOU 467 CB PRO A 61 2180 1691 1829 126 -67 -157 C ATOM 468 CG PRO A 61 21.512 45.698 22.883 1.00 19.34 C ANISOU 468 CG PRO A 61 2771 2193 2383 119 -75 -161 C ATOM 469 CD PRO A 61 22.824 45.549 22.208 1.00 12.85 C ANISOU 469 CD PRO A 61 1917 1370 1596 63 -116 -159 C ATOM 470 N ASN A 62 22.274 41.771 21.700 1.00 10.43 N ANISOU 470 N ASN A 62 1462 1204 1299 51 -134 -152 N ATOM 471 CA ASN A 62 21.994 40.438 21.164 1.00 10.18 C ANISOU 471 CA ASN A 62 1378 1211 1280 48 -152 -149 C ATOM 472 C ASN A 62 23.248 39.589 21.085 1.00 11.00 C ANISOU 472 C ASN A 62 1473 1324 1384 16 -177 -158 C ATOM 473 O ASN A 62 23.240 38.586 20.373 1.00 11.49 O ANISOU 473 O ASN A 62 1509 1408 1449 20 -196 -158 O ATOM 474 CB ASN A 62 21.239 40.517 19.846 1.00 11.33 C ANISOU 474 CB ASN A 62 1498 1373 1435 78 -162 -136 C ATOM 475 CG ASN A 62 19.914 41.173 20.030 1.00 11.93 C ANISOU 475 CG ASN A 62 1564 1443 1525 112 -140 -118 C ATOM 476 ND2 ASN A 62 19.011 40.513 20.754 1.00 10.83 N ANISOU 476 ND2 ASN A 62 1388 1310 1416 117 -130 -104 N ATOM 477 OD1 ASN A 62 19.694 42.288 19.553 1.00 13.00 O ANISOU 477 OD1 ASN A 62 1720 1565 1652 138 -123 -108 O ATOM 478 N ILE A 63 24.325 39.979 21.799 1.00 9.66 N ANISOU 478 N ILE A 63 1327 1130 1213 -12 -186 -164 N ATOM 479 CA AILE A 63 25.563 39.218 21.873 0.70 9.84 C ANISOU 479 CA AILE A 63 1330 1160 1248 -41 -209 -161 C ATOM 480 CA BILE A 63 25.567 39.208 21.875 0.30 8.91 C ANISOU 480 CA BILE A 63 1213 1044 1131 -41 -209 -162 C ATOM 481 C ILE A 63 25.764 38.892 23.337 1.00 10.67 C ANISOU 481 C ILE A 63 1463 1253 1339 -58 -230 -179 C ATOM 482 O ILE A 63 25.773 39.809 24.162 1.00 10.55 O ANISOU 482 O ILE A 63 1498 1201 1310 -60 -241 -193 O ATOM 483 CB AILE A 63 26.743 40.016 21.280 0.70 10.88 C ANISOU 483 CB AILE A 63 1450 1271 1412 -58 -210 -137 C ATOM 484 CB BILE A 63 26.802 39.951 21.299 0.30 10.89 C ANISOU 484 CB BILE A 63 1449 1273 1414 -60 -211 -137 C ATOM 485 CG1AILE A 63 26.460 40.422 19.799 0.70 11.29 C ANISOU 485 CG1AILE A 63 1494 1334 1461 -22 -174 -112 C ATOM 486 CG1BILE A 63 26.668 40.157 19.782 0.30 11.05 C ANISOU 486 CG1BILE A 63 1457 1309 1433 -24 -176 -110 C ATOM 487 CG2AILE A 63 28.088 39.291 21.436 0.70 13.27 C ANISOU 487 CG2AILE A 63 1718 1580 1746 -85 -230 -120 C ATOM 488 CG2BILE A 63 28.121 39.218 21.648 0.30 12.53 C ANISOU 488 CG2BILE A 63 1626 1485 1651 -89 -236 -124 C ATOM 489 CD1AILE A 63 26.294 39.231 18.825 0.70 12.57 C ANISOU 489 CD1AILE A 63 1644 1534 1598 13 -169 -110 C ATOM 490 CD1BILE A 63 27.744 41.012 19.196 0.30 13.40 C ANISOU 490 CD1BILE A 63 1736 1581 1773 -32 -155 -66 C ATOM 491 N VAL A 64 25.947 37.625 23.680 1.00 10.05 N ANISOU 491 N VAL A 64 1366 1196 1257 -63 -240 -181 N ATOM 492 CA VAL A 64 26.211 37.275 25.075 1.00 10.26 C ANISOU 492 CA VAL A 64 1429 1211 1260 -69 -260 -194 C ATOM 493 C VAL A 64 27.456 38.023 25.548 1.00 11.19 C ANISOU 493 C VAL A 64 1569 1294 1389 -99 -312 -200 C ATOM 494 O VAL A 64 28.509 37.941 24.907 1.00 12.83 O ANISOU 494 O VAL A 64 1727 1506 1643 -125 -331 -180 O ATOM 495 CB VAL A 64 26.383 35.734 25.206 1.00 11.30 C ANISOU 495 CB VAL A 64 1530 1369 1394 -70 -262 -187 C ATOM 496 CG1 VAL A 64 26.718 35.349 26.652 1.00 12.67 C ANISOU 496 CG1 VAL A 64 1749 1530 1535 -67 -282 -194 C ATOM 497 CG2 VAL A 64 25.121 34.980 24.765 1.00 11.51 C ANISOU 497 CG2 VAL A 64 1530 1413 1431 -50 -229 -178 C ATOM 498 N LYS A 65 27.351 38.734 26.672 1.00 11.86 N ANISOU 498 N LYS A 65 1730 1339 1438 -92 -339 -224 N ATOM 499 CA LYS A 65 28.457 39.558 27.070 1.00 13.57 C ANISOU 499 CA LYS A 65 1970 1506 1679 -128 -414 -234 C ATOM 500 C LYS A 65 29.655 38.803 27.586 1.00 13.40 C ANISOU 500 C LYS A 65 1924 1487 1681 -157 -479 -229 C ATOM 501 O LYS A 65 29.514 37.933 28.465 1.00 14.73 O ANISOU 501 O LYS A 65 2128 1670 1799 -134 -486 -240 O ATOM 502 CB LYS A 65 28.005 40.584 28.109 1.00 15.93 C ANISOU 502 CB LYS A 65 2385 1748 1921 -103 -440 -269 C ATOM 503 CG LYS A 65 29.035 41.699 28.398 1.00 17.77 C ANISOU 503 CG LYS A 65 2652 1906 2194 -148 -538 -286 C ATOM 504 CD LYS A 65 28.487 42.681 29.388 1.00 20.10 C ANISOU 504 CD LYS A 65 3088 2135 2415 -109 -565 -330 C ATOM 505 CE LYS A 65 29.555 43.591 29.920 1.00 19.11 C ANISOU 505 CE LYS A 65 3015 1919 2326 -156 -696 -357 C ATOM 506 NZ LYS A 65 30.105 44.485 28.876 1.00 17.81 N1+ ANISOU 506 NZ LYS A 65 2771 1722 2273 -216 -709 -326 N1+ ATOM 507 N LEU A 66 30.812 39.101 27.014 1.00 14.31 N ANISOU 507 N LEU A 66 1971 1588 1879 -202 -519 -200 N ATOM 508 CA LEU A 66 32.076 38.554 27.501 1.00 14.43 C ANISOU 508 CA LEU A 66 1947 1598 1939 -233 -593 -185 C ATOM 509 C LEU A 66 32.547 39.466 28.641 1.00 18.67 C ANISOU 509 C LEU A 66 2561 2060 2474 -259 -710 -219 C ATOM 510 O LEU A 66 32.950 40.611 28.411 1.00 17.83 O ANISOU 510 O LEU A 66 2448 1896 2431 -297 -755 -213 O ATOM 511 CB LEU A 66 33.109 38.493 26.388 1.00 16.54 C ANISOU 511 CB LEU A 66 2096 1878 2311 -262 -575 -123 C ATOM 512 CG LEU A 66 34.493 38.001 26.795 1.00 19.71 C ANISOU 512 CG LEU A 66 2431 2272 2786 -294 -649 -88 C ATOM 513 CD1 LEU A 66 34.440 36.600 27.472 1.00 20.60 C ANISOU 513 CD1 LEU A 66 2563 2427 2836 -263 -652 -104 C ATOM 514 CD2 LEU A 66 35.481 38.063 25.601 1.00 22.47 C ANISOU 514 CD2 LEU A 66 2655 2631 3252 -309 -603 -6 C ATOM 515 N LEU A 67 32.417 38.976 29.873 1.00 17.06 N ANISOU 515 N LEU A 67 2444 1849 2190 -231 -758 -255 N ATOM 516 CA LEU A 67 32.753 39.781 31.047 1.00 18.44 C ANISOU 516 CA LEU A 67 2731 1945 2332 -236 -882 -300 C ATOM 517 C LEU A 67 34.236 39.866 31.293 1.00 21.40 C ANISOU 517 C LEU A 67 3045 2279 2806 -299 -1018 -282 C ATOM 518 O LEU A 67 34.710 40.949 31.660 1.00 21.78 O ANISOU 518 O LEU A 67 3138 2243 2897 -338 -1132 -304 O ATOM 519 CB LEU A 67 32.014 39.258 32.291 1.00 19.45 C ANISOU 519 CB LEU A 67 2995 2076 2319 -163 -875 -340 C ATOM 520 CG LEU A 67 30.484 39.188 32.187 1.00 23.23 C ANISOU 520 CG LEU A 67 3524 2588 2715 -95 -737 -344 C ATOM 521 CD1 LEU A 67 29.896 38.391 33.335 1.00 24.03 C ANISOU 521 CD1 LEU A 67 3726 2703 2700 -19 -706 -354 C ATOM 522 CD2 LEU A 67 29.871 40.591 32.222 1.00 28.51 C ANISOU 522 CD2 LEU A 67 4281 3196 3355 -78 -735 -374 C ATOM 523 N ASP A 68 34.966 38.756 31.145 1.00 20.07 N ANISOU 523 N ASP A 68 2781 2162 2684 -309 -1017 -240 N ATOM 524 CA ASP A 68 36.408 38.715 31.360 1.00 22.01 C ANISOU 524 CA ASP A 68 2943 2376 3043 -364 -1143 -206 C ATOM 525 C ASP A 68 37.082 37.545 30.729 1.00 23.95 C ANISOU 525 C ASP A 68 3053 2692 3357 -364 -1085 -139 C ATOM 526 O ASP A 68 36.441 36.534 30.446 1.00 20.03 O ANISOU 526 O ASP A 68 2559 2262 2788 -315 -974 -137 O ATOM 527 CB ASP A 68 36.756 38.746 32.857 1.00 25.05 C ANISOU 527 CB ASP A 68 3451 2706 3363 -354 -1302 -259 C ATOM 528 CG ASP A 68 37.370 40.072 33.261 1.00 37.72 C ANISOU 528 CG ASP A 68 5095 4200 5038 -413 -1465 -285 C ATOM 529 OD1 ASP A 68 38.207 40.600 32.489 1.00 35.04 O ANISOU 529 OD1 ASP A 68 4616 3833 4866 -487 -1495 -227 O ATOM 530 OD2 ASP A 68 36.978 40.608 34.320 1.00 49.47 O1- ANISOU 530 OD2 ASP A 68 6758 5623 6415 -379 -1557 -359 O1- ATOM 531 N VAL A 69 38.388 37.670 30.511 1.00 24.52 N ANISOU 531 N VAL A 69 3003 2740 3575 -418 -1162 -79 N ATOM 532 CA VAL A 69 39.282 36.664 29.987 1.00 25.56 C ANISOU 532 CA VAL A 69 2997 2923 3791 -414 -1122 -1 C ATOM 533 C VAL A 69 40.330 36.473 31.097 1.00 27.41 C ANISOU 533 C VAL A 69 3220 3119 4075 -442 -1296 2 C ATOM 534 O VAL A 69 40.969 37.454 31.525 1.00 28.31 O ANISOU 534 O VAL A 69 3324 3151 4280 -504 -1443 1 O ATOM 535 CB VAL A 69 39.928 37.150 28.661 1.00 31.60 C ANISOU 535 CB VAL A 69 3611 3687 4707 -445 -1049 89 C ATOM 536 CG1 VAL A 69 40.871 36.094 28.090 1.00 31.95 C ANISOU 536 CG1 VAL A 69 3521 3785 4835 -422 -988 180 C ATOM 537 CG2 VAL A 69 38.867 37.545 27.638 1.00 30.66 C ANISOU 537 CG2 VAL A 69 3529 3593 4529 -416 -907 76 C ATOM 538 N ILE A 70 40.485 35.250 31.609 1.00 24.09 N ANISOU 538 N ILE A 70 2811 2746 3595 -397 -1294 4 N ATOM 539 CA ILE A 70 41.482 34.968 32.644 1.00 26.03 C ANISOU 539 CA ILE A 70 3046 2961 3883 -413 -1462 12 C ATOM 540 C ILE A 70 42.433 33.898 32.105 1.00 28.72 C ANISOU 540 C ILE A 70 3230 3358 4325 -400 -1410 106 C ATOM 541 O ILE A 70 41.996 32.789 31.834 1.00 26.34 O ANISOU 541 O ILE A 70 2943 3124 3942 -338 -1286 110 O ATOM 542 CB ILE A 70 40.809 34.604 34.019 1.00 30.08 C ANISOU 542 CB ILE A 70 3751 3464 4213 -358 -1531 -76 C ATOM 543 CG1 ILE A 70 39.882 35.767 34.492 1.00 32.21 C ANISOU 543 CG1 ILE A 70 4183 3672 4385 -358 -1568 -161 C ATOM 544 CG2 ILE A 70 41.869 34.254 35.100 1.00 32.94 C ANISOU 544 CG2 ILE A 70 4116 3795 4606 -364 -1719 -69 C ATOM 545 CD1 ILE A 70 38.750 35.413 35.439 1.00 42.33 C ANISOU 545 CD1 ILE A 70 5658 4963 5463 -274 -1530 -232 C ATOM 546 N HIS A 71 43.747 34.242 31.938 1.00 31.85 N ANISOU 546 N HIS A 71 3471 3720 4911 -455 -1504 189 N ATOM 547 CA HIS A 71 44.754 33.292 31.462 1.00 33.68 C ANISOU 547 CA HIS A 71 3542 3999 5255 -433 -1454 293 C ATOM 548 C HIS A 71 45.665 32.995 32.634 1.00 39.90 C ANISOU 548 C HIS A 71 4316 4757 6089 -449 -1649 300 C ATOM 549 O HIS A 71 46.369 33.896 33.100 1.00 41.89 O ANISOU 549 O HIS A 71 4522 4931 6463 -522 -1827 311 O ATOM 550 CB HIS A 71 45.555 33.844 30.262 1.00 35.54 C ANISOU 550 CB HIS A 71 3589 4225 5689 -469 -1380 411 C ATOM 551 CG HIS A 71 46.577 32.879 29.726 1.00 39.07 C ANISOU 551 CG HIS A 71 3875 4720 6249 -428 -1304 531 C ATOM 552 CD2 HIS A 71 46.500 31.533 29.566 1.00 39.94 C ANISOU 552 CD2 HIS A 71 3999 4901 6274 -344 -1198 542 C ATOM 553 ND1 HIS A 71 47.821 33.306 29.306 1.00 42.39 N ANISOU 553 ND1 HIS A 71 4095 5109 6900 -469 -1334 661 N ATOM 554 CE1 HIS A 71 48.455 32.218 28.896 1.00 41.94 C ANISOU 554 CE1 HIS A 71 3940 5110 6884 -401 -1235 749 C ATOM 555 NE2 HIS A 71 47.704 31.125 29.045 1.00 40.70 N ANISOU 555 NE2 HIS A 71 3915 5014 6537 -325 -1156 677 N ATOM 556 N THR A 72 45.608 31.755 33.148 1.00 36.42 N ANISOU 556 N THR A 72 3924 4367 5546 -382 -1628 288 N ATOM 557 CA THR A 72 46.375 31.349 34.319 1.00 38.60 C ANISOU 557 CA THR A 72 4211 4621 5834 -379 -1811 289 C ATOM 558 C THR A 72 46.813 29.878 34.307 1.00 46.83 C ANISOU 558 C THR A 72 5196 5732 6864 -308 -1738 347 C ATOM 559 O THR A 72 46.010 28.998 33.991 1.00 46.93 O ANISOU 559 O THR A 72 5282 5802 6748 -242 -1576 323 O ATOM 560 CB THR A 72 45.714 31.889 35.609 1.00 45.44 C ANISOU 560 CB THR A 72 5290 5430 6544 -379 -1964 168 C ATOM 561 CG2 THR A 72 44.425 31.154 35.995 1.00 40.13 C ANISOU 561 CG2 THR A 72 4802 4805 5641 -295 -1841 91 C ATOM 562 OG1 THR A 72 46.659 31.901 36.674 1.00 42.16 O ANISOU 562 OG1 THR A 72 4874 4966 6180 -396 -2195 172 O ATOM 563 N GLU A 73 48.114 29.641 34.615 1.00 46.96 N ANISOU 563 N GLU A 73 5072 5736 7034 -325 -1863 431 N ATOM 564 CA GLU A 73 48.802 28.348 34.701 1.00 48.35 C ANISOU 564 CA GLU A 73 5170 5964 7235 -260 -1829 504 C ATOM 565 C GLU A 73 48.523 27.348 33.561 1.00 53.89 C ANISOU 565 C GLU A 73 5826 6740 7909 -188 -1577 555 C ATOM 566 O GLU A 73 48.344 26.154 33.819 1.00 53.60 O ANISOU 566 O GLU A 73 5848 6746 7771 -114 -1515 549 O ATOM 567 CB GLU A 73 48.618 27.724 36.098 1.00 50.03 C ANISOU 567 CB GLU A 73 5541 6173 7296 -215 -1961 433 C ATOM 568 N ASN A 74 48.524 27.846 32.297 1.00 51.69 N ANISOU 568 N ASN A 74 5449 6468 7721 -204 -1439 609 N ATOM 569 CA ASN A 74 48.269 27.113 31.037 1.00 50.67 C ANISOU 569 CA ASN A 74 5288 6394 7569 -133 -1206 656 C ATOM 570 C ASN A 74 46.785 26.876 30.715 1.00 52.66 C ANISOU 570 C ASN A 74 5715 6668 7626 -102 -1082 550 C ATOM 571 O ASN A 74 46.457 26.225 29.715 1.00 52.30 O ANISOU 571 O ASN A 74 5674 6658 7539 -41 -911 570 O ATOM 572 CB ASN A 74 49.118 25.835 30.893 1.00 52.42 C ANISOU 572 CB ASN A 74 5420 6657 7839 -53 -1143 749 C ATOM 573 N LYS A 75 45.890 27.430 31.548 1.00 46.93 N ANISOU 573 N LYS A 75 5132 5914 6784 -140 -1173 442 N ATOM 574 CA LYS A 75 44.452 27.341 31.347 1.00 44.09 C ANISOU 574 CA LYS A 75 4922 5567 6263 -120 -1072 351 C ATOM 575 C LYS A 75 43.888 28.716 30.990 1.00 42.21 C ANISOU 575 C LYS A 75 4707 5295 6036 -180 -1081 311 C ATOM 576 O LYS A 75 44.388 29.745 31.457 1.00 41.11 O ANISOU 576 O LYS A 75 4536 5106 5979 -243 -1218 313 O ATOM 577 CB LYS A 75 43.751 26.765 32.588 1.00 46.22 C ANISOU 577 CB LYS A 75 5347 5836 6380 -93 -1133 272 C ATOM 578 N LEU A 76 42.878 28.732 30.131 1.00 34.32 N ANISOU 578 N LEU A 76 3763 4315 4962 -159 -944 278 N ATOM 579 CA LEU A 76 42.218 29.953 29.720 1.00 31.30 C ANISOU 579 CA LEU A 76 3412 3905 4575 -203 -933 240 C ATOM 580 C LEU A 76 40.764 29.837 30.156 1.00 27.49 C ANISOU 580 C LEU A 76 3088 3428 3931 -184 -901 143 C ATOM 581 O LEU A 76 40.135 28.806 29.913 1.00 28.40 O ANISOU 581 O LEU A 76 3248 3577 3966 -134 -806 129 O ATOM 582 CB LEU A 76 42.352 30.168 28.192 1.00 31.47 C ANISOU 582 CB LEU A 76 3344 3945 4668 -188 -794 303 C ATOM 583 CG LEU A 76 41.748 31.443 27.585 1.00 36.87 C ANISOU 583 CG LEU A 76 4047 4602 5361 -226 -767 280 C ATOM 584 CD1 LEU A 76 42.472 32.693 28.067 1.00 38.21 C ANISOU 584 CD1 LEU A 76 4155 4709 5653 -305 -900 303 C ATOM 585 CD2 LEU A 76 41.816 31.399 26.076 1.00 39.63 C ANISOU 585 CD2 LEU A 76 4336 4977 5746 -183 -614 344 C ATOM 586 N TYR A 77 40.242 30.870 30.824 1.00 21.20 N ANISOU 586 N TYR A 77 2375 2588 3091 -220 -982 83 N ATOM 587 CA TYR A 77 38.843 30.896 31.299 1.00 19.99 C ANISOU 587 CA TYR A 77 2367 2435 2794 -195 -945 5 C ATOM 588 C TYR A 77 38.131 32.097 30.742 1.00 20.55 C ANISOU 588 C TYR A 77 2462 2482 2865 -223 -913 -24 C ATOM 589 O TYR A 77 38.644 33.221 30.803 1.00 21.47 O ANISOU 589 O TYR A 77 2554 2551 3054 -273 -998 -20 O ATOM 590 CB TYR A 77 38.789 30.987 32.833 1.00 23.00 C ANISOU 590 CB TYR A 77 2865 2782 3091 -183 -1067 -44 C ATOM 591 CG TYR A 77 39.536 29.883 33.545 1.00 26.97 C ANISOU 591 CG TYR A 77 3357 3303 3588 -151 -1121 -16 C ATOM 592 CD1 TYR A 77 38.897 28.700 33.898 1.00 29.42 C ANISOU 592 CD1 TYR A 77 3732 3646 3799 -92 -1042 -23 C ATOM 593 CD2 TYR A 77 40.884 30.020 33.868 1.00 29.22 C ANISOU 593 CD2 TYR A 77 3558 3566 3977 -182 -1254 26 C ATOM 594 CE1 TYR A 77 39.575 27.688 34.583 1.00 32.73 C ANISOU 594 CE1 TYR A 77 4150 4079 4209 -56 -1089 5 C ATOM 595 CE2 TYR A 77 41.573 29.011 34.538 1.00 31.25 C ANISOU 595 CE2 TYR A 77 3805 3841 4230 -147 -1309 55 C ATOM 596 CZ TYR A 77 40.919 27.837 34.873 1.00 37.57 C ANISOU 596 CZ TYR A 77 4682 4676 4916 -81 -1221 43 C ATOM 597 OH TYR A 77 41.590 26.837 35.540 1.00 38.59 O ANISOU 597 OH TYR A 77 4807 4820 5037 -40 -1271 75 O ATOM 598 N LEU A 78 36.964 31.880 30.153 1.00 16.36 N ANISOU 598 N LEU A 78 1973 1978 2265 -195 -797 -48 N ATOM 599 CA LEU A 78 36.156 32.956 29.632 1.00 15.88 C ANISOU 599 CA LEU A 78 1942 1899 2193 -211 -759 -75 C ATOM 600 C LEU A 78 34.951 33.088 30.530 1.00 17.00 C ANISOU 600 C LEU A 78 2215 2028 2216 -182 -754 -135 C ATOM 601 O LEU A 78 34.279 32.080 30.814 1.00 16.73 O ANISOU 601 O LEU A 78 2219 2023 2116 -140 -696 -142 O ATOM 602 CB LEU A 78 35.725 32.671 28.193 1.00 14.60 C ANISOU 602 CB LEU A 78 1725 1773 2049 -194 -636 -50 C ATOM 603 CG LEU A 78 36.849 32.442 27.199 1.00 18.32 C ANISOU 603 CG LEU A 78 2080 2260 2622 -195 -605 22 C ATOM 604 CD1 LEU A 78 36.292 32.187 25.803 1.00 18.93 C ANISOU 604 CD1 LEU A 78 2145 2366 2683 -158 -488 36 C ATOM 605 CD2 LEU A 78 37.833 33.599 27.167 1.00 22.45 C ANISOU 605 CD2 LEU A 78 2531 2741 3258 -247 -674 62 C ATOM 606 N VAL A 79 34.671 34.293 30.987 1.00 15.95 N ANISOU 606 N VAL A 79 2151 1847 2062 -197 -808 -172 N ATOM 607 CA VAL A 79 33.555 34.535 31.894 1.00 15.28 C ANISOU 607 CA VAL A 79 2201 1744 1860 -153 -793 -220 C ATOM 608 C VAL A 79 32.501 35.276 31.112 1.00 15.94 C ANISOU 608 C VAL A 79 2290 1830 1938 -150 -707 -230 C ATOM 609 O VAL A 79 32.763 36.381 30.622 1.00 16.20 O ANISOU 609 O VAL A 79 2302 1828 2025 -186 -737 -232 O ATOM 610 CB VAL A 79 34.036 35.389 33.101 1.00 18.78 C ANISOU 610 CB VAL A 79 2751 2119 2266 -155 -932 -260 C ATOM 611 CG1 VAL A 79 32.934 35.514 34.159 1.00 19.43 C ANISOU 611 CG1 VAL A 79 2996 2183 2205 -82 -902 -302 C ATOM 612 CG2 VAL A 79 35.358 34.867 33.718 1.00 19.72 C ANISOU 612 CG2 VAL A 79 2838 2227 2425 -175 -1056 -244 C ATOM 613 N PHE A 80 31.333 34.681 30.986 1.00 13.75 N ANISOU 613 N PHE A 80 2031 1585 1608 -108 -605 -228 N ATOM 614 CA PHE A 80 30.230 35.228 30.201 1.00 13.26 C ANISOU 614 CA PHE A 80 1961 1530 1546 -99 -523 -230 C ATOM 615 C PHE A 80 29.043 35.507 31.062 1.00 14.30 C ANISOU 615 C PHE A 80 2196 1646 1593 -44 -479 -248 C ATOM 616 O PHE A 80 28.834 34.859 32.107 1.00 15.39 O ANISOU 616 O PHE A 80 2398 1783 1665 0 -471 -247 O ATOM 617 CB PHE A 80 29.802 34.216 29.121 1.00 14.36 C ANISOU 617 CB PHE A 80 2016 1719 1721 -98 -445 -202 C ATOM 618 CG PHE A 80 30.738 34.143 27.942 1.00 13.19 C ANISOU 618 CG PHE A 80 1777 1587 1649 -131 -452 -177 C ATOM 619 CD1 PHE A 80 30.689 35.107 26.937 1.00 14.75 C ANISOU 619 CD1 PHE A 80 1943 1776 1884 -146 -434 -171 C ATOM 620 CD2 PHE A 80 31.644 33.092 27.814 1.00 14.65 C ANISOU 620 CD2 PHE A 80 1910 1793 1863 -133 -465 -152 C ATOM 621 CE1 PHE A 80 31.528 35.032 25.841 1.00 15.28 C ANISOU 621 CE1 PHE A 80 1934 1857 2014 -159 -420 -134 C ATOM 622 CE2 PHE A 80 32.488 33.022 26.707 1.00 16.78 C ANISOU 622 CE2 PHE A 80 2101 2076 2198 -144 -450 -117 C ATOM 623 CZ PHE A 80 32.425 33.992 25.741 1.00 15.19 C ANISOU 623 CZ PHE A 80 1875 1867 2030 -154 -424 -106 C ATOM 624 N GLU A 81 28.210 36.415 30.598 1.00 15.12 N ANISOU 624 N GLU A 81 2310 1738 1696 -35 -434 -254 N ATOM 625 CA GLU A 81 26.913 36.635 31.184 1.00 16.60 C ANISOU 625 CA GLU A 81 2569 1918 1819 28 -359 -252 C ATOM 626 C GLU A 81 26.152 35.280 31.142 1.00 15.81 C ANISOU 626 C GLU A 81 2416 1861 1729 50 -280 -213 C ATOM 627 O GLU A 81 26.319 34.493 30.199 1.00 16.34 O ANISOU 627 O GLU A 81 2387 1962 1861 13 -274 -197 O ATOM 628 CB GLU A 81 26.245 37.713 30.303 1.00 20.24 C ANISOU 628 CB GLU A 81 3009 2370 2311 23 -323 -254 C ATOM 629 CG GLU A 81 24.784 37.546 30.007 1.00 25.76 C ANISOU 629 CG GLU A 81 3682 3094 3013 65 -222 -223 C ATOM 630 CD GLU A 81 24.138 38.501 29.025 1.00 19.34 C ANISOU 630 CD GLU A 81 2835 2279 2235 62 -192 -219 C ATOM 631 OE1 GLU A 81 24.763 38.891 28.011 1.00 16.34 O ANISOU 631 OE1 GLU A 81 2404 1901 1903 15 -230 -227 O ATOM 632 OE2 GLU A 81 22.936 38.763 29.229 1.00 25.20 O1- ANISOU 632 OE2 GLU A 81 3593 3019 2963 114 -119 -196 O1- ATOM 633 N PHE A 82 25.341 35.014 32.141 1.00 15.14 N ANISOU 633 N PHE A 82 2400 1769 1585 115 -218 -193 N ATOM 634 CA PHE A 82 24.592 33.787 32.255 1.00 14.39 C ANISOU 634 CA PHE A 82 2255 1699 1513 137 -142 -145 C ATOM 635 C PHE A 82 23.195 33.967 31.723 1.00 16.08 C ANISOU 635 C PHE A 82 2413 1921 1775 155 -55 -107 C ATOM 636 O PHE A 82 22.528 34.953 32.071 1.00 15.95 O ANISOU 636 O PHE A 82 2455 1885 1722 204 -12 -103 O ATOM 637 CB PHE A 82 24.538 33.366 33.750 1.00 16.53 C ANISOU 637 CB PHE A 82 2634 1952 1694 209 -113 -126 C ATOM 638 CG PHE A 82 23.740 32.112 33.980 1.00 14.99 C ANISOU 638 CG PHE A 82 2389 1774 1533 235 -22 -61 C ATOM 639 CD1 PHE A 82 24.298 30.863 33.737 1.00 16.78 C ANISOU 639 CD1 PHE A 82 2552 2018 1804 195 -49 -50 C ATOM 640 CD2 PHE A 82 22.396 32.176 34.340 1.00 17.26 C ANISOU 640 CD2 PHE A 82 2677 2054 1827 297 95 -1 C ATOM 641 CE1 PHE A 82 23.533 29.693 33.870 1.00 17.25 C ANISOU 641 CE1 PHE A 82 2558 2081 1916 208 29 13 C ATOM 642 CE2 PHE A 82 21.649 31.005 34.499 1.00 19.77 C ANISOU 642 CE2 PHE A 82 2926 2377 2206 310 177 73 C ATOM 643 CZ PHE A 82 22.233 29.765 34.291 1.00 17.25 C ANISOU 643 CZ PHE A 82 2554 2068 1931 263 139 77 C ATOM 644 N LEU A 83 22.766 33.010 30.866 1.00 14.24 N ANISOU 644 N LEU A 83 2069 1711 1628 118 -38 -78 N ATOM 645 CA ALEU A 83 21.392 32.951 30.407 0.80 14.83 C ANISOU 645 CA ALEU A 83 2072 1789 1772 130 29 -31 C ATOM 646 CA BLEU A 83 21.411 32.937 30.357 0.20 14.43 C ANISOU 646 CA BLEU A 83 2019 1740 1725 127 26 -33 C ATOM 647 C LEU A 83 20.949 31.542 30.673 1.00 19.62 C ANISOU 647 C LEU A 83 2624 2396 2435 128 66 21 C ATOM 648 O LEU A 83 21.746 30.607 30.611 1.00 20.06 O ANISOU 648 O LEU A 83 2671 2456 2493 96 22 6 O ATOM 649 CB ALEU A 83 21.231 33.310 28.920 0.80 14.47 C ANISOU 649 CB ALEU A 83 1951 1757 1792 82 -15 -53 C ATOM 650 CB BLEU A 83 21.333 33.247 28.860 0.20 13.69 C ANISOU 650 CB BLEU A 83 1850 1660 1694 77 -22 -56 C ATOM 651 CG ALEU A 83 21.420 34.784 28.602 0.80 17.95 C ANISOU 651 CG ALEU A 83 2435 2191 2195 89 -32 -87 C ATOM 652 CG BLEU A 83 21.122 34.729 28.550 0.20 17.48 C ANISOU 652 CG BLEU A 83 2361 2132 2148 94 -20 -76 C ATOM 653 CD1ALEU A 83 22.826 35.013 28.100 0.80 19.39 C ANISOU 653 CD1ALEU A 83 2633 2376 2357 44 -111 -136 C ATOM 654 CD1BLEU A 83 22.442 35.435 28.395 0.20 17.69 C ANISOU 654 CD1BLEU A 83 2442 2153 2128 66 -88 -130 C ATOM 655 CD2ALEU A 83 20.445 35.244 27.487 0.80 19.50 C ANISOU 655 CD2ALEU A 83 2560 2395 2454 84 -23 -72 C ATOM 656 CD2BLEU A 83 20.308 34.917 27.278 0.20 17.69 C ANISOU 656 CD2BLEU A 83 2305 2170 2248 75 -27 -65 C ATOM 657 N HIS A 84 19.692 31.405 31.042 0.79 21.69 N ANISOU 657 N HIS A 84 3079 3488 1676 -148 14 -70 N ATOM 658 CA HIS A 84 19.122 30.143 31.497 0.65 21.21 C ANISOU 658 CA HIS A 84 3085 3441 1533 -226 39 60 C ATOM 659 C HIS A 84 18.809 29.030 30.476 1.00 21.98 C ANISOU 659 C HIS A 84 3207 3426 1718 -293 35 149 C ATOM 660 O HIS A 84 18.720 27.878 30.891 0.88 23.38 O ANISOU 660 O HIS A 84 3464 3577 1843 -347 23 263 O ATOM 661 CB HIS A 84 17.928 30.393 32.458 0.68 23.60 C ANISOU 661 CB HIS A 84 3355 3900 1711 -272 134 68 C ATOM 662 CG HIS A 84 18.235 31.148 33.740 0.48 27.95 C ANISOU 662 CG HIS A 84 3908 4579 2133 -211 131 1 C ATOM 663 CD2 HIS A 84 18.279 30.699 35.021 0.63 31.29 C ANISOU 663 CD2 HIS A 84 4400 5100 2388 -223 137 63 C ATOM 664 ND1 HIS A 84 18.407 32.537 33.758 0.81 29.39 N ANISOU 664 ND1 HIS A 84 4012 4803 2351 -133 126 -148 N ATOM 665 CE1 HIS A 84 18.627 32.865 35.021 0.87 30.14 C ANISOU 665 CE1 HIS A 84 4128 5016 2307 -93 120 -185 C ATOM 666 NE2 HIS A 84 18.545 31.803 35.829 0.93 31.59 N ANISOU 666 NE2 HIS A 84 4400 5248 2355 -142 130 -61 N ATOM 667 N AGLN A 85 18.697 29.304 29.180 0.50 18.45 N ANISOU 667 N AGLN A 85 2705 2906 1401 -288 36 102 N ATOM 668 N BGLN A 85 18.670 29.371 29.176 0.50 19.40 N ANISOU 668 N BGLN A 85 2820 3030 1522 -286 38 97 N ATOM 669 CA AGLN A 85 18.444 28.183 28.276 0.50 17.27 C ANISOU 669 CA AGLN A 85 2582 2653 1325 -344 21 176 C ATOM 670 CA BGLN A 85 18.238 28.396 28.193 0.50 18.67 C ANISOU 670 CA BGLN A 85 2739 2846 1508 -346 37 161 C ATOM 671 C AGLN A 85 18.972 28.540 26.919 0.50 16.42 C ANISOU 671 C AGLN A 85 2437 2459 1344 -299 -14 109 C ATOM 672 C BGLN A 85 18.792 28.609 26.774 0.50 18.93 C ANISOU 672 C BGLN A 85 2742 2780 1672 -305 -4 104 C ATOM 673 O AGLN A 85 19.280 29.712 26.676 0.50 14.78 O ANISOU 673 O AGLN A 85 2174 2277 1166 -243 -9 18 O ATOM 674 O BGLN A 85 18.871 29.742 26.310 0.50 18.22 O ANISOU 674 O BGLN A 85 2589 2710 1625 -260 9 17 O ATOM 675 CB AGLN A 85 16.930 27.869 28.203 0.50 19.74 C ANISOU 675 CB AGLN A 85 2854 3019 1628 -439 105 221 C ATOM 676 CB BGLN A 85 16.686 28.458 28.185 0.50 20.37 C ANISOU 676 CB BGLN A 85 2891 3140 1707 -425 130 177 C ATOM 677 CG AGLN A 85 16.571 26.515 27.603 0.50 24.51 C ANISOU 677 CG AGLN A 85 3500 3524 2288 -517 88 314 C ATOM 678 CG BGLN A 85 15.951 27.526 27.237 0.50 18.89 C ANISOU 678 CG BGLN A 85 2697 2880 1601 -500 139 231 C ATOM 679 CD AGLN A 85 15.115 26.224 27.797 0.50 33.16 C ANISOU 679 CD AGLN A 85 4550 4689 3361 -620 174 359 C ATOM 680 CD BGLN A 85 16.040 26.069 27.586 0.50 37.50 C ANISOU 680 CD BGLN A 85 5147 5167 3936 -569 109 354 C ATOM 681 NE2AGLN A 85 14.804 25.488 28.848 0.50 33.36 N ANISOU 681 NE2AGLN A 85 4632 4754 3287 -694 204 463 N ATOM 682 NE2BGLN A 85 14.896 25.411 27.635 0.50 31.07 N ANISOU 682 NE2BGLN A 85 4314 4371 3118 -674 166 420 N ATOM 683 OE1AGLN A 85 14.261 26.664 27.031 0.50 20.30 O ANISOU 683 OE1AGLN A 85 2832 3084 1797 -635 215 301 O ATOM 684 OE1BGLN A 85 17.125 25.506 27.755 0.50 28.45 O ANISOU 684 OE1BGLN A 85 4084 3939 2785 -531 30 389 O ATOM 685 N ASP A 86 19.111 27.525 26.054 1.00 15.98 N ANISOU 685 N ASP A 86 2413 2300 1359 -324 -52 153 N ATOM 686 CA ASP A 86 19.529 27.647 24.654 1.00 15.13 C ANISOU 686 CA ASP A 86 2274 2117 1360 -290 -81 99 C ATOM 687 C ASP A 86 18.353 27.327 23.732 1.00 15.21 C ANISOU 687 C ASP A 86 2243 2112 1423 -350 -43 112 C ATOM 688 O ASP A 86 17.330 26.768 24.157 1.00 16.58 O ANISOU 688 O ASP A 86 2420 2313 1566 -425 -5 172 O ATOM 689 CB ASP A 86 20.798 26.818 24.333 1.00 16.67 C ANISOU 689 CB ASP A 86 2526 2214 1596 -247 -167 106 C ATOM 690 CG ASP A 86 20.676 25.310 24.327 1.00 22.91 C ANISOU 690 CG ASP A 86 3389 2918 2399 -291 -213 189 C ATOM 691 OD1 ASP A 86 19.731 24.809 23.744 1.00 23.96 O ANISOU 691 OD1 ASP A 86 3507 3025 2569 -352 -187 218 O ATOM 692 OD2 ASP A 86 21.628 24.638 24.766 1.00 30.09 O1- ANISOU 692 OD2 ASP A 86 4363 3771 3297 -253 -288 213 O1- ATOM 693 N LEU A 87 18.478 27.710 22.477 1.00 14.27 N ANISOU 693 N LEU A 87 2083 1958 1380 -319 -52 56 N ATOM 694 CA LEU A 87 17.418 27.500 21.509 1.00 13.38 C ANISOU 694 CA LEU A 87 1929 1836 1319 -361 -29 52 C ATOM 695 C LEU A 87 17.207 26.043 21.183 1.00 15.56 C ANISOU 695 C LEU A 87 2249 2031 1631 -413 -66 108 C ATOM 696 O LEU A 87 16.071 25.657 20.860 1.00 16.25 O ANISOU 696 O LEU A 87 2305 2126 1745 -476 -40 125 O ATOM 697 CB LEU A 87 17.709 28.314 20.222 1.00 12.44 C ANISOU 697 CB LEU A 87 1766 1702 1258 -307 -37 -18 C ATOM 698 CG LEU A 87 16.601 28.338 19.185 1.00 13.87 C ANISOU 698 CG LEU A 87 1899 1889 1483 -331 -21 -36 C ATOM 699 CD1 LEU A 87 15.339 29.048 19.736 1.00 16.07 C ANISOU 699 CD1 LEU A 87 2116 2254 1736 -359 37 -46 C ATOM 700 CD2 LEU A 87 17.089 29.031 17.895 1.00 13.99 C ANISOU 700 CD2 LEU A 87 1894 1884 1538 -274 -38 -89 C ATOM 701 N LYS A 88 18.258 25.216 21.297 1.00 15.51 N ANISOU 701 N LYS A 88 2311 1947 1634 -388 -132 132 N ATOM 702 CA LYS A 88 18.095 23.787 21.015 1.00 16.24 C ANISOU 702 CA LYS A 88 2454 1943 1773 -433 -181 181 C ATOM 703 C LYS A 88 17.132 23.193 22.046 1.00 18.65 C ANISOU 703 C LYS A 88 2786 2266 2033 -530 -145 276 C ATOM 704 O LYS A 88 16.161 22.507 21.692 1.00 18.45 O ANISOU 704 O LYS A 88 2746 2211 2052 -607 -134 306 O ATOM 705 CB LYS A 88 19.449 23.060 21.042 1.00 18.72 C ANISOU 705 CB LYS A 88 2836 2169 2107 -373 -268 181 C ATOM 706 CG LYS A 88 19.345 21.541 20.781 1.00 25.89 C ANISOU 706 CG LYS A 88 3805 2955 3076 -411 -337 227 C ATOM 707 CD LYS A 88 20.204 20.711 21.720 0.50 40.45 C ANISOU 707 CD LYS A 88 5745 4726 4897 -391 -412 290 C ATOM 708 CE LYS A 88 20.242 19.256 21.310 0.50 46.09 C ANISOU 708 CE LYS A 88 6522 5298 5693 -410 -498 319 C ATOM 709 NZ LYS A 88 19.042 18.513 21.780 0.50 53.03 N1+ ANISOU 709 NZ LYS A 88 7434 6141 6573 -533 -473 424 N1+ ATOM 710 N LYS A 89 17.356 23.481 23.340 1.00 17.52 N ANISOU 710 N LYS A 89 2677 2182 1797 -532 -123 322 N ATOM 711 CA LYS A 89 16.468 22.970 24.367 1.00 19.55 C ANISOU 711 CA LYS A 89 2960 2477 1990 -629 -75 420 C ATOM 712 C LYS A 89 15.052 23.542 24.229 1.00 20.43 C ANISOU 712 C LYS A 89 2974 2688 2100 -693 19 397 C ATOM 713 O LYS A 89 14.078 22.799 24.382 1.00 21.64 O ANISOU 713 O LYS A 89 3122 2836 2264 -797 52 461 O ATOM 714 CB LYS A 89 17.079 23.252 25.740 1.00 22.01 C ANISOU 714 CB LYS A 89 3328 2850 2185 -602 -74 461 C ATOM 715 CG LYS A 89 18.347 22.438 25.995 1.00 29.31 C ANISOU 715 CG LYS A 89 4356 3668 3113 -549 -179 500 C ATOM 716 CD LYS A 89 18.897 22.675 27.399 1.00 36.27 C ANISOU 716 CD LYS A 89 5297 4615 3868 -521 -187 544 C ATOM 717 CE LYS A 89 20.275 22.081 27.574 1.00 44.45 C ANISOU 717 CE LYS A 89 6418 5555 4915 -440 -304 553 C ATOM 718 NZ LYS A 89 20.746 22.214 28.980 1.00 57.40 N1+ ANISOU 718 NZ LYS A 89 8126 7260 6423 -414 -323 603 N1+ ATOM 719 N PHE A 90 14.931 24.830 23.856 1.00 18.27 N ANISOU 719 N PHE A 90 2620 2496 1827 -633 54 301 N ATOM 720 CA PHE A 90 13.629 25.480 23.652 1.00 17.82 C ANISOU 720 CA PHE A 90 2460 2532 1777 -671 130 258 C ATOM 721 C PHE A 90 12.882 24.839 22.460 1.00 19.49 C ANISOU 721 C PHE A 90 2633 2680 2091 -717 112 245 C ATOM 722 O PHE A 90 11.677 24.570 22.565 1.00 21.48 O ANISOU 722 O PHE A 90 2828 2980 2354 -802 164 262 O ATOM 723 CB PHE A 90 13.788 27.007 23.501 1.00 18.04 C ANISOU 723 CB PHE A 90 2425 2636 1793 -582 150 159 C ATOM 724 CG PHE A 90 12.494 27.786 23.444 1.00 18.71 C ANISOU 724 CG PHE A 90 2404 2824 1880 -601 218 104 C ATOM 725 CD1 PHE A 90 11.648 27.846 24.543 1.00 23.11 C ANISOU 725 CD1 PHE A 90 2925 3495 2360 -659 293 126 C ATOM 726 CD2 PHE A 90 12.152 28.512 22.314 1.00 19.48 C ANISOU 726 CD2 PHE A 90 2438 2913 2049 -552 203 25 C ATOM 727 CE1 PHE A 90 10.450 28.570 24.482 1.00 24.53 C ANISOU 727 CE1 PHE A 90 2994 3778 2550 -668 353 58 C ATOM 728 CE2 PHE A 90 10.942 29.204 22.245 1.00 22.45 C ANISOU 728 CE2 PHE A 90 2714 3379 2436 -559 251 -32 C ATOM 729 CZ PHE A 90 10.094 29.220 23.322 1.00 22.96 C ANISOU 729 CZ PHE A 90 2731 3555 2436 -615 325 -22 C ATOM 730 N MET A 91 13.598 24.568 21.346 1.00 16.63 N ANISOU 730 N MET A 91 2297 2220 1801 -662 39 209 N ATOM 731 CA AMET A 91 12.920 23.919 20.227 0.50 15.21 C ANISOU 731 CA AMET A 91 2085 1984 1711 -699 13 188 C ATOM 732 CA BMET A 91 13.035 23.896 20.161 0.50 16.66 C ANISOU 732 CA BMET A 91 2274 2158 1898 -692 5 185 C ATOM 733 C MET A 91 12.492 22.515 20.562 1.00 20.37 C ANISOU 733 C MET A 91 2781 2563 2396 -803 -2 271 C ATOM 734 O MET A 91 11.393 22.125 20.158 1.00 21.80 O ANISOU 734 O MET A 91 2903 2747 2631 -878 16 265 O ATOM 735 CB AMET A 91 13.796 23.892 19.008 0.50 15.22 C ANISOU 735 CB AMET A 91 2107 1910 1767 -617 -58 128 C ATOM 736 CB BMET A 91 14.132 23.702 19.091 0.50 18.01 C ANISOU 736 CB BMET A 91 2485 2240 2118 -609 -73 138 C ATOM 737 CG AMET A 91 13.906 25.231 18.354 0.50 15.15 C ANISOU 737 CG AMET A 91 2043 1964 1749 -537 -41 50 C ATOM 738 CG BMET A 91 14.407 24.944 18.263 0.50 20.34 C ANISOU 738 CG BMET A 91 2731 2585 2413 -522 -66 55 C ATOM 739 SD AMET A 91 14.586 25.052 16.729 0.50 14.95 S ANISOU 739 SD AMET A 91 2028 1871 1782 -468 -108 -15 S ATOM 740 SD BMET A 91 16.052 24.947 17.488 0.50 24.14 S ANISOU 740 SD BMET A 91 3263 3000 2910 -425 -131 13 S ATOM 741 CE AMET A 91 16.167 24.388 17.145 0.50 10.16 C ANISOU 741 CE AMET A 91 1508 1186 1165 -428 -160 11 C ATOM 742 CE BMET A 91 15.682 25.706 15.986 0.50 20.38 C ANISOU 742 CE BMET A 91 2727 2554 2463 -380 -130 -63 C ATOM 743 N ASP A 92 13.300 21.753 21.326 1.00 19.58 N ANISOU 743 N ASP A 92 2781 2394 2265 -814 -39 351 N ATOM 744 CA ASP A 92 12.931 20.403 21.751 1.00 21.76 C ANISOU 744 CA ASP A 92 3116 2582 2570 -921 -59 451 C ATOM 745 C ASP A 92 11.698 20.458 22.639 1.00 26.26 C ANISOU 745 C ASP A 92 3636 3251 3089 -1038 40 513 C ATOM 746 O ASP A 92 10.780 19.651 22.445 1.00 27.78 O ANISOU 746 O ASP A 92 3804 3405 3346 -1147 51 549 O ATOM 747 CB ASP A 92 14.090 19.723 22.494 1.00 23.63 C ANISOU 747 CB ASP A 92 3476 2731 2770 -893 -125 528 C ATOM 748 CG ASP A 92 15.239 19.272 21.625 1.00 28.46 C ANISOU 748 CG ASP A 92 4137 3224 3454 -798 -233 472 C ATOM 749 OD1 ASP A 92 15.067 19.218 20.388 1.00 29.96 O ANISOU 749 OD1 ASP A 92 4278 3380 3727 -773 -260 388 O ATOM 750 OD2 ASP A 92 16.324 19.015 22.173 1.00 32.39 O1- ANISOU 750 OD2 ASP A 92 4716 3672 3917 -741 -290 504 O1- ATOM 751 N ALA A 93 11.642 21.422 23.583 1.00 24.00 N ANISOU 751 N ALA A 93 3325 3101 2693 -1018 114 515 N ATOM 752 CA ALA A 93 10.498 21.580 24.489 1.00 27.16 C ANISOU 752 CA ALA A 93 3666 3627 3026 -1121 221 560 C ATOM 753 C ALA A 93 9.232 22.061 23.788 1.00 30.69 C ANISOU 753 C ALA A 93 3973 4152 3536 -1154 275 474 C ATOM 754 O ALA A 93 8.133 21.773 24.267 1.00 33.07 O ANISOU 754 O ALA A 93 4214 4526 3826 -1269 353 513 O ATOM 755 CB ALA A 93 10.853 22.517 25.631 1.00 28.03 C ANISOU 755 CB ALA A 93 3784 3866 2999 -1070 275 560 C ATOM 756 N SER A 94 9.386 22.768 22.651 1.00 27.22 N ANISOU 756 N SER A 94 3482 3701 3160 -1055 233 361 N ATOM 757 CA SER A 94 8.286 23.298 21.841 1.00 27.28 C ANISOU 757 CA SER A 94 3364 3773 3231 -1058 259 268 C ATOM 758 C SER A 94 7.944 22.363 20.661 1.00 34.21 C ANISOU 758 C SER A 94 4231 4537 4230 -1097 192 250 C ATOM 759 O SER A 94 7.203 22.782 19.780 1.00 33.75 O ANISOU 759 O SER A 94 4080 4515 4230 -1075 186 162 O ATOM 760 CB SER A 94 8.653 24.684 21.303 1.00 27.36 C ANISOU 760 CB SER A 94 3333 3833 3227 -923 244 163 C ATOM 761 OG SER A 94 8.990 25.622 22.316 1.00 30.20 O ANISOU 761 OG SER A 94 3696 4288 3488 -876 293 158 O ATOM 762 N ALA A 95 8.488 21.123 20.620 1.00 32.72 N ANISOU 762 N ALA A 95 4139 4211 4083 -1144 131 324 N ATOM 763 CA ALA A 95 8.297 20.173 19.512 1.00 33.34 C ANISOU 763 CA ALA A 95 4218 4168 4281 -1170 53 296 C ATOM 764 C ALA A 95 6.842 19.813 19.180 1.00 37.71 C ANISOU 764 C ALA A 95 4661 4753 4912 -1279 85 270 C ATOM 765 O ALA A 95 6.501 19.681 18.002 1.00 37.63 O ANISOU 765 O ALA A 95 4601 4706 4989 -1253 26 183 O ATOM 766 CB ALA A 95 9.090 18.901 19.763 1.00 35.01 C ANISOU 766 CB ALA A 95 4555 4225 4523 -1207 -17 385 C ATOM 767 N LEU A 96 6.006 19.624 20.202 1.00 34.40 N ANISOU 767 N LEU A 96 4202 4409 4462 -1403 176 341 N ATOM 768 CA LEU A 96 4.610 19.216 20.011 1.00 34.41 C ANISOU 768 CA LEU A 96 4086 4447 4542 -1526 216 321 C ATOM 769 C LEU A 96 3.755 20.291 19.356 1.00 33.29 C ANISOU 769 C LEU A 96 3798 4434 4416 -1464 240 187 C ATOM 770 O LEU A 96 2.945 19.991 18.483 1.00 32.14 O ANISOU 770 O LEU A 96 3567 4273 4373 -1495 205 114 O ATOM 771 CB LEU A 96 3.988 18.776 21.352 1.00 37.02 C ANISOU 771 CB LEU A 96 4407 4842 4817 -1682 323 440 C ATOM 772 CG LEU A 96 3.913 17.270 21.624 1.00 45.24 C ANISOU 772 CG LEU A 96 5526 5737 5928 -1832 297 563 C ATOM 773 CD1 LEU A 96 5.303 16.656 21.793 1.00 45.99 C ANISOU 773 CD1 LEU A 96 5797 5675 6000 -1774 207 645 C ATOM 774 CD2 LEU A 96 3.090 16.997 22.861 1.00 50.01 C ANISOU 774 CD2 LEU A 96 6094 6438 6469 -1997 424 674 C ATOM 775 N THR A 97 3.979 21.545 19.742 1.00 28.92 N ANISOU 775 N THR A 97 3222 3998 3768 -1365 286 148 N ATOM 776 CA THR A 97 3.201 22.688 19.292 1.00 28.78 C ANISOU 776 CA THR A 97 3076 4105 3756 -1294 307 28 C ATOM 777 C THR A 97 3.889 23.574 18.278 1.00 30.25 C ANISOU 777 C THR A 97 3288 4262 3941 -1132 229 -56 C ATOM 778 O THR A 97 3.210 24.260 17.520 1.00 32.73 O ANISOU 778 O THR A 97 3509 4633 4294 -1073 207 -156 O ATOM 779 CB THR A 97 2.821 23.552 20.517 1.00 40.12 C ANISOU 779 CB THR A 97 4453 5702 5089 -1302 419 33 C ATOM 780 CG2 THR A 97 1.846 22.854 21.459 1.00 44.44 C ANISOU 780 CG2 THR A 97 4934 6325 5627 -1470 519 99 C ATOM 781 OG1 THR A 97 4.021 23.905 21.222 1.00 43.10 O ANISOU 781 OG1 THR A 97 4948 6062 5365 -1236 421 92 O ATOM 782 N GLY A 98 5.218 23.609 18.311 1.00 21.60 N ANISOU 782 N GLY A 98 2318 3089 2800 -1060 188 -13 N ATOM 783 CA GLY A 98 6.008 24.526 17.512 1.00 19.83 C ANISOU 783 CA GLY A 98 2127 2849 2560 -917 133 -74 C ATOM 784 C GLY A 98 6.181 25.867 18.215 1.00 21.65 C ANISOU 784 C GLY A 98 2337 3181 2708 -844 186 -97 C ATOM 785 O GLY A 98 5.360 26.259 19.062 1.00 23.25 O ANISOU 785 O GLY A 98 2460 3495 2878 -886 262 -107 O ATOM 786 N ILE A 99 7.266 26.562 17.913 1.00 18.89 N ANISOU 786 N ILE A 99 2054 2796 2326 -739 148 -110 N ATOM 787 CA ILE A 99 7.471 27.901 18.449 1.00 17.67 C ANISOU 787 CA ILE A 99 1881 2719 2113 -661 182 -145 C ATOM 788 C ILE A 99 6.491 28.808 17.669 1.00 19.61 C ANISOU 788 C ILE A 99 2027 3024 2402 -605 167 -240 C ATOM 789 O ILE A 99 6.428 28.715 16.436 1.00 18.59 O ANISOU 789 O ILE A 99 1898 2842 2324 -568 102 -272 O ATOM 790 CB ILE A 99 8.933 28.373 18.248 1.00 18.18 C ANISOU 790 CB ILE A 99 2041 2717 2147 -573 141 -134 C ATOM 791 CG1 ILE A 99 9.943 27.477 18.980 1.00 19.49 C ANISOU 791 CG1 ILE A 99 2306 2824 2277 -613 138 -51 C ATOM 792 CG2 ILE A 99 9.084 29.848 18.653 1.00 19.08 C ANISOU 792 CG2 ILE A 99 2129 2896 2223 -491 163 -184 C ATOM 793 CD1 ILE A 99 11.449 27.855 18.709 1.00 25.31 C ANISOU 793 CD1 ILE A 99 3122 3496 2996 -527 93 -52 C ATOM 794 N PRO A 100 5.688 29.661 18.342 1.00 18.45 N ANISOU 794 N PRO A 100 1790 2987 2233 -592 220 -290 N ATOM 795 CA PRO A 100 4.759 30.530 17.602 1.00 17.80 C ANISOU 795 CA PRO A 100 1612 2952 2198 -525 191 -386 C ATOM 796 C PRO A 100 5.477 31.422 16.592 1.00 18.73 C ANISOU 796 C PRO A 100 1789 3002 2327 -408 116 -410 C ATOM 797 O PRO A 100 6.551 31.919 16.883 1.00 16.38 O ANISOU 797 O PRO A 100 1568 2666 1989 -364 115 -382 O ATOM 798 CB PRO A 100 4.110 31.360 18.723 1.00 20.06 C ANISOU 798 CB PRO A 100 1813 3363 2445 -515 262 -436 C ATOM 799 CG PRO A 100 4.186 30.471 19.918 1.00 25.50 C ANISOU 799 CG PRO A 100 2520 4093 3076 -627 342 -361 C ATOM 800 CD PRO A 100 5.555 29.858 19.802 1.00 20.41 C ANISOU 800 CD PRO A 100 2017 3329 2408 -631 305 -272 C ATOM 801 N LEU A 101 4.898 31.629 15.406 1.00 17.45 N ANISOU 801 N LEU A 101 1590 2826 2216 -361 52 -461 N ATOM 802 CA LEU A 101 5.525 32.447 14.353 1.00 17.20 C ANISOU 802 CA LEU A 101 1619 2732 2185 -259 -18 -470 C ATOM 803 C LEU A 101 5.937 33.821 14.861 1.00 17.01 C ANISOU 803 C LEU A 101 1609 2717 2136 -180 -9 -488 C ATOM 804 O LEU A 101 7.046 34.241 14.535 1.00 14.74 O ANISOU 804 O LEU A 101 1410 2362 1828 -138 -31 -451 O ATOM 805 CB LEU A 101 4.630 32.563 13.099 1.00 19.39 C ANISOU 805 CB LEU A 101 1845 3014 2510 -213 -92 -528 C ATOM 806 CG LEU A 101 5.088 33.571 12.042 1.00 25.14 C ANISOU 806 CG LEU A 101 2632 3694 3227 -104 -162 -532 C ATOM 807 CD1 LEU A 101 6.310 33.079 11.307 1.00 25.30 C ANISOU 807 CD1 LEU A 101 2763 3636 3214 -106 -184 -470 C ATOM 808 CD2 LEU A 101 3.980 33.851 11.060 1.00 31.48 C ANISOU 808 CD2 LEU A 101 3369 4525 4068 -49 -236 -599 C ATOM 809 N PRO A 102 5.140 34.551 15.662 1.00 14.82 N ANISOU 809 N PRO A 102 1246 2522 1864 -159 23 -550 N ATOM 810 CA PRO A 102 5.625 35.875 16.076 1.00 14.10 C ANISOU 810 CA PRO A 102 1178 2420 1760 -76 16 -575 C ATOM 811 C PRO A 102 6.909 35.804 16.887 1.00 15.32 C ANISOU 811 C PRO A 102 1416 2541 1863 -101 56 -518 C ATOM 812 O PRO A 102 7.741 36.715 16.819 1.00 13.19 O ANISOU 812 O PRO A 102 1203 2215 1592 -40 30 -515 O ATOM 813 CB PRO A 102 4.465 36.422 16.911 1.00 16.71 C ANISOU 813 CB PRO A 102 1387 2861 2102 -59 51 -666 C ATOM 814 CG PRO A 102 3.254 35.708 16.358 1.00 21.43 C ANISOU 814 CG PRO A 102 1892 3510 2742 -99 41 -700 C ATOM 815 CD PRO A 102 3.727 34.337 16.075 1.00 17.18 C ANISOU 815 CD PRO A 102 1413 2925 2189 -195 56 -616 C ATOM 816 N LEU A 103 7.109 34.693 17.636 1.00 13.91 N ANISOU 816 N LEU A 103 1252 2390 1646 -192 112 -469 N ATOM 817 CA LEU A 103 8.317 34.505 18.425 1.00 13.07 C ANISOU 817 CA LEU A 103 1225 2254 1487 -212 138 -415 C ATOM 818 C LEU A 103 9.478 34.110 17.525 1.00 13.11 C ANISOU 818 C LEU A 103 1327 2154 1502 -205 93 -358 C ATOM 819 O LEU A 103 10.588 34.617 17.697 1.00 12.36 O ANISOU 819 O LEU A 103 1291 2015 1391 -170 83 -343 O ATOM 820 CB LEU A 103 8.074 33.524 19.588 1.00 14.08 C ANISOU 820 CB LEU A 103 1340 2450 1562 -305 207 -378 C ATOM 821 CG LEU A 103 9.265 33.362 20.561 1.00 14.24 C ANISOU 821 CG LEU A 103 1440 2452 1516 -315 227 -328 C ATOM 822 CD1 LEU A 103 9.642 34.703 21.200 1.00 16.30 C ANISOU 822 CD1 LEU A 103 1693 2744 1756 -236 227 -390 C ATOM 823 CD2 LEU A 103 8.934 32.348 21.658 1.00 17.60 C ANISOU 823 CD2 LEU A 103 1863 2944 1880 -411 290 -274 C ATOM 824 N ILE A 104 9.224 33.243 16.533 1.00 12.62 N ANISOU 824 N ILE A 104 1270 2056 1467 -234 63 -336 N ATOM 825 CA ILE A 104 10.267 32.916 15.570 1.00 11.08 C ANISOU 825 CA ILE A 104 1155 1777 1277 -217 20 -299 C ATOM 826 C ILE A 104 10.730 34.200 14.899 1.00 11.84 C ANISOU 826 C ILE A 104 1275 1841 1383 -135 -13 -318 C ATOM 827 O ILE A 104 11.929 34.428 14.738 1.00 10.70 O ANISOU 827 O ILE A 104 1194 1647 1226 -116 -19 -289 O ATOM 828 CB ILE A 104 9.714 31.948 14.490 1.00 12.66 C ANISOU 828 CB ILE A 104 1345 1957 1510 -244 -17 -300 C ATOM 829 CG1 ILE A 104 9.337 30.602 15.100 1.00 13.55 C ANISOU 829 CG1 ILE A 104 1445 2076 1629 -338 9 -271 C ATOM 830 CG2 ILE A 104 10.762 31.801 13.346 1.00 12.31 C ANISOU 830 CG2 ILE A 104 1375 1844 1461 -207 -62 -280 C ATOM 831 CD1 ILE A 104 8.781 29.529 14.155 1.00 15.16 C ANISOU 831 CD1 ILE A 104 1633 2249 1877 -377 -33 -280 C ATOM 832 N LYS A 105 9.770 35.053 14.511 1.00 11.24 N ANISOU 832 N LYS A 105 1145 1793 1335 -86 -37 -365 N ATOM 833 CA LYS A 105 10.126 36.282 13.800 1.00 10.81 C ANISOU 833 CA LYS A 105 1122 1692 1293 -11 -78 -370 C ATOM 834 C LYS A 105 10.934 37.232 14.702 1.00 11.88 C ANISOU 834 C LYS A 105 1281 1808 1425 12 -56 -374 C ATOM 835 O LYS A 105 11.920 37.813 14.258 1.00 11.39 O ANISOU 835 O LYS A 105 1278 1684 1366 35 -72 -344 O ATOM 836 CB LYS A 105 8.834 36.941 13.296 1.00 13.29 C ANISOU 836 CB LYS A 105 1372 2035 1642 43 -121 -424 C ATOM 837 CG LYS A 105 9.045 38.196 12.461 1.00 14.81 C ANISOU 837 CG LYS A 105 1607 2170 1852 122 -178 -418 C ATOM 838 CD LYS A 105 7.743 38.766 11.907 1.00 15.30 C ANISOU 838 CD LYS A 105 1609 2255 1949 187 -238 -473 C ATOM 839 CE LYS A 105 7.158 37.812 10.900 1.00 14.40 C ANISOU 839 CE LYS A 105 1481 2165 1826 170 -271 -471 C ATOM 840 NZ LYS A 105 6.103 38.468 10.090 1.00 20.11 N1+ ANISOU 840 NZ LYS A 105 2168 2897 2578 249 -352 -515 N1+ ATOM 841 N SER A 106 10.515 37.381 15.963 1.00 11.02 N ANISOU 841 N SER A 106 1121 1759 1307 2 -18 -415 N ATOM 842 CA SER A 106 11.250 38.205 16.922 1.00 10.58 C ANISOU 842 CA SER A 106 1081 1693 1244 25 -3 -434 C ATOM 843 C SER A 106 12.669 37.675 17.096 1.00 11.37 C ANISOU 843 C SER A 106 1252 1750 1317 -11 11 -380 C ATOM 844 O SER A 106 13.640 38.448 17.070 1.00 11.07 O ANISOU 844 O SER A 106 1253 1658 1296 15 -3 -377 O ATOM 845 CB SER A 106 10.538 38.154 18.260 1.00 12.45 C ANISOU 845 CB SER A 106 1251 2026 1452 11 44 -487 C ATOM 846 OG SER A 106 11.287 38.877 19.236 1.00 12.13 O ANISOU 846 OG SER A 106 1228 1984 1397 36 53 -516 O ATOM 847 N TYR A 107 12.812 36.367 17.266 1.00 10.45 N ANISOU 847 N TYR A 107 1151 1652 1167 -70 34 -339 N ATOM 848 CA TYR A 107 14.140 35.804 17.431 1.00 10.27 C ANISOU 848 CA TYR A 107 1191 1589 1124 -93 37 -297 C ATOM 849 C TYR A 107 14.995 36.025 16.202 1.00 10.31 C ANISOU 849 C TYR A 107 1240 1525 1154 -72 7 -273 C ATOM 850 O TYR A 107 16.160 36.423 16.311 1.00 10.70 O ANISOU 850 O TYR A 107 1322 1538 1207 -62 5 -267 O ATOM 851 CB TYR A 107 14.084 34.317 17.786 1.00 11.61 C ANISOU 851 CB TYR A 107 1375 1775 1261 -155 53 -257 C ATOM 852 CG TYR A 107 13.662 33.970 19.195 1.00 10.48 C ANISOU 852 CG TYR A 107 1212 1700 1071 -191 94 -256 C ATOM 853 CD1 TYR A 107 13.565 34.947 20.182 1.00 12.16 C ANISOU 853 CD1 TYR A 107 1395 1965 1259 -160 114 -303 C ATOM 854 CD2 TYR A 107 13.369 32.657 19.547 1.00 11.79 C ANISOU 854 CD2 TYR A 107 1391 1878 1211 -259 110 -207 C ATOM 855 CE1 TYR A 107 13.245 34.607 21.493 1.00 12.57 C ANISOU 855 CE1 TYR A 107 1434 2096 1246 -192 156 -301 C ATOM 856 CE2 TYR A 107 13.018 32.316 20.851 1.00 13.00 C ANISOU 856 CE2 TYR A 107 1535 2099 1304 -301 153 -190 C ATOM 857 CZ TYR A 107 12.962 33.292 21.818 1.00 13.12 C ANISOU 857 CZ TYR A 107 1522 2183 1280 -267 180 -237 C ATOM 858 OH TYR A 107 12.649 32.920 23.108 1.00 14.69 O ANISOU 858 OH TYR A 107 1716 2465 1400 -308 227 -218 O ATOM 859 N LEU A 108 14.438 35.786 15.000 1.00 9.56 N ANISOU 859 N LEU A 108 1143 1418 1071 -67 -16 -262 N ATOM 860 CA LEU A 108 15.238 35.991 13.802 1.00 9.64 C ANISOU 860 CA LEU A 108 1196 1380 1086 -49 -36 -235 C ATOM 861 C LEU A 108 15.687 37.452 13.654 1.00 10.42 C ANISOU 861 C LEU A 108 1308 1440 1209 -12 -44 -237 C ATOM 862 O LEU A 108 16.848 37.736 13.320 1.00 10.49 O ANISOU 862 O LEU A 108 1353 1413 1222 -16 -38 -213 O ATOM 863 CB LEU A 108 14.468 35.530 12.577 1.00 9.87 C ANISOU 863 CB LEU A 108 1222 1417 1112 -42 -65 -230 C ATOM 864 CG LEU A 108 15.185 35.664 11.220 1.00 10.84 C ANISOU 864 CG LEU A 108 1391 1511 1217 -23 -83 -202 C ATOM 865 CD1 LEU A 108 16.395 34.734 11.148 1.00 12.94 C ANISOU 865 CD1 LEU A 108 1687 1766 1465 -50 -66 -190 C ATOM 866 CD2 LEU A 108 14.224 35.302 10.103 1.00 11.28 C ANISOU 866 CD2 LEU A 108 1438 1587 1262 -6 -121 -210 C ATOM 867 N PHE A 109 14.748 38.379 13.948 1.00 9.96 N ANISOU 867 N PHE A 109 1216 1390 1177 23 -60 -270 N ATOM 868 CA PHE A 109 15.029 39.805 13.871 1.00 9.89 C ANISOU 868 CA PHE A 109 1222 1328 1208 61 -80 -275 C ATOM 869 C PHE A 109 16.180 40.186 14.808 1.00 10.53 C ANISOU 869 C PHE A 109 1314 1385 1301 46 -59 -287 C ATOM 870 O PHE A 109 17.133 40.891 14.420 1.00 10.66 O ANISOU 870 O PHE A 109 1364 1342 1345 43 -63 -263 O ATOM 871 CB PHE A 109 13.731 40.539 14.222 1.00 12.34 C ANISOU 871 CB PHE A 109 1483 1659 1548 110 -107 -329 C ATOM 872 CG PHE A 109 13.793 42.032 14.106 1.00 14.12 C ANISOU 872 CG PHE A 109 1724 1814 1828 160 -147 -342 C ATOM 873 CD1 PHE A 109 13.973 42.637 12.863 1.00 15.69 C ANISOU 873 CD1 PHE A 109 1975 1944 2041 179 -185 -285 C ATOM 874 CD2 PHE A 109 13.520 42.836 15.205 1.00 16.81 C ANISOU 874 CD2 PHE A 109 2024 2158 2204 194 -153 -414 C ATOM 875 CE1 PHE A 109 13.965 44.037 12.736 1.00 19.45 C ANISOU 875 CE1 PHE A 109 2475 2337 2578 223 -231 -287 C ATOM 876 CE2 PHE A 109 13.541 44.238 15.078 1.00 20.26 C ANISOU 876 CE2 PHE A 109 2478 2512 2708 245 -203 -433 C ATOM 877 CZ PHE A 109 13.760 44.803 13.844 1.00 19.45 C ANISOU 877 CZ PHE A 109 2437 2325 2629 256 -243 -363 C ATOM 878 N GLN A 110 16.118 39.699 16.051 1.00 10.12 N ANISOU 878 N GLN A 110 1234 1386 1228 33 -35 -324 N ATOM 879 CA GLN A 110 17.149 39.991 17.043 1.00 9.65 C ANISOU 879 CA GLN A 110 1180 1316 1172 26 -25 -348 C ATOM 880 C GLN A 110 18.473 39.350 16.670 1.00 11.06 C ANISOU 880 C GLN A 110 1393 1469 1339 -8 -14 -308 C ATOM 881 O GLN A 110 19.517 40.009 16.819 1.00 11.02 O ANISOU 881 O GLN A 110 1397 1423 1367 -9 -18 -317 O ATOM 882 CB GLN A 110 16.689 39.450 18.380 1.00 10.52 C ANISOU 882 CB GLN A 110 1259 1503 1236 20 -3 -385 C ATOM 883 CG GLN A 110 15.553 40.270 19.019 1.00 11.55 C ANISOU 883 CG GLN A 110 1336 1675 1377 60 -6 -453 C ATOM 884 CD GLN A 110 15.214 39.649 20.337 1.00 11.05 C ANISOU 884 CD GLN A 110 1245 1705 1247 43 29 -480 C ATOM 885 NE2 GLN A 110 14.057 39.004 20.461 1.00 12.05 N ANISOU 885 NE2 GLN A 110 1332 1904 1342 22 57 -479 N ATOM 886 OE1 GLN A 110 16.047 39.709 21.281 1.00 12.50 O ANISOU 886 OE1 GLN A 110 1444 1901 1404 43 32 -500 O ATOM 887 N LEU A 111 18.467 38.131 16.136 1.00 10.10 N ANISOU 887 N LEU A 111 1286 1368 1183 -33 -5 -272 N ATOM 888 CA LEU A 111 19.715 37.504 15.734 1.00 10.26 C ANISOU 888 CA LEU A 111 1332 1370 1197 -53 0 -249 C ATOM 889 C LEU A 111 20.351 38.257 14.565 1.00 10.96 C ANISOU 889 C LEU A 111 1436 1414 1313 -54 2 -224 C ATOM 890 O LEU A 111 21.576 38.408 14.524 1.00 11.12 O ANISOU 890 O LEU A 111 1459 1416 1350 -68 13 -225 O ATOM 891 CB LEU A 111 19.461 36.043 15.389 1.00 11.13 C ANISOU 891 CB LEU A 111 1453 1503 1272 -72 -1 -227 C ATOM 892 CG LEU A 111 19.059 35.207 16.612 1.00 13.12 C ANISOU 892 CG LEU A 111 1701 1790 1493 -89 1 -233 C ATOM 893 CD1 LEU A 111 18.579 33.870 16.191 1.00 16.10 C ANISOU 893 CD1 LEU A 111 2090 2171 1854 -114 -7 -208 C ATOM 894 CD2 LEU A 111 20.195 35.044 17.573 1.00 17.65 C ANISOU 894 CD2 LEU A 111 2288 2361 2058 -87 -5 -246 C ATOM 895 N LEU A 112 19.528 38.720 13.610 1.00 9.98 N ANISOU 895 N LEU A 112 1322 1279 1191 -39 -8 -199 N ATOM 896 CA LEU A 112 20.053 39.512 12.515 1.00 10.34 C ANISOU 896 CA LEU A 112 1394 1284 1250 -44 -5 -159 C ATOM 897 C LEU A 112 20.671 40.818 13.031 1.00 10.99 C ANISOU 897 C LEU A 112 1473 1310 1392 -48 -6 -168 C ATOM 898 O LEU A 112 21.650 41.297 12.478 1.00 11.68 O ANISOU 898 O LEU A 112 1575 1365 1498 -77 13 -138 O ATOM 899 CB LEU A 112 18.984 39.794 11.447 1.00 10.38 C ANISOU 899 CB LEU A 112 1419 1287 1239 -19 -30 -127 C ATOM 900 CG LEU A 112 18.590 38.569 10.645 1.00 10.36 C ANISOU 900 CG LEU A 112 1421 1332 1183 -19 -32 -119 C ATOM 901 CD1 LEU A 112 17.296 38.845 9.906 1.00 12.66 C ANISOU 901 CD1 LEU A 112 1718 1630 1464 16 -72 -109 C ATOM 902 CD2 LEU A 112 19.703 38.256 9.625 1.00 11.29 C ANISOU 902 CD2 LEU A 112 1565 1459 1266 -41 -6 -87 C ATOM 903 N GLN A 113 20.087 41.434 14.076 1.00 10.52 N ANISOU 903 N GLN A 113 1392 1240 1365 -22 -27 -216 N ATOM 904 CA GLN A 113 20.679 42.635 14.656 1.00 11.29 C ANISOU 904 CA GLN A 113 1483 1276 1528 -23 -39 -242 C ATOM 905 C GLN A 113 22.057 42.310 15.243 1.00 11.93 C ANISOU 905 C GLN A 113 1547 1366 1618 -56 -18 -266 C ATOM 906 O GLN A 113 22.982 43.100 15.051 1.00 12.07 O ANISOU 906 O GLN A 113 1566 1330 1690 -84 -13 -259 O ATOM 907 CB GLN A 113 19.780 43.198 15.763 1.00 12.46 C ANISOU 907 CB GLN A 113 1602 1431 1700 22 -68 -312 C ATOM 908 CG GLN A 113 18.544 43.896 15.209 1.00 13.14 C ANISOU 908 CG GLN A 113 1696 1490 1808 66 -104 -305 C ATOM 909 CD GLN A 113 17.709 44.345 16.354 1.00 15.12 C ANISOU 909 CD GLN A 113 1902 1767 2076 114 -125 -392 C ATOM 910 NE2 GLN A 113 16.513 43.833 16.417 1.00 17.57 N ANISOU 910 NE2 GLN A 113 2183 2144 2349 140 -125 -411 N ATOM 911 OE1 GLN A 113 18.178 45.082 17.228 1.00 16.69 O ANISOU 911 OE1 GLN A 113 2087 1937 2319 125 -139 -450 O ATOM 912 N GLY A 114 22.201 41.188 15.933 1.00 11.47 N ANISOU 912 N GLY A 114 1475 1371 1513 -55 -9 -292 N ATOM 913 CA GLY A 114 23.505 40.817 16.497 1.00 11.88 C ANISOU 913 CA GLY A 114 1509 1433 1571 -73 -2 -321 C ATOM 914 C GLY A 114 24.510 40.567 15.383 1.00 13.06 C ANISOU 914 C GLY A 114 1663 1573 1727 -109 26 -282 C ATOM 915 O GLY A 114 25.673 40.988 15.490 1.00 13.08 O ANISOU 915 O GLY A 114 1641 1555 1774 -135 34 -302 O ATOM 916 N LEU A 115 24.105 39.870 14.308 1.00 11.05 N ANISOU 916 N LEU A 115 1431 1342 1427 -112 41 -235 N ATOM 917 CA LEU A 115 25.011 39.644 13.201 1.00 11.93 C ANISOU 917 CA LEU A 115 1541 1463 1529 -142 74 -206 C ATOM 918 C LEU A 115 25.373 40.951 12.517 1.00 12.25 C ANISOU 918 C LEU A 115 1589 1452 1614 -176 95 -165 C ATOM 919 O LEU A 115 26.554 41.153 12.187 1.00 13.16 O ANISOU 919 O LEU A 115 1680 1568 1753 -217 128 -164 O ATOM 920 CB LEU A 115 24.406 38.703 12.153 1.00 11.45 C ANISOU 920 CB LEU A 115 1505 1441 1405 -130 80 -173 C ATOM 921 CG LEU A 115 24.310 37.225 12.510 1.00 14.29 C ANISOU 921 CG LEU A 115 1861 1841 1729 -110 63 -204 C ATOM 922 CD1 LEU A 115 23.870 36.436 11.290 1.00 14.45 C ANISOU 922 CD1 LEU A 115 1900 1892 1700 -103 66 -183 C ATOM 923 CD2 LEU A 115 25.601 36.665 13.060 1.00 17.65 C ANISOU 923 CD2 LEU A 115 2256 2279 2170 -113 64 -248 C ATOM 924 N ALA A 116 24.391 41.842 12.278 1.00 11.72 N ANISOU 924 N ALA A 116 1554 1337 1561 -163 74 -130 N ATOM 925 CA ALA A 116 24.714 43.086 11.583 1.00 12.12 C ANISOU 925 CA ALA A 116 1628 1322 1656 -199 85 -75 C ATOM 926 C ALA A 116 25.749 43.866 12.371 1.00 14.17 C ANISOU 926 C ALA A 116 1851 1532 2000 -236 88 -114 C ATOM 927 O ALA A 116 26.670 44.445 11.777 1.00 14.02 O ANISOU 927 O ALA A 116 1827 1485 2016 -296 124 -76 O ATOM 928 CB ALA A 116 23.475 43.935 11.383 1.00 14.47 C ANISOU 928 CB ALA A 116 1967 1563 1969 -164 41 -44 C ATOM 929 N PHE A 117 25.624 43.866 13.725 1.00 12.86 N ANISOU 929 N PHE A 117 1656 1365 1866 -203 52 -194 N ATOM 930 CA PHE A 117 26.589 44.579 14.558 1.00 13.06 C ANISOU 930 CA PHE A 117 1641 1348 1973 -229 42 -250 C ATOM 931 C PHE A 117 27.971 43.938 14.421 1.00 13.15 C ANISOU 931 C PHE A 117 1606 1407 1982 -270 81 -268 C ATOM 932 O PHE A 117 28.962 44.640 14.160 1.00 13.50 O ANISOU 932 O PHE A 117 1622 1413 2093 -330 105 -263 O ATOM 933 CB PHE A 117 26.116 44.522 16.028 1.00 14.14 C ANISOU 933 CB PHE A 117 1758 1500 2114 -173 -5 -339 C ATOM 934 CG PHE A 117 27.163 45.003 17.006 1.00 14.82 C ANISOU 934 CG PHE A 117 1797 1565 2268 -188 -25 -417 C ATOM 935 CD1 PHE A 117 27.386 46.356 17.199 1.00 17.14 C ANISOU 935 CD1 PHE A 117 2083 1765 2664 -209 -51 -441 C ATOM 936 CD2 PHE A 117 27.961 44.097 17.688 1.00 16.98 C ANISOU 936 CD2 PHE A 117 2034 1905 2511 -180 -27 -470 C ATOM 937 CE1 PHE A 117 28.399 46.797 18.074 1.00 18.57 C ANISOU 937 CE1 PHE A 117 2213 1926 2916 -226 -76 -525 C ATOM 938 CE2 PHE A 117 28.973 44.530 18.535 1.00 19.38 C ANISOU 938 CE2 PHE A 117 2289 2195 2878 -190 -53 -549 C ATOM 939 CZ PHE A 117 29.217 45.871 18.687 1.00 18.32 C ANISOU 939 CZ PHE A 117 2140 1973 2847 -217 -74 -578 C ATOM 940 N CYS A 118 28.087 42.631 14.661 1.00 12.31 N ANISOU 940 N CYS A 118 1487 1381 1811 -240 84 -297 N ATOM 941 CA ACYS A 118 29.401 42.004 14.578 0.60 11.50 C ANISOU 941 CA ACYS A 118 1332 1324 1713 -264 109 -331 C ATOM 942 CA BCYS A 118 29.448 42.084 14.592 0.40 15.68 C ANISOU 942 CA BCYS A 118 1859 1849 2248 -267 109 -332 C ATOM 943 C CYS A 118 30.028 42.124 13.194 1.00 14.63 C ANISOU 943 C CYS A 118 1720 1735 2103 -322 173 -274 C ATOM 944 O CYS A 118 31.220 42.407 13.050 1.00 14.27 O ANISOU 944 O CYS A 118 1618 1697 2107 -372 205 -296 O ATOM 945 CB ACYS A 118 29.346 40.554 15.052 0.60 10.76 C ANISOU 945 CB ACYS A 118 1237 1297 1554 -213 86 -368 C ATOM 946 CB BCYS A 118 29.489 40.677 15.141 0.40 19.02 C ANISOU 946 CB BCYS A 118 2276 2339 2612 -217 85 -375 C ATOM 947 SG ACYS A 118 29.001 40.372 16.841 0.60 13.78 S ANISOU 947 SG ACYS A 118 1620 1683 1932 -158 20 -437 S ATOM 948 SG BCYS A 118 28.500 39.541 14.175 0.40 24.80 S ANISOU 948 SG BCYS A 118 3059 3114 3252 -191 99 -318 S ATOM 949 N HIS A 119 29.210 41.871 12.176 1.00 12.20 N ANISOU 949 N HIS A 119 1464 1442 1729 -314 192 -204 N ATOM 950 CA HIS A 119 29.699 41.949 10.800 1.00 11.98 C ANISOU 950 CA HIS A 119 1439 1446 1669 -364 256 -143 C ATOM 951 C HIS A 119 30.191 43.351 10.438 1.00 15.76 C ANISOU 951 C HIS A 119 1916 1856 2215 -441 288 -89 C ATOM 952 O HIS A 119 31.172 43.489 9.698 1.00 16.37 O ANISOU 952 O HIS A 119 1958 1968 2294 -506 353 -66 O ATOM 953 CB HIS A 119 28.609 41.474 9.834 1.00 11.92 C ANISOU 953 CB HIS A 119 1493 1465 1570 -331 255 -83 C ATOM 954 CG HIS A 119 28.317 40.015 9.952 1.00 11.35 C ANISOU 954 CG HIS A 119 1416 1459 1439 -275 234 -132 C ATOM 955 CD2 HIS A 119 28.955 39.057 10.668 1.00 12.32 C ANISOU 955 CD2 HIS A 119 1494 1617 1570 -250 218 -208 C ATOM 956 ND1 HIS A 119 27.279 39.445 9.261 1.00 12.66 N ANISOU 956 ND1 HIS A 119 1627 1648 1534 -240 219 -101 N ATOM 957 CE1 HIS A 119 27.302 38.153 9.568 1.00 11.64 C ANISOU 957 CE1 HIS A 119 1482 1562 1379 -202 197 -157 C ATOM 958 NE2 HIS A 119 28.291 37.868 10.421 1.00 11.38 N ANISOU 958 NE2 HIS A 119 1399 1534 1390 -203 193 -218 N ATOM 959 N SER A 120 29.559 44.409 11.035 1.00 14.76 N ANISOU 959 N SER A 120 1822 1631 2154 -436 241 -77 N ATOM 960 CA SER A 120 29.992 45.800 10.790 1.00 14.62 C ANISOU 960 CA SER A 120 1811 1520 2223 -511 256 -26 C ATOM 961 C SER A 120 31.396 46.047 11.350 1.00 18.23 C ANISOU 961 C SER A 120 2182 1977 2768 -572 279 -92 C ATOM 962 O SER A 120 32.069 46.970 10.886 1.00 19.96 O ANISOU 962 O SER A 120 2390 2143 3052 -661 318 -43 O ATOM 963 CB SER A 120 28.990 46.797 11.356 1.00 18.18 C ANISOU 963 CB SER A 120 2312 1861 2734 -476 185 -20 C ATOM 964 OG SER A 120 29.082 46.950 12.762 1.00 19.00 O ANISOU 964 OG SER A 120 2373 1939 2905 -442 132 -126 O ATOM 965 N HIS A 121 31.843 45.216 12.311 1.00 15.88 N ANISOU 965 N HIS A 121 1824 1738 2472 -527 254 -198 N ATOM 966 CA HIS A 121 33.171 45.290 12.924 1.00 18.23 C ANISOU 966 CA HIS A 121 2029 2050 2848 -566 262 -282 C ATOM 967 C HIS A 121 34.093 44.225 12.339 1.00 20.92 C ANISOU 967 C HIS A 121 2308 2505 3135 -576 318 -307 C ATOM 968 O HIS A 121 35.164 43.954 12.872 1.00 21.83 O ANISOU 968 O HIS A 121 2336 2659 3299 -584 316 -396 O ATOM 969 CB HIS A 121 33.046 45.162 14.448 1.00 18.47 C ANISOU 969 CB HIS A 121 2038 2066 2913 -497 180 -389 C ATOM 970 CG HIS A 121 32.394 46.351 15.081 1.00 21.98 C ANISOU 970 CG HIS A 121 2519 2403 3430 -493 126 -394 C ATOM 971 CD2 HIS A 121 31.142 46.504 15.565 1.00 22.75 C ANISOU 971 CD2 HIS A 121 