REMARK Date 2020-05-16 Time 18:16:00 CST +0800 (1589624160.06 s) REMARK PHENIX refinement REMARK REMARK ****************** INPUT FILES AND LABELS ****************************** REMARK Reflections: REMARK file name : 3C_11_1_Porpoise_XDS_Aimless.mtz REMARK labels : ['IMEAN,SIGIMEAN'] REMARK R-free flags: REMARK file name : 3C_11_1_Porpoise_XDS_Aimless.mtz REMARK label : FreeR_flag REMARK test_flag_value: 0 REMARK Model file name(s): REMARK WaterTLSCoot.pdb REMARK REMARK ******************** REFINEMENT SUMMARY: QUICK FACTS ******************* REMARK Start: r_work = 0.2240 r_free = 0.2561 bonds = 0.005 angles = 0.759 REMARK Final: r_work = 0.2228 r_free = 0.2485 bonds = 0.005 angles = 0.759 REMARK ************************************************************************ REMARK REMARK ****************** REFINEMENT STATISTICS STEP BY STEP ****************** REMARK leading digit, like 1_, means number of macro-cycle REMARK 0 : statistics at the very beginning when nothing is done yet REMARK 1_bss: bulk solvent correction and/or (anisotropic) scaling REMARK ------------------------------------------------------------------------ REMARK stage r-work r-free bonds angles b_min b_max b_ave n_water shift REMARK 0 : 0.3102 0.3396 0.005 0.759 17.8 89.6 40.4 146 0.000 REMARK 1_bss: 0.2240 0.2561 0.005 0.759 17.8 89.6 40.4 146 0.000 REMARK 1_settarget: 0.2240 0.2561 0.005 0.759 17.8 89.6 40.4 146 0.000 REMARK 1_adp: 0.2359 0.2601 0.005 0.759 21.3 90.0 39.8 146 0.000 REMARK 2_bss: 0.2353 0.2597 0.005 0.759 21.6 90.3 40.0 146 0.000 REMARK 2_settarget: 0.2353 0.2597 0.005 0.759 21.6 90.3 40.0 146 0.000 REMARK 2_adp: 0.2236 0.2491 0.005 0.759 21.1 104.3 41.0 146 0.000 REMARK 3_bss: 0.2233 0.2491 0.005 0.759 21.0 104.2 40.9 146 0.000 REMARK 3_settarget: 0.2233 0.2491 0.005 0.759 21.0 104.2 40.9 146 0.000 REMARK 3_adp: 0.2228 0.2484 0.005 0.759 20.8 103.0 41.0 146 0.000 REMARK end: 0.2228 0.2485 0.005 0.759 20.7 103.0 40.9 146 0.000 REMARK ------------------------------------------------------------------------ REMARK MODEL CONTENT. REMARK ELEMENT ATOM RECORD COUNT OCCUPANCY SUM REMARK C 1504 1504.00 REMARK S 23 23.00 REMARK O 590 590.00 REMARK N 395 395.00 REMARK TOTAL 2512 2512.00 REMARK ----------------------------------------------------------------------- REMARK r_free_flags.md5.hexdigest a3c21a1bb14d375a9e210977cfa582ce REMARK REMARK IF THIS FILE IS FOR PDB DEPOSITION: REMOVE ALL FROM THIS LINE UP. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.16_3549: ???) REMARK 3 AUTHORS : Adams,Afonine,Bunkoczi,Burnley,Chen,Dar,Davis, REMARK 3 : Draizen,Echols,Gildea,Gros,Grosse-Kunstleve,Headd, REMARK 3 : Hintze,Hung,Ioerger,Liebschner,McCoy,McKee,Moriarty, REMARK 3 : Oeffner,Poon,Read,Richardson,Richardson,Sacchettini, REMARK 3 : Sauter,Sobolev,Storoni,Terwilliger,Williams,Zwart REMARK 3 REMARK 3 X-RAY DATA. REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.780 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 55.443 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.34 REMARK 3 COMPLETENESS FOR RANGE (%) : 98.94 REMARK 3 NUMBER OF REFLECTIONS : 25933 REMARK 3 NUMBER OF REFLECTIONS (NON-ANOMALOUS) : 25933 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.2241 REMARK 3 R VALUE (WORKING SET) : 0.2228 REMARK 3 FREE R VALUE : 0.2485 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.99 REMARK 3 FREE R VALUE TEST SET COUNT : 1294 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE CCWORK CCFREE REMARK 3 1 55.4698 - 3.7023 0.98 2796 140 0.1659 0.1833 0.929 0.905 REMARK 3 2 3.7023 - 2.9387 0.99 2751 162 0.2144 0.2381 0.893 0.880 REMARK 3 3 2.9387 - 2.5672 0.99 2724 143 0.2581 0.2996 0.845 0.761 REMARK 3 4 2.5672 - 2.3325 0.99 2753 142 0.2644 0.3200 0.830 0.741 REMARK 3 5 2.3325 - 2.1653 0.99 2719 137 0.2720 0.2798 0.811 0.799 REMARK 3 6 2.1653 - 2.0376 0.99 2739 144 0.2797 0.3074 0.795 0.754 REMARK 3 7 2.0376 - 1.9356 0.99 2717 152 0.2906 0.3404 0.771 0.705 REMARK 3 8 1.9356 - 1.8513 0.99 2734 115 0.3083 0.3107 0.745 0.729 REMARK 3 9 1.8513 - 1.7800 0.99 2706 159 0.3485 0.3912 0.685 0.544 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 GRID STEP FACTOR : 4.00 REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.28 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.25 REMARK 3 REMARK 3 STRUCTURE FACTORS CALCULATION ALGORITHM : FFT REMARK 3 REMARK 3 REMARK 3 GEOMETRY RESTRAINTS LIBRARY: GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND : 0.005 0.170 2421 REMARK 3 ANGLE : 0.759 12.488 3304 REMARK 3 CHIRALITY : 0.051 0.384 377 REMARK 3 PLANARITY : 0.005 0.041 424 REMARK 3 DIHEDRAL : 17.723 179.992 878 REMARK 3 MIN NONBONDED DISTANCE : 2.320 REMARK 3 REMARK 3 MOLPROBITY STATISTICS. REMARK 3 ALL-ATOM CLASHSCORE : 3.46 REMARK 3 RAMACHANDRAN PLOT: REMARK 3 OUTLIERS : 0.33 % REMARK 3 ALLOWED : 2.68 % REMARK 3 FAVORED : 96.99 % REMARK 3 ROTAMER OUTLIERS : 0.39 % REMARK 3 CBETA DEVIATIONS : 0.00 % REMARK 3 PEPTIDE PLANE: REMARK 3 CIS-PROLINE : 0.00 % REMARK 3 CIS-GENERAL : 0.00 % REMARK 3 TWISTED PROLINE : 0.00 % REMARK 3 TWISTED GENERAL : 0.00 % REMARK 3 REMARK 3 min max mean iso aniso REMARK 3 Overall: 20.70 102.96 40.93 3.08 2512 2512 REMARK 3 Protein: 20.70 102.96 40.59 3.11 2317 2317 REMARK 3 Water: 28.17 72.13 48.06 N/A 146 146 REMARK 3 Other: 31.19 43.61 35.51 N/A 49 49 REMARK 3 Chain A: 20.70 102.96 40.49 N/A 2366 2366 REMARK 3 Chain S: 28.17 72.13 48.06 N/A 146 146 REMARK 3 Histogram: REMARK 3 Values Number of atoms REMARK 3 20.70 - 28.93 321 REMARK 3 28.93 - 37.16 791 REMARK 3 37.16 - 45.38 667 REMARK 3 45.38 - 53.61 381 REMARK 3 53.61 - 61.83 224 REMARK 3 61.83 - 70.06 69 REMARK 3 70.06 - 78.29 29 REMARK 3 78.29 - 86.51 3 REMARK 3 86.51 - 94.74 16 REMARK 3 94.74 - 102.96 11 REMARK 3 REMARK 3 REMARK 3 TLS DETAILS. REMARK 3 NUMBER OF TLS GROUPS: 1 REMARK 3 ORIGIN: CENTER OF MASS REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: all REMARK 3 ORIGIN FOR THE GROUP (A): -16.9000 -0.3778 16.8962 REMARK 3 T TENSOR REMARK 3 T11: 0.2108 T22: 0.2242 REMARK 3 T33: 0.2379 T12: -0.0056 REMARK 3 T13: 0.0346 T23: 0.0027 REMARK 3 L TENSOR REMARK 3 L11: 1.4670 L22: 1.3524 REMARK 3 L33: 1.6433 L12: 0.2032 REMARK 3 L13: 0.7279 L23: 0.6231 REMARK 3 S TENSOR REMARK 3 S11: 0.0624 S12: 0.0286 S13: 0.1573 REMARK 3 S21: 0.0232 S22: 0.0227 S23: 0.0029 REMARK 3 S31: 0.1287 S32: 0.0459 S33: -0.0953 REMARK 3 LINK SG CYS A 145 C2 LIG A 401 CRYST1 113.200 54.050 45.970 90.00 101.61 90.00 C 1 2 1 SCALE1 0.008834 0.000000 0.001814 0.00000 SCALE2 0.000000 0.018501 0.000000 0.00000 SCALE3 0.000000 0.000000 0.022207 0.00000 ATOM 1 N SER A 1 -1.680 3.040 39.350 1.00 58.90 N ANISOU 1 N SER A 1 7563 7742 7076 349 -904 -1315 N ATOM 2 CA SER A 1 -2.665 3.914 38.728 1.00 58.69 C ANISOU 2 CA SER A 1 7475 7701 7124 275 -737 -1294 C ATOM 3 C SER A 1 -2.343 4.159 37.258 1.00 56.89 C ANISOU 3 C SER A 1 7102 7444 7069 274 -670 -1268 C ATOM 4 O SER A 1 -1.788 3.293 36.581 1.00 55.30 O ANISOU 4 O SER A 1 6885 7236 6890 325 -716 -1229 O ATOM 5 CB SER A 1 -2.748 5.244 39.476 1.00 61.14 C ANISOU 5 CB SER A 1 7738 8030 7464 234 -712 -1404 C ATOM 6 OG SER A 1 -1.481 5.876 39.534 1.00 64.26 O ANISOU 6 OG SER A 1 8012 8428 7974 260 -798 -1508 O ATOM 7 N GLY A 2 -2.687 5.342 36.775 1.00 43.03 N ANISOU 7 N GLY A 2 5247 5671 5431 216 -566 -1294 N ATOM 8 CA GLY A 2 -2.562 5.628 35.355 1.00 39.57 C ANISOU 8 CA GLY A 2 4692 5207 5137 196 -486 -1251 C ATOM 9 C GLY A 2 -3.792 5.197 34.583 1.00 37.26 C ANISOU 9 C GLY A 2 4455 4890 4813 170 -379 -1139 C ATOM 10 O GLY A 2 -4.484 4.241 34.932 1.00 42.73 O ANISOU 10 O GLY A 2 5272 5589 5374 182 -386 -1078 O ATOM 11 N PHE A 3 -4.073 5.928 33.506 1.00 41.82 N ANISOU 11 N PHE A 3 4941 5437 5511 127 -283 -1108 N ATOM 12 CA PHE A 3 -5.259 5.688 32.693 1.00 41.56 C ANISOU 12 CA PHE A 3 4943 5380 5467 101 -183 -1011 C ATOM 13 C PHE A 3 -4.858 5.650 31.227 1.00 40.32 C ANISOU 13 C PHE A 3 4696 5214 5411 95 -141 -957 C ATOM 14 O PHE A 3 -4.308 6.625 30.705 1.00 38.46 O ANISOU 14 O PHE A 3 4352 4964 5297 60 -115 -984 O ATOM 15 CB PHE A 3 -6.321 6.763 32.934 1.00 40.30 C ANISOU 15 CB PHE A 3 4780 5192 5339 52 -103 -1029 C ATOM 16 CG PHE A 3 -7.702 6.348 32.524 1.00 39.62 C ANISOU 16 CG PHE A 3 4753 5099 5201 33 -20 -946 C ATOM 17 CD1 PHE A 3 -8.445 5.491 33.318 1.00 41.03 C ANISOU 17 CD1 PHE A 3 5046 5312 5231 35 -23 -924 C ATOM 18 CD2 PHE A 3 -8.256 6.808 31.341 1.00 39.88 C ANISOU 18 CD2 PHE A 3 4730 5093 5330 7 57 -887 C ATOM 19 CE1 PHE A 3 -9.717 5.104 32.943 1.00 41.00 C ANISOU 19 CE1 PHE A 3 5083 5309 5185 7 54 -854 C ATOM 20 CE2 PHE A 3 -9.527 6.425 30.960 1.00 40.92 C ANISOU 20 CE2 PHE A 3 4905 5222 5420 -7 123 -819 C ATOM 21 CZ PHE A 3 -10.258 5.571 31.762 1.00 39.81 C ANISOU 21 CZ PHE A 3 4863 5122 5141 -9 124 -807 C ATOM 22 N ARG A 4 -5.141 4.530 30.566 1.00 37.73 N ANISOU 22 N ARG A 4 4417 4892 5025 123 -133 -880 N ATOM 23 CA ARG A 4 -4.778 4.333 29.172 1.00 33.77 C ANISOU 23 CA ARG A 4 3841 4397 4593 125 -94 -833 C ATOM 24 C ARG A 4 -5.952 3.726 28.420 1.00 33.12 C ANISOU 24 C ARG A 4 3826 4294 4464 114 -29 -736 C ATOM 25 O ARG A 4 -6.765 2.995 28.993 1.00 34.13 O ANISOU 25 O ARG A 4 4064 4413 4490 122 -42 -705 O ATOM 26 CB ARG A 4 -3.551 3.419 29.035 1.00 34.31 C ANISOU 26 CB ARG A 4 3880 4507 4649 194 -179 -870 C ATOM 27 CG ARG A 4 -2.277 3.994 29.624 1.00 36.40 C ANISOU 27 CG ARG A 4 4051 4803 4976 206 -247 -973 C ATOM 28 CD ARG A 4 -1.730 5.106 28.748 1.00 35.35 C ANISOU 28 CD ARG A 4 3773 4683 4977 141 -177 -988 C ATOM 29 NE ARG A 4 -1.757 4.738 27.335 1.00 35.73 N ANISOU 29 NE ARG A 4 3777 4751 5047 134 -107 -923 N ATOM 30 CZ ARG A 4 -0.852 3.961 26.748 1.00 37.24 C ANISOU 30 CZ ARG A 4 3905 5004 5241 188 -137 -952 C ATOM 31 NH1 ARG A 4 0.159 3.468 27.449 1.00 37.21 N ANISOU 31 NH1 ARG A 4 3871 5038 5228 258 -243 -1041 N ATOM 32 NH2 ARG A 4 -0.958 3.679 25.457 1.00 37.26 N ANISOU 32 NH2 ARG A 4 3873 5032 5251 177 -64 -898 N ATOM 33 N LYS A 5 -6.034 4.035 27.128 1.00 34.57 N ANISOU 33 N LYS A 5 3943 4474 4718 88 39 -687 N ATOM 34 CA LYS A 5 -7.007 3.375 26.268 1.00 34.77 C ANISOU 34 CA LYS A 5 4021 4486 4702 85 86 -601 C ATOM 35 C LYS A 5 -6.616 1.911 26.118 1.00 34.68 C ANISOU 35 C LYS A 5 4067 4495 4615 149 23 -593 C ATOM 36 O LYS A 5 -5.546 1.597 25.584 1.00 32.87 O ANISOU 36 O LYS A 5 3773 4300 4414 189 -7 -626 O ATOM 37 CB LYS A 5 -7.079 4.063 24.908 1.00 34.94 C ANISOU 37 CB LYS A 5 3964 4503 4807 44 162 -552 C ATOM 38 CG LYS A 5 -8.298 3.668 24.090 1.00 38.03 C ANISOU 38 CG LYS A 5 4409 4875 5167 31 212 -467 C ATOM 39 CD LYS A 5 -8.419 4.506 22.830 1.00 36.98 C ANISOU 39 CD LYS A 5 4210 4732 5109 -15 277 -414 C ATOM 40 CE LYS A 5 -8.813 5.937 23.151 1.00 36.94 C ANISOU 40 CE LYS A 5 4172 4674 5188 -65 304 -422 C ATOM 41 NZ LYS A 5 -9.023 6.742 21.916 1.00 42.08 N ANISOU 41 NZ LYS A 5 4783 5299 5908 -113 353 -352 N ATOM 42 N MET A 6 -7.478 1.019 26.593 1.00 32.60 N ANISOU 42 N MET A 6 3922 4208 4257 157 1 -553 N ATOM 43 CA MET A 6 -7.139 -0.385 26.753 1.00 36.22 C ANISOU 43 CA MET A 6 4464 4661 4637 218 -85 -549 C ATOM 44 C MET A 6 -8.123 -1.252 25.985 1.00 35.76 C ANISOU 44 C MET A 6 4477 4575 4534 206 -57 -471 C ATOM 45 O MET A 6 -9.333 -1.009 26.012 1.00 35.53 O ANISOU 45 O MET A 6 4483 4531 4487 146 6 -420 O ATOM 46 CB MET A 6 -7.145 -0.776 28.233 1.00 36.20 C ANISOU 46 CB MET A 6 4565 4646 4545 227 -164 -571 C ATOM 47 CG MET A 6 -6.291 -1.979 28.569 1.00 38.22 C ANISOU 47 CG MET A 6 4889 4888 4746 308 -292 -592 C ATOM 48 SD MET A 6 -6.202 -2.244 30.349 1.00 41.49 S ANISOU 48 SD MET A 6 5427 5291 5046 311 -393 -613 S ATOM 49 CE MET A 6 -5.628 -0.638 30.894 1.00 40.56 C ANISOU 49 CE MET A 6 5181 5222 5008 287 -357 -705 C ATOM 50 N ALA A 7 -7.595 -2.262 25.303 1.00 28.57 N ANISOU 50 N ALA A 7 3581 3661 3612 267 -109 -472 N ATOM 51 CA ALA A 7 -8.404 -3.216 24.567 1.00 27.17 C ANISOU 51 CA ALA A 7 3478 3452 3393 264 -103 -411 C ATOM 52 C ALA A 7 -8.372 -4.572 25.261 1.00 29.55 C ANISOU 52 C ALA A 7 3918 3701 3607 304 -215 -401 C ATOM 53 O ALA A 7 -7.421 -4.901 25.975 1.00 26.06 O ANISOU 53 O ALA A 7 3497 3254 3150 366 -311 -452 O ATOM 54 CB ALA A 7 -7.915 -3.349 23.125 1.00 29.33 C ANISOU 54 CB ALA A 7 3671 3758 3717 301 -76 -423 C ATOM 55 N PHE A 8 -9.426 -5.354 25.045 1.00 29.72 N ANISOU 55 N PHE A 8 4040 3678 3576 266 -210 -332 N ATOM 56 CA PHE A 8 -9.527 -6.660 25.671 1.00 29.62 C ANISOU 56 CA PHE A 8 4179 3596 3478 284 -317 -304 C ATOM 57 C PHE A 8 -8.439 -7.594 25.144 1.00 28.73 C ANISOU 57 C PHE A 8 4074 3457 3386 399 -426 -357 C ATOM 58 O PHE A 8 -7.930 -7.405 24.036 1.00 28.29 O ANISOU 58 O PHE A 8 3910 3442 3395 447 -392 -402 O ATOM 59 CB PHE A 8 -10.900 -7.273 25.407 1.00 30.86 C ANISOU 59 CB PHE A 8 4427 3712 3587 204 -282 -220 C ATOM 60 CG PHE A 8 -12.003 -6.667 26.224 1.00 30.31 C ANISOU 60 CG PHE A 8 4377 3666 3475 97 -202 -176 C ATOM 61 CD1 PHE A 8 -12.184 -7.033 27.547 1.00 31.90 C ANISOU 61 CD1 PHE A 8 4693 3848 3579 54 -248 -151 C ATOM 62 CD2 PHE A 8 -12.861 -5.734 25.668 1.00 32.01 C ANISOU 62 CD2 PHE A 8 4497 3926 3741 40 -84 -164 C ATOM 63 CE1 PHE A 8 -13.199 -6.477 28.302 1.00 34.91 C ANISOU 63 CE1 PHE A 8 5081 4271 3911 -45 -163 -125 C ATOM 64 CE2 PHE A 8 -13.878 -5.174 26.417 1.00 33.60 C ANISOU 64 CE2 PHE A 8 4700 4156 3909 -46 -10 -143 C ATOM 65 CZ PHE A 8 -14.047 -5.547 27.736 1.00 33.83 C ANISOU 65 CZ PHE A 8 4833 4183 3838 -90 -42 -129 C ATOM 66 N PRO A 9 -8.053 -8.602 25.927 1.00 30.79 N ANISOU 66 N PRO A 9 4462 3650 3588 447 -560 -357 N ATOM 67 CA PRO A 9 -7.152 -9.633 25.402 1.00 31.75 C ANISOU 67 CA PRO A 9 4603 3730 3732 568 -679 -414 C ATOM 68 C PRO A 9 -7.771 -10.319 24.193 1.00 31.94 C ANISOU 68 C PRO A 9 4648 3721 3767 565 -654 -389 C ATOM 69 O PRO A 9 -8.957 -10.654 24.185 1.00 32.31 O ANISOU 69 O PRO A 9 4788 3721 3767 474 -621 -304 O ATOM 70 CB PRO A 9 -6.989 -10.597 26.582 1.00 33.86 C ANISOU 70 CB PRO A 9 5044 3903 3918 593 -833 -386 C ATOM 71 CG PRO A 9 -7.285 -9.769 27.788 1.00 32.44 C ANISOU 71 CG PRO A 9 4881 3760 3685 510 -791 -354 C ATOM 72 CD PRO A 9 -8.341 -8.794 27.359 1.00 29.46 C ANISOU 72 CD PRO A 9 4422 3445 3327 399 -617 -313 C ATOM 73 N SER A 10 -6.955 -10.520 23.161 1.00 27.64 N ANISOU 73 N SER A 10 4010 3211 3282 663 -668 -472 N ATOM 74 CA SER A 10 -7.441 -10.973 21.865 1.00 29.85 C ANISOU 74 CA SER A 10 4280 3486 3574 666 -628 -468 C ATOM 75 C SER A 10 -7.226 -12.461 21.620 1.00 30.90 C ANISOU 75 C SER A 10 4532 3519 3692 757 -771 -499 C ATOM 76 O SER A 10 -7.518 -12.935 20.519 1.00 31.33 O ANISOU 76 O SER A 10 4580 3568 3756 775 -755 -516 O ATOM 77 CB SER A 10 -6.766 -10.173 20.747 1.00 28.40 C ANISOU 77 CB SER A 10 3913 3422 3454 701 -531 -541 C ATOM 78 OG SER A 10 -5.355 -10.266 20.836 1.00 27.11 O ANISOU 78 OG SER A 10 3665 3303 3332 817 -598 -652 O ATOM 79 N GLY A 11 -6.742 -13.206 22.617 1.00 35.91 N ANISOU 79 N GLY A 11 5280 4065 4298 815 -920 -506 N ATOM 80 CA GLY A 11 -6.382 -14.597 22.385 1.00 37.97 C ANISOU 80 CA GLY A 11 5652 4216 4560 923 -1078 -550 C ATOM 81 C GLY A 11 -7.538 -15.447 21.893 1.00 37.40 C ANISOU 81 C GLY A 11 5712 4046 4454 853 -1088 -475 C ATOM 82 O GLY A 11 -7.379 -16.255 20.975 1.00 38.82 O ANISOU 82 O GLY A 11 5906 4185 4660 933 -1145 -537 O ATOM 83 N LYS A 12 -8.717 -15.277 22.496 1.00 39.37 N ANISOU 83 N LYS A 12 6052 4262 4644 701 -1032 -351 N ATOM 84 CA LYS A 12 -9.871 -16.077 22.097 1.00 39.83 C ANISOU 84 CA LYS A 12 6232 4230 4673 616 -1041 -278 C ATOM 85 C LYS A 12 -10.297 -15.780 20.665 1.00 40.63 C ANISOU 85 C LYS A 12 6219 4404 4815 608 -933 -311 C ATOM 86 O LYS A 12 -10.840 -16.658 19.984 1.00 39.51 O ANISOU 86 O LYS A 12 6156 4186 4671 601 -979 -305 O ATOM 87 CB LYS A 12 -11.034 -15.833 23.059 1.00 41.91 C ANISOU 87 CB LYS A 12 6584 4474 4864 445 -982 -148 C ATOM 88 CG LYS A 12 -10.836 -16.443 24.438 1.00 46.20 C ANISOU 88 CG LYS A 12 7297 4920 5337 427 -1109 -91 C ATOM 89 CD LYS A 12 -11.966 -16.058 25.379 1.00 45.74 C ANISOU 89 CD LYS A 12 7301 4882 5196 249 -1020 25 C ATOM 90 CE LYS A 12 -11.894 -16.840 26.680 1.00 51.83 C ANISOU 90 CE LYS A 12 8275 5547 5872 210 -1152 102 C ATOM 91 NZ LYS A 12 -10.556 -16.728 27.323 1.00 50.73 N ANISOU 91 NZ LYS A 12 8132 5406 5736 345 -1263 36 N ATOM 92 N VAL A 13 -10.058 -14.560 20.189 1.00 26.70 N ANISOU 92 N VAL A 13 4280 2781 3085 607 -797 -344 N ATOM 93 CA VAL A 13 -10.472 -14.183 18.843 1.00 29.13 C ANISOU 93 CA VAL A 13 4486 3164 3417 591 -694 -364 C ATOM 94 C VAL A 13 -9.428 -14.558 17.792 1.00 29.40 C ANISOU 94 C VAL A 13 4444 3240 3486 734 -731 -489 C ATOM 95 O VAL A 13 -9.789 -14.879 16.655 1.00 30.25 O ANISOU 95 O VAL A 13 4538 3361 3593 742 -709 -514 O ATOM 96 CB VAL A 13 -10.791 -12.678 18.794 1.00 26.15 C ANISOU 96 CB VAL A 13 3972 2908 3056 511 -535 -328 C ATOM 97 CG1 VAL A 13 -11.340 -12.286 17.429 1.00 26.78 C ANISOU 97 CG1 VAL A 13 3969 3056 3150 483 -439 -327 C ATOM 98 CG2 VAL A 13 -11.776 -12.312 19.892 1.00 26.27 C ANISOU 98 CG2 VAL A 13 4051 2895 3036 384 -498 -228 C ATOM 99 N GLU A 14 -8.140 -14.531 18.149 1.00 31.28 N ANISOU 99 N GLU A 14 4625 3507 3753 847 -789 -578 N ATOM 100 CA GLU A 14 -7.091 -14.840 17.180 1.00 33.34 C ANISOU 100 CA GLU A 14 4788 3832 4047 984 -813 -715 C ATOM 101 C GLU A 14 -7.272 -16.231 16.586 1.00 33.38 C ANISOU 101 C GLU A 14 4909 3729 4045 1059 -933 -763 C ATOM 102 O GLU A 14 -7.056 -16.435 15.386 1.00 36.65 O ANISOU 102 O GLU A 14 5255 4206 4464 1120 -904 -849 O ATOM 103 CB GLU A 14 -5.715 -14.717 17.833 1.00 34.72 C ANISOU 103 CB GLU A 14 4890 4042 4260 1096 -880 -807 C ATOM 104 CG GLU A 14 -5.368 -13.320 18.310 1.00 35.05 C ANISOU 104 CG GLU A 14 4800 4198 4321 1033 -766 -785 C ATOM 105 CD GLU A 14 -4.125 -13.299 19.174 1.00 34.18 C ANISOU 105 CD GLU A 14 4641 4100 4244 1132 -859 -867 C ATOM 106 OE1 GLU A 14 -3.113 -13.913 18.775 1.00 36.95 O ANISOU 106 OE1 GLU A 14 4936 4473 4631 1274 -940 -997 O ATOM 107 OE2 GLU A 14 -4.158 -12.671 20.253 1.00 33.17 O ANISOU 107 OE2 GLU A 14 4528 3967 4110 1072 -855 -811 O ATOM 108 N GLY A 15 -7.670 -17.201 17.408 1.00 32.53 N ANISOU 108 N GLY A 15 4984 3457 3920 1049 -1071 -709 N ATOM 109 CA GLY A 15 -7.889 -18.557 16.940 1.00 33.95 C ANISOU 109 CA GLY A 15 5296 3504 4099 1111 -1204 -748 C ATOM 110 C GLY A 15 -9.097 -18.750 16.050 1.00 34.25 C ANISOU 110 C GLY A 15 5374 3526 4113 1011 -1143 -695 C ATOM 111 O GLY A 15 -9.394 -19.889 15.677 1.00 34.81 O ANISOU 111 O GLY A 15 5566 3474 4185 1045 -1257 -722 O ATOM 112 N CYS A 16 -9.806 -17.673 15.705 1.00 33.59 N ANISOU 112 N CYS A 16 5194 3557 4012 893 -977 -625 N ATOM 113 CA CYS A 16 -10.967 -17.740 14.830 1.00 33.58 C ANISOU 113 CA CYS A 16 5212 3557 3989 800 -917 -578 C ATOM 114 C CYS A 16 -10.788 -16.983 13.522 1.00 31.24 C ANISOU 114 C CYS A 16 4758 3420 3690 824 -792 -638 C ATOM 115 O CYS A 16 -11.668 -17.058 12.659 1.00 32.96 O ANISOU 115 O CYS A 16 4987 3649 3887 765 -754 -614 O ATOM 116 CB CYS A 16 -12.210 -17.196 15.548 1.00 29.80 C ANISOU 116 CB CYS A 16 4775 3062 3488 625 -844 -430 C ATOM 117 SG CYS A 16 -12.431 -17.810 17.230 1.00 34.76 S ANISOU 117 SG CYS A 16 5574 3541 4091 561 -952 -337 S ATOM 118 N MET A 17 -9.689 -16.255 13.353 1.00 30.94 N ANISOU 118 N MET A 17 4578 3508 3668 899 -730 -711 N ATOM 119 CA MET A 17 -9.470 -15.444 12.162 1.00 32.22 C ANISOU 119 CA MET A 17 4595 3831 3815 902 -601 -752 C ATOM 120 C MET A 17 -8.856 -16.292 11.055 1.00 34.79 C ANISOU 120 C MET A 17 4905 4188 4128 1029 -653 -895 C ATOM 121 O MET A 17 -7.813 -16.923 11.252 1.00 35.73 O ANISOU 121 O MET A 17 5015 4289 4273 1162 -743 -1011 O ATOM 122 CB MET A 17 -8.566 -14.251 12.478 1.00 32.49 C ANISOU 122 CB MET A 17 4481 3992 3873 906 -504 -763 C ATOM 123 CG MET A 17 -9.124 -13.320 13.541 1.00 28.52 C ANISOU 123 CG MET A 17 3983 3470 3384 789 -449 -640 C ATOM 124 SD MET A 17 -10.831 -12.839 13.215 1.00 29.38 S ANISOU 124 SD MET A 17 4136 3559 3467 635 -369 -505 S ATOM 125 CE MET A 17 -10.677 -12.081 11.597 1.00 28.32 C ANISOU 125 CE MET A 17 3873 3577 3308 636 -251 -536 C ATOM 126 N VAL A 18 -9.506 -16.299 9.892 1.00 32.28 N ANISOU 126 N VAL A 18 4579 3918 3766 994 -601 -895 N ATOM 127 CA VAL A 18 -9.058 -17.068 8.741 1.00 34.43 C ANISOU 127 CA VAL A 18 4838 4232 4010 1105 -638 -1035 C ATOM 128 C VAL A 18 -8.948 -16.139 7.539 1.00 35.62 C ANISOU 128 C VAL A 18 4857 4573 4104 1073 -488 -1048 C ATOM 129 O VAL A 18 -9.378 -14.985 7.568 1.00 32.21 O ANISOU 129 O VAL A 18 4368 4209 3662 960 -374 -935 O ATOM 130 CB VAL A 18 -9.999 -18.247 8.417 1.00 33.24 C ANISOU 130 CB VAL A 18 4843 3938 3848 1098 -754 -1037 C ATOM 131 CG1 VAL A 18 -10.153 -19.153 9.624 1.00 33.36 C ANISOU 131 CG1 VAL A 18 5007 3755 3911 1107 -904 -1002 C ATOM 132 CG2 VAL A 18 -11.351 -17.732 7.949 1.00 32.32 C ANISOU 132 CG2 VAL A 18 4747 3836 3696 952 -678 -915 C ATOM 133 N GLN A 19 -8.361 -16.669 6.472 1.00 39.43 N ANISOU 133 N GLN A 19 5298 5139 4545 1175 -494 -1190 N ATOM 134 CA GLN A 19 -8.229 -15.968 5.204 1.00 41.93 C ANISOU 134 CA GLN A 19 5508 5641 4784 1148 -362 -1213 C ATOM 135 C GLN A 19 -9.318 -16.437 4.249 1.00 41.30 C ANISOU 135 C GLN A 19 5519 5530 4642 1109 -387 -1195 C ATOM 136 O GLN A 19 -9.582 -17.637 4.136 1.00 41.67 O ANISOU 136 O GLN A 19 5672 5463 4698 1177 -514 -1270 O ATOM 137 CB GLN A 19 -6.849 -16.218 4.592 1.00 42.98 C ANISOU 137 CB GLN A 19 5520 5917 4894 1283 -337 -1396 C ATOM 138 CG GLN A 19 -6.534 -15.380 3.367 1.00 46.50 C ANISOU 138 CG GLN A 19 5843 6581 5246 1240 -180 -1414 C ATOM 139 CD GLN A 19 -5.198 -15.743 2.748 1.00 51.20 C ANISOU 139 CD GLN A 19 6311 7331 5811 1372 -152 -1614 C ATOM 140 OE1 GLN A 19 -4.353 -14.879 2.513 1.00 53.22 O ANISOU 140 OE1 GLN A 19 6417 7760 6044 1344 -25 -1633 O ATOM 141 NE2 GLN A 19 -4.999 -17.030 2.484 1.00 51.01 N ANISOU 141 NE2 GLN A 19 6344 7246 5792 1515 -274 -1772 N ATOM 142 N VAL A 20 -9.956 -15.486 3.571 1.00 33.83 N ANISOU 142 N VAL A 20 4537 4680 3639 999 -277 -1095 N ATOM 143 CA VAL A 20 -11.023 -15.778 2.620 1.00 32.14 C ANISOU 143 CA VAL A 20 4396 4454 3362 953 -298 -1069 C ATOM 144 C VAL A 20 -10.667 -15.121 1.295 1.00 37.09 C ANISOU 144 C VAL A 20 4932 5281 3878 945 -180 -1101 C ATOM 145 O VAL A 20 -10.575 -13.890 1.214 1.00 35.91 O ANISOU 145 O VAL A 20 4704 5232 3710 860 -63 -1003 O ATOM 146 CB VAL A 20 -12.394 -15.285 3.114 1.00 32.78 C ANISOU 146 CB VAL A 20 4541 4437 3476 816 -300 -898 C ATOM 147 CG1 VAL A 20 -13.459 -15.539 2.057 1.00 33.28 C ANISOU 147 CG1 VAL A 20 4664 4506 3475 772 -325 -881 C ATOM 148 CG2 VAL A 20 -12.764 -15.962 4.424 1.00 33.01 C ANISOU 148 CG2 VAL A 20 4666 4283 3595 807 -406 -862 C ATOM 149 N THR A 21 -10.469 -15.935 0.262 1.00 37.18 N ANISOU 149 N THR A 21 4963 5350 3815 1029 -215 -1238 N ATOM 150 CA THR A 21 -10.156 -15.447 -1.074 1.00 36.89 C ANISOU 150 CA THR A 21 4855 5514 3649 1020 -108 -1279 C ATOM 151 C THR A 21 -11.234 -15.923 -2.035 1.00 40.52 C ANISOU 151 C THR A 21 5413 5950 4032 995 -166 -1275 C ATOM 152 O THR A 21 -11.468 -17.129 -2.165 1.00 40.87 O ANISOU 152 O THR A 21 5543 5897 4089 1074 -288 -1385 O ATOM 153 CB THR A 21 -8.777 -15.924 -1.534 1.00 37.94 C ANISOU 153 CB THR A 21 4893 5783 3740 1152 -78 -1476 C ATOM 154 OG1 THR A 21 -7.778 -15.463 -0.616 1.00 38.78 O ANISOU 154 OG1 THR A 21 4898 5912 3925 1173 -32 -1482 O ATOM 155 CG2 THR A 21 -8.467 -15.387 -2.924 1.00 41.05 C ANISOU 155 CG2 THR A 21 5215 6404 3979 1124 48 -1511 C ATOM 156 N CYS A 22 -11.889 -14.975 -2.699 1.00 42.63 N ANISOU 156 N CYS A 22 5673 6300 4223 885 -90 -1151 N ATOM 157 CA CYS A 22 -12.887 -15.259 -3.725 1.00 46.52 C ANISOU 157 CA CYS A 22 6246 6801 4628 855 -138 -1142 C ATOM 158 C CYS A 22 -12.419 -14.602 -5.015 1.00 48.06 C ANISOU 158 C CYS A 22 6381 7217 4663 837 -22 -1160 C ATOM 159 O CYS A 22 -12.438 -13.373 -5.134 1.00 47.74 O ANISOU 159 O CYS A 22 6292 7258 4589 739 80 -1024 O ATOM 160 CB CYS A 22 -14.266 -14.746 -3.315 1.00 42.90 C ANISOU 160 CB CYS A 22 5847 6226 4229 738 -176 -967 C ATOM 161 SG CYS A 22 -15.591 -15.185 -4.462 1.00 48.20 S ANISOU 161 SG CYS A 22 6615 6885 4814 703 -264 -962 S ATOM 162 N GLY A 23 -11.997 -15.417 -5.976 1.00 58.84 N ANISOU 162 N GLY A 23 7755 8679 5924 928 -39 -1328 N ATOM 163 CA GLY A 23 -11.462 -14.892 -7.214 1.00 58.67 C ANISOU 163 CA GLY A 23 7676 8887 5728 912 78 -1362 C ATOM 164 C GLY A 23 -10.228 -14.045 -6.988 1.00 60.07 C ANISOU 164 C GLY A 23 7718 9209 5896 893 226 -1355 C ATOM 165 O GLY A 23 -9.156 -14.563 -6.661 1.00 62.79 O ANISOU 165 O GLY A 23 7984 9595 6279 996 241 -1507 O ATOM 166 N THR A 24 -10.377 -12.733 -7.143 1.00 55.76 N ANISOU 166 N THR A 24 7144 8735 5309 763 327 -1182 N ATOM 167 CA THR A 24 -9.265 -11.799 -7.057 1.00 56.53 C ANISOU 167 CA THR A 24 7114 8979 5384 714 477 -1156 C ATOM 168 C THR A 24 -9.200 -11.051 -5.731 1.00 56.65 C ANISOU 168 C THR A 24 7091 8872 5564 658 487 -1032 C ATOM 169 O THR A 24 -8.245 -10.302 -5.508 1.00 55.16 O ANISOU 169 O THR A 24 6792 8785 5383 617 599 -1017 O ATOM 170 CB THR A 24 -9.347 -10.789 -8.206 1.00 61.55 C ANISOU 170 CB THR A 24 7750 9787 5848 594 588 -1046 C ATOM 171 OG1 THR A 24 -8.169 -9.973 -8.213 1.00 60.33 O ANISOU 171 OG1 THR A 24 7468 9792 5661 538 740 -1039 O ATOM 172 CG2 THR A 24 -10.575 -9.903 -8.045 1.00 59.48 C ANISOU 172 CG2 THR A 24 7577 9399 5622 479 544 -824 C ATOM 173 N THR A 25 -10.178 -11.236 -4.848 1.00 49.98 N ANISOU 173 N THR A 25 6327 7819 4844 651 376 -950 N ATOM 174 CA THR A 25 -10.275 -10.474 -3.609 1.00 44.97 C ANISOU 174 CA THR A 25 5666 7068 4351 591 383 -826 C ATOM 175 C THR A 25 -9.887 -11.350 -2.424 1.00 41.43 C ANISOU 175 C THR A 25 5211 6493 4036 690 302 -925 C ATOM 176 O THR A 25 -10.331 -12.498 -2.324 1.00 41.21 O ANISOU 176 O THR A 25 5264 6360 4033 768 185 -1007 O ATOM 177 CB THR A 25 -11.691 -9.924 -3.418 1.00 43.43 C ANISOU 177 CB THR A 25 5560 6744 4197 501 328 -655 C ATOM 178 OG1 THR A 25 -12.008 -9.034 -4.496 1.00 49.57 O ANISOU 178 OG1 THR A 25 6350 7631 4853 412 392 -553 O ATOM 179 CG2 THR A 25 -11.805 -9.171 -2.099 1.00 40.68 C ANISOU 179 CG2 THR A 25 5184 6280 3994 448 335 -546 C ATOM 180 N THR A 26 -9.063 -10.802 -1.532 1.00 36.26 N ANISOU 180 N THR A 26 4468 5844 3466 682 354 -912 N ATOM 181 CA THR A 26 -8.633 -11.487 -0.320 1.00 34.11 C ANISOU 181 CA THR A 26 4190 5453 3316 768 274 -988 C ATOM 182 C THR A 26 -8.954 -10.615 0.885 1.00 30.54 C ANISOU 182 C THR A 26 3734 4892 2975 686 281 -846 C ATOM 183 O THR A 26 -8.564 -9.443 0.926 1.00 31.38 O ANISOU 183 O THR A 26 3762 5077 3084 603 383 -766 O ATOM 184 CB THR A 26 -7.131 -11.799 -0.357 1.00 37.76 C ANISOU 184 CB THR A 26 4530 6043 3773 866 319 -1154 C ATOM 185 OG1 THR A 26 -6.843 -12.650 -1.473 1.00 41.67 O ANISOU 185 OG1 THR A 26 5024 6645 4163 954 312 -1307 O ATOM 186 CG2 THR A 26 -6.694 -12.486 0.928 1.00 33.08 C ANISOU 186 CG2 THR A 26 3942 5318 3310 961 216 -1224 C ATOM 187 N LEU A 27 -9.661 -11.182 1.858 1.00 33.12 N ANISOU 187 N LEU A 27 4150 5043 3392 702 173 -817 N ATOM 188 CA LEU A 27 -9.977 -10.476 3.095 1.00 33.36 C ANISOU 188 CA LEU A 27 4182 4971 3523 636 172 -703 C ATOM 189 C LEU A 27 -10.047 -11.494 4.229 1.00 30.33 C ANISOU 189 C LEU A 27 3870 4435 3221 704 52 -751 C ATOM 190 O LEU A 27 -9.611 -12.641 4.086 1.00 32.82 O ANISOU 190 O LEU A 27 4215 4727 3527 812 -27 -879 O ATOM 191 CB LEU A 27 -11.271 -9.663 2.949 1.00 32.38 C ANISOU 191 CB LEU A 27 4106 4800 3397 521 190 -546 C ATOM 192 CG LEU A 27 -12.554 -10.360 2.492 1.00 31.54 C ANISOU 192 CG LEU A 27 4107 4614 3262 510 108 -523 C ATOM 193 CD1 LEU A 27 -13.118 -11.262 3.581 1.00 32.33 C ANISOU 193 CD1 LEU A 27 4290 4551 3445 530 -0 -530 C ATOM 194 CD2 LEU A 27 -13.585 -9.325 2.068 1.00 29.83 C ANISOU 194 CD2 LEU A 27 3899 4405 3031 406 145 -383 C ATOM 195 N ASN A 28 -10.601 -11.073 5.362 1.00 30.68 N ANISOU 195 N ASN A 28 3945 4371 3341 641 33 -649 N ATOM 196 CA ASN A 28 -10.621 -11.879 6.573 1.00 28.74 C ANISOU 196 CA ASN A 28 3771 3986 3163 684 -71 -671 C ATOM 197 C ASN A 28 -12.003 -12.471 6.822 1.00 28.22 C ANISOU 197 C ASN A 28 3829 3785 3107 631 -148 -601 C ATOM 198 O ASN A 28 -13.022 -11.929 6.388 1.00 30.00 O ANISOU 198 O ASN A 28 4064 4019 3315 544 -110 -511 O ATOM 199 CB ASN A 28 -10.196 -11.046 7.786 1.00 29.10 C ANISOU 199 CB ASN A 28 3764 4015 3277 649 -37 -619 C ATOM 200 CG ASN A 28 -8.900 -10.298 7.553 1.00 29.47 C ANISOU 200 CG ASN A 28 3674 4201 3323 675 50 -675 C ATOM 201 OD1 ASN A 28 -7.813 -10.857 7.697 1.00 33.83 O ANISOU 201 OD1 ASN A 28 4181 4786 3887 775 14 -794 O ATOM 202 ND2 ASN A 28 -9.008 -9.025 7.192 1.00 30.39 N ANISOU 202 ND2 ASN A 28 3721 4397 3431 582 159 -590 N ATOM 203 N GLY A 29 -12.020 -13.598 7.533 1.00 29.35 N ANISOU 203 N GLY A 29 4068 3803 3283 681 -264 -644 N ATOM 204 CA GLY A 29 -13.263 -14.225 7.931 1.00 28.48 C ANISOU 204 CA GLY A 29 4076 3559 3188 614 -339 -576 C ATOM 205 C GLY A 29 -13.202 -14.658 9.380 1.00 26.91 C ANISOU 205 C GLY A 29 3950 3236 3040 608 -412 -548 C ATOM 206 O GLY A 29 -12.128 -14.765 9.978 1.00 26.65 O ANISOU 206 O GLY A 29 3895 3203 3029 686 -439 -606 O ATOM 207 N LEU A 30 -14.381 -14.907 9.945 1.00 28.26 N ANISOU 207 N LEU A 30 4207 3307 3223 509 -445 -458 N ATOM 208 CA LEU A 30 -14.522 -15.328 11.334 1.00 29.57 C ANISOU 208 CA LEU A 30 4461 3357 3418 474 -509 -409 C ATOM 209 C LEU A 30 -14.986 -16.778 11.365 1.00 30.07 C ANISOU 209 C LEU A 30 4673 3275 3477 476 -643 -428 C ATOM 210 O LEU A 30 -16.069 -17.098 10.865 1.00 29.96 O ANISOU 210 O LEU A 30 4701 3228 3454 399 -654 -393 O ATOM 211 CB LEU A 30 -15.503 -14.430 12.087 1.00 28.56 C ANISOU 211 CB LEU A 30 4310 3237 3303 342 -430 -291 C ATOM 212 CG LEU A 30 -15.642 -14.716 13.584 1.00 29.22 C ANISOU 212 CG LEU A 30 4478 3229 3397 291 -474 -235 C ATOM 213 CD1 LEU A 30 -14.351 -14.382 14.315 1.00 26.88 C ANISOU 213 CD1 LEU A 30 4145 2957 3111 373 -479 -277 C ATOM 214 CD2 LEU A 30 -16.809 -13.940 14.174 1.00 26.62 C ANISOU 214 CD2 LEU A 30 4122 2920 3073 156 -391 -136 C ATOM 215 N TRP A 31 -14.173 -17.644 11.964 1.00 30.43 N ANISOU 215 N TRP A 31 4799 3227 3536 562 -754 -483 N ATOM 216 CA TRP A 31 -14.391 -19.091 11.935 1.00 33.10 C ANISOU 216 CA TRP A 31 5290 3408 3878 587 -905 -516 C ATOM 217 C TRP A 31 -14.947 -19.537 13.284 1.00 32.13 C ANISOU 217 C TRP A 31 5299 3150 3759 486 -970 -410 C ATOM 218 O TRP A 31 -14.204 -19.885 14.202 1.00 35.30 O ANISOU 218 O TRP A 31 5765 3480 4168 541 -1050 -417 O ATOM 219 CB TRP A 31 -13.090 -19.810 11.590 1.00 33.09 C ANISOU 219 CB TRP A 31 5296 3388 3891 765 -1003 -661 C ATOM 220 CG TRP A 31 -13.192 -21.306 11.478 1.00 35.69 C ANISOU 220 CG TRP A 31 5785 3542 4233 816 -1176 -716 C ATOM 221 CD1 TRP A 31 -14.328 -22.049 11.330 1.00 36.15 C ANISOU 221 CD1 TRP A 31 5965 3481 4289 714 -1239 -661 C ATOM 222 CD2 TRP A 31 -12.104 -22.237 11.498 1.00 35.12 C ANISOU 222 CD2 TRP A 31 5766 3389 4190 983 -1318 -844 C ATOM 223 NE1 TRP A 31 -14.013 -23.386 11.261 1.00 38.59 N ANISOU 223 NE1 TRP A 31 6412 3627 4622 802 -1414 -740 N ATOM 224 CE2 TRP A 31 -12.653 -23.527 11.361 1.00 38.39 C ANISOU 224 CE2 TRP A 31 6349 3620 4618 976 -1469 -856 C ATOM 225 CE3 TRP A 31 -10.717 -22.104 11.621 1.00 36.26 C ANISOU 225 CE3 TRP A 31 5826 3597 4356 1141 -1337 -956 C ATOM 226 CZ2 TRP A 31 -11.864 -24.677 11.344 1.00 37.90 C ANISOU 226 CZ2 TRP A 31 6383 3424 4592 1130 -1646 -976 C ATOM 227 CZ3 TRP A 31 -9.936 -23.246 11.604 1.00 40.74 C ANISOU 227 CZ3 TRP A 31 6475 4047 4959 1298 -1509 -1082 C ATOM 228 CH2 TRP A 31 -10.512 -24.515 11.467 1.00 39.73 C ANISOU 228 CH2 TRP A 31 6525 3724 4846 1297 -1665 -1091 C ATOM 229 N LEU A 32 -16.275 -19.635 13.355 1.00 33.48 N ANISOU 229 N LEU A 32 5520 3281 3921 336 -948 -317 N ATOM 230 CA LEU A 32 -16.956 -20.110 14.587 1.00 33.01 C ANISOU 230 CA LEU A 32 5590 3103 3850 209 -997 -208 C ATOM 231 C LEU A 32 -17.624 -21.452 14.277 1.00 36.67 C ANISOU 231 C LEU A 32 6204 3410 4320 160 -1125 -206 C ATOM 232 O LEU A 32 -18.325 -21.538 13.259 1.00 39.14 O ANISOU 232 O LEU A 32 6482 3751 4640 128 -1104 -230 O ATOM 233 CB LEU A 32 -17.977 -19.066 15.040 1.00 34.79 C ANISOU 233 CB LEU A 32 5732 3424 4063 60 -855 -107 C ATOM 234 CG LEU A 32 -17.379 -17.722 15.449 1.00 34.04 C ANISOU 234 CG LEU A 32 5501 3463 3969 96 -738 -105 C ATOM 235 CD1 LEU A 32 -18.468 -16.737 15.833 1.00 31.44 C ANISOU 235 CD1 LEU A 32 5092 3217 3637 -40 -610 -21 C ATOM 236 CD2 LEU A 32 -16.386 -17.899 16.586 1.00 34.95 C ANISOU 236 CD2 LEU A 32 5681 3527 4072 155 -801 -107 C ATOM 237 N ASP A 33 -17.399 -22.448 15.134 1.00 42.73 N ANISOU 237 N ASP A 33 7140 4014 5083 153 -1260 -175 N ATOM 238 CA ASP A 33 -17.962 -23.805 14.921 1.00 42.64 C ANISOU 238 CA ASP A 33 7295 3821 5083 101 -1404 -168 C ATOM 239 C ASP A 33 -17.596 -24.265 13.507 1.00 40.78 C ANISOU 239 C ASP A 33 7029 3587 4879 237 -1461 -311 C ATOM 240 O ASP A 33 -16.408 -24.517 13.261 1.00 43.18 O ANISOU 240 O ASP A 33 7327 3880 5199 416 -1532 -423 O ATOM 241 CB ASP A 33 -19.467 -23.847 15.188 1.00 43.75 C ANISOU 241 CB ASP A 33 7468 3947 5210 -120 -1349 -50 C ATOM 242 CG ASP A 33 -19.824 -23.598 16.642 1.00 44.20 C ANISOU 242 CG ASP A 33 7580 3991 5221 -259 -1306 81 C ATOM 243 OD1 ASP A 33 -19.094 -24.094 17.514 1.00 47.15 O ANISOU 243 OD1 ASP A 33 8079 4260 5576 -215 -1407 104 O ATOM 244 OD2 ASP A 33 -20.829 -22.913 16.886 1.00 47.18 O ANISOU 244 OD2 ASP A 33 7875 4469 5582 -406 -1176 155 O ATOM 245 N ASP A 34 -18.563 -24.280 12.590 1.00 40.06 N ANISOU 245 N ASP A 34 6900 3530 4791 159 -1422 -316 N ATOM 246 CA ASP A 34 -18.255 -24.790 11.257 1.00 42.11 C ANISOU 246 CA ASP A 34 7146 3790 5066 283 -1485 -455 C ATOM 247 C ASP A 34 -18.737 -23.830 10.175 1.00 42.22 C ANISOU 247 C ASP A 34 6995 3990 5058 266 -1345 -479 C ATOM 248 O ASP A 34 -19.082 -24.248 9.066 1.00 40.40 O ANISOU 248 O ASP A 34 6765 3760 4825 288 -1383 -555 O ATOM 249 CB ASP A 34 -18.822 -26.200 11.054 1.00 45.27 C ANISOU 249 CB ASP A 34 7722 3986 5492 234 -1651 -470 C ATOM 250 CG ASP A 34 -20.326 -26.218 10.841 1.00 48.94 C ANISOU 250 CG ASP A 34 8189 4448 5956 36 -1610 -384 C ATOM 251 OD1 ASP A 34 -21.020 -25.295 11.313 1.00 47.04 O ANISOU 251 OD1 ASP A 34 7856 4320 5698 -91 -1472 -279 O ATOM 252 OD2 ASP A 34 -20.814 -27.173 10.199 1.00 51.59 O ANISOU 252 OD2 ASP A 34 8617 4669 6315 12 -1721 -432 O ATOM 253 N VAL A 35 -18.744 -22.536 10.485 1.00 35.13 N ANISOU 253 N VAL A 35 5961 3246 4143 232 -1192 -416 N ATOM 254 CA VAL A 35 -19.158 -21.489 9.560 1.00 34.48 C ANISOU 254 CA VAL A 35 5725 3335 4039 216 -1062 -421 C ATOM 255 C VAL A 35 -18.091 -20.404 9.558 1.00 35.43 C ANISOU 255 C VAL A 35 5716 3602 4146 318 -958 -450 C ATOM 256 O VAL A 35 -17.544 -20.057 10.610 1.00 33.31 O ANISOU 256 O VAL A 35 5444 3326 3886 325 -936 -410 O ATOM 257 CB VAL A 35 -20.532 -20.900 9.950 1.00 34.75 C ANISOU 257 CB VAL A 35 5720 3404 4081 36 -979 -298 C ATOM 258 CG1 VAL A 35 -20.930 -19.779 9.000 1.00 33.16 C ANISOU 258 CG1 VAL A 35 5368 3368 3863 34 -864 -300 C ATOM 259 CG2 VAL A 35 -21.596 -21.988 9.974 1.00 35.49 C ANISOU 259 CG2 VAL A 35 5933 3359 4193 -85 -1079 -268 C ATOM 260 N VAL A 36 -17.786 -19.875 8.377 1.00 32.86 N ANISOU 260 N VAL A 36 5287 3409 3791 390 -895 -521 N ATOM 261 CA VAL A 36 -16.882 -18.740 8.233 1.00 32.54 C ANISOU 261 CA VAL A 36 5111 3520 3733 459 -780 -539 C ATOM 262 C VAL A 36 -17.711 -17.537 7.806 1.00 32.92 C ANISOU 262 C VAL A 36 5055 3687 3766 365 -658 -457 C ATOM 263 O VAL A 36 -18.367 -17.565 6.757 1.00 33.77 O ANISOU 263 O VAL A 36 5150 3835 3846 344 -656 -471 O ATOM 264 CB VAL A 36 -15.756 -19.025 7.227 1.00 33.15 C ANISOU 264 CB VAL A 36 5148 3669 3779 614 -798 -685 C ATOM 265 CG1 VAL A 36 -14.977 -17.753 6.935 1.00 33.40 C ANISOU 265 CG1 VAL A 36 5028 3877 3786 649 -661 -689 C ATOM 266 CG2 VAL A 36 -14.831 -20.107 7.763 1.00 36.53 C ANISOU 266 CG2 VAL A 36 5664 3980 4237 728 -926 -775 C ATOM 267 N TYR A 37 -17.688 -16.487 8.622 1.00 30.72 N ANISOU 267 N TYR A 37 4705 3458 3508 315 -566 -376 N ATOM 268 CA TYR A 37 -18.424 -15.259 8.355 1.00 31.19 C ANISOU 268 CA TYR A 37 4667 3616 3567 236 -458 -298 C ATOM 269 C TYR A 37 -17.482 -14.217 7.769 1.00 30.01 C ANISOU 269 C TYR A 37 4406 3602 3395 303 -366 -325 C ATOM 270 O TYR A 37 -16.365 -14.031 8.261 1.00 29.53 O ANISOU 270 O TYR A 37 4315 3563 3343 368 -347 -361 O ATOM 271 CB TYR A 37 -19.071 -14.712 9.631 1.00 29.77 C ANISOU 271 CB TYR A 37 4478 3404 3428 133 -415 -200 C ATOM 