HEADER MEMBRANE PROTEIN 23-MAY-24 8ZMF TITLE CRYSTAL STRUCTURE OF AN INVERSE AGONIST ANTIPSYCHOTIC DRUG DERIVATIVE- TITLE 2 BOUND 5-HT2C KEYWDS CLASS A G PROTEIN-COUPLED RECEPTOR, INVERSE AGONIST, MEMBRANE KEYWDS 2 PROTEIN EXPDTA X-RAY DIFFRACTION REMARK 2 REMARK 2 RESOLUTION. 3.60 ANGSTROMS. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 1030 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 18430 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 DBREF 8ZMF A 40 245 UNP P28335 5HT2C_HUMAN 40 245 DBREF 8ZMF A 1001 1106 UNP P0ABE7 C562_ECOLX 23 128 DBREF 8ZMF A 301 393 UNP P28335 5HT2C_HUMAN 301 393 SEQRES 1 A 439 MET LYS THR ILE ILE ALA LEU SER TYR ILE PHE CYS LEU SEQRES 2 A 439 VAL PHE ALA ASP TYR LYS ASP ASP ASP ASP GLY ALA PRO SEQRES 3 A 439 THR SER ASP GLY GLY ARG PHE LYS PHE PRO ASP GLY VAL SEQRES 4 A 439 GLN ASN TRP PRO ALA LEU SER ILE VAL ILE ILE ILE ILE SEQRES 5 A 439 MET THR ILE GLY GLY ASN ILE LEU VAL ILE MET ALA VAL SEQRES 6 A 439 SER MET GLU LYS LYS LEU HIS ASN ALA THR ASN TYR PHE SEQRES 7 A 439 LEU MET SER LEU ALA ILE ALA ASP MET LEU VAL GLY LEU SEQRES 8 A 439 LEU VAL MET PRO LEU SER LEU LEU ALA ILE LEU TYR ASP SEQRES 9 A 439 TYR VAL TRP PRO LEU PRO ARG TYR LEU CYS PRO VAL TRP SEQRES 10 A 439 ILE SER LEU ASP VAL LEU PHE SER THR ALA SER ILE MET SEQRES 11 A 439 HIS LEU CYS ALA ILE SER LEU ASP ARG TYR VAL ALA ILE SEQRES 12 A 439 ARG ASN PRO ILE GLU HIS SER ARG PHE ASN SER ARG THR SEQRES 13 A 439 LYS ALA ILE MET LYS ILE ALA ILE VAL TRP ALA ILE SER SEQRES 14 A 439 ILE GLY VAL SER VAL PRO ILE PRO VAL ILE GLY LEU ARG SEQRES 15 A 439 ASP GLU GLU LYS VAL PHE VAL ASN ASN THR THR CYS VAL SEQRES 16 A 439 LEU ASN ASP PRO ASN PHE VAL LEU ILE GLY SER PHE VAL SEQRES 17 A 439 ALA PHE PHE ILE PRO LEU THR ILE MET VAL ILE THR TYR SEQRES 18 A 439 CYS LEU THR ILE TYR VAL LEU ARG ARG GLN ALA ALA ASP SEQRES 19 A 439 LEU GLU ASP ASN TRP GLU THR LEU ASN ASP ASN LEU LYS SEQRES 20 A 439 VAL ILE GLU LYS ALA ASP ASN ALA ALA GLN VAL LYS ASP SEQRES 21 A 439 ALA LEU THR LYS MET ARG ALA ALA ALA LEU ASP ALA GLN SEQRES 22 A 439 LYS ALA THR PRO PRO LYS LEU GLU ASP LYS SER PRO ASP SEQRES 23 A 439 SER PRO GLU MET LYS ASP PHE ARG HIS GLY PHE ASP ILE SEQRES 24 A 439 LEU VAL GLY GLN ILE ASP ASP ALA LEU LYS LEU ALA ASN SEQRES 25 A 439 GLU GLY LYS VAL LYS GLU ALA GLN ALA ALA ALA GLU GLN SEQRES 26 A 439 LEU LYS THR THR ARG ASN ALA TYR ILE GLN LYS TYR LEU SEQRES 27 A 439 GLN ALA ILE ASN ASN GLU ARG LYS ALA SER LYS VAL LEU SEQRES 28 A 439 GLY ILE VAL PHE PHE VAL PHE LEU ILE MET TRP CYS PRO SEQRES 29 A 439 PHE PHE ILE THR ASN ILE LEU SER VAL LEU CYS GLU LYS SEQRES 30 A 439 SER CYS ASN GLN LYS LEU MET GLU LYS LEU LEU ASN VAL SEQRES 31 A 439 PHE VAL TRP ILE GLY TYR VAL ASN SER GLY ILE ASN PRO SEQRES 32 A 439 LEU VAL TYR THR LEU PHE ASN LYS ILE TYR ARG ARG ALA SEQRES 33 A 439 PHE SER ASN TYR LEU ARG CYS ASN TYR LYS VAL GLU LYS SEQRES 34 A 439 LYS PRO LEU GLU GLU ASN LEU TYR PHE GLN HELIX 1 1 TRP A 55 SER A 59 5 5 HELIX 2 2 ILE A 60 GLU A 81 1 22 HELIX 3 3 LYS A 82 HIS A 85 5 4 HELIX 4 4 ASN A 86 TYR A 116 1 31 HELIX 5 5 TYR A 125 ARG A 157 1 33 HELIX 6 6 ASN A 166 VAL A 187 1 22 HELIX 7 7 VAL A 187 ASP A 196 1 10 HELIX 8 8 ASP A 211 PHE A 223 1 13 HELIX 9 9 PHE A 223 ILE A 1017 1 40 HELIX 10 10 ALA A 1029 LYS A 1032 5 4 HELIX 11 11 MET A 1033 ALA A 1043 1 11 HELIX 12 12 HIS A 1063 LEU A 1068 1 6 HELIX 13 13 ARG A 1098 CYS A 337 1 46 HELIX 14 14 ASN A 342 SER A 361 1 20 HELIX 15 15 ILE A 363 ASN A 372 1 10 HELIX 16 16 ASN A 372 TYR A 387 1 16 SHEET 1 AA1 2 PHE A 201 VAL A 202 0 SHEET 2 AA1 2 THR A 206 CYS A 207 -1 O THR A 206 N VAL A 202 SSBOND 1 CYS A 127 CYS A 207 1555 1555 2.03 SSBOND 2 CYS A 337 CYS A 341 1555 1555 2.03 CISPEP 1 PHE A 48 PRO A 49 0 1.97 CRYST1 88.840 96.010 149.000 90.00 90.00 90.00 C 2 2 2 8 ATOM 1 N LYS A 47 25.205 46.883 63.852 1.00101.60 N ANISOU 1 N LYS A 47 14059 13418 11125 -3397 2141 -1103 N ATOM 2 CA LYS A 47 25.565 48.286 64.022 1.00114.55 C ANISOU 2 CA LYS A 47 15368 15082 13072 -3119 2171 -1263 C ATOM 3 C LYS A 47 24.411 49.052 64.668 1.00128.29 C ANISOU 3 C LYS A 47 16810 17024 14911 -3331 2653 -1609 C ATOM 4 O LYS A 47 23.596 49.671 63.982 1.00125.92 O ANISOU 4 O LYS A 47 15917 16861 15065 -3218 2808 -1746 O ATOM 5 CB LYS A 47 25.949 48.905 62.676 1.00100.83 C ANISOU 5 CB LYS A 47 13122 13345 11843 -2692 1944 -1142 C ATOM 6 CG LYS A 47 26.608 50.272 62.770 1.00 84.06 C ANISOU 6 CG LYS A 47 10735 11171 10031 -2382 1863 -1235 C ATOM 7 CD LYS A 47 27.556 50.491 61.603 1.00 71.76 C ANISOU 7 CD LYS A 47 8986 9522 8759 -2030 1526 -1020 C ATOM 8 CE LYS A 47 26.887 50.167 60.276 1.00 59.25 C ANISOU 8 CE LYS A 47 7081 8045 7386 -1995 1519 -889 C ATOM 9 NZ LYS A 47 27.860 50.162 59.150 1.00 48.62 N ANISOU 9 NZ LYS A 47 5654 6627 6195 -1737 1223 -681 N ATOM 10 N PHE A 48 24.355 48.990 65.999 1.00141.60 N ANISOU 10 N PHE A 48 18924 18711 16167 -3651 2866 -1774 N ATOM 11 CA PHE A 48 23.263 49.622 66.736 1.00136.17 C ANISOU 11 CA PHE A 48 17984 18236 15519 -3921 3384 -2177 C ATOM 12 C PHE A 48 23.143 51.128 66.514 1.00141.04 C ANISOU 12 C PHE A 48 17954 18921 16715 -3575 3438 -2436 C ATOM 13 O PHE A 48 22.006 51.603 66.352 1.00142.95 O ANISOU 13 O PHE A 48 17663 19339 17313 -3652 3767 -2749 O ATOM 14 CB PHE A 48 23.402 49.303 68.230 1.00134.45 C ANISOU 14 CB PHE A 48 18440 17995 14651 -4343 3577 -2293 C ATOM 15 CG PHE A 48 23.186 47.854 68.562 1.00134.98 C ANISOU 15 CG PHE A 48 19117 17967 14201 -4753 3535 -2086 C ATOM 16 CD1 PHE A 48 22.321 47.079 67.806 1.00134.14 C ANISOU 16 CD1 PHE A 48 18779 17908 14282 -4825 3562 -2017 C ATOM 17 CD2 PHE A 48 23.851 47.266 69.625 1.00130.22 C ANISOU 17 CD2 PHE A 48 19309 17157 13013 -4995 3339 -1951 C ATOM 18 CE1 PHE A 48 22.120 45.745 68.107 1.00133.72 C ANISOU 18 CE1 PHE A 48 19253 17722 13832 -5150 3450 -1839 C ATOM 19 CE2 PHE A 48 23.655 45.932 69.930 1.00131.69 C ANISOU 19 CE2 PHE A 48 20024 17173 12839 -5329 3187 -1741 C ATOM 20 CZ PHE A 48 22.789 45.170 69.170 1.00131.23 C ANISOU 20 CZ PHE A 48 19712 17188 12961 -5415 3264 -1698 C ATOM 21 N PRO A 49 24.226 51.933 66.496 1.00147.64 N ANISOU 21 N PRO A 49 18775 19607 17714 -3201 3117 -2352 N ATOM 22 CA PRO A 49 25.667 51.679 66.619 1.00145.19 C ANISOU 22 CA PRO A 49 18930 19063 17172 -3006 2682 -2072 C ATOM 23 C PRO A 49 26.195 51.720 68.051 1.00138.49 C ANISOU 23 C PRO A 49 18649 18128 15842 -3197 2706 -2199 C ATOM 24 O PRO A 49 27.411 51.748 68.242 1.00125.79 O ANISOU 24 O PRO A 49 17350 16300 14144 -2984 2315 -2048 O ATOM 25 CB PRO A 49 26.276 52.812 65.798 1.00137.50 C ANISOU 25 CB PRO A 49 17459 18013 16770 -2525 2427 -2025 C ATOM 26 CG PRO A 49 25.349 53.948 66.043 1.00140.27 C ANISOU 26 CG PRO A 49 17291 18513 17493 -2516 2741 -2392 C ATOM 27 CD PRO A 49 23.965 53.351 66.184 1.00142.27 C ANISOU 27 CD PRO A 49 17446 18973 17638 -2896 3155 -2590 C ATOM 28 N ASP A 50 25.299 51.742 69.035 1.00148.91 N ANISOU 28 N ASP A 50 20096 19616 16867 -3604 3157 -2501 N ATOM 29 CA ASP A 50 25.723 51.762 70.428 1.00143.32 C ANISOU 29 CA ASP A 50 19996 18840 15620 -3846 3201 -2630 C ATOM 30 C ASP A 50 26.524 50.508 70.759 1.00135.38 C ANISOU 30 C ASP A 50 19812 17588 14038 -4015 2827 -2289 C ATOM 31 O ASP A 50 26.071 49.384 70.520 1.00135.73 O ANISOU 31 O ASP A 50 20112 17640 13818 -4306 2874 -2112 O ATOM 32 CB ASP A 50 24.506 51.871 71.346 1.00158.12 C ANISOU 32 CB ASP A 50 21875 20977 17227 -4345 3829 -3035 C ATOM 33 CG ASP A 50 23.617 53.050 71.000 1.00152.11 C ANISOU 33 CG ASP A 50 20246 20434 17114 -4176 4168 -3439 C ATOM 34 OD1 ASP A 50 23.971 53.815 70.078 1.00149.46 O ANISOU 34 OD1 ASP A 50 19375 20021 17393 -3682 3879 -3357 O ATOM 35 OD2 ASP A 50 22.562 53.211 71.649 1.00150.37 O ANISOU 35 OD2 ASP A 50 19849 20339 16946 -4460 4489 -3736 O ATOM 36 N GLY A 51 27.718 50.705 71.318 1.00114.02 N ANISOU 36 N GLY A 51 17514 14635 11175 -3824 2415 -2216 N ATOM 37 CA GLY A 51 28.581 49.610 71.708 1.00103.02 C ANISOU 37 CA GLY A 51 16909 12938 9297 -3934 1950 -1937 C ATOM 38 C GLY A 51 29.736 49.316 70.774 1.00 91.32 C ANISOU 38 C GLY A 51 15326 11201 8169 -3475 1362 -1670 C ATOM 39 O GLY A 51 30.468 48.348 71.014 1.00 82.01 O ANISOU 39 O GLY A 51 14752 9734 6674 -3530 909 -1469 O ATOM 40 N VAL A 52 29.926 50.115 69.719 1.00 90.38 N ANISOU 40 N VAL A 52 14477 11166 8698 -3047 1345 -1683 N ATOM 41 CA VAL A 52 31.019 49.871 68.780 1.00 74.58 C ANISOU 41 CA VAL A 52 12338 8961 7038 -2652 863 -1479 C ATOM 42 C VAL A 52 32.354 50.260 69.414 1.00 70.75 C ANISOU 42 C VAL A 52 12129 8185 6567 -2402 421 -1535 C ATOM 43 O VAL A 52 32.421 51.015 70.392 1.00 82.78 O ANISOU 43 O VAL A 52 13792 9699 7962 -2440 507 -1734 O ATOM 44 CB VAL A 52 30.776 50.635 67.467 1.00 71.29 C ANISOU 44 CB VAL A 52 11117 8725 7247 -2341 1008 -1467 C ATOM 45 CG1 VAL A 52 31.085 52.105 67.653 1.00 74.95 C ANISOU 45 CG1 VAL A 52 11183 9209 8084 -2073 1069 -1661 C ATOM 46 CG2 VAL A 52 31.587 50.037 66.321 1.00 58.48 C ANISOU 46 CG2 VAL A 52 9376 6974 5869 -2083 641 -1248 C ATOM 47 N GLN A 53 33.439 49.728 68.844 1.00 56.40 N ANISOU 47 N GLN A 53 10370 6122 4936 -2140 -66 -1397 N ATOM 48 CA GLN A 53 34.777 49.923 69.392 1.00 58.33 C ANISOU 48 CA GLN A 53 10877 6040 5245 -1894 -562 -1474 C ATOM 49 C GLN A 53 35.828 50.355 68.377 1.00 58.22 C ANISOU 49 C GLN A 53 10342 5933 5847 -1452 -817 -1484 C ATOM 50 O GLN A 53 36.869 50.878 68.795 1.00 53.87 O ANISOU 50 O GLN A 53 9822 5157 5487 -1212 -1132 -1621 O ATOM 51 CB GLN A 53 35.264 48.638 70.081 1.00 62.58 C ANISOU 51 CB GLN A 53 12217 6245 5315 -2080 -1044 -1372 C ATOM 52 CG GLN A 53 34.496 48.267 71.345 1.00 64.27 C ANISOU 52 CG GLN A 53 13127 6468 4823 -2565 -871 -1374 C ATOM 53 CD GLN A 53 34.993 49.011 72.570 1.00 70.19 C ANISOU 53 CD GLN A 53 14147 7093 5427 -2514 -985 -1521 C ATOM 54 OE1 GLN A 53 36.173 48.945 72.913 1.00 80.05 O ANISOU 54 OE1 GLN A 53 15513 8041 6862 -2207 -1508 -1482 O ATOM 55 NE2 GLN A 53 34.092 49.726 73.237 1.00 69.04 N ANISOU 55 NE2 GLN A 53 14011 7207 5013 -2788 -471 -1700 N ATOM 56 N ASN A 54 35.609 50.158 67.074 1.00 63.56 N ANISOU 56 N ASN A 54 10553 6770 6827 -1358 -687 -1363 N ATOM 57 CA ASN A 54 36.618 50.472 66.054 1.00 54.08 C ANISOU 57 CA ASN A 54 8896 5499 6151 -1011 -886 -1381 C ATOM 58 C ASN A 54 35.918 51.125 64.862 1.00 47.30 C ANISOU 58 C ASN A 54 7413 4949 5609 -963 -485 -1293 C ATOM 59 O ASN A 54 35.488 50.441 63.929 1.00 46.29 O ANISOU 59 O ASN A 54 7161 4948 5478 -1031 -406 -1153 O ATOM 60 CB ASN A 54 37.379 49.215 65.645 1.00 58.06 C ANISOU 60 CB ASN A 54 9628 5784 6649 -955 -1315 -1337 C ATOM 61 CG ASN A 54 38.482 49.496 64.644 1.00 63.71 C ANISOU 61 CG ASN A 54 9873 6437 7898 -639 -1482 -1431 C ATOM 62 OD1 ASN A 54 38.857 50.645 64.419 1.00 63.06 O ANISOU 62 OD1 ASN A 54 9384 6410 8164 -463 -1346 -1516 O ATOM 63 ND2 ASN A 54 39.017 48.438 64.043 1.00 75.47 N ANISOU 63 ND2 ASN A 54 11412 7802 9461 -586 -1773 -1438 N ATOM 64 N TRP A 55 35.826 52.454 64.891 1.00 48.30 N ANISOU 64 N TRP A 55 7169 5166 6018 -841 -281 -1379 N ATOM 65 CA TRP A 55 35.168 53.208 63.827 1.00 49.90 C ANISOU 65 CA TRP A 55 6822 5601 6538 -792 23 -1294 C ATOM 66 C TRP A 55 36.003 53.350 62.554 1.00 48.13 C ANISOU 66 C TRP A 55 6245 5355 6689 -593 -94 -1212 C ATOM 67 O TRP A 55 35.432 53.283 61.458 1.00 45.57 O ANISOU 67 O TRP A 55 5652 5207 6455 -633 70 -1063 O ATOM 68 CB TRP A 55 34.759 54.597 64.321 1.00 47.70 C ANISOU 68 CB TRP A 55 6280 5384 6459 -736 232 -1429 C ATOM 69 CG TRP A 55 33.383 54.651 64.919 1.00 47.70 C ANISOU 69 CG TRP A 55 6328 5571 6224 -978 564 -1509 C ATOM 70 CD1 TRP A 55 33.052 55.082 66.169 1.00 56.17 C ANISOU 70 CD1 TRP A 55 7596 6645 7102 -1090 691 -1724 C ATOM 71 CD2 TRP A 55 32.152 54.256 64.294 1.00 51.76 C ANISOU 71 CD2 TRP A 55 6672 6304 6691 -1155 829 -1424 C ATOM 72 NE1 TRP A 55 31.695 54.988 66.360 1.00 56.08 N ANISOU 72 NE1 TRP A 55 7516 6854 6936 -1343 1058 -1805 N ATOM 73 CE2 TRP A 55 31.120 54.482 65.225 1.00 52.98 C ANISOU 73 CE2 TRP A 55 6888 6586 6656 -1376 1132 -1624 C ATOM 74 CE3 TRP A 55 31.824 53.737 63.037 1.00 63.34 C ANISOU 74 CE3 TRP A 55 7933 7870 8264 -1154 838 -1226 C ATOM 75 CZ2 TRP A 55 29.784 54.202 64.943 1.00 60.43 C ANISOU 75 CZ2 TRP A 55 7656 7741 7565 -1590 1442 -1654 C ATOM 76 CZ3 TRP A 55 30.496 53.461 62.758 1.00 64.71 C ANISOU 76 CZ3 TRP A 55 7966 8238 8385 -1345 1102 -1223 C ATOM 77 CH2 TRP A 55 29.493 53.694 63.707 1.00 65.31 C ANISOU 77 CH2 TRP A 55 8068 8425 8322 -1557 1401 -1445 C ATOM 78 N PRO A 56 37.325 53.562 62.623 1.00 53.07 N ANISOU 78 N PRO A 56 6850 5774 7540 -399 -359 -1324 N ATOM 79 CA PRO A 56 38.097 53.657 61.371 1.00 54.24 C ANISOU 79 CA PRO A 56 6652 5934 8021 -276 -395 -1284 C ATOM 80 C PRO A 56 38.000 52.416 60.507 1.00 49.90 C ANISOU 80 C PRO A 56 6169 5465 7325 -363 -438 -1187 C ATOM 81 O PRO A 56 38.203 52.509 59.289 1.00 49.52 O ANISOU 81 O PRO A 56 5817 5533 7466 -343 -338 -1116 O ATOM 82 CB PRO A 56 39.537 53.901 61.852 1.00 53.48 C ANISOU 82 CB PRO A 56 6576 5570 8172 -83 -693 -1504 C ATOM 83 CG PRO A 56 39.542 53.547 63.295 1.00 54.15 C ANISOU 83 CG PRO A 56 7133 5471 7969 -106 -917 -1620 C ATOM 84 CD PRO A 56 38.173 53.879 63.786 1.00 59.47 C ANISOU 84 CD PRO A 56 7897 6337 8362 -287 -612 -1521 C ATOM 85 N ALA A 57 37.674 51.263 61.093 1.00 46.79 N ANISOU 85 N ALA A 57 6187 5010 6582 -482 -583 -1180 N ATOM 86 CA ALA A 57 37.452 50.061 60.303 1.00 43.01 C ANISOU 86 CA ALA A 57 5772 4603 5967 -571 -631 -1089 C ATOM 87 C ALA A 57 36.332 50.241 59.289 1.00 41.88 C ANISOU 87 C ALA A 57 5357 4750 5807 -686 -299 -895 C ATOM 88 O ALA A 57 36.307 49.530 58.282 1.00 40.86 O ANISOU 88 O ALA A 57 5137 4713 5673 -713 -306 -829 O ATOM 89 CB ALA A 57 37.139 48.881 61.221 1.00 43.88 C ANISOU 89 CB ALA A 57 6420 4572 5682 -724 -845 -1083 C ATOM 90 N LEU A 58 35.413 51.183 59.521 1.00 44.54 N ANISOU 90 N LEU A 58 5547 5214 6161 -741 -38 -832 N ATOM 91 CA LEU A 58 34.369 51.450 58.538 1.00 39.87 C ANISOU 91 CA LEU A 58 4674 4849 5627 -818 204 -674 C ATOM 92 C LEU A 58 34.965 51.830 57.188 1.00 40.85 C ANISOU 92 C LEU A 58 4486 5031 6004 -721 205 -596 C ATOM 93 O LEU A 58 34.338 51.606 56.147 1.00 35.88 O ANISOU 93 O LEU A 58 3722 4558 5352 -793 298 -452 O ATOM 94 CB LEU A 58 33.442 52.554 59.046 1.00 37.82 C ANISOU 94 CB LEU A 58 4248 4660 5462 -847 420 -697 C ATOM 95 CG LEU A 58 32.022 52.584 58.484 1.00 38.22 C ANISOU 95 CG LEU A 58 4106 4901 5515 -971 628 -603 C ATOM 96 CD1 LEU A 58 31.262 51.331 58.884 1.00 47.81 C ANISOU 96 CD1 LEU A 58 5605 6177 6381 -1185 686 -604 C ATOM 97 CD2 LEU A 58 31.290 53.827 58.959 1.00 44.91 C ANISOU 97 CD2 LEU A 58 4706 5775 6581 -947 789 -706 C ATOM 98 N SER A 59 36.186 52.371 57.180 1.00 41.94 N ANISOU 98 N SER A 59 4524 5041 6370 -584 102 -702 N ATOM 99 CA SER A 59 36.849 52.721 55.929 1.00 38.25 C ANISOU 99 CA SER A 59 3792 4635 6107 -556 149 -657 C ATOM 100 C SER A 59 37.121 51.508 55.046 1.00 38.94 C ANISOU 100 C SER A 59 3927 4802 6065 -613 92 -668 C ATOM 101 O SER A 59 37.545 51.683 53.898 1.00 43.25 O ANISOU 101 O SER A 59 4278 5447 6708 -647 182 -637 O ATOM 102 CB SER A 59 38.155 53.464 56.223 1.00 36.50 C ANISOU 102 CB SER A 59 3449 4244 6173 -426 68 -828 C ATOM 103 OG SER A 59 38.976 52.722 57.106 1.00 43.62 O ANISOU 103 OG SER A 59 4566 4957 7051 -334 -179 -1053 O ATOM 104 N ILE A 60 36.888 50.290 55.544 1.00 39.51 N ANISOU 104 N ILE A 60 4271 4830 5912 -645 -56 -721 N ATOM 105 CA ILE A 60 36.997 49.094 54.710 1.00 42.72 C ANISOU 105 CA ILE A 60 4714 5308 6208 -695 -130 -742 C ATOM 106 C ILE A 60 35.820 48.942 53.755 1.00 44.31 C ANISOU 106 C ILE A 60 4837 5738 6262 -826 47 -522 C ATOM 107 O ILE A 60 35.884 48.114 52.836 1.00 44.29 O ANISOU 107 O ILE A 60 4811 5832 6184 -871 21 -530 O ATOM 108 CB ILE A 60 37.157 47.852 55.613 1.00 39.23 C ANISOU 108 CB ILE A 60 4626 4683 5597 -691 -415 -862 C ATOM 109 CG1 ILE A 60 38.322 48.043 56.582 1.00 37.29 C ANISOU 109 CG1 ILE A 60 4485 4167 5517 -544 -667 -1090 C ATOM 110 CG2 ILE A 60 37.437 46.594 54.806 1.00 36.55 C ANISOU 110 CG2 ILE A 60 4303 4367 5215 -707 -557 -944 C ATOM 111 CD1 ILE A 60 38.561 46.851 57.482 1.00 38.66 C ANISOU 111 CD1 ILE A 60 5074 4091 5525 -543 -1043 -1197 C ATOM 112 N VAL A 61 34.759 49.745 53.911 1.00 43.37 N ANISOU 112 N VAL A 61 4650 5695 6135 -878 204 -361 N ATOM 113 CA VAL A 61 33.603 49.610 53.024 1.00 43.06 C ANISOU 113 CA VAL A 61 4523 5832 6005 -983 311 -181 C ATOM 114 C VAL A 61 34.008 49.781 51.566 1.00 47.54 C ANISOU 114 C VAL A 61 4925 6518 6621 -1004 351 -104 C ATOM 115 O VAL A 61 33.429 49.143 50.676 1.00 46.69 O ANISOU 115 O VAL A 61 4823 6541 6376 -1085 354 -14 O ATOM 116 CB VAL A 61 32.486 50.601 53.410 1.00 40.68 C ANISOU 116 CB VAL A 61 4103 5555 5797 -1006 437 -90 C ATOM 117 CG1 VAL A 61 31.912 50.252 54.777 1.00 40.92 C ANISOU 117 CG1 VAL A 61 4324 5525 5699 -1063 467 -193 C ATOM 118 CG2 VAL A 61 32.992 52.038 53.365 1.00 42.13 C ANISOU 118 CG2 VAL A 61 4096 5671 6242 -913 470 -72 C ATOM 119 N ILE A 62 35.016 50.617 51.297 1.00 56.05 N ANISOU 119 N ILE A 62 5872 7551 7871 -958 391 -149 N ATOM 120 CA ILE A 62 35.499 50.794 49.929 1.00 57.13 C ANISOU 120 CA ILE A 62 5896 7809 8001 -1045 474 -95 C ATOM 121 C ILE A 62 35.896 49.448 49.334 1.00 57.66 C ANISOU 121 C ILE A 62 6024 7968 7916 -1083 428 -240 C ATOM 122 O ILE A 62 35.463 49.083 48.233 1.00 58.68 O ANISOU 122 O ILE A 62 6154 8257 7884 -1190 473 -139 O ATOM 123 CB ILE A 62 36.673 51.789 49.901 1.00 44.09 C ANISOU 123 CB ILE A 62 4107 6075 6569 -1028 550 -180 C ATOM 124 CG1 ILE A 62 36.310 53.060 50.668 1.00 44.01 C ANISOU 124 CG1 ILE A 62 4039 5936 6747 -959 548 -78 C ATOM 125 CG2 ILE A 62 37.054 52.117 48.468 1.00 45.47 C ANISOU 125 CG2 ILE A 62 4205 6388 6683 -1199 694 -94 C ATOM 126 CD1 ILE A 62 37.432 54.068 50.747 1.00 46.35 C ANISOU 126 CD1 ILE A 62 4200 6120 7292 -940 604 -161 C ATOM 127 N ILE A 63 36.681 48.669 50.084 1.00 45.57 N ANISOU 127 N ILE A 63 4562 6312 6443 -986 291 -492 N ATOM 128 CA ILE A 63 37.086 47.343 49.626 1.00 40.15 C ANISOU 128 CA ILE A 63 3916 5664 5675 -992 184 -682 C ATOM 129 C ILE A 63 35.863 46.501 49.291 1.00 46.47 C ANISOU 129 C ILE A 63 4847 6570 6238 -1067 142 -518 C ATOM 130 O ILE A 63 35.857 45.751 48.306 1.00 51.39 O ANISOU 130 O ILE A 63 5444 7328 6755 -1129 144 -568 O ATOM 131 CB ILE A 63 37.968 46.664 50.689 1.00 36.54 C ANISOU 131 CB ILE A 63 3560 4972 5354 -852 -67 -964 C ATOM 132 CG1 ILE A 63 39.291 47.412 50.833 1.00 37.46 C ANISOU 132 CG1 ILE A 63 3482 4986 5763 -772 -36 -1196 C ATOM 133 CG2 ILE A 63 38.207 45.203 50.340 1.00 37.25 C ANISOU 133 CG2 ILE A 63 3716 5048 5390 -840 -260 -1161 C ATOM 134 CD1 ILE A 63 40.135 47.393 49.582 1.00 40.97 C ANISOU 134 CD1 ILE A 63 3673 5588 6304 -856 139 -1391 C ATOM 135 N ILE A 64 34.804 46.618 50.094 1.00 43.14 N ANISOU 135 N ILE A 64 4552 6097 5744 -1077 121 -351 N ATOM 136 CA ILE A 64 33.577 45.884 49.805 1.00 41.87 C ANISOU 136 CA ILE A 64 4477 6028 5403 -1167 104 -214 C ATOM 137 C ILE A 64 32.919 46.422 48.540 1.00 42.96 C ANISOU 137 C ILE A 64 4473 6352 5500 -1244 225 -29 C ATOM 138 O ILE A 64 32.531 45.654 47.650 1.00 44.79 O ANISOU 138 O ILE A 64 4719 6702 5596 -1306 189 -5 O ATOM 139 CB ILE A 64 32.624 45.937 51.011 1.00 40.62 C ANISOU 139 CB ILE A 64 4458 5778 5196 -1202 108 -137 C ATOM 140 CG1 ILE A 64 33.196 45.123 52.174 1.00 45.00 C ANISOU 140 CG1 ILE A 64 5277 6132 5690 -1178 -77 -290 C ATOM 141 CG2 ILE A 64 31.250 45.422 50.627 1.00 39.97 C ANISOU 141 CG2 ILE A 64 4384 5808 4997 -1317 147 -6 C ATOM 142 CD1 ILE A 64 33.500 45.941 53.411 1.00 42.59 C ANISOU 142 CD1 ILE A 64 5051 5681 5451 -1129 -63 -336 C ATOM 143 N ILE A 65 32.825 47.752 48.422 1.00 43.55 N ANISOU 143 N ILE A 65 4429 6428 5691 -1242 328 101 N ATOM 144 CA ILE A 65 32.099 48.349 47.301 1.00 43.10 C ANISOU 144 CA ILE A 65 4299 6482 5595 -1322 361 311 C ATOM 145 C ILE A 65 32.703 47.900 45.980 1.00 43.04 C ANISOU 145 C ILE A 65 4308 6622 5425 -1415 388 282 C ATOM 146 O ILE A 65 31.985 47.564 45.031 1.00 44.64 O ANISOU 146 O ILE A 65 4549 6936 5475 -1494 341 397 O ATOM 147 CB ILE A 65 32.091 49.885 47.422 1.00 42.26 C ANISOU 147 CB ILE A 65 4089 6294 5673 -1304 408 440 C ATOM 148 CG1 ILE A 65 31.283 50.325 48.643 1.00 42.05 C ANISOU 148 CG1 ILE A 65 4016 6155 5807 -1226 398 429 C ATOM 149 CG2 ILE A 65 31.527 50.519 46.158 1.00 37.83 C ANISOU 149 CG2 ILE A 65 3519 5796 5061 -1403 364 669 C ATOM 150 CD1 ILE A 65 31.225 51.823 48.820 1.00 38.25 C ANISOU 150 CD1 ILE A 65 3407 5567 5561 -1182 404 518 C ATOM 151 N MET A 66 34.032 47.868 45.908 1.00 41.93 N ANISOU 151 N MET A 66 4126 6482 5323 -1415 468 90 N ATOM 152 CA MET A 66 34.699 47.443 44.686 1.00 45.56 C ANISOU 152 CA MET A 66 4573 7106 5632 -1536 555 -16 C ATOM 153 C MET A 66 34.612 45.935 44.485 1.00 50.47 C ANISOU 153 C MET A 66 5240 7794 6141 -1510 448 -200 C ATOM 154 O MET A 66 34.584 45.468 43.340 1.00 53.89 O ANISOU 154 O MET A 66 5691 8399 6385 -1622 488 -229 O ATOM 155 CB MET A 66 36.155 47.903 44.714 1.00 47.46 C ANISOU 155 CB MET A 66 4693 7324 6014 -1558 704 -238 C ATOM 156 CG MET A 66 36.316 49.356 45.145 1.00 49.33 C ANISOU 156 CG MET A 66 4881 7443 6419 -1560 776 -81 C ATOM 157 SD MET A 66 38.031 49.904 45.165 1.00 41.20 S ANISOU 157 SD MET A 66 3676 6377 5602 -1610 967 -369 S ATOM 158 CE MET A 66 38.792 48.557 46.066 1.00 58.84 C ANISOU 158 CE MET A 66 5841 8508 8008 -1405 800 -799 C ATOM 159 N THR A 67 34.569 45.158 45.573 1.00 54.28 N ANISOU 159 N THR A 67 5772 8131 6720 -1382 293 -325 N ATOM 160 CA THR A 67 34.528 43.705 45.429 1.00 54.59 C ANISOU 160 CA THR A 67 5873 8183 6685 -1359 139 -500 C ATOM 161 C THR A 67 33.249 43.259 44.733 1.00 54.32 C ANISOU 161 C THR A 67 5908 8269 6462 -1437 97 -303 C ATOM 162 O THR A 67 33.281 42.401 43.843 1.00 59.66 O ANISOU 162 O THR A 67 6585 9067 7018 -1481 55 -415 O ATOM 163 CB THR A 67 34.662 43.032 46.795 1.00 49.43 C ANISOU 163 CB THR A 67 5342 7298 6143 -1244 -66 -614 C ATOM 164 OG1 THR A 67 35.937 43.358 47.361 1.00 43.32 O ANISOU 164 OG1 THR A 67 4497 6389 5574 -1150 -90 -846 O ATOM 165 CG2 THR A 67 34.549 41.522 46.659 1.00 55.31 C ANISOU 165 CG2 THR A 67 6183 8008 6826 -1233 -281 -766 C ATOM 166 N ILE A 68 32.115 43.841 45.117 1.00 46.32 N ANISOU 166 N ILE A 68 4928 7218 5453 -1450 99 -49 N ATOM 167 CA ILE A 68 30.864 43.563 44.421 1.00 46.31 C ANISOU 167 CA ILE A 68 4949 7310 5336 -1516 42 118 C ATOM 168 C ILE A 68 30.921 44.106 42.999 1.00 50.85 C ANISOU 168 C ILE A 68 5507 8048 5767 -1612 99 220 C ATOM 169 O ILE A 68 30.884 43.348 42.021 1.00 54.57 O ANISOU 169 O ILE A 68 6017 8651 6065 -1673 54 154 O ATOM 170 CB ILE A 68 29.678 44.157 45.199 1.00 41.35 C ANISOU 170 CB ILE A 68 4299 6590 4824 -1508 40 292 C ATOM 171 CG1 ILE A 68 29.653 43.617 46.628 1.00 39.22 C ANISOU 171 CG1 ILE A 68 4115 6173 4615 -1480 21 191 C ATOM 172 CG2 ILE A 68 28.368 43.863 44.487 1.00 47.40 C ANISOU 172 CG2 ILE A 68 5041 7424 5544 -1562 -51 414 C ATOM 173 CD1 ILE A 68 28.671 44.333 47.525 1.00 35.83 C ANISOU 173 CD1 ILE A 68 3636 5672 4305 -1500 100 282 C ATOM 174 N GLY A 69 31.072 45.428 42.873 1.00 49.64 N ANISOU 174 N GLY A 69 5325 7873 5663 -1646 187 375 N ATOM 175 CA GLY A 69 30.898 46.081 41.584 1.00 49.82 C ANISOU 175 CA GLY A 69 5417 8000 5513 -1781 192 552 C ATOM 176 C GLY A 69 31.773 45.498 40.497 1.00 48.83 C ANISOU 176 C GLY A 69 5349 8062 5142 -1912 298 388 C ATOM 177 O GLY A 69 31.293 45.176 39.407 1.00 53.90 O ANISOU 177 O GLY A 69 6103 8827 5550 -2017 228 461 O ATOM 178 N GLY A 70 33.061 45.308 40.795 1.00 48.83 N ANISOU 178 N GLY A 70 5259 8083 5210 -1906 458 121 N ATOM 179 CA GLY A 70 33.958 44.743 39.801 1.00 53.28 C ANISOU 179 CA GLY A 70 5815 8840 5588 -2043 603 -132 C ATOM 180 C GLY A 70 33.468 43.405 39.294 1.00 58.01 C ANISOU 180 C GLY A 70 6449 9540 6053 -2017 465 -263 C ATOM 181 O GLY A 70 33.365 43.183 38.084 1.00 58.22 O ANISOU 181 O GLY A 70 6573 9752 5798 -2175 508 -269 O ATOM 182 N ASN A 71 33.084 42.520 40.216 1.00 54.46 N ANISOU 182 N ASN A 71 5956 8956 5781 -1839 281 -345 N ATOM 183 CA ASN A 71 32.549 41.232 39.797 1.00 50.01 C ANISOU 183 CA ASN A 71 5426 8451 5124 -1814 116 -455 C ATOM 184 C ASN A 71 31.245 41.413 39.036 1.00 49.17 C ANISOU 184 C ASN A 71 5441 8410 4833 -1885 9 -162 C ATOM 185 O ASN A 71 31.003 40.720 38.040 1.00 55.26 O ANISOU 185 O ASN A 71 6269 9323 5404 -1953 -52 -236 O ATOM 186 CB ASN A 71 32.365 40.318 41.004 1.00 47.83 C ANISOU 186 CB ASN A 71 5136 7974 5063 -1654 -76 -555 C ATOM 187 CG ASN A 71 33.684 39.842 41.571 1.00 44.41 C ANISOU 187 CG ASN A 71 4609 7448 4818 -1566 -89 -913 C ATOM 188 OD1 ASN A 71 34.369 39.012 40.970 1.00 43.10 O ANISOU 188 OD1 ASN A 71 4360 7364 4651 -1566 -114 -1242 O ATOM 189 ND2 ASN A 71 34.052 40.367 42.732 1.00 44.30 N ANISOU 189 ND2 ASN A 71 4593 7248 4992 -1481 -97 -887 N ATOM 190 N ILE A 72 30.411 42.361 39.471 1.00 46.69 N ANISOU 190 N ILE A 72 5153 7980 4607 -1865 -37 138 N ATOM 191 CA ILE A 72 29.214 42.692 38.704 1.00 49.24 C ANISOU 191 CA ILE A 72 5569 8324 4818 -1920 -190 391 C ATOM 192 C ILE A 72 29.597 43.067 37.282 1.00 55.61 C ANISOU 192 C ILE A 72 6533 9302 5294 -2107 -133 441 C ATOM 193 O ILE A 72 28.970 42.618 36.313 1.00 63.62 O ANISOU 193 O ILE A 72 7666 10406 6101 -2171 -280 484 O ATOM 194 CB ILE A 72 28.423 43.819 39.393 1.00 50.95 C ANISOU 194 CB ILE A 72 5741 8368 5250 -1864 -251 639 C ATOM 195 CG1 ILE A 72 27.698 43.291 40.633 1.00 49.91 C ANISOU 195 CG1 ILE A 72 5490 8103 5369 -1742 -305 584 C ATOM 196 CG2 ILE A 72 27.441 44.465 38.419 1.00 51.39 C ANISOU 196 CG2 ILE A 72 5902 8409 5215 -1930 -451 887 C ATOM 197 CD1 ILE A 72 26.755 44.300 41.259 1.00 49.90 C ANISOU 197 CD1 ILE A 72 5394 7957 5610 -1694 -355 749 C ATOM 198 N LEU A 73 30.654 43.871 37.134 1.00 53.72 N ANISOU 198 N LEU A 73 6317 9111 4982 -2224 90 421 N ATOM 199 CA LEU A 73 31.095 44.262 35.802 1.00 50.75 C ANISOU 199 CA LEU A 73 6140 8908 4235 -2479 202 464 C ATOM 200 C