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*** ***elNémo ID: 240109110516359579Job options:ID = 240109110516359579 JOBID = USERID = unknown PRIVAT = 0 NMODES = 5 DQMIN = -100 DQMAX = 100 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = 0 DORMSD = 0 NRBL = 0 CUTOFF = 0 CAONLY = 0 Input data for this run:CRYST1 54.350 63.372 78.665 90.00 90.00 90.00 P 21 21 21 1 ATOM 1 N ALA A 2 -8.507 26.369 18.831 1.00 20.31 N ANISOU 1 N ALA A 2 2657 2521 2537 164 -33 -240 N ATOM 2 CA ALA A 2 -7.539 25.539 18.092 1.00 16.55 C ANISOU 2 CA ALA A 2 2166 2054 2069 123 -46 -211 C ATOM 3 C ALA A 2 -6.247 25.534 18.881 1.00 17.42 C ANISOU 3 C ALA A 2 2300 2162 2155 110 -71 -225 C ATOM 4 O ALA A 2 -5.967 26.482 19.659 1.00 20.04 O ANISOU 4 O ALA A 2 2664 2472 2476 124 -93 -257 O ATOM 5 CB ALA A 2 -7.345 26.069 16.765 1.00 17.91 C ANISOU 5 CB ALA A 2 2325 2200 2280 100 -67 -195 C ATOM 6 N VAL A 3 -5.454 24.472 18.731 1.00 11.32 N ANISOU 6 N VAL A 3 1516 1411 1376 86 -71 -203 N ATOM 7 CA VAL A 3 -4.229 24.282 19.489 1.00 11.91 C ANISOU 7 CA VAL A 3 1606 1490 1428 74 -94 -210 C ATOM 8 C VAL A 3 -3.096 23.960 18.529 1.00 11.80 C ANISOU 8 C VAL A 3 1573 1474 1438 39 -113 -184 C ATOM 9 O VAL A 3 -3.312 23.696 17.343 1.00 12.16 O ANISOU 9 O VAL A 3 1594 1519 1508 26 -103 -161 O ATOM 10 CB VAL A 3 -4.347 23.178 20.549 1.00 11.98 C ANISOU 10 CB VAL A 3 1621 1534 1395 88 -71 -208 C ATOM 11 CG1 VAL A 3 -5.445 23.569 21.590 1.00 17.08 C ANISOU 11 CG1 VAL A 3 2288 2189 2013 127 -47 -234 C ATOM 12 CG2 VAL A 3 -4.644 21.788 19.982 1.00 12.34 C ANISOU 12 CG2 VAL A 3 1638 1605 1445 78 -42 -174 C ATOM 13 N ARG A 4 -1.881 23.968 19.063 1.00 9.75 N ANISOU 13 N ARG A 4 1321 1215 1167 24 -141 -187 N ATOM 14 CA ARG A 4 -0.646 23.749 18.310 1.00 8.74 C ANISOU 14 CA ARG A 4 1173 1088 1061 -7 -161 -162 C ATOM 15 C ARG A 4 0.098 22.509 18.786 1.00 9.01 C ANISOU 15 C ARG A 4 1197 1152 1073 -9 -155 -148 C ATOM 16 O ARG A 4 0.065 22.140 19.972 1.00 11.19 O ANISOU 16 O ARG A 4 1492 1442 1316 6 -155 -161 O ATOM 17 CB ARG A 4 0.333 24.947 18.412 1.00 9.57 C ANISOU 17 CB ARG A 4 1288 1165 1185 -28 -207 -172 C ATOM 18 CG ARG A 4 -0.232 26.216 17.830 1.00 7.89 C ANISOU 18 CG ARG A 4 1083 915 999 -29 -219 -182 C ATOM 19 CD ARG A 4 0.771 27.298 18.024 1.00 9.53 C ANISOU 19 CD ARG A 4 1302 1093 1225 -53 -268 -190 C ATOM 20 NE ARG A 4 0.429 28.599 17.391 1.00 12.36 N ANISOU 20 NE ARG A 4 1670 1409 1618 -60 -288 -194 N ATOM 21 CZ ARG A 4 -0.199 29.590 18.002 1.00 18.50 C ANISOU 21 CZ ARG A 4 2483 2153 2394 -40 -303 -230 C ATOM 22 NH1 ARG A 4 -0.601 29.441 19.251 1.00 18.87 N1+ ANISOU 22 NH1 ARG A 4 2560 2207 2402 -9 -298 -265 N1+ ATOM 23 NH2 ARG A 4 -0.398 30.763 17.374 1.00 17.24 N ANISOU 23 NH2 ARG A 4 2330 1950 2269 -48 -326 -230 N ATOM 24 N ALA A 5 0.835 21.861 17.865 1.00 8.05 N ANISOU 24 N ALA A 5 1049 1042 970 -27 -152 -119 N ATOM 25 CA ALA A 5 1.602 20.687 18.221 1.00 9.68 C ANISOU 25 CA ALA A 5 1245 1273 1160 -27 -149 -103 C ATOM 26 C ALA A 5 2.808 20.568 17.302 1.00 10.04 C ANISOU 26 C ALA A 5 1261 1324 1231 -48 -160 -77 C ATOM 27 O ALA A 5 2.895 21.223 16.262 1.00 9.77 O ANISOU 27 O ALA A 5 1213 1277 1223 -62 -163 -68 O ATOM 28 CB ALA A 5 0.769 19.367 18.166 1.00 9.24 C ANISOU 28 CB ALA A 5 1186 1235 1088 -10 -111 -92 C ATOM 29 N GLN A 6 3.727 19.671 17.691 1.00 10.23 N ANISOU 29 N GLN A 6 1274 1368 1245 -46 -165 -64 N ATOM 30 CA GLN A 6 4.923 19.394 16.912 1.00 10.54 C ANISOU 30 CA GLN A 6 1281 1419 1305 -60 -170 -37 C ATOM 31 C GLN A 6 5.289 17.925 17.150 1.00 9.42 C ANISOU 31 C GLN A 6 1131 1300 1148 -43 -154 -23 C ATOM 32 O GLN A 6 5.274 17.463 18.293 1.00 12.46 O ANISOU 32 O GLN A 6 1533 1692 1510 -32 -161 -30 O ATOM 33 CB GLN A 6 6.036 20.317 17.339 1.00 14.21 C ANISOU 33 CB GLN A 6 1737 1878 1784 -81 -212 -36 C ATOM 34 CG GLN A 6 7.297 20.201 16.503 1.00 18.40 C ANISOU 34 CG GLN A 6 2227 2425 2341 -97 -217 -3 C ATOM 35 CD GLN A 6 8.351 21.194 16.994 1.00 22.83 C ANISOU 35 CD GLN A 6 2776 2977 2919 -124 -264 0 C ATOM 36 NE2 GLN A 6 8.368 22.355 16.398 1.00 19.07 N ANISOU 36 NE2 GLN A 6 2296 2480 2469 -148 -280 4 N ATOM 37 OE1 GLN A 6 9.097 20.913 17.932 1.00 24.53 O ANISOU 37 OE1 GLN A 6 2989 3204 3126 -124 -290 1 O ATOM 38 N PHE A 7 5.629 17.189 16.093 1.00 11.10 N ANISOU 38 N PHE A 7 1322 1523 1373 -39 -133 -2 N ATOM 39 CA PHE A 7 6.064 15.811 16.240 1.00 11.32 C ANISOU 39 CA PHE A 7 1344 1567 1390 -21 -120 11 C ATOM 40 C PHE A 7 7.532 15.710 15.882 1.00 12.05 C ANISOU 40 C PHE A 7 1401 1676 1500 -24 -132 34 C ATOM 41 O PHE A 7 7.918 15.928 14.740 1.00 13.08 O ANISOU 41 O PHE A 7 1510 1812 1649 -30 -120 48 O ATOM 42 CB PHE A 7 5.240 14.892 15.330 1.00 10.92 C ANISOU 42 CB PHE A 7 1300 1513 1338 -7 -87 14 C ATOM 43 CG PHE A 7 5.674 13.418 15.429 1.00 10.52 C ANISOU 43 CG PHE A 7 1247 1472 1279 14 -75 27 C ATOM 44 CD1 PHE A 7 5.335 12.692 16.564 1.00 16.73 C ANISOU 44 CD1 PHE A 7 2052 2258 2045 24 -78 24 C ATOM 45 CD2 PHE A 7 6.458 12.865 14.468 1.00 14.39 C ANISOU 45 CD2 PHE A 7 1716 1971 1780 24 -63 42 C ATOM 46 CE1 PHE A 7 5.728 11.334 16.704 1.00 18.56 C ANISOU 46 CE1 PHE A 7 2285 2493 2272 44 -71 38 C ATOM 47 CE2 PHE A 7 6.868 11.495 14.577 1.00 15.86 C ANISOU 47 CE2 PHE A 7 1903 2161 1960 48 -54 51 C ATOM 48 CZ PHE A 7 6.498 10.777 15.693 1.00 16.02 C ANISOU 48 CZ PHE A 7 1945 2176 1965 56 -60 50 C ATOM 49 N GLU A 8 8.358 15.349 16.866 1.00 16.94 N ANISOU 49 N GLU A 8 2015 2308 2114 -19 -153 40 N ATOM 50 CA GLU A 8 9.804 15.170 16.646 1.00 23.37 C ANISOU 50 CA GLU A 8 2790 3143 2947 -20 -165 65 C ATOM 51 C GLU A 8 10.379 16.248 15.734 1.00 21.29 C ANISOU 51 C GLU A 8 2497 2882 2711 -44 -171 78 C ATOM 52 O GLU A 8 10.995 15.975 14.696 1.00 25.12 O ANISOU 52 O GLU A 8 2950 3382 3211 -38 -151 100 O ATOM 53 CB GLU A 8 10.126 13.791 16.067 1.00 23.47 C ANISOU 53 CB GLU A 8 2790 3168 2959 9 -136 81 C ATOM 54 CG GLU A 8 9.484 12.655 16.830 1.00 28.98 C ANISOU 54 CG GLU A 8 3519 3859 3633 31 -128 73 C ATOM 55 CD GLU A 8 9.912 11.249 16.384 1.00 48.52 C ANISOU 55 CD GLU A 8 5985 6340 6109 61 -107 88 C ATOM 56 OE1 GLU A 8 10.432 11.075 15.255 1.00 50.75 O ANISOU 56 OE1 GLU A 8 6244 6631 6406 71 -88 99 O ATOM 57 OE2 GLU A 8 9.676 10.304 17.181 1.00 55.40 O1- ANISOU 57 OE2 GLU A 8 6877 7207 6966 77 -110 89 O1- ATOM 58 N AASN A 9 10.110 17.489 16.105 0.36 22.40 N ANISOU 58 N AASN A 9 2649 3004 2857 -69 -198 65 N ATOM 59 N BASN A 9 10.184 17.475 16.150 0.64 21.10 N ANISOU 59 N BASN A 9 2483 2840 2692 -69 -200 66 N ATOM 60 CA AASN A 9 10.686 18.661 15.428 0.36 22.55 C ANISOU 60 CA AASN A 9 2642 3020 2905 -99 -214 80 C ATOM 61 CA BASN A 9 10.714 18.676 15.467 0.64 22.02 C ANISOU 61 CA BASN A 9 2574 2952 2838 -99 -216 80 C ATOM 62 C AASN A 9 10.227 18.768 13.949 0.36 19.10 C ANISOU 62 C AASN A 9 2197 2582 2477 -98 -178 90 C ATOM 63 C BASN A 9 10.005 19.070 14.169 0.64 19.93 C ANISOU 63 C BASN A 9 2312 2678 2581 -104 -187 82 C ATOM 64 O AASN A 9 10.906 19.296 13.054 0.36 15.21 O ANISOU 64 O AASN A 9 1672 2100 2007 -115 -176 116 O ATOM 65 O BASN A 9 10.395 20.094 13.592 0.64 19.80 O ANISOU 65 O BASN A 9 2277 2657 2589 -130 -200 97 O ATOM 66 CB AASN A 9 12.204 18.643 15.683 0.36 29.43 C ANISOU 66 CB AASN A 9 3470 3915 3798 -110 -240 108 C ATOM 67 CB BASN A 9 12.221 18.566 15.173 0.64 29.90 C ANISOU 67 CB BASN A 9 3520 3978 3861 -108 -226 115 C ATOM 68 CG AASN A 9 13.029 18.982 14.508 0.36 31.31 C ANISOU 68 CG AASN A 9 3661 4170 4064 -123 -228 142 C ATOM 69 CG BASN A 9 13.051 18.444 16.456 0.64 30.12 C ANISOU 69 CG BASN A 9 3542 4014 3888 -112 -267 117 C ATOM 70 ND2AASN A 9 13.630 20.175 14.537 0.36 35.72 N ANISOU 70 ND2AASN A 9 4200 4721 4651 -161 -263 156 N ATOM 71 ND2BASN A 9 12.759 19.295 17.422 0.64 27.63 N ANISOU 71 ND2BASN A 9 3256 3677 3566 -131 -306 94 N ATOM 72 OD1AASN A 9 13.166 18.178 13.582 0.36 36.16 O ANISOU 72 OD1AASN A 9 4258 4805 4677 -101 -188 158 O ATOM 73 OD1BASN A 9 13.921 17.579 16.575 0.64 39.90 O ANISOU 73 OD1BASN A 9 4750 5278 5129 -95 -264 138 O ATOM 74 N SER A 10 8.997 18.334 13.696 1.00 12.23 N ANISOU 74 N SER A 10 1359 1701 1588 -82 -152 70 N ATOM 75 CA SER A 10 8.251 18.730 12.499 1.00 10.10 C ANISOU 75 CA SER A 10 1094 1421 1323 -86 -130 71 C ATOM 76 C SER A 10 6.911 19.345 12.882 1.00 10.65 C ANISOU 76 C SER A 10 1201 1462 1384 -89 -136 43 C ATOM 77 O SER A 10 6.183 18.786 13.709 1.00 10.58 O ANISOU 77 O SER A 10 1217 1448 1355 -73 -132 23 O ATOM 78 CB SER A 10 7.916 17.510 11.633 1.00 10.23 C ANISOU 78 CB SER A 10 1113 1450 1324 -60 -92 75 C ATOM 79 OG SER A 10 7.139 17.851 10.525 1.00 9.63 O ANISOU 79 OG SER A 10 1046 1364 1247 -64 -74 75 O ATOM 80 N ASN A 11 6.577 20.443 12.223 1.00 9.08 N ANISOU 80 N ASN A 11 1003 1247 1202 -108 -143 46 N ATOM 81 CA ASN A 11 5.262 21.082 12.394 1.00 8.87 C ANISOU 81 CA ASN A 11 1006 1192 1171 -106 -145 22 C ATOM 82 C ASN A 11 4.191 20.528 11.452 1.00 8.00 C ANISOU 82 C ASN A 11 906 1083 1052 -93 -113 21 C ATOM 83 O ASN A 11 3.077 21.054 11.402 1.00 8.81 O ANISOU 83 O ASN A 11 1026 1165 1155 -91 -113 7 O ATOM 84 CB ASN A 11 5.407 22.600 12.242 1.00 11.63 C ANISOU 84 CB ASN A 11 1356 1518 1546 -133 -174 25 C ATOM 85 CG ASN A 11 6.216 23.203 13.397 1.00 13.66 C ANISOU 85 CG ASN A 11 1615 1766 1810 -147 -214 16 C ATOM 86 ND2 ASN A 11 6.904 24.284 13.136 1.00 16.07 N ANISOU 86 ND2 ASN A 11 1906 2056 2142 -177 -243 31 N ATOM 87 OD1 ASN A 11 6.245 22.645 14.479 1.00 13.94 O ANISOU 87 OD1 ASN A 11 1663 1808 1825 -133 -219 -1 O ATOM 88 N GLU A 12 4.487 19.433 10.736 1.00 7.89 N ANISOU 88 N GLU A 12 880 1090 1028 -80 -89 35 N ATOM 89 CA GLU A 12 3.525 18.886 9.797 1.00 7.79 C ANISOU 89 CA GLU A 12 878 1075 1006 -70 -65 33 C ATOM 90 C GLU A 12 2.580 17.896 10.473 1.00 9.52 C ANISOU 90 C GLU A 12 1119 1291 1208 -52 -54 15 C ATOM 91 O GLU A 12 2.648 16.664 10.317 1.00 8.03 O ANISOU 91 O GLU A 12 932 1112 1007 -37 -38 17 O ATOM 92 CB GLU A 12 4.280 18.269 8.618 1.00 8.22 C ANISOU 92 CB GLU A 12 916 1152 1057 -65 -45 55 C ATOM 93 CG GLU A 12 5.080 19.303 7.828 1.00 10.98 C ANISOU 93 CG GLU A 12 1242 1508 1423 -85 -52 80 C ATOM 94 CD GLU A 12 4.153 20.374 7.221 1.00 13.28 C ANISOU 94 CD GLU A 12 1545 1778 1724 -100 -60 79 C ATOM 95 OE1 GLU A 12 4.086 21.453 7.851 1.00 19.95 O ANISOU 95 OE1 GLU A 12 2392 2602 2586 -117 -85 75 O ATOM 96 OE2 GLU A 12 3.508 20.141 6.151 1.00 16.66 O1- ANISOU 96 OE2 GLU A 12 1981 2207 2140 -95 -44 84 O1- ATOM 97 N VAL A 13 1.658 18.477 11.270 1.00 7.97 N ANISOU 97 N VAL A 13 938 1078 1012 -52 -63 -3 N ATOM 98 CA VAL A 13 0.821 17.657 12.161 1.00 8.13 C ANISOU 98 CA VAL A 13 975 1099 1016 -37 -53 -16 C ATOM 99 C VAL A 13 0.028 16.638 11.367 1.00 8.06 C ANISOU 99 C VAL A 13 971 1091 1002 -30 -33 -11 C ATOM 100 O VAL A 13 -0.134 15.483 11.808 1.00 8.75 O ANISOU 100 O VAL A 13 1065 1183 1077 -20 -23 -11 O ATOM 101 CB VAL A 13 -0.117 18.604 12.945 1.00 9.96 C ANISOU 101 CB VAL A 13 1220 1316 1249 -36 -61 -34 C ATOM 102 CG1 VAL A 13 -1.246 17.777 13.709 1.00 10.52 C ANISOU 102 CG1 VAL A 13 1303 1391 1303 -21 -43 -43 C ATOM 103 CG2 VAL A 13 0.694 19.508 13.863 1.00 11.82 C ANISOU 103 CG2 VAL A 13 1458 1546 1485 -42 -86 -44 C ATOM 104 N GLY A 14 -0.491 17.028 10.176 1.00 7.95 N ANISOU 104 N GLY A 14 954 1070 997 -37 -30 -6 N ATOM 105 CA GLY A 14 -1.294 16.125 9.367 1.00 7.86 C ANISOU 105 CA GLY A 14 950 1057 980 -34 -18 -4 C ATOM 106 C GLY A 14 -0.522 14.974 8.776 1.00 8.12 C ANISOU 106 C GLY A 14 985 1100 1003 -25 -8 4 C ATOM 107 O GLY A 14 -1.157 14.011 8.347 1.00 9.89 O ANISOU 107 O GLY A 14 1221 1318 1220 -20 -2 2 O ATOM 108 N VAL A 15 0.809 15.031 8.768 1.00 7.31 N ANISOU 108 N VAL A 15 869 1010 899 -22 -8 12 N ATOM 109 CA VAL A 15 1.573 13.884 8.296 1.00 8.49 C ANISOU 109 CA VAL A 15 1020 1170 1038 -6 4 17 C ATOM 110 C VAL A 15 1.614 12.800 9.347 1.00 8.46 C ANISOU 110 C VAL A 15 1025 1163 1028 7 5 13 C ATOM 111 O VAL A 15 1.724 11.605 9.011 1.00 8.64 O ANISOU 111 O VAL A 15 1058 1182 1042 22 13 12 O ATOM 112 CB VAL A 15 2.995 14.385 7.926 1.00 8.90 C ANISOU 112 CB VAL A 15 1047 1241 1094 -6 5 32 C ATOM 113 CG1 VAL A 15 3.911 13.209 7.523 1.00 10.78 C ANISOU 113 CG1 VAL A 15 1282 1492 1321 18 21 38 C ATOM 114 CG2 VAL A 15 2.843 15.299 6.721 1.00 10.36 C ANISOU 114 CG2 VAL A 15 1226 1427 1281 -19 7 41 C ATOM 115 N PHE A 16 1.509 13.167 10.638 1.00 7.67 N ANISOU 115 N PHE A 16 923 1062 929 2 -5 9 N ATOM 116 CA PHE A 16 1.752 12.236 11.755 1.00 7.83 C ANISOU 116 CA PHE A 16 950 1084 941 14 -6 10 C ATOM 117 C PHE A 16 0.506 11.944 12.577 1.00 8.52 C ANISOU 117 C PHE A 16 1052 1161 1022 11 -4 4 C ATOM 118 O PHE A 16 0.596 11.284 13.638 1.00 8.38 O ANISOU 118 O PHE A 16 1042 1147 996 18 -5 8 O ATOM 119 CB PHE A 16 2.856 12.822 12.668 1.00 8.57 C ANISOU 119 CB PHE A 16 1029 1192 1036 13 -21 14 C ATOM 120 CG PHE A 16 4.120 13.108 11.904 1.00 8.70 C ANISOU 120 CG PHE A 16 1022 1222 1062 14 -22 25 C ATOM 121 CD1 PHE A 16 4.958 12.068 11.542 1.00 10.57 C ANISOU 121 CD1 PHE A 16 1251 1468 1296 34 -12 35 C ATOM 122 CD2 PHE A 16 4.459 14.398 11.585 1.00 8.85 C ANISOU 122 CD2 PHE A 16 1026 1244 1093 -3 -32 28 C ATOM 123 CE1 PHE A 16 6.147 12.330 10.844 1.00 13.32 C ANISOU 123 CE1 PHE A 16 1572 1835 1653 38 -8 49 C ATOM 124 CE2 PHE A 16 5.631 14.664 10.865 1.00 10.52 C ANISOU 124 CE2 PHE A 16 1210 1473 1315 -5 -30 46 C ATOM 125 CZ PHE A 16 6.470 13.617 10.508 1.00 12.78 C ANISOU 125 CZ PHE A 16 1485 1774 1597 17 -16 57 C ATOM 126 N ALA A 17 -0.671 12.445 12.168 1.00 8.16 N ANISOU 126 N ALA A 17 1011 1108 983 1 -1 -1 N ATOM 127 CA ALA A 17 -1.899 12.198 12.895 1.00 7.51 C ANISOU 127 CA ALA A 17 937 1020 898 -2 5 -2 C ATOM 128 C ALA A 17 -3.092 12.189 11.959 1.00 7.87 C ANISOU 128 C ALA A 17 983 1055 954 -11 8 -2 C ATOM 129 O ALA A 17 -3.040 12.781 10.876 1.00 8.86 O ANISOU 129 O ALA A 17 1104 1176 1086 -16 4 -4 O ATOM 130 CB ALA A 17 -2.165 13.324 13.902 1.00 9.93 C ANISOU 130 CB ALA A 17 1241 1333 1199 -2 1 -12 C ATOM 131 N THR A 18 -4.165 11.480 12.365 1.00 9.77 N ANISOU 131 N THR A 18 1228 1290 1195 -14 15 5 N ATOM 132 CA THR A 18 -5.459 11.458 11.674 1.00 10.17 C ANISOU 132 CA THR A 18 1275 1332 1258 -25 15 8 C ATOM 133 C THR A 18 -6.505 11.782 12.731 1.00 13.15 C ANISOU 133 C THR A 18 1643 1718 1637 -25 26 12 C ATOM 134 O THR A 18 -6.489 11.180 13.804 1.00 16.84 O ANISOU 134 O THR A 18 2113 2192 2092 -21 34 20 O ATOM 135 CB THR A 18 -5.692 10.078 11.054 1.00 12.19 C ANISOU 135 CB THR A 18 1542 1572 1516 -31 11 16 C ATOM 136 CG2 THR A 18 -7.139 9.939 10.512 1.00 16.10 C ANISOU 136 CG2 THR A 18 2031 2058 2027 -47 6 23 C ATOM 137 OG1 THR A 18 -4.789 9.869 9.950 1.00 14.34 O ANISOU 137 OG1 THR A 18 1825 1838 1784 -26 5 9 O ATOM 138 N LEU A 19 -7.360 12.763 12.504 1.00 9.06 N ANISOU 138 N LEU A 19 1112 1201 1129 -27 27 8 N ATOM 139 CA LEU A 19 -8.405 13.127 13.451 1.00 9.01 C ANISOU 139 CA LEU A 19 1094 1206 1124 -21 41 11 C ATOM 140 C LEU A 19 -9.760 13.083 12.760 1.00 10.79 C ANISOU 140 C LEU A 19 1302 1427 1371 -32 41 23 C ATOM 141 O LEU A 19 -9.924 13.676 11.685 1.00 11.30 O ANISOU 141 O LEU A 19 1363 1483 1449 -37 28 18 O ATOM 142 CB LEU A 19 -8.136 14.552 13.969 1.00 9.24 C ANISOU 142 CB LEU A 19 1124 1241 1148 -7 41 -7 C ATOM 143 CG LEU A 19 -9.145 15.077 14.971 1.00 8.25 C ANISOU 143 CG LEU A 19 988 1128 1018 8 59 -9 C ATOM 144 CD1 LEU A 19 -9.180 14.229 16.257 1.00 10.35 C ANISOU 144 CD1 LEU A 19 1261 1412 1261 14 77 1 C ATOM 145 CD2 LEU A 19 -8.819 16.555 15.314 1.00 10.29 C ANISOU 145 CD2 LEU A 19 1254 1382 1273 24 53 -33 C ATOM 146 N THR A 20 -10.695 12.341 13.331 1.00 9.20 N ANISOU 146 N THR A 20 1089 1234 1173 -37 53 41 N ATOM 147 CA THR A 20 -12.071 12.242 12.808 1.00 9.43 C ANISOU 147 CA THR A 20 1095 1262 1227 -49 52 57 C ATOM 148 C THR A 20 -13.033 12.554 13.943 1.00 9.42 C ANISOU 148 C THR A 20 1072 1284 1225 -37 78 68 C ATOM 149 O THR A 20 -12.641 12.855 15.092 1.00 10.42 O ANISOU 149 O THR A 20 1206 1425 1328 -18 96 60 O ATOM 150 CB THR A 20 -12.406 10.862 12.222 1.00 9.27 C ANISOU 150 CB THR A 20 1078 1228 1218 -73 38 76 C ATOM 151 CG2 THR A 20 -11.279 10.306 11.372 1.00 9.66 C ANISOU 151 CG2 THR A 20 1156 1257 1258 -78 19 64 C ATOM 152 OG1 THR A 20 -12.653 9.951 13.289 1.00 10.78 O ANISOU 152 OG1 THR A 20 1266 1427 1403 -77 53 96 O ATOM 153 N ASN A 21 -14.344 12.541 13.602 1.00 11.28 N ANISOU 153 N ASN A 21 1276 1523 1485 -45 79 87 N ATOM 154 CA ASN A 21 -15.322 12.780 14.656 1.00 11.82 C ANISOU 154 CA ASN A 21 1318 1619 1553 -31 109 101 C ATOM 155 C ASN A 21 -15.527 11.600 15.589 1.00 13.15 C ANISOU 155 C ASN A 21 1484 1801 1712 -41 127 128 C ATOM 156 O ASN A 21 -16.185 11.789 16.617 1.00 15.56 O ANISOU 156 O ASN A 21 1770 2135 2009 -26 158 141 O ATOM 157 CB ASN A 21 -16.681 13.162 14.036 1.00 12.51 C ANISOU 157 CB ASN A 21 1367 1711 1674 -35 107 117 C ATOM 158 CG ASN A 21 -16.629 14.542 13.408 1.00 18.14 C ANISOU 158 CG ASN A 21 2081 2415 2396 -17 96 93 C ATOM 159 ND2 ASN A 21 -17.105 14.663 12.135 1.00 21.84 N ANISOU 159 ND2 ASN A 21 2538 2869 2891 -33 69 100 N ATOM 160 OD1 ASN A 21 -16.056 15.444 13.978 1.00 13.23 O ANISOU 160 OD1 ASN A 21 1475 1796 1756 9 106 69 O ATOM 161 N SER A 22 -14.889 10.457 15.327 1.00 10.28 N ANISOU 161 N SER A 22 1142 1419 1346 -63 110 136 N ATOM 162 CA SER A 22 -15.067 9.343 16.236 1.00 10.28 C ANISOU 162 CA SER A 22 1140 1429 1338 -74 124 165 C ATOM 163 C SER A 22 -13.763 8.732 16.738 1.00 10.32 C ANISOU 163 C SER A 22 1181 1424 1315 -70 120 157 C ATOM 164 O SER A 22 -13.836 7.873 17.649 1.00 11.69 O ANISOU 164 O SER A 22 1357 1608 1477 -75 133 183 O ATOM 165 CB SER A 22 -15.920 8.221 15.593 1.00 14.11 C ANISOU 165 CB SER A 22 1608 1898 1855 -110 107 198 C ATOM 166 OG SER A 22 -15.262 7.774 14.453 1.00 15.15 O ANISOU 166 OG SER A 22 1767 1995 1995 -125 73 182 O ATOM 167 N TYR A 23 -12.589 9.160 16.250 1.00 8.77 N ANISOU 167 N TYR A 23 1011 1213 1108 -59 103 126 N ATOM 168 CA TYR A 23 -11.329 8.595 16.772 1.00 9.74 C ANISOU 168 CA TYR A 23 1164 1331 1207 -52 98 120 C ATOM 169 C TYR A 23 -10.186 9.497 16.350 1.00 8.97 C ANISOU 169 C TYR A 23 1082 1227 1099 -37 86 87 C ATOM 170 O TYR A 23 -10.327 10.345 15.446 1.00 9.56 O ANISOU 170 O TYR A 23 1149 1295 1187 -37 77 71 O ATOM 171 CB TYR A 23 -11.045 7.137 16.320 1.00 9.63 C ANISOU 171 CB TYR A 23 1165 1290 1204 -73 80 138 C ATOM 172 CG TYR A 23 -11.046 6.987 14.821 1.00 8.29 C ANISOU 172 CG TYR A 23 1000 1092 1056 -86 54 126 C ATOM 173 CD1 TYR A 23 -9.867 7.190 14.075 1.00 8.52 C ANISOU 173 CD1 TYR A 23 1050 1108 1077 -75 40 100 C ATOM 174 CD2 TYR A 23 -12.230 6.712 14.136 1.00 8.93 C ANISOU 174 CD2 TYR A 23 1064 1165 1165 -109 45 141 C ATOM 175 CE1 TYR A 23 -9.853 7.120 12.648 1.00 9.13 C ANISOU 175 CE1 TYR A 23 1136 1165 1169 -84 19 87 C ATOM 176 CE2 TYR A 23 -12.206 6.605 12.691 1.00 10.42 C ANISOU 176 CE2 TYR A 23 1263 1328 1368 -120 17 127 C ATOM 177 CZ TYR A 23 -11.052 6.850 12.018 1.00 10.56 C ANISOU 177 CZ TYR A 23 1304 1336 1372 -106 7 100 C ATOM 178 OH TYR A 23 -10.990 6.811 10.612 1.00 13.42 O ANISOU 178 OH TYR A 23 1679 1678 1741 -113 -16 86 O ATOM 179 N CYS A 24 -9.018 9.255 16.939 1.00 8.93 N ANISOU 179 N CYS A 24 1098 1224 1072 -27 82 81 N ATOM 180 CA CYS A 24 -7.798 9.975 16.610 1.00 9.06 C ANISOU 180 CA CYS A 24 1126 1236 1081 -15 68 55 C ATOM 181 C CYS A 24 -6.656 8.997 16.533 1.00 10.55 C ANISOU 181 C CYS A 24 1332 1414 1264 -15 56 59 C ATOM 182 O CYS A 24 -6.559 8.171 17.422 1.00 10.26 O ANISOU 182 O CYS A 24 1303 1382 1215 -13 61 76 O ATOM 183 CB CYS A 24 -7.559 11.008 17.680 1.00 8.75 C ANISOU 183 CB CYS A 24 1089 1217 1019 3 77 40 C ATOM 184 SG CYS A 24 -6.048 11.942 17.516 1.00 15.01 S ANISOU 184 SG CYS A 24 1894 2005 1803 11 56 14 S ATOM 185 N LEU A 25 -5.833 9.045 15.465 1.00 8.10 N ANISOU 185 N LEU A 25 1026 1088 962 -15 41 46 N ATOM 186 CA LEU A 25 -4.625 8.233 15.379 1.00 7.84 C ANISOU 186 CA LEU A 25 1008 1048 924 -7 31 48 C ATOM 187 C LEU A 25 -3.442 9.154 15.510 1.00 8.26 C ANISOU 187 C LEU A 25 1058 1113 968 5 25 33 C ATOM 188 O LEU A 25 -3.418 10.231 14.893 1.00 9.75 O ANISOU 188 O LEU A 25 1237 1303 1163 2 22 19 O ATOM 189 CB LEU A 25 -4.517 7.478 14.020 1.00 10.21 C ANISOU 189 CB LEU A 25 1316 1324 1239 -12 22 46 C ATOM 190 CG LEU A 25 -5.785 6.805 13.482 1.00 11.68 C ANISOU 190 CG LEU A 25 1504 1493 1441 -30 19 57 C ATOM 191 CD1 LEU A 25 -5.446 6.184 12.122 1.00 13.89 C ANISOU 191 CD1 LEU A 25 1800 1750 1729 -30 6 47 C ATOM 192 CD2 LEU A 25 -6.341 5.783 14.469 1.00 10.00 C ANISOU 192 CD2 LEU A 25 1294 1275 1228 -37 24 82 C ATOM 193 N AVAL A 26 -2.454 8.759 16.308 0.46 8.74 N ANISOU 193 N AVAL A 26 1124 1180 1015 15 19 38 N ATOM 194 N BVAL A 26 -2.432 8.720 16.290 0.54 8.21 N ANISOU 194 N BVAL A 26 1058 1113 948 16 19 38 N ATOM 195 CA AVAL A 26 -1.213 9.539 16.343 0.46 9.48 C ANISOU 195 CA AVAL A 26 1212 1284 1104 23 8 27 C ATOM 196 CA BVAL A 26 -1.212 9.505 16.570 0.54 7.54 C ANISOU 196 CA BVAL A 26 968 1042 857 24 8 28 C ATOM 197 C AVAL A 26 -0.027 8.606 16.244 0.46 8.61 C ANISOU 197 C AVAL A 26 1105 1173 996 35 0 36 C ATOM 198 C BVAL A 26 0.019 8.620 16.370 0.54 10.05 C ANISOU 198 C BVAL A 26 1287 1356 1176 36 -1 36 C ATOM 199 O AVAL A 26 -0.055 7.453 16.699 0.46 11.30 O ANISOU 199 O AVAL A 26 1456 1506 1332 41 1 50 O ATOM 200 O BVAL A 26 0.058 7.481 16.862 0.54 8.81 O ANISOU 200 O BVAL A 26 1141 1193 1014 43 0 51 O ATOM 201 CB AVAL A 26 -1.083 10.426 17.594 0.46 10.38 C ANISOU 201 CB AVAL A 26 1327 1416 1200 26 3 19 C ATOM 202 CB BVAL A 26 -1.261 10.070 18.014 0.54 9.93 C ANISOU 202 CB BVAL A 26 1275 1361 1137 28 6 25 C ATOM 203 CG1AVAL A 26 -2.175 11.491 17.669 0.46 10.11 C ANISOU 203 CG1AVAL A 26 1291 1384 1167 21 12 6 C ATOM 204 CG1BVAL A 26 0.043 10.766 18.356 0.54 13.23 C ANISOU 204 CG1BVAL A 26 1689 1789 1549 32 -13 16 C ATOM 205 CG2AVAL A 26 -1.102 9.573 18.817 0.46 8.13 C ANISOU 205 CG2AVAL A 26 1055 1140 895 33 5 34 C ATOM 206 CG2BVAL A 26 -2.489 11.040 18.236 0.54 10.48 C ANISOU 206 CG2BVAL A 26 1343 1434 1203 23 18 14 C ATOM 207 N ALA A 27 1.051 9.147 15.686 1.00 9.27 N ANISOU 207 N ALA A 27 1175 1262 1085 40 -8 29 N ATOM 208 CA ALA A 27 2.268 8.384 15.481 1.00 9.63 C ANISOU 208 CA ALA A 27 1215 1309 1134 56 -13 38 C ATOM 209 C ALA A 27 2.889 8.002 16.812 1.00 11.90 C ANISOU 209 C ALA A 27 1506 1607 1409 65 -25 49 C ATOM 210 O ALA A 27 2.899 8.780 17.755 1.00 14.05 O ANISOU 210 O ALA A 27 1777 1892 1668 58 -34 45 O ATOM 211 CB ALA A 27 3.280 9.210 14.688 1.00 12.39 C ANISOU 211 CB ALA A 27 1543 1670 1493 57 -17 34 C ATOM 212 N LEU A 28 3.391 6.757 16.865 1.00 15.91 N ANISOU 212 N LEU A 28 2020 2107 1918 82 -26 63 N ATOM 213 CA LEU A 28 4.208 6.365 18.009 1.00 19.30 C ANISOU 213 CA LEU A 28 2448 2547 2337 93 -41 77 C ATOM 214 C LEU A 28 5.434 7.262 18.096 1.00 24.70 C ANISOU 214 C LEU A 28 3108 3253 3025 95 -57 75 C ATOM 215 O LEU A 28 6.146 7.468 17.106 1.00 28.41 O ANISOU 215 O LEU A 28 3557 3726 3511 100 -53 73 O ATOM 216 CB LEU A 28 4.676 4.912 17.847 1.00 27.54 C ANISOU 216 CB LEU A 28 3500 3574 3388 115 -41 93 C ATOM 217 CG LEU A 28 3.840 3.743 18.259 1.00 30.31 C ANISOU 217 CG LEU A 28 3878 3904 3736 115 -37 107 C ATOM 218 CD1 LEU A 28 4.831 2.587 18.227 1.00 22.45 C ANISOU 218 CD1 LEU A 28 2885 2896 2749 143 -45 121 C ATOM 219 CD2 LEU A 28 3.376 3.984 19.667 1.00 27.65 C ANISOU 219 CD2 LEU A 28 3549 3581 3376 104 -42 118 C ATOM 220 N GLY A 29 5.715 7.760 19.272 1.00 38.26 N ANISOU 220 N GLY A 29 4825 4984 4726 90 -75 77 N ATOM 221 CA GLY A 29 6.984 8.460 19.386 1.00 45.05 C ANISOU 221 CA GLY A 29 5660 5862 5594 89 -97 79 C ATOM 222 C GLY A 29 7.012 9.269 20.663 1.00 59.15 C ANISOU 222 C GLY A 29 7455 7660 7358 77 -121 72 C ATOM 223 O GLY A 29 6.301 8.963 21.623 1.00 55.81 O ANISOU 223 O GLY A 29 7057 7238 6910 78 -120 73 O ATOM 224 N ALA A 30 7.836 10.311 20.636 1.00 68.12 N ANISOU 224 N ALA A 30 8571 8808 8505 65 -144 67 N ATOM 225 CA ALA A 30 7.961 11.205 21.777 1.00 69.20 C ANISOU 225 CA ALA A 30 8719 8952 8621 52 -173 56 C ATOM 226 C ALA A 30 6.625 11.903 22.077 1.00 64.60 C ANISOU 226 C ALA A 30 8166 8361 8019 44 -160 32 C ATOM 227 O ALA A 30 6.082 12.613 21.217 1.00 65.20 O ANISOU 227 O ALA A 30 8237 8425 8110 34 -147 19 O ATOM 228 CB ALA A 30 9.074 12.209 21.482 1.00 72.94 C ANISOU 228 CB ALA A 30 9163 9433 9117 36 -202 56 C ATOM 229 N SER A 31 6.110 11.690 23.311 1.00 49.28 N ANISOU 229 N SER A 31 6255 6427 6043 50 -164 29 N ATOM 230 CA SER A 31 4.784 12.170 23.741 1.00 39.21 C ANISOU 230 CA SER A 31 5006 5148 4743 50 -145 10 C ATOM 231 C SER A 31 4.682 13.688 23.761 1.00 31.84 C ANISOU 231 C SER A 31 4078 4207 3811 38 -161 -19 C ATOM 232 O SER A 31 3.581 14.263 23.620 1.00 37.50 O ANISOU 232 O SER A 31 4808 4917 4524 38 -141 -37 O ATOM 233 CB SER A 31 4.488 11.662 25.151 1.00 38.98 C ANISOU 233 CB SER A 31 5005 5135 4671 61 -148 16 C ATOM 234 OG SER A 31 3.897 10.390 25.139 1.00 44.31 O ANISOU 234 OG SER A 31 5685 5810 5343 70 -121 40 O ATOM 235 N GLU A 32 5.800 14.350 23.986 1.00 41.48 N ANISOU 235 N GLU A 32 5291 5431 5039 