2676 2469 3499 -425 75 -393 C ATOM 972 ND1 HIS A 121 33.065 47.560 15.192 1.00 26.25 N ANISOU 972 ND1 HIS A 121 3026 2855 4094 -566 124 -406 N ATOM 973 CE1 HIS A 121 32.204 48.398 15.738 1.00 25.74 C ANISOU 973 CE1 HIS A 121 3008 2701 4072 -532 63 -416 C ATOM 974 NE2 HIS A 121 31.036 47.817 15.982 1.00 24.74 N ANISOU 974 NE2 HIS A 121 2934 2612 3855 -445 35 -412 N ATOM 975 N ARG A 122 33.628 43.571 11.255 1.00 18.31 N ANISOU 975 N ARG A 122 2021 2234 2702 -563 360 -241 N ATOM 976 CA ARG A 122 34.384 42.545 10.519 1.00 18.44 C ANISOU 976 CA ARG A 122 1985 2366 2657 -563 416 -267 C ATOM 977 C ARG A 122 34.668 41.302 11.388 1.00 21.64 C ANISOU 977 C ARG A 122 2349 2825 3050 -479 360 -376 C ATOM 978 O ARG A 122 35.685 40.619 11.205 1.00 24.11 O ANISOU 978 O ARG A 122 2583 3215 3361 -476 385 -443 O ATOM 979 CB ARG A 122 35.655 43.150 9.857 1.00 22.57 C ANISOU 979 CB ARG A 122 2428 2919 3227 -668 503 -258 C ATOM 980 CG ARG A 122 35.333 44.375 9.000 1.00 27.15 C ANISOU 980 CG ARG A 122 3068 3433 3816 -758 553 -128 C ATOM 981 CD ARG A 122 36.538 45.309 8.816 1.00 40.58 C ANISOU 981 CD ARG A 122 4690 5118 5611 -882 620 -119 C ATOM 982 NE ARG A 122 37.137 45.740 10.089 1.00 48.95 N ANISOU 982 NE ARG A 122 5679 6116 6804 -888 563 -220 N ATOM 983 CZ ARG A 122 36.693 46.743 10.846 1.00 61.01 C ANISOU 983 CZ ARG A 122 7245 7512 8423 -896 499 -213 C ATOM 984 NH1 ARG A 122 35.626 47.443 10.478 1.00 45.09 N1+ ANISOU 984 NH1 ARG A 122 5339 5403 6389 -896 479 -108 N1+ ATOM 985 NH2 ARG A 122 37.310 47.048 11.980 1.00 50.72 N ANISOU 985 NH2 ARG A 122 5870 6170 7230 -896 445 -320 N ATOM 986 N VAL A 123 33.763 40.990 12.315 1.00 17.64 N ANISOU 986 N VAL A 123 1895 2279 2529 -408 284 -393 N ATOM 987 CA VAL A 123 33.867 39.806 13.180 1.00 16.93 C ANISOU 987 CA VAL A 123 1791 2225 2416 -329 223 -472 C ATOM 988 C VAL A 123 32.793 38.815 12.746 1.00 17.37 C ANISOU 988 C VAL A 123 1918 2302 2381 -275 208 -432 C ATOM 989 O VAL A 123 31.607 39.154 12.702 1.00 16.82 O ANISOU 989 O VAL A 123 1916 2191 2283 -268 196 -372 O ATOM 990 CB VAL A 123 33.772 40.152 14.690 1.00 19.52 C ANISOU 990 CB VAL A 123 2119 2505 2794 -297 149 -526 C ATOM 991 CG1 VAL A 123 33.802 38.889 15.567 1.00 19.78 C ANISOU 991 CG1 VAL A 123 2157 2573 2786 -216 82 -585 C ATOM 992 CG2 VAL A 123 34.910 41.107 15.100 1.00 20.35 C ANISOU 992 CG2 VAL A 123 2142 2587 3002 -351 154 -583 C ATOM 993 N LEU A 124 33.224 37.608 12.418 1.00 16.45 N ANISOU 993 N LEU A 124 1778 2247 2226 -236 204 -474 N ATOM 994 CA LEU A 124 32.341 36.529 11.989 1.00 16.53 C ANISOU 994 CA LEU A 124 1845 2274 2161 -188 184 -453 C ATOM 995 C LEU A 124 32.159 35.572 13.170 1.00 15.93 C ANISOU 995 C LEU A 124 1788 2180 2086 -124 103 -497 C ATOM 996 O LEU A 124 33.021 35.465 14.039 1.00 16.98 O ANISOU 996 O LEU A 124 1876 2314 2261 -105 67 -560 O ATOM 997 CB LEU A 124 33.027 35.747 10.823 1.00 19.47 C ANISOU 997 CB LEU A 124 2177 2724 2496 -181 225 -484 C ATOM 998 CG LEU A 124 33.096 36.338 9.417 1.00 25.04 C ANISOU 998 CG LEU A 124 2879 3476 3160 -236 311 -430 C ATOM 999 CD1 LEU A 124 34.024 37.541 9.336 1.00 28.12 C ANISOU 999 CD1 LEU A 124 3211 3867 3607 -316 373 -418 C ATOM 1000 CD2 LEU A 124 33.626 35.310 8.461 1.00 25.63 C ANISOU 1000 CD2 LEU A 124 2916 3639 3181 -206 336 -484 C ATOM 1001 N HIS A 125 31.051 34.808 13.189 1.00 13.64 N ANISOU 1001 N HIS A 125 1562 1874 1746 -92 71 -464 N ATOM 1002 CA HIS A 125 30.885 33.774 14.209 1.00 13.26 C ANISOU 1002 CA HIS A 125 1541 1808 1689 -41 -1 -489 C ATOM 1003 C HIS A 125 31.514 32.477 13.682 1.00 16.06 C ANISOU 1003 C HIS A 125 1878 2188 2035 1 -25 -540 C ATOM 1004 O HIS A 125 32.420 31.904 14.325 1.00 16.44 O ANISOU 1004 O HIS A 125 1897 2238 2112 42 -75 -601 O ATOM 1005 CB HIS A 125 29.414 33.572 14.587 1.00 13.59 C ANISOU 1005 CB HIS A 125 1652 1818 1691 -38 -21 -431 C ATOM 1006 CG HIS A 125 29.259 32.591 15.723 1.00 13.46 C ANISOU 1006 CG HIS A 125 1670 1783 1662 -2 -88 -440 C ATOM 1007 CD2 HIS A 125 28.831 32.824 16.996 1.00 15.56 C ANISOU 1007 CD2 HIS A 125 1961 2036 1914 2 -116 -427 C ATOM 1008 ND1 HIS A 125 29.657 31.292 15.622 1.00 13.55 N ANISOU 1008 ND1 HIS A 125 1691 1788 1669 36 -133 -466 N ATOM 1009 CE1 HIS A 125 29.441 30.742 16.819 1.00 13.85 C ANISOU 1009 CE1 HIS A 125 1770 1800 1691 56 -189 -453 C ATOM 1010 NE2 HIS A 125 28.918 31.630 17.659 1.00 14.58 N ANISOU 1010 NE2 HIS A 125 1872 1898 1769 35 -175 -428 N ATOM 1011 N ARG A 126 31.024 32.009 12.515 1.00 13.08 N ANISOU 1011 N ARG A 126 1519 1831 1621 1 0 -522 N ATOM 1012 CA AARG A 126 31.556 30.821 11.817 0.50 13.67 C ANISOU 1012 CA AARG A 126 1573 1934 1687 46 -21 -583 C ATOM 1013 CA BARG A 126 31.428 30.832 11.748 0.50 14.88 C ANISOU 1013 CA BARG A 126 1733 2086 1836 43 -18 -576 C ATOM 1014 C ARG A 126 30.948 29.482 12.261 1.00 14.42 C ANISOU 1014 C ARG A 126 1726 1976 1777 91 -101 -584 C ATOM 1015 O ARG A 126 31.053 28.479 11.525 1.00 15.39 O ANISOU 1015 O ARG A 126 1848 2107 1893 128 -125 -629 O ATOM 1016 CB AARG A 126 33.107 30.753 11.873 0.50 13.88 C ANISOU 1016 CB AARG A 126 1515 2003 1756 68 -19 -671 C ATOM 1017 CB BARG A 126 32.897 30.881 11.280 0.50 20.42 C ANISOU 1017 CB BARG A 126 2345 2850 2563 54 12 -657 C ATOM 1018 CG AARG A 126 33.851 31.982 11.306 0.50 23.98 C ANISOU 1018 CG AARG A 126 2724 3339 3049 9 69 -673 C ATOM 1019 CG BARG A 126 33.838 29.823 11.821 0.50 27.83 C ANISOU 1019 CG BARG A 126 3249 3784 3541 122 -61 -747 C ATOM 1020 CD AARG A 126 35.269 32.129 11.862 0.50 33.75 C ANISOU 1020 CD AARG A 126 3870 4604 4349 20 59 -758 C ATOM 1021 CD BARG A 126 34.374 28.936 10.716 0.50 25.19 C ANISOU 1021 CD BARG A 126 2873 3505 3194 166 -55 -825 C ATOM 1022 NE AARG A 126 36.084 33.037 11.050 0.50 39.45 N ANISOU 1022 NE AARG A 126 4511 5393 5085 -43 154 -770 N ATOM 1023 NE BARG A 126 33.608 27.701 10.573 0.50 21.96 N ANISOU 1023 NE BARG A 126 2530 3044 2769 213 -124 -826 N ATOM 1024 CZ AARG A 126 36.330 34.310 11.345 0.50 47.54 C ANISOU 1024 CZ AARG A 126 5510 6404 6151 -113 196 -738 C ATOM 1025 CZ BARG A 126 34.126 26.550 10.148 0.50 32.07 C ANISOU 1025 CZ BARG A 126 3787 4332 4065 283 -176 -918 C ATOM 1026 NH1AARG A 126 35.847 34.847 12.457 0.50 39.79 N1+ ANISOU 1026 NH1AARG A 126 4571 5349 5199 -117 149 -707 N1+ ATOM 1027 NH1BARG A 126 35.411 26.469 9.824 0.50 24.16 N1+ ANISOU 1027 NH1BARG A 126 2689 3400 3088 319 -161 -1021 N1+ ATOM 1028 NH2AARG A 126 37.071 35.054 10.532 0.50 24.91 N ANISOU 1028 NH2AARG A 126 2572 3595 3297 -181 287 -739 N ATOM 1029 NH2BARG A 126 33.370 25.468 10.067 0.50 22.54 N ANISOU 1029 NH2BARG A 126 2647 3060 2857 318 -246 -914 N ATOM 1030 N ASP A 127 30.364 29.440 13.458 1.00 13.96 N ANISOU 1030 N ASP A 127 1716 1866 1722 87 -144 -541 N ATOM 1031 CA ASP A 127 29.818 28.169 13.933 1.00 13.49 C ANISOU 1031 CA ASP A 127 1716 1750 1660 116 -217 -528 C ATOM 1032 C ASP A 127 28.503 28.376 14.639 1.00 14.07 C ANISOU 1032 C ASP A 127 1846 1792 1707 76 -216 -447 C ATOM 1033 O ASP A 127 28.268 27.818 15.734 1.00 14.78 O ANISOU 1033 O ASP A 127 1981 1842 1792 83 -267 -418 O ATOM 1034 CB ASP A 127 30.818 27.398 14.810 1.00 15.23 C ANISOU 1034 CB ASP A 127 1933 1941 1912 171 -296 -576 C ATOM 1035 CG ASP A 127 30.445 25.948 15.082 1.00 18.36 C ANISOU 1035 CG ASP A 127 2395 2266 2316 204 -380 -564 C ATOM 1036 OD1 ASP A 127 29.672 25.367 14.287 1.00 17.98 O ANISOU 1036 OD1 ASP A 127 2372 2198 2263 192 -378 -552 O ATOM 1037 OD2 ASP A 127 30.889 25.401 16.129 1.00 21.63 O1- ANISOU 1037 OD2 ASP A 127 2840 2637 2742 240 -455 -564 O1- ATOM 1038 N LEU A 128 27.589 29.115 14.007 1.00 12.63 N ANISOU 1038 N LEU A 128 1665 1631 1502 37 -160 -408 N ATOM 1039 CA LEU A 128 26.284 29.306 14.609 1.00 12.55 C ANISOU 1039 CA LEU A 128 1693 1603 1471 3 -156 -346 C ATOM 1040 C LEU A 128 25.511 28.031 14.583 1.00 12.31 C ANISOU 1040 C LEU A 128 1706 1532 1439 0 -199 -325 C ATOM 1041 O LEU A 128 25.510 27.301 13.590 1.00 13.20 O ANISOU 1041 O LEU A 128 1818 1635 1561 15 -216 -354 O ATOM 1042 CB LEU A 128 25.481 30.328 13.828 1.00 14.26 C ANISOU 1042 CB LEU A 128 1897 1849 1672 -26 -100 -320 C ATOM 1043 CG LEU A 128 25.951 31.739 14.052 1.00 19.77 C ANISOU 1043 CG LEU A 128 2564 2566 2381 -37 -60 -321 C ATOM 1044 CD1 LEU A 128 25.179 32.681 13.148 1.00 21.46 C ANISOU 1044 CD1 LEU A 128 2777 2794 2583 -59 -18 -289 C ATOM 1045 CD2 LEU A 128 25.843 32.122 15.537 1.00 20.12 C ANISOU 1045 CD2 LEU A 128 2616 2600 2427 -40 -76 -314 C ATOM 1046 N LYS A 129 24.769 27.768 15.661 1.00 12.45 N ANISOU 1046 N LYS A 129 1761 1527 1442 -26 -216 -274 N ATOM 1047 CA ALYS A 129 23.957 26.571 15.820 0.60 12.02 C ANISOU 1047 CA ALYS A 129 1751 1424 1393 -49 -254 -239 C ATOM 1048 CA BLYS A 129 23.922 26.593 15.785 0.40 11.37 C ANISOU 1048 CA BLYS A 129 1667 1342 1309 -50 -252 -239 C ATOM 1049 C LYS A 129 22.966 26.838 16.940 1.00 11.71 C ANISOU 1049 C LYS A 129 1732 1398 1320 -96 -232 -176 C ATOM 1050 O LYS A 129 23.251 27.712 17.792 1.00 11.37 O ANISOU 1050 O LYS A 129 1678 1391 1249 -90 -210 -173 O ATOM 1051 CB ALYS A 129 24.846 25.335 16.123 0.60 13.69 C ANISOU 1051 CB ALYS A 129 1999 1573 1631 -11 -331 -257 C ATOM 1052 CB BLYS A 129 24.758 25.313 15.980 0.40 12.34 C ANISOU 1052 CB BLYS A 129 1825 1402 1461 -13 -329 -258 C ATOM 1053 CG ALYS A 129 25.588 25.394 17.468 0.60 17.77 C ANISOU 1053 CG ALYS A 129 2539 2084 2128 10 -363 -240 C ATOM 1054 CG BLYS A 129 25.690 25.389 17.157 0.40 10.49 C ANISOU 1054 CG BLYS A 129 1608 1164 1215 16 -361 -255 C ATOM 1055 CD ALYS A 129 26.643 24.292 17.627 0.60 15.68 C ANISOU 1055 CD ALYS A 129 2303 1758 1897 67 -452 -272 C ATOM 1056 CD BLYS A 129 26.890 24.499 16.952 0.40 13.54 C ANISOU 1056 CD BLYS A 129 1998 1506 1640 81 -435 -313 C ATOM 1057 CE ALYS A 129 27.925 24.639 16.933 0.60 20.21 C ANISOU 1057 CE ALYS A 129 2814 2366 2501 127 -453 -367 C ATOM 1058 CE BLYS A 129 27.791 24.585 18.156 0.40 12.99 C ANISOU 1058 CE BLYS A 129 1944 1434 1557 117 -479 -313 C ATOM 1059 NZ ALYS A 129 29.019 23.688 17.296 0.60 17.56 N1+ ANISOU 1059 NZ ALYS A 129 2494 1978 2199 196 -547 -410 N1+ ATOM 1060 NZ BLYS A 129 28.998 23.723 18.007 0.40 15.84 N1+ ANISOU 1060 NZ BLYS A 129 2302 1753 1964 192 -563 -380 N1+ ATOM 1061 N PRO A 130 21.846 26.105 17.026 1.00 11.14 N ANISOU 1061 N PRO A 130 1683 1302 1249 -144 -237 -132 N ATOM 1062 CA PRO A 130 20.893 26.391 18.107 1.00 11.78 C ANISOU 1062 CA PRO A 130 1771 1417 1290 -194 -201 -76 C ATOM 1063 C PRO A 130 21.492 26.348 19.499 1.00 13.01 C ANISOU 1063 C PRO A 130 1965 1578 1401 -185 -218 -45 C ATOM 1064 O PRO A 130 21.062 27.147 20.351 1.00 13.30 O ANISOU 1064 O PRO A 130 1987 1677 1389 -200 -175 -32 O ATOM 1065 CB PRO A 130 19.805 25.349 17.887 1.00 13.27 C ANISOU 1065 CB PRO A 130 1975 1565 1500 -253 -212 -37 C ATOM 1066 CG PRO A 130 19.829 25.084 16.390 1.00 14.95 C ANISOU 1066 CG PRO A 130 2165 1753 1762 -230 -234 -91 C ATOM 1067 CD PRO A 130 21.291 25.119 16.075 1.00 12.61 C ANISOU 1067 CD PRO A 130 1877 1441 1474 -161 -266 -139 C ATOM 1068 N GLN A 131 22.497 25.511 19.727 1.00 12.81 N ANISOU 1068 N GLN A 131 1984 1495 1388 -150 -285 -45 N ATOM 1069 CA AGLN A 131 23.099 25.421 21.071 0.50 13.12 C ANISOU 1069 CA AGLN A 131 2068 1541 1377 -133 -316 -14 C ATOM 1070 CA BGLN A 131 23.215 25.338 20.982 0.50 15.01 C ANISOU 1070 CA BGLN A 131 2309 1772 1624 -127 -323 -19 C ATOM 1071 C GLN A 131 23.881 26.654 21.472 1.00 14.71 C ANISOU 1071 C GLN A 131 2229 1804 1556 -87 -297 -70 C ATOM 1072 O GLN A 131 24.104 26.840 22.690 1.00 16.93 O ANISOU 1072 O GLN A 131 2538 2118 1779 -77 -310 -49 O ATOM 1073 CB AGLN A 131 23.992 24.187 21.204 0.50 14.41 C ANISOU 1073 CB AGLN A 131 2292 1617 1567 -96 -409 -4 C ATOM 1074 CB BGLN A 131 24.250 24.211 20.760 0.50 17.33 C ANISOU 1074 CB BGLN A 131 2644 1979 1960 -78 -414 -34 C ATOM 1075 CG AGLN A 131 23.277 22.861 21.383 0.50 20.08 C ANISOU 1075 CG AGLN A 131 3079 2255 2295 -149 -445 77 C ATOM 1076 CG BGLN A 131 23.635 22.807 20.536 0.50 31.80 C ANISOU 1076 CG BGLN A 131 4535 3720 3828 -119 -459 22 C ATOM 1077 CD AGLN A 131 24.267 21.747 21.675 0.50 40.27 C ANISOU 1077 CD AGLN A 131 5705 4717 4880 -97 -553 86 C ATOM 1078 CD BGLN A 131 23.001 22.443 19.185 0.50 33.78 C ANISOU 1078 CD BGLN A 131 4753 3940 4140 -141 -448 -11 C ATOM 1079 NE2AGLN A 131 23.901 20.870 22.600 0.50 40.80 N ANISOU 1079 NE2AGLN A 131 5859 4729 4914 -140 -592 188 N ATOM 1080 NE2BGLN A 131 22.413 21.250 19.151 0.50 34.42 N ANISOU 1080 NE2BGLN A 131 4885 3936 4258 -186 -491 38 N ATOM 1081 OE1AGLN A 131 25.361 21.651 21.081 0.50 31.10 O ANISOU 1081 OE1AGLN A 131 4519 3531 3768 -20 -605 4 O ATOM 1082 OE1BGLN A 131 23.057 23.147 18.156 0.50 15.50 O ANISOU 1082 OE1BGLN A 131 2375 1672 1845 -119 -409 -79 O ATOM 1083 N AASN A 132 24.227 27.534 20.486 0.50 12.87 N ANISOU 1083 N AASN A 132 1933 1591 1366 -64 -266 -136 N ATOM 1084 N BASN A 132 24.283 27.529 20.565 0.50 11.20 N ANISOU 1084 N BASN A 132 1723 1380 1152 -62 -269 -136 N ATOM 1085 CA AASN A 132 24.950 28.820 20.621 0.50 12.52 C ANISOU 1085 CA AASN A 132 1839 1593 1326 -33 -244 -194 C ATOM 1086 CA BASN A 132 24.915 28.770 21.024 0.50 10.22 C ANISOU 1086 CA BASN A 132 1559 1307 1018 -33 -250 -184 C ATOM 1087 C AASN A 132 24.007 30.020 20.618 0.50 11.98 C ANISOU 1087 C AASN A 132 1734 1575 1244 -61 -178 -195 C ATOM 1088 C BASN A 132 24.011 30.005 20.907 0.50 11.33 C ANISOU 1088 C BASN A 132 1657 1497 1149 -60 -182 -192 C ATOM 1089 O AASN A 132 24.461 31.148 20.439 0.50 11.08 O ANISOU 1089 O AASN A 132 1576 1480 1152 -44 -157 -242 O ATOM 1090 O BASN A 132 24.493 31.128 21.029 0.50 11.14 O ANISOU 1090 O BASN A 132 1595 1499 1139 -40 -166 -239 O ATOM 1091 CB AASN A 132 25.938 29.004 19.460 0.50 16.58 C ANISOU 1091 CB AASN A 132 2308 2091 1899 -1 -248 -255 C ATOM 1092 CB BASN A 132 26.311 28.975 20.449 0.50 9.73 C ANISOU 1092 CB BASN A 132 1460 1231 1007 16 -277 -253 C ATOM 1093 CG AASN A 132 27.275 28.419 19.719 0.50 35.78 C ANISOU 1093 CG AASN A 132 4744 4500 4352 51 -312 -296 C ATOM 1094 CG BASN A 132 26.430 28.880 18.958 0.50 8.83 C ANISOU 1094 CG BASN A 132 1312 1101 942 15 -256 -281 C ATOM 1095 ND2AASN A 132 27.996 28.142 18.651 0.50 27.65 N ANISOU 1095 ND2AASN A 132 3679 3458 3368 75 -319 -346 N ATOM 1096 ND2BASN A 132 27.515 28.326 18.464 0.50 11.09 N ANISOU 1096 ND2BASN A 132 1582 1366 1264 56 -295 -329 N ATOM 1097 OD1AASN A 132 27.696 28.253 20.870 0.50 28.86 O ANISOU 1097 OD1AASN A 132 3895 3624 3445 74 -358 -290 O ATOM 1098 OD1BASN A 132 25.524 29.214 18.209 0.50 9.00 O ANISOU 1098 OD1BASN A 132 1322 1133 965 -17 -210 -263 O ATOM 1099 N LEU A 133 22.693 29.791 20.739 1.00 10.51 N ANISOU 1099 N LEU A 133 1558 1405 1031 -105 -147 -149 N ATOM 1100 CA LEU A 133 21.719 30.895 20.741 1.00 10.48 C ANISOU 1100 CA LEU A 133 1512 1451 1018 -121 -93 -162 C ATOM 1101 C LEU A 133 20.987 30.806 22.058 1.00 12.06 C ANISOU 1101 C LEU A 133 1728 1705 1149 -146 -75 -132 C ATOM 1102 O LEU A 133 20.357 29.772 22.338 1.00 13.94 O ANISOU 1102 O LEU A 133 1999 1938 1360 -189 -75 -73 O ATOM 1103 CB LEU A 133 20.763 30.785 19.559 1.00 10.78 C ANISOU 1103 CB LEU A 133 1529 1477 1088 -147 -69 -152 C ATOM 1104 CG LEU A 133 21.462 30.759 18.196 1.00 12.17 C ANISOU 1104 CG LEU A 133 1696 1614 1313 -124 -84 -177 C ATOM 1105 CD1 LEU A 133 20.455 30.685 17.099 1.00 12.78 C ANISOU 1105 CD1 LEU A 133 1757 1692 1408 -142 -69 -170 C ATOM 1106 CD2 LEU A 133 22.399 31.950 17.978 1.00 15.24 C ANISOU 1106 CD2 LEU A 133 2057 2009 1725 -92 -73 -219 C ATOM 1107 N LEU A 134 21.184 31.793 22.930 1.00 10.53 N ANISOU 1107 N LEU A 134 1516 1562 925 -120 -64 -172 N ATOM 1108 CA LEU A 134 20.663 31.754 24.302 1.00 11.53 C ANISOU 1108 CA LEU A 134 1657 1760 964 -133 -47 -154 C ATOM 1109 C LEU A 134 19.506 32.667 24.499 1.00 11.95 C ANISOU 1109 C LEU A 134 1656 1883 1003 -143 9 -187 C ATOM 1110 O LEU A 134 19.494 33.767 23.965 1.00 12.13 O ANISOU 1110 O LEU A 134 1633 1897 1079 -113 16 -246 O ATOM 1111 CB LEU A 134 21.762 32.049 25.306 1.00 12.92 C ANISOU 1111 CB LEU A 134 1854 1954 1100 -86 -88 -188 C ATOM 1112 CG LEU A 134 23.043 31.211 25.156 1.00 16.56 C ANISOU 1112 CG LEU A 134 2359 2349 1584 -60 -156 -174 C ATOM 1113 CD1 LEU A 134 24.015 31.518 26.223 1.00 17.71 C ANISOU 1113 CD1 LEU A 134 2519 2524 1687 -11 -204 -213 C ATOM 1114 CD2 LEU A 134 22.770 29.689 25.076 1.00 20.22 C ANISOU 1114 CD2 LEU A 134 2886 2768 2030 -97 -179 -85 C ATOM 1115 N ILE A 135 18.512 32.213 25.257 1.00 12.74 N ANISOU 1115 N ILE A 135 1757 2050 1032 -186 49 -148 N ATOM 1116 CA ILE A 135 17.291 33.002 25.447 1.00 13.02 C ANISOU 1116 CA ILE A 135 1726 2166 1054 -194 106 -190 C ATOM 1117 C ILE A 135 17.067 33.320 26.902 1.00 16.31 C ANISOU 1117 C ILE A 135 2139 2692 1367 -186 134 -212 C ATOM 1118 O ILE A 135 17.520 32.588 27.787 1.00 15.82 O ANISOU 1118 O ILE A 135 2137 2652 1223 -202 121 -159 O ATOM 1119 CB ILE A 135 16.065 32.261 24.858 1.00 14.50 C ANISOU 1119 CB ILE A 135 1890 2360 1260 -260 144 -143 C ATOM 1120 CG1 ILE A 135 15.817 30.905 25.544 1.00 17.01 C ANISOU 1120 CG1 ILE A 135 2260 2692 1511 -333 158 -47 C ATOM 1121 CG2 ILE A 135 16.204 32.070 23.338 1.00 14.21 C ANISOU 1121 CG2 ILE A 135 1850 2228 1320 -256 112 -139 C ATOM 1122 CD1 ILE A 135 14.398 30.322 25.251 1.00 25.69 C ANISOU 1122 CD1 ILE A 135 3313 3825 2623 -413 211 -13 C ATOM 1123 N ASN A 136 16.305 34.388 27.154 1.00 15.42 N ANISOU 1123 N ASN A 136 1956 2654 1251 -160 170 -292 N ATOM 1124 CA ASN A 136 15.922 34.724 28.526 1.00 17.25 C ANISOU 1124 CA ASN A 136 2170 3013 1372 -150 207 -329 C ATOM 1125 C ASN A 136 14.383 34.739 28.627 1.00 18.93 C ANISOU 1125 C ASN A 136 2308 3325 1560 -192 284 -341 C ATOM 1126 O ASN A 136 13.665 34.612 27.631 1.00 19.18 O ANISOU 1126 O ASN A 136 2300 3318 1670 -218 296 -331 O ATOM 1127 CB ASN A 136 16.599 36.013 29.002 1.00 16.55 C ANISOU 1127 CB ASN A 136 2060 2936 1292 -66 171 -440 C ATOM 1128 CG ASN A 136 16.148 37.261 28.314 1.00 17.51 C ANISOU 1128 CG ASN A 136 2111 3031 1513 -19 166 -534 C ATOM 1129 ND2 ASN A 136 16.942 38.321 28.425 1.00 20.89 N ANISOU 1129 ND2 ASN A 136 2532 3418 1989 45 117 -617 N ATOM 1130 OD1 ASN A 136 15.075 37.297 27.709 1.00 17.15 O ANISOU 1130 OD1 ASN A 136 2015 2998 1504 -40 201 -534 O ATOM 1131 N THR A 137 13.850 34.879 29.833 1.00 19.24 N ANISOU 1131 N THR A 137 2322 3503 1485 -198 337 -367 N ATOM 1132 CA THR A 137 12.385 34.813 29.969 1.00 19.50 C ANISOU 1132 CA THR A 137 2271 3647 1491 -246 419 -381 C ATOM 1133 C THR A 137 11.676 36.094 29.513 1.00 22.70 C ANISOU 1133 C THR A 137 2573 4075 1977 -178 421 -513 C ATOM 1134 O THR A 137 10.439 36.109 29.477 1.00 24.77 O ANISOU 1134 O THR A 137 2748 4425 2238 -206 480 -543 O ATOM 1135 CB THR A 137 11.958 34.369 31.385 1.00 28.60 C ANISOU 1135 CB THR A 137 3427 4958 2480 -293 492 -350 C ATOM 1136 CG2 THR A 137 12.456 32.970 31.776 1.00 29.45 C ANISOU 1136 CG2 THR A 137 3645 5034 2512 -374 490 -196 C ATOM 1137 OG1 THR A 137 12.534 35.303 32.255 1.00 24.98 O ANISOU 1137 OG1 THR A 137 2970 4563 1958 -207 468 -446 O ATOM 1138 N GLU A 138 12.429 37.139 29.127 1.00 18.04 N ANISOU 1138 N GLU A 138 2201 3052 1603 186 -14 -446 N ATOM 1139 CA GLU A 138 11.887 38.421 28.664 1.00 19.92 C ANISOU 1139 CA GLU A 138 2460 3277 1833 266 23 -470 C ATOM 1140 C GLU A 138 11.625 38.485 27.160 1.00 22.89 C ANISOU 1140 C GLU A 138 2832 3629 2235 291 52 -439 C ATOM 1141 O GLU A 138 11.064 39.466 26.675 1.00 26.77 O ANISOU 1141 O GLU A 138 3340 4121 2711 370 90 -446 O ATOM 1142 CB GLU A 138 12.805 39.574 29.050 1.00 21.49 C ANISOU 1142 CB GLU A 138 2712 3376 2076 288 30 -527 C ATOM 1143 CG GLU A 138 12.766 39.880 30.542 1.00 33.51 C ANISOU 1143 CG GLU A 138 4238 4943 3552 292 12 -572 C ATOM 1144 CD GLU A 138 13.482 41.143 30.969 1.00 56.84 C ANISOU 1144 CD GLU A 138 7248 7810 6538 312 26 -643 C ATOM 1145 OE1 GLU A 138 14.630 41.375 30.519 1.00 39.86 O ANISOU 1145 OE1 GLU A 138 5124 5559 4463 273 25 -662 O ATOM 1146 OE2 GLU A 138 12.894 41.897 31.777 1.00 54.11 O1- ANISOU 1146 OE2 GLU A 138 6920 7500 6139 363 40 -683 O1- ATOM 1147 N GLY A 139 12.071 37.491 26.413 1.00 16.85 N ANISOU 1147 N GLY A 139 2052 2841 1509 232 38 -406 N ATOM 1148 CA GLY A 139 11.888 37.537 24.965 1.00 15.92 C ANISOU 1148 CA GLY A 139 1929 2706 1415 255 63 -380 C ATOM 1149 C GLY A 139 13.146 37.850 24.194 1.00 14.88 C ANISOU 1149 C GLY A 139 1835 2446 1373 246 66 -383 C ATOM 1150 O GLY A 139 13.084 37.886 22.969 1.00 14.26 O ANISOU 1150 O GLY A 139 1752 2350 1316 267 87 -359 O ATOM 1151 N ALA A 140 14.296 38.024 24.875 1.00 13.37 N ANISOU 1151 N ALA A 140 1674 2178 1229 212 46 -411 N ATOM 1152 CA ALA A 140 15.535 38.277 24.141 1.00 12.67 C ANISOU 1152 CA ALA A 140 1612 1978 1222 194 49 -414 C ATOM 1153 C ALA A 140 16.191 36.980 23.729 1.00 12.87 C ANISOU 1153 C ALA A 140 1618 1996 1278 131 20 -380 C ATOM 1154 O ALA A 140 15.997 35.925 24.357 1.00 13.05 O ANISOU 1154 O ALA A 140 1618 2074 1266 89 -7 -363 O ATOM 1155 CB ALA A 140 16.508 39.082 25.012 1.00 14.73 C ANISOU 1155 CB ALA A 140 1907 2173 1516 180 42 -466 C ATOM 1156 N ILE A 141 16.986 37.059 22.661 1.00 11.46 N ANISOU 1156 N ILE A 141 1452 1742 1162 129 30 -366 N ATOM 1157 CA ILE A 141 17.858 35.979 22.234 1.00 10.18 C ANISOU 1157 CA ILE A 141 1281 1552 1036 78 5 -338 C ATOM 1158 C ILE A 141 19.209 36.568 21.905 1.00 12.06 C ANISOU 1158 C ILE A 141 1539 1698 1344 71 8 -354 C ATOM 1159 O ILE A 141 19.281 37.708 21.442 1.00 11.76 O ANISOU 1159 O ILE A 141 1524 1609 1335 106 41 -371 O ATOM 1160 CB ILE A 141 17.246 35.177 21.091 1.00 10.95 C ANISOU 1160 CB ILE A 141 1359 1679 1122 78 16 -299 C ATOM 1161 CG1 ILE A 141 18.056 33.915 20.788 1.00 11.05 C ANISOU 1161 CG1 ILE A 141 1371 1664 1163 27 -8 -272 C ATOM 1162 CG2 ILE A 141 17.076 36.038 19.838 1.00 12.01 C ANISOU 1162 CG2 ILE A 141 1499 1782 1281 133 53 -292 C ATOM 1163 CD1 ILE A 141 17.260 32.866 19.938 1.00 10.97 C ANISOU 1163 CD1 ILE A 141 1345 1699 1124 6 0 -243 C ATOM 1164 N LYS A 142 20.272 35.827 22.235 1.00 11.12 N ANISOU 1164 N LYS A 142 1412 1564 1248 26 -25 -348 N ATOM 1165 CA LYS A 142 21.622 36.363 22.091 1.00 10.98 C ANISOU 1165 CA LYS A 142 1402 1481 1289 9 -27 -368 C ATOM 1166 C LYS A 142 22.525 35.309 21.513 1.00 10.58 C ANISOU 1166 C LYS A 142 1338 1416 1265 -14 -47 -331 C ATOM 1167 O LYS A 142 22.373 34.084 21.754 1.00 11.92 O ANISOU 1167 O LYS A 142 1500 1624 1405 -27 -68 -300 O ATOM 1168 CB LYS A 142 22.183 36.797 23.462 1.00 11.48 C ANISOU 1168 CB LYS A 142 1462 1561 1339 -16 -49 -418 C ATOM 1169 CG LYS A 142 21.254 37.737 24.226 1.00 11.84 C ANISOU 1169 CG LYS A 142 1526 1628 1347 9 -32 -459 C ATOM 1170 CD LYS A 142 21.992 38.353 25.390 1.00 13.05 C ANISOU 1170 CD LYS A 142 1678 1783 1497 -20 -49 -521 C ATOM 1171 CE LYS A 142 21.046 39.217 26.194 1.00 15.56 C ANISOU 1171 CE LYS A 142 2018 2123 1771 9 -32 -563 C ATOM 1172 NZ LYS A 142 21.823 40.140 27.098 1.00 17.50 N1+ ANISOU 1172 NZ LYS A 142 2275 2348 2025 -23 -35 -640 N1+ ATOM 1173 N LEU A 143 23.512 35.777 20.762 1.00 10.35 N ANISOU 1173 N LEU A 143 1311 1327 1293 -17 -35 -333 N ATOM 1174 CA ALEU A 143 24.541 34.968 20.110 0.50 10.79 C ANISOU 1174 CA ALEU A 143 1354 1366 1380 -30 -50 -301 C ATOM 1175 CA BLEU A 143 24.493 34.875 20.166 0.50 10.70 C ANISOU 1175 CA BLEU A 143 1342 1359 1364 -30 -52 -299 C ATOM 1176 C LEU A 143 25.672 34.691 21.095 1.00 10.84 C ANISOU 1176 C LEU A 143 1339 1398 1381 -60 -84 -318 C ATOM 1177 O LEU A 143 26.298 35.653 21.576 1.00 11.22 O ANISOU 1177 O LEU A 143 1379 1436 1447 -82 -83 -365 O ATOM 1178 CB ALEU A 143 25.116 35.779 18.927 0.50 11.51 C ANISOU 1178 CB ALEU A 143 1451 1391 1531 -19 -18 -298 C ATOM 1179 CB BLEU A 143 24.966 35.374 18.805 0.50 11.38 C ANISOU 1179 CB BLEU A 143 1432 1385 1505 -15 -22 -284 C ATOM 1180 CG ALEU A 143 24.141 36.035 17.762 0.50 15.64 C ANISOU 1180 CG ALEU A 143 1990 1897 2057 24 20 -272 C ATOM 1181 CG BLEU A 143 23.858 35.483 17.773 0.50 12.98 C ANISOU 1181 CG BLEU A 143 1648 1583 1701 24 10 -260 C ATOM 1182 CD1ALEU A 143 24.473 37.288 17.035 0.50 18.10 C ANISOU 1182 CD1ALEU A 143 2319 2143 2416 42 63 -282 C ATOM 1183 CD1BLEU A 143 23.531 36.926 17.437 0.50 12.51 C ANISOU 1183 CD1BLEU A 143 1609 1481 1662 54 54 -281 C ATOM 1184 CD2ALEU A 143 24.108 34.869 16.785 0.50 18.49 C ANISOU 1184 CD2ALEU A 143 2340 2269 2415 33 12 -227 C ATOM 1185 CD2BLEU A 143 24.278 34.835 16.501 0.50 16.24 C ANISOU 1185 CD2BLEU A 143 2054 1976 2140 36 15 -220 C ATOM 1186 N ALA A 144 25.985 33.414 21.368 1.00 10.67 N ANISOU 1186 N ALA A 144 1309 1412 1332 -60 -111 -283 N ATOM 1187 CA ALA A 144 27.084 33.005 22.230 1.00 11.50 C ANISOU 1187 CA ALA A 144 1389 1559 1421 -71 -143 -288 C ATOM 1188 C ALA A 144 28.263 32.569 21.400 1.00 11.54 C ANISOU 1188 C ALA A 144 1380 1546 1460 -65 -147 -259 C ATOM 1189 O ALA A 144 28.100 32.065 20.281 1.00 11.88 O ANISOU 1189 O ALA A 144 1441 1550 1525 -47 -131 -221 O ATOM 1190 CB ALA A 144 26.674 31.866 23.155 1.00 13.18 C ANISOU 1190 CB ALA A 144 1609 1826 1574 -62 -164 -259 C ATOM 1191 N ASP A 145 29.445 32.742 21.974 1.00 13.42 N ANISOU 1191 N ASP A 145 1580 1823 1695 -78 -169 -280 N ATOM 1192 CA ASP A 145 30.722 32.269 21.421 1.00 13.89 C ANISOU 1192 CA ASP A 145 1614 1894 1771 -66 -178 -253 C ATOM 1193 C ASP A 145 31.166 32.945 20.166 1.00 15.11 C ANISOU 1193 C ASP A 145 1763 1991 1988 -76 -153 -255 C ATOM 1194 O ASP A 145 31.956 32.390 19.399 1.00 15.56 O ANISOU 1194 O ASP A 145 1807 2045 2059 -56 -153 -218 O ATOM 1195 CB ASP A 145 30.716 30.732 21.262 1.00 14.21 C ANISOU 1195 CB ASP A 145 1677 1944 1779 -22 -186 -187 C ATOM 1196 CG ASP A 145 30.563 29.946 22.563 1.00 17.39 C ANISOU 1196 CG ASP A 145 2082 2409 2115 -4 -208 -174 C ATOM 1197 OD1 ASP A 145 30.620 30.561 23.668 1.00 16.91 O ANISOU 1197 OD1 ASP A 145 1992 2404 2026 -24 -226 -218 O ATOM 1198 OD2 ASP A 145 30.391 28.711 22.485 1.00 21.73 O1- ANISOU 1198 OD2 ASP A 145 2668 2951 2637 30 -204 -119 O1- ATOM 1199 N PHE A 146 30.662 34.159 19.910 1.00 16.02 N ANISOU 1199 N PHE A 146 1892 2056 2137 -102 -124 -293 N ATOM 1200 CA PHE A 146 31.060 34.907 18.753 1.00 16.21 C ANISOU 1200 CA PHE A 146 1917 2022 2220 -111 -92 -292 C ATOM 1201 C PHE A 146 32.563 35.114 18.769 1.00 19.37 C ANISOU 1201 C PHE A 146 2267 2455 2638 -141 -103 -307 C ATOM 1202 O PHE A 146 33.137 35.478 19.797 1.00 18.67 O ANISOU 1202 O PHE A 146 2145 2420 2528 -180 -123 -354 O ATOM 1203 CB PHE A 146 30.387 36.296 18.800 1.00 19.63 C ANISOU 1203 CB PHE A 146 2378 2400 2679 -133 -55 -338 C ATOM 1204 CG PHE A 146 29.755 36.600 17.475 1.00 19.87 C ANISOU 1204 CG PHE A 146 2441 2364 2744 -99 -13 -304 C ATOM 1205 CD1 PHE A 146 30.530 36.990 16.397 1.00 20.43 C ANISOU 1205 CD1 PHE A 146 2504 2394 2865 -102 14 -286 C ATOM 1206 CD2 PHE A 146 28.390 36.437 17.286 1.00 21.10 C ANISOU 1206 CD2 PHE A 146 2628 2513 2875 -60 -1 -287 C ATOM 1207 CE1 PHE A 146 29.950 37.217 15.163 1.00 20.72 C ANISOU 1207 CE1 PHE A 146 2567 2381 2926 -60 52 -251 C ATOM 1208 CE2 PHE A 146 27.813 36.652 16.038 1.00 25.03 C ANISOU 1208 CE2 PHE A 146 3146 2970 3394 -21 36 -254 C ATOM 1209 CZ PHE A 146 28.603 37.039 14.985 1.00 22.31 C ANISOU 1209 CZ PHE A 146 2796 2583 3098 -18 62 -235 C ATOM 1210 N GLY A 147 33.221 34.882 17.634 1.00 18.98 N ANISOU 1210 N GLY A 147 2206 2385 2621 -125 -90 -269 N ATOM 1211 CA GLY A 147 34.642 35.125 17.528 1.00 19.63 C ANISOU 1211 CA GLY A 147 2234 2507 2719 -155 -96 -280 C ATOM 1212 C GLY A 147 35.563 34.042 18.043 1.00 21.88 C ANISOU 1212 C GLY A 147 2472 2887 2954 -129 -138 -257 C ATOM 1213 O GLY A 147 36.760 34.094 17.771 1.00 21.80 O ANISOU 1213 O GLY A 147 2409 2924 2951 -142 -143 -256 O ATOM 1214 N LEU A 148 35.024 33.023 18.731 1.00 17.78 N ANISOU 1214 N LEU A 148 1973 2400 2383 -87 -164 -233 N ATOM 1215 CA LEU A 148 35.869 31.957 19.285 1.00 17.36 C ANISOU 1215 CA LEU A 148 1885 2436 2274 -46 -197 -202 C ATOM 1216 C LEU A 148 36.436 31.014 