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*** 1014_Man ***elNémo ID: 2604140238591921336Job options:ID = 2604140238591921336 JOBID = 1014_Man 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 1014_Man CRYST1 69.332 69.332 163.726 90.00 90.00 120.00 P 31 2 1 1 ATOM 1 N ASP A 21 21.452 -25.453 -46.492 1.00 45.57 N ANISOU 1 N ASP A 21 6682 5927 4704 -798 -357 238 N ATOM 2 CA ASP A 21 20.088 -24.953 -46.632 1.00 43.95 C ANISOU 2 CA ASP A 21 6455 5730 4515 -832 -436 284 C ATOM 3 C ASP A 21 19.347 -24.935 -45.293 1.00 44.73 C ANISOU 3 C ASP A 21 6472 5827 4697 -818 -464 294 C ATOM 4 O ASP A 21 18.336 -24.248 -45.147 1.00 45.69 O ANISOU 4 O ASP A 21 6548 5961 4852 -830 -517 339 O ATOM 5 CB ASP A 21 19.300 -25.787 -47.660 1.00 54.47 C ANISOU 5 CB ASP A 21 7867 7057 5771 -883 -492 284 C ATOM 6 CG ASP A 21 19.352 -27.303 -47.389 1.00 58.32 C ANISOU 6 CG ASP A 21 8404 7520 6235 -887 -488 233 C ATOM 7 OD1 ASP A 21 18.818 -27.769 -46.353 1.00 58.20 O ANISOU 7 OD1 ASP A 21 8342 7498 6273 -883 -509 228 O ATOM 8 OD2 ASP A 21 19.903 -28.038 -48.243 1.00 62.66 O1- ANISOU 8 OD2 ASP A 21 9045 8057 6708 -896 -463 201 O1- ATOM 9 N ASN A 22 19.855 -25.695 -44.316 1.00 38.03 N ANISOU 9 N ASN A 22 5605 4965 3881 -790 -427 253 N ATOM 10 CA ASN A 22 19.211 -25.846 -43.015 1.00 33.48 C ANISOU 10 CA ASN A 22 4958 4386 3377 -777 -449 256 C ATOM 11 C ASN A 22 20.302 -26.017 -41.950 1.00 33.24 C ANISOU 11 C ASN A 22 4892 4346 3391 -729 -382 220 C ATOM 12 O ASN A 22 20.576 -27.098 -41.431 1.00 27.89 O ANISOU 12 O ASN A 22 4230 3653 2714 -718 -365 181 O ATOM 13 CB ASN A 22 18.212 -27.008 -43.016 1.00 35.08 C ANISOU 13 CB ASN A 22 5189 4581 3560 -814 -504 249 C ATOM 14 CG ASN A 22 17.537 -27.201 -41.666 1.00 29.73 C ANISOU 14 CG ASN A 22 4438 3904 2955 -802 -524 254 C ATOM 15 ND2 ASN A 22 17.308 -28.453 -41.286 1.00 27.54 N ANISOU 15 ND2 ASN A 22 4186 3609 2667 -817 -536 225 N ATOM 16 OD1 ASN A 22 17.170 -26.237 -41.009 1.00 25.24 O ANISOU 16 OD1 ASN A 22 3795 3349 2445 -782 -531 286 O ATOM 17 N THR A 23 20.967 -24.917 -41.619 1.00 29.64 N ANISOU 17 N THR A 23 4391 3900 2973 -701 -345 234 N ATOM 18 CA THR A 23 22.050 -24.916 -40.651 1.00 28.40 C ANISOU 18 CA THR A 23 4195 3739 2857 -660 -285 205 C ATOM 19 C THR A 23 21.732 -23.898 -39.568 1.00 30.72 C ANISOU 19 C THR A 23 4409 4036 3227 -641 -293 231 C ATOM 20 O THR A 23 20.854 -23.041 -39.725 1.00 27.22 O ANISOU 20 O THR A 23 3945 3598 2800 -654 -335 273 O ATOM 21 CB THR A 23 23.376 -24.569 -41.321 1.00 30.17 C ANISOU 21 CB THR A 23 4447 3973 3045 -648 -224 195 C ATOM 22 CG2 THR A 23 23.690 -25.592 -42.402 1.00 30.54 C ANISOU 22 CG2 THR A 23 4578 4015 3010 -661 -212 167 C ATOM 23 OG1 THR A 23 23.250 -23.277 -41.921 1.00 29.91 O ANISOU 23 OG1 THR A 23 4405 3950 3008 -663 -236 237 O ATOM 24 N ILE A 24 22.471 -23.972 -38.459 1.00 27.98 N ANISOU 24 N ILE A 24 4020 3684 2926 -608 -252 208 N ATOM 25 CA ILE A 24 22.098 -23.128 -37.336 1.00 25.84 C ANISOU 25 CA ILE A 24 3682 3412 2725 -590 -262 228 C ATOM 26 C ILE A 24 22.331 -21.652 -37.635 1.00 25.47 C ANISOU 26 C ILE A 24 3620 3369 2689 -590 -255 262 C ATOM 27 O ILE A 24 21.676 -20.805 -37.028 1.00 26.52 O ANISOU 27 O ILE A 24 3712 3497 2868 -580 -278 290 O ATOM 28 CB ILE A 24 22.833 -23.542 -36.048 1.00 23.85 C ANISOU 28 CB ILE A 24 3391 3154 2516 -558 -222 195 C ATOM 29 CG1 ILE A 24 24.346 -23.364 -36.176 1.00 21.67 C ANISOU 29 CG1 ILE A 24 3121 2886 2228 -542 -161 176 C ATOM 30 CG2 ILE A 24 22.456 -24.972 -35.640 1.00 24.58 C ANISOU 30 CG2 ILE A 24 3498 3237 2604 -558 -235 165 C ATOM 31 CD1 ILE A 24 25.079 -23.480 -34.813 1.00 25.03 C ANISOU 31 CD1 ILE A 24 3496 3310 2705 -511 -127 153 C ATOM 32 N ASP A 25 23.216 -21.312 -38.575 1.00 27.96 N ANISOU 32 N ASP A 25 3970 3692 2961 -600 -224 264 N ATOM 33 CA ASP A 25 23.531 -19.918 -38.860 1.00 26.32 C ANISOU 33 CA ASP A 25 3754 3486 2761 -604 -215 297 C ATOM 34 C ASP A 25 22.852 -19.389 -40.122 1.00 29.47 C ANISOU 34 C ASP A 25 4193 3887 3115 -633 -253 335 C ATOM 35 O ASP A 25 23.146 -18.260 -40.550 1.00 27.39 O ANISOU 35 O ASP A 25 3935 3623 2848 -640 -246 364 O ATOM 36 CB ASP A 25 25.053 -19.735 -38.945 1.00 28.19 C ANISOU 36 CB ASP A 25 3993 3733 2985 -599 -152 280 C ATOM 37 CG ASP A 25 25.745 -19.987 -37.602 1.00 30.43 C ANISOU 37 CG ASP A 25 4227 4015 3320 -571 -119 251 C ATOM 38 OD1 ASP A 25 25.295 -19.434 -36.573 1.00 27.21 O ANISOU 38 OD1 ASP A 25 3778 3594 2968 -558 -136 261 O ATOM 39 OD2 ASP A 25 26.728 -20.756 -37.560 1.00 31.20 O1- ANISOU 39 OD2 ASP A 25 4329 4125 3400 -559 -75 220 O1- ATOM 40 N GLY A 26 21.944 -20.163 -40.716 1.00 28.37 N ANISOU 40 N GLY A 26 4085 3753 2943 -651 -296 336 N ATOM 41 CA GLY A 26 21.186 -19.722 -41.869 1.00 26.04 C ANISOU 41 CA GLY A 26 3826 3463 2606 -680 -340 374 C ATOM 42 C GLY A 26 20.101 -18.731 -41.495 1.00 25.54 C ANISOU 42 C GLY A 26 3722 3396 2588 -672 -387 421 C ATOM 43 O GLY A 26 20.091 -18.151 -40.406 1.00 24.01 O ANISOU 43 O GLY A 26 3477 3192 2455 -643 -377 424 O ATOM 44 N GLU A 27 19.181 -18.521 -42.422 1.00 23.55 N ANISOU 44 N GLU A 27 3494 3152 2302 -696 -439 457 N ATOM 45 CA GLU A 27 18.081 -17.601 -42.164 1.00 25.59 C ANISOU 45 CA GLU A 27 3714 3411 2600 -683 -486 506 C ATOM 46 C GLU A 27 17.076 -18.268 -41.235 1.00 24.96 C ANISOU 46 C GLU A 27 3585 3338 2562 -671 -518 503 C ATOM 47 O GLU A 27 16.594 -19.362 -41.544 1.00 24.13 O ANISOU 47 O GLU A 27 3498 3245 2427 -698 -546 490 O ATOM 48 CB GLU A 27 17.394 -17.185 -43.458 1.00 24.88 C ANISOU 48 CB GLU A 27 3661 3331 2459 -711 -534 551 C ATOM 49 CG GLU A 27 16.175 -16.287 -43.245 1.00 24.41 C ANISOU 49 CG GLU A 27 3560 3277 2439 -693 -586 607 C ATOM 50 CD GLU A 27 15.408 -15.986 -44.535 1.00 29.19 C ANISOU 50 CD GLU A 27 4200 3898 2993 -722 -642 655 C ATOM 51 OE1 GLU A 27 15.946 -16.246 -45.637 1.00 26.03 O ANISOU 51 OE1 GLU A 27 3863 3500 2525 -757 -635 646 O ATOM 52 OE2 GLU A 27 14.261 -15.488 -44.454 1.00 31.50 O1- ANISOU 52 OE2 GLU A 27 4457 4202 3311 -709 -693 702 O1- ATOM 53 N PRO A 28 16.746 -17.661 -40.098 1.00 25.74 N ANISOU 53 N PRO A 28 3625 3429 2727 -634 -515 515 N ATOM 54 CA PRO A 28 15.688 -18.220 -39.239 1.00 26.07 C ANISOU 54 CA PRO A 28 3616 3483 2808 -623 -547 519 C ATOM 55 C PRO A 28 14.335 -18.146 -39.936 1.00 23.73 C ANISOU 55 C PRO A 28 3311 3210 2494 -642 -615 569 C ATOM 56 O PRO A 28 13.889 -17.069 -40.334 1.00 22.56 O ANISOU 56 O PRO A 28 3157 3063 2350 -628 -637 616 O ATOM 57 CB PRO A 28 15.741 -17.328 -37.991 1.00 25.19 C ANISOU 57 CB PRO A 28 3452 3355 2763 -575 -522 524 C ATOM 58 CG PRO A 28 17.120 -16.693 -38.020 1.00 26.39 C ANISOU 58 CG PRO A 28 3632 3484 2911 -569 -468 503 C ATOM 59 CD PRO A 28 17.434 -16.513 -39.476 1.00 25.31 C ANISOU 59 CD PRO A 28 3553 3353 2712 -602 -476 518 C ATOM 60 N SER A 29 13.685 -19.299 -40.097 1.00 24.60 N ANISOU 60 N SER A 29 3425 3340 2583 -674 -651 562 N ATOM 61 CA SER A 29 12.328 -19.327 -40.622 1.00 24.83 C ANISOU 61 CA SER A 29 3435 3400 2600 -696 -721 612 C ATOM 62 C SER A 29 11.669 -20.645 -40.254 1.00 25.64 C ANISOU 62 C SER A 29 3522 3519 2701 -726 -750 597 C ATOM 63 O SER A 29 12.341 -21.646 -39.991 1.00 27.55 O ANISOU 63 O SER A 29 3794 3746 2929 -740 -721 546 O ATOM 64 CB SER A 29 12.296 -19.150 -42.143 1.00 30.75 C ANISOU 64 CB SER A 29 4246 4157 3281 -735 -753 636 C ATOM 65 OG SER A 29 13.062 -20.165 -42.753 1.00 38.53 O ANISOU 65 OG SER A 29 5300 5132 4209 -773 -735 589 O ATOM 66 N GLY A 30 10.344 -20.636 -40.274 1.00 25.27 N ANISOU 66 N GLY A 30 3429 3507 2666 -737 -810 646 N ATOM 67 CA GLY A 30 9.557 -21.821 -40.017 1.00 28.35 C ANISOU 67 CA GLY A 30 3801 3918 3051 -776 -849 643 C ATOM 68 C GLY A 30 8.950 -21.825 -38.624 1.00 28.43 C ANISOU 68 C GLY A 30 3727 3942 3131 -741 -841 652 C ATOM 69 O GLY A 30 9.287 -21.023 -37.747 1.00 25.64 O ANISOU 69 O GLY A 30 3338 3576 2829 -683 -798 649 O ATOM 70 N GLU A 31 8.028 -22.760 -38.431 1.00 26.42 N ANISOU 70 N GLU A 31 3446 3716 2875 -779 -886 665 N ATOM 71 CA GLU A 31 7.423 -22.984 -37.132 1.00 27.45 C ANISOU 71 CA GLU A 31 3501 3865 3064 -755 -879 673 C ATOM 72 C GLU A 31 8.286 -23.968 -36.360 1.00 30.36 C ANISOU 72 C GLU A 31 3898 4200 3437 -759 -833 608 C ATOM 73 O GLU A 31 8.606 -25.048 -36.867 1.00 29.66 O ANISOU 73 O GLU A 31 3872 4098 3301 -810 -844 575 O ATOM 74 CB GLU A 31 5.997 -23.518 -37.276 1.00 30.69 C ANISOU 74 CB GLU A 31 3864 4327 3471 -799 -950 723 C ATOM 75 CG GLU A 31 5.307 -23.654 -35.952 1.00 31.16 C ANISOU 75 CG GLU A 31 3837 4411 3589 -772 -942 738 C ATOM 76 CD GLU A 31 3.854 -24.055 -36.072 1.00 37.78 C ANISOU 76 CD GLU A 31 4616 5311 4430 -813 -1011 798 C ATOM 77 OE1 GLU A 31 3.305 -24.123 -37.204 1.00 31.78 O ANISOU 77 OE1 GLU A 31 3875 4576 3625 -862 -1072 834 O ATOM 78 OE2 GLU A 31 3.244 -24.267 -35.005 1.00 42.30 O1- ANISOU 78 OE2 GLU A 31 5116 5909 5047 -797 -1005 813 O1- ATOM 79 N ILE A 32 8.700 -23.582 -35.155 1.00 30.35 N ANISOU 79 N ILE A 32 3857 4185 3490 -704 -782 589 N ATOM 80 CA ILE A 32 9.521 -24.443 -34.310 1.00 27.96 C ANISOU 80 CA ILE A 32 3573 3853 3197 -701 -737 532 C ATOM 81 C ILE A 32 8.735 -24.795 -33.057 1.00 27.48 C ANISOU 81 C ILE A 32 3441 3814 3185 -688 -741 545 C ATOM 82 O ILE A 32 8.025 -23.951 -32.500 1.00 23.94 O ANISOU 82 O ILE A 32 2925 3391 2781 -649 -744 585 O ATOM 83 CB ILE A 32 10.883 -23.808 -33.956 1.00 24.12 C ANISOU 83 CB ILE A 32 3111 3328 2726 -654 -670 491 C ATOM 84 CG1 ILE A 32 10.703 -22.489 -33.209 1.00 25.09 C ANISOU 84 CG1 ILE A 32 3176 3454 2903 -593 -648 518 C ATOM 85 CG2 ILE A 32 11.763 -23.673 -35.196 1.00 26.19 C ANISOU 85 CG2 ILE A 32 3448 3570 2932 -673 -661 474 C ATOM 86 CD1 ILE A 32 12.034 -21.868 -32.692 1.00 23.65 C ANISOU 86 CD1 ILE A 32 3013 3234 2739 -552 -584 479 C ATOM 87 N LYS A 33 8.839 -26.060 -32.642 1.00 24.46 N ANISOU 87 N LYS A 33 3079 3423 2793 -722 -741 512 N ATOM 88 CA LYS A 33 8.242 -26.542 -31.401 1.00 25.58 C ANISOU 88 CA LYS A 33 3161 3581 2977 -715 -738 518 C ATOM 89 C LYS A 33 9.292 -26.525 -30.299 1.00 22.40 C ANISOU 89 C LYS A 33 2761 3144 2606 -667 -672 469 C ATOM 90 O LYS A 33 10.343 -27.162 -30.430 1.00 21.67 O ANISOU 90 O LYS A 33 2731 3015 2489 -676 -645 419 O ATOM 91 CB LYS A 33 7.689 -27.962 -31.548 1.00 26.80 C ANISOU 91 CB LYS A 33 3337 3744 3100 -784 -780 515 C ATOM 92 CG LYS A 33 6.856 -28.374 -30.339 1.00 28.83 C ANISOU 92 CG LYS A 33 3523 4029 3401 -783 -785 535 C ATOM 93 CD LYS A 33 6.742 -29.890 -30.224 1.00 35.71 C ANISOU 93 CD LYS A 33 4435 4890 4245 -846 -808 512 C ATOM 94 CE LYS A 33 5.534 -30.315 -29.399 1.00 40.54 C ANISOU 94 CE LYS A 33 4970 5545 4886 -870 -836 554 C ATOM 95 NZ LYS A 33 4.881 -31.560 -29.928 1.00 44.12 N1+ ANISOU 95 NZ LYS A 33 5459 6007 5296 -960 -897 565 N1+ ATOM 96 N VAL A 34 9.000 -25.822 -29.213 1.00 23.28 N ANISOU 96 N VAL A 34 2807 3267 2770 -617 -648 485 N ATOM 97 CA VAL A 34 9.891 -25.741 -28.064 1.00 26.72 C ANISOU 97 CA VAL A 34 3240 3674 3239 -573 -590 444 C ATOM 98 C VAL A 34 9.295 -26.628 -26.970 1.00 24.60 C ANISOU 98 C VAL A 34 2932 3421 2994 -583 -594 444 C ATOM 99 O VAL A 34 8.198 -26.363 -26.463 1.00 22.51 O ANISOU 99 O VAL A 34 2600 3195 2758 -573 -611 487 O ATOM 100 CB VAL A 34 10.082 -24.285 -27.607 1.00 25.62 C ANISOU 100 CB VAL A 34 3068 3530 3137 -509 -558 457 C ATOM 101 CG1 VAL A 34 10.972 -24.201 -26.374 1.00 23.16 C ANISOU 101 CG1 VAL A 34 2753 3190 2856 -469 -504 417 C ATOM 102 CG2 VAL A 34 10.678 -23.461 -28.744 1.00 25.23 C ANISOU 102 CG2 VAL A 34 3063 3464 3061 -507 -558 460 C ATOM 103 N VAL A 35 10.005 -27.698 -26.618 1.00 23.95 N ANISOU 103 N VAL A 35 2891 3311 2899 -602 -576 399 N ATOM 104 CA VAL A 35 9.542 -28.667 -25.621 1.00 24.03 C ANISOU 104 CA VAL A 35 2876 3330 2925 -619 -579 396 C ATOM 105 C VAL A 35 10.206 -28.343 -24.292 1.00 22.85 C ANISOU 105 C VAL A 35 2704 3163 2816 -564 -525 369 C ATOM 106 O VAL A 35 11.432 -28.378 -24.190 1.00 24.41 O ANISOU 106 O VAL A 35 2944 3324 3007 -545 -488 325 O ATOM 107 CB VAL A 35 9.855 -30.107 -26.062 1.00 23.39 C ANISOU 107 CB VAL A 35 2862 3224 2800 -675 -597 365 C ATOM 108 CG1 VAL A 35 9.053 -31.104 -25.247 1.00 27.39 C ANISOU 108 CG1 VAL A 35 3342 3748 3319 -708 -617 378 C ATOM 109 CG2 VAL A 35 9.539 -30.291 -27.563 1.00 21.01 C ANISOU 109 CG2 VAL A 35 2606 2929 2449 -726 -645 381 C ATOM 110 N THR A 36 9.410 -28.047 -23.262 1.00 24.20 N ANISOU 110 N THR A 36 2808 3362 3025 -540 -520 396 N ATOM 111 CA THR A 36 9.938 -27.547 -22.000 1.00 21.63 C ANISOU 111 CA THR A 36 2460 3021 2736 -485 -470 376 C ATOM 112 C THR A 36 9.450 -28.384 -20.824 1.00 23.81 C ANISOU 112 C THR A 36 2705 3311 3032 -493 -466 377 C ATOM 113 O THR A 36 8.427 -29.071 -20.886 1.00 26.08 O ANISOU 113 O THR A 36 2965 3630 3313 -534 -502 408 O ATOM 114 CB THR A 36 9.546 -26.071 -21.769 1.00 24.85 C ANISOU 114 CB THR A 36 2822 3444 3175 -430 -456 406 C ATOM 115 CG2 THR A 36 8.045 -25.931 -21.628 1.00 23.60 C ANISOU 115 CG2 THR A 36 2596 3339 3034 -432 -486 463 C ATOM 116 OG1 THR A 36 10.183 -25.569 -20.585 1.00 24.88 O ANISOU 116 OG1 THR A 36 2818 3427 3208 -380 -408 380 O ATOM 117 N TRP A 37 10.213 -28.323 -19.742 1.00 22.64 N ANISOU 117 N TRP A 37 2560 3140 2904 -456 -422 344 N ATOM 118 CA TRP A 37 9.810 -28.920 -18.484 1.00 25.05 C ANISOU 118 CA TRP A 37 2832 3456 3229 -454 -411 345 C ATOM 119 C TRP A 37 8.978 -27.961 -17.648 1.00 25.69 C ANISOU 119 C TRP A 37 2846 3570 3346 -407 -395 380 C ATOM 120 O TRP A 37 8.313 -28.399 -16.712 1.00 25.07 O ANISOU 120 O TRP A 37 2728 3515 3283 -408 -390 396 O ATOM 121 CB TRP A 37 11.050 -29.374 -17.709 1.00 22.45 C ANISOU 121 CB TRP A 37 2542 3087 2902 -437 -374 294 C ATOM 122 CG TRP A 37 11.954 -28.228 -17.386 1.00 24.21 C ANISOU 122 CG TRP A 37 2770 3288 3142 -384 -335 273 C ATOM 123 CD1 TRP A 37 12.048 -27.569 -16.192 1.00 22.93 C ANISOU 123 CD1 TRP A 37 2580 3124 3008 -338 -302 269 C ATOM 124 CD2 TRP A 37 12.872 -27.572 -18.283 1.00 23.13 C ANISOU 124 CD2 TRP A 37 2671 3128 2990 -375 -327 255 C ATOM 125 CE2 TRP A 37 13.490 -26.525 -17.558 1.00 25.29 C ANISOU 125 CE2 TRP A 37 2936 3386 3287 -327 -292 242 C ATOM 126 CE3 TRP A 37 13.221 -27.762 -19.630 1.00 21.85 C ANISOU 126 CE3 TRP A 37 2550 2957 2795 -405 -347 249 C ATOM 127 NE1 TRP A 37 12.983 -26.554 -16.282 1.00 24.77 N ANISOU 127 NE1 TRP A 37 2833 3332 3246 -305 -277 249 N ATOM 128 CZ2 TRP A 37 14.452 -25.679 -18.129 1.00 20.73 C ANISOU 128 CZ2 TRP A 37 2388 2786 2702 -312 -276 226 C ATOM 129 CZ3 TRP A 37 14.168 -26.913 -20.197 1.00 24.70 C ANISOU 129 CZ3 TRP A 37 2938 3298 3149 -385 -328 234 C ATOM 130 CH2 TRP A 37 14.769 -25.885 -19.444 1.00 21.68 C ANISOU 130 CH2 TRP A 37 2543 2902 2792 -342 -294 223 C ATOM 131 N ARG A 38 8.964 -26.673 -18.003 1.00 24.77 N ANISOU 131 N ARG A 38 2717 3454 3240 -366 -386 395 N ATOM 132 CA ARG A 38 8.290 -25.636 -17.225 1.00 26.17 C ANISOU 132 CA ARG A 38 2841 3654 3450 -310 -364 423 C ATOM 133 C ARG A 38 6.844 -25.510 -17.694 1.00 27.93 C ANISOU 133 C ARG A 38 3004 3931 3676 -320 -400 485 C ATOM 134 O ARG A 38 6.478 -24.589 -18.430 1.00 26.76 O ANISOU 134 O ARG A 38 2844 3794 3529 -298 -413 514 O ATOM 135 CB ARG A 38 9.031 -24.307 -17.365 1.00 26.14 C ANISOU 135 CB ARG A 38 2862 3617 3453 -260 -338 409 C ATOM 136 CG ARG A 38 10.444 -24.315 -16.811 1.00 24.10 C ANISOU 136 CG ARG A 38 2653 3312 3194 -249 -303 354 C ATOM 137 CD ARG A 38 10.449 -24.434 -15.300 1.00 25.38 C ANISOU 137 CD ARG A 38 2795 3472 3377 -220 -270 340 C ATOM 138 NE ARG A 38 9.680 -23.361 -14.673 1.00 25.55 N ANISOU 138 NE ARG A 38 2778 3509 3422 -164 -252 369 N ATOM 139 CZ ARG A 38 10.215 -22.273 -14.134 1.00 25.13 C ANISOU 139 CZ ARG A 38 2743 3426 3380 -116 -220 353 C ATOM 140 NH1 ARG A 38 11.521 -22.040 -14.190 1.00 24.81 N1+ ANISOU 140 NH1 ARG A 38 2753 3342 3331 -121 -206 312 N1+ ATOM 141 NH2 ARG A 38 9.420 -21.389 -13.538 1.00 24.57 N ANISOU 141 NH2 ARG A 38 2640 3367 3327 -63 -202 380 N ATOM 142 N THR A 39 5.999 -26.448 -17.233 1.00 24.23 N ANISOU 142 N THR A 39 2496 3500 3209 -353 -416 508 N ATOM 143 CA THR A 39 4.572 -26.367 -17.542 1.00 29.16 C ANISOU 143 CA THR A 39 3052 4187 3841 -364 -449 572 C ATOM 144 C THR A 39 3.958 -25.097 -16.961 1.00 31.02 C ANISOU 144 C THR A 39 3232 4446 4106 -286 -420 604 C ATOM 145 O THR A 39 3.069 -24.498 -17.572 1.00 30.98 O ANISOU 145 O THR A 39 3184 4482 4107 -272 -443 655 O ATOM 146 CB THR A 39 3.825 -27.586 -17.003 1.00 29.28 C ANISOU 146 CB THR A 39 3032 4239 3854 -415 -467 591 C ATOM 147 CG2 THR A 39 4.230 -28.848 -17.766 1.00 29.54 C ANISOU 147 CG2 THR A 39 3124 4249 3852 -497 -505 568 C ATOM 148 OG1 THR A 39 4.152 -27.749 -15.621 1.00 28.16 O ANISOU 148 OG1 THR A 39 2885 4083 3729 -384 -421 566 O ATOM 149 N ASP A 40 4.423 -24.674 -15.782 1.00 28.72 N ANISOU 149 N ASP A 40 2946 4131 3834 -233 -369 577 N ATOM 150 CA ASP A 40 3.913 -23.454 -15.158 1.00 29.20 C ANISOU 150 CA ASP A 40 2968 4206 3921 -152 -335 601 C ATOM 151 C ASP A 40 4.029 -22.257 -16.096 1.00 29.25 C ANISOU 151 C ASP A 40 2993 4195 3926 -117 -344 614 C ATOM 152 O ASP A 40 3.099 -21.451 -16.211 1.00 29.60 O ANISOU 152 O ASP A 40 2989 4275 3985 -71 -345 663 O ATOM 153 CB ASP A 40 4.660 -23.197 -13.841 1.00 25.71 C ANISOU 153 CB ASP A 40 2552 3726 3491 -108 -281 557 C ATOM 154 CG ASP A 40 6.167 -23.007 -14.029 1.00 26.70 C ANISOU 154 CG ASP A 40 2758 3783 3604 -114 -268 498 C ATOM 155 OD1 ASP A 40 6.797 -23.777 -14.780 1.00 28.58 O ANISOU 155 OD1 ASP A 40 3034 4003 3821 -170 -294 475 O ATOM 156 OD2 ASP A 40 6.750 -22.115 -13.375 1.00 28.74 O1- ANISOU 156 OD2 ASP A 40 3042 4005 3872 -62 -231 473 O1- ATOM 157 N LEU A 41 5.154 -22.145 -16.800 1.00 27.17 N ANISOU 157 N LEU A 41 2799 3880 3645 -138 -349 574 N ATOM 158 CA LEU A 41 5.406 -21.022 -17.689 1.00 26.44 C ANISOU 158 CA LEU A 41 2734 3764 3548 -111 -355 582 C ATOM 159 C LEU A 41 4.653 -21.149 -19.009 1.00 27.86 C ANISOU 159 C LEU A 41 2892 3982 3712 -147 -409 628 C ATOM 160 O LEU A 41 4.442 -20.135 -19.686 1.00 27.24 O ANISOU 160 O LEU A 41 2816 3901 3635 -114 -418 655 O ATOM 161 CB LEU A 41 6.912 -20.913 -17.938 1.00 27.30 C ANISOU 161 CB LEU A 41 2921 3810 3641 -125 -340 525 C ATOM 162 CG LEU A 41 7.785 -20.555 -16.731 1.00 27.15 C ANISOU 162 CG LEU A 41 2930 3749 3636 -88 -291 481 C ATOM 163 CD1 LEU A 41 9.209 -20.323 -17.171 1.00 23.89 C ANISOU 163 CD1 LEU A 41 2586 3283 3207 -105 -282 435 C ATOM 164 CD2 LEU A 41 7.252 -19.319 -16.022 1.00 25.55 C ANISOU 164 CD2 LEU A 41 2707 3544 3455 -11 -261 502 C ATOM 165 N VAL A 42 4.262 -22.370 -19.397 1.00 28.96 N ANISOU 165 N VAL A 42 3016 4153 3835 -216 -446 638 N ATOM 166 CA VAL A 42 3.335 -22.540 -20.518 1.00 30.57 C ANISOU 166 CA VAL A 42 3188 4403 4023 -254 -502 690 C ATOM 167 C VAL A 42 1.936 -22.082 -20.122 1.00 31.86 C ANISOU 167 C VAL A 42 3261 4631 4212 -213 -507 756 C ATOM 168 O VAL A 42 1.281 -21.343 -20.862 1.00 34.59 O ANISOU 168 O VAL A 42 3580 5004 4560 -191 -532 803 O ATOM 169 CB VAL A 42 3.336 -23.999 -21.017 1.00 30.35 C ANISOU 169 CB VAL A 42 3179 4386 3967 -345 -542 680 C ATOM 170 CG1 VAL A 42 2.295 -24.202 -22.109 1.00 31.89 C ANISOU 170 CG1 VAL A 42 3340 4634 4144 -391 -605 737 C ATOM 171 CG2 VAL A 42 4.692 -24.372 -21.575 1.00 28.55 C ANISOU 171 CG2 VAL A 42 3041 4097 3710 -377 -537 620 C ATOM 172 N GLU A 43 1.473 -22.483 -18.930 1.00 40.51 N ANISOU 172 N GLU A 43 4310 5754 5329 -197 -480 761 N ATOM 173 CA GLU A 43 0.099 -22.189 -18.523 1.00 40.14 C ANISOU 173 CA GLU A 43 4168 5778 5304 -161 -482 827 C ATOM 174 C GLU A 43 -0.095 -20.729 -18.130 1.00 35.39 C ANISOU 174 C GLU A 43 3551 5169 4728 -59 -443 844 C ATOM 175 O GLU A 43 -1.173 -20.174 -18.353 1.00 40.30 O ANISOU 175 O GLU A 43 4106 5845 5362 -20 -456 907 O ATOM 176 CB GLU A 43 -0.337 -23.111 -17.379 1.00 42.18 C ANISOU 176 CB GLU A 43 4382 6070 5574 -180 -464 829 C ATOM 177 CG GLU A 43 0.208 -24.532 -17.465 1.00 46.51 C ANISOU 177 CG GLU A 43 4974 6599 6099 -271 -487 792 C ATOM 178 CD GLU A 43 0.015 -25.349 -16.183 1.00 56.76 C ANISOU 178 CD GLU A 43 6244 7914 7407 -282 -459 783 C ATOM 179 OE1 GLU A 43 -0.246 -24.744 -15.113 1.00 61.63 O ANISOU 179 OE1 GLU A 43 6825 8544 8049 -212 -411 791 O ATOM 180 OE2 GLU A 43 0.153 -26.595 -16.242 1.00 54.97 O1- ANISOU 180 OE2 GLU A 43 6039 7685 7162 -359 -485 768 O1- ATOM 181 N ASP A 44 0.920 -20.073 -17.568 1.00 31.99 N ANISOU 181 N ASP A 44 3182 4671 4302 -12 -396 792 N ATOM 182 CA ASP A 44 0.686 -18.701 -17.119 1.00 33.17 C ANISOU 182 CA ASP A 44 3323 4808 4471 86 -357 808 C ATOM 183 C ASP A 44 0.948 -17.644 -18.214 1.00 33.76 C ANISOU 183 C ASP A 44 3439 4851 4538 110 -376 819 C ATOM 184 O ASP A 44 0.928 -16.440 -17.923 1.00 29.52 O ANISOU 184 O ASP A 44 2916 4287 4014 190 -345 826 O ATOM 185 CB ASP A 44 1.486 -18.417 -15.832 1.00 26.02 C ANISOU 185 CB ASP A 44 2460 3850 3575 129 -297 754 C ATOM 186 CG ASP A 44 2.971 -18.101 -16.075 1.00 32.35 C ANISOU 186 CG ASP A 44 3359 4572 4363 114 -287 691 C ATOM 187 OD1 ASP A 44 3.455 -18.133 -17.231 1.00 29.25 O ANISOU 187 OD1 ASP A 44 3003 4160 3952 71 -321 685 O ATOM 188 OD2 ASP A 44 3.674 -17.826 -15.067 1.00 32.19 O1- ANISOU 188 OD2 ASP A 44 3375 4507 4348 145 -243 647 O1- ATOM 189 N GLY A 45 1.155 -18.057 -19.464 1.00 31.63 N ANISOU 189 N GLY A 45 3191 4582 4244 44 -426 823 N ATOM 190 CA GLY A 45 1.301 -17.132 -20.566 1.00 30.17 C ANISOU 190 CA GLY A 45 3040 4375 4048 60 -448 841 C ATOM 191 C GLY A 45 2.706 -16.622 -20.814 1.00 32.14 C ANISOU 191 C GLY A 45 3385 4544 4285 57 -428 784 C ATOM 192 O GLY A 45 2.928 -15.938 -21.826 1.00 33.45 O ANISOU 192 O GLY A 45 3586 4688 4436 59 -450 796 O ATOM 193 N THR A 46 3.658 -16.936 -19.931 1.00 28.95 N ANISOU 193 N THR A 46 3021 4098 3883 51 -390 724 N ATOM 194 CA THR A 46 5.020 -16.418 -20.060 1.00 27.15 C ANISOU 194 CA THR A 46 2875 3797 3643 48 -368 673 C ATOM 195 C THR A 46 5.649 -16.820 -21.383 1.00 28.14 C ANISOU 195 C THR A 46 3045 3911 3737 -19 -405 661 C ATOM 196 O THR A 46 6.293 -16.001 -22.046 1.00 29.99 O ANISOU 196 O THR A 46 3331 4105 3960 -12 -405 654 O ATOM 197 CB THR A 46 5.891 -16.932 -18.915 1.00 27.18 C ANISOU 197 CB THR A 46 2904 3770 3652 41 -329 615 C ATOM 198 CG2 THR A 46 7.366 -16.595 -19.169 1.00 28.91 C ANISOU 198 CG2 THR A 46 3203 3925 3856 22 -314 563 C ATOM 199 OG1 THR A 46 5.474 -16.335 -17.682 1.00 26.43 O ANISOU 199 OG1 THR A 46 2787 3674 3582 111 -288 620 O ATOM 200 N PHE A 47 5.476 -18.076 -21.789 1.00 26.38 N ANISOU 200 N PHE A 47 2805 3720 3497 -87 -437 660 N ATOM 201 CA PHE A 47 6.222 -18.544 -22.945 1.00 28.37 C ANISOU 201 CA PHE A 47 3110 3954 3715 -150 -464 639 C ATOM 202 C PHE A 47 5.597 -17.995 -24.234 1.00 29.34 C ANISOU 202 C PHE A 47 3228 4098 3821 -155 -508 689 C ATOM 203 O PHE A 47 6.311 -17.605 -25.165 1.00 27.76 O ANISOU 203 O PHE A 47 3084 3867 3597 -172 -515 677 O ATOM 204 CB PHE A 47 6.237 -20.071 -22.960 1.00 29.63 C ANISOU 204 CB PHE A 47 3266 4135 3858 -218 -484 619 C ATOM 205 CG PHE A 47 7.487 -20.663 -22.372 1.00 29.82 C ANISOU 205 CG PHE A 47 3338 4116 3877 -236 -450 555 C ATOM 206 CD1 PHE A 47 8.738 -20.311 -22.838 1.00 34.88 C ANISOU 206 CD1 PHE A 47 4042 4709 4500 -242 -432 517 C ATOM 207 CD2 PHE A 47 7.398 -21.591 -21.351 1.00 27.81 C ANISOU 207 CD2 PHE A 47 3060 3872 3634 -247 -435 536 C ATOM 208 CE1 PHE A 47 9.893 -20.849 -22.269 1.00 38.02 C ANISOU 208 CE1 PHE A 47 4476 5073 4894 -254 -401 462 C ATOM 209 CE2 PHE A 47 8.545 -22.146 -20.783 1.00 29.55 C ANISOU 209 CE2 PHE A 47 3323 4054 3850 -259 -405 480 C ATOM 210 CZ PHE A 47 9.794 -21.766 -21.238 1.00 31.08 C ANISOU 210 CZ PHE A 47 3576 4205 4029 -261 -388 443 C ATOM 211 N GLU A 48 4.262 -17.922 -24.293 1.00 28.01 N ANISOU 211 N GLU A 48 2991 3986 3665 -138 -536 748 N ATOM 212 CA GLU A 48 3.605 -17.348 -25.466 1.00 32.09 C ANISOU 212 CA GLU A 48 3498 4528 4168 -138 -580 802 C ATOM 213 C GLU A 48 3.945 -15.858 -25.589 1.00 30.22 C ANISOU 213 C GLU A 48 3294 4247 3940 -71 -556 809 C ATOM 214 O GLU A 48 4.163 -15.347 -26.695 1.00 28.47 O ANISOU 214 O GLU A 48 3112 4011 3696 -84 -581 823 O ATOM 215 CB GLU A 48 2.093 -17.588 -25.357 1.00 33.67 C ANISOU 215 CB GLU A 48 3606 4803 4383 -130 -612 867 C ATOM 216 CG GLU A 48 1.169 -17.111 -26.505 1.00 43.63 C ANISOU 216 CG GLU A 48 4838 6108 5633 -130 -667 935 C ATOM 217 CD GLU A 48 1.836 -16.935 -27.881 1.00 44.92 C ANISOU 217 CD GLU A 48 5073 6239 5755 -174 -698 925 C ATOM 218 OE1 GLU A 48 2.149 -15.780 -28.255 1.00 41.28 O ANISOU 218 OE1 GLU A 48 4647 5743 5295 -127 -686 934 O ATOM 219 OE2 GLU A 48 2.062 -17.952 -28.580 1.00 45.53 O1- ANISOU 219 OE2 GLU A 48 5177 6324 5798 -255 -732 909 O1- ATOM 220 N LYS A 49 4.049 -15.152 -24.455 1.00 27.93 N ANISOU 220 N LYS A 49 2999 3931 3681 -2 -507 796 N ATOM 221 CA LYS A 49 4.552 -13.780 -24.495 1.00 30.88 C ANISOU 221 CA LYS A 49 3423 4251 4060 54 -482 793 C ATOM 222 C LYS A 49 5.960 -13.724 -25.080 1.00 30.22 C ANISOU 222 C LYS A 49 3423 4111 3950 9 -474 744 C ATOM 223 O LYS A 49 6.263 -12.847 -25.897 1.00 28.03 O ANISOU 223 O LYS A 49 3188 3803 3657 17 -484 758 O ATOM 224 CB LYS A 49 4.523 -13.165 -23.097 1.00 31.34 C ANISOU 224 CB LYS A 49 3473 4285 4150 127 -429 778 C ATOM 225 CG LYS A 49 4.801 -11.662 -23.066 1.00 37.04 C ANISOU 225 CG LYS A 49 4245 4951 4879 194 -406 784 C ATOM 226 CD LYS A 49 3.997 -10.906 -24.144 1.00 46.26 C ANISOU 226 CD LYS A 49 5400 6138 6040 221 -444 848 C ATOM 227 CE LYS A 49 4.418 -9.422 -24.328 1.00 47.46 C ANISOU 227 CE LYS A 49 5618 6223 6191 276 -426 853 C ATOM 228 NZ LYS A 49 5.708 -9.027 -23.675 1.00 46.65 N1+ ANISOU 228 NZ LYS A 49 5591 6047 6086 271 -384 791 N1+ ATOM 229 N TYR A 50 6.832 -14.653 -24.673 1.00 27.62 N ANISOU 229 N TYR A 50 3115 3768 3613 -38 -457 689 N ATOM 230 CA TYR A 50 8.189 -14.689 -25.218 1.00 28.35 C ANISOU 230 CA TYR A 50 3277 3815 3679 -81 -447 645 C ATOM 231 C TYR A 50 8.171 -14.892 -26.731 1.00 27.77 C ANISOU 231 C TYR A 50 3226 3755 3568 -131 -490 666 C ATOM 232 O TYR A 50 8.954 -14.263 -27.455 1.00 28.74 O ANISOU 232 O TYR A 50 3405 3843 3671 -141 -487 657 O ATOM 233 CB TYR A 50 9.004 -15.807 -24.563 1.00 24.43 C ANISOU 233 CB TYR A 50 2790 3311 3180 -120 -425 589 C ATOM 234 CG TYR A 50 9.473 -15.576 -23.137 1.00 25.62 C ANISOU 234 CG TYR A 50 2942 3434 3358 -82 -377 554 C ATOM 235 CD1 TYR A 50 9.312 -14.354 -22.501 1.00 25.14 C ANISOU 235 CD1 TYR A 50 2886 3346 3319 -17 -352 566 C ATOM 236 CD2 TYR A 50 10.063 -16.612 -22.424 1.00 23.84 C ANISOU 236 CD2 TYR A 50 2717 3208 3133 -110 -359 510 C ATOM 237 CE1 TYR A 50 9.746 -14.174 -21.187 1.00 23.72 C ANISOU 237 CE1 TYR A 50 2714 3140 3160 14 -311 533 C ATOM 238 CE2 TYR A 50 10.484 -16.452 -21.122 1.00 24.22 C ANISOU 238 CE2 TYR A 50 2766 3233 3203 -79 -320 480 C ATOM 239 CZ TYR A 50 10.333 -15.240 -20.501 1.00 23.26 C ANISOU 239 CZ TYR A 50 2652 3085 3101 -20 -296 490 C ATOM 240 OH TYR A 50 10.767 -15.111 -19.187 1.00 23.65 O ANISOU 240 OH TYR A 50 2708 3110 3167 7 -259 458 O ATOM 241 N ALA A 51 7.302 -15.780 -27.228 1.00 26.21 N ANISOU 241 N ALA A 51 2990 3610 3359 -167 -532 693 N ATOM 242 CA ALA A 51 7.244 -16.019 -28.674 1.00 28.44 C ANISOU 242 CA ALA A 51 3298 3907 3601 -218 -577 713 C ATOM 243 C ALA A 51 6.873 -14.749 -29.430 1.00 29.41 C ANISOU 243 C ALA A 51 3432 4023 3721 -183 -595 761 C ATOM 244 O ALA A 51 7.456 -14.455 -30.478 1.00 29.13 O ANISOU 244 O ALA A 51 3449 3966 3651 -211 -607 759 O ATOM 245 CB ALA A 51 6.252 -17.137 -29.001 1.00 29.81 C ANISOU 245 CB ALA A 51 3426 4138 3762 -265 -624 740 C ATOM 246 N GLU A 52 5.913 -13.980 -28.907 1.00 27.84 N ANISOU 246 N GLU A 52 3184 3841 3554 -118 -595 805 N ATOM 247 CA GLU A 52 5.527 -12.722 -29.541 1.00 28.89 C ANISOU 247 CA GLU A 52 3327 3963 3686 -73 -609 852 C ATOM 248 C GLU A 52 6.716 -11.778 -29.677 1.00 30.33 C ANISOU 248 C GLU A 52 3588 4076 3860 -61 -576 822 C ATOM 249 O GLU A 52 6.944 -11.213 -30.752 1.00 29.89 O ANISOU 249 O GLU A 52 3574 4005 3777 -76 -597 842 O ATOM 250 CB GLU A 52 4.395 -12.069 -28.748 1.00 28.62 C ANISOU 250 CB GLU A 52 3229 3953 3691 7 -603 898 C ATOM 251 CG GLU A 52 3.153 -12.920 -28.708 1.00 36.50 C ANISOU 251 CG GLU A 52 4142 5028 4696 -8 -640 939 C ATOM 252 CD GLU A 52 1.930 -12.203 -28.159 1.00 43.31 C ANISOU 252 CD GLU A 52 4935 5926 5593 75 -638 998 C ATOM 253 OE1 GLU A 52 2.064 -11.047 -27.684 1.00 44.77 O ANISOU 253 OE1 GLU A 52 5143 6069 5799 151 -602 1001 O ATOM 254 OE2 GLU A 52 0.825 -12.792 -28.241 1.00 44.35 O1- ANISOU 254 OE2 GLU A 52 4990 6130 5731 64 -673 1044 O1- ATOM 255 N GLU A 53 7.489 -11.595 -28.596 1.00 32.57 N ANISOU 255 N GLU A 53 3891 4319 4165 -39 -526 775 N ATOM 256 CA GLU A 53 8.678 -10.741 -28.664 1.00 30.67 C ANISOU 256 CA GLU A 53 3722 4014 3915 -37 -495 746 C ATOM 257 C GLU A 53 9.697 -11.300 -29.649 1.00 27.92 C ANISOU 257 C GLU A 53 3423 3659 3528 -111 -503 717 C ATOM 258 O GLU A 53 10.196 -10.577 -30.522 1.00 28.80 O ANISOU 258 O GLU A 53 3585 3743 3614 -123 -509 728 O ATOM 259 CB GLU A 53 9.308 -10.576 -27.277 1.00 31.66 C ANISOU 259 CB GLU A 53 3857 4103 4068 -8 -445 700 C ATOM 260 CG GLU A 53 8.538 -9.713 -26.264 1.00 36.58 C ANISOU 260 CG GLU A 53 4456 4715 4727 75 -424 722 C ATOM 261 CD GLU A 53 7.985 -8.414 -26.855 1.00 46.67 C ANISOU 261 CD GLU A 53 5755 5971 6004 126 -440 774 C ATOM 262 OE1 GLU A 53 8.801 -7.531 -27.213 1.00 50.28 O ANISOU 262 OE1 GLU A 53 6281 6373 6448 122 -429 765 O ATOM 263 OE2 GLU A 53 6.745 -8.268 -26.957 1.00 50.15 O1- ANISOU 263 OE2 GLU A 53 6143 6452 6458 170 -462 826 O1- ATOM 264 N PHE A 54 10.026 -12.591 -29.524 1.00 26.48 N ANISOU 264 N PHE A 54 3228 3500 3335 -160 -502 680 N ATOM 265 CA PHE A 54 10.997 -13.185 -30.439 1.00 25.59 C ANISOU 265 CA PHE A 54 3162 3381 3181 -224 -504 651 C ATOM 266 C PHE A 54 10.580 -12.958 -31.884 1.00 28.50 C ANISOU 266 C PHE A 54 3550 3766 3512 -249 -548 693 C ATOM 267 O PHE A 54 11.399 -12.573 -32.729 1.00 26.90 O ANISOU 267 O PHE A 54 3402 3540 3278 -275 -543 687 O ATOM 268 CB PHE A 54 11.143 -14.683 -30.164 1.00 26.55 C ANISOU 268 CB PHE A 54 3264 3528 3293 -266 -504 615 C ATOM 269 CG PHE A 54 12.153 -15.369 -31.049 1.00 22.99 C ANISOU 269 CG PHE A 54 2864 3072 2799 -324 -501 582 C ATOM 270 CD1 PHE A 54 13.515 -15.182 -30.838 1.00 23.31 C ANISOU 270 CD1 PHE A 54 2944 3077 2835 -330 -458 539 C ATOM 271 CD2 PHE A 54 11.740 -16.196 -32.091 1.00 25.37 C ANISOU 271 CD2 PHE A 54 3174 3403 3062 -371 -541 594 C ATOM 272 CE1 PHE A 54 14.453 -15.806 -31.646 1.00 22.84 C ANISOU 272 CE1 PHE A 54 2928 3016 2735 -377 -450 511 C ATOM 273 CE2 PHE A 54 12.669 -16.838 -32.911 1.00 24.85 C ANISOU 273 CE2 PHE A 54 3160 3330 2951 -418 -534 562 C ATOM 274 CZ PHE A 54 14.037 -16.639 -32.692 1.00 25.06 C ANISOU 274 CZ PHE A 54 3222 3325 2975 -418 -486 521 C ATOM 275 N GLN A 55 9.293 -13.158 -32.170 1.00 24.86 N ANISOU 275 N GLN A 55 3043 3350 3054 -241 -592 740 N ATOM 276 CA GLN A 55 8.790 -13.102 -33.538 1.00 26.29 C ANISOU 276 CA GLN A 55 3238 3555 3197 -271 -642 782 C ATOM 277 C GLN A 55 8.899 -11.702 -34.126 1.00 30.47 C ANISOU 277 C GLN A 55 3804 4052 3720 -240 -644 817 C ATOM 278 O GLN A 55 9.055 -11.560 -35.349 1.00 28.34 O ANISOU 278 O GLN A 55 3575 3785 3410 -275 -670 835 O ATOM 279 CB GLN A 55 7.347 -13.620 -33.555 1.00 25.07 C ANISOU 279 CB GLN A 55 3015 3459 3052 -269 -689 828 C ATOM 280 CG GLN A 55 7.332 -15.154 -33.639 1.00 32.29 C ANISOU 280 CG GLN A 55 3920 4403 3944 -334 -706 799 C ATOM 281 CD GLN A 55 5.959 -15.805 -33.436 1.00 36.09 C ANISOU 281 CD GLN A 55 4329 4946 4439 -341 -750 840 C ATOM 282 NE2 GLN A 55 4.966 -15.362 -34.214 1.00 34.70 N ANISOU 282 NE2 GLN A 55 4125 4805 4252 -336 -801 904 N ATOM 283 OE1 GLN A 55 5.800 -16.698 -32.583 1.00 33.09 O ANISOU 283 OE1 GLN A 55 3915 4582 4077 -352 -739 817 O ATOM 284 N LYS A 56 8.839 -10.664 -33.280 1.00 26.33 N ANISOU 284 N LYS A 56 3273 3496 3234 -175 -615 825 N ATOM 285 CA LYS A 56 9.095 -9.306 -33.756 1.00 28.40 C ANISOU 285 CA LYS A 56 3584 3717 3491 -146 -612 852 C ATOM 286 C LYS A 56 10.482 -9.205 -34.369 1.00 26.94 C ANISOU 286 C LYS A 56 3470 3495 3271 -196 -589 816 C ATOM 287 O LYS A 56 10.678 -8.543 -35.397 1.00 25.25 O ANISOU 287 O LYS A 56 3302 3266 3027 -211 -606 843 O ATOM 288 CB LYS A 56 8.961 -8.316 -32.599 1.00 29.31 C ANISOU 288 CB LYS A 56 3693 3794 3651 -72 -578 854 C ATOM 289 CG LYS A 56 7.676 -8.471 -31.823 1.00 39.23 C ANISOU 289 CG LYS A 56 4873 5088 4943 -16 -588 884 C ATOM 290 CD LYS A 56 6.951 -7.154 -31.642 1.00 42.72 C ANISOU 290 CD LYS A 56 5315 5509 5407 65 -589 933 C ATOM 291 CE LYS A 56 7.805 -6.189 -30.844 1.00 46.87 C ANISOU 291 CE LYS A 56 5898 5961 5949 100 -540 901 C ATOM 292 NZ LYS A 56 6.973 -5.140 -30.180 1.00 54.87 N1+ ANISOU 292 NZ LYS A 56 6899 6954 6993 195 -529 937 N1+ ATOM 293 N LEU A 57 11.454 -9.857 -33.742 1.00 25.79 N ANISOU 293 N LEU A 57 3332 3337 3129 -223 -551 758 N ATOM 294 CA LEU A 57 12.833 -9.846 -34.205 1.00 28.94 C ANISOU 294 CA LEU A 57 3788 3709 3498 -269 -523 722 C ATOM 295 C LEU A 57 13.065 -10.771 -35.392 1.00 28.33 C ANISOU 295 C LEU A 57 3731 3663 3370 -330 -545 716 C ATOM 296 O LEU A 57 13.994 -10.535 -36.170 1.00 25.36 O ANISOU 296 O LEU A 57 3407 3270 2959 -365 -532 707 O ATOM 297 CB LEU A 57 13.764 -10.239 -33.053 1.00 25.20 C ANISOU 297 CB LEU A 57 3310 3216 3048 -270 -475 665 C ATOM 298 CG LEU A 57 13.799 -9.307 -31.840 1.00 25.68 C ANISOU 298 CG LEU A 57 3368 3238 3152 -216 -447 661 C ATOM 299 CD1 LEU A 57 14.583 -9.949 -30.711 1.00 26.11 C ANISOU 299 CD1 LEU A 57 3408 3285 3226 -223 -408 605 C ATOM 300 CD2 LEU A 57 14.449 -7.988 -32.252 1.00 28.40 C ANISOU 300 CD2 LEU A 57 3773 3533 3486 -215 -436 676 C ATOM 301 N HIS A 58 12.271 -11.835 -35.533 1.00 27.00 N ANISOU 301 N HIS A 58 3526 3538 3194 -348 -577 720 N ATOM 302 CA HIS A 58 12.494 -12.819 -36.590 1.00 28.08 C ANISOU 302 CA HIS A 58 3689 3701 3279 -408 -597 708 C ATOM 303 C HIS A 58 11.146 -13.152 -37.201 1.00 30.67 C ANISOU 303 C HIS A 58 3988 4072 3595 -416 -658 756 C ATOM 304 O HIS A 58 10.476 -14.113 -36.794 1.00 28.65 O ANISOU 304 O HIS A 58 3689 3849 3350 -426 -677 751 O ATOM 305 CB HIS A 58 13.204 -14.052 -36.047 1.00 23.85 C ANISOU 305 CB HIS A 58 3151 3169 2741 -434 -567 649 C ATOM 306 CG HIS A 58 14.500 -13.716 -35.376 1.00 27.76 C ANISOU 306 CG HIS A 58 3666 3629 3252 -425 -510 608 C ATOM 307 CD2 HIS A 58 14.814 -13.573 -34.067 1.00 26.27 C ANISOU 307 CD2 HIS A 58 3451 3422 3109 -392 -475 582 C ATOM 308 ND1 HIS A 58 15.653 -13.434 -36.076 1.00 29.04 N ANISOU 308 ND1 HIS A 58 3880 3774 3381 -452 -484 592 N ATOM 309 CE1 HIS A 58 16.626 -13.153 -35.229 1.00 27.81 C ANISOU 309 CE1 HIS A 58 3725 3592 3249 -440 -437 560 C ATOM 310 NE2 HIS A 58 16.147 -13.239 -34.002 1.00 28.60 N ANISOU 310 NE2 HIS A 58 3780 3690 3396 -404 -433 551 N ATOM 311 N PRO A 59 10.705 -12.356 -38.183 1.00 29.15 N ANISOU 311 N PRO A 59 3815 3882 3379 -414 -692 806 N ATOM 312 CA PRO A 59 9.299 -12.418 -38.608 1.00 32.06 C ANISOU 312 CA PRO A 59 4142 4294 3746 -409 -753 863 C ATOM 313 C PRO A 59 8.930 -13.698 -39.341 1.00 32.73 C ANISOU 313 C PRO A 59 4229 4419 3787 -473 -795 858 C ATOM 314 O PRO A 59 7.746 -14.042 -39.391 1.00 32.14 O ANISOU 314 O PRO A 59 4105 4388 3719 -476 -844 897 O ATOM 315 CB PRO A 59 9.149 -11.188 -39.517 1.00 34.54 C ANISOU 315 CB PRO A 59 4489 4592 4040 -393 -775 914 C ATOM 316 CG PRO A 59 10.350 -10.323 -39.222 1.00 31.14 C ANISOU 316 CG PRO A 59 4107 4106 3619 -376 -720 885 C ATOM 317 CD PRO A 59 11.436 -11.266 -38.848 1.00 31.70 C ANISOU 317 CD PRO A 59 4195 4169 3681 -413 -677 818 C ATOM 318 N ASP A 60 9.890 -14.426 -39.889 1.00 33.27 N ANISOU 318 N ASP A 60 4355 4476 3811 -524 -776 812 N ATOM 319 CA ASP A 60 9.576 -15.668 -40.584 1.00 33.54 C ANISOU 319 CA ASP A 60 4404 4540 3798 -585 -815 804 C ATOM 320 C ASP A 60 9.459 -16.865 -39.647 1.00 34.57 C ANISOU 320 C ASP A 60 4501 4682 3951 -596 -804 765 C ATOM 321 O ASP A 60 9.251 -17.984 -40.128 1.00 35.18 O ANISOU 321 O ASP A 60 4599 4779 3990 -650 -834 752 O ATOM 322 CB ASP A 60 10.635 -15.958 -41.654 1.00 33.87 C ANISOU 322 CB ASP A 60 4529 4563 3775 -631 -798 772 C ATOM 323 CG ASP A 60 10.494 -15.064 -42.850 1.00 41.52 C ANISOU 323 CG ASP A 60 5537 5534 4706 -639 -827 818 C ATOM 324 OD1 ASP A 60 9.993 -13.932 -42.688 1.00 43.22 O ANISOU 324 OD1 ASP A 60 5723 5746 4953 -595 -839 865 O ATOM 325 OD2 ASP A 60 10.873 -15.492 -43.956 1.00 52.71 O1- ANISOU 325 OD2 ASP A 60 7015 6953 6057 -688 -839 809 O1- ATOM 326 N VAL A 61 9.581 -16.663 -38.334 1.00 29.12 N ANISOU 326 N VAL A 61 3765 3979 3318 -550 -765 747 N ATOM 327 CA VAL A 61 9.575 -17.750 -37.362 1.00 27.51 C ANISOU 327 CA VAL A 61 3532 3781 3137 -558 -749 709 C ATOM 328 C VAL A 61 8.286 -17.703 -36.555 1.00 28.13 C ANISOU 328 C VAL A 61 3530 3896 3262 -529 -777 749 C ATOM 329 O VAL A 61 7.802 -16.623 -36.212 1.00 25.63 O ANISOU 329 O VAL A 61 3176 3581 2981 -476 -776 788 O ATOM 330 CB VAL A 61 10.790 -17.664 -36.425 1.00 25.66 C ANISOU 330 CB VAL A 61 3312 3509 2930 -530 -681 654 C ATOM 331 CG1 VAL A 61 10.780 -18.851 -35.468 1.00 25.99 C ANISOU 331 CG1 VAL A 61 3328 3557 2991 -540 -667 616 C ATOM 332 CG2 VAL A 61 12.064 -17.619 -37.229 1.00 26.69 C ANISOU 332 CG2 VAL A 61 3514 3611 3016 -554 -650 621 C ATOM 333 N THR A 62 7.730 -18.876 -36.250 1.00 26.11 N ANISOU 333 N THR A 62 3248 3668 3006 -564 -801 742 N ATOM 334 CA THR A 62 6.630 -18.988 -35.304 1.00 28.42 C ANISOU 334 CA THR A 62 3457 3996 3343 -540 -816 773 C ATOM 335 C THR A 62 7.010 -19.991 -34.216 1.00 29.46 C ANISOU 335 C THR A 62 3580 4119 3497 -547 -782 723 C ATOM 336 O THR A 62 7.414 -21.119 -34.517 1.00 29.87 O ANISOU 336 O THR A 62 3673 4162 3512 -601 -788 686 O ATOM 337 CB THR A 62 5.331 -19.432 -35.989 1.00 31.83 C ANISOU 337 CB THR A 62 3855 4484 3755 -582 -890 828 C ATOM 338 CG2 THR A 62 4.284 -19.705 -34.915 1.00 36.13 C ANISOU 338 CG2 THR A 62 4309 5070 4347 -561 -899 856 C ATOM 339 OG1 THR A 62 4.838 -18.394 -36.851 1.00 33.14 O ANISOU 339 OG1 THR A 62 4017 4665 3910 -563 -923 884 O ATOM 340 N VAL A 63 6.874 -19.590 -32.953 1.00 31.99 N ANISOU 340 N VAL A 63 3848 4436 3871 -492 -747 721 N ATOM 341 CA VAL A 63 7.339 -20.383 -31.817 1.00 28.42 C ANISOU 341 CA VAL A 63 3388 3969 3441 -491 -709 673 C ATOM 342 C VAL A 63 6.130 -20.911 -31.061 1.00 31.29 C ANISOU 342 C VAL A 63 3676 4380 3834 -492 -733 705 C ATOM 343 O VAL A 63 5.335 -20.124 -30.530 1.00 33.54 O ANISOU 343 O VAL A 63 3899 4689 4156 -440 -732 747 O ATOM 344 CB VAL A 63 8.252 -19.568 -30.886 1.00 28.84 C ANISOU 344 CB VAL A 63 3448 3981 3529 -432 -646 641 C ATOM 345 CG1 VAL A 63 8.885 -20.488 -29.829 1.00 26.77 C ANISOU 345 CG1 VAL A 63 3187 3702 3281 -437 -609 588 C ATOM 346 CG2 VAL A 63 9.333 -18.853 -31.684 1.00 24.38 C ANISOU 346 CG2 VAL A 63 2947 3377 2937 -431 -626 623 C ATOM 347 N THR A 64 5.994 -22.242 -31.003 1.00 27.61 N ANISOU 347 N THR A 64 3216 3925 3348 -549 -752 686 N ATOM 348 CA THR A 64 4.954 -22.892 -30.217 1.00 31.04 C ANISOU 348 CA THR A 64 3583 4403 3807 -560 -772 713 C ATOM 349 C THR A 64 5.593 -23.800 -29.174 1.00 30.92 C ANISOU 349 C THR A 64 3580 4362 3804 -566 -733 659 C ATOM 350 O THR A 64 6.655 -24.387 -29.406 1.00 28.38 O ANISOU 350 O THR A 64 3329 4000 3456 -590 -713 605 O ATOM 351 CB THR A 64 4.000 -23.716 -31.080 1.00 31.96 C ANISOU 351 CB THR A 64 3691 4564 3889 -633 -842 750 C ATOM 352 CG2 THR A 64 3.507 -22.879 -32.242 1.00 32.87 C ANISOU 352 CG2 THR A 64 3805 4701 3984 -633 -884 800 C ATOM 353 OG1 THR A 64 4.689 -24.864 -31.582 1.00 32.31 O ANISOU 353 OG1 THR A 64 3813 4578 3887 -698 -850 702 O ATOM 354 N PHE A 65 4.929 -23.928 -28.026 1.00 30.94 N ANISOU 354 N PHE A 65 3517 4392 3848 -542 -721 675 N ATOM 355 CA PHE A 65 5.502 -24.618 -26.884 1.00 28.96 C ANISOU 355 CA PHE A 65 3273 4118 3615 -537 -679 629 C ATOM 356 C PHE A 65 4.701 -25.854 -26.508 1.00 30.54 C ANISOU 356 C PHE A 65 3442 4352 3812 -591 -710 643 C ATOM 357 O PHE A 65 3.529 -26.006 -26.855 1.00 30.33 O ANISOU 357 O PHE A 65 3366 4377 3781 -622 -759 697 O ATOM 358 CB PHE A 65 5.607 -23.691 -25.674 1.00 27.80 C ANISOU 358 CB PHE A 65 3084 3963 3516 -458 -628 627 C ATOM 359 CG PHE A 65 6.360 -22.443 -25.958 1.00 32.26 C ANISOU 359 CG PHE A 65 3680 4492 4085 -408 -599 616 C ATOM 360 CD1 PHE A 65 7.680 -22.311 -25.557 1.00 29.45 C ANISOU 360 CD1 PHE A 65 3374 4084 3730 -390 -551 560 C ATOM 361 CD2 PHE A 65 5.741 -21.381 -26.613 1.00 31.15 C ANISOU 361 CD2 PHE A 65 3518 4370 3948 -380 -620 664 C ATOM 362 CE1 PHE A 65 8.385 -21.157 -25.838 1.00 32.23 C ANISOU 362 CE1 PHE A 65 3757 4404 4085 -353 -527 552 C ATOM 363 CE2 PHE A 65 6.435 -20.218 -26.881 1.00 30.85 C ANISOU 363 CE2 PHE A 65 3515 4294 3912 -338 -595 656 C ATOM 364 CZ PHE A 65 7.753 -20.100 -26.494 1.00 30.84 C ANISOU 364 CZ PHE A 65 3565 4242 3911 -327 -549 600 C ATOM 365 N GLU A 66 5.383 -26.747 -25.805 1.00 27.05 N ANISOU 365 N GLU A 66 3032 3878 3369 -605 -683 594 N ATOM 366 CA GLU A 66 4.767 -27.869 -25.110 1.00 31.72 C ANISOU 366 CA GLU A 66 3596 4492 3965 -646 -698 601 C ATOM 367 C GLU A 66 5.477 -28.045 -23.779 1.00 29.76 C ANISOU 367 C GLU A 66 3349 4213 3744 -607 -641 558 C ATOM 368 O GLU A 66 6.699 -28.227 -23.755 1.00 30.84 O ANISOU 368 O GLU A 66 3548 4299 3869 -597 -609 504 O ATOM 369 CB GLU A 66 4.858 -29.168 -25.905 1.00 32.85 C ANISOU 369 CB GLU A 66 3802 4621 4058 -730 -740 584 C ATOM 370 CG GLU A 66 4.293 -30.327 -25.099 1.00 33.46 C ANISOU 370 CG GLU A 66 3858 4714 4141 -774 -753 589 C ATOM 371 CD GLU A 66 4.409 -31.662 -25.784 1.00 36.74 C ANISOU 371 CD GLU A 66 4347 5107 4507 -856 -793 568 C ATOM 372 OE1 GLU A 66 5.125 -31.755 -26.814 1.00 33.26 O ANISOU 372 OE1 GLU A 66 3984 4630 4026 -872 -800 538 O ATOM 373 OE2 GLU A 66 3.778 -32.624 -25.269 1.00 37.48 O1- ANISOU 373 OE2 GLU A 66 4424 5217 4600 -905 -815 582 O1- ATOM 374 N GLY A 67 4.725 -27.992 -22.683 1.00 30.90 N ANISOU 374 N GLY A 67 3424 4393 3925 -584 -628 585 N ATOM 375 CA GLY A 67 5.236 -28.359 -21.371 1.00 30.57 C ANISOU 375 CA GLY A 67 3381 4329 3905 -559 -582 550 C ATOM 376 C GLY A 67 4.867 -29.800 -21.063 1.00 33.83 C ANISOU 376 C GLY A 67 3800 4750 4303 -624 -607 549 C ATOM 377 O GLY A 67 3.745 -30.236 -21.342 1.00 31.62 O ANISOU 377 O GLY A 67 3480 4519 4017 -673 -652 596 O ATOM 378 N ILE A 68 5.826 -30.541 -20.498 1.00 31.81 N ANISOU 378 N ILE A 68 3597 4449 4041 -628 -579 496 N ATOM 379 CA ILE A 68 5.640 -31.946 -20.142 1.00 30.43 C ANISOU 379 CA ILE A 68 3443 4269 3850 -687 -597 488 C ATOM 380 C ILE A 68 5.864 -32.108 -18.649 1.00 33.75 C ANISOU 380 C ILE A 68 3840 4683 4301 -652 -552 471 C ATOM 381 O ILE A 68 6.907 -31.698 -18.120 1.00 33.94 O ANISOU 381 O ILE A 68 3889 4669 4337 -600 -507 430 O ATOM 382 CB ILE A 68 6.583 -32.881 -20.918 1.00 28.99 C ANISOU 382 CB ILE A 68 3359 4032 3625 -729 -609 440 C ATOM 383 CG1 ILE A 68 6.471 -32.640 -22.414 1.00 31.92 C ANISOU 383 CG1 ILE A 68 3761 4405 3961 -759 -648 452 C ATOM 384 CG2 ILE A 68 6.261 -34.339 -20.614 1.00 30.72 C ANISOU 384 CG2 ILE A 68 3605 4243 3824 -794 -635 437 C ATOM 385 CD1 ILE A 68 7.459 -33.461 -23.195 1.00 33.38 C ANISOU 385 CD1 ILE A 68 4047 4536 4100 -789 -652 403 C ATOM 386 N THR A 69 4.892 -32.726 -17.974 1.00 35.13 N ANISOU 386 N THR A 69 3967 4897 4486 -684 -567 506 N ATOM 387 CA THR A 69 5.040 -33.012 -16.551 1.00 34.56 C ANISOU 387 CA THR A 69 3875 4820 4436 -658 -528 493 C ATOM 388 C THR A 69 6.155 -34.017 -16.316 1.00 32.43 C ANISOU 388 C THR A 69 3687 4489 4147 -675 -515 436 C ATOM 389 O THR A 69 7.119 -33.739 -15.594 1.00 35.34 O ANISOU 389 O THR A 69 4075 4824 4528 -624 -470 397 O ATOM 390 CB THR A 69 3.728 -33.549 -15.985 1.00 37.26 C ANISOU 390 CB THR A 69 4150 5219 4787 -698 -550 546 C ATOM 391 CG2 THR A 69 3.931 -33.994 -14.535 1.00 32.94 C ANISOU 391 CG2 THR A 69 3595 4665 4258 -679 -510 530 C ATOM 392 OG1 THR A 69 2.728 -32.528 -16.053 1.00 41.34 O ANISOU 392 OG1 THR A 69 4582 5797 5328 -666 -552 600 O ATOM 393 N ASP A 70 6.033 -35.197 -16.921 1.00 30.99 N ANISOU 393 N ASP A 70 3554 4290 3929 -747 -556 433 N ATOM 394 CA ASP A 70 7.026 -36.261 -16.782 1.00 33.26 C ANISOU 394 CA ASP A 70 3925 4519 4195 -764 -547 383 C ATOM 395 C ASP A 70 8.117 -36.056 -17.834 1.00 28.44 C ANISOU 395 C ASP A 70 3384 3862 3558 -748 -542 341 C ATOM 396 O ASP A 70 8.294 -36.860 -18.751 1.00 26.22 O ANISOU 396 O ASP A 70 3171 3554 3237 -796 -573 326 O ATOM 397 CB ASP A 70 6.361 -37.626 -16.942 1.00 32.87 C ANISOU 397 CB ASP A 70 3905 4467 4117 -848 -593 400 C ATOM 398 CG ASP A 70 5.383 -37.932 -15.826 1.00 40.73 C ANISOU 398 CG ASP A 70 4834 5506 5135 -867 -593 440 C ATOM 399 OD1 ASP A 70 5.656 -37.517 -14.679 1.00 35.36 O ANISOU 399 OD1 ASP A 70 4119 4831 4486 -812 -547 431 O ATOM 400 OD2 ASP A 70 4.351 -38.599 -16.091 1.00 43.98 O1- ANISOU 400 OD2 ASP A 70 5230 5950 5533 -941 -640 481 O1- ATOM 401 N TYR A 71 8.852 -34.947 -17.692 1.00 28.06 N ANISOU 401 N TYR A 71 3322 3809 3531 -680 -502 322 N ATOM 402 CA TYR A 71 9.733 -34.508 -18.775 1.00 28.44 C ANISOU 402 CA TYR A 71 3419 3829 3558 -664 -498 294 C ATOM 403 C TYR A 71 10.774 -35.564 -19.153 1.00 25.15 C ANISOU 403 C TYR A 71 3092 3358 3106 -681 -493 246 C ATOM 404 O TYR A 71 10.879 -35.945 -20.325 1.00 25.82 O ANISOU 404 O TYR A 71 3232 3427 3153 -715 -520 239 O ATOM 405 CB TYR A 71 10.418 -33.179 -18.435 1.00 26.00 C ANISOU 