LEU A 73 31.484 43.049 34.972 1.00 52.21 C ANISOU 200 C LEU A 73 6337 9315 4184 -2555 268 155 C ATOM 201 O LEU A 73 31.270 43.037 33.755 1.00 55.03 O ANISOU 201 O LEU A 73 6916 9820 4173 -2749 246 222 O ATOM 202 CB LEU A 73 32.257 45.249 35.904 1.00 51.67 C ANISOU 202 CB LEU A 73 6243 9036 4352 -2622 485 442 C ATOM 203 CG LEU A 73 31.899 46.635 36.446 1.00 51.17 C ANISOU 203 CG LEU A 73 6216 8758 4466 -2598 405 773 C ATOM 204 CD1 LEU A 73 33.096 47.569 36.372 1.00 52.66 C ANISOU 204 CD1 LEU A 73 6414 8969 4624 -2786 692 745 C ATOM 205 CD2 LEU A 73 30.710 47.217 35.695 1.00 52.97 C ANISOU 205 CD2 LEU A 73 6688 8899 4539 -2668 106 1138 C ATOM 206 N VAL A 74 32.038 42.014 35.607 1.00 50.67 N ANISOU 206 N VAL A 74 5928 9129 4196 -2406 313 -194 N ATOM 207 CA VAL A 74 32.285 40.766 34.893 1.00 52.06 C ANISOU 207 CA VAL A 74 6076 9480 4226 -2433 310 -524 C ATOM 208 C VAL A 74 30.964 40.106 34.521 1.00 52.52 C ANISOU 208 C VAL A 74 6238 9513 4204 -2363 5 -369 C ATOM 209 O VAL A 74 30.758 39.693 33.373 1.00 58.38 O ANISOU 209 O VAL A 74 7118 10427 4635 -2490 -32 -426 O ATOM 210 CB VAL A 74 33.169 39.829 35.736 1.00 50.78 C ANISOU 210 CB VAL A 74 5661 9257 4376 -2265 335 -939 C ATOM 211 CG1 VAL A 74 33.379 38.506 35.015 1.00 52.68 C ANISOU 211 CG1 VAL A 74 5843 9648 4526 -2267 281 -1316 C ATOM 212 CG2 VAL A 74 34.504 40.492 36.044 1.00 51.90 C ANISOU 212 CG2 VAL A 74 5664 9414 4640 -2330 619 -1144 C ATOM 213 N ILE A 75 30.038 40.029 35.481 1.00 56.37 N ANISOU 213 N ILE A 75 6663 9789 4968 -2180 -205 -187 N ATOM 214 CA ILE A 75 28.741 39.404 35.232 1.00 56.04 C ANISOU 214 CA ILE A 75 6668 9698 4929 -2114 -486 -70 C ATOM 215 C ILE A 75 27.967 40.185 34.180 1.00 58.51 C ANISOU 215 C ILE A 75 7194 10050 4988 -2241 -617 217 C ATOM 216 O ILE A 75 27.303 39.601 33.314 1.00 62.23 O ANISOU 216 O ILE A 75 7768 10588 5288 -2269 -811 212 O ATOM 217 CB ILE A 75 27.952 39.281 36.548 1.00 49.94 C ANISOU 217 CB ILE A 75 5769 8696 4510 -1950 -610 37 C ATOM 218 CG1 ILE A 75 28.704 38.377 37.527 1.00 47.21 C ANISOU 218 CG1 ILE A 75 5307 8274 4358 -1850 -564 -232 C ATOM 219 CG2 ILE A 75 26.549 38.754 36.287 1.00 53.36 C ANISOU 219 CG2 ILE A 75 6211 9070 4992 -1911 -871 145 C ATOM 220 CD1 ILE A 75 28.251 38.517 38.958 1.00 49.04 C ANISOU 220 CD1 ILE A 75 5482 8289 4862 -1759 -593 -122 C ATOM 221 N MET A 76 28.033 41.517 34.240 1.00 55.27 N ANISOU 221 N MET A 76 6872 9567 4563 -2315 -560 471 N ATOM 222 CA MET A 76 27.432 42.331 33.190 1.00 57.98 C ANISOU 222 CA MET A 76 7484 9901 4644 -2461 -741 754 C ATOM 223 C MET A 76 28.107 42.099 31.846 1.00 65.63 C ANISOU 223 C MET A 76 8703 11118 5115 -2713 -618 647 C ATOM 224 O MET A 76 27.454 42.199 30.802 1.00 73.77 O ANISOU 224 O MET A 76 10006 12169 5854 -2827 -852 807 O ATOM 225 CB MET A 76 27.497 43.814 33.560 1.00 57.08 C ANISOU 225 CB MET A 76 7425 9627 4635 -2503 -723 1032 C ATOM 226 CG MET A 76 26.420 44.270 34.529 1.00 63.71 C ANISOU 226 CG MET A 76 8085 10214 5910 -2295 -943 1186 C ATOM 227 SD MET A 76 26.496 46.043 34.854 1.00 69.69 S ANISOU 227 SD MET A 76 8904 10764 6813 -2336 -975 1480 S ATOM 228 CE MET A 76 25.015 46.270 35.837 1.00 92.05 C ANISOU 228 CE MET A 76 11461 13337 10176 -2083 -1257 1530 C ATOM 229 N ALA A 77 29.404 41.782 31.845 1.00 63.21 N ANISOU 229 N ALA A 77 8309 10996 4712 -2812 -261 344 N ATOM 230 CA ALA A 77 30.132 41.647 30.587 1.00 64.13 C ANISOU 230 CA ALA A 77 8642 11380 4344 -3107 -54 182 C ATOM 231 C ALA A 77 29.826 40.317 29.909 1.00 73.14 C ANISOU 231 C ALA A 77 9779 12677 5334 -3071 -173 -85 C ATOM 232 O ALA A 77 29.223 40.282 28.830 1.00 90.35 O ANISOU 232 O ALA A 77 12255 14929 7146 -3211 -357 41 O ATOM 233 CB ALA A 77 31.636 41.794 30.832 1.00 68.85 C ANISOU 233 CB ALA A 77 9078 12119 4963 -3233 392 -127 C ATOM 234 N VAL A 78 30.190 39.209 30.560 1.00 65.73 N ANISOU 234 N VAL A 78 8525 11753 4695 -2873 -126 -447 N ATOM 235 CA VAL A 78 29.993 37.874 30.012 1.00 67.79 C ANISOU 235 CA VAL A 78 8736 12138 4883 -2816 -249 -752 C ATOM 236 C VAL A 78 28.537 37.599 29.652 1.00 72.14 C ANISOU 236 C VAL A 78 9431 12578 5401 -2724 -660 -495 C ATOM 237 O VAL A 78 28.244 36.607 28.977 1.00 77.30 O ANISOU 237 O VAL A 78 10108 13338 5925 -2711 -799 -699 O ATOM 238 CB VAL A 78 30.529 36.826 31.015 1.00 64.88 C ANISOU 238 CB VAL A 78 8015 11692 4946 -2583 -233 -1118 C ATOM 239 CG1 VAL A 78 30.672 35.461 30.362 1.00 72.77 C ANISOU 239 CG1 VAL A 78 8934 12840 5876 -2557 -307 -1535 C ATOM 240 CG2 VAL A 78 31.863 37.280 31.585 1.00 61.82 C ANISOU 240 CG2 VAL A 78 7454 11328 4706 -2624 98 -1335 C ATOM 241 N SER A 79 27.616 38.464 30.071 1.00 67.43 N ANISOU 241 N SER A 79 8907 11760 4955 -2654 -870 -90 N ATOM 242 CA SER A 79 26.221 38.382 29.663 1.00 68.07 C ANISOU 242 CA SER A 79 9108 11712 5045 -2581 -1279 136 C ATOM 243 C SER A 79 25.893 39.326 28.511 1.00 78.46 C ANISOU 243 C SER A 79 10831 13047 5935 -2799 -1434 424 C ATOM 244 O SER A 79 25.279 38.906 27.526 1.00 80.48 O ANISOU 244 O SER A 79 11296 13352 5930 -2852 -1697 428 O ATOM 245 CB SER A 79 25.309 38.678 30.858 1.00 72.60 C ANISOU 245 CB SER A 79 9464 12005 6117 -2363 -1451 332 C ATOM 246 OG SER A 79 25.590 37.802 31.935 1.00 73.68 O ANISOU 246 OG SER A 79 9312 12098 6585 -2208 -1333 104 O ATOM 247 N MET A 80 26.297 40.596 28.606 1.00 80.23 N ANISOU 247 N MET A 80 11204 13209 6072 -2939 -1311 669 N ATOM 248 CA MET A 80 25.882 41.587 27.618 1.00 85.96 C ANISOU 248 CA MET A 80 12371 13864 6426 -3151 -1551 1010 C ATOM 249 C MET A 80 26.813 41.682 26.417 1.00 96.70 C ANISOU 249 C MET A 80 14109 15501 7130 -3534 -1291 929 C ATOM 250 O MET A 80 26.419 42.257 25.396 1.00107.72 O ANISOU 250 O MET A 80 15923 16791 8216 -3699 -1510 1171 O ATOM 251 CB MET A 80 25.762 42.974 28.259 1.00 80.14 C ANISOU 251 CB MET A 80 11650 12876 5924 -3136 -1611 1343 C ATOM 252 CG MET A 80 24.566 43.158 29.177 1.00 86.78 C ANISOU 252 CG MET A 80 12215 13416 7342 -2823 -1951 1470 C ATOM 253 SD MET A 80 24.427 44.861 29.758 1.00 80.13 S ANISOU 253 SD MET A 80 11414 12275 6755 -2821 -2066 1823 S ATOM 254 CE MET A 80 22.906 44.784 30.705 1.00106.13 C ANISOU 254 CE MET A 80 14318 15274 10732 -2464 -2442 1820 C ATOM 255 N GLU A 81 28.027 41.145 26.506 1.00115.16 N ANISOU 255 N GLU A 81 16270 18106 9380 -3636 -812 553 N ATOM 256 CA GLU A 81 28.962 41.140 25.387 1.00125.37 C ANISOU 256 CA GLU A 81 17802 19618 10216 -3962 -463 364 C ATOM 257 C GLU A 81 28.944 39.762 24.739 1.00120.17 C ANISOU 257 C GLU A 81 17056 19150 9452 -3902 -457 -32 C ATOM 258 O GLU A 81 29.249 38.760 25.395 1.00123.48 O ANISOU 258 O GLU A 81 17098 19700 10120 -3725 -362 -403 O ATOM 259 CB GLU A 81 30.377 41.501 25.838 1.00128.80 C ANISOU 259 CB GLU A 81 18041 20202 10696 -4123 76 135 C ATOM 260 CG GLU A 81 30.521 42.910 26.386 1.00129.72 C ANISOU 260 CG GLU A 81 18254 20121 10914 -4205 107 508 C ATOM 261 CD GLU A 81 29.964 43.969 25.450 1.00148.75 C ANISOU 261 CD GLU A 81 21158 22302 13058 -4398 -154 944 C ATOM 262 OE1 GLU A 81 30.324 43.960 24.254 1.00147.44 O ANISOU 262 OE1 GLU A 81 21283 22221 12518 -4665 -18 868 O ATOM 263 OE2 GLU A 81 29.159 44.807 25.911 1.00140.57 O ANISOU 263 OE2 GLU A 81 20218 20990 12201 -4284 -519 1345 O ATOM 264 N LYS A 82 28.586 39.716 23.454 1.00113.83 N ANISOU 264 N LYS A 82 16616 18340 8296 -4043 -587 39 N ATOM 265 CA LYS A 82 28.508 38.440 22.752 1.00119.45 C ANISOU 265 CA LYS A 82 17271 19219 8896 -3983 -608 -323 C ATOM 266 C LYS A 82 29.877 37.792 22.595 1.00110.86 C ANISOU 266 C LYS A 82 15932 18432 7758 -4124 -78 -858 C ATOM 267 O LYS A 82 29.971 36.563 22.503 1.00115.06 O ANISOU 267 O LYS A 82 16221 19098 8399 -3979 -75 -1266 O ATOM 268 CB LYS A 82 27.854 38.633 21.384 1.00135.64 C ANISOU 268 CB LYS A 82 19802 21189 10545 -4119 -863 -119 C ATOM 269 CG LYS A 82 26.380 38.999 21.442 1.00140.08 C ANISOU 269 CG LYS A 82 20541 21429 11254 -3910 -1478 293 C ATOM 270 CD LYS A 82 25.829 39.266 20.050 1.00149.63 C ANISOU 270 CD LYS A 82 22257 22540 12058 -4057 -1744 476 C ATOM 271 CE LYS A 82 24.322 39.460 20.076 1.00146.77 C ANISOU 271 CE LYS A 82 21992 21841 11935 -3798 -2400 782 C ATOM 272 NZ LYS A 82 23.612 38.222 20.500 1.00149.75 N ANISOU 272 NZ LYS A 82 22003 22238 12658 -3466 -2628 537 N ATOM 273 N LYS A 83 30.943 38.589 22.569 1.00104.38 N ANISOU 273 N LYS A 83 15134 17691 6836 -4393 348 -893 N ATOM 274 CA LYS A 83 32.294 38.072 22.391 1.00103.53 C ANISOU 274 CA LYS A 83 14741 17845 6752 -4545 857 -1442 C ATOM 275 C LYS A 83 32.864 37.447 23.658 1.00102.92 C ANISOU 275 C LYS A 83 14124 17813 7168 -4289 973 -1813 C ATOM 276 O LYS A 83 34.069 37.174 23.709 1.00 99.29 O ANISOU 276 O LYS A 83 13361 17513 6851 -4385 1374 -2283 O ATOM 277 CB LYS A 83 33.220 39.187 21.897 1.00103.44 C ANISOU 277 CB LYS A 83 14929 17867 6505 -4944 1253 -1361 C ATOM 278 CG LYS A 83 32.808 39.776 20.560 1.00100.47 C ANISOU 278 CG LYS A 83 15124 17442 5608 -5247 1154 -1048 C ATOM 279 CD LYS A 83 33.730 40.906 20.138 1.00104.83 C ANISOU 279 CD LYS A 83 15883 17997 5949 -5664 1525 -962 C ATOM 280 CE LYS A 83 33.295 41.493 18.806 1.00111.19 C ANISOU 280 CE LYS A 83 17308 18728 6210 -5987 1383 -641 C ATOM 281 NZ LYS A 83 34.151 42.638 18.393 1.00115.93 N ANISOU 281 NZ LYS A 83 18153 19303 6591 -6426 1711 -533 N ATOM 282 N LEU A 84 32.034 37.220 24.677 1.00101.31 N ANISOU 282 N LEU A 84 13789 17450 7255 -3973 608 -1634 N ATOM 283 CA LEU A 84 32.462 36.585 25.917 1.00 95.49 C ANISOU 283 CA LEU A 84 12597 16706 6978 -3716 628 -1964 C ATOM 284 C LEU A 84 31.654 35.329 26.220 1.00100.93 C ANISOU 284 C LEU A 84 13119 17315 7914 -3402 225 -2103 C ATOM 285 O LEU A 84 31.579 34.908 27.377 1.00 96.10 O ANISOU 285 O LEU A 84 12207 16480 7828 -3099 69 -2136 O ATOM 286 CB LEU A 84 32.365 37.572 27.081 1.00 86.48 C ANISOU 286 CB LEU A 84 11401 15339 6119 -3610 591 -1596 C ATOM 287 CG LEU A 84 33.228 38.826 26.953 1.00 83.64 C ANISOU 287 CG LEU A 84 11173 15058 5548 -3926 984 -1486 C ATOM 288 CD1 LEU A 84 32.897 39.814 28.055 1.00 86.33 C ANISOU 288 CD1 LEU A 84 11473 15089 6238 -3756 848 -1048 C ATOM 289 CD2 LEU A 84 34.703 38.459 26.982 1.00 76.66 C ANISOU 289 CD2 LEU A 84 9946 14349 4832 -4018 1438 -2079 C ATOM 290 N HIS A 85 31.039 34.725 25.207 1.00 99.35 N ANISOU 290 N HIS A 85 13097 17148 7505 -3408 43 -2111 N ATOM 291 CA HIS A 85 30.210 33.535 25.387 1.00100.94 C ANISOU 291 CA HIS A 85 13155 17233 7963 -3121 -351 -2215 C ATOM 292 C HIS A 85 31.036 32.311 25.006 1.00 99.43 C ANISOU 292 C HIS A 85 12689 17169 7920 -3056 -198 -2822 C ATOM 293 O HIS A 85 31.173 31.980 23.826 1.00101.37 O ANISOU 293 O HIS A 85 13073 17572 7870 -3194 -92 -2998 O ATOM 294 CB HIS A 85 28.931 33.636 24.562 1.00 97.53 C ANISOU 294 CB HIS A 85 13073 16709 7277 -3125 -707 -1847 C ATOM 295 CG HIS A 85 27.988 34.694 25.043 1.00 87.91 C ANISOU 295 CG HIS A 85 12042 15287 6075 -3109 -966 -1290 C ATOM 296 ND1 HIS A 85 26.850 35.049 24.352 1.00 91.55 N ANISOU 296 ND1 HIS A 85 12820 15601 6364 -3109 -1322 -932 N ATOM 297 CD2 HIS A 85 28.014 35.473 26.150 1.00 87.32 C ANISOU 297 CD2 HIS A 85 11848 15070 6258 -3050 -935 -1048 C ATOM 298 CE1 HIS A 85 26.216 36.002 25.012 1.00 93.53 C ANISOU 298 CE1 HIS A 85 13123 15654 6761 -3070 -1516 -520 C ATOM 299 NE2 HIS A 85 26.902 36.278 26.107 1.00 85.45 N ANISOU 299 NE2 HIS A 85 11835 14623 6010 -3025 -1262 -570 N ATOM 300 N ASN A 86 31.585 31.645 26.014 1.00107.48 N ANISOU 300 N ASN A 86 13325 18085 9427 -2837 -218 -3139 N ATOM 301 CA ASN A 86 32.367 30.425 25.840 1.00 98.62 C ANISOU 301 CA ASN A 86 11884 16988 8601 -2702 -161 -3717 C ATOM 302 C ASN A 86 32.500 29.768 27.209 1.00101.63 C ANISOU 302 C ASN A 86 11959 17067 9589 -2384 -406 -3825 C ATOM 303 O ASN A 86 32.040 30.304 28.223 1.00 93.89 O ANISOU 303 O ASN A 86 11019 15914 8741 -2316 -555 -3479 O ATOM 304 CB ASN A 86 33.731 30.716 25.210 1.00 94.44 C ANISOU 304 CB ASN A 86 11226 16720 7938 -2946 346 -4132 C ATOM 305 CG ASN A 86 34.399 31.935 25.808 1.00100.57 C ANISOU 305 CG ASN A 86 11995 17531 8684 -3115 650 -4004 C ATOM 306 OD1 ASN A 86 35.113 31.839 26.806 1.00108.68 O ANISOU 306 OD1 ASN A 86 12708 18438 10148 -2962 681 -4241 O ATOM 307 ND2 ASN A 86 34.168 33.092 25.200 1.00 93.76 N ANISOU 307 ND2 ASN A 86 11503 16784 7337 -3421 838 -3608 N ATOM 308 N ALA A 87 33.136 28.595 27.230 1.00112.23 N ANISOU 308 N ALA A 87 16008 16052 10581 -976 -720 -523 N ATOM 309 CA ALA A 87 33.238 27.827 28.467 1.00108.91 C ANISOU 309 CA ALA A 87 15484 15426 10472 -1085 -728 -642 C ATOM 310 C ALA A 87 34.036 28.580 29.525 1.00108.26 C ANISOU 310 C ALA A 87 15227 15252 10653 -1126 -531 -452 C ATOM 311 O ALA A 87 33.584 28.734 30.666 1.00106.71 O ANISOU 311 O ALA A 87 14887 14920 10737 -1244 -595 -417 O ATOM 312 CB ALA A 87 33.868 26.463 28.186 1.00109.87 C ANISOU 312 CB ALA A 87 15747 15499 10501 -1020 -685 -892 C ATOM 313 N THR A 88 35.228 29.062 29.162 1.00 98.29 N ANISOU 313 N THR A 88 13973 14068 9303 -1030 -288 -328 N ATOM 314 CA THR A 88 36.095 29.716 30.139 1.00 95.80 C ANISOU 314 CA THR A 88 13491 13669 9241 -1076 -105 -169 C ATOM 315 C THR A 88 35.480 31.009 30.662 1.00 90.80 C ANISOU 315 C THR A 88 12734 13005 8762 -1163 -155 46 C ATOM 316 O THR A 88 35.561 31.300 31.860 1.00 92.49 O ANISOU 316 O THR A 88 12800 13082 9259 -1256 -139 97 O ATOM 317 CB THR A 88 37.469 29.987 29.528 1.00 92.58 C ANISOU 317 CB THR A 88 13105 13370 8702 -963 163 -75 C ATOM 318 OG1 THR A 88 37.312 30.678 28.283 1.00 94.00 O ANISOU 318 OG1 THR A 88 13397 13728 8590 -878 195 51 O ATOM 319 CG2 THR A 88 38.212 28.681 29.292 1.00 86.98 C ANISOU 319 CG2 THR A 88 12486 12658 7904 -867 239 -291 C ATOM 320 N ASN A 89 34.856 31.797 29.787 1.00 86.96 N ANISOU 320 N ASN A 89 12313 12641 8087 -1123 -218 171 N ATOM 321 CA ASN A 89 34.261 33.047 30.247 1.00 83.15 C ANISOU 321 CA ASN A 89 11726 12119 7750 -1185 -262 377 C ATOM 322 C ASN A 89 32.997 32.810 31.066 1.00 80.45 C ANISOU 322 C ASN A 89 11303 11676 7589 -1283 -492 291 C ATOM 323 O ASN A 89 32.700 33.590 31.976 1.00 75.89 O ANISOU 323 O ASN A 89 10597 11000 7238 -1353 -501 411 O ATOM 324 CB ASN A 89 33.983 33.964 29.061 1.00 83.99 C ANISOU 324 CB ASN A 89 11934 12383 7597 -1094 -258 552 C ATOM 325 CG ASN A 89 35.239 34.630 28.539 1.00 90.89 C ANISOU 325 CG ASN A 89 12831 13325 8379 -1029 14 731 C ATOM 326 OD1 ASN A 89 35.518 35.787 28.853 1.00 94.18 O ANISOU 326 OD1 ASN A 89 13167 13688 8927 -1066 122 953 O ATOM 327 ND2 ASN A 89 36.014 33.896 27.750 1.00104.09 N ANISOU 327 ND2 ASN A 89 14612 15107 9831 -934 133 633 N ATOM 328 N TYR A 90 32.246 31.745 30.779 1.00 84.99 N ANISOU 328 N TYR A 90 11947 12271 8075 -1294 -676 83 N ATOM 329 CA TYR A 90 31.136 31.388 31.659 1.00 81.18 C ANISOU 329 CA TYR A 90 11362 11683 7798 -1405 -868 -3 C ATOM 330 C TYR A 90 31.644 30.921 33.021 1.00 75.31 C ANISOU 330 C TYR A 90 10511 10762 7341 -1489 -784 -60 C ATOM 331 O TYR A 90 31.038 31.225 34.059 1.00 74.05 O ANISOU 331 O TYR A 90 10222 10503 7411 -1574 -844 -14 O ATOM 332 CB TYR A 90 30.261 30.324 30.997 1.00 79.34 C ANISOU 332 CB TYR A 90 11225 11506 7415 -1415 -1084 -217 C ATOM 333 CG TYR A 90 29.226 30.899 30.051 1.00 83.41 C ANISOU 333 CG TYR A 90 11778 12179 7733 -1370 -1262 -153 C ATOM 334 CD1 TYR A 90 28.475 32.012 30.408 1.00 85.53 C ANISOU 334 CD1 TYR A 90 11925 12457 8114 -1387 -1322 35 C ATOM 335 CD2 TYR A 90 29.005 30.335 28.802 1.00 93.03 C ANISOU 335 CD2 TYR A 90 13161 13540 8647 -1297 -1376 -284 C ATOM 336 CE1 TYR A 90 27.529 32.544 29.549 1.00 90.40 C ANISOU 336 CE1 TYR A 90 12570 13225 8552 -1327 -1493 103 C ATOM 337 CE2 TYR A 90 28.062 30.861 27.935 1.00102.43 C ANISOU 337 CE2 TYR A 90 14385 14891 9644 -1245 -1556 -224 C ATOM 338 CZ TYR A 90 27.327 31.965 28.314 1.00101.31 C ANISOU 338 CZ TYR A 90 14109 14760 9627 -1258 -1615 -24 C ATOM 339 OH TYR A 90 26.387 32.490 27.455 1.00102.73 O ANISOU 339 OH TYR A 90 14315 15104 9614 -1189 -1802 45 O ATOM 340 N PHE A 91 32.763 30.189 33.037 1.00 77.67 N ANISOU 340 N PHE A 91 10863 11027 7621 -1451 -640 -155 N ATOM 341 CA PHE A 91 33.439 29.891 34.296 1.00 79.78 C ANISOU 341 CA PHE A 91 11028 11143 8140 -1504 -538 -174 C ATOM 342 C PHE A 91 33.775 31.172 35.045 1.00 77.75 C ANISOU 342 C PHE A 91 10638 10848 8055 -1534 -433 34 C ATOM 343 O PHE A 91 33.587 31.263 36.263 1.00 73.41 O ANISOU 343 O PHE A 91 9977 10175 7741 -1610 -453 47 O ATOM 344 CB PHE A 91 34.721 29.099 34.041 1.00 86.59 C ANISOU 344 CB PHE A 91 11962 12007 8930 -1424 -379 -273 C ATOM 345 CG PHE A 91 34.515 27.625 33.886 1.00 92.74 C ANISOU 345 CG PHE A 91 12851 12728 9659 -1417 -472 -513 C ATOM 346 CD1 PHE A 91 33.925 26.883 34.894 1.00 93.78 C ANISOU 346 CD1 PHE A 91 12934 12702 9997 -1515 -584 -614 C ATOM 347 CD2 PHE A 91 34.953 26.974 32.747 1.00 93.69 C ANISOU 347 CD2 PHE A 91 13133 12941 9526 -1308 -435 -635 C ATOM 348 CE1 PHE A 91 33.751 25.522 34.753 1.00 97.08 C ANISOU 348 CE1 PHE A 91 13464 13038 10384 -1519 -665 -830 C ATOM 349 CE2 PHE A 91 34.783 25.617 32.600 1.00 97.23 C ANISOU 349 CE2 PHE A 91 13700 13310 9934 -1299 -523 -869 C ATOM 350 CZ PHE A 91 34.184 24.890 33.603 1.00 98.59 C ANISOU 350 CZ PHE A 91 13823 13306 10330 -1412 -640 -964 C ATOM 351 N LEU A 92 34.304 32.166 34.329 1.00 76.90 N ANISOU 351 N LEU A 92 10552 10839 7829 -1474 -315 198 N ATOM 352 CA LEU A 92 34.665 33.430 34.963 1.00 67.28 C ANISOU 352 CA LEU A 92 9221 9566 6774 -1511 -215 394 C ATOM 353 C LEU A 92 33.440 34.171 35.478 1.00 62.96 C ANISOU 353 C LEU A 92 8610 8968 6343 -1565 -361 474 C ATOM 354 O LEU A 92 33.520 34.848 36.505 1.00 57.17 O ANISOU 354 O LEU A 92 7772 8126 5824 -1619 -327 555 O ATOM 355 CB LEU A 92 35.448 34.311 33.990 1.00 67.36 C ANISOU 355 CB LEU A 92 9279 9685 6629 -1444 -52 564 C ATOM 356 CG LEU A 92 36.774 33.749 33.477 1.00 62.67 C ANISOU 356 CG LEU A 92 8723 9161 5929 -1378 134 518 C ATOM 357 CD1 LEU A 92 37.557 34.816 32.727 1.00 59.04 C ANISOU 357 CD1 LEU A 92 8270 8791 5372 -1338 322 731 C ATOM 358 CD2 LEU A 92 37.596 33.165 34.616 1.00 54.42 C ANISOU 358 CD2 LEU A 92 7567 8003 5109 -1422 204 425 C ATOM 359 N MET A 93 32.310 34.075 34.775 1.00 64.53 N ANISOU 359 N MET A 93 8869 9250 6400 -1541 -526 449 N ATOM 360 CA MET A 93 31.074 34.662 35.286 1.00 63.37 C ANISOU 360 CA MET A 93 8642 9066 6371 -1580 -672 510 C ATOM 361 C MET A 93 30.642 33.984 36.580 1.00 61.73 C ANISOU 361 C MET A 93 8331 8730 6392 -1670 -740 391 C ATOM 362 O MET A 93 30.216 34.651 37.530 1.00 59.88 O ANISOU 362 O MET A 93 7995 8413 6345 -1706 -753 470 O ATOM 363 CB MET A 93 29.964 34.573 34.239 1.00 60.19 C ANISOU 363 CB MET A 93 8305 8799 5765 -1533 -852 492 C ATOM 364 CG MET A 93 28.643 35.162 34.710 1.00 58.15 C ANISOU 364 CG MET A 93 7944 8524 5628 -1557 -1007 558 C ATOM 365 SD MET A 93 27.312 34.964 33.515 1.00 61.10 S ANISOU 365 SD MET A 93 8365 9075 5774 -1505 -1251 519 S ATOM 366 CE MET A 93 25.935 35.658 34.425 1.00 66.46 C ANISOU 366 CE MET A 93 8866 9708 6678 -1535 -1386 603 C ATOM 367 N SER A 94 30.744 32.654 36.634 1.00 62.83 N ANISOU 367 N SER A 94 8509 8848 6514 -1699 -777 204 N ATOM 368 CA SER A 94 30.441 31.943 37.874 1.00 65.44 C ANISOU 368 CA SER A 94 8757 9050 7058 -1783 -817 106 C ATOM 369 C SER A 94 31.385 32.366 38.996 1.00 62.07 C ANISOU 369 C SER A 94 8257 8514 6815 -1797 -667 172 C ATOM 370 O SER A 94 30.961 32.568 40.144 1.00 73.71 O ANISOU 370 O SER A 94 9635 9895 8476 -1848 -690 194 O ATOM 371 CB SER A 94 30.519 30.434 37.640 1.00 64.87 C ANISOU 371 CB SER A 94 8765 8953 6927 -1805 -868 -98 C ATOM 372 OG SER A 94 30.305 29.713 38.841 1.00 61.93 O ANISOU 372 OG SER A 94 8327 8445 6759 -1883 -887 -174 O ATOM 373 N LEU A 95 32.672 32.510 38.678 1.00 50.72 N ANISOU 373 N LEU A 95 6857 7096 5320 -1750 -515 203 N ATOM 374 CA LEU A 95 33.648 32.962 39.663 1.00 47.53 C ANISOU 374 CA LEU A 95 6371 6604 5082 -1766 -385 263 C ATOM 375 C LEU A 95 33.333 34.371 40.147 1.00 49.62 C ANISOU 375 C LEU A 95 6563 6832 5460 -1787 -378 424 C ATOM 376 O LEU A 95 33.481 34.677 41.335 1.00 50.31 O ANISOU 376 O LEU A 95 6569 6816 5731 -1827 -357 439 O ATOM 377 CB LEU A 95 35.053 32.904 39.065 1.00 54.20 C ANISOU 377 CB LEU A 95 7250 7505 5838 -1711 -223 276 C ATOM 378 CG LEU A 95 36.162 33.608 39.847 1.00 56.19 C ANISOU 378 CG LEU A 95 7403 7699 6248 -1732 -88 364 C ATOM 379 CD1 LEU A 95 36.373 32.938 41.191 1.00 52.51 C ANISOU 379 CD1 LEU A 95 6870 7121 5962 -1766 -110 267 C ATOM 380 CD2 LEU A 95 37.453 33.635 39.045 1.00 55.09 C ANISOU 380 CD2 LEU A 95 7278 7647 6005 -1677 77 400 C ATOM 381 N ALA A 96 32.917 35.249 39.233 1.00 50.85 N ANISOU 381 N ALA A 96 6758 7065 5498 -1751 -395 545 N ATOM 382 CA ALA A 96 32.537 36.605 39.609 1.00 47.67 C ANISOU 382 CA ALA A 96 6305 6609 5197 -1757 -395 700 C ATOM 383 C ALA A 96 31.306 36.600 40.503 1.00 49.42 C ANISOU 383 C ALA A 96 6457 6771 5548 -1784 -525 667 C ATOM 384 O ALA A 96 31.209 37.405 41.432 1.00 48.86 O ANISOU 384 O ALA A 96 6325 6604 5637 -1800 -505 732 O ATOM 385 CB ALA A 96 32.291 37.446 38.359 1.00 46.50 C ANISOU 385 CB ALA A 96 6232 6559 4879 -1694 -392 843 C ATOM 386 N ILE A 97 30.355 35.703 40.236 1.00 53.41 N ANISOU 386 N ILE A 97 6972 7334 5989 -1791 -656 564 N ATOM 387 CA ILE A 97 29.211 35.542 41.132 1.00 49.59 C ANISOU 387 CA ILE A 97 6399 6802 5639 -1827 -763 528 C ATOM 388 C ILE A 97 29.685 35.150 42.525 1.00 49.46 C ANISOU 388 C ILE A 97 6327 6664 5801 -1877 -699 465 C ATOM 389 O ILE A 97 29.250 35.718 43.535 1.00 47.13 O ANISOU 389 O ILE A 97 5960 6299 5650 -1883 -701 509 O ATOM 390 CB ILE A 97 28.224 34.504 40.566 1.00 44.48 C ANISOU 390 CB ILE A 97 5762 6236 4904 -1852 -912 414 C ATOM 391 CG1 ILE A 97 27.626 34.992 39.246 1.00 47.12 C ANISOU 391 CG1 ILE A 97 6145 6707 5053 -1790 -1005 481 C ATOM 392 CG2 ILE A 97 27.129 34.206 41.577 1.00 43.61 C ANISOU 392 CG2 ILE A 97 5539 6076 4956 -1906 -997 377 C ATOM 393 CD1 ILE A 97 26.866 33.929 38.492 1.00 50.95 C ANISOU 393 CD1 ILE A 97 6658 7283 5416 -1817 -1160 346 C ATOM 394 N ALA A 98 30.600 34.179 42.596 1.00 53.24 N ANISOU 394 N ALA A 98 6846 7121 6262 -1896 -639 361 N ATOM 395 CA ALA A 98 31.113 33.736 43.890 1.00 45.52 C ANISOU 395 CA ALA A 98 5824 6037 5434 -1928 -585 305 C ATOM 396 C ALA A 98 31.826 34.865 44.628 1.00 43.16 C ANISOU 396 C ALA A 98 5482 5674 5243 -1918 -495 399 C ATOM 397 O ALA A 98 31.631 35.051 45.833 1.00 48.15 O ANISOU 397 O ALA A 98 6059 6225 6009 -1933 -497 396 O ATOM 398 CB ALA A 98 32.050 32.543 43.704 1.00 44.54 C ANISOU 398 CB ALA A 98 5758 5906 5259 -1925 -536 189 C ATOM 399 N ASP A 99 32.649 35.638 43.919 1.00 43.25 N ANISOU 399 N ASP A 99 5519 5717 5196 -1894 -415 483 N ATOM 400 CA ASP A 99 33.411 36.705 44.564 1.00 43.71 C ANISOU 400 CA ASP A 99 5536 5701 5372 -1905 -334 563 C ATOM 401 C ASP A 99 32.510 37.864 44.982 1.00 43.92 C ANISOU 401 C ASP A 99 5539 5672 5477 -1896 -380 656 C ATOM 402 O ASP A 99 32.707 38.462 46.049 1.00 47.16 O ANISOU 402 O ASP A 99 5910 5984 6023 -1910 -361 665 O ATOM 403 CB ASP A 99 34.514 37.193 43.629 1.00 48.13 C ANISOU 403 CB ASP A 99 6122 6308 5858 -1898 -224 640 C ATOM 404 CG ASP A 99 35.450 36.080 43.203 1.00 54.42 C ANISOU 404 CG ASP A 99 6937 7167 6572 -1884 -161 548 C ATOM 405 OD1 ASP A 99 35.305 34.950 43.719 1.00 53.88 O ANISOU 405 OD1 ASP A 99 6870 7081 6523 -1883 -207 422 O ATOM 406 OD2 ASP A 99 36.327 36.333 42.348 1.00 60.88 O ANISOU 406 OD2 ASP A 99 7772 8050 7311 -1867 -57 606 O ATOM 407 N MET A 100 31.527 38.206 44.148 1.00 42.86 N ANISOU 407 N MET A 100 5432 5601 5253 -1860 -447 722 N ATOM 408 CA MET A 100 30.551 39.217 44.528 1.00 42.91 C ANISOU 408 CA MET A 100 5412 5560 5333 -1826 -498 806 C ATOM 409 C MET A 100 29.776 38.780 45.760 1.00 43.30 C ANISOU 409 C MET A 100 5395 5564 5495 -1835 -553 725 C ATOM 410 O MET A 100 29.481 39.597 46.637 1.00 43.16 O ANISOU 410 O MET A 100 5349 5462 5589 -1813 -545 761 O ATOM 411 CB MET A 100 29.601 39.489 43.364 1.00 45.39 C ANISOU 411 CB MET A 100 5756 5974 5515 -1771 -578 884 C ATOM 412 CG MET A 100 28.414 40.351 43.733 1.00 42.08 C ANISOU 412 CG MET A 100 5294 5526 5167 -1715 -648 959 C ATOM 413 SD MET A 100 27.071 40.179 42.551 1.00 53.97 S ANISOU 413 SD MET A 100 6794 7188 6524 -1653 -792 999 S ATOM 414 CE MET A 100 26.804 38.410 42.617 1.00 43.07 C ANISOU 414 CE MET A 100 5377 5884 5105 -1732 -866 814 C ATOM 415 N LEU A 101 29.443 37.491 45.849 1.00 46.97 N ANISOU 415 N LEU A 101 5842 6076 5929 -1867 -601 617 N ATOM 416 CA LEU A 101 28.786 36.993 47.051 1.00 45.51 C ANISOU 416 CA LEU A 101 5594 5846 5850 -1884 -629 554 C ATOM 417 C LEU A 101 29.720 37.015 48.253 1.00 42.73 C ANISOU 417 C LEU A 101 5242 5397 5598 -1897 -553 514 C ATOM 418 O LEU A 101 29.263 37.226 49.381 1.00 43.55 O ANISOU 418 O LEU A 101 5306 5446 5793 -1883 -553 506 O ATOM 419 CB LEU A 101 28.244 35.588 46.809 1.00 45.84 C ANISOU 419 CB LEU A 101 5627 5944 5848 -1929 -694 458 C ATOM 420 CG LEU A 101 27.034 35.596 45.877 1.00 39.57 C ANISOU 420 CG LEU A 101 4803 5250 4981 -1921 -805 485 C ATOM 421 CD1 LEU A 101 26.436 34.208 45.752 1.00 41.53 C ANISOU 421 CD1 LEU A 101 5033 5531 5216 -1990 -882 376 C ATOM 422 CD2 LEU A 101 26.002 36.600 46.372 1.00 39.76 C ANISOU 422 CD2 LEU A 101 4746 5272 5088 -1869 -834 575 C ATOM 423 N VAL A 102 31.020 36.804 48.040 1.00 41.77 N ANISOU 423 N VAL A 102 5156 5263 5452 -1917 -489 487 N ATOM 424 CA VAL A 102 31.977 37.009 49.125 1.00 41.32 C ANISOU 424 CA VAL A 102 5085 5125 5489 -1925 -433 457 C ATOM 425 C VAL A 102 31.863 38.433 49.648 1.00 41.46 C ANISOU 425 C VAL A 102 5094 5068 5592 -1905 -422 528 C ATOM 426 O VAL A 102 31.585 38.657 50.830 1.00 44.76 O ANISOU 426 O VAL A 102 5495 5424 6090 -1887 -431 499 O ATOM 427 CB VAL A 102 33.412 36.703 48.657 1.00 40.74 C ANISOU 427 CB VAL A 102 5026 5070 5383 -1945 -366 434 C ATOM 428 CG1 VAL A 102 34.414 37.176 49.698 1.00 41.97 C ANISOU 428 CG1 VAL A 102 5148 5151 5646 -1957 -326 417 C ATOM 429 CG2 VAL A 102 33.589 35.225 48.394 1.00 45.70 C ANISOU 429 CG2 VAL A 102 5677 5743 5945 -1946 -372 341 C ATOM 430 N GLY A 103 31.973 39.409 48.747 1.00 39.49 N ANISOU 430 N GLY A 103 4869 4819 5316 -1898 -403 626 N ATOM 431 CA GLY A 103 31.886 40.802 49.156 1.00 41.82 C ANISOU 431 CA GLY A 103 5174 5015 5699 -1878 -392 696 C ATOM 432 C GLY A 103 30.539 41.181 49.745 1.00 45.16 C ANISOU 432 C GLY A 103 5582 5415 6160 -1814 -446 708 C ATOM 433 O GLY A 103 30.449 42.111 50.549 1.00 44.96 O ANISOU 433 O GLY A 103 5569 5288 6224 -1784 -438 718 O ATOM 434 N LEU A 104 29.478 40.476 49.352 1.00 44.81 N ANISOU 434 N LEU A 104 5508 5466 6051 -1791 -501 704 N ATOM 435 CA LEU A 104 28.124 40.782 49.798 1.00 38.45 C ANISOU 435 CA LEU A 104 4658 4667 5282 -1726 -547 727 C ATOM 436 C LEU A 104 27.766 40.157 51.138 1.00 43.17 C ANISOU 436 C LEU A 104 5213 5249 5942 -1724 -540 643 C ATOM 437 O LEU A 104 26.970 40.735 51.887 1.00 47.02 O ANISOU 437 O LEU A 104 5674 5705 6488 -1656 -540 659 O ATOM 438 CB LEU A 104 27.109 40.308 48.753 1.00 39.57 C ANISOU 438 CB LEU A 104 4763 4933 5336 -1712 -622 762 C ATOM 439 CG LEU A 104 26.588 41.330 47.747 1.00 39.90 C ANISOU 439 CG LEU A 104 4825 5002 5332 -1644 -658 885 C ATOM 440 CD1 LEU A 104 25.799 40.635 46.653 1.00 40.94 C ANISOU 440 CD1 LEU A 104 4925 5279 5351 -1645 -751 893 C ATOM 441 CD2 LEU A 104 25.726 42.361 48.454 1.00 47.87 C ANISOU 441 CD2 LEU A 104 5804 5949 6436 -1549 -662 940 C ATOM 442 N LEU A 105 28.306 38.991 51.450 1.00 41.80 N ANISOU 442 N LEU A 105 5038 5095 5750 -1782 -528 561 N ATOM 443 CA LEU A 105 27.869 38.269 52.639 1.00 37.74 C ANISOU 443 CA LEU A 105 4490 4574 5277 -1779 -518 501 C ATOM 444 C LEU A 105 29.004 37.931 53.593 1.00 37.42 C ANISOU 444 C LEU A 105 4489 4471 5259 -1796 -476 430 C ATOM 445 O LEU A 105 28.813 38.009 54.809 1.00 43.26 O ANISOU 445 O LEU A 105 5228 5173 6037 -1758 -454 402 O ATOM 446 CB LEU A 105 27.141 36.981 52.214 1.00 35.97 C ANISOU 446 CB LEU A 105 4219 4431 5015 -1828 -557 476 C ATOM 447 CG LEU A 105 26.013 37.171 51.195 1.00 36.92 C ANISOU 447 CG LEU A 105 4285 4638 5106 -1819 -626 533 C ATOM 448 CD1 LEU A 105 25.692 35.862 50.500 1.00 37.24 C ANISOU 448 CD1 LEU A 105 4308 4747 5097 -1896 -683 481 C ATOM 449 CD2 LEU A 105 24.771 37.744 51.860 1.00 37.42 C ANISOU 449 CD2 LEU A 105 4265 4718 5236 -1753 -629 581 C ATOM 450 N VAL A 106 30.175 37.551 53.080 1.00 34.88 N ANISOU 450 N VAL A 106 4198 4149 4906 -1842 -463 401 N ATOM 451 CA VAL A 106 31.282 37.180 53.951 1.00 34.38 C ANISOU 451 CA VAL A 106 4154 4044 4865 -1851 -438 334 C ATOM 452 C VAL A 106 31.993 38.424 54.466 1.00 34.57 C ANISOU 452 C VAL A 106 4195 3992 4949 -1837 -427 337 C ATOM 453 O VAL A 106 32.264 38.550 55.665 1.00 41.50 O ANISOU 453 O VAL A 106 5084 4824 5859 -1809 -429 286 O ATOM 454 CB VAL A 106 32.246 36.244 53.200 1.00 34.30 C ANISOU 454 CB VAL A 106 4155 4072 4807 -1892 -425 300 C ATOM 455 CG1 VAL A 106 33.410 35.859 54.086 1.00 36.16 C ANISOU 455 CG1 VAL A 106 4395 4276 5070 -1885 -408 237 C ATOM 456 CG2 VAL A 106 31.510 35.007 52.712 1.00 34.60 C ANISOU 456 CG2 VAL A 106 4195 4159 4793 -1912 -448 278 C ATOM 457 N MET A 107 32.305 39.358 53.567 1.00 35.13 N ANISOU 457 N MET A 107 4273 4044 5030 -1857 -418 398 N ATOM 458 CA MET A 107 33.003 40.580 53.965 1.00 36.48 C ANISOU 458 CA MET A 107 4463 4121 5279 -1867 -410 403 C ATOM 459 C MET A 107 32.213 41.457 54.930 1.00 36.87 C ANISOU 459 C MET A 107 4541 4091 5377 -1802 -428 394 C ATOM 460 O MET A 107 32.798 41.901 55.933 1.00 35.99 O ANISOU 460 O MET A 107 4451 3907 5316 -1799 -440 327 O ATOM 461 CB MET A 107 33.399 41.378 52.719 1.00 38.80 C ANISOU 461 CB MET A 107 4766 4401 5575 -1906 -382 495 C ATOM 462 CG MET A 107 34.618 40.855 51.987 1.00 44.47 C ANISOU 462 CG MET A 107 5455 5173 6266 -1969 -340 494 C ATOM 463 SD MET A 107 35.196 42.065 50.783 1.00 49.87 S ANISOU 463 SD MET A 107 6155 5820 6973 -2018 -282 621 S ATOM 464 CE MET A 107 36.611 41.221 50.089 1.00 41.20 C ANISOU 464 CE MET A 107 5002 4818 5834 -2074 -214 605 C ATOM 465 N PRO A 108 30.934 41.788 54.687 1.00 40.05 N ANISOU 465 N PRO A 108 4943 4507 5767 -1742 -435 452 N ATOM 466 CA PRO A 108 30.260 42.745 55.585 1.00 38.84 C ANISOU 466 CA PRO A 108 4822 4272 5663 -1660 -438 441 C ATOM 467 C PRO A 108 30.163 42.271 57.024 1.00 40.33 C ANISOU 467 C PRO A 108 5017 4462 5843 -1617 -435 349 C ATOM 468 O PRO A 108 30.311 43.079 57.950 1.00 43.64 O ANISOU 468 O PRO A 108 5490 4792 6300 -1571 -440 295 O ATOM 469 CB PRO A 108 28.873 42.907 54.945 1.00 37.06 C ANISOU 469 CB PRO A 108 4564 4102 5416 -1595 -444 527 C ATOM 470 CG PRO A 108 29.054 42.489 53.533 1.00 37.07 C ANISOU 470 CG PRO A 108 4545 4178 5363 -1654 -456 592 C ATOM 471 CD PRO A 108 30.040 41.372 53.592 1.00 37.53 C ANISOU 471 CD PRO A 108 4593 4281 5388 -1734 -446 523 C ATOM 472 N LEU A 109 29.930 40.977 57.243 1.00 37.78 N ANISOU 472 N LEU A 109 4656 4232 5467 -1628 -427 328 N ATOM 473 CA LEU A 109 29.873 40.470 58.609 1.00 38.78 C ANISOU 473 CA LEU A 109 4801 4365 5570 -1582 -414 259 C ATOM 474 C LEU A 109 31.246 40.520 59.267 1.00 47.15 C ANISOU 474 C LEU A 109 5901 5376 6636 -1611 -441 176 C ATOM 475 O LEU A 109 31.358 40.831 60.459 1.00 54.26 O ANISOU 475 O LEU A 109 6850 6240 7526 -1553 -450 108 O ATOM 476 CB LEU A 109 29.310 39.049 58.622 1.00 34.93 C ANISOU 476 CB LEU A 109 4266 3969 5035 -1599 -394 274 C ATOM 477 CG LEU A 109 27.799 38.929 58.842 1.00 35.29 C ANISOU 477 CG LEU A 109 4260 4067 5080 -1544 -362 325 C ATOM 478 CD1 LEU A 109 27.019 39.767 57.845 1.00 35.82 C ANISOU 478 CD1 LEU A 109 4287 4145 5179 -1526 -380 395 C ATOM 479 CD2 LEU A 109 27.356 37.480 58.774 1.00 35.02 C ANISOU 479 CD2 LEU A 109 4180 4104 5023 -1596 -346 340 C ATOM 480 N SER A 110 32.303 40.229 58.504 1.00 44.24 N ANISOU 480 N SER A 110 5510 5017 6281 -1693 -456 176 N ATOM 481 CA SER A 110 33.653 40.348 59.043 1.00 38.85 C ANISOU 481 CA SER A 110 4837 4301 5624 -1726 -489 102 C ATOM 482 C SER A 110 33.962 41.789 59.426 1.00 41.52 C ANISOU 482 C SER A 110 5216 4528 6033 -1727 -519 68 C ATOM 483 O SER A 110 34.553 42.045 60.480 1.00 50.97 O ANISOU 483 O SER A 110 6443 5687 7237 -1710 -565 -24 O ATOM 484 CB SER A 110 34.671 39.829 58.028 1.00 39.27 C ANISOU 484 CB SER A 110 4838 4397 5687 -1806 -482 123 C ATOM 485 OG SER A 110 35.964 39.751 58.600 1.00 37.33 O ANISOU 485 OG SER A 110 4570 4146 5469 -1831 -517 52 O ATOM 486 N LEU A 111 33.563 42.745 58.585 1.00 39.22 N ANISOU 486 N LEU A 111 4934 4176 5791 -1743 -501 139 N ATOM 487 CA LEU A 111 33.782 44.151 58.911 1.00 38.74 C ANISOU 487 CA LEU A 111 4929 3977 5812 -1745 -527 111 C ATOM 488 C LEU A 111 32.993 44.560 60.148 1.00 42.62 C ANISOU 488 C LEU A 111 5493 4423 6279 -1632 -540 40 C ATOM 489 O LEU A 111 33.502 45.294 61.003 1.00 44.55 O ANISOU 489 O LEU A 111 5796 4572 6560 -1627 -587 -57 O ATOM 490 CB LEU A 111 33.409 45.035 57.722 1.00 38.23 C ANISOU 490 CB LEU A 111 4875 3851 5799 -1767 -496 224 C ATOM 491 CG LEU A 111 33.616 46.524 57.990 1.00 39.59 C ANISOU 491 CG LEU A 111 5122 3847 6075 -1774 -516 206 C ATOM 492 CD1 LEU A 111 35.031 46.743 58.476 1.00 40.15 C ANISOU 492 CD1 LEU A 111 5178 3858 6217 -1878 -562 116 C ATOM 493 CD2 LEU A 111 33.332 47.360 56.754 1.00 40.85 C ANISOU 493 CD2 LEU A 111 5300 3939 6282 -1794 -479 342 C ATOM 494 N LEU A 112 31.747 44.096 60.259 1.00 44.59 N ANISOU 494 N LEU A 112 5733 4744 6464 -1542 -498 82 N ATOM 495 CA LEU A 112 30.949 44.394 61.443 1.00 44.24 C ANISOU 495 CA LEU A 112 5748 4681 6380 -1418 -486 23 C ATOM 496 C LEU A 112 31.604 43.824 62.696 1.00 41.85 C ANISOU 496 C LEU A 112 5478 4409 6012 -1400 -518 -87 C ATOM 497 O LEU A 112 31.618 44.472 63.749 1.00 43.24 O ANISOU 497 O LEU A 112 5739 4523 6169 -1327 -543 -182 O ATOM 498 CB LEU A 112 29.532 43.844 61.268 1.00 41.55 C ANISOU 498 CB LEU A 112 5355 4439 5993 -1341 -424 104 C ATOM 499 CG LEU A 112 28.446 44.363 62.214 1.00 42.35 C ANISOU 499 CG LEU A 112 5497 4527 6066 -1193 -381 81 C ATOM 500 CD1 LEU A 112 28.324 45.875 62.115 1.00 52.90 C ANISOU 500 CD1 LEU A 112 6909 5718 7474 -1135 -396 66 C ATOM 501 CD2 LEU A 112 27.115 43.702 61.907 1.00 42.20 C ANISOU 501 CD2 LEU A 112 5383 4629 6022 -1145 -319 175 C ATOM 502 N ALA A 113 32.157 42.613 62.596 1.00 37.26 N ANISOU 502 N ALA A 113 4844 3924 5390 -1455 -523 -78 N ATOM 503 CA ALA A 113 32.879 42.032 63.722 1.00 37.36 C ANISOU 503 CA ALA A 113 4887 3971 5335 -1431 -564 -168 C ATOM 504 C ALA A 113 34.109 42.858 64.072 1.00 44.10 C ANISOU 504 C ALA A 113 5771 4740 6244 -1482 -654 -271 C ATOM 505 O ALA A 113 34.417 43.059 65.252 1.00 52.85 O ANISOU 505 O ALA A 113 6947 5835 7300 -1423 -709 -377 O ATOM 506 CB ALA A 113 33.273 40.589 63.408 1.00 39.68 C ANISOU 506 CB ALA A 113 5120 4367 5590 -1475 -551 -127 C ATOM 507 N ILE A 114 34.830 43.339 63.056 1.00 45.15 N ANISOU 507 N ILE A 114 5851 4820 6482 -1596 -673 -240 N ATOM 508 CA ILE A 114 35.992 44.190 63.303 1.00 41.27 C ANISOU 508 CA ILE A 114 5367 4239 6076 -1673 -757 -329 C ATOM 509 C ILE A 114 35.571 45.459 64.030 1.00 42.95 C ANISOU 509 C ILE A 114 5690 4316 6313 -1617 -791 -412 C ATOM 510 O ILE A 114 36.273 45.943 64.927 1.00 43.06 O ANISOU 510 O ILE A 114 5750 4273 6337 -1625 -883 -542 O ATOM 511 CB ILE A 114 36.719 44.506 61.983 1.00 39.37 C ANISOU 511 CB ILE A 114 5043 3965 5949 -1809 -740 -251 C ATOM 512 CG1 ILE A 114 37.304 43.233 61.376 1.00 38.38 C ANISOU 512 CG1 ILE A 114 4819 3975 5790 -1849 -712 -201 C ATOM 513 CG2 ILE A 114 37.830 45.513 62.210 1.00 42.38 C ANISOU 513 CG2 ILE A 114 5419 4235 6449 -1910 -818 -332 C ATOM 514 CD1 ILE A 114 38.067 43.469 60.105 1.00 38.59 C ANISOU 514 CD1 ILE A 114 4763 3995 5906 -1968 -678 -124 C ATOM 515 N LEU A 115 34.409 46.008 63.664 1.00 48.82 N ANISOU 515 N LEU A 115 6478 5006 7064 -1550 -723 -344 N ATOM 516 CA LEU A 115 33.910 47.209 64.326 1.00 48.68 C ANISOU 516 CA LEU A 115 6578 4850 7067 -1469 -741 -421 C ATOM 517 C LEU A 115 33.729 46.979 65.821 1.00 51.16 C ANISOU 517 C LEU A 115 6976 5207 7257 -1347 -774 -550 C ATOM 518 O LEU A 115 34.066 47.847 66.635 1.00 56.10 O ANISOU 518 O LEU A 115 7702 5721 7893 -1322 -848 -686 O ATOM 519 CB LEU A 115 32.592 47.652 63.688 1.00 42.73 C ANISOU 519 CB LEU A 115 5841 4066 6327 -1384 -654 -312 C ATOM 520 CG LEU A 115 32.624 48.795 62.670 1.00 42.78 C ANISOU 520 CG LEU A 115 5868 3921 6467 -1444 -648 -239 C ATOM 521 CD1 LEU A 115 33.539 48.476 61.504 1.00 42.18 C ANISOU 521 CD1 LEU A 115 5695 3873 6458 -1605 -648 -148 C ATOM 522 CD2 LEU A 115 31.222 49.095 62.173 1.00 45.09 C ANISOU 522 CD2 LEU A 115 6169 4216 6748 -1323 -572 -131 C ATOM 523 N TYR A 116 33.207 45.812 66.203 1.00 52.92 N ANISOU 523 N TYR A 116 7168 5585 7357 -1272 -720 -509 N ATOM 524 CA TYR A 116 32.986 45.475 67.605 1.00 58.17 C ANISOU 524 CA TYR A 116 7914 6311 7877 -1144 -729 -603 C ATOM 525 C TYR A 116 34.152 44.707 68.222 1.00 56.47 C ANISOU 525 C TYR A 116 7682 6173 7601 -1187 -820 -675 C ATOM 526 O TYR A 116 33.954 43.969 69.196 1.00 59.01 O ANISOU 526 O TYR A 116 8048 6596 7778 -1085 -808 -699 O ATOM 527 CB TYR A 116 31.682 44.690 67.754 1.00 50.62 C ANISOU 527 CB TYR A 116 6937 5472 6825 -1032 -605 -502 C ATOM 528 CG TYR A 116 30.439 45.532 67.556 1.00 52.25 C ANISOU 528 CG TYR A 116 7171 5620 7061 -935 -525 -462 C ATOM 529 CD1 TYR A 116 29.900 45.725 66.291 1.00 58.44 C ANISOU 529 CD1 TYR A 116 7872 6384 7949 -986 -481 -340 C ATOM 530 CD2 TYR A 116 29.808 46.136 68.636 1.00 59.48 C ANISOU 530 CD2 TYR A 116 8197 6510 7893 -775 -494 -547 C ATOM 531 CE1 TYR A 116 28.763 46.497 66.107 1.00 73.47 C ANISOU 531 CE1 TYR A 116 9790 8243 9881 -879 -416 -296 C ATOM 532 CE2 TYR A 116 28.672 46.908 68.462 1.00 77.19 C ANISOU 532 CE2 TYR A 116 10457 8704 10168 -663 -415 -509 C ATOM 533 CZ TYR A 116 28.153 47.085 67.197 1.00 83.29 C ANISOU 533 CZ TYR A 116 11134 9458 11055 -715 -380 -380 C ATOM 534 OH TYR A 116 27.023 47.852 67.022 1.00100.60 O ANISOU 534 OH TYR A 116 13333 11610 13282 -589 -310 -336 O ATOM 535 N ASP A 117 35.362 44.870 67.680 1.00 55.36 N ANISOU 535 N ASP A 117 7474 5992 7567 -1328 -907 -701 N ATOM 536 CA ASP A 117 36.576 44.246 68.217 1.00 58.55 C ANISOU 536 CA ASP A 117 7840 6471 7935 -1367 -1010 -775 C ATOM 537 C ASP A 117 36.440 42.726 68.315 1.00 58.93 C ANISOU 537 C ASP A 117 7842 6674 7876 -1315 -956 -689 C ATOM 538 O ASP A 117 36.762 42.114 69.335 1.00 56.83 O ANISOU 538 O ASP A 117 7618 6488 7486 -1235 -1006 -744 O ATOM 539 CB ASP A 117 36.955 44.849 69.571 1.00 70.00 C ANISOU 539 CB ASP A 117 9405 7886 9307 -1296 -1128 -950 C ATOM 540 CG ASP A 117 37.934 45.997 69.440 1.00 90.94 C ANISOU 540 CG ASP A 117 12049 10400 12104 -1423 -1251 -1064 C ATOM 541 OD1 ASP A 117 38.115 46.498 68.310 1.00 82.61 O ANISOU 541 OD1 ASP A 117 10919 9257 11210 -1551 -1217 -990 O ATOM 542 OD2 ASP A 117 38.532 46.391 70.464 1.00106.95 O ANISOU 542 OD2 ASP A 117 14145 12409 14084 -1400 -1385 -1226 O ATOM 543 N TYR A 118 35.947 42.121 67.233 1.00 57.05 N ANISOU 543 N TYR A 118 7526 6468 7681 -1360 -856 -552 N ATOM 544 CA TYR A 118 35.909 40.666 67.075 1.00 49.33 C ANISOU 544 CA TYR A 118 6498 5606 6640 -1344 -805 -466 C ATOM 545 C TYR A 118 35.139 39.977 68.200 1.00 56.11 C ANISOU 545 C TYR A 118 7441 6534 7346 -1206 -758 -457 C ATOM 546 O TYR A 118 35.439 38.839 68.568 1.00 62.16 O ANISOU 546 O TYR A 118 8202 7379 8036 -1172 -756 -426 O ATOM 547 CB TYR A 118 37.324 40.091 66.955 1.00 48.85 C ANISOU 547 CB TYR A 118 6360 5593 6608 -1406 -888 -498 C ATOM 548 CG TYR A 118 37.994 40.410 65.636 1.00 54.63 C ANISOU 548 CG TYR A 118 6983 6291 7483 -1543 -886 -459 C ATOM 549 CD1 TYR A 118 37.778 39.615 64.518 1.00 66.27 C ANISOU 549 CD1 TYR A 118 8392 7807 8980 -1584 -803 -351 C ATOM 550 CD2 TYR A 118 38.838 41.506 65.507 1.00 48.62 C ANISOU 550 CD2 TYR A 118 6189 5452 6831 -1634 -964 -531 C ATOM 551 CE1 TYR A 118 38.385 39.898 63.308 1.00 60.48 C ANISOU 551 CE1 TYR A 118 7570 7057 8352 -1694 -786 -310 C ATOM 552 CE2 TYR A 118 39.450 41.799 64.299 1.00 47.61 C ANISOU 552 CE2 TYR A 118 5961 5300 6830 -1759 -940 -476 C ATOM 553 CZ TYR A 118 39.219 40.990 63.204 1.00 52.97 C ANISOU 553 CZ TYR A 118 6582 6038 7507 -1780 -846 -363 C ATOM 554 OH TYR A 118 39.822 41.270 61.998 1.00 54.79 O ANISOU 554 OH TYR A 118 6723 6258 7838 -1890 -809 -302 O ATOM 555 N VAL A 119 34.143 40.660 68.753 1.00 59.15 N ANISOU 555 N VAL A 119 7905 6888 7682 -1119 -709 -475 N ATOM 556 CA VAL A 119 33.186 40.072 69.681 1.00 56.69 C ANISOU 556 CA VAL A 119 7661 6648 7232 -989 -621 -436 C ATOM 557 C VAL A 119 31.848 40.066 68.952 1.00 62.40 C ANISOU 557 C VAL A 119 8330 7371 8008 -992 -495 -322 C ATOM 558 O VAL A 119 31.195 41.108 68.830 1.00 61.05 O ANISOU 558 O VAL A 119 8179 7139 7876 -957 -470 -341 O ATOM 559 CB VAL A 119 33.112 40.845 71.002 1.00 52.68 C ANISOU 559 CB VAL A 119 7283 6126 6607 -861 -660 -557 C ATOM 560 CG1 VAL A 119 32.037 40.259 71.903 1.00 59.40 C ANISOU 560 CG1 VAL A 119 8197 7063 7308 -720 -536 -494 C ATOM 561 CG2 VAL A 119 34.463 40.830 71.698 1.00 53.50 C ANISOU 561 CG2 VAL A 119 7427 6243 6659 -865 -812 -678 C ATOM 562 N TRP A 120 31.443 38.886 68.466 1.00 68.48 N ANISOU 562 N TRP A 120 9032 8205 8782 -1032 -424 -206 N ATOM 563 CA TRP A 120 30.348 38.704 67.516 1.00 69.62 C ANISOU 563 CA TRP A 120 9091 8361 9001 -1076 -336 -98 C ATOM 564 C TRP A 120 29.123 39.527 67.898 1.00 70.68 C ANISOU 564 C TRP A 120 9242 8494 9121 -975 -259 -86 C ATOM 565 O TRP A 120 28.497 39.276 68.936 1.00 77.48 O ANISOU 565 O TRP A 120 10150 9410 9879 -867 -183 -74 O ATOM 566 CB TRP A 120 29.988 37.220 67.409 1.00 72.61 C ANISOU 566 CB TRP A 120 9426 8808 9354 -1107 -270 3 C ATOM 567 CG TRP A 120 29.050 36.895 66.281 1.00 73.82 C ANISOU 567 CG TRP A 120 9477 8977 9596 -1185 -215 99 C ATOM 568 CD1 TRP A 120 27.772 36.432 66.387 1.00 72.48 C ANISOU 568 CD1 TRP A 120 9254 8859 9425 -1167 -115 188 C ATOM 569 CD2 TRP A 120 29.318 37.011 64.877 1.00 71.06 C ANISOU 569 CD2 TRP A 120 9057 8600 9342 -1293 -262 113 C ATOM 570 NE1 TRP A 120 27.227 36.251 65.139 1.00 66.89 N ANISOU 570 NE1 TRP A 120 8446 8158 8811 -1261 -117 245 N ATOM 571 CE2 TRP A 120 28.156 36.600 64.195 1.00 69.23 C ANISOU 571 CE2 TRP A 120 8742 8408 9154 -1331 -205 201 C ATOM 572 CE3 TRP A 120 30.428 37.423 64.131 1.00 71.53 C ANISOU 572 CE3 TRP A 120 9113 8614 9451 -1361 -343 65 C ATOM 573 CZ2 TRP A 120 28.071 36.588 62.804 1.00 66.09 C ANISOU 573 CZ2 TRP A 120 8275 8009 8827 -1423 -239 232 C ATOM 574 CZ3 TRP A 120 30.341 37.409 62.749 1.00 64.75 C ANISOU 574 CZ3 TRP A 120 8188 7754 8662 -1450 -353 109 C ATOM 575 CH2 TRP A 120 29.171 36.995 62.101 1.00 62.29 C ANISOU 575 CH2 TRP A 120 7811 7484 8371 -1474 -308 188 C ATOM 576 N PRO A 121 28.765 40.529 67.089 1.00 57.77 N ANISOU 576 N PRO A 121 7572 6796 7581 -995 -269 -83 N ATOM 577 CA PRO A 121 27.640 41.409 67.427 1.00 58.55 C ANISOU 577 CA PRO A 121 7687 6885 7675 -877 -200 -78 C ATOM 578 C PRO A 121 26.277 40.915 66.971 1.00 54.64 C ANISOU 578 C PRO A 121 7076 6474 7211 -866 -97 48 C ATOM 579 O PRO A 121 25.259 41.440 67.444 1.00 53.24 O ANISOU 579 O PRO A 121 6894 6320 7013 -744 -16 63 O ATOM 580 CB PRO A 121 28.010 42.706 66.694 1.00 58.79 C ANISOU 580 CB PRO A 121 7738 6792 7807 -909 -272 -125 C ATOM 581 CG PRO A 121 28.720 42.225 65.469 1.00 53.52 C ANISOU 581 CG PRO A 121 6995 6122 7219 -1064 -326 -74 C ATOM 582 CD PRO A 121 29.469 40.974 65.873 1.00 57.51 C ANISOU 582 CD PRO A 121 7497 6696 7659 -1113 -344 -85 C ATOM 583 N LEU A 122 26.228 39.946 66.072 1.00 58.60 N ANISOU 583 N LEU A 122 7482 7021 7762 -985 -100 130 N ATOM 584 CA LEU A 122 24.980 39.398 65.562 1.00 57.95 C ANISOU 584 CA LEU A 122 7274 7021 7724 -1003 -26 242 C ATOM 585 C LEU A 122 24.516 38.251 66.448 1.00 59.48 C ANISOU 585 C LEU A 122 7453 7295 7850 -986 68 294 C ATOM 586 O LEU A 122 25.245 37.795 67.332 1.00 58.70 O ANISOU 586 O LEU A 122 7451 7191 7662 -962 67 253 O ATOM 587 CB LEU A 122 25.180 38.953 64.114 1.00 53.19 C ANISOU 587 CB LEU A 122 6592 6418 7203 -1145 -91 288 C ATOM 588 CG LEU A 122 25.532 40.086 63.148 1.00 40.55 C ANISOU 588 CG LEU A 122 5000 4743 5664 -1160 -165 268 C ATOM 589 CD1 LEU A 122 25.736 39.549 61.748 1.00 43.28 C ANISOU 589 CD1 LEU A 122 5279 5109 6057 -1287 -219 316 C ATOM 590 CD2 LEU A 122 24.457 41.159 63.157 1.00 38.71 C ANISOU 590 CD2 LEU A 122 4736 4507 5466 -1046 -128 299 C ATOM 591 N PRO A 123 23.282 37.774 66.263 1.00 53.62 N ANISOU 591 N PRO A 123 6589 6634 7151 -996 153 394 N ATOM 592 CA PRO A 123 22.816 36.635 67.062 1.00 50.21 C ANISOU 592 CA PRO A 123 6137 6268 6672 -1001 257 466 C ATOM 593 C PRO A 123 23.698 35.411 66.863 1.00 55.07 C ANISOU 593 C PRO A 123 6796 6850 7279 -1120 210 470 C ATOM 594 O PRO A 123 24.309 35.220 65.810 1.00 58.50 O ANISOU 594 O PRO A 123 7217 7241 7772 -1226 112 444 O ATOM 595 CB PRO A 123 21.397 36.394 66.540 1.00 52.98 C ANISOU 595 CB PRO A 123 6311 6702 7118 -1037 327 570 C ATOM 596 CG PRO A 123 20.954 37.727 66.079 1.00 53.80 C ANISOU 596 CG PRO A 123 6374 6801 7265 -950 297 543 C ATOM 597 CD PRO A 123 22.176 38.390 65.507 1.00 52.13 C ANISOU 597 CD PRO A 123 6273 6483 7050 -977 167 449 C ATOM 598 N ARG A 124 23.757 34.580 67.907 1.00 60.52 N ANISOU 598 N ARG A 124 7548 7562 7886 -1087 288 509 N ATOM 599 CA ARG A 124 24.690 33.459 67.942 1.00 57.85 C ANISOU 599 CA ARG A 124 7280 7178 7521 -1159 247 511 C ATOM 600 C ARG A 124 24.460 32.459 66.815 1.00 56.97 C ANISOU 600 C ARG A 124 7079 7044 7522 -1319 222 563 C ATOM 601 O ARG A 124 25.377 31.699 66.485 1.00 55.39 O ANISOU 601 O ARG A 124 6937 6787 7322 -1381 159 538 O ATOM 602 CB ARG A 124 24.591 32.751 69.294 1.00 60.51 C ANISOU 602 CB ARG A 124 7700 7546 7745 -1079 353 572 C ATOM 603 CG ARG A 124 24.757 33.673 70.493 1.00 58.15 C ANISOU 603 CG ARG A 124 7507 7282 7305 -906 380 511 C ATOM 604 CD ARG A 124 26.183 33.656 71.013 1.00 52.60 C ANISOU 604 CD ARG A 124 6946 6540 6499 -857 272 418 C ATOM 605 NE ARG A 124 26.600 32.306 71.368 1.00 57.63 N ANISOU 605 NE ARG A 124 7637 7166 7093 -886 294 493 N ATOM 606 CZ ARG A 124 27.755 32.003 71.945 1.00 65.59 C ANISOU 606 CZ ARG A 124 8760 8159 8002 -830 214 444 C ATOM 607 NH1 ARG A 124 28.635 32.939 72.264 1.00 61.94 N ANISOU 607 NH1 ARG A 124 8364 7696 7475 -757 101 311 N ATOM 608 NH2 ARG A 124 28.033 30.729 72.210 1.00 67.40 N ANISOU 608 NH2 ARG A 124 9038 8369 8204 -847 244 532 N ATOM 609 N TYR A 125 23.271 32.440 66.214 1.00 53.30 N ANISOU 609 N TYR A 125 6476 6625 7152 -1381 262 626 N ATOM 610 CA TYR A 125 22.994 31.496 65.138 1.00 49.21 C ANISOU 610 CA TYR A 125 5877 6084 6736 -1539 221 658 C ATOM 611 C TYR A 125 23.530 31.957 63.790 1.00 54.38 C ANISOU 611 C TYR A 125 6515 6714 7433 -1598 90 584 C ATOM 612 O TYR A 125 23.350 31.246 62.797 1.00 59.12 O ANISOU 612 O TYR A 125 7062 7300 8101 -1720 40 589 O ATOM 613 CB TYR A 125 21.487 31.224 65.034 1.00 53.98 C ANISOU 613 CB TYR A 125 6320 6760 7430 -1595 302 755 C ATOM 614 CG TYR A 125 20.649 32.347 64.452 1.00 56.83 C ANISOU 614 CG TYR A 125 6553 7196 7844 -1555 279 751 C ATOM 615 CD1 TYR A 125 20.432 32.445 63.082 1.00 50.37 C ANISOU 615 CD1 TYR A 125 5647 6387 7104 -1648 169 729 C ATOM 616 CD2 TYR A 125 20.047 33.289 65.275 1.00 66.23 C ANISOU 616 CD2 TYR A 125 7717 8451 8996 -1408 369 773 C ATOM 617 CE1 TYR A 125 19.659 33.461 62.549 1.00 56.60 C ANISOU 617 CE1 TYR A 125 6324 7247 7936 -1595 141 740 C ATOM 618 CE2 TYR A 125 19.269 34.308 64.750 1.00 71.98 C ANISOU 618 CE2 TYR A 125 8331 9240 9777 -1351 349 777 C ATOM 619 CZ TYR A 125 19.080 34.390 63.387 1.00 68.44 C ANISOU 619 CZ TYR A 125 7794 8799 9410 -1444 232 766 C ATOM 620 OH TYR A 125 18.307 35.403 62.862 1.00 60.85 O ANISOU 620 OH TYR A 125 6724 7900 8496 -1371 206 782 O ATOM 621 N LEU A 126 24.175 33.123 63.727 1.00 55.77 N ANISOU 621 N LEU A 126 6741 6879 7570 -1517 36 515 N ATOM 622 CA LEU A 126 24.725 33.628 62.477 1.00 53.30 C ANISOU 622 CA LEU A 126 6420 6543 7289 -1567 -69 463 C ATOM 623 C LEU A 126 26.229 33.437 62.355 1.00 56.98 C ANISOU 623 C LEU A 126 6990 6947 7713 -1580 -132 391 C ATOM 624 O LEU A 126 26.758 33.536 61.241 1.00 56.15 O ANISOU 624 O LEU A 126 6878 6827 7632 -1640 -202 360 O ATOM 625 CB LEU A 126 24.391 35.115 62.313 1.00 50.41 C ANISOU 625 CB LEU A 126 6027 6192 6934 -1484 -85 450 C ATOM 626 CG LEU A 126 22.917 35.427 62.056 1.00 48.38 C ANISOU 626 CG LEU A 126 5636 6011 6736 -1466 -47 521 C ATOM 627 CD1 LEU A 126 22.702 36.923 61.902 1.00 38.09 C ANISOU 627 CD1 LEU A 126 4330 4700 5440 -1361 -65 508 C ATOM 628 CD2 LEU A 126 22.428 34.684 60.825 1.00 44.87 C ANISOU 628 CD2 LEU A 126 5093 5602 6354 -1595 -106 553 C ATOM 629 N CYS A 127 26.931 33.181 63.460 1.00 56.31 N ANISOU 629 N CYS A 127 6996 6839 7562 -1516 -108 367 N ATOM 630 CA CYS A 127 28.355 32.863 63.368 1.00 59.55 C ANISOU 630 CA CYS A 127 7479 7205 7942 -1525 -171 304 C ATOM 631 C CYS A 127 28.628 31.586 62.582 1.00 62.40 C ANISOU 631 C CYS A 127 7836 7539 8332 -1617 -188 316 C ATOM 632 O CYS A 127 29.556 31.591 61.753 1.00 60.91 O ANISOU 632 O CYS A 127 7657 7333 8154 -1651 -249 266 O ATOM 633 CB CYS A 127 28.972 32.788 64.766 1.00 58.41 C ANISOU 633 CB CYS A 127 7427 7055 7709 -1426 -156 280 C ATOM 634 SG CYS A 127 30.642 32.092 64.763 1.00 52.48 S ANISOU 634 SG CYS A 127 6741 6270 6929 -1426 -231 221 S ATOM 635 N PRO A 128 27.913 30.471 62.793 1.00 81.89 N ANISOU 635 N PRO A 128 10297 9997 10818 -1660 -133 377 N ATOM 636 CA PRO A 128 28.135 29.310 61.910 1.00 78.98 C ANISOU 636 CA PRO A 128 9938 9583 10489 -1752 -160 369 C ATOM 637 C PRO A 128 27.842 29.623 60.456 1.00 79.80 C ANISOU 637 C PRO A 128 9973 9709 10639 -1834 -220 340 C ATOM 638 O PRO A 128 28.700 29.399 59.588 1.00 89.07 O ANISOU 638 O PRO A 128 11177 10864 11803 -1859 -272 285 O ATOM 639 CB PRO A 128 27.180 28.249 62.479 1.00 75.89 C ANISOU 639 CB PRO A 128 9541 9165 10129 -1796 -82 450 C ATOM 640 CG PRO A 128 26.171 29.015 63.264 1.00 76.90 C ANISOU 640 CG PRO A 128 9607 9359 10250 -1747 -12 509 C ATOM 641 CD PRO A 128 26.926 30.163 63.845 1.00 78.31 C ANISOU 641 CD PRO A 128 9836 9566 10353 -1628 -36 456 C ATOM 642 N VAL A 129 26.651 30.166 60.177 1.00 61.68 N ANISOU 642 N VAL A 129 7584 7468 8384 -1862 -211 381 N ATOM 643 CA VAL A 129 26.245 30.476 58.806 1.00 55.40 C ANISOU 643 CA VAL A 129 6723 6710 7618 -1928 -279 365 C ATOM 644 C VAL A 129 27.348 31.238 58.086 1.00 52.05 C ANISOU 644 C VAL A 129 6340 6285 7152 -1898 -331 312 C ATOM 645 O VAL A 129 27.866 30.794 57.053 1.00 51.35 O ANISOU 645 O VAL A 129 6275 6189 7048 -1947 -377 270 O ATOM 646 CB VAL A 129 24.930 31.273 58.801 1.00 40.19 C ANISOU 646 CB VAL A 129 4683 4857 5732 -1917 -266 422 C ATOM 647 CG1 VAL A 129 24.551 31.644 57.380 1.00 36.38 C ANISOU 647 CG1 VAL A 129 4139 4423 5262 -1967 -351 412 C ATOM 648 CG2 VAL A 129 23.823 30.478 59.470 1.00 39.87 C ANISOU 648 CG2 VAL A 129 4574 4829 5746 -1961 -199 487 C ATOM 649 N TRP A 130 27.756 32.375 58.660 1.00 41.19 N ANISOU 649 N TRP A 130 4979 4913 5759 -1816 -320 309 N ATOM 650 CA TRP A 130 28.804 33.186 58.052 1.00 38.68 C ANISOU 650 CA TRP A 130 4689 4586 5423 -1802 -360 271 C ATOM 651 C TRP A 130 30.018 32.332 57.721 1.00 45.58 C ANISOU 651 C TRP A 130 5615 5432 6270 -1826 -374 220 C ATOM 652 O TRP A 130 30.460 32.284 56.565 1.00 48.01 O ANISOU 652 O TRP A 130 5922 5756 6565 -1864 -402 202 O ATOM 653 CB TRP A 130 29.187 34.330 58.994 1.00 41.33 C ANISOU 653 CB TRP A 130 5050 4899 5755 -1721 -347 258 C ATOM 654 CG TRP A 130 30.373 35.132 58.539 1.00 41.12 C ANISOU 654 CG TRP A 130 5047 4847 5731 -1724 -382 222 C ATOM 655 CD1 TRP A 130 30.421 36.000 57.488 1.00 35.12 C ANISOU 655 CD1 TRP A 130 4266 4089 4989 -1749 -404 245 C ATOM 656 CD2 TRP A 130 31.677 35.150 59.134 1.00 42.74 C ANISOU 656 CD2 TRP A 130 5291 5023 5926 -1704 -397 165 C ATOM 657 NE1 TRP A 130 31.674 36.552 57.385 1.00 33.74 N ANISOU 657 NE1 TRP A 130 4111 3881 4826 -1760 -419 212 N ATOM 658 CE2 TRP A 130 32.465 36.047 58.384 1.00 42.42 C ANISOU 658 CE2 TRP A 130 5237 