18.209 1.00 22.71 C ANISOU 1216 C LEU A 148 2567 3103 2956 12 -191 -138 C ATOM 1217 O LEU A 148 37.544 30.502 18.351 1.00 22.16 O ANISOU 1217 O LEU A 148 2452 3112 2855 43 -210 -117 O ATOM 1218 CB LEU A 148 35.155 31.155 20.383 1.00 18.06 C ANISOU 1218 CB LEU A 148 2002 2556 2302 -16 -218 -190 C ATOM 1219 CG LEU A 148 34.630 31.961 21.608 1.00 21.33 C ANISOU 1219 CG LEU A 148 2409 3000 2697 -63 -229 -253 C ATOM 1220 CD1 LEU A 148 34.231 31.032 22.714 1.00 22.56 C ANISOU 1220 CD1 LEU A 148 2577 3210 2783 -24 -252 -230 C ATOM 1221 CD2 LEU A 148 35.657 32.978 22.156 1.00 23.72 C ANISOU 1221 CD2 LEU A 148 2642 3371 3001 -121 -242 -321 C ATOM 1222 N ALA A 149 35.690 30.793 17.118 1.00 19.80 N ANISOU 1222 N ALA A 149 2251 2649 2623 32 -165 -107 N ATOM 1223 CA ALA A 149 36.171 29.938 16.023 1.00 19.77 C ANISOU 1223 CA ALA A 149 2257 2628 2625 87 -156 -52 C ATOM 1224 C ALA A 149 37.433 30.510 15.349 1.00 25.61 C ANISOU 1224 C ALA A 149 2936 3401 3394 75 -151 -54 C ATOM 1225 O ALA A 149 38.306 29.735 14.971 1.00 27.24 O ANISOU 1225 O ALA A 149 3122 3648 3578 128 -158 -14 O ATOM 1226 CB ALA A 149 35.076 29.773 14.997 1.00 20.35 C ANISOU 1226 CB ALA A 149 2390 2614 2729 98 -129 -34 C ATOM 1227 N ARG A 150 37.563 31.836 15.215 1.00 22.06 N ANISOU 1227 N ARG A 150 2458 2934 2989 10 -133 -99 N ATOM 1228 CA ARG A 150 38.761 32.429 14.611 1.00 23.15 C ANISOU 1228 CA ARG A 150 2536 3105 3155 -16 -122 -103 C ATOM 1229 C ARG A 150 39.909 32.339 15.588 1.00 30.15 C ANISOU 1229 C ARG A 150 3347 4113 3995 -31 -155 -126 C ATOM 1230 O ARG A 150 41.047 32.091 15.179 1.00 33.15 O ANISOU 1230 O ARG A 150 3671 4561 4363 -12 -160 -104 O ATOM 1231 CB ARG A 150 38.523 33.892 14.247 1.00 24.83 C ANISOU 1231 CB ARG A 150 2752 3252 3429 -88 -84 -146 C ATOM 1232 CG ARG A 150 39.662 34.544 13.466 1.00 33.27 C ANISOU 1232 CG ARG A 150 3768 4338 4535 -123 -61 -145 C ATOM 1233 CD ARG A 150 39.336 35.974 13.078 1.00 47.00 C ANISOU 1233 CD ARG A 150 5531 5991 6336 -190 -11 -180 C ATOM 1234 NE ARG A 150 40.503 36.690 12.559 1.00 59.14 N ANISOU 1234 NE ARG A 150 7013 7551 7906 -246 16 -190 N ATOM 1235 CZ ARG A 150 40.936 36.626 11.302 1.00 77.38 C ANISOU 1235 CZ ARG A 150 9313 9842 10244 -217 43 -140 C ATOM 1236 NH1 ARG A 150 40.316 35.854 10.415 1.00 66.70 N1+ ANISOU 1236 NH1 ARG A 150 8002 8451 8890 -130 45 -81 N1+ ATOM 1237 NH2 ARG A 150 42.002 37.318 10.926 1.00 64.67 N ANISOU 1237 NH2 ARG A 150 7651 8259 8662 -278 69 -151 N ATOM 1238 N ALA A 151 39.624 32.567 16.877 1.00 24.82 N ANISOU 1238 N ALA A 151 2665 3477 3287 -64 -177 -172 N ATOM 1239 CA ALA A 151 40.671 32.519 17.894 1.00 26.09 C ANISOU 1239 CA ALA A 151 2746 3773 3392 -78 -210 -200 C ATOM 1240 C ALA A 151 41.229 31.116 18.127 1.00 30.97 C ANISOU 1240 C ALA A 151 3350 4478 3941 20 -238 -139 C ATOM 1241 O ALA A 151 42.449 30.972 18.319 1.00 33.37 O ANISOU 1241 O ALA A 151 3572 4902 4203 33 -256 -137 O ATOM 1242 CB ALA A 151 40.149 33.106 19.180 1.00 27.07 C ANISOU 1242 CB ALA A 151 2871 3919 3496 -132 -225 -265 C ATOM 1243 N PHE A 152 40.365 30.081 18.047 1.00 26.36 N ANISOU 1243 N PHE A 152 2844 3832 3341 90 -236 -87 N ATOM 1244 CA PHE A 152 40.744 28.698 18.340 1.00 26.37 C ANISOU 1244 CA PHE A 152 2855 3889 3273 190 -252 -25 C ATOM 1245 C PHE A 152 40.535 27.640 17.233 1.00 30.41 C ANISOU 1245 C PHE A 152 3436 4323 3796 267 -230 44 C ATOM 1246 O PHE A 152 40.937 26.489 17.430 1.00 32.81 O ANISOU 1246 O PHE A 152 3758 4665 4042 356 -235 97 O ATOM 1247 CB PHE A 152 40.070 28.244 19.667 1.00 28.81 C ANISOU 1247 CB PHE A 152 3195 4223 3527 207 -270 -29 C ATOM 1248 CG PHE A 152 40.057 29.222 20.830 1.00 31.33 C ANISOU 1248 CG PHE A 152 3461 4612 3831 134 -291 -103 C ATOM 1249 CD1 PHE A 152 41.244 29.725 21.354 1.00 36.73 C ANISOU 1249 CD1 PHE A 152 4044 5432 4481 108 -314 -143 C ATOM 1250 CD2 PHE A 152 38.864 29.575 21.449 1.00 34.04 C ANISOU 1250 CD2 PHE A 152 3853 4897 4185 95 -288 -135 C ATOM 1251 CE1 PHE A 152 41.229 30.615 22.432 1.00 38.90 C ANISOU 1251 CE1 PHE A 152 4271 5771 4737 35 -333 -220 C ATOM 1252 CE2 PHE A 152 38.849 30.453 22.535 1.00 38.11 C ANISOU 1252 CE2 PHE A 152 4324 5475 4682 33 -307 -206 C ATOM 1253 CZ PHE A 152 40.031 30.968 23.019 1.00 37.65 C ANISOU 1253 CZ PHE A 152 4170 5542 4593 1 -329 -251 C ATOM 1254 N GLY A 153 39.896 28.001 16.113 1.00 25.46 N ANISOU 1254 N GLY A 153 2851 3590 3235 239 -203 43 N ATOM 1255 CA GLY A 153 39.590 27.068 15.030 1.00 24.36 C ANISOU 1255 CA GLY A 153 2776 3373 3105 301 -181 95 C ATOM 1256 C GLY A 153 38.315 26.277 15.290 1.00 27.14 C ANISOU 1256 C GLY A 153 3220 3647 3444 315 -172 110 C ATOM 1257 O GLY A 153 37.820 26.266 16.422 1.00 28.23 O ANISOU 1257 O GLY A 153 3367 3805 3552 296 -185 93 O ATOM 1258 N VAL A 154 37.734 25.662 14.239 1.00 23.71 N ANISOU 1258 N VAL A 154 2850 3127 3030 340 -147 136 N ATOM 1259 CA VAL A 154 36.547 24.805 14.398 1.00 22.39 C ANISOU 1259 CA VAL A 154 2770 2889 2847 344 -133 148 C ATOM 1260 C VAL A 154 37.070 23.382 14.224 1.00 24.31 C ANISOU 1260 C VAL A 154 3066 3124 3047 430 -122 204 C ATOM 1261 O VAL A 154 37.501 23.018 13.132 1.00 24.38 O ANISOU 1261 O VAL A 154 3087 3107 3068 470 -108 226 O ATOM 1262 CB VAL A 154 35.356 25.109 13.458 1.00 25.02 C ANISOU 1262 CB VAL A 154 3141 3139 3225 301 -111 128 C ATOM 1263 CG1 VAL A 154 34.227 24.092 13.683 1.00 24.66 C ANISOU 1263 CG1 VAL A 154 3180 3038 3153 298 -95 138 C ATOM 1264 CG2 VAL A 154 34.850 26.531 13.675 1.00 25.17 C ANISOU 1264 CG2 VAL A 154 3118 3164 3282 232 -114 79 C ATOM 1265 N PRO A 155 37.109 22.583 15.307 1.00 21.80 N ANISOU 1265 N PRO A 155 2781 2830 2672 467 -126 230 N ATOM 1266 CA PRO A 155 37.656 21.229 15.185 1.00 21.09 C ANISOU 1266 CA PRO A 155 2753 2726 2535 561 -107 288 C ATOM 1267 C PRO A 155 36.636 20.236 14.663 1.00 22.01 C ANISOU 1267 C PRO A 155 2982 2726 2656 557 -70 301 C ATOM 1268 O PRO A 155 35.454 20.558 14.587 1.00 21.20 O ANISOU 1268 O PRO A 155 2900 2572 2582 480 -64 266 O ATOM 1269 CB PRO A 155 38.064 20.899 16.622 1.00 22.65 C ANISOU 1269 CB PRO A 155 2937 3001 2667 603 -121 311 C ATOM 1270 CG PRO A 155 37.009 21.595 17.460 1.00 25.99 C ANISOU 1270 CG PRO A 155 3351 3419 3103 516 -134 266 C ATOM 1271 CD PRO A 155 36.649 22.865 16.683 1.00 22.18 C ANISOU 1271 CD PRO A 155 2818 2918 2692 433 -143 210 C ATOM 1272 N VAL A 156 37.093 19.062 14.272 1.00 20.69 N ANISOU 1272 N VAL A 156 2884 2519 2457 637 -43 347 N ATOM 1273 CA VAL A 156 36.203 17.997 13.812 1.00 19.37 C ANISOU 1273 CA VAL A 156 2835 2237 2289 629 -1 356 C ATOM 1274 C VAL A 156 35.439 17.454 15.014 1.00 21.19 C ANISOU 1274 C VAL A 156 3126 2442 2483 607 13 368 C ATOM 1275 O VAL A 156 34.225 17.211 14.943 1.00 18.68 O ANISOU 1275 O VAL A 156 2865 2053 2180 533 34 344 O ATOM 1276 CB VAL A 156 36.976 16.891 13.047 1.00 22.83 C ANISOU 1276 CB VAL A 156 3341 2631 2701 727 30 400 C ATOM 1277 CG1 VAL A 156 36.065 15.728 12.674 1.00 23.24 C ANISOU 1277 CG1 VAL A 156 3527 2556 2747 709 80 402 C ATOM 1278 CG2 VAL A 156 37.650 17.466 11.804 1.00 23.03 C ANISOU 1278 CG2 VAL A 156 3302 2686 2762 744 16 387 C ATOM 1279 N ARG A 157 36.157 17.300 16.141 1.00 17.74 N ANISOU 1279 N ARG A 157 2517 2003 2220 100 -448 -53 N ATOM 1280 CA ARG A 157 35.575 16.769 17.373 1.00 16.92 C ANISOU 1280 CA ARG A 157 2456 1892 2079 73 -472 -6 C ATOM 1281 C ARG A 157 35.853 17.725 18.489 1.00 18.30 C ANISOU 1281 C ARG A 157 2627 2103 2224 66 -456 -12 C ATOM 1282 O ARG A 157 36.870 18.443 18.491 1.00 19.35 O ANISOU 1282 O ARG A 157 2730 2250 2371 91 -451 -56 O ATOM 1283 CB ARG A 157 36.237 15.444 17.744 1.00 18.35 C ANISOU 1283 CB ARG A 157 2668 2032 2272 90 -548 4 C ATOM 1284 CG ARG A 157 36.234 14.428 16.655 1.00 19.32 C ANISOU 1284 CG ARG A 157 2787 2118 2437 107 -578 -4 C ATOM 1285 CD ARG A 157 34.828 14.029 16.290 1.00 18.68 C ANISOU 1285 CD ARG A 157 2719 2028 2351 76 -554 35 C ATOM 1286 NE ARG A 157 34.872 12.867 15.403 1.00 19.66 N ANISOU 1286 NE ARG A 157 2839 2111 2520 95 -595 26 N ATOM 1287 CZ ARG A 157 35.000 11.622 15.839 1.00 19.32 C ANISOU 1287 CZ ARG A 157 2828 2022 2492 96 -661 51 C ATOM 1288 NH1 ARG A 157 34.970 11.361 17.141 1.00 21.82 N1+ ANISOU 1288 NH1 ARG A 157 3188 2328 2774 75 -687 95 N1+ ATOM 1289 NH2 ARG A 157 35.080 10.622 14.978 1.00 19.99 N ANISOU 1289 NH2 ARG A 157 2901 2071 2625 116 -701 35 N ATOM 1290 N THR A 158 34.973 17.747 19.484 1.00 16.25 N ANISOU 1290 N THR A 158 2392 1862 1921 32 -448 28 N ATOM 1291 CA THR A 158 35.168 18.604 20.656 1.00 16.88 C ANISOU 1291 CA THR A 158 2464 1983 1967 25 -437 21 C ATOM 1292 C THR A 158 36.185 17.970 21.577 1.00 18.48 C ANISOU 1292 C THR A 158 2690 2175 2159 48 -496 22 C ATOM 1293 O THR A 158 36.676 16.865 21.330 1.00 18.04 O ANISOU 1293 O THR A 158 2659 2076 2122 66 -548 30 O ATOM 1294 CB THR A 158 33.853 18.796 21.414 1.00 18.41 C ANISOU 1294 CB THR A 158 2672 2208 2113 -21 -411 60 C ATOM 1295 CG2 THR A 158 32.703 19.194 20.505 1.00 19.55 C ANISOU 1295 CG2 THR A 158 2804 2358 2268 -44 -361 62 C ATOM 1296 OG1 THR A 158 33.562 17.581 22.159 1.00 19.08 O ANISOU 1296 OG1 THR A 158 2806 2274 2168 -39 -455 112 O ATOM 1297 N TYR A 159 36.474 18.647 22.704 1.00 18.07 N ANISOU 1297 N TYR A 159 2628 2162 2075 49 -493 11 N ATOM 1298 CA TYR A 159 37.411 18.161 23.686 1.00 18.62 C ANISOU 1298 CA TYR A 159 2718 2230 2128 74 -547 9 C ATOM 1299 C TYR A 159 36.957 16.831 24.318 1.00 21.38 C ANISOU 1299 C TYR A 159 3127 2554 2444 55 -597 74 C ATOM 1300 O TYR A 159 37.796 16.134 24.885 1.00 22.80 O ANISOU 1300 O TYR A 159 3333 2713 2618 81 -656 77 O ATOM 1301 CB TYR A 159 37.645 19.253 24.760 1.00 21.27 C ANISOU 1301 CB TYR A 159 3025 2624 2434 78 -527 -18 C ATOM 1302 CG TYR A 159 36.548 19.345 25.804 1.00 21.47 C ANISOU 1302 CG TYR A 159 3066 2694 2399 37 -513 28 C ATOM 1303 CD1 TYR A 159 35.295 19.854 25.483 1.00 22.79 C ANISOU 1303 CD1 TYR A 159 3220 2883 2556 -4 -462 44 C ATOM 1304 CD2 TYR A 159 36.766 18.919 27.113 1.00 23.03 C ANISOU 1304 CD2 TYR A 159 3290 2916 2545 38 -552 53 C ATOM 1305 CE1 TYR A 159 34.269 19.894 26.425 1.00 24.05 C ANISOU 1305 CE1 TYR A 159 3391 3088 2658 -46 -449 81 C ATOM 1306 CE2 TYR A 159 35.751 18.974 28.069 1.00 24.06 C ANISOU 1306 CE2 TYR A 159 3432 3095 2614 -4 -538 96 C ATOM 1307 CZ TYR A 159 34.511 19.479 27.724 1.00 30.17 C ANISOU 1307 CZ TYR A 159 4190 3892 3381 -47 -486 106 C ATOM 1308 OH TYR A 159 33.495 19.506 28.650 1.00 28.81 O ANISOU 1308 OH TYR A 159 4026 3773 3146 -92 -472 142 O ATOM 1309 N THR A 160 35.646 16.486 24.222 1.00 19.21 N ANISOU 1309 N THR A 160 2873 2279 2149 9 -575 126 N ATOM 1310 CA THR A 160 35.058 15.244 24.770 1.00 19.66 C ANISOU 1310 CA THR A 160 2986 2309 2177 -20 -614 195 C ATOM 1311 C THR A 160 34.914 14.201 23.651 1.00 21.51 C ANISOU 1311 C THR A 160 3236 2477 2460 -16 -638 207 C ATOM 1312 O THR A 160 34.308 13.140 23.868 1.00 21.95 O ANISOU 1312 O THR A 160 3333 2500 2506 -43 -665 263 O ATOM 1313 CB THR A 160 33.622 15.489 25.322 1.00 27.48 C ANISOU 1313 CB THR A 160 3985 3341 3117 -78 -570 239 C ATOM 1314 CG2 THR A 160 33.575 16.390 26.527 1.00 32.82 C ANISOU 1314 CG2 THR A 160 4643 4089 3737 -88 -550 232 C ATOM 1315 OG1 THR A 160 32.733 15.902 24.283 1.00 28.23 O ANISOU 1315 OG1 THR A 160 4054 3435 3237 -97 -518 224 O ATOM 1316 N HIS A 161 35.450 14.501 22.450 1.00 18.68 N ANISOU 1316 N HIS A 161 2840 2101 2155 16 -626 153 N ATOM 1317 CA HIS A 161 35.380 13.644 21.247 1.00 17.97 C ANISOU 1317 CA HIS A 161 2751 1961 2117 27 -645 149 C ATOM 1318 C HIS A 161 34.025 13.692 20.535 1.00 19.39 C ANISOU 1318 C HIS A 161 2924 2143 2300 -8 -596 169 C ATOM 1319 O HIS A 161 33.853 13.013 19.514 1.00 20.07 O ANISOU 1319 O HIS A 161 3005 2192 2429 1 -607 163 O ATOM 1320 CB HIS A 161 35.907 12.198 21.514 1.00 20.23 C ANISOU 1320 CB HIS A 161 3078 2187 2420 42 -729 176 C ATOM 1321 CG HIS A 161 37.192 12.190 22.275 1.00 23.49 C ANISOU 1321 CG HIS A 161 3499 2600 2825 78 -779 152 C ATOM 1322 CD2 HIS A 161 37.416 11.923 23.583 1.00 26.39 C ANISOU 1322 CD2 HIS A 161 3904 2974 3147 74 -815 188 C ATOM 1323 ND1 HIS A 161 38.380 12.602 21.691 1.00 25.67 N ANISOU 1323 ND1 HIS A 161 3738 2878 3137 125 -789 80 N ATOM 1324 CE1 HIS A 161 39.291 12.551 22.656 1.00 25.56 C ANISOU 1324 CE1 HIS A 161 3741 2868 3103 150 -832 69 C ATOM 1325 NE2 HIS A 161 38.753 12.163 23.814 1.00 26.89 N ANISOU 1325 NE2 HIS A 161 3955 3041 3222 122 -850 134 N ATOM 1326 N GLU A 162 33.083 14.535 21.019 1.00 16.12 N ANISOU 1326 N GLU A 162 2504 1776 1844 -45 -541 184 N ATOM 1327 CA GLU A 162 31.769 14.690 20.382 1.00 16.72 C ANISOU 1327 CA GLU A 162 2572 1860 1921 -76 -492 194 C ATOM 1328 C GLU A 162 31.934 15.298 18.998 1.00 16.14 C ANISOU 1328 C GLU A 162 2456 1787 1891 -48 -459 144 C ATOM 1329 O GLU A 162 32.802 16.139 18.782 1.00 16.06 O ANISOU 1329 O GLU A 162 2415 1795 1893 -19 -447 103 O ATOM 1330 CB GLU A 162 30.866 15.592 21.255 1.00 17.58 C ANISOU 1330 CB GLU A 162 2678 2027 1976 -117 -444 207 C ATOM 1331 CG GLU A 162 29.498 15.903 20.663 1.00 27.86 C ANISOU 1331 CG GLU A 162 3968 3343 3274 -149 -392 207 C ATOM 1332 CD GLU A 162 28.530 16.669 21.545 1.00 52.87 C ANISOU 1332 CD GLU A 162 7131 6568 6389 -192 -352 215 C ATOM 1333 OE1 GLU A 162 28.267 16.215 22.683 1.00 38.67 O ANISOU 1333 OE1 GLU A 162 5362 4786 4545 -225 -370 256 O ATOM 1334 OE2 GLU A 162 27.988 17.694 21.071 1.00 51.39 O1- ANISOU 1334 OE2 GLU A 162 6910 6410 6204 -195 -305 180 O1- ATOM 1335 N VAL A 163 31.145 14.842 18.053 1.00 15.29 N ANISOU 1335 N VAL A 163 2344 1658 1806 -54 -444 147 N ATOM 1336 CA VAL A 163 31.227 15.361 16.701 1.00 14.37 C ANISOU 1336 CA VAL A 163 2188 1547 1725 -27 -413 105 C ATOM 1337 C VAL A 163 30.682 16.787 16.635 1.00 15.57 C ANISOU 1337 C VAL A 163 2315 1746 1856 -40 -350 86 C ATOM 1338 O VAL A 163 29.557 17.045 17.076 1.00 16.81 O ANISOU 1338 O VAL A 163 2481 1923 1981 -76 -320 105 O ATOM 1339 CB VAL A 163 30.429 14.417 15.766 1.00 17.70 C ANISOU 1339 CB VAL A 163 2613 1937 2176 -29 -418 112 C ATOM 1340 CG1 VAL A 163 30.390 14.952 14.339 1.00 18.84 C ANISOU 1340 CG1 VAL A 163 2715 2093 2349 0 -383 70 C ATOM 1341 CG2 VAL A 163 31.035 13.012 15.764 1.00 17.72 C ANISOU 1341 CG2 VAL A 163 2634 1886 2211 -12 -487 125 C ATOM 1342 N VAL A 164 31.453 17.718 16.092 1.00 14.10 N ANISOU 1342 N VAL A 164 2094 1576 1687 -12 -330 48 N ATOM 1343 CA VAL A 164 30.969 19.096 15.882 1.00 14.13 C ANISOU 1343 CA VAL A 164 2071 1617 1681 -21 -273 29 C ATOM 1344 C VAL A 164 29.972 19.040 14.699 1.00 15.63 C ANISOU 1344 C VAL A 164 2252 1803 1884 -21 -242 25 C ATOM 1345 O VAL A 164 30.272 18.498 13.636 1.00 14.53 O ANISOU 1345 O VAL A 164 2102 1644 1776 6 -253 13 O ATOM 1346 CB VAL A 164 32.145 20.061 15.649 1.00 16.50 C ANISOU 1346 CB VAL A 164 2338 1931 2002 7 -262 -7 C ATOM 1347 CG1 VAL A 164 31.638 21.452 15.247 1.00 18.21 C ANISOU 1347 CG1 VAL A 164 2525 2176 2219 0 -207 -24 C ATOM 1348 CG2 VAL A 164 33.029 20.147 16.890 1.00 16.65 C ANISOU 1348 CG2 VAL A 164 2363 1957 2005 10 -291 -10 C ATOM 1349 N THR A 165 28.784 19.587 14.890 1.00 13.47 N ANISOU 1349 N THR A 165 1980 1551 1586 -50 -206 31 N ATOM 1350 CA THR A 165 27.778 19.467 13.860 1.00 11.52 C ANISOU 1350 CA THR A 165 1727 1300 1349 -49 -180 25 C ATOM 1351 C THR A 165 28.118 20.199 12.576 1.00 11.67 C ANISOU 1351 C THR A 165 1714 1326 1394 -15 -153 -3 C ATOM 1352 O THR A 165 28.671 21.289 12.579 1.00 11.42 O ANISOU 1352 O THR A 165 1662 1312 1366 -7 -134 -18 O ATOM 1353 CB THR A 165 26.432 19.953 14.422 1.00 13.58 C ANISOU 1353 CB THR A 165 1996 1587 1576 -87 -149 29 C ATOM 1354 CG2 THR A 165 26.356 21.474 14.657 1.00 14.82 C ANISOU 1354 CG2 THR A 165 2130 1780 1723 -92 -115 7 C ATOM 1355 OG1 THR A 165 25.417 19.600 13.471 1.00 15.52 O ANISOU 1355 OG1 THR A 165 2241 1825 1832 -84 -131 21 O ATOM 1356 N LEU A 166 27.749 19.581 11.479 1.00 10.43 N ANISOU 1356 N LEU A 166 1551 1156 1256 4 -152 -10 N ATOM 1357 CA LEU A 166 27.908 20.143 10.135 1.00 10.38 C ANISOU 1357 CA LEU A 166 1514 1161 1268 36 -126 -33 C ATOM 1358 C LEU A 166 26.620 20.766 9.625 1.00 9.98 C ANISOU 1358 C LEU A 166 1461 1127 1205 30 -85 -41 C ATOM 1359 O LEU A 166 26.635 21.364 8.531 1.00 10.69 O ANISOU 1359 O LEU A 166 1528 1230 1304 55 -60 -56 O ATOM 1360 CB LEU A 166 28.303 19.019 9.146 1.00 11.49 C ANISOU 1360 CB LEU A 166 1643 1284 1438 68 -153 -44 C ATOM 1361 CG LEU A 166 29.596 18.276 9.495 1.00 13.11 C ANISOU 1361 CG LEU A 166 1849 1470 1662 81 -202 -45 C ATOM 1362 CD1 LEU A 166 29.830 17.183 8.521 1.00 15.10 C ANISOU 1362 CD1 LEU A 166 2084 1707 1946 112 -232 -62 C ATOM 1363 CD2 LEU A 166 30.778 19.214 9.517 1.00 15.99 C ANISOU 1363 CD2 LEU A 166 2194 1851 2030 93 -192 -60 C ATOM 1364 N TRP A 167 25.525 20.642 10.378 1.00 9.27 N ANISOU 1364 N TRP A 167 1391 1039 1092 -4 -79 -32 N ATOM 1365 CA TRP A 167 24.217 20.929 9.816 1.00 9.36 C ANISOU 1365 CA TRP A 167 1400 1062 1093 -7 -49 -48 C ATOM 1366 C TRP A 167 24.015 22.336 9.349 1.00 8.94 C ANISOU 1366 C TRP A 167 1330 1031 1036 3 -14 -65 C ATOM 1367 O TRP A 167 23.144 22.619 8.490 1.00 9.52 O ANISOU 1367 O TRP A 167 1396 1112 1108 18 10 -82 O ATOM 1368 CB TRP A 167 23.111 20.588 10.811 1.00 9.84 C ANISOU 1368 CB TRP A 167 1484 1126 1128 -50 -48 -41 C ATOM 1369 CG TRP A 167 23.064 19.147 11.246 1.00 9.65 C ANISOU 1369 CG TRP A 167 1482 1076 1109 -65 -80 -19 C ATOM 1370 CD1 TRP A 167 23.840 18.109 10.808 1.00 11.69 C ANISOU 1370 CD1 TRP A 167 1739 1304 1397 -41 -115 -10 C ATOM 1371 CD2 TRP A 167 22.148 18.599 12.193 1.00 10.32 C ANISOU 1371 CD2 TRP A 167 1592 1161 1171 -110 -83 -4 C ATOM 1372 CE2 TRP A 167 22.426 17.218 12.300 1.00 12.09 C ANISOU 1372 CE2 TRP A 167 1832 1349 1414 -112 -119 21 C ATOM 1373 CE3 TRP A 167 21.155 19.162 13.013 1.00 11.28 C ANISOU 1373 CE3 TRP A 167 1720 1311 1255 -152 -60 -10 C ATOM 1374 NE1 TRP A 167 23.437 16.931 11.418 1.00 11.28 N ANISOU 1374 NE1 TRP A 167 1712 1227 1346 -67 -140 13 N ATOM 1375 CZ2 TRP A 167 21.683 16.372 13.128 1.00 13.64 C ANISOU 1375 CZ2 TRP A 167 2055 1533 1594 -156 -129 45 C ATOM 1376 CZ3 TRP A 167 20.394 18.323 13.826 1.00 13.61 C ANISOU 1376 CZ3 TRP A 167 2039 1603 1531 -196 -66 9 C ATOM 1377 CH2 TRP A 167 20.674 16.949 13.893 1.00 14.06 C ANISOU 1377 CH2 TRP A 167 2116 1621 1607 -199 -99 41 C ATOM 1378 N TYR A 168 24.750 23.269 9.940 1.00 8.73 N ANISOU 1378 N TYR A 168 1295 1013 1008 -4 -10 -61 N ATOM 1379 CA TYR A 168 24.568 24.698 9.672 1.00 8.77 C ANISOU 1379 CA TYR A 168 1282 1034 1014 -1 19 -75 C ATOM 1380 C TYR A 168 25.717 25.276 8.872 1.00 8.76 C ANISOU 1380 C TYR A 168 1261 1031 1038 29 27 -72 C ATOM 1381 O TYR A 168 25.796 26.506 8.704 1.00 9.53 O ANISOU 1381 O TYR A 168 1343 1134 1143 30 49 -77 O ATOM 1382 CB TYR A 168 24.399 25.456 11.022 1.00 9.28 C ANISOU 1382 CB TYR A 168 1347 1114 1063 -35 19 -79 C ATOM 1383 CG TYR A 168 23.350 24.765 11.880 1.00 8.78 C ANISOU 1383 CG TYR A 168 1305 1060 971 -70 10 -79 C ATOM 1384 CD1 TYR A 168 21.993 24.991 11.668 1.00 9.69 C ANISOU 1384 CD1 TYR A 168 1422 1187 1071 -82 29 -100 C ATOM 1385 CD2 TYR A 168 23.718 23.823 12.852 1.00 9.63 C ANISOU 1385 CD2 TYR A 168 1431 1163 1065 -91 -17 -57 C ATOM 1386 CE1 TYR A 168 21.027 24.270 12.365 1.00 10.56 C ANISOU 1386 CE1 TYR A 168 1550 1307 1155 -116 24 -102 C ATOM 1387 CE2 TYR A 168 22.768 23.107 13.557 1.00 10.13 C ANISOU 1387 CE2 TYR A 168 1514 1234 1100 -126 -23 -51 C ATOM 1388 CZ TYR A 168 21.422 23.321 13.295 1.00 10.01 C ANISOU 1388 CZ TYR A 168 1499 1233 1072 -140 0 -74 C ATOM 1389 OH TYR A 168 20.496 22.593 13.987 1.00 10.80 O ANISOU 1389 OH TYR A 168 1617 1341 1144 -178 -3 -69 O ATOM 1390 N ARG A 169 26.586 24.415 8.343 1.00 8.86 N ANISOU 1390 N ARG A 169 1269 1033 1064 51 9 -67 N ATOM 1391 CA ARG A 169 27.773 24.866 7.641 1.00 9.46 C ANISOU 1391 CA ARG A 169 1322 1111 1160 74 16 -68 C ATOM 1392 C ARG A 169 27.468 25.314 6.209 1.00 9.67 C ANISOU 1392 C ARG A 169 1333 1150 1190 101 44 -71 C ATOM 1393 O ARG A 169 26.869 24.555 5.437 1.00 10.28 O ANISOU 1393 O ARG A 169 1412 1230 1262 120 42 -76 O ATOM 1394 CB ARG A 169 28.818 23.723 7.658 1.00 11.23 C ANISOU 1394 CB ARG A 169 1544 1325 1397 87 -19 -69 C ATOM 1395 CG ARG A 169 30.158 24.128 7.061 1.00 11.66 C ANISOU 1395 CG ARG A 169 1572 1386 1471 107 -14 -77 C ATOM 1396 CD ARG A 169 31.231 23.082 7.279 1.00 12.62 C ANISOU 1396 CD ARG A 169 1690 1498 1606 118 -55 -87 C ATOM 1397 NE ARG A 169 31.587 23.038 8.699 1.00 13.93 N ANISOU 1397 NE ARG A 169 1874 1652 1768 97 -78 -83 N ATOM 1398 CZ ARG A 169 32.477 22.218 9.238 1.00 15.69 C ANISOU 1398 CZ ARG A 169 2102 1861 1999 102 -120 -91 C ATOM 1399 NH1 ARG A 169 33.174 21.382 8.468 1.00 16.18 N1+ ANISOU 1399 NH1 ARG A 169 2149 1919 2079 128 -145 -108 N1+ ATOM 1400 NH2 ARG A 169 32.682 22.231 10.551 1.00 17.02 N ANISOU 1400 NH2 ARG A 169 2287 2022 2157 84 -139 -85 N ATOM 1401 N ALA A 170 27.985 26.502 5.828 1.00 8.62 N ANISOU 1401 N ALA A 170 1184 1023 1067 105 70 -66 N ATOM 1402 CA ALA A 170 27.783 27.048 4.500 1.00 8.65 C ANISOU 1402 CA ALA A 170 1176 1041 1071 130 97 -62 C ATOM 1403 C ALA A 170 28.481 26.205 3.424 1.00 9.83 C ANISOU 1403 C ALA A 170 1306 1205 1223 160 90 -66 C ATOM 1404 O ALA A 170 29.547 25.600 3.639 1.00 9.87 O ANISOU 1404 O ALA A 170 1301 1209 1241 161 69 -73 O ATOM 1405 CB ALA A 170 28.296 28.469 4.479 1.00 10.00 C ANISOU 1405 CB ALA A 170 1333 1209 1256 122 122 -51 C ATOM 1406 N PRO A 171 27.900 26.206 2.205 1.00 9.24 N ANISOU 1406 N PRO A 171 1224 1148 1137 187 108 -66 N ATOM 1407 CA PRO A 171 28.470 25.358 1.146 1.00 9.65 C ANISOU 1407 CA PRO A 171 1252 1224 1190 218 99 -76 C ATOM 1408 C PRO A 171 29.874 25.753 0.756 1.00 10.82 C ANISOU 1408 C PRO A 171 1375 1387 1349 220 108 -72 C ATOM 1409 O PRO A 171 30.669 24.879 0.392 1.00 11.04 O ANISOU 1409 O PRO A 171 1380 1429 1384 236 87 -91 O ATOM 1410 CB PRO A 171 27.430 25.461 0.017 1.00 10.98 C ANISOU 1410 CB PRO A 171 1418 1413 1340 247 119 -79 C ATOM 1411 CG PRO A 171 26.762 26.822 0.267 1.00 12.42 C ANISOU 1411 CG PRO A 171 1620 1585 1516 231 146 -61 C ATOM 1412 CD PRO A 171 26.674 26.891 1.771 1.00 10.69 C ANISOU 1412 CD PRO A 171 1420 1337 1307 193 130 -63 C ATOM 1413 N GLU A 172 30.203 27.045 0.836 1.00 10.12 N ANISOU 1413 N GLU A 172 1286 1295 1265 204 136 -53 N ATOM 1414 CA GLU A 172 31.560 27.430 0.474 1.00 10.65 C ANISOU 1414 CA GLU A 172 1326 1377 1343 202 148 -51 C ATOM 1415 C GLU A 172 32.582 26.863 1.433 1.00 11.66 C ANISOU 1415 C GLU A 172 1449 1490 1490 189 118 -72 C ATOM 1416 O GLU A 172 33.704 26.571 0.994 1.00 12.85 O ANISOU 1416 O GLU A 172 1574 1661 1649 197 113 -88 O ATOM 1417 CB GLU A 172 31.698 28.960 0.350 1.00 11.32 C ANISOU 1417 CB GLU A 172 1410 1455 1435 186 185 -24 C ATOM 1418 CG GLU A 172 31.376 29.805 1.582 1.00 11.34 C ANISOU 1418 CG GLU A 172 1431 1423 1456 157 186 -19 C ATOM 1419 CD GLU A 172 29.921 30.218 1.748 1.00 11.46 C ANISOU 1419 CD GLU A 172 1470 1424 1458 156 189 -11 C ATOM 1420 OE1 GLU A 172 29.030 29.465 1.282 1.00 10.64 O ANISOU 1420 OE1 GLU A 172 1378 1332 1333 176 181 -18 O ATOM 1421 OE2 GLU A 172 29.679 31.311 2.321 1.00 11.70 O1- ANISOU 1421 OE2 GLU A 172 1506 1434 1505 137 199 -3 O1- ATOM 1422 N ILE A 173 32.233 26.661 2.716 1.00 10.33 N ANISOU 1422 N ILE A 173 1305 1293 1328 170 96 -76 N ATOM 1423 CA ILE A 173 33.189 26.057 3.629 1.00 10.76 C ANISOU 1423 CA ILE A 173 1357 1334 1396 163 63 -95 C ATOM 1424 C ILE A 173 33.352 24.576 3.249 1.00 13.00 C ANISOU 1424 C ILE A 173 1635 1625 1679 185 24 -116 C ATOM 1425 O ILE A 173 34.483 24.078 3.153 1.00 13.34 O ANISOU 1425 O ILE A 173 1658 1675 1736 194 3 -140 O ATOM 1426 CB ILE A 173 32.710 26.202 5.081 1.00 11.31 C ANISOU 1426 CB ILE A 173 1453 1378 1466 138 48 -90 C ATOM 1427 CG1 ILE A 173 32.614 27.686 5.480 1.00 12.28 C ANISOU 1427 CG1 ILE A 173 1573 1494 1597 118 80 -79 C ATOM 1428 CG2 ILE A 173 33.700 25.467 6.025 1.00 12.97 C ANISOU 1428 CG2 ILE A 173 1665 1577 1687 135 9 -110 C ATOM 1429 CD1 ILE A 173 32.011 27.897 6.898 1.00 14.22 C ANISOU 1429 CD1 ILE A 173 1838 1725 1839 94 67 -79 C ATOM 1430 N LEU A 174 32.242 23.887 2.984 1.00 11.79 N ANISOU 1430 N LEU A 174 1496 1470 1514 195 15 -111 N ATOM 1431 CA LEU A 174 32.258 22.479 2.585 1.00 12.79 C ANISOU 1431 CA LEU A 174 1613 1599 1647 217 -22 -132 C ATOM 1432 C LEU A 174 33.012 22.265 1.287 1.00 14.17 C ANISOU 1432 C LEU A 174 1747 1811 1826 246 -19 -154 C ATOM 1433 O LEU A 174 33.603 21.204 1.093 1.00 15.56 O ANISOU 1433 O LEU A 174 1903 1991 2017 264 -58 -182 O ATOM 1434 CB LEU A 174 30.827 21.970 2.442 1.00 12.72 C ANISOU 1434 CB LEU A 174 1622 1582 1628 222 -23 -125 C ATOM 1435 CG LEU A 174 30.046 21.859 3.764 1.00 13.02 C ANISOU 1435 CG LEU A 174 1699 1588 1660 191 -34 -110 C ATOM 1436 CD1 LEU A 174 28.562 21.848 3.525 1.00 13.83 C ANISOU 1436 CD1 LEU A 174 1815 1690 1748 191 -17 -105 C ATOM 1437 CD2 LEU A 174 30.456 20.598 4.560 1.00 15.75 C ANISOU 1437 CD2 LEU A 174 2056 1907 2021 186 -86 -116 C ATOM 1438 N LEU A 175 33.002 23.242 0.398 1.00 12.75 N ANISOU 1438 N LEU A 175 1283 1749 1814 -28 137 -735 N ATOM 1439 CA LEU A 175 33.681 23.164 -0.893 1.00 12.74 C ANISOU 1439 CA LEU A 175 1236 1760 1843 -64 213 -675 C ATOM 1440 C LEU A 175 35.129 23.623 -0.826 1.00 16.47 C ANISOU 1440 C LEU A 175 1632 2189 2438 -58 186 -666 C ATOM 1441 O LEU A 175 35.802 23.647 -1.851 1.00 16.23 O ANISOU 1441 O LEU A 175 1561 2161 2445 -106 240 -641 O ATOM 1442 CB LEU A 175 32.886 23.868 -1.982 1.00 13.36 C ANISOU 1442 CB LEU A 175 1312 1864 1901 -128 238 -621 C ATOM 1443 CG LEU A 175 31.609 23.155 -2.339 1.00 14.98 C ANISOU 1443 CG LEU A 175 1594 2130 1968 -147 301 -616 C ATOM 1444 CD1 LEU A 175 30.715 24.022 -3.239 1.00 18.72 C ANISOU 1444 CD1 LEU A 175 2057 2616 2439 -214 296 -550 C ATOM 1445 CD2 LEU A 175 31.894 21.798 -3.030 1.00 16.39 C ANISOU 1445 CD2 LEU A 175 1802 2361 2065 -179 430 -603 C ATOM 1446 N GLY A 176 35.617 23.962 0.365 1.00 15.92 N ANISOU 1446 N GLY A 176 1544 2081 2422 -16 108 -692 N ATOM 1447 CA GLY A 176 37.042 24.242 0.564 1.00 17.24 C ANISOU 1447 CA GLY A 176 1647 2215 2687 -3 88 -685 C ATOM 1448 C GLY A 176 37.512 25.671 0.482 1.00 21.07 C ANISOU 1448 C GLY A 176 2085 2688 3232 -18 50 -666 C ATOM 1449 O GLY A 176 38.728 25.912 0.397 1.00 21.06 O ANISOU 1449 O GLY A 176 2038 2674 3291 -13 49 -664 O ATOM 1450 N CYS A 177 36.608 26.627 0.544 1.00 18.19 N ANISOU 1450 N CYS A 177 1729 2326 2855 -34 19 -658 N ATOM 1451 CA CYS A 177 36.973 28.041 0.621 1.00 19.35 C ANISOU 1451 CA CYS A 177 1835 2462 3057 -45 -17 -641 C ATOM 1452 C CYS A 177 37.478 28.237 2.083 1.00 22.21 C ANISOU 1452 C CYS A 177 2181 2806 3452 -25 -53 -658 C ATOM 1453 O CYS A 177 36.723 27.966 3.030 1.00 25.19 O ANISOU 1453 O CYS A 177 2585 3171 3814 -34 -77 -688 O ATOM 1454 CB CYS A 177 35.740 28.899 0.337 1.00 20.23 C ANISOU 1454 CB CYS A 177 1951 2568 3167 -71 -40 -627 C ATOM 1455 SG CYS A 177 35.995 30.693 0.362 1.00 25.71 S ANISOU 1455 SG CYS A 177 2593 3243 3933 -89 -81 -605 S ATOM 1456 N LYS A 178 38.712 28.656 2.257 1.00 24.43 N ANISOU 1456 N LYS A 178 2425 3088 3769 -17 -55 -645 N ATOM 1457 CA LYS A 178 39.247 28.935 3.582 1.00 24.12 C ANISOU 1457 CA LYS A 178 2368 3041 3756 -24 -78 -641 C ATOM 1458 C LYS A 178 39.195 30.455 3.849 1.00 26.03 C ANISOU 1458 C LYS A 178 2581 3291 4016 -51 -76 -628 C ATOM 1459 O LYS A 178 39.457 30.859 4.972 1.00 26.34 O ANISOU 1459 O LYS A 178 2604 3331 4074 -86 -78 -620 O ATOM 1460 CB LYS A 178 40.686 28.399 3.739 1.00 28.41 C ANISOU 1460 CB LYS A 178 2885 3584 4325 -1 -75 -626 C ATOM 1461 CG LYS A 178 40.742 26.873 3.716 1.00 42.12 C ANISOU 1461 CG LYS A 178 4637 5298 6068 22 -79 -638 C ATOM 1462 CD LYS A 178 42.123 26.331 4.035 1.00 55.02 C ANISOU 1462 CD LYS A 178 6231 6914 7761 43 -88 -622 C ATOM 1463 CE LYS A 178 42.172 24.822 3.953 1.00 68.69 C ANISOU 1463 CE LYS A 178 7968 8612 9519 66 -90 -633 C ATOM 1464 NZ LYS A 178 41.410 24.169 5.056 1.00 79.46 