27 -199 -24 N ATOM 236 CA GLU A 32 5.787 15.729 24.454 1.00 46.81 C ANISOU 236 CA GLU A 32 5983 6098 5706 16 -226 -53 C ATOM 237 C GLU A 32 5.376 16.657 23.322 1.00 41.77 C ANISOU 237 C GLU A 32 5333 5439 5101 4 -216 -65 C ATOM 238 O GLU A 32 5.917 16.595 22.213 1.00 42.13 O ANISOU 238 O GLU A 32 5347 5480 5182 -7 -213 -48 O ATOM 239 CB GLU A 32 7.158 16.110 25.039 1.00 51.33 C ANISOU 239 CB GLU A 32 6548 6675 6279 4 -277 -50 C ATOM 240 CG GLU A 32 8.283 16.496 24.053 1.00 62.31 C ANISOU 240 CG GLU A 32 7897 8062 7717 -17 -298 -34 C ATOM 241 CD GLU A 32 8.584 15.453 22.972 1.00 74.16 C ANISOU 241 CD GLU A 32 9361 9570 9245 -9 -267 -4 C ATOM 242 OE1 GLU A 32 7.982 14.354 23.027 1.00 76.79 O ANISOU 242 OE1 GLU A 32 9705 9909 9563 10 -236 5 O ATOM 243 OE2 GLU A 32 9.417 15.746 22.061 1.00 75.08 O1- ANISOU 243 OE2 GLU A 32 9442 9688 9398 -23 -274 11 O1- ATOM 244 N ASN A 33 4.376 17.484 23.592 1.00 45.47 N ANISOU 244 N ASN A 33 5827 5895 5556 9 -208 -92 N ATOM 245 CA ASN A 33 3.841 18.449 22.633 1.00 33.16 C ANISOU 245 CA ASN A 33 4262 4314 4025 0 -200 -104 C ATOM 246 C ASN A 33 3.296 17.784 21.360 1.00 30.44 C ANISOU 246 C ASN A 33 3893 3968 3704 0 -163 -84 C ATOM 247 O ASN A 33 3.111 18.502 20.376 1.00 22.09 O ANISOU 247 O ASN A 33 2823 2894 2675 -11 -161 -87 O ATOM 248 CB ASN A 33 4.891 19.529 22.264 1.00 37.82 C ANISOU 248 CB ASN A 33 4839 4888 4644 -25 -241 -107 C ATOM 249 CG ASN A 33 4.254 20.923 21.924 1.00 44.00 C ANISOU 249 CG ASN A 33 5636 5640 5441 -32 -249 -132 C ATOM 250 ND2 ASN A 33 4.843 21.626 20.944 1.00 26.20 N ANISOU 250 ND2 ASN A 33 3358 3370 3227 -56 -265 -121 N ATOM 251 OD1 ASN A 33 3.249 21.338 22.524 1.00 46.82 O ANISOU 251 OD1 ASN A 33 6025 5990 5776 -14 -238 -159 O ATOM 252 N PHE A 34 3.058 16.436 21.358 1.00 27.10 N ANISOU 252 N PHE A 34 3465 3561 3272 12 -137 -65 N ATOM 253 CA PHE A 34 2.272 15.760 20.295 1.00 21.62 C ANISOU 253 CA PHE A 34 2758 2862 2594 15 -103 -52 C ATOM 254 C PHE A 34 1.156 14.880 20.897 1.00 12.94 C ANISOU 254 C PHE A 34 1674 1771 1471 29 -75 -47 C ATOM 255 O PHE A 34 0.078 15.410 21.039 1.00 14.78 O ANISOU 255 O PHE A 34 1917 2000 1698 34 -61 -61 O ATOM 256 CB PHE A 34 3.110 14.966 19.260 1.00 15.28 C ANISOU 256 CB PHE A 34 1930 2062 1815 10 -100 -29 C ATOM 257 CG PHE A 34 2.394 14.868 17.915 1.00 11.26 C ANISOU 257 CG PHE A 34 1410 1541 1326 7 -77 -25 C ATOM 258 CD1 PHE A 34 2.167 16.007 17.216 1.00 13.35 C ANISOU 258 CD1 PHE A 34 1670 1794 1608 -5 -81 -35 C ATOM 259 CD2 PHE A 34 1.993 13.643 17.416 1.00 11.94 C ANISOU 259 CD2 PHE A 34 1496 1628 1413 15 -55 -12 C ATOM 260 CE1 PHE A 34 1.542 15.975 15.996 1.00 12.67 C ANISOU 260 CE1 PHE A 34 1576 1699 1538 -8 -64 -30 C ATOM 261 CE2 PHE A 34 1.354 13.592 16.191 1.00 12.43 C ANISOU 261 CE2 PHE A 34 1553 1680 1491 11 -39 -10 C ATOM 262 CZ PHE A 34 1.105 14.728 15.491 1.00 13.03 C ANISOU 262 CZ PHE A 34 1622 1747 1581 0 -43 -19 C ATOM 263 N TYR A 35 1.340 13.591 21.249 1.00 15.17 N ANISOU 263 N TYR A 35 1958 2064 1742 36 -67 -26 N ATOM 264 CA TYR A 35 0.235 12.863 21.901 1.00 12.68 C ANISOU 264 CA TYR A 35 1656 1757 1405 46 -42 -18 C ATOM 265 C TYR A 35 -0.377 13.662 23.061 1.00 13.76 C ANISOU 265 C TYR A 35 1814 1905 1509 56 -40 -37 C ATOM 266 O TYR A 35 -1.612 13.711 23.189 1.00 14.10 O ANISOU 266 O TYR A 35 1861 1952 1546 62 -13 -38 O ATOM 267 CB TYR A 35 0.705 11.488 22.438 1.00 15.61 C ANISOU 267 CB TYR A 35 2031 2136 1763 52 -43 8 C ATOM 268 CG TYR A 35 -0.337 10.806 23.299 1.00 13.97 C ANISOU 268 CG TYR A 35 1839 1940 1531 59 -19 22 C ATOM 269 CD1 TYR A 35 -1.364 10.042 22.754 1.00 14.92 C ANISOU 269 CD1 TYR A 35 1952 2052 1666 54 6 39 C ATOM 270 CD2 TYR A 35 -0.293 10.941 24.698 1.00 15.48 C ANISOU 270 CD2 TYR A 35 2050 2151 1680 69 -24 21 C ATOM 271 CE1 TYR A 35 -2.340 9.434 23.566 1.00 16.34 C ANISOU 271 CE1 TYR A 35 2141 2245 1824 57 28 58 C ATOM 272 CE2 TYR A 35 -1.275 10.369 25.503 1.00 16.38 C ANISOU 272 CE2 TYR A 35 2175 2280 1767 75 1 38 C ATOM 273 CZ TYR A 35 -2.269 9.616 24.925 1.00 19.78 C ANISOU 273 CZ TYR A 35 2594 2703 2218 68 28 58 C ATOM 274 OH TYR A 35 -3.202 9.047 25.771 1.00 29.52 O ANISOU 274 OH TYR A 35 3835 3955 3427 72 53 81 O ATOM 275 N SER A 36 0.458 14.267 23.918 1.00 14.88 N ANISOU 275 N SER A 36 1971 2053 1630 58 -68 -51 N ATOM 276 CA SER A 36 -0.066 15.012 25.082 1.00 12.36 C ANISOU 276 CA SER A 36 1680 1745 1272 72 -68 -74 C ATOM 277 C SER A 36 -1.062 16.093 24.686 1.00 13.67 C ANISOU 277 C SER A 36 1848 1898 1449 77 -53 -98 C ATOM 278 O SER A 36 -1.989 16.421 25.430 1.00 14.17 O ANISOU 278 O SER A 36 1928 1972 1484 96 -33 -111 O ATOM 279 CB SER A 36 1.088 15.673 25.887 1.00 18.50 C ANISOU 279 CB SER A 36 2475 2524 2031 70 -112 -91 C ATOM 280 OG SER A 36 1.735 16.722 25.159 1.00 25.31 O ANISOU 280 OG SER A 36 3326 3364 2925 54 -140 -108 O ATOM 281 N VAL A 37 -0.820 16.756 23.550 1.00 12.45 N ANISOU 281 N VAL A 37 1676 1721 1334 63 -65 -105 N ATOM 282 CA VAL A 37 -1.729 17.801 23.106 1.00 12.52 C ANISOU 282 CA VAL A 37 1686 1715 1357 69 -54 -126 C ATOM 283 C VAL A 37 -3.086 17.211 22.755 1.00 11.79 C ANISOU 283 C VAL A 37 1580 1631 1270 77 -14 -111 C ATOM 284 O VAL A 37 -4.128 17.734 23.157 1.00 13.07 O ANISOU 284 O VAL A 37 1749 1796 1420 95 7 -124 O ATOM 285 CB VAL A 37 -1.113 18.536 21.890 1.00 12.98 C ANISOU 285 CB VAL A 37 1726 1748 1457 49 -77 -128 C ATOM 286 CG1 VAL A 37 -2.103 19.549 21.352 1.00 14.68 C ANISOU 286 CG1 VAL A 37 1942 1946 1691 55 -67 -145 C ATOM 287 CG2 VAL A 37 0.179 19.236 22.307 1.00 14.81 C ANISOU 287 CG2 VAL A 37 1968 1971 1687 37 -120 -141 C ATOM 288 N PHE A 38 -3.094 16.139 21.948 1.00 10.99 N ANISOU 288 N PHE A 38 1457 1529 1189 64 -3 -83 N ATOM 289 CA PHE A 38 -4.369 15.495 21.624 1.00 10.30 C ANISOU 289 CA PHE A 38 1356 1449 1110 67 30 -66 C ATOM 290 C PHE A 38 -5.076 14.986 22.884 1.00 11.62 C ANISOU 290 C PHE A 38 1535 1642 1240 83 55 -57 C ATOM 291 O PHE A 38 -6.307 15.127 22.990 1.00 13.22 O ANISOU 291 O PHE A 38 1728 1852 1441 93 83 -54 O ATOM 292 CB PHE A 38 -4.130 14.324 20.629 1.00 9.79 C ANISOU 292 CB PHE A 38 1275 1376 1069 49 31 -39 C ATOM 293 CG PHE A 38 -3.717 14.772 19.237 1.00 9.13 C ANISOU 293 CG PHE A 38 1178 1273 1019 36 17 -44 C ATOM 294 CD1 PHE A 38 -4.672 15.145 18.326 1.00 10.62 C ANISOU 294 CD1 PHE A 38 1353 1451 1230 32 27 -44 C ATOM 295 CD2 PHE A 38 -2.364 14.919 18.912 1.00 12.66 C ANISOU 295 CD2 PHE A 38 1624 1714 1473 29 -7 -46 C ATOM 296 CE1 PHE A 38 -4.319 15.512 17.031 1.00 11.61 C ANISOU 296 CE1 PHE A 38 1469 1561 1381 20 15 -45 C ATOM 297 CE2 PHE A 38 -2.002 15.340 17.575 1.00 10.00 C ANISOU 297 CE2 PHE A 38 1273 1363 1164 16 -16 -46 C ATOM 298 CZ PHE A 38 -2.978 15.646 16.690 1.00 11.62 C ANISOU 298 CZ PHE A 38 1469 1558 1386 13 -5 -46 C ATOM 299 N GLU A 39 -4.324 14.326 23.799 1.00 11.17 N ANISOU 299 N GLU A 39 1493 1598 1154 85 46 -48 N ATOM 300 CA GLU A 39 -4.950 13.761 25.003 1.00 12.32 C ANISOU 300 CA GLU A 39 1650 1771 1259 99 71 -33 C ATOM 301 C GLU A 39 -5.569 14.848 25.884 1.00 14.91 C ANISOU 301 C GLU A 39 1996 2113 1556 124 83 -61 C ATOM 302 O GLU A 39 -6.692 14.672 26.395 1.00 17.49 O ANISOU 302 O GLU A 39 2318 2462 1865 138 119 -50 O ATOM 303 CB GLU A 39 -3.905 12.974 25.753 1.00 15.34 C ANISOU 303 CB GLU A 39 2049 2163 1617 97 52 -19 C ATOM 304 CG GLU A 39 -4.519 12.325 27.018 1.00 24.77 C ANISOU 304 CG GLU A 39 3256 3387 2766 110 77 2 C ATOM 305 CD GLU A 39 -5.598 11.229 26.708 1.00 48.74 C ANISOU 305 CD GLU A 39 6270 6428 5819 100 111 41 C ATOM 306 OE1 GLU A 39 -6.561 11.435 25.916 1.00 52.71 O ANISOU 306 OE1 GLU A 39 6750 6923 6353 95 130 42 O ATOM 307 OE2 GLU A 39 -5.490 10.122 27.283 1.00 59.74 O1- ANISOU 307 OE2 GLU A 39 7669 7832 7197 96 115 74 O1- ATOM 308 N ALA A 40 -4.905 16.006 25.977 1.00 12.91 N ANISOU 308 N ALA A 40 1761 1845 1298 130 55 -97 N ATOM 309 CA ALA A 40 -5.440 17.092 26.808 1.00 15.59 C ANISOU 309 CA ALA A 40 2124 2192 1606 158 63 -130 C ATOM 310 C ALA A 40 -6.764 17.587 26.263 1.00 17.62 C ANISOU 310 C ALA A 40 2362 2447 1886 171 95 -134 C ATOM 311 O ALA A 40 -7.686 17.905 27.028 1.00 22.19 O ANISOU 311 O ALA A 40 2949 3047 2435 200 126 -143 O ATOM 312 CB ALA A 40 -4.431 18.249 26.877 1.00 15.45 C ANISOU 312 CB ALA A 40 2131 2150 1588 156 18 -168 C ATOM 313 N GLU A 41 -6.917 17.589 24.932 1.00 14.43 N ANISOU 313 N GLU A 41 1930 2021 1533 151 90 -124 N ATOM 314 CA GLU A 41 -8.168 18.037 24.355 1.00 17.86 C ANISOU 314 CA GLU A 41 2342 2453 1993 162 116 -124 C ATOM 315 C GLU A 41 -9.218 16.926 24.280 1.00 20.25 C ANISOU 315 C GLU A 41 2614 2778 2300 157 153 -85 C ATOM 316 O GLU A 41 -10.408 17.197 24.482 1.00 26.60 O ANISOU 316 O GLU A 41 3404 3599 3104 177 185 -82 O ATOM 317 CB GLU A 41 -7.880 18.639 22.972 1.00 17.14 C ANISOU 317 CB GLU A 41 2236 2326 1949 143 90 -130 C ATOM 318 CG GLU A 41 -6.781 19.788 22.948 1.00 17.90 C ANISOU 318 CG GLU A 41 2357 2395 2048 140 49 -164 C ATOM 319 CD GLU A 41 -7.144 21.009 23.777 1.00 32.17 C ANISOU 319 CD GLU A 41 4193 4197 3833 172 49 -202 C ATOM 320 OE1 GLU A 41 -8.310 21.430 23.638 1.00 30.27 O ANISOU 320 OE1 GLU A 41 3940 3958 3601 194 75 -206 O ATOM 321 OE2 GLU A 41 -6.271 21.499 24.585 1.00 31.89 O1- ANISOU 321 OE2 GLU A 41 4191 4155 3769 176 21 -227 O1- ATOM 322 N LEU A 42 -8.831 15.684 24.019 1.00 16.20 N ANISOU 322 N LEU A 42 2093 2268 1796 132 149 -53 N ATOM 323 CA LEU A 42 -9.776 14.604 23.701 1.00 16.05 C ANISOU 323 CA LEU A 42 2044 2260 1793 119 174 -14 C ATOM 324 C LEU A 42 -9.998 13.576 24.807 1.00 30.00 C ANISOU 324 C LEU A 42 3816 4058 3526 121 198 16 C ATOM 325 O LEU A 42 -10.762 12.619 24.582 1.00 33.51 O ANISOU 325 O LEU A 42 4236 4509 3987 106 216 53 O ATOM 326 CB LEU A 42 -9.307 13.821 22.498 1.00 14.44 C ANISOU 326 CB LEU A 42 1828 2031 1626 88 152 3 C ATOM 327 CG LEU A 42 -9.195 14.627 21.218 1.00 11.74 C ANISOU 327 CG LEU A 42 1477 1662 1321 80 132 -16 C ATOM 328 CD1 LEU A 42 -8.528 13.660 20.243 1.00 15.28 C ANISOU 328 CD1 LEU A 42 1921 2091 1792 54 112 1 C ATOM 329 CD2 LEU A 42 -10.542 15.081 20.726 1.00 11.81 C ANISOU 329 CD2 LEU A 42 1460 1674 1355 86 151 -11 C ATOM 330 N GLN A 43 -9.332 13.695 25.958 1.00 25.43 N ANISOU 330 N GLN A 43 3268 3495 2900 137 194 4 N ATOM 331 CA GLN A 43 -9.418 12.634 26.963 1.00 38.25 C ANISOU 331 CA GLN A 43 4898 5146 4489 137 213 38 C ATOM 332 C GLN A 43 -10.862 12.261 27.265 1.00 30.57 C ANISOU 332 C GLN A 43 3898 4201 3515 142 258 70 C ATOM 333 O GLN A 43 -11.690 13.117 27.583 1.00 31.51 O ANISOU 333 O GLN A 43 4010 4339 3623 169 285 54 O ATOM 334 CB GLN A 43 -8.709 13.063 28.251 1.00 48.52 C ANISOU 334 CB GLN A 43 6238 6466 5732 160 205 16 C ATOM 335 CG GLN A 43 -9.017 12.170 29.458 1.00 61.88 C ANISOU 335 CG GLN A 43 7939 8195 7377 167 232 51 C ATOM 336 CD GLN A 43 -7.878 12.125 30.451 1.00 68.79 C ANISOU 336 CD GLN A 43 8854 9079 8203 175 206 41 C ATOM 337 NE2 GLN A 43 -8.089 11.431 31.568 1.00 70.31 N ANISOU 337 NE2 GLN A 43 9060 9307 8349 183 227 71 N ATOM 338 OE1 GLN A 43 -6.824 12.719 30.227 1.00 70.75 O ANISOU 338 OE1 GLN A 43 9120 9305 8457 173 165 8 O ATOM 339 N ASP A 44 -11.142 10.968 27.158 1.00 44.75 N ANISOU 339 N ASP A 44 5677 6000 5326 117 266 116 N ATOM 340 CA ASP A 44 -12.465 10.388 27.317 1.00 56.67 C ANISOU 340 CA ASP A 44 7154 7534 6845 111 304 158 C ATOM 341 C ASP A 44 -13.272 10.505 26.026 1.00 48.07 C ANISOU 341 C ASP A 44 6026 6423 5814 94 302 162 C ATOM 342 O ASP A 44 -13.894 9.523 25.608 1.00 62.45 O ANISOU 342 O ASP A 44 7822 8240 7666 65 306 203 O ATOM 343 CB ASP A 44 -13.230 11.021 28.492 1.00 69.02 C ANISOU 343 CB ASP A 44 8718 9145 8362 147 348 155 C ATOM 344 CG ASP A 44 -12.732 10.552 29.856 1.00 79.73 C ANISOU 344 CG ASP A 44 10107 10531 9657 159 358 170 C ATOM 345 OD1 ASP A 44 -13.159 11.156 30.868 1.00 82.56 O ANISOU 345 OD1 ASP A 44 10477 10912 9981 186 379 153 O ATOM 346 OD2 ASP A 44 -11.917 9.602 29.922 1.00 80.61 O1- ANISOU 346 OD2 ASP A 44 10233 10627 9766 137 333 191 O1- ATOM 347 N VAL A 45 -13.236 11.671 25.365 1.00 19.33 N ANISOU 347 N VAL A 45 2385 2767 2190 108 290 122 N ATOM 348 CA VAL A 45 -14.312 12.040 24.450 1.00 17.33 C ANISOU 348 CA VAL A 45 2095 2509 1982 103 299 127 C ATOM 349 C VAL A 45 -14.373 11.070 23.260 1.00 16.02 C ANISOU 349 C VAL A 45 1910 2312 1863 62 274 152 C ATOM 350 O VAL A 45 -15.452 10.569 22.871 1.00 18.87 O ANISOU 350 O VAL A 45 2236 2680 2256 44 286 186 O ATOM 351 CB VAL A 45 -14.084 13.501 23.991 1.00 24.61 C ANISOU 351 CB VAL A 45 3026 3414 2909 127 284 77 C ATOM 352 CG1 VAL A 45 -14.990 13.932 22.875 1.00 25.94 C ANISOU 352 CG1 VAL A 45 3160 3570 3127 121 282 80 C ATOM 353 CG2 VAL A 45 -14.206 14.443 25.199 1.00 29.43 C ANISOU 353 CG2 VAL A 45 3656 4052 3473 170 310 51 C ATOM 354 N ILE A 46 -13.238 10.911 22.586 1.00 13.84 N ANISOU 354 N ILE A 46 1659 2004 1596 48 237 133 N ATOM 355 CA ILE A 46 -13.057 9.876 21.563 1.00 13.47 C ANISOU 355 CA ILE A 46 1608 1926 1583 14 211 152 C ATOM 356 C ILE A 46 -11.738 9.164 21.863 1.00 13.01 C ANISOU 356 C ILE A 46 1583 1855 1505 10 191 150 C ATOM 357 O ILE A 46 -10.834 9.727 22.494 1.00 13.22 O ANISOU 357 O ILE A 46 1634 1889 1500 29 186 126 O ATOM 358 CB ILE A 46 -13.055 10.460 20.111 1.00 11.45 C ANISOU 358 CB ILE A 46 1344 1642 1364 5 186 130 C ATOM 359 CG1 ILE A 46 -11.987 11.530 19.982 1.00 12.64 C ANISOU 359 CG1 ILE A 46 1519 1783 1500 24 169 88 C ATOM 360 CG2 ILE A 46 -14.447 10.990 19.724 1.00 14.63 C ANISOU 360 CG2 ILE A 46 1710 2056 1794 7 201 139 C ATOM 361 CD1 ILE A 46 -11.831 12.112 18.497 1.00 12.39 C ANISOU 361 CD1 ILE A 46 1483 1724 1502 14 143 69 C ATOM 362 N PRO A 47 -11.568 7.939 21.385 1.00 11.33 N ANISOU 362 N PRO A 47 1373 1619 1312 -16 175 174 N ATOM 363 CA PRO A 47 -10.318 7.239 21.645 1.00 11.55 C ANISOU 363 CA PRO A 47 1431 1634 1325 -16 156 174 C ATOM 364 C PRO A 47 -9.172 7.749 20.793 1.00 9.59 C ANISOU 364 C PRO A 47 1198 1364 1083 -10 128 138 C ATOM 365 O PRO A 47 -9.368 8.137 19.614 1.00 11.71 O ANISOU 365 O PRO A 47 1456 1614 1379 -17 117 123 O ATOM 366 CB PRO A 47 -10.639 5.786 21.284 1.00 14.55 C ANISOU 366 CB PRO A 47 1809 1991 1730 -43 146 210 C ATOM 367 CG PRO A 47 -11.763 5.823 20.341 1.00 14.80 C ANISOU 367 CG PRO A 47 1814 2013 1798 -63 146 218 C ATOM 368 CD PRO A 47 -12.574 7.074 20.725 1.00 13.16 C ANISOU 368 CD PRO A 47 1581 1838 1580 -45 173 207 C ATOM 369 N ILE A 48 -7.979 7.689 21.357 1.00 10.13 N ANISOU 369 N ILE A 48 1288 1434 1128 3 117 129 N ATOM 370 CA ILE A 48 -6.726 7.947 20.656 1.00 8.66 C ANISOU 370 CA ILE A 48 1113 1230 948 7 91 105 C ATOM 371 C ILE A 48 -5.993 6.632 20.526 1.00 9.60 C ANISOU 371 C ILE A 48 1244 1329 1073 2 76 123 C ATOM 372 O ILE A 48 -5.798 5.920 21.527 1.00 15.63 O ANISOU 372 O ILE A 48 2020 2102 1817 5 79 145 O ATOM 373 CB ILE A 48 -5.839 8.981 21.399 1.00 11.16 C ANISOU 373 CB ILE A 48 1441 1563 1236 26 84 80 C ATOM 374 CG1 ILE A 48 -6.593 10.300 21.517 1.00 15.17 C ANISOU 374 CG1 ILE A 48 1940 2083 1740 35 97 58 C ATOM 375 CG2 ILE A 48 -4.536 9.182 20.610 1.00 14.29 C ANISOU 375 CG2 ILE A 48 1841 1943 1646 27 58 62 C ATOM 376 CD1 ILE A 48 -5.889 11.264 22.440 1.00 16.00 C ANISOU 376 CD1 ILE A 48 2063 2204 1814 53 89 33 C ATOM 377 N CYS A 49 -5.549 6.300 19.322 1.00 9.91 N ANISOU 377 N CYS A 49 1286 1343 1138 -4 60 114 N ATOM 378 CA CYS A 49 -4.740 5.097 19.081 1.00 9.84 C ANISOU 378 CA CYS A 49 1291 1311 1135 -2 45 126 C ATOM 379 C CYS A 49 -3.349 5.553 18.702 1.00 9.31 C ANISOU 379 C CYS A 49 1227 1245 1065 14 31 104 C ATOM 380 O CYS A 49 -3.195 6.211 17.662 1.00 10.07 O ANISOU 380 O CYS A 49 1316 1336 1174 13 27 83 O ATOM 381 CB CYS A 49 -5.380 4.274 17.944 1.00 9.07 C ANISOU 381 CB CYS A 49 1197 1184 1067 -18 38 132 C ATOM 382 SG CYS A 49 -4.491 2.734 17.558 1.00 11.96 S ANISOU 382 SG CYS A 49 1586 1513 1443 -11 19 142 S ATOM 383 N ARG A 50 -2.335 5.139 19.468 1.00 8.95 N ANISOU 383 N ARG A 50 1191 1205 1004 28 21 112 N ATOM 384 CA ARG A 50 -0.935 5.405 19.144 1.00 8.25 C ANISOU 384 CA ARG A 50 1099 1118 916 43 6 98 C ATOM 385 C ARG A 50 -0.435 4.252 18.299 1.00 9.93 C ANISOU 385 C ARG A 50 1321 1305 1149 51 -1 104 C ATOM 386 O ARG A 50 -0.487 3.082 18.732 1.00 12.40 O ANISOU 386 O ARG A 50 1648 1603 1463 54 -4 126 O ATOM 387 CB ARG A 50 -0.090 5.525 20.405 1.00 10.16 C ANISOU 387 CB ARG A 50 1345 1381 1135 55 -4 105 C ATOM 388 CG ARG A 50 -0.383 6.848 21.167 1.00 11.43 C ANISOU 388 CG ARG A 50 1503 1566 1273 52 -1 90 C ATOM 389 CD ARG A 50 0.327 6.914 22.574 1.00 12.74 C ANISOU 389 CD ARG A 50 1679 1754 1407 62 -15 97 C ATOM 390 NE ARG A 50 -0.417 6.073 23.516 1.00 15.78 N ANISOU 390 NE ARG A 50 2079 2145 1772 61 -2 123 N ATOM 391 CZ ARG A 50 -0.508 6.282 24.837 1.00 15.74 C ANISOU 391 CZ ARG A 50 2088 2165 1729 67 -2 130 C ATOM 392 NH1 ARG A 50 0.152 7.318 25.337 1.00 21.07 N1+ ANISOU 392 NH1 ARG A 50 2766 2856 2384 73 -19 107 N1+ ATOM 393 NH2 ARG A 50 -1.288 5.468 25.572 1.00 16.12 N ANISOU 393 NH2 ARG A 50 2146 2218 1759 64 15 159 N ATOM 394 N THR A 51 -0.008 4.546 17.074 1.00 9.33 N ANISOU 394 N THR A 51 1237 1221 1087 56 -2 86 N ATOM 395 CA THR A 51 0.159 3.453 16.112 1.00 9.43 C ANISOU 395 CA THR A 51 1263 1205 1115 64 -6 87 C ATOM 396 C THR A 51 1.361 3.734 15.205 1.00 9.62 C ANISOU 396 C THR A 51 1277 1234 1143 84 -7 72 C ATOM 397 O THR A 51 1.789 4.886 15.033 1.00 10.49 O ANISOU 397 O THR A 51 1368 1367 1251 82 -5 61 O ATOM 398 CB THR A 51 -1.136 3.327 15.279 1.00 14.39 C ANISOU 398 CB THR A 51 1899 1814 1755 44 -1 82 C ATOM 399 CG2 THR A 51 -1.359 4.491 14.353 1.00 14.81 C ANISOU 399 CG2 THR A 51 1938 1878 1811 36 3 62 C ATOM 400 OG1 THR A 51 -1.113 2.090 14.509 1.00 18.58 O ANISOU 400 OG1 THR A 51 2451 2310 2298 51 -10 83 O ATOM 401 N THR A 52 1.848 2.672 14.594 1.00 9.88 N ANISOU 401 N THR A 52 1323 1245 1184 103 -10 72 N ATOM 402 CA THR A 52 2.615 2.727 13.350 1.00 10.59 C ANISOU 402 CA THR A 52 1410 1335 1279 122 -5 56 C ATOM 403 C THR A 52 1.690 2.306 12.216 1.00 10.08 C ANISOU 403 C THR A 52 1367 1244 1219 114 -3 43 C ATOM 404 O THR A 52 0.603 1.751 12.437 1.00 11.86 O ANISOU 404 O THR A 52 1611 1447 1450 95 -10 49 O ATOM 405 CB THR A 52 3.851 1.815 13.369 1.00 12.03 C ANISOU 405 CB THR A 52 1594 1512 1464 158 -7 62 C ATOM 406 CG2 THR A 52 4.900 2.284 14.371 1.00 15.21 C ANISOU 406 CG2 THR A 52 1971 1945 1864 167 -13 76 C ATOM 407 OG1 THR A 52 3.491 0.449 13.692 1.00 12.91 O ANISOU 407 OG1 THR A 52 1734 1588 1582 165 -16 72 O ATOM 408 N ILE A 53 2.110 2.612 10.981 1.00 9.60 N ANISOU 408 N ILE A 53 1305 1189 1155 126 4 26 N ATOM 409 CA ILE A 53 1.421 2.132 9.771 1.00 9.94 C ANISOU 409 CA ILE A 53 1373 1205 1197 123 2 10 C ATOM 410 C ILE A 53 2.510 1.677 8.825 1.00 10.73 C ANISOU 410 C ILE A 53 1481 1306 1290 160 11 -3 C ATOM 411 O ILE A 53 3.466 2.432 8.561 1.00 11.05 O ANISOU 411 O ILE A 53 1495 1379 1324 174 25 -2 O ATOM 412 CB ILE A 53 0.550 3.214 9.096 1.00 9.87 C ANISOU 412 CB ILE A 53 1356 1208 1186 96 4 2 C ATOM 413 CG1 ILE A 53 -0.600 3.742 9.985 1.00 10.47 C ANISOU 413 CG1 ILE A 53 1422 1288 1270 64 -1 14 C ATOM 414 CG2 ILE A 53 0.075 2.685 7.727 1.00 11.64 C ANISOU 414 CG2 ILE A 53 1609 1409 1404 99 -2 -16 C ATOM 415 CD1 ILE A 53 -1.732 2.724 10.179 1.00 12.63 C ANISOU 415 CD1 ILE A 53 1717 1528 1554 47 -14 21 C ATOM 416 N ALA A 54 2.467 0.384 8.460 1.00 11.75 N ANISOU 416 N ALA A 54 1645 1398 1420 179 3 -11 N ATOM 417 CA ALA A 54 3.517 -0.245 7.650 1.00 11.77 C ANISOU 417 CA ALA A 54 1660 1397 1414 224 14 -26 C ATOM 418 C ALA A 54 4.871 -0.122 8.315 1.00 13.52 C ANISOU 418 C ALA A 54 1850 1648 1640 253 25 -11 C ATOM 419 O ALA A 54 5.920 0.001 7.643 1.00 15.17 O ANISOU 419 O ALA A 54 2045 1879 1841 287 44 -16 O ATOM 420 CB ALA A 54 3.493 0.347 6.213 1.00 15.64 C ANISOU 420 CB ALA A 54 2154 1902 1885 229 26 -46 C ATOM 421 N GLY A 55 4.856 -0.143 9.637 1.00 11.64 N ANISOU 421 N GLY A 55 1598 1411 1413 240 15 11 N ATOM 422 CA GLY A 55 6.031 -0.012 10.484 1.00 14.03 C ANISOU 422 CA GLY A 55 1869 1740 1721 260 17 29 C ATOM 423 C GLY A 55 6.606 1.383 10.613 1.00 13.01 C ANISOU 423 C GLY A 55 1697 1658 1590 247 26 36 C ATOM 424 O GLY A 55 7.605 1.565 11.315 1.00 15.91 O ANISOU 424 O GLY A 55 2034 2048 1962 260 23 52 O ATOM 425 N THR A 56 5.973 2.372 9.986 1.00 10.94 N ANISOU 425 N THR A 56 1430 1407 1321 220 32 26 N ATOM 426 CA THR A 56 6.463 3.750 9.990 1.00 11.63 C ANISOU 426 CA THR A 56 1478 1532 1407 205 37 33 C ATOM 427 C THR A 56 5.641 4.610 10.923 1.00 9.42 C ANISOU 427 C THR A 56 1194 1255 1129 167 24 38 C ATOM 428 O THR A 56 4.548 4.240 11.356 1.00 11.44 O ANISOU 428 O THR A 56 1473 1489 1385 150 16 36 O ATOM 429 CB THR A 56 6.377 4.381 8.567 1.00 10.16 C ANISOU 429 CB THR A 56 1290 1357 1212 203 54 21 C ATOM 430 CG2 THR A 56 6.830 3.418 7.474 1.00 13.74 C ANISOU 430 CG2 THR A 56 1764 1803 1656 242 69 9 C ATOM 431 OG1 THR A 56 5.046 4.863 8.304 1.00 10.72 O ANISOU 431 OG1 THR A 56 1379 1414 1279 170 47 11 O ATOM 432 N ARG A 57 6.173 5.816 11.178 1.00 8.60 N ANISOU 432 N ARG A 57 1059 1181 1029 153 22 44 N ATOM 433 CA ARG A 57 5.492 6.836 11.963 1.00 9.08 C ANISOU 433 CA ARG A 57 1114 1246 1089 121 10 44 C ATOM 434 C ARG A 57 4.658 7.785 11.088 1.00 8.95 C ANISOU 434 C ARG A 57 1100 1228 1072 99 16 33 C ATOM 435 O ARG A 57 4.139 8.780 11.603 1.00 11.37 O ANISOU 435 O ARG A 57 1402 1539 1380 76 8 31 O ATOM 436 CB ARG A 57 6.528 7.691 12.716 1.00 15.44 C ANISOU 436 CB ARG A 57 1889 2078 1900 116 -2 55 C ATOM 437 CG ARG A 57 7.203 6.967 13.915 1.00 24.10 C ANISOU 437 CG ARG A 57 2984 3178 2996 132 -16 69 C ATOM 438 CD ARG A 57 8.437 7.722 14.366 1.00 30.76 C ANISOU 438 CD ARG A 57 3791 4048 3847 130 -31 81 C ATOM 439 NE ARG A 57 9.477 7.577 13.362 1.00 43.44 N ANISOU 439 NE ARG A 57 5370 5670 5465 150 -17 90 N ATOM 440 CZ ARG A 57 10.731 7.967 13.517 1.00 53.21 C ANISOU 440 CZ ARG A 57 6568 6934 6715 154 -26 107 C ATOM 441 NH1 ARG A 57 11.086 8.569 14.651 1.00 57.32 N1+ ANISOU 441 NH1 ARG A 57 7077 7464 7238 136 -55 114 N1+ ATOM 442 NH2 ARG A 57 11.617 7.748 12.542 1.00 51.45 N ANISOU 442 NH2 ARG A 57 6318 6728 6502 177 -7 117 N ATOM 443 N ILE A 58 4.549 7.515 9.775 1.00 9.24 N ANISOU 443 N ILE A 58 1146 1260 1105 108 29 26 N ATOM 444 CA ILE A 58 3.939 8.498 8.849 1.00 10.40 C ANISOU 444 CA ILE A 58 1291 1409 1250 88 33 20 C ATOM 445 C ILE A 58 2.453 8.260 8.772 1.00 10.64 C ANISOU 445 C ILE A 58 1347 1417 1280 72 27 10 C ATOM 446 O ILE A 58 1.880 7.971 7.709 1.00 12.43 O ANISOU 446 O ILE A 58 1591 1632 1500 72 30 2 O ATOM 447 CB ILE A 58 4.625 8.377 7.497 1.00 11.08 C ANISOU 447 CB ILE A 58 1373 1508 1328 107 49 20 C ATOM 448 CG1 ILE A 58 6.143 8.347 7.650 1.00 12.95 C ANISOU 448 CG1 ILE A 58 1581 1771 1570 128 57 34 C ATOM 449 CG2 ILE A 58 4.251 9.587 6.584 1.00 17.22 C ANISOU 449 CG2 ILE A 58 2143 2295 2104 86 52 21 C ATOM 450 CD1 ILE A 58 6.744 9.493 8.496 1.00 17.97 C ANISOU 450 CD1 ILE A 58 2183 2426 2220 107 44 49 C ATOM 451 N ILE A 59 1.787 8.373 9.898 1.00 9.45 N ANISOU 451 N ILE A 59 1198 1259 1133 59 18 12 N ATOM 452 CA ILE A 59 0.493 7.674 9.920 1.00 10.33 C ANISOU 452 CA ILE A 59 1332 1348 1246 49 15 9 C ATOM 453 C ILE A 59 -0.652 8.526 9.352 1.00 12.38 C ANISOU 453 C ILE A 59 1589 1604 1509 27 13 4 C ATOM 454 O ILE A 59 -1.594 7.981 8.785 1.00 14.09 O ANISOU 454 O ILE A 59 1822 1803 1728 19 8 1 O ATOM 455 CB ILE A 59 0.231 7.116 11.333 1.00 20.96 C ANISOU 455 CB ILE A 59 2682 2689 2592 47 11 18 C ATOM 456 CG1 ILE A 59 -0.027 8.223 12.263 1.00 16.85 C ANISOU 456 CG1 ILE A 59 2148 2185 2071 35 9 19 C ATOM 457 CG2 ILE A 59 1.449 6.184 11.824 1.00 13.77 C ANISOU 457 CG2 ILE A 59 1773 1779 1678 72 9 26 C ATOM 458 CD1 ILE A 59 -1.492 8.471 12.345 1.00 21.90 C ANISOU 458 CD1 ILE A 59 2791 2816 2714 17 11 19 C ATOM 459 N GLY A 60 -0.576 9.858 9.411 1.00 10.68 N ANISOU 459 N GLY A 60 1356 1403 1297 17 12 3 N ATOM 460 CA GLY A 60 -1.543 10.688 8.733 1.00 9.35 C ANISOU 460 CA GLY A 60 1187 1232 1135 2 9 0 C ATOM 461 C GLY A 60 -1.410 10.653 7.225 1.00 10.64 C ANISOU 461 C GLY A 60 1358 1394 1293 3 10 -3 C ATOM 462 O GLY A 60 -2.394 10.585 6.488 1.00 13.24 O ANISOU 462 O GLY A 60 1697 1712 1622 -7 3 -6 O ATOM 463 N ARG A 61 -0.185 10.740 6.729 1.00 8.70 N ANISOU 463 N ARG A 61 1104 1162 1039 16 18 0 N ATOM 464 CA ARG A 61 -0.014 10.719 5.274 1.00 10.32 C ANISOU 464 CA ARG A 61 1319 1372 1232 22 23 -1 C ATOM 465 C ARG A 61 -0.303 9.357 4.658 1.00 8.78 C ANISOU 465 C ARG A 61 1153 1159 1023 35 22 -12 C ATOM 466 O ARG A 61 -0.620 9.270 3.454 1.00 9.83 O ANISOU 466 O ARG A 61 1303 1290 1143 36 20 -18 O ATOM 467 CB ARG A 61 1.406 11.233 4.957 1.00 9.09 C ANISOU 467 CB ARG A 61 1141 1240 1071 33 35 9 C ATOM 468 CG ARG A 61 1.868 10.991 3.472 1.00 8.61 C ANISOU 468 CG ARG A 61 1091 1192 989 47 49 10 C ATOM 469 CD ARG A 61 3.066 11.936 3.111 1.00 11.32 C ANISOU 469 CD ARG A 61 1402 1565 1333 48 61 29 C ATOM 470 NE ARG A 61 2.488 13.304 3.016 1.00 10.63 N ANISOU 470 NE ARG A 61 1305 1476 1258 19 49 39 N ATOM 471 CZ ARG A 61 3.187 14.414 3.226 1.00 11.40 C ANISOU 471 CZ ARG A 61 1374 1587 1370 5 47 57 C ATOM 472 NH1 ARG A 61 4.525 14.358 3.476 1.00 12.15 N1+ ANISOU 472 NH1 ARG A 61 1444 1705 1470 15 57 71 N1+ ATOM 473 NH2 ARG A 61 2.543 15.569 3.149 1.00 12.43 N ANISOU 473 NH2 ARG A 61 1502 1708 1513 -19 32 62 N ATOM 474 N LEU A 62 -0.215 8.291 5.439 1.00 8.34 N ANISOU 474 N LEU A 62 1107 1090 971 45 21 -15 N ATOM 475 CA LEU A 62 -0.504 6.970 4.885 1.00 8.24 C ANISOU 475 CA LEU A 62 1127 1054 950 57 16 -27 C ATOM 476 C LEU A 62 -1.946 6.531 5.020 1.00 11.40 C ANISOU 476 C LEU A 62 1544 1428 1361 34 -3 -29 C ATOM 477 O LEU A 62 -2.267 5.501 4.423 1.00 15.04 O ANISOU 477 O LEU A 62 2035 1865 1815 39 -14 -39 O ATOM 478 CB LEU A 62 0.386 5.900 5.557 1.00 9.35 C ANISOU 478 CB LEU A 62 1274 1188 1091 82 21 -27 C ATOM 479 CG LEU A 62 1.870 5.961 5.185 1.00 7.49 C ANISOU 479 CG LEU A 62 1025 977 845 113 40 -25 C ATOM 480 CD1 LEU A 62 2.672 4.854 5.927 1.00 11.06 C ANISOU 480 CD1 LEU A 62 1481 1419 1301 140 42 -23 C ATOM 481 CD2 LEU A 62 2.087 5.760 3.691 1.00 13.53 C ANISOU 481 CD2 LEU A 62 1810 1744 1587 130 49 -38 C ATOM 482 N THR A 63 -2.809 7.298 5.664 1.00 10.80 N ANISOU 482 N THR A 63 1449 1356 1299 11 -8 -20 N ATOM 483 CA THR A 63 -4.204 6.855 5.881 1.00 10.29 C ANISOU 483 CA THR A 63 1391 1271 1249 -11 -23 -16 C ATOM 484 C THR A 63 -5.187 7.942 5.487 1.00 10.95 C ANISOU 484 C THR A 63 1459 1362 1340 -31 -30 -12 C ATOM 485 O THR A 63 -4.833 9.104 5.304 1.00 13.57 O ANISOU 485 O THR A 63 1774 1713 1669 -30 -23 -11 O ATOM 486 CB THR A 63 -4.467 6.472 7.359 1.00 13.53 C ANISOU 486 CB THR A 63 1791 1679 1671 -17 -20 -3 C ATOM 487 CG2 THR A 63 -3.464 5.331 7.780 1.00 13.96 C ANISOU 487 CG2 THR A 63 1862 1722 1720 5 -16 -3 C ATOM 488 OG1 THR A 63 -4.226 7.616 8.226 1.00 14.38 O ANISOU 488 OG1 THR A 63 1872 1811 1781 -17 -8 3 O ATOM 489 N ALA A 64 -6.440 7.560 5.339 1.00 10.22 N ANISOU 489 N ALA A 64 1369 1253 1260 -51 -46 -8 N ATOM 490 CA ALA A 64 -7.520 8.495 5.137 1.00 10.54 C ANISOU 490 CA ALA A 64 1391 1301 1314 -69 -54 0 C ATOM 491 C ALA A 64 -8.720 7.922 5.849 1.00 11.47 C ANISOU 491 C ALA A 64 1498 1406 1452 -88 -61 14 C ATOM 492 O ALA A 64 -9.067 6.754 5.607 1.00 12.00 O ANISOU 492 O ALA A 64 1585 1452 1524 -98 -77 15 O ATOM 493 CB ALA A 64 -7.810 8.686 3.632 1.00 13.96 C ANISOU 493 CB ALA A 64 1839 1729 1737 -75 -72 -8 C ATOM 494 N GLY A 65 -9.395 8.732 6.657 1.00 9.54 N ANISOU 494 N GLY A 65 1224 1177 1222 -93 -52 25 N ATOM 495 CA GLY A 65 -10.540 8.243 7.406 1.00 11.81 C ANISOU 495 CA GLY A 65 1495 1462 1530 -110 -53 43 C ATOM 496 C GLY A 65 -11.547 9.310 7.779 1.00 10.58 C ANISOU 496 C GLY A 65 1306 1324 1391 -113 -45 54 C ATOM 497 O GLY A 65 -11.282 10.526 7.692 1.00 13.53 O ANISOU 497 O GLY A 65 1670 1710 1760 -101 -38 45 O ATOM 498 N ASN A 66 -12.723 8.835 8.135 1.00 10.46 N ANISOU 498 N ASN A 66 1272 1307 1396 -131 -49 74 N ATOM 499 CA ASN A 66 -13.757 9.703 8.683 1.00 10.25 C ANISOU 499 CA ASN A 66 1207 1300 1386 -130 -36 87 C ATOM 500 C ASN A 66 -14.413 8.981 9.836 1.00 13.17 C ANISOU 500 C ASN A 66 1559 1678 1765 -138 -20 111 C ATOM 501 O ASN A 66 -13.853 8.021 10.372 1.00 13.25 O ANISOU 501 O ASN A 66 1589 1681 1766 -140 -16 116 O ATOM 502 CB ASN A 66 -14.721 10.151 7.572 1.00 11.58 C ANISOU 502 CB ASN A 66 1361 1464 1574 -143 -60 92 C ATOM 503 CG ASN A 66 -15.515 9.020 7.010 1.00 10.87 C ANISOU 503 CG ASN A 66 1272 1356 1502 -173 -88 108 C ATOM 504 ND2 ASN A 66 -16.280 9.336 5.954 1.00 10.30 N ANISOU 504 ND2 ASN A 66 1191 1279 1444 -187 -115 112 N ATOM 505 OD1 ASN A 66 -15.483 7.889 7.469 1.00 11.68 O ANISOU 505 OD1 ASN A 66 1385 1447 1606 -186 -89 118 O ATOM 506 N AARG A 67 -15.601 9.451 10.244 0.47 13.45 N ANISOU 506 N AARG A 67 1557 1733 1821 -141 -9 130 N ATOM 507 N BARG A 67 -15.590 9.436 10.264 0.53 13.08 N ANISOU 507 N BARG A 67 1511 1686 1774 -141 -9 130 N ATOM 508 CA AARG A 67 -16.262 8.886 11.408 0.47 16.29 C ANISOU 508 CA AARG A 67 1894 2108 2188 -146 13 158 C ATOM 509 CA BARG A 67 -16.161 8.833 11.454 0.53 16.04 C ANISOU 509 CA BARG A 67 1865 2076 2154 -146 14 157 C ATOM 510 C AARG A 67 -16.646 7.436 11.189 0.47 15.07 C ANISOU 510 C AARG A 67 1745 1933 2049 -179 -8 182 C ATOM 511 C BARG A 67 -16.691 7.430 11.196 0.53 15.63 C ANISOU 511 C BARG A 67 1814 2003 2121 -180 -8 183 C ATOM 512 O AARG A 67 -16.752 6.710 12.179 0.47 18.81 O ANISOU 512 O AARG A 67 2213 2412 2520 -185 9 205 O ATOM 513 O BARG A 67 -16.988 6.737 12.172 0.53 20.50 O ANISOU 513 O BARG A 67 2421 2629 2740 -188 9 209 O ATOM 514 CB AARG A 67 -17.511 9.707 11.795 0.47 18.22 C ANISOU 514 CB AARG A 67 2091 2379 2451 -139 31 175 C ATOM 515 CB BARG A 67 -17.275 9.718 12.020 0.53 18.94 C ANISOU 515 CB BARG A 67 2189 2473 2536 -134 37 172 C ATOM 516 CG AARG A 67 -18.764 9.433 10.975 0.47 22.38 C ANISOU 516 CG AARG A 67 2586 2901 3015 -166 7 200 C ATOM 517 CG BARG A 67 -18.594 9.456 11.361 0.53 19.64 C ANISOU 517 CG BARG A 67 2242 2559 2660 -160 18 199 C ATOM 518 CD AARG A 67 -20.030 10.147 11.582 0.47 27.08 C ANISOU 518 CD AARG A 67 3127 3529 3631 -154 33 223 C ATOM 519 CD BARG A 67 -19.810 10.194 12.003 0.53 27.93 C ANISOU 519 CD BARG A 67 3240 3644 3730 -146 46 220 C ATOM 520 NE AARG A 67 -19.925 10.179 13.043 0.47 26.91 N ANISOU 520 NE AARG A 67 3099 3536 3590 -133 77 231 N ATOM 521 NE BARG A 67 -21.053 9.439 11.805 0.53 31.49 N ANISOU 521 NE BARG A 67 3650 4097 4216 -179 33 261 N ATOM 522 CZ AARG A 67 -19.947 11.280 13.789 0.47 31.73 C ANISOU 522 CZ AARG A 67 3699 4172 4185 -95 110 217 C ATOM 523 CZ BARG A 67 -21.794 9.430 10.697 0.53 35.00 C ANISOU 523 CZ BARG A 67 4077 4529 4692 -201 -3 270 C ATOM 524 NH1AARG A 67 -20.114 12.492 13.234 0.47 31.26 N1+ ANISOU 524 NH1AARG A 67 3632 4111 4134 -73 103 196 N1+ ATOM 525 NH1BARG A 67 -21.454 10.152 9.648 0.53 33.37 N1+ ANISOU 525 NH1BARG A 67 3889 4307 4482 -193 -28 243 N1+ ATOM 526 NH2AARG A 67 -19.823 11.159 15.106 0.47 30.81 N ANISOU 526 NH2AARG A 67 3583 4081 4044 -77 147 223 N ATOM 527 NH2BARG A 67 -22.905 8.701 10.646 0.53 37.20 N ANISOU 527 NH2BARG A 67 4317 4812 5005 -234 -15 311 N ATOM 528 N LYS A 68 -16.828 6.999 9.930 1.00 13.84 N ANISOU 528 N LYS A 68 1602 1749 1907 -201 -45 177 N ATOM 529 CA LYS A 68 -17.350 5.700 9.546 1.00 13.78 C ANISOU 529 CA LYS A 68 1601 1715 1921 -237 -75 197 C ATOM 530 C LYS A 68 -16.318 4.654 9.135 1.00 15.65 C ANISOU 530 C LYS A 68 1889 1916 2141 -240 -95 180 C ATOM 531 O LYS A 68 -16.595 3.446 9.265 1.00 16.87 O ANISOU 531 O LYS A 68 2053 2045 2310 -265 -112 199 O ATOM 532 CB LYS A 68 -18.296 5.886 8.342 1.00 16.98 C ANISOU 532 CB LYS A 68 1991 2110 2351 -259 -111 201 C ATOM 533 CG LYS A 68 -19.436 6.847 8.663 1.00 25.97 C ANISOU 533 CG LYS A 68 3074 3282 3512 -256 -95 223 C ATOM 534 CD LYS A 68 -20.405 6.924 7.475 1.00 29.87 C ANISOU 534 CD LYS A 68 3551 3765 4034 -281 -137 231 C ATOM 535 CE LYS A 68 -20.308 8.244 6.799 1.00 27.40 C ANISOU 535 CE LYS A 68 3234 3463 3712 -257 -138 210 C ATOM 536 NZ LYS A 68 -21.565 8.456 5.960 1.00 28.88 N1+ ANISOU 536 NZ LYS A 68 3386 3652 3934 -280 -172 230 N1+ ATOM 537 N GLY A 69 -15.166 5.077 8.589 1.00 13.78 N ANISOU 537 N GLY A 69 1685 1674 1877 -215 -95 145 N ATOM 538 CA GLY A 69 -14.249 4.129 7.995 1.00 14.20 C ANISOU 538 CA GLY A 69 1785 1694 1915 -213 -115 126 C ATOM 539 C GLY A 69 -12.840 4.684 7.992 1.00 11.82 C ANISOU 539 C GLY A 69 1505 1404 1583 -178 -96 97 C ATOM 540 O GLY A 69 -12.611 5.865 8.252 1.00 13.03 O ANISOU 540 O GLY A 69 1639 1584 1726 -160 -75 90 O ATOM 541 N LEU A 70 -11.899 3.789 7.756 1.00 10.11 N ANISOU 541 N LEU A 70 1326 1162 1352 -168 -104 84 N ATOM 542 CA LEU A 70 -10.468 4.094 7.770 1.00 8.51 C ANISOU 542 CA LEU A 70 1142 969 1122 -135 -87 61 C ATOM 543 C LEU A 70 -9.799 3.280 6.682 1.00 9.72 C ANISOU 543 C LEU A 70 1337 1094 1263 -126 -107 39 C ATOM 544 O LEU A 70 -9.889 2.052 6.669 1.00 11.51 O ANISOU 544 O LEU A 70 1589 1287 1498 -135 -125 42 O ATOM 545 CB LEU A 70 -9.883 3.772 9.164 1.00 10.85 C ANISOU 545 CB LEU A 70 1434 1275 1414 -123 -64 74 C ATOM 546 CG LEU A 70 -8.380 3.986 9.229 1.00 11.82 C ANISOU 546 CG LEU A 70 1571 1406 1513 -91 -51 55 C ATOM 547 CD1 LEU A 70 -7.959 5.465 9.032 1.00 12.05 C ANISOU 547 CD1 LEU A 70 1582 1465 1530 -78 -37 42 C ATOM 548 CD2 LEU A 70 -7.808 3.479 10.614 1.00 11.03 C ANISOU 548 CD2 LEU A 70 1470 1311 1407 -80 -36 71 C ATOM 549 N LEU A 71 -9.160 3.967 5.753 1.00 9.29 N ANISOU 549 N LEU A 71 1291 1050 1188 -109 -105 17 N ATOM 550 CA LEU A 71 -8.383 3.340 4.696 1.00 8.79 C ANISOU 550 CA LEU A 71 1268 967 1105 -92 -116 -7 C ATOM 551 C LEU A 71 -6.911 3.358 5.055 1.00 9.21 C ANISOU 551 C LEU A 71 1327 1033 1140 -57 -91 -16 C ATOM 552 O LEU A 71 -6.380 4.407 5.472 1.00 9.45 O ANISOU 552 O LEU A 71 1332 1096 1165 -47 -69 -13 O ATOM 553 CB LEU A 71 -8.568 4.112 3.387 1.00 11.10 C ANISOU 553 CB LEU A 71 1565 1269 1382 -93 -127 -21 C ATOM 554 CG LEU A 71 -10.011 4.060 2.875 1.00 14.33 C ANISOU 554 CG LEU A 71 1970 1664 1810 -127 -158 -12 C ATOM 555 CD1 LEU A 71 -10.189 5.120 1.754 1.00 18.09 C ANISOU 555 CD1 LEU A 71 2443 2159 2271 -127 -165 -20 C ATOM 556 CD2 LEU A 71 -10.327 2.625 2.354 1.00 16.94 C ANISOU 556 CD2 LEU A 71 2342 1951 2143 -139 -192 -21 C ATOM 557 N VAL A 72 -6.249 2.229 4.864 1.00 9.42 N ANISOU 557 N VAL A 72 1387 1035 1158 -39 -97 -28 N ATOM 558 CA VAL A 72 -4.833 2.060 5.216 1.00 9.51 C ANISOU 558 CA VAL A 72 1402 1057 1156 -4 -75 -34 C ATOM 559 C VAL A 72 -4.152 1.383 4.033 1.00 9.91 C ANISOU 559 C VAL A 72 1491 1089 1184 23 -81 -60 C ATOM 560 O VAL A 72 -4.808 0.732 3.199 1.00 11.68 O ANISOU 560 O VAL A 72 1749 1284 1407 13 -107 -73 O ATOM 561 CB VAL A 72 -4.665 1.220 6.505 1.00 8.90 C ANISOU 561 CB VAL A 72 1324 965 1094 -2 -73 -16 C ATOM 562 CG1 VAL A 72 -5.411 1.900 7.695 1.00 11.39 C ANISOU 562 CG1 VAL A 72 1603 1302 1424 -27 -65 9 C ATOM 563 CG2 VAL A 72 -5.157 -0.273 6.343 1.00 11.91 C ANISOU 563 CG2 VAL A 72 1742 1295 1487 -11 -101 -17 C ATOM 564 N PRO A 73 -2.840 1.478 3.928 1.00 9.83 N ANISOU 564 N PRO A 73 1479 1097 1157 59 -58 -68 N ATOM 565 CA PRO A 73 -2.171 0.851 2.767 1.00 11.37 C ANISOU 565 CA PRO A 73 1712 1281 1328 92 -58 -94 C ATOM 566 C PRO A 73 -2.108 -0.677 2.879 1.00 10.42 C ANISOU 566 C PRO A 73 1633 1113 1214 107 -75 -105 C ATOM 567 O PRO A 73 -2.275 -1.280 3.938 1.00 11.20 O ANISOU 567 O PRO A 73 1728 1192 1335 98 -83 -88 O ATOM 568 CB PRO A 73 -0.753 1.463 2.764 1.00 14.48 C ANISOU 568 CB PRO A 73 2081 1715 1706 127 -24 -93 C ATOM 569 CG PRO A 73 -0.562 2.102 4.115 1.00 15.77 C ANISOU 569 CG PRO A 73 2202 1900 1890 114 -14 -68 C ATOM 570 CD PRO A 73 -1.943 2.308 4.750 1.00 10.86 C ANISOU 570 CD PRO A 73 1572 1265 1289 71 -33 -54 C ATOM 571 N THR A 74 -1.839 -1.306 1.709 1.00 12.73 N ANISOU 571 N THR A 74 1970 1386 1482 133 -82 -134 N ATOM 572 CA THR A 74 -1.742 -2.761 1.687 1.00 11.68 C ANISOU 572 CA THR A 74 1884 1201 1354 152 -102 -150 C ATOM 573 C THR A 74 -0.617 -3.295 2.553 1.00 13.49 C ANISOU 573 C THR A 74 2104 1431 1593 189 -83 -141 C ATOM 574 O THR A 74 -0.717 -4.442 3.030 1.00 17.07 O ANISOU 574 O THR A 74 2585 1838 2064 193 -102 -140 O ATOM 575 CB THR A 74 -1.588 -3.268 0.246 1.00 16.04 C ANISOU 575 CB THR A 74 2489 1734 1872 180 -112 -188 C ATOM 576 CG2 THR A 74 -2.671 -2.756 -0.645 1.00 16.41 C ANISOU 576 CG2 THR A 74 2547 1782 1908 145 -135 -196 C ATOM 577 OG1 THR A 74 -0.378 -2.764 -0.277 1.00 23.43 O ANISOU 577 OG1 THR A 74 3412 2712 2778 225 -73 -198 O ATOM 578 N THR A 75 0.424 -2.503 2.810 1.00 14.47 N ANISOU 578 N THR A 75 2187 1602 1707 213 -48 -131 N ATOM 579 CA THR A 75 1.550 -2.884 3.647 1.00 12.90 C ANISOU 579 CA THR A 75 1972 1411 1518 247 -31 -119 C ATOM 580 C THR A 75 1.263 -2.726 5.139 1.00 13.71 C ANISOU 580 C THR A 75 2044 1518 1649 218 -37 -86 C ATOM 581 O THR A 75 2.184 -2.998 5.938 1.00 16.31 O ANISOU 581 O THR A 75 2356 1855 1986 243 -26 -73 O ATOM 582 CB THR A 75 2.765 -2.037 3.277 1.00 14.86 C ANISOU 582 CB THR A 75 2185 1713 1747 279 5 -119 C ATOM 583 CG2 THR A 75 3.269 -2.503 1.900 1.00 21.02 C ANISOU 583 CG2 THR A 75 3002 2488 2496 323 16 -151 C ATOM 584 OG1 THR A 75 2.359 -0.663 3.228 1.00 19.91 O ANISOU 584 OG1 THR A 75 2790 2392 2385 244 13 -106 O ATOM 585 N THR A 76 0.067 -2.260 5.525 1.00 10.22 N ANISOU 585 N THR A 76 1590 1074 1220 169 -51 -72 N ATOM 586 CA THR A 76 -0.294 -2.279 6.963 1.00 8.91 C ANISOU 586 CA THR A 76 1401 908 1075 144 -56 -42 C ATOM 587 C THR A 76 -0.230 -3.714 7.474 1.00 10.08 C ANISOU 587 C THR A 76 1582 1008 1239 155 -74 -35 C ATOM 588 O THR A 76 -0.760 -4.614 6.828 1.00 12.98 O ANISOU 588 O THR A 76 1991 1330 1611 152 -97 -50 O ATOM 589 CB THR A 76 -1.707 -1.721 7.133 1.00 10.69 C ANISOU 589 CB THR A 76 1615 1136 1311 94 -68 -30 C ATOM 590 CG2 THR A 76 -2.090 -1.539 8.646 1.00 10.14 C ANISOU 590 CG2 THR A 76 1517 1078 1257 70 -65 3 C ATOM 591 OG1 THR A 76 -1.741 -0.403 6.522 1.00 12.10 O ANISOU 591 OG1 THR A 76 1768 1353 1476 87 -54 -38 O ATOM 592 N THR A 77 0.392 -3.892 8.640 1.00 10.74 N ANISOU 592 N THR A 77 1648 1102 1331 167 -67 -12 N ATOM 593 CA THR A 77 0.603 -5.259 9.129 1.00 11.71 C ANISOU 593 CA THR A 77 1802 1179 1470 183 -85 -2 C ATOM 594 C THR A 77 -0.634 -5.778 9.868 1.00 12.21 C ANISOU 594 C THR A 77 1874 1212 1554 137 -107 24 C ATOM 595 O THR A 77 -1.487 -5.003 10.339 1.00 12.41 O ANISOU 595 O THR A 77 1872 1263 1581 98 -102 42 O ATOM 596 CB THR A 77 1.827 -5.348 10.035 1.00 14.22 C ANISOU 596 CB THR A 77 2098 1517 1788 217 -72 15 C ATOM 597 CG2 THR A 77 3.084 -4.740 9.416 1.00 14.04 C ANISOU 597 CG2 THR A 77 2054 1533 1749 259 -47 -3 C ATOM 598 OG1 THR A 77 1.537 -4.675 11.275 1.00 14.05 O ANISOU 598 OG1 THR A 77 2042 1528 1769 187 -67 45 O ATOM 599 N ASP A 78 -0.663 -7.118 10.043 1.00 14.36 N ANISOU 599 N ASP A 78 2183 1429 1843 144 -130 31 N ATOM 600 CA ASP A 78 -1.718 -7.707 10.851 1.00 13.39 C ANISOU 600 CA ASP A 78 2067 1277 1743 101 -150 65 C ATOM 601 C ASP A 78 -1.677 -7.175 12.288 1.00 11.95 C ANISOU 601 C ASP A 78 1845 1137 1559 87 -133 104 C ATOM 602 O ASP A 78 -2.742 -6.908 12.849 1.00 13.71 O ANISOU 602 O ASP A 78 2051 1370 1789 44 -134 129 O ATOM 603 CB ASP A 78 -1.605 -9.241 10.840 1.00 15.07 C ANISOU 603 CB ASP A 78 2329 1421 1977 114 -180 69 C ATOM 604 CG ASP A 78 -2.132 -9.847 9.550 1.00 25.80 C ANISOU 604 CG ASP A 78 3733 2728 3340 109 -207 35 C ATOM 605 OD1 ASP A 78 -2.783 -9.171 8.681 1.00 21.32 O ANISOU 605 OD1 ASP A 78 3160 2176 2763 88 -208 14 O ATOM 606 OD2 ASP A 78 -1.931 -11.075 9.379 1.00 31.40 O1- ANISOU 606 OD2 ASP A 78 4490 3376 4066 127 -233 29 O1- ATOM 607 N AGLN A 79 -0.466 -7.055 12.904 0.65 10.70 N ANISOU 607 N AGLN A 79 1673 1003 1389 125 -119 109 N ATOM 608 N BGLN A 79 -0.508 -6.939 12.867 0.35 11.87 N ANISOU 608 N BGLN A 79 1818 1155 1536 123 -118 108 N ATOM 609 CA AGLN A 79 -0.322 -6.415 14.235 0.65 10.72 C ANISOU 609 CA AGLN A 79 1640 1051 1382 115 -105 140 C ATOM 610 CA BGLN A 79 -0.495 -6.435 14.243 0.35 12.02 C ANISOU 610 CA BGLN A 79 1805 1213 1548 109 -106 142 C ATOM 611 C AGLN A 79 -1.057 -5.070 14.236 0.65 11.92 C ANISOU 611 C AGLN A 79 1759 1249 1522 84 -87 136 C ATOM 612 C BGLN A 79 -0.903 -4.953 14.319 0.35 10.35 C ANISOU 612 C BGLN A 79 1556 1056 1320 88 -85 135 C ATOM 613 O AGLN A 79 -1.948 -4.822 15.077 0.65 9.90 O ANISOU 613 O AGLN A 79 1488 1007 1266 51 -83 162 O ATOM 614 O BGLN A 79 -1.443 -4.481 15.327 0.35 11.28 O ANISOU 614 O BGLN A 79 1652 1201 1432 64 -76 160 O ATOM 615 CB AGLN A 79 1.165 -6.170 14.638 0.65 9.84 C ANISOU 615 CB AGLN A 79 1512 968 1258 159 -94 138 C ATOM 616 CB BGLN A 79 0.876 -6.692 14.809 0.35 10.78 C ANISOU 616 CB BGLN A 79 1645 1066 1386 152 -103 148 C ATOM 617 CG AGLN A 79 1.940 -7.419 15.168 0.65 8.89 C ANISOU 617 CG AGLN A 79 1414 812 1150 191 -110 156 C ATOM 618 CG BGLN A 79 1.164 -8.185 14.828 0.35 10.03 C ANISOU 618 CG BGLN A 79 1589 912 1310 173 -125 158 C ATOM 619 CD AGLN A 79 1.417 -7.889 16.518 0.65 8.22 C ANISOU 619 CD AGLN A 79 1332 722 1070 165 -120 202 C ATOM 620 CD BGLN A 79 2.571 -8.417 15.196 0.35 13.81 C ANISOU 620 CD BGLN A 79 2061 1400 1785 222 -123 160 C ATOM 621 NE2AGLN A 79 1.504 -7.057 17.458 0.65 7.23 N ANISOU 621 NE2AGLN A 79 1176 645 925 155 -107 218 N ATOM 622 NE2BGLN A 79 3.104 -9.591 14.874 0.35 24.23 N ANISOU 622 NE2BGLN A 79 3415 2670 3121 257 -138 156 N ATOM 623 OE1AGLN A 79 0.986 -9.065 16.683 0.65 12.63 O ANISOU 623 OE1AGLN A 79 1924 1229 1648 156 -140 222 O ATOM 624 OE1BGLN A 79 3.207 -7.518 15.740 0.35 20.17 O ANISOU 624 OE1BGLN A 79 2831 2259 2575 230 -108 166 O ATOM 625 N GLU A 80 -0.724 -4.202 13.245 1.00 10.82 N ANISOU 625 N GLU A 80 1609 1132 1372 97 -76 103 N ATOM 626 CA GLU A 80 -1.256 -2.859 13.267 1.00 9.88 C ANISOU 626 CA GLU A 80 1457 1054 1241 74 -60 98 C ATOM 627 C GLU A 80 -2.761 -2.875 13.116 1.00 10.86 C ANISOU 627 C GLU A 80 1583 1165 1378 32 -68 108 C ATOM 628 O GLU A 80 -3.459 -2.090 13.796 1.00 11.23 O ANISOU 628 O GLU A 80 1604 1243 1421 9 -56 123 O ATOM 629 CB GLU A 80 -0.615 -2.071 12.133 1.00 10.75 C ANISOU 629 CB GLU A 80 1560 1185 1342 94 -50 66 C ATOM 630 CG GLU A 80 0.889 -1.668 12.426 1.00 13.04 C ANISOU 630 CG GLU A 80 1830 1505 1620 130 -37 63 C ATOM 631 CD GLU A 80 1.668 -1.246 11.172 1.00 12.80 C ANISOU 631 CD GLU A 80 1796 1486 1581 156 -27 36 C ATOM 632 OE1 GLU A 80 1.184 -1.484 10.034 1.00 13.01 O ANISOU 632 OE1 GLU A 80 1845 1492 1606 154 -30 15 O ATOM 633 OE2 GLU A 80 2.781 -0.734 11.373 1.00 13.95 O1- ANISOU 633 OE2 GLU A 80 1917 1664 1721 179 -16 37 O1- ATOM 634 N LEU A 81 -3.307 -3.725 12.209 1.00 9.94 N ANISOU 634 N LEU A 81 1497 1004 1277 22 -89 98 N ATOM 635 CA LEU A 81 -4.755 -3.796 12.048 1.00 10.77 C ANISOU 635 CA LEU A 81 1600 1095 1398 -21 -101 111 C ATOM 636 C LEU A 81 -5.442 -4.247 13.331 1.00 10.48 C ANISOU 636 C LEU A 81 1552 1057 1373 -48 -100 154 C ATOM 637 O LEU A 81 -6.482 -3.692 13.690 1.00 12.01 O ANISOU 637 O LEU A 81 1718 1273 1572 -78 -92 172 O ATOM 638 CB LEU A 81 -5.140 -4.726 10.893 1.00 12.31 C ANISOU 638 CB LEU A 81 1833 1237 1607 -28 -130 92 C ATOM 639 CG LEU A 81 -4.959 -4.196 9.510 1.00 20.09 C ANISOU 639 CG LEU A 81 2828 2226 2578 -15 -132 53 C ATOM 640 CD1 LEU A 81 -5.471 -5.333 8.590 1.00 22.37 C ANISOU 640 CD1 LEU A 81 3163 2455 2881 -25 -168 39 C ATOM 641 CD2 LEU A 81 -5.798 -2.980 9.341 1.00 20.96 C ANISOU 641 CD2 LEU A 81 2903 2373 2686 -41 -122 55 C ATOM 642 N GLN A 82 -4.878 -5.249 14.017 1.00 10.23 N ANISOU 642 N GLN A 82 1540 1001 1346 -34 -108 174 N ATOM 643 CA GLN A 82 -5.510 -5.734 15.236 1.00 11.09 C ANISOU 643 CA GLN A 82 1641 1110 1464 -60 -107 220 C ATOM 644 C GLN A 82 -5.511 -4.660 16.312 1.00 9.81 C ANISOU 644 C GLN A 82 1442 1007 1277 -59 -77 235 C ATOM 645 O GLN A 82 -6.485 -4.524 17.069 1.00 11.19 O ANISOU 645 O GLN A 82 1596 1200 1454 -88 -67 267 O ATOM 646 CB GLN A 82 -4.800 -6.992 15.738 1.00 11.83 C ANISOU 646 CB GLN A 82 1765 1164 1565 -42 -124 239 C ATOM 647 CG GLN A 82 -5.153 -8.181 14.841 1.00 19.63 C ANISOU 647 CG GLN A 82 2794 2083 2582 -53 -158 232 C ATOM 648 CD GLN A 82 -6.677 -8.317 14.824 1.00 47.04 C ANISOU 648 CD GLN A 82 6253 5543 6075 -108 -169 259 C ATOM 649 NE2 GLN A 82 -7.313 -8.061 13.667 1.00 52.03 N ANISOU 649 NE2 GLN A 82 6889 6163 6717 -125 -183 231 N ATOM 650 OE1 GLN A 82 -7.276 -8.577 15.873 1.00 51.88 O ANISOU 650 OE1 GLN A 82 6851 6166 6697 -135 -163 306 O ATOM 651 N HIS A 83 -4.414 -3.890 16.396 1.00 9.77 N ANISOU 651 N HIS A 83 1428 1033 1249 -26 -64 212 N ATOM 652 CA HIS A 83 -4.338 -2.817 17.374 1.00 11.55 C ANISOU 652 CA HIS A 83 1626 1313 1451 -23 -41 219 C ATOM 653 C HIS A 83 -5.304 -1.687 17.045 1.00 10.01 C ANISOU 653 C HIS A 83 1404 1145 1254 -43 -26 207 C ATOM 654 O HIS A 83 -6.006 -1.208 17.951 1.00 10.93 O ANISOU 654 O HIS A 83 1500 1293 1361 -57 -9 228 O ATOM 655 CB HIS A 83 -2.880 -2.346 17.463 1.00 12.06 C ANISOU 655 CB HIS A 83 1688 1397 1497 14 -38 198 C ATOM 656 CG HIS A 83 -2.702 -1.265 18.497 1.00 11.62 C ANISOU 656 CG HIS A 83 1610 1391 1415 17 -21 202 C ATOM 657 CD2 HIS A 83 -2.919 -1.280 19.822 1.00 13.44 C ANISOU 657 CD2 HIS A 83 1836 1644 1627 12 -14 230 C ATOM 658 ND1 HIS A 83 -2.316 0.007 18.175 1.00 16.08 N ANISOU 658 ND1 HIS A 83 2156 1986 1969 26 -13 173 N ATOM 659 CE1 HIS A 83 -2.271 0.742 19.273 1.00 12.33 C ANISOU 659 CE1 HIS A 83 1669 1547 1471 27 -3 181 C ATOM 660 NE2 HIS A 83 -2.638 -0.001 20.286 1.00 14.92 N ANISOU 660 NE2 HIS A 83 2006 1874 1791 20 -2 214 N ATOM 661 N LEU A 84 -5.387 -1.281 15.764 1.00 9.24 N ANISOU 661 N LEU A 84 1307 1039 1166 -43 -33 176 N ATOM 662 CA LEU A 84 -6.374 -0.292 15.381 1.00 8.04 C ANISOU 662 CA LEU A 84 1130 907 1017 -63 -23 169 C ATOM 663 C LEU A 84 -7.776 -0.752 15.746 1.00 9.95 C ANISOU 663 C LEU A 84 1361 1142 1277 -97 -23 202 C ATOM 664 O LEU A 84 -8.566 0.026 16.301 1.00 11.08 O ANISOU 664 O LEU A 84 1476 1318 1415 -108 -4 213 O ATOM 665 CB LEU A 84 -6.303 -0.044 13.842 1.00 10.24 C ANISOU 665 CB LEU A 84 1418 1169 1304 -60 -36 135 C ATOM 666 CG LEU A 84 -5.084 0.754 13.410 1.00 8.43 C ANISOU 666 CG LEU A 84 1187 959 1057 -30 -28 106 C ATOM 667 CD1 LEU A 84 -4.929 0.624 11.905 1.00 12.20 C ANISOU 667 CD1 LEU A 84 1683 1415 1539 -24 -41 79 C ATOM 668 CD2 LEU A 84 -5.319 2.263 13.736 1.00 11.09 C ANISOU 668 CD2 LEU A 84 1494 1337 1383 -32 -11 100 C ATOM 669 N ARG A 85 -8.127 -2.000 15.402 1.00 9.42 N ANISOU 669 N ARG A 85 1316 1032 1233 -115 -46 217 N ATOM 670 CA ARG A 85 -9.466 -2.495 15.694 1.00 11.25 C ANISOU 670 CA ARG A 85 1533 1255 1488 -154 -50 254 C ATOM 671 C ARG A 85 -9.733 -2.533 17.195 1.00 12.12 C ANISOU 671 C ARG A 85 1625 1395 1585 -159 -26 294 C ATOM 672 O ARG A 85 -10.841 -2.198 17.629 1.00 14.26 O ANISOU 672 O ARG A 85 1865 1691 1862 -181 -10 320 O ATOM 673 CB ARG A 85 -9.647 -3.871 15.098 1.00 13.10 C ANISOU 673 CB ARG A 85 1799 1429 1749 -173 -85 263 C ATOM 674 CG ARG A 85 -9.923 -3.685 13.606 1.00 19.93 C ANISOU 674 CG ARG A 85 2674 2272 2626 -179 -108 228 C ATOM 675 CD ARG A 85 -9.772 -4.974 12.814 1.00 30.49 C ANISOU 675 CD ARG A 85 4057 3546 3982 -185 -146 219 C ATOM 676 NE ARG A 85 -9.947 -4.662 11.396 1.00 35.63 N ANISOU 676 NE ARG A 85 4720 4183 4634 -186 -166 182 N ATOM 677 CZ ARG A 85 -9.638 -5.478 10.397 1.00 45.86 C ANISOU 677 CZ ARG A 85 6061 5429 5934 -180 -197 155 C ATOM 678 NH1 ARG A 85 -9.117 -6.667 10.672 1.00 49.57 N1+ ANISOU 678 NH1 ARG A 85 6567 5855 6413 -170 -214 162 N1+ ATOM 679 NH2 ARG A 85 -9.833 -5.097 9.128 1.00 39.99 N ANISOU 679 NH2 ARG A 85 5329 4680 5185 -180 -213 122 N ATOM 680 N ASN A 86 -8.724 -2.863 17.992 1.00 10.10 N ANISOU 680 N ASN A 86 1387 1143 1309 -135 -22 300 N ATOM 681 CA ASN A 86 -8.938 -2.891 19.429 1.00 10.46 C ANISOU 681 CA ASN A 86 1419 1219 1334 -138 0 339 C ATOM 682 C ASN A 86 -9.167 -1.518 20.023 1.00 11.92 C ANISOU 682 C ASN A 86 1576 1461 1491 -125 32 328 C ATOM 683 O ASN A 86 -9.909 -1.377 21.010 1.00 14.93 O ANISOU 683 O ASN A 86 1937 1874 1859 -135 56 361 O ATOM 684 CB ASN A 86 -7.724 -3.581 20.076 1.00 10.30 C ANISOU 684 CB ASN A 86 1428 1187 1299 -113 -9 346 C ATOM 685 CG ASN A 86 -7.986 -3.928 21.539 1.00 12.90 C ANISOU 685 CG ASN A 86 1752 1541 1608 -120 8 395 C ATOM 686 ND2 ASN A 86 -7.305 -3.286 22.439 1.00 14.60 N ANISOU 686 ND2 ASN A 86 1965 1796 1786 -95 23 389 N ATOM 687 OD1 ASN A 86 -8.827 -4.764 21.811 1.00 13.80 O ANISOU 687 OD1 ASN A 86 1863 1637 1741 -150 5 437 O ATOM 688 N SER A 87 -8.531 -0.488 19.450 1.00 9.70 N ANISOU 688 N SER A 87 1293 1193 1199 -103 33 284 N ATOM 689 CA SER A 87 -8.636 0.870 19.984 1.00 9.90 C ANISOU 689 CA SER A 87 1297 1265 1198 -88 58 268 C ATOM 690 C SER A 87 -9.846 1.647 19.500 1.00 10.89 C ANISOU 690 C SER A 87 1393 1405 1338 -103 71 264 C ATOM 691 O SER A 87 -10.357 2.486 20.257 1.00 15.38 O ANISOU 691 O SER A 87 1942 2013 1889 -95 97 267 O ATOM 692 CB SER A 87 -7.398 1.703 19.590 1.00 14.15 C ANISOU 692 CB SER A 87 1845 1809 1721 -60 51 226 C ATOM 693 OG SER A 87 -6.197 1.214 20.200 1.00 18.92 O ANISOU 693 OG SER A 87 2470 2411 2309 -41 42 229 O ATOM 694 N LEU A 88 -10.305 1.389 18.259 1.00 11.12 N ANISOU 694 N LEU A 88 1420 1404 1399 -121 51 255 N ATOM 695 CA LEU A 88 -11.295 2.208 17.615 1.00 11.60 C ANISOU 695 CA LEU A 88 1454 1477 1476 -132 57 246 C ATOM 696 C LEU A 88 -12.681 1.664 17.916 1.00 13.19 C ANISOU 696 C LEU A 88 1629 1682 1700 -163 64 289 C ATOM 697 O LEU A 88 -12.854 0.484 18.250 1.00 15.12 O ANISOU 697 O LEU A 88 1882 1906 1956 -183 55 323 O ATOM 698 CB LEU A 88 -11.062 2.222 16.103 1.00 10.64 C ANISOU 698 CB LEU A 88 1346 1324 1374 -136 29 217 C ATOM 699 CG LEU A 88 -10.213 3.431 15.602 1.00 11.04 C ANISOU 699 CG LEU A 88 1399 1388 1407 -110 31 175 C ATOM 700 CD1 LEU A 88 -8.912 3.652 16.357 1.00 12.67 C ANISOU 700 CD1 LEU A 88 1621 1608 1585 -82 39 163 C ATOM 701 CD2 LEU A 88 -9.947 3.318 14.117 1.00 14.60 C ANISOU 701 CD2 LEU A 88 1866 1810 1872 -113 6 151 C ATOM 702 N PRO A 89 -13.712 2.490 17.777 1.00 12.57 N ANISOU 702 N PRO A 89 1516 1629 1632 -168 79 292 N ATOM 703 CA PRO A 89 -15.080 1.984 17.933 1.00 14.79 C