405 CB TYR A 71 3082 3518 3277 -593 -454 282 C ATOM 406 CG TYR A 71 11.110 -32.632 -19.666 1.00 25.76 C ANISOU 406 CG TYR A 71 3093 3470 3224 -586 -455 266 C ATOM 407 CD1 TYR A 71 10.425 -31.835 -20.574 1.00 23.80 C ANISOU 407 CD1 TYR A 71 2821 3251 2972 -594 -481 301 C ATOM 408 CD2 TYR A 71 12.440 -32.961 -19.945 1.00 25.27 C ANISOU 408 CD2 TYR A 71 3094 3365 3142 -572 -430 218 C ATOM 409 CE1 TYR A 71 11.039 -31.363 -21.723 1.00 23.49 C ANISOU 409 CE1 TYR A 71 2822 3195 2908 -591 -483 289 C ATOM 410 CE2 TYR A 71 13.064 -32.495 -21.090 1.00 24.12 C ANISOU 410 CE2 TYR A 71 2985 3207 2972 -568 -429 206 C ATOM 411 CZ TYR A 71 12.359 -31.691 -21.971 1.00 25.13 C ANISOU 411 CZ TYR A 71 3091 3361 3095 -579 -455 241 C ATOM 412 OH TYR A 71 12.973 -31.225 -23.105 1.00 20.01 O ANISOU 412 OH TYR A 71 2481 2700 2420 -576 -453 230 O ATOM 413 N GLU A 72 11.593 -36.006 -18.191 1.00 26.50 N ANISOU 413 N GLU A 72 3281 3499 3288 -651 -459 213 N ATOM 414 CA GLU A 72 12.657 -36.972 -18.491 1.00 23.83 C ANISOU 414 CA GLU A 72 3026 3109 2918 -654 -449 168 C ATOM 415 C GLU A 72 12.097 -38.243 -19.111 1.00 26.29 C ANISOU 415 C GLU A 72 3395 3403 3190 -723 -493 173 C ATOM 416 O GLU A 72 12.622 -38.747 -20.113 1.00 23.59 O ANISOU 416 O GLU A 72 3128 3029 2807 -738 -502 148 O ATOM 417 CB GLU A 72 13.428 -37.335 -17.222 1.00 25.99 C ANISOU 417 CB GLU A 72 3301 3361 3212 -615 -411 141 C ATOM 418 CG GLU A 72 14.442 -36.347 -16.716 1.00 25.39 C ANISOU 418 CG GLU A 72 3200 3285 3163 -549 -365 120 C ATOM 419 CD GLU A 72 15.525 -36.029 -17.728 1.00 25.20 C ANISOU 419 CD GLU A 72 3219 3240 3117 -528 -349 91 C ATOM 420 OE1 GLU A 72 16.026 -36.960 -18.384 1.00 27.37 O ANISOU 420 OE1 GLU A 72 3562 3483 3356 -543 -354 67 O ATOM 421 OE2 GLU A 72 15.913 -34.851 -17.818 1.00 26.65 O1- ANISOU 421 OE2 GLU A 72 3370 3437 3318 -493 -328 92 O1- ATOM 422 N GLY A 73 11.041 -38.796 -18.510 1.00 25.76 N ANISOU 422 N GLY A 73 3300 3358 3131 -766 -520 205 N ATOM 423 CA GLY A 73 10.510 -40.058 -19.003 1.00 21.22 C ANISOU 423 CA GLY A 73 2785 2762 2517 -840 -565 210 C ATOM 424 C GLY A 73 9.920 -39.922 -20.391 1.00 27.44 C ANISOU 424 C GLY A 73 3592 3563 3271 -889 -611 230 C ATOM 425 O GLY A 73 10.178 -40.747 -21.278 1.00 25.54 O ANISOU 425 O GLY A 73 3439 3282 2983 -926 -634 208 O ATOM 426 N GLU A 74 9.138 -38.860 -20.608 1.00 26.95 N ANISOU 426 N GLU A 74 3453 3557 3232 -886 -623 271 N ATOM 427 CA GLU A 74 8.462 -38.699 -21.892 1.00 28.36 C ANISOU 427 CA GLU A 74 3642 3755 3380 -935 -672 297 C ATOM 428 C GLU A 74 9.461 -38.414 -23.011 1.00 26.23 C ANISOU 428 C GLU A 74 3440 3451 3077 -911 -659 260 C ATOM 429 O GLU A 74 9.321 -38.926 -24.129 1.00 25.64 O ANISOU 429 O GLU A 74 3429 3359 2953 -962 -697 257 O ATOM 430 CB GLU A 74 7.438 -37.569 -21.803 1.00 28.86 C ANISOU 430 CB GLU A 74 3601 3886 3477 -926 -685 352 C ATOM 431 CG GLU A 74 6.046 -38.039 -21.460 1.00 35.50 C ANISOU 431 CG GLU A 74 4388 4775 4325 -989 -730 406 C ATOM 432 CD GLU A 74 5.267 -38.333 -22.696 1.00 41.09 C ANISOU 432 CD GLU A 74 5118 5501 4993 -1064 -795 437 C ATOM 433 OE1 GLU A 74 5.019 -37.380 -23.456 1.00 40.42 O ANISOU 433 OE1 GLU A 74 5001 5446 4909 -1049 -807 459 O ATOM 434 OE2 GLU A 74 4.913 -39.519 -22.909 1.00 45.17 O1- ANISOU 434 OE2 GLU A 74 5688 5999 5475 -1141 -836 438 O1- ATOM 435 N MET A 75 10.473 -37.590 -22.733 1.00 25.34 N ANISOU 435 N MET A 75 3313 3328 2988 -837 -606 233 N ATOM 436 CA MET A 75 11.461 -37.286 -23.768 1.00 25.41 C ANISOU 436 CA MET A 75 3379 3309 2965 -814 -588 200 C ATOM 437 C MET A 75 12.299 -38.506 -24.110 1.00 25.24 C ANISOU 437 C MET A 75 3461 3230 2899 -825 -581 153 C ATOM 438 O MET A 75 12.648 -38.706 -25.279 1.00 24.63 O ANISOU 438 O MET A 75 3452 3131 2775 -841 -591 136 O ATOM 439 CB MET A 75 12.331 -36.103 -23.336 1.00 27.52 C ANISOU 439 CB MET A 75 3604 3583 3269 -738 -535 186 C ATOM 440 CG MET A 75 11.615 -34.746 -23.460 1.00 24.49 C ANISOU 440 CG MET A 75 3143 3247 2915 -722 -544 229 C ATOM 441 SD MET A 75 10.788 -34.505 -25.060 1.00 28.51 S ANISOU 441 SD MET A 75 3670 3779 3383 -776 -601 263 S ATOM 442 CE MET A 75 12.207 -34.174 -26.083 1.00 21.84 C ANISOU 442 CE MET A 75 2898 2898 2504 -745 -567 219 C ATOM 443 N LYS A 76 12.579 -39.363 -23.128 1.00 26.06 N ANISOU 443 N LYS A 76 3580 3307 3013 -818 -565 134 N ATOM 444 CA LYS A 76 13.273 -40.608 -23.439 1.00 27.03 C ANISOU 444 CA LYS A 76 3806 3371 3092 -829 -561 93 C ATOM 445 C LYS A 76 12.513 -41.410 -24.489 1.00 26.68 C ANISOU 445 C LYS A 76 3831 3312 2993 -908 -619 104 C ATOM 446 O LYS A 76 13.117 -41.923 -25.439 1.00 27.67 O ANISOU 446 O LYS A 76 4048 3398 3068 -912 -617 72 O ATOM 447 CB LYS A 76 13.499 -41.432 -22.165 1.00 25.23 C ANISOU 447 CB LYS A 76 3582 3120 2885 -815 -543 80 C ATOM 448 CG LYS A 76 14.294 -42.715 -22.412 1.00 27.00 C ANISOU 448 CG LYS A 76 3915 3278 3064 -814 -534 37 C ATOM 449 CD LYS A 76 14.641 -43.431 -21.103 1.00 26.40 C ANISOU 449 CD LYS A 76 3841 3178 3012 -790 -512 24 C ATOM 450 CE LYS A 76 15.148 -44.860 -21.344 1.00 33.38 C ANISOU 450 CE LYS A 76 4841 3993 3849 -801 -515 -10 C ATOM 451 NZ LYS A 76 16.343 -44.964 -22.240 1.00 33.64 N1+ ANISOU 451 NZ LYS A 76 4945 3990 3845 -753 -482 -53 N1+ ATOM 452 N THR A 77 11.183 -41.507 -24.360 1.00 25.75 N ANISOU 452 N THR A 77 3671 3230 2884 -972 -670 150 N ATOM 453 CA THR A 77 10.413 -42.225 -25.374 1.00 25.17 C ANISOU 453 CA THR A 77 3660 3147 2757 -1056 -732 164 C ATOM 454 C THR A 77 10.462 -41.505 -26.713 1.00 26.20 C ANISOU 454 C THR A 77 3807 3292 2857 -1060 -746 168 C ATOM 455 O THR A 77 10.692 -42.131 -27.751 1.00 26.98 O ANISOU 455 O THR A 77 4004 3352 2895 -1092 -766 145 O ATOM 456 CB THR A 77 8.957 -42.418 -24.938 1.00 25.25 C ANISOU 456 CB THR A 77 3609 3202 2784 -1127 -785 220 C ATOM 457 CG2 THR A 77 8.223 -43.269 -25.936 1.00 28.25 C ANISOU 457 CG2 THR A 77 4061 3568 3105 -1222 -853 233 C ATOM 458 OG1 THR A 77 8.911 -43.068 -23.666 1.00 31.48 O ANISOU 458 OG1 THR A 77 4382 3980 3601 -1124 -770 219 O ATOM 459 N ARG A 78 10.246 -40.184 -26.714 1.00 28.74 N ANISOU 459 N ARG A 78 4039 3666 3216 -1026 -735 197 N ATOM 460 CA ARG A 78 10.203 -39.449 -27.980 1.00 29.53 C ANISOU 460 CA ARG A 78 4151 3783 3288 -1032 -752 207 C ATOM 461 C ARG A 78 11.544 -39.505 -28.706 1.00 27.60 C ANISOU 461 C ARG A 78 3990 3492 3006 -989 -710 154 C ATOM 462 O ARG A 78 11.587 -39.594 -29.942 1.00 26.88 O ANISOU 462 O ARG A 78 3964 3389 2861 -1018 -732 148 O ATOM 463 CB ARG A 78 9.778 -37.997 -27.736 1.00 28.65 C ANISOU 463 CB ARG A 78 3929 3730 3227 -995 -744 247 C ATOM 464 CG ARG A 78 8.376 -37.860 -27.146 1.00 33.03 C ANISOU 464 CG ARG A 78 4394 4339 3815 -1034 -785 306 C ATOM 465 CD ARG A 78 7.970 -36.401 -27.019 1.00 32.71 C ANISOU 465 CD ARG A 78 4256 4354 3820 -989 -775 345 C ATOM 466 NE ARG A 78 6.810 -36.259 -26.147 1.00 38.75 N ANISOU 466 NE ARG A 78 4927 5171 4626 -1004 -795 396 N ATOM 467 CZ ARG A 78 6.156 -35.126 -25.926 1.00 38.61 C ANISOU 467 CZ ARG A 78 4816 5206 4647 -971 -795 441 C ATOM 468 NH1 ARG A 78 6.464 -34.005 -26.569 1.00 34.89 N1+ ANISOU 468 NH1 ARG A 78 4335 4743 4179 -929 -782 445 N1+ ATOM 469 NH2 ARG A 78 5.168 -35.115 -25.035 1.00 37.33 N ANISOU 469 NH2 ARG A 78 4571 5091 4522 -979 -805 483 N ATOM 470 N LEU A 79 12.646 -39.459 -27.952 1.00 25.54 N ANISOU 470 N LEU A 79 3725 3207 2770 -920 -648 118 N ATOM 471 CA LEU A 79 13.986 -39.531 -28.524 1.00 27.36 C ANISOU 471 CA LEU A 79 4025 3400 2970 -872 -601 70 C ATOM 472 C LEU A 79 14.225 -40.830 -29.294 1.00 31.33 C ANISOU 472 C LEU A 79 4651 3848 3404 -908 -617 37 C ATOM 473 O LEU A 79 15.172 -40.899 -30.084 1.00 31.03 O ANISOU 473 O LEU A 79 4680 3784 3326 -877 -585 3 O ATOM 474 CB LEU A 79 15.011 -39.376 -27.400 1.00 28.26 C ANISOU 474 CB LEU A 79 4104 3504 3128 -799 -539 44 C ATOM 475 CG LEU A 79 15.469 -37.987 -26.909 1.00 31.91 C ANISOU 475 CG LEU A 79 4478 4003 3643 -739 -499 54 C ATOM 476 CD1 LEU A 79 16.797 -37.538 -27.450 1.00 29.74 C ANISOU 476 CD1 LEU A 79 4231 3716 3353 -687 -448 23 C ATOM 477 CD2 LEU A 79 14.438 -36.912 -27.235 1.00 25.65 C ANISOU 477 CD2 LEU A 79 3618 3259 2869 -764 -533 103 C ATOM 478 N SER A 80 13.403 -41.866 -29.086 1.00 28.61 N ANISOU 478 N SER A 80 4343 3485 3042 -971 -664 47 N ATOM 479 CA SER A 80 13.535 -43.076 -29.887 1.00 31.63 C ANISOU 479 CA SER A 80 4855 3811 3354 -1012 -685 17 C ATOM 480 C SER A 80 12.862 -42.952 -31.252 1.00 32.36 C ANISOU 480 C SER A 80 4991 3914 3391 -1077 -739 35 C ATOM 481 O SER A 80 12.893 -43.909 -32.034 1.00 32.54 O ANISOU 481 O SER A 80 5129 3889 3347 -1118 -762 11 O ATOM 482 CB SER A 80 12.964 -44.285 -29.143 1.00 34.67 C ANISOU 482 CB SER A 80 5273 4164 3736 -1061 -717 19 C ATOM 483 OG SER A 80 11.550 -44.218 -29.107 1.00 34.41 O ANISOU 483 OG SER A 80 5190 4173 3713 -1141 -783 71 O ATOM 484 N THR A 81 12.245 -41.811 -31.554 1.00 32.71 N ANISOU 484 N THR A 81 4951 4017 3459 -1087 -760 77 N ATOM 485 CA THR A 81 11.770 -41.505 -32.892 1.00 31.61 C ANISOU 485 CA THR A 81 4847 3893 3269 -1135 -804 95 C ATOM 486 C THR A 81 12.719 -40.490 -33.530 1.00 34.26 C ANISOU 486 C THR A 81 5176 4239 3602 -1070 -754 79 C ATOM 487 O THR A 81 13.770 -40.147 -32.970 1.00 33.16 O ANISOU 487 O THR A 81 5013 4092 3494 -994 -688 52 O ATOM 488 CB THR A 81 10.330 -40.979 -32.846 1.00 33.31 C ANISOU 488 CB THR A 81 4975 4170 3511 -1195 -869 160 C ATOM 489 CG2 THR A 81 9.483 -41.854 -31.942 1.00 30.86 C ANISOU 489 CG2 THR A 81 4646 3860 3219 -1249 -905 180 C ATOM 490 OG1 THR A 81 10.318 -39.644 -32.325 1.00 30.81 O ANISOU 490 OG1 THR A 81 4541 3907 3259 -1139 -840 189 O ATOM 491 N THR A 82 12.351 -40.012 -34.721 1.00 33.87 N ANISOU 491 N THR A 82 5149 4210 3512 -1105 -788 99 N ATOM 492 CA THR A 82 13.065 -38.926 -35.381 1.00 35.67 C ANISOU 492 CA THR A 82 5362 4456 3737 -1055 -750 95 C ATOM 493 C THR A 82 12.266 -37.628 -35.358 1.00 34.76 C ANISOU 493 C THR A 82 5138 4403 3665 -1058 -776 152 C ATOM 494 O THR A 82 12.492 -36.745 -36.194 1.00 32.75 O ANISOU 494 O THR A 82 4881 4167 3394 -1044 -770 163 O ATOM 495 CB THR A 82 13.417 -39.302 -36.822 1.00 36.27 C ANISOU 495 CB THR A 82 5554 4503 3726 -1080 -759 71 C ATOM 496 CG2 THR A 82 14.277 -40.557 -36.869 1.00 35.17 C ANISOU 496 CG2 THR A 82 5526 4296 3539 -1064 -725 13 C ATOM 497 OG1 THR A 82 12.211 -39.503 -37.570 1.00 39.18 O ANISOU 497 OG1 THR A 82 5945 4888 4056 -1168 -841 107 O ATOM 498 N ASN A 83 11.325 -37.500 -34.424 1.00 30.24 N ANISOU 498 N ASN A 83 4479 3864 3148 -1075 -805 190 N ATOM 499 CA ASN A 83 10.534 -36.276 -34.320 1.00 36.20 C ANISOU 499 CA ASN A 83 5129 4679 3947 -1070 -826 246 C ATOM 500 C ASN A 83 10.255 -36.036 -32.839 1.00 33.88 C ANISOU 500 C ASN A 83 4737 4406 3729 -1035 -805 261 C ATOM 501 O ASN A 83 9.348 -36.646 -32.266 1.00 31.31 O ANISOU 501 O ASN A 83 4383 4095 3417 -1079 -843 285 O ATOM 502 CB ASN A 83 9.253 -36.383 -35.133 1.00 41.13 C ANISOU 502 CB ASN A 83 5754 5335 4539 -1150 -909 294 C ATOM 503 CG ASN A 83 8.215 -35.361 -34.719 1.00 48.06 C ANISOU 503 CG ASN A 83 6510 6278 5472 -1145 -936 358 C ATOM 504 ND2 ASN A 83 6.982 -35.830 -34.526 1.00 51.68 N ANISOU 504 ND2 ASN A 83 6932 6769 5934 -1209 -998 401 N ATOM 505 OD1 ASN A 83 8.514 -34.166 -34.554 1.00 50.83 O ANISOU 505 OD1 ASN A 83 6802 6650 5862 -1084 -901 370 O ATOM 506 N TYR A 84 11.054 -35.165 -32.218 1.00 27.83 N ANISOU 506 N TYR A 84 3924 3643 3009 -960 -745 248 N ATOM 507 CA TYR A 84 10.874 -34.897 -30.797 1.00 25.93 C ANISOU 507 CA TYR A 84 3597 3419 2835 -923 -721 259 C ATOM 508 C TYR A 84 11.000 -33.408 -30.497 1.00 25.54 C ANISOU 508 C TYR A 84 3470 3400 2835 -864 -691 281 C ATOM 509 O TYR A 84 11.408 -33.022 -29.395 1.00 24.30 O ANISOU 509 O TYR A 84 3263 3242 2726 -812 -648 271 O ATOM 510 CB TYR A 84 11.854 -35.726 -29.951 1.00 25.45 C ANISOU 510 CB TYR A 84 3574 3315 2782 -892 -672 208 C ATOM 511 CG TYR A 84 13.261 -35.858 -30.524 1.00 23.92 C ANISOU 511 CG TYR A 84 3455 3080 2554 -854 -624 157 C ATOM 512 CD1 TYR A 84 14.232 -34.889 -30.285 1.00 23.36 C ANISOU 512 CD1 TYR A 84 3352 3013 2512 -789 -569 144 C ATOM 513 CD2 TYR A 84 13.601 -36.942 -31.339 1.00 26.62 C ANISOU 513 CD2 TYR A 84 3903 3381 2831 -886 -634 125 C ATOM 514 CE1 TYR A 84 15.524 -35.005 -30.813 1.00 22.70 C ANISOU 514 CE1 TYR A 84 3329 2900 2396 -755 -523 102 C ATOM 515 CE2 TYR A 84 14.878 -37.072 -31.877 1.00 25.50 C ANISOU 515 CE2 TYR A 84 3827 3206 2655 -847 -586 81 C ATOM 516 CZ TYR A 84 15.838 -36.104 -31.610 1.00 26.12 C ANISOU 516 CZ TYR A 84 3862 3297 2766 -781 -530 71 C ATOM 517 OH TYR A 84 17.102 -36.244 -32.150 1.00 26.31 O ANISOU 517 OH TYR A 84 3945 3296 2757 -744 -480 32 O ATOM 518 N GLY A 85 10.638 -32.567 -31.457 1.00 23.71 N ANISOU 518 N GLY A 85 3229 3192 2586 -873 -716 313 N ATOM 519 CA GLY A 85 10.651 -31.135 -31.275 1.00 24.19 C ANISOU 519 CA GLY A 85 3224 3279 2688 -821 -695 339 C ATOM 520 C GLY A 85 11.871 -30.496 -31.909 1.00 22.77 C ANISOU 520 C GLY A 85 3087 3074 2489 -785 -652 309 C ATOM 521 O GLY A 85 12.791 -31.161 -32.395 1.00 21.78 O ANISOU 521 O GLY A 85 3038 2915 2323 -790 -630 266 O ATOM 522 N ASP A 86 11.869 -29.166 -31.889 1.00 20.39 N ANISOU 522 N ASP A 86 2738 2791 2218 -745 -638 335 N ATOM 523 CA ASP A 86 12.932 -28.394 -32.519 1.00 19.69 C ANISOU 523 CA ASP A 86 2682 2685 2113 -716 -601 317 C ATOM 524 C ASP A 86 13.930 -27.854 -31.515 1.00 21.46 C ANISOU 524 C ASP A 86 2879 2893 2381 -658 -539 290 C ATOM 525 O ASP A 86 15.139 -27.933 -31.748 1.00 21.06 O ANISOU 525 O ASP A 86 2871 2819 2311 -641 -497 253 O ATOM 526 CB ASP A 86 12.329 -27.242 -33.321 1.00 20.93 C ANISOU 526 CB ASP A 86 2817 2869 2267 -717 -630 365 C ATOM 527 CG ASP A 86 11.497 -27.740 -34.491 1.00 26.77 C ANISOU 527 CG ASP A 86 3593 3624 2953 -778 -693 391 C ATOM 528 OD1 ASP A 86 12.097 -28.189 -35.497 1.00 27.04 O ANISOU 528 OD1 ASP A 86 3705 3638 2929 -804 -691 366 O ATOM 529 OD2 ASP A 86 10.248 -27.708 -34.384 1.00 21.67 O1- ANISOU 529 OD2 ASP A 86 2898 3014 2323 -801 -743 436 O1- ATOM 530 N VAL A 87 13.435 -27.320 -30.402 1.00 20.24 N ANISOU 530 N VAL A 87 2655 2754 2283 -627 -533 310 N ATOM 531 CA VAL A 87 14.236 -26.912 -29.252 1.00 18.98 C ANISOU 531 CA VAL A 87 2466 2579 2165 -578 -481 286 C ATOM 532 C VAL A 87 13.783 -27.738 -28.056 1.00 20.41 C ANISOU 532 C VAL A 87 2616 2764 2376 -578 -483 279 C ATOM 533 O VAL A 87 12.595 -27.722 -27.703 1.00 23.56 O ANISOU 533 O VAL A 87 2968 3190 2796 -589 -516 315 O ATOM 534 CB VAL A 87 14.077 -25.413 -28.963 1.00 20.06 C ANISOU 534 CB VAL A 87 2556 2725 2339 -538 -470 315 C ATOM 535 CG1 VAL A 87 14.861 -25.037 -27.722 1.00 20.97 C ANISOU 535 CG1 VAL A 87 2648 2824 2496 -493 -422 290 C ATOM 536 CG2 VAL A 87 14.572 -24.607 -30.157 1.00 16.39 C ANISOU 536 CG2 VAL A 87 2129 2256 1844 -541 -469 324 C ATOM 537 N ILE A 88 14.720 -28.451 -27.422 1.00 19.06 N ANISOU 537 N ILE A 88 2468 2568 2207 -565 -447 235 N ATOM 538 CA ILE A 88 14.360 -29.319 -26.311 1.00 18.94 C ANISOU 538 CA ILE A 88 2431 2552 2215 -568 -448 227 C ATOM 539 C ILE A 88 15.236 -29.020 -25.107 1.00 20.18 C ANISOU 539 C ILE A 88 2564 2694 2409 -520 -399 200 C ATOM 540 O ILE A 88 16.398 -28.620 -25.241 1.00 21.98 O ANISOU 540 O ILE A 88 2813 2906 2632 -495 -362 175 O ATOM 541 CB ILE A 88 14.457 -30.823 -26.672 1.00 18.75 C ANISOU 541 CB ILE A 88 2467 2508 2150 -609 -464 201 C ATOM 542 CG1 ILE A 88 15.907 -31.262 -26.862 1.00 19.55 C ANISOU 542 CG1 ILE A 88 2625 2575 2227 -588 -421 152 C ATOM 543 CG2 ILE A 88 13.668 -31.131 -27.925 1.00 18.36 C ANISOU 543 CG2 ILE A 88 2451 2469 2055 -663 -515 224 C ATOM 544 CD1 ILE A 88 16.043 -32.780 -27.115 1.00 20.37 C ANISOU 544 CD1 ILE A 88 2797 2652 2290 -619 -432 124 C ATOM 545 N GLY A 89 14.660 -29.199 -23.918 1.00 17.22 N ANISOU 545 N GLY A 89 2143 2329 2069 -510 -398 209 N ATOM 546 CA GLY A 89 15.461 -29.462 -22.740 1.00 18.11 C ANISOU 546 CA GLY A 89 2250 2425 2206 -479 -360 178 C ATOM 547 C GLY A 89 16.102 -30.833 -22.905 1.00 19.62 C ANISOU 547 C GLY A 89 2497 2591 2366 -498 -356 142 C ATOM 548 O GLY A 89 15.393 -31.826 -23.151 1.00 19.97 O ANISOU 548 O GLY A 89 2562 2635 2389 -539 -389 149 O ATOM 549 N ILE A 90 17.429 -30.904 -22.827 1.00 18.94 N ANISOU 549 N ILE A 90 2439 2483 2273 -471 -317 106 N ATOM 550 CA ILE A 90 18.123 -32.152 -23.177 1.00 19.15 C ANISOU 550 CA ILE A 90 2527 2484 2265 -482 -310 73 C ATOM 551 C ILE A 90 17.906 -33.182 -22.071 1.00 18.78 C ANISOU 551 C ILE A 90 2477 2426 2232 -484 -311 62 C ATOM 552 O ILE A 90 18.248 -32.920 -20.911 1.00 18.86 O ANISOU 552 O ILE A 90 2450 2438 2278 -452 -287 56 O ATOM 553 CB ILE A 90 19.620 -31.908 -23.446 1.00 17.65 C ANISOU 553 CB ILE A 90 2360 2283 2064 -448 -265 42 C ATOM 554 CG1 ILE A 90 19.784 -30.942 -24.631 1.00 23.66 C ANISOU 554 CG1 ILE A 90 3129 3054 2805 -453 -266 56 C ATOM 555 CG2 ILE A 90 20.316 -33.221 -23.807 1.00 20.66 C ANISOU 555 CG2 ILE A 90 2806 2637 2407 -449 -254 9 C ATOM 556 CD1 ILE A 90 21.216 -30.387 -24.826 1.00 17.24 C ANISOU 556 CD1 ILE A 90 2321 2240 1988 -421 -220 35 C ATOM 557 N PRO A 91 17.322 -34.345 -22.363 1.00 22.50 N ANISOU 557 N PRO A 91 2989 2884 2675 -523 -341 62 N ATOM 558 CA PRO A 91 17.149 -35.370 -21.325 1.00 23.10 C ANISOU 558 CA PRO A 91 3069 2946 2762 -528 -343 53 C ATOM 559 C PRO A 91 18.462 -36.077 -21.022 1.00 22.84 C ANISOU 559 C PRO A 91 3079 2881 2719 -493 -306 11 C ATOM 560 O PRO A 91 19.456 -35.937 -21.730 1.00 21.97 O ANISOU 560 O PRO A 91 3000 2761 2587 -470 -281 -10 O ATOM 561 CB PRO A 91 16.127 -36.339 -21.931 1.00 21.77 C ANISOU 561 CB PRO A 91 2939 2771 2561 -589 -392 67 C ATOM 562 CG PRO A 91 16.323 -36.195 -23.440 1.00 24.03 C ANISOU 562 CG PRO A 91 3277 3052 2804 -606 -403 62 C ATOM 563 CD PRO A 91 16.734 -34.750 -23.659 1.00 23.26 C ANISOU 563 CD PRO A 91 3133 2978 2728 -570 -379 72 C ATOM 564 N SER A 92 18.443 -36.845 -19.943 1.00 23.80 N ANISOU 564 N SER A 92 3198 2989 2855 -488 -303 4 N ATOM 565 CA SER A 92 19.637 -37.549 -19.504 1.00 26.02 C ANISOU 565 CA SER A 92 3513 3242 3131 -450 -269 -31 C ATOM 566 C SER A 92 20.162 -38.462 -20.607 1.00 26.83 C ANISOU 566 C SER A 92 3701 3312 3182 -456 -269 -56 C ATOM 567 O SER A 92 19.390 -39.176 -21.254 1.00 27.49 O ANISOU 567 O SER A 92 3832 3380 3233 -503 -304 -50 O ATOM 568 CB SER A 92 19.319 -38.363 -18.257 1.00 29.09 C ANISOU 568 CB SER A 92 3896 3619 3538 -453 -275 -30 C ATOM 569 OG SER A 92 20.244 -39.416 -18.130 1.00 37.72 O ANISOU 569 OG SER A 92 5046 4676 4610 -429 -256 -61 O ATOM 570 N MET A 93 21.473 -38.406 -20.853 1.00 26.84 N ANISOU 570 N MET A 93 3721 3306 3174 -410 -228 -83 N ATOM 571 CA MET A 93 22.130 -39.298 -21.806 1.00 26.93 C ANISOU 571 CA MET A 93 3814 3284 3134 -401 -217 -111 C ATOM 572 C MET A 93 23.630 -39.131 -21.634 1.00 27.19 C ANISOU 572 C MET A 93 3839 3321 3172 -338 -165 -134 C ATOM 573 O MET A 93 24.099 -38.183 -21.004 1.00 26.94 O ANISOU 573 O MET A 93 3739 3318 3178 -313 -144 -126 O ATOM 574 CB MET A 93 21.776 -39.006 -23.271 1.00 30.08 C ANISOU 574 CB MET A 93 4249 3687 3492 -433 -234 -105 C ATOM 575 CG MET A 93 21.898 -37.531 -23.664 1.00 26.99 C ANISOU 575 CG MET A 93 3799 3335 3120 -426 -224 -87 C ATOM 576 SD MET A 93 21.571 -37.242 -25.418 1.00 32.61 S ANISOU 576 SD MET A 93 4562 4051 3779 -461 -243 -81 S ATOM 577 CE MET A 93 19.772 -37.065 -25.423 1.00 25.56 C ANISOU 577 CE MET A 93 3642 3172 2896 -529 -309 -40 C ATOM 578 N LEU A 94 24.379 -40.034 -22.255 1.00 31.18 N ANISOU 578 N LEU A 94 4414 3796 3635 -314 -144 -161 N ATOM 579 CA LEU A 94 25.829 -39.955 -22.208 1.00 26.72 C ANISOU 579 CA LEU A 94 3841 3240 3071 -252 -93 -180 C ATOM 580 C LEU A 94 26.329 -38.950 -23.240 1.00 26.78 C ANISOU 580 C LEU A 94 3832 3278 3065 -246 -72 -176 C ATOM 581 O LEU A 94 25.755 -38.838 -24.334 1.00 26.04 O ANISOU 581 O LEU A 94 3776 3180 2937 -282 -91 -171 O ATOM 582 CB LEU A 94 26.440 -41.318 -22.500 1.00 27.03 C ANISOU 582 CB LEU A 94 3965 3238 3069 -220 -75 -209 C ATOM 583 CG LEU A 94 25.924 -42.462 -21.628 1.00 27.90 C ANISOU 583 CG LEU A 94 4110 3307 3182 -230 -99 -213 C ATOM 584 CD1 LEU A 94 26.308 -43.784 -22.262 1.00 28.39 C ANISOU 584 CD1 LEU A 94 4279 3318 3191 -209 -89 -242 C ATOM 585 CD2 LEU A 94 26.474 -42.344 -20.210 1.00 26.76 C ANISOU 585 CD2 LEU A 94 3903 3178 3087 -192 -82 -209 C ATOM 586 N PRO A 95 27.410 -38.223 -22.929 1.00 24.83 N ANISOU 586 N PRO A 95 3529 3062 2841 -206 -33 -176 N ATOM 587 CA PRO A 95 27.949 -37.287 -23.921 1.00 23.08 C ANISOU 587 CA PRO A 95 3294 2871 2604 -203 -10 -170 C ATOM 588 C PRO A 95 28.266 -37.942 -25.249 1.00 26.19 C ANISOU 588 C PRO A 95 3767 3247 2937 -196 6 -188 C ATOM 589 O PRO A 95 28.072 -37.307 -26.295 1.00 23.63 O ANISOU 589 O PRO A 95 3454 2936 2588 -220 2 -179 O ATOM 590 CB PRO A 95 29.191 -36.718 -23.227 1.00 26.45 C ANISOU 590 CB PRO A 95 3657 3330 3062 -159 30 -169 C ATOM 591 CG PRO A 95 28.880 -36.831 -21.755 1.00 26.85 C ANISOU 591 CG PRO A 95 3667 3377 3159 -157 13 -164 C ATOM 592 CD PRO A 95 28.102 -38.118 -21.627 1.00 25.82 C ANISOU 592 CD PRO A 95 3599 3203 3010 -169 -14 -176 C ATOM 593 N SER A 96 28.683 -39.216 -25.247 1.00 26.63 N ANISOU 593 N SER A 96 3886 3269 2964 -163 21 -214 N ATOM 594 CA SER A 96 28.941 -39.922 -26.496 1.00 25.87 C ANISOU 594 CA SER A 96 3878 3149 2803 -153 37 -235 C ATOM 595 C SER A 96 27.691 -40.066 -27.351 1.00 26.72 C ANISOU 595 C SER A 96 4043 3232 2875 -217 -11 -230 C ATOM 596 O SER A 96 27.811 -40.421 -28.527 1.00 27.28 O ANISOU 596 O SER A 96 4188 3289 2890 -220 -2 -244 O ATOM 597 CB SER A 96 29.527 -41.306 -26.214 1.00 28.33 C ANISOU 597 CB SER A 96 4252 3421 3092 -104 60 -263 C ATOM 598 OG SER A 96 28.572 -42.117 -25.545 1.00 29.95 O ANISOU 598 OG SER A 96 4490 3585 3305 -136 16 -264 O ATOM 599 N GLN A 97 26.508 -39.787 -26.797 1.00 27.18 N ANISOU 599 N GLN A 97 4070 3291 2965 -269 -61 -208 N ATOM 600 CA GLN A 97 25.245 -39.889 -27.513 1.00 24.74 C ANISOU 600 CA GLN A 97 3804 2968 2629 -335 -114 -196 C ATOM 601 C GLN A 97 24.702 -38.548 -28.001 1.00 26.84 C ANISOU 601 C GLN A 97 4015 3273 2909 -370 -133 -166 C ATOM 602 O GLN A 97 23.734 -38.546 -28.765 1.00 28.25 O ANISOU 602 O GLN A 97 4227 3446 3060 -422 -175 -153 O ATOM 603 CB GLN A 97 24.174 -40.530 -26.620 1.00 25.40 C ANISOU 603 CB GLN A 97 3887 3028 2735 -373 -160 -187 C ATOM 604 CG GLN A 97 24.457 -41.935 -26.139 1.00 27.93 C ANISOU 604 CG GLN A 97 4274 3301 3039 -351 -153 -213 C ATOM 605 CD GLN A 97 23.359 -42.439 -25.192 1.00 28.39 C ANISOU 605 CD GLN A 97 4321 3343 3122 -396 -200 -197 C ATOM 606 NE2 GLN A 97 22.446 -43.234 -25.735 1.00 30.73 N ANISOU 606 NE2 GLN A 97 4691 3606 3379 -452 -244 -197 N ATOM 607 OE1 GLN A 97 23.325 -42.104 -24.003 1.00 27.99 O ANISOU 607 OE1 GLN A 97 4199 3312 3125 -383 -197 -184 O ATOM 608 N TYR A 98 25.263 -37.416 -27.554 1.00 24.69 N ANISOU 608 N TYR A 98 3662 3039 2680 -344 -107 -152 N ATOM 609 CA TYR A 98 24.761 -36.104 -27.976 1.00 26.57 C ANISOU 609 CA TYR A 98 3853 3310 2933 -374 -124 -122 C ATOM 610 C TYR A 98 24.612 -36.015 -29.494 1.00 28.17 C ANISOU 610 C TYR A 98 4114 3511 3077 -399 -132 -121 C ATOM 611 O TYR A 98 23.564 -35.596 -30.005 1.00 25.58 O ANISOU 611 O TYR A 98 3787 3190 2742 -447 -177 -97 O ATOM 612 CB TYR A 98 25.700 -34.999 -27.497 1.00 24.40 C ANISOU 612 CB TYR A 98 3505 3069 2697 -338 -85 -114 C ATOM 613 CG TYR A 98 25.724 -34.812 -26.009 1.00 23.94 C ANISOU 613 CG TYR A 98 3382 3017 2696 -321 -84 -109 C ATOM 614 CD1 TYR A 98 24.663 -35.240 -25.212 1.00 23.21 C ANISOU 614 CD1 TYR A 98 3280 2910 2627 -345 -122 -100 C ATOM 615 CD2 TYR A 98 26.811 -34.201 -25.397 1.00 22.93 C ANISOU 615 CD2 TYR A 98 3202 2912 2599 -284 -45 -111 C ATOM 616 CE1 TYR A 98 24.692 -35.061 -23.834 1.00 23.32 C ANISOU 616 CE1 TYR A 98 3239 2931 2692 -328 -119 -96 C ATOM 617 CE2 TYR A 98 26.852 -34.009 -24.036 1.00 23.02 C ANISOU 617 CE2 TYR A 98 3159 2929 2659 -270 -46 -107 C ATOM 618 CZ TYR A 98 25.797 -34.437 -23.256 1.00 25.40 C ANISOU 618 CZ TYR A 98 3455 3214 2981 -290 -81 -101 C ATOM 619 OH TYR A 98 25.870 -34.235 -21.898 1.00 24.49 O ANISOU 619 OH TYR A 98 3290 3104 2910 -274 -78 -97 O ATOM 620 N GLU A 99 25.666 -36.421 -30.225 1.00 28.15 N ANISOU 620 N GLU A 99 4162 3501 3031 -366 -89 -146 N ATOM 621 CA GLU A 99 25.677 -36.374 -31.688 1.00 27.76 C ANISOU 621 CA GLU A 99 4176 3451 2920 -384 -88 -148 C ATOM 622 C GLU A 99 24.496 -37.109 -32.296 1.00 28.63 C ANISOU 622 C GLU A 99 4358 3531 2989 -439 -144 -148 C ATOM 623 O GLU A 99 24.021 -36.738 -33.373 1.00 27.45 O ANISOU 623 O GLU A 99 4240 3388 2801 -476 -167 -135 O ATOM 624 CB GLU A 99 26.972 -36.995 -32.226 1.00 32.49 C ANISOU 624 CB GLU A 99 4828 4043 3475 -332 -28 -180 C ATOM 625 CG GLU A 99 27.794 -36.107 -33.160 1.00 37.76 C ANISOU 625 CG GLU A 99 5484 4744 4119 -318 12 -172 C ATOM 626 CD GLU A 99 29.053 -36.808 -33.692 1.00 42.19 C ANISOU 626 CD GLU A 99 6096 5302 4634 -261 75 -202 C ATOM 627 OE1 GLU A 99 29.061 -37.175 -34.883 1.00 44.86 O ANISOU 627 OE1 GLU A 99 6514 5626 4904 -269 82 -215 O ATOM 628 OE2 GLU A 99 30.039 -36.983 -32.932 1.00 43.87 O1- ANISOU 628 OE2 GLU A 99 6267 5527 4874 -207 118 -212 O1- ATOM 629 N GLN A 100 24.030 -38.171 -31.644 1.00 26.93 N ANISOU 629 N GLN A 100 4172 3282 2778 -449 -167 -161 N ATOM 630 CA GLN A 100 22.970 -38.977 -32.228 1.00 29.81 C ANISOU 630 CA GLN A 100 4612 3615 3098 -507 -221 -161 C ATOM 631 C GLN A 100 21.636 -38.238 -32.258 1.00 28.40 C ANISOU 631 C GLN A 100 4384 3463 2943 -568 -282 -119 C ATOM 632 O GLN A 100 20.765 -38.574 -33.069 1.00 30.41 O ANISOU 632 O GLN A 100 4693 3706 3154 -624 -330 -110 O ATOM 633 CB GLN A 100 22.854 -40.292 -31.444 1.00 30.10 C ANISOU 633 CB GLN A 100 4692 3609 3136 -503 -229 -183 C ATOM 634 CG GLN A 100 21.524 -41.005 -31.587 1.00 35.33 C ANISOU 634 CG GLN A 100 5402 4245 3776 -576 -298 -171 C ATOM 635 CD GLN A 100 21.617 -42.500 -31.322 1.00 43.30 C ANISOU 635 CD GLN A 100 6502 5196 4754 -574 -300 -202 C ATOM 636 NE2 GLN A 100 20.842 -43.287 -32.072 1.00 42.84 N ANISOU 636 NE2 GLN A 100 6535 5103 4639 -635 -348 -206 N ATOM 637 OE1 GLN A 100 22.380 -42.941 -30.456 1.00 41.42 O ANISOU 637 OE1 GLN A 100 6254 4943 4541 -520 -262 -221 O ATOM 638 N PHE A 101 21.460 -37.235 -31.405 1.00 25.51 N ANISOU 638 N PHE A 101 3918 3132 2642 -557 -281 -92 N ATOM 639 CA PHE A 101 20.177 -36.576 -31.225 1.00 26.15 C ANISOU 639 CA PHE A 101 3944 3240 2754 -604 -334 -51 C ATOM 640 C PHE A 101 20.219 -35.073 -31.438 1.00 25.13 C ANISOU 640 C PHE A 101 3747 3150 2652 -593 -326 -22 C ATOM 641 O PHE A 101 19.176 -34.485 -31.740 1.00 21.71 O ANISOU 641 O PHE A 101 3286 2738 2226 -632 -371 14 O ATOM 642 CB PHE A 101 19.630 -36.840 -29.811 1.00 25.49 C ANISOU 642 CB PHE A 101 3803 3156 2725 -604 -349 -41 C ATOM 643 CG PHE A 101 19.478 -38.302 -29.463 1.00 28.90 C ANISOU 643 CG PHE A 101 4298 3547 3135 -620 -362 -64 C ATOM 644 CD1 PHE A 101 18.441 -39.062 -30.013 1.00 28.36 C ANISOU 644 CD1 PHE A 101 4285 3462 3028 -685 -418 -55 C ATOM 645 CD2 PHE A 101 20.348 -38.909 -28.567 1.00 27.19 C ANISOU 645 CD2 PHE A 101 4086 3309 2937 -572 -321 -93 C ATOM 646 CE1 PHE A 101 18.286 -40.408 -29.682 1.00 26.23 C ANISOU 646 CE1 PHE A 101 4080 3148 2736 -704 -433 -75 C ATOM 647 CE2 PHE A 101 20.211 -40.253 -28.242 1.00 29.64 C ANISOU 647 CE2 PHE A 101 4459 3576 3226 -584 -334 -113 C ATOM 648 CZ PHE A 101 19.174 -41.004 -28.800 1.00 26.20 C ANISOU 648 CZ PHE A 101 4085 3119 2751 -652 -389 -104 C ATOM 649 N LEU A 102 21.384 -34.441 -31.308 1.00 24.36 N ANISOU 649 N LEU A 102 3623 3063 2570 -544 -272 -34 N ATOM 650 CA LEU A 102 21.490 -32.993 -31.178 1.00 23.06 C ANISOU 650 CA LEU A 102 3388 2931 2442 -531 -261 -7 C ATOM 651 C LEU A 102 22.424 -32.415 -32.234 1.00 25.41 C ANISOU 651 C LEU A 102 3711 3238 2704 -516 -226 -12 C ATOM 652 O LEU A 102 23.485 -32.977 -32.517 1.00 21.28 O ANISOU 652 O LEU A 102 3229 2705 2152 -487 -182 -43 O ATOM 653 CB LEU A 102 22.009 -32.606 -29.784 1.00 20.65 C ANISOU 653 CB LEU A 102 3012 2633 2199 -490 -231 -10 C ATOM 654 CG LEU A 102 21.152 -33.138 -28.632 1.00 23.31 C ANISOU 654 CG LEU A 102 3319 2963 2574 -501 -259 -4 C ATOM 655 CD1 LEU A 102 21.828 -32.871 -27.317 1.00 23.04 C ANISOU 655 CD1 LEU A 102 3230 2933 2591 -458 -225 -14 C ATOM 656 CD2 LEU A 102 19.763 -32.502 -28.668 1.00 20.33 C ANISOU 656 CD2 LEU A 102 2904 2606 2216 -537 -310 37 C ATOM 657 N GLU A 103 22.020 -31.281 -32.791 1.00 22.85 N ANISOU 657 N GLU A 103 3362 2936 2383 -535 -244 20 N ATOM 658 CA GLU A 103 22.841 -30.545 -33.737 1.00 22.00 C ANISOU 658 CA GLU A 103 3271 2843 2247 -525 -212 23 C ATOM 659 C GLU A 103 24.010 -29.860 -33.017 1.00 22.73 C ANISOU 659 C GLU A 103 3309 2948 2377 -482 -158 17 C ATOM 660 O GLU A 103 23.825 -29.274 -31.948 1.00 18.98 O ANISOU 660 O GLU A 103 2772 2480 1960 -471 -162 29 O ATOM 661 CB GLU A 103 21.969 -29.501 -34.434 1.00 22.21 C ANISOU 661 CB GLU A 103 3283 2885 2269 -558 -252 65 C ATOM 662 CG GLU A 103 22.612 -28.761 -35.579 1.00 22.45 C ANISOU 662 CG GLU A 103 3341 2929 2261 -560 -229 73 C ATOM 663 CD GLU A 103 22.746 -29.583 -36.841 1.00 24.86 C ANISOU 663 CD GLU A 103 3733 3223 2488 -580 -230 55 C ATOM 664 OE1 GLU A 103 22.214 -30.714 -36.919 1.00 25.39 O ANISOU 664 OE1 GLU A 103 3848 3269 2528 -599 -257 38 O ATOM 665 OE2 GLU A 103 23.390 -29.082 -37.775 1.00 24.98 O1- ANISOU 665 OE2 GLU A 103 3776 3250 2467 -579 -204 59 O1- ATOM 666 N PRO A 104 25.224 -29.904 -33.576 1.00 22.56 N ANISOU 666 N PRO A 104 3313 2934 2325 -459 -108 -1 N ATOM 667 CA PRO A 104 26.320 -29.107 -33.000 1.00 19.35 C ANISOU 667 CA PRO A 104 2851 2548 1954 -428 -63 1 C ATOM 668 C PRO A 104 25.943 -27.634 -32.966 1.00 22.22 C ANISOU 668 C PRO A 104 3169 2926 2349 -446 -81 38 C ATOM 669 O PRO A 104 25.458 -27.082 -33.953 1.00 22.11 O ANISOU 669 O PRO A 104 3179 2916 2306 -474 -102 60 O ATOM 670 CB PRO A 104 27.493 -29.358 -33.956 1.00 21.87 C ANISOU 670 CB PRO A 104 3210 2878 2220 -411 -12 -16 C ATOM 671 CG PRO A 104 27.161 -30.635 -34.658 1.00 25.95 C ANISOU 671 CG PRO A 104 3807 3371 2681 -416 -23 -41 C ATOM 672 CD PRO A 104 25.653 -30.679 -34.753 1.00 22.63 C ANISOU 672 CD PRO A 104 3401 2935 2264 -461 -90 -23 C ATOM 673 N LEU A 105 26.178 -26.993 -31.823 1.00 21.52 N ANISOU 673 N LEU A 105 3017 2842 2316 -430 -72 44 N ATOM 674 CA LEU A 105 25.926 -25.565 -31.666 1.00 21.24 C ANISOU 674 CA LEU A 105 2944 2814 2312 -441 -84 77 C ATOM 675 C LEU A 105 27.173 -24.726 -31.887 1.00 22.72 C ANISOU 675 C LEU A 105 3115 3020 2497 -435 -41 82 C ATOM 676 O LEU A 105 27.102 -23.494 -31.822 1.00 20.64 O ANISOU 676 O LEU A 105 2829 2760 2256 -446 -48 109 O ATOM 677 CB LEU A 105 25.360 -25.277 -30.275 1.00 22.17 C ANISOU 677 CB LEU A 105 3010 2924 2490 -430 -103 82 C ATOM 678 CG LEU A 105 24.115 -26.087 -29.919 1.00 20.62 C ANISOU 678 CG LEU A 105 2819 2715 2301 -438 -144 82 C ATOM 679 CD1 LEU A 105 23.621 -25.706 -28.535 1.00 17.72 C ANISOU 679 CD1 LEU A 105 2399 2344 1991 -424 -155 89 C ATOM 680 CD2 LEU A 105 23.027 -25.843 -30.984 1.00 18.02 C ANISOU 680 CD2 LEU A 105 2518 2388 1943 -470 -187 109 C ATOM 681 N GLY A 106 28.305 -25.361 -32.144 1.00 23.34 N ANISOU 681 N GLY A 106 3206 3112 2549 -417 3 59 N ATOM 682 CA GLY A 106 29.570 -24.682 -32.308 1.00 24.08 C ANISOU 682 CA GLY A 106 3278 3232 2641 -412 47 65 C ATOM 683 C GLY A 106 30.646 -25.350 -31.489 1.00 25.98 C ANISOU 683 C GLY A 106 3488 3485 2897 -378 87 41 C ATOM 684 O GLY A 106 30.427 -26.357 -30.817 1.00 23.00 O ANISOU 684 O GLY A 106 3114 3094 2532 -356 81 17 O ATOM 685 N GLU A 107 31.832 -24.765 -31.557 1.00 26.04 N ANISOU 685 N GLU A 107 3467 3522 2905 -376 126 49 N ATOM 686 CA GLU A 107 32.995 -25.251 -30.834 1.00 28.35 C ANISOU 686 CA GLU A 107 3721 3837 3212 -344 166 33 C ATOM 687 C GLU A 107 32.984 -24.740 -29.400 1.00 26.83 C ANISOU 687 C GLU A 107 3474 3639 3079 -345 149 37 C ATOM 688 O GLU A 107 32.867 -23.529 -29.166 1.00 26.62 O ANISOU 688 O GLU A 107 3425 3610 3077 -372 134 61 O ATOM 689 CB GLU A 107 34.262 -24.792 -31.556 1.00 30.35 C ANISOU 689 CB GLU A 107 3960 4133 3439 -347 214 47 C ATOM 690 CG GLU A 107 35.546 -25.114 -30.862 1.00 32.43 C ANISOU 690 CG GLU A 107 4172 4430 3719 -317 255 39 C ATOM 691 CD GLU A 107 36.740 -24.500 -31.587 1.00 38.88 C ANISOU 691 CD GLU A 107 4966 5295 4512 -328 300 61 C ATOM 692 OE1 GLU A 107 37.089 -24.920 -32.716 1.00 39.67 O ANISOU 692 OE1 GLU A 107 5101 5413 4560 -316 333 58 O ATOM 693 OE2 GLU A 107 37.272 -23.517 -31.042 1.00 40.08 O1- ANISOU 693 OE2 GLU A 107 5069 5466 4695 -353 300 83 O1- ATOM 694 N THR A 108 33.128 -25.670 -28.448 1.00 24.59 N ANISOU 694 N THR A 108 3176 3351 2818 -313 153 14 N ATOM 695 CA THR A 108 33.106 -25.339 -27.020 1.00 23.72 C ANISOU 695 CA THR A 108 3019 3234 2759 -311 137 15 C ATOM 696 C THR A 108 34.080 -24.213 -26.663 1.00 28.29 C ANISOU 696 C THR A 108 3550 3840 3358 -329 154 35 C ATOM 697 O THR A 108 33.694 -23.227 -26.023 1.00 24.11 O ANISOU 697 O THR A 108 3005 3296 2861 -351 129 49 O ATOM 698 CB THR A 108 33.406 -26.597 -26.195 1.00 23.08 C ANISOU 698 CB THR A 108 2929 3151 2687 -271 148 -12 C ATOM 699 CG2 THR A 108 33.491 -26.286 -24.713 1.00 20.70 C ANISOU 699 CG2 THR A 108 2582 2848 2437 -269 134 -12 C ATOM 700 OG1 THR A 108 32.379 -27.577 -26.422 1.00 21.05 O ANISOU 700 OG1 THR A 108 2720 2863 2414 -264 125 -28 O ATOM 701 N GLU A 109 35.350 -24.341 -27.060 1.00 28.18 N ANISOU 701 N GLU A 109 3516 3866 3325 -319 196 38 N ATOM 702 CA GLU A 109 36.331 -23.330 -26.674 1.00 30.00 C ANISOU 702 CA GLU A 109 3698 4127 3575 -342 210 59 C ATOM 703 C GLU A 109 35.931 -21.954 -27.175 1.00 30.45 C ANISOU 703 C GLU A 109 3768 4171 3631 -389 191 87 C ATOM 704 O GLU A 109 36.061 -20.959 -26.452 1.00 29.40 O ANISOU 704 O GLU A 109 3610 4031 3527 -416 175 101 O ATOM 705 CB GLU A 109 37.718 -23.706 -27.188 1.00 32.88 C ANISOU 705 CB GLU A 109 4035 4544 3914 -325 260 63 C ATOM 706 CG GLU A 109 38.392 -24.780 -26.355 1.00 36.92 C ANISOU 706 CG GLU A 109 4514 5074 4438 -279 279 44 C ATOM 707 CD GLU A 109 38.817 -24.259 -24.995 1.00 44.02 C ANISOU 707 CD GLU A 109 5360 5983 5384 -292 263 52 C ATOM 708 OE1 GLU A 109 38.503 -24.920 -23.980 1.00 48.05 O ANISOU 708 OE1 GLU A 109 5865 6474 5919 -267 246 33 O ATOM 709 OE2 GLU A 109 39.469 -23.185 -24.953 1.00 44.22 O1- ANISOU 709 OE2 GLU A 109 5351 6033 5417 -331 266 78 O1- ATOM 710 N GLU A 110 35.411 -21.876 -28.398 1.00 28.83 N ANISOU 710 N GLU A 110 3608 3958 3390 -400 189 94 N ATOM 711 CA GLU A 110 35.034 -20.574 -28.923 1.00 32.78 C ANISOU 711 CA GLU A 110 4124 4444 3887 -441 171 122 C ATOM 712 C GLU A 110 33.760 -20.067 -28.254 1.00 30.21 C ANISOU 712 C GLU A 110 3813 4072 3594 -448 123 125 C ATOM 713 O GLU A 110 33.637 -18.867 -27.961 1.00 25.77 O ANISOU 713 O GLU A 110 3246 3493 3051 -475 106 146 O ATOM 714 CB GLU A 110 34.882 -20.651 -30.438 1.00 33.56 C ANISOU 714 CB GLU A 110 4267 4551 3934 -450 183 132 C ATOM 715 CG GLU A 110 34.816 -19.300 -31.112 1.00 43.94 C ANISOU 715 CG GLU A 110 5596 5860 5238 -494 174 166 C ATOM 716 CD GLU A 110 34.021 -19.332 -32.400 1.00 47.90 C ANISOU 716 CD GLU A 110 6153 6349 5697 -502 161 175 C ATOM 717 OE1 GLU A 110 33.982 -20.413 -33.041 1.00 44.94 O ANISOU 717 OE1 GLU A 110 5804 5984 5286 -479 177 155 O ATOM 718 OE2 GLU A 110 33.461 -18.274 -32.778 1.00 45.99 O1- ANISOU 718 OE2 GLU A 110 5932 6086 5455 -532 136 202 O1- ATOM 719 N LEU A 111 32.822 -20.972 -27.962 1.00 24.72 N ANISOU 719 N LEU A 111 3134 3356 2905 -422 103 104 N ATOM 720 CA LEU A 111 31.615 -20.567 -27.246 1.00 25.22 C ANISOU 720 CA LEU A 111 3201 3382 3000 -422 62 107 C ATOM 721 C LEU A 111 31.936 -20.095 -25.837 1.00 24.01 C ANISOU 721 C LEU A 111 3011 3222 2890 -420 58 104 C ATOM 722 O LEU A 111 31.183 -19.289 -25.278 1.00 22.84 O ANISOU 722 O LEU A 111 2866 3045 2767 -427 31 115 O ATOM 723 CB LEU A 111 30.600 -21.722 -27.220 1.00 21.59 C ANISOU 723 CB LEU A 111 2762 2907 2535 -399 42 88 C ATOM 724 CG LEU A 111 29.814 -21.955 -28.527 1.00 24.35 C ANISOU 724 CG LEU A 111 3156 3250 2845 -410 27 97 C ATOM 725 CD1 LEU A 111 29.178 -23.335 -28.584 1.00 19.20 C ANISOU 725 CD1 LEU A 111 2528 2590 2179 -393 15 74 C ATOM 726 CD2 LEU A 111 28.732 -20.907 -28.719 1.00 17.45 C ANISOU 726 CD2 LEU A 111 2294 2355 1983 -428 -10 125 C ATOM 727 N ALA A 112 33.056 -20.545 -25.262 1.00 24.88 N ANISOU 727 N ALA A 112 3088 3359 3007 -411 84 91 N ATOM 728 CA ALA A 112 33.411 -20.113 -23.914 1.00 23.65 C ANISOU 728 CA ALA A 112 2899 3198 2888 -413 78 88 C ATOM 729 C ALA A 112 33.804 -18.643 -23.851 1.00 22.98 C ANISOU 729 C ALA A 112 2812 3107 2812 -452 73 113 C ATOM 730 O ALA A 112 33.924 -18.093 -22.751 1.00 21.53 O ANISOU 730 O ALA A 112 2614 2910 2657 -460 60 112 O ATOM 731 CB ALA A 112 34.544 -20.985 -23.357 1.00 23.58 C ANISOU 731 CB ALA A 112 2852 3224 2882 -393 105 72 C ATOM 732 N ASP A 113 34.013 -17.993 -24.989 1.00 24.38 N ANISOU 732 N ASP A 113 3009 3292 2963 -478 81 135 N ATOM 733 CA ASP A 113 34.222 -16.551 -24.963 1.00 24.99 C ANISOU 733 CA ASP A 113 3095 3354 3047 -518 71 161 C ATOM 734 C ASP A 113 32.955 -15.818 -24.555 1.00 24.71 C ANISOU 734 C ASP A 113 3090 3266 3031 -514 36 167 C ATOM 735 O ASP A 113 33.023 -14.668 -24.113 1.00 26.99 O ANISOU 735 O ASP A 113 3391 3529 3334 -538 23 181 O ATOM 736 CB ASP A 113 34.713 -16.081 -26.335 1.00 22.57 C ANISOU 736 CB ASP A 113 2804 3068 2704 -548 89 186 C ATOM 737 CG ASP A 113 36.185 -16.431 -26.576 1.00 29.47 C ANISOU 737 CG ASP A 113 3638 3997 3561 -559 128 189 C ATOM 738 OD1 ASP A 113 36.874 -16.844 -25.618 1.00 26.86 O ANISOU 738 OD1 ASP A 113 3267 3687 3252 -550 137 176 O ATOM 739 OD2 ASP A 113 36.644 -16.315 -27.732 1.00 34.86 O1- ANISOU 739 OD2 ASP A 113 4330 4706 4210 -576 152 205 O1- ATOM 740 N THR A 114 31.809 -16.469 -24.662 1.00 22.98 N ANISOU 740 N THR A 114 2885 3032 2814 -483 20 156 N ATOM 741 CA THR A 114 30.513 -15.847 -24.455 1.00 20.15 C ANISOU 741 CA THR A 114 2553 2633 2471 -472 -11 167 C ATOM 742 C THR A 114 29.703 -16.482 -23.333 1.00 21.41 C ANISOU 742 C THR A 114 2698 2778 2659 -438 -26 146 C ATOM 743 O THR A 114 29.049 -15.760 -22.569 1.00 20.96 O ANISOU 743 O THR A 114 2648 2689 2625 -429 -43 151 O ATOM 744 CB THR A 114 29.697 -15.918 -25.767 1.00 21.39 C ANISOU 744 CB THR A 114 2740 2788 2601 -472 -23 183 C ATOM 745 CG2 THR A 114 28.371 -15.218 -25.608 1.00 18.96 C ANISOU 745 CG2 THR A 114 2451 2443 2309 -458 -55 200 C ATOM 746 OG1 THR A 114 30.440 -15.315 -26.834 1.00 22.72 O ANISOU 746 OG1 THR A 114 2923 2969 2739 -504 -8 204 O ATOM 747 N TYR A 115 29.720 -17.813 -23.221 1.00 19.42 N ANISOU 747 N TYR A 115 2428 2547 2403 -417 -18 124 N ATOM 748 CA TYR A 115 28.787 -18.566 -22.387 1.00 18.34 C ANISOU 748 CA TYR A 115 2282 2399 2286 -388 -33 109 C ATOM 749 C TYR A 115 29.523 -19.350 -21.308 1.00 19.06 C ANISOU 749 C TYR A 115 2344 2504 2393 -375 -18 83 C ATOM 750 O TYR A 115 30.640 -19.824 -21.520 1.00 21.87 O ANISOU 750 O TYR A 115 2686 2888 2736 -380 5 75 O ATOM 751 CB TYR A 115 27.979 -19.552 -23.235 1.00 17.47 C ANISOU 751 CB TYR A 115 2186 2297 2156 -378 -43 107 C ATOM 752 CG TYR A 115 27.129 -18.905 -24.301 1.00 19.09 C ANISOU 752 CG TYR A 115 2418 2492 2345 -389 -63 133 C ATOM 753 CD1 TYR A 115 25.993 -18.170 -23.967 1.00 20.78 C ANISOU 753 CD1 TYR A 115 2635 2681 2578 -379 -89 152 C ATOM 754 CD2 TYR A 115 27.453 -19.042 -25.646 1.00 18.99 C ANISOU 754 CD2 TYR A 115 2428 2494 2293 -407 -56 141 C ATOM 755 CE1 TYR A 115 25.203 -17.588 -24.948 1.00 21.40 C ANISOU 755 CE1 TYR A 115 2735 2753 2641 -386 -109 180 C ATOM 756 CE2 TYR A 115 26.672 -18.460 -26.635 1.00 18.87 C ANISOU 756 CE2 TYR A 115 2438 2470 2260 -418 -77 168 C ATOM 757 CZ TYR A 115 25.552 -17.747 -26.282 1.00 20.95 C ANISOU 757 CZ TYR A 115 2702 2712 2547 -408 -105 188 C ATOM 758 OH TYR A 115 24.773 -17.187 -27.263 1.00 23.38 O ANISOU 758 OH TYR A 115 3033 3013 2838 -416 -129 218 O ATOM 759 N ARG A 116 28.879 -19.514 -20.160 1.00 19.50 N ANISOU 759 N ARG A 116 2391 2545 2475 -355 -31 74 N ATOM 760 CA ARG A 116 29.393 -20.387 -19.120 1.00 19.82 C ANISOU 760 CA ARG A 116 2407 2596 2528 -340 -22 51 C ATOM 761 C ARG A 116 28.557 -21.671 -19.078 1.00 20.52 C ANISOU 761 C ARG A 116 2497 2686 2615 -317 -30 38 C ATOM 762 O ARG A 116 27.723 -21.912 -19.948 1.00 19.03 O ANISOU 762 O ARG A 116 2327 2494 2411 -319 -42 47 O ATOM 763 CB ARG A 116 29.385 -19.694 -17.754 1.00 19.92 C ANISOU 763 CB ARG A 116 2411 2590 2568 -337 -29 47 C ATOM 764 CG ARG A 116 28.024 -19.185 -17.278 1.00 18.39 C ANISOU 764 CG ARG A 116 2230 2366 2390 -321 -49 56 C ATOM 765 CD ARG A 116 28.056 -19.000 -15.774 1.00 18.69 C ANISOU 765 CD ARG A 116 2259 2391 2450 -310 -50 43 C ATOM 766 NE ARG A 116 29.001 -17.975 -15.356 1.00 20.08 N ANISOU 766 NE ARG A 116 2442 2558 2628 -333 -46 45 N ATOM 767 CZ ARG A 116 28.787 -16.666 -15.423 1.00 20.38 C ANISOU 767 CZ ARG A 116 2508 2568 2669 -344 -53 60 C ATOM 768 NH1 ARG A 116 27.636 -16.171 -15.841 1.00 18.07 N1+ ANISOU 768 NH1 ARG A 116 2235 2252 2377 -328 -64 75 N1+ ATOM 769 NH2 ARG A 116 29.743 -15.833 -15.020 1.00 22.82 N ANISOU 769 NH2 ARG A 116 2826 2868 2977 -373 -52 60 N ATOM 770 N PHE A 117 28.774 -22.500 -18.045 1.00 19.05 N ANISOU 770 N PHE A 117 2294 2504 2442 -300 -26 19 N ATOM 771 CA PHE A 117 28.052 -23.767 -17.848 1.00 19.19 C ANISOU 771 CA PHE A 117 2315 2519 2458 -282 -34 7 C ATOM 772 C PHE A 117 28.234 -24.737 -19.017 1.00 20.36 C ANISOU 772 C PHE A 117 2483 2678 2574 -283 -27 1 C ATOM 773 O PHE A 117 27.342 -25.537 -19.318 1.00 18.89 O ANISOU 773 O PHE A 117 2314 2484 2378 -281 -42 -1 O ATOM 774 CB PHE A 117 26.556 -23.534 -17.607 1.00 17.36 C ANISOU 774 CB PHE A 117 2088 2270 2239 -279 -59 20 C ATOM 775 CG PHE A 117 26.255 -22.657 -16.416 1.00 20.18 C ANISOU 775 CG PHE A 117 2432 2612 2623 -271 -63 24 C ATOM 776 CD1 PHE A 117 26.850 -22.903 -15.185 1.00 19.60 C ANISOU 776 CD1 PHE A 117 2344 2540 2565 -261 -54 8 C ATOM 777 CD2 PHE A 117 25.377 -21.587 -16.535 1.00 20.59 C ANISOU 777 CD2 PHE A 117 2491 2649 2684 -270 -76 45 C ATOM 778 CE1 PHE A 117 26.564 -22.086 -14.088 1.00 20.20 C ANISOU 778 CE1 PHE A 117 2416 2600 2660 -253 -58 10 C ATOM 779 CE2 PHE A 117 25.084 -20.775 -15.449 1.00 18.73 C ANISOU 779 CE2 PHE A 117 2252 2396 2470 -257 -76 47 C ATOM 780 CZ PHE A 117 25.677 -21.032 -14.224 1.00 18.77 C ANISOU 780 CZ PHE A 117 2245 2400 2485 -250 -67 28 C ATOM 781 N LEU A 118 29.386 -24.695 -19.686 1.00 20.79 N ANISOU 781 N LEU A 118 2537 2751 2610 -287 -3 -1 N ATOM 782 CA LEU A 118 29.579 -25.474 -20.903 1.00 19.98 C ANISOU 782 CA LEU A 118 2461 2658 2472 -286 8 -7 C ATOM 783 C LEU A 118 30.055 -26.892 -20.645 1.00 19.92 C ANISOU 783 C LEU A 118 2459 2655 2454 -260 22 -30 C ATOM 784 O LEU A 118 30.091 -27.685 -21.587 1.00 20.20 O ANISOU 784 O LEU A 118 2527 2691 2457 -255 30 -38 O ATOM 785 CB LEU A 118 30.596 -24.791 -21.823 1.00 19.89 C ANISOU 785 CB LEU A 118 2449 2669 2440 -299 32 4 C ATOM 786 CG LEU A 118 30.276 -23.416 -22.401 1.00 21.83 C ANISOU 786 CG LEU A 118 2700 2908 2685 -327 21 29 C ATOM 787 CD1 LEU A 118 31.482 -22.955 -23.192 1.00 18.08 C ANISOU 787 CD1 LEU A 118 2221 2461 2190 -341 50 37 C ATOM 788 CD2 LEU A 118 29.078 -23.458 -23.306 1.00 17.22 C ANISOU 788 CD2 LEU A 118 2150 2310 2084 -337 -3 39 C ATOM 789 N THR A 119 30.421 -27.235 -19.408 1.00 18.95 N ANISOU 789 N THR A 119 2311 2533 2355 -242 25 -40 N ATOM 790 CA THR A 119 31.091 -28.511 -19.159 1.00 19.50 C ANISOU 790 CA THR A 119 2386 2609 2415 -213 43 -60 C ATOM 791 C THR A 119 30.156 -29.712 -19.273 1.00 21.17 C ANISOU 791 C THR A 119 2635 2795 2613 -206 26 -72 C ATOM 792 O THR A 119 30.642 -30.827 -19.492 1.00 19.75 O ANISOU 792 O THR A 119 2478 2613 2413 -182 42 -88 O ATOM 793 CB THR A 119 31.734 -28.535 -17.763 1.00 22.49 C ANISOU 793 CB THR A 119 2726 2996 2822 -197 47 -65 C ATOM 794 CG2 THR A 119 32.574 -27.278 -17.517 1.00 21.80 C ANISOU 794 CG2 THR A 119 2602 2931 2749 -214 55 -51 C ATOM 795 OG1 THR A 119 30.701 -28.588 -16.769 1.00 25.15 O ANISOU 795 OG1 THR A 119 3063 3310 3182 -201 20 -65 O ATOM 796 N THR A 120 28.836 -29.533 -19.120 1.00 20.29 N ANISOU 796 N THR A 120 2533 2665 2512 -226 -5 -63 N ATOM 797 CA THR A 120 27.967 -30.711 -19.099 1.00 22.38 C ANISOU 797 CA THR A 120 2831 2908 2766 -226 -24 -72 C ATOM 798 C THR A 120 27.631 -31.218 -20.495 1.00 20.39 C ANISOU 798 C THR A 120 2627 2648 2472 -240 -29 -74 C ATOM 799 O THR A 120 27.463 -32.429 -20.685 1.00 21.57 O ANISOU 799 O THR A 120 2817 2780 2600 -234 -33 -89 O ATOM 800 CB THR A 120 26.663 -30.434 -18.355 1.00 20.14 C ANISOU 800 CB THR A 120 2533 2614 2507 -243 -55 -58 C ATOM 801 CG2 THR A 120 26.960 -30.099 -16.907 1.00 24.23 C ANISOU 801 CG2 THR A 120 3012 3135 3060 -228 -49 -59 C ATOM 802 OG1 THR A 120 25.966 -29.333 -18.965 1.00 21.34 O ANISOU 802 OG1 THR A 120 2677 2770 2661 -265 -69 -36 O ATOM 803 N HIS A 121 27.504 -30.343 -21.483 1.00 18.58 N ANISOU 803 N HIS A 121 2401 2428 2229 -259 -31 -59 N ATOM 804 CA HIS A 121 27.000 -30.796 -22.775 1.00 20.58 C ANISOU 804 CA HIS A 121 2705 2673 2442 -278 -42 -59 C ATOM 805 C HIS A 121 27.982 -30.517 -23.904 1.00 19.35 C ANISOU 805 C HIS A 121 2567 2532 2253 -272 -12 -62 C ATOM 806 O HIS A 121 27.602 -30.253 -25.046 1.00 20.85 O ANISOU 806 O HIS A 121 2787 2723 2414 -294 -21 -53 O ATOM 