272 CG TYR A 37 -19.945 -15.697 10.380 1.00 31.28 C ANISOU 272 CG TYR A 37 4779 3472 3636 43 -491 -161 C ATOM 273 CD1 TYR A 37 -19.387 -16.666 11.207 1.00 31.97 C ANISOU 273 CD1 TYR A 37 4978 3446 3722 67 -579 -179 C ATOM 274 CD2 TYR A 37 -21.329 -15.647 10.273 1.00 30.67 C ANISOU 274 CD2 TYR A 37 4693 3390 3573 -73 -480 -105 C ATOM 275 CE1 TYR A 37 -20.183 -17.563 11.896 1.00 31.49 C ANISOU 275 CE1 TYR A 37 5029 3267 3668 -34 -648 -129 C ATOM 276 CE2 TYR A 37 -22.132 -16.540 10.960 1.00 32.60 C ANISOU 276 CE2 TYR A 37 5029 3529 3827 -177 -539 -66 C ATOM 277 CZ TYR A 37 -21.554 -17.495 11.769 1.00 32.84 C ANISOU 277 CZ TYR A 37 5183 3445 3850 -163 -621 -72 C ATOM 278 OH TYR A 37 -22.349 -18.385 12.453 1.00 33.56 O ANISOU 278 OH TYR A 37 5380 3427 3944 -284 -681 -20 O ATOM 279 N CYS A 38 -17.937 -13.532 6.724 1.00 30.13 N ANISOU 279 N CYS A 38 4362 3708 3379 281 -312 -303 N ATOM 280 CA CYS A 38 -17.121 -12.541 6.040 1.00 28.43 C ANISOU 280 CA CYS A 38 4051 3623 3129 322 -223 -314 C ATOM 281 C CYS A 38 -18.043 -11.591 5.288 1.00 27.87 C ANISOU 281 C CYS A 38 3933 3615 3041 255 -173 -237 C ATOM 282 O CYS A 38 -19.199 -11.938 5.011 1.00 29.21 O ANISOU 282 O CYS A 38 4142 3742 3214 203 -222 -210 O ATOM 283 CB CYS A 38 -16.124 -13.209 5.077 1.00 33.69 C ANISOU 283 CB CYS A 38 4720 4348 3732 428 -246 -434 C ATOM 284 SG CYS A 38 -16.857 -13.829 3.546 1.00 34.54 S ANISOU 284 SG CYS A 38 4874 4487 3762 435 -296 -479 S ATOM 285 N PRO A 39 -17.574 -10.387 4.958 1.00 27.88 N ANISOU 285 N PRO A 39 3854 3712 3029 250 -84 -198 N ATOM 286 CA PRO A 39 -18.405 -9.462 4.177 1.00 26.84 C ANISOU 286 CA PRO A 39 3689 3629 2878 195 -53 -120 C ATOM 287 C PRO A 39 -18.746 -10.044 2.812 1.00 28.83 C ANISOU 287 C PRO A 39 3982 3927 3045 216 -99 -159 C ATOM 288 O PRO A 39 -17.906 -10.658 2.150 1.00 29.35 O ANISOU 288 O PRO A 39 4063 4047 3042 284 -104 -248 O ATOM 289 CB PRO A 39 -17.528 -8.211 4.054 1.00 27.47 C ANISOU 289 CB PRO A 39 3692 3795 2951 193 43 -82 C ATOM 290 CG PRO A 39 -16.569 -8.304 5.193 1.00 25.68 C ANISOU 290 CG PRO A 39 3442 3540 2774 223 64 -121 C ATOM 291 CD PRO A 39 -16.305 -9.765 5.379 1.00 26.48 C ANISOU 291 CD PRO A 39 3611 3589 2863 285 -15 -216 C ATOM 292 N ARG A 40 -19.997 -9.839 2.391 1.00 25.38 N ANISOU 292 N ARG A 40 3556 3473 2613 163 -136 -103 N ATOM 293 CA ARG A 40 -20.486 -10.488 1.180 1.00 25.88 C ANISOU 293 CA ARG A 40 3667 3566 2599 178 -200 -144 C ATOM 294 C ARG A 40 -19.878 -9.908 -0.091 1.00 27.26 C ANISOU 294 C ARG A 40 3825 3871 2663 205 -152 -144 C ATOM 295 O ARG A 40 -19.928 -10.565 -1.136 1.00 27.77 O ANISOU 295 O ARG A 40 3932 3981 2637 238 -196 -208 O ATOM 296 CB ARG A 40 -22.012 -10.405 1.108 1.00 25.27 C ANISOU 296 CB ARG A 40 3596 3440 2563 112 -260 -87 C ATOM 297 CG ARG A 40 -22.570 -9.004 0.913 1.00 28.46 C ANISOU 297 CG ARG A 40 3941 3885 2989 71 -222 17 C ATOM 298 CD ARG A 40 -24.063 -9.055 0.628 1.00 26.11 C ANISOU 298 CD ARG A 40 3640 3555 2724 24 -299 47 C ATOM 299 NE ARG A 40 -24.693 -7.741 0.728 1.00 25.78 N ANISOU 299 NE ARG A 40 3535 3523 2735 -6 -277 138 N ATOM 300 CZ ARG A 40 -25.971 -7.504 0.449 1.00 28.44 C ANISOU 300 CZ ARG A 40 3846 3848 3111 -37 -341 169 C ATOM 301 NH1 ARG A 40 -26.758 -8.493 0.048 1.00 29.23 N ANISOU 301 NH1 ARG A 40 3976 3931 3199 -54 -426 119 N ATOM 302 NH2 ARG A 40 -26.462 -6.278 0.568 1.00 28.70 N ANISOU 302 NH2 ARG A 40 3821 3882 3201 -48 -329 243 N ATOM 303 N HIS A 41 -19.303 -8.706 -0.036 1.00 26.59 N ANISOU 303 N HIS A 41 3681 3845 2576 186 -64 -76 N ATOM 304 CA HIS A 41 -18.715 -8.114 -1.232 1.00 28.47 C ANISOU 304 CA HIS A 41 3908 4211 2698 190 -10 -62 C ATOM 305 C HIS A 41 -17.361 -8.720 -1.590 1.00 31.38 C ANISOU 305 C HIS A 41 4264 4670 2989 256 37 -174 C ATOM 306 O HIS A 41 -16.680 -8.195 -2.478 1.00 31.05 O ANISOU 306 O HIS A 41 4199 4755 2845 250 106 -168 O ATOM 307 CB HIS A 41 -18.599 -6.592 -1.079 1.00 27.82 C ANISOU 307 CB HIS A 41 3775 4150 2644 133 61 59 C ATOM 308 CG HIS A 41 -17.544 -6.146 -0.113 1.00 27.35 C ANISOU 308 CG HIS A 41 3655 4087 2648 134 140 53 C ATOM 309 ND1 HIS A 41 -17.847 -5.622 1.125 1.00 28.32 N ANISOU 309 ND1 HIS A 41 3747 4117 2895 107 145 100 N ATOM 310 CD2 HIS A 41 -16.194 -6.116 -0.213 1.00 30.52 C ANISOU 310 CD2 HIS A 41 4014 4577 3006 158 216 -2 C ATOM 311 CE1 HIS A 41 -16.728 -5.305 1.753 1.00 27.51 C ANISOU 311 CE1 HIS A 41 3594 4037 2823 115 212 78 C ATOM 312 NE2 HIS A 41 -15.711 -5.595 0.962 1.00 26.98 N ANISOU 312 NE2 HIS A 41 3512 4078 2659 145 256 16 N ATOM 313 N VAL A 42 -16.957 -9.806 -0.926 1.00 29.75 N ANISOU 313 N VAL A 42 4072 4403 2828 317 -2 -279 N ATOM 314 CA VAL A 42 -15.781 -10.553 -1.352 1.00 32.97 C ANISOU 314 CA VAL A 42 4469 4893 3167 401 18 -414 C ATOM 315 C VAL A 42 -16.007 -11.186 -2.719 1.00 34.76 C ANISOU 315 C VAL A 42 4745 5198 3267 433 -20 -487 C ATOM 316 O VAL A 42 -15.045 -11.445 -3.451 1.00 35.24 O ANISOU 316 O VAL A 42 4778 5383 3230 489 27 -587 O ATOM 317 CB VAL A 42 -15.411 -11.617 -0.292 1.00 33.62 C ANISOU 317 CB VAL A 42 4572 4865 3337 467 -45 -506 C ATOM 318 CG1 VAL A 42 -16.468 -12.713 -0.232 1.00 30.28 C ANISOU 318 CG1 VAL A 42 4245 4318 2942 471 -168 -534 C ATOM 319 CG2 VAL A 42 -14.033 -12.205 -0.569 1.00 33.05 C ANISOU 319 CG2 VAL A 42 4461 4879 3218 568 -20 -652 C ATOM 320 N ILE A 43 -17.268 -11.428 -3.089 1.00 29.22 N ANISOU 320 N ILE A 43 4107 4434 2560 399 -104 -446 N ATOM 321 CA ILE A 43 -17.592 -12.002 -4.394 1.00 30.69 C ANISOU 321 CA ILE A 43 4348 4692 2623 425 -153 -514 C ATOM 322 C ILE A 43 -17.613 -10.969 -5.506 1.00 32.73 C ANISOU 322 C ILE A 43 4593 5090 2754 376 -89 -432 C ATOM 323 O ILE A 43 -17.756 -11.339 -6.679 1.00 34.74 O ANISOU 323 O ILE A 43 4891 5432 2877 396 -117 -488 O ATOM 324 CB ILE A 43 -18.959 -12.709 -4.353 1.00 31.99 C ANISOU 324 CB ILE A 43 4584 4733 2837 401 -281 -508 C ATOM 325 CG1 ILE A 43 -20.087 -11.675 -4.289 1.00 28.34 C ANISOU 325 CG1 ILE A 43 4109 4245 2415 310 -288 -355 C ATOM 326 CG2 ILE A 43 -19.034 -13.657 -3.166 1.00 30.30 C ANISOU 326 CG2 ILE A 43 4398 4365 2750 422 -346 -558 C ATOM 327 CD1 ILE A 43 -21.471 -12.278 -4.207 1.00 29.04 C ANISOU 327 CD1 ILE A 43 4243 4227 2563 275 -406 -349 C ATOM 328 N CYS A 44 -17.475 -9.688 -5.176 1.00 32.86 N ANISOU 328 N CYS A 44 4559 5126 2801 310 -10 -302 N ATOM 329 CA CYS A 44 -17.590 -8.618 -6.155 1.00 35.48 C ANISOU 329 CA CYS A 44 4896 5564 3022 248 37 -196 C ATOM 330 C CYS A 44 -16.241 -8.304 -6.786 1.00 39.12 C ANISOU 330 C CYS A 44 5312 6194 3359 252 158 -236 C ATOM 331 O CYS A 44 -15.214 -8.263 -6.102 1.00 37.94 O ANISOU 331 O CYS A 44 5091 6062 3264 272 233 -282 O ATOM 332 CB CYS A 44 -18.153 -7.355 -5.502 1.00 35.85 C ANISOU 332 CB CYS A 44 4918 5531 3171 172 50 -34 C ATOM 333 SG CYS A 44 -19.890 -7.449 -5.022 1.00 33.96 S ANISOU 333 SG CYS A 44 4714 5138 3052 150 -80 27 S ATOM 334 N THR A 45 -16.253 -8.093 -8.099 1.00 42.64 N ANISOU 334 N THR A 45 5796 6772 3633 229 176 -221 N ATOM 335 CA THR A 45 -15.128 -7.460 -8.762 1.00 43.88 C ANISOU 335 CA THR A 45 5910 7104 3659 190 308 -212 C ATOM 336 C THR A 45 -15.162 -5.959 -8.486 1.00 45.25 C ANISOU 336 C THR A 45 6065 7253 3874 84 364 -25 C ATOM 337 O THR A 45 -16.140 -5.422 -7.961 1.00 42.74 O ANISOU 337 O THR A 45 5776 6796 3668 52 292 88 O ATOM 338 CB THR A 45 -15.163 -7.733 -10.266 1.00 45.21 C ANISOU 338 CB THR A 45 6137 7429 3610 191 309 -253 C ATOM 339 OG1 THR A 45 -16.267 -7.034 -10.856 1.00 43.71 O ANISOU 339 OG1 THR A 45 6030 7205 3372 124 238 -103 O ATOM 340 CG2 THR A 45 -15.316 -9.225 -10.536 1.00 46.14 C ANISOU 340 CG2 THR A 45 6287 7542 3702 300 227 -441 C ATOM 341 N SER A 46 -14.073 -5.272 -8.839 1.00 60.17 N ANISOU 341 N SER A 46 7904 9280 5678 25 494 2 N ATOM 342 CA SER A 46 -14.052 -3.820 -8.683 1.00 59.01 C ANISOU 342 CA SER A 46 7752 9106 5562 -86 542 182 C ATOM 343 C SER A 46 -15.170 -3.155 -9.477 1.00 59.06 C ANISOU 343 C SER A 46 7865 9078 5497 -143 461 332 C ATOM 344 O SER A 46 -15.622 -2.062 -9.117 1.00 61.60 O ANISOU 344 O SER A 46 8205 9298 5903 -208 438 484 O ATOM 345 CB SER A 46 -12.691 -3.265 -9.103 1.00 60.09 C ANISOU 345 CB SER A 46 7821 9416 5594 -157 697 183 C ATOM 346 OG SER A 46 -12.823 -1.967 -9.654 1.00 66.07 O ANISOU 346 OG SER A 46 8628 10192 6282 -284 729 369 O ATOM 347 N GLU A 47 -15.630 -3.800 -10.552 1.00 47.30 N ANISOU 347 N GLU A 47 6447 7668 3856 -113 406 285 N ATOM 348 CA GLU A 47 -16.746 -3.272 -11.328 1.00 48.20 C ANISOU 348 CA GLU A 47 6665 7747 3900 -152 305 415 C ATOM 349 C GLU A 47 -18.083 -3.568 -10.660 1.00 45.98 C ANISOU 349 C GLU A 47 6404 7284 3782 -98 159 423 C ATOM 350 O GLU A 47 -18.994 -2.732 -10.691 1.00 45.92 O ANISOU 350 O GLU A 47 6440 7184 3822 -135 79 560 O ATOM 351 CB GLU A 47 -16.713 -3.854 -12.741 1.00 51.72 C ANISOU 351 CB GLU A 47 7181 8359 4111 -141 299 354 C ATOM 352 CG GLU A 47 -17.931 -3.545 -13.589 1.00 56.61 C ANISOU 352 CG GLU A 47 7914 8946 4649 -161 167 460 C ATOM 353 CD GLU A 47 -17.588 -3.429 -15.059 1.00 62.11 C ANISOU 353 CD GLU A 47 8689 9837 5072 -210 207 483 C ATOM 354 OE1 GLU A 47 -16.458 -2.999 -15.370 1.00 65.78 O ANISOU 354 OE1 GLU A 47 9125 10445 5425 -280 354 501 O ATOM 355 OE2 GLU A 47 -18.442 -3.775 -15.901 1.00 62.15 O ANISOU 355 OE2 GLU A 47 8783 9861 4971 -185 93 480 O ATOM 356 N ASP A 48 -18.219 -4.750 -10.052 1.00 40.71 N ANISOU 356 N ASP A 48 5702 6562 3202 -14 120 274 N ATOM 357 CA ASP A 48 -19.465 -5.099 -9.376 1.00 41.43 C ANISOU 357 CA ASP A 48 5802 6492 3445 21 -6 274 C ATOM 358 C ASP A 48 -19.767 -4.148 -8.224 1.00 38.22 C ANISOU 358 C ASP A 48 5349 5952 3223 -14 -2 381 C ATOM 359 O ASP A 48 -20.938 -3.925 -7.899 1.00 38.15 O ANISOU 359 O ASP A 48 5349 5831 3315 -14 -101 435 O ATOM 360 CB ASP A 48 -19.403 -6.540 -8.864 1.00 40.31 C ANISOU 360 CB ASP A 48 5640 6313 3362 102 -38 103 C ATOM 361 CG ASP A 48 -19.250 -7.553 -9.983 1.00 43.01 C ANISOU 361 CG ASP A 48 6035 6769 3539 151 -66 -23 C ATOM 362 OD1 ASP A 48 -19.719 -7.278 -11.107 1.00 44.21 O ANISOU 362 OD1 ASP A 48 6252 6996 3550 125 -109 27 O ATOM 363 OD2 ASP A 48 -18.662 -8.627 -9.736 1.00 42.46 O ANISOU 363 OD2 ASP A 48 5945 6710 3480 219 -54 -177 O ATOM 364 N MET A 49 -18.729 -3.578 -7.605 1.00 43.23 N ANISOU 364 N MET A 49 5923 6601 3900 -44 111 402 N ATOM 365 CA MET A 49 -18.917 -2.737 -6.425 1.00 41.26 C ANISOU 365 CA MET A 49 5625 6225 3827 -70 118 479 C ATOM 366 C MET A 49 -19.814 -1.536 -6.705 1.00 40.20 C ANISOU 366 C MET A 49 5531 6022 3720 -119 53 635 C ATOM 367 O MET A 49 -20.496 -1.049 -5.795 1.00 37.06 O ANISOU 367 O MET A 49 5103 5498 3481 -117 8 677 O ATOM 368 CB MET A 49 -17.561 -2.260 -5.902 1.00 40.24 C ANISOU 368 CB MET A 49 5429 6142 3718 -102 247 475 C ATOM 369 CG MET A 49 -16.595 -3.374 -5.540 1.00 44.01 C ANISOU 369 CG MET A 49 5855 6682 4187 -41 304 315 C ATOM 370 SD MET A 49 -17.069 -4.241 -4.035 1.00 44.71 S ANISOU 370 SD MET A 49 5912 6617 4460 28 240 227 S ATOM 371 CE MET A 49 -15.548 -5.107 -3.654 1.00 39.45 C ANISOU 371 CE MET A 49 5181 6032 3777 88 321 73 C ATOM 372 N LEU A 50 -19.829 -1.047 -7.947 1.00 37.35 N ANISOU 372 N LEU A 50 5242 5745 3204 -161 41 719 N ATOM 373 CA LEU A 50 -20.537 0.196 -8.241 1.00 38.42 C ANISOU 373 CA LEU A 50 5428 5809 3362 -207 -28 879 C ATOM 374 C LEU A 50 -22.050 0.022 -8.148 1.00 35.70 C ANISOU 374 C LEU A 50 5098 5361 3107 -157 -178 883 C ATOM 375 O LEU A 50 -22.757 0.932 -7.701 1.00 38.13 O ANISOU 375 O LEU A 50 5396 5553 3538 -162 -241 970 O ATOM 376 CB LEU A 50 -20.134 0.712 -9.622 1.00 42.02 C ANISOU 376 CB LEU A 50 5972 6384 3609 -273 -7 976 C ATOM 377 CG LEU A 50 -18.628 0.778 -9.892 1.00 44.39 C ANISOU 377 CG LEU A 50 6248 6826 3793 -334 152 957 C ATOM 378 CD1 LEU A 50 -18.348 1.182 -11.334 1.00 46.64 C ANISOU 378 CD1 LEU A 50 6628 7247 3844 -408 172 1050 C ATOM 379 CD2 LEU A 50 -17.951 1.731 -8.918 1.00 43.45 C ANISOU 379 CD2 LEU A 50 6066 6634 3811 -388 232 1019 C ATOM 380 N ASN A 51 -22.569 -1.134 -8.564 1.00 37.70 N ANISOU 380 N ASN A 51 5367 5654 3304 -107 -240 780 N ATOM 381 CA ASN A 51 -24.003 -1.392 -8.484 1.00 37.93 C ANISOU 381 CA ASN A 51 5395 5599 3420 -67 -380 769 C ATOM 382 C ASN A 51 -24.262 -2.893 -8.437 1.00 40.86 C ANISOU 382 C ASN A 51 5752 5992 3780 -21 -410 617 C ATOM 383 O ASN A 51 -24.719 -3.478 -9.427 1.00 40.53 O ANISOU 383 O ASN A 51 5767 6009 3622 -3 -489 581 O ATOM 384 CB ASN A 51 -24.734 -0.761 -9.671 1.00 43.99 C ANISOU 384 CB ASN A 51 6246 6386 4081 -79 -492 875 C ATOM 385 CG ASN A 51 -26.230 -0.663 -9.446 1.00 45.55 C ANISOU 385 CG ASN A 51 6418 6482 4409 -41 -640 883 C ATOM 386 OD1 ASN A 51 -26.713 -0.839 -8.326 1.00 45.61 O ANISOU 386 OD1 ASN A 51 6338 6399 4591 -19 -644 830 O ATOM 387 ND2 ASN A 51 -26.972 -0.377 -10.509 1.00 52.18 N ANISOU 387 ND2 ASN A 51 7329 7342 5156 -34 -765 947 N ATOM 388 N PRO A 52 -23.996 -3.547 -7.306 1.00 33.39 N ANISOU 388 N PRO A 52 4742 4993 2952 -2 -359 527 N ATOM 389 CA PRO A 52 -24.060 -5.012 -7.258 1.00 31.67 C ANISOU 389 CA PRO A 52 4528 4787 2719 37 -385 384 C ATOM 390 C PRO A 52 -25.444 -5.562 -6.951 1.00 33.36 C ANISOU 390 C PRO A 52 4724 4915 3037 46 -504 350 C ATOM 391 O PRO A 52 -26.169 -5.069 -6.085 1.00 33.48 O ANISOU 391 O PRO A 52 4681 4840 3201 31 -526 392 O ATOM 392 CB PRO A 52 -23.084 -5.351 -6.124 1.00 32.22 C ANISOU 392 CB PRO A 52 4545 4828 2870 46 -281 322 C ATOM 393 CG PRO A 52 -23.188 -4.180 -5.197 1.00 30.47 C ANISOU 393 CG PRO A 52 4268 4529 2779 14 -245 421 C ATOM 394 CD PRO A 52 -23.532 -2.969 -6.032 1.00 33.73 C ANISOU 394 CD PRO A 52 4716 4963 3137 -17 -278 551 C ATOM 395 N ASN A 53 -25.804 -6.611 -7.688 1.00 33.04 N ANISOU 395 N ASN A 53 4730 4910 2916 67 -579 261 N ATOM 396 CA ASN A 53 -26.960 -7.450 -7.377 1.00 33.06 C ANISOU 396 CA ASN A 53 4713 4837 3011 66 -684 197 C ATOM 397 C ASN A 53 -26.397 -8.706 -6.721 1.00 30.99 C ANISOU 397 C ASN A 53 4454 4540 2780 81 -648 76 C ATOM 398 O ASN A 53 -26.048 -9.678 -7.392 1.00 33.03 O ANISOU 398 O ASN A 53 4769 4842 2938 113 -675 -23 O ATOM 399 CB ASN A 53 -27.771 -7.765 -8.630 1.00 35.43 C ANISOU 399 CB ASN A 53 5066 5187 3207 75 -808 178 C ATOM 400 CG ASN A 53 -29.105 -8.421 -8.317 1.00 34.31 C ANISOU 400 CG ASN A 53 4887 4968 3180 58 -924 128 C ATOM 401 OD1 ASN A 53 -29.180 -9.367 -7.533 1.00 36.93 O ANISOU 401 OD1 ASN A 53 5198 5235 3598 43 -918 46 O ATOM 402 ND2 ASN A 53 -30.168 -7.919 -8.936 1.00 37.82 N ANISOU 402 ND2 ASN A 53 5323 5421 3625 54 -1035 177 N ATOM 403 N TYR A 54 -26.302 -8.675 -5.388 1.00 32.46 N ANISOU 403 N TYR A 54 4585 4643 3105 63 -594 83 N ATOM 404 CA TYR A 54 -25.607 -9.736 -4.664 1.00 32.39 C ANISOU 404 CA TYR A 54 4590 4591 3126 81 -559 -13 C ATOM 405 C TYR A 54 -26.273 -11.092 -4.857 1.00 32.54 C ANISOU 405 C TYR A 54 4653 4560 3151 78 -663 -113 C ATOM 406 O TYR A 54 -25.594 -12.124 -4.829 1.00 32.96 O ANISOU 406 O TYR A 54 4754 4598 3173 114 -665 -212 O ATOM 407 CB TYR A 54 -25.529 -9.391 -3.177 1.00 29.89 C ANISOU 407 CB TYR A 54 4214 4193 2951 52 -496 25 C ATOM 408 CG TYR A 54 -24.488 -8.346 -2.853 1.00 28.91 C ANISOU 408 CG TYR A 54 4057 4108 2819 63 -385 86 C ATOM 409 CD1 TYR A 54 -23.148 -8.688 -2.731 1.00 29.05 C ANISOU 409 CD1 TYR A 54 4088 4163 2786 102 -312 30 C ATOM 410 CD2 TYR A 54 -24.844 -7.016 -2.673 1.00 30.89 C ANISOU 410 CD2 TYR A 54 4260 4355 3121 36 -361 193 C ATOM 411 CE1 TYR A 54 -22.193 -7.736 -2.434 1.00 26.42 C ANISOU 411 CE1 TYR A 54 3716 3870 2453 101 -212 81 C ATOM 412 CE2 TYR A 54 -23.896 -6.057 -2.375 1.00 28.75 C ANISOU 412 CE2 TYR A 54 3964 4110 2852 35 -266 249 C ATOM 413 CZ TYR A 54 -22.572 -6.422 -2.258 1.00 27.57 C ANISOU 413 CZ TYR A 54 3822 4004 2649 62 -188 194 C ATOM 414 OH TYR A 54 -21.623 -5.470 -1.964 1.00 29.16 O ANISOU 414 OH TYR A 54 3988 4235 2856 51 -95 245 O ATOM 415 N GLU A 55 -27.593 -11.114 -5.051 1.00 34.32 N ANISOU 415 N GLU A 55 4860 4754 3425 37 -757 -93 N ATOM 416 CA GLU A 55 -28.273 -12.379 -5.304 1.00 37.19 C ANISOU 416 CA GLU A 55 5265 5069 3797 20 -864 -187 C ATOM 417 C GLU A 55 -27.834 -12.982 -6.633 1.00 37.91 C ANISOU 417 C GLU A 55 5437 5236 3733 75 -913 -272 C ATOM 418 O GLU A 55 -27.577 -14.189 -6.718 1.00 37.06 O ANISOU 418 O GLU A 55 5388 5087 3607 97 -959 -384 O ATOM 419 CB GLU A 55 -29.788 -12.175 -5.277 1.00 38.67 C ANISOU 419 CB GLU A 55 5396 5227 4071 -41 -952 -151 C ATOM 420 CG GLU A 55 -30.366 -11.980 -3.883 1.00 37.71 C ANISOU 420 CG GLU A 55 5195 5027 4108 -106 -914 -109 C ATOM 421 CD GLU A 55 -30.102 -10.596 -3.324 1.00 41.20 C ANISOU 421 CD GLU A 55 5569 5491 4592 -94 -821 -11 C ATOM 422 OE1 GLU A 55 -29.833 -9.672 -4.121 1.00 40.21 O ANISOU 422 OE1 GLU A 55 5451 5435 4393 -53 -814 45 O ATOM 423 OE2 GLU A 55 -30.162 -10.432 -2.088 1.00 46.95 O ANISOU 423 OE2 GLU A 55 6247 6168 5426 -132 -759 12 O ATOM 424 N ASP A 56 -27.731 -12.157 -7.677 1.00 33.90 N ANISOU 424 N ASP A 56 4939 4836 3106 100 -909 -222 N ATOM 425 CA ASP A 56 -27.292 -12.658 -8.975 1.00 35.76 C ANISOU 425 CA ASP A 56 5250 5166 3170 150 -945 -304 C ATOM 426 C ASP A 56 -25.811 -13.014 -8.960 1.00 37.06 C ANISOU 426 C ASP A 56 5441 5382 3257 208 -844 -377 C ATOM 427 O ASP A 56 -25.396 -13.998 -9.585 1.00 39.06 O ANISOU 427 O ASP A 56 5753 5666 3422 259 -879 -507 O ATOM 428 CB ASP A 56 -27.579 -11.623 -10.062 1.00 39.69 C ANISOU 428 CB ASP A 56 5760 5771 3548 148 -965 -215 C ATOM 429 CG ASP A 56 -29.060 -11.451 -10.325 1.00 42.49 C ANISOU 429 CG ASP A 56 6094 6089 3961 112 -1097 -177 C ATOM 430 OD1 ASP A 56 -29.852 -12.286 -9.843 1.00 42.14 O ANISOU 430 OD1 ASP A 56 6029 5956 4028 82 -1173 -240 O ATOM 431 OD2 ASP A 56 -29.431 -10.477 -11.013 1.00 42.32 O ANISOU 431 OD2 ASP A 56 6078 6128 3876 110 -1130 -82 O ATOM 432 N LEU A 57 -24.997 -12.224 -8.256 1.00 33.96 N ANISOU 432 N LEU A 57 5000 5001 2901 207 -723 -307 N ATOM 433 CA LEU A 57 -23.564 -12.496 -8.201 1.00 35.37 C ANISOU 433 CA LEU A 57 5182 5239 3017 263 -625 -380 C ATOM 434 C LEU A 57 -23.273 -13.784 -7.441 1.00 35.25 C ANISOU 434 C LEU A 57 5188 5119 3088 300 -659 -502 C ATOM 435 O LEU A 57 -22.424 -14.580 -7.858 1.00 36.70 O ANISOU 435 O LEU A 57 5405 5345 3195 372 -654 -631 O ATOM 436 CB LEU A 57 -22.830 -11.319 -7.561 1.00 36.11 C ANISOU 436 CB LEU A 57 5212 5360 3147 241 -499 -274 C ATOM 437 CG LEU A 57 -22.827 -10.000 -8.338 1.00 35.65 C ANISOU 437 CG LEU A 57 5149 5405 2993 205 -454 -150 C ATOM 438 CD1 LEU A 57 -22.205 -8.890 -7.506 1.00 34.93 C ANISOU 438 CD1 LEU A 57 4994 5302 2975 174 -344 -47 C ATOM 439 CD2 LEU A 57 -22.094 -10.155 -9.660 1.00 39.59 C ANISOU 439 CD2 LEU A 57 5693 6061 3286 236 -422 -209 C ATOM 440 N LEU A 58 -23.967 -14.006 -6.321 1.00 31.98 N ANISOU 440 N LEU A 58 4756 4566 2829 252 -697 -465 N ATOM 441 CA LEU A 58 -23.732 -15.207 -5.526 1.00 32.81 C ANISOU 441 CA LEU A 58 4898 4552 3017 274 -740 -558 C ATOM 442 C LEU A 58 -24.178 -16.467 -6.256 1.00 34.28 C ANISOU 442 C LEU A 58 5163 4699 3162 297 -866 -682 C ATOM 443 O LEU A 58 -23.614 -17.544 -6.030 1.00 37.34 O ANISOU 443 O LEU A 58 5603 5018 3566 352 -906 -797 O ATOM 444 CB LEU A 58 -24.449 -15.090 -4.180 1.00 35.39 C ANISOU 444 CB LEU A 58 5192 4754 3501 197 -746 -475 C ATOM 445 CG LEU A 58 -24.226 -16.214 -3.166 1.00 32.39 C ANISOU 445 CG LEU A 58 4860 4236 3211 199 -787 -537 C ATOM 446 CD1 LEU A 58 -22.743 -16.401 -2.889 1.00 32.30 C ANISOU 446 CD1 LEU A 58 4855 4246 3170 289 -725 -602 C ATOM 447 CD2 LEU A 58 -24.986 -15.934 -1.879 1.00 33.08 C ANISOU 447 CD2 LEU A 58 4910 4229 3428 105 -774 -440 C ATOM 448 N ILE A 59 -25.179 -16.356 -7.132 1.00 35.82 N ANISOU 448 N ILE A 59 5371 4931 3310 262 -941 -667 N ATOM 449 CA ILE A 59 -25.681 -17.529 -7.843 1.00 41.33 C ANISOU 449 CA ILE A 59 6143 5587 3974 276 -1072 -789 C ATOM 450 C ILE A 59 -24.614 -18.087 -8.778 1.00 41.30 C ANISOU 450 C ILE A 59 6190 5675 3827 382 -1063 -931 C ATOM 451 O ILE A 59 -24.449 -19.308 -8.896 1.00 44.86 O ANISOU 451 O ILE A 59 6708 6051 4284 430 -1147 -1070 O ATOM 452 CB ILE A 59 -26.978 -17.177 -8.594 1.00 41.85 C ANISOU 452 CB ILE A 59 6198 5686 4015 216 -1157 -740 C ATOM 453 CG1 ILE A 59 -28.165 -17.190 -7.629 1.00 40.83 C ANISOU 453 CG1 ILE A 59 6025 5436 4051 114 -1204 -664 C ATOM 454 CG2 ILE A 59 -27.223 -18.142 -9.745 1.00 41.17 C ANISOU 454 CG2 ILE A 59 6192 5622 3830 253 -1275 -877 C ATOM 455 CD1 ILE A 59 -29.455 -16.701 -8.244 1.00 41.11 C ANISOU 455 CD1 ILE A 59 6022 5510 4087 59 -1285 -612 C ATOM 456 N ARG A 60 -23.858 -17.209 -9.441 1.00 51.40 N ANISOU 456 N ARG A 60 7438 7116 4976 420 -959 -903 N ATOM 457 CA ARG A 60 -22.790 -17.661 -10.323 1.00 55.54 C ANISOU 457 CA ARG A 60 7991 7758 5353 518 -928 -1045 C ATOM 458 C ARG A 60 -21.614 -18.268 -9.569 1.00 55.71 C ANISOU 458 C ARG A 60 8001 7732 5432 595 -880 -1141 C ATOM 459 O ARG A 60 -20.702 -18.802 -10.208 1.00 54.69 O ANISOU 459 O ARG A 60 7888 7691 5202 691 -862 -1290 O ATOM 460 CB ARG A 60 -22.297 -16.501 -11.191 1.00 54.62 C ANISOU 460 CB ARG A 60 7840 7837 5076 514 -817 -973 C ATOM 461 CG ARG A 60 -23.397 -15.558 -11.653 1.00 57.76 C ANISOU 461 CG ARG A 60 8236 8264 5444 432 -853 -826 C ATOM 462 CD ARG A 60 -22.857 -14.497 -12.598 1.00 59.83 C ANISOU 462 CD ARG A 60 8491 8713 5529 425 -757 -755 C ATOM 463 NE ARG A 60 -21.645 -13.869 -12.083 1.00 63.71 N ANISOU 463 NE ARG A 60 8920 9264 6023 434 -604 -719 N ATOM 464 CZ ARG A 60 -21.383 -12.568 -12.166 1.00 64.03 C ANISOU 464 CZ ARG A 60 8925 9384 6020 379 -508 -571 C ATOM 465 NH1 ARG A 60 -20.252 -12.085 -11.669 1.00 64.39 N ANISOU 465 NH1 ARG A 60 8909 9479 6078 382 -374 -554 N ATOM 466 NH2 ARG A 60 -22.251 -11.751 -12.746 1.00 62.77 N ANISOU 466 NH2 ARG A 60 8795 9247 5809 320 -557 -443 N ATOM 467 N LYS A 61 -21.610 -18.203 -8.240 1.00 45.89 N ANISOU 467 N LYS A 61 6731 6360 4345 562 -862 -1068 N ATOM 468 CA LYS A 61 -20.516 -18.737 -7.442 1.00 46.24 C ANISOU 468 CA LYS A 61 6768 6350 4453 637 -832 -1149 C ATOM 469 C LYS A 61 -20.819 -20.161 -6.996 1.00 45.91 C ANISOU 469 C LYS A 61 6814 6124 4507 664 -974 -1254 C ATOM 470 O LYS A 61 -21.931 -20.468 -6.559 1.00 49.18 O ANISOU 470 O LYS A 61 7268 6406 5013 577 -1061 -1192 O ATOM 471 CB LYS A 61 -20.260 -17.856 -6.218 1.00 43.53 C ANISOU 471 CB LYS A 61 6354 5970 4213 587 -738 -1011 C ATOM 472 CG LYS A 61 -19.819 -16.441 -6.551 1.00 45.56 C ANISOU 472 CG LYS A 61 6529 6388 4393 559 -600 -908 C ATOM 473 CD LYS A 61 -18.508 -16.443 -7.319 1.00 44.95 C ANISOU 473 CD LYS A 61 6420 6474 4186 648 -516 -1020 C ATOM 474 CE LYS A 61 -18.097 -15.033 -7.706 1.00 46.44 C ANISOU 474 CE LYS A 61 6537 6820 4290 598 -380 -905 C ATOM 475 NZ LYS A 61 -16.839 -15.015 -8.503 1.00 49.85 N ANISOU 475 NZ LYS A 61 6926 7433 4581 665 -284 -1015 N ATOM 476 N SER A 62 -19.821 -21.028 -7.113 1.00 51.25 N ANISOU 476 N SER A 62 7518 6791 5163 784 -999 -1417 N ATOM 477 CA SER A 62 -19.869 -22.380 -6.579 1.00 52.24 C ANISOU 477 CA SER A 62 7736 6723 5389 825 -1137 -1520 C ATOM 478 C SER A 62 -19.044 -22.437 -5.298 1.00 50.84 C ANISOU 478 C SER A 62 7540 6457 5319 860 -1107 -1496 C ATOM 479 O SER A 62 -18.478 -21.436 -4.848 1.00 53.12 O ANISOU 479 O SER A 62 7739 6838 5606 849 -979 -1408 O ATOM 480 CB SER A 62 -19.364 -23.391 -7.613 1.00 56.17 C ANISOU 480 CB SER A 62 8288 7254 5799 952 -1216 -1738 C ATOM 481 OG SER A 62 -20.146 -23.346 -8.795 1.00 59.21 O ANISOU 481 OG SER A 62 8697 7724 6075 918 -1252 -1762 O ATOM 482 N ASN A 63 -18.983 -23.627 -4.699 1.00 48.10 N ANISOU 482 N ASN A 63 7289 5920 5068 900 -1236 -1574 N ATOM 483 CA ASN A 63 -18.211 -23.788 -3.471 1.00 45.95 C ANISOU 483 CA ASN A 63 7018 5549 4894 941 -1234 -1556 C ATOM 484 C ASN A 63 -16.717 -23.637 -3.729 1.00 48.25 C ANISOU 484 C ASN A 63 7230 5973 5130 1092 -1159 -1682 C ATOM 485 O ASN A 63 -15.993 -23.073 -2.899 1.00 46.15 O ANISOU 485 O ASN A 63 6897 5732 4905 1106 -1081 -1626 O ATOM 486 CB ASN A 63 -18.509 -25.143 -2.832 1.00 48.25 C ANISOU 486 CB ASN A 63 7448 5593 5291 946 -1408 -1605 C ATOM 487 CG ASN A 63 -19.818 -25.152 -2.073 1.00 47.88 C ANISOU 487 CG ASN A 63 7456 5408 5328 771 -1451 -1443 C ATOM 488 OD1 ASN A 63 -20.287 -24.113 -1.608 1.00 44.91 O ANISOU 488 OD1 ASN A 63 7004 5098 4961 665 -1344 -1287 O ATOM 489 ND2 ASN A 63 -20.411 -26.331 -1.932 1.00 45.54 N ANISOU 489 ND2 ASN A 63 7290 4918 5097 737 -1608 -1484 N ATOM 490 N HIS A 64 -16.237 -24.126 -4.875 1.00 47.20 N ANISOU 490 N HIS A 64 7096 5938 4900 1204 -1180 -1862 N ATOM 491 CA HIS A 64 -14.806 -24.119 -5.156 1.00 47.66 C ANISOU 491 CA HIS A 64 7069 6131 4907 1355 -1115 -2013 C ATOM 492 C HIS A 64 -14.263 -22.731 -5.471 1.00 49.07 C ANISOU 492 C HIS A 64 7104 6548 4992 1319 -919 -1935 C ATOM 493 O HIS A 64 -13.045 -22.583 -5.617 1.00 47.34 O ANISOU 493 O HIS A 64 6791 6461 4735 1423 -842 -2044 O ATOM 494 CB HIS A 64 -14.493 -25.075 -6.310 1.00 49.07 C ANISOU 494 CB HIS A 64 7286 6356 5004 1486 -1192 -2243 C ATOM 495 CG HIS A 64 -15.039 -24.633 -7.633 1.00 51.67 C ANISOU 495 CG HIS A 64 7597 6858 5178 1436 -1132 -2250 C ATOM 496 ND1 HIS A 64 -14.414 -23.691 -8.421 1.00 53.30 N ANISOU 496 ND1 HIS A 64 7687 7325 5238 1444 -968 -2258 N ATOM 497 CD2 HIS A 64 -16.150 -25.011 -8.309 1.00 50.38 C ANISOU 497 CD2 HIS A 64 7522 6645 4976 1373 -1223 -2247 C ATOM 498 CE1 HIS A 64 -15.117 -23.504 -9.523 1.00 53.99 C ANISOU 498 CE1 HIS A 64 7803 7514 5198 1392 -962 -2254 C ATOM 499 NE2 HIS A 64 -16.176 -24.293 -9.480 1.00 54.24 N ANISOU 499 NE2 HIS A 64 7953 7363 5294 1353 -1118 -2252 N ATOM 500 N ASN A 65 -15.121 -21.718 -5.583 1.00 45.23 N ANISOU 500 N ASN A 65 6596 6117 4471 1176 -842 -1755 N ATOM 501 CA ASN A 65 -14.665 -20.356 -5.828 1.00 46.83 C ANISOU 501 CA ASN A 65 6680 6519 4596 1126 -669 -1660 C ATOM 502 C ASN A 65 -14.196 -19.651 -4.562 1.00 44.87 C ANISOU 502 C ASN A 65 6366 6231 4452 1090 -600 -1545 C ATOM 503 O ASN A 65 -13.706 -18.520 -4.649 1.00 42.11 O ANISOU 503 O ASN A 65 5915 6029 4055 1049 -459 -1470 O ATOM 504 CB ASN A 65 -15.780 -19.537 -6.487 1.00 45.51 C ANISOU 504 CB ASN A 65 6524 6415 4354 997 -633 -1516 C ATOM 505 CG ASN A 65 -16.053 -19.966 -7.916 1.00 49.61 C ANISOU 505 CG ASN A 65 7086 7038 4727 1031 -669 -1629 C ATOM 506 OD1 ASN A 65 -17.201 -20.194 -8.299 1.00 47.40 O ANISOU 506 OD1 ASN A 65 6880 6692 4439 969 -758 -1588 O ATOM 507 ND2 ASN A 65 -14.998 -20.076 -8.714 1.00 49.58 N ANISOU 507 ND2 ASN A 65 7028 7206 4604 1129 -601 -1779 N ATOM 508 N PHE A 66 -14.330 -20.287 -3.398 1.00 43.94 N ANISOU 508 N PHE A 66 6310 5915 4470 1100 -699 -1528 N ATOM 509 CA PHE A 66 -13.952 -19.699 -2.116 1.00 45.46 C ANISOU 509 CA PHE A 66 6456 6057 4760 1066 -651 -1422 C ATOM 510 C PHE A 66 -12.794 -20.497 -1.533 1.00 46.14 C ANISOU 510 C PHE A 66 6537 6086 4907 1207 -711 -1564 C ATOM 511 O PHE A 66 -12.959 -21.666 -1.168 1.00 48.94 O ANISOU 511 O PHE A 66 7000 6266 5328 1264 -860 -1636 O ATOM 512 CB PHE A 66 -15.134 -19.677 -1.150 1.00 43.71 C ANISOU 512 CB PHE A 66 6312 5661 4636 944 -711 -1265 C ATOM 513 CG PHE A 66 -16.316 -18.915 -1.660 1.00 41.37 C ANISOU 513 CG PHE A 66 6009 5411 4297 817 -668 -1136 C ATOM 514 CD1 PHE A 66 -16.356 -17.534 -1.577 1.00 42.70 C ANISOU 514 CD1 PHE A 66 6088 5688 4447 741 -540 -1006 C ATOM 515 CD2 PHE A 66 -17.389 -19.581 -2.225 1.00 42.92 C ANISOU 515 CD2 PHE A 66 6291 5536 4480 778 -767 -1150 C ATOM 516 CE1 PHE A 66 -17.446 -16.833 -2.050 1.00 41.54 C ANISOU 516 CE1 PHE A 66 5938 5576 4270 638 -518 -892 C ATOM 517 CE2 PHE A 66 -18.481 -18.885 -2.697 1.00 43.11 C ANISOU 517 CE2 PHE A 66 6303 5606 4472 671 -741 -1039 C ATOM 518 CZ PHE A 66 -18.511 -17.509 -2.609 1.00 43.31 C ANISOU 518 CZ PHE A 66 6240 5737 4480 607 -620 -910 C ATOM 519 N LEU A 67 -11.627 -19.862 -1.446 1.00 44.98 N ANISOU 519 N LEU A 67 6266 6082 4743 1260 -604 -1604 N ATOM 520 CA LEU A 67 -10.434 -20.469 -0.862 1.00 43.48 C ANISOU 520 CA LEU A 67 6043 5861 4617 1401 -654 -1741 C ATOM 521 C LEU A 67 -10.287 -19.940 0.560 1.00 43.78 C ANISOU 521 C LEU A 67 6065 5810 4757 1348 -644 -1612 C ATOM 522 O LEU A 67 -9.841 -18.809 0.769 1.00 42.96 O ANISOU 522 O LEU A 67 5848 5832 4643 1295 -513 -1537 O ATOM 523 CB LEU A 67 -9.197 -20.174 -1.707 1.00 46.86 C ANISOU 523 CB LEU A 67 6326 6520 4958 1498 -545 -1891 C ATOM 524 CG LEU A 67 -9.099 -20.721 -3.145 1.00 54.53 C ANISOU 524 CG LEU A 67 7296 7617 5808 1574 -542 -2057 C ATOM 525 CD1 LEU A 67 -10.110 -20.113 -4.124 1.00 53.78 C ANISOU 525 CD1 LEU A 67 7230 7609 5595 1446 -474 -1949 C ATOM 526 CD2 LEU A 67 -7.677 -20.613 -3.704 1.00 56.46 C ANISOU 526 CD2 LEU A 67 7385 8079 5989 1691 -444 -2238 C ATOM 527 N VAL A 68 -10.661 -20.763 1.536 1.00 40.60 N ANISOU 527 N VAL A 68 5785 5191 4450 1357 -786 -1585 N ATOM 528 CA VAL A 68 -10.563 -20.408 2.947 1.00 39.50 C ANISOU 528 CA VAL A 68 5655 4956 4399 1310 -796 -1470 C ATOM 529 C VAL A 68 -9.320 -21.066 3.524 1.00 42.79 C ANISOU 529 C VAL A 68 6054 5329 4875 1468 -882 -1608 C ATOM 530 O VAL A 68 -9.003 -22.217 3.200 1.00 42.83 O ANISOU 530 O VAL A 68 6124 5256 4894 1596 -1009 -1759 O ATOM 531 CB VAL A 68 -11.833 -20.822 3.716 1.00 37.79 C ANISOU 531 CB VAL A 68 5586 4537 4234 1195 -889 -1333 C ATOM 532 CG1 VAL A 68 -11.743 -20.397 5.175 1.00 35.75 C ANISOU 532 CG1 VAL A 68 5337 4200 4046 1139 -887 -1214 C ATOM 533 CG2 VAL A 68 -13.065 -20.215 3.061 1.00 34.35 C ANISOU 533 CG2 VAL A 68 5151 4153 3747 1055 -816 -1220 C ATOM 534 N GLN A 69 -8.602 -20.331 4.371 1.00 47.96 N ANISOU 534 N GLN A 69 6620 6033 5569 1466 -822 -1564 N ATOM 535 CA GLN A 69 -7.315 -20.792 4.870 1.00 50.00 C ANISOU 535 CA GLN A 69 6830 6285 5883 1622 -893 -1702 C ATOM 536 C GLN A 69 -7.108 -20.284 6.287 1.00 47.08 C ANISOU 536 C GLN A 69 6460 5846 5581 1574 -902 -1588 C ATOM 537 O GLN A 69 -7.224 -19.082 6.541 1.00 43.32 O ANISOU 537 O GLN A 69 5899 5469 5092 1462 -767 -1471 O ATOM 538 CB GLN A 69 -6.180 -20.313 3.958 1.00 52.99 C ANISOU 538 CB GLN A 69 7021 6904 6210 1709 -773 -1850 C ATOM 539 CG GLN A 69 -4.806 -20.834 4.332 1.00 56.69 C ANISOU 539 CG GLN A 69 7411 7389 6739 1889 -848 -2027 C ATOM 540 CD GLN A 69 -3.860 -20.868 3.148 1.00 61.12 C ANISOU 540 CD GLN A 69 7818 8168 7238 2001 -767 -2228 C ATOM 541 OE1 GLN A 69 -4.182 -20.369 2.069 1.00 61.90 O ANISOU 541 OE1 GLN A 69 7866 8421 7234 1928 -636 -2217 O ATOM 542 NE2 GLN A 69 -2.685 -21.455 3.343 1.00 64.59 N ANISOU 542 NE2 GLN A 69 8171 8630 7740 2142 -842 -2370 N ATOM 543 N ALA A 70 -6.805 -21.201 7.201 1.00 50.98 N ANISOU 543 N ALA A 70 7058 6166 6145 1661 -1068 -1623 N ATOM 544 CA ALA A 70 -6.508 -20.881 8.595 1.00 52.28 C ANISOU 544 CA ALA A 70 7240 6259 6366 1637 -1104 -1535 C ATOM 545 C ALA A 70 -5.048 -21.249 8.840 1.00 54.51 C ANISOU 545 C ALA A 70 7437 6575 6699 1823 -1181 -1705 C ATOM 546 O ALA A 70 -4.731 -22.378 9.219 1.00 57.04 O ANISOU 546 O ALA A 70 7865 6738 7069 1948 -1366 -1789 O ATOM 547 CB ALA A 70 -7.445 -21.622 9.544 1.00 51.62 C ANISOU 547 CB ALA A 70 7365 5937 6310 1564 -1242 -1411 C ATOM 548 N GLY A 71 -4.158 -20.284 8.624 1.00 55.33 N ANISOU 548 N GLY A 71 7344 6883 6795 1839 -1046 -1757 N ATOM 549 CA GLY A 71 -2.737 -20.559 8.673 1.00 59.15 C ANISOU 549 CA GLY A 71 7705 7443 7326 2017 -1098 -1943 C ATOM 550 C GLY A 71 -2.323 -21.464 7.532 1.00 63.63 C ANISOU 550 C GLY A 71 8244 8057 7876 2168 -1145 -2147 C ATOM 551 O GLY A 71 -2.291 -21.036 6.373 1.00 64.81 O ANISOU 551 O GLY A 71 8282 8390 7953 2143 -1002 -2203 O ATOM 552 N ASN A 72 -2.003 -22.718 7.845 1.00 91.66 N ANISOU 552 N ASN A 72 11885 11459 11483 2274 -1342 -2206 N ATOM 553 CA ASN A 72 -1.741 -23.721 6.822 1.00 93.37 C ANISOU 553 CA ASN A 72 12087 11701 11687 2362 -1405 -2334 C ATOM 554 C ASN A 72 -2.922 -24.649 6.585 1.00 94.16 C ANISOU 554 C ASN A 72 12400 11602 11775 2329 -1516 -2281 C ATOM 555 O ASN A 72 -3.029 -25.230 5.500 1.00 96.57 O ANISOU 555 O ASN A 72 12695 11951 12045 2366 -1519 -2371 O ATOM 556 CB ASN A 72 -0.508 -24.552 7.193 1.00 97.14 C ANISOU 556 CB ASN A 72 12505 12166 12237 2506 -1557 -2453 C ATOM 557 CG ASN A 72 0.739 -23.704 7.351 1.00 99.91 C ANISOU 557 CG ASN A 72 12632 12726 12605 2535 -1455 -2525 C ATOM 558 OD1 ASN A 72 1.360 -23.684 8.412 1.00100.79 O ANISOU 558 OD1 ASN A 72 12734 12784 12777 2574 -1546 -2514 O ATOM 559 ND2 ASN A 72 1.107 -22.992 6.291 1.00 98.23 N ANISOU 559 ND2 ASN A 72 12239 12754 12331 2503 -1267 -2596 N ATOM 560 N VAL A 73 -3.804 -24.806 7.576 1.00 77.00 N ANISOU 560 N VAL A 73 10417 9212 9628 2250 -1607 -2136 N ATOM 561 CA VAL A 73 -5.010 -25.599 7.383 1.00 74.95 C ANISOU 561 CA VAL A 73 10357 8763 9356 2183 -1700 -2068 C ATOM 562 C VAL A 73 -5.840 -25.001 6.257 1.00 74.47 C ANISOU 562 C VAL A 73 10266 8819 9209 2096 -1546 -2069 C ATOM 563 O VAL A 73 -5.964 -23.775 6.128 1.00 70.90 O ANISOU 563 O VAL A 73 9701 8531 8707 1996 -1365 -1993 O ATOM 564 CB VAL A 73 -5.825 -25.677 8.686 1.00 72.98 C ANISOU 564 CB VAL A 73 10303 8289 9137 2078 -1792 -1894 C ATOM 565 CG1 VAL A 73 -6.790 -26.858 8.642 1.00 75.47 C ANISOU 565 CG1 VAL A 73 10826 8384 9464 2024 -1943 -1835 C ATOM 566 CG2 VAL A 73 -4.904 -25.769 9.890 1.00 74.35 C ANISOU 566 CG2 VAL A 73 10469 8412 9368 2147 -1891 -1878 C ATOM 567 N GLN A 74 -6.406 -25.874 5.425 1.00 88.45 N ANISOU 567 N GLN A 74 12119 10527 10961 2100 -1614 -2111 N ATOM 568 CA GLN A 74 -7.270 -25.481 4.317 1.00 87.08 C ANISOU 568 CA GLN A 74 11941 10447 10699 2018 -1502 -2115 C ATOM 569 C GLN A 74 -8.652 -26.081 4.540 1.00 87.10 C ANISOU 569 C GLN A 74 12152 10231 10713 1898 -1606 -1999 C ATOM 570 O GLN A 74 -8.797 -27.309 4.573 1.00 89.82 O ANISOU 570 O GLN A 74 12612 10407 11108 1938 -1771 -2023 O ATOM 571 CB GLN A 74 -6.682 -25.937 2.979 1.00 89.36 C ANISOU 571 CB GLN A 74 12117 10891 10946 2120 -1475 -2278 C ATOM 572 CG GLN A 74 -5.693 -24.956 2.377 1.00 89.53 C ANISOU 572 CG GLN A 74 11914 11197 10906 2159 -1292 -2361 C ATOM 573 CD GLN A 74 -6.259 -24.229 1.177 1.00 90.98 C ANISOU 573 CD GLN A 74 12046 11559 10963 2078 -1132 -2365 C ATOM 574 OE1 GLN A 74 -7.469 -24.019 1.079 1.00 89.04 O ANISOU 574 OE1 GLN A 74 11915 11239 10675 1962 -1125 -2261 O ATOM 575 NE2 GLN A 74 -5.389 -23.844 0.252 1.00 93.23 N ANISOU 575 NE2 GLN A 74 12154 12088 11183 2123 -1004 -2469 N ATOM 576 N LEU A 75 -9.658 -25.214 4.694 1.00 59.32 N ANISOU 576 N LEU A 75 8629 6753 7157 1703 -1487 -1806 N ATOM 577 CA LEU A 75 -11.009 -25.616 5.064 1.00 58.74 C ANISOU 577 CA LEU A 75 8717 6502 7100 1548 -1556 -1658 C ATOM 578 C LEU A 75 -11.906 -25.685 3.838 1.00 60.35 C ANISOU 578 C LEU A 75 8927 6762 7240 1485 -1519 -1680 C ATOM 579 O LEU A 75 -12.009 -24.719 3.070 1.00 57.48 O ANISOU 579 O LEU A 75 8435 6602 6801 1440 -1360 -1662 O ATOM 580 CB LEU A 75 -11.607 -24.655 6.083 1.00 57.49 C ANISOU 580 CB LEU A 75 8546 6350 6948 1377 -1459 -1444 C ATOM 581 CG LEU A 75 -10.682 -24.185 7.194 1.00 55.99 C ANISOU 581 CG LEU A 75 8303 6176 6797 1422 -1443 -1414 C ATOM 582 CD1 LEU A 75 -11.462 -23.296 8.133 1.00 48.60 C ANISOU 582 CD1 LEU A 75 7370 5239 5858 1242 -1351 -1209 C ATOM 583 CD2 LEU A 75 -10.115 -25.389 7.917 1.00 55.44 C ANISOU 583 CD2 LEU A 75 8370 5901 6794 1541 -1649 -1484 C ATOM 584 N ARG A 76 -12.532 -26.843 3.681 1.00 46.49 N ANISOU 584 N ARG A 76 7331 4819 5516 1482 -1678 -1716 N ATOM 585 CA ARG A 76 -13.516 -27.140 2.654 1.00 47.49 C ANISOU 585 CA ARG A 76 7500 4947 5597 1414 -1690 -1735 C ATOM 586 C ARG A 76 -14.772 -26.342 2.860 1.00 39.25 C ANISOU 586 C ARG A 76 6447 3934 4534 1203 -1589 -1536 C ATOM 587 O ARG A 76 -15.369 -26.420 3.924 1.00 44.60 O ANISOU 587 O ARG A 76 7206 4475 5265 1084 -1626 -1391 O ATOM 588 CB ARG A 76 -13.839 -28.618 2.762 1.00 49.73 C ANISOU 588 CB ARG A 76 7973 4975 5946 1449 -1908 -1804 C ATOM 589 N VAL A 77 -15.207 -25.613 1.848 1.00 47.93 N ANISOU 589 N VAL A 77 7449 5209 5552 1156 -1471 -1531 N ATOM 590 CA VAL A 77 -16.526 -25.011 1.893 1.00 46.29 C ANISOU 590 CA VAL A 77 7240 5014 5335 969 -1409 -1367 C ATOM 591 C VAL A 77 -17.499 -26.017 1.294 1.00 46.26 C ANISOU 591 C VAL A 77 7355 4883 5339 921 -1539 -1410 C ATOM 592 O VAL A 77 -17.351 -26.420 0.134 1.00 48.34 O ANISOU 592 O VAL A 77 7617 5205 5546 1008 -1574 -1555 O ATOM 593 CB VAL A 77 -16.536 -23.671 1.154 1.00 44.45 C ANISOU 593 CB VAL A 77 6853 5019 5016 939 -1232 -1325 C ATOM 594 CG1 VAL A 77 -17.825 -22.923 1.411 1.00 43.60 C ANISOU 594 CG1 VAL A 77 6729 4921 4918 759 -1169 -1150 C ATOM 595 CG2 VAL A 77 -15.343 -22.865 1.619 1.00 44.60 C ANISOU 595 CG2 VAL A 77 6759 5156 5032 1012 -1124 -1328 C ATOM 596 N ILE A 78 -18.438 -26.481 2.113 1.00 52.22 N ANISOU 