ANISOU 703 CA PRO A 89 1763 1915 1941 -200 84 336 C ATOM 704 C PRO A 89 -15.343 0.743 17.061 1.00 14.10 C ANISOU 704 C PRO A 89 1689 1777 1889 -236 44 351 C ATOM 705 O PRO A 89 -14.850 0.605 15.932 1.00 14.33 O ANISOU 705 O PRO A 89 1745 1771 1928 -237 13 320 O ATOM 706 CB PRO A 89 -15.940 3.199 17.509 1.00 17.60 C ANISOU 706 CB PRO A 89 2083 2298 2307 -193 97 323 C ATOM 707 CG PRO A 89 -15.043 4.404 17.675 1.00 20.40 C ANISOU 707 CG PRO A 89 2452 2671 2629 -153 110 279 C ATOM 708 CD PRO A 89 -13.632 3.925 17.404 1.00 14.52 C ANISOU 708 CD PRO A 89 1752 1897 1869 -144 88 255 C ATOM 709 N ASP A 90 -16.216 -0.159 17.565 1.00 19.66 N ANISOU 709 N ASP A 90 2376 2479 2616 -269 45 403 N ATOM 710 CA ASP A 90 -16.435 -1.403 16.830 1.00 18.30 C ANISOU 710 CA ASP A 90 2221 2252 2479 -306 3 418 C ATOM 711 C ASP A 90 -17.088 -1.218 15.469 1.00 20.14 C ANISOU 711 C ASP A 90 2446 2463 2743 -327 -31 401 C ATOM 712 O ASP A 90 -16.946 -2.090 14.600 1.00 27.35 O ANISOU 712 O ASP A 90 3391 3325 3677 -348 -73 392 O ATOM 713 CB ASP A 90 -17.347 -2.367 17.602 1.00 34.93 C ANISOU 713 CB ASP A 90 4304 4358 4609 -345 7 483 C ATOM 714 CG ASP A 90 -16.927 -2.555 19.007 1.00 52.83 C ANISOU 714 CG ASP A 90 6576 6654 6845 -328 41 511 C ATOM 715 OD1 ASP A 90 -17.830 -2.458 19.872 1.00 61.93 O ANISOU 715 OD1 ASP A 90 7691 7847 7993 -331 72 542 O ATOM 716 OD2 ASP A 90 -15.716 -2.796 19.252 1.00 58.31 O1- ANISOU 716 OD2 ASP A 90 7311 7332 7512 -302 37 489 O1- ATOM 717 N ASP A 91 -17.745 -0.099 15.218 1.00 18.29 N ANISOU 717 N ASP A 91 2175 2265 2512 -320 -15 392 N ATOM 718 CA ASP A 91 -18.403 0.042 13.930 1.00 22.75 C ANISOU 718 CA ASP A 91 2729 2808 3105 -342 -51 379 C ATOM 719 C ASP A 91 -17.539 0.733 12.863 1.00 23.93 C ANISOU 719 C ASP A 91 2911 2945 3235 -314 -66 322 C ATOM 720 O ASP A 91 -18.029 1.010 11.769 1.00 26.56 O ANISOU 720 O ASP A 91 3240 3266 3585 -327 -94 308 O ATOM 721 CB ASP A 91 -19.734 0.786 14.097 1.00 28.36 C ANISOU 721 CB ASP A 91 3378 3560 3839 -353 -32 407 C ATOM 722 CG ASP A 91 -19.592 2.087 14.876 1.00 46.51 C ANISOU 722 CG ASP A 91 5653 5911 6106 -309 18 394 C ATOM 723 OD1 ASP A 91 -18.457 2.528 15.119 1.00 43.05 O ANISOU 723 OD1 ASP A 91 5249 5477 5632 -275 31 359 O ATOM 724 OD2 ASP A 91 -20.629 2.666 15.281 1.00 54.48 O1- ANISOU 724 OD2 ASP A 91 6610 6960 7129 -309 44 420 O1- ATOM 725 N ILE A 92 -16.262 1.000 13.116 1.00 16.41 N ANISOU 725 N ILE A 92 1992 1995 2249 -278 -52 291 N ATOM 726 CA ILE A 92 -15.418 1.555 12.062 1.00 14.74 C ANISOU 726 CA ILE A 92 1809 1771 2019 -256 -66 243 C ATOM 727 C ILE A 92 -15.040 0.456 11.089 1.00 15.74 C ANISOU 727 C ILE A 92 1980 1845 2154 -270 -108 229 C ATOM 728 O ILE A 92 -14.486 -0.575 11.501 1.00 17.87 O ANISOU 728 O ILE A 92 2279 2089 2423 -271 -114 237 O ATOM 729 CB ILE A 92 -14.139 2.188 12.630 1.00 14.90 C ANISOU 729 CB ILE A 92 1847 1812 2004 -215 -39 217 C ATOM 730 CG1 ILE A 92 -14.417 3.175 13.764 1.00 19.08 C ANISOU 730 CG1 ILE A 92 2342 2389 2519 -198 1 228 C ATOM 731 CG2 ILE A 92 -13.323 2.845 11.520 1.00 13.23 C ANISOU 731 CG2 ILE A 92 1658 1593 1777 -195 -51 174 C ATOM 732 CD1 ILE A 92 -15.377 4.303 13.422 1.00 16.22 C ANISOU 732 CD1 ILE A 92 1942 2051 2169 -198 9 226 C ATOM 733 N AARG A 93 -15.327 0.665 9.805 0.44 12.88 N ANISOU 733 N AARG A 93 1627 1467 1800 -279 -138 207 N ATOM 734 N BARG A 93 -15.212 0.717 9.792 0.56 12.22 N ANISOU 734 N BARG A 93 1545 1384 1713 -276 -136 204 N ATOM 735 CA AARG A 93 -14.795 -0.195 8.763 0.44 14.20 C ANISOU 735 CA AARG A 93 1844 1587 1963 -282 -175 181 C ATOM 736 CA BARG A 93 -14.769 -0.210 8.762 0.56 14.29 C ANISOU 736 CA BARG A 93 1856 1598 1974 -281 -175 181 C ATOM 737 C AARG A 93 -13.333 0.181 8.533 0.44 14.51 C ANISOU 737 C AARG A 93 1915 1633 1967 -238 -159 143 C ATOM 738 C BARG A 93 -13.332 0.097 8.339 0.56 12.72 C ANISOU 738 C BARG A 93 1694 1400 1740 -239 -164 140 C ATOM 739 O AARG A 93 -13.064 1.348 8.227 0.44 12.15 O ANISOU 739 O AARG A 93 1602 1363 1651 -218 -142 124 O ATOM 740 O BARG A 93 -13.077 1.106 7.668 0.56 11.98 O ANISOU 740 O BARG A 93 1596 1327 1630 -222 -158 116 O ATOM 741 CB AARG A 93 -15.613 -0.016 7.477 0.44 16.62 C ANISOU 741 CB AARG A 93 2150 1880 2284 -304 -213 171 C ATOM 742 CB BARG A 93 -15.680 -0.142 7.545 0.56 18.53 C ANISOU 742 CB BARG A 93 2392 2120 2530 -308 -214 175 C ATOM 743 CG AARG A 93 -17.117 -0.289 7.661 0.44 21.11 C ANISOU 743 CG AARG A 93 2679 2449 2895 -350 -231 212 C ATOM 744 CG BARG A 93 -15.313 -1.194 6.577 0.56 19.84 C ANISOU 744 CG BARG A 93 2613 2233 2692 -314 -256 151 C ATOM 745 CD AARG A 93 -17.931 0.042 6.385 0.44 21.32 C ANISOU 745 CD AARG A 93 2700 2468 2934 -371 -271 203 C ATOM 746 CD BARG A 93 -16.455 -1.405 5.646 0.56 26.81 C ANISOU 746 CD BARG A 93 3492 3096 3600 -353 -303 157 C ATOM 747 NE AARG A 93 -18.077 1.472 6.035 0.44 14.11 N ANISOU 747 NE AARG A 93 1758 1594 2009 -351 -253 191 N ATOM 748 NE BARG A 93 -16.024 -2.050 4.426 0.56 29.82 N ANISOU 748 NE BARG A 93 3932 3433 3964 -350 -343 120 N ATOM 749 CZ AARG A 93 -19.186 2.181 6.215 0.44 22.86 C ANISOU 749 CZ AARG A 93 2811 2732 3143 -365 -248 218 C ATOM 750 CZ BARG A 93 -16.690 -1.909 3.292 0.56 26.15 C ANISOU 750 CZ BARG A 93 3475 2961 3502 -367 -381 108 C ATOM 751 NH1AARG A 93 -20.272 1.618 6.759 0.44 25.79 N1+ ANISOU 751 NH1AARG A 93 3145 3105 3548 -397 -254 259 N1+ ATOM 752 NH1BARG A 93 -17.798 -1.170 3.272 0.56 26.05 N1+ ANISOU 752 NH1BARG A 93 3409 2981 3509 -386 -381 132 N1+ ATOM 753 NH2AARG A 93 -19.252 3.433 5.835 0.44 25.30 N ANISOU 753 NH2AARG A 93 3100 3070 3442 -344 -236 205 N ATOM 754 NH2BARG A 93 -16.256 -2.516 2.208 0.56 32.78 N ANISOU 754 NH2BARG A 93 4370 3767 4317 -354 -411 71 N ATOM 755 N ILE A 94 -12.395 -0.772 8.724 1.00 13.86 N ANISOU 755 N ILE A 94 1871 1522 1875 -223 -163 135 N ATOM 756 CA ILE A 94 -10.962 -0.564 8.466 1.00 13.21 C ANISOU 756 CA ILE A 94 1815 1443 1761 -181 -149 102 C ATOM 757 C ILE A 94 -10.558 -1.468 7.318 1.00 15.76 C ANISOU 757 C ILE A 94 2189 1722 2079 -175 -181 74 C ATOM 758 O ILE A 94 -10.716 -2.694 7.422 1.00 17.26 O ANISOU 758 O ILE A 94 2405 1868 2284 -188 -205 83 O ATOM 759 CB ILE A 94 -10.107 -0.845 9.717 1.00 13.73 C ANISOU 759 CB ILE A 94 1880 1519 1817 -160 -123 115 C ATOM 760 CG1 ILE A 94 -10.635 -0.041 10.889 1.00 12.66 C ANISOU 760 CG1 ILE A 94 1701 1426 1684 -167 -94 142 C ATOM 761 CG2 ILE A 94 -8.608 -0.533 9.385 1.00 16.53 C ANISOU 761 CG2 ILE A 94 2255 1883 2144 -117 -110 83 C ATOM 762 CD1 ILE A 94 -9.884 -0.324 12.212 1.00 17.72 C ANISOU 762 CD1 ILE A 94 2342 2079 2311 -149 -72 158 C ATOM 763 N AGLN A 95 -10.052 -0.881 6.217 0.58 12.71 N ANISOU 763 N AGLN A 95 1816 1343 1669 -154 -182 41 N ATOM 764 N BGLN A 95 -10.032 -0.909 6.243 0.42 13.44 N ANISOU 764 N BGLN A 95 1910 1435 1762 -154 -182 41 N ATOM 765 CA AGLN A 95 -9.785 -1.591 4.966 0.58 13.63 C ANISOU 765 CA AGLN A 95 1983 1423 1774 -146 -211 10 C ATOM 766 CA BGLN A 95 -9.745 -1.735 5.090 0.42 13.14 C ANISOU 766 CA BGLN A 95 1922 1357 1713 -145 -211 12 C ATOM 767 C AGLN A 95 -8.424 -1.257 4.348 0.58 14.69 C ANISOU 767 C AGLN A 95 2138 1572 1873 -99 -191 -22 C ATOM 768 C BGLN A 95 -8.445 -1.299 4.436 0.42 14.10 C ANISOU 768 C BGLN A 95 2062 1496 1799 -100 -191 -20 C ATOM 769 O AGLN A 95 -8.140 -0.091 4.045 0.58 12.97 O ANISOU 769 O AGLN A 95 1898 1393 1638 -88 -170 -29 O ATOM 770 O BGLN A 95 -8.196 -0.101 4.302 0.42 11.05 O ANISOU 770 O BGLN A 95 1649 1151 1399 -91 -168 -23 O ATOM 771 CB AGLN A 95 -10.890 -1.254 3.943 0.58 16.12 C ANISOU 771 CB AGLN A 95 2296 1734 2095 -176 -242 6 C ATOM 772 CB BGLN A 95 -10.928 -1.651 4.119 0.42 14.58 C ANISOU 772 CB BGLN A 95 2107 1525 1906 -180 -248 10 C ATOM 773 CG AGLN A 95 -10.728 -1.940 2.599 0.58 15.37 C ANISOU 773 CG AGLN A 95 2257 1601 1982 -169 -277 -29 C ATOM 774 CG BGLN A 95 -10.835 -2.532 2.921 0.42 19.92 C ANISOU 774 CG BGLN A 95 2841 2158 2571 -177 -286 -21 C ATOM 775 CD AGLN A 95 -10.816 -3.445 2.757 0.58 21.42 C ANISOU 775 CD AGLN A 95 3063 2309 2766 -179 -308 -29 C ATOM 776 CD BGLN A 95 -12.192 -2.780 2.294 0.42 22.91 C ANISOU 776 CD BGLN A 95 3222 2512 2972 -223 -333 -13 C ATOM 777 NE2AGLN A 95 -9.798 -4.145 2.286 0.58 18.54 N ANISOU 777 NE2AGLN A 95 2749 1919 2378 -142 -309 -61 N ATOM 778 NE2BGLN A 95 -12.248 -2.641 0.992 0.42 21.02 N ANISOU 778 NE2BGLN A 95 3014 2266 2709 -218 -358 -43 N ATOM 779 OE1AGLN A 95 -11.778 -3.964 3.348 0.58 20.76 O ANISOU 779 OE1AGLN A 95 2964 2205 2718 -220 -329 2 O ATOM 780 OE1BGLN A 95 -13.178 -3.089 2.975 0.42 22.63 O ANISOU 780 OE1BGLN A 95 3157 2467 2973 -262 -347 22 O ATOM 781 N ARG A 96 -7.608 -2.278 4.091 1.00 13.80 N ANISOU 781 N ARG A 96 2069 1427 1750 -72 -198 -42 N ATOM 782 CA ARG A 96 -6.451 -2.089 3.214 1.00 13.16 C ANISOU 782 CA ARG A 96 2010 1356 1633 -28 -182 -74 C ATOM 783 C ARG A 96 -6.902 -1.746 1.799 1.00 14.12 C ANISOU 783 C ARG A 96 2153 1478 1735 -35 -202 -98 C ATOM 784 O ARG A 96 -7.850 -2.372 1.271 1.00 16.39 O ANISOU 784 O ARG A 96 2467 1728 2033 -63 -242 -103 O ATOM 785 CB ARG A 96 -5.595 -3.370 3.147 1.00 13.50 C ANISOU 785 CB ARG A 96 2099 1360 1671 5 -188 -92 C ATOM 786 CG ARG A 96 -4.901 -3.701 4.457 1.00 12.65 C ANISOU 786 CG ARG A 96 1974 1256 1577 21 -168 -70 C ATOM 787 CD ARG A 96 -4.007 -4.967 4.196 1.00 15.68 C ANISOU 787 CD ARG A 96 2406 1597 1955 62 -176 -91 C ATOM 788 NE ARG A 96 -3.226 -5.356 5.371 1.00 16.52 N ANISOU 788 NE ARG A 96 2499 1705 2073 82 -160 -70 N ATOM 789 CZ ARG A 96 -3.467 -6.448 6.095 1.00 19.47 C ANISOU 789 CZ ARG A 96 2891 2034 2472 72 -180 -52 C ATOM 790 NH1 ARG A 96 -4.540 -7.212 5.818 1.00 21.69 N1+ ANISOU 790 NH1 ARG A 96 3202 2266 2773 36 -219 -49 N1+ ATOM 791 NH2 ARG A 96 -2.679 -6.726 7.132 1.00 21.95 N ANISOU 791 NH2 ARG A 96 3192 2355 2792 94 -165 -32 N ATOM 792 N ILE A 97 -6.202 -0.822 1.155 1.00 12.33 N ANISOU 792 N ILE A 97 1918 1289 1478 -10 -177 -111 N ATOM 793 CA ILE A 97 -6.546 -0.431 -0.222 1.00 14.15 C ANISOU 793 CA ILE A 97 2171 1525 1683 -13 -193 -131 C ATOM 794 C ILE A 97 -5.272 -0.241 -1.025 1.00 13.14 C ANISOU 794 C ILE A 97 2062 1419 1513 35 -166 -155 C ATOM 795 O ILE A 97 -4.320 0.403 -0.569 1.00 15.39 O ANISOU 795 O ILE A 97 2314 1740 1793 58 -128 -145 O ATOM 796 CB ILE A 97 -7.443 0.811 -0.232 1.00 13.96 C ANISOU 796 CB ILE A 97 2104 1531 1669 -46 -195 -111 C ATOM 797 CG1 ILE A 97 -7.903 1.138 -1.668 1.00 14.30 C ANISOU 797 CG1 ILE A 97 2172 1576 1685 -52 -219 -128 C ATOM 798 CG2 ILE A 97 -6.711 2.041 0.383 1.00 13.95 C ANISOU 798 CG2 ILE A 97 2056 1578 1666 -31 -153 -95 C ATOM 799 CD1 ILE A 97 -8.878 2.302 -1.636 1.00 16.22 C ANISOU 799 CD1 ILE A 97 2372 1845 1946 -84 -226 -105 C ATOM 800 N GLU A 98 -5.265 -0.794 -2.274 1.00 16.26 N ANISOU 800 N GLU A 98 2509 1794 1877 51 -186 -187 N ATOM 801 CA GLU A 98 -4.181 -0.577 -3.206 1.00 16.48 C ANISOU 801 CA GLU A 98 2555 1847 1858 96 -158 -208 C ATOM 802 C GLU A 98 -4.341 0.793 -3.866 1.00 16.70 C ANISOU 802 C GLU A 98 2557 1922 1867 84 -146 -197 C ATOM 803 O GLU A 98 -5.428 1.136 -4.354 1.00 21.49 O ANISOU 803 O GLU A 98 3167 2522 2476 50 -177 -194 O ATOM 804 CB GLU A 98 -4.209 -1.675 -4.289 1.00 22.96 C ANISOU 804 CB GLU A 98 3448 2627 2647 118 -185 -248 C ATOM 805 CG GLU A 98 -3.065 -1.546 -5.257 1.00 35.58 C ANISOU 805 CG GLU A 98 5069 4256 4194 172 -151 -272 C ATOM 806 CD GLU A 98 -3.062 -2.642 -6.316 1.00 55.43 C ANISOU 806 CD GLU A 98 7652 6734 6675 198 -174 -311 C ATOM 807 OE1 GLU A 98 -3.851 -3.605 -6.180 1.00 60.42 O ANISOU 807 OE1 GLU A 98 8309 7314 7333 173 -217 -316 O ATOM 808 OE2 GLU A 98 -2.259 -2.544 -7.273 1.00 59.64 O1- ANISOU 808 OE2 GLU A 98 8195 7298 7167 238 -145 -324 O1- ATOM 809 N GLU A 99 -3.282 1.570 -3.853 1.00 14.93 N ANISOU 809 N GLU A 99 2303 1742 1627 111 -103 -188 N ATOM 810 CA GLU A 99 -3.365 2.900 -4.414 1.00 17.81 C ANISOU 810 CA GLU A 99 2641 2148 1977 99 -92 -172 C ATOM 811 C GLU A 99 -1.930 3.303 -4.683 1.00 17.09 C ANISOU 811 C GLU A 99 2536 2099 1860 140 -46 -170 C ATOM 812 O GLU A 99 -1.153 3.454 -3.735 1.00 21.43 O ANISOU 812 O GLU A 99 3050 2663 2431 151 -20 -155 O ATOM 813 CB GLU A 99 -4.072 3.824 -3.399 1.00 20.78 C ANISOU 813 CB GLU A 99 2965 2534 2397 59 -96 -141 C ATOM 814 CG GLU A 99 -4.300 5.230 -3.884 1.00 20.05 C ANISOU 814 CG GLU A 99 2845 2476 2297 43 -90 -123 C ATOM 815 CD GLU A 99 -3.048 6.038 -3.759 1.00 21.75 C ANISOU 815 CD GLU A 99 3029 2732 2502 65 -49 -109 C ATOM 816 OE1 GLU A 99 -2.585 6.172 -2.610 1.00 24.00 O ANISOU 816 OE1 GLU A 99 3282 3022 2815 66 -33 -97 O ATOM 817 OE2 GLU A 99 -2.511 6.496 -4.774 1.00 21.32 O1- ANISOU 817 OE2 GLU A 99 2983 2704 2413 81 -34 -109 O1- ATOM 818 N ARG A 100 -1.562 3.441 -5.945 1.00 19.61 N ANISOU 818 N ARG A 100 2882 2438 2132 163 -35 -183 N ATOM 819 CA ARG A 100 -0.156 3.586 -6.310 1.00 22.00 C ANISOU 819 CA ARG A 100 3176 2779 2406 208 11 -182 C ATOM 820 C ARG A 100 0.274 4.974 -6.763 1.00 23.43 C ANISOU 820 C ARG A 100 3318 3012 2572 201 37 -153 C ATOM 821 O ARG A 100 1.444 5.142 -7.097 1.00 29.24 O ANISOU 821 O ARG A 100 4040 3784 3285 235 77 -146 O ATOM 822 CB ARG A 100 0.200 2.575 -7.407 1.00 30.51 C ANISOU 822 CB ARG A 100 4314 3845 3432 252 13 -218 C ATOM 823 CG ARG A 100 -0.234 1.168 -7.049 1.00 36.28 C ANISOU 823 CG ARG A 100 5090 4517 4177 258 -18 -248 C ATOM 824 CD ARG A 100 0.541 0.140 -7.834 1.00 54.04 C ANISOU 824 CD ARG A 100 7388 6757 6388 314 -4 -282 C ATOM 825 NE ARG A 100 0.049 -1.196 -7.520 1.00 68.23 N ANISOU 825 NE ARG A 100 9224 8492 8208 312 -41 -305 N ATOM 826 CZ ARG A 100 0.778 -2.156 -6.955 1.00 80.90 C ANISOU 826 CZ ARG A 100 10834 10075 9831 347 -29 -313 C ATOM 827 NH1 ARG A 100 2.040 -1.919 -6.625 1.00 84.07 N1+ ANISOU 827 NH1 ARG A 100 11199 10515 10230 386 19 -300 N1+ ATOM 828 NH2 ARG A 100 0.225 -3.341 -6.712 1.00 85.75 N ANISOU 828 NH2 ARG A 100 11485 10630 10467 338 -68 -330 N ATOM 829 N LEU A 101 -0.608 5.978 -6.788 1.00 18.97 N ANISOU 829 N LEU A 101 2733 2451 2022 158 17 -133 N ATOM 830 CA LEU A 101 -0.219 7.275 -7.328 1.00 19.11 C ANISOU 830 CA LEU A 101 2721 2513 2025 151 38 -104 C ATOM 831 C LEU A 101 0.640 8.043 -6.360 1.00 20.11 C ANISOU 831 C LEU A 101 2790 2665 2186 148 65 -75 C ATOM 832 O LEU A 101 1.575 8.728 -6.766 1.00 25.30 O ANISOU 832 O LEU A 101 3423 3362 2828 160 97 -54 O ATOM 833 CB LEU A 101 -1.445 8.125 -7.669 1.00 16.70 C ANISOU 833 CB LEU A 101 2415 2201 1728 109 4 -91 C ATOM 834 CG LEU A 101 -2.113 7.611 -8.938 1.00 25.63 C ANISOU 834 CG LEU A 101 3602 3321 2814 113 -22 -114 C ATOM 835 CD1 LEU A 101 -3.215 8.499 -9.229 1.00 29.76 C ANISOU 835 CD1 LEU A 101 4117 3843 3349 75 -54 -96 C ATOM 836 CD2 LEU A 101 -1.125 7.698 -10.068 1.00 36.72 C ANISOU 836 CD2 LEU A 101 5026 4765 4161 150 12 -115 C ATOM 837 N SER A 102 0.322 7.971 -5.071 1.00 18.32 N ANISOU 837 N SER A 102 2541 2416 2005 129 52 -72 N ATOM 838 CA SER A 102 1.093 8.662 -4.046 1.00 17.19 C ANISOU 838 CA SER A 102 2347 2291 1894 124 72 -48 C ATOM 839 C SER A 102 0.651 8.004 -2.761 1.00 15.33 C ANISOU 839 C SER A 102 2109 2023 1694 115 54 -57 C ATOM 840 O SER A 102 -0.088 7.016 -2.779 1.00 19.51 O ANISOU 840 O SER A 102 2672 2519 2221 115 33 -79 O ATOM 841 CB SER A 102 0.837 10.192 -4.058 1.00 15.17 C ANISOU 841 CB SER A 102 2057 2054 1654 91 68 -19 C ATOM 842 OG SER A 102 1.631 10.942 -3.080 1.00 15.83 O ANISOU 842 OG SER A 102 2093 2153 1767 84 81 3 O ATOM 843 N ALA A 103 1.046 8.585 -1.641 1.00 13.97 N ANISOU 843 N ALA A 103 1896 1860 1553 104 61 -40 N ATOM 844 CA ALA A 103 0.519 8.111 -0.369 1.00 16.91 C ANISOU 844 CA ALA A 103 2265 2205 1956 92 45 -44 C ATOM 845 C ALA A 103 -0.970 8.382 -0.255 1.00 13.10 C ANISOU 845 C ALA A 103 1790 1699 1488 58 16 -45 C ATOM 846 O ALA A 103 -1.488 9.403 -0.761 1.00 13.53 O ANISOU 846 O ALA A 103 1835 1763 1542 39 9 -35 O ATOM 847 CB ALA A 103 1.265 8.786 0.776 1.00 16.72 C ANISOU 847 CB ALA A 103 2198 2198 1956 87 56 -25 C ATOM 848 N LEU A 104 -1.708 7.466 0.422 1.00 13.90 N ANISOU 848 N LEU A 104 1907 1771 1605 51 -1 -55 N ATOM 849 CA LEU A 104 -3.167 7.568 0.507 1.00 13.88 C ANISOU 849 CA LEU A 104 1908 1747 1618 20 -27 -53 C ATOM 850 C LEU A 104 -3.628 8.915 0.977 1.00 14.38 C ANISOU 850 C LEU A 104 1936 1825 1701 -2 -28 -36 C ATOM 851 O LEU A 104 -4.560 9.512 0.442 1.00 17.38 O ANISOU 851 O LEU A 104 2315 2204 2085 -21 -44 -32 O ATOM 852 CB LEU A 104 -3.799 6.543 1.478 1.00 25.14 C ANISOU 852 CB LEU A 104 3342 3144 3066 12 -41 -55 C ATOM 853 CG LEU A 104 -4.282 5.289 0.894 1.00 19.53 C ANISOU 853 CG LEU A 104 2671 2401 2347 13 -62 -72 C ATOM 854 CD1 LEU A 104 -4.563 4.357 2.143 1.00 13.31 C ANISOU 854 CD1 LEU A 104 1883 1589 1586 6 -68 -65 C ATOM 855 CD2 LEU A 104 -5.429 5.438 -0.046 1.00 16.03 C ANISOU 855 CD2 LEU A 104 2243 1947 1901 -11 -90 -75 C ATOM 856 N GLY A 105 -3.007 9.415 2.066 1.00 11.12 N ANISOU 856 N GLY A 105 1495 1425 1303 1 -13 -26 N ATOM 857 CA GLY A 105 -3.472 10.647 2.572 1.00 13.52 C ANISOU 857 CA GLY A 105 1772 1737 1626 -16 -16 -15 C ATOM 858 C GLY A 105 -3.200 11.836 1.685 1.00 13.14 C ANISOU 858 C GLY A 105 1715 1706 1570 -21 -13 -6 C ATOM 859 O GLY A 105 -3.774 12.915 1.893 1.00 16.29 O ANISOU 859 O GLY A 105 2096 2105 1986 -36 -21 3 O ATOM 860 N ASN A 106 -2.360 11.691 0.666 1.00 10.71 N ANISOU 860 N ASN A 106 1419 1413 1238 -6 -3 -6 N ATOM 861 CA ASN A 106 -2.144 12.779 -0.241 1.00 9.69 C ANISOU 861 CA ASN A 106 1281 1301 1100 -13 -1 8 C ATOM 862 C ASN A 106 -3.193 12.824 -1.352 1.00 10.85 C ANISOU 862 C ASN A 106 1450 1439 1234 -24 -20 6 C ATOM 863 O ASN A 106 -3.382 13.874 -1.963 1.00 12.69 O ANISOU 863 O ASN A 106 1675 1681 1466 -35 -26 22 O ATOM 864 CB ASN A 106 -0.789 12.666 -0.958 1.00 12.11 C ANISOU 864 CB ASN A 106 1587 1633 1381 8 23 14 C ATOM 865 CG ASN A 106 0.398 12.893 -0.024 1.00 12.04 C ANISOU 865 CG ASN A 106 1549 1639 1387 15 40 24 C ATOM 866 ND2 ASN A 106 1.594 12.552 -0.522 1.00 12.42 N ANISOU 866 ND2 ASN A 106 1592 1710 1415 38 63 29 N ATOM 867 OD1 ASN A 106 0.279 13.330 1.103 1.00 14.85 O ANISOU 867 OD1 ASN A 106 1886 1986 1768 4 32 26 O ATOM 868 N VAL A 107 -3.909 11.721 -1.565 1.00 9.88 N ANISOU 868 N VAL A 107 1353 1296 1103 -22 -35 -10 N ATOM 869 CA VAL A 107 -4.793 11.652 -2.734 1.00 9.86 C ANISOU 869 CA VAL A 107 1376 1288 1083 -32 -57 -13 C ATOM 870 C VAL A 107 -6.265 11.712 -2.372 1.00 10.90 C ANISOU 870 C VAL A 107 1501 1399 1243 -56 -86 -11 C ATOM 871 O VAL A 107 -7.114 11.675 -3.291 1.00 11.14 O ANISOU 871 O VAL A 107 1548 1422 1263 -67 -111 -12 O ATOM 872 CB VAL A 107 -4.510 10.398 -3.588 1.00 11.25 C ANISOU 872 CB VAL A 107 1593 1457 1223 -13 -59 -35 C ATOM 873 CG1 VAL A 107 -3.042 10.415 -4.138 1.00 13.96 C ANISOU 873 CG1 VAL A 107 1941 1829 1535 16 -26 -34 C ATOM 874 CG2 VAL A 107 -4.838 9.058 -2.867 1.00 11.90 C ANISOU 874 CG2 VAL A 107 1693 1511 1320 -10 -69 -53 C ATOM 875 N ILE A 108 -6.600 11.818 -1.095 1.00 10.67 N ANISOU 875 N ILE A 108 1446 1361 1246 -63 -82 -8 N ATOM 876 CA ILE A 108 -7.983 11.872 -0.605 1.00 9.53 C ANISOU 876 CA ILE A 108 1287 1202 1131 -82 -103 -2 C ATOM 877 C ILE A 108 -8.077 12.987 0.432 1.00 10.02 C ANISOU 877 C ILE A 108 1314 1272 1220 -84 -91 10 C ATOM 878 O ILE A 108 -7.234 13.073 1.334 1.00 11.83 O ANISOU 878 O ILE A 108 1535 1509 1453 -74 -70 7 O ATOM 879 CB ILE A 108 -8.405 10.554 0.083 1.00 11.87 C ANISOU 879 CB ILE A 108 1593 1480 1438 -86 -109 -10 C ATOM 880 CG1 ILE A 108 -8.342 9.360 -0.863 1.00 14.59 C ANISOU 880 CG1 ILE A 108 1978 1808 1758 -84 -125 -26 C ATOM 881 CG2 ILE A 108 -9.813 10.708 0.709 1.00 13.90 C ANISOU 881 CG2 ILE A 108 1825 1728 1729 -107 -124 2 C ATOM 882 CD1 ILE A 108 -8.279 8.009 -0.090 1.00 14.02 C ANISOU 882 CD1 ILE A 108 1919 1713 1694 -81 -125 -35 C ATOM 883 N VAL A 109 -9.149 13.790 0.380 1.00 10.58 N ANISOU 883 N VAL A 109 1366 1340 1311 -96 -105 21 N ATOM 884 CA VAL A 109 -9.526 14.581 1.560 1.00 11.10 C ANISOU 884 CA VAL A 109 1404 1408 1406 -95 -96 26 C ATOM 885 C VAL A 109 -11.018 14.395 1.777 1.00 11.30 C ANISOU 885 C VAL A 109 1413 1426 1456 -107 -111 34 C ATOM 886 O VAL A 109 -11.774 14.382 0.800 1.00 11.19 O ANISOU 886 O VAL A 109 1402 1407 1442 -118 -136 40 O ATOM 887 CB VAL A 109 -9.122 16.044 1.388 1.00 12.19 C ANISOU 887 CB VAL A 109 1530 1552 1548 -91 -93 34 C ATOM 888 CG1 VAL A 109 -9.777 16.660 0.209 1.00 13.31 C ANISOU 888 CG1 VAL A 109 1674 1693 1691 -100 -115 46 C ATOM 889 CG2 VAL A 109 -9.490 16.898 2.652 1.00 14.45 C ANISOU 889 CG2 VAL A 109 1792 1836 1861 -85 -84 34 C ATOM 890 N CYS A 110 -11.425 14.105 3.025 1.00 10.36 N ANISOU 890 N CYS A 110 1276 1307 1354 -105 -98 35 N ATOM 891 CA CYS A 110 -12.810 13.701 3.256 1.00 10.99 C ANISOU 891 CA CYS A 110 1336 1382 1456 -118 -109 46 C ATOM 892 C CYS A 110 -13.347 14.302 4.541 1.00 9.61 C ANISOU 892 C CYS A 110 1131 1218 1303 -107 -89 52 C ATOM 893 O CYS A 110 -12.587 14.663 5.448 1.00 12.47 O ANISOU 893 O CYS A 110 1495 1587 1657 -92 -67 43 O ATOM 894 CB CYS A 110 -12.966 12.168 3.269 1.00 11.56 C ANISOU 894 CB CYS A 110 1424 1444 1525 -131 -118 46 C ATOM 895 SG CYS A 110 -12.066 11.382 4.546 1.00 15.61 S ANISOU 895 SG CYS A 110 1944 1957 2027 -120 -91 39 S ATOM 896 N ASN A 111 -14.678 14.377 4.612 1.00 10.07 N ANISOU 896 N ASN A 111 1162 1279 1387 -115 -97 67 N ATOM 897 CA ASN A 111 -15.392 14.490 5.902 1.00 9.04 C ANISOU 897 CA ASN A 111 1001 1161 1274 -105 -74 76 C ATOM 898 C ASN A 111 -16.379 13.320 5.969 1.00 10.16 C ANISOU 898 C ASN A 111 1127 1302 1432 -128 -84 95 C ATOM 899 O ASN A 111 -16.119 12.264 5.375 1.00 10.60 O ANISOU 899 O ASN A 111 1206 1343 1478 -147 -103 94 O ATOM 900 CB ASN A 111 -16.021 15.893 6.021 1.00 9.61 C ANISOU 900 CB ASN A 111 1048 1239 1365 -87 -70 79 C ATOM 901 CG ASN A 111 -16.983 16.197 4.900 1.00 8.92 C ANISOU 901 CG ASN A 111 944 1147 1298 -99 -100 94 C ATOM 902 ND2 ASN A 111 -17.288 17.478 4.680 1.00 11.27 N ANISOU 902 ND2 ASN A 111 1228 1443 1609 -82 -104 94 N ATOM 903 OD1 ASN A 111 -17.557 15.271 4.316 1.00 10.65 O ANISOU 903 OD1 ASN A 111 1160 1362 1523 -122 -122 106 O ATOM 904 N ASP A 112 -17.461 13.437 6.733 1.00 10.70 N ANISOU 904 N ASP A 112 1157 1384 1524 -126 -70 114 N ATOM 905 CA ASP A 112 -18.391 12.325 6.875 1.00 9.36 C ANISOU 905 CA ASP A 112 967 1215 1373 -151 -79 139 C ATOM 906 C ASP A 112 -19.384 12.209 5.730 1.00 12.60 C ANISOU 906 C ASP A 112 1362 1618 1809 -175 -118 154 C ATOM 907 O ASP A 112 -20.149 11.238 5.692 1.00 15.41 O ANISOU 907 O ASP A 112 1703 1969 2184 -202 -134 176 O ATOM 908 CB ASP A 112 -19.124 12.402 8.202 1.00 11.29 C ANISOU 908 CB ASP A 112 1174 1484 1631 -140 -44 157 C ATOM 909 CG ASP A 112 -18.155 12.326 9.396 1.00 13.81 C ANISOU 909 CG ASP A 112 1514 1812 1922 -120 -11 143 C ATOM 910 OD1 ASP A 112 -17.118 11.634 9.257 1.00 15.12 O ANISOU 910 OD1 ASP A 112 1716 1962 2066 -127 -18 130 O ATOM 911 OD2 ASP A 112 -18.479 12.920 10.466 1.00 15.87 O1- ANISOU 911 OD2 ASP A 112 1752 2095 2181 -96 22 146 O1- ATOM 912 N HIS A 113 -19.366 13.134 4.757 1.00 12.19 N ANISOU 912 N HIS A 113 1315 1561 1755 -167 -137 146 N ATOM 913 CA HIS A 113 -20.325 13.138 3.673 1.00 13.63 C ANISOU 913 CA HIS A 113 1481 1737 1959 -188 -177 162 C ATOM 914 C HIS A 113 -19.704 13.051 2.307 1.00 11.02 C ANISOU 914 C HIS A 113 1194 1389 1604 -198 -212 146 C ATOM 915 O HIS A 113 -20.334 12.504 1.388 1.00 12.45 O ANISOU 915 O HIS A 113 1378 1559 1794 -224 -252 155 O ATOM 916 CB HIS A 113 -21.177 14.424 3.715 1.00 17.14 C ANISOU 916 CB HIS A 113 1884 2198 2430 -167 -173 174 C ATOM 917 CG HIS A 113 -21.879 14.645 5.056 1.00 21.31 C ANISOU 917 CG HIS A 113 2367 2749 2980 -149 -134 190 C ATOM 918 CD2 HIS A 113 -23.089 14.238 5.487 1.00 23.73 C ANISOU 918 CD2 HIS A 113 2624 3072 3319 -160 -131 221 C ATOM 919 ND1 HIS A 113 -21.313 15.348 6.103 1.00 28.14 N ANISOU 919 ND1 HIS A 113 3237 3626 3831 -115 -93 173 N ATOM 920 CE1 HIS A 113 -22.153 15.360 7.128 1.00 25.77 C ANISOU 920 CE1 HIS A 113 2894 3348 3549 -103 -63 191 C ATOM 921 NE2 HIS A 113 -23.227 14.679 6.777 1.00 28.65 N ANISOU 921 NE2 HIS A 113 3223 3718 3943 -130 -84 222 N ATOM 922 N THR A 114 -18.502 13.612 2.126 1.00 8.94 N ANISOU 922 N THR A 114 964 1123 1311 -178 -198 123 N ATOM 923 CA THR A 114 -17.974 13.811 0.802 1.00 9.77 C ANISOU 923 CA THR A 114 1103 1219 1391 -182 -224 112 C ATOM 924 C THR A 114 -16.469 13.575 0.826 1.00 9.27 C ANISOU 924 C THR A 114 1080 1151 1290 -170 -204 89 C ATOM 925 O THR A 114 -15.789 13.877 1.823 1.00 11.92 O ANISOU 925 O THR A 114 1412 1493 1622 -152 -170 81 O ATOM 926 CB THR A 114 -18.209 15.271 0.349 1.00 10.27 C ANISOU 926 CB THR A 114 1151 1288 1463 -167 -229 119 C ATOM 927 CG2 THR A 114 -17.991 15.426 -1.203 1.00 12.27 C ANISOU 927 CG2 THR A 114 1435 1535 1693 -177 -265 118 C ATOM 928 OG1 THR A 114 -19.504 15.722 0.714 1.00 15.28 O ANISOU 928 OG1 THR A 114 1738 1931 2137 -165 -234 141 O ATOM 929 N ALA A 115 -15.913 13.085 -0.282 1.00 11.63 N ANISOU 929 N ALA A 115 1418 1440 1560 -177 -225 77 N ATOM 930 CA ALA A 115 -14.460 13.015 -0.448 1.00 10.80 C ANISOU 930 CA ALA A 115 1348 1337 1420 -162 -205 58 