807 CB HIS A 121 25.614 -30.209 -23.009 1.00 21.59 C ANISOU 807 CB HIS A 121 2830 2797 2578 -311 -82 -35 C ATOM 808 CG HIS A 121 24.574 -30.865 -22.147 1.00 20.74 C ANISOU 808 CG HIS A 121 2716 2676 2489 -318 -110 -33 C ATOM 809 CD2 HIS A 121 23.664 -31.831 -22.421 1.00 21.62 C ANISOU 809 CD2 HIS A 121 2862 2772 2581 -340 -139 -33 C ATOM 810 ND1 HIS A 121 24.442 -30.583 -20.802 1.00 21.88 N ANISOU 810 ND1 HIS A 121 2818 2823 2674 -305 -110 -29 N ATOM 811 CE1 HIS A 121 23.476 -31.329 -20.292 1.00 20.62 C ANISOU 811 CE1 HIS A 121 2663 2653 2521 -317 -135 -26 C ATOM 812 NE2 HIS A 121 22.999 -32.105 -21.251 1.00 21.63 N ANISOU 812 NE2 HIS A 121 2836 2770 2613 -341 -154 -27 N ATOM 813 N THR A 122 29.269 -30.623 -23.595 1.00 20.72 N ANISOU 813 N THR A 122 2721 2722 2430 -242 25 -74 N ATOM 814 CA THR A 122 30.319 -30.656 -24.600 1.00 19.14 C ANISOU 814 CA THR A 122 2537 2540 2194 -228 62 -79 C ATOM 815 C THR A 122 30.708 -32.106 -24.848 1.00 22.85 C ANISOU 815 C THR A 122 3054 2996 2632 -197 81 -105 C ATOM 816 O THR A 122 30.547 -32.967 -23.973 1.00 20.45 O ANISOU 816 O THR A 122 2754 2673 2342 -179 72 -119 O ATOM 817 CB THR A 122 31.544 -29.840 -24.152 1.00 21.44 C ANISOU 817 CB THR A 122 2773 2865 2508 -215 93 -71 C ATOM 818 CG2 THR A 122 32.184 -30.435 -22.874 1.00 18.49 C ANISOU 818 CG2 THR A 122 2368 2495 2162 -182 105 -84 C ATOM 819 OG1 THR A 122 32.527 -29.842 -25.188 1.00 21.97 O ANISOU 819 OG1 THR A 122 2853 2957 2539 -203 132 -72 O ATOM 820 N TYR A 123 31.188 -32.390 -26.058 1.00 22.05 N ANISOU 820 N TYR A 123 2994 2900 2483 -188 106 -113 N ATOM 821 CA TYR A 123 31.780 -33.700 -26.326 1.00 24.81 C ANISOU 821 CA TYR A 123 3392 3238 2799 -148 133 -139 C ATOM 822 C TYR A 123 32.817 -33.560 -27.434 1.00 24.01 C ANISOU 822 C TYR A 123 3303 3163 2656 -127 180 -140 C ATOM 823 O TYR A 123 32.505 -33.098 -28.538 1.00 21.89 O ANISOU 823 O TYR A 123 3064 2898 2355 -155 177 -132 O ATOM 824 CB TYR A 123 30.711 -34.750 -26.687 1.00 22.57 C ANISOU 824 CB TYR A 123 3182 2909 2485 -165 101 -154 C ATOM 825 CG TYR A 123 31.278 -36.162 -26.833 1.00 25.68 C ANISOU 825 CG TYR A 123 3635 3278 2843 -120 127 -183 C ATOM 826 CD1 TYR A 123 31.822 -36.830 -25.743 1.00 23.95 C ANISOU 826 CD1 TYR A 123 3395 3053 2650 -79 141 -194 C ATOM 827 CD2 TYR A 123 31.330 -36.791 -28.080 1.00 26.99 C ANISOU 827 CD2 TYR A 123 3881 3427 2948 -115 141 -199 C ATOM 828 CE1 TYR A 123 32.361 -38.096 -25.876 1.00 26.10 C ANISOU 828 CE1 TYR A 123 3725 3301 2890 -32 166 -219 C ATOM 829 CE2 TYR A 123 31.867 -38.057 -28.228 1.00 26.86 C ANISOU 829 CE2 TYR A 123 3926 3383 2896 -69 168 -227 C ATOM 830 CZ TYR A 123 32.378 -38.705 -27.120 1.00 27.97 C ANISOU 830 CZ TYR A 123 4044 3517 3065 -26 180 -236 C ATOM 831 OH TYR A 123 32.920 -39.959 -27.262 1.00 32.60 O ANISOU 831 OH TYR A 123 4696 4073 3617 26 208 -262 O ATOM 832 N GLU A 124 34.051 -33.960 -27.124 1.00 24.75 N ANISOU 832 N GLU A 124 3373 3280 2751 -77 225 -148 N ATOM 833 CA GLU A 124 35.182 -33.899 -28.050 1.00 22.74 C ANISOU 833 CA GLU A 124 3121 3061 2460 -48 278 -148 C ATOM 834 C GLU A 124 35.327 -32.525 -28.690 1.00 25.06 C ANISOU 834 C GLU A 124 3380 3389 2754 -87 282 -121 C ATOM 835 O GLU A 124 35.623 -32.397 -29.878 1.00 26.17 O ANISOU 835 O GLU A 124 3552 3543 2848 -88 309 -119 O ATOM 836 CB GLU A 124 35.093 -35.005 -29.101 1.00 27.99 C ANISOU 836 CB GLU A 124 3877 3696 3061 -24 296 -173 C ATOM 837 CG GLU A 124 34.903 -36.385 -28.457 1.00 27.45 C ANISOU 837 CG GLU A 124 3853 3586 2992 12 288 -199 C ATOM 838 CD GLU A 124 35.017 -37.511 -29.449 1.00 32.79 C ANISOU 838 CD GLU A 124 4626 4231 3602 44 312 -226 C ATOM 839 OE1 GLU A 124 34.499 -37.345 -30.576 1.00 31.25 O ANISOU 839 OE1 GLU A 124 4486 4026 3364 11 303 -228 O ATOM 840 OE2 GLU A 124 35.609 -38.563 -29.096 1.00 37.24 O1- ANISOU 840 OE2 GLU A 124 5214 4779 4156 102 339 -245 O1- ATOM 841 N GLY A 125 35.140 -31.485 -27.875 1.00 22.25 N ANISOU 841 N GLY A 125 2962 3044 2446 -118 258 -100 N ATOM 842 CA GLY A 125 35.341 -30.113 -28.278 1.00 24.82 C ANISOU 842 CA GLY A 125 3251 3399 2779 -156 260 -72 C ATOM 843 C GLY A 125 34.128 -29.430 -28.859 1.00 24.86 C ANISOU 843 C GLY A 125 3288 3380 2778 -205 218 -60 C ATOM 844 O GLY A 125 34.203 -28.238 -29.167 1.00 24.01 O ANISOU 844 O GLY A 125 3156 3290 2677 -237 215 -35 O ATOM 845 N THR A 126 33.014 -30.133 -29.017 1.00 22.65 N ANISOU 845 N THR A 126 3061 3060 2484 -213 184 -73 N ATOM 846 CA THR A 126 31.852 -29.612 -29.725 1.00 22.62 C ANISOU 846 CA THR A 126 3090 3038 2467 -257 144 -59 C ATOM 847 C THR A 126 30.712 -29.460 -28.732 1.00 22.37 C ANISOU 847 C THR A 126 3039 2981 2479 -276 95 -54 C ATOM 848 O THR A 126 30.473 -30.351 -27.913 1.00 21.17 O ANISOU 848 O THR A 126 2889 2810 2343 -258 85 -71 O ATOM 849 CB THR A 126 31.462 -30.537 -30.883 1.00 22.75 C ANISOU 849 CB THR A 126 3188 3034 2422 -257 142 -76 C ATOM 850 CG2 THR A 126 30.149 -30.109 -31.510 1.00 22.63 C ANISOU 850 CG2 THR A 126 3203 3000 2394 -305 92 -59 C ATOM 851 OG1 THR A 126 32.480 -30.477 -31.884 1.00 21.79 O ANISOU 851 OG1 THR A 126 3083 2940 2257 -241 191 -77 O ATOM 852 N GLN A 127 30.031 -28.324 -28.782 1.00 23.27 N ANISOU 852 N GLN A 127 3134 3096 2613 -309 66 -28 N ATOM 853 CA GLN A 127 28.968 -28.031 -27.829 1.00 21.27 C ANISOU 853 CA GLN A 127 2855 2825 2402 -323 25 -18 C ATOM 854 C GLN A 127 27.622 -28.488 -28.390 1.00 22.91 C ANISOU 854 C GLN A 127 3105 3010 2589 -348 -18 -14 C ATOM 855 O GLN A 127 27.278 -28.162 -29.529 1.00 21.98 O ANISOU 855 O GLN A 127 3019 2894 2436 -371 -29 0 O ATOM 856 CB GLN A 127 28.942 -26.531 -27.519 1.00 20.57 C ANISOU 856 CB GLN A 127 2723 2745 2346 -340 18 9 C ATOM 857 CG GLN A 127 28.202 -26.184 -26.245 1.00 22.11 C ANISOU 857 CG GLN A 127 2883 2927 2592 -339 -9 16 C ATOM 858 CD GLN A 127 28.927 -26.708 -25.042 1.00 20.67 C ANISOU 858 CD GLN A 127 2670 2749 2436 -312 10 -4 C ATOM 859 NE2 GLN A 127 28.191 -27.047 -23.991 1.00 20.34 N ANISOU 859 NE2 GLN A 127 2613 2691 2424 -306 -12 -8 N ATOM 860 OE1 GLN A 127 30.141 -26.832 -25.069 1.00 20.97 O ANISOU 860 OE1 GLN A 127 2695 2806 2466 -297 45 -13 O ATOM 861 N TYR A 128 26.854 -29.236 -27.583 1.00 17.78 N ANISOU 861 N TYR A 128 2454 2342 1958 -346 -44 -22 N ATOM 862 CA TYR A 128 25.559 -29.740 -28.020 1.00 19.39 C ANISOU 862 CA TYR A 128 2693 2529 2145 -375 -88 -15 C ATOM 863 C TYR A 128 24.395 -29.177 -27.223 1.00 20.42 C ANISOU 863 C TYR A 128 2781 2658 2318 -390 -126 9 C ATOM 864 O TYR A 128 23.240 -29.452 -27.566 1.00 19.16 O ANISOU 864 O TYR A 128 2639 2493 2148 -418 -167 23 O ATOM 865 CB TYR A 128 25.529 -31.275 -27.952 1.00 17.78 C ANISOU 865 CB TYR A 128 2537 2304 1916 -367 -89 -43 C ATOM 866 CG TYR A 128 26.448 -31.908 -28.968 1.00 19.21 C ANISOU 866 CG TYR A 128 2774 2481 2043 -352 -55 -66 C ATOM 867 CD1 TYR A 128 26.063 -32.042 -30.300 1.00 21.15 C ANISOU 867 CD1 TYR A 128 3078 2721 2235 -379 -70 -63 C ATOM 868 CD2 TYR A 128 27.740 -32.296 -28.608 1.00 19.11 C ANISOU 868 CD2 TYR A 128 2754 2476 2032 -308 -7 -87 C ATOM 869 CE1 TYR A 128 26.921 -32.592 -31.237 1.00 22.18 C ANISOU 869 CE1 TYR A 128 3264 2850 2313 -361 -34 -84 C ATOM 870 CE2 TYR A 128 28.592 -32.848 -29.509 1.00 22.77 C ANISOU 870 CE2 TYR A 128 3265 2940 2446 -287 30 -106 C ATOM 871 CZ TYR A 128 28.185 -32.996 -30.833 1.00 27.09 C ANISOU 871 CZ TYR A 128 3875 3478 2938 -312 18 -106 C ATOM 872 OH TYR A 128 29.056 -33.548 -31.733 1.00 22.88 O ANISOU 872 OH TYR A 128 3395 2946 2352 -286 59 -126 O ATOM 873 N GLY A 129 24.660 -28.408 -26.176 1.00 20.93 N ANISOU 873 N GLY A 129 2794 2731 2429 -372 -115 15 N ATOM 874 CA GLY A 129 23.602 -27.724 -25.459 1.00 20.81 C ANISOU 874 CA GLY A 129 2740 2716 2452 -380 -144 39 C ATOM 875 C GLY A 129 24.154 -26.538 -24.710 1.00 18.23 C ANISOU 875 C GLY A 129 2369 2395 2161 -363 -124 47 C ATOM 876 O GLY A 129 25.338 -26.503 -24.361 1.00 18.44 O ANISOU 876 O GLY A 129 2387 2427 2193 -346 -91 30 O ATOM 877 N LEU A 130 23.293 -25.545 -24.479 1.00 16.77 N ANISOU 877 N LEU A 130 2161 2211 2002 -367 -146 74 N ATOM 878 CA LEU A 130 23.580 -24.453 -23.562 1.00 17.87 C ANISOU 878 CA LEU A 130 2265 2347 2177 -351 -134 81 C ATOM 879 C LEU A 130 22.583 -24.462 -22.413 1.00 18.17 C ANISOU 879 C LEU A 130 2273 2380 2250 -339 -152 89 C ATOM 880 O LEU A 130 21.378 -24.640 -22.623 1.00 18.81 O ANISOU 880 O LEU A 130 2351 2464 2331 -348 -181 108 O ATOM 881 CB LEU A 130 23.538 -23.079 -24.271 1.00 18.03 C ANISOU 881 CB LEU A 130 2290 2367 2195 -360 -138 108 C ATOM 882 CG LEU A 130 24.518 -22.779 -25.400 1.00 18.74 C ANISOU 882 CG LEU A 130 2405 2464 2251 -375 -118 107 C ATOM 883 CD1 LEU A 130 24.388 -21.304 -25.838 1.00 17.28 C ANISOU 883 CD1 LEU A 130 2222 2273 2070 -384 -124 137 C ATOM 884 CD2 LEU A 130 25.924 -23.045 -24.900 1.00 17.74 C ANISOU 884 CD2 LEU A 130 2268 2344 2127 -364 -80 83 C ATOM 885 N ALA A 131 23.089 -24.255 -21.197 1.00 17.07 N ANISOU 885 N ALA A 131 2110 2236 2139 -320 -133 76 N ATOM 886 CA ALA A 131 22.209 -24.134 -20.039 1.00 19.48 C ANISOU 886 CA ALA A 131 2388 2538 2477 -305 -144 84 C ATOM 887 C ALA A 131 21.219 -22.980 -20.225 1.00 19.06 C ANISOU 887 C ALA A 131 2324 2482 2436 -300 -162 116 C ATOM 888 O ALA A 131 21.585 -21.895 -20.686 1.00 19.39 O ANISOU 888 O ALA A 131 2376 2517 2476 -301 -156 127 O ATOM 889 CB ALA A 131 23.052 -23.926 -18.771 1.00 16.07 C ANISOU 889 CB ALA A 131 1939 2099 2068 -287 -121 65 C ATOM 890 N ILE A 132 19.941 -23.212 -19.887 1.00 18.00 N ANISOU 890 N ILE A 132 2170 2356 2314 -295 -184 134 N ATOM 891 CA ILE A 132 19.001 -22.090 -19.907 1.00 18.54 C ANISOU 891 CA ILE A 132 2222 2423 2398 -280 -197 167 C ATOM 892 C ILE A 132 19.422 -21.038 -18.885 1.00 16.29 C ANISOU 892 C ILE A 132 1932 2120 2138 -252 -174 161 C ATOM 893 O ILE A 132 19.187 -19.839 -19.071 1.00 17.91 O ANISOU 893 O ILE A 132 2143 2313 2350 -238 -176 181 O ATOM 894 CB ILE A 132 17.548 -22.575 -19.689 1.00 18.67 C ANISOU 894 CB ILE A 132 2210 2459 2424 -277 -222 192 C ATOM 895 CG1 ILE A 132 16.550 -21.488 -20.135 1.00 17.29 C ANISOU 895 CG1 ILE A 132 2021 2291 2256 -262 -240 232 C ATOM 896 CG2 ILE A 132 17.294 -23.004 -18.242 1.00 20.77 C ANISOU 896 CG2 ILE A 132 2449 2727 2714 -258 -210 181 C ATOM 897 CD1 ILE A 132 15.078 -21.959 -20.200 1.00 16.31 C ANISOU 897 CD1 ILE A 132 1863 2198 2138 -266 -270 265 C ATOM 898 N GLY A 133 20.100 -21.461 -17.834 1.00 19.08 N ANISOU 898 N GLY A 133 2280 2467 2502 -245 -155 134 N ATOM 899 CA GLY A 133 20.566 -20.585 -16.782 1.00 20.40 C ANISOU 899 CA GLY A 133 2446 2616 2688 -225 -136 125 C ATOM 900 C GLY A 133 21.129 -21.469 -15.691 1.00 20.43 C ANISOU 900 C GLY A 133 2440 2622 2699 -222 -122 96 C ATOM 901 O GLY A 133 21.126 -22.702 -15.813 1.00 19.99 O ANISOU 901 O GLY A 133 2381 2581 2635 -234 -127 86 O ATOM 902 N GLY A 134 21.594 -20.836 -14.603 1.00 18.20 N ANISOU 902 N GLY A 134 2159 2324 2432 -207 -107 85 N ATOM 903 CA GLY A 134 22.251 -21.589 -13.549 1.00 19.12 C ANISOU 903 CA GLY A 134 2268 2443 2553 -206 -95 59 C ATOM 904 C GLY A 134 21.886 -21.135 -12.147 1.00 17.97 C ANISOU 904 C GLY A 134 2116 2285 2425 -181 -87 56 C ATOM 905 O GLY A 134 21.178 -20.147 -11.954 1.00 18.37 O ANISOU 905 O GLY A 134 2172 2323 2485 -161 -86 71 O ATOM 906 N ASN A 135 22.390 -21.886 -11.167 1.00 18.72 N ANISOU 906 N ASN A 135 2204 2385 2523 -180 -79 35 N ATOM 907 CA ASN A 135 22.289 -21.531 -9.754 1.00 20.59 C ANISOU 907 CA ASN A 135 2442 2610 2771 -160 -69 26 C ATOM 908 C ASN A 135 23.620 -21.759 -9.038 1.00 17.00 C ANISOU 908 C ASN A 135 1992 2153 2313 -172 -61 2 C ATOM 909 O ASN A 135 24.545 -22.376 -9.565 1.00 18.21 O ANISOU 909 O ASN A 135 2142 2318 2458 -190 -62 -8 O ATOM 910 CB ASN A 135 21.194 -22.324 -9.011 1.00 20.26 C ANISOU 910 CB ASN A 135 2379 2581 2736 -143 -70 33 C ATOM 911 CG ASN A 135 19.789 -21.909 -9.405 1.00 25.40 C ANISOU 911 CG ASN A 135 3017 3240 3395 -126 -76 62 C ATOM 912 ND2 ASN A 135 19.299 -20.842 -8.764 1.00 24.45 N ANISOU 912 ND2 ASN A 135 2903 3105 3283 -97 -65 70 N ATOM 913 OD1 ASN A 135 19.185 -22.461 -10.327 1.00 25.44 O ANISOU 913 OD1 ASN A 135 3008 3262 3395 -139 -90 78 O ATOM 914 N ALA A 136 23.702 -21.246 -7.810 1.00 19.11 N ANISOU 914 N ALA A 136 2269 2407 2586 -159 -54 -7 N ATOM 915 CA ALA A 136 24.864 -21.413 -6.960 1.00 16.69 C ANISOU 915 CA ALA A 136 1966 2100 2276 -170 -51 -28 C ATOM 916 C ALA A 136 24.516 -22.302 -5.783 1.00 18.04 C ANISOU 916 C ALA A 136 2126 2278 2449 -155 -48 -36 C ATOM 917 O ALA A 136 23.353 -22.467 -5.418 1.00 17.51 O ANISOU 917 O ALA A 136 2054 2212 2388 -135 -45 -27 O ATOM 918 CB ALA A 136 25.393 -20.073 -6.430 1.00 16.73 C ANISOU 918 CB ALA A 136 1998 2079 2278 -177 -50 -33 C ATOM 919 N ASN A 137 25.554 -22.842 -5.161 1.00 19.66 N ANISOU 919 N ASN A 137 2328 2490 2650 -165 -49 -52 N ATOM 920 CA ASN A 137 25.392 -23.666 -3.979 1.00 16.40 C ANISOU 920 CA ASN A 137 1910 2084 2238 -153 -48 -61 C ATOM 921 C ASN A 137 26.055 -22.973 -2.799 1.00 16.32 C ANISOU 921 C ASN A 137 1916 2060 2222 -156 -47 -73 C ATOM 922 O ASN A 137 27.065 -22.272 -2.948 1.00 13.48 O ANISOU 922 O ASN A 137 1566 1697 1859 -176 -52 -78 O ATOM 923 CB ASN A 137 25.980 -25.058 -4.229 1.00 16.45 C ANISOU 923 CB ASN A 137 1900 2109 2241 -159 -52 -66 C ATOM 924 CG ASN A 137 25.210 -25.803 -5.313 1.00 20.19 C ANISOU 924 CG ASN A 137 2368 2590 2715 -159 -55 -55 C ATOM 925 ND2 ASN A 137 25.851 -26.015 -6.459 1.00 20.14 N ANISOU 925 ND2 ASN A 137 2360 2591 2702 -170 -56 -56 N ATOM 926 OD1 ASN A 137 24.034 -26.127 -5.139 1.00 18.31 O ANISOU 926 OD1 ASN A 137 2125 2353 2480 -151 -56 -45 O ATOM 927 N GLY A 138 25.484 -23.185 -1.623 1.00 16.51 N ANISOU 927 N GLY A 138 1947 2081 2244 -139 -42 -77 N ATOM 928 CA GLY A 138 25.955 -22.495 -0.433 1.00 16.74 C ANISOU 928 CA GLY A 138 2001 2095 2265 -141 -42 -90 C ATOM 929 C GLY A 138 24.950 -22.639 0.688 1.00 18.35 C ANISOU 929 C GLY A 138 2214 2294 2464 -116 -31 -90 C ATOM 930 O GLY A 138 24.173 -23.597 0.723 1.00 16.91 O ANISOU 930 O GLY A 138 2011 2128 2287 -103 -26 -81 O ATOM 931 N ILE A 139 24.957 -21.662 1.592 1.00 18.69 N ANISOU 931 N ILE A 139 2292 2315 2496 -110 -26 -99 N ATOM 932 CA ILE A 139 24.138 -21.721 2.797 1.00 16.19 C ANISOU 932 CA ILE A 139 1989 1993 2170 -84 -11 -101 C ATOM 933 C ILE A 139 23.349 -20.428 2.923 1.00 18.67 C ANISOU 933 C ILE A 139 2335 2279 2479 -58 5 -99 C ATOM 934 O ILE A 139 23.938 -19.340 2.963 1.00 19.51 O ANISOU 934 O ILE A 139 2479 2357 2576 -70 0 -109 O ATOM 935 CB ILE A 139 25.007 -21.987 4.042 1.00 19.54 C ANISOU 935 CB ILE A 139 2430 2417 2577 -97 -20 -118 C ATOM 936 CG1 ILE A 139 25.708 -23.349 3.868 1.00 18.25 C ANISOU 936 CG1 ILE A 139 2233 2282 2420 -113 -34 -116 C ATOM 937 CG2 ILE A 139 24.174 -21.966 5.338 1.00 16.31 C ANISOU 937 CG2 ILE A 139 2043 2002 2153 -70 -2 -121 C ATOM 938 CD1 ILE A 139 26.706 -23.715 4.945 1.00 18.92 C ANISOU 938 CD1 ILE A 139 2326 2372 2490 -128 -48 -128 C ATOM 939 N LEU A 140 22.020 -20.537 2.966 1.00 16.44 N ANISOU 939 N LEU A 140 2039 2006 2202 -24 25 -84 N ATOM 940 CA LEU A 140 21.204 -19.370 3.279 1.00 18.19 C ANISOU 940 CA LEU A 140 2293 2202 2417 13 46 -80 C ATOM 941 C LEU A 140 21.387 -18.984 4.743 1.00 18.28 C ANISOU 941 C LEU A 140 2349 2193 2403 23 57 -100 C ATOM 942 O LEU A 140 21.468 -19.838 5.626 1.00 19.85 O ANISOU 942 O LEU A 140 2539 2410 2593 20 59 -105 O ATOM 943 CB LEU A 140 19.723 -19.639 2.992 1.00 18.90 C ANISOU 943 CB LEU A 140 2347 2315 2519 49 66 -54 C ATOM 944 CG LEU A 140 19.287 -19.487 1.525 1.00 22.00 C ANISOU 944 CG LEU A 140 2712 2717 2931 49 57 -32 C ATOM 945 CD1 LEU A 140 19.777 -20.657 0.704 1.00 18.20 C ANISOU 945 CD1 LEU A 140 2194 2261 2460 10 35 -29 C ATOM 946 CD2 LEU A 140 17.786 -19.389 1.427 1.00 19.66 C ANISOU 946 CD2 LEU A 140 2388 2440 2643 91 77 -4 C ATOM 947 N TYR A 141 21.466 -17.689 5.003 1.00 16.93 N ANISOU 947 N TYR A 141 2232 1982 2217 36 64 -111 N ATOM 948 CA TYR A 141 21.545 -17.226 6.377 1.00 19.72 C ANISOU 948 CA TYR A 141 2639 2311 2542 49 76 -130 C ATOM 949 C TYR A 141 20.698 -15.975 6.516 1.00 20.41 C ANISOU 949 C TYR A 141 2773 2362 2619 97 102 -129 C ATOM 950 O TYR A 141 20.537 -15.215 5.560 1.00 23.44 O ANISOU 950 O TYR A 141 3164 2727 3014 104 100 -119 O ATOM 951 CB TYR A 141 22.994 -16.950 6.809 1.00 18.21 C ANISOU 951 CB TYR A 141 2486 2099 2333 0 47 -153 C ATOM 952 CG TYR A 141 23.599 -15.671 6.260 1.00 20.17 C ANISOU 952 CG TYR A 141 2782 2306 2577 -21 34 -160 C ATOM 953 CD1 TYR A 141 24.100 -15.615 4.962 1.00 20.86 C ANISOU 953 CD1 TYR A 141 2840 2400 2685 -50 15 -149 C ATOM 954 CD2 TYR A 141 23.707 -14.529 7.049 1.00 18.48 C ANISOU 954 CD2 TYR A 141 2646 2043 2333 -15 38 -179 C ATOM 955 CE1 TYR A 141 24.668 -14.451 4.459 1.00 19.71 C ANISOU 955 CE1 TYR A 141 2739 2217 2534 -73 2 -152 C ATOM 956 CE2 TYR A 141 24.288 -13.347 6.547 1.00 19.15 C ANISOU 956 CE2 TYR A 141 2781 2084 2412 -40 23 -184 C ATOM 957 CZ TYR A 141 24.761 -13.328 5.254 1.00 22.47 C ANISOU 957 CZ TYR A 141 3166 2515 2855 -71 5 -169 C ATOM 958 OH TYR A 141 25.336 -12.192 4.731 1.00 21.98 O ANISOU 958 OH TYR A 141 3153 2413 2786 -100 -11 -171 O ATOM 959 N ASN A 142 20.157 -15.764 7.711 1.00 16.10 N ANISOU 959 N ASN A 142 2263 1807 2049 132 129 -138 N ATOM 960 CA ASN A 142 19.327 -14.600 7.972 1.00 20.15 C ANISOU 960 CA ASN A 142 2826 2283 2547 188 160 -138 C ATOM 961 C ASN A 142 20.231 -13.450 8.408 1.00 22.23 C ANISOU 961 C ASN A 142 3179 2485 2781 167 146 -166 C ATOM 962 O ASN A 142 20.827 -13.494 9.490 1.00 18.66 O ANISOU 962 O ASN A 142 2769 2020 2299 146 140 -190 O ATOM 963 CB ASN A 142 18.267 -14.895 9.029 1.00 20.45 C ANISOU 963 CB ASN A 142 2861 2341 2569 241 200 -133 C ATOM 964 CG ASN A 142 17.246 -13.763 9.148 1.00 22.28 C ANISOU 964 CG ASN A 142 3133 2543 2790 313 239 -127 C ATOM 965 ND2 ASN A 142 15.981 -14.084 8.936 1.00 22.85 N ANISOU 965 ND2 ASN A 142 3149 2656 2879 363 269 -96 N ATOM 966 OD1 ASN A 142 17.603 -12.615 9.417 1.00 22.69 O ANISOU 966 OD1 ASN A 142 3266 2536 2818 322 240 -147 O ATOM 967 N LYS A 143 20.309 -12.412 7.566 1.00 21.05 N ANISOU 967 N LYS A 143 3062 2297 2638 169 140 -163 N ATOM 968 CA LYS A 143 21.205 -11.289 7.821 1.00 21.36 C ANISOU 968 CA LYS A 143 3190 2277 2651 138 121 -186 C ATOM 969 C LYS A 143 20.843 -10.562 9.113 1.00 24.23 C ANISOU 969 C LYS A 143 3637 2595 2972 178 148 -209 C ATOM 970 O LYS A 143 21.723 -10.051 9.822 1.00 22.35 O ANISOU 970 O LYS A 143 3472 2318 2703 139 128 -235 O ATOM 971 CB LYS A 143 21.133 -10.318 6.641 1.00 23.47 C ANISOU 971 CB LYS A 143 3476 2510 2933 143 115 -173 C ATOM 972 CG LYS A 143 22.015 -10.658 5.460 1.00 23.01 C ANISOU 972 CG LYS A 143 3369 2473 2900 81 79 -162 C ATOM 973 CD LYS A 143 21.855 -9.585 4.402 1.00 24.64 C ANISOU 973 CD LYS A 143 3606 2641 3114 89 76 -148 C ATOM 974 CE LYS A 143 21.683 -10.174 3.030 1.00 31.76 C ANISOU 974 CE LYS A 143 4430 3586 4051 80 67 -120 C ATOM 975 NZ LYS A 143 22.008 -9.158 1.970 1.00 38.27 N1+ ANISOU 975 NZ LYS A 143 5289 4372 4879 61 51 -109 N1+ ATOM 976 N ARG A 144 19.546 -10.457 9.405 1.00 22.38 N ANISOU 976 N ARG A 144 3399 2368 2737 255 192 -197 N ATOM 977 CA ARG A 144 19.113 -9.759 10.607 1.00 23.74 C ANISOU 977 CA ARG A 144 3655 2498 2866 303 225 -218 C ATOM 978 C ARG A 144 19.458 -10.547 11.866 1.00 25.18 C ANISOU 978 C ARG A 144 3840 2704 3022 281 225 -236 C ATOM 979 O ARG A 144 19.832 -9.958 12.891 1.00 22.14 O ANISOU 979 O ARG A 144 3544 2274 2593 277 227 -265 O ATOM 980 CB ARG A 144 17.614 -9.460 10.526 1.00 21.37 C ANISOU 980 CB ARG A 144 3339 2207 2573 397 277 -195 C ATOM 981 CG ARG A 144 17.016 -8.911 11.818 1.00 26.76 C ANISOU 981 CG ARG A 144 4097 2858 3211 460 321 -214 C ATOM 982 CD ARG A 144 15.536 -8.527 11.658 1.00 28.72 C ANISOU 982 CD ARG A 144 4327 3119 3468 560 375 -187 C ATOM 983 NE ARG A 144 14.635 -9.674 11.565 1.00 38.39 N ANISOU 983 NE ARG A 144 5440 4427 4721 584 396 -154 N ATOM 984 CZ ARG A 144 14.450 -10.618 12.488 1.00 41.40 C ANISOU 984 CZ ARG A 144 5788 4853 5089 580 412 -156 C ATOM 985 NH1 ARG A 144 15.093 -10.604 13.651 1.00 40.39 N1+ ANISOU 985 NH1 ARG A 144 5729 4699 4919 556 410 -190 N1+ ATOM 986 NH2 ARG A 144 13.593 -11.607 12.237 1.00 31.32 N ANISOU 986 NH2 ARG A 144 4409 3650 3841 596 428 -121 N ATOM 987 N VAL A 145 19.348 -11.875 11.814 1.00 23.34 N ANISOU 987 N VAL A 145 3517 2537 2813 266 221 -220 N ATOM 988 CA VAL A 145 19.729 -12.675 12.973 1.00 23.53 C ANISOU 988 CA VAL A 145 3543 2584 2812 242 217 -235 C ATOM 989 C VAL A 145 21.236 -12.601 13.197 1.00 22.73 C ANISOU 989 C VAL A 145 3480 2461 2696 164 167 -258 C ATOM 990 O VAL A 145 21.700 -12.484 14.337 1.00 18.56 O ANISOU 990 O VAL A 145 3012 1913 2128 147 161 -282 O ATOM 991 CB VAL A 145 19.235 -14.128 12.824 1.00 21.75 C ANISOU 991 CB VAL A 145 3217 2431 2616 244 223 -209 C ATOM 992 CG1 VAL A 145 19.867 -15.022 13.866 1.00 17.07 C ANISOU 992 CG1 VAL A 145 2624 1859 2001 206 208 -223 C ATOM 993 CG2 VAL A 145 17.701 -14.174 12.968 1.00 23.52 C ANISOU 993 CG2 VAL A 145 3412 2681 2845 321 277 -186 C ATOM 994 N PHE A 146 22.019 -12.643 12.115 1.00 22.04 N ANISOU 994 N PHE A 146 3358 2378 2638 114 130 -250 N ATOM 995 CA PHE A 146 23.472 -12.528 12.244 1.00 20.60 C ANISOU 995 CA PHE A 146 3202 2181 2442 38 82 -266 C ATOM 996 C PHE A 146 23.876 -11.160 12.792 1.00 23.71 C ANISOU 996 C PHE A 146 3709 2505 2796 25 74 -292 C ATOM 997 O PHE A 146 24.822 -11.056 13.585 1.00 23.36 O ANISOU 997 O PHE A 146 3710 2445 2719 -25 44 -311 O ATOM 998 CB PHE A 146 24.133 -12.779 10.895 1.00 19.70 C ANISOU 998 CB PHE A 146 3027 2090 2368 -6 51 -249 C ATOM 999 CG PHE A 146 24.530 -14.210 10.659 1.00 21.07 C ANISOU 999 CG PHE A 146 3112 2326 2567 -32 35 -236 C ATOM 1000 CD1 PHE A 146 23.710 -15.252 11.054 1.00 19.48 C ANISOU 1000 CD1 PHE A 146 2863 2165 2373 5 59 -225 C ATOM 1001 CD2 PHE A 146 25.709 -14.507 9.989 1.00 19.82 C ANISOU 1001 CD2 PHE A 146 2918 2186 2425 -91 -4 -231 C ATOM 1002 CE1 PHE A 146 24.070 -16.579 10.818 1.00 21.20 C ANISOU 1002 CE1 PHE A 146 3008 2434 2613 -19 43 -213 C ATOM 1003 CE2 PHE A 146 26.077 -15.821 9.753 1.00 22.85 C ANISOU 1003 CE2 PHE A 146 3227 2623 2831 -108 -16 -219 C ATOM 1004 CZ PHE A 146 25.258 -16.864 10.175 1.00 21.78 C ANISOU 1004 CZ PHE A 146 3053 2521 2702 -72 6 -211 C ATOM 1005 N GLU A 147 23.187 -10.095 12.362 1.00 22.97 N ANISOU 1005 N GLU A 147 3664 2365 2700 70 98 -291 N ATOM 1006 CA GLU A 147 23.405 -8.775 12.948 1.00 24.61 C ANISOU 1006 CA GLU A 147 3992 2496 2864 68 97 -316 C ATOM 1007 C GLU A 147 23.099 -8.776 14.438 1.00 24.05 C ANISOU 1007 C GLU A 147 3985 2410 2744 96 120 -340 C ATOM 1008 O GLU A 147 23.893 -8.279 15.243 1.00 26.30 O ANISOU 1008 O GLU A 147 4352 2655 2986 51 94 -366 O ATOM 1009 CB GLU A 147 22.542 -7.732 12.247 1.00 27.78 C ANISOU 1009 CB GLU A 147 4431 2851 3271 127 126 -307 C ATOM 1010 CG GLU A 147 23.123 -6.338 12.279 1.00 37.07 C ANISOU 1010 CG GLU A 147 5724 3944 4415 98 107 -327 C ATOM 1011 CD GLU A 147 22.364 -5.388 11.362 1.00 55.54 C ANISOU 1011 CD GLU A 147 8091 6243 6771 152 130 -312 C ATOM 1012 OE1 GLU A 147 22.463 -4.149 11.566 1.00 59.21 O ANISOU 1012 OE1 GLU A 147 8669 6627 7201 157 129 -329 O ATOM 1013 OE2 GLU A 147 21.676 -5.880 10.433 1.00 55.69 O1- ANISOU 1013 OE2 GLU A 147 8020 6306 6832 189 146 -283 O1- ATOM 1014 N GLU A 148 21.927 -9.292 14.819 1.00 21.69 N ANISOU 1014 N GLU A 148 3651 2141 2448 169 168 -330 N ATOM 1015 CA GLU A 148 21.579 -9.389 16.232 1.00 25.73 C ANISOU 1015 CA GLU A 148 4217 2646 2913 199 195 -350 C ATOM 1016 C GLU A 148 22.614 -10.173 17.028 1.00 26.71 C ANISOU 1016 C GLU A 148 4333 2796 3017 130 156 -362 C ATOM 1017 O GLU A 148 22.846 -9.887 18.212 1.00 25.37 O ANISOU 1017 O GLU A 148 4245 2598 2796 123 156 -388 O ATOM 1018 CB GLU A 148 20.214 -10.052 16.392 1.00 31.19 C ANISOU 1018 CB GLU A 148 4846 3386 3618 279 251 -329 C ATOM 1019 CG GLU A 148 19.720 -10.033 17.840 1.00 36.09 C ANISOU 1019 CG GLU A 148 5528 3998 4186 321 289 -347 C ATOM 1020 CD GLU A 148 18.273 -10.470 17.980 1.00 46.75 C ANISOU 1020 CD GLU A 148 6823 5392 5547 407 352 -323 C ATOM 1021 OE1 GLU A 148 17.653 -10.822 16.942 1.00 49.04 O ANISOU 1021 OE1 GLU A 148 7024 5722 5887 430 361 -291 O ATOM 1022 OE2 GLU A 148 17.773 -10.496 19.130 1.00 45.38 O1- ANISOU 1022 OE2 GLU A 148 6692 5219 5332 448 390 -335 O1- ATOM 1023 N ALA A 149 23.216 -11.188 16.410 1.00 22.80 N ANISOU 1023 N ALA A 149 3742 2357 2562 82 123 -344 N ATOM 1024 CA ALA A 149 24.158 -12.051 17.099 1.00 24.20 C ANISOU 1024 CA ALA A 149 3899 2567 2727 23 86 -349 C ATOM 1025 C ALA A 149 25.543 -11.435 17.208 1.00 24.31 C ANISOU 1025 C ALA A 149 3968 2549 2720 -57 30 -366 C ATOM 1026 O ALA A 149 26.343 -11.899 18.033 1.00 22.58 O ANISOU 1026 O ALA A 149 3758 2346 2476 -104 -1 -375 O ATOM 1027 CB ALA A 149 24.261 -13.399 16.381 1.00 19.36 C ANISOU 1027 CB ALA A 149 3167 2025 2165 9 74 -322 C ATOM 1028 N GLY A 150 25.838 -10.422 16.394 1.00 23.16 N ANISOU 1028 N GLY A 150 3857 2359 2582 -76 16 -368 N ATOM 1029 CA GLY A 150 27.173 -9.852 16.320 1.00 22.02 C ANISOU 1029 CA GLY A 150 3753 2191 2423 -161 -39 -377 C ATOM 1030 C GLY A 150 28.136 -10.586 15.412 1.00 24.90 C ANISOU 1030 C GLY A 150 4020 2609 2831 -219 -79 -354 C ATOM 1031 O GLY A 150 29.350 -10.463 15.597 1.00 25.30 O ANISOU 1031 O GLY A 150 4082 2663 2868 -295 -128 -357 O ATOM 1032 N VAL A 151 27.636 -11.367 14.454 1.00 19.83 N ANISOU 1032 N VAL A 151 3282 2013 2238 -187 -59 -330 N ATOM 1033 CA VAL A 151 28.471 -12.012 13.444 1.00 24.33 C ANISOU 1033 CA VAL A 151 3764 2631 2849 -233 -90 -309 C ATOM 1034 C VAL A 151 28.837 -10.959 12.401 1.00 27.39 C ANISOU 1034 C VAL A 151 4176 2983 3248 -262 -104 -304 C ATOM 1035 O VAL A 151 27.988 -10.558 11.601 1.00 24.98 O ANISOU 1035 O VAL A 151 3869 2660 2963 -217 -75 -295 O ATOM 1036 CB VAL A 151 27.752 -13.205 12.800 1.00 23.68 C ANISOU 1036 CB VAL A 151 3583 2604 2809 -188 -64 -287 C ATOM 1037 CG1 VAL A 151 28.633 -13.856 11.713 1.00 21.20 C ANISOU 1037 CG1 VAL A 151 3186 2335 2534 -231 -92 -267 C ATOM 1038 CG2 VAL A 151 27.362 -14.239 13.871 1.00 23.23 C ANISOU 1038 CG2 VAL A 151 3508 2579 2739 -161 -49 -290 C ATOM 1039 N GLU A 152 30.107 -10.523 12.401 1.00 26.10 N ANISOU 1039 N GLU A 152 4032 2812 3071 -340 -151 -306 N ATOM 1040 CA GLU A 152 30.592 -9.419 11.572 1.00 29.00 C ANISOU 1040 CA GLU A 152 4438 3140 3440 -383 -170 -301 C ATOM 1041 C GLU A 152 31.086 -9.878 10.202 1.00 27.69 C ANISOU 1041 C GLU A 152 4179 3021 3320 -407 -180 -274 C ATOM 1042 O GLU A 152 30.970 -9.133 9.223 1.00 33.48 O ANISOU 1042 O GLU A 152 4927 3728 4067 -410 -176 -264 O ATOM 1043 CB GLU A 152 31.761 -8.682 12.245 1.00 34.72 C ANISOU 1043 CB GLU A 152 5231 3837 4125 -465 -218 -313 C ATOM 1044 CG GLU A 152 31.473 -7.835 13.491 1.00 38.80 C ANISOU 1044 CG GLU A 152 5871 4286 4585 -460 -216 -344 C ATOM 1045 CD GLU A 152 32.751 -7.617 14.341 1.00 36.96 C ANISOU 1045 CD GLU A 152 5677 4052 4313 -550 -273 -352 C ATOM 1046 OE1 GLU A 152 33.748 -7.103 13.791 1.00 41.97 O ANISOU 1046 OE1 GLU A 152 6310 4686 4951 -626 -313 -339 O ATOM 1047 OE2 GLU A 152 32.802 -8.010 15.520 1.00 37.41 O1- ANISOU 1047 OE2 GLU A 152 5759 4117 4338 -549 -280 -367 O1- ATOM 1048 N THR A 153 31.713 -11.052 10.120 1.00 26.46 N ANISOU 1048 N THR A 153 3935 2934 3185 -426 -195 -261 N ATOM 1049 CA THR A 153 32.215 -11.586 8.860 1.00 24.96 C ANISOU 1049 CA THR A 153 3657 2791 3034 -444 -202 -236 C ATOM 1050 C THR A 153 31.741 -13.030 8.712 1.00 25.72 C ANISOU 1050 C THR A 153 3669 2943 3159 -396 -180 -227 C ATOM 1051 O THR A 153 31.527 -13.736 9.701 1.00 26.40 O ANISOU 1051 O THR A 153 3752 3045 3233 -376 -176 -236 O ATOM 1052 CB THR A 153 33.748 -11.539 8.778 1.00 28.44 C ANISOU 1052 CB THR A 153 4072 3262 3470 -527 -248 -225 C ATOM 1053 CG2 THR A 153 34.279 -10.126 9.103 1.00 25.90 C ANISOU 1053 CG2 THR A 153 3843 2883 3114 -587 -276 -235 C ATOM 1054 OG1 THR A 153 34.296 -12.452 9.730 1.00 27.59 O ANISOU 1054 OG1 THR A 153 3933 3197 3353 -538 -266 -228 O ATOM 1055 N LEU A 154 31.572 -13.455 7.480 1.00 21.36 N ANISOU 1055 N LEU A 154 3055 2419 2642 -382 -168 -209 N ATOM 1056 CA LEU A 154 31.044 -14.778 7.236 1.00 20.03 C ANISOU 1056 CA LEU A 154 2816 2296 2499 -338 -148 -201 C ATOM 1057 C LEU A 154 32.137 -15.828 7.432 1.00 23.75 C ANISOU 1057 C LEU A 154 3226 2822 2976 -369 -172 -193 C ATOM 1058 O LEU A 154 33.314 -15.559 7.182 1.00 18.44 O ANISOU 1058 O LEU A 154 2539 2165 2301 -423 -201 -185 O ATOM 1059 CB LEU A 154 30.468 -14.869 5.828 1.00 21.93 C ANISOU 1059 CB LEU A 154 3018 2545 2770 -314 -128 -184 C ATOM 1060 CG LEU A 154 29.268 -13.947 5.600 1.00 23.37 C ANISOU 1060 CG LEU A 154 3250 2678 2950 -272 -102 -187 C ATOM 1061 CD1 LEU A 154 28.863 -13.892 4.123 1.00 17.67 C ANISOU 1061 CD1 LEU A 154 2494 1965 2256 -259 -90 -168 C ATOM 1062 CD2 LEU A 154 28.113 -14.395 6.478 1.00 22.19 C ANISOU 1062 CD2 LEU A 154 3111 2526 2794 -214 -74 -195 C ATOM 1063 N PRO A 155 31.768 -17.026 7.893 1.00 22.68 N ANISOU 1063 N PRO A 155 3054 2717 2847 -335 -162 -192 N ATOM 1064 CA PRO A 155 32.784 -18.032 8.230 1.00 18.12 C ANISOU 1064 CA PRO A 155 2426 2187 2272 -357 -185 -185 C ATOM 1065 C PRO A 155 33.399 -18.697 7.015 1.00 19.24 C ANISOU 1065 C PRO A 155 2497 2371 2443 -364 -187 -167 C ATOM 1066 O PRO A 155 32.725 -18.970 6.015 1.00 19.91 O ANISOU 1066 O PRO A 155 2558 2457 2550 -335 -164 -160 O ATOM 1067 CB PRO A 155 32.008 -19.045 9.082 1.00 18.38 C ANISOU 1067 CB PRO A 155 2454 2230 2301 -313 -168 -190 C ATOM 1068 CG PRO A 155 30.600 -18.921 8.615 1.00 18.07 C ANISOU 1068 CG PRO A 155 2425 2168 2274 -266 -132 -191 C ATOM 1069 CD PRO A 155 30.408 -17.462 8.267 1.00 20.03 C ANISOU 1069 CD PRO A 155 2727 2372 2513 -277 -129 -197 C ATOM 1070 N THR A 156 34.696 -19.001 7.138 1.00 19.33 N ANISOU 1070 N THR A 156 2473 2419 2453 -401 -215 -157 N ATOM 1071 CA THR A 156 35.484 -19.627 6.079 1.00 18.12 C ANISOU 1071 CA THR A 156 2252 2311 2323 -408 -217 -138 C ATOM 1072 C THR A 156 36.138 -20.941 6.502 1.00 19.02 C ANISOU 1072 C THR A 156 2315 2472 2441 -395 -227 -130 C ATOM 1073 O THR A 156 36.890 -21.520 5.706 1.00 18.74 O ANISOU 1073 O THR A 156 2223 2477 2422 -396 -228 -114 O ATOM 1074 CB THR A 156 36.564 -18.649 5.579 1.00 17.76 C ANISOU 1074 CB THR A 156 2202 2273 2272 -467 -239 -127 C ATOM 1075 CG2 THR A 156 35.951 -17.300 5.191 1.00 19.12 C ANISOU 1075 CG2 THR A 156 2435 2392 2437 -482 -231 -135 C ATOM 1076 OG1 THR A 156 37.538 -18.448 6.616 1.00 19.12 O ANISOU 1076 OG1 THR A 156 2381 2460 2423 -510 -275 -126 O ATOM 1077 N THR A 157 35.891 -21.422 7.727 1.00 17.34 N ANISOU 1077 N THR A 157 2121 2254 2212 -380 -234 -138 N ATOM 1078 CA THR A 157 36.363 -22.730 8.188 1.00 19.34 C ANISOU 1078 CA THR A 157 2333 2546 2469 -360 -243 -129 C ATOM 1079 C THR A 157 35.278 -23.338 9.063 1.00 18.79 C ANISOU 1079 C THR A 157 2294 2454 2390 -322 -228 -141 C ATOM 1080 O THR A 157 34.307 -22.667 9.430 1.00 16.33 O ANISOU 1080 O THR A 157 2033 2104 2067 -315 -213 -155 O ATOM 1081 CB THR A 157 37.646 -22.663 9.030 1.00 18.78 C ANISOU 1081 CB THR A 157 2249 2507 2382 -399 -282 -120 C ATOM 1082 CG2 THR A 157 38.742 -21.825 8.340 1.00 21.27 C ANISOU 1082 CG2 THR A 157 2539 2844 2701 -450 -301 -106 C ATOM 1083 OG1 THR A 157 37.328 -22.086 10.301 1.00 20.56 O ANISOU 1083 OG1 THR A 157 2534 2700 2576 -416 -296 -135 O ATOM 1084 N GLU A 158 35.447 -24.618 9.413 1.00 18.89 N ANISOU 1084 N GLU A 158 2276 2493 2406 -296 -230 -133 N ATOM 1085 CA GLU A 158 34.466 -25.260 10.283 1.00 17.59 C ANISOU 1085 CA GLU A 158 2139 2312 2232 -265 -217 -140 C ATOM 1086 C GLU A 158 34.402 -24.573 11.639 1.00 21.24 C ANISOU 1086 C GLU A 158 2655 2755 2662 -285 -232 -152 C ATOM 1087 O GLU A 158 33.306 -24.289 12.147 1.00 19.87 O ANISOU 1087 O GLU A 158 2525 2551 2475 -267 -211 -164 O ATOM 1088 CB GLU A 158 34.775 -26.744 10.465 1.00 22.24 C ANISOU 1088 CB GLU A 158 2693 2928 2828 -238 -221 -128 C ATOM 1089 CG GLU A 158 33.640 -27.522 11.155 1.00 19.40 C ANISOU 1089 CG GLU A 158 2359 2552 2461 -207 -204 -132 C ATOM 1090 CD GLU A 158 33.952 -29.002 11.242 1.00 24.79 C ANISOU 1090 CD GLU A 158 3013 3256 3150 -181 -209 -118 C ATOM 1091 OE1 GLU A 158 34.759 -29.407 12.122 1.00 25.75 O ANISOU 1091 OE1 GLU A 158 3130 3396 3257 -186 -234 -110 O ATOM 1092 OE2 GLU A 158 33.435 -29.751 10.386 1.00 22.36 O1- ANISOU 1092 OE2 GLU A 158 2689 2945 2861 -157 -189 -114 O1- ATOM 1093 N ASP A 159 35.562 -24.268 12.231 1.00 20.50 N ANISOU 1093 N ASP A 159 2558 2679 2550 -322 -268 -148 N ATOM 1094 CA ASP A 159 35.540 -23.617 13.537 1.00 19.36 C ANISOU 1094 CA ASP A 159 2472 2514 2369 -345 -285 -160 C ATOM 1095 C ASP A 159 34.914 -22.230 13.453 1.00 20.58 C ANISOU 1095 C ASP A 159 2687 2623 2511 -360 -272 -179 C ATOM 1096 O ASP A 159 34.148 -21.844 14.346 1.00 22.87 O ANISOU 1096 O ASP A 159 3035 2880 2773 -349 -260 -195 O ATOM 1097 CB ASP A 159 36.940 -23.544 14.141 1.00 21.40 C ANISOU 1097 CB ASP A 159 2715 2805 2612 -389 -332 -149 C ATOM 1098 CG ASP A 159 37.390 -24.860 14.713 1.00 24.93 C ANISOU 1098 CG ASP A 159 3125 3288 3058 -368 -346 -133 C ATOM 1099 OD1 ASP A 159 36.547 -25.772 14.854 1.00 25.30 O ANISOU 1099 OD1 ASP A 159 3174 3327 3112 -323 -321 -134 O ATOM 1100 OD2 ASP A 159 38.594 -24.987 15.020 1.00 27.04 O1- ANISOU 1100 OD2 ASP A 159 3361 3592 3320 -396 -384 -117 O1- ATOM 1101 N GLU A 160 35.218 -21.458 12.405 1.00 18.57 N ANISOU 1101 N GLU A 160 2421 2363 2273 -382 -272 -176 N ATOM 1102 CA GLU A 160 34.561 -20.158 12.275 1.00 20.43 C ANISOU 1102 CA GLU A 160 2717 2549 2496 -389 -258 -192 C ATOM 1103 C GLU A 160 33.054 -20.320 12.148 1.00 18.28 C ANISOU 1103 C GLU A 160 2464 2250 2231 -334 -214 -201 C ATOM 1104 O GLU A 160 32.288 -19.504 12.679 1.00 19.27 O ANISOU 1104 O GLU A 160 2652 2334 2334 -323 -198 -217 O ATOM 1105 CB GLU A 160 35.136 -19.384 11.085 1.00 16.41 C ANISOU 1105 CB GLU A 160 2190 2040 2005 -422 -265 -184 C ATOM 1106 CG GLU A 160 36.581 -18.936 11.324 1.00 17.72 C ANISOU 1106 CG GLU A 160 2347 2229 2158 -487 -310 -174 C ATOM 1107 CD GLU A 160 37.169 -18.170 10.162 1.00 20.43 C ANISOU 1107 CD GLU A 160 2671 2575 2516 -524 -316 -163 C ATOM 1108 OE1 GLU A 160 36.457 -17.913 9.163 1.00 20.66 O ANISOU 1108 OE1 GLU A 160 2700 2584 2564 -499 -286 -164 O ATOM 1109 OE2 GLU A 160 38.365 -17.838 10.243 1.00 25.29 O1- ANISOU 1109 OE2 GLU A 160 3268 3217 3123 -580 -352 -150 O1- ATOM 1110 N TRP A 161 32.615 -21.387 11.482 1.00 18.65 N ANISOU 1110 N TRP A 161 2457 2321 2307 -299 -194 -189 N ATOM 1111 CA TRP A 161 31.190 -21.685 11.369 1.00 18.23 C ANISOU 1111 CA TRP A 161 2412 2254 2262 -251 -156 -191 C ATOM 1112 C TRP A 161 30.587 -21.993 12.733 1.00 20.90 C ANISOU 1112 C TRP A 161 2786 2583 2572 -231 -147 -200 C ATOM 1113 O TRP A 161 29.571 -21.406 13.122 1.00 18.10 O ANISOU 1113 O TRP A 161 2474 2199 2203 -206 -120 -210 O ATOM 1114 CB TRP A 161 31.001 -22.852 10.398 1.00 17.01 C ANISOU 1114 CB TRP A 161 2194 2128 2140 -228 -145 -176 C ATOM 1115 CG TRP A 161 29.662 -23.533 10.427 1.00 20.02 C ANISOU 1115 CG TRP A 161 2571 2507 2529 -186 -114 -172 C ATOM 1116 CD1 TRP A 161 29.334 -24.661 11.131 1.00 17.48 C ANISOU 1116 CD1 TRP A 161 2238 2201 2202 -168 -110 -167 C ATOM 1117 CD2 TRP A 161 28.479 -23.157 9.702 1.00 17.71 C ANISOU 1117 CD2 TRP A 161 2280 2199 2250 -160 -85 -169 C ATOM 1118 CE2 TRP A 161 27.476 -24.098 10.026 1.00 18.94 C ANISOU 1118 CE2 TRP A 161 2423 2366 2409 -130 -65 -161 C ATOM 1119 CE3 TRP A 161 28.165 -22.115 8.822 1.00 19.48 C ANISOU 1119 CE3 TRP A 161 2516 2403 2484 -160 -75 -170 C ATOM 1120 NE1 TRP A 161 28.021 -24.999 10.904 1.00 12.70 N ANISOU 1120 NE1 TRP A 161 1628 1592 1606 -137 -80 -160 N ATOM 1121 CZ2 TRP A 161 26.184 -24.021 9.505 1.00 17.58 C ANISOU 1121 CZ2 TRP A 161 2242 2189 2249 -102 -37 -153 C ATOM 1122 CZ3 TRP A 161 26.871 -22.045 8.303 1.00 17.49 C ANISOU 1122 CZ3 TRP A 161 2258 2144 2245 -127 -47 -162 C ATOM 1123 CH2 TRP A 161 25.902 -22.988 8.654 1.00 17.97 C ANISOU 1123 CH2 TRP A 161 2300 2220 2308 -99 -29 -153 C ATOM 1124 N LEU A 162 31.214 -22.903 13.486 1.00 18.31 N ANISOU 1124 N LEU A 162 2441 2281 2234 -239 -168 -194 N ATOM 1125 CA LEU A 162 30.717 -23.226 14.819 1.00 18.84 C ANISOU 1125 CA LEU A 162 2545 2343 2271 -224 -161 -201 C ATOM 1126 C LEU A 162 30.726 -21.995 15.713 1.00 22.19 C ANISOU 1126 C LEU A 162 3044 2733 2656 -241 -165 -221 C ATOM 1127 O LEU A 162 29.796 -21.782 16.498 1.00 17.72 O ANISOU 1127 O LEU A 162 2522 2146 2066 -215 -139 -231 O ATOM 1128 CB LEU A 162 31.561 -24.336 15.437 1.00 17.44 C ANISOU 1128 CB LEU A 162 2340 2199 2088 -235 -189 -189 C ATOM 1129 CG LEU A 162 31.469 -25.690 14.719 1.00 18.26 C ANISOU 1129 CG LEU A 162 2383 2330 2223 -211 -182 -171 C ATOM 1130 CD1 LEU A 162 32.497 -26.674 15.302 1.00 20.37 C ANISOU 1130 CD1 LEU A 162 2626 2628 2484 -220 -214 -159 C ATOM 1131 CD2 LEU A 162 30.061 -26.258 14.816 1.00 13.94 C ANISOU 1131 CD2 LEU A 162 1841 1776 1680 -173 -145 -168 C ATOM 1132 N GLU A 163 31.777 -21.180 15.612 1.00 21.11 N ANISOU 1132 N GLU A 163 2923 2589 2511 -287 -199 -225 N ATOM 1133 CA GLU A 163 31.856 -19.964 16.412 1.00 24.24 C ANISOU 1133 CA GLU A 163 3399 2945 2866 -310 -208 -246 C ATOM 1134 C GLU A 163 30.709 -19.020 16.077 1.00 22.60 C ANISOU 1134 C GLU A 163 3237 2694 2658 -277 -168 -259 C ATOM 1135 O GLU A 163 30.079 -18.439 16.973 1.00 24.54 O ANISOU 1135 O GLU A 163 3551 2905 2866 -259 -150 -276 O ATOM 1136 CB GLU A 163 33.204 -19.283 16.171 1.00 24.64 C ANISOU 1136 CB GLU A 163 3451 2999 2912 -373 -253 -244 C ATOM 1137 CG GLU A 163 33.669 -18.401 17.309 1.00 38.04 C ANISOU 1137 CG GLU A 163 5228 4667 4559 -414 -282 -261 C ATOM 1138 CD GLU A 163 33.936 -19.199 18.578 1.00 44.92 C ANISOU 1138 CD GLU A 163 6105 5561 5401 -417 -300 -260 C ATOM 1139 OE1 GLU A 163 33.115 -19.107 19.519 1.00 49.23 O ANISOU 1139 OE1 GLU A 163 6710 6081 5913 -389 -277 -276 O ATOM 1140 OE2 GLU A 163 34.962 -19.923 18.633 1.00 46.00 O1- ANISOU 1140 OE2 GLU A 163 6188 5744 5547 -444 -337 -241 O1- ATOM 1141 N ALA A 164 30.418 -18.863 14.784 1.00 20.65 N ANISOU 1141 N ALA A 164 2952 2446 2447 -265 -153 -249 N ATOM 1142 CA ALA A 164 29.353 -17.965 14.377 1.00 21.38 C ANISOU 1142 CA ALA A 164 3083 2500 2541 -230 -117 -257 C ATOM 1143 C ALA A 164 28.009 -18.470 14.877 1.00 22.06 C ANISOU 1143 C ALA A 164 3170 2588 2622 -171 -74 -256 C ATOM 1144 O ALA A 164 27.205 -17.689 15.391 1.00 23.41 O ANISOU 1144 O ALA A 164 3401 2724 2770 -140 -46 -269 O ATOM 1145 CB ALA A 164 29.365 -17.802 12.856 1.00 19.39 C ANISOU 1145 CB ALA A 164 2785 2254 2330 -231 -114 -243 C ATOM 1146 N LEU A 165 27.773 -19.785 14.792 1.00 20.62 N ANISOU 1146 N LEU A 165 2925 2447 2461 -155 -68 -240 N ATOM 1147 CA LEU A 165 26.493 -20.336 15.227 1.00 20.47 C ANISOU 1147 CA LEU A 165 2900 2438 2440 -106 -28 -234 C ATOM 1148 C LEU A 165 26.356 -20.281 16.745 1.00 21.20 C ANISOU 1148 C LEU A 165 3049 2519 2485 -100 -21 -247 C ATOM 1149 O LEU A 165 25.246 -20.111 17.268 1.00 19.06 O ANISOU 1149 O LEU A 165 2804 2240 2199 -57 19 -249 O ATOM 1150 CB LEU A 165 26.344 -21.775 14.739 1.00 16.72 C ANISOU 1150 CB LEU A 165 2350 2005 1995 -100 -28 -212 C ATOM 1151 CG LEU A 165 26.232 -22.055 13.233 1.00 20.43 C ANISOU 1151 CG LEU A 165 2764 2491 2510 -98 -27 -197 C ATOM 1152 CD1 LEU A 165 25.569 -23.404 12.977 1.00 18.96 C ANISOU 1152 CD1 LEU A 165 2524 2337 2344 -79 -15 -177 C ATOM 1153 CD2 LEU A 165 25.533 -20.951 12.491 1.00 22.16 C ANISOU 1153 CD2 LEU A 165 3000 2683 2738 -78 -6 -198 C ATOM 1154 N ARG A 166 27.470 -20.404 17.469 1.00 21.31 N ANISOU 1154 N ARG A 166 3084 2537 2476 -141 -60 -255 N ATOM 1155 CA ARG A 166 27.413 -20.234 18.916 1.00 22.26 C ANISOU 1155 CA ARG A 166 3269 2644 2546 -140 -58 -270 C ATOM 1156 C ARG A 166 27.003 -18.816 19.278 1.00 21.26 C ANISOU 1156 C ARG A 166 3227 2465 2385 -127 -38 -293 C ATOM 1157 O ARG A 166 26.244 -18.606 20.230 1.00 23.13 O ANISOU 1157 O ARG A 166 3516 2687 2586 -94 -7 -304 O ATOM 1158 CB ARG A 166 28.762 -20.600 19.540 1.00 25.66 C ANISOU 1158 CB ARG A 166 3702 3089 2957 -192 -110 -271 C ATOM 1159 CG ARG A 166 28.710 -21.959 20.213 1.00 35.69 C ANISOU 1159 CG ARG A 166 4939 4398 4224 -183 -112 -256 C ATOM 1160 CD ARG A 166 30.079 -22.489 20.604 1.00 43.62 C ANISOU 1160 CD ARG A 166 5926 5426 5220 -229 -166 -249 C ATOM 1161 NE ARG A 166 30.166 -23.935 20.402 1.00 44.87 N ANISOU 1161 NE ARG A 166 6017 5624 5405 -217 -170 -226 N ATOM 1162 CZ ARG A 166 31.042 -24.529 19.600 1.00 41.22 C ANISOU 1162 CZ ARG A 166 5494 5190 4978 -234 -198 -211 C ATOM 1163 NH1 ARG A 166 31.889 -23.828 18.864 1.00 41.61 N1+ ANISOU 1163 NH1 ARG A 166 5530 5238 5041 -265 -222 -213 N1+ ATOM 1164 NH2 ARG A 166 31.081 -25.860 19.547 1.00 36.38 N ANISOU 1164 NH2 ARG A 166 4833 4606 4382 -218 -200 -191 N ATOM 1165 N LEU A 167 27.492 -17.832 18.529 1.00 21.51 N ANISOU 1165 N LEU A 167 3278 2469 2427 -152 -56 -301 N ATOM 1166 CA LEU A 167 27.040 -16.459 18.733 1.00 23.93 C ANISOU 1166 CA LEU A 167 3670 2718 2704 -134 -35 -321 C ATOM 1167 C LEU A 167 25.537 -16.347 18.536 1.00 22.04 C ANISOU 1167 C LEU A 167 3427 2473 2475 -61 25 -316 C ATOM 1168 O LEU A 167 24.840 -15.740 19.355 1.00 21.87 O ANISOU 1168 O LEU A 167 3474 2420 2414 -23 58 -331 O ATOM 1169 CB LEU A 167 27.776 -15.514 17.785 1.00 20.88 C ANISOU 1169 CB LEU A 167 3296 2304 2333 -174 -64 -324 C ATOM 1170 CG LEU A 167 29.230 -15.275 18.134 1.00 20.97 C ANISOU 1170 CG LEU A 167 3330 2313 2324 -250 -122 -331 C ATOM 1171 CD1 LEU A 167 29.822 -14.336 17.108 1.00 21.25 C ANISOU 1171 CD1 LEU A 167 3374 2323 2376 -288 -144 -330 C ATOM 1172 CD2 LEU A 167 29.259 -14.669 19.515 1.00 22.81 C ANISOU 1172 CD2 LEU A 167 3664 2508 2495 -258 -126 -357 C ATOM 1173 N VAL A 168 25.023 -16.938 17.452 1.00 21.58 N ANISOU 1173 N VAL A 168 3288 2446 2466 -39 39 -293 N ATOM 1174 CA VAL A 168 23.585 -16.922 17.193 1.00 21.52 C ANISOU 1174 CA VAL A 168 3262 2444 2471 27 92 -280 C ATOM 1175 C VAL A 168 22.828 -17.568 18.353 1.00 20.87 C ANISOU 1175 C VAL A 168 3186 2383 2361 61 125 -278 C ATOM 1176 O VAL A 168 21.833 -17.027 18.848 1.00 20.70 O ANISOU 1176 O VAL A 168 3203 2345 2316 115 170 -283 O ATOM 1177 CB VAL A 168 23.283 -17.618 15.850 1.00 21.65 C ANISOU 1177 CB VAL A 168 3186 2497 2543 31 92 -253 C ATOM 1178 CG1 VAL A 168 21.772 -17.872 15.691 1.00 17.51 C ANISOU 1178 CG1 VAL A 168 2627 1994 2033 94 142 -234 C ATOM 1179 CG2 VAL A 168 23.825 -16.787 14.684 1.00 17.22 C ANISOU 1179 CG2 VAL A 168 2628 1910 2005 8 70 -255 C ATOM 1180 N ASP A 169 23.298 -18.731 18.808 1.00 19.96 N ANISOU 1180 N ASP A 169 3033 2305 2245 33 103 -270 N ATOM 1181 CA ASP A 169 22.636 -19.439 19.900 1.00 22.09 C ANISOU 1181 CA ASP A 169 3307 2599 2489 58 132 -265 C ATOM 1182 C ASP A 169 22.662 -18.632 21.190 1.00 22.09 C ANISOU 1182 C ASP A 169 3404 2562 2428 68 144 -291 C ATOM 1183 O ASP A 169 21.676 -18.609 21.932 1.00 22.09 O ANISOU 1183 O ASP A 169 3427 2566 2401 116 191 -290 O ATOM 1184 CB ASP A 169 23.313 -20.788 20.139 1.00 20.81 C ANISOU 1184 CB ASP A 169 3096 2475 2335 20 98 -252 C ATOM 1185 CG ASP A 169 22.463 -21.737 20.969 1.00 26.30 C ANISOU 1185 CG ASP A 169 3774 3203 3016 47 130 -236 C ATOM 1186 OD1 ASP A 169 21.233 -21.528 21.073 1.00 28.88 O ANISOU 1186 OD1 ASP A 169 4099 3535 3339 96 180 -228 O ATOM 1187 OD2 ASP A 169 23.037 -22.676 21.542 1.00 28.44 O1- ANISOU 1187 OD2 ASP A 169 4033 3495 3277 19 104 -231 O1- ATOM 1188 N GLU A 170 23.792 -17.998 21.505 1.00 23.19 N ANISOU 1188 N GLU A 170 3602 2668 2541 21 102 -314 N ATOM 1189 CA GLU A 170 23.878 -17.319 22.792 1.00 23.68 C ANISOU 1189 CA GLU A 170 3764 2695 2539 24 108 -341 C ATOM 1190 C GLU A 170 23.224 -15.946 22.776 1.00 22.73 C ANISOU 1190 C GLU A 170 3722 2520 2396 67 145 -360 C ATOM 1191 O GLU A 170 22.691 -15.522 23.807 1.00 22.20 O ANISOU 1191 O GLU A 170 3728 2431 2278 102 179 -377 O ATOM 1192 CB GLU A 170 25.341 -17.226 23.249 1.00 21.96 C ANISOU 1192 CB GLU A 170 3582 2465 2296 -49 44 -355 C ATOM 1193 CG GLU A 170 25.898 -18.604 23.592 1.00 29.33 C ANISOU 1193 CG GLU A 170 4454 3451 3239 -79 15 -337 C ATOM 1194 CD GLU A 170 27.349 -18.612 24.036 1.00 36.27 C ANISOU 1194 CD GLU A 170 5355 4329 4097 -149 -51 -344 C ATOM 1195 OE1 GLU A 170 28.014 -17.563 23.945 1.00 37.97 O ANISOU 1195 OE1 GLU A 170 5625 4506 4295 -184 -78 -362 O ATOM 1196 OE2 GLU A 170 27.827 -19.694 24.458 1.00 41.05 O1- ANISOU 1196 OE2 GLU A 170 5919 4974 4703 -168 -75 -329 O1- ATOM 1197 N ASN A 171 23.224 -15.255 21.628 1.00 22.97 N ANISOU 1197 N ASN A 171 3739 2528 2461 70 141 -358 N ATOM 1198 CA ASN A 171 22.810 -13.854 21.562 1.00 23.31 C ANISOU 1198 CA ASN A 171 3867 2510 2481 104 166 -377 C ATOM 1199 C ASN A 171 21.427 -13.629 20.957 1.00 23.66 C ANISOU 1199 C ASN A 171 3879 2560 2551 184 226 -360 C ATOM 1200 O ASN A 171 20.986 -12.473 20.894 1.00 23.90 O ANISOU 1200 O ASN A 171 3979 2538 2562 225 252 -373 O ATOM 1201 CB ASN A 171 23.827 -13.043 20.748 1.00 22.82 C ANISOU 1201 CB ASN A 171 3828 2409 2432 49 118 -386 C ATOM 1202 CG ASN A 171 25.138 -12.847 21.490 1.00 24.56 C ANISOU 1202 CG ASN A 171 4109 2611 2614 -27 62 -407 C ATOM 1203 ND2 ASN A 171 26.184 -12.460 20.763 1.00 21.39 N ANISOU 1203 ND2 ASN A 171 3700 2196 2229 -91 12 -406 N ATOM 1204 OD1 ASN A 171 25.209 -13.051 22.707 