N1+ ANISOU 1464 NZ LYS A 178 9376 9962 10853 41 -147 -632 N1+ ATOM 1465 N TYR A 179 38.818 31.283 2.835 1.00 23.18 N ANISOU 1465 N TYR A 179 2216 2938 3655 -52 -72 -621 N ATOM 1466 CA TYR A 179 38.762 32.762 2.944 1.00 23.56 C ANISOU 1466 CA TYR A 179 2235 2989 3726 -74 -70 -607 C ATOM 1467 C TYR A 179 37.351 33.234 2.724 1.00 26.50 C ANISOU 1467 C TYR A 179 2604 3331 4136 -94 -89 -613 C ATOM 1468 O TYR A 179 37.053 34.054 1.855 1.00 28.04 O ANISOU 1468 O TYR A 179 2786 3520 4348 -103 -107 -592 O ATOM 1469 CB TYR A 179 39.744 33.403 1.954 1.00 26.38 C ANISOU 1469 CB TYR A 179 2591 3379 4054 -67 -67 -596 C ATOM 1470 CG TYR A 179 41.129 32.822 2.109 1.00 27.91 C ANISOU 1470 CG TYR A 179 2786 3598 4220 -45 -48 -605 C ATOM 1471 CD1 TYR A 179 41.990 33.281 3.102 1.00 28.50 C ANISOU 1471 CD1 TYR A 179 2845 3699 4285 -44 -25 -590 C ATOM 1472 CD2 TYR A 179 41.536 31.726 1.349 1.00 29.45 C ANISOU 1472 CD2 TYR A 179 2992 3787 4411 -35 -44 -626 C ATOM 1473 CE1 TYR A 179 43.244 32.702 3.295 1.00 28.97 C ANISOU 1473 CE1 TYR A 179 2898 3775 4332 -23 -15 -592 C ATOM 1474 CE2 TYR A 179 42.783 31.135 1.539 1.00 30.44 C ANISOU 1474 CE2 TYR A 179 3104 3920 4543 -13 -29 -641 C ATOM 1475 CZ TYR A 179 43.638 31.629 2.510 1.00 34.73 C ANISOU 1475 CZ TYR A 179 3631 4485 5078 -1 -22 -622 C ATOM 1476 OH TYR A 179 44.876 31.045 2.682 1.00 34.69 O ANISOU 1476 OH TYR A 179 3608 4483 5091 21 -14 -632 O ATOM 1477 N TYR A 180 36.470 32.662 3.502 1.00 22.57 N ANISOU 1477 N TYR A 180 2117 2808 3650 -110 -93 -647 N ATOM 1478 CA TYR A 180 35.047 32.935 3.454 1.00 22.19 C ANISOU 1478 CA TYR A 180 2065 2723 3643 -130 -110 -672 C ATOM 1479 C TYR A 180 34.703 34.270 4.165 1.00 23.89 C ANISOU 1479 C TYR A 180 2223 2906 3949 -175 -98 -686 C ATOM 1480 O TYR A 180 35.546 34.942 4.792 1.00 25.67 O ANISOU 1480 O TYR A 180 2418 3147 4187 -197 -65 -673 O ATOM 1481 CB TYR A 180 34.238 31.715 3.947 1.00 23.13 C ANISOU 1481 CB TYR A 180 2234 2836 3718 -137 -118 -726 C ATOM 1482 CG TYR A 180 34.724 31.259 5.303 1.00 26.67 C ANISOU 1482 CG TYR A 180 2691 3285 4157 -178 -116 -763 C ATOM 1483 CD1 TYR A 180 34.443 32.000 6.449 1.00 29.66 C ANISOU 1483 CD1 TYR A 180 3035 3636 4598 -259 -107 -804 C ATOM 1484 CD2 TYR A 180 35.566 30.161 5.426 1.00 26.81 C ANISOU 1484 CD2 TYR A 180 2741 3325 4119 -154 -122 -749 C ATOM 1485 CE1 TYR A 180 34.975 31.649 7.683 1.00 33.84 C ANISOU 1485 CE1 TYR A 180 3569 4169 5119 -335 -108 -823 C ATOM 1486 CE2 TYR A 180 36.070 29.774 6.663 1.00 29.06 C ANISOU 1486 CE2 TYR A 180 3030 3606 4405 -209 -138 -764 C ATOM 1487 CZ TYR A 180 35.789 30.535 7.785 1.00 41.55 C ANISOU 1487 CZ TYR A 180 4584 5169 6035 -308 -133 -796 C ATOM 1488 OH TYR A 180 36.319 30.186 8.998 1.00 49.95 O ANISOU 1488 OH TYR A 180 5651 6231 7098 -398 -150 -799 O ATOM 1489 N SER A 181 33.444 34.650 4.017 1.00 16.89 N ANISOU 1489 N SER A 181 1994 2143 2282 -139 313 -99 N ATOM 1490 CA SER A 181 32.904 35.950 4.388 1.00 14.98 C ANISOU 1490 CA SER A 181 1754 1842 2096 -172 341 -110 C ATOM 1491 C SER A 181 31.840 35.858 5.467 1.00 13.93 C ANISOU 1491 C SER A 181 1630 1705 1958 -170 307 -141 C ATOM 1492 O SER A 181 31.432 34.769 5.900 1.00 13.23 O ANISOU 1492 O SER A 181 1551 1655 1822 -146 264 -146 O ATOM 1493 CB SER A 181 32.306 36.581 3.130 1.00 17.02 C ANISOU 1493 CB SER A 181 2051 2047 2369 -151 375 -48 C ATOM 1494 OG SER A 181 31.043 36.002 2.827 1.00 15.28 O ANISOU 1494 OG SER A 181 1870 1824 2111 -107 343 -22 O ATOM 1495 N THR A 182 31.342 37.020 5.872 1.00 12.54 N ANISOU 1495 N THR A 182 1451 1478 1834 -196 330 -161 N ATOM 1496 CA THR A 182 30.239 37.119 6.828 1.00 12.03 C ANISOU 1496 CA THR A 182 1394 1407 1769 -196 306 -192 C ATOM 1497 C THR A 182 29.020 36.357 6.321 1.00 12.13 C ANISOU 1497 C THR A 182 1449 1420 1740 -150 278 -151 C ATOM 1498 O THR A 182 28.152 35.989 7.121 1.00 12.09 O ANISOU 1498 O THR A 182 1448 1431 1715 -145 250 -174 O ATOM 1499 CB THR A 182 29.939 38.589 7.079 1.00 15.47 C ANISOU 1499 CB THR A 182 1823 1779 2277 -225 341 -216 C ATOM 1500 CG2 THR A 182 31.082 39.326 7.805 1.00 15.94 C ANISOU 1500 CG2 THR A 182 1831 1841 2384 -278 365 -277 C ATOM 1501 OG1 THR A 182 29.632 39.214 5.836 1.00 15.73 O ANISOU 1501 OG1 THR A 182 1890 1751 2337 -207 375 -156 O ATOM 1502 N ALA A 183 28.924 36.091 5.024 1.00 11.45 N ANISOU 1502 N ALA A 183 1392 1323 1637 -117 286 -96 N ATOM 1503 CA ALA A 183 27.816 35.329 4.497 1.00 10.70 C ANISOU 1503 CA ALA A 183 1330 1234 1503 -75 258 -67 C ATOM 1504 C ALA A 183 27.681 33.944 5.128 1.00 10.92 C ANISOU 1504 C ALA A 183 1355 1312 1482 -66 214 -85 C ATOM 1505 O ALA A 183 26.584 33.369 5.107 1.00 10.39 O ANISOU 1505 O ALA A 183 1307 1247 1393 -44 190 -79 O ATOM 1506 CB ALA A 183 27.910 35.198 2.972 1.00 11.63 C ANISOU 1506 CB ALA A 183 1472 1346 1602 -38 272 -11 C ATOM 1507 N VAL A 184 28.785 33.374 5.645 1.00 10.57 N ANISOU 1507 N VAL A 184 1286 1307 1421 -80 205 -104 N ATOM 1508 CA VAL A 184 28.648 32.034 6.242 1.00 9.55 C ANISOU 1508 CA VAL A 184 1160 1220 1249 -66 165 -112 C ATOM 1509 C VAL A 184 27.665 32.056 7.422 1.00 9.71 C ANISOU 1509 C VAL A 184 1180 1243 1267 -80 149 -139 C ATOM 1510 O VAL A 184 26.962 31.072 7.678 1.00 9.83 O ANISOU 1510 O VAL A 184 1212 1272 1252 -66 123 -131 O ATOM 1511 CB VAL A 184 29.992 31.428 6.663 1.00 11.62 C ANISOU 1511 CB VAL A 184 1395 1527 1492 -71 155 -127 C ATOM 1512 CG1 VAL A 184 30.941 31.357 5.496 1.00 12.19 C ANISOU 1512 CG1 VAL A 184 1464 1604 1564 -56 172 -104 C ATOM 1513 CG2 VAL A 184 30.646 32.142 7.858 1.00 12.39 C ANISOU 1513 CG2 VAL A 184 1454 1646 1609 -108 162 -175 C ATOM 1514 N ASP A 185 27.586 33.184 8.158 1.00 9.32 N ANISOU 1514 N ASP A 185 1111 1180 1251 -111 167 -173 N ATOM 1515 CA ASP A 185 26.690 33.270 9.305 1.00 9.41 C ANISOU 1515 CA ASP A 185 1116 1203 1257 -124 155 -204 C ATOM 1516 C ASP A 185 25.255 33.427 8.876 1.00 10.28 C ANISOU 1516 C ASP A 185 1251 1281 1375 -107 155 -189 C ATOM 1517 O ASP A 185 24.351 32.939 9.561 1.00 9.40 O ANISOU 1517 O ASP A 185 1143 1187 1242 -108 138 -200 O ATOM 1518 CB ASP A 185 27.104 34.423 10.181 1.00 10.94 C ANISOU 1518 CB ASP A 185 1275 1396 1485 -158 174 -255 C ATOM 1519 CG ASP A 185 28.415 34.240 10.910 1.00 10.94 C ANISOU 1519 CG ASP A 185 1240 1446 1472 -176 167 -287 C ATOM 1520 OD1 ASP A 185 28.813 33.065 11.160 1.00 11.80 O ANISOU 1520 OD1 ASP A 185 1351 1600 1531 -158 141 -272 O ATOM 1521 OD2 ASP A 185 29.011 35.260 11.298 1.00 12.01 O1- ANISOU 1521 OD2 ASP A 185 1343 1575 1647 -205 188 -331 O1- ATOM 1522 N ILE A 186 25.018 34.113 7.747 1.00 10.06 N ANISOU 1522 N ILE A 186 1240 1208 1375 -91 175 -164 N ATOM 1523 CA ILE A 186 23.670 34.244 7.198 1.00 9.28 C ANISOU 1523 CA ILE A 186 1162 1084 1280 -66 170 -150 C ATOM 1524 C ILE A 186 23.159 32.891 6.768 1.00 9.46 C ANISOU 1524 C ILE A 186 1202 1131 1260 -42 142 -128 C ATOM 1525 O ILE A 186 21.997 32.574 7.033 1.00 9.30 O ANISOU 1525 O ILE A 186 1186 1115 1231 -36 128 -138 O ATOM 1526 CB ILE A 186 23.657 35.271 6.040 1.00 10.62 C ANISOU 1526 CB ILE A 186 1347 1205 1484 -46 198 -119 C ATOM 1527 CG1 ILE A 186 23.925 36.692 6.596 1.00 12.30 C ANISOU 1527 CG1 ILE A 186 1542 1377 1752 -75 228 -148 C ATOM 1528 CG2 ILE A 186 22.337 35.222 5.254 1.00 11.40 C ANISOU 1528 CG2 ILE A 186 1468 1290 1574 -6 186 -99 C ATOM 1529 CD1 ILE A 186 22.704 37.241 7.455 1.00 15.78 C ANISOU 1529 CD1 ILE A 186 1975 1807 2212 -78 222 -189 C ATOM 1530 N TRP A 187 24.004 32.063 6.143 1.00 8.61 N ANISOU 1530 N TRP A 187 1102 1040 1130 -29 134 -104 N ATOM 1531 CA TRP A 187 23.578 30.708 5.781 1.00 8.58 C ANISOU 1531 CA TRP A 187 1114 1055 1094 -8 107 -91 C ATOM 1532 C TRP A 187 23.152 29.950 7.045 1.00 8.97 C ANISOU 1532 C TRP A 187 1156 1126 1126 -29 90 -111 C ATOM 1533 O TRP A 187 22.092 29.327 7.079 1.00 8.90 O ANISOU 1533 O TRP A 187 1155 1117 1108 -25 77 -113 O ATOM 1534 CB TRP A 187 24.758 29.983 5.108 1.00 9.30 C ANISOU 1534 CB TRP A 187 1207 1161 1165 8 103 -71 C ATOM 1535 CG TRP A 187 24.410 28.565 4.780 1.00 8.72 C ANISOU 1535 CG TRP A 187 1148 1100 1066 29 75 -65 C ATOM 1536 CD1 TRP A 187 24.439 27.473 5.616 1.00 10.52 C ANISOU 1536 CD1 TRP A 187 1377 1341 1278 19 55 -71 C ATOM 1537 CD2 TRP A 187 23.954 28.095 3.516 1.00 9.00 C ANISOU 1537 CD2 TRP A 187 1198 1132 1091 64 65 -52 C ATOM 1538 CE2 TRP A 187 23.668 26.716 3.659 1.00 9.97 C ANISOU 1538 CE2 TRP A 187 1329 1261 1200 69 39 -59 C ATOM 1539 CE3 TRP A 187 23.685 28.721 2.289 1.00 10.22 C ANISOU 1539 CE3 TRP A 187 1360 1280 1245 93 76 -37 C ATOM 1540 NE1 TRP A 187 24.033 26.351 4.930 1.00 9.73 N ANISOU 1540 NE1 TRP A 187 1293 1238 1168 42 35 -65 N ATOM 1541 CZ2 TRP A 187 23.190 25.950 2.590 1.00 10.10 C ANISOU 1541 CZ2 TRP A 187 1354 1277 1206 100 23 -61 C ATOM 1542 CZ3 TRP A 187 23.249 27.946 1.237 1.00 10.90 C ANISOU 1542 CZ3 TRP A 187 1454 1377 1310 128 57 -35 C ATOM 1543 CH2 TRP A 187 22.992 26.582 1.413 1.00 11.23 C ANISOU 1543 CH2 TRP A 187 1498 1424 1342 130 30 -53 C ATOM 1544 N SER A 188 24.009 29.931 8.060 1.00 8.59 N ANISOU 1544 N SER A 188 1092 1101 1070 -51 91 -124 N ATOM 1545 CA SER A 188 23.691 29.179 9.274 1.00 8.52 C ANISOU 1545 CA SER A 188 1079 1120 1036 -67 77 -134 C ATOM 1546 C SER A 188 22.383 29.647 9.866 1.00 8.38 C ANISOU 1546 C SER A 188 1057 1099 1027 -82 83 -155 C ATOM 1547 O SER A 188 21.541 28.845 10.267 1.00 8.88 O ANISOU 1547 O SER A 188 1128 1172 1075 -87 74 -151 O ATOM 1548 CB SER A 188 24.784 29.362 10.306 1.00 9.94 C ANISOU 1548 CB SER A 188 1237 1336 1204 -84 77 -152 C ATOM 1549 OG SER A 188 26.052 28.943 9.808 1.00 9.51 O ANISOU 1549 OG SER A 188 1182 1291 1142 -69 71 -137 O ATOM 1550 N LEU A 189 22.192 30.966 9.927 1.00 8.73 N ANISOU 1550 N LEU A 189 1087 1128 1101 -91 101 -180 N ATOM 1551 CA LEU A 189 20.948 31.481 10.497 1.00 8.85 C ANISOU 1551 CA LEU A 189 1093 1143 1127 -101 106 -207 C ATOM 1552 C LEU A 189 19.738 31.125 9.631 1.00 9.14 C ANISOU 1552 C LEU A 189 1145 1161 1167 -80 99 -194 C ATOM 1553 O LEU A 189 18.664 30.843 10.202 1.00 9.46 O ANISOU 1553 O LEU A 189 1178 1216 1200 -90 96 -210 O ATOM 1554 CB LEU A 189 21.060 32.996 10.721 1.00 9.46 C ANISOU 1554 CB LEU A 189 1152 1200 1242 -111 127 -240 C ATOM 1555 CG LEU A 189 19.909 33.652 11.429 1.00 11.05 C ANISOU 1555 CG LEU A 189 1338 1405 1456 -119 133 -278 C ATOM 1556 CD1 LEU A 189 19.677 33.024 12.823 1.00 12.91 C ANISOU 1556 CD1 LEU A 189 1557 1696 1652 -143 126 -300 C ATOM 1557 CD2 LEU A 189 20.228 35.132 11.621 1.00 12.87 C ANISOU 1557 CD2 LEU A 189 1551 1606 1733 -128 153 -313 C ATOM 1558 N GLY A 190 19.913 31.057 8.307 1.00 8.80 N ANISOU 1558 N GLY A 190 1118 1093 1132 -51 96 -168 N ATOM 1559 CA GLY A 190 18.795 30.636 7.473 1.00 8.78 C ANISOU 1559 CA GLY A 190 1124 1083 1127 -27 84 -163 C ATOM 1560 C GLY A 190 18.413 29.195 7.785 1.00 8.33 C ANISOU 1560 C GLY A 190 1072 1046 1048 -39 68 -160 C ATOM 1561 O GLY A 190 17.224 28.851 7.877 1.00 9.90 O ANISOU 1561 O GLY A 190 1264 1250 1249 -43 63 -176 O ATOM 1562 N CYS A 191 19.417 28.351 7.998 1.00 8.53 N ANISOU 1562 N CYS A 191 1106 1079 1055 -45 61 -141 N ATOM 1563 CA CYS A 191 19.128 26.958 8.354 1.00 8.92 C ANISOU 1563 CA CYS A 191 1164 1135 1089 -55 49 -132 C ATOM 1564 C CYS A 191 18.369 26.869 9.677 1.00 9.73 C ANISOU 1564 C CYS A 191 1254 1258 1184 -89 59 -146 C ATOM 1565 O CYS A 191 17.495 25.999 9.846 1.00 9.61 O ANISOU 1565 O CYS A 191 1241 1241 1168 -102 57 -146 O ATOM 1566 CB CYS A 191 20.425 26.160 8.445 1.00 9.05 C ANISOU 1566 CB CYS A 191 1193 1156 1089 -50 41 -108 C ATOM 1567 SG CYS A 191 21.274 25.888 6.873 1.00 10.00 S ANISOU 1567 SG CYS A 191 1326 1262 1212 -11 30 -93 S ATOM 1568 N ILE A 192 18.764 27.713 10.652 1.00 9.07 N ANISOU 1568 N ILE A 192 1156 1196 1094 -104 70 -159 N ATOM 1569 CA ILE A 192 18.099 27.721 11.945 1.00 9.24 C ANISOU 1569 CA ILE A 192 1163 1248 1100 -133 81 -175 C ATOM 1570 C ILE A 192 16.678 28.236 11.830 1.00 10.30 C ANISOU 1570 C ILE A 192 1282 1379 1253 -138 89 -205 C ATOM 1571 O ILE A 192 15.768 27.687 12.473 1.00 10.29 O ANISOU 1571 O ILE A 192 1272 1397 1241 -160 96 -210 O ATOM 1572 CB ILE A 192 18.964 28.522 12.955 1.00 9.97 C ANISOU 1572 CB ILE A 192 1240 1371 1178 -144 88 -192 C ATOM 1573 CG1 ILE A 192 20.273 27.774 13.190 1.00 10.58 C ANISOU 1573 CG1 ILE A 192 1328 1462 1229 -137 77 -164 C ATOM 1574 CG2 ILE A 192 18.204 28.758 14.291 1.00 11.95 C ANISOU 1574 CG2 ILE A 192 1468 1663 1408 -170 101 -218 C ATOM 1575 CD1 ILE A 192 21.362 28.579 13.961 1.00 13.12 C ANISOU 1575 CD1 ILE A 192 1627 1817 1539 -142 79 -187 C ATOM 1576 N PHE A 193 16.448 29.281 11.029 1.00 9.67 N ANISOU 1576 N PHE A 193 1195 1277 1200 -116 89 -223 N ATOM 1577 CA PHE A 193 15.116 29.805 10.759 1.00 9.68 C ANISOU 1577 CA PHE A 193 1180 1276 1221 -109 92 -252 C ATOM 1578 C PHE A 193 14.208 28.684 10.219 1.00 10.77 C ANISOU 1578 C PHE A 193 1321 1414 1358 -109 82 -247 C ATOM 1579 O PHE A 193 13.109 28.454 10.766 1.00 10.38 O ANISOU 1579 O PHE A 193 1252 1385 1308 -130 90 -270 O ATOM 1580 CB PHE A 193 15.273 30.974 9.798 1.00 11.06 C ANISOU 1580 CB PHE A 193 1359 1420 1424 -75 92 -256 C ATOM 1581 CG PHE A 193 14.034 31.620 9.238 1.00 11.09 C ANISOU 1581 CG PHE A 193 1350 1417 1448 -49 89 -280 C ATOM 1582 CD1 PHE A 193 12.849 31.668 9.971 1.00 12.79 C ANISOU 1582 CD1 PHE A 193 1538 1657 1664 -65 94 -317 C ATOM 1583 CD2 PHE A 193 14.080 32.271 8.021 1.00 11.96 C ANISOU 1583 CD2 PHE A 193 1472 1498 1575 -7 84 -265 C ATOM 1584 CE1 PHE A 193 11.720 32.345 9.467 1.00 13.64 C ANISOU 1584 CE1 PHE A 193 1629 1762 1792 -35 89 -344 C ATOM 1585 CE2 PHE A 193 12.966 32.969 7.532 1.00 12.84 C ANISOU 1585 CE2 PHE A 193 1572 1605 1704 26 79 -286 C ATOM 1586 CZ PHE A 193 11.790 32.981 8.248 1.00 12.23 C ANISOU 1586 CZ PHE A 193 1465 1553 1629 13 80 -328 C ATOM 1587 N ALA A 194 14.685 27.938 9.217 1.00 9.89 N ANISOU 1587 N ALA A 194 1229 1281 1245 -90 67 -222 N ATOM 1588 CA ALA A 194 13.879 26.867 8.651 1.00 9.46 C ANISOU 1588 CA ALA A 194 1174 1224 1197 -91 57 -227 C ATOM 1589 C ALA A 194 13.560 25.811 9.718 1.00 10.23 C ANISOU 1589 C ALA A 194 1270 1332 1285 -134 68 -220 C ATOM 1590 O ALA A 194 12.435 25.263 9.743 1.00 10.71 O ANISOU 1590 O ALA A 194 1314 1397 1358 -153 73 -240 O ATOM 1591 CB ALA A 194 14.650 26.224 7.517 1.00 9.97 C ANISOU 1591 CB ALA A 194 1261 1268 1260 -63 39 -205 C ATOM 1592 N GLU A 195 14.506 25.504 10.586 1.00 9.58 N ANISOU 1592 N GLU A 195 1202 1255 1181 -150 75 -191 N ATOM 1593 CA GLU A 195 14.326 24.501 11.627 1.00 10.85 C ANISOU 1593 CA GLU A 195 1368 1426 1327 -185 89 -171 C ATOM 1594 C GLU A 195 13.311 24.959 12.655 1.00 11.35 C ANISOU 1594 C GLU A 195 1405 1525 1383 -215 112 -195 C ATOM 1595 O GLU A 195 12.515 24.156 13.144 1.00 11.59 O ANISOU 1595 O GLU A 195 1429 1560 1413 -247 128 -190 O ATOM 1596 CB GLU A 195 15.688 24.211 12.252 1.00 11.56 C ANISOU 1596 CB GLU A 195 1481 1522 1391 -181 87 -133 C ATOM 1597 CG GLU A 195 15.663 23.130 13.331 1.00 12.09 C ANISOU 1597 CG GLU A 195 1560 1598 1435 -209 101 -98 C ATOM 1598 CD GLU A 195 17.042 22.715 13.799 1.00 13.05 C ANISOU 1598 CD GLU A 195 1704 1727 1528 -193 92 -59 C ATOM 1599 OE1 GLU A 195 18.047 23.041 13.127 1.00 11.75 O ANISOU 1599 OE1 GLU A 195 1545 1552 1367 -163 73 -61 O ATOM 1600 OE2 GLU A 195 17.126 22.036 14.851 1.00 15.64 O1- ANISOU 1600 OE2 GLU A 195 2042 2072 1827 -208 104 -25 O1- ATOM 1601 N MET A 196 13.302 26.243 13.027 1.00 10.17 N ANISOU 1601 N MET A 196 1236 1399 1228 -208 116 -223 N ATOM 1602 CA MET A 196 12.292 26.709 13.976 1.00 10.43 C ANISOU 1602 CA MET A 196 1238 1471 1253 -233 137 -254 C ATOM 1603 C MET A 196 10.910 26.564 13.348 1.00 11.87 C ANISOU 1603 C MET A 196 1398 1648 1464 -236 138 -285 C ATOM 1604 O MET A 196 9.962 26.191 14.048 1.00 12.27 O ANISOU 1604 O MET A 196 1427 1726 1509 -269 159 -298 O ATOM 1605 CB MET A 196 12.520 28.194 14.290 1.00 11.21 C ANISOU 1605 CB MET A 196 1320 1588 1354 -217 138 -290 C ATOM 1606 CG MET A 196 13.714 28.454 15.202 1.00 11.28 C ANISOU 1606 CG MET A 196 1335 1619 1332 -221 140 -278 C ATOM 1607 SD MET A 196 13.699 30.167 15.910 1.00 14.25 S ANISOU 1607 SD MET A 196 1678 2022 1715 -217 149 -338 S ATOM 1608 CE MET A 196 14.417 31.087 14.566 1.00 15.18 C ANISOU 1608 CE MET A 196 1811 2080 1879 -180 134 -339 C ATOM 1609 N VAL A 197 10.760 26.873 12.061 1.00 10.59 N ANISOU 1609 N VAL A 197 1237 1459 1328 -202 117 -300 N ATOM 1610 CA VAL A 197 9.477 26.828 11.388 1.00 11.14 C ANISOU 1610 CA VAL A 197 1280 1532 1421 -196 112 -337 C ATOM 1611 C VAL A 197 8.958 25.412 11.218 1.00 12.22 C ANISOU 1611 C VAL A 197 1415 1658 1568 -226 116 -330 C ATOM 1612 O VAL A 197 7.770 25.156 11.465 1.00 13.14 O ANISOU 1612 O VAL A 197 1499 1795 1697 -253 129 -362 O ATOM 1613 CB VAL A 197 9.571 27.527 10.003 1.00 12.81 C ANISOU 1613 CB VAL A 197 1496 1722 1650 -142 85 -348 C ATOM 1614 CG1 VAL A 197 8.309 27.297 9.152 1.00 14.92 C ANISOU 1614 CG1 VAL A 197 1735 1999 1937 -128 72 -388 C ATOM 1615 CG2 VAL A 197 9.827 29.026 10.167 1.00 14.08 C ANISOU 1615 CG2 VAL A 197 1653 1884 1813 -115 87 -360 C ATOM 1616 N THR A 198 9.818 24.506 10.803 1.00 11.18 N ANISOU 1616 N THR A 198 1317 1494 1437 -224 106 -294 N ATOM 1617 CA THR A 198 9.355 23.158 10.455 1.00 11.20 C ANISOU 1617 CA THR A 198 1320 1474 1462 -249 107 -293 C ATOM 1618 C THR A 198 9.474 22.167 11.564 1.00 13.49 C ANISOU 1618 C THR A 198 1624 1756 1744 -297 135 -255 C ATOM 1619 O THR A 198 8.861 21.096 11.472 1.00 13.77 O ANISOU 1619 O THR A 198 1655 1770 1806 -329 147 -258 O ATOM 1620 CB THR A 198 10.110 22.639 9.243 1.00 13.04 C ANISOU 1620 CB THR A 198 1579 1672 1706 -215 79 -282 C ATOM 1621 CG2 THR A 198 9.939 23.515 8.010 1.00 12.42 C ANISOU 1621 CG2 THR A 198 1487 1602 1630 -163 53 -314 C ATOM 1622 OG1 THR A 198 11.489 22.480 9.585 1.00 12.77 O ANISOU 1622 OG1 THR A 198 1581 1621 1651 -206 78 -233 O ATOM 1623 N ARG A 199 10.258 22.485 12.589 1.00 13.06 N ANISOU 1623 N ARG A 199 1587 1720 1654 -301 147 -219 N ATOM 1624 CA ARG A 199 10.511 21.610 13.751 1.00 14.10 C ANISOU 1624 CA ARG A 199 1738 1854 1764 -337 174 -170 C ATOM 1625 C ARG A 199 11.372 20.421 13.383 1.00 16.30 C ANISOU 1625 C ARG A 199 2057 2082 2054 -330 164 -125 C ATOM 1626 O ARG A 199 11.334 19.375 14.056 1.00 17.48 O ANISOU 1626 O ARG A 199 2225 2213 2204 -360 186 -83 O ATOM 1627 CB ARG A 199 9.230 21.149 14.466 1.00 16.45 C ANISOU 1627 CB ARG A 199 2009 2171 2071 -389 210 -180 C ATOM 1628 CG ARG A 199 8.210 22.258 14.736 1.00 20.88 C ANISOU 1628 CG ARG A 199 2522 2783 2627 -394 219 -236 C ATOM 1629 CD ARG A 199 6.909 21.679 15.313 1.00 19.28 C ANISOU 1629 CD ARG A 199 2288 2600 2438 -448 258 -250 C ATOM 1630 NE ARG A 199 5.728 22.351 14.802 1.00 27.24 N ANISOU 1630 NE ARG A 199 3246 3635 3471 -445 253 -321 N ATOM 1631 CZ ARG A 199 4.504 21.912 15.019 1.00 33.73 C ANISOU 1631 CZ ARG A 199 4028 4473 4313 -489 281 -350 C ATOM 1632 NH1 ARG A 199 4.304 20.836 15.764 1.00 27.26 N1+ ANISOU 1632 NH1 ARG A 199 3218 3644 3496 -544 321 -309 N1+ ATOM 1633 NH2 ARG A 199 3.463 22.566 14.527 1.00 35.91 N ANISOU 1633 NH2 ARG A 199 4255 4780 4610 -478 272 -419 N ATOM 1634 N ARG A 200 12.172 20.555 12.326 1.00 14.02 N ANISOU 1634 N ARG A 200 1782 1768 1775 -288 132 -131 N ATOM 1635 CA AARG A 200 13.084 19.524 11.910 0.60 14.24 C ANISOU 1635 CA AARG A 200 1846 1751 1813 -272 118 -96 C ATOM 1636 CA BARG A 200 13.113 19.531 11.878 0.40 14.11 C ANISOU 1636 CA BARG A 200 1830 1734 1797 -271 117 -96 C ATOM 1637 C ARG A 200 14.316 20.232 11.318 1.00 14.66 C ANISOU 1637 C ARG A 200 1912 1812 1849 -224 90 -93 C ATOM 1638 O ARG A 200 14.165 21.261 10.655 1.00 12.87 O ANISOU 1638 O ARG A 200 1666 1602 1623 -202 78 -128 O ATOM 1639 CB AARG A 200 12.383 18.650 10.877 0.60 17.28 C ANISOU 1639 CB AARG A 200 2225 2094 2248 -280 110 -125 C ATOM 1640 CB BARG A 200 12.534 18.659 10.756 0.40 16.87 C ANISOU 1640 CB BARG A 200 2176 2040 2195 -273 106 -124 C ATOM 1641 CG AARG A 200 13.140 17.417 10.499 0.60 18.72 C ANISOU 1641 CG AARG A 200 2440 2221 2450 -269 100 -96 C ATOM 1642 CG BARG A 200 11.497 17.670 11.184 0.40 21.66 C ANISOU 1642 CG BARG A 200 2774 2622 2834 -325 134 -125 C ATOM 1643 CD AARG A 200 12.277 16.571 9.587 0.60 22.26 C ANISOU 1643 CD AARG A 200 2874 2631 2953 -285 96 -138 C ATOM 1644 CD BARG A 200 12.007 16.571 12.097 0.40 26.46 C ANISOU 1644 CD BARG A 200 3419 3196 3440 -346 156 -59 C ATOM 1645 NE AARG A 200 11.941 15.294 10.202 0.60 34.97 N ANISOU 1645 NE AARG A 200 4500 4191 4595 -329 124 -109 N ATOM 1646 NE BARG A 200 10.883 15.791 12.607 0.40 25.88 N ANISOU 1646 NE BARG A 200 3334 3102 3399 -404 194 -57 N ATOM 1647 CZ AARG A 200 11.411 14.265 9.548 0.60 46.42 C ANISOU 1647 CZ AARG A 200 5944 5589 6102 -348 124 -139 C ATOM 1648 CZ BARG A 200 10.308 14.803 11.935 0.40 32.10 C ANISOU 1648 CZ BARG A 200 4116 3835 4245 -428 197 -82 C ATOM 1649 NH1AARG A 200 11.159 14.353 8.246 0.60 20.78 N1+ ANISOU 1649 NH1AARG A 200 2673 2343 2878 -323 94 -203 N1+ ATOM 1650 NH1BARG A 200 10.765 14.451 10.739 0.40 16.37 N1+ ANISOU 1650 NH1BARG A 200 2131 1807 2282 -393 163 -111 N1+ ATOM 1651 NH2AARG A 200 11.143 13.137 10.186 0.60 44.06 N ANISOU 1651 NH2AARG A 200 5664 5237 5839 -391 156 -104 N ATOM 1652 NH2BARG A 200 9.269 14.163 12.449 0.40 22.98 N ANISOU 1652 NH2BARG A 200 2945 2663 3123 -487 237 -81 N ATOM 1653 N ALA A 201 15.513 19.682 11.519 1.00 13.13 N ANISOU 1653 N ALA A 201 1747 1603 1639 -205 81 -53 N ATOM 1654 CA ALA A 201 16.686 20.308 10.915 1.00 12.44 C ANISOU 1654 CA ALA A 201 1664 1523 1537 -164 59 -54 C ATOM 1655 C ALA A 201 16.558 20.291 9.386 1.00 12.36 C ANISOU 1655 C ALA A 201 1650 1490 1554 -137 38 -86 C ATOM 1656 O ALA A 201 15.986 19.347 8.826 1.00 14.09 O ANISOU 1656 O ALA A 201 1872 1677 1804 -143 34 -98 O ATOM 1657 CB ALA A 201 17.932 19.569 11.343 1.00 14.59 C ANISOU 1657 CB ALA A 201 1965 1787 1791 -146 51 -10 C ATOM 1658 N LEU A 202 17.028 21.332 8.741 1.00 10.96 N ANISOU 1658 N LEU A 202 1465 1332 1369 -108 28 -101 N ATOM 1659 CA LEU A 202 16.921 21.461 7.300 1.00 11.42 C ANISOU 1659 CA LEU A 202 1518 1381 1441 -76 10 -127 C ATOM 1660 C LEU A 202 17.864 20.489 6.593 1.00 11.97 C ANISOU 1660 C LEU A 202 1607 1427 1514 -49 -7 -114 C ATOM 1661 O LEU A 202 17.436 19.757 5.676 1.00 11.94 O ANISOU 1661 O LEU A 202 1602 1403 1531 -38 -20 -138 O ATOM 1662 CB LEU A 202 17.215 22.930 6.928 1.00 11.13 C ANISOU 1662 CB LEU A 202 1470 1368 1391 -54 11 -135 C ATOM 1663 CG LEU A 202 17.086 23.260 5.432 1.00 12.43 C ANISOU 1663 CG LEU A 202 1630 1533 1561 -14 -4 -153 C ATOM 1664 CD1 LEU A 202 15.652 22.981 4.916 1.00 14.26 C ANISOU 1664 CD1 LEU A 202 1843 1766 1810 -16 -11 -191 C ATOM 1665 CD2 LEU A 202 17.417 24.697 5.191 1.00 12.34 C ANISOU 1665 CD2 LEU A 202 1612 1535 1540 5 4 -149 C ATOM 1666 N PHE A 203 19.132 20.465 6.995 1.00 10.28 N ANISOU 1666 N PHE A 203 1408 1218 1281 -37 -9 -84 N ATOM 1667 CA PHE A 203 20.175 19.676 6.336 1.00 9.99 C ANISOU 1667 CA PHE A 203 1385 1165 1244 -5 -26 -75 C ATOM 1668 C PHE A 203 20.969 18.899 7.384 1.00 10.70 C ANISOU 1668 C PHE A 203 1495 1247 1325 -10 -25 -38 C ATOM 1669 O PHE A 203 22.071 19.284 7.746 1.00 9.97 O ANISOU 1669 O PHE A 203 1402 1178 1207 5 -28 -21 O ATOM 1670 CB PHE A 203 21.136 20.578 5.539 1.00 10.02 C ANISOU 1670 CB PHE A 203 1382 1195 1230 28 -31 -78 C ATOM 1671 CG PHE A 203 20.479 21.451 4.515 1.00 10.44 C ANISOU 1671 CG PHE A 203 1420 1260 1284 42 -31 -103 C ATOM 1672 CD1 PHE A 203 19.664 20.905 3.534 1.00 11.86 C ANISOU 1672 CD1 PHE A 203 1596 1431 1479 56 -44 -131 C ATOM 1673 CD2 PHE A 203 20.720 22.812 4.495 1.00 11.37 C ANISOU 1673 CD2 PHE A 203 1528 1399 1391 45 -18 -98 C ATOM 1674 CE1 PHE A 203 19.103 21.720 2.545 1.00 13.04 C ANISOU 1674 CE1 PHE A 203 1733 1602 1622 79 -46 -151 C ATOM 1675 CE2 PHE A 203 20.175 23.618 3.490 1.00 13.13 C ANISOU 1675 CE2 PHE A 203 1743 1632 1614 67 -17 -111 C ATOM 1676 CZ PHE A 203 19.352 23.067 2.548 1.00 12.14 C ANISOU 1676 CZ PHE A 203 1614 1505 1493 86 -32 -136 C ATOM 1677 N PRO A 204 20.415 17.788 7.925 1.00 10.95 N ANISOU 1677 N PRO A 204 1542 1243 1374 -30 -20 -23 N ATOM 1678 CA PRO A 204 21.101 17.074 9.005 1.00 11.54 C ANISOU 1678 CA PRO A 204 1639 1311 1435 -30 -18 22 C ATOM 1679 C PRO A 204 22.163 16.089 8.504 1.00 12.87 C ANISOU 1679 C PRO A 204 1827 1451 1612 10 -38 34 C ATOM 1680 O PRO A 204 22.053 14.846 8.737 1.00 13.00 O ANISOU 1680 O PRO A 204 1867 1418 1653 10 -38 56 O ATOM 1681 CB PRO A 204 19.946 16.407 9.748 1.00 12.64 C ANISOU 1681 CB PRO A 204 1787 1422 1593 -72 4 37 C ATOM 1682 CG PRO A 204 18.957 16.101 8.658 1.00 15.08 C ANISOU 1682 CG PRO A 204 2085 1700 1946 -82 1 -7 C ATOM 1683 CD PRO A 204 19.048 17.280 7.708 1.00 12.38 C ANISOU 1683 CD PRO A 204 1718 1395 1590 -60 -12 -45 C ATOM 1684 N GLY A 205 23.208 16.626 7.904 1.00 10.73 N ANISOU 1684 N GLY A 205 1545 1210 1323 44 -53 22 N ATOM 1685 CA GLY A 205 24.285 15.769 7.380 1.00 10.65 C ANISOU 1685 CA GLY A 205 1546 1181 1318 88 -73 26 C ATOM 1686 C GLY A 205 25.097 15.100 8.458 1.00 11.28 C ANISOU 1686 C GLY A 205 1646 1260 1381 104 -78 71 C ATOM 1687 O GLY A 205 25.276 15.639 9.556 1.00 12.16 O ANISOU 1687 O GLY A 205 1752 1408 1458 91 -70 95 O ATOM 1688 N ASP A 206 25.656 13.924 8.125 1.00 11.07 N ANISOU 1688 N ASP A 206 1638 1192 1375 139 -95 79 N ATOM 1689 CA ASP A 206 26.467 13.187 9.077 1.00 11.70 C ANISOU 1689 CA ASP A 206 1740 1266 1439 166 -103 126 C ATOM 1690 C ASP A 206 27.874 12.947 8.591 1.00 14.28 C ANISOU 1690 C ASP A 206 2060 1613 1755 222 -129 116 C ATOM 1691 O ASP A 206 28.588 12.099 9.151 1.00 14.14 O ANISOU 1691 O ASP A 206 2062 1579 1731 259 -142 150 O ATOM 1692 CB ASP A 206 25.778 11.889 9.511 1.00 13.36 C ANISOU 1692 CB ASP A 206 1988 1402 1687 155 -94 161 C ATOM 1693 CG ASP A 206 25.579 10.894 8.401 1.00 13.72 C ANISOU 1693 CG ASP A 206 2044 1379 1789 170 -105 129 C ATOM 1694 OD1 ASP A 206 25.817 11.260 7.218 1.00 14.74 O ANISOU 1694 OD1 ASP A 206 2149 1527 1923 187 -119 76 O ATOM 1695 OD2 ASP A 206 25.234 9.724 8.712 1.00 16.08 O1- ANISOU 1695 OD2 ASP A 206 2375 1606 2128 166 -99 157 O1- ATOM 1696 N SER A 207 28.275 13.663 7.546 1.00 12.02 N ANISOU 1696 N SER A 207 1744 1359 1463 233 -134 72 N ATOM 1697 CA SER A 207 29.619 13.683 6.982 1.00 12.34 C ANISOU 1697 CA SER A 207 1766 1433 1489 280 -153 54 C ATOM 1698 C SER A 207 29.659 14.873 6.072 1.00 13.25 C ANISOU 1698 C SER A 207 1849 1592 1593 267 -142 17 C ATOM 1699 O SER A 207 28.610 15.452 5.741 1.00 11.57 O ANISOU 1699 O SER A 207 1634 1371 1390 232 -126 4 O ATOM 1700 CB SER A 207 29.958 12.413 6.215 1.00 13.31 C ANISOU 1700 CB SER A 207 1905 1508 1646 324 -172 40 C ATOM 1701 OG SER A 207 29.167 12.368 5.037 1.00 14.85 O ANISOU 1701 OG SER A 207 2096 1678 1870 312 -168 -2 O ATOM 1702 N GLU A 208 30.836 15.297 5.647 1.00 12.88 N ANISOU 1702 N GLU A 208 1776 1593 1526 295 -148 0 N ATOM 1703 CA GLU A 208 30.883 16.457 4.772 1.00 12.49 C ANISOU 1703 CA GLU A 208 1698 1580 1467 281 -131 -27 C ATOM 1704 C GLU A 208 30.158 16.218 3.469 1.00 12.40 C ANISOU 1704 C GLU A 208 1693 1544 1476 287 -131 -53 C ATOM 1705 O GLU A 208 29.453 17.112 2.993 1.00 11.90 O ANISOU 1705 O GLU A 208 1621 1490 1409 262 -114 -62 O ATOM 1706 CB GLU A 208 32.314 16.936 4.521 1.00 14.65 C ANISOU 1706 CB GLU A 208 1938 1909 1717 306 -132 -40 C ATOM 1707 CG GLU A 208 32.960 17.490 5.792 1.00 16.35 C ANISOU 1707 CG GLU A 208 2137 2165 1910 293 -131 -25 C ATOM 1708 CD GLU A 208 34.248 18.251 5.548 1.00 19.95 C ANISOU 1708 CD GLU A 208 2550 2681 2349 302 -124 -47 C ATOM 1709 OE1 GLU A 208 34.304 19.030 4.577 1.00 21.97 O ANISOU 1709 OE1 GLU A 208 2789 2951 2609 289 -102 -64 O ATOM 1710 OE2 GLU A 208 35.152 18.164 6.407 1.00 32.64 O1- ANISOU 1710 OE2 GLU A 208 4138 4325 3937 317 -137 -46 O1- ATOM 1711 N ILE A 209 30.331 15.029 2.850 1.00 12.14 N ANISOU 1711 N ILE A 209 1671 1481 1461 323 -150 -70 N ATOM 1712 CA ILE A 209 29.650 14.803 