596 N ILE A 78 8216 5462 6161 783 -1617 -1295 N ATOM 597 CA ILE A 78 -19.477 -27.411 1.700 1.00 53.06 C ANISOU 597 CA ILE A 78 8437 5432 6292 701 -1743 -1312 C ATOM 598 C ILE A 78 -20.809 -26.687 1.518 1.00 52.18 C ANISOU 598 C ILE A 78 8266 5396 6164 523 -1660 -1181 C ATOM 599 O ILE A 78 -21.866 -27.316 1.511 1.00 54.52 O ANISOU 599 O ILE A 78 8643 5574 6499 402 -1749 -1147 O ATOM 600 CB ILE A 78 -19.602 -28.581 2.691 1.00 55.55 C ANISOU 600 CB ILE A 78 8927 5483 6698 662 -1906 -1285 C ATOM 601 CG1 ILE A 78 -19.988 -28.055 4.077 1.00 52.67 C ANISOU 601 CG1 ILE A 78 8563 5078 6370 517 -1840 -1091 C ATOM 602 CG2 ILE A 78 -18.297 -29.363 2.771 1.00 55.69 C ANISOU 602 CG2 ILE A 78 9007 5412 6739 862 -2016 -1435 C ATOM 603 CD1 ILE A 78 -20.228 -29.139 5.104 1.00 53.19 C ANISOU 603 CD1 ILE A 78 8812 4890 6508 442 -1991 -1031 C ATOM 604 N GLY A 79 -20.770 -25.370 1.390 1.00 42.03 N ANISOU 604 N GLY A 79 6836 4303 4829 505 -1499 -1108 N ATOM 605 CA GLY A 79 -21.976 -24.595 1.183 1.00 44.13 C ANISOU 605 CA GLY A 79 7032 4651 5084 360 -1425 -995 C ATOM 606 C GLY A 79 -21.758 -23.129 1.468 1.00 41.23 C ANISOU 606 C GLY A 79 6527 4450 4691 344 -1258 -894 C ATOM 607 O GLY A 79 -20.844 -22.728 2.191 1.00 40.50 O ANISOU 607 O GLY A 79 6402 4377 4608 400 -1197 -874 O ATOM 608 N HIS A 80 -22.635 -22.310 0.890 1.00 40.91 N ANISOU 608 N HIS A 80 6403 4521 4619 266 -1192 -831 N ATOM 609 CA HIS A 80 -22.558 -20.865 1.050 1.00 39.80 C ANISOU 609 CA HIS A 80 6137 4528 4458 245 -1046 -733 C ATOM 610 C HIS A 80 -23.962 -20.278 1.087 1.00 42.33 C ANISOU 610 C HIS A 80 6405 4872 4808 105 -1023 -626 C ATOM 611 O HIS A 80 -24.872 -20.762 0.407 1.00 42.98 O ANISOU 611 O HIS A 80 6515 4929 4886 55 -1101 -653 O ATOM 612 CB HIS A 80 -21.739 -20.216 -0.075 1.00 38.98 C ANISOU 612 CB HIS A 80 5962 4595 4252 355 -974 -801 C ATOM 613 CG HIS A 80 -22.241 -20.529 -1.450 1.00 42.23 C ANISOU 613 CG HIS A 80 6392 5063 4589 371 -1032 -877 C ATOM 614 ND1 HIS A 80 -21.709 -21.535 -2.227 1.00 43.83 N ANISOU 614 ND1 HIS A 80 6665 5247 4741 474 -1117 -1033 N ATOM 615 CD2 HIS A 80 -23.223 -19.961 -2.191 1.00 42.96 C ANISOU 615 CD2 HIS A 80 6445 5234 4645 303 -1024 -825 C ATOM 616 CE1 HIS A 80 -22.343 -21.577 -3.386 1.00 41.96 C ANISOU 616 CE1 HIS A 80 6433 5079 4433 463 -1154 -1073 C ATOM 617 NE2 HIS A 80 -23.266 -20.632 -3.389 1.00 46.16 N ANISOU 617 NE2 HIS A 80 6900 5668 4971 360 -1103 -945 N ATOM 618 N SER A 81 -24.125 -19.228 1.891 1.00 38.43 N ANISOU 618 N SER A 81 5829 4425 4348 48 -919 -513 N ATOM 619 CA SER A 81 -25.403 -18.543 2.036 1.00 37.69 C ANISOU 619 CA SER A 81 5663 4365 4294 -70 -887 -419 C ATOM 620 C SER A 81 -25.144 -17.103 2.461 1.00 34.90 C ANISOU 620 C SER A 81 5201 4114 3945 -65 -758 -334 C ATOM 621 O SER A 81 -24.020 -16.727 2.800 1.00 32.91 O ANISOU 621 O SER A 81 4937 3892 3674 8 -696 -340 O ATOM 622 CB SER A 81 -26.308 -19.255 3.046 1.00 36.29 C ANISOU 622 CB SER A 81 5533 4060 4197 -201 -937 -372 C ATOM 623 OG SER A 81 -25.699 -19.301 4.324 1.00 40.72 O ANISOU 623 OG SER A 81 6125 4558 4790 -209 -899 -329 O ATOM 624 N MET A 82 -26.210 -16.302 2.468 1.00 37.20 N ANISOU 624 N MET A 82 5410 4454 4270 -144 -726 -261 N ATOM 625 CA MET A 82 -26.118 -14.864 2.705 1.00 36.42 C ANISOU 625 CA MET A 82 5209 4447 4181 -138 -621 -185 C ATOM 626 C MET A 82 -27.045 -14.477 3.849 1.00 36.22 C ANISOU 626 C MET A 82 5126 4391 4243 -243 -583 -113 C ATOM 627 O MET A 82 -28.243 -14.773 3.802 1.00 38.06 O ANISOU 627 O MET A 82 5340 4606 4517 -329 -630 -105 O ATOM 628 CB MET A 82 -26.484 -14.087 1.435 1.00 37.12 C ANISOU 628 CB MET A 82 5246 4640 4218 -109 -623 -175 C ATOM 629 CG MET A 82 -25.903 -12.686 1.349 1.00 38.03 C ANISOU 629 CG MET A 82 5291 4846 4314 -66 -526 -115 C ATOM 630 SD MET A 82 -25.762 -12.107 -0.356 1.00 37.10 S ANISOU 630 SD MET A 82 5170 4845 4082 -7 -541 -120 S ATOM 631 CE MET A 82 -27.449 -12.302 -0.930 1.00 36.65 C ANISOU 631 CE MET A 82 5094 4775 4054 -72 -647 -111 C ATOM 632 N GLN A 83 -26.498 -13.815 4.874 1.00 36.29 N ANISOU 632 N GLN A 83 5103 4406 4281 -239 -498 -69 N ATOM 633 CA GLN A 83 -27.297 -13.256 5.970 1.00 35.40 C ANISOU 633 CA GLN A 83 4921 4291 4239 -327 -444 -9 C ATOM 634 C GLN A 83 -27.157 -11.730 5.945 1.00 32.99 C ANISOU 634 C GLN A 83 4515 4070 3950 -288 -361 36 C ATOM 635 O GLN A 83 -26.348 -11.137 6.661 1.00 36.55 O ANISOU 635 O GLN A 83 4951 4529 4407 -257 -292 56 O ATOM 636 CB GLN A 83 -26.895 -13.842 7.328 1.00 35.91 C ANISOU 636 CB GLN A 83 5046 4277 4320 -370 -426 3 C ATOM 637 CG GLN A 83 -27.900 -13.520 8.427 1.00 36.88 C ANISOU 637 CG GLN A 83 5108 4404 4501 -484 -376 52 C ATOM 638 CD GLN A 83 -27.657 -14.293 9.706 1.00 37.14 C ANISOU 638 CD GLN A 83 5225 4357 4531 -549 -374 70 C ATOM 639 OE1 GLN A 83 -26.721 -15.086 9.801 1.00 36.83 O ANISOU 639 OE1 GLN A 83 5294 4243 4455 -500 -425 47 O ATOM 640 NE2 GLN A 83 -28.505 -14.064 10.703 1.00 38.39 N ANISOU 640 NE2 GLN A 83 5333 4531 4721 -659 -320 109 N ATOM 641 N ASN A 84 -27.957 -11.119 5.075 1.00 37.81 N ANISOU 641 N ASN A 84 5061 4735 4568 -288 -382 51 N ATOM 642 CA ASN A 84 -28.211 -9.698 4.835 1.00 38.59 C ANISOU 642 CA ASN A 84 5069 4899 4696 -262 -339 97 C ATOM 643 C ASN A 84 -27.053 -8.911 4.236 1.00 40.93 C ANISOU 643 C ASN A 84 5375 5240 4936 -178 -299 116 C ATOM 644 O ASN A 84 -27.268 -8.122 3.312 1.00 48.74 O ANISOU 644 O ASN A 84 6335 6278 5904 -149 -314 147 O ATOM 645 CB ASN A 84 -28.546 -8.965 6.145 1.00 39.63 C ANISOU 645 CB ASN A 84 5124 5026 4907 -304 -266 127 C ATOM 646 CG ASN A 84 -29.749 -9.523 6.861 1.00 37.03 C ANISOU 646 CG ASN A 84 4759 4677 4634 -404 -280 115 C ATOM 647 OD1 ASN A 84 -30.871 -9.451 6.365 1.00 41.72 O ANISOU 647 OD1 ASN A 84 5290 5297 5264 -437 -326 108 O ATOM 648 ND2 ASN A 84 -29.528 -10.043 8.063 1.00 38.15 N ANISOU 648 ND2 ASN A 84 4934 4779 4783 -460 -239 114 N ATOM 649 N CYS A 85 -25.823 -9.176 4.676 1.00 34.27 N ANISOU 649 N CYS A 85 4578 4383 4061 -142 -256 96 N ATOM 650 CA CYS A 85 -24.656 -8.508 4.108 1.00 31.53 C ANISOU 650 CA CYS A 85 4232 4090 3658 -75 -210 106 C ATOM 651 C CYS A 85 -23.381 -9.296 4.373 1.00 31.74 C ANISOU 651 C CYS A 85 4316 4103 3641 -28 -196 48 C ATOM 652 O CYS A 85 -22.287 -8.862 3.995 1.00 29.25 O ANISOU 652 O CYS A 85 3992 3842 3280 23 -149 40 O ATOM 653 CB CYS A 85 -24.520 -7.083 4.652 1.00 30.52 C ANISOU 653 CB CYS A 85 4031 3979 3586 -78 -138 167 C ATOM 654 SG CYS A 85 -25.461 -5.816 3.753 1.00 31.23 S ANISOU 654 SG CYS A 85 4064 4106 3695 -82 -163 236 S ATOM 655 N VAL A 86 -23.500 -10.423 5.064 1.00 28.29 N ANISOU 655 N VAL A 86 3934 3592 3223 -49 -238 7 N ATOM 656 CA VAL A 86 -22.357 -11.260 5.399 1.00 30.28 C ANISOU 656 CA VAL A 86 4246 3811 3446 5 -249 -54 C ATOM 657 C VAL A 86 -22.534 -12.591 4.697 1.00 30.09 C ANISOU 657 C VAL A 86 4306 3746 3380 24 -343 -124 C ATOM 658 O VAL A 86 -23.661 -13.087 4.556 1.00 30.53 O ANISOU 658 O VAL A 86 4383 3760 3455 -39 -402 -116 O ATOM 659 CB VAL A 86 -22.184 -11.457 6.924 1.00 31.71 C ANISOU 659 CB VAL A 86 4445 3923 3682 -27 -233 -40 C ATOM 660 CG1 VAL A 86 -21.892 -10.130 7.612 1.00 29.22 C ANISOU 660 CG1 VAL A 86 4048 3649 3406 -34 -143 12 C ATOM 661 CG2 VAL A 86 -23.407 -12.128 7.531 1.00 31.66 C ANISOU 661 CG2 VAL A 86 4472 3842 3715 -121 -279 -17 C ATOM 662 N LEU A 87 -21.431 -13.159 4.231 1.00 37.99 N ANISOU 662 N LEU A 87 5345 4762 4326 111 -360 -203 N ATOM 663 CA LEU A 87 -21.454 -14.457 3.583 1.00 39.07 C ANISOU 663 CA LEU A 87 5567 4852 4426 147 -457 -290 C ATOM 664 C LEU A 87 -21.115 -15.528 4.608 1.00 41.56 C ANISOU 664 C LEU A 87 5965 5042 4783 154 -519 -324 C ATOM 665 O LEU A 87 -20.088 -15.440 5.289 1.00 39.03 O ANISOU 665 O LEU A 87 5640 4718 4474 207 -491 -341 O ATOM 666 CB LEU A 87 -20.470 -14.496 2.415 1.00 42.17 C ANISOU 666 CB LEU A 87 5951 5341 4729 246 -443 -373 C ATOM 667 CG LEU A 87 -20.602 -15.669 1.444 1.00 42.02 C ANISOU 667 CG LEU A 87 6009 5300 4656 292 -541 -477 C ATOM 668 CD1 LEU A 87 -21.951 -15.631 0.750 1.00 44.92 C ANISOU 668 CD1 LEU A 87 6383 5670 5013 218 -588 -439 C ATOM 669 CD2 LEU A 87 -19.481 -15.624 0.427 1.00 45.27 C ANISOU 669 CD2 LEU A 87 6397 5831 4972 395 -505 -570 C ATOM 670 N LYS A 88 -21.984 -16.527 4.722 1.00 40.19 N ANISOU 670 N LYS A 88 5871 4765 4634 94 -611 -331 N ATOM 671 CA LYS A 88 -21.781 -17.640 5.640 1.00 37.07 C ANISOU 671 CA LYS A 88 5580 4230 4274 85 -691 -351 C ATOM 672 C LYS A 88 -21.298 -18.836 4.830 1.00 38.86 C ANISOU 672 C LYS A 88 5896 4400 4468 175 -800 -471 C ATOM 673 O LYS A 88 -22.061 -19.419 4.054 1.00 42.59 O ANISOU 673 O LYS A 88 6407 4845 4929 143 -869 -503 O ATOM 674 CB LYS A 88 -23.067 -17.961 6.399 1.00 37.89 C ANISOU 674 CB LYS A 88 5719 4249 4429 -60 -719 -273 C ATOM 675 CG LYS A 88 -23.529 -16.843 7.323 1.00 37.29 C ANISOU 675 CG LYS A 88 5554 4227 4387 -140 -614 -174 C ATOM 676 CD LYS A 88 -24.488 -17.352 8.386 1.00 40.53 C ANISOU 676 CD LYS A 88 6012 4549 4838 -278 -636 -111 C ATOM 677 CE LYS A 88 -25.805 -17.802 7.777 1.00 44.87 C ANISOU 677 CE LYS A 88 6559 5082 5406 -375 -686 -109 C ATOM 678 NZ LYS A 88 -26.806 -18.143 8.823 1.00 44.33 N ANISOU 678 NZ LYS A 88 6510 4957 5376 -532 -682 -41 N ATOM 679 N LEU A 89 -20.028 -19.191 5.003 1.00 35.32 N ANISOU 679 N LEU A 89 5473 3938 4009 291 -820 -547 N ATOM 680 CA LEU A 89 -19.407 -20.292 4.276 1.00 38.85 C ANISOU 680 CA LEU A 89 5993 4336 4430 403 -922 -684 C ATOM 681 C LEU A 89 -19.302 -21.489 5.213 1.00 39.50 C ANISOU 681 C LEU A 89 6212 4228 4568 402 -1049 -696 C ATOM 682 O LEU A 89 -18.451 -21.512 6.108 1.00 39.01 O ANISOU 682 O LEU A 89 6164 4127 4530 454 -1053 -694 O ATOM 683 CB LEU A 89 -18.033 -19.889 3.748 1.00 39.10 C ANISOU 683 CB LEU A 89 5949 4494 4415 545 -863 -779 C ATOM 684 CG LEU A 89 -17.973 -18.680 2.814 1.00 37.45 C ANISOU 684 CG LEU A 89 5616 4475 4137 543 -736 -759 C ATOM 685 CD1 LEU A 89 -16.530 -18.279 2.553 1.00 38.80 C ANISOU 685 CD1 LEU A 89 5706 4768 4270 660 -666 -841 C ATOM 686 CD2 LEU A 89 -18.690 -18.981 1.511 1.00 39.20 C ANISOU 686 CD2 LEU A 89 5859 4737 4297 533 -774 -804 C ATOM 687 N LYS A 90 -20.166 -22.479 5.008 1.00 34.79 N ANISOU 687 N LYS A 90 5720 3507 3992 337 -1159 -706 N ATOM 688 CA LYS A 90 -20.108 -23.691 5.812 1.00 39.39 C ANISOU 688 CA LYS A 90 6454 3887 4624 325 -1297 -711 C ATOM 689 C LYS A 90 -18.899 -24.523 5.409 1.00 41.93 C ANISOU 689 C LYS A 90 6833 4156 4941 507 -1397 -867 C ATOM 690 O LYS A 90 -18.657 -24.751 4.219 1.00 39.77 O ANISOU 690 O LYS A 90 6535 3947 4628 601 -1417 -992 O ATOM 691 CB LYS A 90 -21.390 -24.505 5.649 1.00 38.30 C ANISOU 691 CB LYS A 90 6410 3628 4513 191 -1388 -680 C ATOM 692 CG LYS A 90 -21.616 -25.518 6.761 1.00 41.88 C ANISOU 692 CG LYS A 90 7021 3872 5019 108 -1503 -620 C ATOM 693 CD LYS A 90 -22.819 -26.400 6.473 1.00 46.07 C ANISOU 693 CD LYS A 90 7643 4281 5579 -28 -1601 -604 C ATOM 694 CE LYS A 90 -23.238 -27.180 7.709 1.00 48.68 C ANISOU 694 CE LYS A 90 8119 4424 5952 -166 -1681 -499 C ATOM 695 NZ LYS A 90 -24.350 -28.127 7.418 1.00 50.75 N ANISOU 695 NZ LYS A 90 8477 4556 6249 -309 -1786 -490 N ATOM 696 N VAL A 91 -18.141 -24.977 6.404 1.00 42.73 N ANISOU 696 N VAL A 91 7008 4146 5080 562 -1465 -865 N ATOM 697 CA VAL A 91 -16.939 -25.759 6.166 1.00 43.23 C ANISOU 697 CA VAL A 91 7119 4153 5155 749 -1573 -1019 C ATOM 698 C VAL A 91 -17.100 -27.138 6.792 1.00 42.93 C ANISOU 698 C VAL A 91 7279 3859 5175 737 -1766 -1021 C ATOM 699 O VAL A 91 -17.959 -27.365 7.647 1.00 44.49 O ANISOU 699 O VAL A 91 7571 3937 5398 576 -1796 -882 O ATOM 700 CB VAL A 91 -15.668 -25.061 6.694 1.00 42.78 C ANISOU 700 CB VAL A 91 6962 4197 5094 862 -1501 -1043 C ATOM 701 CG1 VAL A 91 -15.337 -23.844 5.836 1.00 41.23 C ANISOU 701 CG1 VAL A 91 6581 4245 4838 894 -1329 -1073 C ATOM 702 CG2 VAL A 91 -15.843 -24.667 8.145 1.00 41.00 C ANISOU 702 CG2 VAL A 91 6769 3914 4896 758 -1475 -889 C ATOM 703 N ASP A 92 -16.255 -28.071 6.346 1.00 52.73 N ANISOU 703 N ASP A 92 8584 5016 6437 909 -1901 -1184 N ATOM 704 CA ASP A 92 -16.340 -29.452 6.805 1.00 52.76 C ANISOU 704 CA ASP A 92 8790 4754 6501 918 -2110 -1203 C ATOM 705 C ASP A 92 -15.639 -29.687 8.136 1.00 53.21 C ANISOU 705 C ASP A 92 8933 4687 6597 954 -2189 -1142 C ATOM 706 O ASP A 92 -15.732 -30.794 8.677 1.00 54.57 O ANISOU 706 O ASP A 92 9264 4658 6814 935 -2350 -1104 O ATOM 707 CB ASP A 92 -15.761 -30.401 5.749 1.00 56.73 C ANISOU 707 CB ASP A 92 9316 5220 7018 1095 -2230 -1405 C ATOM 708 CG ASP A 92 -14.276 -30.182 5.509 1.00 58.89 C ANISOU 708 CG ASP A 92 9462 5631 7284 1313 -2198 -1545 C ATOM 709 OD1 ASP A 92 -13.726 -29.167 5.987 1.00 58.41 O ANISOU 709 OD1 ASP A 92 9308 5685 7201 1336 -2088 -1524 O ATOM 710 OD2 ASP A 92 -13.656 -31.026 4.828 1.00 62.40 O ANISOU 710 OD2 ASP A 92 9882 6080 7746 1456 -2279 -1675 O ATOM 711 N THR A 93 -14.947 -28.687 8.674 1.00 44.45 N ANISOU 711 N THR A 93 7698 3726 5466 992 -2067 -1105 N ATOM 712 CA THR A 93 -14.199 -28.826 9.915 1.00 43.87 C ANISOU 712 CA THR A 93 7692 3557 5421 1040 -2141 -1058 C ATOM 713 C THR A 93 -14.694 -27.807 10.927 1.00 43.86 C ANISOU 713 C THR A 93 7641 3637 5386 873 -2000 -871 C ATOM 714 O THR A 93 -14.751 -26.608 10.632 1.00 40.68 O ANISOU 714 O THR A 93 7065 3444 4947 842 -1817 -849 O ATOM 715 CB THR A 93 -12.697 -28.641 9.685 1.00 47.14 C ANISOU 715 CB THR A 93 7994 4072 5848 1272 -2148 -1222 C ATOM 716 OG1 THR A 93 -12.246 -29.563 8.684 1.00 51.17 O ANISOU 716 OG1 THR A 93 8499 4564 6378 1420 -2248 -1389 O ATOM 717 CG2 THR A 93 -11.927 -28.883 10.976 1.00 47.43 C ANISOU 717 CG2 THR A 93 8112 3992 5918 1331 -2256 -1180 C ATOM 718 N ALA A 94 -15.053 -28.285 12.114 1.00 42.62 N ANISOU 718 N ALA A 94 7644 3312 5237 765 -2088 -739 N ATOM 719 CA ALA A 94 -15.382 -27.395 13.214 1.00 43.13 C ANISOU 719 CA ALA A 94 7673 3449 5265 627 -1969 -579 C ATOM 720 C ALA A 94 -14.107 -26.805 13.801 1.00 42.29 C ANISOU 720 C ALA A 94 7484 3427 5159 768 -1950 -622 C ATOM 721 O ALA A 94 -13.114 -27.512 13.991 1.00 42.61 O ANISOU 721 O ALA A 94 7596 3361 5233 929 -2103 -714 O ATOM 722 CB ALA A 94 -16.171 -28.137 14.293 1.00 45.20 C ANISOU 722 CB ALA A 94 8139 3515 5519 454 -2067 -424 C ATOM 723 N ASN A 95 -14.133 -25.508 14.076 1.00 37.15 N ANISOU 723 N ASN A 95 6678 2961 4475 712 -1770 -564 N ATOM 724 CA ASN A 95 -12.970 -24.847 14.660 1.00 32.52 C ANISOU 724 CA ASN A 95 6000 2466 3890 827 -1741 -600 C ATOM 725 C ASN A 95 -12.732 -25.382 16.064 1.00 35.01 C ANISOU 725 C ASN A 95 6480 2624 4198 804 -1872 -513 C ATOM 726 O ASN A 95 -13.579 -25.174 16.944 1.00 36.49 O ANISOU 726 O ASN A 95 6739 2783 4343 627 -1827 -359 O ATOM 727 CB ASN A 95 -13.167 -23.330 14.687 1.00 33.34 C ANISOU 727 CB ASN A 95 5919 2785 3965 750 -1527 -545 C ATOM 728 CG ASN A 95 -11.892 -22.575 15.038 1.00 36.57 C ANISOU 728 CG ASN A 95 6201 3309 4384 875 -1486 -611 C ATOM 729 OD1 ASN A 95 -10.920 -23.156 15.521 1.00 33.62 O ANISOU 729 OD1 ASN A 95 5885 2854 4035 1005 -1621 -677 O ATOM 730 ND2 ASN A 95 -11.896 -21.268 14.798 1.00 34.26 N ANISOU 730 ND2 ASN A 95 5735 3204 4079 836 -1309 -596 N ATOM 731 N PRO A 96 -11.617 -26.070 16.325 1.00 44.13 N ANISOU 731 N PRO A 96 7700 3679 5388 978 -2037 -607 N ATOM 732 CA PRO A 96 -11.385 -26.601 17.676 1.00 47.64 C ANISOU 732 CA PRO A 96 8320 3963 5816 959 -2181 -514 C ATOM 733 C PRO A 96 -11.115 -25.524 18.712 1.00 45.97 C ANISOU 733 C PRO A 96 8029 3877 5561 908 -2074 -433 C ATOM 734 O PRO A 96 -11.261 -25.794 19.910 1.00 48.19 O ANISOU 734 O PRO A 96 8461 4052 5798 828 -2152 -314 O ATOM 735 CB PRO A 96 -10.170 -27.519 17.489 1.00 50.71 C ANISOU 735 CB PRO A 96 8763 4236 6268 1194 -2386 -668 C ATOM 736 CG PRO A 96 -9.451 -26.944 16.312 1.00 51.45 C ANISOU 736 CG PRO A 96 8629 4522 6397 1345 -2281 -846 C ATOM 737 CD PRO A 96 -10.512 -26.388 15.402 1.00 46.31 C ANISOU 737 CD PRO A 96 7887 3991 5716 1205 -2102 -808 C ATOM 738 N LYS A 97 -10.726 -24.322 18.291 1.00 43.01 N ANISOU 738 N LYS A 97 7431 3720 5192 946 -1903 -493 N ATOM 739 CA LYS A 97 -10.495 -23.205 19.196 1.00 40.63 C ANISOU 739 CA LYS A 97 7039 3543 4855 895 -1793 -429 C ATOM 740 C LYS A 97 -11.707 -22.290 19.325 1.00 39.23 C ANISOU 740 C LYS A 97 6805 3470 4632 691 -1603 -305 C ATOM 741 O LYS A 97 -11.562 -21.155 19.793 1.00 38.85 O ANISOU 741 O LYS A 97 6637 3559 4565 656 -1478 -278 O ATOM 742 CB LYS A 97 -9.278 -22.397 18.738 1.00 41.56 C ANISOU 742 CB LYS A 97 6946 3829 5015 1054 -1727 -570 C ATOM 743 CG LYS A 97 -8.066 -23.249 18.392 1.00 45.25 C ANISOU 743 CG LYS A 97 7424 4229 5542 1274 -1897 -730 C ATOM 744 CD LYS A 97 -7.034 -22.463 17.601 1.00 46.25 C ANISOU 744 CD LYS A 97 7310 4553 5708 1407 -1796 -882 C ATOM 745 CE LYS A 97 -5.633 -23.004 17.841 1.00 50.67 C ANISOU 745 CE LYS A 97 7851 5077 6323 1620 -1958 -1028 C ATOM 746 NZ LYS A 97 -5.152 -23.825 16.696 1.00 55.70 N ANISOU 746 NZ LYS A 97 8457 5696 7009 1782 -2035 -1201 N ATOM 747 N THR A 98 -12.885 -22.747 18.911 1.00 38.29 N ANISOU 747 N THR A 98 6761 3288 4500 562 -1586 -239 N ATOM 748 CA THR A 98 -14.100 -21.953 19.038 1.00 37.05 C ANISOU 748 CA THR A 98 6546 3225 4305 373 -1420 -131 C ATOM 749 C THR A 98 -14.365 -21.631 20.509 1.00 38.70 C ANISOU 749 C THR A 98 6827 3425 4450 255 -1399 -9 C ATOM 750 O THR A 98 -14.517 -22.561 21.313 1.00 39.38 O ANISOU 750 O THR A 98 7107 3357 4498 200 -1528 66 O ATOM 751 CB THR A 98 -15.302 -22.689 18.454 1.00 38.64 C ANISOU 751 CB THR A 98 6832 3340 4507 252 -1437 -84 C ATOM 752 OG1 THR A 98 -15.076 -22.961 17.067 1.00 37.07 O ANISOU 752 OG1 THR A 98 6567 3161 4357 363 -1455 -205 O ATOM 753 CG2 THR A 98 -16.562 -21.847 18.599 1.00 37.88 C ANISOU 753 CG2 THR A 98 6657 3355 4382 66 -1268 14 C ATOM 754 N PRO A 99 -14.419 -20.365 20.886 1.00 37.86 N ANISOU 754 N PRO A 99 6582 3476 4327 212 -1247 12 N ATOM 755 CA PRO A 99 -14.733 -20.015 22.278 1.00 34.15 C ANISOU 755 CA PRO A 99 6175 3015 3785 95 -1215 117 C ATOM 756 C PRO A 99 -16.236 -19.927 22.492 1.00 34.96 C ANISOU 756 C PRO A 99 6302 3136 3844 -113 -1112 225 C ATOM 757 O PRO A 99 -17.038 -20.020 21.560 1.00 34.50 O ANISOU 757 O PRO A 99 6196 3092 3820 -166 -1061 218 O ATOM 758 CB PRO A 99 -14.073 -18.641 22.431 1.00 34.41 C ANISOU 758 CB PRO A 99 6026 3213 3834 160 -1097 62 C ATOM 759 CG PRO A 99 -14.216 -18.031 21.071 1.00 32.32 C ANISOU 759 CG PRO A 99 5592 3053 3634 201 -990 -9 C ATOM 760 CD PRO A 99 -14.137 -19.171 20.073 1.00 33.69 C ANISOU 760 CD PRO A 99 5838 3123 3842 272 -1102 -64 C ATOM 761 N LYS A 100 -16.609 -19.754 23.757 1.00 38.70 N ANISOU 761 N LYS A 100 6850 3618 4238 -234 -1084 319 N ATOM 762 CA LYS A 100 -17.989 -19.440 24.097 1.00 39.22 C ANISOU 762 CA LYS A 100 6897 3746 4257 -433 -956 407 C ATOM 763 C LYS A 100 -18.289 -18.012 23.656 1.00 38.86 C ANISOU 763 C LYS A 100 6627 3882 4254 -426 -777 357 C ATOM 764 O LYS A 100 -17.588 -17.076 24.057 1.00 39.79 O ANISOU 764 O LYS A 100 6654 4090 4374 -351 -728 316 O ATOM 765 CB LYS A 100 -18.210 -19.609 25.596 1.00 44.86 C ANISOU 765 CB LYS A 100 7747 4438 4860 -557 -968 510 C ATOM 766 CG LYS A 100 -19.592 -19.212 26.086 1.00 44.98 C ANISOU 766 CG LYS A 100 7726 4547 4817 -766 -819 588 C ATOM 767 CD LYS A 100 -19.797 -19.590 27.551 1.00 53.77 C ANISOU 767 CD LYS A 100 9005 5630 5797 -903 -844 696 C ATOM 768 CE LYS A 100 -18.822 -20.674 28.001 1.00 53.79 C ANISOU 768 CE LYS A 100 9223 5452 5762 -826 -1054 730 C ATOM 769 NZ LYS A 100 -18.875 -20.907 29.469 1.00 57.96 N ANISOU 769 NZ LYS A 100 9915 5963 6145 -943 -1083 837 N ATOM 770 N TYR A 101 -19.318 -17.838 22.828 1.00 34.37 N ANISOU 770 N TYR A 101 5973 3362 3725 -502 -692 359 N ATOM 771 CA TYR A 101 -19.527 -16.559 22.166 1.00 32.84 C ANISOU 771 CA TYR A 101 5575 3316 3588 -467 -553 304 C ATOM 772 C TYR A 101 -21.010 -16.245 22.029 1.00 33.19 C ANISOU 772 C TYR A 101 5548 3429 3634 -620 -441 347 C ATOM 773 O TYR A 101 -21.870 -17.126 22.111 1.00 33.12 O ANISOU 773 O TYR A 101 5633 3353 3599 -746 -474 406 O ATOM 774 CB TYR A 101 -18.861 -16.537 20.781 1.00 31.19 C ANISOU 774 CB TYR A 101 5289 3109 3454 -319 -586 215 C ATOM 775 CG TYR A 101 -19.553 -17.402 19.749 1.00 32.94 C ANISOU 775 CG TYR A 101 5551 3262 3701 -352 -636 213 C ATOM 776 CD1 TYR A 101 -19.257 -18.754 19.637 1.00 36.57 C ANISOU 776 CD1 TYR A 101 6171 3570 4154 -326 -787 211 C ATOM 777 CD2 TYR A 101 -20.497 -16.864 18.881 1.00 33.07 C ANISOU 777 CD2 TYR A 101 5449 3362 3755 -404 -544 206 C ATOM 778 CE1 TYR A 101 -19.886 -19.548 18.695 1.00 35.32 C ANISOU 778 CE1 TYR A 101 6052 3344 4023 -357 -840 199 C ATOM 779 CE2 TYR A 101 -21.132 -17.651 17.939 1.00 36.07 C ANISOU 779 CE2 TYR A 101 5864 3683 4157 -435 -597 197 C ATOM 780 CZ TYR A 101 -20.821 -18.991 17.849 1.00 37.66 C ANISOU 780 CZ TYR A 101 6225 3735 4350 -414 -742 191 C ATOM 781 OH TYR A 101 -21.450 -19.775 16.909 1.00 42.17 O ANISOU 781 OH TYR A 101 6834 4243 4947 -446 -802 173 O ATOM 782 N LYS A 102 -21.292 -14.959 21.818 1.00 36.67 N ANISOU 782 N LYS A 102 5819 4002 4113 -608 -314 314 N ATOM 783 CA LYS A 102 -22.614 -14.474 21.445 1.00 37.78 C ANISOU 783 CA LYS A 102 5850 4224 4282 -711 -212 326 C ATOM 784 C LYS A 102 -22.468 -13.432 20.345 1.00 36.94 C ANISOU 784 C LYS A 102 5582 4199 4254 -608 -155 263 C ATOM 785 O LYS A 102 -21.390 -12.872 20.127 1.00 33.03 O ANISOU 785 O LYS A 102 5046 3723 3782 -484 -161 218 O ATOM 786 CB LYS A 102 -23.377 -13.842 22.620 1.00 39.49 C ANISOU 786 CB LYS A 102 6023 4530 4450 -832 -103 360 C ATOM 787 CG LYS A 102 -23.414 -14.646 23.901 1.00 45.71 C ANISOU 787 CG LYS A 102 6968 5264 5134 -941 -140 430 C ATOM 788 CD LYS A 102 -24.375 -14.024 24.906 1.00 46.75 C ANISOU 788 CD LYS A 102 7036 5513 5213 -1077 -11 451 C ATOM 789 CE LYS A 102 -23.691 -12.958 25.756 1.00 50.63 C ANISOU 789 CE LYS A 102 7474 6084 5677 -1007 44 411 C ATOM 790 NZ LYS A 102 -23.476 -11.675 25.025 1.00 48.14 N ANISOU 790 NZ LYS A 102 6983 5846 5464 -888 107 331 N ATOM 791 N PHE A 103 -23.576 -13.173 19.657 1.00 29.31 N ANISOU 791 N PHE A 103 4525 3281 3328 -668 -102 264 N ATOM 792 CA PHE A 103 -23.682 -12.090 18.686 1.00 31.01 C ANISOU 792 CA PHE A 103 4593 3578 3612 -596 -44 222 C ATOM 793 C PHE A 103 -24.549 -11.001 19.305 1.00 31.07 C ANISOU 793 C PHE A 103 4480 3686 3638 -662 69 224 C ATOM 794 O PHE A 103 -25.739 -11.218 19.555 1.00 32.24 O ANISOU 794 O PHE A 103 4605 3863 3783 -779 104 244 O ATOM 795 CB PHE A 103 -24.282 -12.578 17.368 1.00 31.53 C ANISOU 795 CB PHE A 103 4644 3624 3711 -598 -86 212 C ATOM 796 CG PHE A 103 -23.355 -13.433 16.551 1.00 28.46 C ANISOU 796 CG PHE A 103 4344 3157 3314 -502 -189 182 C ATOM 797 CD1 PHE A 103 -22.010 -13.529 16.866 1.00 27.95 C ANISOU 797 CD1 PHE A 103 4332 3060 3229 -401 -228 156 C ATOM 798 CD2 PHE A 103 -23.835 -14.136 15.459 1.00 30.28 C ANISOU 798 CD2 PHE A 103 4596 3351 3557 -508 -248 166 C ATOM 799 CE1 PHE A 103 -21.161 -14.315 16.107 1.00 28.97 C ANISOU 799 CE1 PHE A 103 4527 3127 3354 -302 -321 109 C ATOM 800 CE2 PHE A 103 -22.993 -14.923 14.697 1.00 27.28 C ANISOU 800 CE2 PHE A 103 4292 2905 3166 -412 -341 121 C ATOM 801 CZ PHE A 103 -21.655 -15.013 15.022 1.00 29.39 C ANISOU 801 CZ PHE A 103 4604 3145 3416 -306 -375 89 C ATOM 802 N VAL A 104 -23.957 -9.837 19.556 1.00 29.55 N ANISOU 802 N VAL A 104 4208 3548 3471 -587 122 194 N ATOM 803 CA VAL A 104 -24.686 -8.710 20.119 1.00 29.17 C ANISOU 803 CA VAL A 104 4043 3589 3452 -625 220 177 C ATOM 804 C VAL A 104 -24.599 -7.536 19.156 1.00 29.14 C ANISOU 804 C VAL A 104 3918 3624 3530 -535 247 145 C ATOM 805 O VAL A 104 -23.628 -7.388 18.406 1.00 28.72 O ANISOU 805 O VAL A 104 3874 3544 3492 -442 209 137 O ATOM 806 CB VAL A 104 -24.159 -8.309 21.517 1.00 32.20 C ANISOU 806 CB VAL A 104 4452 3996 3786 -634 259 168 C ATOM 807 CG1 VAL A 104 -24.184 -9.502 22.460 1.00 33.85 C ANISOU 807 CG1 VAL A 104 4805 4158 3899 -727 220 214 C ATOM 808 CG2 VAL A 104 -22.757 -7.730 21.418 1.00 32.31 C ANISOU 808 CG2 VAL A 104 4464 3992 3819 -512 233 139 C ATOM 809 N ARG A 105 -25.639 -6.709 19.166 1.00 30.04 N ANISOU 809 N ARG A 105 3917 3802 3695 -567 308 127 N ATOM 810 CA ARG A 105 -25.665 -5.455 18.423 1.00 32.18 C ANISOU 810 CA ARG A 105 4078 4102 4047 -490 329 104 C ATOM 811 C ARG A 105 -25.581 -4.324 19.439 1.00 32.18 C ANISOU 811 C ARG A 105 4011 4144 4071 -477 396 65 C ATOM 812 O ARG A 105 -26.537 -4.075 20.181 1.00 33.97 O ANISOU 812 O ARG A 105 4178 4427 4304 -538 452 37 O ATOM 813 CB ARG A 105 -26.923 -5.340 17.566 1.00 32.67 C ANISOU 813 CB ARG A 105 4058 4193 4163 -516 324 103 C ATOM 814 CG ARG A 105 -26.990 -4.056 16.756 1.00 29.92 C ANISOU 814 CG ARG A 105 3613 3860 3896 -434 327 90 C ATOM 815 CD ARG A 105 -28.182 -4.042 15.817 1.00 32.62 C ANISOU 815 CD ARG A 105 3885 4224 4286 -449 298 90 C ATOM 816 NE ARG A 105 -28.203 -2.838 14.991 1.00 31.64 N ANISOU 816 NE ARG A 105 3689 4099 4233 -367 281 91 N ATOM 817 CZ ARG A 105 -27.609 -2.734 13.807 1.00 30.14 C ANISOU 817 CZ ARG A 105 3536 3880 4035 -310 231 128 C ATOM 818 NH1 ARG A 105 -26.946 -3.766 13.302 1.00 27.13 N ANISOU 818 NH1 ARG A 105 3251 3475 3584 -313 195 149 N ATOM 819 NH2 ARG A 105 -27.678 -1.599 13.125 1.00 30.27 N ANISOU 819 NH2 ARG A 105 3499 3890 4111 -250 213 140 N ATOM 820 N ILE A 106 -24.436 -3.647 19.476 1.00 30.93 N ANISOU 820 N ILE A 106 3858 3966 3928 -400 391 54 N ATOM 821 CA ILE A 106 -24.184 -2.622 20.482 1.00 31.73 C ANISOU 821 CA ILE A 106 3912 4094 4050 -384 442 10 C ATOM 822 C ILE A 106 -24.927 -1.342 20.126 1.00 31.25 C ANISOU 822 C ILE A 106 3729 4058 4087 -353 473 -23 C ATOM 823 O ILE A 106 -25.403 -1.175 18.997 1.00 29.20 O ANISOU 823 O ILE A 106 3429 3787 3877 -330 445 -1 O ATOM 824 CB ILE A 106 -22.677 -2.351 20.637 1.00 31.43 C ANISOU 824 CB ILE A 106 3917 4023 4003 -319 418 5 C ATOM 825 CG1 ILE A 106 -22.051 -2.044 19.276 1.00 32.38 C ANISOU 825 CG1 ILE A 106 4020 4114 4170 -254 383 29 C ATOM 826 CG2 ILE A 106 -21.990 -3.533 21.302 1.00 34.87 C ANISOU 826 CG2 ILE A 106 4470 4435 4345 -342 380 21 C ATOM 827 CD1 ILE A 106 -20.786 -1.231 19.365 1.00 32.96 C ANISOU 827 CD1 ILE A 106 4077 4175 4272 -197 384 10 C ATOM 828 N GLN A 107 -25.025 -0.436 21.089 1.00 33.37 N ANISOU 828 N GLN A 107 3942 4355 4380 -346 521 -80 N ATOM 829 CA GLN A 107 -25.652 0.874 21.047 1.00 33.36 C ANISOU 829 CA GLN A 107 3830 4368 4479 -305 544 -132 C ATOM 830 C GLN A 107 -24.622 1.950 20.724 1.00 32.17 C ANISOU 830 C GLN A 107 3672 4159 4391 -230 520 -133 C ATOM 831 O GLN A 107 -23.433 1.791 21.023 1.00 32.71 O ANISOU 831 O GLN A 107 3803 4205 4419 -220 510 -122 O ATOM 832 CB GLN A 107 -26.308 1.189 22.389 1.00 36.79 C ANISOU 832 CB GLN A 107 4212 4870 4895 -342 612 -210 C ATOM 833 CG GLN A 107 -27.394 0.211 22.795 1.00 37.65 C ANISOU 833 CG GLN A 107 4315 5051 4939 -438 651 -211 C ATOM 834 CD GLN A 107 -28.633 0.335 21.933 1.00 41.47 C ANISOU 834 CD GLN A 107 4700 5558 5500 -438 643 -220 C ATOM 835 OE1 GLN A 107 -29.077 1.439 21.619 1.00 43.87 O ANISOU 835 OE1 GLN A 107 4902 5859 5906 -370 637 -269 O ATOM 836 NE2 GLN A 107 -29.199 -0.802 21.544 1.00 44.91 N ANISOU 836 NE2 GLN A 107 5165 6009 5889 -514 631 -174 N ATOM 837 N PRO A 108 -25.047 3.049 20.104 1.00 32.57 N ANISOU 837 N PRO A 108 3648 4183 4545 -181 504 -144 N ATOM 838 CA PRO A 108 -24.135 4.184 19.920 1.00 32.43 C ANISOU 838 CA PRO A 108 3624 4104 4594 -128 484 -145 C ATOM 839 C PRO A 108 -23.670 4.719 21.266 1.00 32.52 C ANISOU 839 C PRO A 108 3628 4126 4603 -125 519 -222 C ATOM 840 O PRO A 108 -24.463 4.892 22.194 1.00 34.80 O ANISOU 840 O PRO A 108 3868 4463 4891 -137 560 -297 O ATOM 841 CB PRO A 108 -24.986 5.209 19.159 1.00 35.21 C ANISOU 841 CB PRO A 108 3902 4419 5056 -82 452 -147 C ATOM 842 CG PRO A 108 -26.405 4.783 19.383 1.00 36.20 C ANISOU 842 CG PRO A 108 3965 4608 5183 -103 472 -189 C ATOM 843 CD PRO A 108 -26.364 3.293 19.494 1.00 34.26 C ANISOU 843 CD PRO A 108 3782 4412 4822 -172 491 -153 C ATOM 844 N GLY A 109 -22.367 4.970 21.369 1.00 32.26 N ANISOU 844 N GLY A 109 3637 4056 4564 -112 505 -210 N ATOM 845 CA GLY A 109 -21.746 5.382 22.605 1.00 32.17 C ANISOU 845 CA GLY A 109 3630 4053 4539 -111 525 -281 C ATOM 846 C GLY A 109 -20.999 4.281 23.329 1.00 33.03 C ANISOU 846 C GLY A 109 3818 4200 4531 -144 529 -274 C ATOM 847 O GLY A 109 -20.184 4.580 24.209 1.00 33.74 O ANISOU 847 O GLY A 109 3925 4291 4604 -137 527 -321 O ATOM 848 N GLN A 110 -21.255 3.023 22.985 1.00 30.08 N ANISOU 848 N GLN A 110 3498 3851 4080 -177 523 -219 N ATOM 849 CA GLN A 110 -20.562 1.897 23.588 1.00 32.40 C ANISOU 849 CA GLN A 110 3882 4163 4266 -202 506 -204 C ATOM 850 C GLN A 110 -19.246 1.632 22.865 1.00 32.05 C ANISOU 850 C GLN A 110 3873 4080 4225 -165 457 -166 C ATOM 851 O GLN A 110 -19.064 1.989 21.698 1.00 30.25 O ANISOU 851 O GLN A 110 3613 3825 4055 -140 446 -130 O ATOM 852 CB GLN A 110 -21.440 0.645 23.562 1.00 33.18 C ANISOU 852 CB GLN A 110 4030 4290 4287 -259 512 -164 C ATOM 853 CG GLN A 110 -22.635 0.710 24.499 1.00 36.66 C ANISOU 853 CG GLN A 110 4437 4794 4697 -315 571 -209 C ATOM 854 CD GLN A 110 -22.238 1.036 25.925 1.00 40.96 C ANISOU 854 CD GLN A 110 5002 5375 5185 -326 596 -271 C ATOM 855 OE1 GLN A 110 -21.661 0.204 26.626 1.00 43.90 O ANISOU 855 OE1 GLN A 110 5472 5752 5455 -355 573 -251 O ATOM 856 NE2 GLN A 110 -22.544 2.252 26.362 1.00 42.01 N ANISOU 856 NE2 GLN A 110 5049 5528 5384 -297 633 -351 N ATOM 857 N THR A 111 -18.324 0.992 23.576 1.00 26.78 N ANISOU 857 N THR A 111 3271 3416 3487 -161 427 -178 N ATOM 858 CA THR A 111 -16.991 0.720 23.064 1.00 27.69 C ANISOU 858 CA THR A 111 3404 3511 3604 -119 381 -166 C ATOM 859 C THR A 111 -16.786 -0.776 22.859 1.00 25.44 C ANISOU 859 C THR A 111 3209 3219 3237 -118 334 -130 C ATOM 860 O THR A 111 -17.541 -1.609 23.368 1.00 27.63 O ANISOU 860 O THR A 111 3552 3501 3446 -161 330 -111 O ATOM 861 CB THR A 111 -15.914 1.262 24.010 1.00 27.04 C ANISOU 861 CB THR A 111 3315 3432 3527 -97 363 -225 C ATOM 862 OG1 THR A 111 -16.112 0.723 25.323 1.00 29.04 O ANISOU 862 OG1 THR A 111 3635 3707 3691 -121 353 -250 O ATOM 863 CG2 THR A 111 -15.976 2.781 24.072 1.00 26.29 C ANISOU 863 CG2 THR A 111 3134 3324 3530 -94 397 -264 C ATOM 864 N PHE A 112 -15.742 -1.103 22.101 1.00 25.52 N ANISOU 864 N PHE A 112 3220 3219 3256 -70 295 -125 N ATOM 865 CA PHE A 112 -15.376 -2.488 21.842 1.00 26.79 C ANISOU 865 CA PHE A 112 3463 3363 3353 -47 234 -108 C ATOM 866 C PHE A 112 -13.949 -2.526 21.321 1.00 24.93 C ANISOU 866 C PHE A 112 3198 3136 3140 20 199 -141 C ATOM 867 O PHE A 112 -13.387 -1.505 20.916 1.00 26.19 O ANISOU 867 O PHE A 112 3269 3318 3363 31 233 -158 O ATOM 868 CB PHE A 112 -16.336 -3.154 20.849 1.00 25.95 C ANISOU 868 CB PHE A 112 3381 3245 3236 -71 238 -60 C ATOM 869 CG PHE A 112 -16.427 -2.453 19.521 1.00 26.89 C ANISOU 869 CG PHE A 112 3422 3379 3415 -56 272 -42 C ATOM 870 CD1 PHE A 112 -15.641 -2.854 18.454 1.00 23.70 C ANISOU 870 CD1 PHE A 112 3014 2984 3007 -10 248 -43 C ATOM 871 CD2 PHE A 112 -17.307 -1.400 19.337 1.00 25.76 C ANISOU 871 CD2 PHE A 112 3214 3244 3329 -87 324 -27 C ATOM 872 CE1 PHE A 112 -15.728 -2.214 17.231 1.00 24.48 C ANISOU 872 CE1 PHE A 112 3054 3105 3142 -7 281 -18 C ATOM 873 CE2 PHE A 112 -17.398 -0.756 18.117 1.00 27.64 C ANISOU 873 CE2 PHE A 112 3398 3488 3615 -77 341 2 C ATOM 874 CZ PHE A 112 -16.607 -1.164 17.063 1.00 28.90 C ANISOU 874 CZ PHE A 112 3565 3662 3756 -44 322 13 C ATOM 875 N SER A 113 -13.371 -3.723 21.335 1.00 26.57 N ANISOU 875 N SER A 113 3475 3323 3296 63 127 -152 N ATOM 876 CA SER A 113 -12.008 -3.943 20.875 1.00 26.32 C ANISOU 876 CA SER A 113 3408 3310 3281 138 86 -201 C ATOM 877 C SER A 113 -12.020 -4.523 19.468 1.00 26.35 C ANISOU 877 C SER A 113 3405 3324 3283 166 86 -191 C ATOM 878 O SER A 113 -12.809 -5.422 19.163 1.00 26.53 O ANISOU 878 O SER A 113 3504 3310 3265 153 60 -158 O ATOM 879 CB SER A 113 -11.258 -4.886 21.819 1.00 27.31 C ANISOU 879 CB SER A 113 3613 3405 3357 188 -12 -237 C ATOM 880 OG SER A 113 -11.146 -4.328 23.115 1.00 28.78 O ANISOU 880 OG SER A 113 3808 3594 3532 165 -16 -253 O ATOM 881 N VAL A 114 -11.139 -4.006 18.616 1.00 26.24 N ANISOU 881 N VAL A 114 3298 3364 3307 198 117 -222 N ATOM 882 CA VAL A 114 -11.008 -4.453 17.234 1.00 24.94 C ANISOU 882 CA VAL A 114 3116 3232 3130 227 126 -225 C ATOM 883 C VAL A 114 -9.703 -5.223 17.098 1.00 25.68 C ANISOU 883 C VAL A 114 3193 3353 3212 318 67 -309 C ATOM 884 O VAL A 114 -8.636 -4.717 17.468 1.00 26.20 O ANISOU 884 O VAL A 114 3183 3461 3312 343 70 -361 O ATOM 885 CB VAL A 114 -11.047 -3.271 16.249 1.00 25.97 C ANISOU 885 CB VAL A 114 3153 3416 3298 184 213 -193 C ATOM 886 CG1 VAL A 114 -10.716 -3.743 14.840 1.00 28.68 C ANISOU 886 CG1 VAL A 114 3476 3814 3608 217 225 -207 C ATOM 887 CG2 VAL A 114 -12.404 -2.594 16.282 1.00 24.62 C ANISOU 887 CG2 VAL A 114 2998 3210 3145 114 253 -120 C ATOM 888 N LEU A 115 -9.789 -6.443 16.574 1.00 22.76 N ANISOU 888 N LEU A 115 2890 2959 2800 370 8 -330 N ATOM 889 CA LEU A 115 -8.608 -7.233 16.230 1.00 24.30 C ANISOU 889 CA LEU A 115 3061 3183 2989 474 -51 -426 C ATOM 890 C LEU A 115 -8.373 -7.050 14.735 1.00 23.68 C ANISOU 890 C LEU A 115 2904 3193 2899 483 17 -448 C ATOM 891 O LEU A 115 -8.945 -7.756 13.904 1.00 26.35 O ANISOU 891 O LEU A 115 3297 3518 3198 494 2 -441 O ATOM 892 CB LEU A 115 -8.790 -8.700 16.605 1.00 24.54 C ANISOU 892 CB LEU A 115 3222 3120 2982 533 -172 -446 C ATOM 893 CG LEU A 115 -7.658 -9.637 16.174 1.00 26.22 C ANISOU 893 CG LEU A 115 3417 3350 3196 661 -251 -559 C ATOM 894 CD1 LEU A 115 -6.334 -9.200 16.776 1.00 26.12 C ANISOU 894 CD1 LEU A 115 3306 3394 3224 719 -268 -637 C ATOM 895 CD2 LEU A 115 -7.968 -11.077 16.549 1.00 25.10 C ANISOU 895 CD2 LEU A 115 3427 3085 3023 713 -386 -567 C ATOM 896 N ALA A 116 -7.531 -6.078 14.394 1.00 26.33 N ANISOU 896 N ALA A 116 3114 3625 3266 468 92 -473 N ATOM 897 CA ALA A 116 -7.222 -5.813 12.996 1.00 29.00 C ANISOU 897 CA ALA A 116 3375 4065 3578 461 168 -488 C ATOM 898 C ALA A 116 -6.396 -6.954 12.416 1.00 30.37 C ANISOU 898 C ALA A 116 3533 4285 3719 573 117 -604 C ATOM 899 O ALA A 116 -5.391 -7.369 13.001 1.00 30.78 O ANISOU 899 O ALA A 116 3548 4348 3801 654 58 -697 O ATOM 900 CB ALA A 116 -6.474 -4.489 12.859 1.00 31.29 C ANISOU 900 CB ALA A 116 3538 4443 3909 400 261 -481 C ATOM 901 N CYS A 117 -6.827 -7.462 11.264 1.00 30.48 N ANISOU 901 N CYS A 117 3577 4327 3677 584 132 -608 N ATOM 902 CA CYS A 117 -6.160 -8.568 10.597 1.00 31.88 C ANISOU 902 CA CYS A 117 3745 4549 3819 696 83 -730 C ATOM 903 C CYS A 117 -5.962 -8.232 9.126 1.00 35.12 C ANISOU 903 C CYS A 117 4080 5097 4168 673 184 -748 C ATOM 904 O CYS A 117 -6.661 -7.386 8.561 1.00 33.87 O ANISOU 904 O CYS A 117 3925 4962 3983 572 262 -644 O ATOM 905 CB CYS A 117 -6.957 -9.873 10.732 1.00 31.53 C ANISOU 905 CB CYS A 117 3848 4378 3753 749 -32 -735 C ATOM 906 SG CYS A 117 -7.389 -10.320 12.428 1.00 32.16 S ANISOU 906 SG CYS A 117 4049 4292 3877 747 -147 -685 S ATOM 907 N TYR A 118 -4.990 -8.903 8.511 1.00 38.15 N ANISOU 907 N TYR A 118 4396 5575 4525 772 176 -885 N ATOM 908 CA TYR A 118 -4.703 -8.737 7.091 1.00 37.81 C ANISOU 908 CA TYR A 118 4282 5683 4402 758 271 -924 C ATOM 909 C TYR A 118 -4.329 -10.092 6.515 1.00 41.15 C ANISOU 909 C TYR A 118 4722 6127 4785 897 199 -1075 C ATOM 910 O TYR A 118 -3.391 -10.733 6.998 1.00 39.33 O ANISOU 910 O TYR A 118 4444 5901 4600 1012 131 -1205 O ATOM 911 CB TYR A 118 -3.584 -7.715 6.866 1.00 41.37 C ANISOU 911 CB TYR A 118 4567 6292 4861 708 389 -950 C ATOM 912 CG TYR A 118 -3.989 -6.312 7.246 1.00 43.76 C ANISOU 912 CG TYR A 118 4859 6569 5199 565 461 -800 C ATOM 913 CD1 TYR A 118 -3.765 -5.824 8.527 1.00 45.54 C ANISOU 913 CD1 TYR A 118 5068 6719 5517 548 428 -776 C ATOM 914 CD2 TYR A 118 -4.621 -5.483 6.331 1.00 45.12 C ANISOU 914 CD2 TYR A 118 5048 6784 5312 452 550 -686 C ATOM 915 CE1 TYR A 118 -4.147 -4.544 8.881 1.00 45.92 C ANISOU 915 CE1 TYR A 118 5108 6734 5604 426 485 -653 C ATOM 916 CE2 TYR A 118 -5.003 -4.206 6.674 1.00 45.42 C ANISOU 916 CE2 TYR A 118 5084 6781 5393 332 600 -555 C ATOM 917 CZ TYR A 118 -4.767 -3.738 7.950 1.00 46.94 C ANISOU 917 CZ TYR A 118 5253 6896 5684 321 569 -544 C ATOM 918 OH TYR A 118 -5.150 -2.462 8.296 1.00 45.28 O ANISOU 918 OH TYR A 118 5043 6639 5524 209 612 -428 O ATOM 919 N ASN A 119 -5.068 -10.520 5.488 1.00 51.20 N ANISOU 919 N ASN A 119 6066 7409 5978 890 203 -1066 N ATOM 920 CA ASN A 119 -4.885 -11.835 4.869 1.00 52.28 C ANISOU 920 CA ASN A 119 