1.00 25.67 O ANISOU 1204 OD1 ASN A 171 4299 2750 2706 -31 63 -421 O ATOM 1205 N THR A 172 20.763 -14.674 20.457 1.00 22.24 N ANISOU 1205 N THR A 172 3596 2440 2413 206 244 -328 N ATOM 1206 CA THR A 172 19.458 -14.557 19.809 1.00 24.76 C ANISOU 1206 CA THR A 172 3870 2776 2762 275 294 -305 C ATOM 1207 C THR A 172 18.602 -15.753 20.202 1.00 25.66 C ANISOU 1207 C THR A 172 3911 2954 2884 302 326 -279 C ATOM 1208 O THR A 172 19.087 -16.738 20.762 1.00 23.63 O ANISOU 1208 O THR A 172 3631 2728 2620 262 304 -277 O ATOM 1209 CB THR A 172 19.550 -14.513 18.276 1.00 21.91 C ANISOU 1209 CB THR A 172 3443 2423 2458 261 273 -286 C ATOM 1210 CG2 THR A 172 20.795 -13.791 17.812 1.00 23.25 C ANISOU 1210 CG2 THR A 172 3659 2547 2627 202 222 -305 C ATOM 1211 OG1 THR A 172 19.586 -15.856 17.783 1.00 19.43 O ANISOU 1211 OG1 THR A 172 3028 2170 2184 234 256 -260 O ATOM 1212 N ASP A 173 17.317 -15.675 19.883 1.00 23.68 N ANISOU 1212 N ASP A 173 3620 2726 2650 367 377 -255 N ATOM 1213 CA ASP A 173 16.426 -16.789 20.147 1.00 26.38 C ANISOU 1213 CA ASP A 173 3886 3133 3004 388 407 -225 C ATOM 1214 C ASP A 173 16.319 -17.744 18.964 1.00 26.31 C ANISOU 1214 C ASP A 173 3771 3171 3054 360 383 -192 C ATOM 1215 O ASP A 173 15.495 -18.666 19.005 1.00 27.04 O ANISOU 1215 O ASP A 173 3794 3317 3161 373 406 -162 O ATOM 1216 CB ASP A 173 15.049 -16.256 20.532 1.00 26.45 C ANISOU 1216 CB ASP A 173 3904 3151 2995 475 477 -212 C ATOM 1217 CG ASP A 173 15.067 -15.559 21.871 1.00 35.25 C ANISOU 1217 CG ASP A 173 5124 4227 4043 505 508 -243 C ATOM 1218 OD1 ASP A 173 14.936 -14.319 21.887 1.00 42.79 O ANISOU 1218 OD1 ASP A 173 6155 5127 4976 548 528 -263 O ATOM 1219 OD2 ASP A 173 15.242 -16.243 22.903 1.00 43.71 O1- ANISOU 1219 OD2 ASP A 173 6208 5318 5081 486 510 -248 O1- ATOM 1220 N ALA A 174 17.140 -17.559 17.926 1.00 21.32 N ANISOU 1220 N ALA A 174 3127 2519 2454 318 338 -198 N ATOM 1221 CA ALA A 174 17.003 -18.342 16.705 1.00 23.42 C ANISOU 1221 CA ALA A 174 3302 2823 2772 297 318 -169 C ATOM 1222 C ALA A 174 17.638 -19.714 16.862 1.00 21.98 C ANISOU 1222 C ALA A 174 3076 2676 2600 242 284 -163 C ATOM 1223 O ALA A 174 18.644 -19.875 17.555 1.00 22.13 O ANISOU 1223 O ALA A 174 3136 2679 2595 204 256 -185 O ATOM 1224 CB ALA A 174 17.652 -17.627 15.522 1.00 20.43 C ANISOU 1224 CB ALA A 174 2930 2413 2421 274 285 -177 C ATOM 1225 N ILE A 175 17.048 -20.706 16.204 1.00 20.12 N ANISOU 1225 N ILE A 175 2759 2486 2399 237 285 -132 N ATOM 1226 CA ILE A 175 17.735 -21.986 16.007 1.00 21.45 C ANISOU 1226 CA ILE A 175 2887 2679 2585 184 247 -125 C ATOM 1227 C ILE A 175 18.905 -21.743 15.057 1.00 19.40 C ANISOU 1227 C ILE A 175 2629 2395 2346 143 201 -139 C ATOM 1228 O ILE A 175 18.689 -21.243 13.943 1.00 19.83 O ANISOU 1228 O ILE A 175 2663 2442 2428 151 199 -132 O ATOM 1229 CB ILE A 175 16.789 -23.058 15.444 1.00 19.62 C ANISOU 1229 CB ILE A 175 2576 2496 2382 185 257 -88 C ATOM 1230 CG1 ILE A 175 15.642 -23.340 16.406 1.00 20.86 C ANISOU 1230 CG1 ILE A 175 2724 2684 2517 221 303 -69 C ATOM 1231 CG2 ILE A 175 17.565 -24.331 15.100 1.00 19.68 C ANISOU 1231 CG2 ILE A 175 2551 2519 2408 133 216 -83 C ATOM 1232 CD1 ILE A 175 14.500 -24.118 15.754 1.00 20.54 C ANISOU 1232 CD1 ILE A 175 2604 2693 2506 226 318 -27 C ATOM 1233 N PRO A 176 20.148 -22.060 15.433 1.00 19.68 N ANISOU 1233 N PRO A 176 2687 2419 2370 100 164 -157 N ATOM 1234 CA PRO A 176 21.276 -21.625 14.585 1.00 18.26 C ANISOU 1234 CA PRO A 176 2514 2218 2207 65 125 -170 C ATOM 1235 C PRO A 176 21.335 -22.309 13.222 1.00 19.52 C ANISOU 1235 C PRO A 176 2607 2400 2410 48 108 -152 C ATOM 1236 O PRO A 176 21.551 -21.624 12.212 1.00 16.61 O ANISOU 1236 O PRO A 176 2236 2017 2061 43 98 -153 O ATOM 1237 CB PRO A 176 22.512 -21.932 15.450 1.00 18.41 C ANISOU 1237 CB PRO A 176 2563 2231 2201 26 91 -188 C ATOM 1238 CG PRO A 176 22.008 -21.988 16.846 1.00 18.34 C ANISOU 1238 CG PRO A 176 2594 2222 2152 47 117 -193 C ATOM 1239 CD PRO A 176 20.592 -22.522 16.759 1.00 19.17 C ANISOU 1239 CD PRO A 176 2657 2357 2269 87 158 -168 C ATOM 1240 N TYR A 177 21.160 -23.632 13.159 1.00 16.84 N ANISOU 1240 N TYR A 177 2220 2094 2083 37 102 -134 N ATOM 1241 CA TYR A 177 21.115 -24.369 11.895 1.00 17.60 C ANISOU 1241 CA TYR A 177 2261 2210 2215 22 88 -117 C ATOM 1242 C TYR A 177 19.949 -25.343 11.950 1.00 16.74 C ANISOU 1242 C TYR A 177 2111 2133 2114 36 108 -90 C ATOM 1243 O TYR A 177 19.855 -26.125 12.898 1.00 17.95 O ANISOU 1243 O TYR A 177 2269 2301 2251 32 112 -86 O ATOM 1244 CB TYR A 177 22.410 -25.150 11.630 1.00 17.75 C ANISOU 1244 CB TYR A 177 2268 2233 2242 -16 49 -123 C ATOM 1245 CG TYR A 177 22.402 -25.844 10.283 1.00 20.20 C ANISOU 1245 CG TYR A 177 2531 2559 2585 -28 37 -109 C ATOM 1246 CD1 TYR A 177 22.675 -25.130 9.125 1.00 20.15 C ANISOU 1246 CD1 TYR A 177 2518 2542 2597 -34 29 -111 C ATOM 1247 CD2 TYR A 177 22.082 -27.198 10.161 1.00 17.60 C ANISOU 1247 CD2 TYR A 177 2171 2253 2265 -35 33 -92 C ATOM 1248 CE1 TYR A 177 22.652 -25.737 7.882 1.00 20.68 C ANISOU 1248 CE1 TYR A 177 2547 2621 2688 -44 19 -99 C ATOM 1249 CE2 TYR A 177 22.060 -27.825 8.913 1.00 18.21 C ANISOU 1249 CE2 TYR A 177 2215 2339 2367 -47 21 -81 C ATOM 1250 CZ TYR A 177 22.342 -27.079 7.775 1.00 22.88 C ANISOU 1250 CZ TYR A 177 2800 2921 2974 -51 15 -86 C ATOM 1251 OH TYR A 177 22.322 -27.656 6.522 1.00 22.66 O ANISOU 1251 OH TYR A 177 2743 2901 2966 -62 4 -76 O ATOM 1252 N TYR A 178 19.079 -25.314 10.928 1.00 18.06 N ANISOU 1252 N TYR A 178 2241 2315 2307 47 118 -70 N ATOM 1253 CA TYR A 178 17.882 -26.153 10.858 1.00 18.12 C ANISOU 1253 CA TYR A 178 2204 2356 2323 55 135 -40 C ATOM 1254 C TYR A 178 18.109 -27.241 9.814 1.00 18.14 C ANISOU 1254 C TYR A 178 2171 2372 2350 21 107 -28 C ATOM 1255 O TYR A 178 18.248 -26.942 8.619 1.00 17.08 O ANISOU 1255 O TYR A 178 2021 2232 2236 14 93 -27 O ATOM 1256 CB TYR A 178 16.666 -25.295 10.526 1.00 15.95 C ANISOU 1256 CB TYR A 178 1913 2092 2056 93 166 -23 C ATOM 1257 CG TYR A 178 15.318 -25.943 10.737 1.00 20.01 C ANISOU 1257 CG TYR A 178 2383 2648 2573 106 191 12 C ATOM 1258 CD1 TYR A 178 14.686 -26.647 9.719 1.00 17.93 C ANISOU 1258 CD1 TYR A 178 2066 2411 2334 87 179 40 C ATOM 1259 CD2 TYR A 178 14.679 -25.859 11.973 1.00 20.35 C ANISOU 1259 CD2 TYR A 178 2436 2704 2590 133 226 18 C ATOM 1260 CE1 TYR A 178 13.440 -27.226 9.923 1.00 19.39 C ANISOU 1260 CE1 TYR A 178 2207 2639 2521 91 198 76 C ATOM 1261 CE2 TYR A 178 13.445 -26.433 12.176 1.00 22.16 C ANISOU 1261 CE2 TYR A 178 2619 2977 2821 142 251 53 C ATOM 1262 CZ TYR A 178 12.832 -27.108 11.142 1.00 19.55 C ANISOU 1262 CZ TYR A 178 2234 2677 2519 119 235 83 C ATOM 1263 OH TYR A 178 11.612 -27.690 11.360 1.00 23.89 O ANISOU 1263 OH TYR A 178 2734 3274 3070 121 256 122 O ATOM 1264 N THR A 179 18.147 -28.505 10.275 1.00 18.95 N ANISOU 1264 N THR A 179 2264 2488 2446 0 98 -20 N ATOM 1265 CA THR A 179 18.544 -29.632 9.422 1.00 20.12 C ANISOU 1265 CA THR A 179 2394 2641 2612 -31 69 -13 C ATOM 1266 C THR A 179 17.452 -30.070 8.448 1.00 17.91 C ANISOU 1266 C THR A 179 2072 2382 2349 -40 71 15 C ATOM 1267 O THR A 179 17.774 -30.673 7.423 1.00 19.74 O ANISOU 1267 O THR A 179 2294 2610 2595 -63 47 16 O ATOM 1268 CB THR A 179 18.939 -30.867 10.260 1.00 18.94 C ANISOU 1268 CB THR A 179 2255 2493 2447 -50 58 -12 C ATOM 1269 CG2 THR A 179 20.015 -30.521 11.299 1.00 14.84 C ANISOU 1269 CG2 THR A 179 1774 1957 1906 -45 52 -36 C ATOM 1270 OG1 THR A 179 17.792 -31.410 10.924 1.00 15.88 O ANISOU 1270 OG1 THR A 179 1853 2130 2050 -48 79 13 O ATOM 1271 N ASN A 180 16.173 -29.815 8.754 1.00 17.50 N ANISOU 1271 N ASN A 180 1996 2356 2296 -22 97 39 N ATOM 1272 CA ASN A 180 15.050 -30.400 8.001 1.00 19.60 C ANISOU 1272 CA ASN A 180 2219 2652 2578 -38 96 73 C ATOM 1273 C ASN A 180 15.205 -31.913 7.842 1.00 18.55 C ANISOU 1273 C ASN A 180 2084 2520 2444 -80 71 82 C ATOM 1274 O ASN A 180 14.900 -32.480 6.790 1.00 18.37 O ANISOU 1274 O ASN A 180 2042 2503 2434 -106 50 96 O ATOM 1275 CB ASN A 180 14.886 -29.749 6.631 1.00 16.54 C ANISOU 1275 CB ASN A 180 1811 2261 2210 -35 85 77 C ATOM 1276 CG ASN A 180 13.879 -28.623 6.644 1.00 19.84 C ANISOU 1276 CG ASN A 180 2208 2698 2632 4 114 94 C ATOM 1277 ND2 ASN A 180 14.327 -27.433 6.254 1.00 16.90 N ANISOU 1277 ND2 ASN A 180 1856 2301 2264 29 117 76 N ATOM 1278 OD1 ASN A 180 12.698 -28.821 6.967 1.00 16.93 O ANISOU 1278 OD1 ASN A 180 1803 2365 2263 12 133 126 O ATOM 1279 N TYR A 181 15.681 -32.567 8.907 1.00 18.96 N ANISOU 1279 N TYR A 181 2162 2565 2478 -86 71 74 N ATOM 1280 CA TYR A 181 15.899 -34.018 8.916 1.00 20.03 C ANISOU 1280 CA TYR A 181 2306 2695 2609 -122 48 82 C ATOM 1281 C TYR A 181 14.660 -34.794 8.456 1.00 19.66 C ANISOU 1281 C TYR A 181 2226 2675 2568 -152 45 119 C ATOM 1282 O TYR A 181 14.760 -35.700 7.619 1.00 18.66 O ANISOU 1282 O TYR A 181 2104 2539 2448 -185 18 124 O ATOM 1283 CB TYR A 181 16.345 -34.418 10.335 1.00 18.50 C ANISOU 1283 CB TYR A 181 2142 2495 2391 -117 56 74 C ATOM 1284 CG TYR A 181 16.419 -35.885 10.734 1.00 20.34 C ANISOU 1284 CG TYR A 181 2391 2724 2614 -148 39 87 C ATOM 1285 CD1 TYR A 181 15.270 -36.681 10.799 1.00 18.95 C ANISOU 1285 CD1 TYR A 181 2194 2571 2436 -176 44 122 C ATOM 1286 CD2 TYR A 181 17.616 -36.445 11.165 1.00 19.28 C ANISOU 1286 CD2 TYR A 181 2294 2563 2470 -149 20 68 C ATOM 1287 CE1 TYR A 181 15.318 -38.003 11.203 1.00 18.36 C ANISOU 1287 CE1 TYR A 181 2140 2486 2348 -207 28 135 C ATOM 1288 CE2 TYR A 181 17.668 -37.786 11.588 1.00 18.19 C ANISOU 1288 CE2 TYR A 181 2176 2415 2319 -173 6 81 C ATOM 1289 CZ TYR A 181 16.511 -38.547 11.607 1.00 17.27 C ANISOU 1289 CZ TYR A 181 2045 2317 2201 -203 10 114 C ATOM 1290 OH TYR A 181 16.536 -39.863 12.021 1.00 17.85 O ANISOU 1290 OH TYR A 181 2144 2378 2261 -230 -5 129 O ATOM 1291 N LYS A 182 13.480 -34.449 8.982 1.00 19.38 N ANISOU 1291 N LYS A 182 2158 2676 2529 -142 73 146 N ATOM 1292 CA LYS A 182 12.285 -35.243 8.685 1.00 18.30 C ANISOU 1292 CA LYS A 182 1984 2572 2396 -177 69 187 C ATOM 1293 C LYS A 182 12.008 -35.285 7.187 1.00 21.51 C ANISOU 1293 C LYS A 182 2370 2981 2822 -199 43 197 C ATOM 1294 O LYS A 182 11.792 -36.360 6.618 1.00 20.35 O ANISOU 1294 O LYS A 182 2225 2832 2675 -246 15 212 O ATOM 1295 CB LYS A 182 11.074 -34.699 9.438 1.00 19.81 C ANISOU 1295 CB LYS A 182 2135 2810 2582 -155 108 218 C ATOM 1296 CG LYS A 182 9.858 -35.643 9.406 1.00 21.85 C ANISOU 1296 CG LYS A 182 2353 3111 2840 -199 104 266 C ATOM 1297 CD LYS A 182 8.530 -34.924 9.703 1.00 24.07 C ANISOU 1297 CD LYS A 182 2573 3448 3123 -172 142 304 C ATOM 1298 CE LYS A 182 8.029 -34.135 8.492 1.00 27.81 C ANISOU 1298 CE LYS A 182 3008 3940 3621 -158 135 315 C ATOM 1299 NZ LYS A 182 7.042 -33.059 8.890 1.00 28.39 N1+ ANISOU 1299 NZ LYS A 182 3033 4058 3696 -105 179 340 N1+ ATOM 1300 N ASP A 183 12.010 -34.125 6.525 1.00 19.26 N ANISOU 1300 N ASP A 183 2069 2697 2551 -168 50 188 N ATOM 1301 CA ASP A 183 11.715 -34.121 5.094 1.00 21.50 C ANISOU 1301 CA ASP A 183 2334 2986 2851 -189 25 198 C ATOM 1302 C ASP A 183 12.857 -34.674 4.246 1.00 20.59 C ANISOU 1302 C ASP A 183 2261 2828 2736 -210 -8 169 C ATOM 1303 O ASP A 183 12.659 -34.881 3.047 1.00 19.76 O ANISOU 1303 O ASP A 183 2148 2723 2638 -235 -31 177 O ATOM 1304 CB ASP A 183 11.335 -32.712 4.641 1.00 21.12 C ANISOU 1304 CB ASP A 183 2258 2950 2815 -148 42 202 C ATOM 1305 CG ASP A 183 9.879 -32.364 4.961 1.00 23.07 C ANISOU 1305 CG ASP A 183 2448 3250 3066 -134 66 245 C ATOM 1306 OD1 ASP A 183 8.961 -32.860 4.270 1.00 22.74 O ANISOU 1306 OD1 ASP A 183 2367 3241 3031 -168 49 281 O ATOM 1307 OD2 ASP A 183 9.641 -31.635 5.939 1.00 23.42 O1- ANISOU 1307 OD2 ASP A 183 2488 3306 3103 -90 103 245 O1- ATOM 1308 N GLY A 184 14.035 -34.911 4.821 1.00 17.72 N ANISOU 1308 N GLY A 184 1939 2432 2363 -200 -8 137 N ATOM 1309 CA GLY A 184 15.043 -35.732 4.173 1.00 18.02 C ANISOU 1309 CA GLY A 184 2014 2435 2397 -220 -36 116 C ATOM 1310 C GLY A 184 15.806 -35.107 3.021 1.00 19.65 C ANISOU 1310 C GLY A 184 2229 2623 2613 -209 -47 93 C ATOM 1311 O GLY A 184 17.032 -34.977 3.082 1.00 19.44 O ANISOU 1311 O GLY A 184 2229 2571 2585 -193 -49 64 O ATOM 1312 N TRP A 185 15.114 -34.731 1.946 1.00 19.16 N ANISOU 1312 N TRP A 185 2142 2576 2561 -220 -55 109 N ATOM 1313 CA TRP A 185 15.836 -34.199 0.796 1.00 19.16 C ANISOU 1313 CA TRP A 185 2154 2559 2568 -213 -66 89 C ATOM 1314 C TRP A 185 16.708 -32.990 1.134 1.00 19.58 C ANISOU 1314 C TRP A 185 2213 2600 2625 -174 -48 65 C ATOM 1315 O TRP A 185 17.779 -32.864 0.516 1.00 19.49 O ANISOU 1315 O TRP A 185 2223 2568 2614 -171 -57 41 O ATOM 1316 CB TRP A 185 14.863 -33.874 -0.361 1.00 20.17 C ANISOU 1316 CB TRP A 185 2253 2707 2703 -229 -78 114 C ATOM 1317 CG TRP A 185 13.827 -32.853 -0.036 1.00 22.75 C ANISOU 1317 CG TRP A 185 2537 3067 3041 -206 -58 139 C ATOM 1318 CD1 TRP A 185 12.542 -33.089 0.389 1.00 24.48 C ANISOU 1318 CD1 TRP A 185 2717 3323 3261 -216 -52 176 C ATOM 1319 CD2 TRP A 185 13.960 -31.426 -0.132 1.00 22.24 C ANISOU 1319 CD2 TRP A 185 2463 3001 2985 -166 -40 132 C ATOM 1320 CE2 TRP A 185 12.728 -30.864 0.266 1.00 21.09 C ANISOU 1320 CE2 TRP A 185 2277 2891 2847 -147 -22 163 C ATOM 1321 CE3 TRP A 185 15.006 -30.571 -0.501 1.00 21.17 C ANISOU 1321 CE3 TRP A 185 2352 2839 2852 -145 -38 103 C ATOM 1322 NE1 TRP A 185 11.883 -31.897 0.581 1.00 24.53 N ANISOU 1322 NE1 TRP A 185 2690 3353 3278 -178 -29 191 N ATOM 1323 CZ2 TRP A 185 12.514 -29.492 0.305 1.00 23.34 C ANISOU 1323 CZ2 TRP A 185 2549 3178 3139 -103 -1 165 C ATOM 1324 CZ3 TRP A 185 14.794 -29.209 -0.463 1.00 22.35 C ANISOU 1324 CZ3 TRP A 185 2493 2990 3010 -109 -20 105 C ATOM 1325 CH2 TRP A 185 13.556 -28.680 -0.063 1.00 23.53 C ANISOU 1325 CH2 TRP A 185 2607 3169 3164 -86 -2 135 C ATOM 1326 N PRO A 186 16.356 -32.093 2.063 1.00 17.86 N ANISOU 1326 N PRO A 186 1983 2394 2409 -146 -24 68 N ATOM 1327 CA PRO A 186 17.272 -30.975 2.323 1.00 19.32 C ANISOU 1327 CA PRO A 186 2184 2560 2594 -117 -13 42 C ATOM 1328 C PRO A 186 18.621 -31.427 2.825 1.00 19.65 C ANISOU 1328 C PRO A 186 2257 2581 2628 -119 -20 15 C ATOM 1329 O PRO A 186 19.611 -30.718 2.613 1.00 19.23 O ANISOU 1329 O PRO A 186 2218 2512 2576 -110 -21 -6 O ATOM 1330 CB PRO A 186 16.517 -30.121 3.349 1.00 17.62 C ANISOU 1330 CB PRO A 186 1958 2360 2377 -88 15 52 C ATOM 1331 CG PRO A 186 15.059 -30.474 3.116 1.00 20.01 C ANISOU 1331 CG PRO A 186 2221 2695 2685 -96 19 89 C ATOM 1332 CD PRO A 186 15.119 -31.953 2.854 1.00 19.01 C ANISOU 1332 CD PRO A 186 2099 2569 2554 -137 -4 96 C ATOM 1333 N LEU A 187 18.707 -32.618 3.422 1.00 20.37 N ANISOU 1333 N LEU A 187 2359 2671 2710 -134 -27 18 N ATOM 1334 CA LEU A 187 19.991 -33.101 3.911 1.00 19.03 C ANISOU 1334 CA LEU A 187 2215 2483 2531 -131 -35 -4 C ATOM 1335 C LEU A 187 20.977 -33.334 2.773 1.00 22.58 C ANISOU 1335 C LEU A 187 2674 2918 2985 -137 -51 -19 C ATOM 1336 O LEU A 187 22.193 -33.268 2.988 1.00 22.71 O ANISOU 1336 O LEU A 187 2705 2926 3000 -128 -55 -38 O ATOM 1337 CB LEU A 187 19.796 -34.381 4.714 1.00 19.96 C ANISOU 1337 CB LEU A 187 2345 2600 2638 -144 -40 5 C ATOM 1338 CG LEU A 187 18.992 -34.260 6.013 1.00 19.04 C ANISOU 1338 CG LEU A 187 2223 2500 2512 -138 -21 19 C ATOM 1339 CD1 LEU A 187 18.766 -35.634 6.550 1.00 19.04 C ANISOU 1339 CD1 LEU A 187 2236 2498 2501 -158 -30 33 C ATOM 1340 CD2 LEU A 187 19.719 -33.437 7.034 1.00 21.91 C ANISOU 1340 CD2 LEU A 187 2601 2858 2866 -114 -10 0 C ATOM 1341 N SER A 188 20.495 -33.601 1.562 1.00 18.86 N ANISOU 1341 N SER A 188 2197 2449 2520 -153 -60 -10 N ATOM 1342 CA SER A 188 21.425 -33.863 0.465 1.00 18.88 C ANISOU 1342 CA SER A 188 2212 2438 2522 -156 -72 -24 C ATOM 1343 C SER A 188 21.815 -32.608 -0.307 1.00 18.72 C ANISOU 1343 C SER A 188 2182 2420 2510 -148 -67 -32 C ATOM 1344 O SER A 188 22.708 -32.668 -1.160 1.00 17.69 O ANISOU 1344 O SER A 188 2060 2283 2378 -148 -72 -44 O ATOM 1345 CB SER A 188 20.831 -34.919 -0.484 1.00 18.93 C ANISOU 1345 CB SER A 188 2229 2440 2524 -181 -87 -13 C ATOM 1346 OG SER A 188 19.667 -34.423 -1.112 1.00 19.53 O ANISOU 1346 OG SER A 188 2283 2532 2606 -195 -89 7 O ATOM 1347 N GLN A 189 21.213 -31.463 0.006 1.00 18.61 N ANISOU 1347 N GLN A 189 2153 2415 2503 -138 -56 -25 N ATOM 1348 CA GLN A 189 21.498 -30.242 -0.734 1.00 17.64 C ANISOU 1348 CA GLN A 189 2026 2289 2387 -132 -52 -30 C ATOM 1349 C GLN A 189 22.975 -29.858 -0.636 1.00 16.55 C ANISOU 1349 C GLN A 189 1900 2142 2246 -127 -53 -51 C ATOM 1350 O GLN A 189 23.579 -29.434 -1.628 1.00 16.75 O ANISOU 1350 O GLN A 189 1926 2165 2273 -132 -56 -56 O ATOM 1351 CB GLN A 189 20.615 -29.113 -0.205 1.00 17.56 C ANISOU 1351 CB GLN A 189 2006 2284 2382 -115 -37 -19 C ATOM 1352 CG GLN A 189 19.147 -29.230 -0.606 1.00 18.85 C ANISOU 1352 CG GLN A 189 2146 2465 2551 -118 -37 9 C ATOM 1353 CD GLN A 189 18.904 -28.728 -2.022 1.00 23.78 C ANISOU 1353 CD GLN A 189 2762 3091 3181 -125 -46 18 C ATOM 1354 NE2 GLN A 189 18.246 -29.541 -2.839 1.00 25.50 N ANISOU 1354 NE2 GLN A 189 2969 3320 3398 -147 -62 35 N ATOM 1355 OE1 GLN A 189 19.284 -27.613 -2.367 1.00 21.04 O ANISOU 1355 OE1 GLN A 189 2423 2734 2839 -113 -41 12 O ATOM 1356 N ALA A 190 23.586 -30.019 0.539 1.00 16.88 N ANISOU 1356 N ALA A 190 1951 2182 2283 -120 -51 -62 N ATOM 1357 CA ALA A 190 24.963 -29.556 0.705 1.00 16.36 C ANISOU 1357 CA ALA A 190 1889 2112 2213 -119 -54 -78 C ATOM 1358 C ALA A 190 25.972 -30.379 -0.095 1.00 17.07 C ANISOU 1358 C ALA A 190 1977 2207 2303 -123 -62 -84 C ATOM 1359 O ALA A 190 27.105 -29.919 -0.313 1.00 15.96 O ANISOU 1359 O ALA A 190 1832 2071 2162 -125 -64 -92 O ATOM 1360 CB ALA A 190 25.334 -29.562 2.194 1.00 18.53 C ANISOU 1360 CB ALA A 190 2174 2387 2480 -113 -54 -85 C ATOM 1361 N PHE A 191 25.599 -31.584 -0.530 1.00 17.76 N ANISOU 1361 N PHE A 191 2070 2293 2387 -124 -67 -79 N ATOM 1362 CA PHE A 191 26.488 -32.392 -1.364 1.00 15.97 C ANISOU 1362 CA PHE A 191 1847 2065 2155 -121 -70 -85 C ATOM 1363 C PHE A 191 26.808 -31.693 -2.674 1.00 17.75 C ANISOU 1363 C PHE A 191 2066 2294 2382 -127 -67 -87 C ATOM 1364 O PHE A 191 27.833 -31.992 -3.295 1.00 18.51 O ANISOU 1364 O PHE A 191 2162 2397 2474 -121 -64 -93 O ATOM 1365 CB PHE A 191 25.856 -33.757 -1.645 1.00 18.16 C ANISOU 1365 CB PHE A 191 2142 2331 2425 -124 -76 -80 C ATOM 1366 CG PHE A 191 26.773 -34.715 -2.372 1.00 19.27 C ANISOU 1366 CG PHE A 191 2298 2466 2557 -113 -78 -88 C ATOM 1367 CD1 PHE A 191 27.965 -35.124 -1.798 1.00 20.24 C ANISOU 1367 CD1 PHE A 191 2420 2593 2677 -92 -76 -96 C ATOM 1368 CD2 PHE A 191 26.458 -35.162 -3.650 1.00 19.68 C ANISOU 1368 CD2 PHE A 191 2367 2510 2601 -121 -79 -88 C ATOM 1369 CE1 PHE A 191 28.826 -35.990 -2.464 1.00 20.49 C ANISOU 1369 CE1 PHE A 191 2464 2621 2699 -72 -73 -103 C ATOM 1370 CE2 PHE A 191 27.314 -36.022 -4.330 1.00 23.62 C ANISOU 1370 CE2 PHE A 191 2886 3002 3088 -105 -76 -98 C ATOM 1371 CZ PHE A 191 28.502 -36.440 -3.733 1.00 21.42 C ANISOU 1371 CZ PHE A 191 2603 2727 2807 -77 -71 -105 C ATOM 1372 N SER A 192 25.969 -30.744 -3.097 1.00 16.80 N ANISOU 1372 N SER A 192 1941 2173 2268 -137 -65 -78 N ATOM 1373 CA SER A 192 26.234 -29.985 -4.319 1.00 18.82 C ANISOU 1373 CA SER A 192 2194 2432 2525 -145 -62 -77 C ATOM 1374 C SER A 192 27.446 -29.067 -4.197 1.00 16.68 C ANISOU 1374 C SER A 192 1914 2168 2255 -146 -58 -85 C ATOM 1375 O SER A 192 27.943 -28.578 -5.221 1.00 16.18 O ANISOU 1375 O SER A 192 1847 2110 2189 -154 -55 -84 O ATOM 1376 CB SER A 192 25.002 -29.163 -4.684 1.00 19.72 C ANISOU 1376 CB SER A 192 2305 2542 2644 -152 -63 -63 C ATOM 1377 OG SER A 192 23.924 -30.028 -4.969 1.00 19.57 O ANISOU 1377 OG SER A 192 2289 2523 2623 -158 -70 -52 O ATOM 1378 N ASN A 193 27.932 -28.818 -2.978 1.00 15.36 N ANISOU 1378 N ASN A 193 1744 2003 2090 -143 -59 -90 N ATOM 1379 CA ASN A 193 29.160 -28.051 -2.787 1.00 16.62 C ANISOU 1379 CA ASN A 193 1894 2171 2248 -151 -60 -95 C ATOM 1380 C ASN A 193 30.408 -28.842 -3.131 1.00 15.77 C ANISOU 1380 C ASN A 193 1772 2084 2137 -144 -59 -98 C ATOM 1381 O ASN A 193 31.496 -28.264 -3.121 1.00 17.96 O ANISOU 1381 O ASN A 193 2034 2377 2413 -154 -60 -98 O ATOM 1382 CB ASN A 193 29.254 -27.560 -1.340 1.00 15.49 C ANISOU 1382 CB ASN A 193 1757 2024 2105 -152 -66 -100 C ATOM 1383 CG ASN A 193 28.146 -26.570 -0.985 1.00 16.37 C ANISOU 1383 CG ASN A 193 1886 2116 2218 -153 -62 -97 C ATOM 1384 ND2 ASN A 193 27.210 -27.003 -0.122 1.00 16.90 N ANISOU 1384 ND2 ASN A 193 1960 2178 2285 -140 -59 -96 N ATOM 1385 OD1 ASN A 193 28.123 -25.436 -1.486 1.00 15.61 O ANISOU 1385 OD1 ASN A 193 1797 2012 2124 -163 -60 -95 O ATOM 1386 N LEU A 194 30.282 -30.134 -3.439 1.00 16.62 N ANISOU 1386 N LEU A 194 1885 2190 2239 -127 -57 -100 N ATOM 1387 CA LEU A 194 31.454 -30.965 -3.690 1.00 17.05 C ANISOU 1387 CA LEU A 194 1928 2261 2288 -110 -53 -102 C ATOM 1388 C LEU A 194 32.325 -30.315 -4.760 1.00 16.81 C ANISOU 1388 C LEU A 194 1881 2251 2256 -119 -43 -100 C ATOM 1389 O LEU A 194 31.841 -29.945 -5.833 1.00 16.03 O ANISOU 1389 O LEU A 194 1791 2146 2154 -129 -37 -97 O ATOM 1390 CB LEU A 194 31.013 -32.374 -4.115 1.00 16.85 C ANISOU 1390 CB LEU A 194 1925 2223 2255 -92 -50 -105 C ATOM 1391 CG LEU A 194 32.067 -33.482 -3.925 1.00 17.70 C ANISOU 1391 CG LEU A 194 2030 2340 2356 -62 -46 -108 C ATOM 1392 CD1 LEU A 194 32.129 -33.989 -2.459 1.00 16.10 C ANISOU 1392 CD1 LEU A 194 1828 2134 2155 -52 -58 -107 C ATOM 1393 CD2 LEU A 194 31.856 -34.637 -4.883 1.00 15.94 C ANISOU 1393 CD2 LEU A 194 1836 2102 2120 -45 -39 -113 C ATOM 1394 N GLY A 195 33.606 -30.120 -4.439 1.00 18.27 N ANISOU 1394 N GLY A 195 2039 2463 2441 -117 -42 -96 N ATOM 1395 CA GLY A 195 34.528 -29.399 -5.291 1.00 18.36 C ANISOU 1395 CA GLY A 195 2027 2498 2450 -131 -33 -89 C ATOM 1396 C GLY A 195 34.941 -28.043 -4.746 1.00 18.74 C ANISOU 1396 C GLY A 195 2062 2555 2504 -164 -44 -84 C ATOM 1397 O GLY A 195 36.073 -27.613 -4.986 1.00 18.14 O ANISOU 1397 O GLY A 195 1956 2509 2426 -177 -42 -74 O ATOM 1398 N ALA A 196 34.055 -27.363 -4.019 1.00 19.05 N ANISOU 1398 N ALA A 196 2124 2568 2548 -179 -56 -88 N ATOM 1399 CA ALA A 196 34.365 -26.021 -3.532 1.00 17.59 C ANISOU 1399 CA ALA A 196 1940 2380 2364 -212 -67 -84 C ATOM 1400 C ALA A 196 35.324 -26.022 -2.357 1.00 19.44 C ANISOU 1400 C ALA A 196 2157 2634 2596 -221 -83 -83 C ATOM 1401 O ALA A 196 36.012 -25.017 -2.130 1.00 18.93 O ANISOU 1401 O ALA A 196 2086 2579 2529 -255 -94 -77 O ATOM 1402 CB ALA A 196 33.088 -25.291 -3.129 1.00 18.07 C ANISOU 1402 CB ALA A 196 2035 2403 2426 -218 -71 -90 C ATOM 1403 N ILE A 197 35.384 -27.119 -1.603 1.00 21.98 N ANISOU 1403 N ILE A 197 2473 2961 2917 -194 -87 -87 N ATOM 1404 CA ILE A 197 36.208 -27.128 -0.398 1.00 20.14 C ANISOU 1404 CA ILE A 197 2225 2746 2680 -202 -105 -84 C ATOM 1405 C ILE A 197 37.685 -27.213 -0.758 1.00 18.66 C ANISOU 1405 C ILE A 197 1992 2606 2493 -208 -107 -69 C ATOM 1406 O ILE A 197 38.534 -26.588 -0.104 1.00 21.23 O ANISOU 1406 O ILE A 197 2300 2952 2815 -238 -126 -60 O ATOM 1407 CB ILE A 197 35.771 -28.268 0.547 1.00 18.42 C ANISOU 1407 CB ILE A 197 2020 2519 2461 -171 -110 -89 C ATOM 1408 CG1 ILE A 197 34.476 -27.893 1.279 1.00 17.83 C ANISOU 1408 CG1 ILE A 197 1984 2406 2383 -175 -112 -100 C ATOM 1409 CG2 ILE A 197 36.842 -28.575 1.552 1.00 17.91 C ANISOU 1409 CG2 ILE A 197 1931 2483 2391 -171 -128 -82 C ATOM 1410 CD1 ILE A 197 33.210 -28.227 0.531 1.00 17.41 C ANISOU 1410 CD1 ILE A 197 1951 2330 2335 -160 -95 -104 C ATOM 1411 N THR A 198 38.026 -27.967 -1.804 1.00 20.99 N ANISOU 1411 N THR A 198 2266 2920 2790 -181 -87 -64 N ATOM 1412 CA THR A 198 39.422 -28.093 -2.218 1.00 20.51 C ANISOU 1412 CA THR A 198 2155 2910 2728 -180 -82 -47 C ATOM 1413 C THR A 198 39.667 -27.529 -3.612 1.00 20.64 C ANISOU 1413 C THR A 198 2160 2940 2743 -194 -62 -40 C ATOM 1414 O THR A 198 40.739 -27.750 -4.162 1.00 18.60 O ANISOU 1414 O THR A 198 1859 2726 2483 -186 -50 -25 O ATOM 1415 CB THR A 198 39.899 -29.554 -2.205 1.00 20.75 C ANISOU 1415 CB THR A 198 2166 2960 2757 -127 -72 -44 C ATOM 1416 CG2 THR A 198 39.655 -30.200 -0.860 1.00 20.79 C ANISOU 1416 CG2 THR A 198 2185 2951 2762 -111 -91 -49 C ATOM 1417 OG1 THR A 198 39.206 -30.299 -3.217 1.00 18.38 O ANISOU 1417 OG1 THR A 198 1893 2637 2455 -95 -48 -54 O ATOM 1418 N ASN A 199 38.700 -26.839 -4.208 1.00 17.97 N ANISOU 1418 N ASN A 199 1857 2566 2405 -213 -57 -48 N ATOM 1419 CA ASN A 199 38.851 -26.301 -5.552 1.00 20.67 C ANISOU 1419 CA ASN A 199 2193 2917 2742 -227 -39 -41 C ATOM 1420 C ASN A 199 39.131 -27.423 -6.548 1.00 22.94 C ANISOU 1420 C ASN A 199 2469 3225 3024 -185 -12 -40 C ATOM 1421 O ASN A 199 40.158 -27.439 -7.225 1.00 19.35 O ANISOU 1421 O ASN A 199 1977 2812 2564 -183 5 -26 O ATOM 1422 CB ASN A 199 39.966 -25.250 -5.613 1.00 20.72 C ANISOU 1422 CB ASN A 199 2166 2959 2748 -273 -46 -21 C ATOM 1423 CG ASN A 199 39.997 -24.535 -6.933 1.00 22.76 C ANISOU 1423 CG ASN A 199 2427 3221 3000 -295 -29 -13 C ATOM 1424 ND2 ASN A 199 41.147 -23.974 -7.278 1.00 23.43 N ANISOU 1424 ND2 ASN A 199 2471 3350 3081 -326 -26 9 N ATOM 1425 OD1 ASN A 199 39.003 -24.512 -7.655 1.00 19.08 O ANISOU 1425 OD1 ASN A 199 1997 2722 2532 -286 -19 -22 O ATOM 1426 N ASP A 200 38.213 -28.383 -6.609 1.00 19.67 N ANISOU 1426 N ASP A 200 2088 2779 2608 -151 -7 -55 N ATOM 1427 CA ASP A 200 38.405 -29.548 -7.471 1.00 20.78 C ANISOU 1427 CA ASP A 200 2230 2928 2739 -108 17 -59 C ATOM 1428 C ASP A 200 37.265 -29.644 -8.475 1.00 19.33 C ANISOU 1428 C ASP A 200 2089 2708 2546 -108 25 -70 C ATOM 1429 O ASP A 200 36.169 -30.132 -8.140 1.00 17.84 O ANISOU 1429 O ASP A 200 1935 2483 2359 -101 15 -81 O ATOM 1430 CB ASP A 200 38.525 -30.820 -6.635 1.00 20.79 C ANISOU 1430 CB ASP A 200 2233 2925 2740 -66 13 -65 C ATOM 1431 CG ASP A 200 38.744 -32.063 -7.479 1.00 19.84 C ANISOU 1431 CG ASP A 200 2125 2807 2606 -17 38 -70 C ATOM 1432 OD1 ASP A 200 38.987 -31.925 -8.699 1.00 21.90 O ANISOU 1432 OD1 ASP A 200 2386 3081 2856 -15 61 -68 O ATOM 1433 OD2 ASP A 200 38.735 -33.174 -6.905 1.00 21.41 O1- ANISOU 1433 OD2 ASP A 200 2337 2994 2804 19 35 -75 O1- ATOM 1434 N PRO A 201 37.476 -29.206 -9.717 1.00 20.97 N ANISOU 1434 N PRO A 201 2295 2929 2743 -119 43 -64 N ATOM 1435 CA PRO A 201 36.409 -29.337 -10.728 1.00 21.66 C ANISOU 1435 CA PRO A 201 2425 2985 2819 -121 48 -72 C ATOM 1436 C PRO A 201 36.051 -30.789 -11.039 1.00 21.75 C ANISOU 1436 C PRO A 201 2467 2978 2817 -81 57 -85 C ATOM 1437 O PRO A 201 34.954 -31.043 -11.548 1.00 22.57 O ANISOU 1437 O PRO A 201 2611 3051 2914 -86 51 -93 O ATOM 1438 CB PRO A 201 36.987 -28.606 -11.955 1.00 20.87 C ANISOU 1438 CB PRO A 201 2313 2910 2706 -139 67 -60 C ATOM 1439 CG PRO A 201 38.505 -28.632 -11.749 1.00 21.88 C ANISOU 1439 CG PRO A 201 2389 3089 2835 -129 82 -47 C ATOM 1440 CD PRO A 201 38.732 -28.644 -10.262 1.00 19.41 C ANISOU 1440 CD PRO A 201 2056 2779 2541 -131 59 -47 C ATOM 1441 N ASP A 202 36.915 -31.750 -10.706 1.00 20.52 N ANISOU 1441 N ASP A 202 2298 2841 2659 -42 69 -87 N ATOM 1442 CA ASP A 202 36.647 -33.168 -10.924 1.00 19.99 C ANISOU 1442 CA ASP A 202 2268 2751 2577 -2 77 -100 C ATOM 1443 C ASP A 202 36.351 -33.880 -9.607 1.00 19.12 C ANISOU 1443 C ASP A 202 2165 2621 2479 13 57 -105 C ATOM 1444 O ASP A 202 36.718 -35.034 -9.406 1.00 19.62 O ANISOU 1444 O ASP A 202 2241 2679 2534 54 65 -110 O ATOM 1445 CB ASP A 202 37.813 -33.822 -11.665 1.00 20.45 C ANISOU 1445 CB ASP A 202 2315 2840 2617 41 109 -99 C ATOM 1446 CG ASP A 202 38.157 -33.093 -12.960 1.00 22.03 C ANISOU 1446 CG ASP A 202 2506 3062 2802 24 132 -92 C ATOM 1447 OD1 ASP A 202 37.295 -33.054 -13.858 1.00 22.85 O ANISOU 1447 OD1 ASP A 202 2653 3139 2890 8 131 -100 O ATOM 1448 OD2 ASP A 202 39.276 -32.540 -13.073 1.00 25.78 O1- ANISOU 1448 OD2 ASP A 202 2930 3585 3279 24 148 -76 O1- ATOM 1449 N ALA A 203 35.642 -33.187 -8.711 1.00 20.09 N ANISOU 1449 N ALA A 203 2284 2731 2619 -20 33 -103 N ATOM 1450 CA ALA A 203 35.369 -33.697 -7.373 1.00 20.21 C ANISOU 1450 CA ALA A 203 2302 2732 2644 -11 15 -105 C ATOM 1451 C ALA A 203 34.580 -35.003 -7.403 1.00 18.13 C ANISOU 1451 C ALA A 203 2086 2431 2370 9 12 -116 C ATOM 1452 O ALA A 203 34.756 -35.852 -6.521 1.00 19.28 O ANISOU 1452 O ALA A 203 2239 2570 2518 33 5 -116 O ATOM 1453 CB ALA A 203 34.613 -32.635 -6.574 1.00 16.93 C ANISOU 1453 CB ALA A 203 1881 2307 2244 -50 -6 -102 C ATOM 1454 N GLY A 204 33.713 -35.182 -8.399 1.00 18.39 N ANISOU 1454 N GLY A 204 2155 2440 2390 -3 14 -122 N ATOM 1455 CA GLY A 204 32.917 -36.398 -8.465 1.00 18.09 C ANISOU 1455 CA GLY A 204 2168 2366 2341 7 6 -130 C ATOM 1456 C GLY A 204 33.774 -37.630 -8.668 1.00 18.62 C ANISOU 1456 C GLY A 204 2257 2428 2391 54 22 -137 C ATOM 1457 O GLY A 204 33.601 -38.642 -7.987 1.00 18.40 O ANISOU 1457 O GLY A 204 2255 2376 2360 73 14 -140 O ATOM 1458 N ILE A 205 34.704 -37.567 -9.623 1.00 18.63 N ANISOU 1458 N ILE A 205 2248 2452 2379 78 48 -138 N ATOM 1459 CA ILE A 205 35.539 -38.726 -9.885 1.00 19.69 C ANISOU 1459 CA ILE A 205 2405 2582 2496 132 68 -145 C ATOM 1460 C ILE A 205 36.625 -38.866 -8.824 1.00 20.85 C ANISOU 1460 C ILE A 205 2506 2758 2657 166 71 -134 C ATOM 1461 O ILE A 205 37.057 -39.988 -8.534 1.00 19.76 O ANISOU 1461 O ILE A 205 2392 2607 2510 213 77 -137 O ATOM 1462 CB ILE A 205 36.122 -38.673 -11.314 1.00 21.19 C ANISOU 1462 CB ILE A 205 2603 2787 2662 150 99 -149 C ATOM 1463 CG1 ILE A 205 36.770 -40.007 -11.683 1.00 22.94 C ANISOU 1463 CG1 ILE A 205 2865 2993 2858 212 123 -159 C ATOM 1464 CG2 ILE A 205 37.116 -37.537 -11.470 1.00 21.71 C ANISOU 1464 CG2 ILE A 205 2601 2909 2739 145 115 -135 C ATOM 1465 CD1 ILE A 205 35.772 -41.159 -11.704 1.00 25.07 C ANISOU 1465 CD1 ILE A 205 3215 3200 3109 210 106 -174 C ATOM 1466 N THR A 206 37.088 -37.756 -8.229 1.00 18.53 N ANISOU 1466 N THR A 206 2152 2504 2385 144 64 -121 N ATOM 1467 CA THR A 206 37.987 -37.870 -7.081 1.00 19.24 C ANISOU 1467 CA THR A 206 2201 2622 2488 167 57 -109 C ATOM 1468 C THR A 206 37.341 -38.700 -5.978 1.00 18.88 C ANISOU 1468 C THR A 206 2188 2539 2446 172 35 -112 C ATOM 1469 O THR A 206 37.947 -39.639 -5.456 1.00 20.42 O ANISOU 1469 O THR A 206 2388 2734 2638 217 37 -108 O ATOM 1470 CB THR A 206 38.363 -36.489 -6.551 1.00 18.96 C ANISOU 1470 CB THR A 206 2107 2625 2472 127 45 -95 C ATOM 1471 CG2 THR A 206 39.347 -36.603 -5.368 1.00 21.44 C ANISOU 1471 CG2 THR A 206 2377 2972 2797 146 34 -80 C ATOM 1472 OG1 THR A 206 38.940 -35.706 -7.603 1.00 17.27 O ANISOU 1472 OG1 THR A 206 1864 2444 2253 116 66 -89 O ATOM 1473 N LEU A 207 36.096 -38.373 -5.631 1.00 19.05 N ANISOU 1473 N LEU A 207 2233 2531 2474 129 14 -117 N ATOM 1474 CA LEU A 207 35.358 -39.129 -4.626 1.00 18.76 C ANISOU 1474 CA LEU A 207 2229 2461 2439 128 -6 -118 C ATOM 1475 C LEU A 207 35.188 -40.588 -5.033 1.00 19.92 C ANISOU 1475 C LEU A 207 2435 2569 2566 162 0 -127 C ATOM 1476 O LEU A 207 35.352 -41.495 -4.209 1.00 17.37 O ANISOU 1476 O LEU A 207 2130 2229 2240 189 -8 -123 O ATOM 1477 CB LEU A 207 33.996 -38.472 -4.404 1.00 19.41 C ANISOU 1477 CB LEU A 207 2322 2524 2528 76 -23 -120 C ATOM 1478 CG LEU A 207 32.997 -39.130 -3.442 1.00 20.08 C ANISOU 1478 CG LEU A 207 2439 2577 2613 63 -42 -119 C ATOM 1479 CD1 LEU A 207 33.610 -39.350 -2.087 1.00 16.70 C ANISOU 1479 CD1 LEU A 207 1993 2161 2192 81 -53 -111 C ATOM 1480 CD2 LEU A 207 31.783 -38.242 -3.310 1.00 17.81 C ANISOU 1480 CD2 LEU A 207 2147 2284 2334 17 -53 -117 C ATOM 1481 N ALA A 208 34.860 -40.840 -6.303 1.00 19.78 N ANISOU 1481 N ALA A 208 2453 2532 2530 161 14 -138 N ATOM 1482 CA ALA A 208 34.635 -42.224 -6.723 1.00 21.59 C ANISOU 1482 CA ALA A 208 2751 2716 2735 189 18 -148 C ATOM 1483 C ALA A 208 35.908 -43.057 -6.628 1.00 21.61 C ANISOU 1483 C ALA A 208 2755 2727 2730 258 37 -146 C ATOM 1484 O ALA A 208 35.847 -44.277 -6.427 1.00 22.12 O ANISOU 1484 O ALA A 208 2874 2751 2778 289 35 -150 O ATOM 1485 CB ALA A 208 34.086 -42.266 -8.152 1.00 19.06 C ANISOU 1485 CB ALA A 208 2473 2376 2394 172 27 -160 C ATOM 1486 N GLU A 209 37.064 -42.426 -6.767 1.00 21.81 N ANISOU 1486 N GLU A 209 2720 2804 2764 283 56 -137 N ATOM 1487 CA GLU A 209 38.322 -43.154 -6.793 1.00 23.46 C ANISOU 1487 CA GLU A 209 2920 3030 2964 354 79 -132 C ATOM 1488 C GLU A 209 39.059 -43.069 -5.470 1.00 22.61 C ANISOU 1488 C GLU A 209 2759 2955 2876 372 65 -113 C ATOM 1489 O GLU A 209 40.100 -43.713 -5.310 1.00 23.77 O ANISOU 1489 O GLU A 209 2892 3120 3019 435 80 -103 O ATOM 1490 CB GLU A 209 39.189 -42.633 -7.937 1.00 22.02 C ANISOU 1490 CB GLU A 209 2704 2891 2774 375 113 -131 C ATOM 1491 CG GLU A 209 38.561 -42.952 -9.300 1.00 24.86 C ANISOU 1491 CG GLU A 209 3129 3213 3105 369 129 -151 C ATOM 1492 CD GLU A 209 39.372 -42.476 -10.487 1.00 33.54 C ANISOU 1492 CD GLU A 209 4201 4353 4190 389 166 -150 C ATOM 1493 OE1 GLU A 209 40.288 -41.625 -10.308 1.00 32.46 O ANISOU 1493 OE1 GLU A 209 3985 4277 4070 391 177 -132 O ATOM 1494 OE2 GLU A 209 39.076 -42.946 -11.615 1.00 36.56 O1- ANISOU 1494 OE2 GLU A 209 4645 4705 4543 399 184 -167 O1- ATOM 1495 N ASP A 210 38.524 -42.318 -4.517 1.00 20.20 N ANISOU 1495 N ASP A 210 2427 2658 2591 321 37 -107 N ATOM 1496 CA ASP A 210 39.145 -42.175 -3.211 1.00 21.37 C ANISOU 1496 CA ASP A 210 2530 2835 2755 329 19 -89 C ATOM 1497 C ASP A 210 38.762 -43.362 -2.330 1.00 19.35 C ANISOU 1497 C ASP A 210 2324 2535 2492 352 2 -88 C ATOM 1498 O ASP A 210 37.572 -43.546 -2.041 1.00 19.36 O ANISOU 1498 O ASP A 210 2371 2495 2492 314 -15 -97 O ATOM 1499 CB ASP A 210 38.712 -40.847 -2.581 1.00 17.68 C ANISOU 1499 CB ASP A 210 2023 2390 2306 265 -3 -85 C ATOM 1500 CG ASP A 210 39.452 -40.528 -1.274 1.00 21.67 C ANISOU 1500 CG ASP A 210 2478 2931 2823 266 -23 -67 C ATOM 1501 OD1 ASP A 210 40.112 -41.423 -0.702 1.00 21.66 O ANISOU 1501 OD1 ASP A 210 2478 2934 2819 314 -27 -56 O ATOM 1502 OD2 ASP A 210 39.382 -39.363 -0.823 1.00 18.25 O1- ANISOU 1502 OD2 ASP A 210 2010 2522 2402 219 -38 -63 O1- ATOM 1503 N PRO A 211 39.720 -44.190 -1.894 1.00 18.99 N ANISOU 1503 N PRO A 211 2273 2499 2443 414 6 -76 N ATOM 1504 CA PRO A 211 39.360 -45.351 -1.053 1.00 19.38 C ANISOU 1504 CA PRO A 211 2377 2502 2484 436 -11 -73 C ATOM 1505 C PRO A 211 38.930 -44.991 0.363 1.00 19.78 C ANISOU 1505 C PRO A 211 2412 2557 2548 396 -44 -62 C ATOM 1506 O PRO A 211 38.294 -45.818 1.020 1.00 19.76 O ANISOU 1506 O PRO A 211 2462 2511 2537 394 -59 -62 O ATOM 1507 CB PRO A 211 40.648 -46.191 -1.039 1.00 21.21 C ANISOU 1507 CB PRO A 211 2598 2752 2710 520 5 -59 C ATOM 1508 CG PRO A 211 41.749 -45.214 -1.304 1.00 19.13 C ANISOU 1508 CG PRO A 211 2245 2563 2459 527 19 -45 C ATOM 1509 CD PRO A 211 41.163 -44.149 -2.206 1.00 19.87 C ANISOU 1509 CD PRO A 211 2328 2665 2556 469 28 -61 C ATOM 1510 N GLU A 212 39.265 -43.806 0.873 1.00 18.74 N ANISOU 1510 N GLU A 212 2215 2476 2432 362 -55 -54 N ATOM 1511 CA GLU A 212 38.844 -43.379 2.213 1.00 18.70 C ANISOU 1511 CA GLU A 212 2198 2473 2433 322 -84 -46 C ATOM 1512 C GLU A 212 38.379 -41.937 2.158 1.00 18.78 C ANISOU 1512 C GLU A 212 2176 2506 2455 260 -89 -53 C ATOM 1513 O GLU A 212 39.012 -41.044 2.723 1.00 19.82 O ANISOU 1513 O GLU A 212 2255 2681 2595 243 -101 -42 O ATOM 1514 CB GLU A 212 39.981 -43.524 3.222 1.00 18.66 C ANISOU 1514 CB GLU A 212 2151 2507 2432 355 -100 -23 C ATOM 1515 CG GLU A 212 40.887 -44.677 2.954 1.00 26.27 C ANISOU 1515 CG GLU A 212 3124 3470 3388 432 -87 -12 C ATOM 1516 CD GLU A 212 41.769 -44.978 4.130 1.00 29.18 C ANISOU 1516 CD GLU A 212 3460 3869 3758 462 -110 14 C ATOM 1517 OE1 GLU A 212 42.504 -44.043 4.538 1.00 26.40 O ANISOU 1517 OE1 GLU A 212 3039 3574 3416 442 -123 28 O ATOM 1518 OE2 GLU A 212 41.723 -46.131 4.623 1.00 31.97 O1- ANISOU 1518 OE2 GLU A 212 3860 4186 4101 503 -117 21 O1- ATOM 1519 N PRO A 213 37.247 -41.676 1.510 1.00 17.37 N ANISOU 1519 N PRO A 213 2029 2297 2275 224 -82 -68 N ATOM 1520 CA PRO A 213 36.825 -40.279 1.333 1.00 15.95 C ANISOU 1520 CA PRO A 213 1820 2136 2105 172 -83 -74 C ATOM 1521 C PRO A 213 36.544 -39.533 2.635 1.00 19.96 C ANISOU 1521 C PRO A 213 2312 2654 2618 137 -105 -69 C ATOM 1522 O PRO A 213 36.720 -38.303 2.686 1.00 16.75 O ANISOU 1522 O PRO A 213 1871 2273 2219 105 -109 -69 O ATOM 1523 CB PRO A 213 35.562 -40.408 0.472 1.00 16.95 C ANISOU 1523 CB PRO A 213 1991 2223 2227 148 -74 -88 C ATOM 1524 CG PRO A 213 35.668 -41.731 -0.177 1.00 17.69 C ANISOU 1524 CG PRO A 213 2129 2286 2306 189 -63 -92 C ATOM 1525 CD PRO A 213 36.373 -42.615 0.795 1.00 18.26 C ANISOU 1525 CD PRO A 213 2205 2358 2375 230 -73 -80 C ATOM 1526 N TRP A 214 36.095 -40.216 3.689 1.00 17.15 N ANISOU 1526 N TRP A 214 1985 2275 2255 140 -120 -64 N ATOM 1527 CA TRP A 214 35.786 -39.514 4.935 1.00 19.83 C ANISOU 1527 CA TRP A 214 2317 2624 2595 107 -139 -60 C ATOM 1528 C TRP A 214 37.045 -39.401 5.786 1.00 18.79 C ANISOU 1528 C TRP A 214 2148 2529 2462 123 -156 -46 C ATOM 1529 O TRP A 214 37.147 -39.907 6.906 1.00 23.67 O ANISOU 1529 O TRP A 214 2778 3144 3071 132 -174 -35 O ATOM 1530 CB TRP A 214 34.629 -40.187 5.668 1.00 18.18 C ANISOU 1530 CB TRP A 214 2154 2376 2376 96 -145 -60 C ATOM 1531 CG TRP A 214 33.353 -39.888 4.964 1.00 17.89 C ANISOU 1531 CG TRP A 214 2138 2317 2343 65 -133 -70 C ATOM 1532 CD1 TRP A 214 32.478 -38.864 5.242 1.00 15.74 C ANISOU 1532 CD1 TRP A 214 1861 2047 2074 28 -132 -75 C ATOM 1533 CD2 TRP A 214 32.817 -40.581 3.829 1.00 18.41 C ANISOU 1533 CD2 TRP A 214 2232 2355 2406 71 -121 -76 C ATOM 1534 CE2 TRP A 214 31.615 -39.928 3.473 1.00 18.95 C ANISOU 1534 CE2 TRP A 214 2306 2415 2479 33 -115 -81 C ATOM 1535 CE3 TRP A 214 33.233 -41.698 3.080 1.00 18.72 C ANISOU 1535 CE3 TRP A 214 2298 2376 2439 106 -114 -77 C ATOM 1536 NE1 TRP A 214 31.434 -38.885 4.350 1.00 17.43 N ANISOU 1536 NE1 TRP A 214 2091 2240 2290 11 -120 -80 N ATOM 1537 CZ2 TRP A 214 30.821 -40.352 2.400 1.00 19.77 C ANISOU 1537 CZ2 TRP A 214 2436 2495 2581 23 -108 -86 C ATOM 1538 CZ3 TRP A 214 32.447 -42.111 2.007 1.00 18.44 C ANISOU 1538 CZ3 TRP A 214 2297 2311 2398 95 -105 -85 C ATOM 1539 CH2 TRP A 214 31.251 -41.440 1.683 1.00 17.09 C ANISOU 1539 CH2 TRP A 214 2126 2136 2232 51 -104 -89 C ATOM 1540 N THR A 215 38.016 -38.711 5.194 1.00 19.73 N ANISOU 1540 N THR A 215 2220 2687 2589 124 -152 -42 N ATOM 1541 CA THR A 215 39.312 -38.433 5.788 1.00 20.42 C ANISOU 1541 CA THR A 215 2260 2822 2678 133 -169 -25 C ATOM 1542 C THR A 215 39.544 -36.926 5.673 1.00 23.24 C ANISOU 1542 C THR A 215 2584 3207 3040 84 -174 -28 C ATOM 1543 O THR A 215 39.238 -36.335 4.631 1.00 22.06 O ANISOU 1543 O THR A 215 2432 3053 2897 68 -156 -38 O ATOM 1544 CB THR A 215 40.404 -39.204 5.035 1.00 20.66 C ANISOU 1544 CB THR A 215 2263 2877 2711 187 -155 -12 C ATOM 1545 CG2 THR A 215 41.776 -38.775 5.521 1.00 24.24 C ANISOU 1545 CG2 THR A 215 2652 3390 3167 191 -173 10 C ATOM 1546 OG1 THR A 215 40.257 -40.611 5.280 1.00 21.49 O ANISOU 1546 OG1 THR A 215 2407 2951 2808 235 -154 -9 O ATOM 1547 N GLU A 216 40.080 -36.293 6.719 1.00 19.86 N ANISOU 1547 N GLU A 216 2135 2805 2607 58 -202 -18 N ATOM 1548 CA GLU A 216 40.294 -34.847 6.660 1.00 22.43 C ANISOU 1548 CA GLU A 216 2438 3150 2934 7 -210 -21 C ATOM 1549 C GLU A 216 41.114 -34.467 5.430 1.00 20.08 C ANISOU 1549 C GLU A 216 2094 2887 2647 10 -193 -14 C ATOM 1550 O GLU A 216 42.108 -35.118 5.104 1.00 18.45 O ANISOU 1550 O GLU A 216 1850 2716 2445 47 -189 4 O ATOM 1551 CB GLU A 216 40.999 -34.349 7.921 1.00 25.67 C ANISOU 1551 CB GLU A 216 2831 3589 3334 -20 -245 -8 C ATOM 1552 CG GLU A 216 41.024 -32.837 7.992 1.00 24.97 C ANISOU 1552 CG GLU A 216 2739 3507 3242 -80 -256 -15 C ATOM 1553 CD GLU A 216 41.809 -32.292 9.157 1.00 31.32 C ANISOU 1553 CD GLU A 216 3529 4340 4032 -114 -295 -2 C ATOM 1554 OE1 GLU A 216 42.536 -33.054 9.846 1.00 28.82 O ANISOU 1554 OE1 GLU A 216 3190 4051 3710 -90 -315 17 O ATOM 1555 OE2 GLU A 216 41.692 -31.073 9.379 1.00 36.15 O1- ANISOU 1555 OE2 GLU A 216 4156 4946 4636 -165 -307 -10 O1- ATOM 1556 N GLY A 217 40.680 -33.420 4.737 1.00 19.60 N ANISOU 1556 N GLY A 217 2039 2816 2591 -28 -182 -25 N ATOM 1557 CA GLY A 217 41.324 -32.975 3.516 1.00 19.10 C ANISOU 1557 CA GLY A 217 1939 2782 2535 -31 -164 -19 C ATOM 1558 C GLY A 217 40.473 -33.104 2.272 1.00 19.82 C ANISOU 1558 C GLY A 217 2058 2843 2632 -20 -134 -34 C ATOM 1559 O GLY A 217 40.813 -32.497 1.255 1.00 20.10 O ANISOU 1559 O GLY A 217 2071 2896 2670 -34 -119 -32 O ATOM 1560 N THR A 218 39.379 -33.860 2.319 1.00 16.22 N ANISOU 1560 N THR A 218 1649 2342 2173 0 -126 -49 N ATOM 1561 CA THR A 218 38.513 -34.074 1.173 1.00 14.42 C ANISOU 1561 CA THR A 218 1449 2083 1945 7 -102 -62 C ATOM 1562 C THR A 218 37.275 -33.206 1.278 1.00 16.19 C ANISOU 1562 C THR A 218 1706 2275 2172 -31 -104 -75 C ATOM 1563 O THR A 218 36.872 -32.778 2.364 1.00 15.86 O ANISOU 1563 O THR A 218 1678 2222 2127 -52 -121 -77 O ATOM 1564 CB THR A 218 38.066 -35.532 1.064 1.00 16.27 C ANISOU 1564 CB THR A 218 1717 2289 2174 51 -92 -66 C ATOM 1565 CG2 THR A 218 39.250 -36.487 1.139 1.00 18.27 C ANISOU 1565 CG2 THR A 218 1946 2571 2426 100 -89 -53 C ATOM 1566 OG1 THR A 218 37.135 -35.808 2.120 1.00 16.62 O ANISOU 1566 OG1 THR A 218 1797 2302 2216 41 -107 -71 O ATOM 1567 N ASP A 219 36.644 -32.983 0.125 1.00 14.51 N ANISOU 1567 N ASP A 219 1507 2046 1961 -37 -87 -82 N ATOM 1568 CA ASP A 219 35.408 -32.216 0.113 1.00 17.88 C ANISOU 1568 CA ASP A 219 1961 2442 2389 -66 -87 -91 C ATOM 1569 C ASP A 219 34.318 -32.920 0.911 1.00 17.16 C ANISOU 1569 C ASP A 219 1905 2321 2296 -58 -93 -96 C ATOM 1570 O ASP A 219 33.633 -32.286 1.723 1.00 17.88 O ANISOU 1570 O ASP A 219 2010 2399 2386 -78 -101 -99 O ATOM 1571 CB ASP A 219 34.965 -31.969 -1.327 1.00 16.21 C ANISOU 1571 CB ASP A 219 1757 2222 2179 -71 -70 -95 C ATOM 1572 CG ASP A 219 36.001 -31.174 -2.104 1.00 18.91 C ANISOU 1572 CG ASP A 219 2067 2597 2523 -84 -62 -87 C ATOM 1573 OD1 ASP A 219 37.121 -31.705 -2.305 1.00 19.67 O ANISOU 1573 OD1 ASP A 219 2134 2724 2617 -62 -56 -79 O ATOM 1574 OD2 ASP A 219 35.714 -30.017 -2.468 1.00 18.63 O1- ANISOU 1574 OD2 ASP A 219 2032 2556 2489 -116 -63 -87 O1- ATOM 1575 N VAL A 220 34.141 -34.237 0.705 1.00 14.08 N ANISOU 1575 N VAL A 220 1532 1918 1901 -29 -88 -96 N ATOM 1576 CA VAL A 220 32.991 -34.860 1.348 1.00 15.37 C ANISOU 1576 CA VAL A 220 1727 2051 2060 -29 -92 -98 C ATOM 1577 C VAL A 220 33.196 -34.901 2.858 1.00 15.98 C ANISOU 1577 C VAL A 220 1804 2133 2133 -30 -108 -94 C ATOM 1578 O VAL A 220 32.229 -34.807 3.623 1.00 16.20 O ANISOU 1578 O VAL A 220 1852 2144 2158 -43 -111 -95 O ATOM 1579 CB VAL A 220 32.693 -36.259 0.788 1.00 18.67 C ANISOU 1579 CB VAL A 220 2173 2448 2471 -5 -86 -99 C ATOM 1580 CG1 VAL A 220 33.609 -37.330 1.397 1.00 16.16 C ANISOU 1580 CG1 VAL A 220 1857 2136 2148 30 -92 -94 C ATOM 1581 CG2 VAL A 220 31.254 -36.597 1.029 1.00 16.97 C ANISOU 1581 CG2 VAL A 220 1989 2205 2254 -22 -89 -99 C ATOM 1582 N TYR A 221 34.445 -35.020 3.312 1.00 14.06 N ANISOU 1582 N TYR A 221 1538 1916 1889 -16 -118 -88 N ATOM 1583 CA TYR A 221 34.716 -34.930 4.739 1.00 15.83 C ANISOU 1583 CA TYR A 221 1762 2148 2106 -21 -137 -83 C ATOM 1584 C TYR A 221 34.198 -33.618 5.301 1.00 16.87 C ANISOU 1584 C TYR A 221 1899 2276 2235 -57 -141 -89 C ATOM 1585 O TYR A 221 33.513 -33.600 6.323 1.00 17.38 O ANISOU 1585 O TYR A 221 1988 2326 2291 -65 -147 -91 O ATOM 1586 CB TYR A 221 36.220 -35.053 5.008 1.00 17.80 C ANISOU 1586 CB TYR A 221 1975 2434 2354 -6 -149 -71 C ATOM 1587 CG TYR A 221 36.560 -34.941 6.478 1.00 19.46 C ANISOU 1587 CG TYR A 221 2185 2654 2554 -15 -174 -65 C ATOM 1588 CD1 TYR A 221 36.804 -33.692 7.062 1.00 19.85 C ANISOU 1588 CD1 TYR A 221 2227 2718 2599 -53 -188 -67 C ATOM 1589 CD2 TYR A 221 36.679 -36.065 7.274 1.00 19.49 C ANISOU 1589 CD2 TYR A 221 2203 2653 2550 12 -184 -56 C ATOM 1590 CE1 TYR A 221 37.102 -33.571 8.391 1.00 18.46 C ANISOU 1590 CE1 TYR A 221 2056 2549 2408 -65 -212 -62 C ATOM 1591 CE2 TYR A 221 37.004 -35.951 8.614 1.00 21.93 C ANISOU 1591 CE2 TYR A 221 2514 2973 2846 2 -208 -49 C ATOM 1592 CZ TYR A 221 37.216 -34.698 9.164 1.00 21.57 C ANISOU 1592 CZ TYR A 221 2460 2941 2794 -37 -222 -52 C ATOM 1593 OH TYR A 221 37.539 -34.559 10.491 1.00 25.35 O ANISOU 1593 OH TYR A 221 2946 3430 3255 -50 -248 -46 O ATOM 1594 N ALA A 222 34.534 -32.499 4.652 1.00 14.92 N ANISOU 1594 N ALA A 222 1634 2040 1994 -79 -138 -92 N ATOM 1595 CA ALA A 222 34.138 -31.203 5.198 1.00 18.15 C ANISOU 1595 CA ALA A 222 2056 2441 2399 -110 -143 -99 C ATOM 1596 C ALA A 222 32.621 -31.060 5.219 1.00 15.14 C ANISOU 1596 C ALA A 222 1706 2029 2017 -111 -129 -105 C ATOM 1597 O ALA A 222 32.057 -30.509 6.169 1.00 13.62 O ANISOU 1597 O ALA A 222 1535 1824 1815 -122 -131 -110 O ATOM 1598 CB ALA A 222 34.784 -30.064 4.397 1.00 14.83 C ANISOU 1598 CB ALA A 222 1616 2035 1985 -135 -143 -98 C ATOM 1599 N ILE A 223 31.945 -31.593 4.196 1.00 16.46 N ANISOU 1599 N ILE A 223 1875 2186 2194 -100 -114 -105 N ATOM 1600 CA ILE A 223 30.502 -31.410 4.067 1.00 16.47 C ANISOU 1600 CA ILE A 223 1895 2165 2196 -103 -101 -106 C ATOM 1601 C ILE A 223 29.761 -32.211 5.138 1.00 18.56 C ANISOU 1601 C ILE A 223 2180 2420 2452 -95 -102 -102 C ATOM 1602 O ILE A 223 28.848 -31.703 5.809 1.00 16.38 O ANISOU 1602 O ILE A 223 1918 2135 2171 -100 -95 -103 O ATOM 1603 CB ILE A 223 30.060 -31.781 2.638 1.00 16.12 C ANISOU 1603 CB ILE A 223 