4967 5914 -1735 -421 157 C ATOM 659 CE3 TRP A 130 32.257 34.492 60.223 1.00 42.86 C ANISOU 659 CE3 TRP A 130 5346 5030 5909 -1660 -396 128 C ATOM 660 CZ2 TRP A 130 33.801 36.303 58.689 1.00 47.52 C ANISOU 660 CZ2 TRP A 130 5888 5593 6576 -1738 -446 105 C ATOM 661 CZ3 TRP A 130 33.583 34.747 60.523 1.00 49.74 C ANISOU 661 CZ3 TRP A 130 6228 5889 6782 -1647 -435 72 C ATOM 662 CH2 TRP A 130 34.340 35.644 59.759 1.00 52.46 C ANISOU 662 CH2 TRP A 130 6537 6221 7172 -1693 -460 57 C ATOM 663 N ILE A 131 30.503 31.569 58.705 1.00 47.41 N ANISOU 663 N ILE A 131 5894 5630 6488 -1792 -350 204 N ATOM 664 CA ILE A 131 31.671 30.725 58.479 1.00 42.41 C ANISOU 664 CA ILE A 131 5307 4972 5835 -1789 -361 158 C ATOM 665 C ILE A 131 31.416 29.787 57.310 1.00 41.46 C ANISOU 665 C ILE A 131 5192 4845 5716 -1858 -373 143 C ATOM 666 O ILE A 131 32.191 29.745 56.345 1.00 45.88 O ANISOU 666 O ILE A 131 5759 5419 6254 -1868 -390 105 O ATOM 667 CB ILE A 131 32.029 29.950 59.759 1.00 40.60 C ANISOU 667 CB ILE A 131 5135 4706 5585 -1729 -337 160 C ATOM 668 CG1 ILE A 131 32.556 30.908 60.827 1.00 46.95 C ANISOU 668 CG1 ILE A 131 5947 5526 6365 -1652 -348 145 C ATOM 669 CG2 ILE A 131 33.038 28.852 59.454 1.00 45.48 C ANISOU 669 CG2 ILE A 131 5799 5290 6191 -1716 -345 123 C ATOM 670 CD1 ILE A 131 32.820 30.247 62.160 1.00 59.67 C ANISOU 670 CD1 ILE A 131 7623 7121 7929 -1574 -332 155 C ATOM 671 N SER A 132 30.278 29.090 57.339 1.00 44.79 N ANISOU 671 N SER A 132 5605 5250 6163 -1911 -364 173 N ATOM 672 CA SER A 132 29.966 28.162 56.260 1.00 47.71 C ANISOU 672 CA SER A 132 5989 5601 6536 -1986 -393 140 C ATOM 673 C SER A 132 29.903 28.888 54.928 1.00 47.64 C ANISOU 673 C SER A 132 5945 5660 6496 -2014 -439 122 C ATOM 674 O SER A 132 30.431 28.398 53.922 1.00 47.67 O ANISOU 674 O SER A 132 5990 5665 6459 -2030 -462 67 O ATOM 675 CB SER A 132 28.648 27.444 56.538 1.00 49.09 C ANISOU 675 CB SER A 132 6135 5749 6766 -2061 -384 179 C ATOM 676 OG SER A 132 27.550 28.332 56.451 1.00 44.46 O ANISOU 676 OG SER A 132 5451 5235 6205 -2082 -395 228 O ATOM 677 N LEU A 133 29.297 30.081 54.911 1.00 43.65 N ANISOU 677 N LEU A 133 5374 5211 6000 -2003 -449 171 N ATOM 678 CA LEU A 133 29.237 30.838 53.667 1.00 41.48 C ANISOU 678 CA LEU A 133 5076 4999 5686 -2016 -491 175 C ATOM 679 C LEU A 133 30.639 31.091 53.140 1.00 47.39 C ANISOU 679 C LEU A 133 5870 5750 6388 -1983 -474 143 C ATOM 680 O LEU A 133 30.916 30.862 51.955 1.00 54.95 O ANISOU 680 O LEU A 133 6852 6742 7284 -2001 -494 116 O ATOM 681 CB LEU A 133 28.481 32.149 53.875 1.00 35.16 C ANISOU 681 CB LEU A 133 4209 4237 4911 -1985 -495 243 C ATOM 682 CG LEU A 133 26.972 32.000 54.091 1.00 35.42 C ANISOU 682 CG LEU A 133 4164 4303 4991 -2014 -513 283 C ATOM 683 CD1 LEU A 133 26.307 33.358 54.214 1.00 35.55 C ANISOU 683 CD1 LEU A 133 4119 4360 5029 -1954 -514 348 C ATOM 684 CD2 LEU A 133 26.346 31.199 52.962 1.00 36.23 C ANISOU 684 CD2 LEU A 133 4247 4445 5076 -2095 -584 256 C ATOM 685 N ASP A 134 31.552 31.501 54.025 1.00 41.93 N ANISOU 685 N ASP A 134 5185 5029 5718 -1933 -438 142 N ATOM 686 CA ASP A 134 32.962 31.562 53.666 1.00 37.51 C ANISOU 686 CA ASP A 134 4643 4475 5134 -1908 -415 110 C ATOM 687 C ASP A 134 33.386 30.255 53.011 1.00 42.27 C ANISOU 687 C ASP A 134 5296 5071 5693 -1913 -411 50 C ATOM 688 O ASP A 134 33.698 30.214 51.812 1.00 45.29 O ANISOU 688 O ASP A 134 5694 5498 6016 -1922 -409 32 O ATOM 689 CB ASP A 134 33.795 31.850 54.916 1.00 40.99 C ANISOU 689 CB ASP A 134 5078 4883 5614 -1860 -399 100 C ATOM 690 CG ASP A 134 34.993 32.729 54.632 1.00 48.60 C ANISOU 690 CG ASP A 134 6009 5867 6590 -1852 -386 98 C ATOM 691 OD1 ASP A 134 35.586 32.602 53.540 1.00 50.06 O ANISOU 691 OD1 ASP A 134 6189 6091 6742 -1866 -363 93 O ATOM 692 OD2 ASP A 134 35.339 33.551 55.507 1.00 50.03 O ANISOU 692 OD2 ASP A 134 6169 6026 6814 -1834 -395 100 O ATOM 693 N VAL A 135 33.279 29.155 53.769 1.00 42.74 N ANISOU 693 N VAL A 135 5394 5069 5775 -1903 -408 22 N ATOM 694 CA VAL A 135 33.704 27.839 53.298 1.00 45.34 C ANISOU 694 CA VAL A 135 5791 5360 6077 -1895 -402 -42 C ATOM 695 C VAL A 135 33.077 27.522 51.956 1.00 52.85 C ANISOU 695 C VAL A 135 6768 6339 6975 -1951 -437 -77 C ATOM 696 O VAL A 135 33.661 26.798 51.142 1.00 54.51 O ANISOU 696 O VAL A 135 7037 6544 7131 -1930 -429 -144 O ATOM 697 CB VAL A 135 33.360 26.754 54.343 1.00 46.48 C ANISOU 697 CB VAL A 135 5983 5412 6266 -1890 -396 -43 C ATOM 698 CG1 VAL A 135 33.898 25.404 53.909 1.00 45.51 C ANISOU 698 CG1 VAL A 135 5946 5220 6125 -1866 -388 -112 C ATOM 699 CG2 VAL A 135 33.906 27.123 55.705 1.00 48.42 C ANISOU 699 CG2 VAL A 135 6212 5649 6537 -1822 -373 -6 C ATOM 700 N LEU A 136 31.890 28.067 51.687 1.00 56.41 N ANISOU 700 N LEU A 136 7175 6825 7433 -2010 -480 -37 N ATOM 701 CA LEU A 136 31.280 27.837 50.380 1.00 54.24 C ANISOU 701 CA LEU A 136 6920 6595 7093 -2059 -536 -74 C ATOM 702 C LEU A 136 31.993 28.669 49.318 1.00 54.22 C ANISOU 702 C LEU A 136 6921 6680 7000 -2020 -519 -63 C ATOM 703 O LEU A 136 32.723 28.135 48.474 1.00 60.02 O ANISOU 703 O LEU A 136 7718 7432 7655 -1991 -500 -126 O ATOM 704 CB LEU A 136 29.784 28.166 50.439 1.00 44.12 C ANISOU 704 CB LEU A 136 5571 5342 5853 -2126 -597 -28 C ATOM 705 CG LEU A 136 28.986 28.124 49.135 1.00 44.45 C ANISOU 705 CG LEU A 136 5610 5454 5827 -2176 -684 -57 C ATOM 706 CD1 LEU A 136 28.998 26.731 48.551 1.00 45.15 C ANISOU 706 CD1 LEU A 136 5784 5487 5884 -2223 -725 -169 C ATOM 707 CD2 LEU A 136 27.559 28.588 49.378 1.00 43.06 C ANISOU 707 CD2 LEU A 136 5329 5319 5712 -2226 -741 5 C ATOM 708 N PHE A 137 31.878 29.993 49.423 1.00 58.70 N ANISOU 708 N PHE A 137 7426 7295 7582 -2008 -510 22 N ATOM 709 CA PHE A 137 32.167 30.841 48.272 1.00 56.22 C ANISOU 709 CA PHE A 137 7116 7064 7181 -1991 -503 60 C ATOM 710 C PHE A 137 33.635 30.761 47.886 1.00 64.03 C ANISOU 710 C PHE A 137 8133 8071 8125 -1944 -423 38 C ATOM 711 O PHE A 137 33.969 30.456 46.734 1.00 67.42 O ANISOU 711 O PHE A 137 8615 8559 8444 -1926 -410 6 O ATOM 712 CB PHE A 137 31.754 32.279 48.571 1.00 53.83 C ANISOU 712 CB PHE A 137 6752 6777 6924 -1985 -504 163 C ATOM 713 CG PHE A 137 30.273 32.460 48.712 1.00 55.96 C ANISOU 713 CG PHE A 137 6978 7061 7224 -2011 -578 195 C ATOM 714 CD1 PHE A 137 29.401 31.769 47.890 1.00 52.84 C ANISOU 714 CD1 PHE A 137 6593 6713 6769 -2049 -657 156 C ATOM 715 CD2 PHE A 137 29.750 33.305 49.677 1.00 56.87 C ANISOU 715 CD2 PHE A 137 7036 7145 7427 -1995 -571 256 C ATOM 716 CE1 PHE A 137 28.038 31.922 48.018 1.00 55.77 C ANISOU 716 CE1 PHE A 137 6894 7113 7182 -2077 -728 188 C ATOM 717 CE2 PHE A 137 28.386 33.461 49.812 1.00 50.56 C ANISOU 717 CE2 PHE A 137 6176 6373 6661 -2006 -626 290 C ATOM 718 CZ PHE A 137 27.529 32.769 48.980 1.00 55.10 C ANISOU 718 CZ PHE A 137 6738 7007 7190 -2050 -706 261 C ATOM 719 N SER A 138 34.526 30.981 48.858 1.00 58.00 N ANISOU 719 N SER A 138 7331 7264 7441 -1919 -371 48 N ATOM 720 CA SER A 138 35.955 30.868 48.596 1.00 57.58 C ANISOU 720 CA SER A 138 7272 7238 7369 -1874 -294 28 C ATOM 721 C SER A 138 36.285 29.532 47.947 1.00 52.09 C ANISOU 721 C SER A 138 6649 6546 6594 -1837 -281 -67 C ATOM 722 O SER A 138 37.008 29.484 46.943 1.00 55.22 O ANISOU 722 O SER A 138 7066 7011 6902 -1799 -223 -80 O ATOM 723 CB SER A 138 36.743 31.049 49.896 1.00 51.48 C ANISOU 723 CB SER A 138 6441 6417 6702 -1854 -273 30 C ATOM 724 OG SER A 138 36.477 32.308 50.492 1.00 49.64 O ANISOU 724 OG SER A 138 6157 6167 6537 -1884 -288 99 O ATOM 725 N THR A 139 35.711 28.439 48.466 1.00 56.73 N ANISOU 725 N THR A 139 7287 7057 7211 -1846 -329 -132 N ATOM 726 CA THR A 139 36.024 27.131 47.903 1.00 61.23 C ANISOU 726 CA THR A 139 7946 7599 7718 -1806 -321 -235 C ATOM 727 C THR A 139 35.654 27.081 46.430 1.00 57.95 C ANISOU 727 C THR A 139 7593 7256 7167 -1816 -342 -271 C ATOM 728 O THR A 139 36.454 26.632 45.598 1.00 58.37 O ANISOU 728 O THR A 139 7701 7351 7126 -1749 -286 -329 O ATOM 729 CB THR A 139 35.304 26.024 48.672 1.00 56.30 C ANISOU 729 CB THR A 139 7375 6857 7160 -1836 -374 -284 C ATOM 730 OG1 THR A 139 35.650 26.102 50.061 1.00 53.14 O ANISOU 730 OG1 THR A 139 6927 6402 6860 -1812 -353 -240 O ATOM 731 CG2 THR A 139 35.703 24.657 48.137 1.00 56.93 C ANISOU 731 CG2 THR A 139 7565 6876 7190 -1789 -365 -397 C ATOM 732 N ALA A 140 34.471 27.600 46.085 1.00 58.77 N ANISOU 732 N ALA A 140 7688 7392 7250 -1885 -419 -234 N ATOM 733 CA ALA A 140 34.056 27.630 44.689 1.00 54.13 C ANISOU 733 CA ALA A 140 7161 6891 6516 -1887 -459 -263 C ATOM 734 C ALA A 140 35.145 28.252 43.830 1.00 59.70 C ANISOU 734 C ALA A 140 7871 7697 7114 -1816 -359 -223 C ATOM 735 O ALA A 140 35.542 27.688 42.802 1.00 66.74 O ANISOU 735 O ALA A 140 8849 8641 7868 -1763 -333 -297 O ATOM 736 CB ALA A 140 32.740 28.397 44.545 1.00 42.32 C ANISOU 736 CB ALA A 140 5619 5437 5025 -1954 -554 -195 C ATOM 737 N SER A 141 35.697 29.380 44.285 1.00 55.21 N ANISOU 737 N SER A 141 7212 7152 6615 -1813 -292 -109 N ATOM 738 CA SER A 141 36.755 30.035 43.526 1.00 53.73 C ANISOU 738 CA SER A 141 7009 7056 6352 -1764 -180 -48 C ATOM 739 C SER A 141 37.916 29.081 43.287 1.00 55.62 C ANISOU 739 C SER A 141 7278 7307 6548 -1683 -91 -136 C ATOM 740 O SER A 141 38.295 28.822 42.138 1.00 58.16 O ANISOU 740 O SER A 141 7667 7714 6716 -1625 -35 -168 O ATOM 741 CB SER A 141 37.226 31.291 44.260 1.00 57.97 C ANISOU 741 CB SER A 141 7436 7578 7012 -1794 -130 72 C ATOM 742 OG SER A 141 37.817 30.969 45.507 1.00 65.34 O ANISOU 742 OG SER A 141 8308 8436 8084 -1790 -117 38 O ATOM 743 N ILE A 142 38.443 28.480 44.359 1.00 60.34 N ANISOU 743 N ILE A 142 7837 7823 7268 -1664 -80 -182 N ATOM 744 CA ILE A 142 39.605 27.621 44.189 1.00 60.21 C ANISOU 744 CA ILE A 142 7834 7820 7224 -1566 8 -257 C ATOM 745 C ILE A 142 39.231 26.355 43.438 1.00 66.67 C ANISOU 745 C ILE A 142 8798 8611 7923 -1519 -26 -393 C ATOM 746 O ILE A 142 40.112 25.674 42.901 1.00 70.37 O ANISOU 746 O ILE A 142 9309 9110 8317 -1416 57 -465 O ATOM 747 CB ILE A 142 40.265 27.286 45.539 1.00 59.74 C ANISOU 747 CB ILE A 142 7699 7683 7317 -1541 15 -267 C ATOM 748 CG1 ILE A 142 41.722 26.871 45.319 1.00 53.32 C ANISOU 748 CG1 ILE A 142 6838 6928 6492 -1429 130 -297 C ATOM 749 CG2 ILE A 142 39.508 26.179 46.245 1.00 70.37 C ANISOU 749 CG2 ILE A 142 9129 8899 8710 -1549 -75 -349 C ATOM 750 CD1 ILE A 142 42.445 26.474 46.577 1.00 51.16 C ANISOU 750 CD1 ILE A 142 6489 6596 6353 -1381 125 -310 C ATOM 751 N MET A 143 37.939 26.020 43.379 1.00 56.37 N ANISOU 751 N MET A 143 7568 7247 6603 -1592 -149 -437 N ATOM 752 CA MET A 143 37.525 24.937 42.499 1.00 56.03 C ANISOU 752 CA MET A 143 7670 7180 6437 -1567 -199 -575 C ATOM 753 C MET A 143 37.469 25.415 41.055 1.00 56.81 C ANISOU 753 C MET A 143 7826 7422 6337 -1539 -179 -570 C ATOM 754 O MET A 143 38.017 24.763 40.157 1.00 58.49 O ANISOU 754 O MET A 143 8139 7677 6406 -1445 -125 -667 O ATOM 755 CB MET A 143 36.174 24.375 42.948 1.00 52.26 C ANISOU 755 CB MET A 143 7236 6592 6030 -1673 -342 -626 C ATOM 756 CG MET A 143 36.228 23.653 44.288 1.00 53.89 C ANISOU 756 CG MET A 143 7425 6648 6404 -1686 -349 -639 C ATOM 757 SD MET A 143 37.311 22.209 44.255 1.00 46.01 S ANISOU 757 SD MET A 143 6539 5552 5392 -1557 -279 -771 S ATOM 758 CE MET A 143 37.436 21.825 46.000 1.00 58.26 C ANISOU 758 CE MET A 143 8033 6961 7141 -1564 -278 -714 C ATOM 759 N HIS A 144 36.857 26.583 40.827 1.00 60.42 N ANISOU 759 N HIS A 144 8226 7957 6774 -1602 -215 -450 N ATOM 760 CA HIS A 144 36.700 27.085 39.465 1.00 55.76 C ANISOU 760 CA HIS A 144 7700 7506 5981 -1570 -207 -424 C ATOM 761 C HIS A 144 38.046 27.183 38.767 1.00 59.08 C ANISOU 761 C HIS A 144 8131 8027 6289 -1458 -35 -405 C ATOM 762 O HIS A 144 38.245 26.602 37.693 1.00 70.02 O ANISOU 762 O HIS A 144 9638 9483 7483 -1375 -8 -499 O ATOM 763 CB HIS A 144 36.006 28.448 39.481 1.00 53.12 C ANISOU 763 CB HIS A 144 7288 7226 5670 -1636 -249 -265 C ATOM 764 CG HIS A 144 34.523 28.372 39.663 1.00 55.06 C ANISOU 764 CG HIS A 144 7538 7433 5950 -1722 -423 -289 C ATOM 765 ND1 HIS A 144 33.936 27.924 40.827 1.00 64.21 N ANISOU 765 ND1 HIS A 144 8642 8466 7288 -1795 -494 -323 N ATOM 766 CD2 HIS A 144 33.506 28.689 38.827 1.00 59.40 C ANISOU 766 CD2 HIS A 144 8127 8064 6378 -1742 -538 -276 C ATOM 767 CE1 HIS A 144 32.622 27.970 40.701 1.00 60.17 C ANISOU 767 CE1 HIS A 144 8123 7962 6776 -1864 -636 -330 C ATOM 768 NE2 HIS A 144 32.335 28.429 39.496 1.00 56.77 N ANISOU 768 NE2 HIS A 144 7745 7658 6167 -1832 -675 -306 N ATOM 769 N LEU A 145 39.001 27.870 39.397 1.00 54.00 N ANISOU 769 N LEU A 145 7357 7393 5769 -1452 84 -294 N ATOM 770 CA LEU A 145 40.347 27.956 38.844 1.00 57.79 C ANISOU 770 CA LEU A 145 7807 7973 6178 -1354 263 -265 C ATOM 771 C LEU A 145 40.926 26.566 38.624 1.00 63.22 C ANISOU 771 C LEU A 145 8583 8636 6802 -1240 303 -433 C ATOM 772 O LEU A 145 41.465 26.266 37.551 1.00 70.59 O ANISOU 772 O LEU A 145 9595 9674 7552 -1133 402 -478 O ATOM 773 CB LEU A 145 41.245 28.770 39.775 1.00 56.32 C ANISOU 773 CB LEU A 145 7444 7774 6181 -1388 353 -144 C ATOM 774 CG LEU A 145 40.716 30.114 40.277 1.00 54.79 C ANISOU 774 CG LEU A 145 7164 7556 6098 -1502 306 6 C ATOM 775 CD1 LEU A 145 41.729 30.771 41.203 1.00 50.09 C ANISOU 775 CD1 LEU A 145 6403 6938 5691 -1534 387 89 C ATOM 776 CD2 LEU A 145 40.371 31.031 39.114 1.00 48.33 C ANISOU 776 CD2 LEU A 145 6396 6843 5124 -1509 340 121 C ATOM 777 N CYS A 146 40.782 25.687 39.620 1.00 60.60 N ANISOU 777 N CYS A 146 8254 8159 6612 -1251 228 -527 N ATOM 778 CA CYS A 146 41.297 24.332 39.478 1.00 55.89 C ANISOU 778 CA CYS A 146 7757 7506 5974 -1134 260 -686 C ATOM 779 C CYS A 146 40.637 23.624 38.305 1.00 63.51 C ANISOU 779 C CYS A 146 8915 8486 6730 -1100 196 -826 C ATOM 780 O CYS A 146 41.285 22.846 37.597 1.00 66.13 O ANISOU 780 O CYS A 146 9348 8848 6932 -966 278 -940 O ATOM 781 CB CYS A 146 41.084 23.549 40.771 1.00 52.62 C ANISOU 781 CB CYS A 146 7332 6916 5747 -1164 176 -742 C ATOM 782 SG CYS A 146 41.746 21.883 40.727 1.00 61.99 S ANISOU 782 SG CYS A 146 8647 7994 6913 -1010 214 -923 S ATOM 783 N ALA A 147 39.347 23.890 38.078 1.00 67.96 N ANISOU 783 N ALA A 147 9532 9036 7256 -1213 45 -826 N ATOM 784 CA ALA A 147 38.689 23.350 36.895 1.00 69.73 C ANISOU 784 CA ALA A 147 9930 9298 7266 -1191 -39 -958 C ATOM 785 C ALA A 147 39.203 24.021 35.630 1.00 68.00 C ANISOU 785 C ALA A 147 9746 9277 6812 -1098 76 -898 C ATOM 786 O ALA A 147 39.463 23.349 34.626 1.00 75.08 O ANISOU 786 O ALA A 147 10794 10231 7504 -986 109 -1029 O ATOM 787 CB ALA A 147 37.173 23.509 37.015 1.00 61.81 C ANISOU 787 CB ALA A 147 8941 8247 6297 -1338 -240 -962 C ATOM 788 N ILE A 148 39.381 25.344 35.669 1.00 65.34 N ANISOU 788 N ILE A 148 9281 9043 6501 -1137 146 -698 N ATOM 789 CA ILE A 148 39.790 26.075 34.473 1.00 60.85 C ANISOU 789 CA ILE A 148 8748 8662 5712 -1062 262 -606 C ATOM 790 C ILE A 148 41.171 25.622 34.023 1.00 75.44 C ANISOU 790 C ILE A 148 10607 10586 7471 -908 469 -646 C ATOM 791 O ILE A 148 41.456 25.539 32.823 1.00 91.86 O ANISOU 791 O ILE A 148 12801 12804 9298 -797 554 -675 O ATOM 792 CB ILE A 148 39.736 27.592 34.735 1.00 59.72 C ANISOU 792 CB ILE A 148 8462 8573 5654 -1147 302 -371 C ATOM 793 CG1 ILE A 148 38.282 28.048 34.891 1.00 67.51 C ANISOU 793 CG1 ILE A 148 9461 9519 6670 -1261 101 -339 C ATOM 794 CG2 ILE A 148 40.408 28.364 33.611 1.00 65.89 C ANISOU 794 CG2 ILE A 148 9262 9535 6237 -1066 470 -242 C ATOM 795 CD1 ILE A 148 38.135 29.509 35.247 1.00 65.61 C ANISOU 795 CD1 ILE A 148 9096 9297 6534 -1337 126 -120 C ATOM 796 N SER A 149 42.047 25.309 34.977 1.00 82.16 N ANISOU 796 N SER A 149 11337 11360 8521 -886 554 -647 N ATOM 797 CA SER A 149 43.347 24.747 34.642 1.00 86.72 C ANISOU 797 CA SER A 149 11906 12004 9038 -725 743 -700 C ATOM 798 C SER A 149 43.284 23.256 34.339 1.00 86.72 C ANISOU 798 C SER A 149 12089 11919 8942 -610 696 -939 C ATOM 799 O SER A 149 44.177 22.741 33.657 1.00 88.40 O ANISOU 799 O SER A 149 12357 12216 9016 -442 848 -1011 O ATOM 800 CB SER A 149 44.340 24.994 35.779 1.00 86.43 C ANISOU 800 CB SER A 149 11657 11930 9254 -735 838 -609 C ATOM 801 OG SER A 149 45.615 24.459 35.460 1.00 89.07 O ANISOU 801 OG SER A 149 11955 12345 9542 -568 1023 -653 O ATOM 802 N LEU A 150 42.259 22.552 34.824 1.00 77.27 N ANISOU 802 N LEU A 150 10987 10552 7820 -694 497 -1062 N ATOM 803 CA LEU A 150 42.193 21.111 34.601 1.00 83.04 C ANISOU 803 CA LEU A 150 11900 11162 8488 -601 445 -1293 C ATOM 804 C LEU A 150 41.676 20.791 33.204 1.00 95.51 C ANISOU 804 C LEU A 150 13693 12825 9772 -543 394 -1428 C ATOM 805 O LEU A 150 42.362 20.132 32.416 1.00 98.87 O ANISOU 805 O LEU A 150 14242 13303 10020 -370 506 -1553 O ATOM 806 CB LEU A 150 41.317 20.442 35.662 1.00 71.79 C ANISOU 806 CB LEU A 150 10496 9510 7270 -726 262 -1365 C ATOM 807 CG LEU A 150 41.256 18.915 35.584 1.00 64.28 C ANISOU 807 CG LEU A 150 9735 8385 6302 -647 205 -1595 C ATOM 808 CD1 LEU A 150 42.654 18.322 35.635 1.00 70.45 C ANISOU 808 CD1 LEU A 150 10508 9172 7088 -441 391 -1639 C ATOM 809 CD2 LEU A 150 40.397 18.353 36.702 1.00 59.03 C ANISOU 809 CD2 LEU A 150 9070 7495 5863 -791 44 -1625 C ATOM 810 N ASP A 151 40.463 21.253 32.881 1.00119.03 N ANISOU 810 N ASP A 151 16716 15825 12684 -677 223 -1409 N ATOM 811 CA ASP A 151 39.898 20.982 31.561 1.00120.92 C ANISOU 811 CA ASP A 151 17158 16156 12630 -628 141 -1541 C ATOM 812 C ASP A 151 40.837 21.461 30.462 1.00120.79 C ANISOU 812 C ASP A 151 17176 16364 12355 -460 350 -1478 C ATOM 813 O ASP A 151 41.053 20.757 29.468 1.00123.33 O ANISOU 813 O ASP A 151 17690 16741 12429 -316 382 -1647 O ATOM 814 CB ASP A 151 38.518 21.636 31.427 1.00118.96 C ANISOU 814 CB ASP A 151 16900 15935 12363 -791 -68 -1483 C ATOM 815 CG ASP A 151 38.590 23.149 31.284 1.00121.08 C ANISOU 815 CG ASP A 151 17028 16371 12605 -824 13 -1225 C ATOM 816 OD1 ASP A 151 39.543 23.760 31.811 1.00128.87 O ANISOU 816 OD1 ASP A 151 17861 17388 13716 -798 194 -1066 O ATOM 817 OD2 ASP A 151 37.691 23.728 30.639 1.00120.69 O ANISOU 817 OD2 ASP A 151 17022 16420 12415 -874 -112 -1180 O ATOM 818 N ARG A 152 41.430 22.644 30.649 1.00 93.75 N ANISOU 818 N ARG A 152 13569 13062 8988 -474 503 -1236 N ATOM 819 CA ARG A 152 42.427 23.154 29.716 1.00 90.36 C ANISOU 819 CA ARG A 152 13138 12845 8351 -327 738 -1138 C ATOM 820 C ARG A 152 43.520 22.123 29.469 1.00 94.03 C ANISOU 820 C ARG A 152 13669 13310 8747 -130 904 -1290 C ATOM 821 O ARG A 152 43.853 21.815 28.319 1.00 95.98 O ANISOU 821 O ARG A 152 14072 13692 8702 31 1003 -1378 O ATOM 822 CB ARG A 152 43.015 24.455 30.263 1.00 86.34 C ANISOU 822 CB ARG A 152 12387 12406 8010 -402 880 -862 C ATOM 823 CG ARG A 152 44.179 25.016 29.476 1.00 90.95 C ANISOU 823 CG ARG A 152 12920 13195 8443 -273 1155 -727 C ATOM 824 CD ARG A 152 44.692 26.294 30.122 1.00 82.59 C ANISOU 824 CD ARG A 152 11615 12167 7597 -386 1268 -462 C ATOM 825 NE ARG A 152 45.726 26.935 29.319 1.00 89.12 N ANISOU 825 NE ARG A 152 12382 13193 8288 -292 1536 -303 N ATOM 826 CZ ARG A 152 45.483 27.738 28.292 1.00 92.17 C ANISOU 826 CZ ARG A 152 12848 13730 8443 -279 1598 -163 C ATOM 827 NH1 ARG A 152 44.248 28.024 27.915 1.00 91.37 N ANISOU 827 NH1 ARG A 152 12886 13614 8214 -344 1399 -167 N ATOM 828 NH2 ARG A 152 46.505 28.264 27.624 1.00 85.57 N ANISOU 828 NH2 ARG A 152 11944 13069 7500 -195 1869 -8 N ATOM 829 N TYR A 153 44.072 21.557 30.545 1.00 92.58 N ANISOU 829 N TYR A 153 13376 12978 8822 -125 932 -1328 N ATOM 830 CA TYR A 153 45.059 20.494 30.389 1.00 92.39 C ANISOU 830 CA TYR A 153 13417 12932 8755 78 1072 -1482 C ATOM 831 C TYR A 153 44.448 19.285 29.692 1.00102.49 C ANISOU 831 C TYR A 153 14985 14115 9841 159 941 -1762 C ATOM 832 O TYR A 153 45.041 18.726 28.760 1.00106.15 O ANISOU 832 O TYR A 153 15593 14669 10071 361 1070 -1890 O ATOM 833 CB TYR A 153 45.635 20.102 31.750 1.00 86.15 C ANISOU 833 CB TYR A 153 12463 11986 8285 65 1088 -1464 C ATOM 834 CG TYR A 153 46.558 18.906 31.693 1.00 85.69 C ANISOU 834 CG TYR A 153 12477 11872 8209 284 1205 -1632 C ATOM 835 CD1 TYR A 153 47.647 18.887 30.833 1.00 91.01 C ANISOU 835 CD1 TYR A 153 13144 12734 8701 494 1447 -1631 C ATOM 836 CD2 TYR A 153 46.346 17.801 32.507 1.00 86.70 C ANISOU 836 CD2 TYR A 153 12680 11756 8504 292 1084 -1782 C ATOM 837 CE1 TYR A 153 48.495 17.798 30.778 1.00 97.89 C ANISOU 837 CE1 TYR A 153 14079 13557 9557 718 1561 -1786 C ATOM 838 CE2 TYR A 153 47.190 16.707 32.460 1.00 92.29 C ANISOU 838 CE2 TYR A 153 13466 12399 9201 511 1190 -1931 C ATOM 839 CZ TYR A 153 48.263 16.712 31.595 1.00 98.27 C ANISOU 839 CZ TYR A 153 14211 13349 9777 729 1426 -1938 C ATOM 840 OH TYR A 153 49.106 15.625 31.545 1.00103.50 O ANISOU 840 OH TYR A 153 14947 13948 10429 970 1538 -2089 O ATOM 841 N VAL A 154 43.240 18.886 30.107 1.00104.19 N ANISOU 841 N VAL A 154 15287 14150 10149 1 684 -1864 N ATOM 842 CA VAL A 154 42.568 17.781 29.436 1.00102.12 C ANISOU 842 CA VAL A 154 15298 13782 9720 42 531 -2137 C ATOM 843 C VAL A 154 42.177 18.177 28.018 1.00104.63 C ANISOU 843 C VAL A 154 15772 14304 9678 94 512 -2173 C ATOM 844 O VAL A 154 41.861 17.310 27.194 1.00115.96 O ANISOU 844 O VAL A 154 17453 15708 10897 180 425 -2415 O ATOM 845 CB VAL A 154 41.352 17.308 30.260 1.00100.19 C ANISOU 845 CB VAL A 154 15078 13300 9688 -167 265 -2216 C ATOM 846 CG1 VAL A 154 40.812 15.987 29.721 1.00111.29 C ANISOU 846 CG1 VAL A 154 16758 14546 10982 -130 115 -2520 C ATOM 847 CG2 VAL A 154 41.735 17.153 31.719 1.00 93.06 C ANISOU 847 CG2 VAL A 154 14001 12231 9128 -223 299 -2122 C ATOM 848 N ALA A 155 42.192 19.474 27.705 1.00103.51 N ANISOU 848 N ALA A 155 15503 14367 9458 50 586 -1939 N ATOM 849 CA ALA A 155 42.041 19.886 26.315 1.00102.66 C ANISOU 849 CA ALA A 155 15544 14482 8978 144 616 -1942 C ATOM 850 C ALA A 155 43.317 19.618 25.525 1.00107.71 C ANISOU 850 C ALA A 155 16250 15275 9398 398 897 -1976 C ATOM 851 O ALA A 155 43.261 19.161 24.377 1.00116.93 O ANISOU 851 O ALA A 155 17651 16544 10231 545 901 -2140 O ATOM 852 CB ALA A 155 41.661 21.365 26.242 1.00102.30 C ANISOU 852 CB ALA A 155 15352 14590 8927 24 617 -1661 C ATOM 853 N ILE A 156 44.476 19.885 26.126 1.00107.80 N ANISOU 853 N ILE A 156 16055 15314 9589 459 1132 -1829 N ATOM 854 CA ILE A 156 45.734 19.733 25.404 1.00106.27 C ANISOU 854 CA ILE A 156 15878 15294 9206 701 1426 -1828 C ATOM 855 C ILE A 156 46.107 18.263 25.266 1.00109.52 C ANISOU 855 C ILE A 156 16476 15576 9560 888 1437 -2124 C ATOM 856 O ILE A 156 46.495 17.805 24.186 1.00113.40 O ANISOU 856 O ILE A 156 17158 16191 9737 1100 1555 -2262 O ATOM 857 CB ILE A 156 46.843 20.542 26.095 1.00100.52 C ANISOU 857 CB ILE A 156 14838 14646 8708 689 1662 -1568 C ATOM 858 CG1 ILE A 156 46.417 22.001 26.218 1.00 94.68 C ANISOU 858 CG1 ILE A 156 13942 14001 8030 497 1639 -1287 C ATOM 859 CG2 ILE A 156 48.127 20.445 25.308 1.00 92.72 C ANISOU 859 CG2 ILE A 156 13837 13864 7528 933 1981 -1547 C ATOM 860 CD1 ILE A 156 47.517 22.904 26.669 1.00 87.27 C ANISOU 860 CD1 ILE A 156 12718 13168 7273 481 1880 -1031 C ATOM 861 N ARG A 157 46.002 17.504 26.352 1.00108.91 N ANISOU 861 N ARG A 157 16357 15245 9777 824 1321 -2223 N ATOM 862 CA ARG A 157 46.173 16.061 26.277 1.00123.64 C ANISOU 862 CA ARG A 157 18432 16935 11613 981 1289 -2514 C ATOM 863 C ARG A 157 44.906 15.444 25.701 1.00134.93 C ANISOU 863 C ARG A 157 20145 18246 12877 901 1013 -2752 C ATOM 864 O ARG A 157 43.800 15.777 26.133 1.00136.23 O ANISOU 864 O ARG A 157 20275 18320 13165 663 779 -2709 O ATOM 865 CB ARG A 157 46.479 15.482 27.659 1.00127.38 C ANISOU 865 CB ARG A 157 18770 17170 12459 939 1258 -2515 C ATOM 866 CG ARG A 157 46.771 13.988 27.660 1.00130.76 C ANISOU 866 CG ARG A 157 19406 17390 12887 1119 1249 -2792 C ATOM 867 CD ARG A 157 47.223 13.512 29.032 1.00124.68 C ANISOU 867 CD ARG A 157 18483 16414 12475 1107 1252 -2747 C ATOM 868 NE ARG A 157 48.482 14.127 29.437 1.00123.68 N ANISOU 868 NE ARG A 157 18075 16460 12459 1214 1497 -2537 N ATOM 869 CZ ARG A 157 49.680 13.629 29.164 1.00126.87 C ANISOU 869 CZ ARG A 157 18461 16939 12805 1487 1724 -2589 C ATOM 870 NH1 ARG A 157 49.823 12.504 28.483 1.00120.99 N ANISOU 870 NH1 ARG A 157 17982 16104 11883 1701 1750 -2849 N ATOM 871 NH2 ARG A 157 50.764 14.276 29.585 1.00130.42 N ANISOU 871 NH2 ARG A 157 18613 17556 13383 1548 1928 -2382 N ATOM 872 N ASN A 158 45.074 14.550 24.718 1.00153.46 N ANISOU 872 N ASN A 158 22765 20599 14942 1103 1040 -3010 N ATOM 873 CA ASN A 158 44.003 13.897 23.962 1.00155.75 C ANISOU 873 CA ASN A 158 23354 20803 15020 1062 789 -3277 C ATOM 874 C ASN A 158 42.897 14.883 23.594 1.00150.52 C ANISOU 874 C ASN A 158 22662 20276 14252 858 601 -3154 C ATOM 875 O ASN A 158 41.788 14.811 24.140 1.00150.35 O ANISOU 875 O ASN A 158 22626 20093 14409 626 334 -3184 O ATOM 876 CB ASN A 158 43.434 12.693 24.729 1.00165.13 C ANISOU 876 CB ASN A 158 24655 21632 16454 964 576 -3499 C ATOM 877 CG ASN A 158 42.972 13.040 26.135 1.00175.02 C ANISOU 877 CG ASN A 158 25666 22723 18112 714 464 -3314 C ATOM 878 OD1 ASN A 158 43.724 12.900 27.101 1.00169.04 O ANISOU 878 OD1 ASN A 158 24746 21871 17610 755 594 -3212 O ATOM 879 ND2 ASN A 158 41.732 13.500 26.255 1.00176.08 N ANISOU 879 ND2 ASN A 158 25771 22836 18293 466 222 -3271 N ATOM 880 N PRO A 159 43.156 15.817 22.669 1.00130.85 N ANISOU 880 N PRO A 159 20161 18085 11472 944 739 -3004 N ATOM 881 CA PRO A 159 42.151 16.841 22.346 1.00126.34 C ANISOU 881 CA PRO A 159 19548 17648 10806 770 571 -2853 C ATOM 882 C PRO A 159 40.891 16.281 21.702 1.00133.21 C ANISOU 882 C PRO A 159 20665 18456 11491 691 247 -3106 C ATOM 883 O PRO A 159 39.781 16.554 22.170 1.00131.59 O ANISOU 883 O PRO A 159 20385 18163 11451 459 -6 -3068 O ATOM 884 CB PRO A 159 42.902 17.774 21.386 1.00112.61 C ANISOU 884 CB PRO A 159 17791 16234 8763 936 833 -2659 C ATOM 885 CG PRO A 159 43.967 16.924 20.786 1.00115.72 C ANISOU 885 CG PRO A 159 18337 16673 8957 1219 1059 -2835 C ATOM 886 CD PRO