6240 7549 6074 1020 124 -1211 C ATOM 921 C ASN A 119 -5.061 -12.957 5.891 1.00 52.79 C ANISOU 921 C ASN A 119 6417 7430 6213 1117 -43 -1252 C ATOM 922 O ASN A 119 -4.366 -13.975 5.851 1.00 54.14 O ANISOU 922 O ASN A 119 6581 7592 6397 1259 -131 -1407 O ATOM 923 CB ASN A 119 -3.525 -11.938 4.173 1.00 56.33 C ANISOU 923 CB ASN A 119 6598 8253 6552 1102 190 -1378 C ATOM 924 CG ASN A 119 -3.311 -10.843 3.148 1.00 58.95 C ANISOU 924 CG ASN A 119 6828 8775 6797 988 360 -1328 C ATOM 925 OD1 ASN A 119 -4.036 -10.757 2.156 1.00 62.77 O ANISOU 925 OD1 ASN A 119 7369 9295 7184 931 403 -1274 O ATOM 926 ND2 ASN A 119 -2.314 -9.999 3.382 1.00 63.13 N ANISOU 926 ND2 ASN A 119 7209 9422 7356 946 453 -1343 N ATOM 927 N GLY A 120 -6.001 -12.769 6.815 1.00 40.44 N ANISOU 927 N GLY A 120 4958 5715 4692 1039 -89 -1115 N ATOM 928 CA GLY A 120 -6.315 -13.773 7.809 1.00 39.97 C ANISOU 928 CA GLY A 120 5027 5473 4686 1098 -242 -1120 C ATOM 929 C GLY A 120 -5.386 -13.828 9.002 1.00 38.30 C ANISOU 929 C GLY A 120 4781 5224 4548 1165 -306 -1166 C ATOM 930 O GLY A 120 -5.579 -14.684 9.874 1.00 41.00 O ANISOU 930 O GLY A 120 5242 5409 4927 1214 -443 -1165 O ATOM 931 N SER A 121 -4.388 -12.948 9.075 1.00 37.18 N ANISOU 931 N SER A 121 4484 5217 4427 1162 -217 -1202 N ATOM 932 CA SER A 121 -3.429 -12.956 10.168 1.00 36.35 C ANISOU 932 CA SER A 121 4329 5090 4392 1230 -282 -1259 C ATOM 933 C SER A 121 -3.631 -11.736 11.051 1.00 33.54 C ANISOU 933 C SER A 121 3945 4730 4070 1107 -215 -1132 C ATOM 934 O SER A 121 -3.685 -10.611 10.539 1.00 33.46 O ANISOU 934 O SER A 121 3843 4828 4042 1004 -77 -1072 O ATOM 935 CB SER A 121 -1.995 -12.973 9.627 1.00 39.02 C ANISOU 935 CB SER A 121 4491 5594 4741 1334 -247 -1431 C ATOM 936 OG SER A 121 -1.632 -14.270 9.188 1.00 45.95 O ANISOU 936 OG SER A 121 5401 6445 5613 1491 -357 -1582 O ATOM 937 N PRO A 122 -3.756 -11.915 12.366 1.00 35.21 N ANISOU 937 N PRO A 122 4239 4816 4323 1112 -312 -1088 N ATOM 938 CA PRO A 122 -3.938 -10.757 13.250 1.00 31.78 C ANISOU 938 CA PRO A 122 3778 4379 3919 1003 -252 -984 C ATOM 939 C PRO A 122 -2.735 -9.827 13.218 1.00 34.94 C ANISOU 939 C PRO A 122 3995 4923 4358 1003 -172 -1051 C ATOM 940 O PRO A 122 -1.583 -10.262 13.260 1.00 35.95 O ANISOU 940 O PRO A 122 4034 5109 4516 1116 -225 -1187 O ATOM 941 CB PRO A 122 -4.125 -11.394 14.633 1.00 34.12 C ANISOU 941 CB PRO A 122 4204 4523 4236 1037 -392 -958 C ATOM 942 CG PRO A 122 -4.635 -12.767 14.343 1.00 35.17 C ANISOU 942 CG PRO A 122 4478 4545 4339 1104 -504 -979 C ATOM 943 CD PRO A 122 -3.947 -13.189 13.077 1.00 33.43 C ANISOU 943 CD PRO A 122 4164 4428 4108 1200 -483 -1112 C ATOM 944 N SER A 123 -3.019 -8.530 13.144 1.00 35.95 N ANISOU 944 N SER A 123 4062 5104 4492 874 -51 -958 N ATOM 945 CA SER A 123 -2.009 -7.483 13.051 1.00 38.29 C ANISOU 945 CA SER A 123 4190 5533 4828 834 41 -996 C ATOM 946 C SER A 123 -1.870 -6.661 14.318 1.00 38.63 C ANISOU 946 C SER A 123 4219 5528 4929 781 25 -951 C ATOM 947 O SER A 123 -0.751 -6.302 14.695 1.00 35.98 O ANISOU 947 O SER A 123 3760 5265 4645 807 22 -1034 O ATOM 948 CB SER A 123 -2.337 -6.544 11.884 1.00 39.60 C ANISOU 948 CB SER A 123 4294 5797 4954 719 191 -925 C ATOM 949 OG SER A 123 -1.236 -5.709 11.570 1.00 45.94 O ANISOU 949 OG SER A 123 4927 6743 5783 680 282 -978 O ATOM 950 N GLY A 124 -2.978 -6.354 14.978 1.00 26.13 N ANISOU 950 N GLY A 124 2754 3832 3341 707 15 -832 N ATOM 951 CA GLY A 124 -2.931 -5.525 16.164 1.00 26.65 C ANISOU 951 CA GLY A 124 2814 3858 3454 653 6 -795 C ATOM 952 C GLY A 124 -4.306 -5.426 16.782 1.00 26.44 C ANISOU 952 C GLY A 124 2928 3714 3404 585 -6 -678 C ATOM 953 O GLY A 124 -5.305 -5.888 16.221 1.00 26.20 O ANISOU 953 O GLY A 124 2985 3640 3329 566 3 -619 O ATOM 954 N VAL A 125 -4.342 -4.811 17.961 1.00 29.32 N ANISOU 954 N VAL A 125 3306 4037 3798 547 -26 -654 N ATOM 955 CA VAL A 125 -5.551 -4.708 18.767 1.00 28.66 C ANISOU 955 CA VAL A 125 3342 3857 3690 487 -38 -564 C ATOM 956 C VAL A 125 -5.688 -3.268 19.241 1.00 29.07 C ANISOU 956 C VAL A 125 3333 3922 3791 396 35 -527 C ATOM 957 O VAL A 125 -4.701 -2.643 19.642 1.00 28.17 O ANISOU 957 O VAL A 125 3126 3854 3726 401 34 -585 O ATOM 958 CB VAL A 125 -5.505 -5.680 19.968 1.00 30.51 C ANISOU 958 CB VAL A 125 3692 4011 3891 548 -166 -584 C ATOM 959 CG1 VAL A 125 -6.779 -5.597 20.775 1.00 32.16 C ANISOU 959 CG1 VAL A 125 4018 4141 4060 471 -162 -493 C ATOM 960 CG2 VAL A 125 -5.264 -7.105 19.501 1.00 33.18 C ANISOU 960 CG2 VAL A 125 4094 4318 4196 647 -258 -631 C ATOM 961 N TYR A 126 -6.909 -2.738 19.194 1.00 26.58 N ANISOU 961 N TYR A 126 3067 3565 3469 318 91 -439 N ATOM 962 CA TYR A 126 -7.147 -1.388 19.685 1.00 28.13 C ANISOU 962 CA TYR A 126 3218 3755 3716 242 147 -411 C ATOM 963 C TYR A 126 -8.623 -1.217 20.005 1.00 26.49 C ANISOU 963 C TYR A 126 3093 3485 3487 187 170 -336 C ATOM 964 O TYR A 126 -9.482 -1.934 19.484 1.00 25.61 O ANISOU 964 O TYR A 126 3048 3350 3333 186 168 -292 O ATOM 965 CB TYR A 126 -6.686 -0.325 18.679 1.00 28.78 C ANISOU 965 CB TYR A 126 3185 3896 3853 191 233 -400 C ATOM 966 CG TYR A 126 -7.265 -0.463 17.289 1.00 30.07 C ANISOU 966 CG TYR A 126 3356 4081 3988 169 288 -341 C ATOM 967 CD1 TYR A 126 -8.494 0.099 16.966 1.00 31.09 C ANISOU 967 CD1 TYR A 126 3526 4165 4121 110 329 -256 C ATOM 968 CD2 TYR A 126 -6.574 -1.142 16.294 1.00 31.37 C ANISOU 968 CD2 TYR A 126 3481 4318 4119 215 294 -381 C ATOM 969 CE1 TYR A 126 -9.022 -0.021 15.694 1.00 31.97 C ANISOU 969 CE1 TYR A 126 3648 4297 4201 92 366 -202 C ATOM 970 CE2 TYR A 126 -7.095 -1.266 15.020 1.00 33.20 C ANISOU 970 CE2 TYR A 126 3726 4578 4312 194 341 -331 C ATOM 971 CZ TYR A 126 -8.318 -0.704 14.725 1.00 32.63 C ANISOU 971 CZ TYR A 126 3703 4454 4240 132 373 -237 C ATOM 972 OH TYR A 126 -8.839 -0.826 13.458 1.00 33.57 O ANISOU 972 OH TYR A 126 3840 4602 4315 114 408 -188 O ATOM 973 N GLN A 127 -8.901 -0.250 20.874 1.00 30.88 N ANISOU 973 N GLN A 127 3636 4019 4079 142 190 -334 N ATOM 974 CA GLN A 127 -10.253 0.018 21.336 1.00 32.24 C ANISOU 974 CA GLN A 127 3865 4146 4237 94 216 -286 C ATOM 975 C GLN A 127 -10.914 1.086 20.475 1.00 34.03 C ANISOU 975 C GLN A 127 4038 4368 4523 42 288 -236 C ATOM 976 O GLN A 127 -10.284 2.079 20.099 1.00 33.07 O ANISOU 976 O GLN A 127 3839 4260 4467 21 319 -242 O ATOM 977 CB GLN A 127 -10.238 0.464 22.797 1.00 33.19 C ANISOU 977 CB GLN A 127 4004 4252 4356 82 194 -326 C ATOM 978 CG GLN A 127 -11.609 0.525 23.436 1.00 38.82 C ANISOU 978 CG GLN A 127 4777 4938 5035 39 219 -295 C ATOM 979 CD GLN A 127 -11.991 -0.761 24.134 1.00 36.37 C ANISOU 979 CD GLN A 127 4580 4615 4624 45 168 -282 C ATOM 980 OE1 GLN A 127 -11.435 -1.823 23.856 1.00 37.80 O ANISOU 980 OE1 GLN A 127 4808 4788 4767 89 108 -280 O ATOM 981 NE2 GLN A 127 -12.942 -0.670 25.056 1.00 36.68 N ANISOU 981 NE2 GLN A 127 4666 4652 4620 -1 190 -275 N ATOM 982 N CYS A 128 -12.193 0.877 20.175 1.00 34.44 N ANISOU 982 N CYS A 128 4135 4396 4555 19 308 -183 N ATOM 983 CA CYS A 128 -12.975 1.803 19.372 1.00 35.77 C ANISOU 983 CA CYS A 128 4266 4549 4776 -19 356 -133 C ATOM 984 C CYS A 128 -14.325 2.035 20.035 1.00 33.74 C ANISOU 984 C CYS A 128 4035 4263 4524 -44 370 -123 C ATOM 985 O CYS A 128 -14.749 1.277 20.910 1.00 32.74 O ANISOU 985 O CYS A 128 3965 4138 4339 -46 351 -141 O ATOM 986 CB CYS A 128 -13.180 1.278 17.945 1.00 36.27 C ANISOU 986 CB CYS A 128 4338 4632 4812 -13 365 -82 C ATOM 987 SG CYS A 128 -11.857 1.699 16.794 1.00 40.35 S ANISOU 987 SG CYS A 128 4783 5201 5346 -13 391 -79 S ATOM 988 N ALA A 129 -14.997 3.098 19.605 1.00 30.44 N ANISOU 988 N ALA A 129 3574 3819 4174 -67 399 -97 N ATOM 989 CA ALA A 129 -16.329 3.433 20.083 1.00 29.94 C ANISOU 989 CA ALA A 129 3510 3737 4130 -83 415 -101 C ATOM 990 C ALA A 129 -17.276 3.572 18.901 1.00 28.77 C ANISOU 990 C ALA A 129 3349 3576 4006 -89 421 -41 C ATOM 991 O ALA A 129 -16.897 4.094 17.848 1.00 31.58 O ANISOU 991 O ALA A 129 3684 3918 4395 -90 420 4 O ATOM 992 CB ALA A 129 -16.319 4.730 20.899 1.00 30.91 C ANISOU 992 CB ALA A 129 3585 3830 4328 -87 428 -153 C ATOM 993 N MET A 130 -18.504 3.092 19.076 1.00 26.97 N ANISOU 993 N MET A 130 3134 3358 3756 -100 425 -39 N ATOM 994 CA MET A 130 -19.550 3.286 18.078 1.00 26.60 C ANISOU 994 CA MET A 130 3066 3300 3740 -102 419 6 C ATOM 995 C MET A 130 -20.056 4.718 18.195 1.00 29.36 C ANISOU 995 C MET A 130 3355 3609 4193 -91 423 -11 C ATOM 996 O MET A 130 -20.773 5.055 19.143 1.00 30.60 O ANISOU 996 O MET A 130 3480 3770 4377 -90 441 -70 O ATOM 997 CB MET A 130 -20.678 2.279 18.277 1.00 27.78 C ANISOU 997 CB MET A 130 3236 3478 3839 -125 419 4 C ATOM 998 CG MET A 130 -21.801 2.392 17.257 1.00 29.17 C ANISOU 998 CG MET A 130 3384 3651 4049 -124 402 42 C ATOM 999 SD MET A 130 -21.248 2.103 15.564 1.00 28.37 S ANISOU 999 SD MET A 130 3317 3544 3920 -108 367 116 S ATOM 1000 CE MET A 130 -20.812 0.367 15.638 1.00 26.86 C ANISOU 1000 CE MET A 130 3204 3381 3620 -120 353 110 C ATOM 1001 N ARG A 131 -19.670 5.566 17.239 1.00 29.31 N ANISOU 1001 N ARG A 131 3335 3560 4240 -83 406 38 N ATOM 1002 CA ARG A 131 -20.038 6.971 17.280 1.00 30.07 C ANISOU 1002 CA ARG A 131 3389 3591 4444 -69 391 29 C ATOM 1003 C ARG A 131 -21.557 7.129 17.227 1.00 33.58 C ANISOU 1003 C ARG A 131 3797 4031 4931 -46 375 12 C ATOM 1004 O ARG A 131 -22.271 6.223 16.788 1.00 30.58 O ANISOU 1004 O ARG A 131 3426 3694 4499 -52 371 34 O ATOM 1005 CB ARG A 131 -19.392 7.726 16.118 1.00 31.94 C ANISOU 1005 CB ARG A 131 3639 3781 4717 -81 368 108 C ATOM 1006 CG ARG A 131 -17.878 7.610 16.046 1.00 33.20 C ANISOU 1006 CG ARG A 131 3813 3962 4840 -111 391 120 C ATOM 1007 CD ARG A 131 -17.215 8.129 17.306 1.00 32.90 C ANISOU 1007 CD ARG A 131 3750 3906 4845 -113 404 42 C ATOM 1008 NE ARG A 131 -17.643 9.486 17.630 1.00 34.15 N ANISOU 1008 NE ARG A 131 3881 3979 5116 -106 380 20 N ATOM 1009 CZ ARG A 131 -17.192 10.180 18.669 1.00 34.79 C ANISOU 1009 CZ ARG A 131 3939 4028 5253 -106 381 -55 C ATOM 1010 NH1 ARG A 131 -16.295 9.643 19.485 1.00 33.78 N ANISOU 1010 NH1 ARG A 131 3812 3952 5073 -115 401 -108 N ATOM 1011 NH2 ARG A 131 -17.635 11.409 18.892 1.00 32.63 N ANISOU 1011 NH2 ARG A 131 3644 3665 5088 -91 349 -82 N ATOM 1012 N PRO A 132 -22.074 8.272 17.687 1.00 28.60 N ANISOU 1012 N PRO A 132 3119 3348 4401 -16 360 -38 N ATOM 1013 CA PRO A 132 -23.520 8.517 17.566 1.00 28.86 C ANISOU 1013 CA PRO A 132 3097 3379 4489 18 337 -66 C ATOM 1014 C PRO A 132 -24.035 8.434 16.139 1.00 29.91 C ANISOU 1014 C PRO A 132 3245 3492 4628 28 283 23 C ATOM 1015 O PRO A 132 -25.208 8.095 15.936 1.00 31.03 O ANISOU 1015 O PRO A 132 3346 3666 4778 45 266 6 O ATOM 1016 CB PRO A 132 -23.681 9.927 18.146 1.00 30.11 C ANISOU 1016 CB PRO A 132 3210 3462 4769 62 314 -134 C ATOM 1017 CG PRO A 132 -22.556 10.055 19.115 1.00 30.16 C ANISOU 1017 CG PRO A 132 3237 3470 4752 38 351 -178 C ATOM 1018 CD PRO A 132 -21.407 9.297 18.510 1.00 28.51 C ANISOU 1018 CD PRO A 132 3092 3285 4456 -9 363 -94 C ATOM 1019 N ASN A 133 -23.201 8.731 15.142 1.00 29.36 N ANISOU 1019 N ASN A 133 3230 3379 4548 12 257 115 N ATOM 1020 CA ASN A 133 -23.586 8.596 13.743 1.00 28.45 C ANISOU 1020 CA ASN A 133 3145 3256 4411 15 206 206 C ATOM 1021 C ASN A 133 -23.240 7.223 13.171 1.00 27.25 C ANISOU 1021 C ASN A 133 3037 3183 4133 -19 231 244 C ATOM 1022 O ASN A 133 -23.197 7.065 11.945 1.00 27.67 O ANISOU 1022 O ASN A 133 3131 3240 4142 -26 197 323 O ATOM 1023 CB ASN A 133 -22.950 9.710 12.905 1.00 30.24 C ANISOU 1023 CB ASN A 133 3412 3394 4682 7 162 291 C ATOM 1024 CG ASN A 133 -21.446 9.559 12.758 1.00 30.79 C ANISOU 1024 CG ASN A 133 3526 3485 4689 -49 210 332 C ATOM 1025 OD1 ASN A 133 -20.805 8.808 13.492 1.00 28.71 O ANISOU 1025 OD1 ASN A 133 3255 3282 4371 -66 267 279 O ATOM 1026 ND2 ASN A 133 -20.874 10.286 11.805 1.00 29.69 N ANISOU 1026 ND2 ASN A 133 3430 3295 4555 -82 184 426 N ATOM 1027 N PHE A 134 -22.980 6.240 14.036 1.00 30.60 N ANISOU 1027 N PHE A 134 3463 3668 4497 -39 283 189 N ATOM 1028 CA PHE A 134 -22.812 4.838 13.649 1.00 29.44 C ANISOU 1028 CA PHE A 134 3358 3584 4243 -62 294 206 C ATOM 1029 C PHE A 134 -21.610 4.622 12.733 1.00 28.73 C ANISOU 1029 C PHE A 134 3321 3506 4087 -75 298 265 C ATOM 1030 O PHE A 134 -21.637 3.768 11.844 1.00 29.43 O ANISOU 1030 O PHE A 134 3448 3633 4101 -79 282 298 O ATOM 1031 CB PHE A 134 -24.085 4.286 13.005 1.00 27.75 C ANISOU 1031 CB PHE A 134 3132 3393 4019 -57 255 218 C ATOM 1032 CG PHE A 134 -25.211 4.085 13.976 1.00 31.18 C ANISOU 1032 CG PHE A 134 3505 3852 4489 -61 270 146 C ATOM 1033 CD1 PHE A 134 -25.239 2.975 14.803 1.00 29.91 C ANISOU 1033 CD1 PHE A 134 3361 3739 4263 -101 311 106 C ATOM 1034 CD2 PHE A 134 -26.237 5.011 14.070 1.00 33.28 C ANISOU 1034 CD2 PHE A 134 3697 4094 4854 -26 243 114 C ATOM 1035 CE1 PHE A 134 -26.273 2.788 15.702 1.00 32.71 C ANISOU 1035 CE1 PHE A 134 3659 4133 4638 -123 338 43 C ATOM 1036 CE2 PHE A 134 -27.273 4.830 14.966 1.00 32.82 C ANISOU 1036 CE2 PHE A 134 3566 4080 4826 -34 270 34 C ATOM 1037 CZ PHE A 134 -27.291 3.717 15.783 1.00 34.55 C ANISOU 1037 CZ PHE A 134 3801 4361 4967 -91 324 2 C ATOM 1038 N THR A 135 -20.549 5.392 12.942 1.00 27.18 N ANISOU 1038 N THR A 135 3124 3285 3919 -84 320 272 N ATOM 1039 CA THR A 135 -19.252 5.133 12.339 1.00 26.41 C ANISOU 1039 CA THR A 135 3056 3222 3758 -105 343 303 C ATOM 1040 C THR A 135 -18.249 4.847 13.448 1.00 24.08 C ANISOU 1040 C THR A 135 2748 2946 3454 -108 380 237 C ATOM 1041 O THR A 135 -18.563 4.940 14.637 1.00 26.67 O ANISOU 1041 O THR A 135 3057 3256 3819 -99 386 178 O ATOM 1042 CB THR A 135 -18.782 6.315 11.480 1.00 27.19 C ANISOU 1042 CB THR A 135 3158 3282 3891 -131 335 378 C ATOM 1043 OG1 THR A 135 -18.692 7.494 12.291 1.00 26.85 O ANISOU 1043 OG1 THR A 135 3084 3166 3953 -135 333 356 O ATOM 1044 CG2 THR A 135 -19.752 6.563 10.335 1.00 28.51 C ANISOU 1044 CG2 THR A 135 3350 3428 4052 -123 283 451 C ATOM 1045 N ILE A 136 -17.032 4.473 13.055 1.00 26.81 N ANISOU 1045 N ILE A 136 3103 3337 3746 -118 402 241 N ATOM 1046 CA ILE A 136 -15.943 4.268 14.001 1.00 28.54 C ANISOU 1046 CA ILE A 136 3304 3576 3963 -114 424 178 C ATOM 1047 C ILE A 136 -14.670 4.861 13.416 1.00 29.91 C ANISOU 1047 C ILE A 136 3449 3774 4141 -145 452 200 C ATOM 1048 O ILE A 136 -14.504 4.947 12.195 1.00 30.11 O ANISOU 1048 O ILE A 136 3484 3830 4129 -167 463 260 O ATOM 1049 CB ILE A 136 -15.726 2.776 14.361 1.00 29.32 C ANISOU 1049 CB ILE A 136 3438 3721 3982 -83 413 130 C ATOM 1050 CG1 ILE A 136 -15.240 1.985 13.146 1.00 26.70 C ANISOU 1050 CG1 ILE A 136 3126 3446 3574 -72 413 149 C ATOM 1051 CG2 ILE A 136 -16.991 2.157 14.947 1.00 26.92 C ANISOU 1051 CG2 ILE A 136 3165 3397 3668 -77 392 116 C ATOM 1052 CD1 ILE A 136 -14.828 0.568 13.476 1.00 30.25 C ANISOU 1052 CD1 ILE A 136 3612 3924 3957 -31 389 93 C ATOM 1053 N LYS A 137 -13.771 5.278 14.301 1.00 35.17 N ANISOU 1053 N LYS A 137 4079 4436 4850 -154 465 149 N ATOM 1054 CA LYS A 137 -12.474 5.834 13.926 1.00 36.05 C ANISOU 1054 CA LYS A 137 4144 4578 4974 -195 496 154 C ATOM 1055 C LYS A 137 -11.419 4.776 14.241 1.00 36.09 C ANISOU 1055 C LYS A 137 4128 4662 4923 -160 501 80 C ATOM 1056 O LYS A 137 -10.890 4.715 15.352 1.00 37.89 O ANISOU 1056 O LYS A 137 4334 4884 5177 -141 486 10 O ATOM 1057 CB LYS A 137 -12.200 7.143 14.664 1.00 37.87 C ANISOU 1057 CB LYS A 137 4340 4740 5308 -233 494 142 C ATOM 1058 CG LYS A 137 -13.279 8.198 14.477 1.00 38.62 C ANISOU 1058 CG LYS A 137 4458 4739 5475 -248 470 199 C ATOM 1059 CD LYS A 137 -13.013 9.421 15.341 1.00 43.57 C ANISOU 1059 CD LYS A 137 5057 5287 6211 -274 457 165 C ATOM 1060 CE LYS A 137 -12.986 9.060 16.817 1.00 40.19 C ANISOU 1060 CE LYS A 137 4613 4865 5790 -230 446 58 C ATOM 1061 NZ LYS A 137 -12.893 10.265 17.686 1.00 46.48 N ANISOU 1061 NZ LYS A 137 5387 5581 6692 -246 426 11 N ATOM 1062 N GLY A 138 -11.118 3.939 13.252 1.00 36.82 N ANISOU 1062 N GLY A 138 4228 4827 4936 -144 515 89 N ATOM 1063 CA GLY A 138 -10.148 2.879 13.439 1.00 37.89 C ANISOU 1063 CA GLY A 138 4341 5033 5021 -93 508 9 C ATOM 1064 C GLY A 138 -8.965 2.975 12.498 1.00 38.67 C ANISOU 1064 C GLY A 138 4373 5229 5091 -118 558 -1 C ATOM 1065 O GLY A 138 -8.652 4.055 11.988 1.00 40.02 O ANISOU 1065 O GLY A 138 4505 5407 5292 -195 603 53 O ATOM 1066 N SER A 139 -8.296 1.847 12.266 1.00 35.65 N ANISOU 1066 N SER A 139 3975 4922 4648 -56 549 -74 N ATOM 1067 CA SER A 139 -7.152 1.770 11.359 1.00 36.58 C ANISOU 1067 CA SER A 139 4014 5159 4726 -69 603 -108 C ATOM 1068 C SER A 139 -7.345 0.531 10.490 1.00 36.90 C ANISOU 1068 C SER A 139 4094 5254 4671 -2 591 -139 C ATOM 1069 O SER A 139 -7.043 -0.587 10.918 1.00 38.64 O ANISOU 1069 O SER A 139 4326 5482 4875 88 537 -227 O ATOM 1070 CB SER A 139 -5.836 1.715 12.128 1.00 38.42 C ANISOU 1070 CB SER A 139 4154 5440 5003 -44 598 -209 C ATOM 1071 OG SER A 139 -4.765 1.346 11.278 1.00 39.85 O ANISOU 1071 OG SER A 139 4249 5756 5138 -34 646 -271 O ATOM 1072 N PHE A 140 -7.845 0.732 9.273 1.00 40.61 N ANISOU 1072 N PHE A 140 4592 5757 5079 -45 629 -67 N ATOM 1073 CA PHE A 140 -8.206 -0.363 8.378 1.00 40.83 C ANISOU 1073 CA PHE A 140 4670 5830 5014 12 612 -91 C ATOM 1074 C PHE A 140 -7.598 -0.104 7.006 1.00 44.22 C ANISOU 1074 C PHE A 140 5051 6391 5361 -35 692 -79 C ATOM 1075 O PHE A 140 -8.041 0.798 6.288 1.00 46.13 O ANISOU 1075 O PHE A 140 5316 6631 5580 -121 731 29 O ATOM 1076 CB PHE A 140 -9.726 -0.507 8.284 1.00 38.41 C ANISOU 1076 CB PHE A 140 4467 5428 4700 10 563 -15 C ATOM 1077 CG PHE A 140 -10.377 -0.930 9.571 1.00 37.69 C ANISOU 1077 CG PHE A 140 4425 5229 4668 49 493 -34 C ATOM 1078 CD1 PHE A 140 -10.330 -2.251 9.987 1.00 36.84 C ANISOU 1078 CD1 PHE A 140 4358 5104 4535 129 431 -112 C ATOM 1079 CD2 PHE A 140 -11.040 -0.007 10.363 1.00 36.56 C ANISOU 1079 CD2 PHE A 140 4290 5000 4599 2 488 24 C ATOM 1080 CE1 PHE A 140 -10.930 -2.642 11.170 1.00 37.28 C ANISOU 1080 CE1 PHE A 140 4469 5066 4630 147 372 -116 C ATOM 1081 CE2 PHE A 140 -11.643 -0.392 11.546 1.00 35.73 C ANISOU 1081 CE2 PHE A 140 4227 4815 4531 29 437 4 C ATOM 1082 CZ PHE A 140 -11.588 -1.711 11.950 1.00 34.78 C ANISOU 1082 CZ PHE A 140 4154 4685 4375 93 382 -59 C ATOM 1083 N LEU A 141 -6.592 -0.894 6.639 1.00 42.33 N ANISOU 1083 N LEU A 141 4748 6266 5071 23 714 -191 N ATOM 1084 CA LEU A 141 -5.968 -0.792 5.330 1.00 44.02 C ANISOU 1084 CA LEU A 141 4909 6632 5186 -17 800 -200 C ATOM 1085 C LEU A 141 -6.671 -1.719 4.340 1.00 44.27 C ANISOU 1085 C LEU A 141 5020 6688 5110 36 773 -212 C ATOM 1086 O LEU A 141 -7.681 -2.356 4.649 1.00 39.23 O ANISOU 1086 O LEU A 141 4478 5943 4486 90 688 -200 O ATOM 1087 CB LEU A 141 -4.481 -1.135 5.409 1.00 45.19 C ANISOU 1087 CB LEU A 141 4923 6911 5335 22 844 -336 C ATOM 1088 CG LEU A 141 -3.476 -0.120 5.944 1.00 51.63 C ANISOU 1088 CG LEU A 141 5623 7766 6228 -58 903 -337 C ATOM 1089 CD1 LEU A 141 -2.430 -0.850 6.761 1.00 51.92 C ANISOU 1089 CD1 LEU A 141 5563 7842 6320 46 864 -494 C ATOM 1090 CD2 LEU A 141 -2.826 0.635 4.799 1.00 51.45 C ANISOU 1090 CD2 LEU A 141 5525 7895 6129 -176 1027 -296 C ATOM 1091 N ASN A 142 -6.126 -1.793 3.128 1.00 46.35 N ANISOU 1091 N ASN A 142 5244 7105 5263 13 849 -238 N ATOM 1092 CA ASN A 142 -6.597 -2.761 2.147 1.00 45.15 C ANISOU 1092 CA ASN A 142 5155 7000 4999 74 824 -281 C ATOM 1093 C ASN A 142 -6.254 -4.169 2.619 1.00 45.31 C ANISOU 1093 C ASN A 142 5168 7006 5040 220 749 -441 C ATOM 1094 O ASN A 142 -5.078 -4.499 2.809 1.00 44.16 O ANISOU 1094 O ASN A 142 4917 6953 4908 274 777 -565 O ATOM 1095 CB ASN A 142 -5.973 -2.481 0.782 1.00 47.19 C ANISOU 1095 CB ASN A 142 5364 7446 5121 13 932 -285 C ATOM 1096 CG ASN A 142 -6.799 -1.519 -0.049 1.00 48.61 C ANISOU 1096 CG ASN A 142 5625 7613 5233 -105 959 -115 C ATOM 1097 OD1 ASN A 142 -8.020 -1.649 -0.139 1.00 46.75 O ANISOU 1097 OD1 ASN A 142 5499 7267 4997 -91 880 -44 O ATOM 1098 ND2 ASN A 142 -6.136 -0.546 -0.662 1.00 52.96 N ANISOU 1098 ND2 ASN A 142 6122 8275 5728 -225 1066 -49 N ATOM 1099 N GLY A 143 -7.279 -4.995 2.817 1.00 39.51 N ANISOU 1099 N GLY A 143 4545 6153 4314 281 648 -439 N ATOM 1100 CA GLY A 143 -7.108 -6.332 3.349 1.00 41.98 C ANISOU 1100 CA GLY A 143 4883 6412 4657 411 553 -569 C ATOM 1101 C GLY A 143 -7.576 -6.504 4.776 1.00 38.81 C ANISOU 1101 C GLY A 143 4534 5843 4367 432 464 -540 C ATOM 1102 O GLY A 143 -7.458 -7.610 5.318 1.00 39.14 O ANISOU 1102 O GLY A 143 4615 5819 4438 531 372 -632 O ATOM 1103 N SER A 144 -8.103 -5.452 5.402 1.00 36.06 N ANISOU 1103 N SER A 144 4195 5425 4081 341 485 -418 N ATOM 1104 CA SER A 144 -8.577 -5.508 6.778 1.00 34.98 C ANISOU 1104 CA SER A 144 4106 5147 4037 348 415 -388 C ATOM 1105 C SER A 144 -10.066 -5.792 6.890 1.00 31.14 C ANISOU 1105 C SER A 144 3733 4546 3554 324 354 -309 C ATOM 1106 O SER A 144 -10.543 -6.066 7.997 1.00 28.83 O ANISOU 1106 O SER A 144 3491 4143 3320 331 293 -295 O ATOM 1107 CB SER A 144 -8.268 -4.193 7.497 1.00 35.70 C ANISOU 1107 CB SER A 144 4132 5230 4202 269 470 -322 C ATOM 1108 OG SER A 144 -8.915 -3.116 6.847 1.00 41.06 O ANISOU 1108 OG SER A 144 4820 5918 4865 170 527 -203 O ATOM 1109 N CYS A 145 -10.809 -5.715 5.788 1.00 29.33 N ANISOU 1109 N CYS A 145 3541 4345 3257 290 369 -259 N ATOM 1110 CA CYS A 145 -12.222 -6.062 5.821 1.00 25.98 C ANISOU 1110 CA CYS A 145 3210 3823 2838 270 305 -199 C ATOM 1111 C CYS A 145 -12.396 -7.498 6.295 1.00 27.37 C ANISOU 1111 C CYS A 145 3458 3921 3019 343 209 -279 C ATOM 1112 O CYS A 145 -11.652 -8.398 5.894 1.00 28.20 O ANISOU 1112 O CYS A 145 3563 4069 3084 424 183 -386 O ATOM 1113 CB CYS A 145 -12.847 -5.874 4.440 1.00 27.58 C ANISOU 1113 CB CYS A 145 3438 4084 2957 237 323 -153 C ATOM 1114 SG CYS A 145 -12.818 -4.167 3.853 1.00 30.00 S ANISOU 1114 SG CYS A 145 3693 4453 3254 137 414 -31 S ATOM 1115 N GLY A 146 -13.380 -7.708 7.164 1.00 25.25 N ANISOU 1115 N GLY A 146 3253 3539 2802 313 155 -230 N ATOM 1116 CA GLY A 146 -13.578 -8.976 7.820 1.00 24.63 C ANISOU 1116 CA GLY A 146 3257 3366 2738 358 61 -281 C ATOM 1117 C GLY A 146 -13.079 -9.022 9.249 1.00 24.10 C ANISOU 1117 C GLY A 146 3192 3237 2729 372 37 -293 C ATOM 1118 O GLY A 146 -13.486 -9.914 10.003 1.00 25.46 O ANISOU 1118 O GLY A 146 3450 3309 2915 379 -43 -298 O ATOM 1119 N SER A 147 -12.202 -8.097 9.635 1.00 27.19 N ANISOU 1119 N SER A 147 3496 3685 3150 370 99 -295 N ATOM 1120 CA SER A 147 -11.808 -7.982 11.032 1.00 27.90 C ANISOU 1120 CA SER A 147 3587 3722 3293 375 75 -299 C ATOM 1121 C SER A 147 -13.018 -7.618 11.883 1.00 25.36 C ANISOU 1121 C SER A 147 3313 3321 3001 292 74 -210 C ATOM 1122 O SER A 147 -13.907 -6.879 11.453 1.00 26.20 O ANISOU 1122 O SER A 147 3401 3440 3115 227 122 -141 O ATOM 1123 CB SER A 147 -10.707 -6.934 11.195 1.00 28.71 C ANISOU 1123 CB SER A 147 3576 3905 3426 374 145 -318 C ATOM 1124 OG SER A 147 -9.782 -6.996 10.124 1.00 30.29 O ANISOU 1124 OG SER A 147 3707 4214 3589 419 183 -385 O ATOM 1125 N VAL A 148 -13.049 -8.146 13.103 1.00 25.71 N ANISOU 1125 N VAL A 148 3420 3289 3060 297 16 -216 N ATOM 1126 CA VAL A 148 -14.243 -8.081 13.932 1.00 25.06 C ANISOU 1126 CA VAL A 148 3392 3140 2989 218 11 -146 C ATOM 1127 C VAL A 148 -13.970 -7.265 15.187 1.00 24.36 C ANISOU 1127 C VAL A 148 3272 3048 2934 192 40 -133 C ATOM 1128 O VAL A 148 -12.832 -7.155 15.655 1.00 23.73 O ANISOU 1128 O VAL A 148 3163 2988 2867 244 26 -183 O ATOM 1129 CB VAL A 148 -14.752 -9.491 14.305 1.00 23.52 C ANISOU 1129 CB VAL A 148 3322 2852 2763 219 -82 -149 C ATOM 1130 CG1 VAL A 148 -15.161 -10.252 13.054 1.00 27.27 C ANISOU 1130 CG1 VAL A 148 3829 3323 3208 237 -115 -167 C ATOM 1131 CG2 VAL A 148 -13.689 -10.254 15.078 1.00 26.56 C ANISOU 1131 CG2 VAL A 148 3760 3193 3140 293 -164 -207 C ATOM 1132 N GLY A 149 -15.039 -6.680 15.725 1.00 23.88 N ANISOU 1132 N GLY A 149 3212 2970 2891 114 79 -74 N ATOM 1133 CA GLY A 149 -15.010 -6.018 17.015 1.00 21.63 C ANISOU 1133 CA GLY A 149 2914 2678 2627 83 101 -67 C ATOM 1134 C GLY A 149 -15.733 -6.873 18.038 1.00 23.18 C ANISOU 1134 C GLY A 149 3212 2814 2783 37 57 -44 C ATOM 1135 O GLY A 149 -16.674 -7.596 17.704 1.00 23.72 O ANISOU 1135 O GLY A 149 3334 2850 2827 -4 37 -13 O ATOM 1136 N PHE A 150 -15.293 -6.791 19.292 1.00 22.26 N ANISOU 1136 N PHE A 150 3122 2684 2651 36 39 -58 N ATOM 1137 CA PHE A 150 -15.801 -7.711 20.299 1.00 24.69 C ANISOU 1137 CA PHE A 150 3546 2936 2900 -11 -11 -30 C ATOM 1138 C PHE A 150 -15.620 -7.128 21.692 1.00 27.29 C ANISOU 1138 C PHE A 150 3878 3281 3211 -38 7 -36 C ATOM 1139 O PHE A 150 -14.774 -6.260 21.924 1.00 27.33 O ANISOU 1139 O PHE A 150 3810 3322 3251 6 26 -78 O ATOM 1140 CB PHE A 150 -15.101 -9.072 20.206 1.00 23.56 C ANISOU 1140 CB PHE A 150 3507 2726 2720 50 -123 -50 C ATOM 1141 CG PHE A 150 -13.624 -9.014 20.488 1.00 24.09 C ANISOU 1141 CG PHE A 150 3553 2801 2798 149 -175 -114 C ATOM 1142 CD1 PHE A 150 -12.726 -8.694 19.483 1.00 24.95 C ANISOU 1142 CD1 PHE A 150 3568 2962 2952 229 -161 -171 C ATOM 1143 CD2 PHE A 150 -13.135 -9.279 21.757 1.00 30.06 C ANISOU 1143 CD2 PHE A 150 4381 3525 3516 158 -237 -118 C ATOM 1144 CE1 PHE A 150 -11.368 -8.637 19.738 1.00 27.04 C ANISOU 1144 CE1 PHE A 150 3792 3248 3234 316 -205 -241 C ATOM 1145 CE2 PHE A 150 -11.779 -9.223 22.019 1.00 29.42 C ANISOU 1145 CE2 PHE A 150 4269 3456 3452 254 -295 -186 C ATOM 1146 CZ PHE A 150 -10.895 -8.903 21.008 1.00 27.97 C ANISOU 1146 CZ PHE A 150 3975 3328 3325 334 -277 -252 C ATOM 1147 N ASN A 151 -16.440 -7.626 22.614 1.00 31.11 N ANISOU 1147 N ASN A 151 4448 3741 3633 -118 1 4 N ATOM 1148 CA ASN A 151 -16.273 -7.436 24.046 1.00 30.35 C ANISOU 1148 CA ASN A 151 4396 3653 3482 -148 -3 1 C ATOM 1149 C ASN A 151 -16.185 -8.803 24.713 1.00 32.29 C ANISOU 1149 C ASN A 151 4805 3825 3641 -170 -102 40 C ATOM 1150 O ASN A 151 -16.664 -9.807 24.178 1.00 31.79 O ANISOU 1150 O ASN A 151 4815 3703 3562 -196 -145 78 O ATOM 1151 CB ASN A 151 -17.431 -6.630 24.652 1.00 32.18 C ANISOU 1151 CB ASN A 151 4578 3943 3707 -241 98 14 C ATOM 1152 CG ASN A 151 -17.338 -5.148 24.346 1.00 32.20 C ANISOU 1152 CG ASN A 151 4438 4002 3795 -209 174 -32 C ATOM 1153 OD1 ASN A 151 -16.544 -4.426 24.948 1.00 33.60 O ANISOU 1153 OD1 ASN A 151 4582 4199 3986 -171 173 -77 O ATOM 1154 ND2 ASN A 151 -18.160 -4.685 23.412 1.00 31.76 N ANISOU 1154 ND2 ASN A 151 4302 3965 3800 -226 229 -20 N ATOM 1155 N ILE A 152 -15.563 -8.842 25.886 1.00 33.61 N ANISOU 1155 N ILE A 152 5036 3985 3749 -160 -150 32 N ATOM 1156 CA ILE A 152 -15.401 -10.073 26.652 1.00 35.46 C ANISOU 1156 CA ILE A 152 5443 4139 3891 -181 -260 78 C ATOM 1157 C ILE A 152 -16.223 -9.919 27.928 1.00 41.77 C ANISOU 1157 C ILE A 152 6303 4977 4592 -303 -207 123 C ATOM 1158 O ILE A 152 -15.836 -9.184 28.843 1.00 40.45 O ANISOU 1158 O ILE A 152 6112 4863 4393 -295 -186 90 O ATOM 1159 CB ILE A 152 -13.928 -10.371 26.955 1.00 32.90 C ANISOU 1159 CB ILE A 152 5158 3775 3568 -59 -381 30 C ATOM 1160 CG1 ILE A 152 -13.151 -10.581 25.653 1.00 33.37 C ANISOU 1160 CG1 ILE A 152 5146 3815 3718 57 -421 -27 C ATOM 1161 CG2 ILE A 152 -13.804 -11.596 27.849 1.00 42.11 C ANISOU 1161 CG2 ILE A 152 6520 4845 4634 -81 -511 87 C ATOM 1162 CD1 ILE A 152 -11.705 -10.974 25.858 1.00 36.62 C ANISOU 1162 CD1 ILE A 152 5579 4192 4142 187 -547 -90 C ATOM 1163 N ASP A 153 -17.403 -10.542 27.943 1.00 53.37 N ANISOU 1163 N ASP A 153 7835 6430 6013 -423 -174 191 N ATOM 1164 CA ASP A 153 -18.326 -10.433 29.104 1.00 57.10 C ANISOU 1164 CA ASP A 153 8354 6961 6381 -561 -102 234 C ATOM 1165 C ASP A 153 -18.145 -11.645 30.021 1.00 59.67 C ANISOU 1165 C ASP A 153 8888 7203 6580 -621 -211 313 C ATOM 1166 O ASP A 153 -18.470 -12.764 29.594 1.00 61.11 O ANISOU 1166 O ASP A 153 9176 7291 6752 -664 -279 375 O ATOM 1167 CB ASP A 153 -19.774 -10.242 28.647 1.00 57.24 C ANISOU 1167 CB ASP A 153 8290 7035 6423 -672 15 253 C ATOM 1168 CG ASP A 153 -19.998 -8.928 27.920 1.00 58.44 C ANISOU 1168 CG ASP A 153 8248 7267 6689 -615 115 180 C ATOM 1169 OD1 ASP A 153 -19.317 -7.948 28.270 1.00 57.61 O ANISOU 1169 OD1 ASP A 153 8073 7205 6610 -543 134 120 O ATOM 1170 OD2 ASP A 153 -20.849 -8.896 27.013 1.00 57.83 O ANISOU 1170 OD2 ASP A 153 8096 7202 6674 -645 162 186 O ATOM 1171 N TYR A 154 -17.657 -11.411 31.240 1.00 67.45 N ANISOU 1171 N TYR A 154 9938 8218 7471 -625 -235 310 N ATOM 1172 CA TYR A 154 -17.417 -12.508 32.212 1.00 73.06 C ANISOU 1172 CA TYR A 154 10867 8848 8046 -680 -353 394 C ATOM 1173 C TYR A 154 -16.562 -13.586 31.528 1.00 73.16 C ANISOU 1173 C TYR A 154 10980 8708 8110 -573 -523 409 C ATOM 1174 O TYR A 154 -15.332 -13.429 31.500 1.00 74.84 O ANISOU 1174 O TYR A 154 11176 8894 8366 -426 -618 347 O ATOM 1175 CB TYR A 154 -18.739 -12.968 32.843 1.00 72.28 C ANISOU 1175 CB TYR A 154 10851 8782 7829 -881 -274 485 C ATOM 1176 CG TYR A 154 -18.630 -14.126 33.805 1.00 74.84 C ANISOU 1176 CG TYR A 154 11417 9016 8002 -969 -390 594 C ATOM 1177 CD1 TYR A 154 -19.595 -15.118 33.838 1.00 76.70 C ANISOU 1177 CD1 TYR A 154 11772 9198 8171 -1133 -387 701 C ATOM 1178 CD2 TYR A 154 -17.528 -14.266 34.631 1.00 75.04 C ANISOU 1178 CD2 TYR A 154 11558 8998 7956 -888 -518 595 C ATOM 1179 CE1 TYR A 154 -19.487 -16.202 34.692 1.00 77.71 C ANISOU 1179 CE1 TYR A 154 12141 9226 8159 -1224 -504 816 C ATOM 1180 CE2 TYR A 154 -17.405 -15.343 35.492 1.00 75.48 C ANISOU 1180 CE2 TYR A 154 11852 8956 7870 -963 -644 705 C ATOM 1181 CZ TYR A 154 -18.387 -16.315 35.521 1.00 76.03 C ANISOU 1181 CZ TYR A 154 12052 8966 7870 -1135 -637 822 C ATOM 1182 OH TYR A 154 -18.272 -17.378 36.367 1.00 79.87 O ANISOU 1182 OH TYR A 154 12790 9343 8213 -1222 -768 944 O ATOM 1183 N ASP A 155 -17.197 -14.610 30.951 1.00 55.45 N ANISOU 1183 N ASP A 155 8823 6373 5873 -641 -560 476 N ATOM 1184 CA ASP A 155 -16.478 -15.723 30.279 1.00 55.95 C ANISOU 1184 CA ASP A 155 8991 6280 5986 -540 -729 481 C ATOM 1185 C ASP A 155 -17.097 -15.915 28.897 1.00 54.13 C ANISOU 1185 C ASP A 155 8672 6033 5861 -542 -682 462 C ATOM 1186 O ASP A 155 -17.238 -17.071 28.463 1.00 54.87 O ANISOU 1186 O ASP A 155 8891 5997 5962 -557 -787 505 O ATOM 1187 CB ASP A 155 -16.652 -17.023 31.064 1.00 58.53 C ANISOU 1187 CB ASP A 155 9567 6474 6196 -635 -859 597 C ATOM 1188 CG ASP A 155 -18.082 -17.537 31.058 1.00 58.81 C ANISOU 1188 CG ASP A 155 9661 6504 6179 -840 -780 693 C ATOM 1189 OD1 ASP A 155 -18.980 -16.786 30.628 1.00 57.68 O ANISOU 1189 OD1 ASP A 155 9355 6482 6078 -908 -615 664 O ATOM 1190 OD2 ASP A 155 -18.287 -18.686 31.488 1.00 62.99 O ANISOU 1190 OD2 ASP A 155 10398 6905 6630 -931 -889 795 O ATOM 1191 N CYS A 156 -17.451 -14.813 28.241 1.00 46.28 N ANISOU 1191 N CYS A 156 7479 5160 4946 -526 -540 399 N ATOM 1192 CA CYS A 156 -18.120 -14.917 26.957 1.00 44.25 C ANISOU 1192 CA CYS A 156 7138 4901 4776 -536 -493 384 C ATOM 1193 C CYS A 156 -17.600 -13.848 26.012 1.00 41.54 C ANISOU 1193 C CYS A 156 6602 4640 4540 -410 -428 287 C ATOM 1194 O CYS A 156 -17.427 -12.688 26.400 1.00 40.69 O ANISOU 1194 O CYS A 156 6382 4635 4443 -393 -339 248 O ATOM 1195 CB CYS A 156 -19.633 -14.776 27.114 1.00 43.46 C ANISOU 1195 CB CYS A 156 7005 4865 4641 -714 -369 439 C ATOM 1196 SG CYS A 156 -20.484 -14.554 25.554 1.00 43.98 S ANISOU 1196 SG CYS A 156 6925 4964 4822 -715 -297 403 S ATOM 1197 N VAL A 157 -17.351 -14.244 24.771 1.00 37.74 N ANISOU 1197 N VAL A 157 6091 4114 4134 -328 -473 249 N ATOM 1198 CA VAL A 157 -16.902 -13.323 23.735 1.00 34.07 C ANISOU 1198 CA VAL A 157 5457 3727 3761 -225 -410 170 C ATOM 1199 C VAL A 157 -18.128 -12.814 22.989 1.00 32.18 C ANISOU 1199 C VAL A 157 5115 3552 3560 -308 -296 186 C ATOM 1200 O VAL A 157 -18.827 -13.585 22.324 1.00 32.14 O ANISOU 1200 O VAL A 157 5154 3496 3562 -356 -323 211 O ATOM 1201 CB VAL A 157 -15.913 -14.000 22.777 1.00 32.91 C ANISOU 1201 CB VAL A 157 5326 3516 3663 -86 -516 109 C ATOM 1202 CG1 VAL A 157 -15.580 -13.068 21.626 1.00 32.26 C ANISOU 1202 CG1 VAL A 157 5073 3527 3659 -9 -435 40 C ATOM 1203 CG2 VAL A 157 -14.654 -14.406 23.524 1.00 33.58 C ANISOU 1203 CG2 VAL A 157 5489 3546 3724 13 -636 78 C ATOM 1204 N SER A 158 -18.387 -11.516 23.093 1.00 29.74 N ANISOU 1204 N SER A 158 4669 3349 3281 -320 -180 164 N ATOM 1205 CA SER A 158 -19.550 -10.898 22.463 1.00 29.59 C ANISOU 1205 CA SER A 158 4541 3395 3305 -387 -79 172 C ATOM 1206 C SER A 158 -19.085 -10.173 21.205 1.00 27.82 C ANISOU 1206 C SER A 158 4197 3210 3162 -287 -55 122 C ATOM 1207 O SER A 158 -18.578 -9.051 21.274 1.00 27.54 O ANISOU 1207 O SER A 158 4064 3235 3166 -238 -1 87 O ATOM 1208 CB SER A 158 -20.250 -9.951 23.431 1.00 29.46 C ANISOU 1208 CB SER A 158 4460 3464 3270 -467 25 179 C ATOM 1209 OG SER A 158 -20.935 -10.673 24.440 1.00 35.18 O ANISOU 1209 OG SER A 158 5290 4172 3906 -590 22 234 O ATOM 1210 N PHE A 159 -19.256 -10.822 20.056 1.00 29.00 N ANISOU 1210 N PHE A 159 4362 3325 3334 -264 -97 119 N ATOM 1211 CA PHE A 159 -18.936 -10.201 18.779 1.00 26.43 C ANISOU 1211 CA PHE A 159 3932 3044 3065 -187 -69 81 C ATOM 1212 C PHE A 159 -19.999 -9.166 18.435 1.00 25.68 C ANISOU 1212 C PHE A 159 3725 3019 3013 -243 25 99 C ATOM 1213 O PHE A 159 -21.198 -9.457 18.485 1.00 27.37 O ANISOU 1213 O PHE A 159 3947 3232 3221 -333 41 130 O ATOM 1214 CB PHE A 159 -18.844 -11.256 17.677 1.00 27.73 C ANISOU 1214 CB PHE A 159 4154 3155 3226 -146 -147 64 C ATOM 1215 CG PHE A 159 -17.730 -12.243 17.873 1.00 26.86 C ANISOU 1215 CG PHE A 159 4143 2972 3090 -64 -253 28 C ATOM 1216 CD1 PHE A 159 -16.419 -11.892 17.597 1.00 24.60 C ANISOU 1216 CD1 PHE A 159 3804 2721 2823 52 -263 -35 C ATOM 1217 CD2 PHE A 159 -17.994 -13.524 18.329 1.00 26.27 C ANISOU 1217 CD2 PHE A 159 4214 2791 2977 -103 -348 55 C ATOM 1218 CE1 PHE A 159 -15.391 -12.798 17.774 1.00 24.53 C ANISOU 1218 CE1 PHE A 159 3872 2648 2800 143 -369 -84 C ATOM 1219 CE2 PHE A 159 -16.971 -14.435 18.508 1.00 26.99 C ANISOU 1219 CE2 PHE A 159 4402 2801 3053 -13 -465 17 C ATOM 1220 CZ PHE A 159 -15.668 -14.072 18.230 1.00 25.92 C ANISOU 1220 CZ PHE A 159 4200 2707 2941 118 -477 -59 C ATOM 1221 N CYS A 160 -19.559 -7.959 18.083 1.00 24.82 N ANISOU 1221 N CYS A 160 3511 2968 2951 -191 80 76 N ATOM 1222 CA CYS A 160 -20.476 -6.854 17.837 1.00 24.64 C ANISOU 1222 CA CYS A 160 3384 2999 2980 -228 155 88 C ATOM 1223 C CYS A 160 -20.276 -6.148 16.506 1.00 23.95 C ANISOU 1223 C CYS A 160 3221 2942 2936 -173 170 85 C ATOM 1224 O CYS A 160 -21.171 -5.401 16.094 1.00 25.33 O ANISOU 1224 O CYS A 160 3326 3146 3154 -199 207 101 O ATOM 1225 CB CYS A 160 -20.366 -5.809 18.958 1.00 24.00 C ANISOU 1225 CB CYS A 160 3251 2952 2917 -240 214 73 C ATOM 1226 SG CYS A 160 -18.707 -5.134 19.181 1.00 25.21 S ANISOU 1226 SG CYS A 160 3379 3111 3087 -153 208 33 S ATOM 1227 N TYR A 161 -19.157 -6.356 15.816 1.00 21.37 N ANISOU 1227 N TYR A 161 2907 2616 2597 -101 141 62 N ATOM 1228 CA TYR A 161 -18.835 -5.553 14.648 1.00 22.42 C ANISOU 1228 CA TYR A 161 2970 2793 2757 -62 168 65 C ATOM 1229 C TYR A 161 -18.006 -6.374 13.671 1.00 24.25 C ANISOU 1229 C TYR A 161 3238 3031 2946 -1 124 34 C ATOM 1230 O TYR A 161 -17.201 -7.211 14.083 1.00 23.84 O ANISOU 1230 O TYR A 161 3241 2952 2866 40 79 -5 O ATOM 1231 CB TYR A 161 -18.076 -4.285 15.061 1.00 22.25 C ANISOU 1231 CB TYR A 161 2876 2799 2779 -44 220 57 C ATOM 1232 CG TYR A 161 -17.643 -3.397 13.917 1.00 23.13 C ANISOU 1232 CG TYR A 161 2926 2951 2913 -21 250 73 C ATOM 1233 CD1 TYR A 161 -18.518 -2.477 13.356 1.00 24.72 C ANISOU 1233 CD1 TYR A 161 3081 3158 3154 -49 274 117 C ATOM 1234 CD2 TYR A 161 -16.352 -3.468 13.409 1.00 23.66 C ANISOU 1234 CD2 TYR A 161 2978 3053 2957 26 252 43 C ATOM 1235 CE1 TYR A 161 -18.123 -1.659 12.314 1.00 23.11 C ANISOU 1235 CE1 TYR A 161 2838 2982 2959 -39 295 147 C ATOM 1236 CE2 TYR A 161 -15.949 -2.655 12.368 1.00 24.84 C ANISOU 1236 CE2 TYR A 161 3076 3249 3114 28 290 67 C ATOM 1237 CZ TYR A 161 -16.838 -1.753 11.823 1.00 25.22 C ANISOU 1237 CZ TYR A 161 3099 3292 3193 -9 309 126 C ATOM 1238 OH TYR A 161 -16.439 -0.941 10.786 1.00 25.21 O ANISOU 1238 OH TYR A 161 3063 3328 3187 -18 339 165 O ATOM 1239 N MET A 162 -18.227 -6.139 12.379 1.00 23.01 N ANISOU 1239 N MET A 162 3052 2910 2781 10 133 48 N ATOM 1240 CA MET A 162 -17.371 -6.661 11.321 1.00 26.47 C ANISOU 1240 CA MET A 162 3501 3382 3172 71 112 9 C ATOM 1241 C MET A 162 -17.170 -5.556 10.296 1.00 25.48 C ANISOU 1241 C MET A 162 3306 3325 3048 70 167 39 C ATOM 1242 O MET A 162 -18.144 -4.959 9.829 1.00 27.94 O ANISOU 1242 O MET A 162 3600 3640 3377 