1848 2116 2162 -99 -91 -104 C ATOM 1604 CG1 ILE A 223 30.627 -30.745 1.639 1.00 15.76 C ANISOU 1604 CG1 ILE A 223 1787 2080 2123 -112 -87 -106 C ATOM 1605 CG2 ILE A 223 28.534 -31.851 2.545 1.00 15.44 C ANISOU 1605 CG2 ILE A 223 1776 2014 2077 -103 -82 -99 C ATOM 1606 CD1 ILE A 223 30.505 -31.117 0.139 1.00 16.29 C ANISOU 1606 CD1 ILE A 223 1850 2146 2194 -108 -78 -104 C ATOM 1607 N ASP A 224 30.163 -33.467 5.339 1.00 16.11 N ANISOU 1607 N ASP A 224 1871 2112 2138 -79 -109 -97 N ATOM 1608 CA ASP A 224 29.517 -34.284 6.350 1.00 14.92 C ANISOU 1608 CA ASP A 224 1741 1951 1978 -74 -111 -91 C ATOM 1609 C ASP A 224 30.001 -33.947 7.751 1.00 16.59 C ANISOU 1609 C ASP A 224 1958 2170 2174 -77 -123 -92 C ATOM 1610 O ASP A 224 29.219 -34.051 8.699 1.00 14.22 O ANISOU 1610 O ASP A 224 1678 1863 1864 -80 -119 -89 O ATOM 1611 CB ASP A 224 29.712 -35.767 6.019 1.00 15.28 C ANISOU 1611 CB ASP A 224 1795 1988 2022 -57 -115 -85 C ATOM 1612 CG ASP A 224 28.913 -36.178 4.780 1.00 17.41 C ANISOU 1612 CG ASP A 224 2072 2244 2299 -61 -106 -84 C ATOM 1613 OD1 ASP A 224 27.989 -35.420 4.408 1.00 19.25 O ANISOU 1613 OD1 ASP A 224 2300 2476 2537 -77 -96 -84 O ATOM 1614 OD2 ASP A 224 29.205 -37.214 4.160 1.00 16.09 O1- ANISOU 1614 OD2 ASP A 224 1917 2068 2131 -47 -108 -83 O1- ATOM 1615 N SER A 225 31.259 -33.516 7.908 1.00 17.57 N ANISOU 1615 N SER A 225 2067 2312 2298 -78 -137 -95 N ATOM 1616 CA SER A 225 31.723 -33.105 9.231 1.00 16.28 C ANISOU 1616 CA SER A 225 1912 2156 2117 -87 -152 -95 C ATOM 1617 C SER A 225 30.985 -31.864 9.724 1.00 18.11 C ANISOU 1617 C SER A 225 2164 2376 2340 -106 -144 -105 C ATOM 1618 O SER A 225 30.686 -31.742 10.923 1.00 18.15 O ANISOU 1618 O SER A 225 2193 2377 2325 -109 -146 -106 O ATOM 1619 CB SER A 225 33.236 -32.856 9.217 1.00 20.50 C ANISOU 1619 CB SER A 225 2420 2716 2652 -91 -173 -93 C ATOM 1620 OG SER A 225 33.676 -32.406 10.485 1.00 20.44 O ANISOU 1620 OG SER A 225 2424 2717 2625 -106 -193 -93 O ATOM 1621 N LEU A 226 30.680 -30.930 8.825 1.00 17.03 N ANISOU 1621 N LEU A 226 2022 2234 2215 -115 -132 -111 N ATOM 1622 CA LEU A 226 29.959 -29.730 9.253 1.00 16.17 C ANISOU 1622 CA LEU A 226 1937 2109 2096 -125 -121 -120 C ATOM 1623 C LEU A 226 28.594 -30.096 9.825 1.00 16.51 C ANISOU 1623 C LEU A 226 2000 2142 2133 -112 -102 -116 C ATOM 1624 O LEU A 226 28.188 -29.588 10.880 1.00 14.93 O ANISOU 1624 O LEU A 226 1826 1933 1912 -112 -96 -121 O ATOM 1625 CB LEU A 226 29.820 -28.754 8.084 1.00 16.19 C ANISOU 1625 CB LEU A 226 1932 2106 2114 -133 -112 -124 C ATOM 1626 CG LEU A 226 29.462 -27.310 8.444 1.00 17.58 C ANISOU 1626 CG LEU A 226 2137 2263 2280 -144 -106 -135 C ATOM 1627 CD1 LEU A 226 30.769 -26.599 8.698 1.00 21.97 C ANISOU 1627 CD1 LEU A 226 2696 2826 2827 -171 -129 -140 C ATOM 1628 CD2 LEU A 226 28.738 -26.649 7.301 1.00 19.03 C ANISOU 1628 CD2 LEU A 226 2316 2435 2479 -141 -89 -133 C ATOM 1629 N LEU A 227 27.893 -31.017 9.165 1.00 17.28 N ANISOU 1629 N LEU A 227 2084 2240 2244 -101 -91 -106 N ATOM 1630 CA LEU A 227 26.616 -31.502 9.679 1.00 16.38 C ANISOU 1630 CA LEU A 227 1980 2122 2123 -94 -74 -97 C ATOM 1631 C LEU A 227 26.795 -32.183 11.029 1.00 18.65 C ANISOU 1631 C LEU A 227 2286 2411 2389 -91 -82 -93 C ATOM 1632 O LEU A 227 26.090 -31.862 11.994 1.00 16.43 O ANISOU 1632 O LEU A 227 2024 2128 2090 -89 -68 -92 O ATOM 1633 CB LEU A 227 25.969 -32.451 8.664 1.00 13.62 C ANISOU 1633 CB LEU A 227 1614 1771 1789 -92 -70 -85 C ATOM 1634 CG LEU A 227 24.731 -33.235 9.109 1.00 19.63 C ANISOU 1634 CG LEU A 227 2380 2533 2544 -92 -57 -69 C ATOM 1635 CD1 LEU A 227 23.565 -32.293 9.406 1.00 20.76 C ANISOU 1635 CD1 LEU A 227 2523 2681 2685 -87 -34 -64 C ATOM 1636 CD2 LEU A 227 24.351 -34.243 8.039 1.00 19.11 C ANISOU 1636 CD2 LEU A 227 2305 2465 2492 -99 -62 -58 C ATOM 1637 N TYR A 228 27.742 -33.126 11.117 1.00 15.69 N ANISOU 1637 N TYR A 228 1906 2041 2013 -90 -102 -89 N ATOM 1638 CA TYR A 228 27.950 -33.841 12.371 1.00 18.18 C ANISOU 1638 CA TYR A 228 2241 2360 2308 -87 -113 -83 C ATOM 1639 C TYR A 228 28.305 -32.875 13.496 1.00 16.03 C ANISOU 1639 C TYR A 228 1990 2090 2013 -95 -118 -93 C ATOM 1640 O TYR A 228 27.699 -32.914 14.576 1.00 16.65 O ANISOU 1640 O TYR A 228 2093 2166 2068 -94 -109 -90 O ATOM 1641 CB TYR A 228 29.042 -34.911 12.215 1.00 15.74 C ANISOU 1641 CB TYR A 228 1922 2055 2003 -78 -135 -76 C ATOM 1642 CG TYR A 228 29.105 -35.856 13.415 1.00 19.19 C ANISOU 1642 CG TYR A 228 2381 2492 2419 -73 -146 -64 C ATOM 1643 CD1 TYR A 228 29.693 -35.449 14.613 1.00 18.83 C ANISOU 1643 CD1 TYR A 228 2349 2454 2350 -78 -161 -67 C ATOM 1644 CD2 TYR A 228 28.554 -37.143 13.357 1.00 19.23 C ANISOU 1644 CD2 TYR A 228 2397 2485 2424 -66 -143 -50 C ATOM 1645 CE1 TYR A 228 29.743 -36.286 15.719 1.00 21.42 C ANISOU 1645 CE1 TYR A 228 2699 2782 2656 -73 -172 -54 C ATOM 1646 CE2 TYR A 228 28.594 -37.984 14.464 1.00 20.67 C ANISOU 1646 CE2 TYR A 228 2603 2664 2586 -63 -153 -37 C ATOM 1647 CZ TYR A 228 29.193 -37.547 15.642 1.00 20.67 C ANISOU 1647 CZ TYR A 228 2614 2675 2563 -65 -167 -39 C ATOM 1648 OH TYR A 228 29.250 -38.352 16.751 1.00 18.76 O ANISOU 1648 OH TYR A 228 2397 2431 2298 -62 -178 -25 O ATOM 1649 N GLU A 229 29.286 -31.995 13.264 1.00 15.64 N ANISOU 1649 N GLU A 229 1933 2044 1965 -105 -133 -104 N ATOM 1650 CA GLU A 229 29.773 -31.132 14.342 1.00 17.65 C ANISOU 1650 CA GLU A 229 2214 2299 2194 -119 -146 -114 C ATOM 1651 C GLU A 229 28.708 -30.129 14.767 1.00 16.35 C ANISOU 1651 C GLU A 229 2081 2118 2014 -118 -120 -124 C ATOM 1652 O GLU A 229 28.548 -29.857 15.964 1.00 16.01 O ANISOU 1652 O GLU A 229 2072 2070 1940 -120 -119 -129 O ATOM 1653 CB GLU A 229 31.056 -30.407 13.915 1.00 17.95 C ANISOU 1653 CB GLU A 229 2236 2347 2237 -138 -171 -120 C ATOM 1654 CG GLU A 229 32.299 -31.302 13.654 1.00 20.64 C ANISOU 1654 CG GLU A 229 2543 2712 2589 -134 -197 -108 C ATOM 1655 CD GLU A 229 32.845 -32.027 14.906 1.00 28.05 C ANISOU 1655 CD GLU A 229 3493 3662 3504 -132 -220 -98 C ATOM 1656 OE1 GLU A 229 32.361 -31.768 16.037 1.00 29.34 O ANISOU 1656 OE1 GLU A 229 3694 3816 3640 -139 -219 -103 O ATOM 1657 OE2 GLU A 229 33.762 -32.870 14.752 1.00 25.61 O1- ANISOU 1657 OE2 GLU A 229 3156 3372 3203 -120 -240 -84 O1- ATOM 1658 N THR A 230 27.970 -29.564 13.804 1.00 14.42 N ANISOU 1658 N THR A 230 1826 1865 1789 -111 -98 -127 N ATOM 1659 CA THR A 230 26.881 -28.650 14.156 1.00 17.66 C ANISOU 1659 CA THR A 230 2263 2260 2187 -101 -69 -134 C ATOM 1660 C THR A 230 25.817 -29.335 15.025 1.00 16.59 C ANISOU 1660 C THR A 230 2138 2130 2036 -85 -47 -123 C ATOM 1661 O THR A 230 25.336 -28.742 15.995 1.00 18.38 O ANISOU 1661 O THR A 230 2400 2349 2235 -77 -30 -130 O ATOM 1662 CB THR A 230 26.267 -28.067 12.882 1.00 16.50 C ANISOU 1662 CB THR A 230 2096 2107 2067 -93 -52 -133 C ATOM 1663 CG2 THR A 230 25.269 -26.936 13.192 1.00 15.12 C ANISOU 1663 CG2 THR A 230 1950 1915 1879 -76 -23 -140 C ATOM 1664 OG1 THR A 230 27.328 -27.540 12.080 1.00 18.57 O ANISOU 1664 OG1 THR A 230 2347 2367 2342 -111 -73 -140 O ATOM 1665 N VAL A 231 25.428 -30.572 14.701 1.00 15.06 N ANISOU 1665 N VAL A 231 1918 1948 1856 -81 -45 -105 N ATOM 1666 CA VAL A 231 24.482 -31.285 15.568 1.00 16.45 C ANISOU 1666 CA VAL A 231 2103 2131 2014 -73 -26 -91 C ATOM 1667 C VAL A 231 25.116 -31.560 16.932 1.00 18.78 C ANISOU 1667 C VAL A 231 2431 2427 2277 -79 -41 -94 C ATOM 1668 O VAL A 231 24.515 -31.298 17.982 1.00 18.06 O ANISOU 1668 O VAL A 231 2369 2337 2157 -72 -21 -94 O ATOM 1669 CB VAL A 231 23.998 -32.593 14.910 1.00 17.84 C ANISOU 1669 CB VAL A 231 2251 2316 2211 -76 -27 -70 C ATOM 1670 CG1 VAL A 231 23.173 -33.418 15.906 1.00 16.60 C ANISOU 1670 CG1 VAL A 231 2105 2168 2033 -76 -12 -51 C ATOM 1671 CG2 VAL A 231 23.160 -32.304 13.654 1.00 18.96 C ANISOU 1671 CG2 VAL A 231 2363 2459 2380 -73 -11 -64 C ATOM 1672 N ALA A 232 26.350 -32.082 16.933 1.00 15.01 N ANISOU 1672 N ALA A 232 1949 1953 1802 -90 -76 -95 N ATOM 1673 CA ALA A 232 26.995 -32.472 18.182 1.00 19.72 C ANISOU 1673 CA ALA A 232 2572 2553 2367 -96 -96 -93 C ATOM 1674 C ALA A 232 27.144 -31.301 19.131 1.00 18.52 C ANISOU 1674 C ALA A 232 2461 2394 2183 -102 -95 -111 C ATOM 1675 O ALA A 232 27.104 -31.488 20.349 1.00 23.39 O ANISOU 1675 O ALA A 232 3111 3012 2764 -104 -96 -109 O ATOM 1676 CB ALA A 232 28.371 -33.087 17.921 1.00 16.59 C ANISOU 1676 CB ALA A 232 2158 2165 1982 -103 -135 -89 C ATOM 1677 N ALA A 233 27.316 -30.100 18.605 1.00 19.99 N ANISOU 1677 N ALA A 233 2651 2568 2375 -107 -92 -128 N ATOM 1678 CA ALA A 233 27.503 -28.924 19.441 1.00 19.18 C ANISOU 1678 CA ALA A 233 2597 2451 2238 -115 -93 -147 C ATOM 1679 C ALA A 233 26.202 -28.368 19.998 1.00 20.64 C ANISOU 1679 C ALA A 233 2815 2626 2402 -92 -49 -152 C ATOM 1680 O ALA A 233 26.239 -27.317 20.638 1.00 18.45 O ANISOU 1680 O ALA A 233 2587 2329 2094 -94 -44 -171 O ATOM 1681 CB ALA A 233 28.233 -27.829 18.657 1.00 20.82 C ANISOU 1681 CB ALA A 233 2803 2648 2460 -132 -110 -162 C ATOM 1682 N GLY A 234 25.066 -29.036 19.789 1.00 22.13 N ANISOU 1682 N GLY A 234 2980 2826 2604 -72 -18 -135 N ATOM 1683 CA GLY A 234 23.801 -28.499 20.255 1.00 18.12 C ANISOU 1683 CA GLY A 234 2493 2315 2078 -45 28 -135 C ATOM 1684 C GLY A 234 23.322 -27.277 19.500 1.00 19.13 C ANISOU 1684 C GLY A 234 2623 2426 2219 -28 50 -147 C ATOM 1685 O GLY A 234 22.580 -26.467 20.055 1.00 15.99 O ANISOU 1685 O GLY A 234 2261 2018 1797 -3 84 -155 O ATOM 1686 N LEU A 235 23.711 -27.127 18.233 1.00 18.23 N ANISOU 1686 N LEU A 235 2475 2309 2143 -38 34 -147 N ATOM 1687 CA LEU A 235 23.377 -25.929 17.470 1.00 18.60 C ANISOU 1687 CA LEU A 235 2528 2337 2203 -24 49 -157 C ATOM 1688 C LEU A 235 22.298 -26.165 16.422 1.00 17.70 C ANISOU 1688 C LEU A 235 2366 2237 2123 -3 74 -138 C ATOM 1689 O LEU A 235 22.135 -25.324 15.525 1.00 18.20 O ANISOU 1689 O LEU A 235 2424 2287 2205 5 80 -142 O ATOM 1690 CB LEU A 235 24.638 -25.357 16.809 1.00 19.01 C ANISOU 1690 CB LEU A 235 2582 2373 2266 -53 12 -172 C ATOM 1691 CG LEU A 235 25.778 -24.921 17.747 1.00 19.30 C ANISOU 1691 CG LEU A 235 2667 2396 2269 -80 -19 -190 C ATOM 1692 CD1 LEU A 235 27.058 -24.616 16.965 1.00 19.22 C ANISOU 1692 CD1 LEU A 235 2641 2385 2278 -115 -59 -195 C ATOM 1693 CD2 LEU A 235 25.324 -23.712 18.604 1.00 17.95 C ANISOU 1693 CD2 LEU A 235 2565 2195 2059 -65 3 -210 C ATOM 1694 N THR A 236 21.567 -27.279 16.491 1.00 16.28 N ANISOU 1694 N THR A 236 2152 2084 1951 1 86 -115 N ATOM 1695 CA THR A 236 20.437 -27.481 15.585 1.00 16.94 C ANISOU 1695 CA THR A 236 2190 2184 2063 16 109 -93 C ATOM 1696 C THR A 236 19.139 -27.557 16.379 1.00 21.14 C ANISOU 1696 C THR A 236 2720 2735 2575 44 151 -76 C ATOM 1697 O THR A 236 19.118 -27.333 17.589 1.00 19.32 O ANISOU 1697 O THR A 236 2530 2501 2309 55 166 -84 O ATOM 1698 CB THR A 236 20.637 -28.717 14.708 1.00 21.16 C ANISOU 1698 CB THR A 236 2680 2733 2625 -8 85 -76 C ATOM 1699 CG2 THR A 236 21.966 -28.599 13.959 1.00 15.06 C ANISOU 1699 CG2 THR A 236 1908 1945 1868 -29 48 -92 C ATOM 1700 OG1 THR A 236 20.621 -29.916 15.510 1.00 19.98 O ANISOU 1700 OG1 THR A 236 2532 2598 2462 -20 80 -64 O ATOM 1701 N GLU A 237 18.039 -27.821 15.666 1.00 19.17 N ANISOU 1701 N GLU A 237 2425 2510 2350 55 170 -50 N ATOM 1702 CA GLU A 237 16.730 -27.876 16.300 1.00 21.54 C ANISOU 1702 CA GLU A 237 2711 2838 2636 81 213 -27 C ATOM 1703 C GLU A 237 16.712 -28.936 17.399 1.00 23.99 C ANISOU 1703 C GLU A 237 3029 3164 2921 65 215 -17 C ATOM 1704 O GLU A 237 17.508 -29.882 17.395 1.00 21.15 O ANISOU 1704 O GLU A 237 2672 2799 2565 31 181 -18 O ATOM 1705 CB GLU A 237 15.649 -28.159 15.256 1.00 20.42 C ANISOU 1705 CB GLU A 237 2507 2725 2526 85 224 5 C ATOM 1706 CG GLU A 237 15.674 -29.581 14.661 1.00 19.55 C ANISOU 1706 CG GLU A 237 2359 2632 2436 43 195 25 C ATOM 1707 CD GLU A 237 16.753 -29.758 13.608 1.00 19.37 C ANISOU 1707 CD GLU A 237 2338 2584 2436 17 153 8 C ATOM 1708 OE1 GLU A 237 17.340 -28.741 13.178 1.00 19.46 O ANISOU 1708 OE1 GLU A 237 2368 2573 2454 29 147 -14 O ATOM 1709 OE2 GLU A 237 17.006 -30.920 13.198 1.00 19.10 O1- ANISOU 1709 OE2 GLU A 237 2288 2554 2414 -15 127 18 O1- ATOM 1710 N ASP A 238 15.815 -28.745 18.373 1.00 20.80 N ANISOU 1710 N ASP A 238 2634 2779 2489 92 257 -5 N ATOM 1711 CA ASP A 238 15.726 -29.680 19.490 1.00 24.39 C ANISOU 1711 CA ASP A 238 3101 3251 2915 77 263 7 C ATOM 1712 C ASP A 238 15.352 -31.080 19.006 1.00 23.94 C ANISOU 1712 C ASP A 238 2996 3219 2880 41 247 40 C ATOM 1713 O ASP A 238 15.918 -32.077 19.468 1.00 24.39 O ANISOU 1713 O ASP A 238 3069 3272 2928 12 222 42 O ATOM 1714 CB ASP A 238 14.707 -29.169 20.513 1.00 26.96 C ANISOU 1714 CB ASP A 238 3439 3597 3206 116 318 17 C ATOM 1715 CG ASP A 238 15.278 -28.088 21.433 1.00 31.99 C ANISOU 1715 CG ASP A 238 4148 4202 3803 142 330 -19 C ATOM 1716 OD1 ASP A 238 16.514 -27.946 21.498 1.00 32.97 O ANISOU 1716 OD1 ASP A 238 4313 4293 3922 120 290 -47 O ATOM 1717 OD2 ASP A 238 14.485 -27.367 22.082 1.00 32.67 O1- ANISOU 1717 OD2 ASP A 238 4254 4298 3863 186 379 -18 O1- ATOM 1718 N ASP A 239 14.436 -31.175 18.044 1.00 20.13 N ANISOU 1718 N ASP A 239 2459 2760 2428 42 256 65 N ATOM 1719 CA ASP A 239 13.925 -32.466 17.583 1.00 21.43 C ANISOU 1719 CA ASP A 239 2583 2949 2610 4 241 98 C ATOM 1720 C ASP A 239 13.975 -32.579 16.065 1.00 21.76 C ANISOU 1720 C ASP A 239 2590 2985 2692 -13 213 102 C ATOM 1721 O ASP A 239 13.076 -32.067 15.373 1.00 21.58 O ANISOU 1721 O ASP A 239 2527 2985 2688 2 230 120 O ATOM 1722 CB ASP A 239 12.506 -32.673 18.091 1.00 21.60 C ANISOU 1722 CB ASP A 239 2567 3018 2621 13 284 137 C ATOM 1723 CG ASP A 239 11.999 -34.089 17.852 1.00 24.56 C ANISOU 1723 CG ASP A 239 2909 3416 3005 -36 267 174 C ATOM 1724 OD1 ASP A 239 12.751 -34.917 17.278 1.00 21.24 O ANISOU 1724 OD1 ASP A 239 2501 2970 2600 -72 223 167 O ATOM 1725 OD2 ASP A 239 10.863 -34.376 18.289 1.00 23.18 O1- ANISOU 1725 OD2 ASP A 239 2701 3285 2821 -39 299 211 O1- ATOM 1726 N PRO A 240 14.987 -33.251 15.507 1.00 19.73 N ANISOU 1726 N PRO A 240 2348 2701 2448 -43 170 87 N ATOM 1727 CA PRO A 240 14.999 -33.474 14.049 1.00 19.85 C ANISOU 1727 CA PRO A 240 2334 2712 2496 -61 145 92 C ATOM 1728 C PRO A 240 13.842 -34.330 13.552 1.00 19.45 C ANISOU 1728 C PRO A 240 2240 2693 2458 -90 146 132 C ATOM 1729 O PRO A 240 13.459 -34.204 12.382 1.00 17.12 O ANISOU 1729 O PRO A 240 1914 2405 2187 -98 135 142 O ATOM 1730 CB PRO A 240 16.350 -34.160 13.810 1.00 19.05 C ANISOU 1730 CB PRO A 240 2264 2577 2398 -83 105 70 C ATOM 1731 CG PRO A 240 16.666 -34.820 15.089 1.00 22.69 C ANISOU 1731 CG PRO A 240 2756 3035 2830 -89 106 71 C ATOM 1732 CD PRO A 240 16.084 -33.959 16.186 1.00 19.80 C ANISOU 1732 CD PRO A 240 2398 2687 2439 -60 145 71 C ATOM 1733 N LEU A 241 13.241 -35.168 14.408 1.00 19.17 N ANISOU 1733 N LEU A 241 2201 2679 2404 -108 158 158 N ATOM 1734 CA LEU A 241 12.213 -36.090 13.937 1.00 20.62 C ANISOU 1734 CA LEU A 241 2345 2891 2597 -147 152 198 C ATOM 1735 C LEU A 241 10.929 -35.373 13.524 1.00 23.78 C ANISOU 1735 C LEU A 241 2688 3336 3010 -130 181 227 C ATOM 1736 O LEU A 241 10.119 -35.950 12.792 1.00 22.61 O ANISOU 1736 O LEU A 241 2501 3214 2877 -165 168 260 O ATOM 1737 CB LEU A 241 11.899 -37.119 15.020 1.00 23.52 C ANISOU 1737 CB LEU A 241 2726 3272 2940 -173 160 222 C ATOM 1738 CG LEU A 241 13.062 -37.974 15.527 1.00 22.31 C ANISOU 1738 CG LEU A 241 2627 3077 2771 -189 131 201 C ATOM 1739 CD1 LEU A 241 12.499 -39.042 16.456 1.00 22.48 C ANISOU 1739 CD1 LEU A 241 2656 3116 2769 -221 138 234 C ATOM 1740 CD2 LEU A 241 13.779 -38.624 14.371 1.00 20.83 C ANISOU 1740 CD2 LEU A 241 2454 2857 2605 -213 88 189 C ATOM 1741 N THR A 242 10.717 -34.136 13.974 1.00 23.79 N ANISOU 1741 N THR A 242 2686 3348 3005 -78 217 217 N ATOM 1742 CA THR A 242 9.469 -33.426 13.717 1.00 21.97 C ANISOU 1742 CA THR A 242 2400 3163 2784 -51 249 248 C ATOM 1743 C THR A 242 9.705 -32.113 12.979 1.00 22.37 C ANISOU 1743 C THR A 242 2451 3196 2851 -8 253 226 C ATOM 1744 O THR A 242 8.904 -31.186 13.094 1.00 23.71 O ANISOU 1744 O THR A 242 2595 3393 3022 37 289 240 O ATOM 1745 CB THR A 242 8.704 -33.149 15.017 1.00 24.59 C ANISOU 1745 CB THR A 242 2724 3531 3089 -20 301 267 C ATOM 1746 CG2 THR A 242 8.301 -34.438 15.714 1.00 26.01 C ANISOU 1746 CG2 THR A 242 2896 3735 3252 -66 300 298 C ATOM 1747 OG1 THR A 242 9.519 -32.361 15.899 1.00 24.40 O ANISOU 1747 OG1 THR A 242 2757 3473 3041 21 319 227 O ATOM 1748 N THR A 243 10.796 -32.000 12.232 1.00 21.85 N ANISOU 1748 N THR A 243 2418 3086 2799 -19 218 192 N ATOM 1749 CA THR A 243 10.972 -30.806 11.412 1.00 22.32 C ANISOU 1749 CA THR A 243 2477 3130 2875 15 218 176 C ATOM 1750 C THR A 243 9.902 -30.737 10.321 1.00 24.60 C ANISOU 1750 C THR A 243 2704 3454 3187 10 215 212 C ATOM 1751 O THR A 243 9.224 -31.715 10.009 1.00 20.48 O ANISOU 1751 O THR A 243 2145 2963 2672 -31 201 246 O ATOM 1752 CB THR A 243 12.368 -30.766 10.779 1.00 20.83 C ANISOU 1752 CB THR A 243 2329 2891 2693 -1 181 137 C ATOM 1753 CG2 THR A 243 13.497 -30.643 11.844 1.00 20.44 C ANISOU 1753 CG2 THR A 243 2337 2809 2620 7 181 101 C ATOM 1754 OG1 THR A 243 12.562 -31.935 9.981 1.00 19.19 O ANISOU 1754 OG1 THR A 243 2111 2682 2499 -51 144 146 O ATOM 1755 N ASN A 244 9.749 -29.552 9.741 1.00 23.54 N ANISOU 1755 N ASN A 244 2564 3316 3066 50 225 208 N ATOM 1756 CA ASN A 244 8.729 -29.334 8.722 1.00 23.02 C ANISOU 1756 CA ASN A 244 2439 3286 3022 52 222 244 C ATOM 1757 C ASN A 244 9.266 -28.341 7.704 1.00 21.00 C ANISOU 1757 C ASN A 244 2201 2997 2782 73 207 222 C ATOM 1758 O ASN A 244 9.538 -27.192 8.058 1.00 21.50 O ANISOU 1758 O ASN A 244 2294 3036 2838 122 231 201 O ATOM 1759 CB ASN A 244 7.432 -28.824 9.347 1.00 22.74 C ANISOU 1759 CB ASN A 244 2357 3301 2981 97 269 281 C ATOM 1760 CG ASN A 244 6.329 -28.636 8.325 1.00 24.20 C ANISOU 1760 CG ASN A 244 2474 3532 3189 99 264 326 C ATOM 1761 ND2 ASN A 244 5.286 -29.450 8.407 1.00 22.20 N ANISOU 1761 ND2 ASN A 244 2161 3335 2937 70 266 373 N ATOM 1762 OD1 ASN A 244 6.407 -27.749 7.488 1.00 21.97 O ANISOU 1762 OD1 ASN A 244 2193 3234 2922 126 257 319 O ATOM 1763 N TRP A 245 9.389 -28.777 6.445 1.00 19.75 N ANISOU 1763 N TRP A 245 2028 2836 2642 34 168 229 N ATOM 1764 CA TRP A 245 9.973 -27.931 5.408 1.00 23.31 C ANISOU 1764 CA TRP A 245 2496 3255 3105 46 151 209 C ATOM 1765 C TRP A 245 9.194 -26.628 5.234 1.00 23.64 C ANISOU 1765 C TRP A 245 2517 3311 3154 103 178 227 C ATOM 1766 O TRP A 245 9.788 -25.544 5.249 1.00 20.37 O ANISOU 1766 O TRP A 245 2143 2859 2737 139 188 199 O ATOM 1767 CB TRP A 245 10.063 -28.701 4.089 1.00 21.11 C ANISOU 1767 CB TRP A 245 2201 2978 2840 -6 107 219 C ATOM 1768 CG TRP A 245 10.264 -27.815 2.912 1.00 22.73 C ANISOU 1768 CG TRP A 245 2410 3168 3059 7 93 214 C ATOM 1769 CD1 TRP A 245 9.380 -27.589 1.896 1.00 27.74 C ANISOU 1769 CD1 TRP A 245 3002 3832 3708 6 81 248 C ATOM 1770 CD2 TRP A 245 11.415 -27.008 2.626 1.00 24.60 C ANISOU 1770 CD2 TRP A 245 2694 3356 3295 22 88 175 C ATOM 1771 CE2 TRP A 245 11.161 -26.332 1.411 1.00 24.72 C ANISOU 1771 CE2 TRP A 245 2696 3373 3324 29 74 188 C ATOM 1772 CE3 TRP A 245 12.633 -26.791 3.279 1.00 20.97 C ANISOU 1772 CE3 TRP A 245 2287 2856 2824 27 92 135 C ATOM 1773 NE1 TRP A 245 9.914 -26.704 0.989 1.00 26.11 N ANISOU 1773 NE1 TRP A 245 2816 3595 3508 20 69 232 N ATOM 1774 CZ2 TRP A 245 12.077 -25.450 0.836 1.00 22.44 C ANISOU 1774 CZ2 TRP A 245 2444 3044 3037 40 67 161 C ATOM 1775 CZ3 TRP A 245 13.555 -25.928 2.699 1.00 23.98 C ANISOU 1775 CZ3 TRP A 245 2703 3202 3208 35 83 109 C ATOM 1776 CH2 TRP A 245 13.267 -25.261 1.490 1.00 25.11 C ANISOU 1776 CH2 TRP A 245 2832 3344 3364 41 72 122 C ATOM 1777 N GLU A 246 7.862 -26.705 5.077 1.00 21.87 N ANISOU 1777 N GLU A 246 2230 3141 2939 114 190 274 N ATOM 1778 CA GLU A 246 7.079 -25.484 4.876 1.00 24.79 C ANISOU 1778 CA GLU A 246 2576 3527 3317 176 217 295 C ATOM 1779 C GLU A 246 7.197 -24.545 6.064 1.00 22.10 C ANISOU 1779 C GLU A 246 2274 3166 2957 240 264 274 C ATOM 1780 O GLU A 246 7.356 -23.332 5.891 1.00 23.53 O ANISOU 1780 O GLU A 246 2485 3317 3139 289 278 260 O ATOM 1781 CB GLU A 246 5.605 -25.803 4.609 1.00 25.12 C ANISOU 1781 CB GLU A 246 2534 3640 3369 178 224 355 C ATOM 1782 CG GLU A 246 5.334 -26.604 3.354 1.00 29.32 C ANISOU 1782 CG GLU A 246 3028 4195 3917 116 175 381 C ATOM 1783 CD GLU A 246 5.625 -25.824 2.082 1.00 40.87 C ANISOU 1783 CD GLU A 246 4502 5632 5394 125 150 375 C ATOM 1784 OE1 GLU A 246 5.860 -26.468 1.024 1.00 43.85 O ANISOU 1784 OE1 GLU A 246 4877 6006 5778 69 105 377 O ATOM 1785 OE2 GLU A 246 5.604 -24.566 2.135 1.00 41.11 O1- ANISOU 1785 OE2 GLU A 246 4548 5645 5426 189 175 368 O1- ATOM 1786 N LYS A 247 7.065 -25.080 7.280 1.00 23.38 N ANISOU 1786 N LYS A 247 2441 3343 3100 240 290 273 N ATOM 1787 CA LYS A 247 7.231 -24.251 8.473 1.00 24.66 C ANISOU 1787 CA LYS A 247 2650 3482 3238 296 334 249 C ATOM 1788 C LYS A 247 8.619 -23.607 8.516 1.00 22.81 C ANISOU 1788 C LYS A 247 2496 3176 2993 295 319 194 C ATOM 1789 O LYS A 247 8.767 -22.453 8.941 1.00 22.71 O ANISOU 1789 O LYS A 247 2530 3131 2967 348 346 174 O ATOM 1790 CB LYS A 247 6.979 -25.085 9.738 1.00 26.37 C ANISOU 1790 CB LYS A 247 2861 3726 3432 285 359 256 C ATOM 1791 CG LYS A 247 7.373 -24.389 11.050 1.00 32.76 C ANISOU 1791 CG LYS A 247 3734 4504 4208 331 398 223 C ATOM 1792 CD LYS A 247 6.669 -24.958 12.297 1.00 39.42 C ANISOU 1792 CD LYS A 247 4559 5392 5028 341 439 244 C ATOM 1793 CE LYS A 247 6.677 -26.498 12.353 1.00 46.18 C ANISOU 1793 CE LYS A 247 5383 6276 5888 268 410 262 C ATOM 1794 NZ LYS A 247 8.041 -27.115 12.206 1.00 39.10 N1+ ANISOU 1794 NZ LYS A 247 4537 5329 4989 212 363 223 N1+ ATOM 1795 N SER A 248 9.647 -24.318 8.046 1.00 20.85 N ANISOU 1795 N SER A 248 2268 2903 2752 236 276 172 N ATOM 1796 CA SER A 248 10.999 -23.778 8.167 1.00 19.50 C ANISOU 1796 CA SER A 248 2167 2673 2570 229 261 124 C ATOM 1797 C SER A 248 11.223 -22.587 7.244 1.00 21.06 C ANISOU 1797 C SER A 248 2384 2838 2780 254 253 115 C ATOM 1798 O SER A 248 12.051 -21.718 7.553 1.00 21.10 O ANISOU 1798 O SER A 248 2450 2795 2771 267 256 82 O ATOM 1799 CB SER A 248 12.035 -24.872 7.903 1.00 19.82 C ANISOU 1799 CB SER A 248 2217 2700 2614 165 219 106 C ATOM 1800 OG SER A 248 12.119 -25.189 6.531 1.00 17.58 O ANISOU 1800 OG SER A 248 1906 2420 2354 134 186 116 O ATOM 1801 N LYS A 249 10.522 -22.528 6.105 1.00 19.88 N ANISOU 1801 N LYS A 249 2186 2713 2654 255 242 147 N ATOM 1802 CA LYS A 249 10.607 -21.341 5.259 1.00 22.84 C ANISOU 1802 CA LYS A 249 2580 3059 3038 284 238 144 C ATOM 1803 C LYS A 249 10.103 -20.114 6.010 1.00 21.47 C ANISOU 1803 C LYS A 249 2437 2870 2849 357 282 143 C ATOM 1804 O LYS A 249 10.770 -19.071 6.043 1.00 22.20 O ANISOU 1804 O LYS A 249 2593 2909 2932 376 284 114 O ATOM 1805 CB LYS A 249 9.813 -21.555 3.967 1.00 26.17 C ANISOU 1805 CB LYS A 249 2941 3517 3485 274 218 184 C ATOM 1806 CG LYS A 249 10.361 -22.685 3.105 1.00 24.15 C ANISOU 1806 CG LYS A 249 2667 3268 3240 203 173 182 C ATOM 1807 CD LYS A 249 9.330 -23.201 2.101 1.00 28.13 C ANISOU 1807 CD LYS A 249 3105 3822 3762 186 155 227 C ATOM 1808 CE LYS A 249 9.189 -22.318 0.898 1.00 30.06 C ANISOU 1808 CE LYS A 249 3346 4056 4020 202 140 239 C ATOM 1809 NZ LYS A 249 8.327 -23.026 -0.102 1.00 32.44 N1+ ANISOU 1809 NZ LYS A 249 3585 4405 4335 170 113 281 N1+ ATOM 1810 N VAL A 250 8.924 -20.229 6.626 1.00 22.50 N ANISOU 1810 N VAL A 250 2526 3046 2976 398 319 174 N ATOM 1811 CA VAL A 250 8.392 -19.140 7.448 1.00 24.11 C ANISOU 1811 CA VAL A 250 2762 3237 3161 475 368 173 C ATOM 1812 C VAL A 250 9.333 -18.831 8.610 1.00 25.59 C ANISOU 1812 C VAL A 250 3033 3374 3316 476 381 125 C ATOM 1813 O VAL A 250 9.602 -17.662 8.919 1.00 23.47 O ANISOU 1813 O VAL A 250 2832 3056 3031 519 399 101 O ATOM 1814 CB VAL A 250 6.978 -19.500 7.949 1.00 22.51 C ANISOU 1814 CB VAL A 250 2491 3103 2959 515 408 218 C ATOM 1815 CG1 VAL A 250 6.351 -18.342 8.703 1.00 24.92 C ANISOU 1815 CG1 VAL A 250 2827 3398 3245 606 464 220 C ATOM 1816 CG2 VAL A 250 6.091 -19.883 6.776 1.00 23.97 C ANISOU 1816 CG2 VAL A 250 2590 3342 3176 502 387 268 C ATOM 1817 N ASP A 251 9.823 -19.870 9.289 1.00 20.56 N ANISOU 1817 N ASP A 251 2396 2749 2668 429 370 112 N ATOM 1818 CA ASP A 251 10.682 -19.646 10.447 1.00 23.31 C ANISOU 1818 CA ASP A 251 2819 3056 2983 427 379 70 C ATOM 1819 C ASP A 251 11.987 -18.972 10.047 1.00 23.02 C ANISOU 1819 C ASP A 251 2848 2955 2944 399 346 31 C ATOM 1820 O ASP A 251 12.465 -18.074 10.751 1.00 22.99 O ANISOU 1820 O ASP A 251 2920 2905 2913 422 359 0 O ATOM 1821 CB ASP A 251 10.951 -20.962 11.172 1.00 22.38 C ANISOU 1821 CB ASP A 251 2683 2964 2854 379 370 68 C ATOM 1822 CG ASP A 251 9.767 -21.414 11.997 1.00 25.40 C ANISOU 1822 CG ASP A 251 3024 3400 3225 411 413 100 C ATOM 1823 OD1 ASP A 251 8.786 -20.644 12.118 1.00 26.76 O ANISOU 1823 OD1 ASP A 251 3184 3589 3395 476 455 121 O ATOM 1824 OD2 ASP A 251 9.811 -22.543 12.512 1.00 29.73 O1- ANISOU 1824 OD2 ASP A 251 3552 3977 3769 371 407 107 O1- ATOM 1825 N PHE A 252 12.568 -19.378 8.914 1.00 20.88 N ANISOU 1825 N PHE A 252 2552 2683 2698 349 302 32 N ATOM 1826 CA PHE A 252 13.784 -18.727 8.444 1.00 19.06 C ANISOU 1826 CA PHE A 252 2375 2399 2467 322 272 1 C ATOM 1827 C PHE A 252 13.503 -17.284 8.083 1.00 21.49 C ANISOU 1827 C PHE A 252 2723 2670 2773 371 288 0 C ATOM 1828 O PHE A 252 14.238 -16.379 8.488 1.00 24.24 O ANISOU 1828 O PHE A 252 3147 2964 3100 374 287 -31 O ATOM 1829 CB PHE A 252 14.369 -19.463 7.241 1.00 18.89 C ANISOU 1829 CB PHE A 252 2315 2390 2473 265 228 7 C ATOM 1830 CG PHE A 252 15.578 -18.785 6.642 1.00 21.25 C ANISOU 1830 CG PHE A 252 2659 2642 2772 235 199 -20 C ATOM 1831 CD1 PHE A 252 16.854 -18.994 7.162 1.00 22.23 C ANISOU 1831 CD1 PHE A 252 2822 2744 2882 194 177 -51 C ATOM 1832 CD2 PHE A 252 15.434 -17.906 5.576 1.00 20.29 C ANISOU 1832 CD2 PHE A 252 2542 2502 2665 249 192 -10 C ATOM 1833 CE1 PHE A 252 17.973 -18.342 6.610 1.00 20.46 C ANISOU 1833 CE1 PHE A 252 2634 2483 2658 163 150 -71 C ATOM 1834 CE2 PHE A 252 16.539 -17.255 5.029 1.00 22.04 C ANISOU 1834 CE2 PHE A 252 2806 2683 2886 218 167 -31 C ATOM 1835 CZ PHE A 252 17.810 -17.473 5.545 1.00 19.20 C ANISOU 1835 CZ PHE A 252 2479 2304 2512 174 146 -61 C ATOM 1836 N ALA A 253 12.418 -17.054 7.331 1.00 20.88 N ANISOU 1836 N ALA A 253 2598 2620 2717 409 302 36 N ATOM 1837 CA ALA A 253 12.093 -15.718 6.842 1.00 23.28 C ANISOU 1837 CA ALA A 253 2935 2887 3021 459 315 40 C ATOM 1838 C ALA A 253 11.795 -14.743 7.969 1.00 23.72 C ANISOU 1838 C ALA A 253 3058 2909 3044 523 358 24 C ATOM 1839 O ALA A 253 11.969 -13.533 7.792 1.00 24.49 O ANISOU 1839 O ALA A 253 3220 2953 3133 554 364 12 O ATOM 1840 CB ALA A 253 10.898 -15.777 5.893 1.00 24.67 C ANISOU 1840 CB ALA A 253 3039 3110 3226 491 321 88 C ATOM 1841 N THR A 254 11.321 -15.228 9.113 1.00 20.82 N ANISOU 1841 N THR A 254 2683 2569 2657 544 391 25 N ATOM 1842 CA THR A 254 10.988 -14.359 10.232 1.00 23.38 C ANISOU 1842 CA THR A 254 3074 2862 2945 609 437 9 C ATOM 1843 C THR A 254 12.034 -14.385 11.342 1.00 25.03 C ANISOU 1843 C THR A 254 3361 3032 3118 574 430 -37 C ATOM 1844 O THR A 254 11.779 -13.860 12.431 1.00 23.75 O ANISOU 1844 O THR A 254 3257 2849 2919 621 469 -52 O ATOM 1845 CB THR A 254 9.613 -14.720 10.795 1.00 24.45 C ANISOU 1845 CB THR A 254 3152 3060 3079 669 487 44 C ATOM 1846 CG2 THR A 254 8.530 -14.485 9.759 1.00 28.30 C ANISOU 1846 CG2 THR A 254 3569 3585 3599 712 496 91 C ATOM 1847 OG1 THR A 254 9.610 -16.088 11.199 1.00 25.18 O ANISOU 1847 OG1 THR A 254 3187 3204 3174 620 478 53 O ATOM 1848 N GLY A 255 13.194 -14.986 11.093 1.00 22.52 N ANISOU 1848 N GLY A 255 3044 2706 2807 496 382 -56 N ATOM 1849 CA GLY A 255 14.291 -14.921 12.031 1.00 23.35 C ANISOU 1849 CA GLY A 255 3222 2773 2879 459 366 -96 C ATOM 1850 C GLY A 255 14.266 -15.941 13.143 1.00 23.79 C ANISOU 1850 C GLY A 255 3261 2863 2915 444 377 -99 C ATOM 1851 O GLY A 255 15.079 -15.835 14.071 1.00 26.28 O ANISOU 1851 O GLY A 255 3641 3148 3196 420 368 -131 O ATOM 1852 N ARG A 256 13.377 -16.929 13.087 1.00 20.73 N ANISOU 1852 N ARG A 256 2793 2539 2545 452 393 -66 N ATOM 1853 CA ARG A 256 13.412 -18.014 14.061 1.00 21.73 C ANISOU 1853 CA ARG A 256 2902 2700 2655 429 398 -66 C ATOM 1854 C ARG A 256 14.436 -19.092 13.713 1.00 20.23 C ANISOU 1854 C ARG A 256 2685 2519 2481 352 347 -72 C ATOM 1855 O ARG A 256 14.799 -19.880 14.591 1.00 19.34 O ANISOU 1855 O ARG A 256 2579 2419 2349 325 341 -80 O ATOM 1856 CB ARG A 256 12.032 -18.648 14.198 1.00 22.71 C ANISOU 1856 CB ARG A 256 2953 2888 2789 465 437 -24 C ATOM 1857 CG ARG A 256 11.062 -17.818 15.013 1.00 28.84 C ANISOU 1857 CG ARG A 256 3759 3664 3536 546 499 -19 C ATOM 1858 CD ARG A 256 9.636 -17.947 14.506 1.00 35.02 C ANISOU 1858 CD ARG A 256 4456 4505 4343 594 532 31 C ATOM 1859 NE ARG A 256 8.798 -16.847 14.974 1.00 43.47 N ANISOU 1859 NE ARG A 256 5560 5566 5392 684 589 35 N ATOM 1860 CZ ARG A 256 7.863 -16.242 14.249 1.00 46.05 C ANISOU 1860 CZ ARG A 256 5847 5910 5740 742 612 67 C ATOM 1861 NH1 ARG A 256 7.589 -16.629 13.009 1.00 40.47 N1+ ANISOU 1861 NH1 ARG A 256 5064 5236 5078 715 580 99 N1+ ATOM 1862 NH2 ARG A 256 7.180 -15.229 14.785 1.00 49.04 N ANISOU 1862 NH2 ARG A 256 6265 6273 6094 830 667 68 N ATOM 1863 N ILE A 257 14.885 -19.156 12.458 1.00 17.62 N ANISOU 1863 N ILE A 257 2326 2185 2185 319 310 -67 N ATOM 1864 CA ILE A 257 15.994 -20.002 12.022 1.00 18.93 C ANISOU 1864 CA ILE A 257 2474 2352 2365 252 262 -77 C ATOM 1865 C ILE A 257 17.068 -19.101 11.418 1.00 19.29 C ANISOU 1865 C ILE A 257 2566 2350 2413 229 232 -101 C ATOM 1866 O ILE A 257 16.748 -18.176 10.665 1.00 21.21 O ANISOU 1866 O ILE A 257 2818 2573 2668 254 239 -96 O ATOM 1867 CB ILE A 257 15.539 -21.049 10.986 1.00 20.28 C ANISOU 1867 CB ILE A 257 2565 2568 2573 230 247 -45 C ATOM 1868 CG1 ILE A 257 14.575 -22.061 11.611 1.00 18.67 C ANISOU 1868 CG1 ILE A 257 2316 2413 2366 238 270 -19 C ATOM 1869 CG2 ILE A 257 16.755 -21.710 10.292 1.00 19.45 C ANISOU 1869 CG2 ILE A 257 2451 2456 2483 170 199 -58 C ATOM 1870 CD1 ILE A 257 13.835 -22.882 10.594 1.00 19.35 C ANISOU 1870 CD1 ILE A 257 2327 2541 2483 223 260 17 C ATOM 1871 N ALA A 258 18.338 -19.378 11.723 1.00 16.19 N ANISOU 1871 N ALA A 258 2200 1942 2010 180 198 -125 N ATOM 1872 CA ALA A 258 19.416 -18.521 11.236 1.00 17.95 C ANISOU 1872 CA ALA A 258 2465 2124 2233 151 169 -146 C ATOM 1873 C ALA A 258 20.063 -19.014 9.941 1.00 18.35 C ANISOU 1873 C ALA A 258 2467 2188 2316 110 135 -137 C ATOM 1874 O ALA A 258 20.414 -18.189 9.094 1.00 17.01 O ANISOU 1874 O ALA A 258 2313 1993 2157 101 122 -139 O ATOM 1875 CB ALA A 258 20.494 -18.366 12.312 1.00 17.02 C ANISOU 1875 CB ALA A 258 2405 1981 2080 120 150 -175 C ATOM 1876 N THR A 259 20.279 -20.324 9.772 1.00 17.09 N ANISOU 1876 N THR A 259 2257 2065 2171 83 119 -126 N ATOM 1877 CA THR A 259 20.973 -20.831 8.590 1.00 18.48 C ANISOU 1877 CA THR A 259 2394 2252 2373 46 88 -120 C ATOM 1878 C THR A 259 20.364 -22.148 8.133 1.00 18.22 C ANISOU 1878 C THR A 259 2300 2261 2361 43 88 -98 C ATOM 1879 O THR A 259 19.780 -22.885 8.934 1.00 19.78 O ANISOU 1879 O THR A 259 2487 2479 2550 54 103 -89 O ATOM 1880 CB THR A 259 22.480 -21.056 8.834 1.00 18.16 C ANISOU 1880 CB THR A 259 2370 2205 2325 1 55 -140 C ATOM 1881 CG2 THR A 259 23.186 -19.743 9.242 1.00 17.11 C ANISOU 1881 CG2 THR A 259 2301 2031 2170 -10 47 -161 C ATOM 1882 OG1 THR A 259 22.645 -22.015 9.880 1.00 19.33 O ANISOU 1882 OG1 THR A 259 2515 2371 2458 -5 52 -142 O ATOM 1883 N MET A 260 20.517 -22.438 6.831 1.00 19.35 N ANISOU 1883 N MET A 260 2409 2413 2529 26 71 -87 N ATOM 1884 CA MET A 260 20.050 -23.681 6.213 1.00 19.61 C ANISOU 1884 CA MET A 260 2392 2478 2579 15 65 -67 C ATOM 1885 C MET A 260 20.859 -23.873 4.938 1.00 20.32 C ANISOU 1885 C MET A 260 2468 2568 2686 -14 39 -69 C ATOM 1886 O MET A 260 20.957 -22.933 4.142 1.00 21.87 O ANISOU 1886 O MET A 260 2673 2748 2889 -12 37 -69 O ATOM 1887 CB MET A 260 18.563 -23.598 5.862 1.00 21.83 C ANISOU 1887 CB MET A 260 2643 2779 2871 44 87 -39 C ATOM 1888 CG MET A 260 17.624 -24.046 6.960 1.00 24.50 C ANISOU 1888 CG MET A 260 2973 3140 3198 66 113 -27 C ATOM 1889 SD MET A 260 15.917 -24.238 6.380 1.00 29.28 S ANISOU 1889 SD MET A 260 3521 3783 3819 89 132 14 S ATOM 1890 CE MET A 260 15.502 -22.540 6.354 1.00 15.54 C ANISOU 1890 CE MET A 260 1810 2019 2076 140 157 12 C ATOM 1891 N ALA A 261 21.461 -25.055 4.746 1.00 16.12 N ANISOU 1891 N ALA A 261 1917 2049 2158 -39 21 -70 N ATOM 1892 CA ALA A 261 22.244 -25.292 3.529 1.00 18.19 C ANISOU 1892 CA ALA A 261 2166 2312 2432 -62 2 -72 C ATOM 1893 C ALA A 261 21.289 -25.680 2.401 1.00 19.10 C ANISOU 1893 C ALA A 261 2252 2442 2562 -61 2 -51 C ATOM 1894 O ALA A 261 20.659 -26.741 2.450 1.00 21.00 O ANISOU 1894 O ALA A 261 2474 2701 2806 -65 1 -37 O ATOM 1895 CB ALA A 261 23.312 -26.362 3.759 1.00 18.46 C ANISOU 1895 CB ALA A 261 2197 2354 2463 -82 -16 -82 C ATOM 1896 N LEU A 262 21.135 -24.799 1.410 1.00 18.06 N ANISOU 1896 N LEU A 262 2121 2303 2440 -58 1 -45 N ATOM 1897 CA LEU A 262 20.236 -25.030 0.281 1.00 18.24 C ANISOU 1897 CA LEU A 262 2117 2340 2474 -59 -2 -23 C ATOM 1898 C LEU A 262 20.805 -24.381 -0.970 1.00 16.48 C ANISOU 1898 C LEU A 262 1899 2106 2256 -71 -13 -25 C ATOM 1899 O LEU A 262 21.610 -23.452 -0.896 1.00 16.77 O ANISOU 1899 O LEU A 262 1960 2123 2289 -73 -13 -39 O ATOM 1900 CB LEU A 262 18.832 -24.477 0.546 1.00 19.88 C ANISOU 1900 CB LEU A 262 2312 2557 2685 -30 16 -1 C ATOM 1901 CG LEU A 262 18.047 -24.934 1.768 1.00 18.90 C ANISOU 1901 CG LEU A 262 2178 2448 2554 -13 34 6 C ATOM 1902 CD1 LEU A 262 16.880 -23.991 2.007 1.00 19.38 C ANISOU 1902 CD1 LEU A 262 2231 2514 2617 26 58 25 C ATOM 1903 CD2 LEU A 262 17.534 -26.362 1.551 1.00 17.92 C ANISOU 1903 CD2 LEU A 262 2024 2351 2434 -36 23 23 C ATOM 1904 N GLY A 263 20.365 -24.873 -2.127 1.00 18.07 N ANISOU 1904 N GLY A 263 2080 2320 2463 -83 -23 -10 N ATOM 1905 CA GLY A 263 20.703 -24.220 -3.382 1.00 17.94 C ANISOU 1905 CA GLY A 263 2069 2296 2450 -93 -32 -7 C ATOM 1906 C GLY A 263 20.092 -22.830 -3.495 1.00 17.17 C ANISOU 1906 C GLY A 263 1982 2186 2357 -70 -22 5 C ATOM 1907 O GLY A 263 19.121 -22.480 -2.824 1.00 16.21 O ANISOU 1907 O GLY A 263 1855 2067 2238 -42 -9 17 O ATOM 1908 N SER A 264 20.671 -21.999 -4.362 1.00 16.57 N ANISOU 1908 N SER A 264 1921 2094 2280 -79 -28 3 N ATOM 1909 CA SER A 264 20.181 -20.622 -4.464 1.00 16.07 C ANISOU 1909 CA SER A 264 1876 2011 2219 -56 -20 14 C ATOM 1910 C SER A 264 18.748 -20.543 -4.989 1.00 19.51 C ANISOU 1910 C SER A 264 2287 2463 2664 -32 -19 44 C ATOM 1911 O SER A 264 18.120 -19.487 -4.874 1.00 18.98 O ANISOU 1911 O SER A 264 2231 2381 2599 0 -9 57 O ATOM 1912 CB SER A 264 21.073 -19.799 -5.383 1.00 19.04 C ANISOU 1912 CB SER A 264 2276 2368 2592 -76 -29 10 C ATOM 1913 OG SER A 264 21.153 -20.433 -6.644 1.00 18.18 O ANISOU 1913 OG SER A 264 2148 2277 2483 -98 -43 19 O ATOM 1914 N TRP A 265 18.230 -21.613 -5.596 1.00 18.39 N ANISOU 1914 N TRP A 265 2112 2350 2524 -48 -32 59 N ATOM 1915 CA TRP A 265 16.801 -21.673 -5.900 1.00 19.88 C ANISOU 1915 CA TRP A 265 2269 2564 2721 -30 -33 92 C ATOM 1916 C TRP A 265 15.943 -21.321 -4.681 1.00 19.64 C ANISOU 1916 C TRP A 265 2229 2538 2694 11 -10 100 C ATOM 1917 O TRP A 265 14.823 -20.812 -4.829 1.00 21.95 O ANISOU 1917 O TRP A 265 2500 2846 2994 42 -3 129 O ATOM 1918 CB TRP A 265 16.448 -23.069 -6.420 1.00 21.33 C ANISOU 1918 CB TRP A 265 2424 2777 2903 -61 -51 101 C ATOM 1919 CG TRP A 265 16.731 -24.135 -5.390 1.00 21.95 C ANISOU 1919 CG TRP A 265 2500 2862 2978 -72 -46 85 C ATOM 1920 CD1 TRP A 265 17.859 -24.904 -5.300 1.00 22.66 C ANISOU 1920 CD1 TRP A 265 2608 2941 3059 -96 -51 59 C ATOM 1921 CD2 TRP A 265 15.891 -24.525 -4.291 1.00 21.67 C ANISOU 1921 CD2 TRP A 265 2444 2844 2945 -55 -32 96 C ATOM 1922 CE2 TRP A 265 16.571 -25.544 -3.585 1.00 24.95 C ANISOU 1922 CE2 TRP A 265 2869 3256 3353 -74 -33 75 C ATOM 1923 CE3 TRP A 265 14.624 -24.126 -3.845 1.00 24.67 C ANISOU 1923 CE3 TRP A 265 2794 3246 3332 -25 -18 124 C ATOM 1924 NE1 TRP A 265 17.768 -25.756 -4.219 1.00 23.41 N ANISOU 1924 NE1 TRP A 265 2698 3044 3153 -96 -45 52 N ATOM 1925 CZ2 TRP A 265 16.030 -26.162 -2.451 1.00 25.09 C ANISOU 1925 CZ2 TRP A 265 2874 3290 3370 -68 -21 80 C ATOM 1926 CZ3 TRP A 265 14.090 -24.734 -2.710 1.00 25.94 C ANISOU 1926 CZ3 TRP A 265 2938 3425 3491 -18 -3 130 C ATOM 1927 CH2 TRP A 265 14.795 -25.746 -2.030 1.00 25.66 C ANISOU 1927 CH2 TRP A 265 2917 3384 3447 -42 -6 108 C ATOM 1928 N ALA A 266 16.449 -21.582 -3.473 1.00 16.50 N ANISOU 1928 N ALA A 266 1847 2132 2291 13 4 77 N ATOM 1929 CA ALA A 266 15.680 -21.336 -2.262 1.00 18.86 C ANISOU 1929 CA ALA A 266 2141 2437 2588 51 30 83 C ATOM 1930 C ALA A 266 15.587 -19.858 -1.901 1.00 19.26 C ANISOU 1930 C ALA A 266 2226 2457 2636 93 49 80 C ATOM 1931 O ALA A 266 14.689 -19.483 -1.137 1.00 19.10 O ANISOU 1931 O ALA A 266 2199 2444 2614 137 74 92 O ATOM 1932 CB ALA A 266 16.289 -22.121 -1.101 1.00 19.74 C ANISOU 1932 CB ALA A 266 2263 2548 2690 38 36 59 C ATOM 1933 N VAL A 267 16.471 -19.013 -2.448 1.00 18.92 N ANISOU 1933 N VAL A 267 2221 2378 2589 83 40 65 N ATOM 1934 CA VAL A 267 16.532 -17.606 -2.048 1.00 19.59 C ANISOU 1934 CA VAL A 267 2354 2423 2667 117 56 58 C ATOM 1935 C VAL A 267 15.197 -16.900 -2.312 1.00 19.81 C ANISOU 1935 C VAL A 267 2366 2459 2703 170 71 91 C ATOM 1936 O VAL A 267 14.598 -16.313 -1.404 1.00 19.73 O ANISOU 1936 O VAL A 267 2372 2439 2686 219 99 92 O ATOM 1937 CB VAL A 267 17.714 -16.901 -2.747 1.00 17.91 C ANISOU 1937 CB VAL A 267 2181 2174 2449 85 39 41 C ATOM 1938 CG1 VAL A 267 17.649 -15.376 -2.553 1.00 18.80 C ANISOU 1938 CG1 VAL A 267 2350 2240 2555 118 51 39 C ATOM 1939 CG2 VAL A 267 19.028 -17.443 -2.181 1.00 15.14 C ANISOU 1939 CG2 VAL A 267 1846 1817 2089 44 29 10 C ATOM 1940 N SER A 268 14.698 -16.964 -3.549 1.00 18.35 N ANISOU 1940 N SER A 268 2150 2294 2530 164 54 119 N ATOM 1941 CA SER A 268 13.446 -16.274 -3.842 1.00 19.77 C ANISOU 1941 CA SER A 268 2309 2485 2717 217 66 154 C ATOM 1942 C SER A 268 12.265 -16.896 -3.104 1.00 20.79 C ANISOU 1942 C SER A 268 2387 2661 2852 247 86 177 C ATOM 1943 O SER A 268 11.299 -16.190 -2.802 1.00 23.66 O ANISOU 1943 O SER A 268 2742 3030 3218 307 109 201 O ATOM 1944 CB SER A 268 13.185 -16.250 -5.352 1.00 23.95 C ANISOU 1944 CB SER A 268 2815 3030 3257 199 38 182 C ATOM 1945 OG SER A 268 13.050 -17.556 -5.857 1.00 28.28 O ANISOU 1945 OG SER A 268 3315 3620 3809 155 16 191 O ATOM 1946 N GLN A 269 12.324 -18.192 -2.770 1.00 19.46 N ANISOU 1946 N GLN A 269 2186 2525 2684 210 78 173 N ATOM 1947 CA GLN A 269 11.259 -18.775 -1.953 1.00 21.87 C ANISOU 1947 CA GLN A 269 2444 2874 2991 234 99 195 C ATOM 1948 C GLN A 269 11.257 -18.185 -0.545 1.00 19.59 C ANISOU 1948 C GLN A 269 2191 2563 2689 280 138 176 C ATOM 1949 O GLN A 269 10.191 -17.922 0.027 1.00 20.45 O ANISOU 1949 O GLN A 269 2275 2698 2799 332 168 200 O ATOM 1950 CB GLN A 269 11.397 -20.300 -1.902 1.00 18.45 C ANISOU 1950 CB GLN A 269 1979 2474 2559 179 81 192 C ATOM 1951 CG GLN A 269 11.276 -20.945 -3.272 1.00 23.30 C ANISOU 1951 CG GLN A 269 2562 3110 3181 135 44 212 C ATOM 1952 CD GLN A 269 11.107 -22.448 -3.214 1.00 25.30 C ANISOU 1952 CD GLN A 269 2782 3396 3433 87 27 218 C ATOM 1953 NE2 GLN A 269 10.986 -22.983 -2.021 1.00 19.30 N ANISOU 1953 NE2 GLN A 269 2018 2648 2668 91 47 211 N ATOM 1954 OE1 GLN A 269 11.074 -23.114 -4.245 1.00 28.98 O ANISOU 1954 OE1 GLN A 269 3232 3876 3901 45 -4 229 O ATOM 1955 N MET A 270 12.440 -17.937 0.018 1.00 20.17 N ANISOU 1955 N MET A 270 2324 2592 2748 263 138 134 N ATOM 1956 CA MET A 270 12.508 -17.354 1.354 1.00 18.43 C ANISOU 1956 CA MET A 270 2148 2346 2509 302 171 113 C ATOM 1957 C MET A 270 12.152 -15.868 1.313 1.00 20.95 C ANISOU 1957 C MET A 270 2509 2627 2823 362 192 118 C ATOM 1958 O MET A 270 11.628 -15.322 2.292 1.00 21.71 O ANISOU 1958 O MET A 270 2628 2715 2906 417 229 116 O ATOM 1959 CB MET A 270 13.912 -17.534 1.928 1.00 19.36 C ANISOU 1959 CB MET A 270 2317 2428 2612 259 159 69 C ATOM 1960 CG MET A 270 14.278 -19.002 2.083 1.00 18.11 C ANISOU 1960 CG MET A 270 2123 2302 2456 209 141 65 C ATOM 1961 SD MET A 270 13.177 -20.019 3.069 1.00 21.01 S ANISOU 1961 SD MET A 270 2442 2721 2821 225 166 86 S ATOM 1962 CE MET A 270 14.046 -21.592 3.014 1.00 17.24 C ANISOU 1962 CE MET A 270 1949 2259 2345 156 134 72 C ATOM 1963 N GLN A 271 12.466 -15.183 0.207 1.00 18.75 N ANISOU 1963 N GLN A 271 2249 2324 2554 354 171 122 N ATOM 1964 CA GLN A 271 12.070 -13.780 0.084 1.00 22.91 C ANISOU 1964 CA GLN A 271 2818 2811 3076 413 189 131 C ATOM 1965 C GLN A 271 10.551 -13.665 -0.011 1.00 22.15 C ANISOU 1965 C GLN A 271 2666 2759 2991 477 213 176 C ATOM 1966 O GLN A 271 9.950 -12.786 0.614 1.00 24.93 O ANISOU 1966 O GLN A 271 3046 3092 3333 548 249 181 O ATOM 1967 CB GLN A 271 12.769 -13.153 -1.126 1.00 17.14 C ANISOU 1967 CB GLN A 271 2116 2045 2350 383 158 129 C ATOM 1968 CG GLN A 271 14.308 -13.102 -1.003 1.00 24.57 C ANISOU 1968 CG GLN A 271 3112 2944 3278 322 137 87 C ATOM 1969 CD GLN A 271 15.017 -12.687 -2.301 1.00 25.56 C ANISOU 1969 CD GLN A 271 3254 3048 3410 282 106 90 C ATOM 1970 NE2 GLN A 271 16.118 -11.944 -2.174 1.00 23.06 N ANISOU 1970 NE2 GLN A 271 3004 2678 3078 255 98 63 N ATOM 1971 OE1 GLN A 271 14.594 -13.060 -3.394 1.00 24.57 O ANISOU 1971 OE1 GLN A 271 3082 2955 3301 272 89 118 O ATOM 1972 N ALA A 272 9.910 -14.572 -0.758 1.00 23.44 N ANISOU 1972 N ALA A 272 2751 2982 3174 454 194 210 N ATOM 1973 CA ALA A 272 8.450 -14.586 -0.808 1.00 23.90 C ANISOU 1973 CA ALA A 272 2743 3094 3243 509 214 259 C ATOM 1974 C ALA A 272 7.858 -14.888 0.562 1.00 26.45 C ANISOU 1974 C ALA A 272 3050 3443 3555 547 256 259 C ATOM 1975 O ALA A 272 6.863 -14.272 0.965 1.00 26.54 O ANISOU 1975 O ALA A 272 3047 3470 3565 622 293 285 O ATOM 1976 CB ALA A 272 7.962 -15.606 -1.835 1.00 24.17 C ANISOU 1976 CB ALA A 272 2699 3188 3297 462 179 294 C ATOM 1977 N ALA A 273 8.463 -15.827 1.295 1.00 22.59 N ANISOU 1977 N ALA A 273 2567 2960 3057 499 253 231 N ATOM 1978 CA ALA A 273 8.007 -16.118 2.652 1.00 24.68 C ANISOU 1978 CA ALA A 273 2825 3245 3306 530 293 228 C ATOM 1979 C ALA A 273 8.138 -14.895 3.560 1.00 25.84 C ANISOU 1979 C ALA A 273 3049 3338 3430 596 333 203 C ATOM 1980 O ALA A 273 7.256 -14.636 4.387 1.00 27.84 O ANISOU 1980 O ALA A 273 3292 3614 3673 661 378 219 O ATOM 1981 CB ALA A 273 8.783 -17.305 3.238 1.00 22.21 C ANISOU 1981 CB ALA A 273 2514 2939 2985 463 278 201 C ATOM 1982 N ALA A 274 9.233 -14.140 3.438 1.00 24.34 N ANISOU 1982 N ALA A 274 2941 3079 3229 579 317 165 N ATOM 1983 CA ALA A 274 9.380 -12.949 4.270 1.00 26.27 C ANISOU 1983 CA ALA A 274 3271 3265 3447 637 351 139 C ATOM 1984 C ALA A 274 8.284 -11.948 3.950 1.00 28.93 C ANISOU 1984 C ALA A 274 3600 3602 3789 724 381 174 C ATOM 1985 O ALA A 274 7.641 -11.389 4.851 1.00 26.84 O ANISOU 1985 O ALA A 274 3361 3332 3506 799 429 176 O ATOM 1986 CB ALA A 274 10.758 -12.319 4.058 1.00 24.77 C ANISOU 1986 CB ALA A 274 3165 3001 3244 592 322 97 C ATOM 1987 N GLU A 275 8.036 -11.755 2.656 1.00 26.76 N ANISOU 1987 N GLU A 275 3291 3337 3538 719 353 203 N ATOM 1988 CA GLU A 275 7.019 -10.825 2.186 1.00 30.57 C ANISOU 1988 CA GLU A 275 3761 3823 4030 800 374 242 C ATOM 1989 C GLU A 275 5.643 -11.209 2.712 1.00 31.96 C ANISOU 1989 C GLU A 275 3859 4073 4212 862 414 284 C ATOM 1990 O GLU A 275 4.881 -10.354 3.179 1.00 29.77 O ANISOU 1990 O GLU A 275 3599 3788 3924 955 459 299 O ATOM 1991 CB GLU A 275 7.051 -10.845 0.665 1.00 33.03 C ANISOU 1991 CB GLU A 275 4037 4145 4367 765 328 269 C ATOM 1992 CG GLU A 275 8.046 -9.854 0.092 1.00 40.62 C ANISOU 1992 CG GLU A 275 5087 5026 5320 747 305 241 C ATOM 1993 CD GLU A 275 7.702 -9.418 -1.307 1.00 55.51 C ANISOU 1993 CD GLU A 275 6949 6917 7227 753 277 278 C ATOM 1994 OE1 GLU A 275 8.377 -8.499 -1.822 1.00 61.49 O ANISOU 1994 OE1 GLU A 275 7778 7608 7976 746 262 263 O ATOM 1995 OE2 GLU A 275 6.772 -10.010 -1.902 1.00 62.90 O1- ANISOU 1995 OE2 GLU A 275 7794 7923 8183 759 269 324 O1- ATOM 1996 N GLU A 276 5.323 -12.501 2.675 1.00 30.36 N ANISOU 1996 N GLU A 276 3571 3942 4023 812 400 304 N ATOM 1997 CA GLU A 276 4.008 -12.968 3.085 1.00 29.95 C ANISOU 1997 CA GLU A 276 3432 3970 3978 857 434 351 C ATOM 1998 C GLU A 276 3.805 -12.869 4.587 1.00 30.42 C ANISOU 1998 C GLU A 276 3522 4027 4009 907 490 333 C ATOM 1999 O GLU A 276 2.661 -12.946 5.049 1.00 33.01 O ANISOU 1999 O GLU A 276 3790 4415 4338 967 531 372 O ATOM 2000 CB GLU A 276 3.825 -14.407 2.620 1.00 30.30 C ANISOU 2000 CB GLU A 276 3388 4084 4041 777 398 375 C ATOM 2001 CG GLU A 276 3.769 -14.506 1.104 1.00 33.32 C ANISOU 2001 CG GLU A 276 3732 4480 4449 738 346 403 C ATOM 2002 CD GLU A 276 3.824 -15.937 0.592 1.00 37.54 C ANISOU 2002 CD GLU A 276 4201 5065 4996 647 304 415 C ATOM 2003 OE1 GLU A 276 3.739 -16.874 1.416 1.00 36.52 O ANISOU 2003 OE1 GLU A 276 4048 4968 4860 618 316 411 O ATOM 2004 OE2 GLU A 276 4.008 -16.120 -0.636 1.00 40.67 O1- ANISOU 2004 OE2 GLU A 276 4581 5463 5406 601 258 427 O1- ATOM 2005 N ASN A 277 4.879 -12.677 5.354 1.00 31.49 N ANISOU 2005 N ASN A 277 3750 4097 4119 883 493 