C ATOM 931 C ALA A 115 -14.090 13.643 -1.775 1.00 12.10 C ANISOU 931 C ALA A 115 1534 1504 1558 -159 -221 57 C ATOM 932 O ALA A 115 -14.818 13.466 -2.778 1.00 13.19 O ANISOU 932 O ALA A 115 1681 1637 1693 -174 -257 63 O ATOM 933 CB ALA A 115 -13.942 11.617 -0.418 1.00 12.76 C ANISOU 933 CB ALA A 115 1626 1571 1649 -166 -205 44 C ATOM 934 N LEU A 116 -12.974 14.393 -1.797 1.00 9.96 N ANISOU 934 N LEU A 116 1271 1244 1270 -142 -198 53 N ATOM 935 CA LEU A 116 -12.348 14.858 -3.047 1.00 10.10 C ANISOU 935 CA LEU A 116 1314 1269 1255 -139 -205 54 C ATOM 936 C LEU A 116 -11.150 13.956 -3.266 1.00 9.91 C ANISOU 936 C LEU A 116 1323 1248 1196 -128 -188 36 C ATOM 937 O LEU A 116 -10.439 13.614 -2.297 1.00 10.59 O ANISOU 937 O LEU A 116 1403 1334 1286 -117 -162 27 O ATOM 938 CB LEU A 116 -11.886 16.314 -2.929 1.00 10.42 C ANISOU 938 CB LEU A 116 1337 1319 1304 -129 -191 67 C ATOM 939 CG LEU A 116 -12.979 17.285 -2.480 1.00 12.23 C ANISOU 939 CG LEU A 116 1532 1543 1573 -131 -202 82 C ATOM 940 CD1 LEU A 116 -12.377 18.673 -2.493 1.00 16.68 C ANISOU 940 CD1 LEU A 116 2089 2109 2142 -122 -192 92 C ATOM 941 CD2 LEU A 116 -14.233 17.170 -3.430 1.00 14.62 C ANISOU 941 CD2 LEU A 116 1833 1842 1882 -146 -242 95 C ATOM 942 N ILE A 117 -10.918 13.554 -4.521 1.00 10.03 N ANISOU 942 N ILE A 117 1373 1265 1174 -127 -203 29 N ATOM 943 CA ILE A 117 -9.791 12.627 -4.800 1.00 8.91 C ANISOU 943 CA ILE A 117 1264 1126 995 -111 -185 10 C ATOM 944 C ILE A 117 -8.972 13.140 -5.964 1.00 9.61 C ANISOU 944 C ILE A 117 1374 1235 1043 -99 -176 14 C ATOM 945 O ILE A 117 -9.467 13.835 -6.869 1.00 11.34 O ANISOU 945 O ILE A 117 1596 1460 1251 -108 -197 28 O ATOM 946 CB ILE A 117 -10.251 11.161 -5.094 1.00 9.68 C ANISOU 946 CB ILE A 117 1395 1201 1081 -116 -209 -11 C ATOM 947 CG1 ILE A 117 -11.192 11.103 -6.335 1.00 9.83 C ANISOU 947 CG1 ILE A 117 1437 1214 1085 -132 -253 -10 C ATOM 948 CG2 ILE A 117 -10.916 10.604 -3.851 1.00 11.16 C ANISOU 948 CG2 ILE A 117 1559 1371 1310 -129 -211 -9 C ATOM 949 CD1 ILE A 117 -11.471 9.645 -6.786 1.00 13.45 C ANISOU 949 CD1 ILE A 117 1938 1646 1524 -137 -281 -34 C ATOM 950 N HIS A 118 -7.706 12.714 -5.992 1.00 10.21 N ANISOU 950 N HIS A 118 1464 1324 1092 -77 -146 3 N ATOM 951 CA HIS A 118 -6.838 12.863 -7.169 1.00 10.33 C ANISOU 951 CA HIS A 118 1504 1362 1059 -61 -132 5 C ATOM 952 C HIS A 118 -7.584 12.440 -8.442 1.00 12.06 C ANISOU 952 C HIS A 118 1763 1575 1243 -66 -167 -4 C ATOM 953 O HIS A 118 -8.175 11.350 -8.464 1.00 13.11 O ANISOU 953 O HIS A 118 1922 1685 1375 -70 -191 -26 O ATOM 954 CB HIS A 118 -5.614 11.964 -6.902 1.00 12.97 C ANISOU 954 CB HIS A 118 1852 1703 1374 -33 -100 -13 C ATOM 955 CG HIS A 118 -4.499 12.068 -7.891 1.00 12.17 C ANISOU 955 CG HIS A 118 1767 1632 1224 -10 -73 -10 C ATOM 956 CD2 HIS A 118 -3.169 12.198 -7.679 1.00 12.86 C ANISOU 956 CD2 HIS A 118 1838 1745 1304 12 -33 -2 C ATOM 957 ND1 HIS A 118 -4.671 11.975 -9.251 1.00 15.58 N ANISOU 957 ND1 HIS A 118 2236 2075 1609 -4 -84 -13 N ATOM 958 CE1 HIS A 118 -3.495 12.115 -9.847 1.00 18.63 C ANISOU 958 CE1 HIS A 118 2627 2494 1958 21 -48 -6 C ATOM 959 NE2 HIS A 118 -2.560 12.222 -8.919 1.00 16.63 N ANISOU 959 NE2 HIS A 118 2339 2250 1729 31 -17 1 N ATOM 960 N PRO A 119 -7.571 13.259 -9.502 1.00 10.79 N ANISOU 960 N PRO A 119 1611 1435 1054 -69 -172 15 N ATOM 961 CA PRO A 119 -8.417 12.946 -10.679 1.00 12.97 C ANISOU 961 CA PRO A 119 1925 1705 1297 -77 -213 8 C ATOM 962 C PRO A 119 -7.987 11.706 -11.443 1.00 15.91 C ANISOU 962 C PRO A 119 2352 2076 1617 -56 -213 -25 C ATOM 963 O PRO A 119 -8.787 11.212 -12.239 1.00 16.27 O ANISOU 963 O PRO A 119 2435 2109 1640 -65 -254 -38 O ATOM 964 CB PRO A 119 -8.333 14.198 -11.525 1.00 16.72 C ANISOU 964 CB PRO A 119 2393 2205 1753 -82 -213 40 C ATOM 965 CG PRO A 119 -7.351 15.065 -10.924 1.00 22.66 C ANISOU 965 CG PRO A 119 3110 2975 2524 -75 -172 61 C ATOM 966 CD PRO A 119 -6.988 14.585 -9.547 1.00 12.93 C ANISOU 966 CD PRO A 119 1853 1729 1331 -70 -151 46 C ATOM 967 N ASP A 120 -6.799 11.154 -11.195 1.00 14.96 N ANISOU 967 N ASP A 120 2240 1967 1479 -27 -172 -40 N ATOM 968 CA ASP A 120 -6.390 9.955 -11.908 1.00 15.02 C ANISOU 968 CA ASP A 120 2302 1968 1435 0 -172 -74 C ATOM 969 C ASP A 120 -6.446 8.682 -11.107 1.00 16.16 C ANISOU 969 C ASP A 120 2460 2078 1603 7 -178 -104 C ATOM 970 O ASP A 120 -5.899 7.665 -11.575 1.00 19.22 O ANISOU 970 O ASP A 120 2892 2458 1951 36 -171 -135 O ATOM 971 CB ASP A 120 -4.963 10.118 -12.419 1.00 17.30 C ANISOU 971 CB ASP A 120 2597 2297 1679 37 -120 -70 C ATOM 972 CG ASP A 120 -4.809 11.330 -13.347 1.00 25.06 C ANISOU 972 CG ASP A 120 3572 3318 2632 31 -112 -36 C ATOM 973 OD1 ASP A 120 -5.763 11.669 -14.104 1.00 26.89 O ANISOU 973 OD1 ASP A 120 3823 3545 2849 11 -152 -29 O ATOM 974 OD2 ASP A 120 -3.725 11.937 -13.279 1.00 29.71 O1- ANISOU 974 OD2 ASP A 120 4133 3939 3215 46 -67 -13 O1- ATOM 975 N LEU A 121 -7.095 8.655 -9.922 1.00 13.66 N ANISOU 975 N LEU A 121 2107 1737 1346 -18 -191 -97 N ATOM 976 CA LEU A 121 -7.238 7.372 -9.243 1.00 16.40 C ANISOU 976 CA LEU A 121 2472 2048 1713 -16 -202 -122 C ATOM 977 C LEU A 121 -8.006 6.381 -10.120 1.00 16.37 C ANISOU 977 C LEU A 121 2525 2013 1683 -23 -250 -150 C ATOM 978 O LEU A 121 -8.911 6.758 -10.876 1.00 16.20 O ANISOU 978 O LEU A 121 2514 1991 1652 -46 -288 -143 O ATOM 979 CB LEU A 121 -7.974 7.492 -7.905 1.00 16.18 C ANISOU 979 CB LEU A 121 2398 2000 1748 -44 -211 -105 C ATOM 980 CG LEU A 121 -7.300 8.294 -6.794 1.00 16.40 C ANISOU 980 CG LEU A 121 2374 2049 1807 -39 -170 -83 C ATOM 981 CD1 LEU A 121 -8.056 8.097 -5.498 1.00 16.55 C ANISOU 981 CD1 LEU A 121 2363 2048 1880 -62 -180 -75 C ATOM 982 CD2 LEU A 121 -5.837 7.966 -6.668 1.00 17.79 C ANISOU 982 CD2 LEU A 121 2556 2241 1960 -3 -128 -93 C ATOM 983 N GLU A 122 -7.681 5.105 -9.980 1.00 17.25 N ANISOU 983 N GLU A 122 2673 2094 1785 -5 -253 -180 N ATOM 984 CA GLU A 122 -8.437 4.101 -10.717 1.00 15.94 C ANISOU 984 CA GLU A 122 2566 1891 1601 -15 -305 -209 C ATOM 985 C GLU A 122 -9.910 4.072 -10.302 1.00 19.04 C ANISOU 985 C GLU A 122 2935 2254 2043 -66 -357 -193 C ATOM 986 O GLU A 122 -10.271 4.444 -9.180 1.00 18.42 O ANISOU 986 O GLU A 122 2803 2177 2020 -87 -347 -167 O ATOM 987 CB GLU A 122 -7.827 2.716 -10.477 1.00 19.89 C ANISOU 987 CB GLU A 122 3099 2358 2100 14 -296 -240 C ATOM 988 CG GLU A 122 -6.382 2.577 -10.914 1.00 26.11 C ANISOU 988 CG GLU A 122 3905 3173 2843 69 -244 -256 C ATOM 989 CD GLU A 122 -6.246 2.718 -12.416 1.00 44.44 C ANISOU 989 CD GLU A 122 6255 5518 5113 87 -242 -265 C ATOM 990 OE1 GLU A 122 -7.214 2.369 -13.130 1.00 50.23 O ANISOU 990 OE1 GLU A 122 7012 6229 5845 64 -287 -273 O ATOM 991 OE2 GLU A 122 -5.194 3.191 -12.906 1.00 51.68 O1- ANISOU 991 OE2 GLU A 122 7167 6477 5990 122 -196 -262 O1- ATOM 992 N ARG A 123 -10.783 3.628 -11.230 1.00 21.08 N ANISOU 992 N ARG A 123 3216 2494 2298 -82 -398 -200 N ATOM 993 CA ARG A 123 -12.197 3.512 -10.893 1.00 18.81 C ANISOU 993 CA ARG A 123 2902 2183 2063 -128 -444 -180 C ATOM 994 C ARG A 123 -12.442 2.590 -9.714 1.00 18.91 C ANISOU 994 C ARG A 123 2903 2159 2124 -144 -450 -179 C ATOM 995 O ARG A 123 -13.283 2.899 -8.842 1.00 18.66 O ANISOU 995 O ARG A 123 2823 2123 2142 -178 -463 -151 O ATOM 996 CB ARG A 123 -13.005 3.052 -12.125 1.00 25.85 C ANISOU 996 CB ARG A 123 3825 3059 2939 -139 -487 -188 C ATOM 997 CG ARG A 123 -13.063 4.186 -13.154 1.00 42.61 C ANISOU 997 CG ARG A 123 5945 5220 5025 -136 -487 -177 C ATOM 998 CD ARG A 123 -13.719 3.797 -14.496 1.00 53.04 C ANISOU 998 CD ARG A 123 7303 6531 6320 -142 -527 -188 C ATOM 999 NE ARG A 123 -15.066 3.264 -14.297 1.00 59.06 N ANISOU 999 NE ARG A 123 8050 7259 7131 -182 -578 -176 N ATOM 1000 CZ ARG A 123 -15.845 2.799 -15.269 1.00 59.04 C ANISOU 1000 CZ ARG A 123 8075 7239 7119 -195 -622 -182 C ATOM 1001 NH1 ARG A 123 -15.420 2.814 -16.532 1.00 53.13 N1+ ANISOU 1001 NH1 ARG A 123 7373 6505 6310 -172 -623 -204 N1+ ATOM 1002 NH2 ARG A 123 -17.050 2.328 -14.969 1.00 55.02 N ANISOU 1002 NH2 ARG A 123 7545 6700 6658 -233 -665 -166 N ATOM 1003 N GLU A 124 -11.761 1.439 -9.663 1.00 20.74 N ANISOU 1003 N GLU A 124 3174 2363 2343 -118 -441 -206 N ATOM 1004 CA GLU A 124 -11.973 0.531 -8.544 1.00 23.41 C ANISOU 1004 CA GLU A 124 3503 2666 2728 -133 -448 -201 C ATOM 1005 C GLU A 124 -11.593 1.194 -7.221 1.00 17.74 C ANISOU 1005 C GLU A 124 2741 1964 2035 -137 -416 -183 C ATOM 1006 O GLU A 124 -12.256 0.985 -6.203 1.00 21.87 O ANISOU 1006 O GLU A 124 3230 2470 2608 -168 -426 -160 O ATOM 1007 CB GLU A 124 -11.153 -0.740 -8.762 1.00 30.66 C ANISOU 1007 CB GLU A 124 4472 3552 3624 -98 -441 -233 C ATOM 1008 CG GLU A 124 -11.387 -1.763 -7.704 1.00 49.20 C ANISOU 1008 CG GLU A 124 6817 5860 6018 -114 -452 -226 C ATOM 1009 CD GLU A 124 -10.415 -2.941 -7.782 1.00 61.90 C ANISOU 1009 CD GLU A 124 8473 7440 7608 -73 -439 -256 C ATOM 1010 OE1 GLU A 124 -10.238 -3.631 -6.744 1.00 60.98 O ANISOU 1010 OE1 GLU A 124 8350 7296 7524 -75 -435 -249 O ATOM 1011 OE2 GLU A 124 -9.829 -3.169 -8.872 1.00 66.09 O1- ANISOU 1011 OE2 GLU A 124 9045 7976 8091 -37 -433 -284 O1- ATOM 1012 N THR A 125 -10.537 1.999 -7.235 1.00 16.99 N ANISOU 1012 N THR A 125 2634 1909 1913 -103 -366 -183 N ATOM 1013 CA THR A 125 -10.109 2.685 -6.010 1.00 16.24 C ANISOU 1013 CA THR A 125 2480 1841 1849 -98 -320 -156 C ATOM 1014 C THR A 125 -11.184 3.661 -5.532 1.00 17.86 C ANISOU 1014 C THR A 125 2629 2064 2095 -135 -330 -121 C ATOM 1015 O THR A 125 -11.544 3.693 -4.326 1.00 15.36 O ANISOU 1015 O THR A 125 2270 1745 1822 -151 -319 -99 O ATOM 1016 CB THR A 125 -8.804 3.433 -6.298 1.00 15.68 C ANISOU 1016 CB THR A 125 2404 1811 1741 -57 -270 -160 C ATOM 1017 CG2 THR A 125 -8.211 3.990 -5.003 1.00 16.49 C ANISOU 1017 CG2 THR A 125 2455 1936 1875 -50 -227 -137 C ATOM 1018 OG1 THR A 125 -7.860 2.525 -6.901 1.00 18.27 O ANISOU 1018 OG1 THR A 125 2786 2127 2028 -18 -261 -193 O ATOM 1019 N GLU A 126 -11.773 4.406 -6.484 1.00 14.66 N ANISOU 1019 N GLU A 126 2223 1673 1674 -148 -353 -116 N ATOM 1020 CA GLU A 126 -12.841 5.333 -6.153 1.00 14.41 C ANISOU 1020 CA GLU A 126 2139 1656 1680 -178 -366 -84 C ATOM 1021 C GLU A 126 -14.050 4.597 -5.565 1.00 16.32 C ANISOU 1021 C GLU A 126 2364 1867 1969 -216 -403 -70 C ATOM 1022 O GLU A 126 -14.656 5.056 -4.596 1.00 15.81 O ANISOU 1022 O GLU A 126 2246 1814 1948 -232 -391 -42 O ATOM 1023 CB GLU A 126 -13.213 6.122 -7.401 1.00 13.82 C ANISOU 1023 CB GLU A 126 2075 1599 1576 -182 -390 -81 C ATOM 1024 CG GLU A 126 -14.439 6.986 -7.212 1.00 18.62 C ANISOU 1024 CG GLU A 126 2634 2218 2225 -213 -412 -49 C ATOM 1025 CD GLU A 126 -14.946 7.605 -8.493 1.00 35.92 C ANISOU 1025 CD GLU A 126 4839 4420 4390 -221 -448 -45 C ATOM 1026 OE1 GLU A 126 -14.377 7.340 -9.590 1.00 28.49 O ANISOU 1026 OE1 GLU A 126 3951 3479 3393 -205 -457 -68 O ATOM 1027 OE2 GLU A 126 -15.932 8.368 -8.374 1.00 46.10 O1- ANISOU 1027 OE2 GLU A 126 6085 5718 5713 -242 -466 -17 O1- ATOM 1028 N GLU A 127 -14.384 3.418 -6.114 1.00 16.58 N ANISOU 1028 N GLU A 127 2443 1861 1994 -230 -447 -90 N ATOM 1029 CA GLU A 127 -15.487 2.632 -5.570 1.00 14.87 C ANISOU 1029 CA GLU A 127 2207 1617 1826 -266 -477 -70 C ATOM 1030 C GLU A 127 -15.264 2.206 -4.118 1.00 14.18 C ANISOU 1030 C GLU A 127 2094 1519 1774 -271 -450 -57 C ATOM 1031 O GLU A 127 -16.187 2.261 -3.289 1.00 17.87 O ANISOU 1031 O GLU A 127 2513 1989 2288 -301 -455 -24 O ATOM 1032 CB GLU A 127 -15.742 1.403 -6.471 1.00 21.80 C ANISOU 1032 CB GLU A 127 3135 2459 2689 -267 -512 -90 C ATOM 1033 CG GLU A 127 -16.318 1.868 -7.832 1.00 39.97 C ANISOU 1033 CG GLU A 127 5449 4771 4965 -271 -541 -92 C ATOM 1034 CD GLU A 127 -16.518 0.738 -8.868 1.00 62.62 C ANISOU 1034 CD GLU A 127 8374 7607 7812 -269 -578 -115 C ATOM 1035 OE1 GLU A 127 -17.076 1.030 -9.953 1.00 64.03 O ANISOU 1035 OE1 GLU A 127 8564 7791 7973 -275 -607 -116 O ATOM 1036 OE2 GLU A 127 -16.118 -0.419 -8.602 1.00 67.23 O1- ANISOU 1036 OE2 GLU A 127 8990 8157 8397 -261 -580 -133 O1- ATOM 1037 N ILE A 128 -14.057 1.748 -3.807 1.00 17.52 N ANISOU 1037 N ILE A 128 2545 1937 2174 -236 -417 -77 N ATOM 1038 CA ILE A 128 -13.721 1.313 -2.449 1.00 16.29 C ANISOU 1038 CA ILE A 128 2367 1776 2046 -232 -386 -62 C ATOM 1039 C ILE A 128 -13.740 2.493 -1.488 1.00 14.27 C ANISOU 1039 C ILE A 128 2049 1564 1809 -228 -342 -35 C ATOM 1040 O ILE A 128 -14.279 2.385 -0.383 1.00 15.90 O ANISOU 1040 O ILE A 128 2218 1772 2053 -246 -333 -7 O ATOM 1041 CB ILE A 128 -12.373 0.611 -2.454 1.00 15.83 C ANISOU 1041 CB ILE A 128 2355 1704 1958 -192 -362 -91 C ATOM 1042 CG1 ILE A 128 -12.481 -0.730 -3.195 1.00 17.30 C ANISOU 1042 CG1 ILE A 128 2605 1837 2132 -198 -408 -119 C ATOM 1043 CG2 ILE A 128 -11.933 0.303 -0.989 1.00 17.66 C ANISOU 1043 CG2 ILE A 128 2559 1937 2215 -185 -328 -72 C ATOM 1044 CD1 ILE A 128 -11.110 -1.260 -3.618 1.00 22.44 C ANISOU 1044 CD1 ILE A 128 3307 2478 2740 -147 -386 -156 C ATOM 1045 N ILE A 129 -13.226 3.651 -1.920 1.00 13.75 N ANISOU 1045 N ILE A 129 1972 1533 1718 -205 -318 -40 N ATOM 1046 CA ILE A 129 -13.282 4.848 -1.080 1.00 14.81 C ANISOU 1046 CA ILE A 129 2053 1704 1871 -201 -283 -18 C ATOM 1047 C ILE A 129 -14.732 5.204 -0.753 1.00 14.14 C ANISOU 1047 C ILE A 129 1923 1624 1826 -234 -303 12 C ATOM 1048 O ILE A 129 -15.108 5.444 0.410 1.00 13.85 O ANISOU 1048 O ILE A 129 1844 1600 1819 -239 -281 35 O ATOM 1049 CB ILE A 129 -12.567 6.020 -1.799 1.00 13.58 C ANISOU 1049 CB ILE A 129 1899 1579 1683 -176 -264 -27 C ATOM 1050 CG1 ILE A 129 -11.063 5.759 -1.865 1.00 13.46 C ANISOU 1050 CG1 ILE A 129 1912 1567 1633 -141 -233 -48 C ATOM 1051 CG2 ILE A 129 -12.828 7.400 -1.057 1.00 15.01 C ANISOU 1051 CG2 ILE A 129 2025 1790 1886 -175 -238 -4 C ATOM 1052 CD1 ILE A 129 -10.298 6.658 -2.873 1.00 14.60 C ANISOU 1052 CD1 ILE A 129 2069 1739 1741 -119 -220 -57 C ATOM 1053 N ALA A 130 -15.588 5.286 -1.780 1.00 13.28 N ANISOU 1053 N ALA A 130 1821 1507 1719 -256 -346 13 N ATOM 1054 CA ALA A 130 -16.975 5.624 -1.507 1.00 13.48 C ANISOU 1054 CA ALA A 130 1797 1540 1786 -286 -366 44 C ATOM 1055 C ALA A 130 -17.648 4.627 -0.571 1.00 15.11 C ANISOU 1055 C ALA A 130 1985 1727 2031 -313 -373 66 C ATOM 1056 O ALA A 130 -18.436 5.027 0.300 1.00 16.60 O ANISOU 1056 O ALA A 130 2119 1934 2255 -324 -358 96 O ATOM 1057 CB ALA A 130 -17.728 5.655 -2.823 1.00 14.75 C ANISOU 1057 CB ALA A 130 1974 1691 1941 -307 -419 42 C ATOM 1058 N ASP A 131 -17.370 3.319 -0.767 1.00 15.80 N ANISOU 1058 N ASP A 131 2117 1775 2111 -323 -397 51 N ATOM 1059 CA ASP A 131 -17.988 2.265 0.055 1.00 21.21 C ANISOU 1059 CA ASP A 131 2789 2436 2833 -354 -409 74 C ATOM 1060 C ASP A 131 -17.500 2.313 1.512 1.00 16.90 C ANISOU 1060 C ASP A 131 2217 1908 2296 -336 -356 90 C ATOM 1061 O ASP A 131 -18.313 2.348 2.449 1.00 18.32 O ANISOU 1061 O ASP A 131 2348 2102 2511 -356 -344 126 O ATOM 1062 CB ASP A 131 -17.661 0.917 -0.573 1.00 18.28 C ANISOU 1062 CB ASP A 131 2479 2022 2445 -353 -439 51 C ATOM 1063 CG ASP A 131 -18.268 -0.258 0.194 1.00 32.06 C ANISOU 1063 CG ASP A 131 4214 3744 4224 -376 -448 77 C ATOM 1064 OD1 ASP A 131 -19.367 -0.116 0.753 1.00 38.64 O ANISOU 1064 OD1 ASP A 131 4994 4595 5093 -399 -446 114 O ATOM 1065 OD2 ASP A 131 -17.617 -1.310 0.254 1.00 40.19 O1- ANISOU 1065 OD2 ASP A 131 5289 4738 5243 -369 -454 60 O1- ATOM 1066 N VAL A 132 -16.175 2.263 1.705 1.00 14.93 N ANISOU 1066 N VAL A 132 1998 1659 2014 -300 -325 65 N ATOM 1067 CA VAL A 132 -15.621 2.181 3.067 1.00 14.77 C ANISOU 1067 CA VAL A 132 1961 1652 1998 -284 -282 78 C ATOM 1068 C VAL A 132 -15.928 3.457 3.865 1.00 14.61 C ANISOU 1068 C VAL A 132 1886 1678 1987 -274 -244 97 C ATOM 1069 O VAL A 132 -16.316 3.398 5.042 1.00 15.30 O ANISOU 1069 O VAL A 132 1939 1779 2094 -280 -220 124 O ATOM 1070 CB VAL A 132 -14.112 1.903 3.021 1.00 14.91 C ANISOU 1070 CB VAL A 132 2022 1664 1981 -246 -261 48 C ATOM 1071 CG1 VAL A 132 -13.478 2.030 4.452 1.00 15.20 C ANISOU 1071 CG1 VAL A 132 2037 1721 2018 -227 -216 62 C ATOM 1072 CG2 VAL A 132 -13.841 0.522 2.393 1.00 16.26 C ANISOU 1072 CG2 VAL A 132 2249 1784 2144 -251 -296 29 C ATOM 1073 N LEU A 133 -15.722 4.626 3.248 1.00 12.44 N ANISOU 1073 N LEU A 133 1604 1426 1695 -256 -236 83 N ATOM 1074 CA LEU A 133 -15.940 5.895 3.951 1.00 13.97 C ANISOU 1074 CA LEU A 133 1753 1658 1897 -242 -203 96 C ATOM 1075 C LEU A 133 -17.403 6.310 3.933 1.00 14.24 C ANISOU 1075 C LEU A 133 1741 1703 1965 -265 -218 123 C ATOM 1076 O LEU A 133 -17.787 7.166 4.711 1.00 13.56 O ANISOU 1076 O LEU A 133 1614 1645 1891 -254 -189 138 O ATOM 1077 CB LEU A 133 -15.054 7.006 3.357 1.00 12.55 C ANISOU 1077 CB LEU A 133 1586 1495 1689 -213 -190 72 C ATOM 1078 CG LEU A 133 -13.560 6.715 3.395 1.00 12.27 C ANISOU 1078 CG LEU A 133 1586 1454 1620 -187 -171 48 C ATOM 1079 CD1 LEU A 133 -12.829 7.976 2.834 1.00 15.72 C ANISOU 1079 CD1 LEU A 133 2025 1913 2037 -164 -157 34 C ATOM 1080 CD2 LEU A 133 -13.162 6.385 4.875 1.00 14.44 C ANISOU 1080 CD2 LEU A 133 1849 1736 1901 -178 -140 59 C ATOM 1081 N GLY A 134 -18.252 5.660 3.110 1.00 14.18 N ANISOU 1081 N GLY A 134 1738 1674 1976 -297 -263 132 N ATOM 1082 CA GLY A 134 -19.644 6.065 3.051 1.00 15.78 C ANISOU 1082 CA GLY A 134 1891 1891 2215 -320 -279 162 C ATOM 1083 C GLY A 134 -19.878 7.501 2.611 1.00 16.35 C ANISOU 1083 C GLY A 134 1939 1989 2286 -301 -273 159 C ATOM 1084 O GLY A 134 -20.659 8.235 3.226 1.00 18.12 O ANISOU 1084 O GLY A 134 2111 2239 2535 -296 -254 182 O ATOM 1085 N VAL A 135 -19.213 7.910 1.528 1.00 13.85 N ANISOU 1085 N VAL A 135 1659 1666 1939 -288 -289 132 N ATOM 1086 CA VAL A 135 -19.210 9.301 1.085 1.00 12.40 C ANISOU 1086 CA VAL A 135 1460 1502 1748 -268 -282 129 C ATOM 1087 C VAL A 135 -19.471 9.344 -0.403 1.00 13.71 C ANISOU 1087 C VAL A 135 1651 1656 1902 -281 -330 122 C ATOM 1088 O VAL A 135 -19.178 8.413 -1.139 1.00 14.12 O ANISOU 1088 O VAL A 135 1747 1685 1934 -295 -359 106 O ATOM 1089 CB VAL A 135 -17.874 10.038 1.376 1.00 13.34 C ANISOU 1089 CB VAL A 135 1600 1632 1836 -232 -244 106 C ATOM 1090 CG1 VAL A 135 -17.654 10.137 2.929 1.00 14.54 C ANISOU 1090 CG1 VAL A 135 1728 1799 1997 -217 -198 113 C ATOM 1091 CG2 VAL A 135 -16.667 9.346 0.688 1.00 13.06 C ANISOU 1091 CG2 VAL A 135 1622 1579 1760 -226 -250 79 C ATOM 1092 N GLU A 136 -19.990 10.506 -0.828 1.00 11.20 N ANISOU 1092 N GLU A 136 1307 1355 1595 -274 -337 133 N ATOM 1093 CA GLU A 136 -20.038 10.865 -2.240 1.00 9.70 C ANISOU 1093 CA GLU A 136 1142 1160 1384 -278 -375 127 C ATOM 1094 C GLU A 136 -18.640 11.309 -2.676 1.00 10.80 C ANISOU 1094 C GLU A 136 1324 1302 1477 -252 -353 101 C ATOM 1095 O GLU A 136 -18.013 12.113 -1.976 1.00 13.53 O ANISOU 1095 O GLU A 136 1658 1663 1822 -227 -313 99 O ATOM 1096 CB GLU A 136 -21.018 12.025 -2.393 1.00 12.35 C ANISOU 1096 CB GLU A 136 1430 1513 1749 -275 -386 151 C ATOM 1097 CG GLU A 136 -21.471 12.271 -3.834 1.00 13.82 C ANISOU 1097 CG GLU A 136 1634 1695 1924 -287 -436 155 C ATOM 1098 CD GLU A 136 -22.407 13.446 -3.907 1.00 13.80 C ANISOU 1098 CD GLU A 136 1585 1707 1950 -275 -438 180 C ATOM 1099 OE1 GLU A 136 -22.237 14.372 -3.093 1.00 15.24 O ANISOU 1099 OE1 GLU A 136 1735 1903 2151 -254 -406 186 O ATOM 1100 OE2 GLU A 136 -23.245 13.455 -4.831 1.00 14.42 O1- ANISOU 1100 OE2 GLU A 136 1665 1782 2032 -285 -472 192 O1- ATOM 1101 N VAL A 137 -18.138 10.855 -3.825 1.00 11.10 N ANISOU 1101 N VAL A 137 1413 1329 1476 -255 -379 82 N ATOM 1102 CA VAL A 137 -16.767 11.135 -4.242 1.00 9.56 C ANISOU 1102 CA VAL A 137 1256 1140 1236 -230 -354 61 C ATOM 1103 C VAL A 137 -16.724 12.021 -5.472 1.00 9.52 C ANISOU 1103 C VAL A 137 1266 1146 1205 -225 -373 65 C ATOM 1104 O VAL A 137 -17.494 11.804 -6.427 1.00 12.90 O ANISOU 1104 O VAL A 137 1707 1568 1629 -244 -420 70 O ATOM 1105 CB VAL A 137 -15.997 9.825 -4.511 1.00 11.66 C ANISOU 1105 CB VAL A 137 1574 1387 1470 -229 -356 34 C ATOM 1106 CG1 VAL A 137 -14.545 10.128 -4.935 1.00 13.95 C ANISOU 1106 CG1 VAL A 137 1896 1689 1713 -199 -325 16 C ATOM 1107 CG2 VAL A 137 -15.994 8.920 -3.265 1.00 14.70 C ANISOU 1107 CG2 VAL A 137 1945 1759 1880 -233 -338 34 C ATOM 1108 N PHE A 138 -15.797 13.000 -5.471 1.00 10.58 N ANISOU 1108 N PHE A 138 1401 1296 1322 -202 -341 65 N ATOM 1109 CA PHE A 138 -15.551 13.838 -6.649 1.00 9.92 C ANISOU 1109 CA PHE A 138 1336 1225 1209 -197 -354 72 C ATOM 1110 C PHE A 138 -14.066 13.915 -6.974 1.00 11.97 C ANISOU 1110 C PHE A 138 1628 1497 1425 -176 -321 58 C ATOM 1111 O PHE A 138 -13.254 14.199 -6.096 1.00 11.16 O ANISOU 1111 O PHE A 138 1511 1400 1331 -161 -281 55 O ATOM 1112 CB PHE A 138 -16.085 15.310 -6.486 1.00 9.46 C ANISOU 1112 CB PHE A 138 1237 1176 1182 -193 -353 99 C ATOM 1113 CG PHE A 138 -17.575 15.378 -6.284 1.00 9.61 C ANISOU 1113 CG PHE A 138 1218 1189 1245 -209 -385 117 C ATOM 1114 CD1 PHE A 138 -18.423 15.379 -7.375 1.00 10.85 C ANISOU 1114 CD1 PHE A 138 1382 1345 1398 -226 -435 129 C ATOM 1115 CD2 PHE A 138 -18.110 15.387 -5.009 1.00 11.46 C ANISOU 1115 CD2 PHE A 138 1409 1423 1524 -207 -365 123 C ATOM 1116 CE1 PHE A 138 -19.839 15.417 -7.197 1.00 11.46 C ANISOU 1116 CE1 PHE A 138 1416 1418 1519 -242 -467 151 C ATOM 1117 CE2 PHE A 138 -19.542 15.374 -4.795 1.00 13.10 C ANISOU 1117 CE2 PHE A 138 1573 1628 1775 -222 -392 144 C ATOM 1118 CZ PHE A 138 -20.388 15.363 -5.943 1.00 9.70 C ANISOU 1118 CZ PHE A 138 1147 1196 1344 -240 -444 158 C ATOM 1119 N ARG A 139 -13.735 13.707 -8.244 1.00 12.32 N ANISOU 1119 N ARG A 139 1714 1546 1421 -173 -337 51 N ATOM 1120 CA ARG A 139 -12.387 13.985 -8.729 1.00 11.49 C ANISOU 1120 CA ARG A 139 1634 1460 1273 -152 -305 46 C ATOM 1121 C ARG A 139 -12.197 15.485 -8.829 1.00 12.23 C ANISOU 1121 C ARG A 139 1701 1569 1377 -149 -293 75 C ATOM 1122 O ARG A 139 -13.016 16.168 -9.462 1.00 16.81 O ANISOU 1122 O ARG A 139 2275 2150 1962 -160 -325 95 O ATOM 1123 CB ARG A 139 -12.194 13.294 -10.092 1.00 11.62 C ANISOU 1123 CB ARG A 139 1705 1480 1231 -148 -326 31 C ATOM 1124 CG ARG A 139 -12.250 11.787 -9.920 1.00 12.93 C ANISOU 1124 CG ARG A 139 1901 1623 1389 -149 -337 -1 C ATOM 1125 CD ARG A 139 -12.417 11.025 -11.326 1.00 14.93 C ANISOU 1125 CD ARG A 139 2216 1872 1586 -149 -375 -21 C ATOM 1126 NE ARG A 139 -12.582 9.618 -11.028 1.00 16.33 N ANISOU 1126 NE ARG A 139 2420 2018 1767 -152 -391 -51 N ATOM 1127 CZ ARG A 139 -11.571 8.753 -10.911 1.00 17.24 C ANISOU 1127 CZ ARG A 139 2567 2129 1856 -126 -362 -78 C ATOM 1128 NH1 ARG A 139 -10.327 9.170 -11.150 1.00 16.14 N1+ ANISOU 1128 NH1 ARG A 139 2434 2018 1682 -95 -316 -78 N1+ ATOM 1129 NH2 ARG A 139 -11.802 7.499 -10.521 1.00 16.61 N ANISOU 1129 NH2 ARG A 139 2509 2014 1789 -131 -380 -102 N ATOM 1130 N GLN A 140 -11.127 16.007 -8.232 1.00 11.59 N ANISOU 1130 N GLN A 140 1605 1498 1298 -135 -252 78 N ATOM 1131 CA GLN A 140 -10.952 17.457 -8.153 1.00 12.47 C ANISOU 1131 CA GLN A 140 1691 1617 1428 -136 -244 105 C ATOM 1132 C GLN A 140 -9.472 17.807 -8.064 1.00 14.10 C ANISOU 1132 C GLN A 140 1899 1841 1616 -122 -204 109 C ATOM 1133 O GLN A 140 -8.635 16.945 -7.787 1.00 14.96 O ANISOU 1133 O GLN A 140 2021 1957 1707 -110 -179 90 O ATOM 1134 CB GLN A 140 -11.673 18.078 -6.911 1.00 17.57 C ANISOU 1134 CB GLN A 140 2294 2248 2133 -139 -244 111 C ATOM 1135 CG GLN A 140 -13.066 18.581 -7.159 1.00 25.68 C ANISOU 1135 CG GLN A 140 3304 3266 3189 -150 -281 127 C ATOM 1136 CD GLN A 140 -13.091 19.705 -8.136 1.00 35.28 C ANISOU 1136 CD GLN A 140 4524 4487 4395 -152 -297 155 C ATOM 1137 NE2 GLN A 140 -14.199 19.820 -8.840 1.00 41.78 N ANISOU 1137 NE2 GLN A 140 5345 5305 5222 -162 -338 168 N ATOM 1138 OE1 GLN A 140 -12.105 20.442 -8.313 1.00 30.22 O ANISOU 1138 OE1 GLN A 140 3887 3854 3740 -147 -276 167 O ATOM 1139 N THR A 141 -9.159 19.055 -8.383 1.00 15.35 N ANISOU 1139 N THR A 141 2045 2008 1779 -125 -201 137 N ATOM 1140 CA THR A 141 -7.847 19.602 -8.086 1.00 15.16 C ANISOU 1140 CA THR A 141 2010 1997 1753 -119 -166 148 C ATOM 1141 C THR A 141 -8.024 20.805 -7.176 1.00 15.54 C ANISOU 1141 C THR A 141 2025 2028 1851 -126 -168 162 C ATOM 1142 O THR A 141 -9.097 21.412 -7.129 1.00 17.39 O ANISOU 1142 O THR A 141 2249 2246 2114 -132 -195 171 O ATOM 1143 CB THR A 141 -7.071 20.026 -9.335 1.00 17.00 C ANISOU 1143 CB THR A 141 2261 2257 1942 -118 -157 172 C ATOM 1144 CG2 THR A 141 -6.686 18.824 -10.174 1.00 17.66 C ANISOU 1144 CG2 THR A 141 2382 2360 1970 -104 -148 153 C ATOM 1145 OG1 THR A 141 -7.840 20.927 -10.132 1.00 19.13 O ANISOU 1145 OG1 THR A 141 2533 2522 2213 -130 -187 200 O ATOM 1146 N AILE A 142 -6.963 21.164 -6.467 0.51 13.40 N ANISOU 1146 N AILE A 142 1738 1761 1591 -123 -142 164 N ATOM 1147 N BILE A 142 -6.957 21.128 -6.423 0.49 13.07 N ANISOU 1147 N BILE A 142 1696 1719 1550 -123 -142 163 N ATOM 1148 CA AILE A 142 -6.998 22.356 -5.633 0.51 15.42 C ANISOU 1148 CA AILE A 142 1969 1998 1891 -129 -146 175 C ATOM 1149 CA BILE A 142 -6.900 22.291 -5.511 0.49 13.47 C ANISOU 1149 CA BILE A 142 1721 1751 1645 -128 -143 173 C ATOM 1150 C AILE A 142 -5.838 23.240 -6.046 0.51 14.13 C ANISOU 