31 177 92 O ATOM 1243 CB MET A 162 -17.969 -7.908 10.658 1.00 27.31 C ANISOU 1243 CB MET A 162 3682 3458 3236 76 44 -10 C ATOM 1244 CG MET A 162 -17.179 -8.395 9.448 1.00 29.17 C ANISOU 1244 CG MET A 162 3923 3743 3416 144 27 -64 C ATOM 1245 SD MET A 162 -17.757 -9.969 8.779 1.00 29.14 S ANISOU 1245 SD MET A 162 4019 3686 3367 162 -71 -109 S ATOM 1246 CE MET A 162 -16.959 -11.127 9.887 1.00 30.20 C ANISOU 1246 CE MET A 162 4233 3733 3509 211 -144 -168 C ATOM 1247 N HIS A 163 -15.914 -5.287 9.952 1.00 24.73 N ANISOU 1247 N HIS A 163 3172 3288 2936 110 199 5 N ATOM 1248 CA HIS A 163 -15.580 -4.130 9.133 1.00 25.09 C ANISOU 1248 CA HIS A 163 3155 3398 2982 90 260 46 C ATOM 1249 C HIS A 163 -15.868 -4.389 7.659 1.00 27.04 C ANISOU 1249 C HIS A 163 3422 3697 3156 95 252 58 C ATOM 1250 O HIS A 163 -15.585 -5.471 7.136 1.00 24.81 O ANISOU 1250 O HIS A 163 3176 3437 2814 142 218 -4 O ATOM 1251 CB HIS A 163 -14.110 -3.760 9.318 1.00 23.87 C ANISOU 1251 CB HIS A 163 2941 3298 2831 115 303 2 C ATOM 1252 CG HIS A 163 -13.680 -2.587 8.497 1.00 27.41 C ANISOU 1252 CG HIS A 163 3329 3810 3273 74 370 51 C ATOM 1253 ND1 HIS A 163 -14.222 -1.331 8.657 1.00 27.31 N ANISOU 1253 ND1 HIS A 163 3296 3762 3319 15 395 130 N ATOM 1254 CD2 HIS A 163 -12.767 -2.481 7.503 1.00 28.06 C ANISOU 1254 CD2 HIS A 163 3374 3991 3297 78 416 32 C ATOM 1255 CE1 HIS A 163 -13.656 -0.499 7.801 1.00 27.62 C ANISOU 1255 CE1 HIS A 163 3299 3861 3336 -22 446 171 C ATOM 1256 NE2 HIS A 163 -12.772 -1.172 7.088 1.00 27.52 N ANISOU 1256 NE2 HIS A 163 3272 3939 3246 8 468 115 N ATOM 1257 N HIS A 164 -16.430 -3.383 6.990 1.00 25.19 N ANISOU 1257 N HIS A 164 3168 3477 2925 51 276 135 N ATOM 1258 CA HIS A 164 -16.806 -3.489 5.584 1.00 24.44 C ANISOU 1258 CA HIS A 164 3099 3434 2753 48 264 161 C ATOM 1259 C HIS A 164 -16.213 -2.405 4.695 1.00 26.22 C ANISOU 1259 C HIS A 164 3292 3731 2940 14 323 219 C ATOM 1260 O HIS A 164 -15.771 -2.706 3.583 1.00 27.83 O ANISOU 1260 O HIS A 164 3507 4021 3046 24 339 203 O ATOM 1261 CB HIS A 164 -18.336 -3.452 5.443 1.00 24.11 C ANISOU 1261 CB HIS A 164 3088 3337 2737 22 208 212 C ATOM 1262 CG HIS A 164 -19.008 -4.760 5.724 1.00 24.69 C ANISOU 1262 CG HIS A 164 3209 3366 2804 39 144 159 C ATOM 1263 ND1 HIS A 164 -19.721 -5.450 4.767 1.00 24.86 N ANISOU 1263 ND1 HIS A 164 3275 3400 2770 44 88 150 N ATOM 1264 CD2 HIS A 164 -19.088 -5.498 6.857 1.00 24.20 C ANISOU 1264 CD2 HIS A 164 3168 3244 2783 42 122 118 C ATOM 1265 CE1 HIS A 164 -20.208 -6.558 5.297 1.00 23.30 C ANISOU 1265 CE1 HIS A 164 3120 3145 2588 46 35 105 C ATOM 1266 NE2 HIS A 164 -19.836 -6.612 6.563 1.00 25.67 N ANISOU 1266 NE2 HIS A 164 3411 3401 2943 42 55 90 N ATOM 1267 N MET A 165 -16.186 -1.151 5.148 1.00 31.70 N ANISOU 1267 N MET A 165 3948 4391 3705 -31 355 284 N ATOM 1268 CA MET A 165 -16.027 -0.029 4.233 1.00 30.21 C ANISOU 1268 CA MET A 165 3753 4238 3486 -83 388 372 C ATOM 1269 C MET A 165 -15.341 1.138 4.927 1.00 32.75 C ANISOU 1269 C MET A 165 4023 4531 3888 -127 438 404 C ATOM 1270 O MET A 165 -15.294 1.218 6.156 1.00 30.96 O ANISOU 1270 O MET A 165 3768 4246 3750 -113 435 366 O ATOM 1271 CB MET A 165 -17.388 0.429 3.703 1.00 33.04 C ANISOU 1271 CB MET A 165 4154 4545 3856 -99 327 452 C ATOM 1272 CG MET A 165 -18.310 0.878 4.827 1.00 35.21 C ANISOU 1272 CG MET A 165 4409 4715 4256 -97 291 461 C ATOM 1273 SD MET A 165 -20.062 0.917 4.418 1.00 45.00 S ANISOU 1273 SD MET A 165 5675 5902 5522 -88 202 504 S ATOM 1274 CE MET A 165 -20.169 -0.436 3.258 1.00 30.97 C ANISOU 1274 CE MET A 165 3952 4202 3612 -64 168 467 C ATOM 1275 N GLU A 166 -14.838 2.066 4.115 1.00 38.07 N ANISOU 1275 N GLU A 166 4693 5247 4526 -186 479 477 N ATOM 1276 CA GLU A 166 -14.268 3.317 4.594 1.00 37.96 C ANISOU 1276 CA GLU A 166 4639 5194 4589 -246 518 525 C ATOM 1277 C GLU A 166 -15.093 4.486 4.072 1.00 39.28 C ANISOU 1277 C GLU A 166 4852 5287 4786 -294 478 647 C ATOM 1278 O GLU A 166 -15.588 4.455 2.940 1.00 37.31 O ANISOU 1278 O GLU A 166 4657 5067 4451 -305 452 710 O ATOM 1279 CB GLU A 166 -12.806 3.474 4.157 1.00 42.22 C ANISOU 1279 CB GLU A 166 5129 5843 5070 -294 603 509 C ATOM 1280 CG GLU A 166 -12.087 4.637 4.827 1.00 43.56 C ANISOU 1280 CG GLU A 166 5247 5970 5334 -360 641 537 C ATOM 1281 CD GLU A 166 -10.852 5.080 4.069 1.00 47.47 C ANISOU 1281 CD GLU A 166 5698 6576 5762 -445 728 561 C ATOM 1282 OE1 GLU A 166 -10.875 6.187 3.490 1.00 48.22 O ANISOU 1282 OE1 GLU A 166 5822 6643 5854 -538 741 676 O ATOM 1283 OE2 GLU A 166 -9.857 4.326 4.056 1.00 48.38 O ANISOU 1283 OE2 GLU A 166 5748 6806 5829 -420 781 463 O ATOM 1284 N LEU A 167 -15.239 5.513 4.903 1.00 39.24 N ANISOU 1284 N LEU A 167 4827 5180 4901 -315 465 674 N ATOM 1285 CA LEU A 167 -16.001 6.707 4.578 1.00 43.41 C ANISOU 1285 CA LEU A 167 5397 5610 5486 -348 411 779 C ATOM 1286 C LEU A 167 -15.090 7.765 3.971 1.00 43.43 C ANISOU 1286 C LEU A 167 5411 5621 5470 -446 454 870 C ATOM 1287 O LEU A 167 -13.873 7.743 4.178 1.00 43.89 O ANISOU 1287 O LEU A 167 5418 5746 5513 -490 531 834 O ATOM 1288 CB LEU A 167 -16.676 7.255 5.836 1.00 41.39 C ANISOU 1288 CB LEU A 167 5113 5235 5378 -312 368 744 C ATOM 1289 CG LEU A 167 -18.044 6.716 6.275 1.00 40.78 C ANISOU 1289 CG LEU A 167 5036 5117 5341 -238 304 699 C ATOM 1290 CD1 LEU A 167 -19.165 7.356 5.469 1.00 43.70 C ANISOU 1290 CD1 LEU A 167 5451 5425 5726 -230 221 784 C ATOM 1291 CD2 LEU A 167 -18.124 5.194 6.202 1.00 38.55 C ANISOU 1291 CD2 LEU A 167 4755 4921 4971 -198 316 628 C ATOM 1292 N PRO A 168 -15.646 8.712 3.207 1.00 43.29 N ANISOU 1292 N PRO A 168 5460 5534 5452 -488 400 992 N ATOM 1293 CA PRO A 168 -14.808 9.801 2.674 1.00 47.61 C ANISOU 1293 CA PRO A 168 6033 6071 5986 -601 436 1096 C ATOM 1294 C PRO A 168 -14.141 10.620 3.760 1.00 47.46 C ANISOU 1294 C PRO A 168 5958 5974 6100 -639 460 1066 C ATOM 1295 O PRO A 168 -13.125 11.272 3.497 1.00 51.22 O ANISOU 1295 O PRO A 168 6425 6472 6563 -745 518 1118 O ATOM 1296 CB PRO A 168 -15.799 10.648 1.864 1.00 49.88 C ANISOU 1296 CB PRO A 168 6418 6258 6275 -615 337 1229 C ATOM 1297 CG PRO A 168 -17.145 10.289 2.403 1.00 49.32 C ANISOU 1297 CG PRO A 168 6340 6113 6284 -500 247 1170 C ATOM 1298 CD PRO A 168 -17.049 8.845 2.782 1.00 42.34 C ANISOU 1298 CD PRO A 168 5400 5341 5347 -437 296 1043 C ATOM 1299 N THR A 169 -14.675 10.594 4.977 1.00 67.71 N ANISOU 1299 N THR A 169 8484 8455 8788 -562 421 980 N ATOM 1300 CA THR A 169 -14.104 11.301 6.113 1.00 67.23 C ANISOU 1300 CA THR A 169 8370 8321 8853 -584 436 930 C ATOM 1301 C THR A 169 -12.820 10.661 6.622 1.00 66.93 C ANISOU 1301 C THR A 169 8250 8397 8784 -604 526 836 C ATOM 1302 O THR A 169 -11.989 11.359 7.213 1.00 69.56 O ANISOU 1302 O THR A 169 8540 8699 9192 -662 553 819 O ATOM 1303 CB THR A 169 -15.149 11.350 7.240 1.00 67.23 C ANISOU 1303 CB THR A 169 8352 8221 8970 -488 369 853 C ATOM 1304 OG1 THR A 169 -16.377 11.880 6.721 1.00 71.20 O ANISOU 1304 OG1 THR A 169 8917 8630 9507 -455 278 925 O ATOM 1305 CG2 THR A 169 -14.687 12.206 8.400 1.00 68.50 C ANISOU 1305 CG2 THR A 169 8471 8294 9262 -505 370 800 C ATOM 1306 N GLY A 170 -12.616 9.374 6.358 1.00 44.14 N ANISOU 1306 N GLY A 170 5342 5638 5792 -556 565 773 N ATOM 1307 CA GLY A 170 -11.579 8.607 7.009 1.00 44.05 C ANISOU 1307 CA GLY A 170 5250 5720 5767 -537 624 660 C ATOM 1308 C GLY A 170 -12.083 7.747 8.145 1.00 40.92 C ANISOU 1308 C GLY A 170 4837 5301 5411 -433 589 551 C ATOM 1309 O GLY A 170 -11.274 7.094 8.816 1.00 42.33 O ANISOU 1309 O GLY A 170 4959 5539 5586 -405 617 455 O ATOM 1310 N VAL A 171 -13.390 7.732 8.381 1.00 34.61 N ANISOU 1310 N VAL A 171 4082 4419 4648 -381 525 565 N ATOM 1311 CA VAL A 171 -13.987 6.896 9.401 1.00 31.39 C ANISOU 1311 CA VAL A 171 3666 3997 4263 -300 497 475 C ATOM 1312 C VAL A 171 -14.536 5.641 8.725 1.00 31.83 C ANISOU 1312 C VAL A 171 3759 4118 4219 -253 483 465 C ATOM 1313 O VAL A 171 -14.629 5.549 7.512 1.00 31.74 O ANISOU 1313 O VAL A 171 3780 4150 4128 -273 486 527 O ATOM 1314 CB VAL A 171 -15.085 7.647 10.196 1.00 32.91 C ANISOU 1314 CB VAL A 171 3867 4072 4564 -276 443 475 C ATOM 1315 CG1 VAL A 171 -14.502 8.880 10.872 1.00 34.50 C ANISOU 1315 CG1 VAL A 171 4038 4200 4869 -319 449 472 C ATOM 1316 CG2 VAL A 171 -16.251 8.025 9.295 1.00 34.19 C ANISOU 1316 CG2 VAL A 171 4078 4186 4726 -270 390 559 C ATOM 1317 N HIS A 172 -14.890 4.651 9.543 1.00 28.97 N ANISOU 1317 N HIS A 172 3395 3759 3854 -194 465 387 N ATOM 1318 CA HIS A 172 -15.200 3.321 9.044 1.00 29.18 C ANISOU 1318 CA HIS A 172 3455 3841 3790 -153 449 359 C ATOM 1319 C HIS A 172 -16.611 2.908 9.438 1.00 30.01 C ANISOU 1319 C HIS A 172 3589 3893 3920 -122 397 353 C ATOM 1320 O HIS A 172 -17.188 3.415 10.405 1.00 27.74 O ANISOU 1320 O HIS A 172 3284 3543 3714 -120 384 338 O ATOM 1321 CB HIS A 172 -14.180 2.307 9.569 1.00 30.57 C ANISOU 1321 CB HIS A 172 3612 4076 3929 -117 468 268 C ATOM 1322 CG HIS A 172 -12.762 2.673 9.262 1.00 31.58 C ANISOU 1322 CG HIS A 172 3686 4273 4041 -146 523 254 C ATOM 1323 ND1 HIS A 172 -11.948 3.323 10.166 1.00 31.21 N ANISOU 1323 ND1 HIS A 172 3585 4209 4064 -166 544 222 N ATOM 1324 CD2 HIS A 172 -12.016 2.493 8.146 1.00 32.68 C ANISOU 1324 CD2 HIS A 172 3810 4509 4099 -163 564 261 C ATOM 1325 CE1 HIS A 172 -10.760 3.520 9.622 1.00 34.76 C ANISOU 1325 CE1 HIS A 172 3981 4742 4485 -199 596 211 C ATOM 1326 NE2 HIS A 172 -10.775 3.026 8.397 1.00 33.59 N ANISOU 1326 NE2 HIS A 172 3853 4668 4241 -199 615 234 N ATOM 1327 N ALA A 173 -17.160 1.970 8.668 1.00 24.72 N ANISOU 1327 N ALA A 173 2958 3256 3177 -101 369 355 N ATOM 1328 CA ALA A 173 -18.509 1.471 8.879 1.00 22.28 C ANISOU 1328 CA ALA A 173 2670 2911 2884 -85 320 349 C ATOM 1329 C ALA A 173 -18.538 -0.030 8.636 1.00 22.75 C ANISOU 1329 C ALA A 173 2771 3010 2865 -59 298 301 C ATOM 1330 O ALA A 173 -17.739 -0.566 7.863 1.00 23.63 O ANISOU 1330 O ALA A 173 2900 3180 2899 -44 310 286 O ATOM 1331 CB ALA A 173 -19.520 2.173 7.963 1.00 23.70 C ANISOU 1331 CB ALA A 173 2860 3067 3078 -96 280 422 C ATOM 1332 N GLY A 174 -19.468 -0.702 9.304 1.00 21.47 N ANISOU 1332 N GLY A 174 2621 2813 2722 -56 267 272 N ATOM 1333 CA GLY A 174 -19.591 -2.135 9.178 1.00 22.17 C ANISOU 1333 CA GLY A 174 2760 2913 2750 -40 233 229 C ATOM 1334 C GLY A 174 -20.929 -2.622 9.687 1.00 21.57 C ANISOU 1334 C GLY A 174 2693 2799 2703 -65 197 224 C ATOM 1335 O GLY A 174 -21.862 -1.843 9.891 1.00 22.19 O ANISOU 1335 O GLY A 174 2729 2859 2843 -85 197 250 O ATOM 1336 N THR A 175 -21.008 -3.932 9.897 1.00 23.03 N ANISOU 1336 N THR A 175 2932 2973 2847 -65 164 185 N ATOM 1337 CA THR A 175 -22.235 -4.600 10.304 1.00 23.31 C ANISOU 1337 CA THR A 175 2982 2978 2897 -108 131 180 C ATOM 1338 C THR A 175 -22.031 -5.310 11.635 1.00 23.35 C ANISOU 1338 C THR A 175 3024 2948 2899 -131 136 150 C ATOM 1339 O THR A 175 -20.911 -5.445 12.134 1.00 20.70 O ANISOU 1339 O THR A 175 2713 2608 2546 -99 147 126 O ATOM 1340 CB THR A 175 -22.687 -5.622 9.252 1.00 24.54 C ANISOU 1340 CB THR A 175 3187 3138 3000 -106 70 171 C ATOM 1341 OG1 THR A 175 -21.788 -6.738 9.257 1.00 23.59 O ANISOU 1341 OG1 THR A 175 3138 3003 2823 -75 44 126 O ATOM 1342 CG2 THR A 175 -22.698 -5.003 7.867 1.00 22.64 C ANISOU 1342 CG2 THR A 175 2928 2941 2733 -80 59 202 C ATOM 1343 N ASP A 176 -23.140 -5.770 12.211 1.00 26.41 N ANISOU 1343 N ASP A 176 3416 3316 3302 -191 125 152 N ATOM 1344 CA ASP A 176 -23.060 -6.754 13.276 1.00 25.28 C ANISOU 1344 CA ASP A 176 3340 3135 3130 -230 112 136 C ATOM 1345 C ASP A 176 -22.780 -8.124 12.660 1.00 26.38 C ANISOU 1345 C ASP A 176 3573 3234 3215 -216 39 119 C ATOM 1346 O ASP A 176 -22.655 -8.271 11.441 1.00 27.70 O ANISOU 1346 O ASP A 176 3743 3418 3364 -175 9 110 O ATOM 1347 CB ASP A 176 -24.338 -6.750 14.117 1.00 26.07 C ANISOU 1347 CB ASP A 176 3409 3240 3257 -317 136 145 C ATOM 1348 CG ASP A 176 -25.602 -6.938 13.288 1.00 30.46 C ANISOU 1348 CG ASP A 176 3927 3812 3836 -356 109 153 C ATOM 1349 OD1 ASP A 176 -25.528 -7.487 12.169 1.00 29.36 O ANISOU 1349 OD1 ASP A 176 3824 3660 3672 -329 52 153 O ATOM 1350 OD2 ASP A 176 -26.683 -6.537 13.768 1.00 30.74 O ANISOU 1350 OD2 ASP A 176 3890 3877 3914 -412 141 151 O ATOM 1351 N LEU A 177 -22.685 -9.148 13.501 1.00 25.96 N ANISOU 1351 N LEU A 177 3605 3127 3134 -250 5 113 N ATOM 1352 CA LEU A 177 -22.373 -10.475 12.988 1.00 25.60 C ANISOU 1352 CA LEU A 177 3659 3022 3047 -229 -79 89 C ATOM 1353 C LEU A 177 -23.581 -11.172 12.375 1.00 28.84 C ANISOU 1353 C LEU A 177 4089 3411 3459 -297 -123 99 C ATOM 1354 O LEU A 177 -23.470 -12.340 11.985 1.00 29.28 O ANISOU 1354 O LEU A 177 4235 3403 3486 -291 -203 75 O ATOM 1355 CB LEU A 177 -21.762 -11.338 14.093 1.00 25.14 C ANISOU 1355 CB LEU A 177 3701 2892 2957 -236 -120 85 C ATOM 1356 CG LEU A 177 -20.231 -11.318 14.130 1.00 25.24 C ANISOU 1356 CG LEU A 177 3730 2903 2955 -127 -139 41 C ATOM 1357 CD1 LEU A 177 -19.658 -11.835 12.819 1.00 29.16 C ANISOU 1357 CD1 LEU A 177 4241 3404 3435 -42 -188 -13 C ATOM 1358 CD2 LEU A 177 -19.703 -9.919 14.428 1.00 27.48 C ANISOU 1358 CD2 LEU A 177 3911 3261 3267 -98 -55 43 C ATOM 1359 N GLU A 178 -24.722 -10.491 12.279 1.00 25.38 N ANISOU 1359 N GLU A 178 3563 3020 3059 -356 -82 123 N ATOM 1360 CA GLU A 178 -25.878 -10.984 11.545 1.00 30.13 C ANISOU 1360 CA GLU A 178 4156 3619 3672 -413 -125 124 C ATOM 1361 C GLU A 178 -26.045 -10.291 10.198 1.00 28.56 C ANISOU 1361 C GLU A 178 3891 3477 3483 -354 -133 117 C ATOM 1362 O GLU A 178 -27.039 -10.531 9.506 1.00 31.33 O ANISOU 1362 O GLU A 178 4219 3838 3847 -392 -174 114 O ATOM 1363 CB GLU A 178 -27.147 -10.823 12.384 1.00 29.97 C ANISOU 1363 CB GLU A 178 4078 3621 3690 -528 -84 147 C ATOM 1364 CG GLU A 178 -27.215 -11.760 13.580 1.00 30.50 C ANISOU 1364 CG GLU A 178 4232 3629 3726 -620 -89 166 C ATOM 1365 CD GLU A 178 -28.512 -11.632 14.354 1.00 36.44 C ANISOU 1365 CD GLU A 178 4916 4426 4504 -748 -35 183 C ATOM 1366 OE1 GLU A 178 -29.117 -10.540 14.327 1.00 37.54 O ANISOU 1366 OE1 GLU A 178 4925 4646 4692 -740 26 171 O ATOM 1367 OE2 GLU A 178 -28.925 -12.624 14.990 1.00 38.33 O ANISOU 1367 OE2 GLU A 178 5231 4618 4714 -859 -55 206 O ATOM 1368 N GLY A 179 -25.101 -9.434 9.818 1.00 24.79 N ANISOU 1368 N GLY A 179 3385 3038 2996 -269 -98 117 N ATOM 1369 CA GLY A 179 -25.111 -8.808 8.513 1.00 23.71 C ANISOU 1369 CA GLY A 179 3208 2953 2846 -218 -108 122 C ATOM 1370 C GLY A 179 -25.860 -7.500 8.411 1.00 25.56 C ANISOU 1370 C GLY A 179 3343 3232 3138 -227 -73 159 C ATOM 1371 O GLY A 179 -26.023 -6.987 7.299 1.00 26.69 O ANISOU 1371 O GLY A 179 3464 3411 3268 -194 -96 175 O ATOM 1372 N ASN A 180 -26.319 -6.938 9.524 1.00 28.86 N ANISOU 1372 N ASN A 180 3703 3648 3614 -268 -23 169 N ATOM 1373 CA ASN A 180 -27.070 -5.690 9.498 1.00 28.12 C ANISOU 1373 CA ASN A 180 3510 3587 3589 -265 1 189 C ATOM 1374 C ASN A 180 -26.123 -4.523 9.748 1.00 28.37 C ANISOU 1374 C ASN A 180 3518 3625 3638 -213 54 208 C ATOM 1375 O ASN A 180 -25.434 -4.484 10.773 1.00 28.89 O ANISOU 1375 O ASN A 180 3596 3677 3704 -216 101 194 O ATOM 1376 CB ASN A 180 -28.189 -5.714 10.534 1.00 30.85 C ANISOU 1376 CB ASN A 180 3792 3940 3991 -338 27 172 C ATOM 1377 CG ASN A 180 -29.141 -6.877 10.334 1.00 32.98 C ANISOU 1377 CG ASN A 180 4080 4204 4248 -412 -22 156 C ATOM 1378 OD1 ASN A 180 -29.221 -7.780 11.167 1.00 33.14 O ANISOU 1378 OD1 ASN A 180 4146 4199 4246 -483 -11 147 O ATOM 1379 ND2 ASN A 180 -29.870 -6.861 9.223 1.00 32.07 N ANISOU 1379 ND2 ASN A 180 3933 4107 4145 -401 -85 156 N ATOM 1380 N PHE A 181 -26.096 -3.576 8.815 1.00 27.65 N ANISOU 1380 N PHE A 181 3396 3549 3559 -170 40 241 N ATOM 1381 CA PHE A 181 -25.178 -2.450 8.909 1.00 23.65 C ANISOU 1381 CA PHE A 181 2875 3041 3071 -133 83 266 C ATOM 1382 C PHE A 181 -25.544 -1.535 10.069 1.00 25.57 C ANISOU 1382 C PHE A 181 3048 3267 3400 -143 125 253 C ATOM 1383 O PHE A 181 -26.722 -1.292 10.346 1.00 24.14 O ANISOU 1383 O PHE A 181 2804 3089 3279 -160 113 237 O ATOM 1384 CB PHE A 181 -25.183 -1.652 7.605 1.00 27.40 C ANISOU 1384 CB PHE A 181 3348 3529 3534 -102 49 319 C ATOM 1385 CG PHE A 181 -24.085 -2.031 6.660 1.00 27.84 C ANISOU 1385 CG PHE A 181 3468 3617 3493 -81 51 333 C ATOM 1386 CD1 PHE A 181 -22.779 -1.635 6.900 1.00 24.72 C ANISOU 1386 CD1 PHE A 181 3081 3232 3082 -68 108 337 C ATOM 1387 CD2 PHE A 181 -24.356 -2.787 5.532 1.00 26.34 C ANISOU 1387 CD2 PHE A 181 3323 3457 3228 -74 -3 331 C ATOM 1388 CE1 PHE A 181 -21.766 -1.988 6.033 1.00 25.59 C ANISOU 1388 CE1 PHE A 181 3232 3391 3102 -50 121 335 C ATOM 1389 CE2 PHE A 181 -23.347 -3.141 4.661 1.00 25.90 C ANISOU 1389 CE2 PHE A 181 3318 3447 3076 -51 7 329 C ATOM 1390 CZ PHE A 181 -22.051 -2.744 4.912 1.00 25.42 C ANISOU 1390 CZ PHE A 181 3254 3405 2999 -40 74 329 C ATOM 1391 N TYR A 182 -24.520 -1.034 10.755 1.00 23.88 N ANISOU 1391 N TYR A 182 2838 3041 3194 -130 175 247 N ATOM 1392 CA TYR A 182 -24.694 0.079 11.677 1.00 25.21 C ANISOU 1392 CA TYR A 182 2944 3191 3444 -126 210 232 C ATOM 1393 C TYR A 182 -24.782 1.365 10.865 1.00 25.34 C ANISOU 1393 C TYR A 182 2931 3184 3514 -92 184 277 C ATOM 1394 O TYR A 182 -23.858 1.694 10.113 1.00 27.30 O ANISOU 1394 O TYR A 182 3216 3429 3729 -80 184 322 O ATOM 1395 CB TYR A 182 -23.537 0.149 12.672 1.00 21.65 C ANISOU 1395 CB TYR A 182 2512 2733 2981 -126 260 206 C ATOM 1396 CG TYR A 182 -23.489 -0.986 13.671 1.00 24.82 C ANISOU 1396 CG TYR A 182 2952 3144 3334 -159 276 167 C ATOM 1397 CD1 TYR A 182 -24.300 -0.981 14.799 1.00 23.79 C ANISOU 1397 CD1 TYR A 182 2787 3023 3229 -196 304 131 C ATOM 1398 CD2 TYR A 182 -22.619 -2.054 13.496 1.00 21.38 C ANISOU 1398 CD2 TYR A 182 2591 2709 2824 -153 260 165 C ATOM 1399 CE1 TYR A 182 -24.254 -2.013 15.718 1.00 22.65 C ANISOU 1399 CE1 TYR A 182 2694 2885 3027 -240 315 110 C ATOM 1400 CE2 TYR A 182 -22.566 -3.091 14.409 1.00 22.32 C ANISOU 1400 CE2 TYR A 182 2763 2818 2898 -184 257 140 C ATOM 1401 CZ TYR A 182 -23.385 -3.065 15.518 1.00 24.58 C ANISOU 1401 CZ TYR A 182 3027 3111 3202 -234 285 121 C ATOM 1402 OH TYR A 182 -23.334 -4.095 16.429 1.00 23.37 O ANISOU 1402 OH TYR A 182 2942 2946 2991 -278 279 111 O ATOM 1403 N GLY A 183 -25.893 2.084 11.000 1.00 27.21 N ANISOU 1403 N GLY A 183 3101 3404 3834 -79 160 265 N ATOM 1404 CA GLY A 183 -26.093 3.313 10.271 1.00 26.88 C ANISOU 1404 CA GLY A 183 3041 3321 3853 -42 114 311 C ATOM 1405 C GLY A 183 -26.882 3.114 8.993 1.00 28.86 C ANISOU 1405 C GLY A 183 3302 3582 4082 -29 37 355 C ATOM 1406 O GLY A 183 -27.290 1.998 8.654 1.00 28.95 O ANISOU 1406 O GLY A 183 3330 3635 4034 -51 21 341 O ATOM 1407 N PRO A 184 -27.108 4.198 8.255 1.00 31.24 N ANISOU 1407 N PRO A 184 3603 3837 4429 5 -22 409 N ATOM 1408 CA PRO A 184 -27.890 4.122 7.015 1.00 29.98 C ANISOU 1408 CA PRO A 184 3459 3685 4247 24 -113 454 C ATOM 1409 C PRO A 184 -27.131 3.564 5.821 1.00 33.50 C ANISOU 1409 C PRO A 184 3998 4167 4565 3 -122 520 C ATOM 1410 O PRO A 184 -27.640 3.646 4.699 1.00 37.25 O ANISOU 1410 O PRO A 184 4502 4646 5005 19 -201 569 O ATOM 1411 CB PRO A 184 -28.265 5.591 6.776 1.00 34.90 C ANISOU 1411 CB PRO A 184 4062 4230 4969 71 -179 494 C ATOM 1412 CG PRO A 184 -27.092 6.343 7.308 1.00 32.29 C ANISOU 1412 CG PRO A 184 3760 3854 4656 56 -117 515 C ATOM 1413 CD PRO A 184 -26.618 5.565 8.514 1.00 32.90 C ANISOU 1413 CD PRO A 184 3809 3976 4714 26 -20 435 C ATOM 1414 N PHE A 185 -25.948 2.998 6.029 1.00 28.94 N ANISOU 1414 N PHE A 185 3463 3619 3912 -26 -47 514 N ATOM 1415 CA PHE A 185 -25.063 2.651 4.929 1.00 30.03 C ANISOU 1415 CA PHE A 185 3679 3802 3930 -41 -41 565 C ATOM 1416 C PHE A 185 -25.464 1.333 4.275 1.00 31.55 C ANISOU 1416 C PHE A 185 3901 4050 4035 -43 -75 535 C ATOM 1417 O PHE A 185 -26.007 0.429 4.917 1.00 29.70 O ANISOU 1417 O PHE A 185 3641 3823 3821 -51 -73 468 O ATOM 1418 CB PHE A 185 -23.619 2.567 5.422 1.00 29.78 C ANISOU 1418 CB PHE A 185 3664 3789 3864 -62 48 552 C ATOM 1419 CG PHE A 185 -23.198 3.745 6.252 1.00 29.27 C ANISOU 1419 CG PHE A 185 3564 3664 3892 -67 82 563 C ATOM 1420 CD1 PHE A 185 -23.038 4.993 5.673 1.00 30.43 C ANISOU 1420 CD1 PHE A 185 3730 3764 4067 -75 56 645 C ATOM 1421 CD2 PHE A 185 -22.971 3.608 7.611 1.00 27.87 C ANISOU 1421 CD2 PHE A 185 3345 3473 3773 -67 132 492 C ATOM 1422 CE1 PHE A 185 -22.654 6.082 6.433 1.00 30.38 C ANISOU 1422 CE1 PHE A 185 3698 3691 4157 -82 77 649 C ATOM 1423 CE2 PHE A 185 -22.586 4.693 8.377 1.00 27.19 C ANISOU 1423 CE2 PHE A 185 3227 3332 3771 -70 157 491 C ATOM 1424 CZ PHE A 185 -22.428 5.931 7.786 1.00 29.13 C ANISOU 1424 CZ PHE A 185 3488 3524 4057 -76 129 565 C ATOM 1425 N VAL A 186 -25.191 1.241 2.976 1.00 30.77 N ANISOU 1425 N VAL A 186 3865 3992 3833 -43 -107 585 N ATOM 1426 CA VAL A 186 -25.365 0.020 2.201 1.00 30.86 C ANISOU 1426 CA VAL A 186 3919 4060 3745 -41 -140 551 C ATOM 1427 C VAL A 186 -24.028 -0.329 1.564 1.00 28.41 C ANISOU 1427 C VAL A 186 3667 3816 3313 -49 -83 556 C ATOM 1428 O VAL A 186 -23.194 0.547 1.311 1.00 32.18 O ANISOU 1428 O VAL A 186 4157 4303 3768 -64 -39 615 O ATOM 1429 CB VAL A 186 -26.466 0.164 1.127 1.00 33.69 C ANISOU 1429 CB VAL A 186 4293 4425 4082 -27 -247 589 C ATOM 1430 CG1 VAL A 186 -27.806 0.476 1.776 1.00 34.85 C ANISOU 1430 CG1 VAL A 186 4360 4522 4360 -14 -302 565 C ATOM 1431 CG2 VAL A 186 -26.094 1.243 0.120 1.00 34.42 C ANISOU 1431 CG2 VAL A 186 4438 4522 4119 -27 -270 692 C ATOM 1432 N ASP A 187 -23.818 -1.622 1.311 1.00 27.69 N ANISOU 1432 N ASP A 187 3607 3768 3146 -39 -85 487 N ATOM 1433 CA ASP A 187 -22.555 -2.090 0.737 1.00 24.61 C ANISOU 1433 CA ASP A 187 3258 3453 2642 -33 -31 462 C ATOM 1434 C ASP A 187 -22.591 -1.914 -0.783 1.00 30.60 C ANISOU 1434 C ASP A 187 4071 4281 3274 -35 -66 510 C ATOM 1435 O ASP A 187 -22.650 -2.866 -1.564 1.00 29.92 O ANISOU 1435 O ASP A 187 4028 4249 3092 -17 -100 459 O ATOM 1436 CB ASP A 187 -22.275 -3.532 1.141 1.00 26.10 C ANISOU 1436 CB ASP A 187 3460 3646 2809 -10 -30 358 C ATOM 1437 CG ASP A 187 -23.455 -4.450 0.901 1.00 26.43 C ANISOU 1437 CG ASP A 187 3525 3664 2854 -9 -118 320 C ATOM 1438 OD1 ASP A 187 -24.545 -3.950 0.554 1.00 28.86 O ANISOU 1438 OD1 ASP A 187 3817 3953 3193 -22 -179 367 O ATOM 1439 OD2 ASP A 187 -23.289 -5.678 1.062 1.00 29.45 O ANISOU 1439 OD2 ASP A 187 3939 4040 3212 6 -136 240 O ATOM 1440 N ARG A 188 -22.554 -0.648 -1.193 1.00 29.96 N ANISOU 1440 N ARG A 188 3996 4193 3193 -61 -63 613 N ATOM 1441 CA ARG A 188 -22.471 -0.264 -2.594 1.00 32.32 C ANISOU 1441 CA ARG A 188 4360 4560 3361 -78 -89 684 C ATOM 1442 C ARG A 188 -21.560 0.948 -2.705 1.00 33.31 C ANISOU 1442 C ARG A 188 4491 4695 3472 -127 -19 777 C ATOM 1443 O ARG A 188 -21.611 1.848 -1.861 1.00 33.04 O ANISOU 1443 O ARG A 188 4417 4574 3561 -140 -8 817 O ATOM 1444 CB ARG A 188 -23.855 0.051 -3.178 1.00 33.64 C ANISOU 1444 CB ARG A 188 4551 4686 3544 -65 -212 737 C ATOM 1445 CG ARG A 188 -23.833 0.490 -4.635 1.00 37.83 C ANISOU 1445 CG ARG A 188 5164 5281 3928 -85 -254 824 C ATOM 1446 CD ARG A 188 -25.176 1.055 -5.068 1.00 40.31 C ANISOU 1446 CD ARG A 188 5496 5534 4285 -65 -390 889 C ATOM 1447 NE ARG A 188 -25.134 1.587 -6.427 1.00 44.08 N ANISOU 1447 NE ARG A 188 6069 6065 4616 -88 -441 991 N ATOM 1448 CZ ARG A 188 -26.109 2.301 -6.981 1.00 45.38 C ANISOU 1448 CZ ARG A 188 6269 6177 4795 -73 -568 1075 C ATOM 1449 NH1 ARG A 188 -27.209 2.571 -6.291 1.00 47.00 N ANISOU 1449 NH1 ARG A 188 6407 6284 5167 -29 -652 1056 N ATOM 1450 NH2 ARG A 188 -25.986 2.744 -8.224 1.00 48.73 N ANISOU 1450 NH2 ARG A 188 6796 6654 5065 -101 -614 1175 N ATOM 1451 N GLN A 189 -20.727 0.969 -3.745 1.00 35.56 N ANISOU 1451 N GLN A 189 4822 5086 3604 -160 29 806 N ATOM 1452 CA GLN A 189 -19.739 2.032 -3.928 1.00 34.16 C ANISOU 1452 CA GLN A 189 4651 4934 3395 -228 108 894 C ATOM 1453 C GLN A 189 -20.418 3.234 -4.581 1.00 38.09 C ANISOU 1453 C GLN A 189 5214 5370 3888 -266 30 1042 C ATOM 1454 O GLN A 189 -20.312 3.481 -5.785 1.00 37.59 O ANISOU 1454 O GLN A 189 5228 5379 3676 -306 16 1121 O ATOM 1455 CB GLN A 189 -18.561 1.529 -4.753 1.00 36.97 C ANISOU 1455 CB GLN A 189 5018 5445 3582 -256 203 856 C ATOM 1456 CG GLN A 189 -17.385 2.487 -4.812 1.00 35.79 C ANISOU 1456 CG GLN A 189 4851 5340 3405 -342 308 927 C ATOM 1457 CD GLN A 189 -16.168 1.870 -5.472 1.00 39.34 C ANISOU 1457 CD GLN A 189 5281 5966 3702 -363 418 855 C ATOM 1458 OE1 GLN A 189 -15.786 0.741 -5.165 1.00 39.65 O ANISOU 1458 OE1 GLN A 189 5271 6057 3736 -296 444 712 O ATOM 1459 NE2 GLN A 189 -15.557 2.607 -6.392 1.00 38.37 N ANISOU 1459 NE2 GLN A 189 5195 5934 3450 -458 479 952 N ATOM 1460 N THR A 190 -21.134 3.997 -3.756 1.00 37.64 N ANISOU 1460 N THR A 190 5129 5177 3995 -249 -29 1078 N ATOM 1461 CA THR A 190 -21.816 5.198 -4.218 1.00 39.45 C ANISOU 1461 CA THR A 190 5417 5318 4254 -268 -123 1210 C ATOM 1462 C THR A 190 -21.931 6.181 -3.061 1.00 40.29 C ANISOU 1462 C THR A 190 5472 5289 4549 -265 -128 1228 C ATOM 1463 O THR A 190 -21.791 5.813 -1.892 1.00 38.52 O ANISOU 1463 O THR A 190 5165 5041 4431 -236 -78 1130 O ATOM 1464 CB THR A 190 -23.202 4.882 -4.791 1.00 39.93 C ANISOU 1464 CB THR A 190 5510 5356 4307 -208 -262 1212 C ATOM 1465 OG1 THR A 190 -23.756 6.063 -5.385 1.00 43.08 O ANISOU 1465 OG1 THR A 190 5979 5674 4717 -222 -366 1348 O ATOM 1466 CG2 THR A 190 -24.133 4.387 -3.695 1.00 38.62 C ANISOU 1466 CG2 THR A 190 5253 5121 4301 -139 -303 1107 C ATOM 1467 N ALA A 191 -22.203 7.439 -3.407 1.00 40.20 N ANISOU 1467 N ALA A 191 5517 5184 4572 -292 -198 1353 N ATOM 1468 CA ALA A 191 -22.220 8.520 -2.426 1.00 41.40 C ANISOU 1468 CA ALA A 191 5633 5199 4897 -293 -209 1375 C ATOM 1469 C ALA A 191 -23.245 8.254 -1.330 1.00 39.44 C ANISOU 1469 C ALA A 191 5296 4880 4811 -202 -259 1266 C ATOM 1470 O ALA A 191 -24.434 8.069 -1.609 1.00 42.37 O ANISOU 1470 O ALA A 191 5664 5227 5206 -140 -366 1255 O ATOM 1471 CB ALA A 191 -22.515 9.848 -3.120 1.00 41.83 C ANISOU 1471 CB ALA A 191 5784 5149 4961 -327 -309 1530 C ATOM 1472 N GLN A 192 -22.776 8.235 -0.083 1.00 45.75 N ANISOU 1472 N GLN A 192 6016 5655 5713 -200 -179 1184 N ATOM 1473 CA GLN A 192 -23.628 8.021 1.083 1.00 44.96 C ANISOU 1473 CA GLN A 192 5827 5501 5755 -130 -203 1077 C ATOM 1474 C GLN A 192 -23.115 8.895 2.216 1.00 45.54 C ANISOU 1474 C GLN A 192 5857 5490 5958 -142 -158 1057 C ATOM 1475 O GLN A 192 -21.953 8.773 2.615 1.00 47.03 O ANISOU 1475 O GLN A 192 6032 5718 6119 -192 -57 1037 O ATOM 1476 CB GLN A 192 -23.637 6.548 1.507 1.00 44.26 C ANISOU 1476 CB GLN A 192 5688 5509 5621 -109 -144 961 C ATOM 1477 CG GLN A 192 -24.177 5.591 0.458 1.00 42.94 C ANISOU 1477 CG GLN A 192 5559 5420 5334 -94 -194 960 C ATOM 1478 CD GLN A 192 -24.118 4.146 0.906 1.00 40.11 C ANISOU 1478 CD GLN A 192 5164 5136 4940 -80 -144 847 C ATOM 1479 OE1 GLN A 192 -24.680 3.782 1.938 1.00 42.65 O ANISOU 1479 OE1 GLN A 192 5419 5428 5357 -54 -141 768 O ATOM 1480 NE2 GLN A 192 -23.432 3.314 0.132 1.00 39.95 N ANISOU 1480 NE2 GLN A 192 5190 5211 4778 -99 -107 838 N ATOM 1481 N ALA A 193 -23.974 9.765 2.736 1.00 46.96 N ANISOU 1481 N ALA A 193 6006 5555 6280 -92 -237 1049 N ATOM 1482 CA ALA A 193 -23.587 10.686 3.795 1.00 48.43 C ANISOU 1482 CA ALA A 193 6156 5649 6597 -95 -211 1020 C ATOM 1483 C ALA A 193 -23.751 10.034 5.161 1.00 45.15 C ANISOU 1483 C ALA A 193 5641 5266 6246 -59 -147 878 C ATOM 1484 O ALA A 193 -24.749 9.356 5.425 1.00 47.07 O ANISOU 1484 O ALA A 193 5833 5544 6509 -7 -173 806 O ATOM 1485 CB ALA A 193 -24.416 11.968 3.725 1.00 48.32 C ANISOU 1485 CB ALA A 193 6158 5489 6710 -48 -335 1066 C ATOM 1486 N ALA A 194 -22.732 10.211 5.995 1.00 34.22 N ANISOU 1486 N ALA A 194 4235 3879 4886 -96 -63 842 N ATOM 1487 CA ALA A 194 -22.845 9.801 7.407 1.00 34.22 C ANISOU 1487 CA ALA A 194 4155 3895 4952 -65 -10 715 C ATOM 1488 C ALA A 194 -23.544 10.965 8.118 1.00 36.26 C ANISOU 1488 C ALA A 194 4373 4037 5366 -16 -70 680 C ATOM 1489 O ALA A 194 -23.445 12.116 7.643 1.00 40.55 O ANISOU 1489 O ALA A 194 4964 4478 5967 -24 -133 758 O ATOM 1490 CB ALA A 194 -21.478 9.537 7.985 1.00 33.41 C ANISOU 1490 CB ALA A 194 4045 3837 4811 -117 88 687 C ATOM 1491 N GLY A 195 -24.195 10.710 9.250 1.00 41.41 N ANISOU 1491 N GLY A 195 4947 4703 6085 31 -51 562 N ATOM 1492 CA GLY A 195 -24.884 11.817 9.939 1.00 47.43 C ANISOU 1492 CA GLY A 195 5660 5364 6995 90 -107 505 C ATOM 1493 C GLY A 195 -23.925 12.761 10.646 1.00 45.74 C ANISOU 1493 C GLY A 195 5457 5073 6850 63 -80 492 C ATOM 1494 O GLY A 195 -22.750 12.382 10.868 1.00 42.75 O ANISOU 1494 O GLY A 195 5099 4742 6403 -1 -1 501 O ATOM 1495 N THR A 196 -24.397 13.964 10.988 1.00 41.70 N ANISOU 1495 N THR A 196 4929 4440 6476 114 -153 463 N ATOM 1496 CA THR A 196 -23.542 14.901 11.760 1.00 37.80 C ANISOU 1496 CA THR A 196 4440 3860 6061 90 -136 432 C ATOM 1497 C THR A 196 -23.127 14.165 13.033 1.00 37.82 C ANISOU 1497 C THR A 196 4382 3960 6026 79 -31 314 C ATOM 1498 O THR A 196 -24.012 13.647 13.733 1.00 39.26 O ANISOU 1498 O THR A 196 4495 4206 6216 131 -11 212 O ATOM 1499 CB THR A 196 -24.299 16.167 12.170 1.00 37.63 C ANISOU 1499 CB THR A 196 4395 3699 6205 170 -232 374 C ATOM 1500 OG1 THR A 196 -24.534 16.950 11.002 1.00 43.45 O ANISOU 1500 OG1 THR A 196 5210 4321 6978 174 -346 499 O ATOM 1501 CG2 THR A 196 -23.540 16.986 13.190 1.00 41.13 C ANISOU 1501 CG2 THR A 196 4829 4067 6732 154 -211 304 C ATOM 1502 N ASP A 197 -21.830 14.097 13.309 1.00 40.55 N ANISOU 1502 N ASP A 197 4753 4326 6330 10 32 329 N ATOM 1503 CA ASP A 197 -21.415 13.358 14.491 1.00 42.00 C ANISOU 1503 CA ASP A 197 4890 4599 6467 3 115 224 C ATOM 1504 C ASP A 197 -21.448 14.267 15.710 1.00 43.84 C ANISOU 1504 C ASP A 197 5083 4764 6811 37 106 112 C ATOM 1505 O ASP A 197 -21.135 15.458 15.623 1.00 50.01 O ANISOU 1505 O ASP A 197 5887 5423 7693 31 52 131 O ATOM 1506 CB ASP A 197 -20.012 12.778 14.310 1.00 43.07 C ANISOU 1506 CB ASP A 197 5058 4800 6508 -73 180 270 C ATOM 1507 CG ASP A 197 -19.694 11.703 15.329 1.00 41.33 C ANISOU 1507 CG ASP A 197 4806 4685 6213 -71 250 180 C ATOM 1508 OD1 ASP A 197 -20.644 11.105 15.878 1.00 40.46 O ANISOU 1508 OD1 ASP A 197 4665 4623 6086 -29 259 115 O ATOM 1509 OD2 ASP A 197 -18.497 11.458 15.585 1.00 38.87 O ANISOU 1509 OD2 ASP A 197 4501 4409 5859 -115 292 176 O ATOM 1510 N THR A 198 -21.832 13.698 16.846 1.00 37.33 N ANISOU 1510 N THR A 198 4204 4019 5963 67 156 -6 N ATOM 1511 CA THR A 198 -21.911 14.420 18.104 1.00 38.15 C ANISOU 1511 CA THR A 198 4264 4086 6147 103 158 -134 C ATOM 1512 C THR A 198 -20.975 13.779 19.121 1.00 38.00 C ANISOU 1512 C THR A 198 4243 4150 6045 62 231 -193 C ATOM 1513 O THR A 198 -20.480 12.665 18.932 1.00 36.81 O ANISOU 1513 O THR A 198 4116 4090 5780 21 278 -148 O ATOM 1514 CB THR A 198 -23.350 14.444 18.637 1.00 42.24 C ANISOU 1514 CB THR A 198 4709 4632 6709 181 148 -239 C ATOM 1515 OG1 THR A 198 -23.854 13.105 18.718 1.00 40.51 O ANISOU 1515 OG1 THR A 198 4469 4547 6376 165 208 -242 O ATOM 1516 CG2 THR A 198 -24.245 15.259 17.714 1.00 44.43 C ANISOU 1516 CG2 THR A 198 4981 4807 7093 239 51 -197 C ATOM 1517 N THR A 199 -20.731 14.501 20.210 1.00 35.18 N ANISOU 1517 N THR A 199 3861 3756 5749 79 230 -300 N ATOM 1518 CA THR A 199 -19.843 14.032 21.263 1.00 33.37 C ANISOU 1518 CA THR A 199 3634 3596 5448 48 282 -365 C ATOM 1519 C THR A 199 -20.645 13.274 22.312 1.00 35.05 C ANISOU 1519 C THR A 199 3812 3920 5587 76 334 -466 C ATOM 1520 O THR A 199 -21.689 13.751 22.770 1.00 32.90 O ANISOU 1520 O THR A 199 3488 3642 5371 130 328 -556 O ATOM 1521 CB THR A 199 -19.098 15.204 21.905 1.00 34.42 C ANISOU 1521 CB THR A 199 3764 3636 5678 43 249 -432 C ATOM 1522 OG1 THR A 199 -18.334 15.891 20.906 1.00 36.32 O ANISOU 1522 OG1 THR A 199 4042 3776 5983 -6 206 -326 O ATOM 1523 CG2 THR A 199 -18.161 14.709 22.994 1.00 33.27 C ANISOU 1523 CG2 THR A 199 3621 3568 5454 14 290 -503 C ATOM 1524 N ILE A 200 -20.153 12.096 22.692 1.00 32.66 N ANISOU 1524 N ILE A 200 3536 3718 5155 37 384 -454 N ATOM 1525 CA ILE A 200 -20.819 11.265 23.688 1.00 30.62 C ANISOU 1525 CA ILE A 200 3264 3568 4803 40 436 -528 C ATOM 1526 C ILE A 200 -20.609 11.895 25.059 1.00 31.30 C ANISOU 1526 C ILE A 200 3330 3662 4902 57 447 -660 C ATOM 1527 O ILE A 200 -19.542 11.750 25.666 1.00 30.07 O ANISOU 1527 O ILE A 200 3208 3519 4698 31 448 -678 O ATOM 1528 CB ILE A 200 -20.298 9.818 23.645 1.00 30.56 C ANISOU 1528 CB ILE A 200 3311 3643 4657 -7 466 -464 C ATOM 1529 CG1 ILE A 200 -20.196 9.339 22.195 1.00 29.23 C ANISOU 1529 CG1 ILE A 200 3168 3455 4483 -21 446 -341 C ATOM 1530 CG2 ILE A 200 -21.208 8.902 24.447 1.00 30.02 C ANISOU 1530 CG2 ILE A 200 3239 3677 4491 -21 517 -510 C ATOM 1531 CD1 ILE A 200 -19.387 8.073 22.020 1.00 28.59 C ANISOU 1531 CD1 ILE A 200 3144 3429 4289 -55 457 -285 C ATOM 1532 N THR A 201 -21.634 12.596 25.551 1.00 31.88 N ANISOU 1532 N THR A 201 3342 3731 5039 106 452 -763 N ATOM 1533 CA THR A 201 -21.480 13.425 26.743 1.00 31.62 C ANISOU 1533 CA THR A 201 3285 3690 5038 134 452 -904 C ATOM 1534 C THR A 201 -21.185 12.585 27.979 1.00 29.32 C ANISOU 1534 C THR A 201 3023 3521 4597 97 509 -961 C ATOM 1535 O THR A 201 -20.296 12.921 28.771 1.00 30.44 O ANISOU 1535 O THR A 201 3189 3652 4723 91 494 -1022 O ATOM 1536 CB THR A 201 -22.737 14.269 26.957 1.00 32.11 C ANISOU 1536 CB THR A 201 3267 3736 5199 206 447 -1016 C ATOM 1537 OG1 THR A 201 -23.028 15.007 25.763 1.00 33.38 O ANISOU 1537 OG1 THR A 201 3416 3773 5496 244 376 -948 O ATOM 1538 CG2 THR A 201 -22.537 15.239 28.110 1.00 35.03 C ANISOU 1538 CG2 THR A 201 3612 4083 5613 245 438 -1174 C ATOM 1539 N VAL A 202 -21.925 11.489 28.168 1.00 29.74 N ANISOU 1539 N VAL A 202 3079 3687 4535 67 568 -942 N ATOM 1540 CA VAL A 202 -21.722 10.653 29.349 1.00 31.53 C ANISOU 1540 CA VAL A 202 3349 4026 4604 22 617 -982 C ATOM 1541 C VAL A 202 -20.322 10.054 29.353 1.00 29.99 C ANISOU 1541 C VAL A 202 3239 3812 4342 -13 582 -907 C ATOM 1542 O VAL A 202 -19.761 9.770 30.419 1.00 28.34 O ANISOU 1542 O VAL A 202 3075 3657 4035 -33 587 -957 O ATOM 1543 CB VAL A 202 -22.814 9.565 29.427 1.00 32.46 C ANISOU 1543 CB VAL A 202 3460 4256 4618 -23 684 -956 C ATOM 1544 CG1 VAL A 202 -22.702 8.600 28.255 1.00 33.52 C ANISOU 1544 CG1 VAL A 202 3637 4366 4734 -55 663 -807 C ATOM 1545 CG2 VAL A 202 -22.744 8.822 30.756 1.00 31.77 C ANISOU 1545 CG2 VAL A 202 3424 4285 4362 -78 736 -1002 C ATOM 1546 N ASN A 203 -19.726 9.871 28.172 1.00 26.03 N ANISOU 1546 N ASN A 203 2757 3242 3891 -18 542 -794 N ATOM 1547 CA ASN A 203 -18.362 9.360 28.105 1.00 24.86 C ANISOU 1547 CA ASN A 203 2669 3082 3695 -40 506 -738 C ATOM 1548 C ASN A 203 -17.353 10.419 28.533 1.00 26.33 C ANISOU 1548 C ASN A 203 2840 3207 3959 -24 463 -806 C ATOM 1549 O ASN A 203 -16.361 10.104 29.202 1.00 27.35 O ANISOU 1549 O ASN A 203 3006 3362 4025 -37 440 -829 O ATOM 1550 CB ASN A 203 -18.056 8.868 26.691 1.00 25.17 C ANISOU 1550 CB ASN A 203 2721 3082 3759 -51 487 -612 C ATOM 1551 CG ASN A 203 -18.678 7.516 26.397 1.00 25.16 C ANISOU 1551 CG ASN A 203 2761 3144 3655 -77 512 -544 C ATOM 1552 OD1 ASN A 203 -19.451 6.988 27.196 1.00 25.33 O ANISOU 1552 OD1 ASN A 203 2795 3236 3593 -97 550 -580 O ATOM 1553 ND2 ASN A 203 -18.343 6.951 25.243 1.00 24.10 N ANISOU 1553 ND2 ASN A 203 2647 2988 3521 -83 493 -447 N ATOM 1554 N VAL A 204 -17.583 11.678 28.150 1.00 25.81 N ANISOU 1554 N VAL A 204 2722 3051 4033 3 443 -839 N ATOM 1555 CA VAL A 204 -16.691 12.758 28.565 1.00 25.86 C ANISOU 1555 CA VAL A 204 2713 2986 4126 9 397 -909 C ATOM 1556 C VAL A 204 -16.686 12.888 30.082 1.00 25.88 C ANISOU 1556 C VAL A 204 2722 3049 4061 22 405 -1047 C ATOM 1557 O VAL A 204 -15.629 13.058 30.703 1.00 26.58 O ANISOU 1557 O VAL A 204 2829 3135 4136 10 368 -1092 O ATOM 1558 CB VAL A 204 -17.097 14.081 27.888 1.00 27.61 C ANISOU 1558 CB VAL A 204 2892 3083 4515 35 363 -917 C ATOM 1559 CG1 VAL A 204 -16.299 15.241 28.464 1.00 28.93 C ANISOU 1559 CG1 VAL A 204 3047 3166 4777 36 312 -1007 C ATOM 1560 CG2 VAL A 204 -16.901 13.994 26.389 1.00 26.34 C ANISOU 1560 CG2 VAL A 204 2740 2864 4405 10 347 -772 C ATOM 1561 N LEU A 205 -17.865 12.805 30.702 1.00 29.61 N ANISOU 1561 N LEU A 205 3176 3589 4484 45 454 -1120 N ATOM 1562 CA LEU A 205 -17.946 12.918 32.154 1.00 32.36 C ANISOU 1562 CA LEU A 205 3533 4015 4747 53 473 -1255 C ATOM 1563 C LEU A 205 -17.231 11.759 32.838 1.00 32.62 C ANISOU 1563 C LEU A 205 3643 4139 4611 10 475 -1221 C ATOM 1564 O LEU A 205 -16.532 11.957 33.838 1.00 32.79 O ANISOU 1564 O LEU A 205 3692 4185 4581 11 