1.581 1.00 11.31 C ANISOU 1712 CA ILE A 209 1565 1363 1371 332 -152 -106 C ATOM 1713 C ILE A 209 28.149 14.633 1.759 1.00 11.77 C ANISOU 1713 C ILE A 209 1640 1376 1455 295 -148 -108 C ATOM 1714 O ILE A 209 27.384 15.059 0.887 1.00 11.07 O ANISOU 1714 O ILE A 209 1542 1299 1367 288 -143 -134 O ATOM 1715 CB ILE A 209 30.303 13.635 0.812 1.00 13.30 C ANISOU 1715 CB ILE A 209 1817 1600 1637 383 -175 -137 C ATOM 1716 CG1 ILE A 209 29.976 13.739 -0.697 1.00 14.54 C ANISOU 1716 CG1 ILE A 209 1957 1779 1788 401 -175 -183 C ATOM 1717 CG2 ILE A 209 29.877 12.267 1.386 1.00 16.30 C ANISOU 1717 CG2 ILE A 209 2228 1905 2060 387 -190 -130 C ATOM 1718 CD1 ILE A 209 30.568 14.941 -1.383 1.00 17.47 C ANISOU 1718 CD1 ILE A 209 2301 2220 2116 407 -156 -182 C ATOM 1719 N ASP A 210 27.709 14.042 2.891 1.00 11.50 N ANISOU 1719 N ASP A 210 1630 1299 1442 272 -147 -79 N ATOM 1720 CA ASP A 210 26.280 13.926 3.118 1.00 10.98 C ANISOU 1720 CA ASP A 210 1575 1195 1402 231 -138 -82 C ATOM 1721 C ASP A 210 25.695 15.310 3.333 1.00 10.32 C ANISOU 1721 C ASP A 210 1476 1152 1295 197 -118 -76 C ATOM 1722 O ASP A 210 24.604 15.583 2.850 1.00 11.14 O ANISOU 1722 O ASP A 210 1573 1251 1410 177 -113 -99 O ATOM 1723 CB ASP A 210 26.005 13.027 4.324 1.00 12.06 C ANISOU 1723 CB ASP A 210 1740 1280 1561 213 -135 -44 C ATOM 1724 CG ASP A 210 24.554 12.747 4.557 1.00 12.68 C ANISOU 1724 CG ASP A 210 1827 1317 1673 167 -121 -49 C ATOM 1725 OD1 ASP A 210 23.949 12.023 3.724 1.00 17.35 O ANISOU 1725 OD1 ASP A 210 2418 1870 2304 168 -128 -89 O ATOM 1726 OD2 ASP A 210 24.030 13.186 5.573 1.00 12.64 O1- ANISOU 1726 OD2 ASP A 210 1827 1319 1657 130 -103 -17 O1- ATOM 1727 N GLN A 211 26.416 16.187 4.037 1.00 10.03 N ANISOU 1727 N GLN A 211 1430 1154 1227 191 -109 -50 N ATOM 1728 CA GLN A 211 25.950 17.546 4.228 1.00 10.30 C ANISOU 1728 CA GLN A 211 1448 1219 1244 162 -90 -49 C ATOM 1729 C GLN A 211 25.794 18.242 2.883 1.00 10.60 C ANISOU 1729 C GLN A 211 1471 1280 1277 177 -87 -76 C ATOM 1730 O GLN A 211 24.746 18.839 2.589 1.00 10.96 O ANISOU 1730 O GLN A 211 1511 1326 1327 160 -78 -87 O ATOM 1731 CB GLN A 211 26.960 18.289 5.108 1.00 11.00 C ANISOU 1731 CB GLN A 211 1526 1347 1307 158 -83 -28 C ATOM 1732 CG GLN A 211 26.446 19.673 5.533 1.00 10.77 C ANISOU 1732 CG GLN A 211 1483 1342 1269 123 -62 -28 C ATOM 1733 CD GLN A 211 25.236 19.573 6.411 1.00 9.84 C ANISOU 1733 CD GLN A 211 1374 1203 1160 88 -54 -20 C ATOM 1734 NE2 GLN A 211 24.287 20.513 6.264 1.00 10.75 N ANISOU 1734 NE2 GLN A 211 1480 1323 1281 65 -40 -35 N ATOM 1735 OE1 GLN A 211 25.127 18.679 7.259 1.00 10.97 O ANISOU 1735 OE1 GLN A 211 1535 1329 1304 82 -59 1 O ATOM 1736 N LEU A 212 26.839 18.171 2.038 1.00 10.45 N ANISOU 1736 N LEU A 212 1442 1285 1244 214 -93 -85 N ATOM 1737 CA ALEU A 212 26.790 18.788 0.703 0.60 10.73 C ANISOU 1737 CA ALEU A 212 1463 1349 1264 235 -87 -104 C ATOM 1738 CA BLEU A 212 26.793 18.826 0.747 0.40 10.04 C ANISOU 1738 CA BLEU A 212 1376 1262 1177 234 -87 -103 C ATOM 1739 C LEU A 212 25.678 18.255 -0.129 1.00 12.16 C ANISOU 1739 C LEU A 212 1648 1514 1458 244 -100 -135 C ATOM 1740 O LEU A 212 24.922 19.023 -0.759 1.00 11.70 O ANISOU 1740 O LEU A 212 1582 1473 1390 244 -92 -143 O ATOM 1741 CB ALEU A 212 28.088 18.539 -0.077 0.60 12.00 C ANISOU 1741 CB ALEU A 212 1611 1540 1406 275 -92 -112 C ATOM 1742 CB BLEU A 212 28.167 18.665 0.093 0.40 10.56 C ANISOU 1742 CB BLEU A 212 1429 1360 1224 271 -89 -107 C ATOM 1743 CG ALEU A 212 29.174 19.546 0.185 0.60 14.31 C ANISOU 1743 CG ALEU A 212 1887 1871 1680 269 -71 -92 C ATOM 1744 CG BLEU A 212 28.502 19.551 -1.069 0.40 11.29 C ANISOU 1744 CG BLEU A 212 1505 1495 1290 289 -72 -110 C ATOM 1745 CD1ALEU A 212 30.481 19.080 -0.416 0.60 15.54 C ANISOU 1745 CD1ALEU A 212 2027 2057 1821 307 -76 -103 C ATOM 1746 CD1BLEU A 212 28.610 21.016 -0.651 0.40 11.28 C ANISOU 1746 CD1BLEU A 212 1495 1509 1283 259 -43 -83 C ATOM 1747 CD2ALEU A 212 28.797 20.945 -0.376 0.60 16.36 C ANISOU 1747 CD2ALEU A 212 2137 2150 1928 255 -44 -81 C ATOM 1748 CD2BLEU A 212 29.817 19.079 -1.677 0.40 12.14 C ANISOU 1748 CD2BLEU A 212 1598 1634 1382 327 -77 -121 C ATOM 1749 N PHE A 213 25.539 16.943 -0.185 1.00 11.16 N ANISOU 1749 N PHE A 213 1531 1353 1356 255 -119 -156 N ATOM 1750 CA PHE A 213 24.518 16.382 -1.046 1.00 11.41 C ANISOU 1750 CA PHE A 213 1559 1372 1404 263 -133 -198 C ATOM 1751 C PHE A 213 23.111 16.644 -0.539 1.00 11.72 C ANISOU 1751 C PHE A 213 1598 1391 1463 222 -126 -201 C ATOM 1752 O PHE A 213 22.193 16.789 -1.344 1.00 12.19 O ANISOU 1752 O PHE A 213 1645 1465 1522 229 -133 -236 O ATOM 1753 CB PHE A 213 24.803 14.904 -1.321 1.00 13.40 C ANISOU 1753 CB PHE A 213 1819 1587 1686 285 -154 -228 C ATOM 1754 CG PHE A 213 26.005 14.604 -2.220 1.00 13.95 C ANISOU 1754 CG PHE A 213 1878 1688 1734 337 -165 -246 C ATOM 1755 CD1 PHE A 213 26.744 15.633 -2.804 1.00 13.79 C ANISOU 1755 CD1 PHE A 213 1842 1729 1668 357 -152 -233 C ATOM 1756 CD2 PHE A 213 26.346 13.292 -2.522 1.00 16.83 C ANISOU 1756 CD2 PHE A 213 2248 2019 2127 364 -186 -279 C ATOM 1757 CE1 PHE A 213 27.807 15.342 -3.681 1.00 16.94 C ANISOU 1757 CE1 PHE A 213 2228 2165 2045 403 -158 -252 C ATOM 1758 CE2 PHE A 213 27.406 13.005 -3.399 1.00 18.22 C ANISOU 1758 CE2 PHE A 213 2410 2230 2282 414 -196 -304 C ATOM 1759 CZ PHE A 213 28.132 14.025 -3.946 1.00 17.33 C ANISOU 1759 CZ PHE A 213 2279 2186 2119 432 -181 -290 C ATOM 1760 N ARG A 214 22.919 16.794 0.775 1.00 10.85 N ANISOU 1760 N ARG A 214 1500 1258 1364 183 -113 -168 N ATOM 1761 CA ARG A 214 21.600 17.190 1.290 1.00 10.82 C ANISOU 1761 CA ARG A 214 1492 1246 1374 144 -102 -171 C ATOM 1762 C ARG A 214 21.289 18.601 0.828 1.00 11.58 C ANISOU 1762 C ARG A 214 1572 1384 1442 150 -92 -171 C ATOM 1763 O ARG A 214 20.158 18.884 0.417 1.00 11.43 O ANISOU 1763 O ARG A 214 1540 1374 1429 146 -95 -198 O ATOM 1764 CB ARG A 214 21.559 17.114 2.815 1.00 11.02 C ANISOU 1764 CB ARG A 214 1531 1249 1408 104 -87 -133 C ATOM 1765 CG ARG A 214 21.397 15.681 3.285 1.00 11.25 C ANISOU 1765 CG ARG A 214 1579 1223 1472 92 -91 -130 C ATOM 1766 CD ARG A 214 21.506 15.622 4.803 1.00 11.99 C ANISOU 1766 CD ARG A 214 1689 1306 1562 61 -75 -82 C ATOM 1767 NE ARG A 214 21.224 14.286 5.320 1.00 13.44 N ANISOU 1767 NE ARG A 214 1895 1431 1782 45 -72 -68 N ATOM 1768 CZ ARG A 214 20.008 13.823 5.596 1.00 17.30 C ANISOU 1768 CZ ARG A 214 2383 1887 2305 4 -58 -78 C ATOM 1769 NH1 ARG A 214 18.929 14.561 5.331 1.00 17.70 N1+ ANISOU 1769 NH1 ARG A 214 2408 1962 2356 -20 -50 -110 N1+ ATOM 1770 NH2 ARG A 214 19.853 12.600 6.094 1.00 21.77 N ANISOU 1770 NH2 ARG A 214 2972 2391 2908 -12 -51 -57 N ATOM 1771 N ILE A 215 22.294 19.489 0.847 1.00 9.59 N ANISOU 1771 N ILE A 215 1320 1160 1163 163 -81 -143 N ATOM 1772 CA ILE A 215 22.084 20.855 0.361 1.00 9.55 C ANISOU 1772 CA ILE A 215 1304 1186 1138 172 -68 -137 C ATOM 1773 C ILE A 215 21.711 20.792 -1.119 1.00 11.08 C ANISOU 1773 C ILE A 215 1489 1405 1317 213 -81 -164 C ATOM 1774 O ILE A 215 20.743 21.438 -1.539 1.00 10.90 O ANISOU 1774 O ILE A 215 1457 1396 1288 219 -81 -175 O ATOM 1775 CB ILE A 215 23.312 21.731 0.610 1.00 9.79 C ANISOU 1775 CB ILE A 215 1334 1235 1151 174 -50 -105 C ATOM 1776 CG1 ILE A 215 23.560 21.908 2.129 1.00 10.69 C ANISOU 1776 CG1 ILE A 215 1451 1336 1274 135 -40 -86 C ATOM 1777 CG2 ILE A 215 23.140 23.098 -0.067 1.00 10.56 C ANISOU 1777 CG2 ILE A 215 1425 1354 1234 186 -32 -94 C ATOM 1778 CD1 ILE A 215 24.940 22.461 2.457 1.00 11.07 C ANISOU 1778 CD1 ILE A 215 1493 1404 1310 136 -27 -67 C ATOM 1779 N PHE A 216 22.446 20.019 -1.907 1.00 10.37 N ANISOU 1779 N PHE A 216 1399 1325 1217 245 -94 -179 N ATOM 1780 CA PHE A 216 22.204 19.945 -3.349 1.00 10.46 C ANISOU 1780 CA PHE A 216 1399 1372 1204 290 -107 -208 C ATOM 1781 C PHE A 216 20.846 19.370 -3.689 1.00 12.63 C ANISOU 1781 C PHE A 216 1661 1640 1495 289 -128 -257 C ATOM 1782 O PHE A 216 20.203 19.826 -4.639 1.00 12.43 O ANISOU 1782 O PHE A 216 1623 1654 1446 320 -136 -276 O ATOM 1783 CB PHE A 216 23.290 19.114 -4.005 1.00 11.57 C ANISOU 1783 CB PHE A 216 1538 1525 1332 323 -118 -222 C ATOM 1784 CG PHE A 216 24.725 19.594 -3.984 1.00 11.19 C ANISOU 1784 CG PHE A 216 1491 1498 1262 334 -99 -186 C ATOM 1785 CD1 PHE A 216 25.066 20.821 -3.417 1.00 12.73 C ANISOU 1785 CD1 PHE A 216 1689 1698 1451 311 -72 -143 C ATOM 1786 CD2 PHE A 216 25.730 18.819 -4.548 1.00 12.73 C ANISOU 1786 CD2 PHE A 216 1681 1709 1446 366 -109 -203 C ATOM 1787 CE1 PHE A 216 26.398 21.265 -3.449 1.00 14.12 C ANISOU 1787 CE1 PHE A 216 1859 1895 1610 316 -52 -117 C ATOM 1788 CE2 PHE A 216 27.053 19.243 -4.549 1.00 15.44 C ANISOU 1788 CE2 PHE A 216 2019 2079 1771 374 -90 -176 C ATOM 1789 CZ PHE A 216 27.378 20.468 -4.027 1.00 14.63 C ANISOU 1789 CZ PHE A 216 1915 1981 1661 348 -61 -134 C ATOM 1790 N ARG A 217 20.375 18.376 -2.917 1.00 12.27 N ANISOU 1790 N ARG A 217 1620 1550 1493 255 -136 -276 N ATOM 1791 CA ARG A 217 19.090 17.755 -3.221 1.00 12.57 C ANISOU 1791 CA ARG A 217 1641 1579 1556 246 -152 -330 C ATOM 1792 C ARG A 217 17.933 18.676 -2.964 1.00 15.21 C ANISOU 1792 C ARG A 217 1963 1929 1889 229 -145 -330 C ATOM 1793 O ARG A 217 16.861 18.504 -3.577 1.00 16.67 O ANISOU 1793 O ARG A 217 2124 2133 2078 239 -162 -380 O ATOM 1794 CB ARG A 217 18.929 16.464 -2.417 1.00 16.33 C ANISOU 1794 CB ARG A 217 2126 1993 2085 208 -155 -344 C ATOM 1795 CG ARG A 217 19.767 15.349 -2.993 1.00 20.23 C ANISOU 1795 CG ARG A 217 2625 2470 2590 236 -171 -369 C ATOM 1796 CD ARG A 217 19.382 13.991 -2.440 1.00 29.69 C ANISOU 1796 CD ARG A 217 3831 3599 3849 204 -175 -392 C ATOM 1797 NE ARG A 217 19.910 13.824 -1.086 1.00 36.68 N ANISOU 1797 NE ARG A 217 4745 4441 4750 172 -156 -332 N ATOM 1798 CZ ARG A 217 21.061 13.233 -0.791 1.00 49.29 C ANISOU 1798 CZ ARG A 217 6364 6013 6351 190 -159 -306 C ATOM 1799 NH1 ARG A 217 21.814 12.709 -1.753 1.00 37.35 N1+ ANISOU 1799 NH1 ARG A 217 4847 4512 4833 236 -178 -338 N1+ ATOM 1800 NH2 ARG A 217 21.465 13.149 0.468 1.00 40.30 N ANISOU 1800 NH2 ARG A 217 5249 4845 5218 165 -144 -250 N ATOM 1801 N THR A 218 18.102 19.680 -2.120 1.00 12.16 N ANISOU 1801 N THR A 218 1587 1539 1494 208 -123 -282 N ATOM 1802 CA THR A 218 17.039 20.645 -1.860 1.00 12.79 C ANISOU 1802 CA THR A 218 1654 1634 1573 197 -115 -283 C ATOM 1803 C THR A 218 17.202 21.867 -2.759 1.00 13.79 C ANISOU 1803 C THR A 218 1778 1802 1658 244 -113 -264 C ATOM 1804 O THR A 218 16.203 22.337 -3.355 1.00 14.38 O ANISOU 1804 O THR A 218 1836 1907 1722 269 -123 -287 O ATOM 1805 CB THR A 218 17.042 21.081 -0.387 1.00 14.40 C ANISOU 1805 CB THR A 218 1868 1810 1794 149 -92 -249 C ATOM 1806 CG2 THR A 218 16.000 22.154 -0.094 1.00 14.48 C ANISOU 1806 CG2 THR A 218 1863 1836 1804 141 -83 -253 C ATOM 1807 OG1 THR A 218 16.749 19.923 0.407 1.00 17.16 O ANISOU 1807 OG1 THR A 218 2221 2123 2179 107 -92 -261 O ATOM 1808 N LEU A 219 18.406 22.434 -2.863 1.00 11.21 N ANISOU 1808 N LEU A 219 1468 1480 1310 258 -97 -219 N ATOM 1809 CA LEU A 219 18.601 23.706 -3.558 1.00 11.85 C ANISOU 1809 CA LEU A 219 1552 1590 1359 295 -84 -187 C ATOM 1810 C LEU A 219 19.062 23.558 -4.993 1.00 13.24 C ANISOU 1810 C LEU A 219 1727 1811 1494 351 -93 -191 C ATOM 1811 O LEU A 219 19.188 24.571 -5.686 1.00 13.39 O ANISOU 1811 O LEU A 219 1750 1855 1482 386 -80 -158 O ATOM 1812 CB LEU A 219 19.570 24.573 -2.730 1.00 12.27 C ANISOU 1812 CB LEU A 219 1621 1621 1420 268 -53 -138 C ATOM 1813 CG LEU A 219 19.116 24.852 -1.286 1.00 14.21 C ANISOU 1813 CG LEU A 219 1866 1834 1698 217 -42 -137 C ATOM 1814 CD1 LEU A 219 20.167 25.640 -0.566 1.00 13.84 C ANISOU 1814 CD1 LEU A 219 1828 1773 1656 195 -16 -101 C ATOM 1815 CD2 LEU A 219 17.779 25.641 -1.240 1.00 17.45 C ANISOU 1815 CD2 LEU A 219 2265 2249 2115 221 -43 -151 C ATOM 1816 N GLY A 220 19.323 22.320 -5.401 1.00 11.85 N ANISOU 1816 N GLY A 220 1545 1641 1319 359 -114 -228 N ATOM 1817 CA GLY A 220 19.843 21.994 -6.710 1.00 13.22 C ANISOU 1817 CA GLY A 220 1711 1861 1450 412 -125 -242 C ATOM 1818 C GLY A 220 21.355 21.931 -6.662 1.00 13.35 C ANISOU 1818 C GLY A 220 1741 1875 1458 411 -106 -208 C ATOM 1819 O GLY A 220 21.972 22.685 -5.908 1.00 13.27 O ANISOU 1819 O GLY A 220 1743 1842 1458 383 -79 -162 O ATOM 1820 N THR A 221 21.981 21.076 -7.475 1.00 12.37 N ANISOU 1820 N THR A 221 1609 1778 1314 443 -120 -237 N ATOM 1821 CA THR A 221 23.438 21.070 -7.507 1.00 12.88 C ANISOU 1821 CA THR A 221 1678 1849 1365 447 -101 -208 C ATOM 1822 C THR A 221 23.883 22.396 -8.104 1.00 15.09 C ANISOU 1822 C THR A 221 1962 2166 1604 469 -69 -153 C ATOM 1823 O THR A 221 23.401 22.786 -9.164 1.00 15.17 O ANISOU 1823 O THR A 221 1968 2223 1572 513 -72 -153 O ATOM 1824 CB THR A 221 23.940 19.895 -8.332 1.00 15.15 C ANISOU 1824 CB THR A 221 1953 2163 1638 484 -123 -256 C ATOM 1825 CG2 THR A 221 25.494 19.819 -8.359 1.00 15.37 C ANISOU 1825 CG2 THR A 221 1981 2204 1653 491 -105 -233 C ATOM 1826 OG1 THR A 221 23.405 18.700 -7.748 1.00 15.14 O ANISOU 1826 OG1 THR A 221 1952 2115 1686 460 -150 -305 O ATOM 1827 N PRO A 222 24.798 23.129 -7.443 1.00 13.08 N ANISOU 1827 N PRO A 222 1717 1892 1362 439 -36 -106 N ATOM 1828 CA PRO A 222 25.188 24.436 -7.968 1.00 13.05 C ANISOU 1828 CA PRO A 222 1718 1911 1330 452 1 -51 C ATOM 1829 C PRO A 222 26.039 24.287 -9.211 1.00 14.47 C ANISOU 1829 C PRO A 222 1888 2151 1458 497 12 -45 C ATOM 1830 O PRO A 222 26.754 23.287 -9.392 1.00 16.09 O ANISOU 1830 O PRO A 222 2081 2374 1658 508 -2 -79 O ATOM 1831 CB PRO A 222 26.028 25.036 -6.829 1.00 14.04 C ANISOU 1831 CB PRO A 222 1847 1996 1492 400 30 -19 C ATOM 1832 CG PRO A 222 26.569 23.884 -6.114 1.00 16.14 C ANISOU 1832 CG PRO A 222 2106 2245 1780 381 8 -53 C ATOM 1833 CD PRO A 222 25.459 22.840 -6.160 1.00 13.77 C ANISOU 1833 CD PRO A 222 1807 1936 1490 392 -32 -101 C ATOM 1834 N ASP A 223 25.936 25.273 -10.069 1.00 14.06 N ANISOU 1834 N ASP A 223 1842 2131 1367 527 38 -1 N ATOM 1835 CA ASP A 223 26.679 25.337 -11.308 1.00 15.27 C ANISOU 1835 CA ASP A 223 1988 2351 1462 573 57 17 C ATOM 1836 C ASP A 223 27.152 26.749 -11.532 1.00 15.93 C ANISOU 1836 C ASP A 223 2084 2432 1535 566 112 95 C ATOM 1837 O ASP A 223 26.894 27.629 -10.719 1.00 14.05 O ANISOU 1837 O ASP A 223 1860 2137 1340 528 130 127 O ATOM 1838 CB ASP A 223 25.844 24.777 -12.470 1.00 18.21 C ANISOU 1838 CB ASP A 223 2353 2786 1781 636 23 -20 C ATOM 1839 CG ASP A 223 24.591 25.565 -12.832 1.00 24.74 C ANISOU 1839 CG ASP A 223 3191 3620 2589 665 17 2 C ATOM 1840 OD1 ASP A 223 24.414 26.678 -12.319 1.00 21.16 O ANISOU 1840 OD1 ASP A 223 2756 3123 2160 641 45 56 O ATOM 1841 OD2 ASP A 223 23.782 25.053 -13.628 1.00 31.59 O1- ANISOU 1841 OD2 ASP A 223 4047 4538 3417 714 -18 -42 O1- ATOM 1842 N GLU A 224 27.847 26.973 -12.637 1.00 15.57 N ANISOU 1842 N GLU A 224 2034 2447 1435 603 140 126 N ATOM 1843 CA GLU A 224 28.402 28.271 -12.963 1.00 15.72 C ANISOU 1843 CA GLU A 224 2065 2463 1445 596 200 206 C ATOM 1844 C GLU A 224 27.349 29.326 -13.197 1.00 18.73 C ANISOU 1844 C GLU A 224 2473 2823 1819 619 210 256 C ATOM 1845 O GLU A 224 27.630 30.508 -13.034 1.00 20.04 O ANISOU 1845 O GLU A 224 2655 2949 2009 595 258 321 O ATOM 1846 CB GLU A 224 29.315 28.158 -14.171 1.00 17.08 C ANISOU 1846 CB GLU A 224 2224 2714 1550 635 230 227 C ATOM 1847 CG GLU A 224 30.625 27.442 -13.853 1.00 18.73 C ANISOU 1847 CG GLU A 224 2405 2936 1775 606 237 192 C ATOM 1848 CD GLU A 224 31.581 28.206 -12.955 1.00 18.69 C ANISOU 1848 CD GLU A 224 2396 2879 1828 539 283 226 C ATOM 1849 OE1 GLU A 224 31.503 29.455 -12.951 1.00 17.98 O ANISOU 1849 OE1 GLU A 224 2323 2755 1753 520 329 291 O ATOM 1850 OE2 GLU A 224 32.360 27.576 -12.204 1.00 18.10 O1- ANISOU 1850 OE2 GLU A 224 2299 2792 1787 506 272 183 O1- ATOM 1851 N VAL A 225 26.114 28.928 -13.534 1.00 16.32 N ANISOU 1851 N VAL A 225 2171 2541 1490 662 163 222 N ATOM 1852 CA VAL A 225 25.054 29.911 -13.729 1.00 15.65 C ANISOU 1852 CA VAL A 225 2107 2439 1398 691 166 265 C ATOM 1853 C VAL A 225 24.658 30.555 -12.400 1.00 18.15 C ANISOU 1853 C VAL A 225 2436 2665 1796 633 172 270 C ATOM 1854 O VAL A 225 24.575 31.780 -12.305 1.00 18.46 O ANISOU 1854 O VAL A 225 2496 2662 1855 627 209 332 O ATOM 1855 CB VAL A 225 23.821 29.263 -14.410 1.00 18.88 C ANISOU 1855 CB VAL A 225 2507 2906 1760 754 110 215 C ATOM 1856 CG1 VAL A 225 22.616 30.231 -14.456 1.00 18.60 C ANISOU 1856 CG1 VAL A 225 2491 2852 1725 786 105 250 C ATOM 1857 CG2 VAL A 225 24.174 28.771 -15.808 1.00 20.59 C ANISOU 1857 CG2 VAL A 225 2712 3223 1889 820 107 211 C ATOM 1858 N VAL A 226 24.383 29.728 -11.385 1.00 16.14 N ANISOU 1858 N VAL A 226 2167 2380 1586 592 135 204 N ATOM 1859 CA VAL A 226 23.949 30.289 -10.116 1.00 16.01 C ANISOU 1859 CA VAL A 226 2158 2289 1637 540 138 202 C ATOM 1860 C VAL A 226 25.101 30.730 -9.230 1.00 15.89 C ANISOU 1860 C VAL A 226 2141 2225 1671 476 177 221 C ATOM 1861 O VAL A 226 24.908 31.598 -8.385 1.00 16.76 O ANISOU 1861 O VAL A 226 2259 2276 1831 439 196 237 O ATOM 1862 CB VAL A 226 22.945 29.381 -9.367 1.00 20.48 C ANISOU 1862 CB VAL A 226 2712 2842 2228 525 86 131 C ATOM 1863 CG1 VAL A 226 21.680 29.149 -10.191 1.00 21.85 C ANISOU 1863 CG1 VAL A 226 2880 3060 2361 585 49 107 C ATOM 1864 CG2 VAL A 226 23.587 28.065 -8.965 1.00 19.85 C ANISOU 1864 CG2 VAL A 226 2614 2770 2157 497 65 79 C ATOM 1865 N TRP A 227 26.290 30.161 -9.431 1.00 14.67 N ANISOU 1865 N TRP A 227 1972 2099 1502 465 189 215 N ATOM 1866 CA TRP A 227 27.431 30.451 -8.586 1.00 14.18 C ANISOU 1866 CA TRP A 227 1899 2003 1484 406 221 221 C ATOM 1867 C TRP A 227 28.710 30.484 -9.410 1.00 15.50 C ANISOU 1867 C TRP A 227 2055 2214 1620 414 259 249 C ATOM 1868 O TRP A 227 29.462 29.501 -9.489 1.00 14.30 O ANISOU 1868 O TRP A 227 1883 2100 1451 416 244 214 O ATOM 1869 CB TRP A 227 27.516 29.413 -7.474 1.00 13.23 C ANISOU 1869 CB TRP A 227 1763 1868 1394 371 183 160 C ATOM 1870 CG TRP A 227 28.536 29.701 -6.408 1.00 12.27 C ANISOU 1870 CG TRP A 227 1628 1717 1318 312 206 156 C ATOM 1871 CD1 TRP A 227 29.407 30.751 -6.329 1.00 14.44 C ANISOU 1871 CD1 TRP A 227 1897 1974 1617 281 257 192 C ATOM 1872 CD2 TRP A 227 28.751 28.907 -5.234 1.00 12.58 C ANISOU 1872 CD2 TRP A 227 1654 1742 1384 279 177 110 C ATOM 1873 CE2 TRP A 227 29.793 29.511 -4.500 1.00 13.80 C ANISOU 1873 CE2 TRP A 227 1791 1880 1572 233 208 116 C ATOM 1874 CE3 TRP A 227 28.163 27.737 -4.739 1.00 12.90 C ANISOU 1874 CE3 TRP A 227 1695 1781 1425 284 130 67 C ATOM 1875 NE1 TRP A 227 30.208 30.606 -5.201 1.00 14.30 N ANISOU 1875 NE1 TRP A 227 1856 1940 1636 232 257 162 N ATOM 1876 CZ2 TRP A 227 30.257 28.976 -3.277 1.00 14.26 C ANISOU 1876 CZ2 TRP A 227 1833 1931 1654 199 188 79 C ATOM 1877 CZ3 TRP A 227 28.612 27.214 -3.531 1.00 13.80 C ANISOU 1877 CZ3 TRP A 227 1798 1879 1565 248 115 40 C ATOM 1878 CH2 TRP A 227 29.650 27.834 -2.821 1.00 14.21 C ANISOU 1878 CH2 TRP A 227 1834 1925 1641 210 142 47 C ATOM 1879 N PRO A 228 28.979 31.614 -10.055 1.00 15.63 N ANISOU 1879 N PRO A 228 2085 2226 1629 422 311 316 N ATOM 1880 CA PRO A 228 30.202 31.727 -10.861 1.00 15.81 C ANISOU 1880 CA PRO A 228 2094 2293 1621 425 356 349 C ATOM 1881 C PRO A 228 31.437 31.426 -10.029 1.00 17.50 C ANISOU 1881 C PRO A 228 2277 2498 1874 368 369 315 C ATOM 1882 O PRO A 228 31.595 31.911 -8.901 1.00 18.24 O ANISOU 1882 O PRO A 228 2365 2535 2031 313 377 304 O ATOM 1883 CB PRO A 228 30.187 33.190 -11.306 1.00 18.51 C ANISOU 1883 CB PRO A 228 2459 2600 1973 424 417 431 C ATOM 1884 CG PRO A 228 28.721 33.542 -11.338 1.00 22.45 C ANISOU 1884 CG PRO A 228 2988 3073 2469 461 388 442 C ATOM 1885 CD PRO A 228 28.157 32.846 -10.132 1.00 17.71 C ANISOU 1885 CD PRO A 228 2376 2442 1910 431 334 368 C ATOM 1886 N GLY A 229 32.263 30.546 -10.574 1.00 17.07 N ANISOU 1886 N GLY A 229 2199 2507 1780 388 363 291 N ATOM 1887 CA GLY A 229 33.485 30.086 -9.942 1.00 18.12 C ANISOU 1887 CA GLY A 229 2296 2650 1937 349 368 254 C ATOM 1888 C GLY A 229 33.324 28.805 -9.145 1.00 17.83 C ANISOU 1888 C GLY A 229 2250 2613 1912 351 305 184 C ATOM 1889 O GLY A 229 34.342 28.263 -8.710 1.00 18.82 O ANISOU 1889 O GLY A 229 2346 2757 2048 333 302 151 O ATOM 1890 N VAL A 230 32.084 28.308 -8.898 1.00 14.04 N ANISOU 1890 N VAL A 230 1792 2111 1432 371 256 161 N ATOM 1891 CA VAL A 230 31.891 27.122 -8.053 1.00 12.88 C ANISOU 1891 CA VAL A 230 1640 1952 1304 367 203 102 C ATOM 1892 C VAL A 230 32.656 25.915 -8.571 1.00 15.01 C ANISOU 1892 C VAL A 230 1888 2274 1542 400 182 62 C ATOM 1893 O VAL A 230 33.179 25.153 -7.744 1.00 14.20 O ANISOU 1893 O VAL A 230 1771 2160 1463 385 158 26 O ATOM 1894 CB VAL A 230 30.387 26.769 -7.827 1.00 14.60 C ANISOU 1894 CB VAL A 230 1881 2140 1526 381 160 83 C ATOM 1895 CG1 VAL A 230 29.702 26.257 -9.109 1.00 15.34 C ANISOU 1895 CG1 VAL A 230 1981 2280 1566 442 140 73 C ATOM 1896 CG2 VAL A 230 30.216 25.757 -6.701 1.00 14.62 C ANISOU 1896 CG2 VAL A 230 1881 2113 1561 360 118 36 C ATOM 1897 N THR A 231 32.734 25.731 -9.892 1.00 16.01 N ANISOU 1897 N THR A 231 2011 2458 1613 449 190 69 N ATOM 1898 CA THR A 231 33.372 24.523 -10.398 1.00 17.20 C ANISOU 1898 CA THR A 231 2140 2659 1737 486 166 21 C ATOM 1899 C THR A 231 34.871 24.535 -10.252 1.00 19.84 C ANISOU 1899 C THR A 231 2442 3022 2075 469 194 18 C ATOM 1900 O THR A 231 35.497 23.505 -10.545 1.00 22.22 O ANISOU 1900 O THR A 231 2721 3361 2359 500 173 -26 O ATOM 1901 CB THR A 231 32.951 24.218 -11.835 1.00 21.18 C ANISOU 1901 CB THR A 231 2646 3226 2176 548 159 14 C ATOM 1902 CG2 THR A 231 31.456 24.070 -11.984 1.00 19.77 C ANISOU 1902 CG2 THR A 231 2491 3028 1993 569 123 2 C ATOM 1903 OG1 THR A 231 33.477 25.215 -12.709 1.00 20.29 O ANISOU 1903 OG1 THR A 231 2528 3157 2023 556 216 72 O ATOM 1904 N SER A 232 35.458 25.642 -9.814 1.00 19.97 N ANISOU 1904 N SER A 232 2864 2496 2227 290 586 -89 N ATOM 1905 CA ASER A 232 36.898 25.752 -9.630 0.50 21.31 C ANISOU 1905 CA ASER A 232 2991 2641 2464 259 655 -89 C ATOM 1906 CA BSER A 232 36.902 25.720 -9.635 0.50 21.25 C ANISOU 1906 CA BSER A 232 2983 2634 2456 260 654 -90 C ATOM 1907 C SER A 232 37.261 25.701 -8.150 1.00 24.82 C ANISOU 1907 C SER A 232 3368 3058 3005 192 618 -104 C ATOM 1908 O SER A 232 38.448 25.832 -7.797 1.00 26.39 O ANISOU 1908 O SER A 232 3521 3232 3275 161 664 -111 O ATOM 1909 CB ASER A 232 37.433 27.015 -10.303 0.50 25.31 C ANISOU 1909 CB ASER A 232 3529 3131 2958 273 766 -35 C ATOM 1910 CB BSER A 232 37.467 26.957 -10.329 0.50 25.13 C ANISOU 1910 CB BSER A 232 3506 3110 2935 274 766 -37 C ATOM 1911 OG ASER A 232 37.273 26.942 -11.710 0.50 28.00 O ANISOU 1911 OG ASER A 232 3934 3503 3203 343 807 -22 O ATOM 1912 OG BSER A 232 37.102 28.127 -9.620 0.50 27.83 O ANISOU 1912 OG BSER A 232 3844 3420 3308 240 777 -1 O ATOM 1913 N MET A 233 36.250 25.499 -7.265 1.00 18.31 N ANISOU 1913 N MET A 233 2536 2238 2184 173 535 -111 N ATOM 1914 CA AMET A 233 36.556 25.453 -5.856 0.50 14.72 C ANISOU 1914 CA AMET A 233 2025 1763 1807 118 500 -123 C ATOM 1915 CA BMET A 233 36.460 25.437 -5.811 0.50 18.33 C ANISOU 1915 CA BMET A 233 2483 2221 2262 118 494 -123 C ATOM 1916 C MET A 233 37.322 24.206 -5.439 1.00 18.70 C ANISOU 1916 C MET A 233 2481 2265 2360 104 462 -165 C ATOM 1917 O MET A 233 37.221 23.194 -6.098 1.00 17.19 O ANISOU 1917 O MET A 233 2301 2091 2139 133 437 -190 O ATOM 1918 CB AMET A 233 35.301 25.664 -5.060 0.50 14.13 C ANISOU 1918 CB AMET A 233 1956 1695 1717 105 436 -112 C ATOM 1919 CB BMET A 233 35.118 25.406 -5.042 0.50 20.44 C ANISOU 1919 CB BMET A 233 2756 2500 2511 108 418 -118 C ATOM 1920 CG AMET A 233 34.700 26.992 -5.382 0.50 12.89 C ANISOU 1920 CG AMET A 233 1840 1534 1525 118 475 -73 C ATOM 1921 CG BMET A 233 34.345 26.735 -5.073 0.50 24.25 C ANISOU 1921 CG BMET A 233 3272 2978 2962 113 443 -80 C ATOM 1922 SD AMET A 233 33.279 27.294 -4.364 0.50 13.17 S ANISOU 1922 SD AMET A 233 1875 1578 1550 101 404 -65 S ATOM 1923 SD BMET A 233 34.719 27.986 -3.797 0.50 28.50 S ANISOU 1923 SD BMET A 233 3773 3484 3570 64 464 -64 S ATOM 1924 CE AMET A 233 34.129 27.527 -2.865 0.50 11.04 C ANISOU 1924 CE AMET A 233 1542 1285 1368 46 399 -77 C ATOM 1925 CE BMET A 233 33.959 27.266 -2.415 0.50 25.28 C ANISOU 1925 CE BMET A 233 3333 3094 3179 37 371 -84 C ATOM 1926 N PRO A 234 38.144 24.285 -4.354 1.00 18.19 N ANISOU 1926 N PRO A 234 2361 2177 2372 63 457 -178 N ATOM 1927 CA PRO A 234 39.039 23.151 -4.037 1.00 17.96 C ANISOU 1927 CA PRO A 234 2288 2143 2392 55 429 -218 C ATOM 1928 C PRO A 234 38.448 21.758 -3.964 1.00 18.23 C ANISOU 1928 C PRO A 234 2324 2193 2409 68 350 -241 C ATOM 1929 O PRO A 234 39.055 20.809 -4.443 1.00 19.20 O ANISOU 1929 O PRO A 234 2434 2317 2545 84 344 -272 O ATOM 1930 CB PRO A 234 39.711 23.593 -2.731 1.00 19.07 C ANISOU 1930 CB PRO A 234 2376 2261 2608 13 419 -226 C ATOM 1931 CG PRO A 234 39.725 25.070 -2.812 1.00 24.29 C ANISOU 1931 CG PRO A 234 3048 2907 3275 3 482 -197 C ATOM 1932 CD PRO A 234 38.413 25.438 -3.461 1.00 20.23 C ANISOU 1932 CD PRO A 234 2595 2412 2679 28 480 -162 C ATOM 1933 N ASP A 235 37.263 21.618 -3.381 1.00 14.46 N ANISOU 1933 N ASP A 235 1861 1725 1910 60 290 -227 N ATOM 1934 CA ASP A 235 36.656 20.318 -3.165 1.00 14.00 C ANISOU 1934 CA ASP A 235 1797 1671 1852 66 216 -244 C ATOM 1935 C ASP A 235 35.504 20.057 -4.097 1.00 17.08 C ANISOU 1935 C ASP A 235 2228 2080 2181 99 195 -245 C ATOM 1936 O ASP A 235 34.807 19.048 -3.963 1.00 18.69 O ANISOU 1936 O ASP A 235 2427 2284 2391 103 132 -260 O ATOM 1937 CB ASP A 235 36.276 20.152 -1.688 1.00 16.44 C ANISOU 1937 CB ASP A 235 2079 1973 2195 32 162 -231 C ATOM 1938 CG ASP A 235 37.443 20.235 -0.751 1.00 23.92 C ANISOU 1938 CG ASP A 235 2983 2905 3201 8 167 -241 C ATOM 1939 OD1 ASP A 235 38.506 19.673 -1.076 1.00 24.97 O ANISOU 1939 OD1 ASP A 235 3093 3026 3368 15 179 -271 O ATOM 1940 OD2 ASP A 235 37.338 20.947 0.249 1.00 25.63 O1- ANISOU 1940 OD2 ASP A 235 3188 3120 3429 -13 162 -225 O1- ATOM 1941 N TYR A 236 35.318 20.926 -5.101 1.00 13.36 N ANISOU 1941 N TYR A 236 1799 1623 1655 128 247 -231 N ATOM 1942 CA TYR A 236 34.289 20.672 -6.091 1.00 13.17 C ANISOU 1942 CA TYR A 236 1816 1620 1567 171 223 -240 C ATOM 1943 C TYR A 236 34.745 19.504 -6.975 1.00 14.65 C ANISOU 1943 C TYR A 236 2003 1814 1751 206 208 -286 C ATOM 1944 O TYR A 236 35.903 19.483 -7.415 1.00 15.55 O ANISOU 1944 O TYR A 236 2109 1926 1874 215 260 -297 O ATOM 1945 CB TYR A 236 34.056 21.914 -6.957 1.00 14.51 C ANISOU 1945 CB TYR A 236 2037 1804 1673 202 285 -211 C ATOM 1946 CG TYR A 236 33.046 21.643 -8.043 1.00 16.60 C ANISOU 1946 CG TYR A 236 2347 2095 1866 257 255 -226 C ATOM 1947 CD1 TYR A 236 31.686 21.835 -7.819 1.00 17.72 C ANISOU 1947 CD1 TYR A 236 2503 2244 1986 260 203 -220 C ATOM 1948 CD2 TYR A 236 33.447 21.165 -9.288 1.00 17.55 C ANISOU 1948 CD2 TYR A 236 2495 2234 1941 310 274 -254 C ATOM 1949 CE1 TYR A 236 30.745 21.528 -8.803 1.00 17.44 C ANISOU 1949 CE1 TYR A 236 2503 2232 1891 315 165 -245 C ATOM 1950 CE2 TYR A 236 32.517 20.823 -10.261 1.00 18.02 C ANISOU 1950 CE2 TYR A 236 2593 2319 1934 368 234 -280 C ATOM 1951 CZ TYR A 236 31.170 21.011 -10.013 1.00 18.45 C ANISOU 1951 CZ TYR A 236 2658 2379 1974 370 177 -276 C ATOM 1952 OH TYR A 236 30.253 20.697 -10.983 1.00 22.02 O ANISOU 1952 OH TYR A 236 3145 2857 2365 431 131 -309 O ATOM 1953 N LYS A 237 33.824 18.596 -7.317 1.00 13.44 N ANISOU 1953 N LYS A 237 1855 1668 1583 229 141 -315 N ATOM 1954 CA LYS A 237 34.128 17.509 -8.233 1.00 13.82 C ANISOU 1954 CA LYS A 237 1905 1723 1624 270 119 -366 C ATOM 1955 C LYS A 237 33.092 17.528 -9.324 1.00 15.84 C ANISOU 1955 C LYS A 237 2206 2006 1808 326 94 -387 C ATOM 1956 O LYS A 237 31.892 17.488 -9.036 1.00 15.22 O ANISOU 1956 O LYS A 237 2128 1926 1729 321 40 -385 O ATOM 1957 CB LYS A 237 34.136 16.142 -7.511 1.00 16.64 C ANISOU 1957 CB LYS A 237 2214 2053 2056 244 48 -396 C ATOM 1958 CG LYS A 237 35.192 15.963 -6.364 1.00 19.07 