A 159 44.380 15.964 21.862 1.00126.31 C ANISOU 886 CD PRO A 159 19613 17739 10639 1217 1063 -2959 C ATOM 887 N ILE A 160 41.057 15.500 20.635 1.00130.81 N ANISOU 887 N ILE A 160 20650 18203 10849 886 252 -3369 N ATOM 888 CA ILE A 160 39.939 14.957 19.863 1.00135.95 C ANISOU 888 CA ILE A 160 21557 18823 11274 833 -58 -3637 C ATOM 889 C ILE A 160 39.022 16.074 19.372 1.00135.05 C ANISOU 889 C ILE A 160 21388 18923 11002 709 -216 -3460 C ATOM 890 O ILE A 160 39.378 16.833 18.471 1.00130.71 O ANISOU 890 O ILE A 160 20879 18654 10129 853 -69 -3322 O ATOM 891 CB ILE A 160 39.143 13.918 20.678 1.00135.21 C ANISOU 891 CB ILE A 160 21504 18382 11488 641 -327 -3859 C ATOM 892 CG1 ILE A 160 40.033 12.729 21.042 1.00133.14 C ANISOU 892 CG1 ILE A 160 21347 17896 11344 795 -181 -4055 C ATOM 893 CG2 ILE A 160 37.918 13.459 19.901 1.00139.73 C ANISOU 893 CG2 ILE A 160 22304 18934 11855 546 -672 -4122 C ATOM 894 CD1 ILE A 160 39.318 11.646 21.821 1.00129.84 C ANISOU 894 CD1 ILE A 160 20994 17113 11226 618 -422 -4266 C ATOM 895 N PHE A 165 27.777 16.127 24.478 1.00182.22 N ANISOU 895 N PHE A 165 26210 23916 19111 -1571 -2717 -3499 N ATOM 896 CA PHE A 165 27.052 17.388 24.593 1.00172.42 C ANISOU 896 CA PHE A 165 24739 22877 17896 -1629 -2788 -3239 C ATOM 897 C PHE A 165 27.819 18.521 23.917 1.00163.58 C ANISOU 897 C PHE A 165 23651 22022 16479 -1404 -2593 -3029 C ATOM 898 O PHE A 165 28.789 18.283 23.198 1.00165.27 O ANISOU 898 O PHE A 165 24073 22296 16427 -1208 -2435 -3112 O ATOM 899 CB PHE A 165 26.790 17.722 26.063 1.00161.60 C ANISOU 899 CB PHE A 165 23093 21360 16949 -1791 -2711 -3026 C ATOM 900 CG PHE A 165 25.810 16.797 26.730 1.00162.37 C ANISOU 900 CG PHE A 165 23114 21232 17347 -2038 -2917 -3176 C ATOM 901 CD1 PHE A 165 26.232 15.599 27.284 1.00160.78 C ANISOU 901 CD1 PHE A 165 23019 20742 17326 -2092 -2854 -3343 C ATOM 902 CD2 PHE A 165 24.466 17.125 26.801 1.00157.18 C ANISOU 902 CD2 PHE A 165 22273 20650 16798 -2215 -3169 -3140 C ATOM 903 CE1 PHE A 165 25.332 14.746 27.896 1.00157.39 C ANISOU 903 CE1 PHE A 165 22524 20093 17183 -2332 -3031 -3464 C ATOM 904 CE2 PHE A 165 23.562 16.277 27.413 1.00154.15 C ANISOU 904 CE2 PHE A 165 21796 20066 16709 -2453 -3341 -3263 C ATOM 905 CZ PHE A 165 23.995 15.086 27.961 1.00154.23 C ANISOU 905 CZ PHE A 165 21897 19784 16919 -2498 -3247 -3410 C ATOM 906 N ASN A 166 27.377 19.753 24.148 1.00163.66 N ANISOU 906 N ASN A 166 23458 22184 16541 -1429 -2595 -2753 N ATOM 907 CA ASN A 166 27.995 20.932 23.561 1.00172.17 C ANISOU 907 CA ASN A 166 24548 23498 17371 -1242 -2418 -2518 C ATOM 908 C ASN A 166 28.836 21.665 24.604 1.00163.91 C ANISOU 908 C ASN A 166 23328 22382 16569 -1227 -2121 -2245 C ATOM 909 O ASN A 166 28.750 21.404 25.806 1.00156.62 O ANISOU 909 O ASN A 166 22251 21258 15999 -1364 -2089 -2216 O ATOM 910 CB ASN A 166 26.924 21.862 22.977 1.00166.91 C ANISOU 910 CB ASN A 166 23801 23055 16562 -1258 -2636 -2395 C ATOM 911 CG ASN A 166 27.500 22.890 22.020 1.00161.52 C ANISOU 911 CG ASN A 166 23215 22629 15528 -1043 -2493 -2204 C ATOM 912 OD1 ASN A 166 28.560 22.680 21.428 1.00157.40 O ANISOU 912 OD1 ASN A 166 22877 22155 14771 -875 -2291 -2248 O ATOM 913 ND2 ASN A 166 26.804 24.011 21.865 1.00164.07 N ANISOU 913 ND2 ASN A 166 23413 23113 15814 -1041 -2587 -1981 N ATOM 914 N SER A 167 29.665 22.594 24.120 1.00144.97 N ANISOU 914 N SER A 167 20958 20154 13971 -1058 -1904 -2044 N ATOM 915 CA SER A 167 30.543 23.346 25.013 1.00133.13 C ANISOU 915 CA SER A 167 19299 18601 12682 -1041 -1626 -1792 C ATOM 916 C SER A 167 29.744 24.173 26.012 1.00132.10 C ANISOU 916 C SER A 167 18919 18420 12854 -1192 -1701 -1590 C ATOM 917 O SER A 167 30.046 24.171 27.213 1.00127.97 O ANISOU 917 O SER A 167 18247 17730 12645 -1277 -1589 -1515 O ATOM 918 CB SER A 167 31.475 24.241 24.198 1.00127.23 C ANISOU 918 CB SER A 167 18626 18057 11659 -851 -1396 -1606 C ATOM 919 OG SER A 167 32.350 24.966 25.044 1.00119.11 O ANISOU 919 OG SER A 167 17437 16973 10847 -850 -1137 -1373 O ATOM 920 N ARG A 168 28.704 24.864 25.541 1.00135.80 N ANISOU 920 N ARG A 168 19340 19033 13224 -1217 -1898 -1507 N ATOM 921 CA ARG A 168 27.887 25.703 26.409 1.00129.39 C ANISOU 921 CA ARG A 168 18295 18191 12675 -1334 -1972 -1315 C ATOM 922 C ARG A 168 27.040 24.895 27.384 1.00133.58 C ANISOU 922 C ARG A 168 18699 18536 13520 -1529 -2136 -1453 C ATOM 923 O ARG A 168 26.362 25.495 28.225 1.00137.98 O ANISOU 923 O ARG A 168 19052 19055 14318 -1628 -2181 -1307 O ATOM 924 CB ARG A 168 26.995 26.619 25.563 1.00133.22 C ANISOU 924 CB ARG A 168 18772 18893 12954 -1281 -2145 -1194 C ATOM 925 CG ARG A 168 26.858 28.034 26.121 1.00129.97 C ANISOU 925 CG ARG A 168 18183 18510 12690 -1273 -2053 -879 C ATOM 926 CD ARG A 168 25.970 28.926 25.255 1.00133.18 C ANISOU 926 CD ARG A 168 18591 19126 12884 -1197 -2229 -750 C ATOM 927 NE ARG A 168 26.583 29.270 23.976 1.00137.23 N ANISOU 927 NE ARG A 168 19311 19826 13005 -1015 -2146 -696 N ATOM 928 CZ ARG A 168 26.123 30.202 23.152 1.00134.50 C ANISOU 928 CZ ARG A 168 19002 19670 12430 -903 -2228 -526 C ATOM 929 NH1 ARG A 168 25.050 30.918 23.448 1.00133.62 N ANISOU 929 NH1 ARG A 168 18731 19591 12448 -943 -2399 -396 N ATOM 930 NH2 ARG A 168 26.756 30.424 22.004 1.00134.18 N ANISOU 930 NH2 ARG A 168 19168 19796 12019 -734 -2129 -478 N ATOM 931 N THR A 169 27.055 23.566 27.290 1.00132.99 N ANISOU 931 N THR A 169 18744 18340 13447 -1584 -2218 -1724 N ATOM 932 CA THR A 169 26.367 22.687 28.231 1.00127.25 C ANISOU 932 CA THR A 169 17915 17408 13027 -1777 -2342 -1852 C ATOM 933 C THR A 169 27.316 21.876 29.100 1.00120.60 C ANISOU 933 C THR A 169 17108 16340 12377 -1791 -2148 -1919 C ATOM 934 O THR A 169 27.035 21.662 30.283 1.00115.04 O ANISOU 934 O THR A 169 16256 15468 11986 -1923 -2133 -1876 O ATOM 935 CB THR A 169 25.433 21.731 27.480 1.00135.60 C ANISOU 935 CB THR A 169 19074 18474 13974 -1864 -2637 -2122 C ATOM 936 OG1 THR A 169 26.201 20.913 26.589 1.00146.42 O ANISOU 936 OG1 THR A 169 20709 19839 15084 -1746 -2599 -2338 O ATOM 937 CG2 THR A 169 24.401 22.514 26.682 1.00137.40 C ANISOU 937 CG2 THR A 169 19242 18937 14028 -1852 -2862 -2055 C ATOM 938 N LYS A 170 28.444 21.412 28.554 1.00115.37 N ANISOU 938 N LYS A 170 16636 15673 11528 -1645 -1992 -2018 N ATOM 939 CA LYS A 170 29.445 20.790 29.413 1.00103.73 C ANISOU 939 CA LYS A 170 15173 14003 10236 -1625 -1788 -2043 C ATOM 940 C LYS A 170 30.073 21.814 30.351 1.00 96.97 C ANISOU 940 C LYS A 170 14136 13153 9554 -1601 -1573 -1769 C ATOM 941 O LYS A 170 30.490 21.464 31.463 1.00 93.77 O ANISOU 941 O LYS A 170 13654 12575 9401 -1649 -1465 -1743 O ATOM 942 CB LYS A 170 30.509 20.081 28.573 1.00106.56 C ANISOU 942 CB LYS A 170 15767 14372 10348 -1452 -1666 -2211 C ATOM 943 CG LYS A 170 31.339 20.977 27.671 1.00117.26 C ANISOU 943 CG LYS A 170 17184 15959 11411 -1259 -1494 -2078 C ATOM 944 CD LYS A 170 32.106 20.139 26.652 1.00120.68 C ANISOU 944 CD LYS A 170 17872 16426 11557 -1089 -1425 -2294 C ATOM 945 CE LYS A 170 33.059 20.983 25.820 1.00113.48 C ANISOU 945 CE LYS A 170 17012 15742 10364 -891 -1205 -2143 C ATOM 946 NZ LYS A 170 33.660 20.200 24.706 1.00 94.39 N ANISOU 946 NZ LYS A 170 14854 13390 7619 -711 -1154 -2362 N ATOM 947 N ALA A 171 30.118 23.084 29.939 1.00 98.46 N ANISOU 947 N ALA A 171 14261 13533 9617 -1531 -1518 -1564 N ATOM 948 CA ALA A 171 30.496 24.141 30.871 1.00 90.68 C ANISOU 948 CA ALA A 171 13092 12538 8824 -1541 -1358 -1310 C ATOM 949 C ALA A 171 29.505 24.227 32.024 1.00 88.47 C ANISOU 949 C ALA A 171 12629 12139 8847 -1709 -1476 -1256 C ATOM 950 O ALA A 171 29.901 24.408 33.182 1.00 83.38 O ANISOU 950 O ALA A 171 11865 11377 8439 -1748 -1351 -1155 O ATOM 951 CB ALA A 171 30.591 25.479 30.140 1.00 88.16 C ANISOU 951 CB ALA A 171 12756 12425 8314 -1446 -1301 -1103 C ATOM 952 N ILE A 172 28.209 24.096 31.727 1.00 85.13 N ANISOU 952 N ILE A 172 12176 11755 8414 -1807 -1715 -1322 N ATOM 953 CA ILE A 172 27.194 24.086 32.778 1.00 84.08 C ANISOU 953 CA ILE A 172 11860 11520 8565 -1968 -1824 -1281 C ATOM 954 C ILE A 172 27.393 22.889 33.699 1.00 78.94 C ANISOU 954 C ILE A 172 11222 10639 8132 -2063 -1791 -1413 C ATOM 955 O ILE A 172 27.253 22.996 34.924 1.00 77.07 O ANISOU 955 O ILE A 172 10843 10287 8152 -2142 -1731 -1315 O ATOM 956 CB ILE A 172 25.785 24.097 32.156 1.00 84.80 C ANISOU 956 CB ILE A 172 11908 11719 8593 -2050 -2097 -1342 C ATOM 957 CG1 ILE A 172 25.580 25.364 31.324 1.00 84.52 C ANISOU 957 CG1 ILE A 172 11857 11909 8348 -1937 -2125 -1178 C ATOM 958 CG2 ILE A 172 24.718 23.983 33.235 1.00 87.25 C ANISOU 958 CG2 ILE A 172 12016 11930 9206 -2220 -2197 -1307 C ATOM 959 CD1 ILE A 172 25.706 26.645 32.117 1.00 79.66 C ANISOU 959 CD1 ILE A 172 11081 11305 7880 -1908 -1985 -913 C ATOM 960 N MET A 173 27.714 21.729 33.124 1.00 81.57 N ANISOU 960 N MET A 173 11738 10897 8358 -2046 -1829 -1636 N ATOM 961 CA MET A 173 27.976 20.542 33.937 1.00 81.07 C ANISOU 961 CA MET A 173 11717 10594 8491 -2118 -1789 -1759 C ATOM 962 C MET A 173 29.148 20.773 34.886 1.00 71.06 C ANISOU 962 C MET A 173 10405 9245 7348 -2034 -1542 -1629 C ATOM 963 O MET A 173 29.077 20.437 36.074 1.00 60.16 O ANISOU 963 O MET A 173 8938 7703 6216 -2118 -1500 -1587 O ATOM 964 CB MET A 173 28.243 19.333 33.037 1.00 87.61 C ANISOU 964 CB MET A 173 12779 11354 9154 -2080 -1858 -2026 C ATOM 965 CG MET A 173 26.996 18.548 32.653 1.00 93.70 C ANISOU 965 CG MET A 173 13581 12070 9952 -2244 -2127 -2214 C ATOM 966 SD MET A 173 26.411 17.446 33.960 1.00111.53 S ANISOU 966 SD MET A 173 15765 14026 12585 -2457 -2171 -2271 S ATOM 967 CE MET A 173 27.208 15.907 33.502 1.00103.27 C ANISOU 967 CE MET A 173 15012 12764 11462 -2394 -2148 -2555 C ATOM 968 N LYS A 174 30.237 21.356 34.377 1.00 70.20 N ANISOU 968 N LYS A 174 10351 9255 7067 -1870 -1378 -1559 N ATOM 969 CA LYS A 174 31.403 21.604 35.221 1.00 69.91 C ANISOU 969 CA LYS A 174 10256 9161 7145 -1792 -1156 -1443 C ATOM 970 C LYS A 174 31.107 22.645 36.298 1.00 70.58 C ANISOU 970 C LYS A 174 10134 9252 7430 -1861 -1118 -1225 C ATOM 971 O LYS A 174 31.571 22.516 37.441 1.00 70.64 O ANISOU 971 O LYS A 174 10068 9138 7633 -1875 -1017 -1167 O ATOM 972 CB LYS A 174 32.587 22.035 34.360 1.00 73.00 C ANISOU 972 CB LYS A 174 10729 9696 7311 -1614 -990 -1410 C ATOM 973 CG LYS A 174 33.777 21.090 34.415 1.00 94.99 C ANISOU 973 CG LYS A 174 13626 12384 10084 -1497 -843 -1528 C ATOM 974 CD LYS A 174 34.337 20.976 35.827 1.00 90.60 C ANISOU 974 CD LYS A 174 12950 11681 9794 -1518 -733 -1442 C ATOM 975 CE LYS A 174 35.556 20.065 35.866 1.00 77.46 C ANISOU 975 CE LYS A 174 11383 9932 8115 -1377 -589 -1548 C ATOM 976 NZ LYS A 174 36.090 19.911 37.247 1.00 59.05 N ANISOU 976 NZ LYS A 174 8940 7466 6031 -1387 -502 -1465 N ATOM 977 N ILE A 175 30.344 23.687 35.952 1.00 66.87 N ANISOU 977 N ILE A 175 9578 8924 6906 -1891 -1200 -1106 N ATOM 978 CA ILE A 175 29.931 24.676 36.945 1.00 60.29 C ANISOU 978 CA ILE A 175 8561 8088 6259 -1951 -1178 -917 C ATOM 979 C ILE A 175 29.117 24.009 38.045 1.00 56.82 C ANISOU 979 C ILE A 175 8038 7493 6060 -2089 -1260 -955 C ATOM 980 O ILE A 175 29.323 24.266 39.240 1.00 56.49 O ANISOU 980 O ILE A 175 7893 7366 6205 -2112 -1169 -854 O ATOM 981 CB ILE A 175 29.139 25.815 36.273 1.00 59.39 C ANISOU 981 CB ILE A 175 8387 8144 6034 -1945 -1272 -798 C ATOM 982 CG1 ILE A 175 30.046 26.658 35.376 1.00 65.85 C ANISOU 982 CG1 ILE A 175 9273 9105 6641 -1808 -1147 -700 C ATOM 983 CG2 ILE A 175 28.466 26.693 37.316 1.00 52.27 C ANISOU 983 CG2 ILE A 175 7303 7219 5339 -2012 -1282 -635 C ATOM 984 CD1 ILE A 175 29.301 27.733 34.609 1.00 63.48 C ANISOU 984 CD1 ILE A 175 8945 8967 6206 -1781 -1239 -576 C ATOM 985 N ALA A 176 28.182 23.138 37.659 1.00 59.78 N ANISOU 985 N ALA A 176 8457 7828 6429 -2186 -1432 -1103 N ATOM 986 CA ALA A 176 27.383 22.423 38.646 1.00 58.70 C ANISOU 986 CA ALA A 176 8242 7538 6525 -2333 -1500 -1136 C ATOM 987 C ALA A 176 28.261 21.555 39.536 1.00 54.02 C ANISOU 987 C ALA A 176 7711 6755 6059 -2316 -1367 -1176 C ATOM 988 O ALA A 176 28.061 21.506 40.753 1.00 53.26 O ANISOU 988 O ALA A 176 7516 6556 6166 -2378 -1319 -1091 O ATOM 989 CB ALA A 176 26.320 21.577 37.946 1.00 59.36 C ANISOU 989 CB ALA A 176 8370 7606 6577 -2451 -1713 -1305 C ATOM 990 N ILE A 177 29.244 20.870 38.948 1.00 56.83 N ANISOU 990 N ILE A 177 8235 7070 6288 -2215 -1303 -1301 N ATOM 991 CA ILE A 177 30.109 19.988 39.731 1.00 56.42 C ANISOU 991 CA ILE A 177 8251 6838 6349 -2175 -1185 -1344 C ATOM 992 C ILE A 177 30.901 20.787 40.762 1.00 55.30 C ANISOU 992 C ILE A 177 7992 6712 6306 -2105 -1022 -1165 C ATOM 993 O ILE A 177 30.963 20.421 41.944 1.00 55.98 O ANISOU 993 O ILE A 177 8034 6664 6573 -2140 -973 -1118 O ATOM 994 CB ILE A 177 31.039 19.187 38.803 1.00 58.79 C ANISOU 994 CB ILE A 177 8748 7113 6475 -2049 -1140 -1513 C ATOM 995 CG1 ILE A 177 30.225 18.230 37.931 1.00 56.35 C ANISOU 995 CG1 ILE A 177 8576 6744 6091 -2133 -1320 -1722 C ATOM 996 CG2 ILE A 177 32.073 18.418 39.614 1.00 53.28 C ANISOU 996 CG2 ILE A 177 8108 6251 5887 -1967 -1001 -1531 C ATOM 997 CD1 ILE A 177 31.002 17.652 36.772 1.00 58.39 C ANISOU 997 CD1 ILE A 177 9040 7027 6117 -1992 -1294 -1898 C ATOM 998 N VAL A 178 31.512 21.896 40.335 1.00 56.38 N ANISOU 998 N VAL A 178 8084 7014 6325 -2008 -939 -1062 N ATOM 999 CA VAL A 178 32.339 22.662 41.265 1.00 50.31 C ANISOU 999 CA VAL A 178 7208 6256 5652 -1949 -796 -912 C ATOM 1000 C VAL A 178 31.477 23.307 42.349 1.00 52.32 C ANISOU 1000 C VAL A 178 7314 6488 6079 -2050 -834 -782 C ATOM 1001 O VAL A 178 31.851 23.323 43.532 1.00 55.26 O ANISOU 1001 O VAL A 178 7624 6778 6593 -2045 -759 -714 O ATOM 1002 CB VAL A 178 33.203 23.691 40.510 1.00 49.01 C ANISOU 1002 CB VAL A 178 7030 6258 5335 -1840 -693 -830 C ATOM 1003 CG1 VAL A 178 34.154 22.977 39.560 1.00 60.13 C ANISOU 1003 CG1 VAL A 178 8581 7690 6577 -1721 -622 -956 C ATOM 1004 CG2 VAL A 178 32.351 24.682 39.749 1.00 49.38 C ANISOU 1004 CG2 VAL A 178 7036 6448 5277 -1877 -781 -755 C ATOM 1005 N TRP A 179 30.296 23.817 41.979 1.00 51.48 N ANISOU 1005 N TRP A 179 7146 6460 5956 -2132 -955 -750 N ATOM 1006 CA TRP A 179 29.406 24.392 42.982 1.00 50.98 C ANISOU 1006 CA TRP A 179 6938 6381 6053 -2214 -984 -634 C ATOM 1007 C TRP A 179 28.927 23.335 43.971 1.00 52.05 C ANISOU 1007 C TRP A 179 7067 6353 6358 -2307 -1005 -679 C ATOM 1008 O TRP A 179 28.812 23.608 45.170 1.00 54.62 O ANISOU 1008 O TRP A 179 7304 6627 6823 -2325 -948 -580 O ATOM 1009 CB TRP A 179 28.217 25.076 42.309 1.00 45.91 C ANISOU 1009 CB TRP A 179 6223 5864 5357 -2267 -1115 -596 C ATOM 1010 CG TRP A 179 28.455 26.519 42.004 1.00 44.93 C ANISOU 1010 CG TRP A 179 6042 5872 5156 -2188 -1068 -457 C ATOM 1011 CD1 TRP A 179 28.553 27.091 40.772 1.00 46.76 C ANISOU 1011 CD1 TRP A 179 6326 6241 5200 -2125 -1099 -444 C ATOM 1012 CD2 TRP A 179 28.635 27.576 42.954 1.00 49.88 C ANISOU 1012 CD2 TRP A 179 6564 6496 5891 -2161 -980 -309 C ATOM 1013 NE1 TRP A 179 28.777 28.441 40.893 1.00 53.91 N ANISOU 1013 NE1 TRP A 179 7164 7215 6105 -2068 -1029 -284 N ATOM 1014 CE2 TRP A 179 28.833 28.765 42.223 1.00 54.46 C ANISOU 1014 CE2 TRP A 179 7138 7195 6359 -2092 -960 -209 C ATOM 1015 CE3 TRP A 179 28.646 27.634 44.352 1.00 50.64 C ANISOU 1015 CE3 TRP A 179 6583 6496 6160 -2185 -916 -253 C ATOM 1016 CZ2 TRP A 179 29.041 29.997 42.842 1.00 48.83 C ANISOU 1016 CZ2 TRP A 179 6346 6488 5720 -2056 -885 -66 C ATOM 1017 CZ3 TRP A 179 28.852 28.858 44.964 1.00 56.32 C ANISOU 1017 CZ3 TRP A 179 7227 7239 6934 -2140 -847 -124 C ATOM 1018 CH2 TRP A 179 29.047 30.023 44.209 1.00 52.96 C ANISOU 1018 CH2 TRP A 179 6797 6912 6412 -2082 -835 -36 C ATOM 1019 N ALA A 180 28.634 22.125 43.486 1.00 49.97 N ANISOU 1019 N ALA A 180 6908 5999 6081 -2366 -1085 -827 N ATOM 1020 CA ALA A 180 28.199 21.052 44.372 1.00 47.99 C ANISOU 1020 CA ALA A 180 6667 5568 5997 -2464 -1096 -862 C ATOM 1021 C ALA A 180 29.305 20.651 45.335 1.00 53.14 C ANISOU 1021 C ALA A 180 7372 6103 6717 -2376 -955 -830 C ATOM 1022 O ALA A 180 29.037 20.360 46.505 1.00 57.53 O ANISOU 1022 O ALA A 180 7882 6555 7423 -2424 -916 -759 O ATOM 1023 CB ALA A 180 27.742 19.846 43.553 1.00 54.80 C ANISOU 1023 CB ALA A 180 7652 6339 6831 -2548 -1217 -1042 C ATOM 1024 N ILE A 181 30.551 20.615 44.860 1.00 52.85 N ANISOU 1024 N ILE A 181 7427 6090 6565 -2240 -876 -877 N ATOM 1025 CA ILE A 181 31.671 20.347 45.760 1.00 51.11 C ANISOU 1025 CA ILE A 181 7230 5787 6404 -2137 -751 -838 C ATOM 1026 C ILE A 181 31.750 21.423 46.836 1.00 54.37 C ANISOU 1026 C ILE A 181 7499 6262 6895 -2123 -688 -675 C ATOM 1027 O ILE A 181 31.919 21.126 48.030 1.00 58.27 O ANISOU 1027 O ILE A 181 7976 6660 7502 -2115 -637 -617 O ATOM 1028 CB ILE A 181 32.984 20.242 44.963 1.00 45.31 C ANISOU 1028 CB ILE A 181 6584 5101 5528 -1987 -674 -911 C ATOM 1029 CG1 ILE A 181 32.932 19.051 44.006 1.00 47.40 C ANISOU 1029 CG1 ILE A 181 7020 5278 5714 -1982 -731 -1094 C ATOM 1030 CG2 ILE A 181 34.172 20.115 45.903 1.00 44.43 C ANISOU 1030 CG2 ILE A 181 6459 4939 5482 -1871 -554 -857 C ATOM 1031 CD1 ILE A 181 34.071 19.017 43.013 1.00 48.26 C ANISOU 1031 CD1 ILE A 181 7216 5469 5651 -1828 -653 -1173 C ATOM 1032 N SER A 182 31.608 22.689 46.435 1.00 48.84 N ANISOU 1032 N SER A 182 6707 5718 6132 -2116 -694 -601 N ATOM 1033 CA SER A 182 31.656 23.781 47.403 1.00 51.58 C ANISOU 1033 CA SER A 182 6932 6114 6551 -2103 -643 -462 C ATOM 1034 C SER A 182 30.548 23.641 48.445 1.00 53.20 C ANISOU 1034 C SER A 182 7070 6251 6891 -2197 -677 -403 C ATOM 1035 O SER A 182 30.785 23.794 49.652 1.00 53.60 O ANISOU 1035 O SER A 182 7082 6258 7025 -2170 -616 -329 O ATOM 1036 CB SER A 182 31.548 25.120 46.673 1.00 50.67 C ANISOU 1036 CB SER A 182 6749 6152 6350 -2088 -654 -396 C ATOM 1037 OG SER A 182 32.323 25.111 45.488 1.00 50.32 O ANISOU 1037 OG SER A 182 6778 6180 6161 -2020 -630 -454 O ATOM 1038 N ILE A 183 29.331 23.332 47.992 1.00 55.46 N ANISOU 1038 N ILE A 183 7337 6538 7195 -2307 -775 -435 N ATOM 1039 CA ILE A 183 28.203 23.166 48.906 1.00 54.97 C ANISOU 1039 CA ILE A 183 7191 6426 7268 -2406 -796 -372 C ATOM 1040 C ILE A 183 28.452 22.002 49.854 1.00 53.48 C ANISOU 1040 C ILE A 183 7074 6068 7176 -2421 -741 -383 C ATOM 1041 O ILE A 183 28.192 22.097 51.060 1.00 56.01 O ANISOU 1041 O ILE A 183 7340 6351 7588 -2427 -682 -287 O ATOM 1042 CB ILE A 183 26.893 22.978 48.117 1.00 48.20 C ANISOU 1042 CB ILE A 183 6283 5611 6420 -2529 -923 -416 C ATOM 1043 CG1 ILE A 183 26.598 24.206 47.255 1.00 49.40 C ANISOU 1043 CG1 ILE A 183 6363 5937 6470 -2494 -979 -378 C ATOM 1044 CG2 ILE A 183 25.734 22.716 49.062 1.00 43.07 C ANISOU 1044 CG2 ILE A 183 5527 4913 5926 -2640 -929 -346 C ATOM 1045 CD1 ILE A 183 25.439 24.015 46.302 1.00 44.21 C ANISOU 1045 CD1 ILE A 183 5663 5347 5790 -2593 -1129 -437 C ATOM 1046 N GLY A 184 28.964 20.888 49.327 1.00 52.59 N ANISOU 1046 N GLY A 184 7097 5848 7035 -2414 -754 -499 N ATOM 1047 CA GLY A 184 29.240 19.739 50.171 1.00 48.15 C ANISOU 1047 CA GLY A 184 6625 5106 6565 -2414 -702 -503 C ATOM 1048 C GLY A 184 30.261 20.039 51.249 1.00 55.35 C ANISOU 1048 C GLY A 184 7536 6011 7483 -2284 -596 -418 C ATOM 1049 O GLY A 184 30.175 19.512 52.360 1.00 55.13 O ANISOU 1049 O GLY A 184 7528 5877 7542 -2287 -546 -350 O ATOM 1050 N VAL A 185 31.249 20.881 50.935 1.00 57.62 N ANISOU 1050 N VAL A 185 7801 6415 7676 -2169 -563 -417 N ATOM 1051 CA VAL A 185 32.211 21.274 51.964 1.00 53.72 C ANISOU 1051 CA VAL A 185 7284 5934 7193 -2056 -484 -343 C ATOM 1052 C VAL A 185 31.564 22.214 52.981 1.00 55.44 C ANISOU 1052 C VAL A 185 7390 6212 7463 -2086 -469 -224 C ATOM 1053 O VAL A 185 31.844 22.134 54.184 1.00 50.63 O ANISOU 1053 O VAL A 185 6782 5561 6894 -2034 -419 -157 O ATOM 1054 CB VAL A 185 33.466 21.896 51.327 1.00 52.29 C ANISOU 1054 CB VAL A 185 7093 5858 6917 -1943 -452 -376 C ATOM 1055 CG1 VAL A 185 34.500 22.204 52.398 1.00 57.90 C ANISOU 1055 CG1 VAL A 185 7770 6579 7651 -1834 -391 -315 C ATOM 1056 CG2 VAL A 185 34.055 20.952 50.298 1.00 50.29 C ANISOU 1056 CG2 VAL A 185 6954 5555 6597 -1895 -453 -498 C ATOM 1057 N SER A 186 30.688 23.114 52.523 1.00 75.76 N ANISOU 1057 N SER A 186 9871 8888 10027 -2155 -512 -197 N ATOM 1058 CA SER A 186 30.153 24.143 53.416 1.00 73.25 C ANISOU 1058 CA SER A 186 9450 8636 9748 -2156 -490 -94 C ATOM 1059 C SER A 186 29.117 23.584 54.390 1.00 64.01 C ANISOU 1059 C SER A 186 8257 7394 8671 -2227 -469 -30 C ATOM 1060 O SER A 186 29.100 23.962 55.567 1.00 59.80 O ANISOU 1060 O SER A 186 7695 6865 8160 -2181 -413 50 O ATOM 1061 CB SER A 186 29.545 25.282 52.598 1.00 80.63 C ANISOU 1061 CB SER A 186 10296 9694 10645 -2188 -539 -77 C ATOM 1062 OG SER A 186 28.269 24.927 52.088 1.00 83.33 O ANISOU 1062 OG SER A 186 10597 10041 11021 -2298 -606 -89 O ATOM 1063 N VAL A 187 28.250 22.683 53.914 1.00 57.44 N ANISOU 1063 N VAL A 187 7439 6496 7891 -2342 -513 -65 N ATOM 1064 CA VAL A 187 27.044 22.325 54.677 1.00 53.32 C ANISOU 1064 CA VAL A 187 6853 5933 7473 -2440 -492 12 C ATOM 1065 C VAL A 187 27.329 21.769 56.067 1.00 52.08 C ANISOU 1065 C VAL A 187 6752 5679 7357 -2393 -395 92 C ATOM 1066 O VAL A 187 26.571 22.082 56.997 1.00 52.58 O ANISOU 1066 O VAL A 187 6739 5773 7466 -2410 -339 193 O ATOM 1067 CB VAL A 187 26.147 21.404 53.837 1.00 44.87 C ANISOU 1067 CB VAL A 187 5783 4800 6465 -2591 -570 -55 C ATOM 1068 CG1 VAL A 187 25.083 20.741 54.697 1.00 48.78 C ANISOU 1068 CG1 VAL A 187 6225 5217 7093 -2706 -527 29 C ATOM 1069 CG2 VAL A 187 25.491 22.198 52.721 1.00 43.99 C ANISOU 1069 CG2 VAL A 187 5572 4828 6312 -2636 -670 -94 C ATOM 1070 N PRO A 188 28.341 20.921 56.290 1.00 47.90 N ANISOU 1070 N PRO A 188 6355 5037 6808 -2324 -369 60 N ATOM 1071 CA PRO A 188 28.557 20.412 57.658 1.00 49.01 C ANISOU 1071 CA PRO A 188 6554 5094 6974 -2266 -282 155 C ATOM 1072 C PRO A 188 28.797 21.497 58.699 1.00 54.02 C ANISOU 1072 C PRO A 188 7131 5840 7554 -2160 -233 234 C ATOM 1073 O PRO A 188 28.448 21.302 59.875 1.00 55.41 O ANISOU 1073 O PRO A 188 7318 5988 7746 -2140 -159 335 O ATOM 1074 CB PRO A 188 29.787 19.509 57.500 1.00 45.04 C ANISOU 1074 CB PRO A 188 6196 4478 6439 -2174 -283 91 C ATOM 1075 CG PRO A 188 29.733 19.062 56.093 1.00 45.01 C ANISOU 1075 CG PRO A 188 6226 4440 6438 -2246 -357 -35 C ATOM 1076 CD PRO A 188 29.202 20.225 55.316 1.00 45.55 C ANISOU 1076 CD PRO A 188 6166 4671 6468 -2295 -412 -59 C ATOM 1077 N ILE A 189 29.372 22.636 58.299 1.00 54.14 N ANISOU 1077 N ILE A 189 7094 5975 7501 -2092 -269 190 N ATOM 1078 CA ILE A 189 29.788 23.646 59.275 1.00 51.99 C ANISOU 1078 CA ILE A 189 6792 5787 7177 -1986 -238 238 C ATOM 1079 C ILE A 189 28.627 24.149 60.127 1.00 54.20 C ANISOU 1079 C ILE A 189 6997 6114 7483 -2013 -185 331 C ATOM 1080 O ILE A 189 28.796 24.262 61.353 1.00 56.89 O ANISOU 1080 O ILE A 189 7371 6460 7786 -1929 -128 393 O ATOM 1081 CB ILE A 189 30.542 24.785 58.569 1.00 47.32 C ANISOU 1081 CB ILE A 189 6153 5294 6533 -1938 -287 175 C ATOM 1082 CG1 ILE A 189 31.701 24.233 57.737 1.00 50.12 C ANISOU 1082 CG1 ILE A 189 6569 5615 6858 -1902 -317 91 C ATOM 1083 CG2 ILE A 189 31.056 25.794 59.585 1.00 47.47 C ANISOU 1083 CG2 ILE A 189 6151 5376 6508 -1838 -270 204 C ATOM 1084 CD1 ILE A 189 32.840 23.677 58.561 1.00 53.81 C ANISOU 1084 CD1 ILE A 189 7110 6033 7301 -1787 -295 93 C ATOM 1085 N PRO A 190 27.459 24.507 59.569 1.00 52.70 N ANISOU 1085 N PRO A 190 6703 5975 7345 -2111 -200 345 N ATOM 1086 CA PRO A 190 26.347 24.907 60.448 1.00 54.91 C ANISOU 1086 CA PRO A 190 6901 6307 7656 -2120 -130 440 C ATOM 1087 C PRO A 190 25.908 23.824 61.415 1.00 53.33 C ANISOU 1087 C PRO A 190 6747 6020 7497 -2151 -39 531 C ATOM 1088 O PRO A 190 25.571 24.138 62.561 1.00 52.44 O ANISOU 1088 O PRO A 190 6624 5947 7354 -2086 47 616 O ATOM 1089 CB PRO A 190 25.233 25.270 59.458 1.00 54.74 C ANISOU 1089 CB PRO A 190 6750 6350 7697 -2226 -180 430 C ATOM 1090 CG PRO A 190 25.951 25.698 58.247 1.00 59.42 C ANISOU 1090 CG PRO A 190 7362 6970 8245 -2217 -275 334 C ATOM 1091 CD PRO A 190 27.147 24.794 58.158 1.00 57.21 C ANISOU 1091 CD PRO A 190 7215 6590 7931 -2188 -282 277 C ATOM 1092 N VAL A 191 25.902 22.555 60.998 1.00 58.36 N ANISOU 1092 N VAL A 191 7445 6533 8196 -2244 -52 518 N ATOM 1093 CA VAL A 191 25.503 21.485 61.910 1.00 52.53 C ANISOU 1093 CA VAL A 191 6763 5687 7507 -2281 43 622 C ATOM 1094 C VAL A 191 26.480 21.395 63.073 1.00 53.02 C ANISOU 1094 C VAL A 191 6951 5726 7470 -2122 99 670 C ATOM 1095 O VAL A 191 26.079 21.317 64.242 1.00 56.05 O ANISOU 1095 O VAL A 191 7348 6119 7829 -2080 202 786 O ATOM 1096 CB VAL A 191 25.389 20.146 61.161 1.00 49.74 C ANISOU 1096 CB VAL A 191 6474 5176 7251 -2413 6 582 C ATOM 1097 CG1 VAL A 191 25.388 18.986 62.145 1.00 65.51 C ANISOU 1097 CG1 VAL A 191 8583 7023 9286 -2418 104 691 C ATOM 1098 CG2 VAL A 191 24.127 20.122 60.321 1.00 46.05 C ANISOU 1098 CG2 VAL A 191 5866 4738 6894 -2590 -40 564 C ATOM 1099 N ILE A 192 27.780 21.438 62.773 1.00 54.62 N ANISOU 1099 N ILE A 192 7236 5912 7604 -2024 31 583 N ATOM 1100 CA ILE A 192 28.782 21.370 63.836 1.00 59.07 C ANISOU 1100 CA ILE A 192 7905 6468 8069 -1866 58 617 C ATOM 1101 C ILE A 192 28.657 22.575 64.762 1.00 54.50 C ANISOU 1101 C ILE A 192 7277 6028 7405 -1770 88 651 C ATOM 1102 O ILE A 192 28.689 22.443 65.991 1.00 52.27 O ANISOU 1102 O ILE A 192 7059 5751 7050 -1679 156 738 O ATOM 1103 CB ILE A 192 30.196 21.265 63.239 1.00 55.81 C ANISOU 1103 CB ILE A 192 7553 6035 7616 -1782 -27 510 C ATOM 1104 CG1 ILE A 192 30.244 20.169 62.176 1.00 58.02 C ANISOU 1104 CG1 ILE A 192 7886 6184 7975 -1870 -58 452 C ATOM 1105 CG2 ILE A 192 31.211 20.972 64.333 1.00 57.48 C ANISOU 1105 CG2 ILE A 192 7869 6231 7741 -1621 -14 551 C ATOM 1106 CD1 ILE A 192 31.332 20.372 61.150 1.00 55.21 C ANISOU 1106 CD1 ILE A 192 7535 5855 7589 -1820 -138 325 C ATOM 1107 N GLY A 193 28.509 23.769 64.184 1.00 51.37 N ANISOU 1107 N GLY A 193 6778 5736 7005 -1783 37 582 N ATOM 1108 CA GLY A 193 28.488 24.977 64.992 1.00 53.08 C ANISOU 1108 CA GLY A 193 6964 6063 7142 -1684 53 588 C ATOM 1109 C GLY A 193 27.253 25.098 65.864 1.00 57.48 C ANISOU 1109 C GLY A 193 7479 6662 7698 -1689 165 696 C ATOM 1110 O GLY A 193 27.351 25.430 67.048 1.00 66.51 O ANISOU 1110 O GLY A 193 8676 7852 8742 -1573 219 738 O ATOM 1111 N LEU A 194 26.075 24.833 65.296 1.00 55.36 N ANISOU 1111 N LEU A 194 7110 6389 7535 -1820 201 738 N ATOM 1112 CA LEU A 194 24.836 24.933 66.054 1.00 48.40 C ANISOU 1112 CA LEU A 194 6155 5563 6673 -1833 322 849 C ATOM 1113 C LEU A 194 24.664 23.772 67.021 1.00 53.73 C ANISOU 1113 C LEU A 194 6917 6160 7337 -1834 435 975 C ATOM 1114 O LEU A 194 23.976 23.920 68.037 1.00 56.05 O ANISOU 1114 O LEU A 194 7195 6513 7588 -1784 559 1079 O ATOM 1115 CB LEU A 194 23.650 25.011 65.094 1.00 41.58 C ANISOU 1115 CB LEU A 194 5130 4731 5940 -1978 310 855 C ATOM 1116 CG LEU A 194 23.648 26.202 64.133 1.00 40.43 C ANISOU 1116 CG LEU A 194 4895 4667 5799 -1969 209 758 C ATOM 1117 CD1 LEU A 194 22.729 25.945 62.949 1.00 41.32 C ANISOU 1117 CD1 LEU A 194 4876 4790 6035 -2122 154 747 C ATOM 1118 CD2 LEU A 194 23.243 27.475 64.858 1.00 47.92 C ANISOU 1118 CD2 LEU A 194 5795 5727 6687 -1845 263 777 C ATOM 1119 N ARG A 195 25.276 22.620 66.735 1.00 51.86 N ANISOU 1119 N ARG A 195 6781 5788 7135 -1882 403 973 N ATOM 1120 CA ARG A 195 25.265 21.525 67.699 1.00 55.40 C ANISOU 1120 CA ARG A 195 7343 6143 7565 -1862 508 1103 C ATOM 1121 C ARG A 195 26.196 21.828 68.866 1.00 64.49 C ANISOU 1121 C ARG A 195 8624 7339 8540 -1662 521 1122 C ATOM 1122 O ARG A 195 25.768 21.879 70.025 1.00 65.99 O ANISOU 1122 O ARG A 195 8848 7580 8644 -1584 640 1236 O ATOM 1123 CB ARG A 195 25.664 20.216 67.015 1.00 52.68 C ANISOU 1123 CB ARG A 195 7082 5620 7315 -1958 464 1088 C ATOM 1124 CG ARG A 195 25.609 19.010 67.935 1.00 57.38 C ANISOU 1124 CG ARG A 195 7806 6084 7911 -1949 575 1238 C ATOM 1125 CD ARG A 195 26.167 17.760 67.273 1.00 63.27 C ANISOU 1125 CD ARG A 195 8665 6631 8744 -2013 520 1204 C ATOM 1126 NE ARG A 195 25.941 16.577 68.096 1.00 80.10 N ANISOU 1126 NE ARG A 195 10918 8612 10905 -2028 638 1368 N ATOM 1127 CZ ARG A 195 26.419 15.370 67.826 1.00 81.09 C ANISOU 1127 CZ ARG A 195 11181 8531 11096 -2054 619 1375 C ATOM 1128 NH1 ARG A 195 26.146 14.330 68.599 1.00 68.98 N ANISOU 1128 NH1 ARG A 195 9764 6848 9597 -2072 737 1543 N ATOM 1129 NH2 ARG A 195 27.189 15.201 66.756 1.00 83.47 N ANISOU 1129 NH2 ARG A 195 11514 8772 11429 -2053 489 1214 N ATOM 1130 N ASP A 196 27.477 22.041 68.576 1.00 64.54 N ANISOU 1130 N ASP A 196 8697 7339 8486 -1573 400 1009 N ATOM 1131 CA ASP A 196 28.485 22.365 69.582 1.00 59.70 C ANISOU 1131 CA ASP A 196 8193 6779 7711 -1387 372 1000 C ATOM 1132 C ASP A 196 29.012 23.760 69.265 1.00 62.03 C ANISOU 1132 C ASP A 196 8420 7188 7961 -1332 266 859 C ATOM 1133 O ASP A 196 29.834 23.926 68.358 1.00 67.06 O ANISOU 1133 O ASP A 196 9033 7807 8639 -1353 156 748 O ATOM 1134 CB ASP A 196 29.605 21.329 69.586 1.00 58.06 C ANISOU 1134 CB ASP A 196 8113 6460 7487 -1325 317 1000 C ATOM 1135 CG ASP A 196 30.014 20.917 70.984 1.00 70.46 C ANISOU 1135 CG ASP A 196 9825 8037 8911 -1164 367 1107 C ATOM 1136 OD1 ASP A 196 29.350 21.345 71.951 1.00 76.16 O ANISOU 1136 OD1 ASP A 196 10553 8844 9539 -1112 461 1188 O ATOM 1137 OD2 ASP A 196 31.001 20.163 71.117 1.00 83.85 O ANISOU 1137 OD2 ASP A 196 11626 9658 10574 -1076 314 1112 O ATOM 1138 N GLU A 197 28.550 24.761 70.016 1.00 77.64 N ANISOU 1138 N GLU A 197 10372 9275 9854 -1259 308 864 N ATOM 1139 CA GLU A 197 28.911 26.149 69.742 1.00 78.12 C ANISOU 1139 CA GLU A 197 10374 9421 9888 -1220 218 736 C ATOM 1140 C GLU A 197 30.372 26.457 70.031 1.00 73.62 C ANISOU 1140 C GLU A 197 9876 8868 9230 -1110 95 638 C ATOM 1141 O GLU A 197 30.784 27.608 69.857 1.00 73.48 O ANISOU 1141 O GLU A 197 9817 8904 9198 -1085 14 530 O ATOM 1142 CB GLU A 197 28.020 27.095 70.551 1.00 81.12 C ANISOU 1142 CB GLU A 197 10728 9898 10197 -1152 301 761 C ATOM 1143 CG GLU A 197 26.529 26.932 70.287 1.00103.95 C ANISOU 1143 CG GLU A 197 13510 12802 13186 -1253 425 857 C ATOM 1144 CD GLU A 197 25.861 28.233 69.878 1.00100.73 C ANISOU 1144 CD GLU A 197 12987 12471 12815 -1255 416 796 C ATOM 1145 OE1 GLU A 197 26.041 28.659 68.716 1.00 83.91 O ANISOU 1145 OE1 GLU A 197 10782 10322 10779 -1336 319 715 O ATOM 1146 OE2 GLU A 197 25.164 28.833 70.723 1.00110.97 O ANISOU 1146 OE2 GLU A 197 14278 13847 14040 -1163 512 832 O ATOM 1147 N GLU A 198 31.159 25.476 70.462 1.00 61.99 N ANISOU 1147 N GLU A 198 8502 7346 7707 -1045 76 677 N ATOM 1148 CA GLU A 198 32.560 25.695 70.789 1.00 60.02 C ANISOU 1148 CA GLU A 198 8300 7128 7378 -933 -49 591 C ATOM 1149 C GLU A 198 33.495 25.429 69.619 1.00 61.61 C ANISOU 1149 C GLU A 198 8447 7282 7682 -992 -142 510 C ATOM 1150 O GLU A 198 34.689 25.735 69.719 1.00 57.51 O ANISOU 1150 O GLU A 198 7923 6802 7125 -918 -251 428 O ATOM 1151 CB GLU A 198 32.959 24.822 71.979 1.00 67.04 C ANISOU 1151 CB GLU A 198 9327 8010 8136 -795 -27 684 C ATOM 1152 CG GLU A 198 32.318 25.249 73.287 1.00 76.56 C ANISOU 1152 CG GLU A 198 10605 9296 9187 -693 51 745 C ATOM 1153 CD GLU A 198 30.825 24.986 73.343 1.00 75.56 C ANISOU 1153 CD GLU A 198 10453 9148 9106 -776 223 869 C ATOM 1154 OE1 GLU A 198 30.404 23.869 72.981 1.00 79.20 O ANISOU 1154 OE1 GLU A 198 10924 9509 9661 -862 301 976 O ATOM 1155 OE2 GLU A 198 30.073 25.902 73.739 1.00 74.88 O ANISOU 1155 OE2 GLU A 198 10334 9144 8972 -755 280 855 O ATOM 1156 N LYS A 199 32.989 24.867 68.523 1.00 61.51 N ANISOU 1156 N LYS A 199 8386 7192 7793 -1120 -103 527 N ATOM 1157 CA LYS A 199 33.766 24.715 67.301 1.00 60.04 C ANISOU 1157 CA LYS A 199 8147 6973 7693 -1175 -176 443 C ATOM 1158 C LYS A 199 33.709 25.952 66.414 1.00 59.10 C ANISOU 1158 C LYS A 199 7914 6915 7625 -1252 -223 351 C ATOM 1159 O LYS A 199 34.495 26.055 65.465 1.00 59.71 O ANISOU 1159 O LYS A 199 7943 6993 7752 -1280 -282 277 O ATOM 1160 CB LYS A 199 33.274 23.499 66.508 1.00 54.03 C ANISOU 1160 CB LYS A 199 7410 6094 7025 -1270 -123 489 C ATOM 1161 CG LYS A 199 32.925 22.287 67.358 1.00 60.61 C ANISOU 1161 CG LYS A 199 8361 6835 7835 -1231 -43 612 C ATOM 1162 CD LYS A 199 34.136 21.724 68.081 1.00 63.40 C ANISOU 1162 CD LYS A 199 8810 7174 8104 -1070 -90 624 C ATOM 1163 CE LYS A 199 33.782 20.426 68.792 1.00 68.56 C ANISOU 1163 CE LYS A 199 9598 7709 8744 -1034 -4 765 C ATOM 1164 NZ LYS A 199 34.954 19.823 69.485 1.00 73.43 N ANISOU 1164 NZ LYS A 199 10316 8310 9275 -857 -56 789 N ATOM 1165 N VAL A 200 32.801 26.883 66.697 1.00 55.47 N ANISOU 1165 N VAL A 200 7417 6506 7155 -1276 -188 362 N ATOM 1166 CA VAL A 200 32.699 28.119 65.934 1.00 54.36 C ANISOU 1166 CA VAL A 200 7183 6409 7061 -1334 -229 291 C ATOM 1167 C VAL A 200 32.916 29.362 66.785 1.00 55.02 C ANISOU 1167 C VAL A 200 7273 6555 7077 -1255 -266 240 C ATOM 1168 O VAL A 200 33.232 30.426 66.228 1.00 56.76 O ANISOU 1168 O VAL A 200 7434 6794 7337 -1288 -321 169 O ATOM 1169 CB VAL A 200 31.342 28.208 65.205 1.00 60.76 C ANISOU 1169 CB VAL A 200 7928 7212 7946 -1442 -168 335 C ATOM 1170 CG1 VAL A 200 31.285 27.199 64.070 1.00 60.60 C ANISOU 1170 CG1 VAL A 200 7895 7130 8002 -1539 -171 338 C ATOM 1171 CG2 VAL A 200 30.200 27.980 66.185 1.00 64.11 C ANISOU 1171 CG2 VAL A 200 8374 7648 8338 -1418 -68 429 C ATOM 1172 N PHE A 201 32.758 29.281 68.102 1.00 57.80 N ANISOU 1172 N PHE A 201 7704 6934 7325 -1152 -236 274 N ATOM 1173 CA PHE A 201 33.034 30.389 69.004 1.00 59.37 C ANISOU 1173 CA PHE A 201 7934 7186 7438 -1063 -284 205 C ATOM 1174 C PHE A 201 34.266 30.069 69.836 1.00 58.46 C ANISOU 1174 C PHE A 201 7886 7096 7230 -959 -373 165 C ATOM 1175 O PHE A 201 34.407 28.955 70.351 1.00 59.60 O ANISOU 1175 O PHE A 201 8101 7230 7316 -899 -343 239 O ATOM 1176 CB PHE A 201 31.845 30.669 69.929 1.00 65.46 C ANISOU 1176 CB PHE A 201 8748 7990 8132 -1002 -182 264 C ATOM 1177 CG PHE A 201 30.800 31.564 69.327 1.00 56.70 C ANISOU 1177 CG PHE A 201 7559 6885 7099 -1063 -133 261 C ATOM 1178 CD1 PHE A 201 30.913 32.941 69.422 1.00 56.80 C ANISOU 1178 CD1 PHE A 201 7566 6909 7105 -1029 -186 167 C ATOM 1179 CD2 PHE A 201 29.698 31.030 68.680 1.00 55.22 C ANISOU 1179 CD2 PHE A 201 7300 6685 6995 -1150 -42 353 C ATOM 1180 CE1 PHE A 201 29.952 33.769 68.875 1.00 56.77 C ANISOU 1180 CE1 PHE A 201 7494 6903 7171 -1063 -142 174 C ATOM 1181 CE2 PHE A 201 28.732 31.854 68.133 1.00 58.80 C ANISOU 1181 CE2 PHE A 201 7668 7156 7516 -1189 -9 356 C ATOM 1182 CZ PHE A 201 28.860 33.225 68.231 1.00 58.25 C ANISOU 1182 CZ PHE A 201 7601 7098 7434 -1136 -55 272 C ATOM 1183 N VAL A 202 35.158 31.047 69.958 1.00 62.76 N ANISOU 1183 N VAL A 202 8407 7670 7767 -939 -487 50 N ATOM 1184 CA VAL A 202 36.366 30.926 70.765 1.00 64.01 C ANISOU 1184 CA VAL A 202 8607 7874 7842 -841 -600 -8 C ATOM 1185 C VAL A 202 36.232 31.876 71.946 1.00 70.23 C ANISOU 1185 C VAL A 202 9470 8709 8506 -749 -644 -79 C ATOM 1186 O VAL A 202 36.028 33.082 71.761 1.00 77.09 O ANISOU 1186 O VAL A 202 10311 9564 9418 -792 -669 -161 O ATOM 1187 CB VAL A 202 37.630 31.225 69.947 1.00 61.27 C ANISOU 1187 CB VAL A 202 8152 7529 7597 -903 -711 -94 C ATOM 1188 CG1 VAL A 202 38.775 31.625 70.862 1.00 65.72 C ANISOU 1188 CG1 VAL A 202 8727 8157 8088 -817 -857 -190 C ATOM 1189 CG2 VAL A 202 38.014 30.010 69.126 1.00 64.88 C ANISOU 1189 CG2 VAL A 202 8574 7958 8120 -929 -679 -32 C ATOM 1190 N ASN A 203 36.337 31.327 73.157 1.00 72.31 N ANISOU 1190 N ASN A 203 9844 9022 8607 -612 -650 -46 N ATOM 1191 CA ASN A 203 36.200 32.094 74.394 1.00 67.75 C ANISOU 1191 CA ASN A 203 9368 8502 7871 -497 -689 -116 C ATOM 1192 C ASN A 203 34.861 32.824 74.460 1.00 70.30 C ANISOU 1192 C ASN A 203 9714 8809 8188 -507 -565 -100 C ATOM 1193 O ASN A 203 34.775 33.936 74.988 1.00 72.20 O ANISOU 1193 O ASN A 203 10000 9064 8370 -460 -611 -210 O ATOM 1194 CB ASN A 203 37.363 33.073 74.571 1.00 66.61 C ANISOU 1194 CB ASN A 203 9191 8382 7734 -497 -878 -286 C ATOM 1195 CG ASN A 203 38.713 32.376 74.571 1.00 73.77 C ANISOU 1195 CG ASN A 203 10052 9330 8649 -470 -1006 -301 C ATOM 1196 OD1 ASN A 203 38.807 31.182 74.860 1.00 77.50 O ANISOU 1196 OD1 ASN A 203 10572 9822 9054 -391 -968 -194 O ATOM 1197 ND2 ASN A 203 39.765 33.119 74.247 1.00 59.51 N ANISOU 1197 ND2 ASN A 203 8147 7532 6933 -534 -1154 -430 N ATOM 1198 N ASN A 204 33.826 32.209 73.881 1.00 87.14 N ANISOU 1198 N ASN A 204 11808 10908 10394 -571 -413 29 N ATOM 1199 CA ASN A 204 32.430 32.614 74.023 1.00 89.27 C ANISOU 1199 CA ASN A 204 12083 11184 10653 -562 -270 83 C ATOM 1200 C ASN A 204 32.093 33.891 73.258 1.00 88.12 C ANISOU 1200 C ASN A 204 11858 10998 10624 -636 -291 -5 C ATOM 1201 O ASN A 204 30.920 34.267 73.166 1.00 88.86 O ANISOU 1201 O ASN A 204 11926 11095 10741 -634 -177 41 O ATOM 1202 CB ASN A 204 32.077 32.781 75.506 1.00 91.95 C ANISOU 1202 CB ASN A 204 12560 11598 10779 -393 -222 86 C ATOM 1203 CG ASN A 204 30.585 32.844 75.747 1.00 93.23 C ANISOU 1203 CG ASN A 204 12718 11786 10920 -366 -32 186 C ATOM 1204 OD1 ASN A 204 29.803 32.222 75.029 1.00 91.78 O ANISOU 1204 OD1 ASN A 204 12442 11573 10857 -467 78 304 O ATOM 1205 ND2 ASN A 204 30.179 33.604 76.758 1.00 97.24 N ANISOU 1205 ND2 ASN A 204 13320 12352 11275 -227 6 131 N ATOM 1206 N THR A 205 33.090 34.558 72.691 1.00 64.25 N ANISOU 1206 N THR A 205 8791 7938 7685 -700 -430 -119 N ATOM 1207 CA THR A 205 32.805 35.823 72.018 1.00 60.81 C ANISOU 1207 CA THR A 205 8300 7447 7356 -762 -449 -191 C ATOM 1208 C THR A 205 33.299 35.878 70.581 1.00 61.30 C ANISOU 1208 C THR A 205 8245 7456 7591 -912 -495 -189 C ATOM 1209 O THR A 205 32.603 36.425 69.722 1.00 68.45 O ANISOU 1209 O THR A 205 9089 8323 8597 -977 -447 -163 O ATOM 1210 CB THR A 205 33.415 36.998 72.805 1.00 64.04 C ANISOU 1210 CB THR A 205 8790 7844 7698 -693 -565 -350 C ATOM 1211 OG1 THR A 205 34.824 36.793 72.963 1.00 66.27 O ANISOU 1211 OG1 THR A 205 9067 8141 7973 -712 -715 -426 O ATOM 1212 CG2 THR A 205 32.764 37.129 74.173 1.00 71.23 C ANISOU 1212 CG2 THR A 205 9833 8813 8420 -528 -505 -364 C ATOM 1213 N THR A 206 34.477 35.332 70.294 1.00 61.32 N ANISOU 1213 N THR A 206 8213 7464 7622 -954 -584 -211 N ATOM 1214 CA THR A 206 35.083 35.456 68.976 1.00 52.40 C ANISOU 1214 CA THR A 206 6976 6295 6639 -1082 -623 -218 C ATOM 1215 C THR A 206 34.563 34.363 68.051 1.00 58.69 C ANISOU 1215 C THR A 206 7721 7091 7489 -1145 -534 -105 C ATOM 1216 O THR A 206 34.491 33.193 68.440 1.00 63.17 O ANISOU 1216 O THR A 206 8325 7680 7997 -1102 -494 -41 O ATOM 1217 CB THR A 206 36.606 35.385 69.081 1.00 56.41 C ANISOU 1217 CB THR A 206 7452 6822 7159 -1092 -752 -297 C ATOM 1218 OG1 THR A 206 37.063 36.362 70.024 1.00 57.88 O ANISOU 1218 OG1 THR A 206 7692 7009 7292 -1041 -854 -416 O ATOM 1219 CG2 THR A 206 37.246 35.660 67.728 1.00 61.58 C ANISOU 1219 CG2 THR A 206 7990 7445 7961 -1220 -774 -302 C ATOM 1220 N CYS A 207 34.213 34.746 66.824 1.00 54.64 N ANISOU 1220 N CYS A 207 7132 6544 7084 -1244 -508 -82 N ATOM 1221 CA CYS A 207 33.628 33.831 65.842 1.00 55.44 C ANISOU 1221 CA CYS A 207 7187 6642 7236 -1313 -438 4 C ATOM 1222 C CYS A 207 34.712 33.399 64.859 1.00 59.96 C ANISOU 1222 C CYS A 207 7704 7209 7869 -1380 -485 -16 C ATOM 1223 O CYS A 207 34.919 34.024 63.818 1.00 66.71 O ANISOU 1223 O CYS A 207 8499 8051 8799 -1455 -500 -28 O ATOM 1224 CB CYS A 207 32.457 34.488 65.121 1.00 59.30 C ANISOU 1224 CB CYS A 207 7631 7118 7783 -1362 -384 45 C ATOM 1225 SG CYS A 207 31.755 33.483 63.791 1.00 56.34 S ANISOU 1225 SG CYS A 207 7190 6745 7471 -1462 -334 126 S ATOM 1226 N VAL A 208 35.411 32.316 65.198 1.00 59.47 N ANISOU 1226 N VAL A 208 7667 7160 7769 -1338 -501 -10 N ATOM 1227 CA VAL A 208 36.385 31.694 64.310 1.00 61.67 C ANISOU 1227 CA VAL A 208 7897 7441 8096 -1375 -525 -23 C ATOM 1228 C VAL A 208 36.242 30.184 64.425 1.00 63.08 C ANISOU 1228 C VAL A 208 8128 7598 8243 -1339 -481 32 C ATOM 1229 O VAL A 208 35.800 29.660 65.452 1.00 66.92 O ANISOU 1229 O VAL A 208 8690 8078 8660 -1271 -454 76 O ATOM 1230 CB VAL A 208 37.838 32.121 64.629 1.00 70.70 C ANISOU 1230 CB VAL A 208 8997 8618 9247 -1344 -618 -100 C ATOM 1231 CG1 VAL A 208 38.060 33.589 64.293 1.00 86.81 C ANISOU 1231 CG1 VAL A 208 10980 10650 11352 -1412 -658 -153 C ATOM 1232 CG2 VAL A 208 38.167 31.847 66.084 1.00 59.48 C ANISOU 1232 CG2 VAL A 208 7645 7225 7731 -1229 -671 -120 C ATOM 1233 N LEU A 209 36.621 29.481 63.360 1.00 75.03 N ANISOU 1233 N LEU A 209 9611 9093 9802 -1382 -468 33 N ATOM 1234 CA LEU A 209 36.592 28.025 63.387 1.00 73.37 C ANISOU 1234 CA LEU A 209 9465 8836 9578 -1348 -433 73 C ATOM 1235 C LEU A 209 37.625 27.513 64.384 1.00 75.26 C ANISOU 1235 C LEU A 209 9742 9091 9762 -1225 -480 64 C ATOM 1236 O LEU A 209 38.802 27.879 64.318 1.00 82.76 O ANISOU 1236 O LEU A 209 10629 10092 10724 -1190 -547 6 O ATOM 1237 CB LEU A 209 36.861 27.462 61.992 1.00 67.04 C ANISOU 1237 CB LEU A 209 8634 8010 8827 -1406 -416 51 C ATOM 1238 CG LEU A 209 36.329 26.055 61.722 1.00 59.76 C ANISOU 1238 CG LEU A 209 7789 7003 7913 -1417 -368 88 C ATOM 1239 CD1 LEU A 209 34.822 26.019 61.917 1.00 60.50 C ANISOU 1239 CD1 LEU A 209 7905 7064 8018 -1492 -320 149 C ATOM 1240 CD2 LEU A 209 36.700 25.607 60.319 1.00 56.74 C ANISOU 1240 CD2 LEU A 209 7390 6606 7563 -1459 -363 39 C ATOM 1241 N ASN A 210 37.183 26.666 65.313 1.00 67.44 N ANISOU 1241 N ASN A 210 8849 8062 8713 -1159 -447 132 N ATOM 1242 CA ASN A 210 37.998 26.287 66.461 1.00 67.71 C ANISOU 1242 CA ASN A 210 8937 8123 8667 -1022 -498 140 C ATOM 1243 C ASN A 210 38.445 24.832 66.460 1.00 69.27 C ANISOU 1243 C ASN A 210 9205 8253 8862 -946 -479 188 C ATOM 1244 O ASN A 210 39.530 24.538 66.967 1.00 70.81 O ANISOU 1244 O ASN A 210 9403 8484 9018 -827 -547 171 O ATOM 1245 CB ASN A 210 37.236 26.574 67.763 1.00 60.66 C ANISOU 1245 CB ASN A 210 8123 7250 7675 -968 -474 191 C ATOM 1246 CG ASN A 210 38.031 26.206 69.000 1.00 68.90 C ANISOU 1246 CG ASN A 210 9238 8334 8606 -813 -537 204 C ATOM 1247 OD1 ASN A 210 38.909 26.951 69.431 1.00 72.03 O ANISOU 1247 OD1 ASN A 210 9592 8810 8967 -759 -645 122 O ATOM 1248 ND2 ASN A 210 37.720 25.054 69.584 1.00 72.19 N ANISOU 1248 ND2 ASN A 210 9766 8695 8969 -742 -477 309 N ATOM 1249 N ASP A 211 37.653 23.922 65.908 1.00 65.80 N ANISOU 1249 N ASP A 211 8821 7711 8468 -1010 -398 242 N ATOM 1250 CA ASP A 211 37.982 22.500 65.968 1.00 59.60 C ANISOU 1250 CA ASP A 211 8131 6828 7688 -936 -373 292 C ATOM 1251 C ASP A 211 39.225 22.217 65.134 1.00 61.10 C ANISOU 1251 C ASP A 211 8266 7030 7920 -884 -422 214 C ATOM 1252 O ASP A 211 39.232 22.510 63.931 1.00 63.40 O ANISOU 1252 O ASP A 211 8486 7329 8274 -975 -412 149 O ATOM 1253 CB ASP A 211 36.802 21.664 65.477 1.00 69.63 C ANISOU 1253 CB ASP A 211 9466 7970 9018 -1046 -282 351 C ATOM 1254 CG ASP A 211 36.886 20.211 65.916 1.00 73.11 C ANISOU 1254 CG ASP A 211 10044 8277 9457 -971 -241 434 C ATOM 1255 OD1 ASP A 211 37.990 19.629 65.871 1.00 76.14 O ANISOU 1255 OD1 ASP A 211 10458 8640 9833 -849 -283 409 O ATOM 1256 OD2 ASP A 211 35.840 19.645 66.297 1.00 70.53 O ANISOU 1256 OD2 ASP A 211 9792 7860 9147 -1033 -161 531 O ATOM 1257 N PRO A 212 40.285 21.648 65.717 1.00 62.24 N ANISOU 1257 N PRO A 212 8436 7185 8025 -728 -471 223 N ATOM 1258 CA PRO A 212 41.530 21.467 64.946 1.00 61.59 C ANISOU 1258 CA PRO A 212 8272 7142 7988 -664 -510 147 C ATOM 1259 C PRO A 212 41.387 20.513 63.772 1.00 57.50 C ANISOU 1259 C PRO A 212 7803 6509 7536 -698 -444 126 C ATOM 1260 O PRO A 212 41.777 20.857 62.647 1.00 56.98 O ANISOU 1260 O PRO A 212 7648 6488 7516 -748 -437 47 O ATOM 1261 CB PRO A 212 42.516 20.936 66.000 1.00 61.71 C ANISOU 1261 CB PRO A 212 8319 7188 7940 -471 -578 182 C ATOM 1262 CG PRO A 212 41.914 21.297 67.325 1.00 63.97 C ANISOU 1262 CG PRO A 212 8676 7501 8129 -449 -597 251 C ATOM 1263 CD PRO A 212 40.435 21.244 67.124 1.00 63.48 C ANISOU 1263 CD PRO A 212 8688 7346 8086 -591 -495 304 C ATOM 1264 N ASN A 213 40.836 19.318 64.007 1.00 61.62 N ANISOU 1264 N ASN A 213 8473 6877 8061 -673 -392 194 N ATOM 1265 CA ASN A 213 40.733 18.323 62.944 1.00 64.08 C ANISOU 1265 CA ASN A 213 8856 7056 8436 -697 -341 157 C ATOM 1266 C ASN A 213 39.987 18.875 61.740 1.00 61.63 C ANISOU 1266 C ASN A 213 8488 6760 8167 -874 -315 88 C ATOM 1267 O ASN A 213 40.388 18.645 60.594 1.00 64.84 O ANISOU 1267 O ASN A 213 8878 7160 8600 -878 -303 4 O ATOM 1268 CB ASN A 213 40.038 17.063 63.461 1.00 71.71 C ANISOU 1268 CB ASN A 213 9999 7830 9416 -684 -288 250 C ATOM 1269 CG ASN A 213 40.925 16.237 64.370 1.00 79.20 C ANISOU 1269 CG ASN A 213 11034 8735 10326 -477 -310 316 C ATOM 1270 OD1 ASN A 213 41.885 15.612 63.918 1.00 86.22 O ANISOU 1270 OD1 ASN A 213 11934 9592 11235 -348 -323 267 O ATOM 1271 ND2 ASN A 213 40.600 16.218 65.658 1.00 70.00 N ANISOU 1271 ND2 ASN A 213 9932 7571 9095 -428 -309 433 N ATOM 1272 N PHE A 214 38.898 19.605 61.978 1.00 59.76 N ANISOU 1272 N PHE A 214 8224 6553 7927 -1007 -304 125 N ATOM 1273 CA PHE A 214 38.138 20.158 60.865 1.00 63.68 C ANISOU 1273 CA PHE A 214 8664 7073 8457 -1163 -292 71 C ATOM 1274 C PHE A 214 38.941 21.212 60.118 1.00 56.82 C ANISOU 1274 C PHE A 214 7665 6348 7578 -1161 -323 -5 C ATOM 1275 O PHE A 214 38.920 21.247 58.884 1.00 57.98 O ANISOU 1275 O PHE A 214 7789 6503 7737 -1219 -310 -71 O ATOM 1276 CB PHE A 214 36.810 20.717 61.367 1.00 66.96 C ANISOU 1276 CB PHE A 214 9067 7498 8878 -1282 -272 137 C ATOM 1277 CG PHE A 214 35.861 19.653 61.828 1.00 78.46 C ANISOU 1277 CG PHE A 214 10635 8807 10368 -1328 -221 216 C ATOM 1278 CD1 PHE A 214 36.001 19.080 63.078 1.00 78.90 C ANISOU 1278 CD1 PHE A 214 10778 8809 10391 -1229 -196 313 C ATOM 1279 CD2 PHE A 214 34.851 19.199 61.000 1.00 90.73 C ANISOU 1279 CD2 PHE A 214 12209 10275 11988 -1473 -201 198 C ATOM 1280 CE1 PHE A 214 35.142 18.089 63.507 1.00 83.83 C ANISOU 1280 CE1 PHE A 214 11507 9287 11056 -1280 -132 405 C ATOM 1281 CE2 PHE A 214 33.988 18.205 61.421 1.00105.54 C ANISOU 1281 CE2 PHE A 214 14176 12005 13918 -1537 -151 275 C ATOM 1282 CZ PHE A 214 34.132 17.651 62.678 1.00 92.62 C ANISOU 1282 CZ PHE A 214 12627 10306 12257 -1444 -107 386 C ATOM 1283 N VAL A 215 39.680 22.055 60.841 1.00 52.95 N ANISOU 1283 N VAL A 215 7089 5968 7060 -1094 -365 2 N ATOM 1284 CA VAL A 215 40.527 23.045 60.180 1.00 56.81 C ANISOU 1284 CA VAL A 215 7445 6583 7559 -1103 -388 -59 C ATOM 1285 C VAL A 215 41.535 22.356 59.266 1.00 59.52 C ANISOU 1285 C VAL A 215 7774 6927 7914 -1024 -365 -117 C ATOM 1286 O VAL A 215 41.674 22.709 58.088 1.00 64.31 O ANISOU 1286 O VAL A 215 8328 7581 8528 -1079 -335 -166 O ATOM 1287 CB VAL A 215 41.226 23.939 61.221 1.00 53.59 C ANISOU 1287 CB VAL A 215 6952 6275 7133 -1046 -452 -51 C ATOM 1288 CG1 VAL A 215 42.300 24.786 60.556 1.00 55.23 C ANISOU 1288 CG1 VAL A 215 7013 6597 7376 -1054 -473 -108 C ATOM 1289 CG2 VAL A 215 40.212 24.825 61.923 1.00 52.04 C ANISOU 1289 CG2 VAL A 215 6767 6089 6917 -1125 -465 -14 C ATOM 1290 N LEU A 216 42.227 21.336 59.783 1.00 59.27 N ANISOU 1290 N LEU A 216 7799 6843 7877 -880 -371 -108 N ATOM 1291 CA LEU A 216 43.261 20.671 58.990 1.00 55.41 C ANISOU 1291 CA LEU A 216 7292 6362 7399 -772 -342 -167 C ATOM 1292 C LEU A 216 42.667 19.939 57.791 1.00 59.01 C ANISOU 1292 C LEU A 216 7850 6715 7855 -827 -283 -218 C ATOM 1293 O LEU A 216 43.162 20.072 56.663 1.00 63.53 O ANISOU 1293 O LEU A 216 8371 7349 8418 -822 -245 -284 O ATOM 1294 CB LEU A 216 44.060 19.701 59.860 1.00 48.90 C ANISOU 1294 CB LEU A 216 6517 5492 6570 -586 -366 -137 C ATOM 1295 CG LEU A 216 45.226 20.271 60.665 1.00 42.57 C ANISOU 1295 CG LEU A 216 5573 4834 5766 -477 -437 -128 C ATOM 1296 CD1 LEU A 216 44.726 20.980 61.898 1.00 45.91 C ANISOU 1296 CD1 LEU A 216 6000 5289 6155 -522 -503 -72 C ATOM 1297 CD2 LEU A 216 46.195 19.169 61.043 1.00 44.21 C ANISOU 1297 CD2 LEU A 216 5815 5011 5974 -264 -449 -118 C ATOM 1298 N ILE A 217 41.613 19.150 58.014 1.00 53.81 N ANISOU 1298 N ILE A 217 7337 5903 7205 -882 -275 -190 N ATOM 1299 CA ILE A 217 41.039 18.364 56.926 1.00 53.84 C ANISOU 1299 CA ILE A 217 7449 5794 7214 -940 -241 -256 C ATOM 1300 C ILE A 217 40.437 19.275 55.864 1.00 58.78 C ANISOU 1300 C ILE A 217 8008 6510 7817 -1086 -239 -299 C ATOM 1301 O ILE A 217 40.611 19.043 54.662 1.00 59.90 O ANISOU 1301 O ILE A 217 8172 6659 7927 -1086 -214 -383 O ATOM 1302 CB ILE A 217 40.008 17.360 57.469 1.00 46.96 C ANISOU 1302 CB ILE A 217 6733 4731 6380 -993 -238 -209 C ATOM 1303 CG1 ILE A 217 40.661 16.415 58.483 1.00 53.50 C ANISOU 1303 CG1 ILE A 217 7648 5461 7220 -828 -234 -150 C ATOM 1304 CG2 ILE A 217 39.387 16.570 56.328 1.00 43.22 C ANISOU 1304 CG2 ILE A 217 6370 4133 5921 -1074 -224 -297 C ATOM 1305 CD1 ILE A 217 41.955 15.783 58.007 1.00 56.93 C ANISOU 1305 CD1 ILE A 217 8094 5892 7645 -644 -218 -219 C ATOM 1306 N GLY A 218 39.719 20.322 56.280 1.00 58.45 N ANISOU 1306 N GLY A 218 7890 6538 7780 -1198 -265 -242 N ATOM 1307 CA GLY A 218 39.172 21.259 55.319 1.00 54.98 C ANISOU 1307 CA GLY A 218 7385 6187 7318 -1318 -268 -266 C ATOM 1308 C GLY A 218 40.234 22.024 54.560 1.00 54.17 C ANISOU 1308 C GLY A 218 7175 6225 7184 -1272 -244 -300 C ATOM 1309 O GLY A 218 40.049 22.338 53.384 1.00 57.80 O ANISOU 1309 O GLY A 218 7626 6735 7601 -1326 -225 -340 O ATOM 1310 N SER A 219 41.356 22.340 55.212 1.00 57.62 N ANISOU 1310 N SER A 219 7522 6732 7639 -1173 -244 -280 N ATOM 1311 CA SER A 219 42.441 23.013 54.506 1.00 62.38 C ANISOU 1311 CA SER A 219 8003 7468 8232 -1137 -208 -304 C ATOM 1312 C SER A 219 43.098 22.091 53.487 1.00 61.81 C ANISOU 1312 C SER A 219 7978 7387 8120 -1039 -145 -378 C ATOM 1313 O SER A 219 43.497 22.538 52.405 1.00 66.47 O ANISOU 1313 O SER A 219 8512 8074 8670 -1049 -91 -404 O ATOM 1314 CB SER A 219 43.469 23.535 55.507 1.00 66.24 C ANISOU 1314 CB SER A 219 8367 8035 8765 -1066 -239 -272 C ATOM 1315 OG SER A 219 42.912 24.556 56.318 1.00 56.67 O ANISOU 1315 OG SER A 219 7115 6843 7575 -1156 -293 -223 O ATOM 1316 N PHE A 220 43.227 20.804 53.810 1.00 62.39 N ANISOU 1316 N PHE A 220 8163 7342 8200 -934 -145 -408 N ATOM 1317 CA PHE A 220 43.849 19.887 52.861 1.00 61.69 C ANISOU 1317 CA PHE A 220 8138 7230 8072 -820 -83 -492 C ATOM 1318 C PHE A 220 42.918 19.508 51.715 1.00 65.06 C ANISOU 1318 C PHE A 220 8695 7590 8436 -906 -72 -564 C ATOM 1319 O PHE A 220 43.391 19.281 50.596 1.00 71.02 O ANISOU 1319 O PHE A 220 9470 8392 9122 -846 -12 -639 O ATOM 1320 CB PHE A 220 44.343 18.632 53.580 1.00 72.61 C ANISOU 1320 CB PHE A 220 9611 8491 9488 -661 -88 -502 C ATOM 1321 CG PHE A 220 45.712 18.781 54.180 1.00 92.40 C ANISOU 1321 CG PHE A 220 11976 11106 12027 -507 -82 -474 C ATOM 1322 CD1 PHE A 220 45.874 19.315 55.448 1.00 91.87 C ANISOU 1322 CD1 PHE A 220 11823 11082 12003 -510 -151 -395 C ATOM 1323 CD2 PHE A 220 46.839 18.395 53.472 1.00104.06 C ANISOU 1323 CD2 PHE A 220 13399 12651 13488 -355 -10 -531 C ATOM 1324 CE1 PHE A 220 47.133 19.457 56.003 1.00 90.87 C ANISOU 1324 CE1 PHE A 220 11553 11066 11908 -374 -168 -377 C ATOM 1325 CE2 PHE A 220 48.101 18.535 54.021 1.00108.19 C ANISOU 1325 CE2 PHE A 220 13764 13290 14055 -215 -12 -503 C ATOM 1326 CZ PHE A 220 48.248 19.067 55.288 1.00 95.31 C ANISOU 1326 CZ PHE A 220 12040 11702 12471 -230 -100 -428 C ATOM 1327 N VAL A 221 41.606 19.440 51.957 1.00 57.31 N ANISOU 1327 N VAL A 221 7794 6511 7472 -1043 -130 -545 N ATOM 1328 CA VAL A 221 40.658 19.030 50.921 1.00 54.33 C ANISOU 1328 CA VAL A 221 7532 6068 7042 -1136 -147 -621 C ATOM 1329 C VAL A 221 40.031 20.217 50.189 1.00 54.41 C ANISOU 1329 C VAL A 221 7465 6208 7000 -1265 -164 -599 C ATOM 1330 O VAL A 221 39.400 20.021 49.138 1.00 62.47 O ANISOU 1330 O VAL A 221 8563 7222 7950 -1325 -184 -669 O ATOM 1331 CB VAL A 221 39.564 18.114 51.519 1.00 51.81 C ANISOU 1331 CB VAL A 221 7342 5557 6787 -1216 -202 -618 C ATOM 1332 CG1 VAL A 221 38.709 17.476 50.433 1.00 48.00 C ANISOU 1332 CG1 VAL A 221 6986 4990 6263 -1303 -235 -725 C ATOM 1333 CG2 VAL A 221 40.202 