446 -1304 O ATOM 1565 CB LEU A 205 -19.408 12.987 32.591 1.00 35.46 C ANISOU 1565 CB LEU A 205 3879 4484 5113 77 541 -1338 C ATOM 1566 CG LEU A 205 -20.208 14.149 31.999 1.00 34.14 C ANISOU 1566 CG LEU A 205 3631 4224 5118 139 524 -1392 C ATOM 1567 CD1 LEU A 205 -21.699 13.936 32.198 1.00 35.36 C ANISOU 1567 CD1 LEU A 205 3722 4474 5240 160 595 -1452 C ATOM 1568 CD2 LEU A 205 -19.764 15.470 32.607 1.00 33.87 C ANISOU 1568 CD2 LEU A 205 3575 4106 5188 185 470 -1528 C ATOM 1569 N ALA A 206 -17.392 10.543 32.310 1.00 31.43 N ANISOU 1569 N ALA A 206 3534 4033 4375 -23 498 -1102 N ATOM 1570 CA ALA A 206 -16.660 9.402 32.852 1.00 28.68 C ANISOU 1570 CA ALA A 206 3271 3747 3879 -56 478 -1057 C ATOM 1571 C ALA A 206 -15.157 9.604 32.720 1.00 29.71 C ANISOU 1571 C ALA A 206 3413 3819 4056 -46 400 -1046 C ATOM 1572 O ALA A 206 -14.387 9.207 33.602 1.00 32.39 O ANISOU 1572 O ALA A 206 3806 4200 4301 -51 359 -1079 O ATOM 1573 CB ALA A 206 -17.094 8.117 32.148 1.00 29.04 C ANISOU 1573 CB ALA A 206 3359 3822 3852 -88 503 -930 C ATOM 1574 N TRP A 207 -14.722 10.225 31.622 1.00 30.34 N ANISOU 1574 N TRP A 207 3441 3808 4280 -37 377 -1001 N ATOM 1575 CA TRP A 207 -13.305 10.513 31.436 1.00 31.68 C ANISOU 1575 CA TRP A 207 3599 3931 4507 -40 313 -999 C ATOM 1576 C TRP A 207 -12.829 11.612 32.377 1.00 32.96 C ANISOU 1576 C TRP A 207 3735 4066 4722 -30 275 -1129 C ATOM 1577 O TRP A 207 -11.675 11.591 32.820 1.00 33.40 O ANISOU 1577 O TRP A 207 3797 4128 4766 -35 217 -1162 O ATOM 1578 CB TRP A 207 -13.048 10.893 29.978 1.00 29.95 C ANISOU 1578 CB TRP A 207 3333 3633 4413 -51 312 -908 C ATOM 1579 CG TRP A 207 -11.660 11.364 29.689 1.00 33.90 C ANISOU 1579 CG TRP A 207 3798 4090 4992 -70 262 -910 C ATOM 1580 CD1 TRP A 207 -10.524 10.608 29.663 1.00 34.83 C ANISOU 1580 CD1 TRP A 207 3924 4252 5059 -75 226 -887 C ATOM 1581 CD2 TRP A 207 -11.262 12.699 29.358 1.00 35.24 C ANISOU 1581 CD2 TRP A 207 3914 4165 5310 -91 238 -938 C ATOM 1582 NE1 TRP A 207 -9.442 11.393 29.346 1.00 36.92 N ANISOU 1582 NE1 TRP A 207 4129 4470 5430 -103 193 -905 N ATOM 1583 CE2 TRP A 207 -9.869 12.680 29.154 1.00 36.90 C ANISOU 1583 CE2 TRP A 207 4093 4378 5549 -122 200 -929 C ATOM 1584 CE3 TRP A 207 -11.949 13.909 29.220 1.00 35.15 C ANISOU 1584 CE3 TRP A 207 3877 4062 5417 -87 239 -972 C ATOM 1585 CZ2 TRP A 207 -9.149 13.825 28.819 1.00 38.28 C ANISOU 1585 CZ2 TRP A 207 4215 4470 5860 -167 172 -945 C ATOM 1586 CZ3 TRP A 207 -11.233 15.044 28.888 1.00 36.98 C ANISOU 1586 CZ3 TRP A 207 4071 4193 5785 -123 199 -984 C ATOM 1587 CH2 TRP A 207 -9.848 14.993 28.689 1.00 36.18 C ANISOU 1587 CH2 TRP A 207 3942 4101 5704 -172 171 -965 C ATOM 1588 N LEU A 208 -13.698 12.576 32.696 1.00 34.66 N ANISOU 1588 N LEU A 208 3918 4251 5001 -10 300 -1213 N ATOM 1589 CA LEU A 208 -13.339 13.595 33.675 1.00 34.78 C ANISOU 1589 CA LEU A 208 3915 4240 5058 5 260 -1355 C ATOM 1590 C LEU A 208 -13.237 13.010 35.077 1.00 35.37 C ANISOU 1590 C LEU A 208 4048 4428 4965 9 257 -1438 C ATOM 1591 O LEU A 208 -12.395 13.447 35.869 1.00 38.51 O ANISOU 1591 O LEU A 208 4449 4822 5359 12 198 -1529 O ATOM 1592 CB LEU A 208 -14.353 14.738 33.646 1.00 35.63 C ANISOU 1592 CB LEU A 208 3975 4285 5278 40 281 -1437 C ATOM 1593 CG LEU A 208 -14.289 15.660 32.426 1.00 37.57 C ANISOU 1593 CG LEU A 208 4176 4388 5710 37 253 -1377 C ATOM 1594 CD1 LEU A 208 -15.382 16.716 32.490 1.00 35.80 C ANISOU 1594 CD1 LEU A 208 3912 4098 5592 88 257 -1468 C ATOM 1595 CD2 LEU A 208 -12.917 16.308 32.314 1.00 36.30 C ANISOU 1595 CD2 LEU A 208 4004 4146 5643 -0 182 -1382 C ATOM 1596 N TYR A 209 -14.083 12.029 35.402 1.00 34.51 N ANISOU 1596 N TYR A 209 3985 4417 4710 1 316 -1404 N ATOM 1597 CA TYR A 209 -13.955 11.341 36.682 1.00 33.05 C ANISOU 1597 CA TYR A 209 3876 4341 4341 -11 310 -1453 C ATOM 1598 C TYR A 209 -12.644 10.569 36.759 1.00 34.67 C ANISOU 1598 C TYR A 209 4135 4550 4487 -21 230 -1394 C ATOM 1599 O TYR A 209 -11.993 10.545 37.809 1.00 34.14 O ANISOU 1599 O TYR A 209 4112 4526 4333 -16 174 -1469 O ATOM 1600 CB TYR A 209 -15.144 10.404 36.901 1.00 32.39 C ANISOU 1600 CB TYR A 209 3835 4356 4116 -39 394 -1408 C ATOM 1601 CG TYR A 209 -16.373 11.088 37.455 1.00 34.50 C ANISOU 1601 CG TYR A 209 4053 4677 4378 -27 471 -1524 C ATOM 1602 CD1 TYR A 209 -16.417 11.522 38.773 1.00 36.86 C ANISOU 1602 CD1 TYR A 209 4368 5051 4584 -20 476 -1668 C ATOM 1603 CD2 TYR A 209 -17.492 11.297 36.659 1.00 35.13 C ANISOU 1603 CD2 TYR A 209 4063 4739 4544 -18 535 -1501 C ATOM 1604 CE1 TYR A 209 -17.541 12.148 39.282 1.00 39.06 C ANISOU 1604 CE1 TYR A 209 4590 5392 4859 -2 552 -1794 C ATOM 1605 CE2 TYR A 209 -18.618 11.922 37.158 1.00 36.89 C ANISOU 1605 CE2 TYR A 209 4224 5019 4773 4 602 -1623 C ATOM 1606 CZ TYR A 209 -18.637 12.345 38.470 1.00 39.74 C ANISOU 1606 CZ TYR A 209 4596 5460 5042 13 615 -1774 C ATOM 1607 OH TYR A 209 -19.758 12.967 38.970 1.00 40.04 O ANISOU 1607 OH TYR A 209 4561 5568 5085 42 687 -1914 O ATOM 1608 N ALA A 210 -12.243 9.933 35.654 1.00 33.35 N ANISOU 1608 N ALA A 210 3964 4343 4366 -28 217 -1269 N ATOM 1609 CA ALA A 210 -10.960 9.238 35.621 1.00 34.00 C ANISOU 1609 CA ALA A 210 4077 4427 4415 -22 136 -1227 C ATOM 1610 C ALA A 210 -9.808 10.194 35.897 1.00 34.11 C ANISOU 1610 C ALA A 210 4035 4397 4530 -11 63 -1319 C ATOM 1611 O ALA A 210 -8.841 9.835 36.578 1.00 36.43 O ANISOU 1611 O ALA A 210 4359 4724 4759 2 -18 -1355 O ATOM 1612 CB ALA A 210 -10.771 8.548 34.270 1.00 31.88 C ANISOU 1612 CB ALA A 210 3792 4123 4197 -25 144 -1098 C ATOM 1613 N ALA A 211 -9.894 11.420 35.373 1.00 32.67 N ANISOU 1613 N ALA A 211 3769 4134 4508 -17 81 -1357 N ATOM 1614 CA ALA A 211 -8.856 12.411 35.636 1.00 33.44 C ANISOU 1614 CA ALA A 211 3811 4180 4714 -23 12 -1447 C ATOM 1615 C ALA A 211 -8.821 12.795 37.109 1.00 34.65 C ANISOU 1615 C ALA A 211 4001 4379 4787 -6 -28 -1591 C ATOM 1616 O ALA A 211 -7.742 12.966 37.688 1.00 35.16 O ANISOU 1616 O ALA A 211 4057 4450 4853 -4 -112 -1660 O ATOM 1617 CB ALA A 211 -9.078 13.645 34.764 1.00 31.83 C ANISOU 1617 CB ALA A 211 3533 3864 4698 -42 36 -1447 C ATOM 1618 N VAL A 212 -9.994 12.943 37.730 1.00 43.62 N ANISOU 1618 N VAL A 212 5170 5554 5848 7 32 -1646 N ATOM 1619 CA VAL A 212 -10.048 13.258 39.155 1.00 44.49 C ANISOU 1619 CA VAL A 212 5321 5728 5855 22 5 -1789 C ATOM 1620 C VAL A 212 -9.465 12.114 39.976 1.00 44.56 C ANISOU 1620 C VAL A 212 5422 5834 5675 21 -49 -1765 C ATOM 1621 O VAL A 212 -8.751 12.338 40.961 1.00 46.87 O ANISOU 1621 O VAL A 212 5739 6158 5911 32 -128 -1866 O ATOM 1622 CB VAL A 212 -11.494 13.579 39.578 1.00 44.31 C ANISOU 1622 CB VAL A 212 5303 5750 5784 35 97 -1855 C ATOM 1623 CG1 VAL A 212 -11.560 13.873 41.069 1.00 48.07 C ANISOU 1623 CG1 VAL A 212 5823 6312 6130 48 79 -2011 C ATOM 1624 CG2 VAL A 212 -12.032 14.755 38.778 1.00 44.13 C ANISOU 1624 CG2 VAL A 212 5192 5613 5960 52 125 -1885 C ATOM 1625 N ILE A 213 -9.759 10.872 39.582 1.00 41.48 N ANISOU 1625 N ILE A 213 5090 5486 5184 10 -19 -1633 N ATOM 1626 CA ILE A 213 -9.210 9.716 40.285 1.00 40.75 C ANISOU 1626 CA ILE A 213 5101 5465 4918 11 -87 -1593 C ATOM 1627 C ILE A 213 -7.692 9.684 40.168 1.00 39.41 C ANISOU 1627 C ILE A 213 4899 5258 4815 36 -207 -1604 C ATOM 1628 O ILE A 213 -6.997 9.249 41.096 1.00 41.79 O ANISOU 1628 O ILE A 213 5268 5609 5002 53 -301 -1643 O ATOM 1629 CB ILE A 213 -9.852 8.418 39.752 1.00 42.74 C ANISOU 1629 CB ILE A 213 5421 5743 5076 -9 -37 -1445 C ATOM 1630 CG1 ILE A 213 -11.356 8.410 40.034 1.00 42.98 C ANISOU 1630 CG1 ILE A 213 5476 5833 5022 -43 80 -1448 C ATOM 1631 CG2 ILE A 213 -9.202 7.190 40.372 1.00 43.05 C ANISOU 1631 CG2 ILE A 213 5577 5826 4952 -2 -129 -1390 C ATOM 1632 CD1 ILE A 213 -12.104 7.295 39.334 1.00 43.42 C ANISOU 1632 CD1 ILE A 213 5576 5899 5024 -75 138 -1306 C ATOM 1633 N ASN A 214 -7.149 10.162 39.048 1.00 46.35 N ANISOU 1633 N ASN A 214 5674 6058 5878 34 -207 -1574 N ATOM 1634 CA ASN A 214 -5.713 10.135 38.804 1.00 46.76 C ANISOU 1634 CA ASN A 214 5669 6088 6009 49 -306 -1587 C ATOM 1635 C ASN A 214 -5.033 11.466 39.116 1.00 48.05 C ANISOU 1635 C ASN A 214 5746 6206 6304 36 -353 -1716 C ATOM 1636 O ASN A 214 -3.907 11.698 38.664 1.00 47.68 O ANISOU 1636 O ASN A 214 5615 6131 6371 29 -413 -1727 O ATOM 1637 CB ASN A 214 -5.433 9.718 37.359 1.00 42.70 C ANISOU 1637 CB ASN A 214 5093 5533 5598 44 -275 -1471 C ATOM 1638 CG ASN A 214 -5.565 8.221 37.152 1.00 48.54 C ANISOU 1638 CG ASN A 214 5918 6314 6212 69 -285 -1364 C ATOM 1639 OD1 ASN A 214 -4.614 7.468 37.363 1.00 47.50 O ANISOU 1639 OD1 ASN A 214 5805 6207 6035 107 -381 -1362 O ATOM 1640 ND2 ASN A 214 -6.748 7.782 36.739 1.00 46.29 N ANISOU 1640 ND2 ASN A 214 5683 6030 5877 52 -195 -1279 N ATOM 1641 N GLY A 215 -5.690 12.344 39.874 1.00 57.81 N ANISOU 1641 N GLY A 215 6997 7438 7529 31 -328 -1821 N ATOM 1642 CA GLY A 215 -5.064 13.529 40.416 1.00 57.89 C ANISOU 1642 CA GLY A 215 6949 7407 7639 23 -393 -1962 C ATOM 1643 C GLY A 215 -5.342 14.819 39.669 1.00 60.43 C ANISOU 1643 C GLY A 215 7183 7615 8162 -9 -347 -1988 C ATOM 1644 O GLY A 215 -5.152 15.898 40.242 1.00 64.48 O ANISOU 1644 O GLY A 215 7668 8081 8749 -16 -390 -2120 O ATOM 1645 N ASP A 216 -5.778 14.745 38.413 1.00 54.69 N ANISOU 1645 N ASP A 216 6422 6835 7523 -29 -271 -1865 N ATOM 1646 CA ASP A 216 -6.040 15.946 37.624 1.00 55.96 C ANISOU 1646 CA ASP A 216 6514 6874 7874 -62 -239 -1868 C ATOM 1647 C ASP A 216 -7.358 16.561 38.082 1.00 57.67 C ANISOU 1647 C ASP A 216 6763 7071 8078 -32 -186 -1943 C ATOM 1648 O ASP A 216 -8.433 16.011 37.818 1.00 56.98 O ANISOU 1648 O ASP A 216 6711 7022 7918 -11 -105 -1876 O ATOM 1649 CB ASP A 216 -6.071 15.612 36.136 1.00 53.36 C ANISOU 1649 CB ASP A 216 6147 6506 7622 -93 -182 -1710 C ATOM 1650 CG ASP A 216 -4.706 15.731 35.483 1.00 58.31 C ANISOU 1650 CG ASP A 216 6693 7108 8353 -143 -230 -1677 C ATOM 1651 OD1 ASP A 216 -3.751 16.149 36.171 1.00 61.13 O ANISOU 1651 OD1 ASP A 216 7016 7469 8743 -157 -312 -1780 O ATOM 1652 OD2 ASP A 216 -4.589 15.407 34.283 1.00 58.26 O ANISOU 1652 OD2 ASP A 216 6654 7090 8394 -172 -184 -1554 O ATOM 1653 N ARG A 217 -7.280 17.705 38.768 1.00 55.18 N ANISOU 1653 N ARG A 217 6429 6696 7839 -27 -233 -2091 N ATOM 1654 CA ARG A 217 -8.456 18.340 39.351 1.00 55.43 C ANISOU 1654 CA ARG A 217 6481 6720 7859 16 -193 -2201 C ATOM 1655 C ARG A 217 -8.564 19.826 39.029 1.00 55.81 C ANISOU 1655 C ARG A 217 6479 6610 8118 11 -225 -2279 C ATOM 1656 O ARG A 217 -9.431 20.504 39.593 1.00 57.67 O ANISOU 1656 O ARG A 217 6720 6826 8364 60 -211 -2406 O ATOM 1657 CB ARG A 217 -8.466 18.162 40.874 1.00 54.64 C ANISOU 1657 CB ARG A 217 6437 6734 7591 49 -222 -2347 C ATOM 1658 CG ARG A 217 -8.303 16.734 41.352 1.00 56.42 C ANISOU 1658 CG ARG A 217 6735 7104 7598 51 -213 -2275 C ATOM 1659 CD ARG A 217 -8.312 16.673 42.869 1.00 59.93 C ANISOU 1659 CD ARG A 217 7245 7655 7868 75 -248 -2419 C ATOM 1660 NE ARG A 217 -9.666 16.582 43.409 1.00 59.94 N ANISOU 1660 NE ARG A 217 7285 7742 7748 98 -150 -2470 N ATOM 1661 CZ ARG A 217 -10.391 17.626 43.800 1.00 62.39 C ANISOU 1661 CZ ARG A 217 7561 8027 8117 131 -121 -2621 C ATOM 1662 NH1 ARG A 217 -11.614 17.441 44.278 1.00 62.53 N ANISOU 1662 NH1 ARG A 217 7599 8147 8014 151 -22 -2670 N ATOM 1663 NH2 ARG A 217 -9.900 18.854 43.710 1.00 63.56 N ANISOU 1663 NH2 ARG A 217 7652 8048 8451 142 -192 -2728 N ATOM 1664 N TRP A 218 -7.710 20.354 38.148 1.00 48.17 N ANISOU 1664 N TRP A 218 5462 5527 7315 -49 -270 -2212 N ATOM 1665 CA TRP A 218 -7.674 21.795 37.918 1.00 48.08 C ANISOU 1665 CA TRP A 218 5418 5346 7506 -68 -322 -2284 C ATOM 1666 C TRP A 218 -8.955 22.321 37.289 1.00 49.99 C ANISOU 1666 C TRP A 218 5664 5498 7833 -27 -272 -2257 C ATOM 1667 O TRP A 218 -9.245 23.517 37.408 1.00 51.31 O ANISOU 1667 O TRP A 218 5823 5530 8142 -9 -322 -2360 O ATOM 1668 CB TRP A 218 -6.480 22.163 37.034 1.00 48.63 C ANISOU 1668 CB TRP A 218 5436 5321 7720 -164 -370 -2193 C ATOM 1669 CG TRP A 218 -6.518 21.575 35.646 1.00 47.56 C ANISOU 1669 CG TRP A 218 5285 5182 7602 -205 -304 -1992 C ATOM 1670 CD1 TRP A 218 -5.846 20.471 35.207 1.00 45.98 C ANISOU 1670 CD1 TRP A 218 5068 5090 7313 -232 -277 -1881 C ATOM 1671 CD2 TRP A 218 -7.248 22.073 34.514 1.00 48.61 C ANISOU 1671 CD2 TRP A 218 5421 5200 7849 -218 -268 -1885 C ATOM 1672 NE1 TRP A 218 -6.117 20.247 33.879 1.00 45.44 N ANISOU 1672 NE1 TRP A 218 4990 4988 7288 -264 -217 -1719 N ATOM 1673 CE2 TRP A 218 -6.975 21.216 33.430 1.00 45.64 C ANISOU 1673 CE2 TRP A 218 5031 4878 7433 -260 -212 -1712 C ATOM 1674 CE3 TRP A 218 -8.109 23.157 34.314 1.00 48.52 C ANISOU 1674 CE3 TRP A 218 5426 5042 7968 -192 -287 -1924 C ATOM 1675 CZ2 TRP A 218 -7.531 21.409 32.167 1.00 45.10 C ANISOU 1675 CZ2 TRP A 218 4968 4729 7438 -283 -172 -1572 C ATOM 1676 CZ3 TRP A 218 -8.660 23.346 33.060 1.00 48.01 C ANISOU 1676 CZ3 TRP A 218 5368 4888 7984 -210 -257 -1780 C ATOM 1677 CH2 TRP A 218 -8.370 22.477 32.004 1.00 48.04 C ANISOU 1677 CH2 TRP A 218 5363 4957 7934 -259 -198 -1603 C ATOM 1678 N PHE A 219 -9.720 21.464 36.619 1.00 46.34 N ANISOU 1678 N PHE A 219 5213 5101 7293 -8 -187 -2128 N ATOM 1679 CA PHE A 219 -10.942 21.871 35.942 1.00 46.69 C ANISOU 1679 CA PHE A 219 5253 5070 7416 34 -147 -2094 C ATOM 1680 C PHE A 219 -12.155 21.856 36.855 1.00 44.28 C ANISOU 1680 C PHE A 219 4956 4847 7021 123 -102 -2233 C ATOM 1681 O PHE A 219 -13.191 22.413 36.488 1.00 47.23 O ANISOU 1681 O PHE A 219 5311 5151 7482 176 -86 -2256 O ATOM 1682 CB PHE A 219 -11.219 20.952 34.754 1.00 42.87 C ANISOU 1682 CB PHE A 219 4772 4625 6893 10 -80 -1896 C ATOM 1683 CG PHE A 219 -11.139 19.494 35.100 1.00 41.98 C ANISOU 1683 CG PHE A 219 4684 4688 6577 11 -23 -1843 C ATOM 1684 CD1 PHE A 219 -12.247 18.818 35.588 1.00 41.10 C ANISOU 1684 CD1 PHE A 219 4595 4691 6330 62 47 -1871 C ATOM 1685 CD2 PHE A 219 -9.952 18.801 34.944 1.00 43.47 C ANISOU 1685 CD2 PHE A 219 4874 4927 6715 -42 -44 -1769 C ATOM 1686 CE1 PHE A 219 -12.170 17.476 35.908 1.00 40.29 C ANISOU 1686 CE1 PHE A 219 4532 4733 6043 52 89 -1811 C ATOM 1687 CE2 PHE A 219 -9.869 17.461 35.262 1.00 40.56 C ANISOU 1687 CE2 PHE A 219 4541 4701 6169 -34 -10 -1720 C ATOM 1688 CZ PHE A 219 -10.980 16.796 35.744 1.00 40.99 C ANISOU 1688 CZ PHE A 219 4634 4852 6087 9 54 -1735 C ATOM 1689 N LEU A 220 -12.062 21.225 38.019 1.00 39.55 N ANISOU 1689 N LEU A 220 4382 4399 6245 139 -82 -2325 N ATOM 1690 CA LEU A 220 -13.181 21.236 38.943 1.00 41.48 C ANISOU 1690 CA LEU A 220 4629 4742 6389 210 -27 -2467 C ATOM 1691 C LEU A 220 -13.454 22.660 39.379 1.00 47.41 C ANISOU 1691 C LEU A 220 5353 5373 7288 266 -88 -2653 C ATOM 1692 O LEU A 220 -12.562 23.372 39.846 1.00 45.89 O ANISOU 1692 O LEU A 220 5166 5105 7165 248 -176 -2748 O ATOM 1693 CB LEU A 220 -12.890 20.365 40.160 1.00 41.82 C ANISOU 1693 CB LEU A 220 4720 4964 6205 202 -6 -2528 C ATOM 1694 CG LEU A 220 -12.731 18.881 39.839 1.00 40.81 C ANISOU 1694 CG LEU A 220 4633 4953 5919 158 46 -2356 C ATOM 1695 CD1 LEU A 220 -12.400 18.122 41.103 1.00 41.59 C ANISOU 1695 CD1 LEU A 220 4797 5207 5797 149 44 -2418 C ATOM 1696 CD2 LEU A 220 -14.004 18.370 39.202 1.00 37.17 C ANISOU 1696 CD2 LEU A 220 4157 4534 5433 174 145 -2271 C ATOM 1697 N ASN A 221 -14.696 23.080 39.225 1.00 56.48 N ANISOU 1697 N ASN A 221 6466 6501 8492 338 -48 -2715 N ATOM 1698 CA ASN A 221 -15.083 24.385 39.719 1.00 57.40 C ANISOU 1698 CA ASN A 221 6557 6511 8742 412 -107 -2917 C ATOM 1699 C ASN A 221 -16.066 24.174 40.864 1.00 61.20 C ANISOU 1699 C ASN A 221 7019 7175 9059 480 -30 -3073 C ATOM 1700 O ASN A 221 -16.616 23.083 41.062 1.00 59.57 O ANISOU 1700 O ASN A 221 6815 7143 8676 470 76 -3039 O ATOM 1701 CB ASN A 221 -15.691 25.283 38.621 1.00 59.52 C ANISOU 1701 CB ASN A 221 6795 6585 9237 453 -151 -2873 C ATOM 1702 CG ASN A 221 -16.948 24.699 38.016 1.00 57.17 C ANISOU 1702 CG ASN A 221 6460 6362 8901 498 -62 -2797 C ATOM 1703 OD1 ASN A 221 -17.713 24.002 38.682 1.00 56.08 O ANISOU 1703 OD1 ASN A 221 6299 6411 8598 529 34 -2864 O ATOM 1704 ND2 ASN A 221 -17.193 25.015 36.754 1.00 58.46 N ANISOU 1704 ND2 ASN A 221 6617 6379 9215 496 -97 -2660 N ATOM 1705 N ARG A 222 -16.223 25.213 41.671 1.00 85.90 N ANISOU 1705 N ARG A 222 10132 10282 12225 531 -84 -3209 N ATOM 1706 CA ARG A 222 -17.220 25.219 42.721 1.00 87.03 C ANISOU 1706 CA ARG A 222 10245 10595 12228 591 -15 -3339 C ATOM 1707 C ARG A 222 -18.474 25.956 42.288 1.00 91.33 C ANISOU 1707 C ARG A 222 10718 11083 12902 678 -10 -3378 C ATOM 1708 O ARG A 222 -18.808 26.959 42.934 1.00 91.83 O ANISOU 1708 O ARG A 222 10752 11121 13016 742 -58 -3515 O ATOM 1709 CB ARG A 222 -16.624 25.797 44.013 1.00 92.66 C ANISOU 1709 CB ARG A 222 10985 11349 12872 598 -73 -3481 C ATOM 1710 CG ARG A 222 -17.398 25.550 45.344 1.00 94.96 C ANISOU 1710 CG ARG A 222 11267 11863 12952 632 11 -3613 C ATOM 1711 CD ARG A 222 -17.079 24.217 46.022 1.00 97.52 C ANISOU 1711 CD ARG A 222 11654 12389 13012 564 90 -3571 C ATOM 1712 NE ARG A 222 -17.934 23.158 45.514 1.00 97.84 N ANISOU 1712 NE ARG A 222 11676 12541 12957 542 210 -3472 N ATOM 1713 CZ ARG A 222 -19.144 22.843 45.976 1.00100.26 C ANISOU 1713 CZ ARG A 222 11940 13012 13142 561 321 -3518 C ATOM 1714 NH1 ARG A 222 -19.786 21.854 45.379 1.00 97.43 N ANISOU 1714 NH1 ARG A 222 11567 12735 12717 526 419 -3408 N ATOM 1715 NH2 ARG A 222 -19.704 23.456 47.015 1.00102.96 N ANISOU 1715 NH2 ARG A 222 12251 13445 13425 608 338 -3669 N ATOM 1716 N PHE A 223 -19.057 25.554 41.142 1.00 59.54 N ANISOU 1716 N PHE A 223 6664 7012 8949 682 27 -3258 N ATOM 1717 CA PHE A 223 -20.425 25.733 40.662 1.00 57.82 C ANISOU 1717 CA PHE A 223 6369 6805 8792 754 65 -3266 C ATOM 1718 C PHE A 223 -21.083 24.405 40.253 1.00 59.30 C ANISOU 1718 C PHE A 223 6535 7145 8849 722 193 -3169 C ATOM 1719 O PHE A 223 -20.422 23.401 39.975 1.00 58.50 O ANISOU 1719 O PHE A 223 6486 7084 8658 646 235 -3062 O ATOM 1720 CB PHE A 223 -20.448 26.666 39.459 1.00 57.44 C ANISOU 1720 CB PHE A 223 6316 6511 8996 790 -44 -3193 C ATOM 1721 CG PHE A 223 -19.803 27.994 39.704 1.00 59.94 C ANISOU 1721 CG PHE A 223 6661 6654 9460 810 -177 -3264 C ATOM 1722 CD1 PHE A 223 -18.567 28.303 39.160 1.00 59.87 C ANISOU 1722 CD1 PHE A 223 6717 6471 9560 737 -264 -3170 C ATOM 1723 CD2 PHE A 223 -20.414 28.920 40.534 1.00 62.32 C ANISOU 1723 CD2 PHE A 223 6922 6974 9785 894 -213 -3432 C ATOM 1724 CE1 PHE A 223 -17.970 29.540 39.408 1.00 62.30 C ANISOU 1724 CE1 PHE A 223 7051 6619 10001 743 -387 -3233 C ATOM 1725 CE2 PHE A 223 -19.822 30.152 40.788 1.00 64.66 C ANISOU 1725 CE2 PHE A 223 7246 7105 10215 912 -339 -3503 C ATOM 1726 CZ PHE A 223 -18.601 30.461 40.223 1.00 65.56 C ANISOU 1726 CZ PHE A 223 7429 7042 10439 833 -426 -3399 C ATOM 1727 N THR A 224 -22.410 24.432 40.176 1.00 55.92 N ANISOU 1727 N THR A 224 6026 6798 8423 780 247 -3209 N ATOM 1728 CA THR A 224 -23.210 23.300 39.738 1.00 54.26 C ANISOU 1728 CA THR A 224 5779 6726 8113 752 362 -3123 C ATOM 1729 C THR A 224 -24.278 23.807 38.784 1.00 53.19 C ANISOU 1729 C THR A 224 5562 6502 8144 829 329 -3103 C ATOM 1730 O THR A 224 -24.478 25.014 38.630 1.00 57.53 O ANISOU 1730 O THR A 224 6089 6908 8863 907 224 -3171 O ATOM 1731 CB THR A 224 -23.852 22.572 40.924 1.00 53.73 C ANISOU 1731 CB THR A 224 5686 6921 7809 721 488 -3206 C ATOM 1732 OG1 THR A 224 -24.221 21.247 40.525 1.00 54.63 O ANISOU 1732 OG1 THR A 224 5799 7162 7796 651 598 -3087 O ATOM 1733 CG2 THR A 224 -25.092 23.323 41.406 1.00 56.14 C ANISOU 1733 CG2 THR A 224 5888 7292 8151 803 498 -3351 C ATOM 1734 N THR A 225 -24.984 22.862 38.168 1.00 68.64 N ANISOU 1734 N THR A 225 7480 8552 10049 805 414 -3010 N ATOM 1735 CA THR A 225 -25.903 23.151 37.086 1.00 67.15 C ANISOU 1735 CA THR A 225 7224 8277 10012 868 377 -2959 C ATOM 1736 C THR A 225 -27.132 22.266 37.227 1.00 66.91 C ANISOU 1736 C THR A 225 7106 8459 9856 852 499 -2966 C ATOM 1737 O THR A 225 -27.239 21.451 38.149 1.00 66.75 O ANISOU 1737 O THR A 225 7087 8642 9632 783 613 -3000 O ATOM 1738 CB THR A 225 -25.232 22.924 35.730 1.00 66.02 C ANISOU 1738 CB THR A 225 7138 7958 9987 842 322 -2782 C ATOM 1739 OG1 THR A 225 -26.100 23.386 34.693 1.00 67.74 O ANISOU 1739 OG1 THR A 225 7302 8072 10365 914 258 -2737 O ATOM 1740 CG2 THR A 225 -24.951 21.439 35.520 1.00 62.67 C ANISOU 1740 CG2 THR A 225 6747 7667 9397 740 430 -2645 C ATOM 1741 N THR A 226 -28.065 22.441 36.299 1.00 52.23 N ANISOU 1741 N THR A 226 5176 6550 8120 908 467 -2929 N ATOM 1742 CA THR A 226 -29.227 21.581 36.152 1.00 50.80 C ANISOU 1742 CA THR A 226 4906 6544 7853 885 568 -2909 C ATOM 1743 C THR A 226 -29.119 20.794 34.852 1.00 49.34 C ANISOU 1743 C THR A 226 4740 6296 7711 850 570 -2728 C ATOM 1744 O THR A 226 -28.333 21.128 33.960 1.00 48.36 O ANISOU 1744 O THR A 226 4683 5976 7717 867 479 -2628 O ATOM 1745 CB THR A 226 -30.531 22.390 36.165 1.00 54.16 C ANISOU 1745 CB THR A 226 5213 6984 8381 985 526 -3032 C ATOM 1746 OG1 THR A 226 -30.517 23.355 35.104 1.00 54.87 O ANISOU 1746 OG1 THR A 226 5312 6839 8696 1078 375 -2992 O ATOM 1747 CG2 THR A 226 -30.709 23.105 37.496 1.00 56.46 C ANISOU 1747 CG2 THR A 226 5473 7359 8619 1020 535 -3223 C ATOM 1748 N LEU A 227 -29.928 19.737 34.754 1.00 48.94 N ANISOU 1748 N LEU A 227 4630 6417 7547 793 676 -2682 N ATOM 1749 CA LEU A 227 -29.929 18.927 33.541 1.00 47.78 C ANISOU 1749 CA LEU A 227 4491 6231 7432 758 683 -2516 C ATOM 1750 C LEU A 227 -30.425 19.729 32.347 1.00 49.10 C ANISOU 1750 C LEU A 227 4617 6222 7816 861 556 -2480 C ATOM 1751 O LEU A 227 -29.925 19.564 31.227 1.00 47.04 O ANISOU 1751 O LEU A 227 4420 5826 7626 844 491 -2313 O ATOM 1752 CB LEU A 227 -30.785 17.677 33.739 1.00 48.72 C ANISOU 1752 CB LEU A 227 4551 6572 7388 668 816 -2483 C ATOM 1753 CG LEU A 227 -30.410 16.466 32.880 1.00 48.35 C ANISOU 1753 CG LEU A 227 4578 6526 7266 563 838 -2261 C ATOM 1754 CD1 LEU A 227 -28.904 16.253 32.877 1.00 46.49 C ANISOU 1754 CD1 LEU A 227 4505 6191 6969 497 794 -2126 C ATOM 1755 CD2 LEU A 227 -31.130 15.222 33.372 1.00 46.12 C ANISOU 1755 CD2 LEU A 227 4254 6469 6800 453 978 -2250 C ATOM 1756 N ASN A 228 -31.407 20.605 32.563 1.00 53.00 N ANISOU 1756 N ASN A 228 5026 6717 8394 950 502 -2606 N ATOM 1757 CA ASN A 228 -31.884 21.454 31.479 1.00 53.35 C ANISOU 1757 CA ASN A 228 5045 6585 8642 1054 361 -2577 C ATOM 1758 C ASN A 228 -30.797 22.424 31.034 1.00 53.81 C ANISOU 1758 C ASN A 228 5213 6390 8844 1094 228 -2526 C ATOM 1759 O ASN A 228 -30.358 22.392 29.879 1.00 54.80 O ANISOU 1759 O ASN A 228 5397 6360 9065 1094 156 -2375 O ATOM 1760 CB ASN A 228 -33.143 22.206 31.916 1.00 57.46 C ANISOU 1760 CB ASN A 228 5451 7166 9215 1144 329 -2741 C ATOM 1761 CG ASN A 228 -34.415 21.521 31.461 1.00 55.69 C ANISOU 1761 CG ASN A 228 5113 7079 8967 1140 376 -2729 C ATOM 1762 OD1 ASN A 228 -34.445 20.870 30.417 1.00 57.89 O ANISOU 1762 OD1 ASN A 228 5402 7324 9268 1113 366 -2584 O ATOM 1763 ND2 ASN A 228 -35.475 21.666 32.242 1.00 56.61 N ANISOU 1763 ND2 ASN A 228 5116 7354 9040 1163 427 -2884 N ATOM 1764 N ASP A 229 -30.313 23.261 31.959 1.00 51.91 N ANISOU 1764 N ASP A 229 5003 6108 8610 1116 198 -2645 N ATOM 1765 CA ASP A 229 -29.356 24.305 31.602 1.00 51.42 C ANISOU 1765 CA ASP A 229 5041 5801 8695 1145 62 -2608 C ATOM 1766 C ASP A 229 -28.097 23.735 30.958 1.00 50.98 C ANISOU 1766 C ASP A 229 5092 5648 8631 1059 70 -2440 C ATOM 1767 O ASP A 229 -27.518 24.368 30.068 1.00 51.00 O ANISOU 1767 O ASP A 229 5172 5430 8777 1069 -48 -2334 O ATOM 1768 CB ASP A 229 -28.988 25.126 32.838 1.00 53.35 C ANISOU 1768 CB ASP A 229 5298 6052 8921 1164 47 -2770 C ATOM 1769 CG ASP A 229 -30.147 25.959 33.350 1.00 57.74 C ANISOU 1769 CG ASP A 229 5754 6653 9530 1267 6 -2940 C ATOM 1770 OD1 ASP A 229 -31.059 26.266 32.553 1.00 58.09 O ANISOU 1770 OD1 ASP A 229 5745 6641 9684 1340 -65 -2922 O ATOM 1771 OD2 ASP A 229 -30.147 26.307 34.550 1.00 62.47 O ANISOU 1771 OD2 ASP A 229 6330 7347 10061 1277 41 -3097 O ATOM 1772 N PHE A 230 -27.657 22.549 31.386 1.00 49.36 N ANISOU 1772 N PHE A 230 4900 5604 8250 963 201 -2402 N ATOM 1773 CA PHE A 230 -26.495 21.936 30.752 1.00 48.08 C ANISOU 1773 CA PHE A 230 4860 5391 8016 839 195 -2175 C ATOM 1774 C PHE A 230 -26.816 21.484 29.333 1.00 45.69 C ANISOU 1774 C PHE A 230 4573 5039 7748 818 160 -1978 C ATOM 1775 O PHE A 230 -26.021 21.702 28.412 1.00 45.03 O ANISOU 1775 O PHE A 230 4581 4806 7722 773 84 -1813 O ATOM 1776 CB PHE A 230 -25.988 20.756 31.581 1.00 46.08 C ANISOU 1776 CB PHE A 230 4638 5334 7537 731 321 -2152 C ATOM 1777 CG PHE A 230 -24.909 19.961 30.898 1.00 43.93 C ANISOU 1777 CG PHE A 230 4471 5035 7185 616 321 -1930 C ATOM 1778 CD1 PHE A 230 -23.592 20.391 30.924 1.00 44.87 C ANISOU 1778 CD1 PHE A 230 4676 5039 7334 572 262 -1882 C ATOM 1779 CD2 PHE A 230 -25.211 18.788 30.223 1.00 43.58 C ANISOU 1779 CD2 PHE A 230 4432 5084 7040 555 377 -1781 C ATOM 1780 CE1 PHE A 230 -22.597 19.665 30.293 1.00 43.13 C ANISOU 1780 CE1 PHE A 230 4535 4808 7044 473 265 -1696 C ATOM 1781 CE2 PHE A 230 -24.222 18.060 29.590 1.00 41.48 C ANISOU 1781 CE2 PHE A 230 4258 4798 6705 462 375 -1596 C ATOM 1782 CZ PHE A 230 -22.913 18.499 29.626 1.00 39.21 C ANISOU 1782 CZ PHE A 230 4044 4406 6446 425 321 -1557 C ATOM 1783 N ASN A 231 -27.974 20.845 29.140 1.00 47.31 N ANISOU 1783 N ASN A 231 4687 5376 7913 843 218 -1994 N ATOM 1784 CA ASN A 231 -28.351 20.372 27.813 1.00 47.47 C ANISOU 1784 CA ASN A 231 4718 5361 7957 825 182 -1819 C ATOM 1785 C ASN A 231 -28.533 21.515 26.823 1.00 48.82 C ANISOU 1785 C ASN A 231 4908 5310 8331 915 26 -1782 C ATOM 1786 O ASN A 231 -28.462 21.286 25.611 1.00 47.84 O ANISOU 1786 O ASN A 231 4838 5113 8226 884 -29 -1602 O ATOM 1787 CB ASN A 231 -29.630 19.537 27.895 1.00 46.11 C ANISOU 1787 CB ASN A 231 4430 5377 7715 836 268 -1871 C ATOM 1788 CG ASN A 231 -29.372 18.130 28.395 1.00 47.67 C ANISOU 1788 CG ASN A 231 4651 5764 7696 709 404 -1809 C ATOM 1789 OD1 ASN A 231 -28.244 17.638 28.346 1.00 45.40 O ANISOU 1789 OD1 ASN A 231 4477 5456 7318 618 417 -1684 O ATOM 1790 ND2 ASN A 231 -30.419 17.472 28.879 1.00 46.03 N ANISOU 1790 ND2 ASN A 231 4338 5741 7409 700 502 -1897 N ATOM 1791 N LEU A 232 -28.770 22.736 27.308 1.00 55.08 N ANISOU 1791 N LEU A 232 5665 5990 9272 1025 -53 -1948 N ATOM 1792 CA LEU A 232 -28.751 23.891 26.418 1.00 55.81 C ANISOU 1792 CA LEU A 232 5809 5836 9561 1099 -220 -1897 C ATOM 1793 C LEU A 232 -27.337 24.175 25.922 1.00 56.03 C ANISOU 1793 C LEU A 232 5986 5709 9594 995 -273 -1726 C ATOM 1794 O LEU A 232 -27.139 24.493 24.744 1.00 56.67 O ANISOU 1794 O LEU A 232 6145 5638 9748 977 -371 -1557 O ATOM 1795 CB LEU A 232 -29.338 25.116 27.124 1.00 60.89 C ANISOU 1795 CB LEU A 232 6396 6411 10328 1222 -300 -2102 C ATOM 1796 CG LEU A 232 -30.858 25.313 27.044 1.00 63.71 C ANISOU 1796 CG LEU A 232 6636 6854 10716 1321 -331 -2196 C ATOM 1797 CD1 LEU A 232 -31.592 24.576 28.157 1.00 63.21 C ANISOU 1797 CD1 LEU A 232 6449 7063 10504 1309 -177 -2352 C ATOM 1798 CD2 LEU A 232 -31.213 26.800 27.047 1.00 67.54 C ANISOU 1798 CD2 LEU A 232 7138 7173 11352 1420 -491 -2276 C ATOM 1799 N VAL A 233 -26.342 24.059 26.805 1.00 50.80 N ANISOU 1799 N VAL A 233 5363 5090 8850 921 -208 -1766 N ATOM 1800 CA VAL A 233 -24.952 24.213 26.385 1.00 50.96 C ANISOU 1800 CA VAL A 233 5503 4995 8863 808 -241 -1612 C ATOM 1801 C VAL A 233 -24.519 23.028 25.530 1.00 49.35 C ANISOU 1801 C VAL A 233 5346 4887 8517 695 -173 -1399 C ATOM 1802 O VAL A 233 -23.742 23.180 24.580 1.00 48.29 O ANISOU 1802 O VAL A 233 5300 4641 8406 620 -224 -1225 O ATOM 1803 CB VAL A 233 -24.040 24.389 27.614 1.00 51.40 C ANISOU 1803 CB VAL A 233 5573 5084 8872 768 -198 -1732 C ATOM 1804 CG1 VAL A 233 -22.575 24.453 27.197 1.00 49.31 C ANISOU 1804 CG1 VAL A 233 5412 4728 8595 642 -222 -1578 C ATOM 1805 CG2 VAL A 233 -24.431 25.636 28.394 1.00 51.82 C ANISOU 1805 CG2 VAL A 233 5589 5026 9076 884 -278 -1950 C ATOM 1806 N ALA A 234 -25.022 21.833 25.848 1.00 47.17 N ANISOU 1806 N ALA A 234 5012 4818 8091 678 -58 -1414 N ATOM 1807 CA ALA A 234 -24.587 20.627 25.150 1.00 45.06 C ANISOU 1807 CA ALA A 234 4790 4646 7683 576 6 -1234 C ATOM 1808 C ALA A 234 -24.934 20.686 23.667 1.00 45.06 C ANISOU 1808 C ALA A 234 4824 4555 7742 579 -68 -1071 C ATOM 1809 O ALA A 234 -24.098 20.375 22.810 1.00 45.79 O ANISOU 1809 O ALA A 234 4997 4612 7789 492 -75 -901 O ATOM 1810 CB ALA A 234 -25.211 19.393 25.805 1.00 43.09 C ANISOU 1810 CB ALA A 234 4476 4619 7277 560 129 -1291 C ATOM 1811 N MET A 235 -26.167 21.089 23.341 1.00 47.57 N ANISOU 1811 N MET A 235 5078 4840 8157 682 -128 -1128 N ATOM 1812 CA MET A 235 -26.577 21.126 21.940 1.00 50.87 C ANISOU 1812 CA MET A 235 5531 5177 8621 693 -211 -976 C ATOM 1813 C MET A 235 -25.871 22.240 21.173 1.00 48.92 C ANISOU 1813 C MET A 235 5389 4705 8493 677 -335 -868 C ATOM 1814 O MET A 235 -25.735 22.156 19.948 1.00 50.05 O ANISOU 1814 O MET A 235 5604 4787 8627 636 -387 -692 O ATOM 1815 CB MET A 235 -28.095 21.276 21.833 1.00 53.10 C ANISOU 1815 CB MET A 235 5707 5486 8982 815 -255 -1077 C ATOM 1816 CG MET A 235 -28.625 21.220 20.401 1.00 58.69 C ANISOU 1816 CG MET A 235 6447 6128 9724 833 -348 -927 C ATOM 1817 SD MET A 235 -30.236 21.993 20.174 1.00 75.05 S ANISOU 1817 SD MET A 235 8409 8137 11968 1009 -473 -1054 S ATOM 1818 CE MET A 235 -31.099 21.380 21.617 1.00 61.88 C ANISOU 1818 CE MET A 235 6567 6701 10244 1051 -330 -1295 C ATOM 1819 N LYS A 236 -25.412 23.285 21.863 1.00 52.07 N ANISOU 1819 N LYS A 236 5806 4979 9000 702 -385 -967 N ATOM 1820 CA LYS A 236 -24.670 24.337 21.175 1.00 51.42 C ANISOU 1820 CA LYS A 236 5832 4675 9029 663 -501 -855 C ATOM 1821 C LYS A 236 -23.345 23.812 20.637 1.00 52.51 C ANISOU 1821 C LYS A 236 6056 4840 9054 506 -441 -678 C ATOM 1822 O LYS A 236 -22.937 24.164 19.525 1.00 50.62 O ANISOU 1822 O LYS A 236 5907 4485 8840 444 -508 -505 O ATOM 1823 CB LYS A 236 -24.435 25.528 22.107 1.00 53.30 C ANISOU 1823 CB LYS A 236 6069 4774 9408 716 -567 -1013 C ATOM 1824 CG LYS A 236 -24.228 26.840 21.362 1.00 59.19 C ANISOU 1824 CG LYS A 236 6915 5248 10324 724 -732 -930 C ATOM 1825 CD LYS A 236 -23.456 27.859 22.186 1.00 61.52 C ANISOU 1825 CD LYS A 236 7244 5402 10728 708 -782 -1035 C ATOM 1826 CE LYS A 236 -22.483 28.645 21.314 1.00 60.33 C ANISOU 1826 CE LYS A 236 7230 5041 10651 592 -876 -851 C ATOM 1827 NZ LYS A 236 -21.671 27.755 20.436 1.00 61.32 N ANISOU 1827 NZ LYS A 236 7404 5272 10622 440 -787 -636 N ATOM 1828 N TYR A 237 -22.664 22.961 21.404 1.00 47.71 N ANISOU 1828 N TYR A 237 5420 4390 8317 441 -318 -720 N ATOM 1829 CA TYR A 237 -21.383 22.393 21.005 1.00 45.62 C ANISOU 1829 CA TYR A 237 5214 4174 7947 305 -257 -582 C ATOM 1830 C TYR A 237 -21.522 20.989 20.428 1.00 42.67 C ANISOU 1830 C TYR A 237 4830 3971 7410 267 -169 -483 C ATOM 1831 O TYR A 237 -20.542 20.236 20.407 1.00 41.87 O ANISOU 1831 O TYR A 237 4750 3964 7197 177 -94 -421 O ATOM 1832 CB TYR A 237 -20.419 22.385 22.191 1.00 44.63 C ANISOU 1832 CB TYR A 237 5072 4095 7790 261 -201 -690 C ATOM 1833 CG TYR A 237 -20.021 23.767 22.651 1.00 47.94 C ANISOU 1833 CG TYR A 237 5517 4332 8367 271 -292 -770 C ATOM 1834 CD1 TYR A 237 -19.014 24.470 22.004 1.00 49.90 C ANISOU 1834 CD1 TYR A 237 5842 4437 8681 170 -349 -648 C ATOM 1835 CD2 TYR A 237 -20.652 24.370 23.730 1.00 50.46 C ANISOU 1835 CD2 TYR A 237 5783 4623 8767 376 -322 -971 C ATOM 1836 CE1 TYR A 237 -18.645 25.734 22.419 1.00 52.58 C ANISOU 1836 CE1 TYR A 237 6212 4595 9172 168 -441 -719 C ATOM 1837 CE2 TYR A 237 -20.290 25.634 24.154 1.00 52.60 C ANISOU 1837 CE2 TYR A 237 6083 4716 9189 390 -416 -1055 C ATOM 1838 CZ TYR A 237 -19.286 26.311 23.495 1.00 52.80 C ANISOU 1838 CZ TYR A 237 6192 4585 9286 283 -480 -925 C ATOM 1839 OH TYR A 237 -18.924 27.570 23.915 1.00 55.36 O ANISOU 1839 OH TYR A 237 6550 4717 9766 286 -582 -1007 O ATOM 1840 N ASN A 238 -22.719 20.628 19.959 1.00 46.77 N ANISOU 1840 N ASN A 238 5315 4532 7924 338 -185 -477 N ATOM 1841 CA ASN A 238 -22.979 19.319 19.358 1.00 46.27 C ANISOU 1841 CA ASN A 238 5244 4617 7719 307 -117 -390 C ATOM 1842 C ASN A 238 -22.635 18.187 20.321 1.00 41.95 C ANISOU 1842 C ASN A 238 4659 4245 7037 272 3 -461 C ATOM 1843 O ASN A 238 -22.093 17.152 19.929 1.00 43.02 O ANISOU 1843 O ASN A 238 4822 4478 7047 204 63 -372 O ATOM 1844 CB ASN A 238 -22.234 19.159 18.032 1.00 46.25 C ANISOU 1844 CB ASN A 238 5328 4578 7666 218 -134 -194 C ATOM 1845 CG ASN A 238 -22.921 19.882 16.892 1.00 52.89 C ANISOU 1845 CG ASN A 238 6214 5289 8594 257 -250 -98 C ATOM 1846 OD1 ASN A 238 -24.147 20.003 16.870 1.00 54.84 O ANISOU 1846 OD1 ASN A 238 6412 5527 8900 356 -303 -159 O ATOM 1847 ND2 ASN A 238 -22.137 20.370 15.939 1.00 53.97 N ANISOU 1847 ND2 ASN A 238 6442 5328 8735 175 -293 54 N ATOM 1848 N TYR A 239 -22.935 18.399 21.596 1.00 37.56 N ANISOU 1848 N TYR A 239 4044 3726 6503 321 31 -627 N ATOM 1849 CA TYR A 239 -22.889 17.333 22.578 1.00 34.87 C ANISOU 1849 CA TYR A 239 3669 3554 6028 297 135 -702 C ATOM 1850 C TYR A 239 -24.268 16.710 22.690 1.00 38.09 C ANISOU 1850 C TYR A 239 4002 4069 6400 349 169 -759 C ATOM 1851 O TYR A 239 -25.293 17.385 22.569 1.00 39.98 O ANISOU 1851 O TYR A 239 4184 4258 6747 433 116 -826 O ATOM 1852 CB TYR A 239 -22.438 17.848 23.945 1.00 35.41 C ANISOU 1852 CB TYR A 239 3717 3624 6113 310 153 -852 C ATOM 1853 CG TYR A 239 -20.942 17.847 24.142 1.00 35.07 C ANISOU 1853 CG TYR A 239 3732 3559 6034 230 161 -808 C ATOM 1854 CD1 TYR A 239 -20.102 18.435 23.208 1.00 38.95 C ANISOU 1854 CD1 TYR A 239 4278 3926 6593 179 104 -688 C ATOM 1855 CD2 TYR A 239 -20.370 17.270 25.269 1.00 36.41 C ANISOU 1855 CD2 TYR A 239 3899 3835 6098 202 223 -887 C ATOM 1856 CE1 TYR A 239 -18.734 18.443 23.384 1.00 38.31 C ANISOU 1856 CE1 TYR A 239 4230 3839 6487 102 115 -659 C ATOM 1857 CE2 TYR A 239 -19.001 17.274 25.455 1.00 36.83 C ANISOU 1857 CE2 TYR A 239 3993 3873 6127 137 220 -857 C ATOM 1858 CZ TYR A 239 -18.188 17.863 24.509 1.00 35.09 C ANISOU 1858 CZ TYR A 239 3809 3538 5986 87 169 -749 C ATOM 1859 OH TYR A 239 -16.825 17.871 24.687 1.00 35.51 O ANISOU 1859 OH TYR A 239 3882 3588 6021 17 169 -729 O ATOM 1860 N GLU A 240 -24.275 15.372 22.640 1.00 51.14 N ANISOU 1860 N GLU A 240 5664 5857 7911 293 244 -705 N ATOM 1861 CA GLU A 240 -25.508 14.542 22.715 1.00 50.55 C ANISOU 1861 CA GLU A 240 5523 5905 7780 310 291 -741 C ATOM 1862 C GLU A 240 -26.079 14.809 24.097 1.00 49.79 C ANISOU 1862 C GLU A 240 5349 5882 7685 349 342 -921 C ATOM 1863 O GLU A 240 -25.277 14.804 25.048 1.00 49.11 O ANISOU 1863 O GLU A 240 5294 5823 7543 318 380 -974 O ATOM 1864 CB GLU A 240 -25.105 13.069 22.687 1.00 52.68 C ANISOU 1864 CB GLU A 240 5839 6291 7888 226 362 -660 C ATOM 1865 CG GLU A 240 -25.589 12.311 21.470 1.00 50.90 C ANISOU 1865 CG GLU A 240 5625 6084 7630 207 343 -544 C ATOM 1866 CD GLU A 240 -25.697 10.824 21.749 1.00 54.48 C ANISOU 1866 CD GLU A 240 6095 6667 7937 141 417 -520 C ATOM 1867 OE1 GLU A 240 -24.896 10.325 22.565 1.00 54.51 O ANISOU 1867 OE1 GLU A 240 6143 6717 7851 96 465 -535 O ATOM 1868 OE2 GLU A 240 -26.587 10.176 21.166 1.00 56.84 O ANISOU 1868 OE2 GLU A 240 6366 7015 8215 134 416 -487 O ATOM 1869 N PRO A 241 -27.531 14.997 24.432 1.00 35.60 N ANISOU 1869 N PRO A 241 3436 4152 5939 417 356 -1048 N ATOM 1870 CA PRO A 241 -28.215 15.351 25.674 1.00 35.98 C ANISOU 1870 CA PRO A 241 3391 4286 5994 464 409 -1239 C ATOM 1871 C PRO A 241 -27.946 14.351 26.795 1.00 37.16 C ANISOU 1871 C PRO A 241 3558 4595 5968 378 526 -1275 C ATOM 1872 O PRO A 241 -27.840 13.142 26.572 1.00 39.31 O ANISOU 1872 O PRO A 241 3873 4948 6116 294 574 -1171 O ATOM 1873 CB PRO A 241 -29.697 15.358 25.291 1.00 39.03 C ANISOU 1873 CB PRO A 241 3657 4725 6447 525 400 -1298 C ATOM 1874 CG PRO A 241 -29.717 15.397 23.788 1.00 35.05 C ANISOU 1874 CG PRO A 241 3198 4109 6012 538 303 -1143 C ATOM 1875 CD PRO A 241 -28.495 14.659 23.361 1.00 38.34 C ANISOU 1875 CD PRO A 241 3742 4507 6319 438 320 -980 C ATOM 1876 N LEU A 242 -27.853 14.879 28.011 1.00 38.72 N ANISOU 1876 N LEU A 242 3727 4833 6154 403 562 -1427 N ATOM 1877 CA LEU A 242 -27.658 14.063 29.201 1.00 39.98 C ANISOU 1877 CA LEU A 242 3906 5145 6139 328 666 -1477 C ATOM 1878 C LEU A 242 -29.007 13.761 29.840 1.00 41.90 C ANISOU 1878 C LEU A 242 4031 5554 6334 330 756 -1603 C ATOM 1879 O LEU A 242 -29.826 14.665 30.037 1.00 43.15 O ANISOU 1879 O LEU A 242 4079 5712 6605 424 744 -1752 O ATOM 1880 CB LEU