C ANISOU 1958 CG LYS A 237 2476 2334 2435 196 59 -382 C ATOM 1959 CD LYS A 237 36.671 16.226 -6.761 1.00 20.47 C ANISOU 1959 CD LYS A 237 2645 2513 2619 204 126 -392 C ATOM 1960 CE LYS A 237 37.650 15.994 -5.603 1.00 24.54 C ANISOU 1960 CE LYS A 237 3111 3003 3211 162 123 -388 C ATOM 1961 NZ LYS A 237 39.053 16.403 -5.948 1.00 25.53 N1+ ANISOU 1961 NZ LYS A 237 3221 3128 3352 166 193 -399 N1+ ATOM 1962 N PRO A 238 33.529 17.504 -10.594 1.00 15.56 N ANISOU 1962 N PRO A 238 2204 1995 1711 385 128 -411 N ATOM 1963 CA PRO A 238 32.572 17.417 -11.715 1.00 15.30 C ANISOU 1963 CA PRO A 238 2218 1993 1602 453 94 -442 C ATOM 1964 C PRO A 238 31.648 16.190 -11.666 1.00 17.14 C ANISOU 1964 C PRO A 238 2423 2215 1872 461 -9 -498 C ATOM 1965 O PRO A 238 30.573 16.177 -12.301 1.00 18.29 O ANISOU 1965 O PRO A 238 2596 2380 1974 505 -56 -525 O ATOM 1966 CB PRO A 238 33.487 17.337 -12.953 1.00 18.02 C ANISOU 1966 CB PRO A 238 2595 2367 1886 514 150 -465 C ATOM 1967 CG PRO A 238 34.723 18.005 -12.538 1.00 20.52 C ANISOU 1967 CG PRO A 238 2896 2670 2231 476 240 -421 C ATOM 1968 CD PRO A 238 34.909 17.672 -11.085 1.00 16.95 C ANISOU 1968 CD PRO A 238 2383 2178 1880 398 206 -411 C ATOM 1969 N SER A 239 32.054 15.148 -10.895 1.00 14.74 N ANISOU 1969 N SER A 239 2064 1878 1658 418 -46 -518 N ATOM 1970 CA SER A 239 31.267 13.913 -10.759 1.00 13.81 C ANISOU 1970 CA SER A 239 1913 1738 1597 417 -139 -568 C ATOM 1971 C SER A 239 30.140 14.066 -9.708 1.00 15.19 C ANISOU 1971 C SER A 239 2063 1889 1818 367 -179 -535 C ATOM 1972 O SER A 239 29.403 13.101 -9.491 1.00 15.82 O ANISOU 1972 O SER A 239 2110 1944 1958 359 -251 -568 O ATOM 1973 CB SER A 239 32.175 12.741 -10.394 1.00 13.18 C ANISOU 1973 CB SER A 239 1788 1626 1595 397 -159 -598 C ATOM 1974 OG SER A 239 32.925 13.105 -9.247 1.00 14.02 O ANISOU 1974 OG SER A 239 1869 1712 1746 336 -118 -544 O ATOM 1975 N PHE A 240 29.980 15.246 -9.061 1.00 14.35 N ANISOU 1975 N PHE A 240 1971 1791 1690 335 -134 -473 N ATOM 1976 CA PHE A 240 28.839 15.400 -8.165 1.00 13.67 C ANISOU 1976 CA PHE A 240 1864 1691 1640 297 -171 -447 C ATOM 1977 C PHE A 240 27.574 15.129 -8.980 1.00 16.55 C ANISOU 1977 C PHE A 240 2239 2066 1981 342 -232 -493 C ATOM 1978 O PHE A 240 27.401 15.684 -10.075 1.00 17.87 O ANISOU 1978 O PHE A 240 2455 2268 2068 402 -220 -511 O ATOM 1979 CB PHE A 240 28.721 16.833 -7.647 1.00 14.98 C ANISOU 1979 CB PHE A 240 2052 1871 1767 275 -117 -387 C ATOM 1980 CG PHE A 240 29.749 17.281 -6.651 1.00 14.70 C ANISOU 1980 CG PHE A 240 2001 1824 1762 226 -65 -342 C ATOM 1981 CD1 PHE A 240 30.468 16.360 -5.892 1.00 16.94 C ANISOU 1981 CD1 PHE A 240 2242 2079 2114 192 -81 -346 C ATOM 1982 CD2 PHE A 240 29.957 18.633 -6.414 1.00 15.71 C ANISOU 1982 CD2 PHE A 240 2152 1963 1855 216 -6 -298 C ATOM 1983 CE1 PHE A 240 31.379 16.804 -4.907 1.00 17.26 C ANISOU 1983 CE1 PHE A 240 2265 2111 2183 152 -42 -311 C ATOM 1984 CE2 PHE A 240 30.874 19.068 -5.466 1.00 16.68 C ANISOU 1984 CE2 PHE A 240 2253 2072 2011 173 34 -266 C ATOM 1985 CZ PHE A 240 31.552 18.159 -4.704 1.00 14.44 C ANISOU 1985 CZ PHE A 240 1929 1768 1792 143 13 -274 C ATOM 1986 N PRO A 241 26.612 14.401 -8.412 1.00 15.32 N ANISOU 1986 N PRO A 241 2042 1884 1897 315 -294 -507 N ATOM 1987 CA PRO A 241 25.334 14.227 -9.113 1.00 16.30 C ANISOU 1987 CA PRO A 241 2168 2016 2010 355 -355 -555 C ATOM 1988 C PRO A 241 24.618 15.572 -9.297 1.00 19.09 C ANISOU 1988 C PRO A 241 2561 2402 2290 375 -332 -525 C ATOM 1989 O PRO A 241 24.782 16.490 -8.476 1.00 16.35 O ANISOU 1989 O PRO A 241 2220 2058 1934 335 -281 -462 O ATOM 1990 CB PRO A 241 24.558 13.302 -8.178 1.00 18.49 C ANISOU 1990 CB PRO A 241 2382 2248 2396 304 -407 -557 C ATOM 1991 CG PRO A 241 25.640 12.569 -7.368 1.00 21.16 C ANISOU 1991 CG PRO A 241 2691 2554 2795 259 -388 -532 C ATOM 1992 CD PRO A 241 26.656 13.638 -7.147 1.00 17.54 C ANISOU 1992 CD PRO A 241 2269 2123 2273 251 -311 -481 C ATOM 1993 N LYS A 242 23.825 15.688 -10.370 1.00 17.92 N ANISOU 1993 N LYS A 242 2440 2279 2091 440 -373 -574 N ATOM 1994 CA LYS A 242 23.073 16.884 -10.701 1.00 19.34 C ANISOU 1994 CA LYS A 242 2661 2489 2199 472 -362 -554 C ATOM 1995 C LYS A 242 21.617 16.712 -10.294 1.00 22.04 C ANISOU 1995 C LYS A 242 2961 2817 2596 457 -426 -575 C ATOM 1996 O LYS A 242 20.861 16.007 -10.964 1.00 23.44 O ANISOU 1996 O LYS A 242 3121 2992 2792 497 -498 -645 O ATOM 1997 CB LYS A 242 23.217 17.210 -12.199 1.00 23.21 C ANISOU 1997 CB LYS A 242 3216 3021 2584 565 -361 -591 C ATOM 1998 CG LYS A 242 24.643 17.628 -12.574 1.00 33.34 C ANISOU 1998 CG LYS A 242 4542 4320 3807 577 -278 -556 C ATOM 1999 CD LYS A 242 24.745 18.050 -14.037 1.00 45.08 C ANISOU 1999 CD LYS A 242 6099 5851 5177 674 -266 -580 C ATOM 2000 CE LYS A 242 26.163 18.371 -14.444 1.00 55.32 C ANISOU 2000 CE LYS A 242 7434 7163 6425 686 -176 -547 C ATOM 2001 NZ LYS A 242 26.920 17.149 -14.817 1.00 62.93 N1+ ANISOU 2001 NZ LYS A 242 8372 8122 7415 700 -195 -603 N1+ ATOM 2002 N TRP A 243 21.234 17.328 -9.178 1.00 17.95 N ANISOU 2002 N TRP A 243 2422 2288 2108 400 -399 -518 N ATOM 2003 CA TRP A 243 19.880 17.325 -8.651 1.00 18.66 C ANISOU 2003 CA TRP A 243 2471 2368 2252 379 -443 -526 C ATOM 2004 C TRP A 243 19.216 18.628 -8.953 1.00 19.78 C ANISOU 2004 C TRP A 243 2654 2542 2321 414 -431 -509 C ATOM 2005 O TRP A 243 19.860 19.681 -8.989 1.00 17.16 O ANISOU 2005 O TRP A 243 2372 2229 1920 421 -369 -460 O ATOM 2006 CB TRP A 243 19.892 17.126 -7.138 1.00 19.08 C ANISOU 2006 CB TRP A 243 2474 2392 2385 296 -417 -472 C ATOM 2007 CG TRP A 243 20.248 15.729 -6.734 1.00 20.27 C ANISOU 2007 CG TRP A 243 2575 2503 2626 260 -441 -488 C ATOM 2008 CD1 TRP A 243 19.442 14.630 -6.790 1.00 23.90 C ANISOU 2008 CD1 TRP A 243 2979 2929 3172 255 -504 -536 C ATOM 2009 CD2 TRP A 243 21.458 15.306 -6.101 1.00 18.83 C ANISOU 2009 CD2 TRP A 243 2387 2303 2466 222 -402 -453 C ATOM 2010 CE2 TRP A 243 21.342 13.919 -5.853 1.00 23.45 C ANISOU 2010 CE2 TRP A 243 2920 2844 3147 199 -445 -479 C ATOM 2011 CE3 TRP A 243 22.638 15.964 -5.729 1.00 17.15 C ANISOU 2011 CE3 TRP A 243 2206 2103 2208 207 -338 -404 C ATOM 2012 NE1 TRP A 243 20.088 13.541 -6.256 1.00 23.84 N ANISOU 2012 NE1 TRP A 243 2937 2882 3238 216 -505 -528 N ATOM 2013 CZ2 TRP A 243 22.347 13.188 -5.202 1.00 22.63 C ANISOU 2013 CZ2 TRP A 243 2799 2712 3088 163 -427 -453 C ATOM 2014 CZ3 TRP A 243 23.637 15.232 -5.107 1.00 18.33 C ANISOU 2014 CZ3 TRP A 243 2334 2228 2403 172 -322 -386 C ATOM 2015 CH2 TRP A 243 23.474 13.870 -4.823 1.00 19.39 C ANISOU 2015 CH2 TRP A 243 2421 2321 2626 151 -367 -408 C ATOM 2016 N ALA A 244 17.884 18.556 -9.195 1.00 21.02 N ANISOU 2016 N ALA A 244 2787 2700 2501 437 -494 -553 N ATOM 2017 CA ALA A 244 17.070 19.733 -9.457 1.00 20.99 C ANISOU 2017 CA ALA A 244 2814 2723 2437 474 -496 -544 C ATOM 2018 C ALA A 244 16.696 20.434 -8.168 1.00 22.92 C ANISOU 2018 C ALA A 244 3032 2959 2717 410 -458 -485 C ATOM 2019 O ALA A 244 16.608 19.813 -7.118 1.00 23.94 O ANISOU 2019 O ALA A 244 3104 3063 2931 345 -453 -467 O ATOM 2020 CB ALA A 244 15.797 19.336 -10.195 1.00 22.35 C ANISOU 2020 CB ALA A 244 2965 2900 2628 526 -585 -624 C ATOM 2021 N ARG A 245 16.491 21.737 -8.242 1.00 19.60 N ANISOU 2021 N ARG A 245 2655 2561 2230 433 -428 -452 N ATOM 2022 CA ARG A 245 16.107 22.562 -7.119 1.00 19.05 C ANISOU 2022 CA ARG A 245 2567 2491 2183 385 -394 -402 C ATOM 2023 C ARG A 245 14.621 22.381 -6.738 1.00 21.42 C ANISOU 2023 C ARG A 245 2808 2785 2544 377 -447 -434 C ATOM 2024 O ARG A 245 13.757 22.337 -7.632 1.00 21.69 O ANISOU 2024 O ARG A 245 2846 2830 2564 434 -508 -491 O ATOM 2025 CB ARG A 245 16.363 24.024 -7.469 1.00 17.61 C ANISOU 2025 CB ARG A 245 2451 2329 1912 420 -350 -363 C ATOM 2026 CG ARG A 245 15.940 24.991 -6.398 1.00 18.64 C ANISOU 2026 CG ARG A 245 2565 2458 2058 381 -319 -319 C ATOM 2027 CD ARG A 245 16.354 26.390 -6.768 1.00 19.32 C ANISOU 2027 CD ARG A 245 2717 2555 2067 414 -272 -280 C ATOM 2028 NE ARG A 245 16.053 27.369 -5.738 1.00 20.37 N ANISOU 2028 NE ARG A 245 2837 2686 2217 378 -241 -242 N ATOM 2029 CZ ARG A 245 16.921 27.759 -4.807 1.00 18.57 C ANISOU 2029 CZ ARG A 245 2603 2448 2006 327 -184 -197 C ATOM 2030 NH1 ARG A 245 18.129 27.200 -4.733 1.00 18.79 N1+ ANISOU 2030 NH1 ARG A 245 2632 2464 2042 302 -152 -183 N1+ ATOM 2031 NH2 ARG A 245 16.604 28.733 -3.963 1.00 21.80 N ANISOU 2031 NH2 ARG A 245 3002 2857 2422 306 -162 -171 N ATOM 2032 N GLN A 246 14.323 22.324 -5.436 1.00 18.72 N ANISOU 2032 N GLN A 246 2414 2431 2267 310 -423 -400 N ATOM 2033 CA AGLN A 246 12.942 22.196 -4.950 0.70 19.12 C ANISOU 2033 CA AGLN A 246 2404 2478 2384 295 -459 -423 C ATOM 2034 CA BGLN A 246 12.954 22.192 -4.920 0.30 18.91 C ANISOU 2034 CA BGLN A 246 2377 2451 2358 293 -458 -421 C ATOM 2035 C GLN A 246 12.356 23.569 -4.621 1.00 22.14 C ANISOU 2035 C GLN A 246 2805 2883 2725 307 -439 -398 C ATOM 2036 O GLN A 246 13.084 24.502 -4.271 1.00 21.86 O ANISOU 2036 O GLN A 246 2812 2858 2636 298 -384 -347 O ATOM 2037 CB AGLN A 246 12.898 21.309 -3.687 0.70 19.79 C ANISOU 2037 CB AGLN A 246 2421 2537 2563 220 -439 -395 C ATOM 2038 CB BGLN A 246 12.948 21.366 -3.621 0.30 19.91 C ANISOU 2038 CB BGLN A 246 2437 2552 2575 217 -434 -390 C ATOM 2039 CG AGLN A 246 13.525 19.927 -3.838 0.70 21.63 C ANISOU 2039 CG AGLN A 246 2630 2738 2849 201 -455 -411 C ATOM 2040 CG BGLN A 246 13.194 19.873 -3.800 0.30 29.53 C ANISOU 2040 CG BGLN A 246 3618 3737 3865 200 -464 -419 C ATOM 2041 CD AGLN A 246 12.834 19.069 -4.873 0.70 41.64 C ANISOU 2041 CD AGLN A 246 5138 5257 5425 240 -531 -492 C ATOM 2042 CD BGLN A 246 13.231 19.123 -2.485 0.30 41.84 C ANISOU 2042 CD BGLN A 246 5120 5270 5507 128 -433 -374 C ATOM 2043 NE2AGLN A 246 13.583 18.621 -5.877 0.70 34.17 N ANISOU 2043 NE2AGLN A 246 4229 4311 4442 281 -554 -527 N ATOM 2044 NE2BGLN A 246 14.027 18.067 -2.440 0.30 33.21 N ANISOU 2044 NE2BGLN A 246 4018 4148 4451 107 -433 -371 N ATOM 2045 OE1AGLN A 246 11.627 18.808 -4.795 0.70 40.90 O ANISOU 2045 OE1AGLN A 246 4989 5153 5399 238 -571 -528 O ATOM 2046 OE1BGLN A 246 12.540 19.456 -1.510 0.30 33.85 O ANISOU 2046 OE1BGLN A 246 4073 4263 4525 94 -408 -342 O ATOM 2047 N ASP A 247 11.021 23.682 -4.663 1.00 21.39 N ANISOU 2047 N ASP A 247 2670 2792 2665 323 -483 -436 N ATOM 2048 CA AASP A 247 10.323 24.918 -4.319 0.50 20.27 C ANISOU 2048 CA AASP A 247 2537 2670 2496 335 -471 -421 C ATOM 2049 CA BASP A 247 10.337 24.919 -4.328 0.50 20.03 C ANISOU 2049 CA BASP A 247 2507 2640 2465 335 -471 -420 C ATOM 2050 C ASP A 247 10.324 25.098 -2.816 1.00 22.58 C ANISOU 2050 C ASP A 247 2788 2961 2830 266 -416 -368 C ATOM 2051 O ASP A 247 10.055 24.142 -2.092 1.00 20.27 O ANISOU 2051 O ASP A 247 2433 2653 2617 218 -414 -366 O ATOM 2052 CB AASP A 247 8.852 24.876 -4.788 0.50 23.42 C ANISOU 2052 CB AASP A 247 2894 3073 2932 373 -540 -486 C ATOM 2053 CB BASP A 247 8.895 24.869 -4.862 0.50 22.92 C ANISOU 2053 CB BASP A 247 2835 3010 2865 377 -542 -487 C ATOM 2054 CG AASP A 247 8.581 24.628 -6.260 0.50 34.61 C ANISOU 2054 CG AASP A 247 4342 4496 4314 452 -612 -553 C ATOM 2055 CG BASP A 247 8.250 26.223 -5.070 0.50 30.47 C ANISOU 2055 CG BASP A 247 3822 3988 3765 423 -548 -487 C ATOM 2056 OD1AASP A 247 9.527 24.729 -7.066 0.50 37.10 O ANISOU 2056 OD1AASP A 247 4726 4818 4552 490 -603 -545 O ATOM 2057 OD1BASP A 247 8.070 26.959 -4.071 0.50 28.34 O ANISOU 2057 OD1BASP A 247 3539 3726 3504 388 -504 -447 O ATOM 2058 OD2AASP A 247 7.406 24.379 -6.611 0.50 42.95 O1- ANISOU 2058 OD2AASP A 247 5351 5551 5417 481 -678 -618 O1- ATOM 2059 OD2BASP A 247 7.912 26.543 -6.225 0.50 40.45 O1- ANISOU 2059 OD2BASP A 247 5127 5263 4977 498 -599 -529 O1- ATOM 2060 N PHE A 248 10.555 26.321 -2.332 1.00 17.69 N ANISOU 2060 N PHE A 248 2202 2358 2160 266 -373 -328 N ATOM 2061 CA PHE A 248 10.508 26.540 -0.877 1.00 18.37 C ANISOU 2061 CA PHE A 248 2251 2449 2278 209 -325 -285 C ATOM 2062 C PHE A 248 9.136 26.298 -0.281 1.00 18.45 C ANISOU 2062 C PHE A 248 2188 2464 2358 192 -343 -306 C ATOM 2063 O PHE A 248 9.037 26.035 0.935 1.00 19.20 O ANISOU 2063 O PHE A 248 2240 2562 2494 142 -305 -273 O ATOM 2064 CB PHE A 248 10.998 27.955 -0.529 1.00 21.27 C ANISOU 2064 CB PHE A 248 2667 2832 2584 218 -282 -248 C ATOM 2065 CG PHE A 248 12.490 28.007 -0.365 1.00 23.93 C ANISOU 2065 CG PHE A 248 3044 3160 2887 198 -237 -208 C ATOM 2066 CD1 PHE A 248 13.306 28.381 -1.420 1.00 27.41 C ANISOU 2066 CD1 PHE A 248 3548 3593 3271 236 -233 -207 C ATOM 2067 CD2 PHE A 248 13.095 27.561 0.810 1.00 26.30 C ANISOU 2067 CD2 PHE A 248 3316 3459 3217 144 -200 -174 C ATOM 2068 CE1 PHE A 248 14.703 28.395 -1.277 1.00 27.89 C ANISOU 2068 CE1 PHE A 248 3639 3644 3313 215 -189 -174 C ATOM 2069 CE2 PHE A 248 14.492 27.540 0.934 1.00 28.34 C ANISOU 2069 CE2 PHE A 248 3607 3709 3453 128 -165 -145 C ATOM 2070 CZ PHE A 248 15.282 27.962 -0.116 1.00 24.68 C ANISOU 2070 CZ PHE A 248 3200 3236 2942 161 -159 -148 C ATOM 2071 N SER A 249 8.064 26.318 -1.110 1.00 18.20 N ANISOU 2071 N SER A 249 2139 2434 2343 236 -402 -363 N ATOM 2072 CA SER A 249 6.731 26.037 -0.614 1.00 17.36 C ANISOU 2072 CA SER A 249 1954 2328 2315 220 -420 -391 C ATOM 2073 C SER A 249 6.715 24.596 -0.089 1.00 16.10 C ANISOU 2073 C SER A 249 1730 2141 2245 165 -413 -385 C ATOM 2074 O SER A 249 5.962 24.344 0.826 1.00 17.48 O ANISOU 2074 O SER A 249 1840 2316 2486 127 -390 -374 O ATOM 2075 CB SER A 249 5.692 26.227 -1.716 1.00 19.18 C ANISOU 2075 CB SER A 249 2177 2561 2551 282 -494 -463 C ATOM 2076 OG SER A 249 5.961 25.382 -2.822 1.00 19.23 O ANISOU 2076 OG SER A 249 2198 2550 2560 312 -546 -506 O ATOM 2077 N LYS A 250 7.556 23.686 -0.634 1.00 14.75 N ANISOU 2077 N LYS A 250 1579 1948 2078 162 -427 -390 N ATOM 2078 CA LYS A 250 7.612 22.299 -0.162 1.00 16.23 C ANISOU 2078 CA LYS A 250 1710 2103 2356 112 -421 -381 C ATOM 2079 C LYS A 250 8.542 22.153 1.050 1.00 21.77 C ANISOU 2079 C LYS A 250 2420 2806 3046 59 -350 -304 C ATOM 2080 O LYS A 250 8.276 21.311 1.932 1.00 23.19 O ANISOU 2080 O LYS A 250 2543 2966 3301 10 -324 -276 O ATOM 2081 CB LYS A 250 8.066 21.420 -1.342 1.00 18.70 C ANISOU 2081 CB LYS A 250 2038 2391 2676 141 -475 -430 C ATOM 2082 CG LYS A 250 8.238 19.915 -1.073 1.00 29.08 C ANISOU 2082 CG LYS A 250 3301 3662 4088 96 -479 -429 C ATOM 2083 CD LYS A 250 8.938 19.247 -2.267 1.00 30.91 C ANISOU 2083 CD LYS A 250 3565 3877 4302 134 -528 -476 C ATOM 2084 CE LYS A 250 9.533 17.882 -1.989 1.00 29.59 C ANISOU 2084 CE LYS A 250 3368 3667 4209 92 -523 -464 C ATOM 2085 NZ LYS A 250 8.496 16.800 -2.043 1.00 27.95 N1+ ANISOU 2085 NZ LYS A 250 3073 3415 4134 73 -567 -513 N1+ ATOM 2086 N VAL A 251 9.591 22.982 1.101 1.00 17.57 N ANISOU 2086 N VAL A 251 1957 2295 2425 70 -320 -271 N ATOM 2087 CA VAL A 251 10.649 22.907 2.109 1.00 17.42 C ANISOU 2087 CA VAL A 251 1955 2278 2385 31 -263 -208 C ATOM 2088 C VAL A 251 10.260 23.458 3.467 1.00 20.91 C ANISOU 2088 C VAL A 251 2373 2745 2827 3 -214 -165 C ATOM 2089 O VAL A 251 10.597 22.832 4.480 1.00 21.49 O ANISOU 2089 O VAL A 251 2424 2813 2927 -37 -178 -119 O ATOM 2090 CB VAL A 251 11.922 23.578 1.576 1.00 19.93 C ANISOU 2090 CB VAL A 251 2349 2605 2620 56 -252 -199 C ATOM 2091 CG1 VAL A 251 13.079 23.452 2.577 1.00 20.41 C ANISOU 2091 CG1 VAL A 251 2424 2667 2665 20 -203 -144 C ATOM 2092 CG2 VAL A 251 12.345 22.993 0.219 1.00 20.98 C ANISOU 2092 CG2 VAL A 251 2509 2719 2744 90 -296 -241 C ATOM 2093 N VAL A 252 9.552 24.613 3.517 1.00 16.25 N ANISOU 2093 N VAL A 252 1787 2182 2205 27 -213 -179 N ATOM 2094 CA VAL A 252 9.199 25.223 4.818 1.00 14.64 C ANISOU 2094 CA VAL A 252 1562 2007 1993 6 -166 -143 C ATOM 2095 C VAL A 252 7.731 25.591 4.996 1.00 17.65 C ANISOU 2095 C VAL A 252 1890 2403 2411 14 -174 -169 C ATOM 2096 O VAL A 252 7.437 26.645 5.546 1.00 16.72 O ANISOU 2096 O VAL A 252 1780 2316 2258 26 -153 -163 O ATOM 2097 CB VAL A 252 10.136 26.421 5.110 1.00 15.91 C ANISOU 2097 CB VAL A 252 1783 2190 2071 21 -140 -122 C ATOM 2098 CG1 VAL A 252 11.574 25.948 5.368 1.00 16.07 C ANISOU 2098 CG1 VAL A 252 1836 2199 2071 1 -118 -87 C ATOM 2099 CG2 VAL A 252 10.090 27.449 3.969 1.00 16.28 C ANISOU 2099 CG2 VAL A 252 1877 2238 2071 70 -171 -158 C ATOM 2100 N PRO A 253 6.746 24.733 4.620 1.00 16.77 N ANISOU 2100 N PRO A 253 1719 2270 2382 8 -204 -202 N ATOM 2101 CA PRO A 253 5.359 25.085 4.937 1.00 19.00 C ANISOU 2101 CA PRO A 253 1943 2568 2710 11 -204 -226 C ATOM 2102 C PRO A 253 5.174 25.082 6.461 1.00 23.33 C ANISOU 2102 C PRO A 253 2456 3139 3268 -27 -134 -170 C ATOM 2103 O PRO A 253 5.873 24.311 7.139 1.00 21.53 O ANISOU 2103 O PRO A 253 2230 2902 3048 -62 -97 -119 O ATOM 2104 CB PRO A 253 4.544 23.974 4.269 1.00 19.72 C ANISOU 2104 CB PRO A 253 1971 2622 2901 5 -248 -271 C ATOM 2105 CG PRO A 253 5.461 22.822 4.229 1.00 22.82 C ANISOU 2105 CG PRO A 253 2373 2981 3316 -24 -243 -244 C ATOM 2106 CD PRO A 253 6.868 23.355 4.126 1.00 18.98 C ANISOU 2106 CD PRO A 253 1972 2509 2731 -11 -230 -214 C ATOM 2107 N PRO A 254 4.356 25.972 7.051 1.00 22.31 N ANISOU 2107 N PRO A 254 2303 3045 3128 -16 -112 -175 N ATOM 2108 CA PRO A 254 3.426 26.939 6.453 1.00 22.75 C ANISOU 2108 CA PRO A 254 2350 3114 3178 25 -151 -232 C ATOM 2109 C PRO A 254 3.949 28.375 6.396 1.00 25.42 C ANISOU 2109 C PRO A 254 2757 3480 3422 63 -152 -233 C ATOM 2110 O PRO A 254 3.162 29.318 6.484 1.00 25.51 O ANISOU 2110 O PRO A 254 2756 3514 3425 89 -159 -260 O ATOM 2111 CB PRO A 254 2.218 26.812 7.392 1.00 25.38 C ANISOU 2111 CB PRO A 254 2601 3465 3576 3 -111 -227 C ATOM 2112 CG PRO A 254 2.860 26.675 8.753 1.00 28.78 C ANISOU 2112 CG PRO A 254 3042 3920 3973 -29 -37 -155 C ATOM 2113 CD PRO A 254 4.183 25.936 8.522 1.00 23.79 C ANISOU 2113 CD PRO A 254 2460 3261 3317 -46 -42 -122 C ATOM 2114 N LEU A 255 5.256 28.559 6.230 1.00 19.13 N ANISOU 2114 N LEU A 255 2029 2677 2562 65 -147 -207 N ATOM 2115 CA LEU A 255 5.851 29.871 6.160 1.00 17.79 C ANISOU 2115 CA LEU A 255 1921 2522 2316 95 -144 -206 C ATOM 2116 C LEU A 255 5.262 30.667 4.988 1.00 19.35 C ANISOU 2116 C LEU A 255 2141 2712 2498 148 -198 -256 C ATOM 2117 O LEU A 255 5.163 30.171 3.861 1.00 17.27 O ANISOU 2117 O LEU A 255 1887 2426 2248 169 -245 -285 O ATOM 2118 CB LEU A 255 7.374 29.744 6.101 1.00 16.77 C ANISOU 2118 CB LEU A 255 1852 2381 2141 84 -129 -172 C ATOM 2119 CG LEU A 255 8.180 31.023 6.293 1.00 17.10 C ANISOU 2119 CG LEU A 255 1950 2433 2116 103 -112 -161 C ATOM 2120 CD1 LEU A 255 7.979 31.657 7.699 1.00 17.53 C ANISOU 2120 CD1 LEU A 255 1982 2523 2157 93 -71 -145 C ATOM 2121 CD2 LEU A 255 9.638 30.768 6.020 1.00 15.18 C ANISOU 2121 CD2 LEU A 255 1756 2168 1842 93 -103 -136 C ATOM 2122 N ASP A 256 4.881 31.915 5.284 1.00 16.06 N ANISOU 2122 N ASP A 256 1734 2316 2050 175 -193 -266 N ATOM 2123 CA ASP A 256 4.314 32.794 4.276 1.00 15.39 C ANISOU 2123 CA ASP A 256 1675 2225 1946 230 -242 -307 C ATOM 2124 C ASP A 256 5.353 33.231 3.207 1.00 15.77 C ANISOU 2124 C ASP A 256 1809 2250 1934 262 -260 -298 C ATOM 2125 O ASP A 256 6.566 33.006 3.354 1.00 15.00 O ANISOU 2125 O ASP A 256 1748 2142 1810 238 -229 -262 O ATOM 2126 CB ASP A 256 3.612 33.996 4.943 1.00 16.38 C ANISOU 2126 CB ASP A 256 1786 2376 2063 250 -230 -321 C ATOM 2127 CG ASP A 256 4.534 35.039 5.586 1.00 17.97 C ANISOU 2127 CG ASP A 256 2035 2584 2209 250 -192 -290 C ATOM 2128 OD1 ASP A 256 5.548 35.370 4.998 1.00 16.18 O ANISOU 2128 OD1 ASP A 256 1872 2334 1942 261 -194 -273 O ATOM 2129 OD2 ASP A 256 4.093 35.717 6.532 1.00 30.13 O1- ANISOU 2129 OD2 ASP A 256 3548 4150 3750 250 -169 -295 O1- ATOM 2130 N GLU A 257 4.868 33.870 2.145 1.00 15.35 N ANISOU 2130 N GLU A 257 1786 2187 1858 319 -307 -331 N ATOM 2131 CA GLU A 257 5.736 34.260 1.042 1.00 14.63 C ANISOU 2131 CA GLU A 257 1776 2074 1707 356 -320 -319 C ATOM 2132 C GLU A 257 6.854 35.227 1.450 1.00 14.96 C ANISOU 2132 C GLU A 257 1872 2108 1705 348 -271 -275 C ATOM 2133 O GLU A 257 7.952 35.146 0.899 1.00 15.01 O ANISOU 2133 O GLU A 257 1931 2095 1677 349 -255 -249 O ATOM 2134 CB GLU A 257 4.907 34.801 -0.121 1.00 18.02 C ANISOU 2134 CB GLU A 257 2231 2499 2116 428 -380 -360 C ATOM 2135 CG GLU A 257 5.711 35.372 -1.275 1.00 22.78 C ANISOU 2135 CG GLU A 257 2925 3082 2647 477 -387 -341 C ATOM 2136 CD GLU A 257 6.851 34.553 -1.855 1.00 31.65 C ANISOU 2136 CD GLU A 257 4087 4193 3747 465 -372 -318 C ATOM 2137 OE1 GLU A 257 6.804 33.300 -1.802 1.00 24.91 O ANISOU 2137 OE1 GLU A 257 3190 3343 2933 435 -385 -335 O ATOM 2138 OE2 GLU A 257 7.825 35.184 -2.324 1.00 31.30 O1- ANISOU 2138 OE2 GLU A 257 4112 4133 3648 482 -343 -281 O1- ATOM 2139 N ASP A 258 6.562 36.128 2.387 1.00 14.02 N ANISOU 2139 N ASP A 258 1735 2002 1591 341 -248 -272 N ATOM 2140 CA ASP A 258 7.640 37.020 2.840 1.00 14.05 C ANISOU 2140 CA ASP A 258 1781 1993 1565 331 -205 -238 C ATOM 2141 C ASP A 258 8.756 36.215 3.527 1.00 14.42 C ANISOU 2141 C ASP A 258 1819 2041 1617 276 -165 -207 C ATOM 2142 O ASP A 258 9.933 36.440 3.253 1.00 14.06 O ANISOU 2142 O ASP A 258 1821 1974 1549 271 -142 -181 O ATOM 2143 CB ASP A 258 7.090 38.036 3.838 1.00 14.94 C ANISOU 2143 CB ASP A 258 1867 2123 1688 333 -192 -250 C ATOM 2144 CG ASP A 258 6.281 39.181 3.232 1.00 17.28 C ANISOU 2144 CG ASP A 258 2185 2408 1973 391 -225 -274 C ATOM 2145 OD1 ASP A 258 6.598 39.599 2.117 1.00 17.91 O ANISOU 2145 OD1 ASP A 258 2324 2458 2021 430 -242 -264 O ATOM 2146 OD2 ASP A 258 5.376 39.677 3.906 1.00 19.75 O1- ANISOU 2146 OD2 ASP A 258 2456 2742 2306 399 -231 -300 O1- ATOM 2147 N GLY A 259 8.372 35.255 4.367 1.00 12.52 N ANISOU 2147 N GLY A 259 1521 1825 1412 239 -157 -208 N ATOM 2148 CA GLY A 259 9.366 34.422 5.038 1.00 12.22 C ANISOU 2148 CA GLY A 259 1475 1789 1379 193 -124 -178 C ATOM 2149 C GLY A 259 10.115 33.548 4.061 1.00 13.84 C ANISOU 2149 C GLY A 259 1710 1969 1579 190 -135 -168 C ATOM 2150 O GLY A 259 11.345 33.388 4.167 1.00 13.04 O ANISOU 2150 O GLY A 259 1636 1855 1463 170 -110 -143 O ATOM 2151 N ARG A 260 9.395 32.976 3.059 1.00 13.15 N ANISOU 2151 N ARG A 260 1617 1875 1504 213 -177 -195 N ATOM 2152 CA ARG A 260 10.076 32.138 2.064 1.00 12.91 C ANISOU 2152 CA ARG A 260 1615 1823 1465 218 -192 -194 C ATOM 2153 C ARG A 260 11.034 32.985 1.217 1.00 13.10 C ANISOU 2153 C ARG A 260 1714 1828 1436 250 -180 -178 C ATOM 2154 O ARG A 260 12.140 32.521 0.896 1.00 13.06 O ANISOU 2154 O ARG A 260 1735 1808 1417 237 -162 -159 O ATOM 2155 CB ARG A 260 9.069 31.379 1.196 1.00 14.68 C ANISOU 2155 CB ARG A 260 1815 2046 1717 243 -246 -235 C ATOM 2156 CG ARG A 260 8.281 30.373 2.051 1.00 17.29 C ANISOU 2156 CG ARG A 260 2066 2386 2118 202 -247 -244 C ATOM 2157 CD ARG A 260 7.391 29.362 1.313 1.00 22.01 C ANISOU 2157 CD ARG A 260 2622 2974 2767 213 -299 -289 C ATOM 2158 NE ARG A 260 6.752 29.912 0.123 1.00 27.23 N ANISOU 2158 NE ARG A 260 3310 3634 3402 277 -354 -334 N ATOM 2159 CZ ARG A 260 5.509 30.396 0.054 1.00 33.70 C ANISOU 2159 CZ ARG A 260 4097 4465 4243 306 -386 -372 C ATOM 2160 NH1 ARG A 260 4.751 30.475 1.145 1.00 30.04 N1+ ANISOU 2160 NH1 ARG A 260 3570 4016 3828 273 -362 -368 N1+ ATOM 2161 NH2 ARG A 260 5.028 30.840 -1.099 1.00 34.23 N ANISOU 2161 NH2 ARG A 260 4195 4530 4280 371 -442 -413 N ATOM 2162 N SER A 261 10.630 34.221 0.848 1.00 13.03 N ANISOU 2162 N SER A 261 1737 1816 1399 291 -187 -184 N ATOM 2163 CA SER A 261 11.509 35.115 0.086 1.00 13.48 C ANISOU 2163 CA SER A 261 1863 1848 1409 321 -166 -160 C ATOM 2164 C SER A 261 12.789 35.382 0.902 1.00 13.92 C ANISOU 2164 C SER A 261 1925 1893 1472 278 -112 -127 C ATOM 2165 O SER A 261 13.890 35.295 0.367 1.00 13.22 O ANISOU 2165 O SER A 261 1874 1784 1366 276 -86 -105 O ATOM 2166 CB SER A 261 10.785 36.431 -0.171 1.00 17.89 C ANISOU 2166 CB SER A 261 2447 2403 1950 367 -179 -167 C ATOM 2167 OG SER A 261 11.662 37.508 -0.485 1.00 19.91 O ANISOU 2167 OG SER A 261 2759 2628 2177 383 -142 -134 O ATOM 2168 N LEU A 262 12.635 35.740 2.176 1.00 12.81 N ANISOU 2168 N LEU A 262 1745 1766 1356 248 -96 -127 N ATOM 2169 CA LEU A 262 13.803 36.012 2.994 1.00 11.59 C ANISOU 2169 CA LEU A 262 1592 1603 1209 214 -54 -106 C ATOM 2170 C LEU A 262 14.695 34.773 3.121 1.00 11.91 C ANISOU 2170 C LEU A 262 1621 1643 1260 178 -43 -93 C ATOM 2171 O LEU A 262 15.913 34.869 2.938 1.00 11.39 O ANISOU 2171 O LEU A 262 1581 1556 1191 168 -15 -76 O ATOM 2172 CB LEU A 262 13.359 36.520 4.361 1.00 11.21 C ANISOU 2172 CB LEU A 262 1502 1579 1179 197 -47 -116 C ATOM 2173 CG LEU A 262 14.500 36.690 5.375 1.00 12.56 C ANISOU 2173 CG LEU A 262 1665 1747 1359 164 -15 -105 C ATOM 2174 CD1 LEU A 262 15.552 37.668 4.909 1.00 13.77 C ANISOU 2174 CD1 LEU A 262 1861 1860 1512 173 10 -94 C ATOM 2175 CD2 LEU A 262 13.935 37.158 6.719 1.00 13.52 C ANISOU 2175 CD2 LEU A 262 1747 1902 1489 158 -13 -121 C ATOM 2176 N LEU A 263 14.096 33.622 3.425 1.00 11.43 N ANISOU 2176 N LEU A 263 1519 1604 1219 160 -64 -102 N ATOM 2177 CA LEU A 263 14.899 32.406 3.558 1.00 10.65 C ANISOU 2177 CA LEU A 263 1409 1502 1136 128 -57 -90 C ATOM 2178 C LEU A 263 15.653 32.093 2.287 1.00 12.35 C ANISOU 2178 C LEU A 263 1668 1693 1333 146 -58 -87 C ATOM 2179 O LEU A 263 16.854 31.738 2.346 1.00 12.10 O ANISOU 2179 O LEU A 263 1646 1648 1303 126 -34 -72 O ATOM 2180 CB LEU A 263 13.996 31.245 3.905 1.00 11.38 C ANISOU 2180 CB LEU A 263 1452 1611 1260 111 -79 -98 C ATOM 2181 CG LEU A 263 14.739 29.907 4.118 1.00 12.28 C ANISOU 2181 CG LEU A 263 1551 1717 1398 78 -75 -83 C ATOM 2182 CD1 LEU A 263 15.775 29.974 5.251 1.00 12.65 C ANISOU 2182 CD1 LEU A 263 1594 1769 1442 49 -42 -58 C ATOM 2183 CD2 LEU A 263 13.768 28.771 4.345 1.00 14.81 C ANISOU 2183 CD2 LEU A 263 1821 2044 1762 62 -96 -90 C ATOM 2184 N SER A 264 14.996 32.215 1.136 1.00 11.88 N ANISOU 2184 N SER A 264 1633 1628 1251 188 -86 -104 N ATOM 2185 CA ASER A 264 15.678 31.907 -0.117 0.50 12.28 C ANISOU 2185 CA ASER A 264 1728 1662 1274 215 -86 -103 C ATOM 2186 CA BSER A 264 15.664 31.908 -0.122 0.50 12.27 C ANISOU 2186 CA BSER A 264 1727 1661 1273 215 -86 -103 C ATOM 2187 C SER A 264 16.894 32.798 -0.312 1.00 13.39 C ANISOU 2187 C SER A 264 1913 1781 1394 217 -37 -75 C ATOM 2188 O SER A 264 17.937 32.343 -0.805 1.00 15.18 O ANISOU 2188 O SER A 264 2160 1995 1614 212 -16 -65 O ATOM 2189 CB ASER A 264 14.721 32.085 -1.280 0.50 15.17 C ANISOU 2189 CB ASER A 264 2120 2032 1610 271 -126 -128 C ATOM 2190 CB BSER A 264 14.676 32.045 -1.274 0.50 14.85 C ANISOU 2190 CB BSER A 264 2078 1993 1571 271 -128 -129 C ATOM 2191 OG ASER A 264 15.434 31.821 -2.479 0.50 16.99 O ANISOU 2191 OG ASER A 264 2400 2252 1803 303 -122 -125 O ATOM 2192 OG BSER A 264 14.297 33.378 -1.575 0.50 15.17 O ANISOU 2192 OG BSER A 264 2155 2029 1582 308 -123 -122 O ATOM 2193 N GLN A 265 16.815 34.071 0.098 1.00 12.10 N ANISOU 2193 N GLN A 265 1760 1610 1228 222 -17 -63 N ATOM 2194 CA GLN A 265 17.935 34.996 -0.036 1.00 11.60 C ANISOU 2194 CA GLN A 265 1730 1517 1160 220 32 -38 C ATOM 2195 C GLN A 265 19.029 34.715 0.983 1.00 12.21 C ANISOU 2195 C GLN A 265 1776 1589 1274 171 60 -32 C ATOM 2196 O GLN A 265 20.196 34.990 0.692 1.00 12.82 O ANISOU 2196 O GLN A 265 1873 1641 1358 164 99 -16 O ATOM 2197 CB GLN A 265 17.465 36.426 0.072 1.00 12.44 C ANISOU 2197 CB GLN A 265 1855 1610 1263 243 40 -32 C ATOM 2198 CG GLN A 265 16.524 36.797 -1.075 1.00 15.44 C ANISOU 2198 CG GLN A 265 2275 1990 1600 302 14 -34 C ATOM 2199 CD GLN A 265 15.950 38.172 -0.896 1.00 19.48 C ANISOU 2199 CD GLN A 265 2802 2488 2114 326 15 -30 C ATOM 2200 NE2 GLN A 265 14.651 38.273 -0.607 1.00 19.60 N ANISOU 2200 NE2 GLN A 265 2791 2525 2129 343 -29 -57 N ATOM 2201 OE1 GLN A 265 16.663 39.159 -0.938 1.00 27.83 O ANISOU 2201 OE1 GLN A 265 3885 3510 3180 326 57 -5 O ATOM 2202 N MET A 266 18.696 34.136 2.126 1.00 10.27 N ANISOU 2202 N MET A 266 1483 1369 1052 140 41 -44 N ATOM 2203 CA MET A 266 19.708 33.733 3.104 1.00 9.45 C ANISOU 2203 CA MET A 266 1350 1266 976 100 59 -41 C ATOM 