1150 C AILE A 142 1801 1847 1722 -137 -134 204 C ATOM 1151 C BILE A 142 -5.798 23.231 -6.023 0.49 13.70 C ANISOU 1151 C BILE A 142 1746 1792 1668 -137 -133 204 C ATOM 1152 O AILE A 142 -4.676 22.856 -5.931 0.51 13.57 O ANISOU 1152 O AILE A 142 1727 1795 1635 -134 -108 203 O ATOM 1153 O BILE A 142 -4.616 22.897 -5.930 0.49 13.73 O ANISOU 1153 O BILE A 142 1746 1815 1654 -134 -107 205 O ATOM 1154 CB AILE A 142 -6.952 22.000 -4.150 0.51 13.00 C ANISOU 1154 CB AILE A 142 1647 1680 1612 -122 -134 149 C ATOM 1155 CB BILE A 142 -6.616 21.859 -4.057 0.49 15.15 C ANISOU 1155 CB BILE A 142 1920 1957 1881 -120 -127 147 C ATOM 1156 CG1AILE A 142 -8.115 21.064 -3.822 0.51 20.33 C ANISOU 1156 CG1AILE A 142 2579 2600 2546 -117 -145 127 C ATOM 1157 CG1BILE A 142 -7.616 20.791 -3.544 0.49 18.39 C ANISOU 1157 CG1BILE A 142 2333 2359 2295 -114 -133 121 C ATOM 1158 CG2AILE A 142 -7.007 23.286 -3.235 0.51 16.34 C ANISOU 1158 CG2AILE A 142 2051 2080 2079 -124 -141 155 C ATOM 1159 CG2BILE A 142 -6.564 23.090 -3.066 0.49 13.63 C ANISOU 1159 CG2BILE A 142 1707 1743 1730 -124 -132 152 C ATOM 1160 CD1AILE A 142 -8.047 20.640 -2.424 0.51 14.59 C ANISOU 1160 CD1AILE A 142 1839 1866 1838 -109 -130 105 C ATOM 1161 CD1BILE A 142 -9.046 21.338 -3.392 0.49 17.36 C ANISOU 1161 CD1BILE A 142 2191 2210 2196 -116 -158 125 C ATOM 1162 N ALA A 143 -6.163 24.436 -6.499 1.00 15.73 N ANISOU 1162 N ALA A 143 2000 2036 1942 -148 -154 233 N ATOM 1163 CA ALA A 143 -5.150 25.384 -6.991 1.00 15.99 C ANISOU 1163 CA ALA A 143 2026 2077 1972 -161 -146 269 C ATOM 1164 C ALA A 143 -4.186 24.690 -7.973 1.00 18.16 C ANISOU 1164 C ALA A 143 2313 2392 2194 -158 -120 281 C ATOM 1165 O ALA A 143 -2.949 24.822 -7.904 1.00 19.25 O ANISOU 1165 O ALA A 143 2438 2550 2328 -162 -95 297 O ATOM 1166 CB ALA A 143 -4.391 26.030 -5.804 1.00 17.90 C ANISOU 1166 CB ALA A 143 2246 2302 2252 -167 -139 266 C ATOM 1167 N ASP A 144 -4.784 23.844 -8.844 1.00 19.05 N ANISOU 1167 N ASP A 144 2451 2519 2267 -149 -125 271 N ATOM 1168 CA ASP A 144 -4.147 23.075 -9.917 1.00 22.44 C ANISOU 1168 CA ASP A 144 2903 2987 2637 -139 -104 275 C ATOM 1169 C ASP A 144 -3.308 21.912 -9.437 1.00 19.38 C ANISOU 1169 C ASP A 144 2515 2616 2232 -121 -71 246 C ATOM 1170 O ASP A 144 -2.638 21.247 -10.240 1.00 26.14 O ANISOU 1170 O ASP A 144 3389 3504 3040 -106 -48 247 O ATOM 1171 CB ASP A 144 -3.295 23.974 -10.809 1.00 27.40 C ANISOU 1171 CB ASP A 144 3525 3638 3246 -150 -91 323 C ATOM 1172 CG ASP A 144 -4.151 25.007 -11.515 1.00 43.90 C ANISOU 1172 CG ASP A 144 5623 5713 5345 -165 -125 355 C ATOM 1173 OD1 ASP A 144 -5.302 24.650 -11.884 1.00 48.57 O ANISOU 1173 OD1 ASP A 144 6234 6293 5925 -161 -153 339 O ATOM 1174 OD2 ASP A 144 -3.705 26.157 -11.672 1.00 49.31 O1- ANISOU 1174 OD2 ASP A 144 6293 6395 6049 -183 -127 396 O1- ATOM 1175 N HIS A 145 -3.398 21.574 -8.177 1.00 14.59 N ANISOU 1175 N HIS A 145 1894 1989 1661 -118 -71 219 N ATOM 1176 CA HIS A 145 -2.690 20.417 -7.629 1.00 15.86 C ANISOU 1176 CA HIS A 145 2055 2161 1809 -99 -45 192 C ATOM 1177 C HIS A 145 -3.588 19.194 -7.621 1.00 16.13 C ANISOU 1177 C HIS A 145 2116 2183 1829 -87 -58 156 C ATOM 1178 O HIS A 145 -4.745 19.257 -7.174 1.00 16.65 O ANISOU 1178 O HIS A 145 2181 2223 1922 -96 -85 145 O ATOM 1179 CB HIS A 145 -2.249 20.691 -6.196 1.00 14.11 C ANISOU 1179 CB HIS A 145 1804 1925 1633 -103 -39 184 C ATOM 1180 CG HIS A 145 -1.200 21.749 -6.099 1.00 16.77 C ANISOU 1180 CG HIS A 145 2114 2272 1986 -117 -28 217 C ATOM 1181 CD2 HIS A 145 -1.275 23.054 -5.739 1.00 22.66 C ANISOU 1181 CD2 HIS A 145 2842 2997 2769 -137 -45 239 C ATOM 1182 ND1 HIS A 145 0.122 21.491 -6.392 1.00 25.74 N ANISOU 1182 ND1 HIS A 145 3237 3441 3101 -109 4 232 N ATOM 1183 CE1 HIS A 145 0.826 22.595 -6.185 1.00 28.49 C ANISOU 1183 CE1 HIS A 145 3558 3790 3476 -129 3 265 C ATOM 1184 NE2 HIS A 145 -0.004 23.564 -5.830 1.00 24.72 N ANISOU 1184 NE2 HIS A 145 3081 3278 3034 -147 -28 269 N ATOM 1185 N VAL A 146 -3.028 18.057 -8.016 1.00 13.95 N ANISOU 1185 N VAL A 146 1860 1924 1514 -67 -38 137 N ATOM 1186 CA VAL A 146 -3.764 16.799 -7.918 1.00 14.09 C ANISOU 1186 CA VAL A 146 1906 1926 1523 -57 -52 102 C ATOM 1187 C VAL A 146 -3.676 16.100 -6.571 1.00 13.34 C ANISOU 1187 C VAL A 146 1797 1813 1459 -52 -45 79 C ATOM 1188 O VAL A 146 -4.533 15.260 -6.275 1.00 13.84 O ANISOU 1188 O VAL A 146 1875 1854 1529 -53 -64 56 O ATOM 1189 CB VAL A 146 -3.322 15.811 -9.010 1.00 15.56 C ANISOU 1189 CB VAL A 146 2130 2131 1650 -34 -40 87 C ATOM 1190 CG1 VAL A 146 -3.658 16.413 -10.398 1.00 16.45 C ANISOU 1190 CG1 VAL A 146 2264 2260 1725 -41 -53 109 C ATOM 1191 CG2 VAL A 146 -1.785 15.478 -8.892 1.00 16.49 C ANISOU 1191 CG2 VAL A 146 2238 2278 1752 -9 5 90 C ATOM 1192 N LEU A 147 -2.678 16.450 -5.730 1.00 13.11 N ANISOU 1192 N LEU A 147 1738 1792 1449 -48 -22 87 N ATOM 1193 CA LEU A 147 -2.525 15.821 -4.413 1.00 13.32 C ANISOU 1193 CA LEU A 147 1753 1805 1502 -42 -16 68 C ATOM 1194 C LEU A 147 -3.427 16.556 -3.432 1.00 13.11 C ANISOU 1194 C LEU A 147 1707 1756 1520 -61 -36 70 C ATOM 1195 O LEU A 147 -2.997 17.321 -2.545 1.00 12.65 O ANISOU 1195 O LEU A 147 1622 1695 1488 -67 -31 79 O ATOM 1196 CB LEU A 147 -1.081 15.838 -3.946 1.00 15.24 C ANISOU 1196 CB LEU A 147 1975 2069 1747 -30 14 76 C ATOM 1197 CG LEU A 147 -0.155 15.081 -4.854 1.00 16.51 C ANISOU 1197 CG LEU A 147 2152 2256 1866 -4 39 74 C ATOM 1198 CD1 LEU A 147 1.246 15.234 -4.241 1.00 21.95 C ANISOU 1198 CD1 LEU A 147 2807 2967 2567 6 66 87 C ATOM 1199 CD2 LEU A 147 -0.571 13.612 -4.960 1.00 17.51 C ANISOU 1199 CD2 LEU A 147 2314 2367 1972 16 35 40 C ATOM 1200 N VAL A 148 -4.734 16.326 -3.599 1.00 11.12 N ANISOU 1200 N VAL A 148 1467 1485 1272 -70 -61 61 N ATOM 1201 CA VAL A 148 -5.702 17.181 -2.901 1.00 12.25 C ANISOU 1201 CA VAL A 148 1589 1610 1454 -84 -79 67 C ATOM 1202 C VAL A 148 -5.578 17.044 -1.379 1.00 13.58 C ANISOU 1202 C VAL A 148 1739 1769 1650 -81 -69 56 C ATOM 1203 O VAL A 148 -5.875 18.008 -0.643 1.00 15.86 O ANISOU 1203 O VAL A 148 2009 2049 1967 -86 -74 61 O ATOM 1204 CB VAL A 148 -7.146 16.866 -3.357 1.00 12.40 C ANISOU 1204 CB VAL A 148 1620 1616 1477 -93 -107 63 C ATOM 1205 CG1 VAL A 148 -7.343 17.197 -4.819 1.00 14.22 C ANISOU 1205 CG1 VAL A 148 1869 1854 1680 -98 -123 77 C ATOM 1206 CG2 VAL A 148 -7.509 15.375 -3.098 1.00 14.04 C ANISOU 1206 CG2 VAL A 148 1844 1813 1677 -89 -111 41 C ATOM 1207 N GLY A 149 -5.161 15.873 -0.869 1.00 11.91 N ANISOU 1207 N GLY A 149 1537 1559 1429 -70 -56 39 N ATOM 1208 CA GLY A 149 -5.071 15.713 0.578 1.00 11.86 C ANISOU 1208 CA GLY A 149 1515 1546 1445 -66 -48 31 C ATOM 1209 C GLY A 149 -3.994 16.556 1.198 1.00 14.62 C ANISOU 1209 C GLY A 149 1846 1905 1803 -65 -36 38 C ATOM 1210 O GLY A 149 -4.019 16.749 2.427 1.00 14.37 O ANISOU 1210 O GLY A 149 1803 1868 1790 -64 -34 32 O ATOM 1211 N SER A 150 -2.963 16.906 0.427 1.00 11.51 N ANISOU 1211 N SER A 150 1451 1529 1395 -63 -26 52 N ATOM 1212 CA SER A 150 -1.919 17.789 0.937 1.00 11.74 C ANISOU 1212 CA SER A 150 1458 1565 1436 -67 -20 64 C ATOM 1213 C SER A 150 -2.341 19.223 1.044 1.00 10.46 C ANISOU 1213 C SER A 150 1286 1391 1299 -83 -36 75 C ATOM 1214 O SER A 150 -1.719 19.952 1.820 1.00 11.89 O ANISOU 1214 O SER A 150 1451 1567 1497 -89 -39 79 O ATOM 1215 CB SER A 150 -0.662 17.726 0.040 1.00 15.48 C ANISOU 1215 CB SER A 150 1929 2065 1889 -62 -2 80 C ATOM 1216 OG SER A 150 -0.160 16.396 0.117 1.00 22.11 O ANISOU 1216 OG SER A 150 2778 2915 2710 -41 14 66 O ATOM 1217 N TYR A 151 -3.343 19.663 0.290 1.00 11.99 N ANISOU 1217 N TYR A 151 1487 1574 1494 -90 -51 82 N ATOM 1218 CA TYR A 151 -3.613 21.065 0.078 1.00 11.54 C ANISOU 1218 CA TYR A 151 1422 1504 1458 -102 -67 98 C ATOM 1219 C TYR A 151 -4.933 21.541 0.628 1.00 12.59 C ANISOU 1219 C TYR A 151 1554 1615 1616 -101 -83 88 C ATOM 1220 O TYR A 151 -5.339 22.680 0.354 1.00 13.24 O ANISOU 1220 O TYR A 151 1633 1681 1716 -108 -100 102 O ATOM 1221 CB TYR A 151 -3.487 21.346 -1.424 1.00 12.86 C ANISOU 1221 CB TYR A 151 1597 1684 1604 -109 -69 123 C ATOM 1222 CG TYR A 151 -2.063 21.250 -1.854 1.00 13.68 C ANISOU 1222 CG TYR A 151 1694 1813 1690 -110 -48 139 C ATOM 1223 CD1 TYR A 151 -1.091 22.168 -1.408 1.00 12.80 C ANISOU 1223 CD1 TYR A 151 1563 1702 1600 -122 -48 156 C ATOM 1224 CD2 TYR A 151 -1.676 20.246 -2.727 1.00 14.18 C ANISOU 1224 CD2 TYR A 151 1772 1901 1716 -97 -31 138 C ATOM 1225 CE1 TYR A 151 0.216 22.085 -1.802 1.00 15.79 C ANISOU 1225 CE1 TYR A 151 1927 2107 1965 -124 -28 177 C ATOM 1226 CE2 TYR A 151 -0.376 20.136 -3.191 1.00 18.22 C ANISOU 1226 CE2 TYR A 151 2273 2441 2208 -93 -7 155 C ATOM 1227 CZ TYR A 151 0.590 21.042 -2.719 1.00 21.36 C ANISOU 1227 CZ TYR A 151 2643 2843 2630 -106 -5 177 C ATOM 1228 OH TYR A 151 1.889 20.950 -3.179 1.00 26.52 O ANISOU 1228 OH TYR A 151 3280 3529 3269 -103 20 200 O ATOM 1229 N AMET A 152 -5.662 20.700 1.377 0.50 10.58 N ANISOU 1229 N AMET A 152 1301 1356 1363 -92 -80 68 N ATOM 1230 N BMET A 152 -5.582 20.752 1.469 0.50 9.61 N ANISOU 1230 N BMET A 152 1177 1233 1241 -92 -79 68 N ATOM 1231 CA AMET A 152 -6.946 21.037 1.991 0.50 11.48 C ANISOU 1231 CA AMET A 152 1408 1454 1500 -87 -90 60 C ATOM 1232 CA BMET A 152 -6.855 21.158 2.035 0.50 9.30 C ANISOU 1232 CA BMET A 152 1131 1177 1224 -87 -90 60 C ATOM 1233 C AMET A 152 -7.005 20.372 3.363 0.50 8.46 C ANISOU 1233 C AMET A 152 1022 1073 1120 -77 -76 40 C ATOM 1234 C BMET A 152 -7.093 20.368 3.325 0.50 10.12 C ANISOU 1234 C BMET A 152 1232 1283 1330 -77 -77 40 C ATOM 1235 O AMET A 152 -6.473 19.264 3.542 0.50 11.18 O ANISOU 1235 O AMET A 152 1373 1429 1446 -75 -64 34 O ATOM 1236 O BMET A 152 -6.752 19.176 3.411 0.50 10.50 O ANISOU 1236 O BMET A 152 1287 1342 1361 -75 -66 34 O ATOM 1237 CB AMET A 152 -8.181 20.535 1.143 0.50 8.45 C ANISOU 1237 CB AMET A 152 1028 1070 1113 -90 -102 65 C ATOM 1238 CB BMET A 152 -7.975 20.907 1.006 0.50 14.82 C ANISOU 1238 CB BMET A 152 1835 1875 1922 -91 -104 69 C ATOM 1239 CG AMET A 152 -9.518 20.919 1.755 0.50 12.00 C ANISOU 1239 CG AMET A 152 1463 1507 1591 -83 -111 61 C ATOM 1240 CG BMET A 152 -9.313 21.022 1.560 0.50 12.83 C ANISOU 1240 CG BMET A 152 1570 1612 1692 -85 -111 64 C ATOM 1241 SD AMET A 152 -11.024 20.538 0.776 0.50 17.16 S ANISOU 1241 SD AMET A 152 2112 2160 2250 -89 -133 73 S ATOM 1242 SD BMET A 152 -10.350 20.704 0.150 0.50 14.80 S ANISOU 1242 SD BMET A 152 1824 1864 1936 -94 -135 79 S ATOM 1243 CE AMET A 152 -12.034 21.746 1.547 0.50 19.05 C ANISOU 1243 CE AMET A 152 2326 2384 2527 -75 -138 74 C ATOM 1244 CE BMET A 152 -11.760 21.581 0.767 0.50 17.56 C ANISOU 1244 CE BMET A 152 2148 2199 2325 -84 -145 82 C ATOM 1245 N ALA A 153 -7.698 21.034 4.307 1.00 9.76 N ANISOU 1245 N ALA A 153 1178 1225 1305 -68 -78 31 N ATOM 1246 CA ALA A 153 -8.219 20.389 5.499 1.00 9.32 C ANISOU 1246 CA ALA A 153 1117 1173 1249 -57 -65 17 C ATOM 1247 C ALA A 153 -9.720 20.615 5.572 1.00 9.32 C ANISOU 1247 C ALA A 153 1104 1169 1269 -50 -69 19 C ATOM 1248 O ALA A 153 -10.211 21.688 5.181 1.00 10.40 O ANISOU 1248 O ALA A 153 1235 1292 1423 -47 -82 24 O ATOM 1249 CB ALA A 153 -7.570 20.956 6.754 1.00 10.20 C ANISOU 1249 CB ALA A 153 1231 1282 1363 -48 -60 2 C ATOM 1250 N LEU A 154 -10.464 19.575 5.940 1.00 8.65 N ANISOU 1250 N LEU A 154 1012 1093 1181 -49 -60 18 N ATOM 1251 CA LEU A 154 -11.915 19.556 5.778 1.00 9.05 C ANISOU 1251 CA LEU A 154 1044 1143 1251 -47 -65 28 C ATOM 1252 C LEU A 154 -12.595 18.875 6.961 1.00 10.58 C ANISOU 1252 C LEU A 154 1225 1349 1448 -39 -46 25 C ATOM 1253 O LEU A 154 -12.163 17.795 7.385 1.00 11.06 O ANISOU 1253 O LEU A 154 1294 1417 1493 -45 -35 23 O ATOM 1254 CB LEU A 154 -12.236 18.773 4.478 1.00 10.00 C ANISOU 1254 CB LEU A 154 1169 1264 1366 -66 -83 41 C ATOM 1255 CG LEU A 154 -13.713 18.598 4.129 1.00 9.73 C ANISOU 1255 CG LEU A 154 1114 1231 1354 -71 -96 55 C ATOM 1256 CD1 LEU A 154 -14.403 19.934 3.835 1.00 12.38 C ANISOU 1256 CD1 LEU A 154 1433 1559 1713 -60 -108 63 C ATOM 1257 CD2 LEU A 154 -13.835 17.627 2.910 1.00 13.72 C ANISOU 1257 CD2 LEU A 154 1633 1734 1846 -92 -118 63 C ATOM 1258 N SER A 155 -13.653 19.515 7.464 1.00 9.38 N ANISOU 1258 N SER A 155 1051 1198 1315 -23 -39 27 N ATOM 1259 CA SER A 155 -14.546 18.848 8.430 1.00 8.44 C ANISOU 1259 CA SER A 155 912 1096 1201 -16 -19 32 C ATOM 1260 C SER A 155 -15.966 18.910 7.873 1.00 8.62 C ANISOU 1260 C SER A 155 903 1122 1252 -19 -28 52 C ATOM 1261 O SER A 155 -16.166 19.365 6.730 1.00 10.24 O ANISOU 1261 O SER A 155 1108 1316 1469 -27 -54 60 O ATOM 1262 CB SER A 155 -14.460 19.543 9.787 1.00 10.18 C ANISOU 1262 CB SER A 155 1132 1322 1415 12 5 16 C ATOM 1263 OG SER A 155 -15.154 20.815 9.751 1.00 10.42 O ANISOU 1263 OG SER A 155 1149 1343 1465 34 2 12 O ATOM 1264 N ASN A 156 -16.952 18.533 8.695 1.00 8.39 N ANISOU 1264 N ASN A 156 845 1110 1233 -10 -8 63 N ATOM 1265 CA ASN A 156 -18.335 18.748 8.257 1.00 9.87 C ANISOU 1265 CA ASN A 156 994 1303 1452 -9 -17 84 C ATOM 1266 C ASN A 156 -18.778 20.179 8.370 1.00 11.49 C ANISOU 1266 C ASN A 156 1187 1503 1674 23 -14 77 C ATOM 1267 O ASN A 156 -19.909 20.505 7.910 1.00 14.60 O ANISOU 1267 O ASN A 156 1547 1901 2099 28 -24 96 O ATOM 1268 CB ASN A 156 -19.268 17.878 9.084 1.00 12.12 C ANISOU 1268 CB ASN A 156 1247 1611 1745 -12 6 104 C ATOM 1269 CG ASN A 156 -18.963 16.385 8.980 1.00 11.43 C ANISOU 1269 CG ASN A 156 1172 1524 1647 -45 -1 115 C ATOM 1270 ND2 ASN A 156 -19.053 15.702 10.087 1.00 16.66 N ANISOU 1270 ND2 ASN A 156 1827 2202 2299 -43 27 123 N ATOM 1271 OD1 ASN A 156 -18.719 15.852 7.883 1.00 12.85 O ANISOU 1271 OD1 ASN A 156 1368 1687 1826 -72 -32 118 O ATOM 1272 N GLN A 157 -17.968 21.042 8.996 1.00 11.02 N ANISOU 1272 N GLN A 157 1152 1434 1600 46 -2 51 N ATOM 1273 CA GLN A 157 -18.372 22.422 9.293 1.00 12.51 C ANISOU 1273 CA GLN A 157 1335 1614 1805 81 2 40 C ATOM 1274 C GLN A 157 -17.756 23.425 8.335 1.00 12.15 C ANISOU 1274 C GLN A 157 1312 1538 1767 78 -29 33 C ATOM 1275 O GLN A 157 -18.308 24.549 8.183 1.00 14.36 O ANISOU 1275 O GLN A 157 1582 1803 2070 103 -37 32 O ATOM 1276 CB GLN A 157 -17.981 22.849 10.732 1.00 13.78 C ANISOU 1276 CB GLN A 157 1512 1780 1945 113 32 13 C ATOM 1277 CG GLN A 157 -18.486 21.896 11.776 1.00 20.17 C ANISOU 1277 CG GLN A 157 2302 2621 2741 118 66 21 C ATOM 1278 CD GLN A 157 -19.947 22.032 11.957 1.00 37.02 C ANISOU 1278 CD GLN A 157 4390 4776 4901 139 84 40 C ATOM 1279 NE2 GLN A 157 -20.358 23.022 12.749 1.00 39.41 N ANISOU 1279 NE2 GLN A 157 4688 5081 5204 185 106 22 N ATOM 1280 OE1 GLN A 157 -20.724 21.281 11.371 1.00 42.53 O ANISOU 1280 OE1 GLN A 157 5054 5485 5619 117 76 71 O ATOM 1281 N GLY A 158 -16.616 23.089 7.719 1.00 10.67 N ANISOU 1281 N GLY A 158 1154 1341 1561 50 -45 31 N ATOM 1282 CA GLY A 158 -15.872 24.099 6.965 1.00 10.77 C ANISOU 1282 CA GLY A 158 1189 1327 1577 46 -70 27 C ATOM 1283 C GLY A 158 -14.647 23.442 6.353 1.00 10.87 C ANISOU 1283 C GLY A 158 1226 1340 1564 16 -79 29 C ATOM 1284 O GLY A 158 -14.330 22.260 6.588 1.00 10.54 O ANISOU 1284 O GLY A 158 1187 1314 1502 2 -67 28 O ATOM 1285 N GLY A 159 -13.956 24.220 5.523 1.00 9.88 N ANISOU 1285 N GLY A 159 1118 1197 1441 6 -100 33 N ATOM 1286 CA GLY A 159 -12.700 23.745 4.928 1.00 11.30 C ANISOU 1286 CA GLY A 159 1318 1378 1596 -18 -105 36 C ATOM 1287 C GLY A 159 -11.744 24.902 4.724 1.00 10.05 C ANISOU 1287 C GLY A 159 1177 1200 1443 -21 -118 35 C ATOM 1288 O GLY A 159 -12.145 26.054 4.523 1.00 9.73 O ANISOU 1288 O GLY A 159 1134 1137 1424 -11 -133 40 O ATOM 1289 N LEU A 160 -10.470 24.556 4.704 1.00 8.78 N ANISOU 1289 N LEU A 160 1030 1045 1261 -36 -114 33 N ATOM 1290 CA LEU A 160 -9.369 25.508 4.495 1.00 9.05 C ANISOU 1290 CA LEU A 160 1077 1063 1298 -46 -127 37 C ATOM 1291 C LEU A 160 -8.558 24.973 3.331 1.00 9.39 C ANISOU 1291 C LEU A 160 1125 1122 1322 -68 -129 58 C ATOM 1292 O LEU A 160 -8.108 23.809 3.378 1.00 9.80 O ANISOU 1292 O LEU A 160 1179 1195 1350 -73 -113 53 O ATOM 1293 CB LEU A 160 -8.491 25.593 5.763 1.00 10.49 C ANISOU 1293 CB LEU A 160 1268 1244 1475 -41 -118 15 C ATOM 1294 CG LEU A 160 -7.355 26.622 5.669 1.00 10.13 C ANISOU 1294 CG LEU A 160 1232 1178 1438 -55 -136 21 C ATOM 1295 CD1 LEU A 160 -7.847 28.058 5.524 1.00 13.44 C ANISOU 1295 CD1 LEU A 160 1657 1563 1888 -48 -158 24 C ATOM 1296 CD2 LEU A 160 -6.437 26.492 6.957 1.00 11.90 C ANISOU 1296 CD2 LEU A 160 1465 1405 1652 -53 -131 -1 C ATOM 1297 N VAL A 161 -8.323 25.817 2.310 1.00 8.95 N ANISOU 1297 N VAL A 161 1073 1055 1273 -80 -146 81 N ATOM 1298 CA VAL A 161 -7.636 25.370 1.085 1.00 8.94 C ANISOU 1298 CA VAL A 161 1076 1072 1247 -98 -145 103 C ATOM 1299 C VAL A 161 -6.357 26.209 0.860 1.00 10.75 C ANISOU 1299 C VAL A 161 1309 1297 1480 -114 -150 120 C ATOM 1300 O VAL A 161 -6.196 27.320 1.401 1.00 10.37 O ANISOU 1300 O VAL A 161 1261 1222 1459 -115 -164 119 O ATOM 1301 CB VAL A 161 -8.554 25.420 -0.178 1.00 9.97 C ANISOU 1301 CB VAL A 161 1208 1204 1375 -102 -161 123 C ATOM 1302 CG1 VAL A 161 -9.713 24.442 -0.065 1.00 13.21 C ANISOU 1302 CG1 VAL A 161 1614 1624 1783 -92 -159 110 C ATOM 1303 CG2 VAL A 161 -9.050 26.849 -0.499 1.00 10.76 C ANISOU 1303 CG2 VAL A 161 1306 1276 1504 -101 -185 141 C ATOM 1304 N HIS A 162 -5.531 25.723 -0.070 1.00 9.99 N ANISOU 1304 N HIS A 162 1214 1224 1358 -127 -140 139 N ATOM 1305 CA HIS A 162 -4.315 26.408 -0.507 1.00 11.98 C ANISOU 1305 CA HIS A 162 1462 1479 1611 -145 -141 165 C ATOM 1306 C HIS A 162 -4.551 27.898 -0.710 1.00 11.68 C ANISOU 1306 C HIS A 162 1425 1409 1604 -155 -167 185 C ATOM 1307 O HIS A 162 -5.553 28.278 -1.314 1.00 11.59 O ANISOU 1307 O HIS A 162 1418 1385 1599 -151 -182 194 O ATOM 1308 CB HIS A 162 -3.913 25.709 -1.816 1.00 12.59 C ANISOU 1308 CB HIS A 162 1543 1588 1651 -150 -127 186 C ATOM 1309 CG HIS A 162 -2.593 26.125 -2.376 1.00 12.71 C ANISOU 1309 CG HIS A 162 1550 1620 1658 -167 -118 218 C ATOM 1310 CD2 HIS A 162 -1.507 25.375 -2.714 1.00 13.03 C ANISOU 1310 CD2 HIS A 162 1584 1695 1671 -166 -93 225 C ATOM 1311 ND1 HIS A 162 -2.300 27.430 -2.720 1.00 13.50 N ANISOU 1311 ND1 HIS A 162 1645 1703 1781 -187 -136 249 N ATOM 1312 CE1 HIS A 162 -1.067 27.461 -3.227 1.00 13.44 C ANISOU 1312 CE1 HIS A 162 1625 1722 1761 -201 -120 278 C ATOM 1313 NE2 HIS A 162 -0.568 26.238 -3.239 1.00 13.54 N ANISOU 1313 NE2 HIS A 162 1635 1767 1742 -187 -93 264 N ATOM 1314 N PRO A 163 -3.669 28.769 -0.210 1.00 10.31 N ANISOU 1314 N PRO A 163 1247 1218 1453 -170 -177 193 N ATOM 1315 CA PRO A 163 -3.927 30.223 -0.283 1.00 13.13 C ANISOU 1315 CA PRO A 163 1608 1534 1844 -179 -207 209 C ATOM 1316 C PRO A 163 -4.056 30.768 -1.679 1.00 14.55 C ANISOU 1316 C PRO A 163 1791 1716 2022 -193 -217 252 C ATOM 1317 O PRO A 163 -4.614 31.884 -1.812 1.00 17.27 O ANISOU 1317 O PRO A 163 2142 2023 2396 -195 -244 264 O ATOM 1318 CB PRO A 163 -2.725 30.835 0.457 1.00 17.55 C ANISOU 1318 CB PRO A 163 2164 2081 2425 -198 -216 211 C ATOM 1319 CG PRO A 163 -1.772 29.775 0.574 1.00 21.55 C ANISOU 1319 CG PRO A 163 2657 2626 2904 -201 -190 209 C ATOM 1320 CD PRO A 163 -2.486 28.419 0.565 1.00 13.45 C ANISOU 1320 CD PRO A 163 1635 1628 1846 -177 -166 184 C ATOM 1321 N LYS A 164 -3.562 30.076 -2.710 1.00 13.68 N ANISOU 1321 N LYS A 164 1678 1646 1876 -202 -198 275 N ATOM 1322 CA LYS A 164 -3.683 30.594 -4.069 1.00 14.36 C ANISOU 1322 CA LYS A 164 1768 1736 1952 -215 -207 319 C ATOM 1323 C LYS A 164 -4.919 30.091 -4.780 1.00 14.31 C ANISOU 1323 C LYS A 164 1773 1738 1925 -198 -211 313 C ATOM 1324 O LYS A 164 -5.125 30.419 -5.966 1.00 17.79 O ANISOU 1324 O LYS A 164 2221 2186 2350 -207 -221 348 O ATOM 1325 CB LYS A 164 -2.446 30.254 -4.884 1.00 16.14 C ANISOU 1325 CB LYS A 164 1984 2002 2145 -232 -183 351 C ATOM 1326 CG LYS A 164 -1.146 30.899 -4.383 1.00 19.85 C ANISOU 1326 CG LYS A 164 2436 2466 2640 -256 -183 371 C ATOM 1327 CD LYS A 164 0.031 30.447 -5.307 1.00 36.33 C ANISOU 1327 CD LYS A 164 4508 4604 4692 -268 -152 408 C ATOM 1328 CE LYS A 164 1.417 30.605 -4.640 1.00 44.46 C ANISOU 1328 CE LYS A 164 5511 5641 5741 -287 -144 419 C ATOM 1329 NZ LYS A 164 2.416 29.547 -5.000 1.00 43.97 N1+ ANISOU 1329 NZ LYS A 164 5431 5635 5642 -278 -104 426 N1+ ATOM 1330 N THR A 165 -5.790 29.307 -4.103 1.00 13.77 N ANISOU 1330 N THR A 165 1706 1669 1856 -176 -208 273 N ATOM 1331 CA THR A 165 -7.033 28.881 -4.761 1.00 12.92 C ANISOU 1331 CA THR A 165 1606 1566 1736 -164 -219 271 C ATOM 1332 C THR A 165 -7.863 30.101 -5.153 1.00 12.72 C ANISOU 1332 C THR A 165 1582 1509 1742 -165 -251 295 C ATOM 1333 O THR A 165 -8.140 30.972 -4.327 1.00 15.10 O ANISOU 1333 O THR A 165 1879 1774 2084 -157 -264 285 O ATOM 1334 CB THR A 165 -7.818 28.000 -3.766 1.00 12.34 C ANISOU 1334 CB THR A 165 1527 1492 1668 -144 -211 229 C ATOM 1335 CG2 THR A 165 -9.086 27.404 -4.465 1.00 12.08 C ANISOU 1335 CG2 THR A 165 1498 1468 1624 -137 -224 228 C ATOM 1336 OG1 THR A 165 -6.987 26.933 -3.333 1.00 11.76 O ANISOU 1336 OG1 THR A 165 1453 1443 1570 -144 -183 210 O ATOM 1337 N SER A 166 -8.338 30.129 -6.412 1.00 12.79 N ANISOU 1337 N SER A 166 1600 1529 1730 -170 -265 323 N ATOM 1338 CA SER A 166 -9.101 31.300 -6.844 1.00 15.23 C ANISOU 1338 CA SER A 166 1911 1808 2069 -169 -298 350 C ATOM 1339 C SER A 166 -10.451 31.386 -6.146 1.00 15.53 C ANISOU 1339 C SER A 166 1938 1821 2141 -144 -314 325 C ATOM 1340 O SER A 166 -10.977 30.384 -5.643 1.00 14.72 O ANISOU 1340 O SER A 166 1828 1734 2030 -132 -301 293 O ATOM 1341 CB SER A 166 -9.336 31.231 -8.355 1.00 15.74 C ANISOU 1341 CB SER A 166 1988 1894 2098 -179 -312 387 C ATOM 1342 OG SER A 166 -10.317 30.233 -8.659 1.00 17.18 O ANISOU 1342 OG SER A 166 2173 2095 2259 -167 -318 368 O ATOM 1343 N AILE A 167 -11.018 32.595 -6.086 0.51 15.89 N ANISOU 1343 N AILE A 167 1981 1828 2227 -137 -341 340 N ATOM 1344 N BILE A 167 -11.004 32.604 -6.110 0.49 15.82 N ANISOU 1344 N BILE A 167 1973 1819 2218 -137 -341 341 N ATOM 1345 CA AILE A 167 -12.298 32.705 -5.395 0.51 14.60 C ANISOU 1345 CA AILE A 167 1804 1646 2098 -108 -351 316 C ATOM 1346 CA BILE A 167 -12.288 32.809 -5.448 0.49 14.69 C ANISOU 1346 CA BILE A 167 1816 1655 2111 -108 -353 319 C ATOM 1347 C AILE A 167 -13.374 31.903 -6.144 0.51 14.59 C ANISOU 1347 C AILE A 167 1795 1670 2078 -103 -362 322 C ATOM 1348 C BILE A 167 -13.385 31.988 -6.144 0.49 14.22 C ANISOU 1348 C BILE A 167 1749 1621 2034 -102 -364 323 C ATOM 1349 O AILE A 167 -14.224 31.241 -5.524 0.51 14.42 O ANISOU 1349 O AILE A 167 1757 1656 2066 -86 -355 295 O ATOM 1350 O BILE A 167 -14.277 31.418 -5.486 0.49 17.38 O ANISOU 1350 O BILE A 167 2131 2027 2447 -84 -358 297 O ATOM 1351 CB AILE A 167 -12.694 34.183 -5.169 0.51 17.44 C ANISOU 1351 CB AILE A 167 2165 1956 2507 -94 -378 329 C ATOM 1352 CB BILE A 167 -12.619 34.320 -5.388 0.49 17.72 C ANISOU 1352 CB BILE A 167 2202 1989 2541 -98 -383 338 C ATOM 1353 CG1AILE A 167 -13.942 34.251 -4.282 0.51 20.77 C ANISOU 1353 CG1AILE A 167 2568 2361 2962 -57 -380 300 C ATOM 1354 CG1BILE A 167 -11.710 35.042 -4.377 0.49 21.10 C ANISOU 1354 CG1BILE A 167 2638 2384 2993 -100 -376 321 C ATOM 1355 CG2AILE A 167 -12.879 34.912 -6.479 0.51 18.82 C ANISOU 1355 CG2AILE A 167 2348 2121 2681 -107 -410 379 C ATOM 1356 CG2BILE A 167 -14.065 34.540 -5.045 0.49 22.00 C ANISOU 1356 CG2BILE A 167 2728 2515 3117 -65 -397 326 C ATOM 1357 CD1AILE A 167 -13.816 33.468 -2.981 0.51 24.45 C ANISOU 1357 CD1AILE A 167 3027 2841 3423 -44 -347 254 C ATOM 1358 CD1BILE A 167 -11.804 36.568 -4.440 0.49 26.73 C ANISOU 1358 CD1BILE A 167 3363 3043 3751 -96 -409 343 C ATOM 1359 N GLN A 168 -13.303 31.862 -7.477 1.00 16.78 N ANISOU 1359 N GLN A 168 2085 1964 2326 -120 -379 357 N ATOM 1360 CA GLN A 168 -14.246 31.029 -8.234 1.00 16.75 C ANISOU 1360 CA GLN A 168 2079 1986 2300 -120 -395 360 C ATOM 1361 C GLN A 168 -14.123 29.566 -7.850 1.00 14.64 C ANISOU 1361 C GLN A 168 1811 1748 2003 -122 -370 326 C ATOM 1362 O GLN A 168 -15.142 28.884 -7.635 1.00 15.03 O ANISOU 1362 O GLN A 168 1845 1805 2061 -113 -378 310 O ATOM 1363 CB GLN A 168 -13.998 31.160 -9.742 1.00 19.30 C ANISOU 1363 CB GLN A 168 2424 2326 2584 -139 -415 401 C ATOM 1364 CG GLN A 168 -14.502 32.445 -10.327 1.00 41.66 C ANISOU 1364 CG GLN A 168 5256 5130 5445 -136 -451 441 C ATOM 1365 CD GLN A 168 -14.931 32.303 -11.785 1.00 60.70 C ANISOU 1365 CD GLN A 168 7682 7562 7818 -148 -481 476 C ATOM 1366 NE2 GLN A 168 -15.692 33.290 -12.268 1.00 64.28 N ANISOU 1366 NE2 GLN A 168 8130 7995 8299 -142 -506 496 N ATOM 1367 OE1 GLN A 168 -14.617 31.308 -12.459 1.00 67.64 O ANISOU 1367 OE1 GLN A 168 8579 8478 8642 -160 -473 472 O ATOM 1368 N ASP A 169 -12.873 29.067 -7.693 1.00 13.34 N ANISOU 1368 N ASP A 169 1660 1601 1808 -133 -339 314 N ATOM 1369 CA ASP A 169 -12.716 27.679 -7.307 1.00 12.76 C ANISOU 1369 CA ASP A 169 1589 1551 1709 -133 -317 282 C ATOM 1370 C ASP A 169 -13.173 27.448 -5.869 1.00 12.93 C ANISOU 1370 C ASP A 169 1588 1560 1765 -117 -302 250 C ATOM 1371 O ASP A 169 -13.731 26.398 -5.571 1.00 13.04 O ANISOU 1371 O ASP A 169 1595 1587 1773 -114 -297 229 O ATOM 1372 CB ASP A 169 -11.270 27.257 -7.467 1.00 14.07 C ANISOU 1372 CB ASP A 169 1771 1737 1837 -144 -287 280 C ATOM 1373 CG ASP A 169 -10.874 27.060 -8.929 1.00 23.31 C ANISOU 1373 CG ASP A 169 2966 2934 2959 -157 -294 307 C ATOM 1374 OD1 ASP A 169 -11.735 27.281 -9.820 1.00 25.15 O ANISOU 1374 OD1 ASP A 169 3205 3166 3185 -159 -326 327 O ATOM 1375 OD2 ASP A 169 -9.708 26.663 -9.183 1.00 23.68 O1- ANISOU 1375 OD2 ASP A 169 3024 3002 2970 -163 -267 308 O1- ATOM 1376 N GLN A 170 -12.921 28.399 -4.964 1.00 11.62 N ANISOU 1376 N GLN A 170 1413 1369 1633 -106 -295 244 N ATOM 1377 CA GLN A 170 -13.435 28.295 -3.595 1.00 13.25 C ANISOU 1377 CA GLN A 170 1600 1564 1868 -86 -281 214 C ATOM 1378 C GLN A 170 -14.945 28.187 -3.572 1.00 12.95 C ANISOU 1378 C GLN A 170 1541 1525 1856 -71 -297 215 C ATOM 1379 O GLN A 170 -15.495 27.340 -2.841 1.00 13.39 O ANISOU 1379 O GLN A 170 1580 1593 1915 -63 -282 194 O ATOM 1380 CB GLN A 170 -13.017 29.487 -2.748 1.00 14.24 C ANISOU 1380 CB GLN A 170 1726 1658 2025 -75 -278 208 C ATOM 1381 CG GLN A 170 -11.490 29.573 -2.504 1.00 12.87 C ANISOU 1381 CG GLN A 170 1568 1486 1835 -91 -262 205 C ATOM 1382 CD GLN A 170 -11.170 30.939 -1.884 1.00 14.60 C ANISOU 1382 CD GLN A 170 1792 1666 2090 -85 -273 205 C ATOM 1383 NE2 GLN A 170 -10.218 31.638 -2.459 1.00 16.53 N ANISOU 1383 NE2 GLN A 170 2048 1901 2333 -106 -282 231 N ATOM 1384 OE1 GLN A 170 -11.784 31.326 -0.882 1.00 17.61 O ANISOU 1384 OE1 GLN A 170 2166 2027 2498 -60 -272 181 O ATOM 1385 N ASP A 171 -15.620 29.019 -4.380 1.00 13.17 N ANISOU 1385 N ASP A 171 1564 1538 1900 -68 -328 243 N ATOM 1386 CA ASP A 171 -17.079 28.965 -4.417 1.00 12.96 C ANISOU 1386 CA ASP A 171 1510 1512 1901 -53 -347 249 C ATOM 1387 C ASP A 171 -17.567 27.624 -4.974 1.00 12.90 C ANISOU 1387 C ASP A 171 1500 1534 1868 -70 -354 249 C ATOM 1388 O ASP A 171 -18.543 27.045 -4.467 1.00 13.45 O ANISOU 1388 O ASP A 171 1541 1612 1956 -62 -353 240 O ATOM 1389 CB ASP A 171 -17.577 30.091 -5.321 1.00 13.54 C ANISOU 1389 CB ASP A 171 1583 1565 1995 -48 -383 284 C ATOM 1390 CG ASP A 171 -17.369 31.465 -4.719 1.00 17.18 C ANISOU 1390 CG ASP A 171 2045 1988 2492 -28 -383 283 C ATOM 1391 OD1 ASP A 171 -17.093 31.598 -3.497 1.00 23.09 O ANISOU 1391 OD1 ASP A 171 2792 2727 3256 -11 -357 253 O ATOM 1392 OD2 ASP A 171 -17.527 32.460 -5.499 1.00 21.96 O1- ANISOU 1392 OD2 ASP A 171 2658 2573 3114 -27 -413 315 O1- ATOM 1393 N GLU A 172 -16.894 27.108 -6.019 1.00 12.73 N ANISOU 1393 N GLU A 172 1506 1528 1802 -94 -363 258 N ATOM 1394 CA GLU A 172 -17.288 25.831 -6.584 1.00 13.19 C ANISOU 1394 CA GLU A 172 1571 1609 1833 -110 -374 254 C ATOM 1395 C GLU A 172 -17.119 24.717 -5.574 1.00 12.82 C ANISOU 1395 C GLU A 172 1517 1571 1782 -110 -344 223 C ATOM 1396 O GLU A 172 -18.052 23.914 -5.340 1.00 13.34 O ANISOU 1396 O GLU A 172 1563 1644 1860 -113 -352 218 O ATOM 1397 CB GLU A 172 -16.462 25.543 -7.829 1.00 16.45 C ANISOU 1397 CB GLU A 172 2021 2036 2193 -129 -383 265 C ATOM 1398 CG GLU A 172 -16.820 24.204 -8.480 1.00 20.12 C ANISOU 1398 CG GLU A 172 2501 2519 2624 -144 -399 256 C ATOM 1399 CD GLU A 172 -17.769 24.320 -9.718 1.00 31.45 C ANISOU 1399 CD GLU A 172 3941 3958 4052 -154 -449 282 C ATOM 1400 OE1 GLU A 172 -18.277 25.412 -10.104 1.00 22.94 O ANISOU 1400 OE1 GLU A 172 2850 2869 2996 -148 -473 311 O ATOM 1401 OE2 GLU A 172 -18.032 23.265 -10.337 1.00 37.79 O1- ANISOU 1401 OE2 GLU A 172 4762 4773 4823 -169 -469 273 O1- ATOM 1402 N LEU A 173 -15.937 24.667 -4.932 1.00 12.38 N ANISOU 1402 N LEU A 173 1476 1516 1713 -107 -310 205 N ATOM 1403 CA LEU A 173 -15.724 23.612 -3.947 1.00 13.31 C ANISOU 1403 CA LEU A 173 1589 1642 1825 -106 -283 178 C ATOM 1404 C LEU A 173 -16.664 23.740 -2.757 1.00 11.13 C ANISOU 1404 C LEU A 173 1278 1360 1589 -89 -272 169 C ATOM 1405 O LEU A 173 -17.150 22.714 -2.245 1.00 13.57 O ANISOU 1405 O LEU A 173 1575 1680 1902 -93 -264 159 O ATOM 1406 CB LEU A 173 -14.275 23.639 -3.442 1.00 14.72 C ANISOU 1406 CB LEU A 173 1786 1822 1984 -105 -252 163 C ATOM 1407 CG LEU A 173 -13.220 23.289 -4.459 1.00 19.63 C ANISOU 1407 CG LEU A 173 2439 2458 2562 -119 -250 169 C ATOM 1408 CD1 LEU A 173 -11.882 23.693 -3.806 1.00 23.63 C ANISOU 1408 CD1 LEU A 173 2951 2964 3065 -115 -222 162 C ATOM 1409 CD2 LEU A 173 -13.315 21.787 -4.680 1.00 24.93 C ANISOU 1409 CD2 LEU A 173 3123 3142 3205 -127 -249 153 C ATOM 1410 N SER A 174 -16.922 24.964 -2.271 1.00 10.81 N ANISOU 1410 N SER A 174 1222 1304 1581 -68 -271 174 N ATOM 1411 CA SER A 174 -17.847 25.160 -1.151 1.00 11.86 C ANISOU 1411 CA SER A 174 1322 1434 1750 -45 -257 165 C ATOM 1412 C SER A 174 -19.241 24.632 -1.477 1.00 12.71 C ANISOU 1412 C SER A 174 1399 1554 1878 -48 -277 181 C ATOM 1413 O SER A 174 -19.909 23.998 -0.637 1.00 12.73 O ANISOU 1413 O SER A 174 1373 1568 1894 -42 -260 175 O ATOM 1414 CB SER A 174 -17.900 26.658 -0.818 1.00 11.22 C ANISOU 1414 CB SER A 174 1237 1329 1698 -19 -259 167 C ATOM 1415 OG SER A 174 -18.808 26.926 0.187 1.00 15.12 O ANISOU 1415 OG SER A 174 1701 1821 2223 10 -244 159 O ATOM 1416 N SER A 175 -19.715 24.954 -2.698 1.00 12.75 N ANISOU 1416 N SER A 175 1404 1555 1884 -58 -315 206 N ATOM 1417 CA SER A 175 -21.051 24.538 -3.116 1.00 12.81 C ANISOU 1417 CA SER A 175 1380 1574 1915 -64 -343 225 C ATOM 1418 C SER A 175 -21.153 23.024 -3.263 1.00 13.26 C ANISOU 1418 C SER A 175 1442 1647 1951 -92 -347 219 C ATOM 1419 O SER A 175 -22.135 22.415 -2.841 1.00 13.45 O ANISOU 1419 O SER A 175 1431 1682 1999 -96 -349 226 O ATOM 1420 CB SER A 175 -21.359 25.212 -4.440 1.00 13.50 C ANISOU 1420 CB SER A 175 1475 1653 2002 -71 -386 253 C ATOM 1421 OG SER A 175 -21.353 26.605 -4.282 1.00 14.57 O ANISOU 1421 OG SER A 175 1605 1768 2162 -44 -386 261 O ATOM 1422 N LEU A 176 -20.114 22.411 -3.792 1.00 11.53 N ANISOU 1422 N LEU A 176 1265 1429 1687 -111 -346 207 N ATOM 1423 CA LEU A 176 -20.060 20.966 -3.911 1.00 12.12 C ANISOU 1423 CA LEU A 176 1354 1513 1740 -135 -350 196 C ATOM 1424 C LEU A 176 -20.106 20.271 -2.547 1.00 12.12 C ANISOU 1424 C LEU A 176 1334 1518 1753 -129 -314 181 C ATOM 1425 O LEU A 176 -20.804 19.263 -2.338 1.00 14.08 O ANISOU 1425 O LEU A 176 1565 1772 2013 -146 -322 184 O ATOM 1426 CB LEU A 176 -18.781 20.599 -4.631 1.00 17.57 C ANISOU 1426 CB LEU A 176 2094 2203 2380 -145 -347 183 C ATOM 1427 CG LEU A 176 -18.509 19.242 -5.160 1.00 22.48 C ANISOU 1427 CG LEU A 176 2747 2829 2967 -166 -358 170 C ATOM 1428 CD1 LEU A 176 -19.576 18.901 -6.274 1.00 17.10 C ANISOU 1428 CD1 LEU A 176 2064 2147 2285 -187 -411 187 C ATOM 1429 CD2 LEU A 176 -17.110 19.307 -5.821 1.00 24.71 C ANISOU 1429 CD2 LEU A 176 3073 3114 3200 -164 -345 159 C ATOM 1430 N LEU A 177 -19.335 20.804 -1.599 1.00 11.36 N ANISOU 1430 N LEU A 177 1241 1419 1656 -109 -276 165 N ATOM 1431 CA LEU A 177 -19.233 20.203 -0.276 1.00 12.37 C ANISOU 1431 CA LEU A 177 1357 1554 1790 -102 -241 151 C ATOM 1432 C LEU A 177 -20.364 20.606 0.647 1.00 13.10 C ANISOU 1432 C LEU A 177 1402 1654 1922 -82 -227 161 C ATOM 1433 O LEU A 177 -20.560 19.962 1.695 1.00 14.87 O ANISOU 1433 O LEU A 177 1609 1888 2151 -79 -200 156 O ATOM 1434 CB LEU A 177 -17.887 20.641 0.333 1.00 12.37 C ANISOU 1434 CB LEU A 177 1383 1549 1768 -88 -210 130 C ATOM 1435 CG LEU A 177 -16.660 20.105 -0.401 1.00 11.46 C ANISOU 1435 CG LEU A 177 1310 1433 1612 -103 -213 120 C ATOM 1436 CD1 LEU A 177 -15.390 20.849 0.097 1.00 13.43 C ANISOU 1436 CD1 LEU A 177 1576 1677 1850 -90 -190 107 C ATOM 1437 CD2 LEU A 177 -16.477 18.592 -0.143 1.00 17.62 C ANISOU 1437 CD2 LEU A 177 2101 2218 2375 -118 -206 110 C ATOM 1438 N GLY A 178 -21.088 21.689 0.343 1.00 12.95 N ANISOU 1438 N GLY A 178 1360 1630 1931 -65 -242 176 N ATOM 1439 CA GLY A 178 -22.076 22.198 1.287 1.00 14.10 C ANISOU 1439 CA GLY A 178 1460 1785 2114 -37 -222 182 C ATOM 1440 C GLY A 178 -21.507 22.760 2.566 1.00 14.61 C ANISOU 1440 C GLY A 178 1531 1847 2173 -6 -180 159 C ATOM 1441 O GLY A 178 -22.194 22.764 3.588 1.00 17.61 O ANISOU 1441 O GLY A 178 1878 2241 2571 16 -153 159 O ATOM 1442 N VAL A 179 -20.263 23.254 2.541 1.00 13.62 N ANISOU 1442 N VAL A 179 1446 1705 2023 -4 -175 139 N ATOM 1443 CA VAL A 179 -19.655 23.870 3.734 1.00 12.50 C ANISOU 1443 CA VAL A 179 1316 1558 1877 24 -143 115 C ATOM 1444 C VAL A 179 -18.928 25.132 3.319 1.00 11.86 C ANISOU 1444 C VAL A 179 1261 1450 1795 33 -157 108 C ATOM 1445 O VAL A 179 -18.389 25.213 2.213 1.00 13.40 O ANISOU 1445 O VAL A 179 1478 1636 1979 11 -183 119 O ATOM 1446 CB VAL A 179 -18.641 22.929 4.461 1.00 14.05 C ANISOU 1446 CB VAL A 179 1536 1763 2039 11 -119 96 C ATOM 1447 CG1 VAL A 179 -19.296 21.561 4.838 1.00 18.48 C ANISOU 1447 CG1 VAL A 179 2074 2347 2599 -5 -107 106 C ATOM 1448 CG2 VAL A 179 -17.367 22.694 3.674 1.00 15.07 C ANISOU 1448 CG2 VAL A 179 1704 1883 2139 -14 -133 91 C ATOM 1449 N PRO A 180 -18.817 26.105 4.227 1.00 12.83 N ANISOU 1449 N PRO A 180 1387 1559 1929 65 -141 90 N ATOM 1450 CA PRO A 180 -18.011 27.298 3.943 1.00 13.52 C ANISOU 1450 CA PRO A 180 1503 1615 2018 70 -157 83 C ATOM 1451 C PRO A 180 -16.532 26.918 3.780 1.00 12.70 C ANISOU 1451 C PRO A 180 1434 1510 1882 42 -156 75 C ATOM 1452 O PRO A 180 -16.028 26.029 4.473 1.00 11.60 O ANISOU 1452 O PRO A 180 1302 1388 1720 35 -134 60 O ATOM 1453 CB PRO A 180 -18.219 28.193 5.174 1.00 18.00 C ANISOU 1453 CB PRO A 180 2070 2168 2600 112 -137 58 C ATOM 1454 CG PRO A 180 -19.480 27.681 5.775 1.00 26.24 C ANISOU 1454 CG PRO A 180 3075 3239 3657 134 -115 62 C ATOM 1455 CD PRO A 180 -19.525 26.181 5.509 1.00 16.58 C ANISOU 1455 CD PRO A 180 1840 2046 2415 99 -110 76 C ATOM 1456 N LEU A 181 -15.848 27.611 2.876 1.00 12.72 N ANISOU 1456 N LEU A 181 1457 1492 1883 27 -180 87 N ATOM 1457 CA LEU A 181 -14.423 27.395 2.628 1.00 13.15 C ANISOU 1457 CA LEU A 181 1538 1547 1910 2 -179 84 C ATOM 1458 C LEU A 181 -13.729 28.731 2.578 1.00 15.85 C ANISOU 1458 C LEU A 181 1899 1857 2266 5 -195 85 C ATOM 1459 O LEU A 181 -14.326 29.751 2.200 1.00 18.23 O ANISOU 1459 O LEU A 181 2198 2135 2596 18 -215 97 O ATOM 1460 CB LEU A 181 -14.107 26.734 1.292 1.00 19.98 C ANISOU 1460 CB LEU A 181 2411 2427 2753 -27 -193 107 C ATOM 1461 CG LEU A 181 -14.553 25.352 0.995 1.00 22.95 C ANISOU 1461 CG LEU A 181 2780 2829 3112 -39 -189 109 C ATOM 1462 CD1 LEU A 181 -13.951 24.993 -0.381 1.00 23.04 C ANISOU 1462 CD1 LEU A 181 2810 2848 3095 -64 -205 127 C ATOM 1463 CD2 LEU A 181 -14.059 24.379 1.998 1.00 21.06 C ANISOU 1463 CD2 LEU A 181 2542 2604 2854 -39 -161 87 C ATOM 1464 N AVAL A 182 -12.470 28.730 2.953 0.56 11.91 N ANISOU 1464 N AVAL A 182 1419 1356 1751 -9 -188 75 N ATOM 1465 N BVAL A 182 -12.459 28.755 3.031 0.44 11.26 N ANISOU 1465 N BVAL A 182 1336 1272 1669 -8 -187 73 N ATOM 1466 CA AVAL A 182 -11.654 29.889 2.677 0.56 13.47 C ANISOU 1466 CA AVAL A 182 1634 1524 1961 -19 -208 84 C ATOM 1467 CA BVAL A 182 -11.577 29.936 3.045 0.44 11.39 C ANISOU 1467 CA BVAL A 182 1371 1257 1698 -14 -204 75 C ATOM 1468 C AVAL A 182 -10.283 29.392 2.281 0.56 9.96 C ANISOU 1468 C AVAL A 182 1199 1095 1490 -49 -203 94 C ATOM 1469 C BVAL A 182 -10.201 29.485 2.533 0.44 11.93 C ANISOU 1469 C BVAL A 182 1450 1341 1741 -47 -202 88 C ATOM 1470 O AVAL A 182 -9.918 28.229 2.499 0.56 10.88 O ANISOU 1470 O AVAL A 182 1313 1241 1579 -55 -182 85 O ATOM 1471 O BVAL A 182 -9.731 28.405 2.915 0.44 11.47 O ANISOU 1471 O BVAL A 182 1390 1310 1657 -52 -181 76 O ATOM 1472 CB AVAL A 182 -11.585 30.857 3.859 0.56 16.55 C ANISOU 1472 CB AVAL A 182 2035 1882 2371 4 -210 57 C ATOM 1473 CB BVAL A 182 -11.435 30.537 4.476 0.44 11.75 C ANISOU 1473 CB BVAL A 182 1428 1282 1755 9 -198 41 C ATOM 1474 CG1AVAL A 182 -12.975 31.481 4.107 0.56 19.16 C ANISOU 1474 CG1AVAL A 182 2354 2196 2731 40 -214 50 C ATOM 1475 CG1BVAL A 182 -10.469 31.707 4.493 0.44 15.94 C ANISOU 1475 CG1BVAL A 182 1980 1776 2301 -4 -222 44 C ATOM 1476 CG2AVAL A 182 -10.995 30.161 5.068 0.56 10.85 C ANISOU 1476 CG2AVAL A 182 1318 1177 1627 8 -187 27 C ATOM 1477 CG2BVAL A 182 -12.741 31.001 5.022 0.44 15.08 C ANISOU 1477 CG2BVAL A 182 1839 1691 2198 47 -195 27 C ATOM 1478 N ALA A 183 -9.534 30.300 1.682 1.00 12.72 N ANISOU 1478 N ALA A 183 1559 1425 1849 -67 -221 115 N ATOM 1479 CA ALA A 183 -8.138 30.055 1.315 1.00 12.59 C ANISOU 1479 CA ALA A 183 1547 1423 1812 -95 -216 130 C ATOM 1480 C ALA A 183 -7.270 30.690 2.384 1.00 11.73 C ANISOU 1480 C ALA A 183 1447 1293 1717 -97 -221 112 C ATOM 1481 O ALA A 183 -7.556 31.820 2.797 1.00 16.27 O ANISOU 1481 O ALA A 183 2031 1828 2322 -88 -242 105 O ATOM 1482 CB ALA A 183 -7.833 30.686 -0.051 1.00 13.42 C ANISOU 1482 CB ALA A 183 1656 1524 1919 -116 -234 172 C ATOM 1483 N GLY A 184 -6.235 29.972 2.847 1.00 11.76 N ANISOU 1483 N GLY A 184 1448 1318 1700 -109 -206 103 N ATOM 1484 CA GLY A 184 -5.416 30.511 3.917 1.00 11.29 C ANISOU 1484 CA GLY A 184 1397 1240 1653 -113 -215 85 C ATOM 1485 C GLY A 184 -4.213 29.623 4.090 1.00 12.82 C ANISOU 1485 C GLY A 184 1583 1466 1823 -129 -199 88 C ATOM 1486 O GLY A 184 -3.964 28.732 3.271 1.00 17.86 O ANISOU 1486 O GLY A 184 2212 2138 2438 -136 -181 105 O ATOM 1487 N SER A 185 -3.411 29.909 5.131 1.00 12.87 N ANISOU 1487 N SER A 185 1594 1462 1836 -134 -208 71 N ATOM 1488 CA SER A 185 -2.154 29.190 5.306 1.00 11.75 C ANISOU 1488 CA SER A 185 1440 1348 1676 -150 -197 77 C ATOM 1489 C SER A 185 -2.060 28.659 6.723 1.00 9.73 C ANISOU 1489 C SER A 185 1191 1097 1409 -133 -192 41 C ATOM 1490 O SER A 185 -2.858 28.999 7.602 1.00 12.42 O ANISOU 1490 O SER A 185 1547 1417 1753 -112 -197 11 O ATOM 1491 CB SER A 185 -0.937 30.107 5.028 1.00 14.22 C ANISOU 1491 CB SER A 185 1746 1647 2010 -182 -221 105 C ATOM 1492 OG SER A 185 -1.049 31.345 5.783 1.00 15.85 O ANISOU 1492 OG SER A 185 1970 1805 2247 -185 -254 89 O ATOM 1493 N VAL A 186 -1.077 27.776 6.932 1.00 8.93 N ANISOU 1493 N VAL A 186 1078 1026 1290 -141 -179 45 N ATOM 1494 CA VAL A 186 -0.750 27.291 8.269 1.00 10.85 C ANISOU 1494 CA VAL A 186 1327 1276 1520 -130 -178 17 C ATOM 1495 C VAL A 186 0.765 27.395 8.426 1.00 11.22 C ANISOU 1495 C VAL A 186 1359 1331 1572 -155 -192 33 C ATOM 1496 O VAL A 186 1.497 27.630 7.473 1.00 10.78 O ANISOU 1496 O VAL A 186 1286 1284 1527 -177 -194 67 O ATOM 1497 CB VAL A 186 -1.242 25.837 8.513 1.00 11.47 C ANISOU 1497 CB VAL A 186 1403 1385 1569 -109 -147 6 C ATOM 1498 CG1 VAL A 186 -2.756 25.771 8.412 1.00 13.28 C ANISOU 1498 CG1 VAL A 186 1641 1607 1797 -88 -136 -7 C ATOM 1499 CG2 VAL A 186 -0.560 24.840 7.532 1.00 11.85 C ANISOU 1499 CG2 VAL A 186 1434 1466 1604 -118 -127 31 C ATOM 1500 N ASN A 187 1.275 27.210 9.648 1.00 9.09 N ANISOU 1500 N ASN A 187 1095 1062 1294 -152 -203 12 N ATOM 1501 CA ASN A 187 2.713 27.157 9.851 1.00 10.66 C ANISOU 1501 CA ASN A 187 1276 1274 1499 -174 -217 29 C ATOM 1502 C ASN A 187 3.455 28.374 9.242 1.00 13.94 C ANISOU 1502 C ASN A 187 1680 1668 1949 -209 -246 58 C ATOM 1503 O ASN A 187 4.548 28.248 8.705 1.00 14.36 O ANISOU 1503 O ASN A 187 1703 1743 2009 -231 -245 91 O ATOM 1504 CB ASN A 187 3.291 25.843 9.318 1.00 10.63 C ANISOU 1504 CB ASN A 187 1248 1315 1476 -169 -186 49 C ATOM 1505 CG ASN A 187 3.046 24.749 10.252 1.00 14.97 C ANISOU 1505 CG ASN A 187 1806 1880 2000 -145 -171 24 C ATOM 1506 ND2 ASN A 187 2.782 23.587 9.741 1.00 12.65 N ANISOU 1506 ND2 ASN A 187 1507 1612 1687 -129 -140 29 N ATOM 1507 OD1 ASN A 187 3.149 24.947 11.484 1.00 13.92 O ANISOU 1507 OD1 ASN A 187 1689 1738 1863 -141 -190 1 O ATOM 1508 N ARG A 188 2.885 29.564 9.415 1.00 12.71 N ANISOU 1508 N ARG A 188 1547 1468 1813 -213 -273 45 N ATOM 1509 CA ARG A 188 3.545 30.834 9.050 1.00 13.73 C ANISOU 1509 CA ARG A 188 1671 1565 1979 -248 -310 70 C ATOM 1510 C ARG A 188 3.795 30.862 7.542 1.00 14.34 C ANISOU 1510 C ARG A 188 1723 1662 2065 -267 -292 119 C ATOM 1511 O ARG A 188 4.914 31.084 7.030 1.00 17.99 O ANISOU 1511 O ARG A 188 2156 2137 2544 -298 -299 159 O ATOM 1512 CB ARG A 188 4.824 31.064 9.851 1.00 17.60 C ANISOU 1512 CB ARG A 188 2151 2053 2482 -274 -342 73 C ATOM 1513 CG ARG A 188 5.204 32.548 9.909 1.00 19.61 C ANISOU 1513 CG ARG A 188 2418 2258 2777 -307 -392 82 C ATOM 1514 CD ARG A 188 6.486 32.743 10.704 1.00 29.86 C ANISOU 1514 CD ARG A 188 3706 3560 4078 -324 -417 85 C ATOM 1515 NE ARG A 188 6.243 32.530 12.119 1.00 42.81 N ANISOU 1515 NE ARG A 188 5377 5189 5699 -305 -435 35 N ATOM 1516 CZ ARG A 188 6.937 31.663 12.847 1.00 55.94 C ANISOU 1516 CZ ARG A 188 7027 6885 7344 -304 -435 28 C ATOM 1517 NH1 ARG A 188 6.679 31.495 14.141 1.00 60.88 N1+ ANISOU 1517 NH1 ARG A 188 7685 7502 7946 -285 -452 -17 N1+ ATOM 1518 NH2 ARG A 188 7.918 30.981 12.270 1.00 57.33 N ANISOU 1518 NH2 ARG A 188 7158 7104 7522 -319 -417 69 N ATOM 1519 N GLY A 189 2.701 30.663 6.834 1.00 11.90 N ANISOU 1519 N GLY A 189 1423 1354 1744 -246 -269 118 N ATOM 1520 CA GLY A 189 2.673 30.883 5.388 1.00 14.15 C ANISOU 1520 CA GLY A 189 1693 1648 2034 -260 -257 160 C ATOM 1521 C GLY A 189 2.845 29.631 4.547 1.00 15.76 C ANISOU 1521 C GLY A 189 1877 1904 2205 -249 -216 177 C ATOM 1522 O GLY A 189 2.986 29.736 3.324 1.00 17.18 O ANISOU 1522 O GLY A 189 2046 2100 2382 -260 -203 214 O ATOM 1523 N SER A 190 2.783 28.435 5.133 1.00 11.55 N ANISOU 1523 N SER A 190 1344 1398 1646 -225 -193 151 N ATOM 1524 CA SER A 190 2.826 27.234 4.331 1.00 11.03 C ANISOU 1524 CA SER A 190 1268 1374 1549 -211 -156 161 C ATOM 1525 C SER A 190 1.514 27.007 3.597 1.00 11.84 C ANISOU 1525 C SER A 190 1388 1472 1637 -193 -144 155 C ATOM 1526 O SER A 190 0.418 27.189 4.164 1.00 12.00 O ANISOU 1526 O SER A 190 1428 1469 1664 -178 -153 126 O ATOM 1527 CB SER A 190 3.081 26.032 5.278 1.00 12.23 C ANISOU 1527 CB SER A 190 1418 1547 1681 -190 -141 134 C ATOM 1528 OG SER A 190 3.128 24.787 4.549 1.00 11.87 O ANISOU 1528 OG SER A 190 1367 1538 1607 -173 -107 140 O ATOM 1529 N AASN A 191 1.612 26.583 2.340 0.56 11.34 N ANISOU 1529 N AASN A 191 1318 1436 1555 -194 -124 180 N ATOM 1530 N BASN A 191 1.633 26.594 2.324 0.44 11.26 N ANISOU 1530 N BASN A 191 1307 1426 1545 -194 -124 181 N ATOM 1531 CA AASN A 191 0.401 26.256 1.615 0.56 11.55 C ANISOU 1531 CA AASN A 191 1362 1462 1566 -179 -116 174 C ATOM 1532 CA BASN A 191 0.486 26.223 1.507 0.44 11.88 C ANISOU 1532 CA BASN A 191 1402 1507 1606 -180 -114 177 C ATOM 1533 C AASN A 191 0.037 24.773 1.692 0.56 10.35 C ANISOU 1533 C AASN A 191 1216 1333 1383 -155 -92 151 C ATOM 1534 C BASN A 191 0.020 24.788 1.725 0.44 10.37 C ANISOU 1534 C BASN A 191 1219 1335 1387 -155 -92 150 C ATOM 1535 O AASN A 191 -0.984 24.379 1.116 0.56 11.02 O ANISOU 1535 O AASN A 191 1314 1417 1454 -144 -88 144 O ATOM 1536 O BASN A 191 -1.065 24.438 1.233 0.44 9.40 O ANISOU 1536 O BASN A 191 1110 1208 1252 -144 -90 142 O ATOM 1537 CB AASN A 191 0.524 26.724 0.149 0.56 9.97 C ANISOU 1537 CB AASN A 191 1158 1272 1358 -193 -113 214 C ATOM 1538 CB BASN A 191 0.792 26.374 0.002 0.44 13.49 C ANISOU 1538 CB BASN A 191 1600 1732 1794 -191 -104 217 C ATOM 1539 CG AASN A 191 1.671 26.056 -0.599 0.56 13.81 C ANISOU 1539 CG AASN A 191 1626 1801 1818 -195 -86 239 C ATOM 1540 CG BASN A 191 1.189 27.764 -0.401 0.44 16.03 C ANISOU 1540 CG BASN A 191 1914 2035 2143 -219 -125 252 C ATOM 1541 ND2AASN A 191 2.296 26.801 -1.491 0.56 15.54 N ANISOU 1541 ND2AASN A 191 1833 2030 2040 -216 -86 282 N ATOM 1542 ND2BASN A 191 1.945 27.853 -1.462 0.44 15.37 N ANISOU 1542 ND2BASN A 191 1816 1978 2045 -232 -111 293 N ATOM 1543 OD1AASN A 191 1.990 24.884 -0.382 0.56 15.23 O ANISOU 1543 OD1AASN A 191 1805 2007 1976 -177 -63 222 O ATOM 1544 OD1BASN A 191 0.825 28.726 0.226 0.44 18.35 O ANISOU 1544 OD1BASN A 191 2215 2290 2469 -227 -153 245 O ATOM 1545 N VAL A 192 0.793 23.967 2.439 1.00 10.04 N ANISOU 1545 N VAL A 192 1169 1311 1336 -147 -79 138 N ATOM 1546 CA VAL A 192 0.544 22.532 2.532 1.00 9.61 C ANISOU 1546 CA VAL A 192 1122 1274 1255 -125 -59 118 C ATOM 1547 C VAL A 192 -0.430 22.313 3.709 1.00 9.95 C ANISOU 1547 C VAL A 192 1177 1296 1306 -113 -67 86 C ATOM 1548 O VAL A 192 -0.055 21.886 4.813 1.00 12.35 O ANISOU 1548 O VAL A 192 1479 1603 1610 -106 -65 70 O ATOM 1549 CB VAL A 192 1.871 21.785 2.727 1.00 12.19 C ANISOU 1549 CB VAL A 192 1432 1629 1571 -120 -41 125 C ATOM 1550 CG1 VAL A 192 1.610 20.261 2.647 1.00 16.35 C ANISOU 1550 CG1 VAL A 192 1972 2169 2070 -95 -21 106 C ATOM 1551 CG2 VAL A 192 2.917 22.200 1.647 1.00 15.60 C ANISOU 1551 CG2 VAL A 192 1844 2084 1998 -132 -31 162 C ATOM 1552 N ILE A 193 -1.660 22.710 3.492 1.00 8.75 N ANISOU 1552 N ILE A 193 1037 1127 1162 -111 -76 81 N ATOM 1553 CA ILE A 193 -2.645 22.782 4.592 1.00 9.60 C ANISOU 1553 CA ILE A 193 1152 1217 1280 -100 -83 55 C ATOM 1554 C ILE A 193 -2.876 21.411 5.193 1.00 8.41 C ANISOU 1554 C ILE A 193 1005 1079 1111 -85 -66 38 C ATOM 1555 O ILE A 193 -2.911 21.223 6.435 1.00 9.85 O ANISOU 1555 O ILE A 193 1190 1259 1295 -77 -64 20 O ATOM 1556 CB ILE A 193 -3.994 23.322 4.048 1.00 9.88 C ANISOU 1556 CB ILE A 193 1192 1235 1327 -97 -93 57 C ATOM 1557 CG1 ILE A 193 -3.848 24.649 3.236 1.00 10.96 C ANISOU 1557 CG1 ILE A 193 1328 1355 1481 -112 -111 80 C ATOM 1558 CG2 ILE A 193 -5.033 23.456 5.178 1.00 10.87 C ANISOU 1558 CG2 ILE A 193 1321 1346 1464 -81 -94 33 C ATOM 1559 CD1 ILE A 193 -3.065 25.722 4.028 1.00 13.74 C ANISOU 1559 CD1 ILE A 193 1678 1688 1855 -121 -127 78 C ATOM 1560 N GLY A 194 -3.141 20.413 4.339 1.00 9.08 N ANISOU 1560 N GLY A 194 1095 1176 1178 -82 -55 43 N ATOM 1561 CA GLY A 194 -3.417 19.063 4.865 1.00 10.18 C ANISOU 1561 CA GLY A 194 1241 1323 1304 -70 -43 29 C ATOM 1562 C GLY A 194 -2.210 18.456 5.556 1.00 10.79 C ANISOU 1562 C GLY A 194 1314 1413 1372 -64 -33 25 C ATOM 1563 O GLY A 194 -2.350 17.605 6.469 1.00 13.52 O ANISOU 1563 O GLY A 194 1664 1761 1712 -55 -27 14 O ATOM 1564 N GLY A 195 -1.005 18.821 5.147 1.00 10.31 N ANISOU 1564 N GLY A 195 1244 1365 1310 -69 -32 39 N ATOM 1565 CA GLY A 195 0.173 18.382 5.879 1.00 9.39 C ANISOU 1565 CA GLY A 195 1117 1260 1189 -64 -26 39 C ATOM 1566 C GLY A 195 0.341 19.031 7.235 1.00 9.31 C ANISOU 1566 C GLY A 195 1104 1241 1193 -68 -40 29 C ATOM 1567 O GLY A 195 0.984 18.446 8.118 1.00 9.41 O ANISOU 1567 O GLY A 195 1113 1262 1200 -60 -39 24 O ATOM 1568 N GLY A 196 -0.130 20.271 7.379 1.00 8.34 N ANISOU 1568 N GLY A 196 982 1100 1087 -78 -56 27 N ATOM 1569 CA GLY A 196 0.215 21.058 8.548 1.00 8.94 C ANISOU 1569 CA GLY A 196 1059 1165 1174 -83 -74 16 C ATOM 1570 C GLY A 196 -0.806 21.041 9.661 1.00 9.33 C ANISOU 1570 C GLY A 196 1123 1203 1219 -69 -75 -8 C ATOM 1571 O GLY A 196 -0.523 21.616 10.709 1.00 11.58 O ANISOU 1571 O GLY A 196 1414 1479 1506 -69 -90 -22 O ATOM 1572 N MET A 197 -1.984 20.454 9.443 1.00 8.49 N ANISOU 1572 N MET A 197 1023 1096 1107 -59 -61 -13 N ATOM 1573 CA MET A 197 -2.988 20.463 10.495 1.00 8.88 C ANISOU 1573 CA MET A 197 1082 1140 1153 -45 -57 -31 C ATOM 1574 C MET A 197 -3.944 19.279 10.322 1.00 9.21 C ANISOU 1574 C MET A 197 1124 1191 1185 -37 -38 -29 C ATOM 1575 O MET A 197 -4.032 18.661 9.256 1.00 10.97 O ANISOU 1575 O MET A 197 1344 1418 1407 -43 -34 -17 O ATOM 1576 CB MET A 197 -3.804 21.783 10.521 1.00 9.19 C ANISOU 1576 CB MET A 197 1125 1157 1209 -42 -68 -40 C ATOM 1577 CG MET A 197 -4.654 21.966 9.273 1.00 10.00 C ANISOU 1577 CG MET A 197 1222 1254 1325 -46 -67 -27 C ATOM 1578 SD MET A 197 -5.822 23.382 9.346 1.00 11.27 S ANISOU 1578 SD MET A 197 1385 1387 1509 -35 -79 -36 S ATOM 1579 CE MET A 197 -7.014 22.693 10.481 1.00 14.51 C ANISOU 1579 CE MET A 197 1795 1810 1908 -10 -56 -52 C ATOM 1580 N VAL A 198 -4.679 18.983 11.414 1.00 8.13 N ANISOU 1580 N VAL A 198 992 1058 1041 -24 -28 -39 N ATOM 1581 CA VAL A 198 -5.826 18.066 11.391 1.00 8.10 C ANISOU 1581 CA VAL A 198 983 1059 1034 -20 -13 -34 C ATOM 1582 C VAL A 198 -7.023 18.747 12.064 1.00 7.61 C ANISOU 1582 C VAL A 198 918 994 979 -6 -6 -43 C ATOM 1583 O VAL A 198 -6.849 19.631 12.907 1.00 8.16 O ANISOU 1583 O VAL A 198 996 1060 1045 5 -10 -59 O ATOM 1584 CB VAL A 198 -5.517 16.714 12.092 1.00 6.08 C ANISOU 1584 CB VAL A 198 733 817 761 -17 -2 -30 C ATOM 1585 CG1 VAL A 198 -4.349 15.959 11.316 1.00 9.06 C ANISOU 1585 CG1 VAL A 198 1113 1197 1133 -24 -6 -21 C ATOM 1586 CG2 VAL A 198 -5.188 16.879 13.584 1.00 8.90 C ANISOU 1586 CG2 VAL A 198 1098 1182 1101 -5 1 -41 C ATOM 1587 N VAL A 199 -8.224 18.234 11.756 1.00 8.15 N ANISOU 1587 N VAL A 199 974 1066 1055 -6 4 -33 N ATOM 1588 CA VAL A 199 -9.442 18.924 12.206 1.00 8.51 C ANISOU 1588 CA VAL A 199 1010 1113 1112 10 12 -37 C ATOM 1589 C VAL A 199 -10.594 17.926 12.254 1.00 10.01 C ANISOU 1589 C VAL A 199 1182 1314 1305 7 28 -20 C ATOM 1590 O VAL A 199 -10.707 17.034 11.397 1.00 11.43 O ANISOU 1590 O VAL A 199 1359 1493 1491 -11 21 -6 O ATOM 1591 CB VAL A 199 -9.725 20.170 11.316 1.00 8.75 C ANISOU 1591 CB VAL A 199 1036 1124 1164 10 -4 -39 C ATOM 1592 CG1 VAL A 199 -10.038 19.833 9.855 1.00 11.04 C ANISOU 1592 CG1 VAL A 199 1317 1410 1468 -8 -16 -21 C ATOM 1593 CG2 VAL A 199 -10.888 21.019 11.945 1.00 10.63 C ANISOU 1593 CG2 