17.025 52.365 1.00 57.79 C ANISOU 1333 CG2 VAL A 221 8182 6178 7599 -1079 -181 -609 C ATOM 1334 N ALA A 222 40.215 21.439 50.681 1.00 51.83 N ANISOU 1334 N ALA A 222 6997 5997 6700 -1301 -163 -508 N ATOM 1335 CA ALA A 222 39.659 22.613 50.033 1.00 50.05 C ANISOU 1335 CA ALA A 222 6704 5880 6433 -1407 -175 -471 C ATOM 1336 C ALA A 222 40.707 23.621 49.593 1.00 57.32 C ANISOU 1336 C ALA A 222 7501 6952 7327 -1366 -109 -434 C ATOM 1337 O ALA A 222 40.380 24.516 48.807 1.00 66.68 O ANISOU 1337 O ALA A 222 8652 8224 8458 -1435 -101 -403 O ATOM 1338 CB ALA A 222 38.652 23.316 50.958 1.00 47.53 C ANISOU 1338 CB ALA A 222 6338 5541 6181 -1516 -234 -387 C ATOM 1339 N PHE A 223 41.939 23.529 50.087 1.00 55.15 N ANISOU 1339 N PHE A 223 7149 6712 7094 -1260 -63 -427 N ATOM 1340 CA PHE A 223 43.004 24.400 49.612 1.00 55.07 C ANISOU 1340 CA PHE A 223 7004 6846 7075 -1231 10 -393 C ATOM 1341 C PHE A 223 44.164 23.637 48.995 1.00 62.39 C ANISOU 1341 C PHE A 223 7926 7821 7961 -1084 99 -455 C ATOM 1342 O PHE A 223 44.536 23.908 47.849 1.00 61.91 O ANISOU 1342 O PHE A 223 7847 7859 7816 -1067 182 -465 O ATOM 1343 CB PHE A 223 43.513 25.289 50.755 1.00 49.64 C ANISOU 1343 CB PHE A 223 6174 6195 6491 -1253 -20 -320 C ATOM 1344 CG PHE A 223 44.306 26.470 50.288 1.00 48.91 C ANISOU 1344 CG PHE A 223 5935 6233 6417 -1289 40 -266 C ATOM 1345 CD1 PHE A 223 43.668 27.569 49.743 1.00 50.61 C ANISOU 1345 CD1 PHE A 223 6139 6480 6610 -1407 42 -207 C ATOM 1346 CD2 PHE A 223 45.687 26.483 50.389 1.00 46.11 C ANISOU 1346 CD2 PHE A 223 5444 5966 6110 -1206 95 -265 C ATOM 1347 CE1 PHE A 223 44.389 28.662 49.307 1.00 49.11 C ANISOU 1347 CE1 PHE A 223 5823 6388 6447 -1450 106 -142 C ATOM 1348 CE2 PHE A 223 46.415 27.575 49.954 1.00 45.94 C ANISOU 1348 CE2 PHE A 223 5275 6057 6125 -1261 159 -205 C ATOM 1349 CZ PHE A 223 45.765 28.665 49.413 1.00 48.20 C ANISOU 1349 CZ PHE A 223 5569 6355 6390 -1388 168 -140 C ATOM 1350 N PHE A 224 44.738 22.671 49.716 1.00 61.37 N ANISOU 1350 N PHE A 224 7814 7623 7879 -963 91 -491 N ATOM 1351 CA PHE A 224 46.000 22.080 49.283 1.00 63.45 C ANISOU 1351 CA PHE A 224 8033 7951 8124 -799 182 -537 C ATOM 1352 C PHE A 224 45.815 21.185 48.063 1.00 65.96 C ANISOU 1352 C PHE A 224 8505 8233 8324 -731 240 -640 C ATOM 1353 O PHE A 224 46.589 21.267 47.103 1.00 73.76 O ANISOU 1353 O PHE A 224 9447 9338 9240 -651 349 -664 O ATOM 1354 CB PHE A 224 46.634 21.314 50.443 1.00 76.34 C ANISOU 1354 CB PHE A 224 9647 9519 9841 -672 144 -539 C ATOM 1355 CG PHE A 224 47.046 22.197 51.589 1.00 95.80 C ANISOU 1355 CG PHE A 224 11949 12049 12402 -712 85 -457 C ATOM 1356 CD1 PHE A 224 47.620 23.435 51.351 1.00 93.72 C ANISOU 1356 CD1 PHE A 224 11506 11934 12171 -784 118 -405 C ATOM 1357 CD2 PHE A 224 46.844 21.801 52.900 1.00 93.69 C ANISOU 1357 CD2 PHE A 224 11719 11689 12189 -682 -6 -433 C ATOM 1358 CE1 PHE A 224 47.996 24.255 52.399 1.00 81.62 C ANISOU 1358 CE1 PHE A 224 9833 10449 10730 -831 48 -351 C ATOM 1359 CE2 PHE A 224 47.217 22.618 53.953 1.00 77.90 C ANISOU 1359 CE2 PHE A 224 9584 9755 10258 -712 -73 -375 C ATOM 1360 CZ PHE A 224 47.794 23.846 53.700 1.00 70.54 C ANISOU 1360 CZ PHE A 224 8473 8963 9364 -790 -54 -344 C ATOM 1361 N ILE A 225 44.795 20.324 48.076 1.00 59.29 N ANISOU 1361 N ILE A 225 7844 7227 7455 -765 172 -703 N ATOM 1362 CA ILE A 225 44.518 19.491 46.903 1.00 55.80 C ANISOU 1362 CA ILE A 225 7569 6737 6897 -717 204 -823 C ATOM 1363 C ILE A 225 44.137 20.325 45.682 1.00 55.08 C ANISOU 1363 C ILE A 225 7472 6776 6682 -803 235 -821 C ATOM 1364 O ILE A 225 44.739 20.124 44.612 1.00 53.02 O ANISOU 1364 O ILE A 225 7241 6601 6303 -700 331 -883 O ATOM 1365 CB ILE A 225 43.462 18.425 47.248 1.00 48.33 C ANISOU 1365 CB ILE A 225 6810 5574 5977 -766 109 -889 C ATOM 1366 CG1 ILE A 225 44.067 17.334 48.132 1.00 49.87 C ANISOU 1366 CG1 ILE A 225 7057 5634 6258 -621 113 -907 C ATOM 1367 CG2 ILE A 225 42.870 17.823 45.984 1.00 54.22 C ANISOU 1367 CG2 ILE A 225 7728 6273 6599 -780 101 -1020 C ATOM 1368 CD1 ILE A 225 43.079 16.259 48.528 1.00 53.38 C ANISOU 1368 CD1 ILE A 225 7690 5844 6750 -676 35 -954 C ATOM 1369 N PRO A 226 43.160 21.245 45.751 1.00 53.51 N ANISOU 1369 N PRO A 226 7244 6599 6490 -971 163 -749 N ATOM 1370 CA PRO A 226 42.847 22.041 44.551 1.00 55.37 C ANISOU 1370 CA PRO A 226 7481 6962 6595 -1030 193 -733 C ATOM 1371 C PRO A 226 44.017 22.878 44.074 1.00 58.48 C ANISOU 1371 C PRO A 226 7730 7532 6956 -968 326 -660 C ATOM 1372 O PRO A 226 44.252 22.973 42.863 1.00 61.57 O ANISOU 1372 O PRO A 226 8163 8029 7200 -920 409 -686 O ATOM 1373 CB PRO A 226 41.668 22.915 45.006 1.00 53.58 C ANISOU 1373 CB PRO A 226 7221 6715 6421 -1201 88 -648 C ATOM 1374 CG PRO A 226 41.097 22.213 46.186 1.00 53.61 C ANISOU 1374 CG PRO A 226 7266 6557 6545 -1236 0 -664 C ATOM 1375 CD PRO A 226 42.271 21.601 46.873 1.00 54.68 C ANISOU 1375 CD PRO A 226 7363 6664 6751 -1098 59 -677 C ATOM 1376 N LEU A 227 44.770 23.477 44.999 1.00 56.92 N ANISOU 1376 N LEU A 227 7361 7373 6892 -969 350 -570 N ATOM 1377 CA LEU A 227 45.927 24.276 44.609 1.00 55.24 C ANISOU 1377 CA LEU A 227 6983 7322 6682 -931 478 -494 C ATOM 1378 C LEU A 227 46.983 23.418 43.927 1.00 58.05 C ANISOU 1378 C LEU A 227 7349 7744 6963 -748 605 -572 C ATOM 1379 O LEU A 227 47.582 23.833 42.927 1.00 63.11 O ANISOU 1379 O LEU A 227 7940 8530 7509 -707 737 -541 O ATOM 1380 CB LEU A 227 46.518 24.973 45.832 1.00 50.51 C ANISOU 1380 CB LEU A 227 6199 6735 6256 -974 451 -407 C ATOM 1381 CG LEU A 227 47.431 26.170 45.585 1.00 51.61 C ANISOU 1381 CG LEU A 227 6143 7022 6444 -1018 548 -299 C ATOM 1382 CD1 LEU A 227 46.598 27.384 45.218 1.00 50.60 C ANISOU 1382 CD1 LEU A 227 6029 6906 6292 -1176 523 -207 C ATOM 1383 CD2 LEU A 227 48.286 26.442 46.808 1.00 51.14 C ANISOU 1383 CD2 LEU A 227 5904 6972 6554 -1013 513 -264 C ATOM 1384 N THR A 228 47.235 22.220 44.461 1.00 55.65 N ANISOU 1384 N THR A 228 7111 7333 6699 -626 578 -665 N ATOM 1385 CA THR A 228 48.228 21.331 43.869 1.00 52.88 C ANISOU 1385 CA THR A 228 6779 7030 6283 -424 698 -749 C ATOM 1386 C THR A 228 47.821 20.920 42.461 1.00 58.15 C ANISOU 1386 C THR A 228 7627 7719 6748 -380 754 -846 C ATOM 1387 O THR A 228 48.641 20.940 41.530 1.00 62.91 O ANISOU 1387 O THR A 228 8195 8465 7244 -262 906 -858 O ATOM 1388 CB THR A 228 48.416 20.098 44.755 1.00 51.31 C ANISOU 1388 CB THR A 228 6651 6676 6169 -300 639 -826 C ATOM 1389 OG1 THR A 228 48.808 20.509 46.070 1.00 50.41 O ANISOU 1389 OG1 THR A 228 6373 6560 6219 -331 577 -735 O ATOM 1390 CG2 THR A 228 49.482 19.181 44.176 1.00 54.18 C ANISOU 1390 CG2 THR A 228 7030 7082 6474 -66 767 -915 C ATOM 1391 N ILE A 229 46.550 20.546 42.286 1.00 55.81 N ANISOU 1391 N ILE A 229 7520 7292 6392 -473 631 -916 N ATOM 1392 CA ILE A 229 46.073 20.182 40.955 1.00 54.65 C ANISOU 1392 CA ILE A 229 7555 7168 6040 -443 652 -1023 C ATOM 1393 C ILE A 229 46.207 21.366 40.009 1.00 60.70 C ANISOU 1393 C ILE A 229 8243 8137 6685 -493 744 -921 C ATOM 1394 O ILE A 229 46.656 21.221 38.864 1.00 70.05 O ANISOU 1394 O ILE A 229 9488 9437 7690 -380 865 -970 O ATOM 1395 CB ILE A 229 44.622 19.671 41.021 1.00 52.59 C ANISOU 1395 CB ILE A 229 7479 6738 5766 -567 478 -1107 C ATOM 1396 CG1 ILE A 229 44.531 18.427 41.906 1.00 52.66 C ANISOU 1396 CG1 ILE A 229 7582 6530 5894 -515 408 -1197 C ATOM 1397 CG2 ILE A 229 44.101 19.369 39.624 1.00 54.25 C ANISOU 1397 CG2 ILE A 229 7872 6987 5753 -546 472 -1227 C ATOM 1398 CD1 ILE A 229 43.124 17.897 42.070 1.00 52.19 C ANISOU 1398 CD1 ILE A 229 7680 6294 5857 -657 245 -1267 C ATOM 1399 N MET A 230 45.839 22.558 40.481 1.00 64.38 N ANISOU 1399 N MET A 230 8579 8641 7241 -654 698 -774 N ATOM 1400 CA MET A 230 45.957 23.768 39.676 1.00 66.30 C ANISOU 1400 CA MET A 230 8746 9052 7392 -712 786 -649 C ATOM 1401 C MET A 230 47.389 23.979 39.201 1.00 67.11 C ANISOU 1401 C MET A 230 8712 9319 7467 -586 993 -597 C ATOM 1402 O MET A 230 47.636 24.176 38.005 1.00 70.89 O ANISOU 1402 O MET A 230 9239 9935 7760 -523 1116 -585 O ATOM 1403 CB MET A 230 45.472 24.960 40.501 1.00 66.06 C ANISOU 1403 CB MET A 230 8588 9000 7511 -889 704 -504 C ATOM 1404 CG MET A 230 45.770 26.328 39.929 1.00 66.87 C ANISOU 1404 CG MET A 230 8581 9246 7581 -957 803 -343 C ATOM 1405 SD MET A 230 45.389 27.603 41.148 1.00 71.40 S ANISOU 1405 SD MET A 230 9004 9752 8373 -1140 705 -200 S ATOM 1406 CE MET A 230 43.767 27.071 41.691 1.00 62.86 C ANISOU 1406 CE MET A 230 8078 8506 7299 -1216 494 -287 C ATOM 1407 N VAL A 231 48.349 23.915 40.126 1.00 59.87 N ANISOU 1407 N VAL A 231 7619 8401 6729 -542 1033 -563 N ATOM 1408 CA VAL A 231 49.743 24.202 39.788 1.00 59.61 C ANISOU 1408 CA VAL A 231 7402 8537 6709 -440 1228 -496 C ATOM 1409 C VAL A 231 50.280 23.173 38.801 1.00 62.41 C ANISOU 1409 C VAL A 231 7870 8956 6886 -226 1360 -621 C ATOM 1410 O VAL A 231 50.911 23.521 37.793 1.00 66.00 O ANISOU 1410 O VAL A 231 8281 9584 7211 -156 1541 -570 O ATOM 1411 CB VAL A 231 50.604 24.261 41.063 1.00 54.75 C ANISOU 1411 CB VAL A 231 6570 7905 6329 -433 1208 -453 C ATOM 1412 CG1 VAL A 231 52.079 24.356 40.704 1.00 62.05 C ANISOU 1412 CG1 VAL A 231 7288 9009 7277 -309 1406 -404 C ATOM 1413 CG2 VAL A 231 50.189 25.438 41.931 1.00 55.28 C ANISOU 1413 CG2 VAL A 231 6521 7933 6551 -640 1101 -330 C ATOM 1414 N ILE A 232 50.039 21.887 39.076 1.00 60.99 N ANISOU 1414 N ILE A 232 7846 8630 6696 -114 1280 -783 N ATOM 1415 CA ILE A 232 50.586 20.837 38.219 1.00 60.37 C ANISOU 1415 CA ILE A 232 7891 8587 6461 111 1401 -923 C ATOM 1416 C ILE A 232 49.984 20.920 36.820 1.00 61.64 C ANISOU 1416 C ILE A 232 8246 8821 6353 117 1442 -975 C ATOM 1417 O ILE A 232 50.700 20.846 35.809 1.00 65.27 O ANISOU 1417 O ILE A 232 8712 9440 6646 266 1628 -991 O ATOM 1418 CB ILE A 232 50.360 19.455 38.857 1.00 60.35 C ANISOU 1418 CB ILE A 232 8040 8371 6520 216 1289 -1084 C ATOM 1419 CG1 ILE A 232 51.199 19.317 40.131 1.00 59.75 C ANISOU 1419 CG1 ILE A 232 7764 8264 6675 268 1279 -1025 C ATOM 1420 CG2 ILE A 232 50.692 18.348 37.870 1.00 63.00 C ANISOU 1420 CG2 ILE A 232 8562 8703 6670 440 1390 -1258 C ATOM 1421 CD1 ILE A 232 50.994 18.010 40.863 1.00 59.77 C ANISOU 1421 CD1 ILE A 232 7914 8044 6752 371 1172 -1150 C ATOM 1422 N THR A 233 48.659 21.086 36.739 1.00 61.31 N ANISOU 1422 N THR A 233 8358 8677 6258 -39 1270 -1001 N ATOM 1423 CA THR A 233 48.011 21.179 35.437 1.00 67.14 C ANISOU 1423 CA THR A 233 9285 9492 6733 -36 1275 -1054 C ATOM 1424 C THR A 233 48.497 22.396 34.664 1.00 67.69 C ANISOU 1424 C THR A 233 9232 9789 6699 -59 1441 -877 C ATOM 1425 O THR A 233 48.757 22.305 33.460 1.00 78.27 O ANISOU 1425 O THR A 233 10675 11269 7794 63 1572 -911 O ATOM 1426 CB THR A 233 46.491 21.224 35.600 1.00 65.81 C ANISOU 1426 CB THR A 233 9258 9185 6560 -213 1043 -1095 C ATOM 1427 OG1 THR A 233 46.140 22.229 36.559 1.00 68.92 O ANISOU 1427 OG1 THR A 233 9482 9551 7151 -397 964 -929 O ATOM 1428 CG2 THR A 233 45.962 19.872 36.058 1.00 60.01 C ANISOU 1428 CG2 THR A 233 8694 8227 5880 -181 901 -1289 C ATOM 1429 N TYR A 234 48.636 23.542 35.337 1.00 64.59 N ANISOU 1429 N TYR A 234 8628 9429 6483 -211 1444 -686 N ATOM 1430 CA TYR A 234 49.088 24.742 34.643 1.00 67.84 C ANISOU 1430 CA TYR A 234 8924 10031 6823 -253 1605 -498 C ATOM 1431 C TYR A 234 50.507 24.575 34.113 1.00 74.85 C ANISOU 1431 C TYR A 234 9690 11092 7660 -79 1863 -472 C ATOM 1432 O TYR A 234 50.805 24.986 32.984 1.00 79.95 O ANISOU 1432 O TYR A 234 10366 11910 8101 -18 2032 -400 O ATOM 1433 CB TYR A 234 48.999 25.955 35.569 1.00 67.75 C ANISOU 1433 CB TYR A 234 8713 9984 7043 -453 1548 -315 C ATOM 1434 CG TYR A 234 49.481 27.234 34.926 1.00 66.81 C ANISOU 1434 CG TYR A 234 8472 10028 6885 -517 1714 -106 C ATOM 1435 CD1 TYR A 234 48.721 27.874 33.956 1.00 74.53 C ANISOU 1435 CD1 TYR A 234 9589 11067 7662 -565 1710 -30 C ATOM 1436 CD2 TYR A 234 50.697 27.801 35.283 1.00 67.68 C ANISOU 1436 CD2 TYR A 234 8324 10228 7162 -531 1873 21 C ATOM 1437 CE1 TYR A 234 49.158 29.042 33.360 1.00 71.05 C ANISOU 1437 CE1 TYR A 234 9052 10759 7185 -621 1873 181 C ATOM 1438 CE2 TYR A 234 51.142 28.970 34.692 1.00 70.03 C ANISOU 1438 CE2 TYR A 234 8510 10658 7442 -607 2035 224 C ATOM 1439 CZ TYR A 234 50.368 29.584 33.730 1.00 63.61 C ANISOU 1439 CZ TYR A 234 7856 9889 6424 -649 2041 309 C ATOM 1440 OH TYR A 234 50.802 30.748 33.139 1.00 64.49 O ANISOU 1440 OH TYR A 234 7872 10116 6518 -723 2211 530 O ATOM 1441 N CYS A 235 51.399 23.977 34.908 1.00 81.71 N ANISOU 1441 N CYS A 235 10414 11927 8705 13 1902 -520 N ATOM 1442 CA CYS A 235 52.773 23.794 34.447 1.00 83.27 C ANISOU 1442 CA CYS A 235 10464 12302 8873 191 2152 -494 C ATOM 1443 C CYS A 235 52.836 22.841 33.257 1.00 86.86 C ANISOU 1443 C CYS A 235 11142 12822 9037 414 2261 -652 C ATOM 1444 O CYS A 235 53.516 23.120 32.259 1.00 99.52 O ANISOU 1444 O CYS A 235 12711 14630 10474 521 2490 -586 O ATOM 1445 CB CYS A 235 53.655 23.298 35.593 1.00 84.04 C ANISOU 1445 CB CYS A 235 10360 12349 9223 258 2142 -521 C ATOM 1446 SG CYS A 235 54.171 24.605 36.732 1.00 83.27 S ANISOU 1446 SG CYS A 235 9920 12279 9439 42 2114 -310 S ATOM 1447 N LEU A 236 52.118 21.715 33.332 1.00 77.82 N ANISOU 1447 N LEU A 236 10241 11505 7824 485 2102 -864 N ATOM 1448 CA LEU A 236 52.120 20.787 32.203 1.00 82.44 C ANISOU 1448 CA LEU A 236 11068 12130 8126 694 2183 -1043 C ATOM 1449 C LEU A 236 51.528 21.437 30.958 1.00 83.86 C ANISOU 1449 C LEU A 236 11397 12447 8019 652 2224 -994 C ATOM 1450 O LEU A 236 52.039 21.252 29.843 1.00 94.50 O ANISOU 1450 O LEU A 236 12828 13963 9116 830 2416 -1028 O ATOM 1451 CB LEU A 236 51.357 19.513 32.566 1.00 77.29 C ANISOU 1451 CB LEU A 236 10656 11231 7480 738 1979 -1279 C ATOM 1452 CG LEU A 236 51.947 18.707 33.726 1.00 82.16 C ANISOU 1452 CG LEU A 236 11170 11701 8346 823 1944 -1337 C ATOM 1453 CD1 LEU A 236 51.231 17.375 33.879 1.00 90.70 C ANISOU 1453 CD1 LEU A 236 12527 12532 9401 886 1776 -1570 C ATOM 1454 CD2 LEU A 236 53.446 18.503 33.542 1.00 86.68 C ANISOU 1454 CD2 LEU A 236 11562 12441 8932 1053 2196 -1308 C ATOM 1455 N THR A 237 50.455 22.212 31.132 1.00 81.21 N ANISOU 1455 N THR A 237 11097 12049 7709 430 2048 -907 N ATOM 1456 CA THR A 237 49.828 22.907 30.014 1.00 77.55 C ANISOU 1456 CA THR A 237 10769 11714 6982 386 2062 -837 C ATOM 1457 C THR A 237 50.796 23.884 29.355 1.00 84.54 C ANISOU 1457 C THR A 237 11489 12842 7790 424 2340 -619 C ATOM 1458 O THR A 237 50.948 23.891 28.126 1.00 92.04 O ANISOU 1458 O THR A 237 12573 13961 8439 555 2487 -623 O ATOM 1459 CB THR A 237 48.576 23.633 30.513 1.00 75.83 C ANISOU 1459 CB THR A 237 10568 11379 6863 143 1824 -759 C ATOM 1460 OG1 THR A 237 47.496 22.699 30.644 1.00 77.10 O ANISOU 1460 OG1 THR A 237 10947 11362 6986 123 1584 -971 O ATOM 1461 CG2 THR A 237 48.176 24.754 29.573 1.00 73.90 C ANISOU 1461 CG2 THR A 237 10365 11292 6422 77 1873 -588 C ATOM 1462 N ILE A 238 51.462 24.717 30.160 1.00 79.38 N ANISOU 1462 N ILE A 238 10545 12208 7406 307 2416 -427 N ATOM 1463 CA ILE A 238 52.357 25.726 29.609 1.00 82.02 C ANISOU 1463 CA ILE A 238 10698 12754 7712 301 2676 -197 C ATOM 1464 C ILE A 238 53.613 25.094 29.022 1.00 88.67 C ANISOU 1464 C ILE A 238 11474 13768 8449 544 2950 -244 C ATOM 1465 O ILE A 238 54.304 25.725 28.213 1.00 90.35 O ANISOU 1465 O ILE A 238 11599 14191 8542 589 3204 -80 O ATOM 1466 CB ILE A 238 52.692 26.775 30.689 1.00 78.63 C ANISOU 1466 CB ILE A 238 9977 12276 7624 89 2657 1 C ATOM 1467 CG1 ILE A 238 53.253 28.050 30.054 1.00 91.91 C ANISOU 1467 CG1 ILE A 238 11514 14133 9276 11 2879 267 C ATOM 1468 CG2 ILE A 238 53.668 26.215 31.712 1.00 87.36 C ANISOU 1468 CG2 ILE A 238 10858 13341 8994 147 2684 -58 C ATOM 1469 CD1 ILE A 238 52.289 28.743 29.117 1.00 94.44 C ANISOU 1469 CD1 ILE A 238 12043 14490 9349 -51 2843 363 C ATOM 1470 N TYR A 239 53.928 23.855 29.405 1.00 85.39 N ANISOU 1470 N TYR A 239 11100 13268 8078 709 2914 -456 N ATOM 1471 CA TYR A 239 55.021 23.132 28.759 1.00 91.14 C ANISOU 1471 CA TYR A 239 11804 14153 8672 979 3168 -532 C ATOM 1472 C TYR A 239 54.609 22.607 27.383 1.00 97.74 C ANISOU 1472 C TYR A 239 12961 15077 9098 1156 3231 -669 C ATOM 1473 O TYR A 239 55.297 22.850 26.373 1.00110.98 O ANISOU 1473 O TYR A 239 14621 16986 10559 1296 3503 -587 O ATOM 1474 CB TYR A 239 55.477 21.997 29.681 1.00 95.51 C ANISOU 1474 CB TYR A 239 12304 14565 9421 1108 3097 -707 C ATOM 1475 CG TYR A 239 56.065 20.778 29.009 1.00104.24 C ANISOU 1475 CG TYR A 239 13549 15724 10333 1426 3243 -909 C ATOM 1476 CD1 TYR A 239 57.331 20.815 28.439 1.00116.31 C ANISOU 1476 CD1 TYR A 239 14903 17491 11799 1620 3560 -835 C ATOM 1477 CD2 TYR A 239 55.370 19.575 28.985 1.00102.68 C ANISOU 1477 CD2 TYR A 239 13652 15328 10033 1532 3067 -1175 C ATOM 1478 CE1 TYR A 239 57.876 19.695 27.840 1.00125.23 C ANISOU 1478 CE1 TYR A 239 16164 18667 12749 1933 3702 -1027 C ATOM 1479 CE2 TYR A 239 55.907 18.449 28.388 1.00113.37 C ANISOU 1479 CE2 TYR A 239 15153 16706 11216 1832 3197 -1374 C ATOM 1480 CZ TYR A 239 57.161 18.516 27.817 1.00126.36 C ANISOU 1480 CZ TYR A 239 16629 18596 12785 2043 3516 -1302 C ATOM 1481 OH TYR A 239 57.706 17.402 27.221 1.00128.33 O ANISOU 1481 OH TYR A 239 17029 18871 12859 2364 3656 -1505 O ATOM 1482 N VAL A 240 53.477 21.900 27.322 1.00 93.47 N ANISOU 1482 N VAL A 240 12713 14359 8442 1145 2980 -878 N ATOM 1483 CA VAL A 240 53.046 21.329 26.049 1.00 99.03 C ANISOU 1483 CA VAL A 240 13739 15134 8753 1312 3002 -1045 C ATOM 1484 C VAL A 240 52.776 22.434 25.034 1.00103.28 C ANISOU 1484 C VAL A 240 14323 15876 9045 1247 3104 -850 C ATOM 1485 O VAL A 240 53.118 22.302 23.851 1.00115.78 O ANISOU 1485 O VAL A 240 16043 17652 10296 1438 3299 -875 O ATOM 1486 CB VAL A 240 51.820 20.418 26.239 1.00 84.47 C ANISOU 1486 CB VAL A 240 12180 13047 6869 1270 2685 -1301 C ATOM 1487 CG1 VAL A 240 51.517 19.687 24.946 1.00 99.48 C ANISOU 1487 CG1 VAL A 240 14414 15017 8368 1468 2705 -1515 C ATOM 1488 CG2 VAL A 240 52.066 19.415 27.354 1.00 91.22 C ANISOU 1488 CG2 VAL A 240 12982 13679 7999 1311 2584 -1451 C ATOM 1489 N LEU A 241 52.178 23.546 25.477 1.00 96.48 N ANISOU 1489 N LEU A 241 13352 14973 8332 992 2985 -648 N ATOM 1490 CA LEU A 241 51.879 24.641 24.557 1.00 98.11 C ANISOU 1490 CA LEU A 241 13609 15351 8318 928 3072 -441 C ATOM 1491 C LEU A 241 53.144 25.170 23.897 1.00110.00 C ANISOU 1491 C LEU A 241 14948 17111 9735 1045 3448 -245 C ATOM 1492 O LEU A 241 53.173 25.407 22.684 1.00110.77 O ANISOU 1492 O LEU A 241 15198 17403 9486 1163 3606 -187 O ATOM 1493 CB LEU A 241 51.160 25.770 25.293 1.00 89.62 C ANISOU 1493 CB LEU A 241 12410 14166 7474 643 2899 -245 C ATOM 1494 CG LEU A 241 49.700 25.538 25.671 1.00 82.99 C ANISOU 1494 CG LEU A 241 11750 13128 6654 510 2544 -381 C ATOM 1495 CD1 LEU A 241 49.236 26.632 26.610 1.00 88.02 C ANISOU 1495 CD1 LEU A 241 12206 13654 7582 254 2416 -183 C ATOM 1496 CD2 LEU A 241 48.814 25.475 24.435 1.00 83.68 C ANISOU 1496 CD2 LEU A 241 12137 13310 6347 582 2461 -452 C ATOM 1497 N ARG A 242 54.203 25.370 24.683 1.00119.14 N ANISOU 1497 N ARG A 242 15785 18282 11200 1014 3598 -134 N ATOM 1498 CA ARG A 242 55.458 25.832 24.102 1.00117.41 C ANISOU 1498 CA ARG A 242 15370 18310 10931 1117 3967 55 C ATOM 1499 C ARG A 242 55.983 24.822 23.091 1.00120.04 C ANISOU 1499 C ARG A 242 15875 18802 10935 1440 4165 -122 C ATOM 1500 O ARG A 242 56.438 25.199 22.005 1.00125.36 O ANISOU 1500 O ARG A 242 16583 19712 11336 1557 4435 5 O ATOM 1501 CB ARG A 242 56.490 26.102 25.204 1.00119.94 C ANISOU 1501 CB ARG A 242 15300 18609 11664 1028 4055 168 C ATOM 1502 CG ARG A 242 57.778 26.809 24.744 1.00130.48 C ANISOU 1502 CG ARG A 242 16357 20195 13026 1063 4429 415 C ATOM 1503 CD ARG A 242 58.854 25.860 24.203 1.00133.35 C ANISOU 1503 CD ARG A 242 16677 20739 13252 1373 4698 299 C ATOM 1504 NE ARG A 242 60.032 26.605 23.781 1.00134.00 N ANISOU 1504 NE ARG A 242 16468 21068 13378 1382 5060 557 N ATOM 1505 CZ ARG A 242 61.175 26.069 23.375 1.00132.70 C ANISOU 1505 CZ ARG A 242 16158 21105 13156 1622 5356 536 C ATOM 1506 NH1 ARG A 242 61.403 24.769 23.464 1.00136.92 N ANISOU 1506 NH1 ARG A 242 16787 21605 13629 1881 5329 264 N ATOM 1507 NH2 ARG A 242 62.106 26.858 22.844 1.00131.94 N ANISOU 1507 NH2 ARG A 242 15819 21248 13065 1606 5697 800 N ATOM 1508 N ARG A 243 55.919 23.528 23.423 1.00121.59 N ANISOU 1508 N ARG A 243 16194 18864 11143 1594 4040 -416 N ATOM 1509 CA ARG A 243 56.439 22.533 22.484 1.00129.19 C ANISOU 1509 CA ARG A 243 17334 19958 11796 1920 4229 -606 C ATOM 1510 C ARG A 243 55.686 22.560 21.155 1.00130.56 C ANISOU 1510 C ARG A 243 17859 20241 11506 2008 4222 -667 C ATOM 1511 O ARG A 243 56.304 22.557 20.083 1.00134.20 O ANISOU 1511 O ARG A 243 18384 20945 11662 2218 4509 -628 O ATOM 1512 CB ARG A 243 56.392 21.136 23.094 1.00137.04 C ANISOU 1512 CB ARG A 243 18434 20743 12891 2061 4067 -918 C ATOM 1513 CG ARG A 243 57.500 20.869 24.077 1.00140.42 C ANISOU 1513 CG ARG A 243 18533 21151 13669 2112 4176 -881 C ATOM 1514 CD ARG A 243 57.573 19.399 24.347 1.00147.24 C ANISOU 1514 CD ARG A 243 19558 21849 14537 2334 4087 -1189 C ATOM 1515 NE ARG A 243 56.238 18.821 24.361 1.00145.65 N ANISOU 1515 NE ARG A 243 19699 21409 14233 2255 3761 -1407 N ATOM 1516 CZ ARG A 243 55.983 17.535 24.541 1.00148.00 C ANISOU 1516 CZ ARG A 243 20216 21502 14515 2402 3622 -1695 C ATOM 1517 NH1 ARG A 243 56.947 16.672 24.813 1.00143.27 N ANISOU 1517 NH1 ARG A 243 19536 20889 14009 2645 3762 -1802 N ATOM 1518 NH2 ARG A 243 54.730 17.101 24.435 1.00148.75 N ANISOU 1518 NH2 ARG A 243 20615 21399 14502 2304 3335 -1879 N ATOM 1519 N GLN A 244 54.350 22.589 21.203 1.00126.91 N ANISOU 1519 N GLN A 244 17626 19616 10978 1857 3896 -759 N ATOM 1520 CA GLN A 244 53.572 22.592 19.964 1.00131.99 C ANISOU 1520 CA GLN A 244 18607 20366 11178 1940 3846 -832 C ATOM 1521 C GLN A 244 53.805 23.869 19.162 1.00134.66 C ANISOU 1521 C GLN A 244 18878 20952 11335 1896 4073 -507 C ATOM 1522 O GLN A 244 53.925 23.825 17.931 1.00141.45 O ANISOU 1522 O GLN A 244 19938 22025 11781 2089 4244 -514 O ATOM 1523 CB GLN A 244 52.081 22.423 20.265 1.00131.08 C ANISOU 1523 CB GLN A 244 18702 20030 11074 1763 3435 -980 C ATOM 1524 CG GLN A 244 51.735 21.384 21.328 1.00135.48 C ANISOU 1524 CG GLN A 244 19272 20295 11910 1718 3185 -1230 C ATOM 1525 CD GLN A 244 52.082 19.958 20.932 1.00148.57 C ANISOU 1525 CD GLN A 244 21142 21909 13398 1991 3224 -1554 C ATOM 1526 OE1 GLN A 244 51.203 19.172 20.581 1.00165.79 O ANISOU 1526 OE1 GLN A 244 23623 23967 15403 2024 2994 -1818 O ATOM 1527 NE2 GLN A 244 53.362 19.610 21.011 1.00140.68 N ANISOU 1527 NE2 GLN A 244 19983 21004 12467 2187 3508 -1540 N ATOM 1528 N ALA A 245 53.864 25.015 19.842 1.00132.67 N ANISOU 1528 N ALA A 245 18359 20669 11382 1647 4079 -220 N ATOM 1529 CA ALA A 245 54.111 26.272 19.145 1.00133.68 C ANISOU 1529 CA ALA A 245 18414 21000 11377 1586 4302 114 C ATOM 1530 C ALA A 245 55.521 26.333 18.574 1.00136.47 C ANISOU 1530 C ALA A 245 18601 21608 11644 1771 4736 248 C ATOM 1531 O ALA A 245 55.737 26.964 17.534 1.00141.25 O ANISOU 1531 O ALA A 245 19275 22439 11956 1843 4971 445 O ATOM 1532 CB ALA A 245 53.868 27.452 20.090 1.00140.00 C ANISOU 1532 CB ALA A 245 18969 21672 12555 1271 4197 371 C ATOM 1533 N ALA A1001 56.480 25.664 19.224 1.00139.32 N ANISOU 1533 N ALA A1001 18744 21945 12247 1862 4851 150 N ATOM 1534 CA ALA A1001 57.888 25.834 18.872 1.00143.94 C ANISOU 1534 CA ALA A1001 19081 22770 12839 2002 5268 312 C ATOM 1535 C ALA A1001 58.158 25.457 17.421 1.00144.76 C ANISOU 1535 C ALA A1001 19420 23078 12503 2257 5473 248 C ATOM 1536 O ALA A1001 58.895 26.162 16.723 1.00148.25 O ANISOU 1536 O ALA A1001 19729 23671 12927 2227 5719 477 O ATOM 1537 CB ALA A1001 58.773 25.011 19.810 1.00141.79 C ANISOU 1537 CB ALA A1001 18563 22422 12889 2088 5302 168 C ATOM 1538 N ASP A1002 57.565 24.358 16.947 1.00146.65 N ANISOU 1538 N ASP A1002 20005 23258 12457 2452 5309 -82 N ATOM 1539 CA ASP A1002 57.813 23.904 15.582 1.00155.11 C ANISOU 1539 CA ASP A1002 21300 24454 13180 2653 5422 -192 C ATOM 1540 C ASP A1002 57.532 25.009 14.571 1.00155.50 C ANISOU 1540 C ASP A1002 21432 24640 13012 2544 5492 69 C ATOM 1541 O ASP A1002 58.403 25.383 13.779 1.00163.57 O ANISOU 1541 O ASP A1002 22355 25832 13964 2600 5769 231 O ATOM 1542 CB ASP A1002 56.950 22.678 15.267 1.00147.94 C ANISOU 1542 CB ASP A1002 20781 23419 12010 2816 5159 -586 C ATOM 1543 CG ASP A1002 57.053 21.596 16.327 1.00151.58 C ANISOU 1543 CG ASP A1002 21205 23695 12692 2907 5046 -849 C ATOM 1544 OD1 ASP A1002 56.004 21.032 16.710 1.00141.59 O ANISOU 1544 OD1 ASP A1002 20177 22245 11378 2880 4737 -1080 O ATOM 1545 OD2 ASP A1002 58.180 21.311 16.781 1.00168.40 O ANISOU 1545 OD2 ASP A1002 23067 25862 15056 3005 5259 -821 O ATOM 1546 N LEU A1003 56.317 25.562 14.605 1.00149.21 N ANISOU 1546 N LEU A1003 20812 23768 12113 2388 5240 121 N ATOM 1547 CA LEU A1003 55.932 26.561 13.615 1.00150.58 C ANISOU 1547 CA LEU A1003 21104 24054 12056 2305 5270 353 C ATOM 1548 C LEU A1003 56.732 27.850 13.768 1.00153.42 C ANISOU 1548 C LEU A1003 21137 24490 12665 2124 5529 754 C ATOM 1549 O LEU A1003 57.193 28.415 12.770 1.00168.76 O ANISOU 1549 O LEU A1003 23091 26581 14449 2149 5735 938 O ATOM 1550 CB LEU A1003 54.432 26.843 13.704 1.00148.40 C ANISOU 1550 CB LEU A1003 21070 23671 11645 2183 4918 314 C ATOM 1551 CG LEU A1003 53.560 26.075 12.708 1.00147.67 C ANISOU 1551 CG LEU A1003 21378 23592 11140 2334 4697 33 C ATOM 1552 CD1 LEU A1003 53.662 24.568 12.923 1.00141.24 C ANISOU 1552 CD1 LEU A1003 20685 22680 10300 2520 4605 -372 C ATOM 1553 CD2 LEU A1003 52.111 26.536 12.783 1.00159.04 C ANISOU 1553 CD2 LEU A1003 23005 24948 12474 2189 4354 45 C ATOM 1554 N GLU A1004 56.925 28.327 15.002 1.00143.59 N ANISOU 1554 N GLU A1004 19599 23142 11818 1936 5521 891 N ATOM 1555 CA GLU A1004 57.540 29.642 15.175 1.00141.75 C ANISOU 1555 CA GLU A1004 19074 22940 11845 1718 5715 1267 C ATOM 1556 C GLU A1004 59.026 29.637 14.827 