2204 C MET A 266 20.426 32.455 2.694 1.00 11.45 C ANISOU 2204 C MET A 266 1601 1515 1234 87 57 -37 C ATOM 2205 O MET A 266 21.524 32.187 3.181 1.00 10.99 O ANISOU 2205 O MET A 266 1531 1448 1196 62 75 -34 O ATOM 2206 CB MET A 266 19.024 33.495 4.451 1.00 10.42 C ANISOU 2206 CB MET A 266 1427 1420 1110 80 40 -49 C ATOM 2207 CG MET A 266 18.407 34.770 5.039 1.00 9.66 C ANISOU 2207 CG MET A 266 1328 1332 1013 93 42 -59 C ATOM 2208 SD MET A 266 17.565 34.491 6.627 1.00 11.57 S ANISOU 2208 SD MET A 266 1518 1620 1260 77 28 -69 S ATOM 2209 CE MET A 266 19.001 34.476 7.752 1.00 12.05 C ANISOU 2209 CE MET A 266 1565 1681 1334 52 46 -69 C ATOM 2210 N LEU A 267 19.805 31.681 1.765 1.00 10.51 N ANISOU 2210 N LEU A 267 1493 1401 1098 107 31 -44 N ATOM 2211 CA LEU A 267 20.348 30.407 1.295 1.00 10.40 C ANISOU 2211 CA LEU A 267 1476 1384 1092 99 23 -48 C ATOM 2212 C LEU A 267 20.846 30.437 -0.139 1.00 12.93 C ANISOU 2212 C LEU A 267 1842 1688 1382 133 36 -49 C ATOM 2213 O LEU A 267 21.037 29.384 -0.745 1.00 12.12 O ANISOU 2213 O LEU A 267 1739 1585 1278 139 19 -61 O ATOM 2214 CB LEU A 267 19.359 29.281 1.514 1.00 10.87 C ANISOU 2214 CB LEU A 267 1501 1460 1170 91 -19 -62 C ATOM 2215 CG LEU A 267 18.946 29.016 2.983 1.00 11.38 C ANISOU 2215 CG LEU A 267 1519 1543 1264 57 -23 -54 C ATOM 2216 CD1 LEU A 267 17.982 27.837 3.031 1.00 13.25 C ANISOU 2216 CD1 LEU A 267 1719 1786 1528 49 -57 -63 C ATOM 2217 CD2 LEU A 267 20.153 28.680 3.874 1.00 11.77 C ANISOU 2217 CD2 LEU A 267 1555 1587 1329 26 -2 -39 C ATOM 2218 N HIS A 268 21.110 31.639 -0.679 1.00 12.31 N ANISOU 2218 N HIS A 268 1804 1595 1280 157 68 -34 N ATOM 2219 CA HIS A 268 21.707 31.705 -2.004 1.00 12.65 C ANISOU 2219 CA HIS A 268 1894 1624 1288 192 94 -25 C ATOM 2220 C HIS A 268 23.058 31.028 -1.940 1.00 12.00 C ANISOU 2220 C HIS A 268 1800 1530 1230 165 122 -23 C ATOM 2221 O HIS A 268 23.810 31.186 -0.990 1.00 12.41 O ANISOU 2221 O HIS A 268 1822 1571 1321 127 143 -18 O ATOM 2222 CB HIS A 268 21.920 33.156 -2.473 1.00 16.13 C ANISOU 2222 CB HIS A 268 2379 2042 1709 217 137 2 C ATOM 2223 CG HIS A 268 20.705 33.831 -3.053 1.00 20.63 C ANISOU 2223 CG HIS A 268 2980 2620 2238 264 111 2 C ATOM 2224 CD2 HIS A 268 20.274 35.107 -2.882 1.00 23.49 C ANISOU 2224 CD2 HIS A 268 3359 2968 2599 278 123 17 C ATOM 2225 ND1 HIS A 268 19.898 33.211 -3.999 1.00 24.83 N ANISOU 2225 ND1 HIS A 268 3533 3172 2728 309 68 -18 N ATOM 2226 CE1 HIS A 268 18.957 34.102 -4.301 1.00 23.45 C ANISOU 2226 CE1 HIS A 268 3384 2998 2526 348 52 -15 C ATOM 2227 NE2 HIS A 268 19.155 35.260 -3.673 1.00 23.89 N ANISOU 2227 NE2 HIS A 268 3440 3033 2604 331 85 8 N ATOM 2228 N TYR A 269 23.398 30.299 -3.006 1.00 12.24 N ANISOU 2228 N TYR A 269 1854 1562 1234 191 123 -31 N ATOM 2229 CA TYR A 269 24.684 29.606 -3.065 1.00 11.74 C ANISOU 2229 CA TYR A 269 1779 1488 1193 172 149 -33 C ATOM 2230 C TYR A 269 25.849 30.570 -3.122 1.00 12.12 C ANISOU 2230 C TYR A 269 1841 1509 1254 162 218 -7 C ATOM 2231 O TYR A 269 26.785 30.441 -2.339 1.00 12.39 O ANISOU 2231 O TYR A 269 1840 1530 1336 123 236 -9 O ATOM 2232 CB TYR A 269 24.752 28.730 -4.312 1.00 11.81 C ANISOU 2232 CB TYR A 269 1815 1507 1165 211 137 -51 C ATOM 2233 CG TYR A 269 24.214 27.352 -4.095 1.00 11.10 C ANISOU 2233 CG TYR A 269 1690 1430 1096 202 76 -84 C ATOM 2234 CD1 TYR A 269 24.798 26.500 -3.164 1.00 11.95 C ANISOU 2234 CD1 TYR A 269 1751 1531 1258 156 67 -90 C ATOM 2235 CD2 TYR A 269 23.149 26.879 -4.839 1.00 11.76 C ANISOU 2235 CD2 TYR A 269 1787 1531 1152 242 25 -112 C ATOM 2236 CE1 TYR A 269 24.348 25.202 -2.994 1.00 11.28 C ANISOU 2236 CE1 TYR A 269 1635 1450 1201 147 16 -116 C ATOM 2237 CE2 TYR A 269 22.687 25.578 -4.685 1.00 11.78 C ANISOU 2237 CE2 TYR A 269 1751 1536 1188 231 -29 -145 C ATOM 2238 CZ TYR A 269 23.299 24.745 -3.763 1.00 11.23 C ANISOU 2238 CZ TYR A 269 1637 1454 1175 182 -31 -144 C ATOM 2239 OH TYR A 269 22.856 23.477 -3.570 1.00 12.90 O ANISOU 2239 OH TYR A 269 1812 1662 1428 170 -80 -170 O ATOM 2240 N ASP A 270 25.775 31.580 -4.011 1.00 12.82 N ANISOU 2240 N ASP A 270 1978 1586 1305 199 256 18 N ATOM 2241 CA ASP A 270 26.887 32.509 -4.180 1.00 13.69 C ANISOU 2241 CA ASP A 270 2100 1663 1437 191 330 46 C ATOM 2242 C ASP A 270 26.929 33.429 -2.957 1.00 14.03 C ANISOU 2242 C ASP A 270 2110 1687 1535 152 335 50 C ATOM 2243 O ASP A 270 25.982 34.207 -2.727 1.00 13.55 O ANISOU 2243 O ASP A 270 2060 1627 1461 164 317 56 O ATOM 2244 CB ASP A 270 26.701 33.308 -5.474 1.00 15.74 C ANISOU 2244 CB ASP A 270 2426 1914 1639 245 372 80 C ATOM 2245 CG ASP A 270 27.827 34.264 -5.787 1.00 17.95 C ANISOU 2245 CG ASP A 270 2722 2154 1946 239 460 117 C ATOM 2246 OD1 ASP A 270 28.710 34.456 -4.912 1.00 16.28 O ANISOU 2246 OD1 ASP A 270 2461 1916 1807 189 483 111 O ATOM 2247 OD2 ASP A 270 27.904 34.714 -6.945 1.00 21.10 O1- ANISOU 2247 OD2 ASP A 270 3178 2546 2295 286 506 151 O1- ATOM 2248 N PRO A 271 28.008 33.367 -2.153 1.00 13.02 N ANISOU 2248 N PRO A 271 1939 1541 1469 109 356 40 N ATOM 2249 CA PRO A 271 28.051 34.204 -0.937 1.00 15.35 C ANISOU 2249 CA PRO A 271 2198 1820 1813 77 351 32 C ATOM 2250 C PRO A 271 27.896 35.669 -1.276 1.00 18.42 C ANISOU 2250 C PRO A 271 2615 2175 2207 93 393 59 C ATOM 2251 O PRO A 271 27.398 36.433 -0.451 1.00 18.69 O ANISOU 2251 O PRO A 271 2633 2205 2263 83 374 51 O ATOM 2252 CB PRO A 271 29.417 33.908 -0.323 1.00 17.77 C ANISOU 2252 CB PRO A 271 2460 2110 2183 41 372 14 C ATOM 2253 CG PRO A 271 29.920 32.696 -1.024 1.00 19.59 C ANISOU 2253 CG PRO A 271 2695 2353 2395 48 374 9 C ATOM 2254 CD PRO A 271 29.190 32.479 -2.277 1.00 14.93 C ANISOU 2254 CD PRO A 271 2157 1778 1736 92 375 27 C ATOM 2255 N ASN A 272 28.267 36.072 -2.494 1.00 16.66 N ANISOU 2255 N ASN A 272 2438 1930 1963 121 449 92 N ATOM 2256 CA ASN A 272 28.137 37.473 -2.884 1.00 17.78 C ANISOU 2256 CA ASN A 272 2611 2032 2112 139 494 127 C ATOM 2257 C ASN A 272 26.690 37.864 -3.166 1.00 19.90 C ANISOU 2257 C ASN A 272 2920 2321 2322 179 454 136 C ATOM 2258 O ASN A 272 26.363 39.077 -3.148 1.00 23.67 O ANISOU 2258 O ASN A 272 3414 2766 2813 190 472 156 O ATOM 2259 CB ASN A 272 29.036 37.730 -4.100 1.00 20.75 C ANISOU 2259 CB ASN A 272 3025 2378 2481 159 577 167 C ATOM 2260 CG ASN A 272 30.479 37.614 -3.697 1.00 32.05 C ANISOU 2260 CG ASN A 272 4406 3779 3991 115 622 155 C ATOM 2261 ND2 ASN A 272 31.077 36.438 -3.903 1.00 31.68 N ANISOU 2261 ND2 ASN A 272 4344 3757 3934 109 618 136 N ATOM 2262 OD1 ASN A 272 31.016 38.495 -3.030 1.00 34.44 O ANISOU 2262 OD1 ASN A 272 4674 4039 4372 83 648 151 O ATOM 2263 N LYS A 273 25.820 36.905 -3.454 1.00 18.30 N ANISOU 2263 N LYS A 273 2729 2164 2060 203 398 119 N ATOM 2264 CA LYS A 273 24.405 37.166 -3.722 1.00 19.13 C ANISOU 2264 CA LYS A 273 2864 2291 2115 243 351 118 C ATOM 2265 C LYS A 273 23.639 37.050 -2.421 1.00 18.70 C ANISOU 2265 C LYS A 273 2758 2258 2088 213 294 83 C ATOM 2266 O LYS A 273 22.555 37.591 -2.309 1.00 18.15 O ANISOU 2266 O LYS A 273 2698 2197 2001 235 262 80 O ATOM 2267 CB LYS A 273 23.790 36.165 -4.732 1.00 21.74 C ANISOU 2267 CB LYS A 273 3227 2660 2374 288 315 108 C ATOM 2268 CG LYS A 273 24.381 36.201 -6.147 1.00 21.57 C ANISOU 2268 CG LYS A 273 3265 2629 2301 334 367 141 C ATOM 2269 CD LYS A 273 23.668 35.247 -7.111 1.00 26.90 C ANISOU 2269 CD LYS A 273 3971 3345 2903 387 319 119 C ATOM 2270 CE LYS A 273 24.206 35.301 -8.521 1.00 32.56 C ANISOU 2270 CE LYS A 273 4753 4061 3555 443 369 150 C ATOM 2271 NZ LYS A 273 25.544 34.656 -8.637 1.00 26.42 N1+ ANISOU 2271 NZ LYS A 273 3958 3278 2803 415 420 151 N1+ ATOM 2272 N ARG A 274 24.154 36.270 -1.451 1.00 14.34 N ANISOU 2272 N ARG A 274 2154 1720 1576 168 278 58 N ATOM 2273 CA ARG A 274 23.453 36.000 -0.203 1.00 13.28 C ANISOU 2273 CA ARG A 274 1974 1613 1459 143 229 30 C ATOM 2274 C ARG A 274 23.155 37.309 0.526 1.00 13.18 C ANISOU 2274 C ARG A 274 1951 1582 1474 139 234 28 C ATOM 2275 O ARG A 274 24.024 38.185 0.600 1.00 13.96 O ANISOU 2275 O ARG A 274 2050 1640 1612 128 278 38 O ATOM 2276 CB ARG A 274 24.309 35.015 0.625 1.00 12.93 C ANISOU 2276 CB ARG A 274 1885 1580 1450 102 222 11 C ATOM 2277 CG ARG A 274 23.520 34.247 1.670 1.00 13.57 C ANISOU 2277 CG ARG A 274 1926 1698 1531 85 170 -10 C ATOM 2278 CD ARG A 274 24.412 33.211 2.365 1.00 12.40 C ANISOU 2278 CD ARG A 274 1743 1559 1412 52 164 -20 C ATOM 2279 NE ARG A 274 24.933 32.219 1.412 1.00 11.56 N ANISOU 2279 NE ARG A 274 1650 1447 1294 58 170 -17 N ATOM 2280 CZ ARG A 274 26.115 31.603 1.519 1.00 10.34 C ANISOU 2280 CZ ARG A 274 1480 1282 1167 39 186 -22 C ATOM 2281 NH1 ARG A 274 26.886 31.806 2.577 1.00 10.69 N1+ ANISOU 2281 NH1 ARG A 274 1490 1320 1251 11 191 -33 N1+ ATOM 2282 NH2 ARG A 274 26.547 30.809 0.548 1.00 11.36 N ANISOU 2282 NH2 ARG A 274 1625 1408 1283 51 194 -22 N ATOM 2283 N ILE A 275 21.916 37.474 1.011 1.00 12.00 N ANISOU 2283 N ILE A 275 1792 1459 1309 151 191 13 N ATOM 2284 CA ILE A 275 21.519 38.706 1.665 1.00 11.78 C ANISOU 2284 CA ILE A 275 1755 1417 1303 153 191 6 C ATOM 2285 C ILE A 275 22.423 39.002 2.882 1.00 11.61 C ANISOU 2285 C ILE A 275 1690 1385 1337 115 203 -14 C ATOM 2286 O ILE A 275 22.850 38.083 3.598 1.00 12.50 O ANISOU 2286 O ILE A 275 1768 1522 1458 88 189 -30 O ATOM 2287 CB ILE A 275 20.025 38.651 2.048 1.00 13.15 C ANISOU 2287 CB ILE A 275 1917 1629 1452 171 142 -13 C ATOM 2288 CG1 ILE A 275 19.436 40.037 2.372 1.00 13.61 C ANISOU 2288 CG1 ILE A 275 1979 1669 1523 190 140 -19 C ATOM 2289 CG2 ILE A 275 19.767 37.648 3.191 1.00 13.28 C ANISOU 2289 CG2 ILE A 275 1882 1688 1475 141 111 -36 C ATOM 2290 CD1 ILE A 275 17.901 40.058 2.407 1.00 15.33 C ANISOU 2290 CD1 ILE A 275 2192 1920 1713 218 96 -35 C ATOM 2291 N SER A 276 22.721 40.281 3.123 1.00 11.76 N ANISOU 2291 N SER A 276 1708 1365 1395 116 226 -16 N ATOM 2292 CA SER A 276 23.484 40.660 4.312 1.00 12.02 C ANISOU 2292 CA SER A 276 1696 1388 1483 87 227 -48 C ATOM 2293 C SER A 276 22.526 40.744 5.496 1.00 12.14 C ANISOU 2293 C SER A 276 1680 1448 1485 91 181 -80 C ATOM 2294 O SER A 276 21.297 40.870 5.324 1.00 12.12 O ANISOU 2294 O SER A 276 1691 1467 1446 115 158 -77 O ATOM 2295 CB SER A 276 24.147 42.019 4.115 1.00 12.62 C ANISOU 2295 CB SER A 276 1777 1399 1617 87 267 -44 C ATOM 2296 OG SER A 276 23.157 43.025 4.028 1.00 14.69 O ANISOU 2296 OG SER A 276 2059 1650 1872 116 256 -41 O ATOM 2297 N ALA A 277 23.078 40.753 6.721 1.00 11.14 N ANISOU 2297 N ALA A 277 1512 1334 1388 71 168 -115 N ATOM 2298 CA ALA A 277 22.215 40.914 7.895 1.00 10.98 C ANISOU 2298 CA ALA A 277 1463 1358 1350 80 131 -146 C ATOM 2299 C ALA A 277 21.522 42.266 7.861 1.00 12.25 C ANISOU 2299 C ALA A 277 1633 1496 1526 104 129 -158 C ATOM 2300 O ALA A 277 20.323 42.354 8.175 1.00 12.28 O ANISOU 2300 O ALA A 277 1634 1537 1497 124 104 -167 O ATOM 2301 CB ALA A 277 23.049 40.792 9.165 1.00 12.10 C ANISOU 2301 CB ALA A 277 1565 1517 1517 65 117 -183 C ATOM 2302 N LYS A 278 22.258 43.325 7.474 1.00 13.08 N ANISOU 2302 N LYS A 278 1682 1495 1791 -47 -55 76 N ATOM 2303 CA LYS A 278 21.616 44.655 7.417 1.00 13.62 C ANISOU 2303 CA LYS A 278 1860 1468 1846 -76 -50 38 C ATOM 2304 C LYS A 278 20.461 44.701 6.418 1.00 15.90 C ANISOU 2304 C LYS A 278 2211 1704 2126 25 -28 36 C ATOM 2305 O LYS A 278 19.392 45.256 6.727 1.00 16.45 O ANISOU 2305 O LYS A 278 2346 1723 2180 68 -32 5 O ATOM 2306 CB LYS A 278 22.673 45.718 7.089 1.00 18.30 C ANISOU 2306 CB LYS A 278 2473 2038 2441 -187 -27 62 C ATOM 2307 CG LYS A 278 22.139 47.127 6.848 1.00 31.80 C ANISOU 2307 CG LYS A 278 4328 3609 4143 -208 8 40 C ATOM 2308 CD LYS A 278 23.256 48.173 6.818 1.00 45.47 C ANISOU 2308 CD LYS A 278 6095 5306 5874 -367 37 50 C ATOM 2309 CE LYS A 278 23.431 48.869 8.148 1.00 60.64 C ANISOU 2309 CE LYS A 278 8070 7199 7771 -500 17 -24 C ATOM 2310 NZ LYS A 278 22.219 49.629 8.567 1.00 68.48 N1+ ANISOU 2310 NZ LYS A 278 9223 8043 8755 -435 47 -82 N1+ ATOM 2311 N ALA A 279 20.651 44.127 5.226 1.00 13.72 N ANISOU 2311 N ALA A 279 1907 1458 1847 67 -2 69 N ATOM 2312 CA ALA A 279 19.567 44.128 4.251 1.00 13.96 C ANISOU 2312 CA ALA A 279 1980 1482 1845 148 7 68 C ATOM 2313 C ALA A 279 18.405 43.244 4.699 1.00 15.66 C ANISOU 2313 C ALA A 279 2171 1737 2045 194 -22 23 C ATOM 2314 O ALA A 279 17.241 43.586 4.476 1.00 16.62 O ANISOU 2314 O ALA A 279 2315 1869 2133 249 -34 15 O ATOM 2315 CB ALA A 279 20.077 43.735 2.857 1.00 15.21 C ANISOU 2315 CB ALA A 279 2124 1674 1982 163 45 102 C ATOM 2316 N ALA A 280 18.699 42.140 5.394 1.00 12.65 N ANISOU 2316 N ALA A 280 1739 1384 1685 174 -29 4 N ATOM 2317 CA ALA A 280 17.649 41.255 5.894 1.00 12.35 C ANISOU 2317 CA ALA A 280 1684 1374 1633 192 -45 -36 C ATOM 2318 C ALA A 280 16.768 41.960 6.905 1.00 13.73 C ANISOU 2318 C ALA A 280 1875 1544 1800 203 -74 -58 C ATOM 2319 O ALA A 280 15.570 41.746 6.926 1.00 13.57 O ANISOU 2319 O ALA A 280 1843 1562 1750 234 -84 -82 O ATOM 2320 CB ALA A 280 18.269 40.005 6.503 1.00 13.06 C ANISOU 2320 CB ALA A 280 1739 1472 1753 177 -29 -31 C ATOM 2321 N LEU A 281 17.351 42.870 7.720 1.00 13.10 N ANISOU 2321 N LEU A 281 1821 1422 1733 171 -81 -55 N ATOM 2322 CA LEU A 281 16.530 43.592 8.707 1.00 13.49 C ANISOU 2322 CA LEU A 281 1907 1452 1766 188 -89 -89 C ATOM 2323 C LEU A 281 15.486 44.462 8.050 1.00 15.76 C ANISOU 2323 C LEU A 281 2240 1717 2030 272 -70 -81 C ATOM 2324 O LEU A 281 14.448 44.741 8.674 1.00 16.66 O ANISOU 2324 O LEU A 281 2361 1845 2124 327 -65 -103 O ATOM 2325 CB LEU A 281 17.422 44.458 9.598 1.00 13.95 C ANISOU 2325 CB LEU A 281 2008 1463 1828 112 -90 -104 C ATOM 2326 CG LEU A 281 18.279 43.680 10.587 1.00 14.91 C ANISOU 2326 CG LEU A 281 2065 1652 1950 42 -121 -101 C ATOM 2327 CD1 LEU A 281 19.342 44.595 11.206 1.00 17.55 C ANISOU 2327 CD1 LEU A 281 2424 1976 2269 -69 -131 -115 C ATOM 2328 CD2 LEU A 281 17.401 43.051 11.685 1.00 15.55 C ANISOU 2328 CD2 LEU A 281 2127 1777 2005 66 -135 -128 C ATOM 2329 N ALA A 282 15.739 44.885 6.816 1.00 14.58 N ANISOU 2329 N ALA A 282 2114 1547 1878 297 -53 -39 N ATOM 2330 CA ALA A 282 14.822 45.746 6.058 1.00 15.76 C ANISOU 2330 CA ALA A 282 2302 1691 1996 400 -33 -1 C ATOM 2331 C ALA A 282 13.789 44.925 5.279 1.00 16.24 C ANISOU 2331 C ALA A 282 2278 1884 2008 451 -60 9 C ATOM 2332 O ALA A 282 12.924 45.496 4.614 1.00 17.52 O ANISOU 2332 O ALA A 282 2437 2095 2126 548 -56 55 O ATOM 2333 CB ALA A 282 15.616 46.617 5.086 1.00 17.91 C ANISOU 2333 CB ALA A 282 2645 1887 2274 395 1 54 C ATOM 2334 N HIS A 283 13.871 43.593 5.337 1.00 14.06 N ANISOU 2334 N HIS A 283 1938 1673 1731 383 -84 -31 N ATOM 2335 CA HIS A 283 12.973 42.784 4.559 1.00 12.68 C ANISOU 2335 CA HIS A 283 1698 1621 1499 385 -105 -41 C ATOM 2336 C HIS A 283 11.511 42.962 5.013 1.00 15.10 C ANISOU 2336 C HIS A 283 1944 2028 1766 446 -122 -42 C ATOM 2337 O HIS A 283 11.235 43.030 6.218 1.00 14.80 O ANISOU 2337 O HIS A 283 1903 1965 1755 450 -115 -65 O ATOM 2338 CB HIS A 283 13.407 41.312 4.661 1.00 12.46 C ANISOU 2338 CB HIS A 283 1650 1599 1487 289 -102 -92 C ATOM 2339 CG HIS A 283 12.742 40.435 3.653 1.00 13.08 C ANISOU 2339 CG HIS A 283 1693 1780 1497 248 -110 -122 C ATOM 2340 CD2 HIS A 283 13.197 39.995 2.460 1.00 14.09 C ANISOU 2340 CD2 HIS A 283 1844 1923 1587 215 -94 -133 C ATOM 2341 ND1 HIS A 283 11.448 39.986 3.836 1.00 14.36 N ANISOU 2341 ND1 HIS A 283 1789 2059 1610 223 -136 -152 N ATOM 2342 CE1 HIS A 283 11.146 39.288 2.752 1.00 14.65 C ANISOU 2342 CE1 HIS A 283 1811 2180 1574 158 -141 -186 C ATOM 2343 NE2 HIS A 283 12.177 39.235 1.913 1.00 15.02 N ANISOU 2343 NE2 HIS A 283 1920 2162 1624 154 -113 -181 N ATOM 2344 N PRO A 284 10.539 42.927 4.073 1.00 14.34 N ANISOU 2344 N PRO A 284 1780 2076 1592 484 -146 -16 N ATOM 2345 CA PRO A 284 9.115 43.027 4.476 1.00 14.97 C ANISOU 2345 CA PRO A 284 1765 2296 1626 544 -163 -5 C ATOM 2346 C PRO A 284 8.628 41.957 5.462 1.00 15.83 C ANISOU 2346 C PRO A 284 1818 2452 1747 448 -168 -72 C ATOM 2347 O PRO A 284 7.636 42.213 6.161 1.00 16.56 O ANISOU 2347 O PRO A 284 1843 2629 1821 504 -164 -61 O ATOM 2348 CB PRO A 284 8.367 42.916 3.151 1.00 17.27 C ANISOU 2348 CB PRO A 284 1973 2775 1815 561 -201 33 C ATOM 2349 CG PRO A 284 9.335 43.357 2.119 1.00 20.23 C ANISOU 2349 CG PRO A 284 2431 3071 2186 576 -190 71 C ATOM 2350 CD PRO A 284 10.696 42.918 2.603 1.00 15.17 C ANISOU 2350 CD PRO A 284 1883 2247 1635 484 -159 16 C ATOM 2351 N PHE A 285 9.328 40.815 5.600 1.00 13.73 N ANISOU 2351 N PHE A 285 1585 2121 1512 320 -163 -130 N ATOM 2352 CA PHE A 285 8.948 39.817 6.601 1.00 13.80 C ANISOU 2352 CA PHE A 285 1565 2142 1536 232 -153 -177 C ATOM 2353 C PHE A 285 8.898 40.455 8.006 1.00 14.63 C ANISOU 2353 C PHE A 285 1684 2191 1682 297 -134 -165 C ATOM 2354 O PHE A 285 8.124 40.005 8.867 1.00 16.18 O ANISOU 2354 O PHE A 285 1828 2455 1866 266 -125 -183 O ATOM 2355 CB PHE A 285 9.967 38.661 6.630 1.00 13.10 C ANISOU 2355 CB PHE A 285 1547 1938 1492 128 -127 -216 C ATOM 2356 CG PHE A 285 9.617 37.516 7.558 1.00 12.62 C ANISOU 2356 CG PHE A 285 1480 1870 1445 35 -103 -249 C ATOM 2357 CD1 PHE A 285 8.425 36.802 7.399 1.00 14.56 C ANISOU 2357 CD1 PHE A 285 1658 2242 1633 -58 -106 -286 C ATOM 2358 CD2 PHE A 285 10.494 37.115 8.560 1.00 12.56 C ANISOU 2358 CD2 PHE A 285 1530 1743 1500 30 -74 -237 C ATOM 2359 CE1 PHE A 285 8.139 35.690 8.191 1.00 14.39 C ANISOU 2359 CE1 PHE A 285 1649 2193 1625 -163 -68 -313 C ATOM 2360 CE2 PHE A 285 10.199 36.003 9.364 1.00 14.40 C ANISOU 2360 CE2 PHE A 285 1771 1958 1742 -49 -40 -249 C ATOM 2361 CZ PHE A 285 9.022 35.301 9.167 1.00 14.29 C ANISOU 2361 CZ PHE A 285 1712 2039 1680 -148 -31 -289 C ATOM 2362 N PHE A 286 9.711 41.502 8.262 1.00 13.28 N ANISOU 2362 N PHE A 286 1592 1903 1550 369 -121 -142 N ATOM 2363 CA PHE A 286 9.766 42.127 9.588 1.00 12.86 C ANISOU 2363 CA PHE A 286 1578 1788 1519 408 -97 -151 C ATOM 2364 C PHE A 286 8.847 43.309 9.754 1.00 17.27 C ANISOU 2364 C PHE A 286 2131 2382 2050 541 -71 -126 C ATOM 2365 O PHE A 286 8.892 43.954 10.811 1.00 17.20 O ANISOU 2365 O PHE A 286 2179 2306 2050 578 -36 -147 O ATOM 2366 CB PHE A 286 11.215 42.494 9.980 1.00 13.28 C ANISOU 2366 CB PHE A 286 1726 1700 1620 372 -92 -157 C ATOM 2367 CG PHE A 286 12.092 41.273 10.010 1.00 11.82 C ANISOU 2367 CG PHE A 286 1533 1496 1463 275 -104 -163 C ATOM 2368 CD1 PHE A 286 11.887 40.272 10.954 1.00 13.17 C ANISOU 2368 CD1 PHE A 286 1675 1695 1632 223 -100 -176 C ATOM 2369 CD2 PHE A 286 13.120 41.124 9.100 1.00 12.14 C ANISOU 2369 CD2 PHE A 286 1597 1487 1527 251 -106 -145 C ATOM 2370 CE1 PHE A 286 12.689 39.125 10.972 1.00 11.86 C ANISOU 2370 CE1 PHE A 286 1517 1494 1494 162 -93 -163 C ATOM 2371 CE2 PHE A 286 13.931 39.990 9.123 1.00 12.10 C ANISOU 2371 CE2 PHE A 286 1589 1460 1550 194 -97 -140 C ATOM 2372 CZ PHE A 286 13.713 38.991 10.055 1.00 11.83 C ANISOU 2372 CZ PHE A 286 1537 1439 1519 158 -88 -146 C ATOM 2373 N GLN A 287 7.941 43.547 8.783 1.00 16.71 N ANISOU 2373 N GLN A 287 1986 2431 1934 619 -81 -81 N ATOM 2374 CA GLN A 287 7.008 44.666 8.876 1.00 19.18 C ANISOU 2374 CA GLN A 287 2281 2788 2217 787 -42 -33 C ATOM 2375 C GLN A 287 6.186 44.617 10.159 1.00 21.69 C ANISOU 2375 C GLN A 287 2555 3163 2523 818 -6 -61 C ATOM 2376 O GLN A 287 5.920 45.666 10.755 1.00 24.13 O ANISOU 2376 O GLN A 287 2928 3406 2834 948 58 -51 O ATOM 2377 CB GLN A 287 6.104 44.687 7.637 1.00 20.86 C ANISOU 2377 CB GLN A 287 2378 3185 2363 859 -73 37 C ATOM 2378 CG GLN A 287 5.264 45.968 7.479 1.00 30.99 C ANISOU 2378 CG GLN A 287 3648 4510 3616 1081 -25 126 C ATOM 2379 CD GLN A 287 4.827 46.220 6.054 1.00 54.03 C ANISOU 2379 CD GLN A 287 6488 7574 6466 1164 -60 221 C ATOM 2380 NE2 GLN A 287 3.882 47.137 5.887 1.00 51.65 N ANISOU 2380 NE2 GLN A 287 6133 7371 6123 1377 -21 323 N ATOM 2381 OE1 GLN A 287 5.349 45.641 5.088 1.00 49.70 O ANISOU 2381 OE1 GLN A 287 5935 7055 5896 1053 -115 212 O ATOM 2382 N ASP A 288 5.733 43.442 10.546 1.00 17.01 N ANISOU 2382 N ASP A 288 1864 2688 1911 706 -32 -93 N ATOM 2383 CA ASP A 288 4.867 43.305 11.726 1.00 17.42 C ANISOU 2383 CA ASP A 288 1856 2824 1940 726 8 -111 C ATOM 2384 C ASP A 288 5.589 42.655 12.919 1.00 17.27 C ANISOU 2384 C ASP A 288 1909 2706 1949 604 15 -169 C ATOM 2385 O ASP A 288 4.943 42.061 13.788 1.00 17.35 O ANISOU 2385 O ASP A 288 1854 2805 1932 561 36 -183 O ATOM 2386 CB ASP A 288 3.602 42.508 11.345 1.00 20.25 C ANISOU 2386 CB ASP A 288 2028 3427 2238 686 -17 -88 C ATOM 2387 CG ASP A 288 3.895 41.065 10.970 1.00 25.13 C ANISOU 2387 CG ASP A 288 2621 4069 2857 478 -64 -129 C ATOM 2388 OD1 ASP A 288 5.099 40.710 10.866 1.00 27.42 O ANISOU 2388 OD1 ASP A 288 3028 4191 3198 402 -77 -158 O ATOM 2389 OD2 ASP A 288 2.928 40.282 10.779 1.00 25.12 O1- ANISOU 2389 OD2 ASP A 288 2486 4255 2804 389 -79 -131 O1- ATOM 2390 N VAL A 289 6.918 42.766 12.960 1.00 15.37 N ANISOU 2390 N VAL A 289 1787 2299 1752 551 0 -190 N ATOM 2391 CA VAL A 289 7.651 42.174 14.058 1.00 13.43 C ANISOU 2391 CA VAL A 289 1593 1991 1518 451 -1 -224 C ATOM 2392 C VAL A 289 7.270 42.812 15.407 1.00 15.66 C ANISOU 2392 C VAL A 289 1913 2273 1765 504 51 -255 C ATOM 2393 O VAL A 289 7.001 44.022 15.501 1.00 16.65 O ANISOU 2393 O VAL A 289 2097 2352 1878 620 98 -266 O ATOM 2394 CB VAL A 289 9.183 42.190 13.814 1.00 14.37 C ANISOU 2394 CB VAL A 289 1803 1975 1682 387 -32 -228 C ATOM 2395 CG1 VAL A 289 9.764 43.594 13.915 1.00 15.95 C ANISOU 2395 CG1 VAL A 289 2112 2061 1889 444 -10 -246 C ATOM 2396 CG2 VAL A 289 9.921 41.244 14.753 1.00 13.96 C ANISOU 2396 CG2 VAL A 289 1763 1908 1633 285 -45 -233 C ATOM 2397 N THR A 290 7.236 41.954 16.440 1.00 13.40 N ANISOU 2397 N THR A 290 1604 2032 1455 421 54 -266 N ATOM 2398 CA THR A 290 6.917 42.294 17.827 1.00 13.64 C ANISOU 2398 CA THR A 290 1665 2085 1431 442 103 -299 C ATOM 2399 C THR A 290 7.929 41.549 18.704 1.00 15.34 C ANISOU 2399 C THR A 290 1924 2268 1635 325 72 -300 C ATOM 2400 O THR A 290 8.748 40.752 18.197 1.00 13.72 O ANISOU 2400 O THR A 290 1714 2025 1473 251 25 -266 O ATOM 2401 CB THR A 290 5.486 41.855 18.161 1.00 16.89 C ANISOU 2401 CB THR A 290 1958 2658 1802 473 146 -281 C ATOM 2402 CG2 THR A 290 4.445 42.476 17.249 1.00 16.28 C ANISOU 2402 CG2 THR A 290 1795 2666 1723 599 167 -255 C ATOM 2403 OG1 THR A 290 5.387 40.422 18.131 1.00 16.85 O ANISOU 2403 OG1 THR A 290 1880 2717 1804 344 119 -251 O ATOM 2404 N LYS A 291 7.831 41.732 20.017 1.00 14.99 N ANISOU 2404 N LYS A 291 1916 2255 1525 317 105 -328 N ATOM 2405 CA LYS A 291 8.715 41.064 20.957 1.00 15.31 C ANISOU 2405 CA LYS A 291 1984 2303 1530 221 74 -312 C ATOM 2406 C LYS A 291 7.873 40.316 21.991 1.00 15.78 C ANISOU 2406 C LYS A 291 1993 2476 1528 199 117 -288 C ATOM 2407 O LYS A 291 7.651 40.826 23.105 1.00 16.38 O ANISOU 2407 O LYS A 291 2109 2595 1519 214 156 -329 O ATOM 2408 CB LYS A 291 9.691 42.059 21.600 1.00 16.67 C ANISOU 2408 CB LYS A 291 2262 2415 1655 196 60 -370 C ATOM 2409 CG LYS A 291 10.766 41.348 22.403 1.00 20.34 C ANISOU 2409 CG LYS A 291 2727 2924 2077 98 7 -330 C ATOM 2410 CD LYS A 291 11.606 42.343 23.223 1.00 24.94 C ANISOU 2410 CD LYS A 291 3401 3498 2577 39 -9 -403 C ATOM 2411 CE LYS A 291 12.664 41.615 24.015 1.00 34.68 C ANISOU 2411 CE LYS A 291 4600 4826 3749 -50 -74 -342 C ATOM 2412 NZ LYS A 291 13.625 42.560 24.645 1.00 47.92 N1+ ANISOU 2412 NZ LYS A 291 6347 6521 5338 -146 -110 -415 N1+ ATOM 2413 N PRO A 292 7.359 39.117 21.643 1.00 14.73 N ANISOU 2413 N PRO A 292 1780 2390 1427 154 121 -229 N ATOM 2414 CA PRO A 292 6.564 38.350 22.597 1.00 15.72 C ANISOU 2414 CA PRO A 292 1860 2619 1495 114 171 -196 C ATOM 2415 C PRO A 292 7.403 37.792 23.732 1.00 18.26 C ANISOU 2415 C PRO A 292 2233 2944 1760 58 158 -151 C ATOM 2416 O PRO A 292 8.649 37.673 23.593 1.00 18.80 O ANISOU 2416 O PRO A 292 2347 2945 1851 37 101 -124 O ATOM 2417 CB PRO A 292 5.988 37.197 21.749 1.00 17.27 C ANISOU 2417 CB PRO A 292 1982 2832 1749 46 178 -150 C ATOM 2418 CG PRO A 292 6.215 37.555 20.317 1.00 18.69 C ANISOU 2418 CG PRO A 292 2153 2949 1999 75 135 -174 C ATOM 2419 CD PRO A 292 7.459 38.419 20.346 1.00 15.04 C ANISOU 2419 CD PRO A 292 1780 2386 1548 122 92 -197 C ATOM 2420 N VAL A 293 6.714 37.473 24.830 1.00 19.37 N ANISOU 2420 N VAL A 293 2355 3186 1819 40 213 -132 N ATOM 2421 CA VAL A 293 7.241 36.843 26.048 1.00 21.27 C ANISOU 2421 CA VAL A 293 2631 3473 1979 -8 214 -67 C ATOM 2422 C VAL A 293 7.121 35.323 25.768 1.00 26.81 C ANISOU 2422 C VAL A 293 3307 4144 2736 -76 236 39 C ATOM 2423 O VAL A 293 6.028 34.840 25.454 1.00 29.60 O ANISOU 2423 O VAL A 293 3604 4531 3114 -114 291 42 O ATOM 2424 CB VAL A 293 6.458 37.257 27.328 1.00 27.34 C ANISOU 2424 CB VAL A 293 3401 4366 2623 6 280 -98 C ATOM 2425 CG1 VAL A 293 6.983 36.525 28.564 1.00 27.32 C ANISOU 2425 CG1 VAL A 293 3430 4432 2520 -46 278 -13 C ATOM 2426 CG2 VAL A 293 6.503 38.769 27.549 1.00 28.25 C ANISOU 2426 CG2 VAL A 293 3574 4475 2684 74 285 -220 C ATOM 2427 N PRO A 294 8.225 34.569 25.810 1.00 21.89 N ANISOU 2427 N PRO A 294 2727 3456 2134 -92 202 126 N ATOM 2428 CA PRO A 294 8.146 33.125 25.525 1.00 21.86 C ANISOU 2428 CA PRO A 294 2737 3381 2188 -145 248 225 C ATOM 2429 C PRO A 294 7.514 32.345 26.665 1.00 27.40 C ANISOU 2429 C PRO A 294 3444 4154 2812 -193 322 306 C ATOM 2430 O PRO A 294 7.613 32.750 27.818 1.00 26.17 O ANISOU 2430 O PRO A 294 3292 4106 2544 -171 317 320 O ATOM 2431 CB PRO A 294 9.608 32.720 25.362 1.00 23.31 C ANISOU 2431 CB PRO A 294 2966 3485 2405 -105 201 305 C ATOM 2432 CG PRO A 294 10.373 33.694 26.215 1.00 27.00 C ANISOU 2432 CG PRO A 294 3430 4055 2776 -66 133 286 C ATOM 2433 CD PRO A 294 9.600 34.992 26.139 1.00 22.99 C ANISOU 2433 CD PRO A 294 2903 3594 2240 -62 129 143 C ATOM 2434 N HIS A 295 6.875 31.228 26.321 1.00 28.49 N ANISOU 2434 N HIS A 295 3592 4230 3002 -274 395 355 N ATOM 2435 CA HIS A 295 6.276 30.307 27.280 1.00 30.86 C ANISOU 2435 CA HIS A 295 3913 4570 3243 -342 483 451 C ATOM 2436 C HIS A 295 7.432 29.417 27.756 1.00 38.74 C ANISOU 2436 C HIS A 295 5003 5479 4238 -298 489 600 C ATOM 2437 O HIS A 295 7.893 28.550 27.008 1.00 39.84 O ANISOU 2437 O HIS A 295 5209 5458 4471 -305 517 651 O ATOM 2438 CB HIS A 295 5.140 29.506 26.612 0.50 31.83 C ANISOU 2438 CB HIS A 295 4016 4654 3425 -475 563 432 C ATOM 2439 CG HIS A 295 4.452 28.537 27.522 0.50 36.80 C ANISOU 2439 CG HIS A 295 4670 5311 3999 -573 669 529 C ATOM 2440 CD2 HIS A 295 4.430 27.185 27.482 0.50 39.69 C ANISOU 2440 CD2 HIS A 295 5133 5539 4407 -670 759 625 C ATOM 2441 ND1 HIS A 295 3.666 28.967 28.577 0.50 39.50 N ANISOU 2441 ND1 HIS A 295 4944 5832 4232 -579 703 529 N ATOM 2442 CE1 HIS A 295 3.214 27.867 29.156 0.50 40.42 C ANISOU 2442 CE1 HIS A 295 5107 5927 4325 -684 806 635 C ATOM 2443 NE2 HIS A 295 3.645 26.771 28.530 0.50 40.91 N ANISOU 2443 NE2 HIS A 295 5277 5789 4479 -745 845 696 N ATOM 2444 N LEU A 296 7.952 29.709 28.967 0.50 35.13 N ANISOU 2444 N LEU A 296 4547 5137 3662 -239 461 667 N ATOM 2445 CA LEU A 296 9.074 29.011 29.598 1.00 63.40 C ANISOU 2445 CA LEU A 296 8185 8700 7206 -169 453 833 C ATOM 2446 C LEU A 296 8.700 28.528 31.000 0.50 89.27 C ANISOU 2446 C LEU A 296 11481 12088 10350 -187 514 952 C ATOM 2447 O LEU A 296 9.488 27.849 31.657 0.50 46.15 O ANISOU 2447 O LEU A 296 6063 6635 4837 -123 521 1120 O ATOM 2448 CB LEU A 296 10.314 29.929 29.664 1.00 62.84 C ANISOU 2448 CB LEU A 296 8076 8708 7093 -82 331 808 C ATOM 2449 CG LEU A 296 11.153 30.059 28.385 1.00 66.59 C ANISOU 2449 CG LEU A 296 8547 9060 7693 -37 280 770 C ATOM 2450 CD1 LEU A 296 12.105 31.227 28.479 1.00 66.19 C ANISOU 2450 CD1 LEU A 296 8442 9118 7588 2 164 707 C ATOM 2451 CD2 LEU A 296 11.951 28.798 28.111 1.00 70.27 C ANISOU 2451 CD2 LEU A 296 9073 9396 8228 30 330 934 C TER CONECT 1 2 3 4 CONECT 2 1 CONECT 3 1 CONECT 4 1 END If you find results from this site helpful for your research, please cite one of our papers:
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