276 N ATOM 2006 CA ASN A 277 4.846 -12.789 6.811 1.00 30.79 C ANISOU 2006 CA ASN A 277 3695 4007 3999 911 538 253 C ATOM 2007 C ASN A 277 5.371 -11.528 7.491 1.00 33.67 C ANISOU 2007 C ASN A 277 4180 4285 4330 964 566 210 C ATOM 2008 O ASN A 277 5.880 -11.582 8.613 1.00 35.91 O ANISOU 2008 O ASN A 277 4524 4540 4581 958 585 171 O ATOM 2009 CB ASN A 277 5.637 -14.015 7.264 1.00 26.81 C ANISOU 2009 CB ASN A 277 3183 3515 3489 820 512 226 C ATOM 2010 CG ASN A 277 4.902 -15.308 6.974 1.00 27.08 C ANISOU 2010 CG ASN A 277 3107 3637 3546 781 499 270 C ATOM 2011 ND2 ASN A 277 5.201 -15.914 5.835 1.00 29.97 N ANISOU 2011 ND2 ASN A 277 3432 4017 3939 713 446 281 N ATOM 2012 OD1 ASN A 277 4.051 -15.736 7.741 1.00 29.02 O ANISOU 2012 OD1 ASN A 277 3305 3938 3784 810 538 296 O ATOM 2013 N GLY A 278 5.265 -10.386 6.820 1.00 32.60 N ANISOU 2013 N GLY A 278 4084 4103 4198 1013 566 216 N ATOM 2014 CA GLY A 278 5.612 -9.128 7.452 1.00 37.36 C ANISOU 2014 CA GLY A 278 4806 4622 4768 1071 595 180 C ATOM 2015 C GLY A 278 7.081 -8.914 7.735 1.00 34.29 C ANISOU 2015 C GLY A 278 4518 4155 4356 1001 562 120 C ATOM 2016 O GLY A 278 7.424 -8.045 8.540 1.00 31.74 O ANISOU 2016 O GLY A 278 4300 3763 3996 1036 586 85 O ATOM 2017 N ALA A 279 7.963 -9.675 7.102 1.00 29.87 N ANISOU 2017 N ALA A 279 3931 3602 3815 902 507 110 N ATOM 2018 CA ALA A 279 9.398 -9.488 7.260 1.00 30.50 C ANISOU 2018 CA ALA A 279 4095 3617 3877 831 471 60 C ATOM 2019 C ALA A 279 9.985 -8.946 5.964 1.00 30.69 C ANISOU 2019 C ALA A 279 4136 3602 3921 795 427 63 C ATOM 2020 O ALA A 279 9.355 -8.976 4.901 1.00 32.32 O ANISOU 2020 O ALA A 279 4280 3843 4158 810 416 102 O ATOM 2021 CB ALA A 279 10.092 -10.799 7.665 1.00 28.77 C ANISOU 2021 CB ALA A 279 3838 3434 3660 748 445 43 C ATOM 2022 N SER A 280 11.199 -8.434 6.065 1.00 29.99 N ANISOU 2022 N SER A 280 4135 3446 3814 745 400 22 N ATOM 2023 CA SER A 280 11.834 -7.866 4.882 1.00 27.67 C ANISOU 2023 CA SER A 280 3864 3114 3535 707 360 24 C ATOM 2024 C SER A 280 12.537 -8.956 4.090 1.00 31.34 C ANISOU 2024 C SER A 280 4260 3622 4026 617 314 28 C ATOM 2025 O SER A 280 13.309 -9.736 4.665 1.00 28.55 O ANISOU 2025 O SER A 280 3903 3280 3664 559 299 2 O ATOM 2026 CB SER A 280 12.841 -6.792 5.263 1.00 29.78 C ANISOU 2026 CB SER A 280 4254 3290 3770 687 350 -17 C ATOM 2027 OG SER A 280 13.312 -6.136 4.094 1.00 36.65 O ANISOU 2027 OG SER A 280 5148 4123 4655 659 317 -8 O ATOM 2028 N PRO A 281 12.310 -9.038 2.782 1.00 29.50 N ANISOU 2028 N PRO A 281 3975 3411 3822 604 289 59 N ATOM 2029 CA PRO A 281 13.089 -9.983 1.971 1.00 28.68 C ANISOU 2029 CA PRO A 281 3821 3338 3737 519 246 58 C ATOM 2030 C PRO A 281 14.583 -9.683 1.954 1.00 29.89 C ANISOU 2030 C PRO A 281 4040 3441 3877 449 215 21 C ATOM 2031 O PRO A 281 15.372 -10.582 1.630 1.00 25.70 O ANISOU 2031 O PRO A 281 3473 2936 3355 380 185 12 O ATOM 2032 CB PRO A 281 12.466 -9.849 0.576 1.00 28.83 C ANISOU 2032 CB PRO A 281 3790 3380 3783 531 230 99 C ATOM 2033 CG PRO A 281 11.823 -8.470 0.585 1.00 32.73 C ANISOU 2033 CG PRO A 281 4341 3827 4268 611 256 111 C ATOM 2034 CD PRO A 281 11.321 -8.290 1.989 1.00 31.37 C ANISOU 2034 CD PRO A 281 4199 3648 4074 670 302 97 C ATOM 2035 N GLU A 282 15.001 -8.460 2.304 1.00 25.49 N ANISOU 2035 N GLU A 282 3579 2811 3296 464 221 0 N ATOM 2036 CA GLU A 282 16.428 -8.161 2.401 1.00 27.11 C ANISOU 2036 CA GLU A 282 3846 2971 3485 392 190 -34 C ATOM 2037 C GLU A 282 17.145 -9.017 3.446 1.00 27.42 C ANISOU 2037 C GLU A 282 3880 3030 3510 347 185 -63 C ATOM 2038 O GLU A 282 18.381 -9.112 3.415 1.00 24.07 O ANISOU 2038 O GLU A 282 3477 2591 3078 277 153 -84 O ATOM 2039 CB GLU A 282 16.630 -6.674 2.717 1.00 29.04 C ANISOU 2039 CB GLU A 282 4203 3131 3702 417 198 -50 C ATOM 2040 CG GLU A 282 17.830 -6.020 2.043 1.00 34.11 C ANISOU 2040 CG GLU A 282 4897 3725 4338 347 160 -61 C ATOM 2041 CD GLU A 282 17.611 -5.683 0.576 1.00 40.32 C ANISOU 2041 CD GLU A 282 5657 4514 5148 347 144 -29 C ATOM 2042 OE1 GLU A 282 16.765 -6.341 -0.088 1.00 40.39 O ANISOU 2042 OE1 GLU A 282 5583 4580 5184 375 150 2 O ATOM 2043 OE2 GLU A 282 18.301 -4.762 0.075 1.00 36.82 O1- ANISOU 2043 OE2 GLU A 282 5279 4016 4695 313 124 -33 O1- ATOM 2044 N ASP A 283 16.407 -9.624 4.379 1.00 26.13 N ANISOU 2044 N ASP A 283 3688 2899 3340 388 215 -62 N ATOM 2045 CA ASP A 283 17.032 -10.434 5.415 1.00 26.49 C ANISOU 2045 CA ASP A 283 3732 2963 3370 350 210 -88 C ATOM 2046 C ASP A 283 17.609 -11.732 4.869 1.00 20.38 C ANISOU 2046 C ASP A 283 2881 2243 2619 286 180 -82 C ATOM 2047 O ASP A 283 18.367 -12.399 5.573 1.00 21.76 O ANISOU 2047 O ASP A 283 3055 2429 2782 245 167 -102 O ATOM 2048 CB ASP A 283 16.014 -10.754 6.506 1.00 26.70 C ANISOU 2048 CB ASP A 283 3747 3014 3382 411 253 -85 C ATOM 2049 CG ASP A 283 15.607 -9.533 7.307 1.00 26.85 C ANISOU 2049 CG ASP A 283 3859 2975 3369 474 288 -99 C ATOM 2050 OD1 ASP A 283 16.180 -8.441 7.097 1.00 29.23 O ANISOU 2050 OD1 ASP A 283 4241 3211 3656 464 274 -115 O ATOM 2051 OD2 ASP A 283 14.687 -9.669 8.141 1.00 27.07 O1- ANISOU 2051 OD2 ASP A 283 3879 3022 3383 535 330 -94 O1- ATOM 2052 N VAL A 284 17.268 -12.102 3.640 1.00 22.39 N ANISOU 2052 N VAL A 284 3074 2531 2905 280 167 -54 N ATOM 2053 CA VAL A 284 17.636 -13.398 3.079 1.00 22.54 C ANISOU 2053 CA VAL A 284 3020 2601 2944 231 143 -46 C ATOM 2054 C VAL A 284 19.031 -13.276 2.473 1.00 21.61 C ANISOU 2054 C VAL A 284 2922 2463 2826 164 107 -62 C ATOM 2055 O VAL A 284 19.206 -12.669 1.416 1.00 21.02 O ANISOU 2055 O VAL A 284 2855 2371 2761 153 94 -51 O ATOM 2056 CB VAL A 284 16.612 -13.865 2.037 1.00 21.46 C ANISOU 2056 CB VAL A 284 2811 2508 2834 252 145 -8 C ATOM 2057 CG1 VAL A 284 17.053 -15.176 1.397 1.00 21.21 C ANISOU 2057 CG1 VAL A 284 2718 2520 2819 198 118 -3 C ATOM 2058 CG2 VAL A 284 15.247 -14.015 2.679 1.00 19.82 C ANISOU 2058 CG2 VAL A 284 2576 2330 2627 315 181 12 C ATOM 2059 N GLY A 285 20.033 -13.828 3.158 1.00 20.52 N ANISOU 2059 N GLY A 285 2792 2330 2677 120 92 -85 N ATOM 2060 CA GLY A 285 21.397 -13.822 2.685 1.00 21.30 C ANISOU 2060 CA GLY A 285 2899 2420 2775 56 60 -97 C ATOM 2061 C GLY A 285 21.834 -15.189 2.178 1.00 19.34 C ANISOU 2061 C GLY A 285 2581 2222 2545 21 43 -91 C ATOM 2062 O GLY A 285 21.191 -16.209 2.416 1.00 18.93 O ANISOU 2062 O GLY A 285 2484 2208 2501 38 53 -83 O ATOM 2063 N PHE A 286 22.960 -15.190 1.465 1.00 18.68 N ANISOU 2063 N PHE A 286 2493 2139 2465 -29 18 -95 N ATOM 2064 CA PHE A 286 23.512 -16.401 0.861 1.00 18.40 C ANISOU 2064 CA PHE A 286 2401 2147 2444 -61 2 -90 C ATOM 2065 C PHE A 286 25.024 -16.370 1.035 1.00 19.60 C ANISOU 2065 C PHE A 286 2564 2297 2586 -112 -20 -106 C ATOM 2066 O PHE A 286 25.677 -15.433 0.565 1.00 21.05 O ANISOU 2066 O PHE A 286 2778 2456 2765 -139 -32 -106 O ATOM 2067 CB PHE A 286 23.127 -16.494 -0.627 1.00 18.13 C ANISOU 2067 CB PHE A 286 2334 2127 2428 -60 -1 -68 C ATOM 2068 CG PHE A 286 23.303 -17.868 -1.232 1.00 16.39 C ANISOU 2068 CG PHE A 286 2058 1951 2220 -78 -10 -62 C ATOM 2069 CD1 PHE A 286 22.371 -18.868 -0.996 1.00 16.34 C ANISOU 2069 CD1 PHE A 286 2017 1972 2221 -55 -1 -53 C ATOM 2070 CD2 PHE A 286 24.395 -18.153 -2.045 1.00 18.14 C ANISOU 2070 CD2 PHE A 286 2265 2184 2443 -117 -26 -64 C ATOM 2071 CE1 PHE A 286 22.516 -20.143 -1.569 1.00 17.62 C ANISOU 2071 CE1 PHE A 286 2138 2167 2391 -72 -11 -48 C ATOM 2072 CE2 PHE A 286 24.566 -19.424 -2.617 1.00 17.87 C ANISOU 2072 CE2 PHE A 286 2188 2185 2416 -128 -32 -60 C ATOM 2073 CZ PHE A 286 23.623 -20.426 -2.376 1.00 16.95 C ANISOU 2073 CZ PHE A 286 2045 2090 2307 -106 -25 -53 C ATOM 2074 N MET A 287 25.586 -17.371 1.722 1.00 17.63 N ANISOU 2074 N MET A 287 2291 2073 2333 -127 -27 -115 N ATOM 2075 CA MET A 287 27.023 -17.427 1.959 1.00 17.41 C ANISOU 2075 CA MET A 287 2265 2053 2297 -173 -50 -126 C ATOM 2076 C MET A 287 27.640 -18.670 1.324 1.00 18.10 C ANISOU 2076 C MET A 287 2295 2184 2398 -189 -59 -119 C ATOM 2077 O MET A 287 26.979 -19.698 1.120 1.00 16.71 O ANISOU 2077 O MET A 287 2085 2030 2232 -166 -50 -113 O ATOM 2078 CB MET A 287 27.351 -17.411 3.466 1.00 18.64 C ANISOU 2078 CB MET A 287 2452 2199 2431 -177 -55 -144 C ATOM 2079 CG MET A 287 27.144 -18.778 4.153 1.00 21.12 C ANISOU 2079 CG MET A 287 2731 2547 2748 -161 -51 -145 C ATOM 2080 SD MET A 287 27.720 -18.881 5.867 1.00 24.01 S ANISOU 2080 SD MET A 287 3130 2908 3086 -173 -62 -163 S ATOM 2081 CE MET A 287 26.353 -18.116 6.745 1.00 18.41 C ANISOU 2081 CE MET A 287 2475 2163 2358 -127 -32 -171 C ATOM 2082 N ALA A 288 28.943 -18.584 1.058 1.00 18.82 N ANISOU 2082 N ALA A 288 2377 2287 2487 -229 -77 -121 N ATOM 2083 CA ALA A 288 29.694 -19.749 0.611 1.00 17.27 C ANISOU 2083 CA ALA A 288 2130 2132 2299 -239 -84 -116 C ATOM 2084 C ALA A 288 29.861 -20.767 1.744 1.00 16.49 C ANISOU 2084 C ALA A 288 2020 2052 2196 -229 -88 -124 C ATOM 2085 O ALA A 288 29.824 -20.434 2.936 1.00 15.29 O ANISOU 2085 O ALA A 288 1898 1884 2028 -229 -92 -135 O ATOM 2086 CB ALA A 288 31.077 -19.324 0.106 1.00 15.53 C ANISOU 2086 CB ALA A 288 1899 1926 2077 -283 -99 -112 C ATOM 2087 N PHE A 289 30.098 -22.019 1.363 1.00 17.64 N ANISOU 2087 N PHE A 289 2124 2227 2350 -220 -87 -119 N ATOM 2088 CA PHE A 289 30.332 -23.049 2.363 1.00 14.86 C ANISOU 2088 CA PHE A 289 1761 1892 1993 -210 -93 -124 C ATOM 2089 C PHE A 289 31.540 -22.655 3.211 1.00 15.93 C ANISOU 2089 C PHE A 289 1903 2034 2115 -240 -113 -129 C ATOM 2090 O PHE A 289 32.507 -22.091 2.686 1.00 16.60 O ANISOU 2090 O PHE A 289 1978 2130 2200 -270 -125 -124 O ATOM 2091 CB PHE A 289 30.552 -24.406 1.683 1.00 16.68 C ANISOU 2091 CB PHE A 289 1953 2150 2234 -197 -90 -117 C ATOM 2092 CG PHE A 289 30.660 -25.561 2.636 1.00 17.73 C ANISOU 2092 CG PHE A 289 2078 2295 2362 -182 -95 -120 C ATOM 2093 CD1 PHE A 289 31.869 -25.871 3.251 1.00 16.72 C ANISOU 2093 CD1 PHE A 289 1938 2188 2228 -193 -111 -120 C ATOM 2094 CD2 PHE A 289 29.553 -26.343 2.916 1.00 15.00 C ANISOU 2094 CD2 PHE A 289 1738 1943 2018 -159 -84 -118 C ATOM 2095 CE1 PHE A 289 31.951 -26.947 4.135 1.00 16.85 C ANISOU 2095 CE1 PHE A 289 1949 2213 2238 -177 -117 -120 C ATOM 2096 CE2 PHE A 289 29.634 -27.415 3.788 1.00 15.61 C ANISOU 2096 CE2 PHE A 289 1813 2029 2090 -147 -89 -118 C ATOM 2097 CZ PHE A 289 30.839 -27.713 4.399 1.00 18.35 C ANISOU 2097 CZ PHE A 289 2150 2392 2429 -154 -105 -120 C ATOM 2098 N PRO A 290 31.508 -22.884 4.532 1.00 15.98 N ANISOU 2098 N PRO A 290 1928 2038 2108 -235 -121 -137 N ATOM 2099 CA PRO A 290 32.621 -22.414 5.365 1.00 17.32 C ANISOU 2099 CA PRO A 290 2107 2213 2261 -269 -145 -141 C ATOM 2100 C PRO A 290 33.872 -23.260 5.197 1.00 19.13 C ANISOU 2100 C PRO A 290 2288 2485 2495 -279 -162 -130 C ATOM 2101 O PRO A 290 34.204 -24.069 6.068 1.00 17.36 O ANISOU 2101 O PRO A 290 2054 2278 2264 -271 -173 -129 O ATOM 2102 CB PRO A 290 32.047 -22.500 6.782 1.00 18.26 C ANISOU 2102 CB PRO A 290 2262 2316 2360 -255 -145 -152 C ATOM 2103 CG PRO A 290 31.047 -23.631 6.693 1.00 16.17 C ANISOU 2103 CG PRO A 290 1981 2057 2107 -215 -125 -148 C ATOM 2104 CD PRO A 290 30.430 -23.487 5.339 1.00 17.79 C ANISOU 2104 CD PRO A 290 2171 2258 2332 -204 -107 -141 C ATOM 2105 N ALA A 291 34.565 -23.076 4.069 1.00 17.55 N ANISOU 2105 N ALA A 291 2056 2304 2306 -295 -162 -120 N ATOM 2106 CA ALA A 291 35.869 -23.689 3.818 1.00 17.96 C ANISOU 2106 CA ALA A 291 2059 2401 2363 -305 -174 -106 C ATOM 2107 C ALA A 291 36.659 -22.742 2.935 1.00 18.85 C ANISOU 2107 C ALA A 291 2158 2527 2479 -344 -179 -96 C ATOM 2108 O ALA A 291 36.113 -21.772 2.399 1.00 19.46 O ANISOU 2108 O ALA A 291 2264 2573 2556 -357 -171 -100 O ATOM 2109 CB ALA A 291 35.743 -25.060 3.158 1.00 16.51 C ANISOU 2109 CB ALA A 291 1842 2238 2194 -264 -158 -101 C ATOM 2110 N ASN A 292 37.955 -23.022 2.784 1.00 17.74 N ANISOU 2110 N ASN A 292 1969 2431 2340 -361 -192 -81 N ATOM 2111 CA ASN A 292 38.815 -22.182 1.953 1.00 19.98 C ANISOU 2111 CA ASN A 292 2232 2735 2624 -402 -196 -66 C ATOM 2112 C ASN A 292 40.068 -22.955 1.560 1.00 24.05 C ANISOU 2112 C ASN A 292 2679 3312 3146 -397 -198 -46 C ATOM 2113 O ASN A 292 40.512 -23.853 2.283 1.00 21.85 O ANISOU 2113 O ASN A 292 2376 3059 2867 -376 -208 -42 O ATOM 2114 CB ASN A 292 39.196 -20.878 2.670 1.00 19.37 C ANISOU 2114 CB ASN A 292 2189 2641 2531 -460 -225 -67 C ATOM 2115 CG ASN A 292 40.231 -21.088 3.769 1.00 21.38 C ANISOU 2115 CG ASN A 292 2421 2929 2773 -485 -257 -58 C ATOM 2116 ND2 ASN A 292 39.754 -21.232 4.999 1.00 17.97 N ANISOU 2116 ND2 ASN A 292 2027 2473 2328 -475 -269 -73 N ATOM 2117 OD1 ASN A 292 41.440 -21.093 3.522 1.00 21.68 O ANISOU 2117 OD1 ASN A 292 2407 3017 2813 -514 -271 -36 O ATOM 2118 N VAL A 293 40.633 -22.599 0.407 1.00 21.35 N ANISOU 2118 N VAL A 293 2307 2994 2809 -415 -186 -31 N ATOM 2119 CA VAL A 293 41.901 -23.161 -0.046 1.00 22.92 C ANISOU 2119 CA VAL A 293 2438 3258 3014 -412 -183 -8 C ATOM 2120 C VAL A 293 42.940 -22.049 0.038 1.00 27.47 C ANISOU 2120 C VAL A 293 2994 3861 3582 -480 -207 13 C ATOM 2121 O VAL A 293 42.925 -21.117 -0.773 1.00 27.23 O ANISOU 2121 O VAL A 293 2976 3821 3550 -516 -201 18 O ATOM 2122 CB VAL A 293 41.811 -23.733 -1.471 1.00 25.77 C ANISOU 2122 CB VAL A 293 2776 3632 3383 -377 -147 -4 C ATOM 2123 CG1 VAL A 293 43.130 -24.381 -1.856 1.00 29.16 C ANISOU 2123 CG1 VAL A 293 3135 4131 3815 -363 -139 21 C ATOM 2124 CG2 VAL A 293 40.678 -24.743 -1.600 1.00 22.17 C ANISOU 2124 CG2 VAL A 293 2349 3142 2931 -320 -127 -24 C ATOM 2125 N ASP A 294 43.840 -22.135 1.019 1.00 25.50 N ANISOU 2125 N ASP A 294 2716 3647 3325 -503 -237 26 N ATOM 2126 CA ASP A 294 44.910 -21.152 1.183 1.00 27.94 C ANISOU 2126 CA ASP A 294 3001 3989 3625 -575 -266 49 C ATOM 2127 C ASP A 294 44.368 -19.730 1.258 1.00 26.85 C ANISOU 2127 C ASP A 294 2933 3795 3476 -632 -281 37 C ATOM 2128 O ASP A 294 44.978 -18.789 0.745 1.00 24.52 O ANISOU 2128 O ASP A 294 2629 3512 3175 -691 -290 55 O ATOM 2129 CB ASP A 294 45.947 -21.251 0.061 1.00 32.84 C ANISOU 2129 CB ASP A 294 3549 4675 4254 -583 -249 80 C ATOM 2130 CG ASP A 294 46.749 -22.541 0.100 1.00 42.13 C ANISOU 2130 CG ASP A 294 4653 5916 5440 -531 -239 98 C ATOM 2131 OD1 ASP A 294 47.093 -23.058 -0.992 1.00 49.57 O ANISOU 2131 OD1 ASP A 294 5551 6894 6390 -497 -204 110 O ATOM 2132 OD2 ASP A 294 47.050 -23.028 1.215 1.00 47.72 O1- ANISOU 2132 OD2 ASP A 294 5349 6638 6144 -522 -265 100 O1- ATOM 2133 N GLY A 295 43.221 -19.565 1.908 1.00 23.05 N ANISOU 2133 N GLY A 295 2521 3248 2988 -614 -282 8 N ATOM 2134 CA GLY A 295 42.651 -18.256 2.109 1.00 22.71 C ANISOU 2134 CA GLY A 295 2553 3146 2931 -657 -294 -6 C ATOM 2135 C GLY A 295 41.651 -17.824 1.062 1.00 21.18 C ANISOU 2135 C GLY A 295 2396 2907 2745 -637 -263 -16 C ATOM 2136 O GLY A 295 41.027 -16.775 1.234 1.00 23.15 O ANISOU 2136 O GLY A 295 2714 3100 2984 -660 -269 -29 O ATOM 2137 N GLN A 296 41.488 -18.588 -0.023 1.00 20.42 N ANISOU 2137 N GLN A 296 2260 2834 2666 -594 -231 -11 N ATOM 2138 CA GLN A 296 40.534 -18.280 -1.089 1.00 22.55 C ANISOU 2138 CA GLN A 296 2559 3067 2941 -573 -203 -18 C ATOM 2139 C GLN A 296 39.329 -19.200 -0.954 1.00 18.42 C ANISOU 2139 C GLN A 296 2053 2518 2428 -506 -182 -39 C ATOM 2140 O GLN A 296 39.489 -20.419 -0.960 1.00 18.83 O ANISOU 2140 O GLN A 296 2065 2603 2488 -466 -172 -38 O ATOM 2141 CB GLN A 296 41.164 -18.472 -2.466 1.00 20.85 C ANISOU 2141 CB GLN A 296 2293 2895 2734 -576 -182 3 C ATOM 2142 CG GLN A 296 40.220 -18.159 -3.626 1.00 19.87 C ANISOU 2142 CG GLN A 296 2200 2737 2615 -557 -157 -1 C ATOM 2143 CD GLN A 296 39.728 -16.722 -3.621 1.00 22.61 C ANISOU 2143 CD GLN A 296 2611 3028 2952 -598 -169 -4 C ATOM 2144 NE2 GLN A 296 38.423 -16.537 -3.488 1.00 21.40 N ANISOU 2144 NE2 GLN A 296 2511 2820 2801 -564 -161 -23 N ATOM 2145 OE1 GLN A 296 40.519 -15.787 -3.746 1.00 20.69 O ANISOU 2145 OE1 GLN A 296 2370 2791 2699 -658 -185 12 O ATOM 2146 N GLN A 297 38.135 -18.621 -0.854 1.00 19.15 N ANISOU 2146 N GLN A 297 2204 2553 2517 -493 -176 -55 N ATOM 2147 CA GLN A 297 36.894 -19.382 -0.796 1.00 20.28 C ANISOU 2147 CA GLN A 297 2363 2674 2669 -436 -157 -70 C ATOM 2148 C GLN A 297 36.319 -19.593 -2.185 1.00 21.19 C ANISOU 2148 C GLN A 297 2468 2787 2794 -413 -132 -65 C ATOM 2149 O GLN A 297 36.400 -18.712 -3.050 1.00 22.38 O ANISOU 2149 O GLN A 297 2631 2928 2943 -439 -129 -55 O ATOM 2150 CB GLN A 297 35.824 -18.666 0.014 1.00 20.83 C ANISOU 2150 CB GLN A 297 2496 2688 2730 -429 -160 -87 C ATOM 2151 CG GLN A 297 35.847 -18.827 1.498 1.00 23.30 C ANISOU 2151 CG GLN A 297 2829 2993 3030 -428 -176 -99 C ATOM 2152 CD GLN A 297 34.517 -18.405 2.089 1.00 21.46 C ANISOU 2152 CD GLN A 297 2654 2709 2791 -399 -166 -116 C ATOM 2153 NE2 GLN A 297 33.765 -19.369 2.618 1.00 20.44 N ANISOU 2153 NE2 GLN A 297 2518 2583 2666 -356 -154 -124 N ATOM 2154 OE1 GLN A 297 34.172 -17.221 2.079 1.00 18.96 O ANISOU 2154 OE1 GLN A 297 2389 2352 2465 -415 -167 -120 O ATOM 2155 N TYR A 298 35.676 -20.743 -2.369 1.00 19.50 N ANISOU 2155 N TYR A 298 2240 2580 2589 -366 -116 -71 N ATOM 2156 CA TYR A 298 35.012 -21.074 -3.617 1.00 19.46 C ANISOU 2156 CA TYR A 298 2231 2572 2590 -343 -96 -68 C ATOM 2157 C TYR A 298 33.573 -21.470 -3.363 1.00 20.77 C ANISOU 2157 C TYR A 298 2423 2707 2761 -306 -88 -78 C ATOM 2158 O TYR A 298 33.220 -21.950 -2.282 1.00 19.43 O ANISOU 2158 O TYR A 298 2261 2531 2591 -288 -93 -88 O ATOM 2159 CB TYR A 298 35.720 -22.200 -4.348 1.00 16.01 C ANISOU 2159 CB TYR A 298 1749 2178 2156 -325 -84 -61 C ATOM 2160 CG TYR A 298 37.139 -21.844 -4.716 1.00 20.55 C ANISOU 2160 CG TYR A 298 2289 2794 2727 -359 -86 -45 C ATOM 2161 CD1 TYR A 298 38.159 -21.950 -3.788 1.00 22.05 C ANISOU 2161 CD1 TYR A 298 2452 3012 2915 -375 -103 -40 C ATOM 2162 CD2 TYR A 298 37.458 -21.403 -5.990 1.00 18.97 C ANISOU 2162 CD2 TYR A 298 2078 2605 2523 -376 -73 -32 C ATOM 2163 CE1 TYR A 298 39.450 -21.638 -4.110 1.00 21.71 C ANISOU 2163 CE1 TYR A 298 2369 3013 2869 -407 -107 -21 C ATOM 2164 CE2 TYR A 298 38.761 -21.076 -6.326 1.00 24.40 C ANISOU 2164 CE2 TYR A 298 2729 3336 3207 -408 -74 -13 C ATOM 2165 CZ TYR A 298 39.750 -21.198 -5.372 1.00 23.64 C ANISOU 2165 CZ TYR A 298 2601 3271 3110 -424 -91 -7 C ATOM 2166 OH TYR A 298 41.048 -20.881 -5.659 1.00 22.91 O ANISOU 2166 OH TYR A 298 2463 3229 3014 -459 -93 16 O ATOM 2167 N ALA A 299 32.750 -21.280 -4.387 1.00 17.95 N ANISOU 2167 N ALA A 299 2078 2336 2407 -295 -77 -74 N ATOM 2168 CA ALA A 299 31.395 -21.795 -4.386 1.00 17.71 C ANISOU 2168 CA ALA A 299 2060 2288 2383 -262 -69 -78 C ATOM 2169 C ALA A 299 31.128 -22.407 -5.754 1.00 17.19 C ANISOU 2169 C ALA A 299 1980 2233 2317 -252 -58 -70 C ATOM 2170 O ALA A 299 31.551 -21.854 -6.778 1.00 18.62 O ANISOU 2170 O ALA A 299 2159 2420 2495 -270 -55 -61 O ATOM 2171 CB ALA A 299 30.384 -20.682 -4.052 1.00 18.12 C ANISOU 2171 CB ALA A 299 2150 2300 2434 -259 -70 -78 C ATOM 2172 N THR A 300 30.488 -23.575 -5.773 1.00 17.66 N ANISOU 2172 N THR A 300 2033 2298 2380 -226 -54 -74 N ATOM 2173 CA THR A 300 30.163 -24.206 -7.042 1.00 18.61 C ANISOU 2173 CA THR A 300 2149 2427 2497 -218 -47 -69 C ATOM 2174 C THR A 300 28.912 -23.579 -7.634 1.00 17.37 C ANISOU 2174 C THR A 300 2010 2248 2342 -217 -48 -59 C ATOM 2175 O THR A 300 27.980 -23.211 -6.919 1.00 14.95 O ANISOU 2175 O THR A 300 1714 1923 2041 -206 -51 -58 O ATOM 2176 CB THR A 300 29.942 -25.715 -6.902 1.00 17.59 C ANISOU 2176 CB THR A 300 2012 2305 2365 -196 -45 -75 C ATOM 2177 CG2 THR A 300 31.239 -26.437 -6.487 1.00 16.25 C ANISOU 2177 CG2 THR A 300 1823 2159 2193 -190 -42 -82 C ATOM 2178 OG1 THR A 300 28.924 -25.958 -5.938 1.00 18.09 O ANISOU 2178 OG1 THR A 300 2085 2354 2435 -184 -50 -78 O ATOM 2179 N ILE A 301 28.905 -23.463 -8.953 1.00 17.23 N ANISOU 2179 N ILE A 301 1994 2236 2318 -225 -45 -50 N ATOM 2180 CA ILE A 301 27.732 -23.078 -9.714 1.00 15.65 C ANISOU 2180 CA ILE A 301 1806 2022 2117 -222 -49 -37 C ATOM 2181 C ILE A 301 27.554 -24.103 -10.821 1.00 17.86 C ANISOU 2181 C ILE A 301 2084 2315 2386 -221 -48 -36 C ATOM 2182 O ILE A 301 28.524 -24.698 -11.307 1.00 19.46 O ANISOU 2182 O ILE A 301 2281 2535 2579 -224 -39 -42 O ATOM 2183 CB ILE A 301 27.876 -21.647 -10.290 1.00 18.74 C ANISOU 2183 CB ILE A 301 2212 2400 2507 -240 -50 -25 C ATOM 2184 CG1 ILE A 301 29.026 -21.583 -11.308 1.00 19.80 C ANISOU 2184 CG1 ILE A 301 2341 2553 2629 -262 -43 -22 C ATOM 2185 CG2 ILE A 301 28.065 -20.618 -9.158 1.00 18.14 C ANISOU 2185 CG2 ILE A 301 2150 2304 2438 -243 -52 -29 C ATOM 2186 CD1 ILE A 301 29.081 -20.263 -12.111 1.00 22.68 C ANISOU 2186 CD1 ILE A 301 2724 2904 2989 -283 -44 -6 C ATOM 2187 N GLY A 302 26.315 -24.293 -11.237 1.00 17.44 N ANISOU 2187 N GLY A 302 2037 2255 2333 -216 -57 -25 N ATOM 2188 CA GLY A 302 26.025 -25.261 -12.273 1.00 16.32 C ANISOU 2188 CA GLY A 302 1902 2122 2177 -219 -61 -23 C ATOM 2189 C GLY A 302 24.777 -24.848 -13.008 1.00 18.02 C ANISOU 2189 C GLY A 302 2123 2332 2391 -224 -74 -3 C ATOM 2190 O GLY A 302 23.904 -24.177 -12.454 1.00 17.77 O ANISOU 2190 O GLY A 302 2086 2293 2374 -215 -80 9 O ATOM 2191 N GLY A 303 24.685 -25.265 -14.261 1.00 17.66 N ANISOU 2191 N GLY A 303 2090 2292 2326 -236 -79 1 N ATOM 2192 CA GLY A 303 23.507 -24.957 -15.037 1.00 19.88 C ANISOU 2192 CA GLY A 303 2376 2573 2604 -243 -97 24 C ATOM 2193 C GLY A 303 22.331 -25.858 -14.700 1.00 21.41 C ANISOU 2193 C GLY A 303 2563 2771 2802 -243 -113 31 C ATOM 2194 O GLY A 303 22.461 -26.951 -14.140 1.00 20.86 O ANISOU 2194 O GLY A 303 2495 2702 2731 -241 -112 16 O ATOM 2195 N ASP A 304 21.151 -25.365 -15.053 1.00 20.75 N ANISOU 2195 N ASP A 304 2470 2691 2722 -245 -130 56 N ATOM 2196 CA ASP A 304 19.919 -26.130 -14.983 1.00 21.90 C ANISOU 2196 CA ASP A 304 2604 2848 2868 -253 -150 72 C ATOM 2197 C ASP A 304 19.827 -26.941 -16.282 1.00 21.93 C ANISOU 2197 C ASP A 304 2632 2856 2844 -281 -168 73 C ATOM 2198 O ASP A 304 20.857 -27.278 -16.874 1.00 21.39 O ANISOU 2198 O ASP A 304 2590 2781 2757 -286 -157 53 O ATOM 2199 CB ASP A 304 18.735 -25.179 -14.799 1.00 20.19 C ANISOU 2199 CB ASP A 304 2363 2640 2669 -239 -159 102 C ATOM 2200 CG ASP A 304 17.521 -25.854 -14.202 1.00 29.24 C ANISOU 2200 CG ASP A 304 3483 3804 3825 -240 -172 120 C ATOM 2201 OD1 ASP A 304 16.643 -26.310 -14.954 1.00 25.95 O ANISOU 2201 OD1 ASP A 304 3060 3403 3398 -262 -197 142 O ATOM 2202 OD2 ASP A 304 17.440 -25.897 -12.949 1.00 40.81 O1- ANISOU 2202 OD2 ASP A 304 4932 5268 5306 -221 -157 114 O1- ATOM 2203 N TYR A 305 18.623 -27.265 -16.747 1.00 21.04 N ANISOU 2203 N TYR A 305 2512 2756 2725 -299 -195 97 N ATOM 2204 CA TYR A 305 18.491 -27.959 -18.025 1.00 21.30 C ANISOU 2204 CA TYR A 305 2576 2790 2727 -330 -216 100 C ATOM 2205 C TYR A 305 19.275 -27.234 -19.115 1.00 20.58 C ANISOU 2205 C TYR A 305 2508 2694 2617 -331 -207 96 C ATOM 2206 O TYR A 305 19.314 -26.000 -19.171 1.00 16.98 O ANISOU 2206 O TYR A 305 2038 2239 2175 -316 -200 109 O ATOM 2207 CB TYR A 305 17.021 -28.064 -18.432 1.00 21.68 C ANISOU 2207 CB TYR A 305 2606 2859 2774 -352 -251 135 C ATOM 2208 CG TYR A 305 16.335 -29.362 -18.063 1.00 20.91 C ANISOU 2208 CG TYR A 305 2509 2766 2670 -378 -270 137 C ATOM 2209 CD1 TYR A 305 16.569 -30.525 -18.796 1.00 21.96 C ANISOU 2209 CD1 TYR A 305 2689 2887 2769 -410 -285 121 C ATOM 2210 CD2 TYR A 305 15.436 -29.425 -17.005 1.00 22.65 C ANISOU 2210 CD2 TYR A 305 2688 3004 2916 -371 -274 156 C ATOM 2211 CE1 TYR A 305 15.946 -31.720 -18.475 1.00 22.07 C ANISOU 2211 CE1 TYR A 305 2711 2900 2775 -439 -305 124 C ATOM 2212 CE2 TYR A 305 14.803 -30.631 -16.663 1.00 20.21 C ANISOU 2212 CE2 TYR A 305 2380 2699 2599 -401 -293 161 C ATOM 2213 CZ TYR A 305 15.058 -31.773 -17.406 1.00 26.57 C ANISOU 2213 CZ TYR A 305 3235 3488 3372 -437 -310 145 C ATOM 2214 OH TYR A 305 14.433 -32.982 -17.085 1.00 25.76 O ANISOU 2214 OH TYR A 305 3143 3386 3260 -473 -332 151 O ATOM 2215 N ASN A 306 19.923 -28.008 -19.972 1.00 18.67 N ANISOU 2215 N ASN A 306 2305 2445 2343 -347 -205 77 N ATOM 2216 CA ASN A 306 20.530 -27.441 -21.161 1.00 18.39 C ANISOU 2216 CA ASN A 306 2294 2409 2284 -353 -199 78 C ATOM 2217 C ASN A 306 19.532 -27.513 -22.314 1.00 18.51 C ANISOU 2217 C ASN A 306 2326 2434 2275 -383 -234 103 C ATOM 2218 O ASN A 306 18.688 -28.413 -22.381 1.00 17.97 O ANISOU 2218 O ASN A 306 2264 2368 2196 -405 -261 109 O ATOM 2219 CB ASN A 306 21.823 -28.179 -21.528 1.00 20.14 C ANISOU 2219 CB ASN A 306 2551 2623 2481 -349 -173 46 C ATOM 2220 CG ASN A 306 23.045 -27.672 -20.760 1.00 20.83 C ANISOU 2220 CG ASN A 306 2618 2708 2587 -323 -138 29 C ATOM 2221 ND2 ASN A 306 22.898 -27.440 -19.452 1.00 17.88 N ANISOU 2221 ND2 ASN A 306 2213 2334 2248 -306 -134 29 N ATOM 2222 OD1 ASN A 306 24.116 -27.513 -21.341 1.00 21.16 O ANISOU 2222 OD1 ASN A 306 2675 2754 2612 -319 -115 18 O ATOM 2223 N LEU A 307 19.617 -26.533 -23.211 1.00 20.56 N ANISOU 2223 N LEU A 307 2592 2697 2524 -386 -236 119 N ATOM 2224 CA LEU A 307 18.757 -26.458 -24.390 1.00 20.79 C ANISOU 2224 CA LEU A 307 2636 2736 2526 -414 -271 145 C ATOM 2225 C LEU A 307 19.532 -26.894 -25.626 1.00 18.53 C ANISOU 2225 C LEU A 307 2404 2444 2193 -432 -264 128 C ATOM 2226 O LEU A 307 20.649 -26.424 -25.851 1.00 19.59 O ANISOU 2226 O LEU A 307 2549 2573 2321 -418 -231 114 O ATOM 2227 CB LEU A 307 18.235 -25.031 -24.576 1.00 18.29 C ANISOU 2227 CB LEU A 307 2294 2427 2227 -402 -280 180 C ATOM 2228 CG LEU A 307 17.463 -24.433 -23.394 1.00 18.41 C ANISOU 2228 CG LEU A 307 2259 2448 2287 -376 -282 199 C ATOM 2229 CD1 LEU A 307 17.123 -22.983 -23.644 1.00 16.55 C ANISOU 2229 CD1 LEU A 307 2010 2213 2065 -357 -286 230 C ATOM 2230 CD2 LEU A 307 16.179 -25.224 -23.233 1.00 19.21 C ANISOU 2230 CD2 LEU A 307 2339 2569 2391 -394 -316 219 C ATOM 2231 N GLY A 308 18.922 -27.766 -26.439 1.00 20.22 N ANISOU 2231 N GLY A 308 2653 2659 2372 -465 -294 132 N ATOM 2232 CA GLY A 308 19.547 -28.242 -27.655 1.00 19.37 C ANISOU 2232 CA GLY A 308 2604 2544 2213 -482 -288 115 C ATOM 2233 C GLY A 308 18.619 -28.134 -28.854 1.00 17.52 C ANISOU 2233 C GLY A 308 2393 2319 1944 -519 -332 143 C ATOM 2234 O GLY A 308 17.411 -27.937 -28.725 1.00 17.78 O ANISOU 2234 O GLY A 308 2396 2367 1993 -535 -371 176 O ATOM 2235 N VAL A 309 19.220 -28.260 -30.032 1.00 15.75 N ANISOU 2235 N VAL A 309 2224 2091 1672 -531 -323 132 N ATOM 2236 CA VAL A 309 18.506 -28.258 -31.306 1.00 19.15 C ANISOU 2236 CA VAL A 309 2690 2529 2058 -570 -363 155 C ATOM 2237 C VAL A 309 18.496 -29.689 -31.824 1.00 20.40 C ANISOU 2237 C VAL A 309 2914 2669 2167 -598 -376 128 C ATOM 2238 O VAL A 309 19.548 -30.342 -31.881 1.00 18.86 O ANISOU 2238 O VAL A 309 2759 2456 1949 -580 -337 90 O ATOM 2239 CB VAL A 309 19.175 -27.306 -32.319 1.00 22.15 C ANISOU 2239 CB VAL A 309 3091 2913 2412 -566 -344 163 C ATOM 2240 CG1 VAL A 309 18.559 -27.432 -33.712 1.00 18.74 C ANISOU 2240 CG1 VAL A 309 2708 2488 1925 -607 -384 182 C ATOM 2241 CG2 VAL A 309 19.133 -25.855 -31.823 1.00 20.22 C ANISOU 2241 CG2 VAL A 309 2790 2680 2215 -541 -336 191 C ATOM 2242 N SER A 310 17.315 -30.185 -32.180 1.00 17.67 N ANISOU 2242 N SER A 310 2581 2329 1804 -642 -431 149 N ATOM 2243 CA SER A 310 17.230 -31.541 -32.702 1.00 22.22 C ANISOU 2243 CA SER A 310 3230 2884 2329 -676 -449 125 C ATOM 2244 C SER A 310 18.002 -31.652 -34.009 1.00 22.53 C ANISOU 2244 C SER A 310 3345 2911 2304 -681 -431 105 C ATOM 2245 O SER A 310 17.827 -30.840 -34.926 1.00 19.81 O ANISOU 2245 O SER A 310 3005 2583 1939 -694 -445 130 O ATOM 2246 CB SER A 310 15.770 -31.949 -32.921 1.00 20.50 C ANISOU 2246 CB SER A 310 3009 2680 2101 -732 -517 158 C ATOM 2247 OG SER A 310 15.687 -33.229 -33.526 1.00 18.35 O ANISOU 2247 OG SER A 310 2820 2381 1772 -773 -539 135 O ATOM 2248 N ARG A 311 18.858 -32.670 -34.089 1.00 23.56 N ANISOU 2248 N ARG A 311 3537 3012 2401 -668 -398 62 N ATOM 2249 CA ARG A 311 19.494 -32.999 -35.358 1.00 22.10 C ANISOU 2249 CA ARG A 311 3437 2814 2147 -674 -382 40 C ATOM 2250 C ARG A 311 18.468 -33.177 -36.474 1.00 22.45 C ANISOU 2250 C ARG A 311 3531 2861 2140 -735 -444 62 C ATOM 2251 O ARG A 311 18.792 -32.990 -37.648 1.00 23.31 O ANISOU 2251 O ARG A 311 3694 2970 2194 -745 -438 60 O ATOM 2252 CB ARG A 311 20.315 -34.277 -35.203 1.00 26.63 C ANISOU 2252 CB ARG A 311 4075 3352 2691 -651 -347 -8 C ATOM 2253 CG ARG A 311 21.260 -34.542 -36.363 1.00 37.62 C ANISOU 2253 CG ARG A 311 5547 4732 4015 -637 -309 -36 C ATOM 2254 CD ARG A 311 22.217 -35.665 -36.022 1.00 41.47 C ANISOU 2254 CD ARG A 311 6084 5187 4485 -596 -263 -82 C ATOM 2255 NE ARG A 311 21.494 -36.871 -35.631 1.00 38.87 N ANISOU 2255 NE ARG A 311 5800 4823 4146 -625 -302 -95 N ATOM 2256 CZ ARG A 311 20.954 -37.736 -36.479 1.00 45.79 C ANISOU 2256 CZ ARG A 311 6770 5669 4958 -670 -338 -105 C ATOM 2257 NH1 ARG A 311 21.059 -37.576 -37.792 1.00 46.21 N1+ ANISOU 2257 NH1 ARG A 311 6887 5724 4947 -687 -340 -107 N1+ ATOM 2258 NH2 ARG A 311 20.314 -38.802 -35.998 1.00 40.54 N ANISOU 2258 NH2 ARG A 311 6141 4972 4289 -700 -374 -114 N ATOM 2259 N HIS A 312 17.235 -33.549 -36.131 1.00 23.88 N ANISOU 2259 N HIS A 312 3692 3046 2334 -779 -503 86 N ATOM 2260 CA HIS A 312 16.168 -33.762 -37.094 1.00 22.85 C ANISOU 2260 CA HIS A 312 3601 2922 2157 -844 -569 113 C ATOM 2261 C HIS A 312 15.327 -32.519 -37.353 1.00 24.90 C ANISOU 2261 C HIS A 312 3793 3225 2443 -858 -607 168 C ATOM 2262 O HIS A 312 14.374 -32.585 -38.136 1.00 27.06 O ANISOU 2262 O HIS A 312 4087 3512 2682 -912 -667 197 O ATOM 2263 CB HIS A 312 15.265 -34.894 -36.609 1.00 24.66 C ANISOU 2263 CB HIS A 312 3846 3137 2385 -890 -617 113 C ATOM 2264 CG HIS A 312 15.992 -36.184 -36.426 1.00 27.33 C ANISOU 2264 CG HIS A 312 4264 3429 2693 -880 -587 61 C ATOM 2265 CD2 HIS A 312 16.380 -36.839 -35.305 1.00 27.90 C ANISOU 2265 CD2 HIS A 312 4323 3478 2799 -850 -558 36 C ATOM 2266 ND1 HIS A 312 16.469 -36.922 -37.486 1.00 26.69 N ANISOU 2266 ND1 HIS A 312 4295 3314 2534 -894 -582 28 N ATOM 2267 CE1 HIS A 312 17.090 -37.996 -37.029 1.00 31.56 C ANISOU 2267 CE1 HIS A 312 4965 3887 3139 -872 -551 -14 C ATOM 2268 NE2 HIS A 312 17.053 -37.968 -35.709 1.00 30.96 N ANISOU 2268 NE2 HIS A 312 4814 3818 3131 -845 -537 -10 N ATOM 2269 N SER A 313 15.640 -31.392 -36.729 1.00 23.45 N ANISOU 2269 N SER A 313 3532 3061 2317 -811 -574 183 N ATOM 2270 CA SER A 313 14.835 -30.198 -36.932 1.00 21.97 C ANISOU 2270 CA SER A 313 3283 2909 2154 -817 -607 236 C ATOM 2271 C SER A 313 14.936 -29.740 -38.377 1.00 23.88 C ANISOU 2271 C SER A 313 3579 3156 2337 -839 -622 249 C ATOM 2272 O SER A 313 16.030 -29.687 -38.950 1.00 23.81 O ANISOU 2272 O SER A 313 3622 3132 2294 -819 -576 220 O ATOM 2273 CB SER A 313 15.282 -29.085 -35.996 1.00 21.76 C ANISOU 2273 CB SER A 313 3181 2893 2195 -759 -565 245 C ATOM 2274 OG SER A 313 14.474 -27.949 -36.187 1.00 24.55 O ANISOU 2274 OG SER A 313 3481 3275 2571 -760 -596 296 O ATOM 2275 N GLU A 314 13.792 -29.440 -38.978 1.00 23.37 N ANISOU 2275 N GLU A 314 3503 3118 2259 -881 -687 296 N ATOM 2276 CA GLU A 314 13.808 -28.825 -40.294 1.00 26.17 C ANISOU 2276 CA GLU A 314 3898 3482 2563 -900 -704 317 C ATOM 2277 C GLU A 314 14.014 -27.313 -40.220 1.00 27.27 C ANISOU 2277 C GLU A 314 3980 3639 2742 -858 -682 348 C ATOM 2278 O GLU A 314 14.104 -26.658 -41.263 1.00 28.27 O ANISOU 2278 O GLU A 314 4138 3774 2831 -868 -692 368 O ATOM 2279 CB GLU A 314 12.516 -29.171 -41.042 1.00 31.02 C ANISOU 2279 CB GLU A 314 4529 4118 3140 -966 -787 355 C ATOM 2280 CG GLU A 314 12.452 -30.665 -41.421 1.00 35.05 C ANISOU 2280 CG GLU A 314 5126 4601 3590 -1018 -810 320 C ATOM 2281 CD GLU A 314 11.114 -31.084 -42.007 1.00 46.06 C ANISOU 2281 CD GLU A 314 6531 6018 4951 -1093 -899 360 C ATOM 2282 OE1 GLU A 314 10.182 -30.250 -42.037 1.00 44.25 O ANISOU 2282 OE1 GLU A 314 6230 5831 4752 -1100 -943 418 O ATOM 2283 OE2 GLU A 314 10.982 -32.267 -42.397 1.00 50.53 O1- ANISOU 2283 OE2 GLU A 314 7176 6559 5462 -1144 -926 335 O1- ATOM 2284 N HIS A 315 14.130 -26.744 -39.019 1.00 24.94 N ANISOU 2284 N HIS A 315 3611 3348 2519 -811 -652 352 N ATOM 2285 CA HIS A 315 14.298 -25.301 -38.861 1.00 25.75 C ANISOU 2285 CA HIS A 315 3664 3461 2660 -771 -633 381 C ATOM 2286 C HIS A 315 15.393 -24.993 -37.842 1.00 25.20 C ANISOU 2286 C HIS A 315 3568 3373 2636 -720 -564 348 C ATOM 2287 O HIS A 315 15.160 -24.384 -36.799 1.00 21.87 O ANISOU 2287 O HIS A 315 3079 2955 2275 -686 -555 361 O ATOM 2288 CB HIS A 315 12.976 -24.649 -38.474 1.00 26.87 C ANISOU 2288 CB HIS A 315 3733 3632 2846 -769 -682 437 C ATOM 2289 CG HIS A 315 11.850 -25.028 -39.375 1.00 29.81 C ANISOU 2289 CG HIS A 315 4122 4029 3177 -824 -755 473 C ATOM 2290 CD2 HIS A 315 10.682 -25.665 -39.126 1.00 29.99 C ANISOU 2290 CD2 HIS A 315 4112 4076 3206 -858 -809 498 C ATOM 2291 ND1 HIS A 315 11.870 -24.769 -40.730 1.00 33.13 N ANISOU 2291 ND1 HIS A 315 4598 4453 3536 -854 -780 489 N ATOM 2292 CE1 HIS A 315 10.756 -25.223 -41.274 1.00 32.32 C ANISOU 2292 CE1 HIS A 315 4499 4376 3406 -905 -850 523 C ATOM 2293 NE2 HIS A 315 10.022 -25.776 -40.324 1.00 32.48 N ANISOU 2293 NE2 HIS A 315 4463 4409 3467 -910 -869 529 N ATOM 2294 N LYS A 316 16.624 -25.394 -38.179 1.00 21.69 N ANISOU 2294 N LYS A 316 3176 2909 2157 -713 -516 305 N ATOM 2295 CA LYS A 316 17.717 -25.327 -37.215 1.00 21.22 C ANISOU 2295 CA LYS A 316 3093 2834 2135 -670 -454 271 C ATOM 2296 C LYS A 316 18.163 -23.894 -36.950 1.00 21.99 C ANISOU 2296 C LYS A 316 3150 2935 2269 -639 -426 292 C ATOM 2297 O LYS A 316 18.546 -23.575 -35.818 1.00 18.37 O ANISOU 2297 O LYS A 316 2646 2471 1863 -605 -396 282 O ATOM 2298 CB LYS A 316 18.890 -26.186 -37.689 1.00 22.19 C ANISOU 2298 CB LYS A 316 3280 2942 2210 -669 -409 224 C ATOM 2299 CG LYS A 316 18.512 -27.674 -37.818 1.00 21.91 C ANISOU 2299 CG LYS A 316 3294 2892 2138 -697 -433 197 C ATOM 2300 CD LYS A 316 19.677 -28.566 -38.242 1.00 21.49 C ANISOU 2300 CD LYS A 316 3309 2819 2036 -686 -384 149 C ATOM 2301 CE LYS A 316 19.194 -30.014 -38.361 1.00 23.90 C ANISOU 2301 CE LYS A 316 3671 3103 2304 -715 -413 125 C ATOM 2302 NZ LYS A 316 20.277 -30.999 -38.641 1.00 25.23 N1+ ANISOU 2302 NZ LYS A 316 3911 3248 2429 -695 -365 75 N1+ ATOM 2303 N ALA A 317 18.096 -23.008 -37.952 1.00 24.00 N ANISOU 2303 N ALA A 317 3425 3197 2496 -651 -439 323 N ATOM 2304 CA ALA A 317 18.492 -21.617 -37.716 1.00 20.45 C ANISOU 2304 CA ALA A 317 2944 2744 2079 -624 -417 345 C ATOM 2305 C ALA A 317 17.493 -20.905 -36.813 1.00 21.19 C ANISOU 2305 C ALA A 317 2975 2843 2234 -602 -444 379 C ATOM 2306 O ALA A 317 17.891 -20.188 -35.887 1.00 20.93 O ANISOU 2306 O ALA A 317 2906 2799 2248 -569 -415 376 O ATOM 2307 CB ALA A 317 18.645 -20.867 -39.034 1.00 24.79 C ANISOU 2307 CB ALA A 317 3537 3299 2582 -644 -425 373 C ATOM 2308 N ALA A 318 16.191 -21.101 -37.051 1.00 20.66 N ANISOU 2308 N ALA A 318 2894 2792 2164 -619 -501 411 N ATOM 2309 CA ALA A 318 15.190 -20.604 -36.112 1.00 21.78 C ANISOU 2309 CA ALA A 318 2970 2942 2362 -592 -524 442 C ATOM 2310 C ALA A 318 15.381 -21.217 -34.722 1.00 22.25 C ANISOU 2310 C ALA A 318 2992 2996 2466 -570 -496 408 C ATOM 2311 O ALA A 318 15.284 -20.519 -33.701 1.00 19.43 O ANISOU 2311 O ALA A 318 2589 2632 2160 -532 -480 416 O ATOM 2312 CB ALA A 318 13.785 -20.901 -36.638 1.00 22.72 C ANISOU 2312 CB ALA A 318 3076 3090 2467 -620 -590 483 C ATOM 2313 N ALA A 319 15.640 -22.526 -34.661 1.00 20.28 N ANISOU 2313 N ALA A 319 2766 2744 2194 -592 -492 372 N ATOM 2314 CA ALA A 319 15.812 -23.181 -33.369 1.00 18.88 C ANISOU 2314 CA ALA A 319 2558 2559 2055 -573 -468 342 C ATOM 2315 C ALA A 319 17.003 -22.593 -32.619 1.00 21.99 C ANISOU 2315 C ALA A 319 2942 2934 2478 -536 -411 316 C ATOM 2316 O ALA A 319 16.908 -22.275 -31.426 1.00 19.96 O ANISOU 2316 O ALA A 319 2640 2674 2271 -506 -397 314 O ATOM 2317 CB ALA A 319 15.978 -24.690 -33.567 1.00 19.08 C ANISOU 2317 CB ALA A 319 2625 2580 2045 -604 -473 307 C ATOM 2318 N TRP A 320 18.136 -22.424 -33.311 1.00 20.27 N ANISOU 2318 N TRP A 320 2767 2707 2229 -541 -379 297 N ATOM 2319 CA TRP A 320 19.327 -21.886 -32.656 1.00 19.94 C ANISOU 2319 CA TRP A 320 2713 2652 2211 -514 -327 275 C ATOM 2320 C TRP A 320 19.143 -20.416 -32.309 1.00 21.21 C ANISOU 2320 C TRP A 320 2845 2806 2407 -492 -327 306 C ATOM 2321 O TRP A 320 19.525 -19.987 -31.213 1.00 19.11 O ANISOU 2321 O TRP A 320 2549 2530 2183 -465 -302 296 O ATOM 2322 CB TRP A 320 20.553 -22.099 -33.548 1.00 19.18 C ANISOU 2322 CB TRP A 320 2665 2554 2068 -526 -293 252 C ATOM 2323 CG TRP A 320 21.839 -21.465 -33.094 1.00 22.14 C ANISOU 2323 CG TRP A 320 3028 2922 2460 -507 -242 237 C ATOM 2324 CD1 TRP A 320 22.674 -20.673 -33.854 1.00 20.51 C ANISOU 2324 CD1 TRP A 320 2844 2719 2231 -515 -218 246 C ATOM 2325 CD2 TRP A 320 22.456 -21.564 -31.798 1.00 20.15 C ANISOU 2325 CD2 TRP A 320 2741 2665 2252 -481 -212 212 C ATOM 2326 CE2 TRP A 320 23.658 -20.818 -31.849 1.00 19.75 C ANISOU 2326 CE2 TRP A 320 2689 2614 2200 -478 -173 209 C ATOM 2327 CE3 TRP A 320 22.108 -22.208 -30.597 1.00 19.21 C ANISOU 2327 CE3 TRP A 320 2590 2541 2169 -463 -215 195 C ATOM 2328 NE1 TRP A 320 23.772 -20.299 -33.115 1.00 20.51 N ANISOU 2328 NE1 TRP A 320 2820 2716 2256 -499 -176 230 N ATOM 2329 CZ2 TRP A 320 24.516 -20.697 -30.748 1.00 21.88 C ANISOU 2329 CZ2 TRP A 320 2927 2881 2504 -459 -140 189 C ATOM 2330 CZ3 TRP A 320 22.958 -22.085 -29.502 1.00 19.41 C ANISOU 2330 CZ3 TRP A 320 2587 2562 2228 -441 -181 174 C ATOM 2331 CH2 TRP A 320 24.152 -21.335 -29.586 1.00 18.41 C ANISOU 2331 CH2 TRP A 320 2459 2436 2099 -440 -146 172 C ATOM 2332 N ALA A 321 18.537 -19.635 -33.217 1.00 21.02 N ANISOU 2332 N ALA A 321 2834 2787 2366 -502 -357 345 N ATOM 2333 CA ALA A 321 18.259 -18.235 -32.907 1.00 21.26 C ANISOU 2333 CA ALA A 321 2844 2806 2429 -477 -360 378 C ATOM 2334 C ALA A 321 17.442 -18.121 -31.633 1.00 22.99 C ANISOU 2334 C ALA A 321 3011 3024 2701 -444 -368 385 C ATOM 2335 O ALA A 321 17.727 -17.271 -30.782 1.00 20.32 O ANISOU 2335 O ALA A 321 2656 2667 2398 -415 -346 385 O ATOM 2336 CB ALA A 321 17.522 -17.560 -34.063 1.00 19.28 C ANISOU 2336 CB ALA A 321 2612 2562 2151 -490 -398 424 C ATOM 2337 N PHE A 322 16.436 -18.997 -31.472 1.00 20.02 N ANISOU 2337 N PHE A 322 2612 2669 2328 -451 -400 392 N ATOM 2338 CA PHE A 322 15.557 -18.900 -30.311 1.00 22.23 C ANISOU 2338 CA PHE A 322 2838 2953 2654 -420 -408 404 C ATOM 2339 C PHE A 322 16.287 -19.246 -29.023 1.00 20.48 C ANISOU 2339 C PHE A 322 2601 2717 2462 -400 -368 363 C ATOM 2340 O PHE A 322 16.035 -18.620 -27.985 1.00 19.20 O ANISOU 2340 O PHE A 322 2407 2546 2340 -364 -356 369 O ATOM 2341 CB PHE A 322 14.340 -19.809 -30.450 1.00 18.74 C ANISOU 2341 CB PHE A 322 2373 2542 2206 -439 -451 423 C ATOM 2342 CG PHE A 322 13.353 -19.630 -29.335 1.00 22.26 C ANISOU 2342 CG PHE A 322 2759 3001 2699 -405 -459 444 C ATOM 2343 CD1 PHE A 322 12.532 -18.514 -29.298 1.00 22.82 C ANISOU 2343 CD1 PHE A 322 2801 3078 2791 -371 -474 489 C ATOM 2344 CD2 PHE A 322 13.320 -20.525 -28.271 1.00 19.78 C ANISOU 2344 CD2 PHE A 322 2419 2690 2405 -403 -445 417 C ATOM 2345 CE1 PHE A 322 11.649 -18.325 -28.254 1.00 24.76 C ANISOU 2345 CE1 PHE A 322 2992 3339 3079 -333 -474 508 C ATOM 2346 CE2 PHE A 322 12.443 -20.340 -27.217 1.00 22.06 C ANISOU 2346 CE2 PHE A 322 2654 2995 2735 -370 -447 437 C ATOM 2347 CZ PHE A 322 11.611 -19.241 -27.205 1.00 22.27 C ANISOU 2347 CZ PHE A 322 2650 3031 2783 -334 -460 481 C ATOM 2348 N ILE A 323 17.158 -20.259 -29.056 1.00 17.63 N ANISOU 2348 N ILE A 323 2263 2355 2082 -421 -348 323 N ATOM 2349 CA ILE A 323 17.908 -20.621 -27.856 1.00 17.89 C ANISOU 2349 CA ILE A 323 2281 2376 2141 -403 -312 287 C ATOM 2350 C ILE A 323 18.750 -19.440 -27.396 1.00 18.80 C ANISOU 2350 C ILE A 323 2397 2470 2277 -381 -280 283 C ATOM 2351 O ILE A 323 18.737 -19.062 -26.218 1.00 19.26 O ANISOU 2351 O ILE A 323 2429 2517 2372 -353 -265 277 O ATOM 2352 CB ILE A 323 18.772 -21.872 -28.108 1.00 20.30 C ANISOU 2352 CB ILE A 323 2615 2681 2416 -425 -294 247 C ATOM 2353 CG1 ILE A 323 17.889 -23.113 -28.209 1.00 16.78 C ANISOU 2353 CG1 ILE A 323 2169 2249 1957 -447 -326 247 C ATOM 2354 CG2 ILE A 323 19.787 -22.061 -26.980 1.00 19.42 C ANISOU 2354 CG2 ILE A 323 2491 2558 2330 -405 -254 212 C ATOM 2355 CD1 ILE A 323 18.640 -24.357 -28.560 1.00 17.30 C ANISOU 2355 CD1 ILE A 323 2275 2309 1988 -465 -312 209 C ATOM 2356 N GLN A 324 19.465 -18.810 -28.334 1.00 18.40 N ANISOU 2356 N GLN A 324 2379 2411 2199 -396 -270 289 N ATOM 2357 CA GLN A 324 20.309 -17.671 -27.978 1.00 20.30 C ANISOU 2357 CA GLN A 324 2626 2632 2456 -385 -243 288 C ATOM 2358 C GLN A 324 19.490 -16.540 -27.378 1.00 18.29 C ANISOU 2358 C GLN A 324 2355 2360 2235 -354 -256 317 C ATOM 2359 O GLN A 324 19.910 -15.904 -26.403 1.00 17.68 O ANISOU 2359 O GLN A 324 2271 2262 2185 -334 -235 307 O ATOM 2360 CB GLN A 324 21.060 -17.182 -29.208 1.00 16.84 C ANISOU 2360 CB GLN A 324 2226 2192 1980 -411 -235 297 C ATOM 2361 CG GLN A 324 22.020 -18.211 -29.738 1.00 20.94 C ANISOU 2361 CG GLN A 324 2763 2727 2465 -433 -213 267 C ATOM 2362 CD GLN A 324 22.674 -17.737 -30.983 1.00 24.23 C ANISOU 2362 CD GLN A 324 3217 3148 2842 -458 -204 279 C ATOM 2363 NE2 GLN A 324 22.017 -17.970 -32.111 1.00 25.85 N ANISOU 2363 NE2 GLN A 324 3448 3363 3011 -476 -231 298 N ATOM 2364 OE1 GLN A 324 23.745 -17.135 -30.945 1.00 27.28 O ANISOU 2364 OE1 GLN A 324 3609 3530 3228 -465 -173 275 O ATOM 2365 N TRP A 325 18.326 -16.269 -27.951 1.00 17.98 N ANISOU 2365 N TRP A 325 2311 2330 2192 -347 -290 354 N ATOM 2366 CA TRP A 325 17.527 -15.151 -27.466 1.00 19.17 C ANISOU 2366 CA TRP A 325 2448 2464 2371 -310 -300 385 C ATOM 2367 C TRP A 325 16.935 -15.454 -26.096 1.00 20.08 C ANISOU 2367 C TRP A 325 2522 2582 2524 -276 -294 375 C ATOM 2368 O TRP A 325 16.953 -14.598 -25.199 1.00 20.03 O ANISOU 2368 O TRP A 325 2513 2551 2545 -243 -278 376 O ATOM 2369 CB TRP A 325 16.431 -14.828 -28.477 1.00 20.31 C ANISOU 2369 CB TRP A 325 2593 2624 2501 -309 -340 432 C ATOM 2370 CG TRP A 325 15.439 -13.836 -27.964 1.00 22.10 C ANISOU 2370 CG TRP A 325 2799 2840 2758 -261 -351 467 C ATOM 2371 CD1 TRP A 325 15.499 -12.475 -28.074 1.00 21.83 C ANISOU 2371 CD1 TRP A 325 2791 2773 2730 -236 -347 490 C ATOM 2372 CD2 TRP A 325 14.235 -14.134 -27.260 1.00 21.41 C ANISOU 2372 CD2 TRP A 325 2661 2775 2697 -229 -366 484 C ATOM 2373 CE2 TRP A 325 13.605 -12.905 -26.970 1.00 23.84 C ANISOU 2373 CE2 TRP A 325 2967 3064 3028 -178 -368 518 C ATOM 2374 CE3 TRP A 325 13.620 -15.323 -26.853 1.00 23.20 C ANISOU 2374 CE3 TRP A 325 2848 3037 2931 -238 -378 477 C ATOM 2375 NE1 TRP A 325 14.397 -11.906 -27.474 1.00 21.04 N ANISOU 2375 NE1 TRP A 325 2663 2672 2659 -184 -357 520 N ATOM 2376 CZ2 TRP A 325 12.397 -12.832 -26.285 1.00 24.74 C ANISOU 2376 CZ2 TRP A 325 3033 3198 3170 -133 -377 545 C ATOM 2377 CZ3 TRP A 325 12.409 -15.247 -26.171 1.00 24.05 C ANISOU 2377 CZ3 TRP A 325 2905 3165 3067 -199 -390 505 C ATOM 2378 CH2 TRP A 325 11.816 -14.011 -25.892 1.00 24.26 C ANISOU 2378 CH2 TRP A 325 2925 3178 3116 -145 -387 539 C ATOM 2379 N LEU A 326 16.416 -16.670 -25.914 1.00 20.06 N ANISOU 2379 N LEU A 326 2493 2609 2522 -287 -307 366 N ATOM 2380 CA LEU A 326 15.810 -17.039 -24.640 1.00 19.24 C ANISOU 2380 CA LEU A 326 2348 2512 2450 -258 -301 360 C ATOM 2381 C LEU A 326 16.797 -16.908 -23.492 1.00 18.84 C ANISOU 2381 C LEU A 326 2303 2437 2419 -246 -263 323 C ATOM 2382 O LEU A 326 16.450 -16.384 -22.427 1.00 19.36 O ANISOU 2382 O LEU A 326 2352 2491 2513 -209 -251 325 O ATOM 2383 CB LEU A 326 15.271 -18.466 -24.702 1.00 17.26 C ANISOU 2383 CB LEU A 326 2074 2293 2190 -284 -320 354 C ATOM 2384 CG LEU A 326 14.566 -18.946 -23.427 1.00 21.70 C ANISOU 2384 CG LEU A 326 2593 2869 2784 -260 -315 351 C ATOM 2385 CD1 LEU A 326 13.223 -18.261 -23.242 1.00 18.46 C ANISOU 2385 CD1 LEU A 326 2144 2476 2395 -225 -334 398 C ATOM 2386 CD2 LEU A 326 14.389 -20.458 -23.445 1.00 20.01 C ANISOU 2386 CD2 LEU A 326 2369 2677 2555 -295 -329 336 C ATOM 2387 N ILE A 327 18.035 -17.371 -23.685 1.00 15.84 N ANISOU 2387 N ILE A 327 1946 2050 2021 -274 -244 289 N ATOM 2388 CA ILE A 327 18.982 -17.379 -22.581 1.00 16.64 C ANISOU 2388 CA ILE A 327 2048 2136 2140 -267 -212 256 C ATOM 2389 C ILE A 327 19.641 -16.030 -22.359 1.00 20.87 C ANISOU 2389 C ILE A 327 2607 2640 2683 -257 -196 258 C ATOM 2390 O ILE A 327 20.256 -15.832 -21.306 1.00 19.28 O ANISOU 2390 O ILE A 327 2405 2422 2497 -248 -175 236 O ATOM 2391 CB ILE A 327 20.082 -18.444 -22.774 1.00 18.53 C ANISOU 2391 CB ILE A 327 2296 2385 2358 -296 -197 221 C ATOM 2392 CG1 ILE A 327 21.018 -18.044 -23.911 1.00 18.81 C ANISOU 2392 CG1 ILE A 327 2365 2418 2365 -322 -189 222 C ATOM 2393 CG2 ILE A 327 19.487 -19.825 -22.993 1.00 18.57 C ANISOU 2393 CG2 ILE A 327 2288 2414 2352 -308 -214 216 C ATOM 2394 CD1 ILE A 327 22.116 -19.083 -24.186 1.00 21.79 C ANISOU 2394 CD1 ILE A 327 2751 2810 2720 -344 -169 191 C ATOM 2395 N GLU A 328 19.500 -15.088 -23.292 1.00 21.29 N ANISOU 2395 N GLU A 328 2685 2681 2722 -261 -207 287 N ATOM 2396 CA GLU A 328 20.148 -13.781 -23.201 1.00 18.39 C ANISOU 2396 CA GLU A 328 2350 2278 2358 -260 -195 292 C ATOM 2397 C GLU A 328 19.183 -12.610 -23.063 1.00 22.13 C ANISOU 2397 C GLU A 328 2835 2727 2847 -221 -207 325 C ATOM 2398 O GLU A 328 19.415 -11.707 -22.244 1.00 22.89 O ANISOU 2398 O GLU A 328 2951 2788 2959 -202 -193 320 O ATOM 2399 CB GLU A 328 21.041 -13.550 -24.428 1.00 18.31 C ANISOU 2399 CB GLU A 328 2371 2270 2316 -300 -192 297 C ATOM 2400 CG GLU A 328 21.848 -12.268 -24.307 1.00 18.78 C ANISOU 2400 CG GLU A 328 2465 2293 2376 -309 -179 302 C ATOM 2401 CD GLU A 328 22.978 -12.188 -25.298 1.00 25.75 C ANISOU 2401 CD GLU A 328 3371 3185 3229 -354 -168 301 C ATOM 2402 OE1 GLU A 328 23.144 -13.135 -26.116 1.00 21.96 O ANISOU 2402 OE1 GLU A 328 2881 2737 2724 -373 -168 295 O ATOM 2403 OE2 GLU A 328 23.696 -11.166 -25.258 1.00 25.11 O1- ANISOU 2403 OE2 GLU A 328 3318 3077 3146 -371 -159 307 O1- ATOM 2404 N ASP A 329 18.119 -12.558 -23.865 1.00 21.67 N ANISOU 2404 N ASP A 329 2767 2684 2782 -209 -233 360 N ATOM 2405 CA ASP A 329 17.333 -11.333 -23.962 1.00 23.05 C ANISOU 2405 CA ASP A 329 2958 2834 2967 -171 -245 397 C ATOM 2406 C ASP A 329 15.887 -11.461 -23.520 1.00 22.46 C ANISOU 2406 C ASP A 329 2842 2778 2913 -123 -259 422 C ATOM 2407 O ASP A 329 15.180 -10.452 -23.504 1.00 22.52 O ANISOU 2407 O ASP A 329 2860 2766 2931 -81 -265 454 O ATOM 2408 CB ASP A 329 17.370 -10.792 -25.398 1.00 23.47 C ANISOU 2408 CB ASP A 329 3042 2884 2991 -193 -265 428 C ATOM 2409 CG ASP A 329 18.773 -10.502 -25.854 1.00 25.49 C ANISOU 2409 CG ASP A 329 3338 3122 3226 -239 -248 410 C ATOM 2410 OD1 ASP A 329 19.444 -9.726 -25.158 1.00 26.66 O ANISOU 2410 OD1 ASP A 329 3511 3233 3385 -236 -228 397 O ATOM 2411 OD2 ASP A 329 19.212 -11.063 -26.888 1.00 32.14 O1- ANISOU 2411 OD2 ASP A 329 4186 3988 4038 -279 -253 409 O1- ATOM 2412 N SER A 330 15.430 -12.651 -23.138 1.00 23.72 N ANISOU 2412 N SER A 330 2957 2977 3080 -127 -263 411 N ATOM 2413 CA SER A 330 14.001 -12.843 -22.902 1.00 23.96 C ANISOU 2413 CA SER A 330 2941 3037 3127 -90 -281 443 C ATOM 2414 C SER A 330 13.542 -12.224 -21.586 1.00 24.67 C ANISOU 2414 C SER A 330 3019 3108 3246 -32 -258 443 C ATOM 2415 O SER A 330 12.360 -11.889 -21.443 1.00 22.97 O ANISOU 2415 O SER A 330 2774 2909 3046 14 -267 479 O ATOM 2416 CB SER A 330 13.680 -14.336 -22.882 1.00 22.80 C ANISOU 2416 CB SER A 330 2753 2935 2976 -120 -293 432 C ATOM 2417 OG SER A 330 14.235 -14.923 -21.715 1.00 21.47 O ANISOU 2417 OG SER A 330 2576 2760 2821 -121 -266 392 O ATOM 2418 N GLY A 331 14.446 -12.085 -20.618 1.00 20.54 N ANISOU 2418 N GLY A 331 2520 2553 2730 -32 -228 403 N ATOM 2419 CA GLY A 331 14.073 -11.828 -19.246 1.00 21.67 C ANISOU 2419 CA GLY A 331 2652 2684 2897 15 -204 394 C ATOM 2420 C GLY A 331 13.911 -13.064 -18.375 1.00 19.59 C ANISOU 2420 C GLY A 331 2344 2455 2643 7 -195 371 C ATOM 2421 O GLY A 331 13.618 -12.920 -17.187 1.00 19.02 O ANISOU 2421 O GLY A 331 2263 2376 2588 45 -173 362 O ATOM 2422 N PHE A 332 14.119 -14.270 -18.923 1.00 20.10 N ANISOU 2422 N PHE A 332 2388 2553 2696 -41 -211 361 N ATOM 2423 CA PHE A 332 13.869 -15.511 -18.181 1.00 20.41 C ANISOU 2423 CA PHE A 332 2389 2624 2743 -51 -207 345 C ATOM 2424 C PHE A 332 14.748 -15.622 -16.936 1.00 19.55 C ANISOU 2424 C PHE A 332 2295 2491 2642 -48 -176 303 C ATOM 2425 O PHE A 332 14.236 -15.837 -15.829 1.00 18.63 O ANISOU 2425 O PHE A 332 2154 2383 2541 -19 -161 299 O ATOM 2426 CB PHE A 332 14.091 -16.715 -19.096 1.00 17.99 C ANISOU 2426 CB PHE A 332 2074 2346 2416 -106 -230 339 C ATOM 2427 CG PHE A 332 13.952 -18.055 -18.422 1.00 20.66 C ANISOU 2427 CG PHE A 332 2382 2709 2757 -123 -228 320 C ATOM 2428 CD1 PHE A 332 12.715 -18.672 -18.323 1.00 20.58 C ANISOU 2428 CD1 PHE A 332 2325 2739 2755 -120 -247 348 C ATOM 2429 CD2 PHE A 332 15.060 -18.709 -17.903 1.00 19.61 C ANISOU 2429 CD2 PHE A 332 2267 2563 2620 -145 -209 277 C ATOM 2430 CE1 PHE A 332 12.584 -19.927 -17.717 1.00 19.84 C ANISOU 2430 CE1 PHE A 332 2210 2667 2663 -142 -247 333 C ATOM 2431 CE2 PHE A 332 14.933 -19.955 -17.293 1.00 21.37 C ANISOU 2431 CE2 PHE A 332 2468 2805 2845 -161 -209 261 C ATOM 2432 CZ PHE A 332 13.681 -20.567 -17.208 1.00 18.18 C ANISOU 2432 CZ PHE A 332 2023 2437 2447 -161 -228 289 C ATOM 2433 N THR A 333 16.079 -15.512 -17.089 1.00 19.35 N ANISOU 2433 N THR A 333 2308 2440 2605 -79 -167 272 N ATOM 2434 CA THR A 333 16.926 -15.717 -15.911 1.00 19.08 C ANISOU 2434 CA THR A 333 2284 2390 2577 -81 -143 234 C ATOM 2435 C THR A 333 16.696 -14.637 -14.861 1.00 16.92 C ANISOU 2435 C THR A 333 2029 2084 2317 -35 -123 234 C ATOM 2436 O THR A 333 16.797 -14.917 -13.659 1.00 18.32 O ANISOU 2436 O THR A 333 2199 2257 2502 -22 -106 213 O ATOM 2437 CB THR A 333 18.419 -15.780 -16.264 1.00 15.97 C ANISOU 2437 CB THR A 333 1919 1979 2167 -123 -137 206 C ATOM 2438 CG2 THR A 333 18.711 -16.919 -17.249 1.00 17.96 C ANISOU 2438 CG2 THR A 333 2160 2261 2402 -162 -150 202 C ATOM 2439 OG1 THR A 333 18.848 -14.540 -16.825 1.00 17.58 O ANISOU 2439 OG1 THR A 333 2163 2153 2365 -125 -137 217 O ATOM 2440 N GLU A 334 16.381 -13.413 -15.285 1.00 18.96 N ANISOU 2440 N GLU A 334 2315 2315 2576 -10 -126 258 N ATOM 2441 CA GLU A 334 16.106 -12.343 -14.328 1.00 20.20 C ANISOU 2441 CA GLU A 334 2499 2435 2741 39 -106 258 C ATOM 2442 C GLU A 334 14.849 -12.659 -13.524 1.00 20.69 C ANISOU 2442 C GLU A 334 2518 2523 2818 88 -96 273 C ATOM 2443 O GLU A 334 14.860 -12.611 -12.287 1.00 21.79 O ANISOU 2443 O GLU A 334 2665 2651 2964 113 -73 253 O ATOM 2444 CB GLU A 334 15.948 -10.999 -15.051 1.00 20.04 C ANISOU 2444 CB GLU A 334 2521 2378 2716 58 -113 284 C ATOM 2445 CG GLU A 334 17.242 -10.381 -15.632 1.00 24.26 C ANISOU 2445 CG GLU A 334 3107 2876 3234 12 -117 270 C ATOM 2446 CD GLU A 334 17.620 -10.935 -17.008 1.00 24.05 C ANISOU 2446 CD GLU A 334 3068 2878 3193 -37 -138 280 C ATOM 2447 OE1 GLU A 334 16.846 -11.759 -17.572 1.00 22.24 O ANISOU 2447 OE1 GLU A 334 2795 2692 2965 -36 -153 298 O ATOM 2448 OE2 GLU A 334 18.660 -10.491 -17.556 1.00 20.69 O1- ANISOU 2448 OE2 GLU A 334 2679 2431 2754 -76 -139 272 O1- ATOM 2449 N THR A 335 13.761 -13.003 -14.221 1.00 19.40 N ANISOU 2449 N THR A 335 2311 2400 2661 101 -114 310 N ATOM 2450 CA THR A 335 12.521 -13.404 -13.557 1.00 20.33 C ANISOU 2450 CA THR A 335 2376 2555 2793 142 -106 332 C ATOM 2451 C THR A 335 12.723 -14.618 -12.655 1.00 22.32 C ANISOU 2451 C THR A 335 2600 2832 3047 119 -96 304 C ATOM 2452 O THR A 335 12.176 -14.670 -11.549 1.00 20.09 O ANISOU 2452 O THR A 335 2300 2559 2775 156 -74 304 O ATOM 2453 CB THR A 335 11.448 -13.678 -14.618 1.00 22.86 C ANISOU 2453 CB THR A 335 2649 2921 3115 143 -135 379 C ATOM 2454 CG2 THR A 335 10.119 -14.122 -14.023 1.00 20.83 C ANISOU 2454 CG2 THR A 335 2328 2713 2874 181 -130 409 C ATOM 2455 OG1 THR A 335 11.259 -12.499 -15.408 1.00 21.29 O ANISOU 2455 OG1 THR A 335 2480 2697 2914 170 -144 406 O ATOM 2456 N GLN A 336 13.499 -15.602 -13.103 1.00 19.57 N ANISOU 2456 N GLN A 336 2250 2495 2690 61 -111 283 N ATOM 2457 CA GLN A 336 13.701 -16.833 -12.349 1.00 20.13 C ANISOU 2457 CA GLN A 336 2298 2588 2762 37 -105 260 C ATOM 2458 C GLN A 336 14.806 -16.724 -11.309 1.00 20.62 C ANISOU 2458 C GLN A 336 2396 2618 2822 33 -83 217 C ATOM 2459 O GLN A 336 15.074 -17.702 -10.603 1.00 19.20 O ANISOU 2459 O GLN A 336 2202 2452 2642 15 -77 197 O ATOM 2460 CB GLN A 336 14.018 -17.995 -13.307 1.00 20.22 C ANISOU 2460 CB GLN A 336 2297 2625 2761 -20 -131 256 C ATOM 2461 CG GLN A 336 12.906 -18.258 -14.333 1.00 20.36 C ANISOU 2461 CG GLN A 336 2279 2679 2777 -26 -160 298 C ATOM 2462 CD GLN A 336 11.576 -18.565 -13.674 1.00 23.78 C ANISOU 2462 CD GLN A 336 2659 3152 3226 2 -158 328 C ATOM 2463 NE2 GLN A 336 10.497 -18.020 -14.232 1.00 21.68 N ANISOU 2463 NE2 GLN A 336 2363 2909 2965 28 -172 373 N ATOM 2464 OE1 GLN A 336 11.517 -19.283 -12.662 1.00 24.44 O ANISOU 2464 OE1 GLN A 336 2725 3247 3315 1 -144 313 O ATOM 2465 N ASN A 337 15.462 -15.572 -11.221 1.00 19.23 N ANISOU 2465 N ASN A 337 2268 2398 2642 45 -73 206 N ATOM 2466 CA ASN A 337 16.572 -15.361 -10.299 1.00 19.97 C ANISOU 2466 CA ASN A 337 2399 2459 2730 34 -56 168 C ATOM 2467 C ASN A 337 17.669 -16.406 -10.516 1.00 20.89 C ANISOU 2467 C ASN A 337 2510 2589 2839 -19 -65 142 C ATOM 2468 O ASN A 337 18.196 -16.993 -9.569 1.00 18.52 O ANISOU 2468 O ASN A 337 2208 2290 2538 -28 -56 116 O ATOM 2469 CB ASN A 337 16.078 -15.349 -8.849 1.00 20.09 C ANISOU 2469 CB ASN A 337 2409 2472 2751 73 -32 159 C ATOM 2470 CG ASN A 337 16.948 -14.491 -7.953 1.00 22.64 C ANISOU 2470 CG ASN A 337 2788 2748 3066 78 -17 130 C ATOM 2471 ND2 ASN A 337 17.149 -14.925 -6.715 1.00 19.78 N ANISOU 2471 ND2 ASN A 337 2427 2387 2701 83 -2 107 N ATOM 2472 OD1 ASN A 337 17.398 -13.417 -8.367 1.00 22.38 O ANISOU 2472 OD1 ASN A 337 2801 2677 3027 77 -20 131 O ATOM 2473 N MET A 338 18.015 -16.641 -11.783 1.00 19.84 N ANISOU 2473 N MET A 338 2376 2465 2697 -52 -83 150 N ATOM 2474 CA MET A 338 19.065 -17.597 -12.101 1.00 20.24 C ANISOU 2474 CA MET A 338 2424 2528 2738 -96 -88 127 C ATOM 2475 C MET A 338 20.325 -16.878 -12.579 1.00 19.21 C ANISOU 2475 C MET A 338 2328 2373 2597 -123 -87 115 C ATOM 2476 O MET A 338 20.282 -15.739 -13.059 1.00 18.17 O ANISOU 2476 O MET A 338 2223 2217 2462 -117 -89 129 O ATOM 2477 CB MET A 338 18.632 -18.621 -13.158 1.00 16.60 C ANISOU 2477 CB MET A 338 1938 2100 2270 -118 -107 141 C ATOM 2478 CG MET A 338 17.540 -19.583 -12.685 1.00 21.02 C ANISOU 2478 CG MET A 338 2460 2689 2838 -107 -112 152 C ATOM 2479 SD MET A 338 16.743 -20.487 -14.055 1.00 27.67 S ANISOU 2479 SD MET A 338 3280 3565 3669 -135 -142 178 S ATOM 2480 CE MET A 338 18.062 -21.598 -14.468 1.00 22.32 C ANISOU 2480 CE MET A 338 2622 2885 2972 -176 -143 143 C ATOM 2481 N ILE A 339 21.465 -17.544 -12.397 1.00 15.80 N ANISOU 2481 N ILE A 339 1896 1949 2159 -152 -82 89 N ATOM 2482 CA ILE A 339 22.695 -17.079 -13.020 1.00 18.53 C ANISOU 2482 CA ILE A 339 2263 2284 2493 -184 -82 82 C ATOM 2483 C ILE A 339 22.529 -17.152 -14.529 1.00 17.29 C ANISOU 2483 C ILE A 339 2106 2140 2323 -200 -93 102 C ATOM 2484 O ILE A 339 22.003 -18.138 -15.061 1.00 16.97 O ANISOU 2484 O ILE A 339 2045 2125 2278 -202 -102 107 O ATOM 2485 CB ILE A 339 23.881 -17.939 -12.552 1.00 17.87 C ANISOU 2485 CB ILE A 339 2168 2216 2405 -206 -74 56 C ATOM 2486 CG1 ILE A 339 24.066 -17.802 -11.036 1.00 21.13 C ANISOU 2486 CG1 ILE A 339 2585 2616 2827 -193 -66 38 C ATOM 2487 CG2 ILE A 339 25.157 -17.562 -13.309 1.00 14.67 C ANISOU 2487 CG2 ILE A 339 1774 1812 1986 -241 -71 53 C ATOM 2488 CD1 ILE A 339 24.964 -18.880 -10.433 1.00 20.33 C ANISOU 2488 CD1 ILE A 339 2465 2536 2725 -206 -62 15 C ATOM 2489 N SER A 340 22.951 -16.103 -15.232 1.00 18.88 N ANISOU 2489 N SER A 340 2335 2323 2516 -214 -95 114 N ATOM 2490 CA SER A 340 22.856 -16.121 -16.686 1.00 17.05 C ANISOU 2490 CA SER A 340 2107 2102 2267 -232 -105 133 C ATOM 2491 C SER A 340 23.938 -17.017 -17.265 1.00 20.38 C ANISOU 2491 C SER A 340 2521 2550 2673 -264 -98 116 C ATOM 2492 O SER A 340 25.079 -17.039 -16.790 1.00 17.66 O ANISOU 2492 O SER A 340 2176 2207 2328 -280 -85 98 O ATOM 2493 CB SER A 340 22.988 -14.720 -17.276 1.00 19.76 C ANISOU 2493 CB SER A 340 2485 2417 2604 -239 -108 153 C ATOM 2494 OG SER A 340 22.943 -14.773 -18.698 1.00 19.12 O ANISOU 2494 OG SER A 340 2410 2349 2505 -258 -118 172 O ATOM 2495 N THR A 341 23.574 -17.767 -18.297 1.00 19.34 N ANISOU 2495 N THR A 341 2383 2440 2526 -272 -107 124 N ATOM 2496 CA THR A 341 24.577 -18.479 -19.065 1.00 17.95 C ANISOU 2496 CA THR A 341 2208 2284 2328 -297 -97 112 C ATOM 2497 C THR A 341 25.478 -17.520 -19.840 1.00 20.09 C ANISOU 2497 C THR A 341 2500 2548 2583 -322 -89 122 C ATOM 2498 O THR A 341 26.610 -17.886 -20.171 1.00 19.79 O ANISOU 2498 O THR A 341 2458 2529 2531 -342 -72 111 O ATOM 2499 CB THR A 341 23.868 -19.483 -19.987 1.00 20.07 C ANISOU 2499 CB THR A 341 2476 2571 2579 -300 -111 117 C ATOM 2500 CG2 THR A 341 24.856 -20.256 -20.873 1.00 18.69 C ANISOU 2500 CG2 THR A 341 2310 2415 2375 -320 -97 104 C ATOM 2501 OG1 THR A 341 23.101 -20.404 -19.184 1.00 20.06 O ANISOU 2501 OG1 THR A 341 2454 2576 2591 -283 -119 109 O ATOM 2502 N VAL A 342 25.023 -16.296 -20.108 1.00 19.70 N ANISOU 2502 N VAL A 342 2472 2475 2537 -322 -99 146 N ATOM 2503 CA VAL A 342 25.873 -15.295 -20.758 1.00 19.93 C ANISOU 2503 CA VAL A 342 2526 2495 2553 -350 -92 158 C ATOM 2504 C VAL A 342 26.813 -14.708 -19.709 1.00 20.85 C ANISOU 2504 C VAL A 342 2644 2597 2682 -361 -80 145 C ATOM 2505 O VAL A 342 26.356 -14.114 -18.723 1.00 19.66 O ANISOU 2505 O VAL A 342 2502 2417 2550 -342 -86 143 O ATOM 2506 CB VAL A 342 25.040 -14.194 -21.437 1.00 18.06 C ANISOU 2506 CB VAL A 342 2317 2233 2312 -345 -109 190 C ATOM 2507 CG1 VAL A 342 25.942 -13.178 -22.135 1.00 22.27 C ANISOU 2507 CG1 VAL A 342 2880 2754 2828 -380 -103 205 C ATOM 2508 CG2 VAL A 342 24.063 -14.793 -22.464 1.00 20.81 C ANISOU 2508 CG2 VAL A 342 2662 2600 2646 -337 -127 207 C ATOM 2509 N ILE A 343 28.131 -14.857 -19.934 1.00 18.64 N ANISOU 2509 N ILE A 343 2355 2338 2390 -393 -64 137 N ATOM 2510 CA ILE A 343 29.122 -14.398 -18.956 1.00 21.45 C ANISOU 2510 CA ILE A 343 2707 2688 2756 -411 -56 126 C ATOM 2511 C ILE A 343 29.056 -12.885 -18.762 1.00 18.50 C ANISOU 2511 C ILE A 343 2373 2271 2385 -426 -66 143 C ATOM 2512 O ILE A 343 29.147 -12.388 -17.633 1.00 19.18 O ANISOU 2512 O ILE A 343 2471 2333 2486 -424 -70 133 O ATOM 2513 CB ILE A 343 30.545 -14.848 -19.348 1.00 18.03 C ANISOU 2513 CB ILE A 343 2250 2294 2308 -442 -37 121 C ATOM 2514 CG1 ILE A 343 30.701 -16.363 -19.232 1.00 20.20 C ANISOU 2514 CG1 ILE A 343 2490 2603 2581 -419 -26 100 C ATOM 2515 CG2 ILE A 343 31.629 -14.101 -18.526 1.00 21.25 C ANISOU 2515 CG2 ILE A 343 2655 2698 2722 -475 -35 120 C ATOM 2516 CD1 ILE A 343 31.654 -16.943 -20.265 1.00 23.59 C ANISOU 2516 CD1 ILE A 343 2904 3073 2985 -435 -4 102 C ATOM 2517 N ASP A 344 28.924 -12.132 -19.850 1.00 19.40 N ANISOU 2517 N ASP A 344 2515 2374 2484 -443 -71 168 N ATOM 2518 CA ASP A 344 28.912 -10.670 -19.794 1.00 22.90 C ANISOU 2518 CA ASP A 344 3005 2771 2927 -460 -81 187 C ATOM 2519 C ASP A 344 27.503 -10.135 -19.512 1.00 23.48 C ANISOU 2519 C ASP A 344 3105 2804 3013 -414 -96 196 C ATOM 2520 O ASP A 344 26.914 -9.389 -20.296 1.00 25.80 O ANISOU 2520 O ASP A 344 3430 3074 3298 -409 -106 222 O ATOM 2521 CB ASP A 344 29.460 -10.088 -21.094 1.00 20.18 C ANISOU 2521 CB ASP A 344 2679 2433 2557 -499 -78 213 C ATOM 2522 CG ASP A 344 29.686 -8.576 -21.014 1.00 23.49 C ANISOU 2522 CG ASP A 344 3150 2802 2972 -528 -88 232 C ATOM 2523 OD1 ASP A 344 29.791 -8.013 -19.900 1.00 25.03 O ANISOU 2523 OD1 ASP A 344 3366 2964 3181 -528 -94 221 O ATOM 2524 OD2 ASP A 344 29.677 -7.934 -22.072 1.00 23.30 O1- ANISOU 2524 OD2 ASP A 344 3154 2768 2930 -548 -92 260 O1- ATOM 2525 N LYS A 345 26.966 -10.518 -18.358 1.00 20.05 N ANISOU 2525 N LYS A 345 2657 2362 2597 -379 -96 176 N ATOM 2526 CA LYS A 345 25.680 -10.037 -17.877 1.00 21.17 C ANISOU 2526 CA LYS A 345 2819 2471 2754 -330 -104 184 C ATOM 2527 C LYS A 345 25.755 -9.905 -16.361 1.00 22.27 C ANISOU 2527 C LYS A 345 2966 2588 2907 -315 -99 160 C ATOM 2528 O LYS A 345 26.514 -10.631 -15.715 1.00 19.47 O ANISOU 2528 O LYS A 345 2584 2258 2556 -332 -91 137 O ATOM 2529 CB LYS A 345 24.523 -10.983 -18.240 1.00 21.94 C ANISOU 2529 CB LYS A 345 2882 2598 2858 -292 -109 190 C ATOM 2530 CG LYS A 345 24.072 -10.924 -19.691 1.00 21.47 C ANISOU 2530 CG LYS A 345 2825 2549 2782 -298 -121 218 C ATOM 2531 CD LYS A 345 22.688 -11.550 -19.873 1.00 19.60 C ANISOU 2531 CD LYS A 345 2562 2332 2554 -258 -133 231 C ATOM 2532 CE LYS A 345 21.602 -10.663 -19.242 1.00 20.96 C ANISOU 2532 CE LYS A 345 2751 2470 2743 -208 -139 247 C ATOM 2533 NZ LYS A 345 20.248 -11.257 -19.433 1.00 19.56 N1+ ANISOU 2533 NZ LYS A 345 2538 2320 2575 -172 -151 266 N1+ ATOM 2534 N PRO A 346 24.974 -8.997 -15.778 1.00 23.60 N ANISOU 2534 N PRO A 346 3173 2711 3083 -279 -102 166 N ATOM 2535 CA PRO A 346 24.983 -8.845 -14.313 1.00 20.58 C ANISOU 2535 CA PRO A 346 2805 2305 2710 -262 -95 143 C ATOM 2536 C PRO A 346 24.522 -10.116 -13.603 1.00 22.11 C ANISOU 2536 C PRO A 346 2947 2538 2917 -233 -88 124 C ATOM 2537 O PRO A 346 23.859 -10.986 -14.177 1.00 20.54 O ANISOU 2537 O PRO A 346 2708 2374 2723 -216 -89 133 O ATOM 2538 CB PRO A 346 24.004 -7.685 -14.067 1.00 22.29 C ANISOU 2538 CB PRO A 346 3074 2468 2929 -216 -96 158 C ATOM 2539 CG PRO A 346 23.895 -6.968 -15.409 1.00 22.04 C ANISOU 2539 CG PRO A 346 3066 2421 2886 -229 -107 190 C ATOM 2540 CD PRO A 346 24.103 -8.022 -16.455 1.00 21.06 C ANISOU 2540 CD PRO A 346 2888 2355 2758 -253 -110 196 C ATOM 2541 N ALA A 347 24.886 -10.215 -12.290 1.00 21.85 N ANISOU 2541 N ALA A 347 2920 2495 2887 -232 -81 99 N ATOM 2542 CA ALA A 347 24.575 -11.375 -11.452 1.00 18.47 C ANISOU 2542 CA ALA A 347 2449 2099 2470 -209 -74 80 C ATOM 2543 C ALA A 347 23.253 -11.188 -10.712 1.00 21.12 C ANISOU 2543 C ALA A 347 2791 2418 2815 -149 -66 84 C ATOM 2544 O ALA A 347 22.901 -10.058 -10.336 1.00 20.02 O ANISOU 2544 O ALA A 347 2702 2232 2673 -126 -62 88 O ATOM 2545 CB ALA A 347 25.686 -11.593 -10.424 1.00 17.14 C ANISOU 2545 CB ALA A 347 2282 1932 2297 -240 -72 54 C ATOM 2546 N PRO A 348 22.521 -12.281 -10.448 1.00 19.12 N ANISOU 2546 N PRO A 348 2491 2201 2572 -123 -61 82 N ATOM 2547 CA PRO A 348 21.435 -12.216 -9.462 1.00 18.24 C ANISOU 2547 CA PRO A 348 2379 2081 2469 -70 -48 82 C ATOM 2548 C PRO A 348 21.977 -11.883 -8.073 1.00 19.55 C ANISOU 2548 C PRO A 348 2579 2219 2628 -70 -39 55 C ATOM 2549 O PRO A 348 23.171 -12.030 -7.793 1.00 17.58 O ANISOU 2549 O PRO A 348 2337 1971 2372 -115 -45 35 O ATOM 2550 CB PRO A 348 20.823 -13.627 -9.496 1.00 17.25 C ANISOU 2550 CB PRO A 348 2193 2007 2354 -61 -48 85 C ATOM 2551 CG PRO A 348 21.914 -14.520 -10.006 1.00 18.61 C ANISOU 2551 CG PRO A 348 2344 2205 2520 -110 -57 71 C ATOM 2552 CD PRO A 348 22.748 -13.657 -10.945 1.00 19.09 C ANISOU 2552 CD PRO A 348 2436 2247 2571 -144 -65 78 C ATOM 2553 N ASP A 349 21.066 -11.436 -7.195 1.00 18.53 N ANISOU 2553 N ASP A 349 2470 2070 2502 -19 -23 55 N ATOM 2554 CA ASP A 349 21.457 -10.902 -5.890 1.00 19.04 C ANISOU 2554 CA ASP A 349 2582 2098 2554 -14 -14 30 C ATOM 2555 C ASP A 349 22.387 -11.856 -5.127 1.00 20.98 C ANISOU 2555 C ASP A 349 2806 2371 2797 -52 -18 4 C ATOM 2556 O ASP A 349 23.452 -11.447 -4.646 1.00 20.01 O ANISOU 2556 O ASP A 349 2718 2225 2660 -90 -26 -15 O ATOM 2557 CB ASP A 349 20.209 -10.558 -5.045 1.00 19.27 C ANISOU 2557 CB ASP A 349 2625 2114 2584 56 9 35 C ATOM 2558 CG ASP A 349 19.116 -11.652 -5.076 1.00 25.12 C ANISOU 2558 CG ASP A 349 3295 2909 3341 88 18 52 C ATOM 2559 OD1 ASP A 349 19.411 -12.819 -5.421 1.00 25.42 O ANISOU 2559 OD1 ASP A 349 3282 2990 3386 55 7 50 O ATOM 2560 OD2 ASP A 349 17.951 -11.358 -4.695 1.00 26.98 O1- ANISOU 2560 OD2 ASP A 349 3527 3144 3580 148 38 67 O1- ATOM 2561 N TYR A 350 22.016 -13.136 -5.016 1.00 17.81 N ANISOU 2561 N TYR A 350 2346 2016 2405 -44 -15 5 N ATOM 2562 CA TYR A 350 22.834 -14.051 -4.225 1.00 19.06 C ANISOU 2562 CA TYR A 350 2486 2196 2560 -72 -18 -18 C ATOM 2563 C TYR A 350 24.226 -14.242 -4.824 1.00 18.61 C ANISOU 2563 C TYR A 350 2423 2151 2499 -129 -35 -25 C ATOM 2564 O TYR A 350 25.190 -14.427 -4.082 1.00 19.23 O ANISOU 2564 O TYR A 350 2506 2230 2569 -158 -41 -43 O ATOM 2565 CB TYR A 350 22.149 -15.404 -4.073 1.00 18.69 C ANISOU 2565 CB TYR A 350 2383 2194 2523 -55 -12 -13 C ATOM 2566 CG TYR A 350 21.822 -16.053 -5.398 1.00 20.34 C ANISOU 2566 CG TYR A 350 2551 2434 2743 -63 -22 7 C ATOM 2567 CD1 TYR A 350 22.796 -16.772 -6.098 1.00 18.43 C ANISOU 2567 CD1 TYR A 350 2289 2214 2500 -105 -34 1 C ATOM 2568 CD2 TYR A 350 20.543 -15.942 -5.955 1.00 15.38 C ANISOU 2568 CD2 TYR A 350 1905 1814 2123 -30 -18 33 C ATOM 2569 CE1 TYR A 350 22.513 -17.360 -7.316 1.00 19.48 C ANISOU 2569 CE1 TYR A 350 2393 2372 2638 -113 -42 17 C ATOM 2570 CE2 TYR A 350 20.244 -16.531 -7.175 1.00 17.77 C ANISOU 2570 CE2 TYR A 350 2175 2145 2432 -43 -31 51 C ATOM 2571 CZ TYR A 350 21.231 -17.245 -7.848 1.00 19.91 C ANISOU 2571 CZ TYR A 350 2434 2433 2699 -85 -43 41 C ATOM 2572 OH TYR A 350 20.957 -17.828 -9.062 1.00 17.24 O ANISOU 2572 OH TYR A 350 2071 2118 2360 -99 -55 57 O ATOM 2573 N LEU A 351 24.360 -14.207 -6.154 1.00 17.29 N ANISOU 2573 N LEU A 351 2240 1994 2336 -147 -43 -8 N ATOM 2574 CA LEU A 351 25.693 -14.348 -6.737 1.00 18.82 C ANISOU 2574 CA LEU A 351 2425 2202 2524 -198 -55 -12 C ATOM 2575 C LEU A 351 26.526 -13.088 -6.526 1.00 20.13 C ANISOU 2575 C LEU A 351 2641 2329 2677 -230 -62 -16 C ATOM 2576 O LEU A 351 27.710 -13.171 -6.165 1.00 18.63 O ANISOU 2576 O LEU A 351 2449 2149 2480 -272 -71 -27 O ATOM 2577 CB LEU A 351 25.600 -14.686 -8.230 1.00 18.70 C ANISOU 2577 CB LEU A 351 2383 2210 2513 -208 -58 7 C ATOM 2578 CG LEU A 351 26.967 -14.783 -8.916 1.00 18.13 C ANISOU 2578 CG LEU A 351 2300 2156 2432 -257 -65 6 C ATOM 2579 CD1 LEU A 351 27.728 -15.926 -8.292 1.00 22.61 C ANISOU 2579 CD1 LEU A 351 2833 2758 3001 -267 -63 -12 C ATOM 2580 CD2 LEU A 351 26.840 -15.015 -10.417 1.00 19.01 C ANISOU 2580 CD2 LEU A 351 2395 2287 2542 -265 -66 24 C ATOM 2581 N ALA A 352 25.935 -11.909 -6.765 1.00 17.72 N ANISOU 2581 N ALA A 352 2384 1981 2369 -214 -61 -5 N ATOM 2582 CA ALA A 352 26.651 -10.669 -6.485 1.00 18.54 C ANISOU 2582 CA ALA A 352 2548 2040 2458 -246 -70 -9 C ATOM 2583 C ALA A 352 27.086 -10.622 -5.029 1.00 20.37 C ANISOU 2583 C ALA A 352 2805 2257 2679 -254 -72 -34 C ATOM 2584 O ALA A 352 28.189 -10.172 -4.712 1.00 19.57 O ANISOU 2584 O ALA A 352 2727 2144 2565 -305 -87 -42 O ATOM 2585 CB ALA A 352 25.776 -9.459 -6.822 1.00 18.96 C ANISOU 2585 CB ALA A 352 2655 2041 2507 -214 -66 6 C ATOM 2586 N GLU A 353 26.235 -11.121 -4.135 1.00 19.97 N ANISOU 2586 N GLU A 353 2746 2209 2631 -207 -58 -44 N ATOM 2587 CA GLU A 353 26.569 -11.199 -2.718 1.00 20.45 C ANISOU 2587 CA GLU A 353 2830 2261 2680 -210 -59 -68 C ATOM 2588 C GLU A 353 27.792 -12.093 -2.480 1.00 20.73 C ANISOU 2588 C GLU A 353 2822 2338 2714 -258 -73 -77 C ATOM 2589 O GLU A 353 28.756 -11.684 -1.818 1.00 18.49 O ANISOU 2589 O GLU A 353 2567 2042 2415 -300 -89 -89 O ATOM 2590 CB GLU A 353 25.333 -11.709 -1.972 1.00 22.84 C ANISOU 2590 CB GLU A 353 3121 2569 2987 -148 -37 -72 C ATOM 2591 CG GLU A 353 25.395 -11.702 -0.486 1.00 29.24 C ANISOU 2591 CG GLU A 353 3964 3364 3781 -139 -32 -95 C ATOM 2592 CD GLU A 353 24.150 -12.341 0.152 1.00 25.81 C ANISOU 2592 CD GLU A 353 3508 2947 3353 -78 -7 -94 C ATOM 2593 OE1 GLU A 353 23.187 -12.712 -0.580 1.00 29.19 O ANISOU 2593 OE1 GLU A 353 3895 3397 3798 -44 4 -74 O ATOM 2594 OE2 GLU A 353 24.149 -12.479 1.389 1.00 25.56 O1- ANISOU 2594 OE2 GLU A 353 3498 2909 3306 -68 -1 -112 O1- ATOM 2595 N LEU A 354 27.772 -13.325 -3.012 1.00 20.74 N ANISOU 2595 N LEU A 354 2758 2390 2731 -252 -70 -71 N ATOM 2596 CA LEU A 354 28.950 -14.199 -2.945 1.00 21.85 C ANISOU 2596 CA LEU A 354 2855 2574 2873 -289 -82 -76 C ATOM 2597 C LEU A 354 30.206 -13.467 -3.402 1.00 20.09 C ANISOU 2597 C LEU A 354 2645 2349 2642 -348 -98 -70 C ATOM 2598 O LEU A 354 31.249 -13.489 -2.729 1.00 19.20 O ANISOU 2598 O LEU A 354 2530 2247 2519 -386 -114 -78 O ATOM 2599 CB LEU A 354 28.735 -15.426 -3.828 1.00 18.20 C ANISOU 2599 CB LEU A 354 2333 2156 2426 -274 -74 -67 C ATOM 2600 CG LEU A 354 27.823 -16.540 -3.337 1.00 20.43 C ANISOU 2600 CG LEU A 354 2588 2458 2717 -233 -63 -71 C ATOM 2601 CD1 LEU A 354 27.832 -17.672 -4.358 1.00 17.15 C ANISOU 2601 CD1 LEU A 354 2123 2081 2311 -231 -61 -62 C ATOM 2602 CD2 LEU A 354 28.263 -17.031 -1.950 1.00 18.22 C ANISOU 2602 CD2 LEU A 354 2309 2185 2430 -235 -67 -89 C ATOM 2603 N GLU A 355 30.126 -12.821 -4.568 1.00 20.66 N ANISOU 2603 N GLU A 355 2726 2408 2715 -359 -97 -53 N ATOM 2604 CA GLU A 355 31.290 -12.132 -5.095 1.00 19.81 C ANISOU 2604 CA GLU A 355 2626 2301 2598 -418 -111 -43 C ATOM 2605 C GLU A 355 31.705 -10.971 -4.208 1.00 22.16 C ANISOU 2605 C GLU A 355 2989 2553 2878 -452 -128 -51 C ATOM 2606 O GLU A 355 32.902 -10.710 -4.060 1.00 22.65 O ANISOU 2606 O GLU A 355 3047 2627 2930 -510 -146 -48 O ATOM 2607 CB GLU A 355 31.007 -11.674 -6.524 1.00 20.16 C ANISOU 2607 CB GLU A 355 2674 2340 2646 -421 -106 -21 C ATOM 2608 CG GLU A 355 31.020 -12.824 -7.465 1.00 23.29 C ANISOU 2608 CG GLU A 355 3008 2788 3054 -408 -95 -13 C ATOM 2609 CD GLU A 355 30.790 -12.429 -8.895 1.00 31.58 C ANISOU 2609 CD GLU A 355 4061 3836 4103 -413 -91 8 C ATOM 2610 OE1 GLU A 355 29.831 -11.680 -9.178 1.00 30.84 O ANISOU 2610 OE1 GLU A 355 4005 3702 4009 -389 -89 17 O ATOM 2611 OE2 GLU A 355 31.597 -12.859 -9.741 1.00 38.78 O1- ANISOU 2611 OE2 GLU A 355 4936 4786 5011 -440 -88 18 O1- ATOM 2612 N SER A 356 30.752 -10.271 -3.587 1.00 20.09 N ANISOU 2612 N SER A 356 2787 2237 2609 -417 -122 -61 N ATOM 2613 CA SER A 356 31.176 -9.211 -2.684 1.00 21.71 C ANISOU 2613 CA SER A 356 3064 2393 2791 -450 -138 -72 C ATOM 2614 C SER A 356 31.809 -9.758 -1.410 1.00 21.61 C ANISOU 2614 C SER A 356 3041 2400 2769 -468 -151 -91 C ATOM 2615 O SER A 356 32.472 -9.007 -0.693 1.00 20.13 O ANISOU 2615 O SER A 356 2905 2184 2560 -513 -171 -99 O ATOM 2616 CB SER A 356 30.001 -8.298 -2.356 1.00 20.26 C ANISOU 2616 CB SER A 356 2954 2144 2599 -400 -125 -78 C ATOM 2617 OG SER A 356 29.224 -8.869 -1.323 1.00 24.68 O ANISOU 2617 OG SER A 356 3512 2706 3159 -348 -110 -96 O ATOM 2618 N ALA A 357 31.675 -11.050 -1.139 1.00 22.06 N ANISOU 2618 N ALA A 357 3036 2507 2840 -439 -141 -96 N ATOM 2619 CA ALA A 357 32.363 -11.668 -0.013 1.00 21.37 C ANISOU 2619 CA ALA A 357 2932 2445 2743 -457 -155 -110 C ATOM 2620 C ALA A 357 33.741 -12.208 -0.386 1.00 22.17 C ANISOU 2620 C ALA A 357 2972 2602 2849 -510 -173 -97 C ATOM 2621 O ALA A 357 34.391 -12.830 0.459 1.00 22.75 O ANISOU 2621 O ALA A 357 3021 2706 2917 -524 -186 -104 O ATOM 2622 CB ALA A 357 31.497 -12.796 0.577 1.00 22.77 C ANISOU 2622 CB ALA A 357 3079 2643 2930 -398 -136 -120 C ATOM 2623 N GLY A 358 34.203 -11.986 -1.624 1.00 21.85 N ANISOU 2623 N GLY A 358 2906 2579 2817 -536 -172 -77 N ATOM 2624 CA GLY A 358 35.507 -12.441 -2.067 1.00 21.59 C ANISOU 2624 CA GLY A 358 2813 2603 2787 -582 -184 -61 C ATOM 2625 C GLY A 358 35.544 -13.846 -2.619 1.00 20.74 C ANISOU 2625 C GLY A 358 2629 2553 2698 -546 -166 -57 C ATOM 2626 O GLY A 358 36.639 -14.356 -2.885 1.00 23.74 O ANISOU 2626 O GLY A 358 2953 2985 3080 -573 -172 -44 O ATOM 2627 N VAL A 359 34.385 -14.477 -2.815 1.00 20.59 N ANISOU 2627 N VAL A 359 2607 2526 2691 -487 -145 -65 N ATOM 2628 CA VAL A 359 34.268 -15.881 -3.198 1.00 22.21 C ANISOU 2628 CA VAL A 359 2754 2775 2911 -450 -130 -64 C ATOM 2629 C VAL A 359 34.480 -16.025 -4.702 1.00 22.32 C ANISOU 2629 C VAL A 359 2736 2812 2930 -455 -117 -47 C ATOM 2630 O VAL A 359 33.961 -15.232 -5.493 1.00 20.06 O ANISOU 2630 O VAL A 359 2480 2498 2643 -458 -112 -38 O ATOM 2631 CB VAL A 359 32.881 -16.425 -2.786 1.00 19.07 C ANISOU 2631 CB VAL A 359 2370 2357 2520 -392 -115 -77 C ATOM 2632 CG1 VAL A 359 32.723 -17.909 -3.168 1.00 19.48 C ANISOU 2632 CG1 VAL A 359 2370 2448 2584 -359 -103 -76 C ATOM 2633 CG2 VAL A 359 32.613 -16.171 -1.302 1.00 19.09 C ANISOU 2633 CG2 VAL A 359 2410 2332 2511 -386 -124 -93 C ATOM 2634 N GLU A 360 35.229 -17.051 -5.102 1.00 21.27 N ANISOU 2634 N GLU A 360 2547 2732 2803 -452 -111 -41 N ATOM 2635 CA GLU A 360 35.454 -17.393 -6.501 1.00 23.08 C ANISOU 2635 CA GLU A 360 2747 2989 3035 -450 -94 -27 C ATOM 2636 C GLU A 360 34.513 -18.509 -6.930 1.00 23.72 C ANISOU 2636 C GLU A 360 2816 3073 3123 -398 -78 -35 C ATOM 2637 O GLU A 360 34.157 -19.380 -6.131 1.00 22.93 O ANISOU 2637 O GLU A 360 2708 2975 3028 -368 -78 -47 O ATOM 2638 CB GLU A 360 36.909 -17.822 -6.706 1.00 23.46 C ANISOU 2638 CB GLU A 360 2741 3093 3079 -475 -94 -15 C ATOM 2639 CG GLU A 360 37.821 -16.632 -6.800 1.00 29.88 C ANISOU 2639 CG GLU A 360 3560 3908 3883 -537 -108 2 C ATOM 2640 CD GLU A 360 39.239 -16.994 -7.216 1.00 34.50 C ANISOU 2640 CD GLU A 360 4085 4559 4466 -564 -104 22 C ATOM 2641 OE1 GLU A 360 39.434 -17.971 -7.973 1.00 33.84 O ANISOU 2641 OE1 GLU A 360 3961 4513 4385 -531 -81 25 O ATOM 2642 OE2 GLU A 360 40.158 -16.261 -6.790 1.00 43.04 O1- ANISOU 2642 OE2 GLU A 360 5160 5654 5541 -618 -124 35 O1- ATOM 2643 N LEU A 361 34.109 -18.481 -8.200 1.00 21.32 N ANISOU 2643 N LEU A 361 2514 2769 2818 -391 -65 -25 N ATOM 2644 CA LEU A 361 33.137 -19.444 -8.705 1.00 21.24 C ANISOU 2644 CA LEU A 361 2499 2758 2811 -350 -54 -30 C ATOM 2645 C LEU A 361 33.818 -20.649 -9.340 1.00 23.22 C ANISOU 2645 C LEU A 361 2712 3051 3058 -337 -40 -30 C ATOM 2646 O LEU A 361 34.834 -20.516 -10.020 1.00 22.72 O ANISOU 2646 O LEU A 361 2628 3018 2988 -358 -32 -19 O ATOM 2647 CB LEU A 361 32.203 -18.783 -9.719 1.00 22.82 C ANISOU 2647 CB LEU A 361 2728 2933 3010 -348 -51 -20 C ATOM 2648 CG LEU A 361 31.511 -17.523 -9.203 1.00 23.39 C ANISOU 2648 CG LEU A 361 2842 2960 3084 -353 -61 -18 C ATOM 2649 CD1 LEU A 361 30.592 -17.021 -10.285 1.00 24.69 C ANISOU 2649 CD1 LEU A 361 3028 3105 3247 -345 -59 -3 C ATOM 2650 CD2 LEU A 361 30.741 -17.834 -7.900 1.00 21.12 C ANISOU 2650 CD2 LEU A 361 2565 2655 2805 -324 -65 -33 C ATOM 2651 N LEU A 362 33.240 -21.830 -9.125 1.00 21.11 N ANISOU 2651 N LEU A 362 2440 2786 2795 -302 -36 -41 N ATOM 2652 CA LEU A 362 33.787 -23.067 -9.660 1.00 21.68 C ANISOU 2652 CA LEU A 362 2487 2890 2861 -282 -23 -44 C ATOM 2653 C LEU A 362 32.672 -23.841 -10.358 1.00 20.71 C ANISOU 2653 C LEU A 362 2382 2752 2734 -257 -18 -48 C ATOM 2654 O LEU A 362 31.644 -24.152 -9.742 1.00 19.25 O ANISOU 2654 O LEU A 362 2212 2546 2558 -242 -27 -55 O ATOM 2655 CB LEU A 362 34.426 -23.900 -8.541 1.00 20.56 C ANISOU 2655 CB LEU A 362 2323 2766 2724 -266 -26 -53 C ATOM 2656 CG LEU A 362 34.901 -25.297 -8.931 1.00 20.07 C ANISOU 2656 CG LEU A 362 2241 2728 2655 -234 -11 -57 C ATOM 2657 CD1 LEU A 362 36.040 -25.206 -9.940 1.00 20.62 C ANISOU 2657 CD1 LEU A 362 2285 2835 2714 -242 7 -45 C ATOM 2658 CD2 LEU A 362 35.330 -26.060 -7.699 1.00 21.08 C ANISOU 2658 CD2 LEU A 362 2354 2867 2790 -216 -19 -64 C ATOM 2659 N GLU A 363 32.853 -24.110 -11.653 1.00 22.80 N ANISOU 2659 N GLU A 363 2648 3031 2986 -257 -5 -43 N ATOM 2660 CA GLU A 363 32.052 -25.107 -12.360 1.00 19.80 C ANISOU 2660 CA GLU A 363 2285 2642 2596 -236 -2 -49 C ATOM 2661 C GLU A 363 32.739 -26.458 -12.245 1.00 22.46 C ANISOU 2661 C GLU A 363 2611 2998 2926 -209 10 -60 C ATOM 2662 O GLU A 363 33.963 -26.551 -12.390 1.00 22.24 O ANISOU 2662 O GLU A 363 2558 3000 2892 -207 25 -57 O ATOM 2663 CB GLU A 363 31.882 -24.745 -13.838 1.00 20.53 C ANISOU 2663 CB GLU A 363 2392 2736 2671 -249 5 -38 C ATOM 2664 CG GLU A 363 31.097 -23.450 -14.084 1.00 23.15 C ANISOU 2664 CG GLU A 363 2741 3045 3008 -270 -8 -24 C ATOM 2665 CD GLU A 363 31.016 -23.099 -15.566 1.00 22.54 C ANISOU 2665 CD GLU A 363 2679 2973 2912 -284 -2 -11 C ATOM 2666 OE1 GLU A 363 31.366 -23.961 -16.402 1.00 24.54 O ANISOU 2666 OE1 GLU A 363 2936 3243 3146 -276 12 -16 O ATOM 2667 OE2 GLU A 363 30.621 -21.962 -15.901 1.00 22.11 O1- ANISOU 2667 OE2 GLU A 363 2639 2903 2860 -303 -10 3 O1- ATOM 2668 N THR A 364 31.962 -27.506 -11.966 1.00 17.91 N ANISOU 2668 N THR A 364 2050 2405 2348 -189 4 -70 N ATOM 2669 CA THR A 364 32.544 -28.838 -11.894 1.00 20.57 C ANISOU 2669 CA THR A 364 2387 2752 2676 -160 14 -81 C ATOM 2670 C THR A 364 32.367 -29.541 -13.232 1.00 24.14 C ANISOU 2670 C THR A 364 2867 3201 3105 -152 26 -84 C ATOM 2671 O THR A 364 31.539 -29.152 -14.059 1.00 21.26 O ANISOU 2671 O THR A 364 2522 2823 2731 -170 19 -79 O ATOM 2672 CB THR A 364 31.919 -29.688 -10.773 1.00 19.18 C ANISOU 2672 CB THR A 364 2220 2557 2510 -145 1 -89 C ATOM 2673 CG2 THR A 364 32.176 -29.068 -9.385 1.00 20.57 C ANISOU 2673 CG2 THR A 364 2373 2737 2705 -151 -9 -87 C ATOM 2674 OG1 THR A 364 30.514 -29.830 -10.989 1.00 20.55 O ANISOU 2674 OG1 THR A 364 2420 2706 2684 -154 -13 -88 O ATOM 2675 N ASN A 365 33.201 -30.597 -13.452 1.00 26.45 N ANISOU 2675 N ASN A 365 3161 3505 3383 -121 44 -93 N ATOM 2676 CA ASN A 365 33.179 -31.395 -14.676 1.00 21.11 C ANISOU 2676 CA ASN A 365 2520 2824 2678 -107 59 -100 C ATOM 2677 C ASN A 365 32.376 -32.671 -14.499 1.00 24.18 C ANISOU 2677 C ASN A 365 2949 3180 3057 -93 47 -113 C ATOM 2678 O ASN A 365 32.368 -33.264 -13.418 1.00 25.70 O ANISOU 2678 O ASN A 365 3137 3364 3263 -78 39 -118 O ATOM 2679 CB ASN A 365 34.594 -31.766 -15.112 1.00 20.84 C ANISOU 2679 CB ASN A 365 2468 2822 2629 -77 91 -102 C ATOM 2680 CG ASN A 365 35.449 -30.550 -15.400 1.00 26.39 C ANISOU 2680 CG ASN A 365 3130 3561 3336 -98 104 -85 C ATOM 2681 ND2 ASN A 365 36.758 -30.671 -15.167 1.00 23.16 N ANISOU 2681 ND2 ASN A 365 2681 3191 2929 -76 125 -79 N ATOM 2682 OD1 ASN A 365 34.943 -29.521 -15.866 1.00 24.82 O ANISOU 2682 OD1 ASN A 365 2934 3357 3138 -133 94 -76 O ATOM 2683 N PRO A 366 31.692 -33.126 -15.549 1.00 24.89 N ANISOU 2683 N PRO A 366 3083 3250 3122 -101 43 -118 N ATOM 2684 CA PRO A 366 31.113 -34.470 -15.513 1.00 24.93 C ANISOU 2684 CA PRO A 366 3136 3224 3112 -90 33 -131 C ATOM 2685 C PRO A 366 32.222 -35.509 -15.488 1.00 28.42 C ANISOU 2685 C PRO A 366 3591 3669 3539 -43 59 -144 C ATOM 2686 O PRO A 366 33.368 -35.247 -15.859 1.00 25.72 O ANISOU 2686 O PRO A 366 3224 3357 3190 -20 88 -143 O ATOM 2687 CB PRO A 366 30.310 -34.552 -16.812 1.00 27.48 C ANISOU 2687 CB PRO A 366 3503 3532 3407 -114 24 -131 C ATOM 2688 CG PRO A 366 31.026 -33.630 -17.741 1.00 28.57 C ANISOU 2688 CG PRO A 366 3624 3698 3535 -117 46 -124 C ATOM 2689 CD PRO A 366 31.577 -32.503 -16.881 1.00 24.79 C ANISOU 2689 CD PRO A 366 3084 3245 3089 -121 50 -112 C ATOM 2690 N ALA A 367 31.861 -36.698 -15.023 1.00 24.92 N ANISOU 2690 N ALA A 367 3185 3195 3090 -28 49 -154 N ATOM 2691 CA ALA A 367 32.788 -37.814 -14.983 1.00 27.68 C ANISOU 2691 CA ALA A 367 3557 3539 3423 23 72 -167 C ATOM 2692 C ALA A 367 33.341 -38.101 -16.382 1.00 30.39 C ANISOU 2692 C ALA A 367 3935 3885 3728 43 101 -176 C ATOM 2693 O ALA A 367 32.694 -37.802 -17.395 1.00 31.90 O ANISOU 2693 O ALA A 367 4155 4067 3899 12 94 -177 O ATOM 2694 CB ALA A 367 32.081 -39.049 -14.422 1.00 24.79 C ANISOU 2694 CB ALA A 367 3241 3128 3050 26 52 -176 C ATOM 2695 N PRO A 368 34.550 -38.656 -16.473 1.00 32.38 N ANISOU 2695 N PRO A 368 4183 4151 3968 98 134 -182 N ATOM 2696 CA PRO A 368 35.120 -38.969 -17.787 1.00 30.98 C ANISOU 2696 CA PRO A 368 4042 3979 3751 125 168 -192 C ATOM 2697 C PRO A 368 34.325 -40.051 -18.505 1.00 29.13 C ANISOU 2697 C PRO A 368 3901 3689 3477 122 158 -211 C ATOM 2698 O PRO A 368 33.572 -40.818 -17.897 1.00 26.42 O ANISOU 2698 O PRO A 368 3595 3305 3137 112 130 -217 O ATOM 2699 CB PRO A 368 36.535 -39.455 -17.454 1.00 34.34 C ANISOU 2699 CB PRO A 368 4439 4433 4177 192 205 -191 C ATOM 2700 CG PRO A 368 36.765 -39.119 -16.032 1.00 32.73 C ANISOU 2700 CG PRO A 368 4173 4248 4015 190 187 -177 C ATOM 2701 CD PRO A 368 35.440 -39.070 -15.375 1.00 28.84 C ANISOU 2701 CD PRO A 368 3700 3719 3540 141 144 -179 C ATOM 2702 N GLU A 369 34.510 -40.104 -19.827 1.00 30.18 N ANISOU 2702 N GLU A 369 4074 3822 3570 128 181 -220 N ATOM 2703 CA GLU A 369 33.814 -41.083 -20.650 1.00 30.06 C ANISOU 2703 CA GLU A 369 4157 3755 3511 121 171 -239 C ATOM 2704 C GLU A 369 34.113 -42.486 -20.150 1.00 27.73 C ANISOU 2704 C GLU A 369 3915 3419 3202 172 178 -256 C ATOM 2705 O GLU A 369 35.260 -42.815 -19.845 1.00 27.00 O ANISOU 2705 O GLU A 369 3800 3347 3113 236 214 -257 O ATOM 2706 CB GLU A 369 34.225 -40.949 -22.119 1.00 30.31 C ANISOU 2706 CB GLU A 369 4223 3796 3495 132 203 -247 C ATOM 2707 CG GLU A 369 33.485 -41.901 -23.051 1.00 29.59 C ANISOU 2707 CG GLU A 369 4241 3649 3352 118 189 -269 C ATOM 2708 CD GLU A 369 33.683 -41.557 -24.529 1.00 36.00 C ANISOU 2708 CD GLU A 369 5088 4474 4117 114 213 -274 C ATOM 2709 OE1 GLU A 369 34.361 -40.553 -24.830 1.00 36.05 O ANISOU 2709 OE1 GLU A 369 5030 4533 4134 119 240 -259 O ATOM 2710 OE2 GLU A 369 33.164 -42.302 -25.388 1.00 36.28 O1- ANISOU 2710 OE2 GLU A 369 5217 4465 4102 102 204 -292 O1- ATOM 2711 N GLY A 370 33.072 -43.302 -20.044 1.00 27.20 N ANISOU 2711 N GLY A 370 3917 3296 3121 141 143 -266 N ATOM 2712 CA GLY A 370 33.196 -44.627 -19.482 1.00 28.77 C ANISOU 2712 CA GLY A 370 4175 3449 3309 179 142 -279 C ATOM 2713 C GLY A 370 33.034 -44.684 -17.982 1.00 29.74 C ANISOU 2713 C GLY A 370 4250 3574 3478 176 120 -266 C ATOM 2714 O GLY A 370 32.860 -45.778 -17.430 1.00 27.41 O ANISOU 2714 O GLY A 370 4007 3232 3174 192 108 -273 O ATOM 2715 N LYS A 371 33.090 -43.545 -17.303 1.00 28.46 N ANISOU 2715 N LYS A 371 3995 3460 3360 154 113 -246 N ATOM 2716 CA LYS A 371 32.896 -43.504 -15.863 1.00 27.73 C ANISOU 2716 CA LYS A 371 3858 3372 3308 147 91 -233 C ATOM 2717 C LYS A 371 31.699 -42.641 -15.502 1.00 28.51 C ANISOU 2717 C LYS A 371 3922 3479 3433 76 53 -218 C ATOM 2718 O LYS A 371 31.637 -42.110 -14.386 1.00 24.35 O ANISOU 2718 O LYS A 371 3335 2973 2943 67 41 -204 O ATOM 2719 CB LYS A 371 34.158 -42.988 -15.168 1.00 28.64 C ANISOU 2719 CB LYS A 371 3893 3538 3451 194 118 -222 C ATOM 2720 CG LYS A 371 35.461 -43.697 -15.563 1.00 30.12 C ANISOU 2720 CG LYS A 371 4097 3732 3616 272 161 -231 C ATOM 2721 CD LYS A 371 36.599 -43.257 -14.625 1.00 32.00 C ANISOU 2721 CD LYS A 371 4249 4023 3887 310 178 -213 C ATOM 2722 CE LYS A 371 37.950 -43.909 -14.945 1.00 36.65 C ANISOU 2722 CE LYS A 371 4838 4630 4457 394 223 -216 C ATOM 2723 NZ LYS A 371 37.900 -45.393 -14.890 1.00 34.00 N1+ ANISOU 2723 NZ LYS A 371 4589 4235 4094 443 226 -232 N1+ ATOM 2724 N GLU A 372 30.759 -42.464 -16.438 1.00 27.84 N ANISOU 2724 N GLU A 372 3872 3379 3327 28 34 -220 N ATOM 2725 CA GLU A 372 29.648 -41.544 -16.192 1.00 27.60 C ANISOU 2725 CA GLU A 372 3802 3363 3321 -32 2 -202 C ATOM 2726 C GLU A 372 28.848 -41.959 -14.968 1.00 26.84 C ANISOU 2726 C GLU A 372 3700 3249 3248 -55 -28 -193 C ATOM 2727 O GLU A 372 28.372 -41.110 -14.206 1.00 28.51 O ANISOU 2727 O GLU A 372 3853 3485 3493 -79 -41 -176 O ATOM 2728 CB GLU A 372 28.726 -41.459 -17.408 1.00 28.78 C ANISOU 2728 CB GLU A 372 3995 3498 3440 -79 -17 -202 C ATOM 2729 CG GLU A 372 29.337 -40.746 -18.593 1.00 28.79 C ANISOU 2729 CG GLU A 372 3991 3526 3423 -68 8 -206 C ATOM 2730 CD GLU A 372 30.104 -41.668 -19.491 1.00 29.71 C ANISOU 2730 CD GLU A 372 4176 3619 3493 -27 37 -228 C ATOM 2731 OE1 GLU A 372 30.292 -42.846 -19.132 1.00 32.39 O ANISOU 2731 OE1 GLU A 372 4567 3922 3818 1 40 -242 O ATOM 2732 OE2 GLU A 372 30.517 -41.213 -20.571 1.00 34.58 O1- ANISOU 2732 OE2 GLU A 372 4799 4254 4085 -22 59 -231 O1- ATOM 2733 N ASN A 373 28.696 -43.258 -14.750 1.00 28.17 N ANISOU 2733 N ASN A 373 3933 3373 3396 -46 -36 -202 N ATOM 2734 CA ASN A 373 27.825 -43.722 -13.687 1.00 28.15 C ANISOU 2734 CA ASN A 373 3933 3351 3411 -75 -66 -191 C ATOM 2735 C ASN A 373 28.616 -44.337 -12.537 1.00 26.68 C ANISOU 2735 C ASN A 373 3741 3157 3238 -28 -53 -194 C ATOM 2736 O ASN A 373 28.024 -44.940 -11.639 1.00 26.99 O ANISOU 2736 O ASN A 373 3794 3174 3285 -46 -75 -186 O ATOM 2737 CB ASN A 373 26.807 -44.709 -14.267 1.00 34.00 C ANISOU 2737 CB ASN A 373 4756 4045 4118 -119 -96 -194 C ATOM 2738 CG ASN A 373 25.878 -44.046 -15.299 1.00 32.12 C ANISOU 2738 CG ASN A 373 4515 3820 3868 -173 -116 -186 C ATOM 2739 ND2 ASN A 373 25.751 -44.667 -16.466 1.00 38.63 N ANISOU 2739 ND2 ASN A 373 5416 4614 4649 -186 -122 -200 N ATOM 2740 OD1 ASN A 373 25.296 -42.997 -15.046 1.00 33.77 O ANISOU 2740 OD1 ASN A 373 4658 4065 4106 -202 -127 -167 O ATOM 2741 N LEU A 374 29.938 -44.160 -12.524 1.00 24.74 N ANISOU 2741 N LEU A 374 3469 2934 2996 31 -20 -201 N ATOM 2742 CA LEU A 374 30.776 -44.867 -11.562 1.00 25.97 C ANISOU 2742 CA LEU A 374 3625 3082 3160 83 -8 -202 C ATOM 2743 C LEU A 374 30.451 -44.447 -10.132 1.00 25.23 C ANISOU 2743 C LEU A 374 3476 3007 3102 64 -26 -185 C ATOM 2744 O LEU A 374 30.299 -45.297 -9.238 1.00 21.50 O ANISOU 2744 O LEU A 374 3031 2508 2632 71 -39 -182 O ATOM 2745 CB LEU A 374 32.257 -44.617 -11.869 1.00 23.75 C ANISOU 2745 CB LEU A 374 3311 2834 2877 146 31 -208 C ATOM 2746 CG LEU A 374 33.190 -45.313 -10.873 1.00 22.20 C ANISOU 2746 CG LEU A 374 3108 2637 2691 205 42 -205 C ATOM 2747 CD1 LEU A 374 32.917 -46.816 -10.874 1.00 28.16 C ANISOU 2747 CD1 LEU A 374 3957 3326 3416 224 34 -216 C ATOM 2748 CD2 LEU A 374 34.636 -45.026 -11.212 1.00 23.02 C ANISOU 2748 CD2 LEU A 374 3170 2783 2794 266 81 -205 C ATOM 2749 N LEU A 375 30.354 -43.133 -9.894 1.00 22.42 N ANISOU 2749 N LEU A 375 3049 2696 2774 41 -27 -174 N ATOM 2750 CA LEU A 375 30.034 -42.652 -8.549 1.00 19.42 C ANISOU 2750 CA LEU A 375 2621 2334 2425 25 -42 -160 C ATOM 2751 C LEU A 375 28.674 -43.169 -8.076 1.00 22.25 C ANISOU 2751 C LEU A 375 3010 2663 2782 -21 -71 -151 C ATOM 2752 O LEU A 375 28.543 -43.611 -6.930 1.00 20.66 O ANISOU 2752 O LEU A 375 2808 2453 2590 -19 -81 -143 O ATOM 2753 CB LEU A 375 30.098 -41.126 -8.500 1.00 21.46 C ANISOU 2753 CB LEU A 375 2809 2637 2707 7 -37 -151 C ATOM 2754 CG LEU A 375 29.889 -40.515 -7.109 1.00 20.63 C ANISOU 2754 CG LEU A 375 2658 2552 2630 -5 -49 -139 C ATOM 2755 CD1 LEU A 375 31.007 -40.929 -6.164 1.00 18.89 C ANISOU 2755 CD1 LEU A 375 2422 2340 2416 38 -41 -139 C ATOM 2756 CD2 LEU A 375 29.834 -38.980 -7.205 1.00 18.87 C ANISOU 2756 CD2 LEU A 375 2380 2364 2426 -27 -46 -132 C ATOM 2757 N ARG A 376 27.656 -43.145 -8.942 1.00 25.09 N ANISOU 2757 N ARG A 376 3396 3010 3128 -65 -86 -149 N ATOM 2758 CA ARG A 376 26.356 -43.696 -8.551 1.00 25.34 C ANISOU 2758 CA ARG A 376 3453 3018 3156 -113 -115 -137 C ATOM 2759 C ARG A 376 26.459 -45.179 -8.231 1.00 24.51 C ANISOU 2759 C ARG A 376 3417 2864 3030 -101 -122 -142 C ATOM 2760 O ARG A 376 25.865 -45.651 -7.255 1.00 25.33 O ANISOU 2760 O ARG A 376 3527 2957 3141 -121 -139 -129 O ATOM 2761 CB ARG A 376 25.296 -43.482 -9.644 1.00 30.51 C ANISOU 2761 CB ARG A 376 4126 3670 3797 -164 -133 -132 C ATOM 2762 CG ARG A 376 23.896 -43.095 -9.103 1.00 35.43 C ANISOU 2762 CG ARG A 376 4716 4308 4436 -217 -158 -107 C ATOM 2763 CD ARG A 376 23.098 -42.161 -10.033 1.00 38.62 C ANISOU 2763 CD ARG A 376 5094 4737 4842 -253 -169 -96 C ATOM 2764 NE ARG A 376 23.466 -40.745 -9.988 1.00 42.78 N ANISOU 2764 NE ARG A 376 5557 5303 5393 -234 -151 -94 N ATOM 2765 CZ ARG A 376 22.807 -39.802 -9.318 1.00 42.61 C ANISOU 2765 CZ ARG A 376 5480 5312 5399 -247 -154 -75 C ATOM 2766 NH1 ARG A 376 21.757 -40.091 -8.554 1.00 40.75 N1+ ANISOU 2766 NH1 ARG A 376 5234 5078 5171 -276 -171 -56 N1+ ATOM 2767 NH2 ARG A 376 23.203 -38.533 -9.424 1.00 36.86 N ANISOU 2767 NH2 ARG A 376 4707 4610 4687 -231 -139 -76 N ATOM 2768 N GLU A 377 27.211 -45.932 -9.046 1.00 25.47 N ANISOU 2768 N GLU A 377 3597 2957 3124 -65 -109 -161 N ATOM 2769 CA GLU A 377 27.329 -47.375 -8.840 1.00 25.93 C ANISOU 2769 CA GLU A 377 3734 2961 3158 -49 -115 -168 C ATOM 2770 C GLU A 377 27.979 -47.687 -7.501 1.00 25.31 C ANISOU 2770 C GLU A 377 3635 2885 3097 -10 -109 -161 C ATOM 2771 O GLU A 377 27.542 -48.595 -6.788 1.00 24.82 O ANISOU 2771 O GLU A 377 3614 2787 3028 -23 -126 -153 O ATOM 2772 CB GLU A 377 28.136 -48.000 -9.982 1.00 25.36 C ANISOU 2772 CB GLU A 377 3725 2859 3051 -6 -94 -191 C ATOM 2773 CG GLU A 377 27.568 -47.698 -11.360 1.00 28.85 C ANISOU 2773 CG GLU A 377 4193 3298 3470 -45 -101 -199 C ATOM 2774 CD GLU A 377 28.279 -48.418 -12.483 1.00 38.73 C ANISOU 2774 CD GLU A 377 5521 4515 4680 -4 -80 -223 C ATOM 2775 OE1 GLU A 377 27.625 -48.721 -13.509 1.00 44.59 O ANISOU 2775 OE1 GLU A 377 6324 5230 5389 -43 -95 -231 O ATOM 2776 OE2 GLU A 377 29.500 -48.670 -12.337 1.00 36.28 O1- ANISOU 2776 OE2 GLU A 377 5209 4208 4368 69 -47 -233 O1- ATOM 2777 N ILE A 378 29.043 -46.964 -7.153 1.00 24.34 N ANISOU 2777 N ILE A 378 3450 2803 2995 37 -85 -163 N ATOM 2778 CA ILE A 378 29.704 -47.216 -5.875 1.00 24.05 C ANISOU 2778 CA ILE A 378 3391 2773 2973 74 -82 -154 C ATOM 2779 C ILE A 378 28.780 -46.825 -4.729 1.00 21.56 C ANISOU 2779 C ILE A 378 3041 2472 2680 27 -104 -135 C ATOM 2780 O ILE A 378 28.580 -47.588 -3.778 1.00 21.95 O ANISOU 2780 O ILE A 378 3115 2497 2726 26 -117 -126 O ATOM 2781 CB ILE A 378 31.048 -46.468 -5.810 1.00 21.01 C ANISOU 2781 CB ILE A 378 2944 2436 2605 127 -56 -157 C ATOM 2782 CG1 ILE A 378 32.049 -47.075 -6.801 1.00 24.55 C ANISOU 2782 CG1 ILE A 378 3429 2869 3028 184 -30 -172 C ATOM 2783 CG2 ILE A 378 31.617 -46.485 -4.373 1.00 21.17 C ANISOU 2783 CG2 ILE A 378 2925 2473 2644 152 -60 -143 C ATOM 2784 CD1 ILE A 378 33.106 -46.092 -7.240 1.00 23.68 C ANISOU 2784 CD1 ILE A 378 3252 2815 2931 216 -3 -173 C ATOM 2785 N SER A 379 28.176 -45.641 -4.832 1.00 20.50 N ANISOU 2785 N SER A 379 2851 2374 2563 -11 -107 -129 N ATOM 2786 CA SER A 379 27.232 -45.167 -3.826 1.00 24.56 C ANISOU 2786 CA SER A 379 3330 2906 3096 -52 -122 -112 C ATOM 2787 C SER A 379 26.070 -46.142 -3.624 1.00 25.05 C ANISOU 2787 C SER A 379 3444 2932 3144 -96 -145 -100 C ATOM 2788 O SER A 379 25.714 -46.469 -2.483 1.00 22.87 O ANISOU 2788 O SER A 379 3166 2652 2873 -107 -155 -86 O ATOM 2789 CB SER A 379 26.715 -43.791 -4.233 1.00 20.28 C ANISOU 2789 CB SER A 379 2733 2403 2571 -80 -119 -108 C ATOM 2790 OG SER A 379 25.677 -43.403 -3.354 1.00 28.93 O ANISOU 2790 OG SER A 379 3800 3512 3679 -117 -131 -90 O ATOM 2791 N ASP A 380 25.433 -46.582 -4.718 1.00 23.02 N ANISOU 2791 N ASP A 380 3233 2649 2866 -128 -157 -104 N ATOM 2792 CA ASP A 380 24.379 -47.589 -4.593 1.00 25.66 C ANISOU 2792 CA ASP A 380 3620 2946 3182 -176 -182 -91 C ATOM 2793 C ASP A 380 24.916 -48.855 -3.936 1.00 25.41 C ANISOU 2793 C ASP A 380 3650 2870 3136 -148 -185 -93 C ATOM 2794 O ASP A 380 24.275 -49.419 -3.044 1.00 24.93 O ANISOU 2794 O ASP A 380 3604 2795 3074 -177 -201 -75 O ATOM 2795 CB ASP A 380 23.756 -47.919 -5.965 1.00 23.77 C ANISOU 2795 CB ASP A 380 3430 2684 2918 -215 -197 -97 C ATOM 2796 CG ASP A 380 22.906 -46.768 -6.536 1.00 32.91 C ANISOU 2796 CG ASP A 380 4530 3884 4089 -255 -203 -86 C ATOM 2797 OD1 ASP A 380 22.555 -45.839 -5.773 1.00 36.11 O ANISOU 2797 OD1 ASP A 380 4866 4332 4523 -261 -199 -71 O ATOM 2798 OD2 ASP A 380 22.584 -46.780 -7.752 1.00 33.88 O1- ANISOU 2798 OD2 ASP A 380 4681 3998 4193 -279 -213 -92 O1- ATOM 2799 N THR A 381 26.099 -49.310 -4.357 1.00 23.45 N ANISOU 2799 N THR A 381 3436 2599 2875 -88 -167 -113 N ATOM 2800 CA THR A 381 26.653 -50.550 -3.820 1.00 25.15 C ANISOU 2800 CA THR A 381 3715 2767 3074 -52 -169 -115 C ATOM 2801 C THR A 381 27.020 -50.397 -2.354 1.00 26.76 C ANISOU 2801 C THR A 381 3876 2994 3299 -30 -167 -100 C ATOM 2802 O THR A 381 26.830 -51.326 -1.557 1.00 23.04 O ANISOU 2802 O THR A 381 3448 2488 2818 -35 -181 -88 O ATOM 2803 CB THR A 381 27.877 -50.979 -4.633 1.00 28.05 C ANISOU 2803 CB THR A 381 4122 3113 3423 17 -146 -138 C ATOM 2804 CG2 THR A 381 28.581 -52.196 -4.003 1.00 25.24 C ANISOU 2804 CG2 THR A 381 3827 2711 3053 69 -144 -138 C ATOM 2805 OG1 THR A 381 27.486 -51.265 -5.982 1.00 27.17 O ANISOU 2805 OG1 THR A 381 4067 2972 3284 -6 -149 -152 O ATOM 2806 N ALA A 382 27.560 -49.235 -1.986 1.00 25.34 N ANISOU 2806 N ALA A 382 3613 2869 3144 -8 -152 -100 N ATOM 2807 CA ALA A 382 27.947 -48.985 -0.607 1.00 26.46 C ANISOU 2807 CA ALA A 382 3714 3036 3304 11 -151 -87 C ATOM 2808 C ALA A 382 26.753 -48.770 0.310 1.00 26.17 C ANISOU 2808 C ALA A 382 3657 3010 3275 -47 -167 -67 C ATOM 2809 O ALA A 382 26.922 -48.804 1.532 1.00 24.38 O ANISOU 2809 O ALA A 382 3415 2794 3055 -37 -170 -54 O ATOM 2810 CB ALA A 382 28.870 -47.761 -0.535 1.00 23.83 C ANISOU 2810 CB ALA A 382 3303 2757 2993 44 -133 -93 C ATOM 2811 N GLN A 383 25.560 -48.529 -0.238 1.00 27.13 N ANISOU 2811 N GLN A 383 3779 3134 3395 -104 -177 -61 N ATOM 2812 CA GLN A 383 24.426 -48.064 0.556 1.00 25.40 C ANISOU 2812 CA GLN A 383 3522 2941 3187 -154 -186 -39 C ATOM 2813 C GLN A 383 24.768 -46.772 1.305 1.00 26.85 C ANISOU 2813 C GLN A 383 3631 3177 3395 -135 -171 -38 C ATOM 2814 O GLN A 383 24.275 -46.520 2.408 1.00 25.94 O ANISOU 2814 O GLN A 383 3490 3080 3286 -151 -172 -23 O ATOM 2815 CB GLN A 383 23.952 -49.153 1.526 1.00 29.53 C ANISOU 2815 CB GLN A 383 4091 3434 3697 -176 -201 -20 C ATOM 2816 CG GLN A 383 23.738 -50.516 0.850 1.00 33.82 C ANISOU 2816 CG GLN A 383 4723 3916 4213 -193 -218 -22 C ATOM 2817 CD GLN A 383 22.899 -51.466 1.676 1.00 40.51 C ANISOU 2817 CD GLN A 383 5611 4736 5046 -238 -238 3 C ATOM 2818 NE2 GLN A 383 21.593 -51.253 1.688 1.00 40.23 N ANISOU 2818 NE2 GLN A 383 5553 4721 5013 -305 -250 25 N ATOM 2819 OE1 GLN A 383 23.424 -52.380 2.303 1.00 43.94 O ANISOU 2819 OE1 GLN A 383 6094 5133 5467 -213 -242 6 O ATOM 2820 N ILE A 384 25.644 -45.954 0.733 1.00 23.99 N ANISOU 2820 N ILE A 384 3235 2836 3043 -101 -156 -55 N ATOM 2821 CA ILE A 384 25.903 -44.602 1.212 1.00 21.33 C ANISOU 2821 CA ILE A 384 2833 2545 2727 -92 -144 -56 C ATOM 2822 C ILE A 384 25.222 -43.685 0.204 1.00 23.62 C ANISOU 2822 C ILE A 384 3095 2854 3025 -120 -140 -59 C ATOM 2823 O ILE A 384 25.738 -43.451 -0.897 1.00 20.87 O ANISOU 2823 O ILE A 384 2750 2506 2676 -106 -134 -73 O ATOM 2824 CB ILE A 384 27.406 -44.317 1.356 1.00 22.04 C ANISOU 2824 CB ILE A 384 2903 2649 2822 -40 -133 -69 C ATOM 2825 CG1 ILE A 384 28.031 -45.264 2.399 1.00 22.08 C ANISOU 2825 CG1 ILE A 384 2934 2636 2818 -11 -140 -62 C ATOM 2826 CG2 ILE A 384 27.652 -42.853 1.714 1.00 20.99 C ANISOU 2826 CG2 ILE A 384 2709 2560 2708 -40 -124 -71 C ATOM 2827 CD1 ILE A 384 29.564 -45.319 2.373 1.00 20.27 C ANISOU 2827 CD1 ILE A 384 2692 2417 2591 46 -132 -71 C ATOM 2828 N ASP A 385 24.027 -43.210 0.546 1.00 19.48 N ANISOU 2828 N ASP A 385 2548 2347 2508 -158 -144 -43 N ATOM 2829 CA ASP A 385 23.154 -42.566 -0.437 1.00 20.10 C ANISOU 2829 CA ASP A 385 2607 2439 2591 -189 -146 -38 C ATOM 2830 C ASP A 385 23.501 -41.081 -0.529 1.00 22.19 C ANISOU 2830 C ASP A 385 2820 2737 2873 -172 -131 -45 C ATOM 2831 O ASP A 385 22.945 -40.238 0.172 1.00 19.32 O ANISOU 2831 O ASP A 385 2420 2398 2521 -179 -125 -35 O ATOM 2832 CB ASP A 385 21.688 -42.832 -0.090 1.00 21.10 C ANISOU 2832 CB ASP A 385 2731 2571 2715 -236 -158 -13 C ATOM 2833 CG ASP A 385 21.298 -42.374 1.317 1.00 21.72 C ANISOU 2833 CG ASP A 385 2775 2674 2803 -235 -148 1 C ATOM 2834 OD1 ASP A 385 22.111 -42.488 2.260 1.00 22.31 O ANISOU 2834 OD1 ASP A 385 2855 2745 2877 -206 -142 -6 O ATOM 2835 OD2 ASP A 385 20.123 -41.981 1.499 1.00 23.92 O1- ANISOU 2835 OD2 ASP A 385 3025 2976 3087 -264 -148 22 O1- ATOM 2836 N LEU A 386 24.424 -40.758 -1.444 1.00 20.45 N ANISOU 2836 N LEU A 386 2601 2518 2654 -150 -124 -62 N ATOM 2837 CA LEU A 386 24.963 -39.400 -1.546 1.00 20.81 C ANISOU 2837 CA LEU A 386 2604 2591 2714 -134 -111 -70 C ATOM 2838 C LEU A 386 23.896 -38.373 -1.905 1.00 21.46 C ANISOU 2838 C LEU A 386 2657 2691 2806 -160 -111 -58 C ATOM 2839 O LEU A 386 23.995 -37.204 -1.498 1.00 17.37 O ANISOU 2839 O LEU A 386 2105 2193 2300 -152 -101 -59 O ATOM 2840 CB LEU A 386 26.091 -39.378 -2.582 1.00 19.83 C ANISOU 2840 CB LEU A 386 2487 2464 2585 -110 -103 -86 C ATOM 2841 CG LEU A 386 27.307 -40.230 -2.227 1.00 22.19 C ANISOU 2841 CG LEU A 386 2805 2752 2875 -73 -99 -95 C ATOM 2842 CD1 LEU A 386 28.328 -40.168 -3.343 1.00 19.34 C ANISOU 2842 CD1 LEU A 386 2445 2394 2507 -48 -86 -108 C ATOM 2843 CD2 LEU A 386 27.911 -39.744 -0.903 1.00 20.41 C ANISOU 2843 CD2 LEU A 386 2548 2545 2660 -57 -97 -93 C ATOM 2844 N TRP A 387 22.880 -38.781 -2.662 1.00 21.91 N ANISOU 2844 N TRP A 387 2727 2741 2856 -190 -123 -47 N ATOM 2845 CA TRP A 387 21.803 -37.901 -3.098 1.00 22.11 C ANISOU 2845 CA TRP A 387 2724 2787 2891 -213 -125 -32 C ATOM 2846 C TRP A 387 20.501 -38.165 -2.354 1.00 22.71 C ANISOU 2846 C TRP A 387 2786 2873 2969 -238 -131 -7 C ATOM 2847 O TRP A 387 19.451 -37.677 -2.779 1.00 23.48 O ANISOU 2847 O TRP A 387 2860 2989 3072 -259 -136 12 O ATOM 2848 CB TRP A 387 21.575 -38.060 -4.603 1.00 20.51 C ANISOU 2848 CB TRP A 387 2538 2577 2677 -231 -136 -32 C ATOM 2849 CG TRP A 387 22.803 -37.752 -5.382 1.00 23.67 C ANISOU 2849 CG TRP A 387 2948 2973 3074 -206 -125 -54 C ATOM 2850 CD1 TRP A 387 23.236 -36.523 -5.785 1.00 25.17 C ANISOU 2850 CD1 TRP A 387 3111 3180 3274 -194 -114 -58 C ATOM 2851 CD2 TRP A 387 23.782 -38.693 -5.826 1.00 23.18 C ANISOU 2851 CD2 TRP A 387 2925 2887 2994 -188 -123 -71 C ATOM 2852 CE2 TRP A 387 24.780 -37.965 -6.503 1.00 27.83 C ANISOU 2852 CE2 TRP A 387 3502 3487 3584 -166 -108 -84 C ATOM 2853 CE3 TRP A 387 23.909 -40.089 -5.717 1.00 25.02 C ANISOU 2853 CE3 TRP A 387 3206 3090 3210 -187 -130 -76 C ATOM 2854 NE1 TRP A 387 24.416 -36.642 -6.469 1.00 26.51 N ANISOU 2854 NE1 TRP A 387 3294 3343 3434 -173 -104 -76 N ATOM 2855 CZ2 TRP A 387 25.896 -38.578 -7.078 1.00 27.98 C ANISOU 2855 CZ2 TRP A 387 3548 3494 3589 -139 -97 -101 C ATOM 2856 CZ3 TRP A 387 25.019 -40.703 -6.286 1.00 26.18 C ANISOU 2856 CZ3 TRP A 387 3386 3219 3341 -157 -121 -95 C ATOM 2857 CH2 TRP A 387 26.003 -39.944 -6.957 1.00 25.31 C ANISOU 2857 CH2 TRP A 387 3256 3126 3233 -131 -103 -107 C ATOM 2858 N GLY A 388 20.541 -38.938 -1.270 1.00 22.38 N ANISOU 2858 N GLY A 388 2759 2823 2922 -237 -131 -4 N ATOM 2859 CA GLY A 388 19.376 -39.214 -0.456 1.00 18.08 C ANISOU 2859 CA GLY A 388 2200 2291 2378 -262 -134 21 C ATOM 2860 C GLY A 388 19.628 -38.821 0.995 1.00 20.08 C ANISOU 2860 C GLY A 388 2438 2556 2637 -238 -117 20 C ATOM 2861 O GLY A 388 20.624 -38.169 1.318 1.00 19.68 O ANISOU 2861 O GLY A 388 2382 2504 2590 -207 -106 1 O ATOM 2862 N PRO A 389 18.733 -39.232 1.902 1.00 18.73 N ANISOU 2862 N PRO A 389 2259 2396 2461 -256 -116 42 N ATOM 2863 CA PRO A 389 18.773 -38.718 3.282 1.00 19.03 C ANISOU 2863 CA PRO A 389 2282 2449 2501 -235 -97 44 C ATOM 2864 C PRO A 389 19.304 -39.664 4.350 1.00 20.94 C ANISOU 2864 C PRO A 389 2554 2673 2729 -231 -100 41 C ATOM 2865 O PRO A 389 19.625 -39.220 5.460 1.00 21.62 O ANISOU 2865 O PRO A 389 2635 2768 2812 -211 -86 37 O ATOM 2866 CB PRO A 389 17.297 -38.426 3.558 1.00 19.74 C ANISOU 2866 CB PRO A 389 2336 2570 2593 -256 -88 75 C ATOM 2867 CG PRO A 389 16.587 -39.538 2.801 1.00 20.88 C ANISOU 2867 CG PRO A 389 2495 2708 2731 -301 -111 94 C ATOM 2868 CD PRO A 389 17.427 -39.845 1.581 1.00 20.34 C ANISOU 2868 CD PRO A 389 2458 2610 2661 -300 -129 72 C ATOM 2869 N LEU A 390 19.389 -40.959 4.041 1.00 18.66 N ANISOU 2869 N LEU A 390 2303 2358 2429 -251 -118 45 N ATOM 2870 CA LEU A 390 19.474 -41.979 5.090 1.00 20.51 C ANISOU 2870 CA LEU A 390 2567 2577 2648 -257 -123 54 C ATOM 2871 C LEU A 390 20.809 -41.949 5.837 1.00 19.75 C ANISOU 2871 C LEU A 390 2486 2469 2548 -218 -119 34 C ATOM 2872 O LEU A 390 20.835 -41.971 7.073 1.00 19.98 O ANISOU 2872 O LEU A 390 2516 2505 2569 -211 -112 40 O ATOM 2873 CB LEU A 390 19.231 -43.361 4.484 1.00 19.18 C ANISOU 2873 CB LEU A 390 2443 2376 2467 -289 -145 63 C ATOM 2874 CG LEU A 390 17.859 -43.560 3.811 1.00 21.06 C ANISOU 2874 CG LEU A 390 2669 2629 2705 -340 -156 88 C ATOM 2875 CD1 LEU A 390 17.714 -44.994 3.314 1.00 17.24 C ANISOU 2875 CD1 LEU A 390 2242 2104 2202 -376 -181 95 C ATOM 2876 CD2 LEU A 390 16.699 -43.195 4.733 1.00 17.12 C ANISOU 2876 CD2 LEU A 390 2128 2169 2208 -360 -142 119 C ATOM 2877 N TYR A 391 21.936 -41.951 5.124 1.00 19.30 N ANISOU 2877 N TYR A 391 2443 2396 2496 -192 -125 11 N ATOM 2878 CA TYR A 391 23.198 -42.051 5.858 1.00 20.45 C ANISOU 2878 CA TYR A 391 2598 2534 2636 -157 -125 -2 C ATOM 2879 C TYR A 391 23.500 -40.766 6.614 1.00 19.94 C ANISOU 2879 C TYR A 391 2499 2498 2578 -141 -112 -9 C ATOM 2880 O TYR A 391 24.136 -40.812 7.675 1.00 20.14 O ANISOU 2880 O TYR A 391 2531 2525 2595 -124 -113 -11 O ATOM 2881 CB TYR A 391 24.352 -42.448 4.925 1.00 20.56 C ANISOU 2881 CB TYR A 391 2631 2529 2652 -131 -132 -20 C ATOM 2882 CG TYR A 391 25.177 -41.324 4.333 1.00 18.47 C ANISOU 2882 CG TYR A 391 2334 2284 2400 -109 -123 -38 C ATOM 2883 CD1 TYR A 391 24.878 -40.809 3.073 1.00 19.28 C ANISOU 2883 CD1 TYR A 391 2425 2390 2510 -120 -119 -44 C ATOM 2884 CD2 TYR A 391 26.292 -40.819 4.998 1.00 17.56 C ANISOU 2884 CD2 TYR A 391 2203 2183 2287 -81 -121 -47 C ATOM 2885 CE1 TYR A 391 25.631 -39.795 2.514 1.00 17.84 C ANISOU 2885 CE1 TYR A 391 2216 2225 2338 -103 -111 -57 C ATOM 2886 CE2 TYR A 391 27.056 -39.800 4.440 1.00 18.70 C ANISOU 2886 CE2 TYR A 391 2317 2345 2442 -68 -115 -60 C ATOM 2887 CZ TYR A 391 26.720 -39.295 3.198 1.00 18.26 C ANISOU 2887 CZ TYR A 391 2252 2292 2394 -79 -109 -65 C ATOM 2888 OH TYR A 391 27.474 -38.286 2.645 1.00 16.90 O ANISOU 2888 OH TYR A 391 2052 2137 2230 -70 -103 -76 O ATOM 2889 N ARG A 392 23.007 -39.623 6.130 1.00 17.46 N ANISOU 2889 N ARG A 392 2154 2203 2276 -146 -101 -12 N ATOM 2890 CA ARG A 392 23.200 -38.384 6.885 1.00 19.72 C ANISOU 2890 CA ARG A 392 2417 2509 2565 -132 -88 -19 C ATOM 2891 C ARG A 392 22.211 -38.272 8.039 1.00 20.28 C ANISOU 2891 C ARG A 392 2486 2594 2626 -142 -75 -3 C ATOM 2892 O ARG A 392 22.552 -37.714 9.093 1.00 16.54 O ANISOU 2892 O ARG A 392 2013 2129 2144 -129 -68 -9 O ATOM 2893 CB ARG A 392 23.084 -37.176 5.958 1.00 17.68 C ANISOU 2893 CB ARG A 392 2134 2263 2321 -131 -80 -28 C ATOM 2894 CG ARG A 392 24.192 -37.120 4.947 1.00 19.98 C ANISOU 2894 CG ARG A 392 2426 2546 2619 -119 -88 -44 C ATOM 2895 CD ARG A 392 24.096 -35.912 4.045 1.00 23.84 C ANISOU 2895 CD ARG A 392 2893 3045 3121 -120 -80 -50 C ATOM 2896 NE ARG A 392 25.045 -36.006 2.940 1.00 18.90 N ANISOU 2896 NE ARG A 392 2268 2413 2499 -113 -86 -62 N ATOM 2897 CZ ARG A 392 24.724 -36.356 1.702 1.00 20.20 C ANISOU 2897 CZ ARG A 392 2437 2571 2666 -123 -89 -61 C ATOM 2898 NH1 ARG A 392 23.473 -36.626 1.359 1.00 19.74 N1+ ANISOU 2898 NH1 ARG A 392 2380 2512 2607 -144 -91 -46 N1+ ATOM 2899 NH2 ARG A 392 25.680 -36.437 0.782 1.00 19.91 N ANISOU 2899 NH2 ARG A 392 2404 2531 2629 -112 -90 -72 N ATOM 2900 N GLN A 393 20.998 -38.804 7.872 1.00 18.83 N ANISOU 2900 N GLN A 393 2298 2415 2441 -167 -72 19 N ATOM 2901 CA GLN A 393 20.108 -38.958 9.023 1.00 21.70 C ANISOU 2901 CA GLN A 393 2659 2793 2792 -177 -59 39 C ATOM 2902 C GLN A 393 20.775 -39.794 10.110 1.00 18.83 C ANISOU 2902 C GLN A 393 2328 2416 2411 -172 -68 39 C ATOM 2903 O GLN A 393 20.685 -39.466 11.296 1.00 18.65 O ANISOU 2903 O GLN A 393 2307 2405 2373 -164 -56 42 O ATOM 2904 CB GLN A 393 18.772 -39.584 8.593 1.00 19.39 C ANISOU 2904 CB GLN A 393 2355 2510 2501 -211 -59 67 C ATOM 2905 CG GLN A 393 17.798 -38.589 7.930 1.00 20.84 C ANISOU 2905 CG GLN A 393 2498 2722 2699 -213 -45 77 C ATOM 2906 CD GLN A 393 16.541 -39.242 7.360 1.00 19.05 C ANISOU 2906 CD GLN A 393 2255 2509 2474 -253 -52 108 C ATOM 2907 NE2 GLN A 393 15.476 -38.453 7.195 1.00 15.80 N ANISOU 2907 NE2 GLN A 393 1800 2131 2071 -253 -36 127 N ATOM 2908 OE1 GLN A 393 16.525 -40.440 7.088 1.00 19.54 O ANISOU 2908 OE1 GLN A 393 2344 2552 2529 -282 -73 116 O ATOM 2909 N LYS A 394 21.465 -40.870 9.718 1.00 20.38 N ANISOU 2909 N LYS A 394 2553 2586 2605 -173 -89 36 N ATOM 2910 CA LYS A 394 22.198 -41.681 10.694 1.00 19.11 C ANISOU 2910 CA LYS A 394 2424 2410 2428 -163 -100 37 C ATOM 2911 C LYS A 394 23.293 -40.870 11.379 1.00 18.95 C ANISOU 2911 C LYS A 394 2398 2399 2404 -133 -100 19 C ATOM 2912 O LYS A 394 23.473 -40.973 12.602 1.00 19.78 O ANISOU 2912 O LYS A 394 2516 2508 2491 -128 -100 24 O ATOM 2913 CB LYS A 394 22.780 -42.921 10.016 1.00 16.47 C ANISOU 2913 CB LYS A 394 2123 2042 2092 -161 -121 36 C ATOM 2914 CG LYS A 394 23.676 -43.789 10.913 1.00 22.52 C ANISOU 2914 CG LYS A 394 2924 2790 2844 -142 -135 39 C ATOM 2915 CD LYS A 394 22.945 -44.411 12.093 1.00 25.09 C ANISOU 2915 CD LYS A 394 3269 3115 3149 -163 -133 63 C ATOM 2916 CE LYS A 394 21.938 -45.456 11.659 1.00 28.54 C ANISOU 2916 CE LYS A 394 3731 3533 3581 -201 -139 84 C ATOM 2917 NZ LYS A 394 21.558 -46.320 12.834 1.00 34.72 N1+ ANISOU 2917 NZ LYS A 394 4544 4306 4341 -219 -142 109 N1+ ATOM 2918 N LEU A 395 24.049 -40.075 10.605 1.00 17.01 N ANISOU 2918 N LEU A 395 2133 2157 2173 -117 -102 -1 N ATOM 2919 CA LEU A 395 25.055 -39.191 11.198 1.00 17.86 C ANISOU 2919 CA LEU A 395 2233 2276 2278 -98 -104 -17 C ATOM 2920 C LEU A 395 24.437 -38.240 12.213 1.00 17.18 C ANISOU 2920 C LEU A 395 2141 2206 2179 -102 -87 -16 C ATOM 2921 O LEU A 395 25.010 -38.005 13.282 1.00 16.23 O ANISOU 2921 O LEU A 395 2034 2091 2042 -95 -92 -20 O ATOM 2922 CB LEU A 395 25.774 -38.387 10.107 1.00 18.70 C ANISOU 2922 CB LEU A 395 2317 2387 2402 -88 -106 -34 C ATOM 2923 CG LEU A 395 26.776 -39.140 9.241 1.00 20.32 C ANISOU 2923 CG LEU A 395 2526 2581 2615 -73 -120 -39 C ATOM 2924 CD1 LEU A 395 27.442 -38.179 8.239 1.00 17.63 C ANISOU 2924 CD1 LEU A 395 2159 2251 2290 -66 -117 -55 C ATOM 2925 CD2 LEU A 395 27.825 -39.839 10.124 1.00 17.24 C ANISOU 2925 CD2 LEU A 395 2150 2187 2212 -53 -137 -36 C ATOM 2926 N VAL A 396 23.263 -37.683 11.894 1.00 16.55 N ANISOU 2926 N VAL A 396 2046 2136 2106 -112 -67 -10 N ATOM 2927 CA VAL A 396 22.587 -36.783 12.821 1.00 16.93 C ANISOU 2927 CA VAL A 396 2093 2200 2141 -109 -45 -8 C ATOM 2928 C VAL A 396 22.198 -37.515 14.097 1.00 17.49 C ANISOU 2928 C VAL A 396 2185 2274 2186 -115 -40 8 C ATOM 2929 O VAL A 396 22.376 -36.996 15.206 1.00 18.06 O ANISOU 2929 O VAL A 396 2273 2353 2238 -107 -33 2 O ATOM 2930 CB VAL A 396 21.358 -36.148 12.145 1.00 19.49 C ANISOU 2930 CB VAL A 396 2391 2537 2478 -113 -22 0 C ATOM 2931 CG1 VAL A 396 20.371 -35.660 13.206 1.00 19.25 C ANISOU 2931 CG1 VAL A 396 2360 2524 2429 -108 6 11 C ATOM 2932 CG2 VAL A 396 21.786 -35.005 11.215 1.00 17.93 C ANISOU 2932 CG2 VAL A 396 2179 2337 2298 -103 -22 -18 C ATOM 2933 N ASP A 397 21.655 -38.728 13.963 1.00 18.94 N ANISOU 2933 N ASP A 397 2374 2452 2369 -133 -45 29 N ATOM 2934 CA ASP A 397 21.253 -39.484 15.144 1.00 18.99 C ANISOU 2934 CA ASP A 397 2402 2462 2351 -143 -41 48 C ATOM 2935 C ASP A 397 22.458 -39.849 16.003 1.00 18.29 C ANISOU 2935 C ASP A 397 2343 2361 2245 -130 -62 40 C ATOM 2936 O ASP A 397 22.383 -39.805 17.233 1.00 19.17 O ANISOU 2936 O ASP A 397 2472 2480 2331 -129 -55 45 O ATOM 2937 CB ASP A 397 20.479 -40.734 14.725 1.00 17.51 C ANISOU 2937 CB ASP A 397 2218 2267 2167 -171 -47 74 C ATOM 2938 CG ASP A 397 19.130 -40.384 14.092 1.00 21.42 C ANISOU 2938 CG ASP A 397 2680 2785 2676 -189 -26 90 C ATOM 2939 OD1 ASP A 397 18.504 -39.390 14.528 1.00 22.41 O ANISOU 2939 OD1 ASP A 397 2784 2935 2797 -177 1 91 O ATOM 2940 OD2 ASP A 397 18.701 -41.081 13.161 1.00 19.26 O1- ANISOU 2940 OD2 ASP A 397 2401 2502 2413 -212 -38 102 O1- ATOM 2941 N ILE A 398 23.585 -40.206 15.382 1.00 18.31 N ANISOU 2941 N ILE A 398 2349 2347 2260 -119 -87 28 N ATOM 2942 CA ILE A 398 24.783 -40.490 16.173 1.00 16.88 C ANISOU 2942 CA ILE A 398 2189 2161 2065 -104 -109 23 C ATOM 2943 C ILE A 398 25.254 -39.230 16.888 1.00 19.21 C ANISOU 2943 C ILE A 398 2480 2472 2347 -95 -106 6 C ATOM 2944 O ILE A 398 25.564 -39.255 18.086 1.00 18.59 O ANISOU 2944 O ILE A 398 2424 2398 2242 -94 -113 10 O ATOM 2945 CB ILE A 398 25.892 -41.090 15.291 1.00 18.53 C ANISOU 2945 CB ILE A 398 2396 2355 2291 -87 -133 17 C ATOM 2946 CG1 ILE A 398 25.478 -42.476 14.784 1.00 18.22 C ANISOU 2946 CG1 ILE A 398 2378 2290 2254 -95 -139 33 C ATOM 2947 CG2 ILE A 398 27.199 -41.183 16.053 1.00 20.63 C ANISOU 2947 CG2 ILE A 398 2671 2624 2543 -68 -157 14 C ATOM 2948 CD1 ILE A 398 26.371 -43.026 13.711 1.00 20.53 C ANISOU 2948 CD1 ILE A 398 2673 2566 2564 -75 -154 25 C ATOM 2949 N ALA A 399 25.292 -38.109 16.169 1.00 15.32 N ANISOU 2949 N ALA A 399 1964 1985 1870 -92 -97 -11 N ATOM 2950 CA ALA A 399 25.800 -36.866 16.742 1.00 18.31 C ANISOU 2950 CA ALA A 399 2347 2373 2237 -88 -97 -29 C ATOM 2951 C ALA A 399 24.960 -36.392 17.924 1.00 19.26 C ANISOU 2951 C ALA A 399 2489 2500 2328 -91 -74 -26 C ATOM 2952 O ALA A 399 25.499 -35.802 18.869 1.00 17.26 O ANISOU 2952 O ALA A 399 2258 2250 2050 -90 -82 -37 O ATOM 2953 CB ALA A 399 25.854 -35.775 15.665 1.00 15.88 C ANISOU 2953 CB ALA A 399 2015 2066 1952 -87 -90 -46 C ATOM 2954 N ARG A 400 23.649 -36.623 17.899 1.00 18.21 N ANISOU 2954 N ARG A 400 2350 2373 2195 -95 -46 -11 N ATOM 2955 CA ARG A 400 22.788 -36.154 18.979 1.00 18.60 C ANISOU 2955 CA ARG A 400 2418 2434 2216 -93 -17 -7 C ATOM 2956 C ARG A 400 22.567 -37.193 20.076 1.00 21.80 C ANISOU 2956 C ARG A 400 2847 2843 2594 -101 -18 14 C ATOM 2957 O ARG A 400 21.811 -36.928 21.018 1.00 22.90 O ANISOU 2957 O ARG A 400 3002 2995 2705 -99 9 21 O ATOM 2958 CB ARG A 400 21.438 -35.698 18.408 1.00 19.20 C ANISOU 2958 CB ARG A 400 2468 2523 2306 -89 18 2 C ATOM 2959 CG ARG A 400 20.514 -36.821 17.995 1.00 20.91 C ANISOU 2959 CG ARG A 400 2664 2748 2535 -106 24 31 C ATOM 2960 CD ARG A 400 19.468 -36.328 16.965 1.00 18.43 C ANISOU 2960 CD ARG A 400 2311 2446 2245 -105 46 39 C ATOM 2961 NE ARG A 400 18.531 -37.369 16.553 1.00 19.40 N ANISOU 2961 NE ARG A 400 2414 2579 2377 -129 48 70 N ATOM 2962 CZ ARG A 400 17.395 -37.663 17.179 1.00 21.94 C ANISOU 2962 CZ ARG A 400 2726 2926 2685 -138 74 97 C ATOM 2963 NH1 ARG A 400 16.991 -36.985 18.248 1.00 19.98 N1+ ANISOU 2963 NH1 ARG A 400 2486 2694 2410 -119 105 97 N1+ ATOM 2964 NH2 ARG A 400 16.633 -38.653 16.710 1.00 20.56 N ANISOU 2964 NH2 ARG A 400 2533 2759 2519 -169 69 126 N ATOM 2965 N GLY A 401 23.195 -38.364 19.983 1.00 22.09 N ANISOU 2965 N GLY A 401 2891 2869 2635 -109 -47 25 N ATOM 2966 CA GLY A 401 23.050 -39.383 21.006 1.00 21.84 C ANISOU 2966 CA GLY A 401 2886 2836 2576 -118 -52 47 C ATOM 2967 C GLY A 401 21.862 -40.303 20.840 1.00 26.62 C ANISOU 2967 C GLY A 401 3485 3445 3185 -137 -34 76 C ATOM 2968 O GLY A 401 21.544 -41.057 21.771 1.00 25.69 O ANISOU 2968 O GLY A 401 3392 3329 3041 -148 -32 97 O ATOM 2969 N ALA A 402 21.186 -40.261 19.694 1.00 23.90 N ANISOU 2969 N ALA A 402 3109 3102 2869 -144 -24 79 N ATOM 2970 CA ALA A 402 20.111 -41.202 19.418 1.00 23.87 C ANISOU 2970 CA ALA A 402 3098 3102 2870 -170 -15 109 C ATOM 2971 C ALA A 402 20.628 -42.540 18.884 1.00 27.38 C ANISOU 2971 C ALA A 402 3562 3517 3324 -183 -47 118 C ATOM 2972 O ALA A 402 19.829 -43.465 18.668 1.00 23.10 O ANISOU 2972 O ALA A 402 3024 2971 2783 -212 -47 144 O ATOM 2973 CB ALA A 402 19.129 -40.570 18.434 1.00 21.45 C ANISOU 2973 CB ALA A 402 2749 2813 2588 -175 7 111 C ATOM 2974 N ALA A 403 21.942 -42.661 18.683 1.00 24.02 N ANISOU 2974 N ALA A 403 3150 3071 2904 -162 -75 100 N ATOM 2975 CA ALA A 403 22.554 -43.841 18.092 1.00 23.37 C ANISOU 2975 CA ALA A 403 3089 2957 2832 -163 -104 105 C ATOM 2976 C ALA A 403 24.022 -43.872 18.498 1.00 25.45 C ANISOU 2976 C ALA A 403 3368 3211 3089 -133 -129 91 C ATOM 2977 O ALA A 403 24.647 -42.823 18.699 1.00 23.27 O ANISOU 2977 O ALA A 403 3077 2953 2814 -116 -129 71 O ATOM 2978 CB ALA A 403 22.395 -43.841 16.561 1.00 21.82 C ANISOU 2978 CB ALA A 403 2873 2752 2667 -167 -106 96 C ATOM 2979 N ASP A 404 24.562 -45.088 18.604 1.00 25.54 N ANISOU 2979 N ASP A 404 3413 3197 3095 -127 -153 104 N ATOM 2980 CA ASP A 404 25.919 -45.302 19.104 1.00 25.00 C ANISOU 2980 CA ASP A 404 3358 3123 3018 -96 -179 100 C ATOM 2981 C ASP A 404 26.964 -44.750 18.135 1.00 20.63 C ANISOU 2981 C ASP A 404 2775 2574 2490 -69 -190 77 C ATOM 2982 O ASP A 404 26.803 -44.833 16.912 1.00 24.40 O ANISOU 2982 O ASP A 404 3240 3041 2991 -69 -184 69 O ATOM 2983 CB ASP A 404 26.150 -46.803 19.313 1.00 26.36 C ANISOU 2983 CB ASP A 404 3575 3262 3180 -92 -199 122 C ATOM 2984 CG ASP A 404 25.397 -47.359 20.518 1.00 28.69 C ANISOU 2984 CG ASP A 404 3902 3555 3443 -117 -195 149 C ATOM 2985 OD1 ASP A 404 24.696 -46.595 21.202 1.00 30.55 O ANISOU 2985 OD1 ASP A 404 4125 3819 3665 -135 -173 149 O ATOM 2986 OD2 ASP A 404 25.474 -48.582 20.762 1.00 33.73 O1- ANISOU 2986 OD2 ASP A 404 4582 4163 4069 -118 -211 170 O1- ATOM 2987 N GLY A 405 28.037 -44.172 18.678 1.00 22.87 N ANISOU 2987 N GLY A 405 3048 2876 2768 -50 -205 68 N ATOM 2988 CA GLY A 405 29.216 -43.840 17.890 1.00 23.21 C ANISOU 2988 CA GLY A 405 3062 2925 2831 -24 -219 53 C ATOM 2989 C GLY A 405 29.726 -42.435 18.144 1.00 23.89 C ANISOU 2989 C GLY A 405 3119 3042 2917 -27 -220 35 C ATOM 2990 O GLY A 405 29.201 -41.684 18.963 1.00 24.25 O ANISOU 2990 O GLY A 405 3171 3099 2943 -46 -210 31 O ATOM 2991 N ASP A 406 30.809 -42.092 17.437 1.00 21.32 N ANISOU 2991 N ASP A 406 2764 2728 2610 -9 -233 25 N ATOM 2992 CA ASP A 406 31.256 -40.708 17.351 1.00 23.99 C ANISOU 2992 CA ASP A 406 3072 3090 2952 -19 -233 7 C ATOM 2993 C ASP A 406 31.651 -40.443 15.893 1.00 23.09 C ANISOU 2993 C ASP A 406 2926 2979 2869 -8 -227 -4 C ATOM 2994 O ASP A 406 31.491 -41.307 15.016 1.00 20.28 O ANISOU 2994 O ASP A 406 2574 2605 2527 6 -220 0 O ATOM 2995 CB ASP A 406 32.359 -40.412 18.390 1.00 23.19 C ANISOU 2995 CB ASP A 406 2969 3012 2831 -16 -263 12 C ATOM 2996 CG ASP A 406 33.631 -41.244 18.196 1.00 25.07 C ANISOU 2996 CG ASP A 406 3190 3259 3077 17 -290 27 C ATOM 2997 OD1 ASP A 406 33.812 -41.878 17.141 1.00 19.14 O ANISOU 2997 OD1 ASP A 406 2428 2497 2349 40 -283 28 O ATOM 2998 OD2 ASP A 406 34.457 -41.285 19.134 1.00 25.39 O1- ANISOU 2998 OD2 ASP A 406 3231 3318 3099 21 -318 39 O1- ATOM 2999 N LYS A 407 32.125 -39.231 15.601 1.00 23.70 N ANISOU 2999 N LYS A 407 2975 3076 2953 -19 -228 -19 N ATOM 3000 CA LYS A 407 32.413 -38.917 14.203 1.00 25.20 C ANISOU 3000 CA LYS A 407 3135 3270 3170 -12 -218 -29 C ATOM 3001 C LYS A 407 33.482 -39.851 13.655 1.00 24.46 C ANISOU 3001 C LYS A 407 3026 3181 3087 21 -231 -19 C ATOM 3002 O LYS A 407 33.345 -40.375 12.541 1.00 22.12 O ANISOU 3002 O LYS A 407 2728 2870 2806 36 -218 -21 O ATOM 3003 CB LYS A 407 32.841 -37.458 14.043 1.00 24.32 C ANISOU 3003 CB LYS A 407 2999 3178 3062 -32 -220 -43 C ATOM 3004 CG LYS A 407 32.786 -36.990 12.581 1.00 22.94 C ANISOU 3004 CG LYS A 407 2800 3003 2913 -33 -204 -54 C ATOM 3005 CD LYS A 407 33.069 -35.486 12.419 1.00 19.94 C ANISOU 3005 CD LYS A 407 2403 2636 2535 -57 -204 -67 C ATOM 3006 CE LYS A 407 34.541 -35.158 12.647 1.00 25.13 C ANISOU 3006 CE LYS A 407 3033 3324 3190 -60 -231 -61 C ATOM 3007 NZ LYS A 407 34.790 -33.695 12.531 1.00 23.29 N1+ ANISOU 3007 NZ LYS A 407 2792 3101 2956 -91 -234 -73 N1+ ATOM 3008 N ASP A 408 34.521 -40.112 14.459 1.00 21.39 N ANISOU 3008 N ASP A 408 2629 2810 2686 36 -257 -6 N ATOM 3009 CA ASP A 408 35.654 -40.926 14.032 1.00 22.26 C ANISOU 3009 CA ASP A 408 2720 2933 2806 75 -269 7 C ATOM 3010 C ASP A 408 35.211 -42.322 13.615 1.00 23.85 C ANISOU 3010 C ASP A 408 2954 3097 3008 104 -259 15 C ATOM 3011 O ASP A 408 35.510 -42.778 12.505 1.00 23.15 O ANISOU 3011 O ASP A 408 2859 3003 2935 131 -247 12 O ATOM 3012 CB ASP A 408 36.672 -41.011 15.172 1.00 25.52 C ANISOU 3012 CB ASP A 408 3122 3373 3203 84 -302 25 C ATOM 3013 CG ASP A 408 37.694 -39.908 15.123 1.00 31.46 C ANISOU 3013 CG ASP A 408 3826 4169 3960 68 -318 24 C ATOM 3014 OD1 ASP A 408 37.305 -38.770 14.805 1.00 33.80 O ANISOU 3014 OD1 ASP A 408 4116 4467 4260 33 -307 6 O ATOM 3015 OD2 ASP A 408 38.880 -40.167 15.461 1.00 36.81 O1- ANISOU 3015 OD2 ASP A 408 4474 4879 4635 88 -343 43 O1- ATOM 3016 N THR A 409 34.499 -43.024 14.501 1.00 22.79 N ANISOU 3016 N THR A 409 2862 2939 2856 98 -263 24 N ATOM 3017 CA THR A 409 34.105 -44.394 14.182 1.00 23.33 C ANISOU 3017 CA THR A 409 2971 2969 2923 120 -258 33 C ATOM 3018 C THR A 409 33.047 -44.426 13.088 1.00 21.99 C ANISOU 3018 C THR A 409 2816 2773 2765 102 -233 20 C ATOM 3019 O THR A 409 33.030 -45.352 12.282 1.00 19.49 O ANISOU 3019 O THR A 409 2523 2429 2453 124 -227 21 O ATOM 3020 CB THR A 409 33.596 -45.123 15.429 1.00 21.68 C ANISOU 3020 CB THR A 409 2806 2741 2690 112 -270 51 C ATOM 3021 CG2 THR A 409 34.736 -45.302 16.446 1.00 21.91 C ANISOU 3021 CG2 THR A 409 2824 2793 2706 137 -299 68 C ATOM 3022 OG1 THR A 409 32.528 -44.375 16.026 1.00 20.40 O ANISOU 3022 OG1 THR A 409 2650 2582 2518 68 -259 44 O ATOM 3023 N SER A 410 32.170 -43.423 13.039 1.00 23.21 N ANISOU 3023 N SER A 410 2959 2936 2923 63 -220 8 N ATOM 3024 CA SER A 410 31.194 -43.338 11.960 1.00 22.74 C ANISOU 3024 CA SER A 410 2906 2860 2876 44 -199 -3 C ATOM 3025 C SER A 410 31.888 -43.166 10.612 1.00 22.48 C ANISOU 3025 C SER A 410 2849 2832 2861 65 -192 -15 C ATOM 3026 O SER A 410 31.564 -43.855 9.636 1.00 18.99 O ANISOU 3026 O SER A 410 2429 2365 2423 72 -184 -18 O ATOM 3027 CB SER A 410 30.231 -42.174 12.222 1.00 25.08 C ANISOU 3027 CB SER A 410 3188 3170 3172 7 -186 -11 C ATOM 3028 OG SER A 410 29.610 -42.316 13.492 1.00 27.36 O ANISOU 3028 OG SER A 410 3498 3457 3441 -10 -188 1 O ATOM 3029 N PHE A 411 32.844 -42.235 10.534 1.00 20.31 N ANISOU 3029 N PHE A 411 2532 2592 2594 73 -196 -21 N ATOM 3030 CA PHE A 411 33.546 -42.027 9.272 1.00 19.78 C ANISOU 3030 CA PHE A 411 2438 2535 2541 92 -186 -30 C ATOM 3031 C PHE A 411 34.393 -43.236 8.905 1.00 19.37 C ANISOU 3031 C PHE A 411 2399 2472 2487 140 -189 -21 C ATOM 3032 O PHE A 411 34.585 -43.520 7.713 1.00 19.45 O ANISOU 3032 O PHE A 411 2411 2473 2505 159 -175 -29 O ATOM 3033 CB PHE A 411 34.407 -40.763 9.341 1.00 19.59 C ANISOU 3033 CB PHE A 411 2365 2553 2525 83 -191 -34 C ATOM 3034 CG PHE A 411 33.630 -39.474 9.174 1.00 19.56 C ANISOU 3034 CG PHE A 411 2352 2554 2527 43 -181 -47 C ATOM 3035 CD1 PHE A 411 32.245 -39.466 9.212 1.00 19.95 C ANISOU 3035 CD1 PHE A 411 2428 2579 2573 19 -170 -51 C ATOM 3036 CD2 PHE A 411 34.295 -38.272 9.025 1.00 19.59 C ANISOU 3036 CD2 PHE A 411 2320 2588 2537 28 -185 -53 C ATOM 3037 CE1 PHE A 411 31.533 -38.284 9.074 1.00 21.07 C ANISOU 3037 CE1 PHE A 411 2560 2725 2719 -10 -159 -61 C ATOM 3038 CE2 PHE A 411 33.597 -37.089 8.900 1.00 21.39 C ANISOU 3038 CE2 PHE A 411 2545 2813 2767 -4 -175 -64 C ATOM 3039 CZ PHE A 411 32.213 -37.092 8.911 1.00 15.54 C ANISOU 3039 CZ PHE A 411 1831 2048 2025 -19 -162 -68 C ATOM 3040 N ALA A 412 34.911 -43.956 9.901 1.00 20.17 N ANISOU 3040 N ALA A 412 2513 2572 2578 164 -207 -5 N ATOM 3041 CA ALA A 412 35.693 -45.154 9.600 1.00 20.83 C ANISOU 3041 CA ALA A 412 2615 2641 2658 218 -209 5 C ATOM 3042 C ALA A 412 34.818 -46.237 8.974 1.00 21.27 C ANISOU 3042 C ALA A 412 2732 2643 2707 221 -198 0 C ATOM 3043 O ALA A 412 35.245 -46.913 8.023 1.00 18.43 O ANISOU 3043 O ALA A 412 2389 2266 2348 259 -187 -4 O ATOM 3044 CB ALA A 412 36.379 -45.669 10.860 1.00 19.23 C ANISOU 3044 CB ALA A 412 2414 2449 2445 242 -233 26 C ATOM 3045 N GLU A 413 33.586 -46.411 9.473 1.00 20.75 N ANISOU 3045 N GLU A 413 2702 2551 2633 179 -201 2 N ATOM 3046 CA GLU A 413 32.687 -47.362 8.814 1.00 21.16 C ANISOU 3046 CA GLU A 413 2811 2553 2677 169 -194 -1 C ATOM 3047 C GLU A 413 32.364 -46.917 7.396 1.00 20.50 C ANISOU 3047 C GLU A 413 2717 2468 2604 157 -176 -19 C ATOM 3048 O GLU A 413 32.347 -47.742 6.478 1.00 20.38 O ANISOU 3048 O GLU A 413 2743 2418 2582 175 -170 -25 O ATOM 3049 CB GLU A 413 31.371 -47.570 9.572 1.00 23.64 C ANISOU 3049 CB GLU A 413 3155 2846 2980 120 -200 9 C ATOM 3050 CG GLU A 413 31.374 -47.514 11.078 1.00 33.81 C ANISOU 3050 CG GLU A 413 4442 4149 4258 112 -214 25 C ATOM 3051 CD GLU A 413 29.935 -47.524 11.640 1.00 42.39 C ANISOU 3051 CD GLU A 413 5549 5223 5334 59 -211 33 C ATOM 3052 OE1 GLU A 413 29.726 -47.946 12.805 1.00 46.97 O ANISOU 3052 OE1 GLU A 413 6151 5798 5898 51 -221 50 O ATOM 3053 OE2 GLU A 413 29.004 -47.135 10.891 1.00 49.96 O1- ANISOU 3053 OE2 GLU A 413 6501 6180 6301 26 -198 25 O1- ATOM 3054 N LEU A 414 32.091 -45.618 7.194 1.00 19.12 N ANISOU 3054 N LEU A 414 2496 2326 2441 126 -169 -29 N ATOM 3055 CA LEU A 414 31.841 -45.134 5.836 1.00 22.17 C ANISOU 3055 CA LEU A 414 2872 2715 2837 116 -153 -44 C ATOM 3056 C LEU A 414 33.015 -45.449 4.918 1.00 18.91 C ANISOU 3056 C LEU A 414 2454 2307 2426 165 -143 -51 C ATOM 3057 O LEU A 414 32.818 -45.875 3.777 1.00 18.86 O ANISOU 3057 O LEU A 414 2475 2276 2414 171 -132 -61 O ATOM 3058 CB LEU A 414 31.549 -43.627 5.825 1.00 17.36 C ANISOU 3058 CB LEU A 414 2212 2141 2241 83 -148 -51 C ATOM 3059 CG LEU A 414 30.249 -43.155 6.500 1.00 19.00 C ANISOU 3059 CG LEU A 414 2423 2348 2447 37 -149 -46 C ATOM 3060 CD1 LEU A 414 30.161 -41.596 6.551 1.00 17.75 C ANISOU 3060 CD1 LEU A 414 2219 2224 2302 16 -142 -54 C ATOM 3061 CD2 LEU A 414 29.048 -43.747 5.795 1.00 17.63 C ANISOU 3061 CD2 LEU A 414 2284 2144 2270 9 -146 -45 C ATOM 3062 N ASN A 415 34.245 -45.242 5.398 1.00 18.57 N ANISOU 3062 N ASN A 415 2373 2296 2387 201 -147 -44 N ATOM 3063 CA ASN A 415 35.418 -45.546 4.587 1.00 17.48 C ANISOU 3063 CA ASN A 415 2221 2170 2250 254 -134 -46 C ATOM 3064 C ASN A 415 35.494 -47.035 4.264 1.00 19.50 C ANISOU 3064 C ASN A 415 2540 2377 2490 297 -130 -44 C ATOM 3065 O ASN A 415 35.767 -47.412 3.120 1.00 20.18 O ANISOU 3065 O ASN A 415 2647 2450 2571 325 -112 -55 O ATOM 3066 CB ASN A 415 36.682 -45.096 5.315 1.00 18.23 C ANISOU 3066 CB ASN A 415 2259 2315 2352 281 -143 -32 C ATOM 3067 CG ASN A 415 36.862 -43.599 5.295 1.00 19.85 C ANISOU 3067 CG ASN A 415 2404 2566 2571 244 -143 -36 C ATOM 3068 ND2 ASN A 415 37.562 -43.071 6.304 1.00 17.34 N ANISOU 3068 ND2 ASN A 415 2046 2286 2255 241 -161 -23 N ATOM 3069 OD1 ASN A 415 36.334 -42.908 4.418 1.00 18.12 O ANISOU 3069 OD1 ASN A 415 2180 2347 2358 215 -129 -49 O ATOM 3070 N ALA A 416 35.261 -47.893 5.264 1.00 18.00 N ANISOU 3070 N ALA A 416 2389 2159 2289 303 -148 -31 N ATOM 3071 CA ALA A 416 35.298 -49.335 5.039 1.00 22.10 C ANISOU 3071 CA ALA A 416 2981 2625 2792 342 -147 -28 C ATOM 3072 C ALA A 416 34.224 -49.771 4.053 1.00 20.70 C ANISOU 3072 C ALA A 416 2862 2399 2603 309 -140 -44 C ATOM 3073 O ALA A 416 34.486 -50.579 3.157 1.00 24.21 O ANISOU 3073 O ALA A 416 3356 2809 3034 345 -128 -53 O ATOM 3074 CB ALA A 416 35.141 -50.077 6.368 1.00 22.02 C ANISOU 3074 CB ALA A 416 3002 2593 2772 344 -169 -9 C ATOM 3075 N THR A 417 33.003 -49.253 4.203 1.00 21.66 N ANISOU 3075 N THR A 417 2983 2519 2728 241 -148 -46 N ATOM 3076 CA THR A 417 31.932 -49.592 3.268 1.00 22.17 C ANISOU 3076 CA THR A 417 3096 2545 2782 202 -146 -56 C ATOM 3077 C THR A 417 32.202 -49.055 1.858 1.00 22.42 C ANISOU 3077 C THR A 417 3111 2590 2817 210 -126 -75 C ATOM 3078 O THR A 417 31.938 -49.745 0.865 1.00 21.70 O ANISOU 3078 O THR A 417 3077 2458 2708 213 -121 -86 O ATOM 3079 CB THR A 417 30.613 -49.054 3.806 1.00 24.08 C ANISOU 3079 CB THR A 417 3326 2795 3030 131 -157 -49 C ATOM 3080 CG2 THR A 417 29.490 -49.400 2.872 1.00 23.92 C ANISOU 3080 CG2 THR A 417 3349 2740 2999 86 -160 -55 C ATOM 3081 OG1 THR A 417 30.375 -49.620 5.106 1.00 23.63 O ANISOU 3081 OG1 THR A 417 3289 2725 2966 124 -173 -30 O ATOM 3082 N TRP A 418 32.711 -47.824 1.755 1.00 19.63 N ANISOU 3082 N TRP A 418 2685 2291 2482 211 -116 -78 N ATOM 3083 CA TRP A 418 33.037 -47.242 0.456 1.00 20.89 C ANISOU 3083 CA TRP A 418 2825 2468 2644 219 -96 -94 C ATOM 3084 C TRP A 418 34.105 -48.060 -0.254 1.00 22.26 C ANISOU 3084 C TRP A 418 3026 2627 2803 286 -78 -100 C ATOM 3085 O TRP A 418 34.006 -48.342 -1.456 1.00 22.67 O ANISOU 3085 O TRP A 418 3115 2657 2841 293 -64 -115 O ATOM 3086 CB TRP A 418 33.529 -45.803 0.651 1.00 20.52 C ANISOU 3086 CB TRP A 418 2696 2482 2619 209 -91 -92 C ATOM 3087 CG TRP A 418 33.601 -45.004 -0.614 1.00 18.47 C ANISOU 3087 CG TRP A 418 2413 2242 2362 199 -74 -104 C ATOM 3088 CD1 TRP A 418 34.722 -44.721 -1.354 1.00 18.61 C ANISOU 3088 CD1 TRP A 418 2401 2290 2381 238 -53 -108 C ATOM 3089 CD2 TRP A 418 32.509 -44.375 -1.278 1.00 19.28 C ANISOU 3089 CD2 TRP A 418 2519 2340 2466 147 -75 -111 C ATOM 3090 CE2 TRP A 418 33.028 -43.725 -2.421 1.00 21.71 C ANISOU 3090 CE2 TRP A 418 2803 2671 2775 156 -56 -120 C ATOM 3091 CE3 TRP A 418 31.134 -44.306 -1.028 1.00 19.66 C ANISOU 3091 CE3 TRP A 418 2586 2369 2515 94 -90 -107 C ATOM 3092 NE1 TRP A 418 34.385 -43.943 -2.444 1.00 19.16 N ANISOU 3092 NE1 TRP A 418 2459 2370 2452 211 -42 -118 N ATOM 3093 CZ2 TRP A 418 32.217 -43.008 -3.299 1.00 19.13 C ANISOU 3093 CZ2 TRP A 418 2474 2347 2449 114 -55 -126 C ATOM 3094 CZ3 TRP A 418 30.333 -43.588 -1.905 1.00 21.06 C ANISOU 3094 CZ3 TRP A 418 2755 2553 2695 55 -88 -112 C ATOM 3095 CH2 TRP A 418 30.878 -42.949 -3.021 1.00 21.08 C ANISOU 3095 CH2 TRP A 418 2737 2575 2698 66 -72 -122 C ATOM 3096 N SER A 419 35.159 -48.401 0.481 1.00 22.85 N ANISOU 3096 N SER A 419 3081 2718 2881 339 -78 -88 N ATOM 3097 CA SER A 419 36.260 -49.209 -0.035 1.00 23.18 C ANISOU 3097 CA SER A 419 3145 2752 2911 416 -58 -89 C ATOM 3098 C SER A 419 35.760 -50.549 -0.565 1.00 26.77 C ANISOU 3098 C SER A 419 3701 3132 3338 430 -57 -99 C ATOM 3099 O SER A 419 36.118 -50.978 -1.673 1.00 23.56 O ANISOU 3099 O SER A 419 3331 2707 2914 468 -35 -113 O ATOM 3100 CB SER A 419 37.268 -49.424 1.103 1.00 21.53 C ANISOU 3100 CB SER A 419 2900 2570 2711 463 -67 -68 C ATOM 3101 OG SER A 419 38.537 -49.771 0.613 1.00 34.10 O ANISOU 3101 OG SER A 419 4475 4183 4299 540 -44 -64 O ATOM 3102 N ASP A 420 34.950 -51.240 0.239 1.00 23.94 N ANISOU 3102 N ASP A 420 3393 2731 2973 401 -82 -91 N ATOM 3103 CA ASP A 420 34.414 -52.529 -0.185 1.00 24.88 C ANISOU 3103 CA ASP A 420 3616 2774 3064 405 -86 -99 C ATOM 3104 C ASP A 420 33.622 -52.381 -1.473 1.00 25.72 C ANISOU 3104 C ASP A 420 3758 2859 3157 362 -80 -119 C ATOM 3105 O ASP A 420 33.776 -53.185 -2.402 1.00 25.49 O ANISOU 3105 O ASP A 420 3801 2784 3101 392 -68 -134 O ATOM 3106 CB ASP A 420 33.534 -53.115 0.917 1.00 26.29 C ANISOU 3106 CB ASP A 420 3834 2917 3239 362 -116 -83 C ATOM 3107 CG ASP A 420 32.973 -54.471 0.547 1.00 34.12 C ANISOU 3107 CG ASP A 420 4938 3827 4200 358 -125 -88 C ATOM 3108 OD1 ASP A 420 33.744 -55.452 0.526 1.00 33.55 O ANISOU 3108 OD1 ASP A 420 4920 3716 4111 426 -117 -88 O ATOM 3109 OD2 ASP A 420 31.771 -54.544 0.237 1.00 38.39 O1- ANISOU 3109 OD2 ASP A 420 5515 4341 4732 286 -140 -91 O1- ATOM 3110 N ALA A 421 32.802 -51.326 -1.559 1.00 24.28 N ANISOU 3110 N ALA A 421 3526 2710 2990 294 -88 -119 N ATOM 3111 CA ALA A 421 31.977 -51.104 -2.740 1.00 24.41 C ANISOU 3111 CA ALA A 421 3570 2712 2995 248 -87 -134 C ATOM 3112 C ALA A 421 32.826 -50.861 -3.972 1.00 26.03 C ANISOU 3112 C ALA A 421 3769 2931 3190 293 -57 -152 C ATOM 3113 O ALA A 421 32.483 -51.316 -5.069 1.00 27.83 O ANISOU 3113 O ALA A 421 4060 3121 3392 285 -53 -168 O ATOM 3114 CB ALA A 421 31.044 -49.920 -2.517 1.00 22.58 C ANISOU 3114 CB ALA A 421 3275 2521 2785 178 -100 -127 C ATOM 3115 N GLN A 422 33.923 -50.118 -3.820 1.00 24.95 N ANISOU 3115 N GLN A 422 3556 2851 3073 337 -37 -148 N ATOM 3116 CA GLN A 422 34.823 -49.900 -4.946 1.00 25.16 C ANISOU 3116 CA GLN A 422 3572 2899 3090 384 -5 -160 C ATOM 3117 C GLN A 422 35.381 -51.219 -5.452 1.00 27.81 C ANISOU 3117 C GLN A 422 3991 3183 3394 451 12 -170 C ATOM 3118 O GLN A 422 35.451 -51.454 -6.666 1.00 28.99 O ANISOU 3118 O GLN A 422 4185 3312 3517 467 33 -189 O ATOM 3119 CB GLN A 422 35.970 -48.973 -4.538 1.00 25.06 C ANISOU 3119 CB GLN A 422 3460 2958 3102 419 11 -148 C ATOM 3120 CG GLN A 422 35.570 -47.530 -4.331 1.00 24.36 C ANISOU 3120 CG GLN A 422 3296 2921 3040 358 1 -142 C ATOM 3121 CD GLN A 422 36.716 -46.724 -3.761 1.00 26.35 C ANISOU 3121 CD GLN A 422 3459 3238 3314 386 9 -128 C ATOM 3122 NE2 GLN A 422 36.714 -45.412 -4.015 1.00 26.42 N ANISOU 3122 NE2 GLN A 422 3405 3293 3339 348 12 -126 N ATOM 3123 OE1 GLN A 422 37.601 -47.274 -3.105 1.00 26.56 O ANISOU 3123 OE1 GLN A 422 3474 3273 3342 440 11 -116 O ATOM 3124 N ALA A 423 35.822 -52.079 -4.528 1.00 25.23 N ANISOU 3124 N ALA A 423 3687 2833 3066 496 6 -159 N ATOM 3125 CA ALA A 423 36.326 -53.389 -4.923 1.00 28.23 C ANISOU 3125 CA ALA A 423 4155 3156 3415 566 22 -167 C ATOM 3126 C ALA A 423 35.261 -54.174 -5.672 1.00 31.99 C ANISOU 3126 C ALA A 423 4741 3555 3857 523 9 -186 C ATOM 3127 O ALA A 423 35.550 -54.802 -6.696 1.00 37.52 O ANISOU 3127 O ALA A 423 5513 4217 4525 564 31 -205 O ATOM 3128 CB ALA A 423 36.804 -54.166 -3.697 1.00 26.88 C ANISOU 3128 CB ALA A 423 3994 2968 3249 612 9 -148 C ATOM 3129 N ARG A 424 34.017 -54.125 -5.194 1.00 29.83 N ANISOU 3129 N ARG A 424 4484 3260 3589 439 -27 -180 N ATOM 3130 CA ARG A 424 32.966 -54.923 -5.811 1.00 35.82 C ANISOU 3130 CA ARG A 424 5347 3948 4315 389 -46 -192 C ATOM 3131 C ARG A 424 32.584 -54.388 -7.193 1.00 37.63 C ANISOU 3131 C ARG A 424 5584 4185 4528 355 -36 -212 C ATOM 3132 O ARG A 424 32.341 -55.169 -8.117 1.00 37.32 O ANISOU 3132 O ARG A 424 5643 4087 4451 355 -35 -230 O ATOM 3133 CB ARG A 424 31.756 -54.987 -4.881 1.00 34.28 C ANISOU 3133 CB ARG A 424 5155 3739 4132 306 -86 -175 C ATOM 3134 CG ARG A 424 31.924 -56.061 -3.829 1.00 40.20 C ANISOU 3134 CG ARG A 424 5956 4442 4875 334 -99 -161 C ATOM 3135 CD ARG A 424 31.151 -55.789 -2.552 1.00 44.07 C ANISOU 3135 CD ARG A 424 6405 4952 5389 274 -128 -136 C ATOM 3136 NE ARG A 424 29.755 -56.205 -2.656 1.00 50.02 N ANISOU 3136 NE ARG A 424 7215 5664 6126 186 -159 -131 N ATOM 3137 CZ ARG A 424 28.752 -55.619 -2.015 1.00 50.45 C ANISOU 3137 CZ ARG A 424 7219 5750 6199 111 -180 -113 C ATOM 3138 NH1 ARG A 424 28.947 -54.575 -1.224 1.00 48.33 N1+ ANISOU 3138 NH1 ARG A 424 6850 5548 5964 114 -174 -102 N1+ ATOM 3139 NH2 ARG A 424 27.520 -56.090 -2.174 1.00 48.82 N ANISOU 3139 NH2 ARG A 424 7066 5508 5977 33 -207 -106 N ATOM 3140 N VAL A 425 32.542 -53.062 -7.362 1.00 34.90 N ANISOU 3140 N VAL A 425 5142 3909 4210 327 -30 -208 N ATOM 3141 CA VAL A 425 32.200 -52.485 -8.661 1.00 32.72 C ANISOU 3141 CA VAL A 425 4869 3643 3919 295 -22 -224 C ATOM 3142 C VAL A 425 33.327 -52.692 -9.661 1.00 36.09 C ANISOU 3142 C VAL A 425 5319 4071 4322 373 20 -242 C ATOM 3143 O VAL A 425 33.086 -52.777 -10.871 1.00 38.88 O ANISOU 3143 O VAL A 425 5725 4403 4644 360 28 -260 O ATOM 3144 CB VAL A 425 31.838 -50.998 -8.488 1.00 29.25 C ANISOU 3144 CB VAL A 425 4323 3274 3516 245 -28 -212 C ATOM 3145 CG1 VAL A 425 31.840 -50.262 -9.822 1.00 32.29 C ANISOU 3145 CG1 VAL A 425 4697 3684 3889 232 -12 -225 C ATOM 3146 CG2 VAL A 425 30.476 -50.894 -7.835 1.00 27.97 C ANISOU 3146 CG2 VAL A 425 4159 3103 3366 163 -67 -197 C ATOM 3147 N GLY A 426 34.563 -52.809 -9.180 1.00 37.92 N ANISOU 3147 N GLY A 426 5514 4329 4566 455 47 -235 N ATOM 3148 CA GLY A 426 35.685 -53.094 -10.056 1.00 47.54 C ANISOU 3148 CA GLY A 426 6752 5552 5761 538 91 -249 C ATOM 3149 C GLY A 426 35.906 -54.561 -10.397 1.00 54.84 C ANISOU 3149 C GLY A 426 7798 6396 6642 596 102 -264 C ATOM 3150 O GLY A 426 36.778 -54.856 -11.224 1.00 58.94 O ANISOU 3150 O GLY A 426 8345 6915 7136 670 144 -278 O ATOM 3151 N GLU A 427 35.163 -55.481 -9.775 1.00 63.06 N ANISOU 3151 N GLU A 427 8916 7370 7673 566 69 -262 N ATOM 3152 CA GLU A 427 35.234 -56.909 -10.124 1.00 68.26 C ANISOU 3152 CA GLU A 427 9709 7939 8286 611 74 -278 C ATOM 3153 C GLU A 427 34.779 -57.168 -11.551 1.00 78.90 C ANISOU 3153 C GLU A 427 11148 9244 9587 587 81 -307 C ATOM 3154 O GLU A 427 35.425 -57.919 -12.284 1.00 87.22 O ANISOU 3154 O GLU A 427 12283 10256 10601 660 114 -326 O ATOM 3155 CB GLU A 427 34.384 -57.762 -9.179 1.00 67.74 C ANISOU 3155 CB GLU A 427 9708 7810 8219 565 30 -267 C ATOM 3156 CG GLU A 427 35.002 -58.090 -7.833 1.00 67.96 C ANISOU 3156 CG GLU A 427 9701 7849 8274 616 27 -243 C ATOM 3157 CD GLU A 427 33.996 -58.735 -6.890 1.00 73.19 C ANISOU 3157 CD GLU A 427 10414 8458 8935 550 -19 -229 C ATOM 3158 OE1 GLU A 427 32.803 -58.805 -7.256 1.00 74.63 O ANISOU 3158 OE1 GLU A 427 10644 8608 9103 460 -49 -235 O ATOM 3159 OE2 GLU A 427 34.395 -59.178 -5.791 1.00 75.81 O1- ANISOU 3159 OE2 GLU A 427 10738 8784 9282 588 -26 -210 O1- ATOM 3160 OXT GLU A 427 33.749 -56.646 -11.986 1.00 81.83 O1- ANISOU 3160 OXT GLU A 427 11516 9619 9957 496 54 -310 O1- TER HETATM 3161 C1A MAB A 504 7.762 -26.797 -1.538 1.00 43.29 C ANISOU 3161 C1A MAB A 504 4884 5854 5711 -13 18 324 C HETATM 3162 C1B MAB A 504 11.858 -29.289 -4.268 1.00 41.07 C ANISOU 3162 C1B MAB A 504 4770 5437 5398 -170 -87 205 C HETATM 3163 O1A MAB A 504 6.379 -26.438 -1.455 1.00 46.33 O ANISOU 3163 O1A MAB A 504 5205 6295 6105 15 32 375 O HETATM 3164 C2A MAB A 504 8.025 -28.228 -1.210 1.00 43.02 C ANISOU 3164 C2A MAB A 504 4859 5820 5666 -70 1 316 C HETATM 3165 C2B MAB A 504 12.541 -28.160 -5.042 1.00 40.23 C ANISOU 3165 C2B MAB A 504 4684 5307 5295 -147 -86 189 C HETATM 3166 O2A MAB A 504 6.803 -29.064 -1.500 1.00 55.12 O ANISOU 3166 O2A MAB A 504 6334 7408 7201 -111 -18 366 O HETATM 3167 O2B MAB A 504 13.049 -27.234 -4.043 1.00 43.44 O ANISOU 3167 O2B MAB A 504 5105 5694 5705 -103 -55 168 O HETATM 3168 C3A MAB A 504 9.278 -28.859 -1.733 1.00 39.32 C ANISOU 3168 C3A MAB A 504 4444 5305 5189 -110 -25 277 C HETATM 3169 C3B MAB A 504 13.703 -28.443 -5.897 1.00 38.97 C ANISOU 3169 C3B MAB A 504 4565 5116 5125 -169 -102 159 C HETATM 3170 O3A MAB A 504 9.079 -30.317 -1.726 1.00 43.08 O ANISOU 3170 O3A MAB A 504 4917 5793 5656 -168 -49 287 O HETATM 3171 O3B MAB A 504 14.187 -27.194 -6.469 1.00 35.06 O ANISOU 3171 O3B MAB A 504 4083 4604 4635 -144 -96 151 O HETATM 3172 C4A MAB A 504 9.873 -28.411 -3.035 1.00 39.82 C ANISOU 3172 C4A MAB A 504 4532 5344 5256 -117 -49 263 C HETATM 3173 C4B MAB A 504 14.739 -29.095 -5.029 1.00 35.87 C ANISOU 3173 C4B MAB A 504 4203 4700 4726 -172 -92 126 C HETATM 3174 O4A MAB A 504 11.288 -28.817 -3.086 1.00 32.46 O ANISOU 3174 O4A MAB A 504 3655 4365 4313 -134 -57 217 O HETATM 3175 O4B MAB A 504 15.978 -29.209 -5.724 1.00 35.92 O ANISOU 3175 O4B MAB A 504 4245 4679 4725 -182 -100 97 O HETATM 3176 C5A MAB A 504 9.713 -26.853 -3.119 1.00 40.61 C ANISOU 3176 C5A MAB A 504 4626 5439 5365 -58 -27 267 C HETATM 3177 C5B MAB A 504 14.143 -30.451 -4.654 1.00 39.72 C ANISOU 3177 C5B MAB A 504 4681 5202 5207 -204 -104 140 C HETATM 3178 O5A MAB A 504 8.265 -26.429 -2.876 1.00 49.07 O ANISOU 3178 O5A MAB A 504 5636 6561 6446 -28 -12 315 O HETATM 3179 O5B MAB A 504 12.815 -30.453 -3.983 1.00 36.33 O ANISOU 3179 O5B MAB A 504 4208 4810 4784 -199 -96 175 O HETATM 3180 C6A MAB A 504 10.024 -26.250 -4.366 1.00 42.09 C ANISOU 3180 C6A MAB A 504 4826 5610 5555 -61 -48 264 C HETATM 3181 C6B MAB A 504 15.154 -31.181 -3.748 1.00 34.21 C ANISOU 3181 C6B MAB A 504 4016 4482 4502 -204 -95 110 C HETATM 3182 O6A MAB A 504 11.229 -25.569 -4.165 1.00 41.19 O ANISOU 3182 O6A MAB A 504 4763 5450 5438 -41 -35 224 O HETATM 3183 O6B MAB A 504 15.829 -32.130 -4.491 1.00 46.73 O ANISOU 3183 O6B MAB A 504 5633 6048 6075 -232 -115 94 O CONECT 3161 3163 3164 3178 CONECT 3162 3165 3174 3179 CONECT 3163 3161 CONECT 3164 3161 3166 3168 CONECT 3165 3162 3167 3169 CONECT 3166 3164 CONECT 3167 3165 CONECT 3168 3164 3170 3172 CONECT 3169 3165 3171 3173 CONECT 3170 3168 CONECT 3171 3169 CONECT 3172 3168 3174 3176 CONECT 3173 3169 3175 3177 CONECT 3174 3162 3172 CONECT 3175 3173 CONECT 3176 3172 3178 3180 CONECT 3177 3173 3179 3181 CONECT 3178 3161 3176 CONECT 3179 3162 3177 CONECT 3180 3176 3182 CONECT 3181 3177 3183 CONECT 3182 3180 CONECT 3183 3181 END If you find results from this site helpful for your research, please cite one of our papers:
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