A 242 -26.745 14.773 30.202 1.00 39.39 C ANISOU 1880 CB LEU A 242 3874 5035 6057 344 655 -1574 C ATOM 1881 CG LEU A 242 -25.952 13.859 31.138 1.00 40.09 C ANISOU 1881 CG LEU A 242 4048 5228 5957 252 719 -1550 C ATOM 1882 CD1 LEU A 242 -24.872 13.111 30.370 1.00 40.96 C ANISOU 1882 CD1 LEU A 242 4267 5273 6023 188 680 -1363 C ATOM 1883 CD2 LEU A 242 -25.350 14.656 32.281 1.00 41.00 C ANISOU 1883 CD2 LEU A 242 4176 5336 6066 282 712 -1693 C ATOM 1884 N THR A 243 -29.233 12.492 30.158 1.00 43.72 N ANISOU 1884 N THR A 243 4284 5926 6403 225 845 -1546 N ATOM 1885 CA THR A 243 -30.474 12.036 30.765 1.00 43.41 C ANISOU 1885 CA THR A 243 4135 6065 6293 192 948 -1646 C ATOM 1886 C THR A 243 -30.226 11.611 32.207 1.00 45.94 C ANISOU 1886 C THR A 243 4492 6528 6434 117 1049 -1721 C ATOM 1887 O THR A 243 -29.086 11.529 32.672 1.00 42.87 O ANISOU 1887 O THR A 243 4222 6097 5970 89 1028 -1679 O ATOM 1888 CB THR A 243 -31.077 10.875 29.965 1.00 46.56 C ANISOU 1888 CB THR A 243 4529 6518 6645 112 970 -1516 C ATOM 1889 OG1 THR A 243 -30.264 9.706 30.128 1.00 44.47 O ANISOU 1889 OG1 THR A 243 4403 6274 6221 -3 996 -1378 O ATOM 1890 CG2 THR A 243 -31.151 11.229 28.487 1.00 42.66 C ANISOU 1890 CG2 THR A 243 4027 5877 6304 180 859 -1421 C ATOM 1891 N GLN A 244 -31.323 11.349 32.921 1.00 44.53 N ANISOU 1891 N GLN A 244 4207 6529 6183 80 1157 -1836 N ATOM 1892 CA GLN A 244 -31.209 10.831 34.279 1.00 47.33 C ANISOU 1892 CA GLN A 244 4604 7043 6338 -12 1264 -1894 C ATOM 1893 C GLN A 244 -30.590 9.439 34.289 1.00 45.40 C ANISOU 1893 C GLN A 244 4509 6817 5923 -151 1281 -1708 C ATOM 1894 O GLN A 244 -29.890 9.080 35.243 1.00 45.69 O ANISOU 1894 O GLN A 244 4653 6903 5805 -212 1309 -1701 O ATOM 1895 CB GLN A 244 -32.582 10.824 34.955 1.00 50.18 C ANISOU 1895 CB GLN A 244 4806 7606 6653 -35 1387 -2053 C ATOM 1896 CG GLN A 244 -32.589 10.306 36.386 1.00 52.91 C ANISOU 1896 CG GLN A 244 5207 8124 6772 -146 1492 -2096 C ATOM 1897 CD GLN A 244 -31.696 11.108 37.311 1.00 50.40 C ANISOU 1897 CD GLN A 244 4954 7775 6420 -85 1465 -2200 C ATOM 1898 OE1 GLN A 244 -31.599 12.330 37.198 1.00 53.33 O ANISOU 1898 OE1 GLN A 244 5271 8043 6950 50 1388 -2312 O ATOM 1899 NE2 GLN A 244 -31.036 10.419 38.236 1.00 51.65 N ANISOU 1899 NE2 GLN A 244 5238 8015 6371 -188 1517 -2159 N ATOM 1900 N ASP A 245 -30.833 8.648 33.239 1.00 41.41 N ANISOU 1900 N ASP A 245 4020 6268 5445 -196 1253 -1562 N ATOM 1901 CA ASP A 245 -30.151 7.364 33.105 1.00 40.83 C ANISOU 1901 CA ASP A 245 4100 6176 5239 -307 1242 -1385 C ATOM 1902 C ASP A 245 -28.639 7.549 33.079 1.00 37.23 C ANISOU 1902 C ASP A 245 3780 5586 4781 -268 1152 -1316 C ATOM 1903 O ASP A 245 -27.903 6.800 33.732 1.00 36.41 O ANISOU 1903 O ASP A 245 3803 5506 4525 -341 1158 -1252 O ATOM 1904 CB ASP A 245 -30.621 6.646 31.840 1.00 38.71 C ANISOU 1904 CB ASP A 245 3818 5859 5030 -337 1207 -1257 C ATOM 1905 CG ASP A 245 -32.036 6.116 31.960 1.00 44.97 C ANISOU 1905 CG ASP A 245 4495 6804 5788 -417 1302 -1301 C ATOM 1906 OD1 ASP A 245 -32.571 6.092 33.087 1.00 47.20 O ANISOU 1906 OD1 ASP A 245 4728 7243 5963 -476 1409 -1407 O ATOM 1907 OD2 ASP A 245 -32.612 5.721 30.924 1.00 46.13 O ANISOU 1907 OD2 ASP A 245 4597 6921 6010 -426 1270 -1232 O ATOM 1908 N HIS A 246 -28.158 8.546 32.331 1.00 37.87 N ANISOU 1908 N HIS A 246 3836 5524 5030 -157 1063 -1327 N ATOM 1909 CA HIS A 246 -26.725 8.819 32.285 1.00 35.91 C ANISOU 1909 CA HIS A 246 3694 5156 4794 -125 982 -1274 C ATOM 1910 C HIS A 246 -26.190 9.194 33.661 1.00 37.24 C ANISOU 1910 C HIS A 246 3900 5384 4868 -126 1008 -1385 C ATOM 1911 O HIS A 246 -25.062 8.835 34.017 1.00 36.45 O ANISOU 1911 O HIS A 246 3913 5250 4687 -153 967 -1328 O ATOM 1912 CB HIS A 246 -26.436 9.931 31.277 1.00 35.54 C ANISOU 1912 CB HIS A 246 3602 4953 4946 -20 892 -1275 C ATOM 1913 CG HIS A 246 -26.741 9.558 29.859 1.00 36.01 C ANISOU 1913 CG HIS A 246 3652 4945 5085 -18 849 -1149 C ATOM 1914 ND1 HIS A 246 -27.200 10.469 28.932 1.00 38.21 N ANISOU 1914 ND1 HIS A 246 3855 5132 5533 66 792 -1165 N ATOM 1915 CD2 HIS A 246 -26.650 8.374 29.209 1.00 36.63 C ANISOU 1915 CD2 HIS A 246 3796 5032 5092 -86 847 -1010 C ATOM 1916 CE1 HIS A 246 -27.380 9.862 27.773 1.00 37.06 C ANISOU 1916 CE1 HIS A 246 3725 4949 5405 45 760 -1038 C ATOM 1917 NE2 HIS A 246 -27.054 8.590 27.914 1.00 37.71 N ANISOU 1917 NE2 HIS A 246 3889 5092 5346 -45 794 -948 N ATOM 1918 N VAL A 247 -26.987 9.921 34.448 1.00 34.34 N ANISOU 1918 N VAL A 247 3432 5108 4508 -93 1070 -1555 N ATOM 1919 CA VAL A 247 -26.574 10.269 35.804 1.00 34.57 C ANISOU 1919 CA VAL A 247 3494 5211 4429 -96 1100 -1676 C ATOM 1920 C VAL A 247 -26.461 9.016 36.664 1.00 35.01 C ANISOU 1920 C VAL A 247 3656 5397 4250 -223 1164 -1608 C ATOM 1921 O VAL A 247 -25.495 8.849 37.419 1.00 36.30 O ANISOU 1921 O VAL A 247 3928 5560 4303 -244 1133 -1600 O ATOM 1922 CB VAL A 247 -27.553 11.290 36.413 1.00 36.03 C ANISOU 1922 CB VAL A 247 3538 5480 4671 -28 1159 -1888 C ATOM 1923 CG1 VAL A 247 -27.200 11.569 37.866 1.00 37.95 C ANISOU 1923 CG1 VAL A 247 3819 5825 4776 -39 1201 -2023 C ATOM 1924 CG2 VAL A 247 -27.552 12.576 35.600 1.00 36.92 C ANISOU 1924 CG2 VAL A 247 3571 5433 5022 104 1069 -1949 C ATOM 1925 N ASP A 248 -27.440 8.114 36.560 1.00 36.68 N ANISOU 1925 N ASP A 248 3840 5715 4382 -312 1245 -1556 N ATOM 1926 CA ASP A 248 -27.413 6.892 37.358 1.00 39.34 C ANISOU 1926 CA ASP A 248 4290 6166 4493 -448 1302 -1478 C ATOM 1927 C ASP A 248 -26.251 5.990 36.956 1.00 39.20 C ANISOU 1927 C ASP A 248 4433 6033 4427 -480 1207 -1301 C ATOM 1928 O ASP A 248 -25.657 5.319 37.809 1.00 37.67 O ANISOU 1928 O ASP A 248 4370 5881 4061 -548 1200 -1256 O ATOM 1929 CB ASP A 248 -28.742 6.149 37.224 1.00 41.62 C ANISOU 1929 CB ASP A 248 4505 6580 4727 -547 1405 -1455 C ATOM 1930 CG ASP A 248 -29.913 6.951 37.756 1.00 43.32 C ANISOU 1930 CG ASP A 248 4548 6941 4970 -520 1511 -1648 C ATOM 1931 OD1 ASP A 248 -29.690 7.850 38.595 1.00 46.52 O ANISOU 1931 OD1 ASP A 248 4927 7387 5363 -455 1525 -1801 O ATOM 1932 OD2 ASP A 248 -31.058 6.683 37.335 1.00 45.50 O ANISOU 1932 OD2 ASP A 248 4709 7295 5284 -560 1577 -1659 O ATOM 1933 N ILE A 249 -25.917 5.957 35.664 1.00 36.15 N ANISOU 1933 N ILE A 249 4042 5508 4187 -429 1129 -1204 N ATOM 1934 CA ILE A 249 -24.808 5.125 35.200 1.00 32.95 C ANISOU 1934 CA ILE A 249 3771 4998 3749 -446 1038 -1054 C ATOM 1935 C ILE A 249 -23.493 5.599 35.807 1.00 33.18 C ANISOU 1935 C ILE A 249 3873 4974 3760 -393 966 -1091 C ATOM 1936 O ILE A 249 -22.629 4.790 36.167 1.00 33.48 O ANISOU 1936 O ILE A 249 4042 4996 3684 -430 913 -1010 O ATOM 1937 CB ILE A 249 -24.754 5.117 33.660 1.00 33.56 C ANISOU 1937 CB ILE A 249 3812 4953 3987 -396 978 -964 C ATOM 1938 CG1 ILE A 249 -25.988 4.423 33.082 1.00 35.34 C ANISOU 1938 CG1 ILE A 249 3984 5233 4211 -462 1035 -914 C ATOM 1939 CG2 ILE A 249 -23.493 4.427 33.166 1.00 35.08 C ANISOU 1939 CG2 ILE A 249 4124 5041 4162 -391 884 -840 C ATOM 1940 CD1 ILE A 249 -26.162 4.630 31.592 1.00 32.07 C ANISOU 1940 CD1 ILE A 249 3510 4718 3959 -403 983 -856 C ATOM 1941 N LEU A 250 -23.326 6.914 35.944 1.00 34.35 N ANISOU 1941 N LEU A 250 3939 5091 4023 -305 953 -1217 N ATOM 1942 CA LEU A 250 -22.111 7.487 36.511 1.00 36.50 C ANISOU 1942 CA LEU A 250 4263 5312 4296 -257 881 -1269 C ATOM 1943 C LEU A 250 -22.049 7.377 38.029 1.00 39.27 C ANISOU 1943 C LEU A 250 4674 5784 4462 -300 918 -1356 C ATOM 1944 O LEU A 250 -21.078 7.855 38.625 1.00 42.36 O ANISOU 1944 O LEU A 250 5107 6146 4841 -262 855 -1415 O ATOM 1945 CB LEU A 250 -21.985 8.956 36.098 1.00 35.79 C ANISOU 1945 CB LEU A 250 4069 5129 4401 -157 847 -1374 C ATOM 1946 CG LEU A 250 -21.764 9.225 34.609 1.00 33.76 C ANISOU 1946 CG LEU A 250 3772 4734 4323 -112 789 -1282 C ATOM 1947 CD1 LEU A 250 -22.197 10.637 34.250 1.00 33.86 C ANISOU 1947 CD1 LEU A 250 3673 4676 4517 -29 777 -1389 C ATOM 1948 CD2 LEU A 250 -20.308 8.996 34.234 1.00 30.05 C ANISOU 1948 CD2 LEU A 250 3380 4170 3869 -106 699 -1194 C ATOM 1949 N GLY A 251 -23.055 6.771 38.657 1.00 38.30 N ANISOU 1949 N GLY A 251 4556 5803 4194 -385 1017 -1367 N ATOM 1950 CA GLY A 251 -23.115 6.615 40.093 1.00 39.35 C ANISOU 1950 CA GLY A 251 4752 6073 4126 -442 1066 -1442 C ATOM 1951 C GLY A 251 -21.846 6.093 40.744 1.00 41.10 C ANISOU 1951 C GLY A 251 5131 6266 4221 -458 973 -1382 C ATOM 1952 O GLY A 251 -21.342 6.680 41.707 1.00 41.55 O ANISOU 1952 O GLY A 251 5212 6361 4213 -430 951 -1493 O ATOM 1953 N PRO A 252 -21.316 4.967 40.252 1.00 39.13 N ANISOU 1953 N PRO A 252 4989 5947 3931 -499 907 -1216 N ATOM 1954 CA PRO A 252 -20.063 4.448 40.827 1.00 39.42 C ANISOU 1954 CA PRO A 252 5171 5947 3861 -497 798 -1162 C ATOM 1955 C PRO A 252 -18.901 5.422 40.743 1.00 40.97 C ANISOU 1955 C PRO A 252 5331 6050 4185 -391 701 -1242 C ATOM 1956 O PRO A 252 -18.044 5.425 41.635 1.00 43.12 O ANISOU 1956 O PRO A 252 5687 6339 4358 -381 631 -1278 O ATOM 1957 CB PRO A 252 -19.800 3.183 40.000 1.00 39.57 C ANISOU 1957 CB PRO A 252 5278 5883 3875 -533 740 -983 C ATOM 1958 CG PRO A 252 -21.148 2.747 39.557 1.00 37.69 C ANISOU 1958 CG PRO A 252 4989 5702 3632 -611 849 -939 C ATOM 1959 CD PRO A 252 -21.918 4.010 39.306 1.00 40.37 C ANISOU 1959 CD PRO A 252 5152 6075 4110 -555 930 -1078 C ATOM 1960 N LEU A 253 -18.843 6.251 39.699 1.00 39.73 N ANISOU 1960 N LEU A 253 5055 5795 4246 -317 690 -1268 N ATOM 1961 CA LEU A 253 -17.755 7.216 39.586 1.00 38.81 C ANISOU 1961 CA LEU A 253 4900 5586 4260 -234 603 -1340 C ATOM 1962 C LEU A 253 -17.980 8.421 40.491 1.00 40.06 C ANISOU 1962 C LEU A 253 4997 5797 4426 -200 633 -1523 C ATOM 1963 O LEU A 253 -17.028 8.943 41.082 1.00 38.70 O ANISOU 1963 O LEU A 253 4848 5601 4255 -164 556 -1600 O ATOM 1964 CB LEU A 253 -17.594 7.658 38.132 1.00 35.88 C ANISOU 1964 CB LEU A 253 4439 5089 4105 -184 579 -1288 C ATOM 1965 CG LEU A 253 -17.044 6.591 37.184 1.00 32.36 C ANISOU 1965 CG LEU A 253 4049 4578 3668 -198 526 -1128 C ATOM 1966 CD1 LEU A 253 -16.915 7.138 35.772 1.00 31.87 C ANISOU 1966 CD1 LEU A 253 3896 4408 3805 -154 513 -1088 C ATOM 1967 CD2 LEU A 253 -15.707 6.070 37.687 1.00 32.51 C ANISOU 1967 CD2 LEU A 253 4163 4580 3611 -187 421 -1103 C ATOM 1968 N SER A 254 -19.229 8.878 40.609 1.00 41.28 N ANISOU 1968 N SER A 254 5067 6024 4592 -205 738 -1607 N ATOM 1969 CA SER A 254 -19.525 9.986 41.510 1.00 42.87 C ANISOU 1969 CA SER A 254 5208 6285 4795 -165 770 -1801 C ATOM 1970 C SER A 254 -19.366 9.581 42.969 1.00 43.38 C ANISOU 1970 C SER A 254 5375 6488 4619 -216 785 -1859 C ATOM 1971 O SER A 254 -18.971 10.406 43.800 1.00 45.92 O ANISOU 1971 O SER A 254 5691 6831 4925 -174 755 -2008 O ATOM 1972 CB SER A 254 -20.940 10.507 41.256 1.00 40.96 C ANISOU 1972 CB SER A 254 4840 6097 4625 -149 878 -1886 C ATOM 1973 OG SER A 254 -21.908 9.515 41.550 1.00 43.51 O ANISOU 1973 OG SER A 254 5186 6560 4785 -241 982 -1830 O ATOM 1974 N ALA A 255 -19.663 8.322 43.298 1.00 39.18 N ANISOU 1974 N ALA A 255 4945 6047 3895 -311 824 -1742 N ATOM 1975 CA ALA A 255 -19.523 7.866 44.677 1.00 42.27 C ANISOU 1975 CA ALA A 255 5454 6571 4035 -374 833 -1775 C ATOM 1976 C ALA A 255 -18.057 7.736 45.072 1.00 43.25 C ANISOU 1976 C ALA A 255 5688 6626 4121 -342 686 -1749 C ATOM 1977 O ALA A 255 -17.688 8.033 46.214 1.00 44.92 O ANISOU 1977 O ALA A 255 5956 6913 4198 -340 659 -1853 O ATOM 1978 CB ALA A 255 -20.250 6.535 44.866 1.00 42.86 C ANISOU 1978 CB ALA A 255 5621 6746 3920 -498 908 -1638 C ATOM 1979 N GLN A 256 -17.207 7.294 44.142 1.00 57.51 N ANISOU 1979 N GLN A 256 7517 8294 6041 -314 588 -1622 N ATOM 1980 CA GLN A 256 -15.791 7.130 44.453 1.00 57.80 C ANISOU 1980 CA GLN A 256 7637 8268 6056 -277 442 -1602 C ATOM 1981 C GLN A 256 -15.108 8.477 44.660 1.00 55.40 C ANISOU 1981 C GLN A 256 7249 7913 5887 -196 384 -1764 C ATOM 1982 O GLN A 256 -14.259 8.619 45.547 1.00 58.52 O ANISOU 1982 O GLN A 256 7708 8330 6196 -179 295 -1830 O ATOM 1983 CB GLN A 256 -15.098 6.342 43.341 1.00 55.00 C ANISOU 1983 CB GLN A 256 7306 7791 5800 -262 362 -1443 C ATOM 1984 CG GLN A 256 -13.617 6.097 43.580 1.00 57.02 C ANISOU 1984 CG GLN A 256 7631 7986 6047 -217 206 -1426 C ATOM 1985 CD GLN A 256 -12.941 5.413 42.408 1.00 56.76 C ANISOU 1985 CD GLN A 256 7594 7841 6130 -189 137 -1296 C ATOM 1986 OE1 GLN A 256 -13.594 5.022 41.440 1.00 54.45 O ANISOU 1986 OE1 GLN A 256 7267 7516 5904 -210 201 -1205 O ATOM 1987 NE2 GLN A 256 -11.623 5.266 42.488 1.00 52.84 N ANISOU 1987 NE2 GLN A 256 7125 7293 5658 -138 2 -1295 N ATOM 1988 N THR A 257 -15.468 9.477 43.856 1.00 40.16 N ANISOU 1988 N THR A 257 5180 5908 4169 -148 425 -1827 N ATOM 1989 CA THR A 257 -14.843 10.789 43.942 1.00 43.21 C ANISOU 1989 CA THR A 257 5488 6220 4708 -79 364 -1971 C ATOM 1990 C THR A 257 -15.587 11.752 44.856 1.00 45.07 C ANISOU 1990 C THR A 257 5677 6542 4907 -60 430 -2166 C ATOM 1991 O THR A 257 -15.022 12.785 45.232 1.00 44.43 O ANISOU 1991 O THR A 257 5558 6412 4911 -9 366 -2306 O ATOM 1992 CB THR A 257 -14.732 11.416 42.548 1.00 40.30 C ANISOU 1992 CB THR A 257 5009 5703 4599 -39 352 -1929 C ATOM 1993 OG1 THR A 257 -16.043 11.595 41.999 1.00 39.06 O ANISOU 1993 OG1 THR A 257 4778 5562 4499 -41 463 -1927 O ATOM 1994 CG2 THR A 257 -13.920 10.523 41.624 1.00 40.02 C ANISOU 1994 CG2 THR A 257 5010 5594 4603 -52 289 -1757 C ATOM 1995 N GLY A 258 -16.830 11.445 45.220 1.00 47.46 N ANISOU 1995 N GLY A 258 5974 6972 5087 -100 555 -2186 N ATOM 1996 CA GLY A 258 -17.612 12.370 46.014 1.00 47.95 C ANISOU 1996 CA GLY A 258 5971 7127 5122 -72 630 -2388 C ATOM 1997 C GLY A 258 -18.043 13.614 45.274 1.00 48.19 C ANISOU 1997 C GLY A 258 5857 7048 5406 10 640 -2493 C ATOM 1998 O GLY A 258 -18.400 14.610 45.908 1.00 52.18 O ANISOU 1998 O GLY A 258 6303 7587 5937 62 660 -2691 O ATOM 1999 N ILE A 259 -18.021 13.584 43.944 1.00 45.62 N ANISOU 1999 N ILE A 259 5479 6588 5266 25 621 -2368 N ATOM 2000 CA ILE A 259 -18.370 14.727 43.109 1.00 45.10 C ANISOU 2000 CA ILE A 259 5294 6392 5449 99 610 -2436 C ATOM 2001 C ILE A 259 -19.626 14.358 42.333 1.00 48.14 C ANISOU 2001 C ILE A 259 5611 6810 5871 88 709 -2368 C ATOM 2002 O ILE A 259 -19.597 13.452 41.489 1.00 45.59 O ANISOU 2002 O ILE A 259 5316 6460 5545 43 714 -2186 O ATOM 2003 CB ILE A 259 -17.228 15.115 42.162 1.00 45.38 C ANISOU 2003 CB ILE A 259 5328 6241 5675 120 494 -2349 C ATOM 2004 CG1 ILE A 259 -15.950 15.385 42.957 1.00 46.46 C ANISOU 2004 CG1 ILE A 259 5524 6358 5770 121 391 -2417 C ATOM 2005 CG2 ILE A 259 -17.613 16.328 41.328 1.00 43.08 C ANISOU 2005 CG2 ILE A 259 4932 5805 5632 187 474 -2409 C ATOM 2006 CD1 ILE A 259 -14.725 15.562 42.095 1.00 45.42 C ANISOU 2006 CD1 ILE A 259 5389 6074 5795 118 286 -2319 C ATOM 2007 N ALA A 260 -20.725 15.054 42.615 1.00 45.24 N ANISOU 2007 N ALA A 260 5146 6503 5541 135 783 -2523 N ATOM 2008 CA ALA A 260 -21.991 14.766 41.958 1.00 43.48 C ANISOU 2008 CA ALA A 260 4839 6326 5356 131 875 -2485 C ATOM 2009 C ALA A 260 -21.888 15.010 40.454 1.00 42.05 C ANISOU 2009 C ALA A 260 4615 5965 5397 167 812 -2359 C ATOM 2010 O ALA A 260 -21.037 15.765 39.974 1.00 42.81 O ANISOU 2010 O ALA A 260 4716 5898 5650 211 710 -2353 O ATOM 2011 CB ALA A 260 -23.110 15.618 42.556 1.00 43.76 C ANISOU 2011 CB ALA A 260 4757 6454 5414 196 951 -2707 C ATOM 2012 N VAL A 261 -22.775 14.350 39.706 1.00 43.44 N ANISOU 2012 N VAL A 261 4750 6178 5578 137 875 -2257 N ATOM 2013 CA VAL A 261 -22.748 14.454 38.249 1.00 42.78 C ANISOU 2013 CA VAL A 261 4636 5942 5675 163 821 -2125 C ATOM 2014 C VAL A 261 -23.040 15.882 37.806 1.00 43.14 C ANISOU 2014 C VAL A 261 4589 5856 5947 270 764 -2242 C ATOM 2015 O VAL A 261 -22.380 16.416 36.906 1.00 41.91 O ANISOU 2015 O VAL A 261 4446 5526 5950 297 671 -2166 O ATOM 2016 CB VAL A 261 -23.734 13.451 37.621 1.00 42.08 C ANISOU 2016 CB VAL A 261 4519 5933 5535 110 898 -2011 C ATOM 2017 CG1 VAL A 261 -23.892 13.718 36.133 1.00 40.19 C ANISOU 2017 CG1 VAL A 261 4235 5548 5487 151 841 -1906 C ATOM 2018 CG2 VAL A 261 -23.253 12.031 37.850 1.00 41.32 C ANISOU 2018 CG2 VAL A 261 4540 5914 5247 3 920 -1863 C ATOM 2019 N LEU A 262 -24.029 16.526 38.432 1.00 43.06 N ANISOU 2019 N LEU A 262 4485 5924 5953 331 817 -2431 N ATOM 2020 CA LEU A 262 -24.360 17.897 38.060 1.00 46.47 C ANISOU 2020 CA LEU A 262 4833 6218 6607 446 748 -2557 C ATOM 2021 C LEU A 262 -23.224 18.859 38.384 1.00 42.43 C ANISOU 2021 C LEU A 262 4374 5564 6182 480 642 -2625 C ATOM 2022 O LEU A 262 -23.072 19.887 37.713 1.00 45.22 O ANISOU 2022 O LEU A 262 4705 5733 6745 548 546 -2642 O ATOM 2023 CB LEU A 262 -25.652 18.333 38.751 1.00 46.27 C ANISOU 2023 CB LEU A 262 4687 6323 6571 512 827 -2765 C ATOM 2024 CG LEU A 262 -26.928 17.681 38.211 1.00 47.70 C ANISOU 2024 CG LEU A 262 4779 6610 6736 494 908 -2709 C ATOM 2025 CD1 LEU A 262 -28.162 18.237 38.907 1.00 53.66 C ANISOU 2025 CD1 LEU A 262 5428 7479 7483 539 939 -2850 C ATOM 2026 CD2 LEU A 262 -27.028 17.865 36.704 1.00 44.84 C ANISOU 2026 CD2 LEU A 262 4396 6076 6566 535 828 -2579 C ATOM 2027 N ASP A 263 -22.417 18.549 39.402 1.00 45.10 N ANISOU 2027 N ASP A 263 4788 5982 6365 430 650 -2662 N ATOM 2028 CA ASP A 263 -21.231 19.354 39.674 1.00 45.06 C ANISOU 2028 CA ASP A 263 4836 5846 6440 446 542 -2713 C ATOM 2029 C ASP A 263 -20.216 19.219 38.545 1.00 44.97 C ANISOU 2029 C ASP A 263 4879 5674 6534 402 459 -2512 C ATOM 2030 O ASP A 263 -19.667 20.218 38.065 1.00 46.18 O ANISOU 2030 O ASP A 263 5029 5648 6871 433 361 -2525 O ATOM 2031 CB ASP A 263 -20.614 18.945 41.015 1.00 46.23 C ANISOU 2031 CB ASP A 263 5053 6130 6380 401 564 -2792 C ATOM 2032 CG ASP A 263 -19.613 19.966 41.543 1.00 53.53 C ANISOU 2032 CG ASP A 263 6006 6943 7389 434 457 -2916 C ATOM 2033 OD1 ASP A 263 -19.534 20.137 42.778 1.00 56.44 O ANISOU 2033 OD1 ASP A 263 6394 7419 7630 442 470 -3069 O ATOM 2034 OD2 ASP A 263 -18.896 20.588 40.734 1.00 55.08 O ANISOU 2034 OD2 ASP A 263 6208 6948 7770 441 357 -2849 O ATOM 2035 N MET A 264 -19.956 17.985 38.105 1.00 44.41 N ANISOU 2035 N MET A 264 4859 5668 6347 324 496 -2329 N ATOM 2036 CA MET A 264 -19.009 17.774 37.015 1.00 40.66 C ANISOU 2036 CA MET A 264 4425 5067 5956 282 430 -2147 C ATOM 2037 C MET A 264 -19.486 18.422 35.723 1.00 38.48 C ANISOU 2037 C MET A 264 4099 4644 5879 321 394 -2080 C ATOM 2038 O MET A 264 -18.664 18.870 34.914 1.00 40.27 O ANISOU 2038 O MET A 264 4346 4724 6230 303 318 -1989 O ATOM 2039 CB MET A 264 -18.777 16.277 36.803 1.00 41.46 C ANISOU 2039 CB MET A 264 4587 5272 5892 206 477 -1982 C ATOM 2040 CG MET A 264 -17.628 15.959 35.862 1.00 37.49 C ANISOU 2040 CG MET A 264 4127 4671 5445 163 414 -1819 C ATOM 2041 SD MET A 264 -16.023 16.358 36.580 1.00 38.80 S ANISOU 2041 SD MET A 264 4339 4794 5609 143 323 -1877 S ATOM 2042 CE MET A 264 -15.863 15.052 37.794 1.00 36.60 C ANISOU 2042 CE MET A 264 4140 4701 5064 104 363 -1883 C ATOM 2043 N CYS A 265 -20.803 18.486 35.513 1.00 41.15 N ANISOU 2043 N CYS A 265 4369 5023 6245 371 445 -2123 N ATOM 2044 CA CYS A 265 -21.329 19.109 34.303 1.00 42.72 C ANISOU 2044 CA CYS A 265 4523 5080 6627 418 396 -2063 C ATOM 2045 C CYS A 265 -21.038 20.603 34.266 1.00 43.24 C ANISOU 2045 C CYS A 265 4577 4963 6889 482 293 -2165 C ATOM 2046 O CYS A 265 -20.854 21.170 33.183 1.00 42.21 O ANISOU 2046 O CYS A 265 4458 4667 6913 488 216 -2065 O ATOM 2047 CB CYS A 265 -22.831 18.857 34.195 1.00 44.02 C ANISOU 2047 CB CYS A 265 4604 5342 6779 465 466 -2111 C ATOM 2048 SG CYS A 265 -23.260 17.285 33.426 1.00 43.72 S ANISOU 2048 SG CYS A 265 4582 5420 6611 386 544 -1915 S ATOM 2049 N ALA A 266 -20.999 21.257 35.429 1.00 46.39 N ANISOU 2049 N ALA A 266 4960 5386 7280 526 284 -2364 N ATOM 2050 CA ALA A 266 -20.600 22.659 35.466 1.00 45.36 C ANISOU 2050 CA ALA A 266 4832 5068 7337 579 173 -2468 C ATOM 2051 C ALA A 266 -19.138 22.828 35.076 1.00 45.93 C ANISOU 2051 C ALA A 266 4977 5017 7456 495 98 -2349 C ATOM 2052 O ALA A 266 -18.777 23.830 34.448 1.00 45.00 O ANISOU 2052 O ALA A 266 4875 4701 7523 502 -1 -2325 O ATOM 2053 CB ALA A 266 -20.854 23.245 36.853 1.00 48.39 C ANISOU 2053 CB ALA A 266 5183 5518 7684 644 183 -2721 C ATOM 2054 N SER A 267 -18.287 21.865 35.439 1.00 51.71 N ANISOU 2054 N SER A 267 5755 5865 8028 413 139 -2276 N ATOM 2055 CA SER A 267 -16.898 21.903 34.994 1.00 50.51 C ANISOU 2055 CA SER A 267 5653 5621 7917 331 78 -2161 C ATOM 2056 C SER A 267 -16.800 21.692 33.489 1.00 49.86 C ANISOU 2056 C SER A 267 5582 5450 7914 288 66 -1951 C ATOM 2057 O SER A 267 -16.017 22.368 32.811 1.00 51.43 O ANISOU 2057 O SER A 267 5800 5497 8243 243 -7 -1879 O ATOM 2058 CB SER A 267 -16.079 20.849 35.740 1.00 49.86 C ANISOU 2058 CB SER A 267 5610 5693 7642 271 117 -2140 C ATOM 2059 OG SER A 267 -16.111 21.072 37.139 1.00 54.04 O ANISOU 2059 OG SER A 267 6142 6307 8085 304 120 -2331 O ATOM 2060 N LEU A 268 -17.590 20.760 32.948 1.00 39.86 N ANISOU 2060 N LEU A 268 4303 4279 6562 293 138 -1852 N ATOM 2061 CA LEU A 268 -17.607 20.546 31.505 1.00 37.93 C ANISOU 2061 CA LEU A 268 4070 3961 6379 259 128 -1663 C ATOM 2062 C LEU A 268 -18.181 21.749 30.769 1.00 39.52 C ANISOU 2062 C LEU A 268 4256 3982 6777 311 52 -1668 C ATOM 2063 O LEU A 268 -17.735 22.069 29.661 1.00 41.60 O ANISOU 2063 O LEU A 268 4551 4123 7133 265 2 -1526 O ATOM 2064 CB LEU A 268 -18.406 19.285 31.173 1.00 38.27 C ANISOU 2064 CB LEU A 268 4104 4148 6288 257 214 -1576 C ATOM 2065 CG LEU A 268 -18.554 18.926 29.693 1.00 37.87 C ANISOU 2065 CG LEU A 268 4065 4047 6276 229 209 -1390 C ATOM 2066 CD1 LEU A 268 -17.189 18.779 29.040 1.00 38.01 C ANISOU 2066 CD1 LEU A 268 4129 4014 6301 145 181 -1260 C ATOM 2067 CD2 LEU A 268 -19.372 17.655 29.528 1.00 35.04 C ANISOU 2067 CD2 LEU A 268 3697 3835 5782 226 291 -1331 C ATOM 2068 N LYS A 269 -19.168 22.422 31.366 1.00 48.16 N ANISOU 2068 N LYS A 269 5305 5061 7934 408 38 -1833 N ATOM 2069 CA LYS A 269 -19.703 23.645 30.779 1.00 49.35 C ANISOU 2069 CA LYS A 269 5446 5020 8284 476 -58 -1860 C ATOM 2070 C LYS A 269 -18.619 24.707 30.640 1.00 49.45 C ANISOU 2070 C LYS A 269 5512 4842 8436 427 -161 -1849 C ATOM 2071 O LYS A 269 -18.520 25.374 29.604 1.00 51.78 O ANISOU 2071 O LYS A 269 5843 4963 8868 408 -240 -1736 O ATOM 2072 CB LYS A 269 -20.861 24.163 31.633 1.00 52.03 C ANISOU 2072 CB LYS A 269 5715 5393 8660 599 -54 -2078 C ATOM 2073 CG LYS A 269 -21.392 25.530 31.236 1.00 53.77 C ANISOU 2073 CG LYS A 269 5926 5402 9102 693 -175 -2149 C ATOM 2074 CD LYS A 269 -22.724 25.803 31.920 1.00 56.15 C ANISOU 2074 CD LYS A 269 6133 5777 9426 829 -154 -2360 C ATOM 2075 CE LYS A 269 -22.931 27.287 32.174 1.00 61.80 C ANISOU 2075 CE LYS A 269 6850 6334 10298 907 -283 -2471 C ATOM 2076 NZ LYS A 269 -23.311 28.011 30.930 1.00 61.39 N ANISOU 2076 NZ LYS A 269 6828 6081 10417 943 -403 -2351 N ATOM 2077 N GLU A 270 -17.789 24.867 31.673 1.00 49.92 N ANISOU 2077 N GLU A 270 5579 4931 8457 399 -164 -1962 N ATOM 2078 CA GLU A 270 -16.705 25.843 31.615 1.00 52.96 C ANISOU 2078 CA GLU A 270 6007 5143 8973 338 -260 -1962 C ATOM 2079 C GLU A 270 -15.661 25.451 30.578 1.00 52.38 C ANISOU 2079 C GLU A 270 5973 5041 8890 210 -257 -1744 C ATOM 2080 O GLU A 270 -15.123 26.316 29.875 1.00 50.67 O ANISOU 2080 O GLU A 270 5794 4642 8816 150 -338 -1664 O ATOM 2081 CB GLU A 270 -16.061 25.984 32.994 1.00 52.21 C ANISOU 2081 CB GLU A 270 5904 5112 8821 335 -262 -2140 C ATOM 2082 CG GLU A 270 -15.294 27.277 33.201 1.00 57.61 C ANISOU 2082 CG GLU A 270 6616 5597 9676 308 -380 -2218 C ATOM 2083 CD GLU A 270 -16.116 28.331 33.915 1.00 63.69 C ANISOU 2083 CD GLU A 270 7368 6271 10560 430 -447 -2438 C ATOM 2084 OE1 GLU A 270 -17.054 28.879 33.299 1.00 63.92 O ANISOU 2084 OE1 GLU A 270 7392 6208 10688 502 -488 -2406 O ATOM 2085 OE2 GLU A 270 -15.826 28.608 35.098 1.00 66.70 O ANISOU 2085 OE2 GLU A 270 7738 6726 10878 449 -457 -2589 O ATOM 2086 N LEU A 271 -15.360 24.154 30.470 1.00 42.44 N ANISOU 2086 N LEU A 271 4707 3958 7461 163 -164 -1648 N ATOM 2087 CA LEU A 271 -14.347 23.704 29.521 1.00 41.14 C ANISOU 2087 CA LEU A 271 4566 3792 7274 50 -152 -1462 C ATOM 2088 C LEU A 271 -14.794 23.928 28.081 1.00 42.22 C ANISOU 2088 C LEU A 271 4729 3824 7489 33 -173 -1294 C ATOM 2089 O LEU A 271 -13.972 24.244 27.212 1.00 44.90 O ANISOU 2089 O LEU A 271 5098 4075 7887 -65 -201 -1161 O ATOM 2090 CB LEU A 271 -14.024 22.230 29.759 1.00 40.06 C ANISOU 2090 CB LEU A 271 4418 3862 6940 25 -59 -1416 C ATOM 2091 CG LEU A 271 -13.297 21.899 31.063 1.00 41.16 C ANISOU 2091 CG LEU A 271 4548 4108 6984 19 -51 -1544 C ATOM 2092 CD1 LEU A 271 -13.159 20.395 31.233 1.00 37.70 C ANISOU 2092 CD1 LEU A 271 4114 3857 6353 8 27 -1485 C ATOM 2093 CD2 LEU A 271 -11.934 22.574 31.105 1.00 41.87 C ANISOU 2093 CD2 LEU A 271 4637 4108 7163 -65 -116 -1550 C ATOM 2094 N LEU A 272 -16.090 23.765 27.809 1.00 40.27 N ANISOU 2094 N LEU A 272 4470 3593 7237 122 -159 -1297 N ATOM 2095 CA LEU A 272 -16.589 23.975 26.454 1.00 41.58 C ANISOU 2095 CA LEU A 272 4667 3662 7471 117 -192 -1142 C ATOM 2096 C LEU A 272 -16.647 25.457 26.106 1.00 46.29 C ANISOU 2096 C LEU A 272 5304 4018 8267 125 -315 -1149 C ATOM 2097 O LEU A 272 -16.398 25.842 24.958 1.00 44.31 O ANISOU 2097 O LEU A 272 5107 3649 8081 59 -362 -986 O ATOM 2098 CB LEU A 272 -17.966 23.335 26.298 1.00 42.85 C ANISOU 2098 CB LEU A 272 4792 3918 7572 212 -150 -1154 C ATOM 2099 CG LEU A 272 -17.959 21.807 26.315 1.00 41.34 C ANISOU 2099 CG LEU A 272 4582 3937 7190 184 -39 -1095 C ATOM 2100 CD1 LEU A 272 -19.307 21.246 26.752 1.00 41.24 C ANISOU 2100 CD1 LEU A 272 4515 4041 7114 276 12 -1184 C ATOM 2101 CD2 LEU A 272 -17.561 21.288 24.948 1.00 41.46 C ANISOU 2101 CD2 LEU A 272 4636 3949 7169 108 -28 -889 C ATOM 2102 N GLN A 273 -16.974 26.304 27.082 1.00 49.98 N ANISOU 2102 N GLN A 273 5753 4409 8830 205 -373 -1338 N ATOM 2103 CA GLN A 273 -17.118 27.730 26.817 1.00 53.68 C ANISOU 2103 CA GLN A 273 6267 4629 9501 229 -506 -1362 C ATOM 2104 C GLN A 273 -15.779 28.457 26.813 1.00 53.84 C ANISOU 2104 C GLN A 273 6335 4519 9602 102 -562 -1324 C ATOM 2105 O GLN A 273 -15.627 29.456 26.103 1.00 56.43 O ANISOU 2105 O GLN A 273 6731 4633 10080 58 -666 -1240 O ATOM 2106 CB GLN A 273 -18.051 28.368 27.849 1.00 54.93 C ANISOU 2106 CB GLN A 273 6380 4753 9737 377 -552 -1599 C ATOM 2107 CG GLN A 273 -19.499 27.910 27.755 1.00 54.77 C ANISOU 2107 CG GLN A 273 6300 4829 9680 506 -517 -1647 C ATOM 2108 CD GLN A 273 -20.351 28.441 28.892 1.00 55.54 C ANISOU 2108 CD GLN A 273 6332 4938 9832 649 -538 -1907 C ATOM 2109 OE1 GLN A 273 -21.578 28.483 28.799 1.00 59.28 O ANISOU 2109 OE1 GLN A 273 6750 5432 10341 769 -547 -1978 O ATOM 2110 NE2 GLN A 273 -19.701 28.852 29.975 1.00 54.43 N ANISOU 2110 NE2 GLN A 273 6190 4793 9697 638 -546 -2061 N ATOM 2111 N ASN A 274 -14.803 27.980 27.587 1.00 60.04 N ANISOU 2111 N ASN A 274 7089 5426 10296 36 -502 -1382 N ATOM 2112 CA ASN A 274 -13.527 28.666 27.723 1.00 61.07 C ANISOU 2112 CA ASN A 274 7245 5450 10508 -85 -555 -1376 C ATOM 2113 C ASN A 274 -12.337 27.888 27.182 1.00 62.53 C ANISOU 2113 C ASN A 274 7419 5748 10589 -229 -480 -1224 C ATOM 2114 O ASN A 274 -11.227 28.433 27.166 1.00 62.64 O ANISOU 2114 O ASN A 274 7443 5685 10675 -348 -517 -1203 O ATOM 2115 CB ASN A 274 -13.259 29.009 29.197 1.00 61.60 C ANISOU 2115 CB ASN A 274 7279 5540 10588 -38 -578 -1608 C ATOM 2116 CG ASN A 274 -14.367 29.839 29.812 1.00 66.52 C ANISOU 2116 CG ASN A 274 7901 6056 11317 110 -652 -1791 C ATOM 2117 OD1 ASN A 274 -14.847 29.541 30.906 1.00 65.84 O ANISOU 2117 OD1 ASN A 274 7766 6097 11152 208 -612 -1974 O ATOM 2118 ND2 ASN A 274 -14.780 30.889 29.112 1.00 65.25 N ANISOU 2118 ND2 ASN A 274 7794 5681 11316 128 -760 -1734 N ATOM 2119 N GLY A 275 -12.523 26.650 26.738 1.00 54.54 N ANISOU 2119 N GLY A 275 6384 4917 9420 -223 -379 -1127 N ATOM 2120 CA GLY A 275 -11.389 25.857 26.312 1.00 53.07 C ANISOU 2120 CA GLY A 275 6176 4853 9134 -340 -309 -1013 C ATOM 2121 C GLY A 275 -10.547 25.411 27.498 1.00 52.75 C ANISOU 2121 C GLY A 275 6084 4939 9019 -349 -282 -1148 C ATOM 2122 O GLY A 275 -10.926 25.542 28.663 1.00 51.80 O ANISOU 2122 O GLY A 275 5950 4842 8889 -262 -301 -1323 O ATOM 2123 N MET A 276 -9.370 24.876 27.175 1.00 55.54 N ANISOU 2123 N MET A 276 6408 5382 9315 -455 -240 -1069 N ATOM 2124 CA MET A 276 -8.458 24.368 28.190 1.00 54.84 C ANISOU 2124 CA MET A 276 6267 5418 9150 -467 -226 -1181 C ATOM 2125 C MET A 276 -7.368 25.358 28.577 1.00 59.23 C ANISOU 2125 C MET A 276 6802 5869 9832 -564 -300 -1248 C ATOM 2126 O MET A 276 -6.620 25.088 29.523 1.00 55.31 O ANISOU 2126 O MET A 276 6263 5462 9291 -567 -310 -1363 O ATOM 2127 CB MET A 276 -7.815 23.058 27.720 1.00 55.72 C ANISOU 2127 CB MET A 276 6342 5711 9118 -504 -144 -1082 C ATOM 2128 CG MET A 276 -8.395 21.824 28.390 1.00 54.08 C ANISOU 2128 CG MET A 276 6133 5670 8743 -398 -90 -1136 C ATOM 2129 SD MET A 276 -7.762 20.284 27.705 1.00 54.11 S ANISOU 2129 SD MET A 276 6110 5855 8595 -426 -10 -1015 S ATOM 2130 CE MET A 276 -9.292 19.404 27.402 1.00 49.20 C ANISOU 2130 CE MET A 276 5535 5295 7865 -326 47 -961 C ATOM 2131 N ASN A 277 -7.260 26.487 27.872 1.00 59.70 N ANISOU 2131 N ASN A 277 6896 5739 10049 -647 -358 -1176 N ATOM 2132 CA ASN A 277 -6.329 27.563 28.218 1.00 61.01 C ANISOU 2132 CA ASN A 277 7051 5772 10357 -750 -439 -1240 C ATOM 2133 C ASN A 277 -4.878 27.087 28.252 1.00 60.57 C ANISOU 2133 C ASN A 277 6915 5842 10258 -867 -405 -1226 C ATOM 2134 O ASN A 277 -4.056 27.622 29.000 1.00 63.28 O ANISOU 2134 O ASN A 277 7221 6150 10672 -920 -465 -1341 O ATOM 2135 CB ASN A 277 -6.707 28.212 29.554 1.00 63.74 C ANISOU 2135 CB ASN A 277 7408 6047 10762 -655 -519 -1458 C ATOM 2136 CG ASN A 277 -7.338 29.580 29.380 1.00 69.28 C ANISOU 2136 CG ASN A 277 8179 6497 11648 -642 -622 -1482 C ATOM 2137 OD1 ASN A 277 -8.084 29.814 28.428 1.00 69.65 O ANISOU 2137 OD1 ASN A 277 8280 6447 11738 -630 -626 -1355 O ATOM 2138 ND2 ASN A 277 -7.046 30.489 30.302 1.00 70.84 N ANISOU 2138 ND2 ASN A 277 8379 6581 11956 -641 -716 -1650 N ATOM 2139 N GLY A 278 -4.547 26.083 27.442 1.00 52.14 N ANISOU 2139 N GLY A 278 5813 4923 9077 -903 -313 -1094 N ATOM 2140 CA GLY A 278 -3.185 25.605 27.337 1.00 53.35 C ANISOU 2140 CA GLY A 278 5874 5203 9193 -1007 -278 -1079 C ATOM 2141 C GLY A 278 -2.825 24.448 28.243 1.00 49.17 C ANISOU 2141 C GLY A 278 5288 4871 8523 -919 -253 -1187 C ATOM 2142 O GLY A 278 -1.686 23.968 28.179 1.00 50.32 O ANISOU 2142 O GLY A 278 5347 5133 8637 -986 -231 -1187 O ATOM 2143 N ARG A 279 -3.746 23.985 29.084 1.00 50.73 N ANISOU 2143 N ARG A 279 5530 5113 8634 -774 -258 -1279 N ATOM 2144 CA ARG A 279 -3.468 22.881 29.987 1.00 49.36 C ANISOU 2144 CA ARG A 279 5326 5115 8315 -693 -245 -1371 C ATOM 2145 C ARG A 279 -3.924 21.561 29.369 1.00 46.04 C ANISOU 2145 C ARG A 279 4917 4829 7745 -634 -160 -1261 C ATOM 2146 O ARG A 279 -4.458 21.513 28.259 1.00 46.27 O ANISOU 2146 O ARG A 279 4974 4824 7781 -654 -109 -1124 O ATOM 2147 CB ARG A 279 -4.137 23.119 31.339 1.00 50.80 C ANISOU 2147 CB ARG A 279 5551 5280 8470 -586 -298 -1539 C ATOM 2148 CG ARG A 279 -3.328 23.992 32.279 1.00 53.27 C ANISOU 2148 CG ARG A 279 5832 5530 8876 -628 -391 -1691 C ATOM 2149 CD ARG A 279 -4.168 24.443 33.456 1.00 53.14 C ANISOU 2149 CD ARG A 279 5870 5473 8848 -524 -438 -1857 C ATOM 2150 NE ARG A 279 -5.324 25.227 33.032 1.00 53.69 N ANISOU 2150 NE ARG A 279 5995 5394 9009 -487 -438 -1834 N ATOM 2151 CZ ARG A 279 -6.230 25.729 33.863 1.00 56.94 C ANISOU 2151 CZ ARG A 279 6447 5757 9430 -390 -470 -1975 C ATOM 2152 NH1 ARG A 279 -6.121 25.526 35.169 1.00 54.80 N ANISOU 2152 NH1 ARG A 279 6175 5578 9067 -329 -498 -2143 N ATOM 2153 NH2 ARG A 279 -7.252 26.430 33.389 1.00 57.31 N ANISOU 2153 NH2 ARG A 279 6534 5666 9574 -349 -479 -1954 N ATOM 2154 N THR A 280 -3.707 20.470 30.101 1.00 44.08 N ANISOU 2154 N THR A 280 4657 4730 7359 -562 -153 -1323 N ATOM 2155 CA THR A 280 -4.046 19.135 29.635 1.00 44.33 C ANISOU 2155 CA THR A 280 4706 4888 7250 -506 -86 -1234 C ATOM 2156 C THR A 280 -4.843 18.399 30.703 1.00 42.33 C ANISOU 2156 C THR A 280 4512 4709 6862 -392 -90 -1315 C ATOM 2157 O THR A 280 -4.808 18.745 31.887 1.00 44.05 O ANISOU 2157 O THR A 280 4742 4923 7071 -359 -144 -1450 O ATOM 2158 CB THR A 280 -2.793 18.318 29.279 1.00 42.66 C ANISOU 2158 CB THR A 280 4417 4798 6993 -545 -74 -1205 C ATOM 2159 OG1 THR A 280 -1.982 18.148 30.448 1.00 43.73 O ANISOU 2159 OG1 THR A 280 4518 4996 7101 -520 -144 -1340 O ATOM 2160 CG2 THR A 280 -1.981 19.016 28.197 1.00 43.73 C ANISOU 2160 CG2 THR A 280 4483 4884 7247 -676 -53 -1123 C ATOM 2161 N ILE A 281 -5.567 17.374 30.263 1.00 40.02 N ANISOU 2161 N ILE A 281 4260 4489 6459 -340 -30 -1229 N ATOM 2162 CA ILE A 281 -6.313 16.483 31.144 1.00 38.85 C ANISOU 2162 CA ILE A 281 4171 4427 6163 -252 -20 -1276 C ATOM 2163 C ILE A 281 -5.948 15.055 30.769 1.00 38.17 C ANISOU 2163 C ILE A 281 4090 4457 5956 -232 5 -1199 C ATOM 2164 O ILE A 281 -6.249 14.609 29.655 1.00 39.69 O ANISOU 2164 O ILE A 281 4283 4655 6141 -243 59 -1081 O ATOM 2165 CB ILE A 281 -7.832 16.697 31.041 1.00 40.26 C ANISOU 2165 CB ILE A 281 4400 4562 6336 -207 25 -1260 C ATOM 2166 CG1 ILE A 281 -8.208 18.111 31.481 1.00 39.46 C ANISOU 2166 CG1 ILE A 281 4294 4338 6360 -208 -14 -1358 C ATOM 2167 CG2 ILE A 281 -8.568 15.673 31.882 1.00 37.45 C ANISOU 2167 CG2 ILE A 281 4101 4315 5815 -140 50 -1294 C ATOM 2168 CD1 ILE A 281 -9.691 18.400 31.398 1.00 39.97 C ANISOU 2168 CD1 ILE A 281 4390 4361 6436 -151 21 -1364 C ATOM 2169 N LEU A 282 -5.300 14.343 31.693 1.00 38.86 N ANISOU 2169 N LEU A 282 4186 4632 5947 -198 -43 -1268 N ATOM 2170 CA LEU A 282 -4.822 12.981 31.450 1.00 39.53 C ANISOU 2170 CA LEU A 282 4280 4815 5925 -167 -45 -1212 C ATOM 2171 C LEU A 282 -3.933 12.924 30.210 1.00 42.31 C ANISOU 2171 C LEU A 282 4549 5173 6353 -216 -24 -1137 C ATOM 2172 O LEU A 282 -4.000 11.989 29.409 1.00 42.21 O ANISOU 2172 O LEU A 282 4544 5209 6284 -198 13 -1051 O ATOM 2173 CB LEU A 282 -5.989 11.997 31.334 1.00 37.20 C ANISOU 2173 CB LEU A 282 4070 4556 5509 -120 6 -1141 C ATOM 2174 CG LEU A 282 -6.660 11.578 32.644 1.00 36.76 C ANISOU 2174 CG LEU A 282 4099 4546 5323 -74 -12 -1208 C ATOM 2175 CD1 LEU A 282 -7.838 10.653 32.374 1.00 34.82 C ANISOU 2175 CD1 LEU A 282 3924 4332 4973 -52 49 -1124 C ATOM 2176 CD2 LEU A 282 -5.656 10.915 33.574 1.00 37.45 C ANISOU 2176 CD2 LEU A 282 4205 4701 5322 -44 -98 -1270 C ATOM 2177 N GLY A 283 -3.091 13.942 30.051 1.00 53.95 N ANISOU 2177 N GLY A 283 5943 6602 7956 -286 -46 -1175 N ATOM 2178 CA GLY A 283 -2.176 13.991 28.927 1.00 52.31 C ANISOU 2178 CA GLY A 283 5643 6415 7817 -353 -17 -1114 C ATOM 2179 C GLY A 283 -2.819 14.287 27.591 1.00 55.89 C ANISOU 2179 C GLY A 283 6107 6816 8311 -402 64 -985 C ATOM 2180 O GLY A 283 -2.272 13.904 26.552 1.00 57.44 O ANISOU 2180 O GLY A 283 6250 7066 8507 -438 107 -914 O ATOM 2181 N SER A 284 -3.967 14.961 27.585 1.00 41.91 N ANISOU 2181 N SER A 284 4402 4948 6573 -400 81 -958 N ATOM 2182 CA SER A 284 -4.652 15.320 26.352 1.00 39.99 C ANISOU 2182 CA SER A 284 4179 4643 6371 -441 139 -835 C ATOM 2183 C SER A 284 -5.112 16.768 26.418 1.00 42.78 C ANISOU 2183 C SER A 284 4550 4850 6855 -488 115 -847 C ATOM 2184 O SER A 284 -5.633 17.217 27.443 1.00 42.56 O ANISOU 2184 O SER A 284 4555 4772 6843 -441 74 -944 O ATOM 2185 CB SER A 284 -5.855 14.404 26.091 1.00 41.53 C ANISOU 2185 CB SER A 284 4448 4870 6460 -366 178 -774 C ATOM 2186 OG SER A 284 -6.435 14.676 24.826 1.00 43.96 O ANISOU 2186 OG SER A 284 4774 5130 6801 -402 224 -653 O ATOM 2187 N ALA A 285 -4.916 17.492 25.319 1.00 39.51 N ANISOU 2187 N ALA A 285 4118 4365 6527 -579 138 -749 N ATOM 2188 CA ALA A 285 -5.374 18.869 25.194 1.00 42.13 C ANISOU 2188 CA ALA A 285 4482 4533 6992 -626 104 -737 C ATOM 2189 C ALA A 285 -6.778 18.967 24.610 1.00 42.50 C ANISOU 2189 C ALA A 285 4604 4511 7034 -575 120 -658 C ATOM 2190 O ALA A 285 -7.242 20.076 24.324 1.00 43.06 O ANISOU 2190 O ALA A 285 4710 4434 7217 -605 83 -630 O ATOM 2191 CB ALA A 285 -4.394 19.676 24.339 1.00 42.92 C ANISOU 2191 CB ALA A 285 4536 4580 7192 -770 109 -663 C ATOM 2192 N LEU A 286 -7.457 17.837 24.426 1.00 40.98 N ANISOU 2192 N LEU A 286 4436 4415 6719 -499 163 -623 N ATOM 2193 CA LEU A 286 -8.824 17.804 23.931 1.00 39.45 C ANISOU 2193 CA LEU A 286 4301 4177 6513 -443 176 -562 C ATOM 2194 C LEU A 286 -9.667 16.934 24.853 1.00 39.87 C ANISOU 2194 C LEU A 286 4374 4310 6464 -339 188 -643 C ATOM 2195 O LEU A 