VAL A 199 1264 1361 1414 35 6 -48 C ATOM 1594 N ASN A 200 -11.497 18.137 13.213 1.00 8.58 N ANISOU 1594 N ASN A 200 991 1147 1124 26 47 -22 N ATOM 1595 CA ASN A 200 -12.820 17.503 13.165 1.00 8.64 C ANISOU 1595 CA ASN A 200 972 1166 1144 23 61 -1 C ATOM 1596 C ASN A 200 -13.867 18.559 13.533 1.00 10.28 C ANISOU 1596 C ASN A 200 1162 1379 1365 49 73 -7 C ATOM 1597 O ASN A 200 -13.583 19.766 13.456 1.00 11.56 O ANISOU 1597 O ASN A 200 1334 1526 1532 64 63 -26 O ATOM 1598 CB ASN A 200 -12.877 16.224 14.057 1.00 8.84 C ANISOU 1598 CB ASN A 200 997 1209 1152 17 79 13 C ATOM 1599 CG ASN A 200 -12.793 16.529 15.524 1.00 10.01 C ANISOU 1599 CG ASN A 200 1153 1376 1275 42 102 2 C ATOM 1600 ND2 ASN A 200 -12.609 15.500 16.318 1.00 11.42 N ANISOU 1600 ND2 ASN A 200 1336 1569 1433 37 116 15 N ATOM 1601 OD1 ASN A 200 -12.896 17.681 15.954 1.00 10.14 O ANISOU 1601 OD1 ASN A 200 1173 1391 1287 66 107 -19 O ATOM 1602 N ASP A 201 -15.096 18.138 13.871 1.00 9.88 N ANISOU 1602 N ASP A 201 1081 1347 1324 54 93 13 N ATOM 1603 CA ASP A 201 -16.115 19.194 14.005 1.00 9.99 C ANISOU 1603 CA ASP A 201 1074 1365 1357 82 104 9 C ATOM 1604 C ASP A 201 -15.934 20.056 15.246 1.00 11.80 C ANISOU 1604 C ASP A 201 1319 1602 1563 119 124 -18 C ATOM 1605 O ASP A 201 -16.661 21.056 15.389 1.00 15.21 O ANISOU 1605 O ASP A 201 1740 2032 2009 150 133 -28 O ATOM 1606 CB ASP A 201 -17.529 18.556 13.971 1.00 13.25 C ANISOU 1606 CB ASP A 201 1443 1800 1791 78 120 41 C ATOM 1607 CG ASP A 201 -17.918 18.018 12.595 1.00 13.74 C ANISOU 1607 CG ASP A 201 1489 1850 1883 45 90 63 C ATOM 1608 OD1 ASP A 201 -17.187 18.194 11.571 1.00 17.26 O ANISOU 1608 OD1 ASP A 201 1957 2272 2330 28 60 54 O ATOM 1609 OD2 ASP A 201 -18.988 17.366 12.490 1.00 17.92 O1- ANISOU 1609 OD2 ASP A 201 1982 2394 2432 33 95 92 O1- ATOM 1610 N TRP A 202 -15.047 19.710 16.192 1.00 10.48 N ANISOU 1610 N TRP A 202 1180 1442 1361 121 133 -31 N ATOM 1611 CA TRP A 202 -14.870 20.539 17.385 1.00 11.67 C ANISOU 1611 CA TRP A 202 1351 1598 1484 157 148 -60 C ATOM 1612 C TRP A 202 -13.426 20.874 17.773 1.00 12.60 C ANISOU 1612 C TRP A 202 1511 1699 1577 153 127 -87 C ATOM 1613 O TRP A 202 -13.219 21.620 18.748 1.00 14.12 O ANISOU 1613 O TRP A 202 1728 1892 1746 182 133 -116 O ATOM 1614 CB TRP A 202 -15.590 19.899 18.594 1.00 13.04 C ANISOU 1614 CB TRP A 202 1512 1810 1632 176 189 -47 C ATOM 1615 CG TRP A 202 -14.967 18.681 19.143 1.00 14.08 C ANISOU 1615 CG TRP A 202 1655 1957 1737 154 194 -32 C ATOM 1616 CD1 TRP A 202 -14.082 18.627 20.163 1.00 15.56 C ANISOU 1616 CD1 TRP A 202 1876 2151 1884 163 196 -50 C ATOM 1617 CD2 TRP A 202 -15.185 17.322 18.712 1.00 12.55 C ANISOU 1617 CD2 TRP A 202 1441 1771 1555 120 195 5 C ATOM 1618 CE2 TRP A 202 -14.398 16.503 19.551 1.00 15.75 C ANISOU 1618 CE2 TRP A 202 1869 2187 1927 113 200 8 C ATOM 1619 CE3 TRP A 202 -16.005 16.709 17.746 1.00 14.36 C ANISOU 1619 CE3 TRP A 202 1636 1998 1821 96 189 35 C ATOM 1620 NE1 TRP A 202 -13.717 17.318 20.414 1.00 16.45 N ANISOU 1620 NE1 TRP A 202 1990 2277 1983 139 200 -24 N ATOM 1621 CZ2 TRP A 202 -14.384 15.135 19.443 1.00 17.03 C ANISOU 1621 CZ2 TRP A 202 2023 2354 2092 84 200 40 C ATOM 1622 CZ3 TRP A 202 -15.975 15.322 17.636 1.00 13.82 C ANISOU 1622 CZ3 TRP A 202 1562 1934 1755 64 187 65 C ATOM 1623 CH2 TRP A 202 -15.181 14.563 18.487 1.00 15.44 C ANISOU 1623 CH2 TRP A 202 1792 2147 1928 60 194 67 C ATOM 1624 N LEU A 203 -12.428 20.349 17.068 1.00 12.59 N ANISOU 1624 N LEU A 203 1520 1685 1580 121 102 -80 N ATOM 1625 CA LEU A 203 -11.045 20.511 17.474 1.00 9.98 C ANISOU 1625 CA LEU A 203 1221 1344 1228 114 83 -99 C ATOM 1626 C LEU A 203 -10.200 20.667 16.221 1.00 10.25 C ANISOU 1626 C LEU A 203 1257 1354 1285 87 52 -94 C ATOM 1627 O LEU A 203 -10.368 19.902 15.283 1.00 10.38 O ANISOU 1627 O LEU A 203 1257 1371 1316 66 50 -71 O ATOM 1628 CB LEU A 203 -10.532 19.246 18.231 1.00 9.74 C ANISOU 1628 CB LEU A 203 1197 1336 1168 104 94 -86 C ATOM 1629 CG LEU A 203 -9.022 19.182 18.508 1.00 12.74 C ANISOU 1629 CG LEU A 203 1603 1708 1530 93 70 -97 C ATOM 1630 CD1 LEU A 203 -8.602 20.327 19.428 1.00 14.10 C ANISOU 1630 CD1 LEU A 203 1803 1872 1682 114 59 -131 C ATOM 1631 CD2 LEU A 203 -8.597 17.837 19.150 1.00 13.77 C ANISOU 1631 CD2 LEU A 203 1737 1859 1636 84 79 -79 C ATOM 1632 N ALA A 204 -9.257 21.607 16.231 1.00 9.08 N ANISOU 1632 N ALA A 204 1129 1184 1136 86 27 -114 N ATOM 1633 CA ALA A 204 -8.228 21.682 15.201 1.00 9.51 C ANISOU 1633 CA ALA A 204 1186 1223 1206 59 2 -106 C ATOM 1634 C ALA A 204 -6.869 21.683 15.894 1.00 7.85 C ANISOU 1634 C ALA A 204 995 1013 976 52 -14 -117 C ATOM 1635 O ALA A 204 -6.694 22.363 16.934 1.00 9.96 O ANISOU 1635 O ALA A 204 1282 1275 1227 68 -20 -141 O ATOM 1636 CB ALA A 204 -8.290 22.955 14.348 1.00 10.46 C ANISOU 1636 CB ALA A 204 1306 1314 1354 56 -20 -110 C ATOM 1637 N VAL A 205 -5.918 20.901 15.346 1.00 7.33 N ANISOU 1637 N VAL A 205 924 952 910 30 -22 -100 N ATOM 1638 CA VAL A 205 -4.552 20.865 15.862 1.00 7.35 C ANISOU 1638 CA VAL A 205 937 956 899 21 -40 -105 C ATOM 1639 C VAL A 205 -3.630 21.215 14.694 1.00 9.42 C ANISOU 1639 C VAL A 205 1190 1207 1184 -2 -59 -92 C ATOM 1640 O VAL A 205 -3.674 20.542 13.659 1.00 8.66 O ANISOU 1640 O VAL A 205 1079 1115 1095 -12 -51 -73 O ATOM 1641 CB VAL A 205 -4.188 19.499 16.426 1.00 7.95 C ANISOU 1641 CB VAL A 205 1012 1055 952 21 -27 -94 C ATOM 1642 CG1 VAL A 205 -2.782 19.544 17.005 1.00 9.34 C ANISOU 1642 CG1 VAL A 205 1198 1235 1117 14 -49 -98 C ATOM 1643 CG2 VAL A 205 -5.167 19.039 17.480 1.00 10.13 C ANISOU 1643 CG2 VAL A 205 1295 1348 1206 41 -3 -98 C ATOM 1644 N ATHR A 206 -2.834 22.281 14.847 0.46 8.46 N ANISOU 1644 N ATHR A 206 1076 1068 1071 -10 -86 -102 N ATOM 1645 N BTHR A 206 -2.873 22.333 14.835 0.54 7.62 N ANISOU 1645 N BTHR A 206 970 960 965 -10 -86 -103 N ATOM 1646 CA ATHR A 206 -2.012 22.770 13.746 0.46 7.40 C ANISOU 1646 CA ATHR A 206 929 923 959 -33 -103 -85 C ATOM 1647 CA BTHR A 206 -2.017 22.911 13.795 0.54 7.52 C ANISOU 1647 CA BTHR A 206 946 936 976 -33 -106 -87 C ATOM 1648 C ATHR A 206 -0.556 22.860 14.201 0.46 8.31 C ANISOU 1648 C ATHR A 206 1043 1042 1073 -48 -126 -82 C ATOM 1649 C BTHR A 206 -0.550 22.842 14.215 0.54 7.84 C ANISOU 1649 C BTHR A 206 983 983 1013 -48 -126 -82 C ATOM 1650 O ATHR A 206 -0.250 22.781 15.385 0.46 8.21 O ANISOU 1650 O ATHR A 206 1044 1033 1041 -41 -135 -99 O ATOM 1651 O BTHR A 206 -0.229 22.698 15.392 0.54 9.15 O ANISOU 1651 O BTHR A 206 1162 1154 1159 -41 -134 -98 O ATOM 1652 CB ATHR A 206 -2.570 24.107 13.240 0.46 9.42 C ANISOU 1652 CB ATHR A 206 1190 1150 1240 -35 -118 -90 C ATOM 1653 CB BTHR A 206 -2.394 24.371 13.523 0.54 8.68 C ANISOU 1653 CB BTHR A 206 1102 1051 1146 -35 -125 -96 C ATOM 1654 CG2ATHR A 206 -2.557 25.214 14.354 0.46 11.85 C ANISOU 1654 CG2ATHR A 206 1523 1434 1546 -25 -140 -120 C ATOM 1655 CG2BTHR A 206 -3.941 24.490 13.310 0.54 8.23 C ANISOU 1655 CG2BTHR A 206 1045 988 1093 -14 -106 -102 C ATOM 1656 OG1ATHR A 206 -1.913 24.485 12.011 0.46 10.49 O ANISOU 1656 OG1ATHR A 206 1311 1278 1396 -59 -129 -66 O ATOM 1657 OG1BTHR A 206 -1.974 25.200 14.654 0.54 12.12 O ANISOU 1657 OG1BTHR A 206 1559 1470 1577 -31 -150 -121 O ATOM 1658 N GLY A 207 0.373 23.030 13.245 1.00 7.85 N ANISOU 1658 N GLY A 207 966 984 1032 -70 -136 -59 N ATOM 1659 CA GLY A 207 1.778 23.045 13.592 1.00 7.67 C ANISOU 1659 CA GLY A 207 933 969 1011 -85 -156 -50 C ATOM 1660 C GLY A 207 2.141 24.251 14.470 1.00 8.50 C ANISOU 1660 C GLY A 207 1054 1049 1124 -95 -194 -69 C ATOM 1661 O GLY A 207 1.492 25.308 14.466 1.00 8.46 O ANISOU 1661 O GLY A 207 1067 1015 1132 -94 -206 -84 O ATOM 1662 N LEU A 208 3.274 24.112 15.150 1.00 9.75 N ANISOU 1662 N LEU A 208 1208 1218 1280 -106 -215 -67 N ATOM 1663 CA LEU A 208 3.667 25.081 16.187 1.00 9.46 C ANISOU 1663 CA LEU A 208 1192 1158 1243 -114 -256 -89 C ATOM 1664 C LEU A 208 3.963 26.460 15.610 1.00 10.34 C ANISOU 1664 C LEU A 208 1302 1235 1390 -140 -288 -83 C ATOM 1665 O LEU A 208 3.784 27.472 16.306 1.00 10.51 O ANISOU 1665 O LEU A 208 1353 1223 1415 -141 -319 -110 O ATOM 1666 CB LEU A 208 4.887 24.525 16.957 1.00 11.28 C ANISOU 1666 CB LEU A 208 1412 1410 1463 -123 -276 -82 C ATOM 1667 CG LEU A 208 5.346 25.227 18.231 1.00 13.38 C ANISOU 1667 CG LEU A 208 1705 1659 1721 -129 -322 -108 C ATOM 1668 CD1 LEU A 208 4.186 25.384 19.244 1.00 16.49 C ANISOU 1668 CD1 LEU A 208 2143 2042 2080 -98 -314 -149 C ATOM 1669 CD2 LEU A 208 6.513 24.428 18.769 1.00 13.45 C ANISOU 1669 CD2 LEU A 208 1694 1696 1720 -136 -336 -92 C ATOM 1670 N ASP A 209 4.408 26.564 14.343 1.00 9.06 N ANISOU 1670 N ASP A 209 1109 1078 1254 -161 -281 -47 N ATOM 1671 CA ASP A 209 4.678 27.880 13.778 1.00 10.16 C ANISOU 1671 CA ASP A 209 1248 1184 1429 -189 -311 -35 C ATOM 1672 C ASP A 209 3.425 28.618 13.289 1.00 9.71 C ANISOU 1672 C ASP A 209 1212 1096 1381 -177 -304 -47 C ATOM 1673 O ASP A 209 3.531 29.807 12.899 1.00 12.71 O ANISOU 1673 O ASP A 209 1597 1440 1791 -198 -333 -39 O ATOM 1674 CB ASP A 209 5.621 27.764 12.538 1.00 10.55 C ANISOU 1674 CB ASP A 209 1253 1254 1501 -217 -303 14 C ATOM 1675 CG ASP A 209 7.087 27.601 12.898 1.00 20.32 C ANISOU 1675 CG ASP A 209 2462 2510 2748 -241 -326 35 C ATOM 1676 OD1 ASP A 209 7.494 27.843 14.055 1.00 16.91 O ANISOU 1676 OD1 ASP A 209 2045 2066 2313 -246 -361 14 O ATOM 1677 OD2 ASP A 209 7.875 27.243 11.988 1.00 29.90 O1- ANISOU 1677 OD2 ASP A 209 3636 3752 3973 -255 -310 75 O1- ATOM 1678 N THR A 210 2.252 28.000 13.352 1.00 8.86 N ANISOU 1678 N THR A 210 1117 999 1251 -144 -270 -64 N ATOM 1679 CA THR A 210 1.039 28.666 12.901 1.00 8.27 C ANISOU 1679 CA THR A 210 1057 898 1186 -130 -263 -74 C ATOM 1680 C THR A 210 0.819 29.960 13.687 1.00 9.33 C ANISOU 1680 C THR A 210 1225 986 1333 -126 -300 -104 C ATOM 1681 O THR A 210 0.978 29.985 14.927 1.00 10.36 O ANISOU 1681 O THR A 210 1379 1113 1445 -115 -315 -136 O ATOM 1682 CB THR A 210 -0.145 27.727 13.056 1.00 6.58 C ANISOU 1682 CB THR A 210 847 706 946 -96 -224 -88 C ATOM 1683 CG2 THR A 210 -1.433 28.364 12.593 1.00 10.23 C ANISOU 1683 CG2 THR A 210 1319 1146 1422 -79 -217 -95 C ATOM 1684 OG1 THR A 210 0.106 26.552 12.282 1.00 8.99 O ANISOU 1684 OG1 THR A 210 1126 1047 1242 -101 -196 -61 O ATOM 1685 N THR A 211 0.500 31.040 12.983 1.00 9.67 N ANISOU 1685 N THR A 211 1274 993 1408 -135 -317 -95 N ATOM 1686 CA THR A 211 0.437 32.359 13.638 1.00 9.26 C ANISOU 1686 CA THR A 211 1257 889 1374 -135 -359 -123 C ATOM 1687 C THR A 211 -0.963 32.649 14.175 1.00 10.57 C ANISOU 1687 C THR A 211 1452 1037 1528 -89 -344 -162 C ATOM 1688 O THR A 211 -1.945 31.974 13.866 1.00 12.31 O ANISOU 1688 O THR A 211 1660 1282 1734 -64 -304 -159 O ATOM 1689 CB THR A 211 0.764 33.448 12.663 1.00 12.44 C ANISOU 1689 CB THR A 211 1653 1253 1819 -166 -388 -93 C ATOM 1690 CG2 THR A 211 2.106 33.210 11.987 1.00 14.18 C ANISOU 1690 CG2 THR A 211 1838 1496 2054 -211 -397 -48 C ATOM 1691 OG1 THR A 211 -0.310 33.487 11.678 1.00 12.85 O ANISOU 1691 OG1 THR A 211 1698 1305 1879 -149 -362 -79 O ATOM 1692 N ALA A 212 -1.068 33.750 14.967 1.00 12.20 N ANISOU 1692 N ALA A 212 1698 1196 1743 -78 -379 -197 N ATOM 1693 CA ALA A 212 -2.388 34.128 15.468 1.00 12.71 C ANISOU 1693 CA ALA A 212 1789 1244 1797 -29 -364 -234 C ATOM 1694 C ALA A 212 -3.395 34.395 14.363 1.00 12.50 C ANISOU 1694 C ALA A 212 1746 1208 1796 -17 -345 -212 C ATOM 1695 O ALA A 212 -4.542 33.923 14.496 1.00 13.99 O ANISOU 1695 O ALA A 212 1929 1418 1967 21 -307 -224 O ATOM 1696 CB ALA A 212 -2.233 35.355 16.407 1.00 15.49 C ANISOU 1696 CB ALA A 212 2191 1540 2156 -19 -409 -277 C ATOM 1697 N PRO A 213 -3.081 35.137 13.282 1.00 12.67 N ANISOU 1697 N PRO A 213 1758 1200 1857 -47 -369 -179 N ATOM 1698 CA PRO A 213 -4.101 35.347 12.237 1.00 14.94 C ANISOU 1698 CA PRO A 213 2031 1482 2165 -34 -353 -157 C ATOM 1699 C PRO A 213 -4.475 34.037 11.578 1.00 14.23 C ANISOU 1699 C PRO A 213 1904 1450 2054 -33 -308 -131 C ATOM 1700 O PRO A 213 -5.634 33.849 11.271 1.00 14.13 O ANISOU 1700 O PRO A 213 1882 1445 2040 -4 -284 -131 O ATOM 1701 CB PRO A 213 -3.424 36.309 11.228 1.00 15.93 C ANISOU 1701 CB PRO A 213 2153 1569 2332 -75 -391 -120 C ATOM 1702 CG PRO A 213 -2.275 36.903 12.004 1.00 17.41 C ANISOU 1702 CG PRO A 213 2362 1725 2527 -101 -434 -135 C ATOM 1703 CD PRO A 213 -1.871 35.952 13.059 1.00 14.02 C ANISOU 1703 CD PRO A 213 1935 1336 2058 -93 -418 -161 C ATOM 1704 N GLU A 214 -3.508 33.126 11.416 1.00 11.49 N ANISOU 1704 N GLU A 214 1536 1140 1690 -62 -299 -111 N ATOM 1705 CA GLU A 214 -3.858 31.849 10.784 1.00 10.14 C ANISOU 1705 CA GLU A 214 1335 1018 1498 -59 -259 -89 C ATOM 1706 C GLU A 214 -4.778 31.042 11.682 1.00 11.53 C ANISOU 1706 C GLU A 214 1515 1220 1646 -22 -227 -119 C ATOM 1707 O GLU A 214 -5.741 30.404 11.189 1.00 12.02 O ANISOU 1707 O GLU A 214 1561 1305 1703 -7 -200 -108 O ATOM 1708 CB GLU A 214 -2.574 31.058 10.486 1.00 9.60 C ANISOU 1708 CB GLU A 214 1248 983 1419 -93 -256 -64 C ATOM 1709 CG GLU A 214 -1.727 31.595 9.322 1.00 11.31 C ANISOU 1709 CG GLU A 214 1448 1190 1660 -131 -275 -22 C ATOM 1710 CD GLU A 214 -0.372 30.955 9.177 1.00 12.99 C ANISOU 1710 CD GLU A 214 1639 1433 1864 -160 -273 1 C ATOM 1711 OE1 GLU A 214 0.235 30.451 10.177 1.00 11.29 O ANISOU 1711 OE1 GLU A 214 1426 1232 1632 -158 -274 -18 O ATOM 1712 OE2 GLU A 214 0.185 30.986 8.035 1.00 13.88 O1- ANISOU 1712 OE2 GLU A 214 1730 1557 1986 -185 -270 42 O1- ATOM 1713 N LEU A 215 -4.503 31.028 12.994 1.00 11.58 N ANISOU 1713 N LEU A 215 1543 1225 1631 -8 -232 -152 N ATOM 1714 CA LEU A 215 -5.379 30.315 13.919 1.00 12.25 C ANISOU 1714 CA LEU A 215 1632 1336 1686 28 -199 -177 C ATOM 1715 C LEU A 215 -6.770 30.929 13.965 1.00 14.30 C ANISOU 1715 C LEU A 215 1897 1579 1957 66 -188 -192 C ATOM 1716 O LEU A 215 -7.776 30.207 14.125 1.00 14.82 O ANISOU 1716 O LEU A 215 1947 1674 2009 91 -153 -192 O ATOM 1717 CB LEU A 215 -4.779 30.350 15.323 1.00 15.88 C ANISOU 1717 CB LEU A 215 2119 1796 2119 36 -211 -210 C ATOM 1718 CG LEU A 215 -3.803 29.278 15.711 1.00 24.95 C ANISOU 1718 CG LEU A 215 3259 2980 3242 17 -206 -201 C ATOM 1719 CD1 LEU A 215 -3.506 29.461 17.198 1.00 26.96 C ANISOU 1719 CD1 LEU A 215 3546 3231 3466 34 -218 -238 C ATOM 1720 CD2 LEU A 215 -4.305 27.849 15.503 1.00 20.03 C ANISOU 1720 CD2 LEU A 215 2610 2401 2599 24 -164 -182 C ATOM 1721 N ASER A 216 -6.843 32.265 13.875 0.57 12.36 N ANISOU 1721 N ASER A 216 1673 1285 1739 72 -218 -204 N ATOM 1722 N BSER A 216 -6.874 32.259 13.851 0.43 12.81 N ANISOU 1722 N BSER A 216 1729 1342 1796 73 -217 -204 N ATOM 1723 CA ASER A 216 -8.126 32.963 13.853 0.57 14.14 C ANISOU 1723 CA ASER A 216 1902 1489 1980 112 -210 -218 C ATOM 1724 CA BSER A 216 -8.196 32.891 13.879 0.43 14.94 C ANISOU 1724 CA BSER A 216 2002 1593 2080 114 -207 -218 C ATOM 1725 C ASER A 216 -8.986 32.519 12.675 0.57 13.76 C ANISOU 1725 C ASER A 216 1818 1460 1949 110 -190 -182 C ATOM 1726 C BSER A 216 -9.023 32.529 12.651 0.43 13.54 C ANISOU 1726 C BSER A 216 1790 1433 1923 111 -190 -182 C ATOM 1727 O ASER A 216 -10.177 32.248 12.838 0.57 14.07 O ANISOU 1727 O ASER A 216 1843 1517 1986 144 -162 -187 O ATOM 1728 O BSER A 216 -10.238 32.339 12.752 0.43 14.65 O ANISOU 1728 O BSER A 216 1916 1587 2063 145 -164 -185 O ATOM 1729 CB ASER A 216 -7.903 34.475 13.803 0.57 17.58 C ANISOU 1729 CB ASER A 216 2369 1862 2448 114 -253 -232 C ATOM 1730 CB BSER A 216 -8.058 34.403 14.003 0.43 17.29 C ANISOU 1730 CB BSER A 216 2334 1831 2406 123 -247 -239 C ATOM 1731 OG ASER A 216 -9.148 35.119 13.946 0.57 18.28 O ANISOU 1731 OG ASER A 216 2464 1931 2550 162 -242 -251 O ATOM 1732 OG BSER A 216 -7.549 34.709 15.272 0.43 23.55 O ANISOU 1732 OG BSER A 216 3164 2609 3175 135 -261 -280 O ATOM 1733 N VAL A 217 -8.382 32.431 11.482 1.00 12.77 N ANISOU 1733 N VAL A 217 1677 1334 1840 71 -205 -145 N ATOM 1734 CA VAL A 217 -9.079 31.951 10.285 1.00 13.50 C ANISOU 1734 CA VAL A 217 1739 1445 1943 64 -192 -111 C ATOM 1735 C VAL A 217 -9.555 30.519 10.481 1.00 13.27 C ANISOU 1735 C VAL A 217 1689 1467 1887 70 -155 -107 C ATOM 1736 O VAL A 217 -10.702 30.178 10.133 1.00 14.51 O ANISOU 1736 O VAL A 217 1824 1638 2050 87 -138 -97 O ATOM 1737 CB VAL A 217 -8.161 32.075 9.063 1.00 12.11 C ANISOU 1737 CB VAL A 217 1557 1264 1781 21 -214 -74 C ATOM 1738 CG1 VAL A 217 -8.758 31.315 7.848 1.00 12.97 C ANISOU 1738 CG1 VAL A 217 1638 1401 1887 11 -199 -40 C ATOM 1739 CG2 VAL A 217 -7.960 33.553 8.718 1.00 16.29 C ANISOU 1739 CG2 VAL A 217 2105 1740 2345 15 -251 -68 C ATOM 1740 N ILE A 218 -8.690 29.671 11.054 1.00 12.81 N ANISOU 1740 N ILE A 218 1634 1433 1801 55 -146 -113 N ATOM 1741 CA ILE A 218 -9.050 28.275 11.296 1.00 11.76 C ANISOU 1741 CA ILE A 218 1483 1343 1642 58 -114 -108 C ATOM 1742 C ILE A 218 -10.243 28.187 12.242 1.00 12.36 C ANISOU 1742 C ILE A 218 1555 1430 1710 98 -88 -129 C ATOM 1743 O ILE A 218 -11.227 27.460 11.994 1.00 12.05 O ANISOU 1743 O ILE A 218 1491 1415 1672 106 -66 -114 O ATOM 1744 CB ILE A 218 -7.815 27.530 11.844 1.00 12.09 C ANISOU 1744 CB ILE A 218 1533 1403 1658 38 -112 -112 C ATOM 1745 CG1 ILE A 218 -6.873 27.215 10.679 1.00 13.04 C ANISOU 1745 CG1 ILE A 218 1642 1528 1784 3 -124 -83 C ATOM 1746 CG2 ILE A 218 -8.226 26.234 12.579 1.00 13.13 C ANISOU 1746 CG2 ILE A 218 1655 1571 1761 50 -81 -116 C ATOM 1747 CD1 ILE A 218 -5.486 26.909 11.117 1.00 16.76 C ANISOU 1747 CD1 ILE A 218 2120 2007 2241 -17 -132 -84 C ATOM 1748 N AGLU A 219 -10.198 28.944 13.326 0.49 13.21 N ANISOU 1748 N AGLU A 219 1688 1521 1811 123 -92 -161 N ATOM 1749 N BGLU A 219 -10.187 28.924 13.357 0.51 13.11 N ANISOU 1749 N BGLU A 219 1676 1509 1797 123 -91 -162 N ATOM 1750 CA AGLU A 219 -11.290 28.849 14.282 0.49 12.40 C ANISOU 1750 CA AGLU A 219 1582 1434 1695 165 -61 -180 C ATOM 1751 CA BGLU A 219 -11.303 28.887 14.302 0.51 12.92 C ANISOU 1751 CA BGLU A 219 1649 1500 1761 166 -62 -181 C ATOM 1752 C AGLU A 219 -12.603 29.369 13.705 0.49 11.69 C ANISOU 1752 C AGLU A 219 1470 1336 1635 190 -55 -170 C ATOM 1753 C BGLU A 219 -12.605 29.327 13.649 0.51 12.16 C ANISOU 1753 C BGLU A 219 1528 1397 1695 189 -55 -169 C ATOM 1754 O AGLU A 219 -13.680 28.844 14.039 0.49 13.95 O ANISOU 1754 O AGLU A 219 1733 1652 1917 214 -23 -166 O ATOM 1755 O BGLU A 219 -13.674 28.748 13.910 0.51 14.94 O ANISOU 1755 O BGLU A 219 1855 1779 2044 210 -23 -161 O ATOM 1756 CB AGLU A 219 -10.879 29.608 15.556 0.49 15.23 C ANISOU 1756 CB AGLU A 219 1979 1774 2033 190 -69 -221 C ATOM 1757 CB BGLU A 219 -11.011 29.802 15.511 0.51 11.49 C ANISOU 1757 CB BGLU A 219 1505 1295 1564 195 -71 -223 C ATOM 1758 CG AGLU A 219 -9.692 28.868 16.277 0.49 18.03 C ANISOU 1758 CG AGLU A 219 2349 2147 2353 167 -73 -228 C ATOM 1759 CG BGLU A 219 -10.118 29.185 16.612 0.51 24.74 C ANISOU 1759 CG BGLU A 219 3205 2994 3201 188 -67 -241 C ATOM 1760 CD AGLU A 219 -9.006 29.710 17.367 0.49 18.41 C ANISOU 1760 CD AGLU A 219 2441 2170 2383 180 -96 -268 C ATOM 1761 CD BGLU A 219 -10.821 28.188 17.546 0.51 23.72 C ANISOU 1761 CD BGLU A 219 3065 2910 3037 212 -24 -243 C ATOM 1762 OE1AGLU A 219 -9.335 30.932 17.446 0.49 23.04 O ANISOU 1762 OE1AGLU A 219 3049 2718 2987 204 -114 -291 O ATOM 1763 OE1BGLU A 219 -11.730 28.513 18.371 0.51 26.38 O ANISOU 1763 OE1BGLU A 219 3407 3256 3360 256 1 -264 O ATOM 1764 OE2AGLU A 219 -8.152 29.171 18.139 0.49 19.49 O1- ANISOU 1764 OE2AGLU A 219 2593 2324 2489 169 -100 -276 O1- ATOM 1765 OE2BGLU A 219 -10.400 27.036 17.466 0.51 33.93 O1- ANISOU 1765 OE2BGLU A 219 4344 4232 4315 186 -14 -221 O1- ATOM 1766 N SER A 220 -12.551 30.375 12.818 1.00 12.89 N ANISOU 1766 N SER A 220 1627 1451 1820 184 -85 -163 N ATOM 1767 CA SER A 220 -13.764 30.891 12.192 1.00 13.65 C ANISOU 1767 CA SER A 220 1701 1537 1948 208 -83 -150 C ATOM 1768 C SER A 220 -14.342 29.901 11.165 1.00 13.01 C ANISOU 1768 C SER A 220 1582 1487 1875 185 -74 -111 C ATOM 1769 O SER A 220 -15.515 29.535 11.257 1.00 16.13 O ANISOU 1769 O SER A 220 1947 1906 2277 207 -51 -102 O ATOM 1770 CB SER A 220 -13.436 32.233 11.526 1.00 17.61 C ANISOU 1770 CB SER A 220 2223 1986 2482 204 -123 -149 C ATOM 1771 OG SER A 220 -14.549 32.692 10.793 1.00 22.27 O ANISOU 1771 OG SER A 220 2791 2568 3105 224 -126 -131 O ATOM 1772 N VAL A 221 -13.523 29.436 10.208 1.00 11.32 N ANISOU 1772 N VAL A 221 1368 1275 1659 141 -91 -88 N ATOM 1773 CA VAL A 221 -14.113 28.643 9.132 1.00 11.73 C ANISOU 1773 CA VAL A 221 1390 1348 1717 122 -90 -55 C ATOM 1774 C VAL A 221 -14.509 27.248 9.614 1.00 11.80 C ANISOU 1774 C VAL A 221 1380 1399 1706 119 -60 -51 C ATOM 1775 O VAL A 221 -15.516 26.702 9.132 1.00 13.70 O ANISOU 1775 O VAL A 221 1591 1658 1958 119 -54 -30 O ATOM 1776 CB VAL A 221 -13.176 28.593 7.888 1.00 11.03 C ANISOU 1776 CB VAL A 221 1310 1251 1630 81 -116 -31 C ATOM 1777 CG1 VAL A 221 -11.991 27.616 8.109 1.00 12.40 C ANISOU 1777 CG1 VAL A 221 1495 1445 1772 54 -107 -34 C ATOM 1778 CG2 VAL A 221 -13.945 28.118 6.642 1.00 12.85 C ANISOU 1778 CG2 VAL A 221 1517 1494 1870 68 -123 0 C ATOM 1779 N PHE A 222 -13.859 26.708 10.636 1.00 11.10 N ANISOU 1779 N PHE A 222 1306 1324 1588 119 -43 -69 N ATOM 1780 CA PHE A 222 -14.271 25.400 11.144 1.00 9.91 C ANISOU 1780 CA PHE A 222 1136 1209 1418 117 -15 -62 C ATOM 1781 C PHE A 222 -15.281 25.491 12.285 1.00 13.88 C ANISOU 1781 C PHE A 222 1626 1729 1917 155 16 -73 C ATOM 1782 O PHE A 222 -15.656 24.472 12.869 1.00 14.09 O ANISOU 1782 O PHE A 222 1638 1788 1929 155 42 -65 O ATOM 1783 CB PHE A 222 -12.982 24.653 11.572 1.00 11.28 C ANISOU 1783 CB PHE A 222 1333 1392 1561 95 -14 -69 C ATOM 1784 CG PHE A 222 -12.108 24.223 10.378 1.00 8.31 C ANISOU 1784 CG PHE A 222 961 1011 1186 58 -34 -51 C ATOM 1785 CD1 PHE A 222 -12.561 23.259 9.471 1.00 9.57 C ANISOU 1785 CD1 PHE A 222 1103 1185 1349 39 -34 -27 C ATOM 1786 CD2 PHE A 222 -10.850 24.781 10.217 1.00 10.69 C ANISOU 1786 CD2 PHE A 222 1284 1295 1483 45 -53 -58 C ATOM 1787 CE1 PHE A 222 -11.732 22.840 8.408 1.00 8.85 C ANISOU 1787 CE1 PHE A 222 1020 1091 1250 11 -50 -14 C ATOM 1788 CE2 PHE A 222 -10.028 24.401 9.088 1.00 10.25 C ANISOU 1788 CE2 PHE A 222 1230 1239 1425 15 -67 -39 C ATOM 1789 CZ PHE A 222 -10.486 23.445 8.202 1.00 9.16 C ANISOU 1789 CZ PHE A 222 1079 1117 1285 1 -64 -19 C ATOM 1790 N ARG A 223 -15.740 26.705 12.598 1.00 12.16 N ANISOU 1790 N ARG A 223 1414 1492 1715 191 14 -91 N ATOM 1791 CA ARG A 223 -16.820 26.905 13.584 1.00 15.37 C ANISOU 1791 CA ARG A 223 1804 1917 2119 236 47 -102 C ATOM 1792 C ARG A 223 -16.412 26.340 14.937 1.00 15.60 C ANISOU 1792 C ARG A 223 1851 1971 2107 246 75 -121 C ATOM 1793 O ARG A 223 -17.207 25.657 15.635 1.00 18.67 O ANISOU 1793 O ARG A 223 2215 2396 2483 262 111 -111 O ATOM 1794 CB ARG A 223 -18.143 26.326 13.051 1.00 16.31 C ANISOU 1794 CB ARG A 223 1873 2062 2263 236 61 -68 C ATOM 1795 CG ARG A 223 -18.573 27.070 11.796 1.00 22.54 C ANISOU 1795 CG ARG A 223 2648 2824 3090 233 30 -53 C ATOM 1796 CD ARG A 223 -19.988 26.745 11.343 1.00 41.96 C ANISOU 1796 CD ARG A 223 5056 5307 5580 240 39 -21 C ATOM 1797 NE ARG A 223 -20.866 26.334 12.443 1.00 58.40 N ANISOU 1797 NE ARG A 223 7110 7426 7655 271 83 -21 N ATOM 1798 CZ ARG A 223 -21.657 27.143 13.151 1.00 66.15 C ANISOU 1798 CZ ARG A 223 8077 8411 8644 324 107 -34 C ATOM 1799 NH1 ARG A 223 -21.708 28.452 12.902 1.00 66.02 N1+ ANISOU 1799 NH1 ARG A 223 8077 8359 8649 355 88 -52 N1+ ATOM 1800 NH2 ARG A 223 -22.399 26.629 14.126 1.00 68.00 N ANISOU 1800 NH2 ARG A 223 8284 8687 8866 349 151 -28 N ATOM 1801 N LEU A 224 -15.169 26.659 15.338 1.00 14.59 N ANISOU 1801 N LEU A 224 1763 1823 1957 236 57 -146 N ATOM 1802 CA LEU A 224 -14.621 26.105 16.579 1.00 17.54 C ANISOU 1802 CA LEU A 224 2159 2219 2288 242 75 -162 C ATOM 1803 C LEU A 224 -14.810 27.006 17.786 1.00 29.70 C ANISOU 1803 C LEU A 224 3726 3753 3806 290 88 -201 C ATOM 1804 O LEU A 224 -14.679 26.519 18.914 1.00 28.25 O ANISOU 1804 O LEU A 224 3555 3596 3582 303 112 -212 O ATOM 1805 CB LEU A 224 -13.128 25.778 16.425 1.00 17.05 C ANISOU 1805 CB LEU A 224 2123 2144 2210 204 48 -165 C ATOM 1806 CG LEU A 224 -12.869 24.800 15.287 1.00 14.88 C ANISOU 1806 CG LEU A 224 1826 1877 1950 162 39 -131 C ATOM 1807 CD1 LEU A 224 -11.340 24.617 15.057 1.00 17.67 C ANISOU 1807 CD1 LEU A 224 2203 2219 2293 130 13 -134 C ATOM 1808 CD2 LEU A 224 -13.619 23.476 15.498 1.00 17.31 C ANISOU 1808 CD2 LEU A 224 2106 2223 2248 157 69 -106 C ATOM 1809 N GLY A 225 -15.124 28.275 17.586 1.00 30.86 N ANISOU 1809 N GLY A 225 3884 3866 3976 317 73 -221 N ATOM 1810 CA GLY A 225 -15.376 29.159 18.718 1.00 50.59 C ANISOU 1810 CA GLY A 225 6413 6356 6453 369 85 -262 C ATOM 1811 C GLY A 225 -16.834 29.217 19.183 1.00 57.12 C ANISOU 1811 C GLY A 225 7209 7212 7280 420 131 -260 C ATOM 1812 O GLY A 225 -17.414 28.216 19.635 1.00 59.78 O ANISOU 1812 O GLY A 225 7516 7598 7598 423 170 -238 O TER END If you find results from this site helpful for your research, please cite one of our papers:
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