286 -9.151 16.093 25.592 1.00 36.47 O ANISOU 2195 O LEU A 286 3929 3985 5942 -315 195 -705 O ATOM 2196 CB LEU A 286 -8.899 17.262 22.495 1.00 40.68 C ANISOU 2196 CB LEU A 286 4469 4373 6615 -478 225 -412 C ATOM 2197 CG LEU A 286 -8.308 18.105 21.364 1.00 43.63 C ANISOU 2197 CG LEU A 286 4840 4671 7066 -594 226 -299 C ATOM 2198 CD1 LEU A 286 -8.082 17.243 20.131 1.00 43.72 C ANISOU 2198 CD1 LEU A 286 4849 4786 6978 -625 290 -180 C ATOM 2199 CD2 LEU A 286 -9.212 19.283 21.036 1.00 47.99 C ANISOU 2199 CD2 LEU A 286 5451 5053 7731 -596 172 -254 C ATOM 2200 N LEU A 287 -10.979 17.147 24.799 1.00 38.63 N ANISOU 2200 N LEU A 287 4252 4104 6322 -281 186 -640 N ATOM 2201 CA LEU A 287 -11.906 16.349 25.588 1.00 36.24 C ANISOU 2201 CA LEU A 287 3966 3885 5921 -198 210 -707 C ATOM 2202 C LEU A 287 -12.124 14.998 24.917 1.00 33.28 C ANISOU 2202 C LEU A 287 3607 3616 5423 -189 260 -614 C ATOM 2203 O LEU A 287 -12.389 14.927 23.712 1.00 35.26 O ANISOU 2203 O LEU A 287 3869 3845 5685 -209 275 -501 O ATOM 2204 CB LEU A 287 -13.232 17.089 25.760 1.00 36.46 C ANISOU 2204 CB LEU A 287 4003 3832 6019 -139 192 -754 C ATOM 2205 CG LEU A 287 -13.135 18.432 26.491 1.00 36.18 C ANISOU 2205 CG LEU A 287 3957 3680 6111 -132 133 -868 C ATOM 2206 CD1 LEU A 287 -14.423 19.228 26.353 1.00 38.99 C ANISOU 2206 CD1 LEU A 287 4316 3938 6560 -66 104 -900 C ATOM 2207 CD2 LEU A 287 -12.788 18.223 27.958 1.00 34.31 C ANISOU 2207 CD2 LEU A 287 3708 3519 5809 -106 132 -1015 C ATOM 2208 N GLU A 288 -12.011 13.927 25.698 1.00 35.20 N ANISOU 2208 N GLU A 288 3861 3967 5545 -159 279 -662 N ATOM 2209 CA GLU A 288 -12.067 12.563 25.187 1.00 35.56 C ANISOU 2209 CA GLU A 288 3931 4106 5475 -150 313 -587 C ATOM 2210 C GLU A 288 -13.428 11.950 25.496 1.00 33.15 C ANISOU 2210 C GLU A 288 3656 3840 5098 -105 341 -596 C ATOM 2211 O GLU A 288 -13.915 12.048 26.627 1.00 32.66 O ANISOU 2211 O GLU A 288 3601 3801 5008 -77 342 -691 O ATOM 2212 CB GLU A 288 -10.950 11.716 25.799 1.00 35.61 C ANISOU 2212 CB GLU A 288 3937 4196 5398 -151 298 -625 C ATOM 2213 CG GLU A 288 -10.913 10.281 25.309 1.00 38.19 C ANISOU 2213 CG GLU A 288 4295 4604 5612 -134 318 -560 C ATOM 2214 CD GLU A 288 -10.547 10.175 23.842 1.00 40.54 C ANISOU 2214 CD GLU A 288 4570 4899 5935 -165 339 -459 C ATOM 2215 OE1 GLU A 288 -9.735 10.999 23.369 1.00 38.63 O ANISOU 2215 OE1 GLU A 288 4280 4621 5775 -214 335 -446 O ATOM 2216 OE2 GLU A 288 -11.070 9.268 23.163 1.00 42.11 O ANISOU 2216 OE2 GLU A 288 4800 5133 6065 -148 361 -394 O ATOM 2217 N ASP A 289 -14.034 11.309 24.489 1.00 31.49 N ANISOU 2217 N ASP A 289 3462 3648 4854 -103 365 -502 N ATOM 2218 CA ASP A 289 -15.387 10.779 24.618 1.00 29.41 C ANISOU 2218 CA ASP A 289 3215 3420 4539 -73 392 -503 C ATOM 2219 C ASP A 289 -15.491 9.317 24.192 1.00 30.49 C ANISOU 2219 C ASP A 289 3391 3633 4560 -78 413 -435 C ATOM 2220 O ASP A 289 -16.588 8.850 23.869 1.00 28.87 O ANISOU 2220 O ASP A 289 3195 3449 4326 -69 433 -404 O ATOM 2221 CB ASP A 289 -16.377 11.628 23.814 1.00 30.51 C ANISOU 2221 CB ASP A 289 3331 3484 4779 -59 385 -469 C ATOM 2222 CG ASP A 289 -16.283 11.387 22.318 1.00 31.09 C ANISOU 2222 CG ASP A 289 3417 3539 4858 -81 382 -343 C ATOM 2223 OD1 ASP A 289 -15.178 11.076 21.824 1.00 33.10 O ANISOU 2223 OD1 ASP A 289 3680 3811 5085 -116 383 -293 O ATOM 2224 OD2 ASP A 289 -17.321 11.510 21.634 1.00 32.62 O ANISOU 2224 OD2 ASP A 289 3608 3708 5080 -61 376 -300 O ATOM 2225 N GLU A 290 -14.382 8.577 24.186 1.00 30.16 N ANISOU 2225 N GLU A 290 3371 3631 4458 -88 400 -418 N ATOM 2226 CA GLU A 290 -14.398 7.174 23.795 1.00 31.03 C ANISOU 2226 CA GLU A 290 3525 3798 4466 -84 404 -364 C ATOM 2227 C GLU A 290 -14.146 6.239 24.974 1.00 30.87 C ANISOU 2227 C GLU A 290 3557 3833 4340 -74 388 -413 C ATOM 2228 O GLU A 290 -13.715 5.098 24.777 1.00 29.30 O ANISOU 2228 O GLU A 290 3402 3665 4065 -66 368 -380 O ATOM 2229 CB GLU A 290 -13.386 6.923 22.676 1.00 33.39 C ANISOU 2229 CB GLU A 290 3811 4102 4774 -93 396 -304 C ATOM 2230 CG GLU A 290 -13.663 7.732 21.416 1.00 33.55 C ANISOU 2230 CG GLU A 290 3801 4074 4872 -115 410 -234 C ATOM 2231 CD GLU A 290 -13.654 6.886 20.157 1.00 35.77 C ANISOU 2231 CD GLU A 290 4101 4390 5099 -116 420 -155 C ATOM 2232 OE1 GLU A 290 -12.982 5.833 20.148 1.00 36.46 O ANISOU 2232 OE1 GLU A 290 4207 4532 5114 -100 412 -163 O ATOM 2233 OE2 GLU A 290 -14.324 7.272 19.176 1.00 34.60 O ANISOU 2233 OE2 GLU A 290 3952 4212 4982 -127 428 -89 O ATOM 2234 N PHE A 291 -14.407 6.701 26.195 1.00 29.72 N ANISOU 2234 N PHE A 291 3414 3696 4184 -73 390 -492 N ATOM 2235 CA PHE A 291 -14.355 5.873 27.394 1.00 32.77 C ANISOU 2235 CA PHE A 291 3863 4136 4452 -73 376 -532 C ATOM 2236 C PHE A 291 -15.741 5.844 28.019 1.00 33.44 C ANISOU 2236 C PHE A 291 3961 4254 4491 -92 425 -557 C ATOM 2237 O PHE A 291 -16.236 6.877 28.482 1.00 34.15 O ANISOU 2237 O PHE A 291 4003 4335 4638 -86 449 -629 O ATOM 2238 CB PHE A 291 -13.337 6.409 28.404 1.00 34.82 C ANISOU 2238 CB PHE A 291 4116 4398 4717 -62 335 -616 C ATOM 2239 CG PHE A 291 -11.909 6.296 27.957 1.00 34.08 C ANISOU 2239 CG PHE A 291 3999 4293 4656 -48 286 -607 C ATOM 2240 CD1 PHE A 291 -11.208 5.113 28.123 1.00 36.93 C ANISOU 2240 CD1 PHE A 291 4414 4689 4930 -27 237 -589 C ATOM 2241 CD2 PHE A 291 -11.261 7.379 27.389 1.00 36.49 C ANISOU 2241 CD2 PHE A 291 4227 4554 5082 -59 284 -619 C ATOM 2242 CE1 PHE A 291 -9.891 5.009 27.719 1.00 38.02 C ANISOU 2242 CE1 PHE A 291 4511 4831 5104 -5 193 -598 C ATOM 2243 CE2 PHE A 291 -9.943 7.282 26.983 1.00 39.75 C ANISOU 2243 CE2 PHE A 291 4602 4976 5525 -56 250 -618 C ATOM 2244 CZ PHE A 291 -9.258 6.096 27.148 1.00 37.58 C ANISOU 2244 CZ PHE A 291 4363 4749 5165 -24 206 -615 C ATOM 2245 N THR A 292 -16.365 4.669 28.035 1.00 28.04 N ANISOU 2245 N THR A 292 3336 3609 3707 -116 438 -506 N ATOM 2246 CA THR A 292 -17.639 4.521 28.716 1.00 29.84 C ANISOU 2246 CA THR A 292 3572 3891 3875 -150 493 -533 C ATOM 2247 C THR A 292 -17.429 4.570 30.228 1.00 29.19 C ANISOU 2247 C THR A 292 3532 3862 3699 -164 493 -610 C ATOM 2248 O THR A 292 -16.307 4.403 30.713 1.00 29.52 O ANISOU 2248 O THR A 292 3617 3894 3703 -147 436 -624 O ATOM 2249 CB THR A 292 -18.310 3.205 28.327 1.00 32.06 C ANISOU 2249 CB THR A 292 3911 4196 4074 -191 503 -451 C ATOM 2250 OG1 THR A 292 -17.575 2.108 28.885 1.00 29.68 O ANISOU 2250 OG1 THR A 292 3715 3904 3659 -204 454 -420 O ATOM 2251 CG2 THR A 292 -18.370 3.058 26.816 1.00 30.54 C ANISOU 2251 CG2 THR A 292 3690 3956 3959 -173 491 -377 C ATOM 2252 N PRO A 293 -18.494 4.823 30.996 1.00 26.54 N ANISOU 2252 N PRO A 293 3177 3589 3320 -193 556 -669 N ATOM 2253 CA PRO A 293 -18.372 4.683 32.457 1.00 29.39 C ANISOU 2253 CA PRO A 293 3595 4020 3553 -219 562 -734 C ATOM 2254 C PRO A 293 -17.888 3.307 32.879 1.00 29.68 C ANISOU 2254 C PRO A 293 3759 4074 3442 -258 517 -658 C ATOM 2255 O PRO A 293 -17.135 3.190 33.854 1.00 31.67 O ANISOU 2255 O PRO A 293 4078 4346 3607 -255 471 -691 O ATOM 2256 CB PRO A 293 -19.796 4.970 32.950 1.00 29.00 C ANISOU 2256 CB PRO A 293 3493 4052 3474 -255 655 -795 C ATOM 2257 CG PRO A 293 -20.363 5.878 31.915 1.00 28.61 C ANISOU 2257 CG PRO A 293 3330 3949 3591 -210 673 -812 C ATOM 2258 CD PRO A 293 -19.784 5.419 30.605 1.00 28.58 C ANISOU 2258 CD PRO A 293 3345 3862 3651 -194 620 -699 C ATOM 2259 N PHE A 294 -18.301 2.258 32.163 1.00 37.58 N ANISOU 2259 N PHE A 294 4802 5060 4415 -292 518 -558 N ATOM 2260 CA PHE A 294 -17.795 0.919 32.447 1.00 36.59 C ANISOU 2260 CA PHE A 294 4809 4925 4169 -320 455 -480 C ATOM 2261 C PHE A 294 -16.295 0.834 32.197 1.00 36.88 C ANISOU 2261 C PHE A 294 4871 4898 4244 -248 354 -475 C ATOM 2262 O PHE A 294 -15.562 0.225 32.984 1.00 38.89 O ANISOU 2262 O PHE A 294 5223 5154 4399 -244 282 -469 O ATOM 2263 CB PHE A 294 -18.545 -0.111 31.600 1.00 40.48 C ANISOU 2263 CB PHE A 294 5333 5398 4649 -366 468 -383 C ATOM 2264 CG PHE A 294 -18.138 -1.535 31.865 1.00 43.81 C ANISOU 2264 CG PHE A 294 5903 5790 4954 -398 394 -300 C ATOM 2265 CD1 PHE A 294 -18.796 -2.289 32.823 1.00 46.83 C ANISOU 2265 CD1 PHE A 294 6385 6222 5186 -494 417 -266 C ATOM 2266 CD2 PHE A 294 -17.113 -2.125 31.144 1.00 43.73 C ANISOU 2266 CD2 PHE A 294 5932 5702 4981 -334 300 -259 C ATOM 2267 CE1 PHE A 294 -18.430 -3.599 33.065 1.00 47.00 C ANISOU 2267 CE1 PHE A 294 6560 6195 5103 -526 334 -180 C ATOM 2268 CE2 PHE A 294 -16.744 -3.434 31.382 1.00 43.40 C ANISOU 2268 CE2 PHE A 294 6030 5616 4842 -350 216 -191 C ATOM 2269 CZ PHE A 294 -17.402 -4.173 32.344 1.00 49.06 C ANISOU 2269 CZ PHE A 294 6863 6363 5416 -446 226 -146 C ATOM 2270 N ASP A 295 -15.822 1.435 31.100 1.00 31.97 N ANISOU 2270 N ASP A 295 4160 4226 3763 -193 345 -478 N ATOM 2271 CA ASP A 295 -14.393 1.417 30.798 1.00 31.27 C ANISOU 2271 CA ASP A 295 4068 4095 3720 -131 262 -485 C ATOM 2272 C ASP A 295 -13.583 2.065 31.913 1.00 34.71 C ANISOU 2272 C ASP A 295 4503 4551 4135 -110 223 -572 C ATOM 2273 O ASP A 295 -12.511 1.571 32.280 1.00 34.43 O ANISOU 2273 O ASP A 295 4517 4505 4059 -74 134 -578 O ATOM 2274 CB ASP A 295 -14.125 2.126 29.469 1.00 31.41 C ANISOU 2274 CB ASP A 295 3979 4071 3884 -98 281 -476 C ATOM 2275 CG ASP A 295 -14.690 1.377 28.279 1.00 30.36 C ANISOU 2275 CG ASP A 295 3856 3917 3764 -107 297 -393 C ATOM 2276 OD1 ASP A 295 -14.984 0.171 28.416 1.00 32.43 O ANISOU 2276 OD1 ASP A 295 4209 4180 3931 -129 273 -342 O ATOM 2277 OD2 ASP A 295 -14.842 1.998 27.205 1.00 28.80 O ANISOU 2277 OD2 ASP A 295 3580 3697 3667 -96 329 -377 O ATOM 2278 N VAL A 296 -14.082 3.174 32.462 1.00 30.51 N ANISOU 2278 N VAL A 296 3912 4047 3635 -123 279 -649 N ATOM 2279 CA VAL A 296 -13.361 3.871 33.522 1.00 32.02 C ANISOU 2279 CA VAL A 296 4099 4257 3809 -104 239 -745 C ATOM 2280 C VAL A 296 -13.366 3.045 34.803 1.00 34.45 C ANISOU 2280 C VAL A 296 4531 4620 3937 -131 203 -746 C ATOM 2281 O VAL A 296 -12.330 2.881 35.459 1.00 37.23 O ANISOU 2281 O VAL A 296 4930 4974 4244 -101 114 -777 O ATOM 2282 CB VAL A 296 -13.965 5.269 33.747 1.00 29.13 C ANISOU 2282 CB VAL A 296 3642 3897 3527 -106 304 -837 C ATOM 2283 CG1 VAL A 296 -13.261 5.972 34.894 1.00 31.30 C ANISOU 2283 CG1 VAL A 296 3919 4193 3779 -88 259 -948 C ATOM 2284 CG2 VAL A 296 -13.879 6.093 32.471 1.00 30.54 C ANISOU 2284 CG2 VAL A 296 3718 4005 3881 -83 321 -820 C ATOM 2285 N VAL A 297 -14.532 2.515 35.180 1.00 37.34 N ANISOU 2285 N VAL A 297 4954 5037 4197 -195 269 -710 N ATOM 2286 CA VAL A 297 -14.620 1.676 36.372 1.00 43.56 C ANISOU 2286 CA VAL A 297 5876 5880 4795 -242 241 -691 C ATOM 2287 C VAL A 297 -13.776 0.418 36.201 1.00 45.87 C ANISOU 2287 C VAL A 297 6279 6117 5030 -221 128 -602 C ATOM 2288 O VAL A 297 -13.132 -0.050 37.148 1.00 50.28 O ANISOU 2288 O VAL A 297 6944 6687 5472 -215 41 -605 O ATOM 2289 CB VAL A 297 -16.092 1.340 36.681 1.00 41.72 C ANISOU 2289 CB VAL A 297 5668 5718 4465 -332 348 -663 C ATOM 2290 CG1 VAL A 297 -16.189 0.234 37.722 1.00 45.09 C ANISOU 2290 CG1 VAL A 297 6259 6190 4685 -404 316 -603 C ATOM 2291 CG2 VAL A 297 -16.831 2.583 37.151 1.00 42.27 C ANISOU 2291 CG2 VAL A 297 5634 5857 4569 -338 445 -782 C ATOM 2292 N ARG A 298 -13.760 -0.141 34.988 1.00 47.09 N ANISOU 2292 N ARG A 298 6414 6210 5267 -202 119 -529 N ATOM 2293 CA ARG A 298 -12.942 -1.321 34.721 1.00 50.29 C ANISOU 2293 CA ARG A 298 6914 6556 5639 -165 5 -461 C ATOM 2294 C ARG A 298 -11.466 -1.042 34.975 1.00 50.31 C ANISOU 2294 C ARG A 298 6895 6538 5682 -78 -104 -525 C ATOM 2295 O ARG A 298 -10.743 -1.904 35.488 1.00 52.33 O ANISOU 2295 O ARG A 298 7258 6770 5855 -47 -221 -502 O ATOM 2296 CB ARG A 298 -13.152 -1.791 33.282 1.00 48.42 C ANISOU 2296 CB ARG A 298 6635 6264 5498 -149 21 -397 C ATOM 2297 N GLN A 299 -11.002 0.156 34.627 1.00 54.89 N ANISOU 2297 N GLN A 299 7338 7125 6393 -42 -75 -605 N ATOM 2298 CA GLN A 299 -9.596 0.507 34.766 1.00 55.26 C ANISOU 2298 CA GLN A 299 7336 7160 6499 30 -169 -674 C ATOM 2299 C GLN A 299 -9.244 1.064 36.141 1.00 58.73 C ANISOU 2299 C GLN A 299 7806 7645 6864 28 -212 -758 C ATOM 2300 O GLN A 299 -8.065 1.327 36.400 1.00 62.36 O ANISOU 2300 O GLN A 299 8230 8101 7364 83 -303 -823 O ATOM 2301 CB GLN A 299 -9.199 1.520 33.684 1.00 53.99 C ANISOU 2301 CB GLN A 299 7015 6980 6517 54 -121 -712 C ATOM 2302 CG GLN A 299 -7.709 1.545 33.371 1.00 52.65 C ANISOU 2302 CG GLN A 299 6780 6798 6426 122 -212 -758 C ATOM 2303 CD GLN A 299 -7.400 2.168 32.026 1.00 49.16 C ANISOU 2303 CD GLN A 299 6203 6339 6138 127 -156 -755 C ATOM 2304 OE1 GLN A 299 -6.323 2.726 31.823 1.00 49.04 O ANISOU 2304 OE1 GLN A 299 6091 6329 6213 153 -190 -815 O ATOM 2305 NE2 GLN A 299 -8.343 2.070 31.096 1.00 47.37 N ANISOU 2305 NE2 GLN A 299 5969 6094 5935 96 -71 -684 N ATOM 2306 N CYS A 300 -10.222 1.253 37.028 1.00 67.42 N ANISOU 2306 N CYS A 300 8966 8796 7854 -36 -148 -767 N ATOM 2307 CA CYS A 300 -9.949 1.756 38.367 1.00 69.24 C ANISOU 2307 CA CYS A 300 9236 9081 7992 -41 -185 -854 C ATOM 2308 C CYS A 300 -10.200 0.737 39.471 1.00 71.42 C ANISOU 2308 C CYS A 300 9690 9395 8054 -81 -237 -801 C ATOM 2309 O CYS A 300 -9.730 0.944 40.596 1.00 75.59 O ANISOU 2309 O CYS A 300 10275 9965 8483 -73 -303 -863 O ATOM 2310 CB CYS A 300 -10.771 3.026 38.640 1.00 68.43 C ANISOU 2310 CB CYS A 300 9047 9024 7931 -76 -69 -942 C ATOM 2311 SG CYS A 300 -10.414 4.398 37.509 1.00 70.84 S ANISOU 2311 SG CYS A 300 9163 9269 8484 -38 -28 -1006 S ATOM 2312 N SER A 301 -10.924 -0.347 39.187 1.00 71.89 N ANISOU 2312 N SER A 301 9844 9437 8034 -131 -214 -685 N ATOM 2313 CA SER A 301 -11.065 -1.461 40.115 1.00 75.32 C ANISOU 2313 CA SER A 301 10467 9883 8267 -178 -282 -608 C ATOM 2314 C SER A 301 -10.358 -2.720 39.627 1.00 75.98 C ANISOU 2314 C SER A 301 10644 9873 8353 -127 -416 -517 C ATOM 2315 O SER A 301 -10.362 -3.734 40.334 1.00 78.89 O ANISOU 2315 O SER A 301 11188 10224 8564 -159 -502 -440 O ATOM 2316 CB SER A 301 -12.548 -1.759 40.371 1.00 74.35 C ANISOU 2316 CB SER A 301 10400 9819 8030 -299 -152 -547 C ATOM 2317 OG SER A 301 -13.086 -2.620 39.379 1.00 75.02 O ANISOU 2317 OG SER A 301 10502 9843 8158 -327 -128 -441 O HETATM 2318 C1 LIG A 401 -10.918 -4.971 2.009 1.00 34.72 C ANISOU 2318 C1 LIG A 401 4217 5315 3660 201 506 -190 C HETATM 2319 C10 LIG A 401 -16.673 -2.214 -0.495 1.00 31.88 C ANISOU 2319 C10 LIG A 401 4138 4736 3241 -38 317 345 C HETATM 2320 C11 LIG A 401 -18.060 -1.671 -0.754 1.00 32.88 C ANISOU 2320 C11 LIG A 401 4307 4787 3399 -60 237 438 C HETATM 2321 C12 LIG A 401 -18.577 -0.568 0.144 1.00 32.19 C ANISOU 2321 C12 LIG A 401 4191 4592 3447 -91 226 516 C HETATM 2322 C13 LIG A 401 -19.142 -2.653 -1.148 1.00 33.16 C ANISOU 2322 C13 LIG A 401 4390 4802 3409 -23 144 396 C HETATM 2323 C14 LIG A 401 -16.961 -1.406 -1.746 1.00 34.53 C ANISOU 2323 C14 LIG A 401 4517 5125 3477 -91 315 450 C HETATM 2324 C15 LIG A 401 -16.217 -0.089 -1.651 1.00 34.29 C ANISOU 2324 C15 LIG A 401 4455 5106 3469 -164 390 540 C HETATM 2325 C16 LIG A 401 -14.924 0.871 0.263 1.00 34.20 C ANISOU 2325 C16 LIG A 401 4325 5023 3647 -199 485 523 C HETATM 2326 C17 LIG A 401 -14.894 2.209 -0.475 1.00 33.74 C ANISOU 2326 C17 LIG A 401 4295 4967 3556 -290 506 662 C HETATM 2327 C18 LIG A 401 -13.475 2.714 -0.788 1.00 35.68 C ANISOU 2327 C18 LIG A 401 4492 5321 3746 -364 617 671 C HETATM 2328 C19 LIG A 401 -12.668 1.609 -1.476 1.00 36.00 C ANISOU 2328 C19 LIG A 401 4505 5522 3651 -329 675 561 C HETATM 2329 C2 LIG A 401 -12.282 -4.356 2.179 1.00 32.25 C ANISOU 2329 C2 LIG A 401 3970 4892 3391 140 464 -61 C HETATM 2330 C20 LIG A 401 -13.547 3.918 -1.731 1.00 36.16 C ANISOU 2330 C20 LIG A 401 4611 5387 3743 -469 628 826 C HETATM 2331 C21 LIG A 401 -12.741 3.141 0.486 1.00 35.59 C ANISOU 2331 C21 LIG A 401 4399 5257 3868 -375 657 632 C HETATM 2332 C22 LIG A 401 -16.908 3.554 -0.184 1.00 34.67 C ANISOU 2332 C22 LIG A 401 4483 4871 3820 -299 362 815 C HETATM 2333 C23 LIG A 401 -18.967 4.874 0.431 1.00 35.98 C ANISOU 2333 C23 LIG A 401 4678 4812 4180 -271 206 919 C HETATM 2334 C24 LIG A 401 -19.990 3.751 0.189 1.00 32.54 C ANISOU 2334 C24 LIG A 401 4255 4397 3711 -207 139 858 C HETATM 2335 C25 LIG A 401 -20.240 2.905 1.428 1.00 32.14 C ANISOU 2335 C25 LIG A 401 4146 4317 3749 -158 147 744 C HETATM 2336 C26 LIG A 401 -20.698 3.768 2.586 1.00 32.58 C ANISOU 2336 C26 LIG A 401 4154 4264 3960 -152 132 748 C HETATM 2337 C27 LIG A 401 -19.674 4.844 2.878 1.00 32.98 C ANISOU 2337 C27 LIG A 401 4192 4290 4049 -201 191 794 C HETATM 2338 C28 LIG A 401 -19.419 5.701 1.646 1.00 33.56 C ANISOU 2338 C28 LIG A 401 4328 4376 4047 -256 178 915 C HETATM 2339 C29 LIG A 401 -18.907 5.781 -0.822 1.00 38.10 C ANISOU 2339 C29 LIG A 401 5025 5092 4360 -335 182 1056 C HETATM 2340 C3 LIG A 401 -12.340 -2.983 1.483 1.00 33.69 C ANISOU 2340 C3 LIG A 401 4138 5124 3540 42 529 62 C HETATM 2341 C30 LIG A 401 -17.471 7.606 -2.502 1.00 41.41 C ANISOU 2341 C30 LIG A 401 5555 5566 4615 -531 252 1298 C HETATM 2342 C31 LIG A 401 -18.738 8.170 -3.137 1.00 43.56 C ANISOU 2342 C31 LIG A 401 5914 5743 4893 -507 114 1401 C HETATM 2343 C32 LIG A 401 -17.055 6.336 -3.235 1.00 42.34 C ANISOU 2343 C32 LIG A 401 5668 5854 4567 -513 311 1219 C HETATM 2344 C33 LIG A 401 -16.355 8.640 -2.558 1.00 43.61 C ANISOU 2344 C33 LIG A 401 5836 5843 4891 -649 330 1383 C HETATM 2345 C34 LIG A 401 -9.382 -6.119 0.528 1.00 35.68 C ANISOU 2345 C34 LIG A 401 4269 5675 3613 297 569 -393 C HETATM 2346 C35 LIG A 401 -8.455 -5.405 -0.391 1.00 37.84 C ANISOU 2346 C35 LIG A 401 4459 6127 3791 237 692 -391 C HETATM 2347 C36 LIG A 401 -9.155 -6.634 -0.849 1.00 35.08 C ANISOU 2347 C36 LIG A 401 4198 5741 3390 324 601 -466 C HETATM 2348 C4 LIG A 401 -11.454 -1.962 2.201 1.00 34.00 C ANISOU 2348 C4 LIG A 401 4097 5167 3653 -10 598 91 C HETATM 2349 C5 LIG A 401 -11.399 -0.619 1.510 1.00 36.49 C ANISOU 2349 C5 LIG A 401 4407 5520 3938 -116 658 215 C HETATM 2350 C6 LIG A 401 -10.717 0.437 2.344 1.00 38.81 C ANISOU 2350 C6 LIG A 401 4633 5782 4331 -176 706 250 C HETATM 2351 C7 LIG A 401 -9.306 0.088 2.752 1.00 42.23 C ANISOU 2351 C7 LIG A 401 4965 6306 4773 -151 765 136 C HETATM 2352 C8 LIG A 401 -14.285 -2.171 0.227 1.00 36.00 C ANISOU 2352 C8 LIG A 401 4545 5363 3770 -33 463 242 C HETATM 2353 C9 LIG A 401 -15.631 -1.457 0.308 1.00 31.89 C ANISOU 2353 C9 LIG A 401 4071 4736 3309 -68 397 354 C HETATM 2354 N1 LIG A 401 -13.718 -2.477 1.394 1.00 31.49 N ANISOU 2354 N1 LIG A 401 3925 4751 3290 3 472 172 N HETATM 2355 N2 LIG A 401 -15.562 -0.146 -0.337 1.00 33.08 N ANISOU 2355 N2 LIG A 401 4230 4907 3431 -147 431 477 N HETATM 2356 N3 LIG A 401 -15.693 3.171 0.266 1.00 33.99 N ANISOU 2356 N3 LIG A 401 4335 4854 3724 -304 450 736 N HETATM 2357 N4 LIG A 401 -17.628 4.303 0.679 1.00 34.73 N ANISOU 2357 N4 LIG A 401 4477 4748 3971 -289 310 847 N HETATM 2358 N5 LIG A 401 -10.648 -5.498 0.811 1.00 35.76 N ANISOU 2358 N5 LIG A 401 4354 5563 3671 229 527 -250 N HETATM 2359 O1 LIG A 401 -10.118 -4.971 2.949 1.00 35.77 O ANISOU 2359 O1 LIG A 401 4290 5433 3867 228 516 -242 O HETATM 2360 O2 LIG A 401 -16.570 6.802 -0.204 1.00 38.65 O ANISOU 2360 O2 LIG A 401 5028 5203 4453 -464 358 1076 O HETATM 2361 O3 LIG A 401 -18.531 8.311 -0.250 1.00 41.22 O ANISOU 2361 O3 LIG A 401 5439 5295 4929 -432 166 1218 O HETATM 2362 O4 LIG A 401 -17.315 3.223 -1.312 1.00 35.83 O ANISOU 2362 O4 LIG A 401 4689 5077 3849 -297 328 846 O HETATM 2363 O5 LIG A 401 -14.413 0.730 1.370 1.00 32.04 O ANISOU 2363 O5 LIG A 401 3996 4715 3464 -176 507 459 O HETATM 2364 O6 LIG A 401 -13.766 -2.415 -0.861 1.00 34.57 O ANISOU 2364 O6 LIG A 401 4368 5305 3461 -35 502 216 O HETATM 2365 O7 LIG A 401 -13.289 -5.216 1.656 1.00 31.19 O ANISOU 2365 O7 LIG A 401 3918 4721 3212 172 386 -74 O HETATM 2366 S1 LIG A 401 -17.820 7.189 -0.787 1.00 39.11 S ANISOU 2366 S1 LIG A 401 5160 5186 4516 -439 245 1158 S TER HETATM 2367 O HOH S 1 -21.315 1.314 10.545 1.00 28.17 O ANISOU 2367 O HOH S 1 3380 3566 3757 -83 261 304 O HETATM 2368 O HOH S 2 -20.483 -6.221 2.094 1.00 32.38 O ANISOU 2368 O HOH S 2 4304 4449 3550 65 1 140 O HETATM 2369 O HOH S 3 -23.421 -9.019 16.341 1.00 31.07 O ANISOU 2369 O HOH S 3 4270 3763 3772 -394 79 147 O HETATM 2370 O HOH S 4 -14.431 9.302 27.376 1.00 29.39 O ANISOU 2370 O HOH S 4 3283 3573 4311 -64 384 -655 O HETATM 2371 O HOH S 5 -11.089 4.739 21.019 1.00 32.94 O ANISOU 2371 O HOH S 5 3759 4159 4600 -62 369 -248 O HETATM 2372 O HOH S 6 -10.696 -9.772 13.685 1.00 33.92 O ANISOU 2372 O HOH S 6 4484 4311 4092 495 -128 -398 O HETATM 2373 O HOH S 7 -21.930 5.473 26.730 1.00 29.17 O ANISOU 2373 O HOH S 7 3265 3831 3989 -163 630 -520 O HETATM 2374 O HOH S 8 -27.504 -0.014 17.702 1.00 33.75 O ANISOU 2374 O HOH S 8 3826 4394 4604 -300 426 -23 O HETATM 2375 O HOH S 9 -27.852 -3.713 6.547 1.00 32.31 O ANISOU 2375 O HOH S 9 3967 4174 4133 -161 -102 270 O HETATM 2376 O HOH S 10 -28.488 -6.948 -3.895 1.00 36.39 O ANISOU 2376 O HOH S 10 4924 5010 3893 -8 -646 235 O HETATM 2377 O HOH S 11 -24.488 -7.213 -10.441 1.00 35.19 O ANISOU 2377 O HOH S 11 5157 5461 2753 103 -557 185 O HETATM 2378 O HOH S 13 -17.946 10.124 11.721 1.00 36.26 O ANISOU 2378 O HOH S 13 4286 4202 5291 -200 297 461 O HETATM 2379 O HOH S 14 -28.324 0.717 6.736 1.00 33.71 O ANISOU 2379 O HOH S 14 3980 4290 4539 -57 -96 372 O HETATM 2380 O HOH S 15 -23.766 -21.045 4.355 1.00 42.18 O ANISOU 2380 O HOH S 15 6502 4579 4944 -28 -1037 -483 O HETATM 2381 O HOH S 16 -15.219 -2.007 25.555 1.00 31.58 O ANISOU 2381 O HOH S 16 4157 3997 3845 -102 222 -190 O HETATM 2382 O HOH S 17 -12.165 2.245 25.780 1.00 43.08 O ANISOU 2382 O HOH S 17 5300 5475 5593 -12 248 -386 O HETATM 2383 O HOH S 18 -24.414 -24.039 -1.021 1.00 46.57 O ANISOU 2383 O HOH S 18 7252 5131 5313 196 -1438 -982 O HETATM 2384 O HOH S 20 -19.860 -6.661 22.312 1.00 33.79 O ANISOU 2384 O HOH S 20 4663 4168 4008 -327 192 69 O HETATM 2385 O HOH S 22 -28.223 1.560 12.783 1.00 32.40 O ANISOU 2385 O HOH S 22 3614 4120 4577 -128 193 135 O HETATM 2386 O HOH S 23 -14.448 5.082 17.057 1.00 31.84 O ANISOU 2386 O HOH S 23 3664 3962 4471 -110 435 18 O HETATM 2387 O HOH S 24 -22.809 1.971 36.381 1.00 38.34 O ANISOU 2387 O HOH S 24 4897 5654 4018 -625 904 -758 O HETATM 2388 O HOH S 25 -6.566 0.761 22.234 1.00 30.12 O ANISOU 2388 O HOH S 25 3404 3976 4066 172 132 -478 O HETATM 2389 O HOH S 26 -24.060 10.044 39.947 1.00 43.82 O ANISOU 2389 O HOH S 26 4978 6591 5079 -196 1101 -1858 O HETATM 2390 O HOH S 27 -20.643 1.869 30.654 1.00 38.91 O ANISOU 2390 O HOH S 27 4870 5253 4661 -358 630 -484 O HETATM 2391 O HOH S 28 -10.729 -23.563 0.863 1.00 44.49 O ANISOU 2391 O HOH S 28 6503 5423 4980 1573 -1110 -1877 O HETATM 2392 O HOH S 29 -26.755 -3.120 2.125 1.00 31.66 O ANISOU 2392 O HOH S 29 4044 4197 3788 -58 -232 389 O HETATM 2393 O HOH S 30 -14.102 12.637 19.878 1.00 42.19 O ANISOU 2393 O HOH S 30 4822 4837 6372 -204 354 -145 O HETATM 2394 O HOH S 31 -14.453 -19.873 25.970 1.00 51.08 O ANISOU 2394 O HOH S 31 8591 5110 5708 -70 -1295 322 O HETATM 2395 O HOH S 32 -10.208 1.330 27.451 1.00 36.45 O ANISOU 2395 O HOH S 32 4530 4661 4658 55 104 -477 O HETATM 2396 O HOH S 33 -30.474 -1.487 3.991 1.00 43.02 O ANISOU 2396 O HOH S 33 5203 5555 5590 -77 -321 359 O HETATM 2397 O HOH S 35 -28.781 0.226 15.058 1.00 39.08 O ANISOU 2397 O HOH S 35 4437 5046 5368 -242 303 38 O HETATM 2398 O HOH S 36 -12.284 -30.006 14.756 1.00 49.25 O ANISOU 2398 O HOH S 36 8758 3822 6134 1078 -2525 -758 O HETATM 2399 O HOH S 37 -20.360 17.302 44.582 1.00 53.57 O ANISOU 2399 O HOH S 37 6154 7572 6627 268 718 -2985 O HETATM 2400 O HOH S 38 -4.137 6.117 26.142 1.00 44.27 O ANISOU 2400 O HOH S 38 4922 5724 6175 4 81 -755 O HETATM 2401 O HOH S 39 -25.124 8.247 10.225 1.00 38.66 O ANISOU 2401 O HOH S 39 4513 4544 5633 40 37 413 O HETATM 2402 O HOH S 41 -12.921 -24.197 -0.763 1.00 46.39 O ANISOU 2402 O HOH S 41 6900 5603 5122 1427 -1181 -1846 O HETATM 2403 O HOH S 42 -19.050 -1.211 25.707 1.00 37.96 O ANISOU 2403 O HOH S 42 4877 4883 4665 -268 413 -162 O HETATM 2404 O HOH S 43 -28.559 -3.220 0.197 1.00 42.83 O ANISOU 2404 O HOH S 43 5472 5648 5153 -43 -416 414 O HETATM 2405 O HOH S 44 -26.335 -9.399 16.637 1.00 40.63 O ANISOU 2405 O HOH S 44 5403 5022 5012 -610 124 177 O HETATM 2406 O HOH S 45 -27.932 -1.988 4.581 1.00 37.71 O ANISOU 2406 O HOH S 45 4650 4880 4800 -87 -177 368 O HETATM 2407 O HOH S 46 -11.726 11.120 1.010 1.00 47.84 O ANISOU 2407 O HOH S 46 6050 6302 5825 -937 658 1269 O HETATM 2408 O HOH S 47 -24.928 -14.700 11.530 1.00 42.20 O ANISOU 2408 O HOH S 47 6030 4896 5109 -426 -360 70 O HETATM 2409 O HOH S 48 -24.476 3.822 24.934 1.00 41.95 O ANISOU 2409 O HOH S 48 4834 5510 5595 -237 661 -398 O HETATM 2410 O HOH S 50 -26.861 -2.495 -5.667 1.00 55.04 O ANISOU 2410 O HOH S 50 7358 7481 6074 5 -546 607 O HETATM 2411 O HOH S 51 -11.134 -2.851 27.135 1.00 39.08 O ANISOU 2411 O HOH S 51 5181 4926 4740 85 -35 -320 O HETATM 2412 O HOH S 52 -29.859 -17.316 9.245 1.00 52.27 O ANISOU 2412 O HOH S 52 7303 6084 6475 -818 -589 46 O HETATM 2413 O HOH S 53 -30.102 -5.413 7.127 1.00 48.98 O ANISOU 2413 O HOH S 53 6022 6288 6298 -283 -166 195 O HETATM 2414 O HOH S 54 -31.161 -10.138 11.315 1.00 38.61 O ANISOU 2414 O HOH S 54 4882 4856 4932 -704 -92 128 O HETATM 2415 O HOH S 55 -24.505 12.314 41.029 1.00 43.18 O ANISOU 2415 O HOH S 55 4737 6547 5122 -43 1121 -2235 O HETATM 2416 O HOH S 56 -9.528 -18.874 19.869 1.00 42.27 O ANISOU 2416 O HOH S 56 6694 4318 5051 834 -1300 -432 O HETATM 2417 O HOH S 57 -28.871 -7.981 14.798 1.00 65.52 O ANISOU 2417 O HOH S 57 8282 8300 8313 -625 148 146 O HETATM 2418 O HOH S 58 -2.411 -16.562 19.252 1.00 48.54 O ANISOU 2418 O HOH S 58 6644 5686 6112 1533 -1318 -1118 O HETATM 2419 O HOH S 59 -19.546 -29.103 8.791 1.00 62.56 O ANISOU 2419 O HOH S 59 10176 5840 7753 306 -2017 -716 O HETATM 2420 O HOH S 60 -18.826 17.938 19.355 1.00 45.66 O ANISOU 2420 O HOH S 60 5276 4691 7382 0 63 -202 O HETATM 2421 O HOH S 61 -13.997 -11.063 -6.257 1.00 48.48 O ANISOU 2421 O HOH S 61 6425 7439 4557 499 165 -678 O HETATM 2422 O HOH S 62 -27.136 7.839 17.796 1.00 36.71 O ANISOU 2422 O HOH S 62 3917 4496 5536 61 333 -188 O HETATM 2423 O HOH S 63 -25.874 -15.266 19.620 1.00 47.08 O ANISOU 2423 O HOH S 63 6910 5433 5545 -967 -162 356 O HETATM 2424 O HOH S 64 -11.467 5.431 17.743 1.00 48.88 O ANISOU 2424 O HOH S 64 5736 6181 6655 -125 443 -75 O HETATM 2425 O HOH S 65 -11.588 -1.631 -2.567 1.00 51.38 O ANISOU 2425 O HOH S 65 6412 7744 5366 -135 707 213 O HETATM 2426 O HOH S 66 -4.117 22.995 25.463 1.00 50.06 O ANISOU 2426 O HOH S 66 5470 5089 8460 -905 -71 -807 O HETATM 2427 O HOH S 67 -3.698 3.006 24.171 1.00 32.79 O ANISOU 2427 O HOH S 67 3507 4375 4576 143 62 -687 O HETATM 2428 O HOH S 68 -28.287 -17.255 0.270 1.00 53.47 O ANISOU 2428 O HOH S 68 7492 6531 6294 -213 -924 -344 O HETATM 2429 O HOH S 69 -28.971 -1.248 9.087 1.00 58.20 O ANISOU 2429 O HOH S 69 7031 7429 7653 -163 2 239 O HETATM 2430 O HOH S 70 -15.130 18.569 22.804 1.00 45.33 O ANISOU 2430 O HOH S 70 5178 4695 7351 -131 124 -499 O HETATM 2431 O HOH S 71 -21.030 -20.529 13.608 1.00 48.62 O ANISOU 2431 O HOH S 71 7586 5056 5832 -215 -915 -41 O HETATM 2432 O HOH S 72 -31.388 -12.385 10.142 1.00 48.59 O ANISOU 2432 O HOH S 72 6308 6012 6142 -772 -251 110 O HETATM 2433 O HOH S 73 -31.571 -14.303 14.853 1.00 51.01 O ANISOU 2433 O HOH S 73 6818 6212 6352 -1165 -102 225 O HETATM 2434 O HOH S 74 -27.016 -19.033 -1.425 1.00 49.50 O ANISOU 2434 O HOH S 74 7166 5994 5649 -50 -1068 -561 O HETATM 2435 O HOH S 76 -27.375 4.859 2.422 1.00 44.45 O ANISOU 2435 O HOH S 76 5541 5529 5817 31 -321 750 O HETATM 2436 O HOH S 77 -2.057 7.896 32.896 1.00 43.87 O ANISOU 2436 O HOH S 77 4932 5685 6051 71 -308 -1241 O HETATM 2437 O HOH S 78 -28.963 -10.614 1.903 1.00 38.20 O ANISOU 2437 O HOH S 78 5090 4904 4519 -215 -525 38 O HETATM 2438 O HOH S 80 -17.843 11.153 9.438 1.00 45.61 O ANISOU 2438 O HOH S 80 5561 5334 6435 -275 245 670 O HETATM 2439 O HOH S 81 -24.239 7.826 22.169 1.00 45.64 O ANISOU 2439 O HOH S 81 5136 5704 6501 -17 512 -392 O HETATM 2440 O HOH S 82 -12.414 -5.103 -1.655 1.00 37.00 O ANISOU 2440 O HOH S 82 4653 5793 3611 141 504 -100 O HETATM 2441 O HOH S 84 -30.421 7.644 28.006 1.00 45.74 O ANISOU 2441 O HOH S 84 4660 6378 6339 -122 938 -1062 O HETATM 2442 O HOH S 85 -14.750 -25.997 -1.538 1.00 54.58 O ANISOU 2442 O HOH S 85 8192 6367 6180 1362 -1436 -1901 O HETATM 2443 O HOH S 86 -25.948 -1.234 25.984 1.00 51.23 O ANISOU 2443 O HOH S 86 6277 6834 6356 -579 712 -211 O HETATM 2444 O HOH S 87 0.554 2.321 39.506 1.00 50.58 O ANISOU 2444 O HOH S 87 6428 6704 6087 490 -1158 -1411 O HETATM 2445 O HOH S 89 -0.835 26.308 32.926 1.00 52.66 O ANISOU 2445 O HOH S 89 5634 5234 9139 -888 -585 -1874 O HETATM 2446 O HOH S 90 -27.304 7.121 11.654 1.00 38.73 O ANISOU 2446 O HOH S 90 4372 4650 5694 76 57 235 O HETATM 2447 O HOH S 91 -4.653 19.154 39.037 1.00 52.63 O ANISOU 2447 O HOH S 91 5989 6249 7758 -118 -431 -2233 O HETATM 2448 O HOH S 92 -4.716 24.183 36.642 1.00 59.13 O ANISOU 2448 O HOH S 92 6685 6395 9387 -323 -521 -2258 O HETATM 2449 O HOH S 93 -17.872 3.397 44.068 1.00 51.21 O ANISOU 2449 O HOH S 93 7062 7556 4839 -558 595 -1167 O HETATM 2450 O HOH S 94 -21.342 -6.731 24.554 1.00 53.58 O ANISOU 2450 O HOH S 94 7219 6741 6397 -508 278 90 O HETATM 2451 O HOH S 95 -28.719 11.312 24.529 1.00 46.86 O ANISOU 2451 O HOH S 95 4846 5953 7007 214 560 -928 O HETATM 2452 O HOH S 96 -24.591 -23.535 3.400 1.00 65.84 O ANISOU 2452 O HOH S 96 9717 7333 7965 -64 -1311 -623 O HETATM 2453 O HOH S 97 -7.604 -19.804 21.243 1.00 50.92 O ANISOU 2453 O HOH S 97 7900 5282 6165 1060 -1588 -526 O HETATM 2454 O HOH S 98 -29.661 -5.102 -6.033 1.00 54.59 O ANISOU 2454 O HOH S 98 7260 7393 6088 22 -809 394 O HETATM 2455 O HOH S 99 -23.011 4.219 28.897 1.00 52.65 O ANISOU 2455 O HOH S 99 6293 6985 6726 -279 731 -590 O HETATM 2456 O HOH S 100 -31.969 -14.961 12.573 1.00 49.30 O ANISOU 2456 O HOH S 100 6603 5947 6180 -1096 -255 171 O HETATM 2457 O HOH S 101 -2.101 28.260 31.294 1.00 53.06 O ANISOU 2457 O HOH S 101 5810 4892 9457 -984 -606 -1691 O HETATM 2458 O HOH S 102 -6.916 10.792 27.826 1.00 66.79 O ANISOU 2458 O HOH S 102 7807 8301 9271 -151 160 -825 O HETATM 2459 O HOH S 103 -31.138 -16.256 16.629 1.00 56.75 O ANISOU 2459 O HOH S 103 7824 6774 6963 -1362 -148 323 O HETATM 2460 O HOH S 104 -22.559 -6.251 -11.704 1.00 45.91 O ANISOU 2460 O HOH S 104 6564 7054 3826 69 -373 251 O HETATM 2461 O HOH S 105 -6.742 22.707 23.999 1.00 48.26 O ANISOU 2461 O HOH S 105 5397 4772 8168 -767 -29 -608 O HETATM 2462 O HOH S 106 -24.037 6.280 25.815 1.00 47.49 O ANISOU 2462 O HOH S 106 5435 6162 6449 -132 661 -557 O HETATM 2463 O HOH S 107 -30.292 -13.154 1.428 1.00 53.26 O ANISOU 2463 O HOH S 107 7092 6713 6431 -321 -705 -76 O HETATM 2464 O HOH S 108 -14.071 23.803 33.960 1.00 60.26 O ANISOU 2464 O HOH S 108 6942 6467 9487 179 -144 -2052 O HETATM 2465 O HOH S 109 -28.865 -3.651 -8.332 1.00 48.46 O ANISOU 2465 O HOH S 109 6638 6750 5026 42 -845 561 O HETATM 2466 O HOH S 110 -30.588 -12.231 4.062 1.00 55.95 O ANISOU 2466 O HOH S 110 7318 7023 6918 -423 -544 11 O HETATM 2467 O HOH S 111 -26.616 1.810 26.118 1.00 49.23 O ANISOU 2467 O HOH S 111 5759 6622 6323 -428 777 -405 O HETATM 2468 O HOH S 112 -28.039 -8.865 -12.624 1.00 53.03 O ANISOU 2468 O HOH S 112 7531 7696 4921 133 -1023 62 O HETATM 2469 O HOH S 113 -30.333 -15.584 7.386 1.00 55.58 O ANISOU 2469 O HOH S 113 7521 6688 6907 -686 -558 8 O HETATM 2470 O HOH S 115 -11.738 0.344 5.256 1.00 53.88 O ANISOU 2470 O HOH S 115 6550 7423 6497 -101 586 211 O HETATM 2471 O HOH S 116 -5.458 -8.083 0.327 1.00 45.74 O ANISOU 2471 O HOH S 116 5245 7295 4840 572 654 -904 O HETATM 2472 O HOH S 117 -31.683 19.027 37.024 1.00 54.19 O ANISOU 2472 O HOH S 117 5155 7544 7891 709 899 -2907 O HETATM 2473 O HOH S 118 -13.447 -32.346 0.112 1.00 57.16 O ANISOU 2473 O HOH S 118 9012 5756 6951 1744 -2265 -2189 O HETATM 2474 O HOH S 119 -27.695 18.150 22.464 1.00 46.54 O ANISOU 2474 O HOH S 119 4854 5082 7749 611 40 -993 O HETATM 2475 O HOH S 120 -21.801 3.422 -8.557 1.00 52.15 O ANISOU 2475 O HOH S 120 7278 7318 5217 -306 -191 1259 O HETATM 2476 O HOH S 122 -8.272 13.701 42.776 1.00 56.94 O ANISOU 2476 O HOH S 122 7019 7464 7151 55 -216 -2138 O HETATM 2477 O HOH S 123 -2.293 -22.630 0.807 1.00 72.13 O ANISOU 2477 O HOH S 123 9039 9795 8572 2240 -816 -2609 O HETATM 2478 O HOH S 125 -4.609 -17.621 8.217 1.00 53.38 O ANISOU 2478 O HOH S 125 6881 6930 6471 1562 -682 -1544 O HETATM 2479 O HOH S 126 -8.324 12.959 23.593 1.00 55.00 O ANISOU 2479 O HOH S 126 6270 6598 8030 -310 299 -501 O HETATM 2480 O HOH S 127 -10.837 0.764 30.175 1.00 43.35 O ANISOU 2480 O HOH S 127 5582 5564 5326 22 46 -518 O HETATM 2481 O HOH S 128 -12.046 -19.771 -8.012 1.00 66.10 O ANISOU 2481 O HOH S 128 8894 9506 6715 1310 -401 -1965 O HETATM 2482 O HOH S 129 -29.569 12.380 40.632 1.00 48.33 O ANISOU 2482 O HOH S 129 4912 7587 5863 -54 1448 -2458 O HETATM 2483 O HOH S 130 -1.385 30.730 30.448 1.00 59.24 O ANISOU 2483 O HOH S 130 6653 5311 10545 -1220 -729 -1590 O HETATM 2484 O HOH S 131 -6.703 -8.582 -2.565 1.00 55.35 O ANISOU 2484 O HOH S 131 6603 8685 5744 535 692 -891 O HETATM 2485 O HOH S 132 -30.042 -7.801 1.936 1.00 54.10 O ANISOU 2485 O HOH S 132 6918 6995 6643 -196 -478 162 O HETATM 2486 O HOH S 134 -17.537 4.400 46.715 1.00 58.99 O ANISOU 2486 O HOH S 134 8137 8760 5516 -571 597 -1412 O HETATM 2487 O HOH S 136 -11.786 -7.286 -9.629 1.00 59.51 O ANISOU 2487 O HOH S 136 7692 9512 5406 188 633 -407 O HETATM 2488 O HOH S 137 -10.816 8.005 11.580 1.00 54.74 O ANISOU 2488 O HOH S 137 6455 6977 7365 -383 581 322 O HETATM 2489 O HOH S 139 -6.288 4.642 37.108 1.00 49.83 O ANISOU 2489 O HOH S 139 6357 6536 6042 115 -333 -1119 O HETATM 2490 O HOH S 140 -29.648 -6.086 3.753 1.00 57.61 O ANISOU 2490 O HOH S 140 7257 7421 7213 -193 -334 220 O HETATM 2491 O HOH S 141 -27.816 26.100 35.541 1.00 56.94 O ANISOU 2491 O HOH S 141 5800 6600 9235 1144 74 -3064 O HETATM 2492 O HOH S 142 -16.195 20.340 41.978 1.00 54.77 O ANISOU 2492 O HOH S 142 6316 6907 7586 343 214 -2851 O HETATM 2493 O HOH S 143 -19.098 26.280 35.314 1.00 59.11 O ANISOU 2493 O HOH S 143 6635 6228 9597 648 -166 -2662 O HETATM 2494 O HOH S 144 -19.985 25.801 18.773 1.00 68.54 O ANISOU 2494 O HOH S 144 8389 6447 11205 152 -585 -256 O HETATM 2495 O HOH S 145 -31.487 0.223 19.611 1.00 57.11 O ANISOU 2495 O HOH S 145 6462 7589 7650 -440 569 -225 O HETATM 2496 O HOH S 148 -28.293 4.634 -0.337 1.00 61.81 O ANISOU 2496 O HOH S 148 7869 7786 7832 50 -514 874 O HETATM 2497 O HOH S 149 -24.638 11.134 26.714 1.00 41.72 O ANISOU 2497 O HOH S 149 4466 5252 6133 102 599 -903 O HETATM 2498 O HOH S 150 -20.840 -20.453 22.575 1.00 42.47 O ANISOU 2498 O HOH S 150 7307 4111 4716 -734 -874 486 O HETATM 2499 O HOH S 151 -4.624 5.446 22.515 1.00 39.37 O ANISOU 2499 O HOH S 151 4250 5155 5553 0 246 0 O HETATM 2500 O HOH S 152 -14.927 -20.932 -11.781 1.00 60.54 O ANISOU 2500 O HOH S 152 8474 8915 5612 1245 -622 -2092 O HETATM 2501 O HOH S 156 -30.020 14.711 37.470 1.00 55.85 O ANISOU 2501 O HOH S 156 5636 8078 7504 281 1199 -2501 O HETATM 2502 O HOH S 157 -3.078 32.851 31.130 1.00 66.41 O ANISOU 2502 O HOH S 157 7752 5877 11604 -1051 -894 -1703 O HETATM 2503 O HOH S 159 -13.597 -18.087 -11.930 1.00 59.54 O ANISOU 2503 O HOH S 159 8127 9174 5323 1089 -236 -1823 O HETATM 2504 O HOH S 161 -8.757 -13.471 24.879 1.00 58.18 O ANISOU 2504 O HOH S 161 8405 6749 6950 562 -935 -266 O HETATM 2505 O HOH S 162 -13.347 13.144 0.492 1.00 60.15 O ANISOU 2505 O HOH S 162 7802 7556 7496 -981 460 1515 O HETATM 2506 O HOH S 163 -31.840 -9.902 13.759 1.00 46.16 O ANISOU 2506 O HOH S 163 5771 5867 5900 -857 54 134 O HETATM 2507 O HOH S 164 -21.068 -25.339 -5.336 1.00 52.71 O ANISOU 2507 O HOH S 164 8067 6251 5709 784 -1514 -1634 O HETATM 2508 O HOH S 166 -22.948 -28.093 10.934 1.00 59.76 O ANISOU 2508 O HOH S 166 9807 5524 7377 -355 -1778 -248 O HETATM 2509 O HOH S 167 -29.504 18.450 24.353 1.00 62.69 O ANISOU 2509 O HOH S 167 6673 7307 9839 744 123 -1360 O HETATM 2510 O HOH S 168 -12.402 18.164 20.410 1.00 58.38 O ANISOU 2510 O HOH S 168 6854 6392 8935 -379 178 -197 O HETATM 2511 O HOH S 169 -29.566 5.945 17.948 1.00 48.08 O ANISOU 2511 O HOH S 169 5239 6123 6905 -9 379 -252 O HETATM 2512 O HOH S 172 -19.083 -21.173 -10.515 1.00 53.34 O ANISOU 2512 O HOH S 172 7789 7469 5008 936 -961 -1702 O END