1.00156.06 C ANISOU 1556 C GLU A1004 20628 24897 13771 1792 6064 1364 C ATOM 1557 O GLU A1004 59.538 30.644 14.328 1.00164.72 O ANISOU 1557 O GLU A1004 21602 26073 14912 1674 6261 1651 O ATOM 1558 CB GLU A1004 57.309 30.161 16.599 1.00137.91 C ANISOU 1558 CB GLU A1004 18346 22293 11761 1483 5588 1375 C ATOM 1559 CG GLU A1004 57.777 29.261 17.725 1.00139.96 C ANISOU 1559 CG GLU A1004 18407 22486 12285 1544 5564 1176 C ATOM 1560 CD GLU A1004 56.954 29.455 18.986 1.00133.48 C ANISOU 1560 CD GLU A1004 17526 21418 11773 1320 5235 1136 C ATOM 1561 OE1 GLU A1004 56.007 30.268 18.947 1.00121.98 O ANISOU 1561 OE1 GLU A1004 16189 19868 10291 1145 5053 1264 O ATOM 1562 OE2 GLU A1004 57.247 28.798 20.008 1.00132.93 O ANISOU 1562 OE2 GLU A1004 17293 21206 12009 1302 5117 962 O ATOM 1563 N ASP A1005 59.731 28.528 15.068 1.00157.75 N ANISOU 1563 N ASP A1005 20760 25143 14035 1987 6144 1131 N ATOM 1564 CA ASP A1005 61.151 28.465 14.724 1.00159.21 C ANISOU 1564 CA ASP A1005 20691 25479 14321 2076 6471 1211 C ATOM 1565 C ASP A1005 61.358 28.485 13.211 1.00159.86 C ANISOU 1565 C ASP A1005 20985 25737 14017 2232 6648 1243 C ATOM 1566 O ASP A1005 62.145 29.287 12.687 1.00160.22 O ANISOU 1566 O ASP A1005 20860 25907 14111 2159 6905 1502 O ATOM 1567 CB ASP A1005 61.782 27.214 15.336 1.00157.77 C ANISOU 1567 CB ASP A1005 20394 25280 14272 2276 6490 940 C ATOM 1568 CG ASP A1005 61.586 27.134 16.837 1.00162.80 C ANISOU 1568 CG ASP A1005 20828 25753 15275 2142 6314 901 C ATOM 1569 OD1 ASP A1005 61.125 28.134 17.427 1.00151.93 O ANISOU 1569 OD1 ASP A1005 19346 24290 14091 1877 6214 1110 O ATOM 1570 OD2 ASP A1005 61.868 26.067 17.423 1.00168.56 O ANISOU 1570 OD2 ASP A1005 21515 26433 16097 2309 6270 659 O ATOM 1571 N ASN A1006 60.646 27.607 12.494 1.00163.71 N ANISOU 1571 N ASN A1006 21848 26234 14120 2440 6505 976 N ATOM 1572 CA ASN A1006 60.740 27.556 11.036 1.00166.12 C ANISOU 1572 CA ASN A1006 22387 26706 14023 2603 6643 979 C ATOM 1573 C ASN A1006 60.272 28.865 10.409 1.00170.87 C ANISOU 1573 C ASN A1006 23064 27352 14506 2423 6657 1293 C ATOM 1574 O ASN A1006 60.883 29.370 9.454 1.00171.41 O ANISOU 1574 O ASN A1006 23116 27583 14430 2459 6909 1480 O ATOM 1575 CB ASN A1006 59.906 26.390 10.491 1.00159.70 C ANISOU 1575 CB ASN A1006 21976 25858 12844 2825 6420 612 C ATOM 1576 CG ASN A1006 59.969 25.148 11.367 1.00162.59 C ANISOU 1576 CG ASN A1006 22324 26089 13365 2950 6292 286 C ATOM 1577 OD1 ASN A1006 60.943 24.923 12.082 1.00175.42 O ANISOU 1577 OD1 ASN A1006 23641 27714 15296 2972 6452 304 O ATOM 1578 ND2 ASN A1006 58.914 24.337 11.316 1.00157.54 N ANISOU 1578 ND2 ASN A1006 22013 25326 12519 3029 5991 -14 N ATOM 1579 N TRP A1007 59.171 29.415 10.926 1.00188.50 N ANISOU 1579 N TRP A1007 25391 29440 16792 2239 6388 1353 N ATOM 1580 CA TRP A1007 58.653 30.678 10.416 1.00195.13 C ANISOU 1580 CA TRP A1007 26307 30291 17543 2069 6374 1653 C ATOM 1581 C TRP A1007 59.650 31.806 10.635 1.00191.32 C ANISOU 1581 C TRP A1007 25477 29838 17379 1873 6648 2007 C ATOM 1582 O TRP A1007 59.833 32.657 9.759 1.00195.20 O ANISOU 1582 O TRP A1007 26010 30424 17735 1829 6807 2255 O ATOM 1583 CB TRP A1007 57.313 31.000 11.080 1.00205.70 C ANISOU 1583 CB TRP A1007 27777 31452 18925 1914 6024 1637 C ATOM 1584 CG TRP A1007 56.788 32.360 10.764 1.00204.22 C ANISOU 1584 CG TRP A1007 27631 31240 18722 1723 5995 1962 C ATOM 1585 CD1 TRP A1007 56.048 32.718 9.678 1.00186.76 C ANISOU 1585 CD1 TRP A1007 25718 29101 16142 1780 5911 2024 C ATOM 1586 CD2 TRP A1007 56.960 33.550 11.545 1.00200.52 C ANISOU 1586 CD2 TRP A1007 26902 30654 18633 1449 6039 2265 C ATOM 1587 NE1 TRP A1007 55.755 34.058 9.728 1.00188.63 N ANISOU 1587 NE1 TRP A1007 25900 29271 16502 1570 5909 2356 N ATOM 1588 CE2 TRP A1007 56.300 34.591 10.866 1.00196.95 C ANISOU 1588 CE2 TRP A1007 26618 30197 18018 1359 5985 2503 C ATOM 1589 CE3 TRP A1007 57.609 33.835 12.751 1.00188.38 C ANISOU 1589 CE3 TRP A1007 25008 29008 17561 1270 6107 2350 C ATOM 1590 CZ2 TRP A1007 56.268 35.898 11.351 1.00197.92 C ANISOU 1590 CZ2 TRP A1007 26577 30191 18433 1099 6003 2819 C ATOM 1591 CZ3 TRP A1007 57.577 35.134 13.231 1.00181.22 C ANISOU 1591 CZ3 TRP A1007 23932 27978 16944 999 6115 2655 C ATOM 1592 CH2 TRP A1007 56.912 36.148 12.532 1.00188.01 C ANISOU 1592 CH2 TRP A1007 24980 28817 17638 917 6066 2883 C ATOM 1593 N GLU A1008 60.303 31.829 11.801 1.00165.38 N ANISOU 1593 N GLU A1008 21846 26466 14524 1748 6697 2033 N ATOM 1594 CA GLU A1008 61.328 32.835 12.056 1.00159.06 C ANISOU 1594 CA GLU A1008 20690 25684 14059 1548 6944 2337 C ATOM 1595 C GLU A1008 62.497 32.683 11.094 1.00161.34 C ANISOU 1595 C GLU A1008 20895 26187 14221 1698 7286 2395 C ATOM 1596 O GLU A1008 63.044 33.682 10.611 1.00157.19 O ANISOU 1596 O GLU A1008 20250 25725 13752 1569 7497 2686 O ATOM 1597 CB GLU A1008 61.811 32.747 13.505 1.00148.10 C ANISOU 1597 CB GLU A1008 18949 24174 13148 1405 6902 2308 C ATOM 1598 CG GLU A1008 61.077 33.670 14.468 1.00142.93 C ANISOU 1598 CG GLU A1008 18222 23313 12771 1119 6688 2460 C ATOM 1599 CD GLU A1008 61.262 35.140 14.132 1.00137.30 C ANISOU 1599 CD GLU A1008 17422 22571 12176 880 6808 2818 C ATOM 1600 OE1 GLU A1008 62.269 35.487 13.479 1.00142.64 O ANISOU 1600 OE1 GLU A1008 17958 23379 12858 885 7092 2970 O ATOM 1601 OE2 GLU A1008 60.393 35.950 14.521 1.00134.22 O ANISOU 1601 OE2 GLU A1008 17108 22019 11873 690 6617 2947 O ATOM 1602 N THR A1009 62.891 31.442 10.801 1.00163.06 N ANISOU 1602 N THR A1009 21177 26510 14268 1973 7348 2121 N ATOM 1603 CA THR A1009 63.961 31.223 9.830 1.00163.31 C ANISOU 1603 CA THR A1009 21150 26756 14145 2146 7675 2158 C ATOM 1604 C THR A1009 63.595 31.814 8.471 1.00168.78 C ANISOU 1604 C THR A1009 22120 27567 14443 2187 7759 2318 C ATOM 1605 O THR A1009 64.359 32.601 7.890 1.00183.74 O ANISOU 1605 O THR A1009 23874 29578 16361 2117 8034 2585 O ATOM 1606 CB THR A1009 64.264 29.727 9.700 1.00159.41 C ANISOU 1606 CB THR A1009 20745 26330 13494 2459 7685 1805 C ATOM 1607 OG1 THR A1009 64.504 29.169 10.997 1.00161.97 O ANISOU 1607 OG1 THR A1009 20836 26531 14176 2429 7578 1657 O ATOM 1608 CG2 THR A1009 65.493 29.501 8.827 1.00166.61 C ANISOU 1608 CG2 THR A1009 21541 27464 14299 2636 8044 1851 C ATOM 1609 N LEU A1010 62.413 31.460 7.956 1.00160.77 N ANISOU 1609 N LEU A1010 21499 26521 13065 2294 7517 2160 N ATOM 1610 CA LEU A1010 62.041 31.931 6.622 1.00160.03 C ANISOU 1610 CA LEU A1010 21686 26554 12564 2364 7579 2289 C ATOM 1611 C LEU A1010 61.835 33.444 6.606 1.00169.68 C ANISOU 1611 C LEU A1010 22834 27716 13920 2093 7609 2673 C ATOM 1612 O LEU A1010 62.186 34.115 5.626 1.00181.75 O ANISOU 1612 O LEU A1010 24410 29376 15271 2101 7825 2903 O ATOM 1613 CB LEU A1010 60.801 31.188 6.111 1.00150.14 C ANISOU 1613 CB LEU A1010 20859 25280 10909 2532 7278 2014 C ATOM 1614 CG LEU A1010 59.376 31.475 6.587 1.00153.52 C ANISOU 1614 CG LEU A1010 21478 25531 11322 2395 6897 1978 C ATOM 1615 CD1 LEU A1010 58.725 32.572 5.757 1.00147.60 C ANISOU 1615 CD1 LEU A1010 20916 24818 10348 2306 6863 2245 C ATOM 1616 CD2 LEU A1010 58.551 30.200 6.517 1.00148.04 C ANISOU 1616 CD2 LEU A1010 21077 24795 10375 2587 6617 1571 C ATOM 1617 N ASN A1011 61.288 34.003 7.689 1.00163.17 N ANISOU 1617 N ASN A1011 21896 26688 13415 1855 7402 2748 N ATOM 1618 CA ASN A1011 61.085 35.445 7.767 1.00166.66 C ANISOU 1618 CA ASN A1011 22266 27035 14023 1590 7415 3101 C ATOM 1619 C ASN A1011 62.407 36.199 7.806 1.00182.27 C ANISOU 1619 C ASN A1011 23893 29068 16294 1444 7753 3369 C ATOM 1620 O ASN A1011 62.539 37.250 7.177 1.00182.25 O ANISOU 1620 O ASN A1011 23908 29091 16247 1332 7896 3665 O ATOM 1621 CB ASN A1011 60.239 35.790 8.990 1.00164.87 C ANISOU 1621 CB ASN A1011 21986 26569 14089 1381 7116 3093 C ATOM 1622 CG ASN A1011 58.780 35.454 8.795 1.00168.66 C ANISOU 1622 CG ASN A1011 22830 26988 14265 1466 6777 2927 C ATOM 1623 OD1 ASN A1011 57.925 36.338 8.759 1.00166.80 O ANISOU 1623 OD1 ASN A1011 22718 26650 14008 1330 6619 3101 O ATOM 1624 ND2 ASN A1011 58.487 34.170 8.649 1.00173.81 N ANISOU 1624 ND2 ASN A1011 23657 27699 14683 1695 6657 2584 N ATOM 1625 N ASP A1012 63.393 35.690 8.550 1.00196.24 N ANISOU 1625 N ASP A1012 25337 30852 18372 1440 7877 3271 N ATOM 1626 CA ASP A1012 64.712 36.315 8.557 1.00204.64 C ANISOU 1626 CA ASP A1012 26050 31991 19714 1310 8196 3499 C ATOM 1627 C ASP A1012 65.357 36.259 7.177 1.00202.53 C ANISOU 1627 C ASP A1012 25880 31965 19108 1495 8503 3588 C ATOM 1628 O ASP A1012 65.955 37.243 6.712 1.00205.85 O ANISOU 1628 O ASP A1012 26179 32437 19598 1355 8736 3888 O ATOM 1629 CB ASP A1012 65.598 35.631 9.600 1.00199.92 C ANISOU 1629 CB ASP A1012 25096 31382 19482 1309 8240 3338 C ATOM 1630 CG ASP A1012 67.063 35.978 9.444 1.00205.74 C ANISOU 1630 CG ASP A1012 25477 32254 20440 1248 8586 3509 C ATOM 1631 OD1 ASP A1012 67.438 37.129 9.747 1.00211.21 O ANISOU 1631 OD1 ASP A1012 25952 32866 21433 964 8663 3780 O ATOM 1632 OD2 ASP A1012 67.840 35.094 9.025 1.00205.57 O ANISOU 1632 OD2 ASP A1012 25393 32416 20299 1484 8776 3365 O ATOM 1633 N ASN A1013 65.238 35.113 6.500 1.00209.61 N ANISOU 1633 N ASN A1013 27004 33005 19633 1809 8507 3326 N ATOM 1634 CA ASN A1013 65.823 34.994 5.169 1.00216.23 C ANISOU 1634 CA ASN A1013 27953 34081 20123 2007 8795 3391 C ATOM 1635 C ASN A1013 65.155 35.946 4.181 1.00220.06 C ANISOU 1635 C ASN A1013 28715 34590 20308 1955 8795 3636 C ATOM 1636 O ASN A1013 65.817 36.489 3.287 1.00223.80 O ANISOU 1636 O ASN A1013 29160 35217 20656 1970 9088 3863 O ATOM 1637 CB ASN A1013 65.737 33.549 4.688 1.00216.87 C ANISOU 1637 CB ASN A1013 28251 34283 19866 2354 8761 3032 C ATOM 1638 CG ASN A1013 66.596 32.614 5.515 1.00217.29 C ANISOU 1638 CG ASN A1013 28018 34342 20202 2440 8825 2819 C ATOM 1639 OD1 ASN A1013 66.128 31.581 5.993 1.00217.45 O ANISOU 1639 OD1 ASN A1013 28152 34284 20187 2579 8607 2503 O ATOM 1640 ND2 ASN A1013 67.860 32.978 5.697 1.00219.46 N ANISOU 1640 ND2 ASN A1013 27914 34705 20765 2356 9118 2991 N ATOM 1641 N LEU A1014 63.843 36.161 4.320 1.00196.26 N ANISOU 1641 N LEU A1014 25968 31430 17173 1901 8469 3598 N ATOM 1642 CA LEU A1014 63.189 37.199 3.525 1.00190.59 C ANISOU 1642 CA LEU A1014 25479 30705 16232 1823 8445 3862 C ATOM 1643 C LEU A1014 63.634 38.594 3.950 1.00190.32 C ANISOU 1643 C LEU A1014 25187 30552 16576 1505 8575 4231 C ATOM 1644 O LEU A1014 63.716 39.500 3.112 1.00184.11 O ANISOU 1644 O LEU A1014 24487 29823 15645 1454 8733 4516 O ATOM 1645 CB LEU A1014 61.669 37.078 3.633 1.00186.00 C ANISOU 1645 CB LEU A1014 25222 29995 15454 1843 8047 3725 C ATOM 1646 CG LEU A1014 60.920 36.683 2.357 1.00182.30 C ANISOU 1646 CG LEU A1014 25171 29674 14421 2090 7961 3623 C ATOM 1647 CD1 LEU A1014 59.413 36.759 2.558 1.00189.91 C ANISOU 1647 CD1 LEU A1014 26406 30495 15255 2057 7553 3530 C ATOM 1648 CD2 LEU A1014 61.360 37.522 1.162 1.00172.74 C ANISOU 1648 CD2 LEU A1014 24034 28621 12979 2112 8241 3934 C ATOM 1649 N LYS A1015 63.914 38.783 5.242 1.00191.12 N ANISOU 1649 N LYS A1015 24979 30480 17159 1287 8501 4226 N ATOM 1650 CA LYS A1015 64.386 40.068 5.745 1.00184.97 C ANISOU 1650 CA LYS A1015 23937 29564 16780 966 8605 4542 C ATOM 1651 C LYS A1015 65.707 40.464 5.106 1.00177.97 C ANISOU 1651 C LYS A1015 22834 28848 15941 944 9009 4755 C ATOM 1652 O LYS A1015 65.953 41.656 4.879 1.00171.79 O ANISOU 1652 O LYS A1015 21982 28006 15283 736 9142 5074 O ATOM 1653 CB LYS A1015 64.513 40.009 7.272 1.00180.27 C ANISOU 1653 CB LYS A1015 23043 28773 16680 767 8444 4441 C ATOM 1654 CG LYS A1015 65.545 40.950 7.885 1.00173.33 C ANISOU 1654 CG LYS A1015 21769 27811 16277 472 8627 4675 C ATOM 1655 CD LYS A1015 65.067 42.394 7.905 1.00163.55 C ANISOU 1655 CD LYS A1015 20591 26380 15171 205 8566 4981 C ATOM 1656 CE LYS A1015 66.118 43.308 8.518 1.00159.38 C ANISOU 1656 CE LYS A1015 19675 25759 15124 -99 8736 5189 C ATOM 1657 NZ LYS A1015 65.658 44.721 8.588 1.00159.42 N ANISOU 1657 NZ LYS A1015 19748 25545 15279 -366 8667 5474 N ATOM 1658 N VAL A1016 66.569 39.488 4.809 1.00177.18 N ANISOU 1658 N VAL A1016 22622 28952 15745 1157 9210 4584 N ATOM 1659 CA VAL A1016 67.803 39.797 4.085 1.00176.03 C ANISOU 1659 CA VAL A1016 22288 28999 15595 1168 9610 4781 C ATOM 1660 C VAL A1016 67.484 40.506 2.772 1.00180.53 C ANISOU 1660 C VAL A1016 23147 29668 15779 1221 9742 5028 C ATOM 1661 O VAL A1016 67.938 41.629 2.524 1.00183.48 O ANISOU 1661 O VAL A1016 23404 30017 16292 1017 9934 5355 O ATOM 1662 CB VAL A1016 68.631 38.523 3.846 1.00178.17 C ANISOU 1662 CB VAL A1016 22460 29490 15748 1449 9786 4531 C ATOM 1663 CG1 VAL A1016 69.767 38.815 2.875 1.00184.89 C ANISOU 1663 CG1 VAL A1016 23182 30571 16495 1505 10206 4739 C ATOM 1664 CG2 VAL A1016 69.180 37.995 5.159 1.00175.10 C ANISOU 1664 CG2 VAL A1016 21716 29011 15803 1367 9709 4352 C ATOM 1665 N ILE A1017 66.686 39.868 1.921 1.00163.22 N ANISOU 1665 N ILE A1017 22059 28923 11036 -4112 -2026 -2772 N ATOM 1666 CA ILE A1017 66.306 40.462 0.643 1.00153.71 C ANISOU 1666 CA ILE A1017 21465 27278 9661 -3766 -1993 -2923 C ATOM 1667 C ILE A1017 64.814 40.768 0.614 1.00153.67 C ANISOU 1667 C ILE A1017 21924 26630 9834 -3252 -2100 -3361 C ATOM 1668 O ILE A1017 64.350 41.707 1.260 1.00152.87 O ANISOU 1668 O ILE A1017 22233 26173 9676 -3476 -2076 -3593 O ATOM 1669 CB ILE A1017 66.692 39.552 -0.534 1.00141.81 C ANISOU 1669 CB ILE A1017 19760 26044 8076 -3305 -1919 -2674 C ATOM 1670 CG1 ILE A1017 68.213 39.433 -0.640 1.00147.32 C ANISOU 1670 CG1 ILE A1017 20045 27453 8476 -3807 -1737 -2139 C ATOM 1671 CG2 ILE A1017 66.103 40.085 -1.831 1.00138.79 C ANISOU 1671 CG2 ILE A1017 20069 25137 7528 -2848 -1925 -2871 C ATOM 1672 CD1 ILE A1017 68.679 38.572 -1.791 1.00141.16 C ANISOU 1672 CD1 ILE A1017 19140 26793 7703 -3240 -1514 -1787 C ATOM 1673 N ALA A1029 70.332 33.651 0.984 1.00159.58 N ANISOU 1673 N ALA A1029 18457 31571 10606 -2912 -1122 -479 N ATOM 1674 CA ALA A1029 69.167 34.052 1.763 1.00169.32 C ANISOU 1674 CA ALA A1029 19949 32376 12007 -3045 -1474 -1118 C ATOM 1675 C ALA A1029 67.929 33.269 1.345 1.00162.76 C ANISOU 1675 C ALA A1029 19418 30980 11444 -2332 -1540 -1547 C ATOM 1676 O ALA A1029 67.346 32.538 2.144 1.00169.35 O ANISOU 1676 O ALA A1029 19951 31816 12577 -2187 -1602 -1688 O ATOM 1677 CB ALA A1029 68.919 35.542 1.615 1.00171.76 C ANISOU 1677 CB ALA A1029 20865 32180 12217 -3452 -1643 -1425 C ATOM 1678 N LEU A1030 67.537 33.426 0.078 1.00155.06 N ANISOU 1678 N LEU A1030 19045 29532 10339 -1919 -1542 -1725 N ATOM 1679 CA LEU A1030 66.318 32.786 -0.406 1.00153.10 C ANISOU 1679 CA LEU A1030 19136 28711 10325 -1341 -1709 -2121 C ATOM 1680 C LEU A1030 66.428 31.267 -0.387 1.00153.98 C ANISOU 1680 C LEU A1030 18899 29127 10480 -943 -1534 -1941 C ATOM 1681 O LEU A1030 65.418 30.575 -0.215 1.00148.47 O ANISOU 1681 O LEU A1030 18224 28113 10073 -658 -1713 -2242 O ATOM 1682 CB LEU A1030 65.985 33.281 -1.815 1.00141.74 C ANISOU 1682 CB LEU A1030 18446 26738 8671 -1019 -1777 -2289 C ATOM 1683 CG LEU A1030 65.310 34.651 -1.942 1.00129.35 C ANISOU 1683 CG LEU A1030 17374 24638 7136 -1197 -2013 -2617 C ATOM 1684 CD1 LEU A1030 66.271 35.797 -1.648 1.00131.67 C ANISOU 1684 CD1 LEU A1030 17652 25209 7165 -1792 -1867 -2413 C ATOM 1685 CD2 LEU A1030 64.690 34.809 -3.320 1.00129.53 C ANISOU 1685 CD2 LEU A1030 18096 24106 7014 -732 -2153 -2806 C ATOM 1686 N THR A1031 67.638 30.730 -0.564 1.00156.54 N ANISOU 1686 N THR A1031 18902 29963 10615 -896 -1132 -1382 N ATOM 1687 CA THR A1031 67.832 29.286 -0.499 1.00152.50 C ANISOU 1687 CA THR A1031 18094 29643 10208 -474 -841 -1125 C ATOM 1688 C THR A1031 67.551 28.731 0.893 1.00157.94 C ANISOU 1688 C THR A1031 18132 30749 11130 -660 -937 -1170 C ATOM 1689 O THR A1031 67.210 27.550 1.021 1.00155.76 O ANISOU 1689 O THR A1031 17731 30441 11011 -282 -816 -1179 O ATOM 1690 CB THR A1031 69.259 28.933 -0.933 1.00149.07 C ANISOU 1690 CB THR A1031 17411 29608 9619 -342 -284 -381 C ATOM 1691 OG1 THR A1031 69.555 29.588 -2.173 1.00150.81 O ANISOU 1691 OG1 THR A1031 18249 29443 9609 -198 -166 -317 O ATOM 1692 CG2 THR A1031 69.414 27.430 -1.123 1.00141.35 C ANISOU 1692 CG2 THR A1031 16355 28657 8695 240 126 -114 C ATOM 1693 N LYS A1032 67.657 29.559 1.929 1.00180.78 N ANISOU 1693 N LYS A1032 20688 33960 14038 -1237 -1140 -1212 N ATOM 1694 CA LYS A1032 67.420 29.137 3.303 1.00180.04 C ANISOU 1694 CA LYS A1032 20041 34144 14221 -1425 -1203 -1230 C ATOM 1695 C LYS A1032 65.958 29.264 3.714 1.00179.43 C ANISOU 1695 C LYS A1032 20234 33409 14533 -1320 -1500 -1818 C ATOM 1696 O LYS A1032 65.631 29.021 4.881 1.00175.92 O ANISOU 1696 O LYS A1032 19423 33105 14316 -1452 -1529 -1870 O ATOM 1697 CB LYS A1032 68.303 29.950 4.257 1.00177.90 C ANISOU 1697 CB LYS A1032 19358 34367 13870 -2112 -1237 -926 C ATOM 1698 CG LYS A1032 68.767 29.187 5.484 1.00172.19 C ANISOU 1698 CG LYS A1032 17882 34312 13229 -2258 -1128 -573 C ATOM 1699 CD LYS A1032 69.631 30.056 6.381 1.00168.07 C ANISOU 1699 CD LYS A1032 17037 34223 12599 -3021 -1242 -280 C ATOM 1700 CE LYS A1032 70.480 29.203 7.304 1.00153.39 C ANISOU 1700 CE LYS A1032 14330 33238 10712 -3135 -1087 317 C ATOM 1701 NZ LYS A1032 69.674 28.140 7.965 1.00158.96 N ANISOU 1701 NZ LYS A1032 14858 33865 11674 -2692 -1004 105 N ATOM 1702 N MET A1033 65.076 29.638 2.787 1.00174.68 N ANISOU 1702 N MET A1033 20247 32127 13995 -1070 -1702 -2195 N ATOM 1703 CA MET A1033 63.658 29.814 3.074 1.00161.30 C ANISOU 1703 CA MET A1033 18765 29863 12659 -943 -1978 -2640 C ATOM 1704 C MET A1033 62.837 28.561 2.796 1.00142.21 C ANISOU 1704 C MET A1033 16301 27296 10435 -489 -2053 -2793 C ATOM 1705 O MET A1033 61.878 28.280 3.523 1.00138.87 O ANISOU 1705 O MET A1033 15681 26746 10339 -429 -2185 -2998 O ATOM 1706 CB MET A1033 63.099 30.976 2.251 1.00163.15 C ANISOU 1706 CB MET A1033 19644 29498 12849 -944 -2200 -2899 C ATOM 1707 CG MET A1033 62.822 32.231 3.046 1.00167.49 C ANISOU 1707 CG MET A1033 20326 29870 13443 -1313 -2272 -3044 C ATOM 1708 SD MET A1033 62.107 33.523 2.019 1.00172.39 S ANISOU 1708 SD MET A1033 21710 29838 13952 -1214 -2486 -3320 S ATOM 1709 CE MET A1033 63.575 34.278 1.326 1.00170.55 C ANISOU 1709 CE MET A1033 21699 29834 13269 -1549 -2301 -3046 C ATOM 1710 N ARG A1034 63.196 27.807 1.754 1.00140.49 N ANISOU 1710 N ARG A1034 16312 27090 9977 -172 -1955 -2691 N ATOM 1711 CA ARG A1034 62.353 26.703 1.301 1.00124.85 C ANISOU 1711 CA ARG A1034 14488 24834 8113 210 -2095 -2899 C ATOM 1712 C ARG A1034 62.185 25.649 2.389 1.00118.06 C ANISOU 1712 C ARG A1034 13034 24373 7452 265 -1967 -2844 C ATOM 1713 O ARG A1034 61.065 25.215 2.682 1.00117.79 O ANISOU 1713 O ARG A1034 12923 24084 7747 366 -2215 -3116 O ATOM 1714 CB ARG A1034 62.947 26.078 0.038 1.00120.84 C ANISOU 1714 CB ARG A1034 14468 24227 7220 539 -1903 -2752 C ATOM 1715 CG ARG A1034 63.750 27.040 -0.826 1.00124.23 C ANISOU 1715 CG ARG A1034 15300 24618 7286 473 -1790 -2588 C ATOM 1716 CD ARG A1034 62.871 28.094 -1.484 1.00126.47 C ANISOU 1716 CD ARG A1034 16111 24271 7670 409 -2215 -2928 C ATOM 1717 NE ARG A1034 63.665 29.103 -2.177 1.00134.30 N ANISOU 1717 NE ARG A1034 17445 25259 8324 311 -2077 -2764 N ATOM 1718 CZ ARG A1034 63.957 29.073 -3.470 1.00126.76 C ANISOU 1718 CZ ARG A1034 17126 24037 6998 597 -1998 -2712 C ATOM 1719 NH1 ARG A1034 63.521 28.102 -4.256 1.00126.63 N ANISOU 1719 NH1 ARG A1034 17570 23667 6875 976 -2074 -2833 N ATOM 1720 NH2 ARG A1034 64.705 30.044 -3.989 1.00127.47 N ANISOU 1720 NH2 ARG A1034 17456 24190 6788 489 -1833 -2530 N ATOM 1721 N ALA A1035 63.292 25.234 3.012 1.00122.65 N ANISOU 1721 N ALA A1035 13151 25555 7897 199 -1561 -2424 N ATOM 1722 CA ALA A1035 63.226 24.173 4.011 1.00115.42 C ANISOU 1722 CA ALA A1035 11687 24946 7219 302 -1353 -2280 C ATOM 1723 C ALA A1035 62.466 24.610 5.257 1.00117.38 C ANISOU 1723 C ALA A1035 11566 25326 7709 53 -1582 -2516 C ATOM 1724 O ALA A1035 61.838 23.778 5.919 1.00116.83 O ANISOU 1724 O ALA A1035 11196 25248 7948 208 -1548 -2579 O ATOM 1725 CB ALA A1035 64.635 23.712 4.381 1.00122.46 C ANISOU 1725 CB ALA A1035 12128 26481 7918 303 -858 -1675 C ATOM 1726 N ALA A1036 62.513 25.900 5.596 1.00116.99 N ANISOU 1726 N ALA A1036 11610 25152 7688 -309 -1702 -2577 N ATOM 1727 CA ALA A1036 61.740 26.391 6.732 1.00119.68 C ANISOU 1727 CA ALA A1036 11788 25376 8310 -483 -1806 -2767 C ATOM 1728 C ALA A1036 60.246 26.214 6.493 1.00128.03 C ANISOU 1728 C ALA A1036 13016 25928 9700 -213 -2090 -3144 C ATOM 1729 O ALA A1036 59.517 25.723 7.364 1.00131.53 O ANISOU 1729 O ALA A1036 13119 26468 10390 -115 -2098 -3239 O ATOM 1730 CB ALA A1036 62.078 27.857 6.995 1.00128.93 C ANISOU 1730 CB ALA A1036 13223 26404 9361 -902 -1852 -2773 C ATOM 1731 N ALA A1037 59.771 26.600 5.306 1.00127.45 N ANISOU 1731 N ALA A1037 13437 25357 9630 -91 -2346 -3326 N ATOM 1732 CA ALA A1037 58.367 26.392 4.972 1.00118.55 C ANISOU 1732 CA ALA A1037 12409 23810 8826 138 -2693 -3611 C ATOM 1733 C ALA A1037 58.037 24.911 4.847 1.00120.34 C ANISOU 1733 C ALA A1037 12402 24135 9186 383 -2740 -3638 C ATOM 1734 O ALA A1037 56.922 24.502 5.181 1.00124.79 O ANISOU 1734 O ALA A1037 12744 24501 10170 497 -2931 -3766 O ATOM 1735 CB ALA A1037 58.012 27.130 3.683 1.00113.32 C ANISOU 1735 CB ALA A1037 12339 22632 8087 194 -2988 -3740 C ATOM 1736 N LEU A1038 58.985 24.097 4.374 1.00121.88 N ANISOU 1736 N LEU A1038 12679 24497 9132 477 -2483 -3435 N ATOM 1737 CA LEU A1038 58.784 22.650 4.357 1.00117.36 C ANISOU 1737 CA LEU A1038 11987 23828 8777 704 -2348 -3366 C ATOM 1738 C LEU A1038 58.532 22.118 5.763 1.00115.46 C ANISOU 1738 C LEU A1038 11096 23911 8863 703 -2138 -3270 C ATOM 1739 O LEU A1038 57.582 21.361 5.997 1.00116.42 O ANISOU 1739 O LEU A1038 11048 23786 9400 820 -2249 -3373 O ATOM 1740 CB LEU A1038 60.005 21.959 3.745 1.00124.97 C ANISOU 1740 CB LEU A1038 13172 24931 9379 859 -1936 -3068 C ATOM 1741 CG LEU A1038 59.957 21.459 2.299 1.00121.63 C ANISOU 1741 CG LEU A1038 13484 23976 8753 1063 -2028 -3156 C ATOM 1742 CD1 LEU A1038 60.001 22.610 1.309 1.00120.80 C ANISOU 1742 CD1 LEU A1038 13905 23641 8353 975 -2321 -3298 C ATOM 1743 CD2 LEU A1038 61.098 20.483 2.044 1.00119.47 C ANISOU 1743 CD2 LEU A1038 13323 23857 8211 1324 -1428 -2774 C ATOM 1744 N ASP A1039 59.380 22.515 6.713 1.00117.12 N ANISOU 1744 N ASP A1039 10945 24678 8877 542 -1851 -3049 N ATOM 1745 CA ASP A1039 59.240 22.057 8.090 1.00130.84 C ANISOU 1745 CA ASP A1039 12112 26765 10835 545 -1630 -2930 C ATOM 1746 C ASP A1039 57.945 22.566 8.715 1.00132.82 C ANISOU 1746 C ASP A1039 12253 26755 11456 521 -1882 -3199 C ATOM 1747 O ASP A1039 57.283 21.839 9.464 1.00125.06 O ANISOU 1747 O ASP A1039 10905 25756 10856 671 -1780 -3179 O ATOM 1748 CB ASP A1039 60.454 22.502 8.907 1.00138.34 C ANISOU 1748 CB ASP A1039 12770 28382 11409 301 -1366 -2622 C ATOM 1749 CG ASP A1039 60.783 21.544 10.034 1.00149.86 C ANISOU 1749 CG ASP A1039 13666 30306 12966 408 -1011 -2324 C ATOM 1750 OD1 ASP A1039 60.969 20.341 9.754 1.00147.45 O ANISOU 1750 OD1 ASP A1039 13262 29976 12785 710 -741 -2130 O ATOM 1751 OD2 ASP A1039 60.868 21.995 11.196 1.00160.37 O ANISOU 1751 OD2 ASP A1039 14715 32006 14214 197 -980 -2273 O ATOM 1752 N ALA A1040 57.570 23.815 8.422 1.00138.29 N ANISOU 1752 N ALA A1040 13262 27229 12054 372 -2156 -3407 N ATOM 1753 CA ALA A1040 56.309 24.346 8.933 1.00130.25 C ANISOU 1753 CA ALA A1040 12170 25919 11399 433 -2325 -3590 C ATOM 1754 C ALA A1040 55.116 23.591 8.358 1.00134.63 C ANISOU 1754 C ALA A1040 12654 26024 12478 668 -2595 -3677 C ATOM 1755 O ALA A1040 54.144 23.313 9.070 1.00135.97 O ANISOU 1755 O ALA A1040 12465 26087 13112 803 -2578 -3662 O ATOM 1756 CB ALA A1040 56.199 25.839 8.623 1.00128.28 C ANISOU 1756 CB ALA A1040 12349 25481 10911 272 -2504 -3751 C ATOM 1757 N GLN A1041 55.169 23.260 7.065 1.00133.90 N ANISOU 1757 N GLN A1041 12921 25651 12303 698 -2854 -3743 N ATOM 1758 CA GLN A1041 54.109 22.476 6.443 1.00119.73 C ANISOU 1758 CA GLN A1041 11122 23431 10941 815 -3196 -3817 C ATOM 1759 C GLN A1041 54.014 21.091 7.068 1.00123.48 C ANISOU 1759 C GLN A1041 11204 23988 11727 913 -2945 -3692 C ATOM 1760 O GLN A1041 52.915 20.553 7.242 1.00116.47 O ANISOU 1760 O GLN A1041 10035 22848 11370 966 -3135 -3695 O ATOM 1761 CB GLN A1041 54.358 22.370 4.939 1.00114.07 C ANISOU 1761 CB GLN A1041 11015 22402 9924 791 -3499 -3919 C ATOM 1762 CG GLN A1041 53.225 21.739 4.161 1.00116.80 C ANISOU 1762 CG GLN A1041 11480 22272 10626 800 -4002 -4018 C ATOM 1763 CD GLN A1041 52.417 22.761 3.394 1.00132.17 C ANISOU 1763 CD GLN A1041 13664 23936 12618 769 -4529 -4119 C ATOM 1764 OE1 GLN A1041 52.776 23.938 3.340 1.00129.86 O ANISOU 1764 OE1 GLN A1041 13550 23746 12045 769 -4465 -4145 O ATOM 1765 NE2 GLN A1041 51.319 22.318 2.793 1.00153.96 N ANISOU 1765 NE2 GLN A1041 16427 26340 15730 721 -5064 -4146 N ATOM 1766 N LYS A1042 55.161 20.493 7.397 1.00132.15 N ANISOU 1766 N LYS A1042 12252 25440 12518 942 -2502 -3528 N ATOM 1767 CA LYS A1042 55.155 19.219 8.109 1.00126.61 C ANISOU 1767 CA LYS A1042 11171 24850 12083 1076 -2166 -3367 C ATOM 1768 C LYS A1042 54.534 19.369 9.494 1.00115.34 C ANISOU 1768 C LYS A1042 9170 23626 11029 1123 -2006 -3298 C ATOM 1769 O LYS A1042 53.716 18.541 9.913 1.00111.12 O ANISOU 1769 O LYS A1042 8310 22918 10994 1230 -1974 -3254 O ATOM 1770 CB LYS A1042 56.579 18.671 8.207 1.00125.87 C ANISOU 1770 CB LYS A1042 11106 25161 11558 1151 -1674 -3114 C ATOM 1771 CG LYS A1042 57.194 18.319 6.862 1.00127.35 C ANISOU 1771 CG LYS A1042 11904 25091 11392 1205 -1690 -3117 C ATOM 1772 CD LYS A1042 58.709 18.400 6.903 1.00119.81 C ANISOU 1772 CD LYS A1042 10949 24630 9944 1258 -1232 -2792 C ATOM 1773 CE LYS A1042 59.296 18.183 5.521 1.00117.89 C ANISOU 1773 CE LYS A1042 11381 24081 9330 1370 -1189 -2768 C ATOM 1774 NZ LYS A1042 58.645 19.066 4.516 1.00114.35 N ANISOU 1774 NZ LYS A1042 11444 23189 8816 1222 -1750 -3108 N ATOM 1775 N ALA A1043 54.907 20.427 10.213 1.00115.82 N ANISOU 1775 N ALA A1043 9156 24017 10835 1030 -1890 -3281 N ATOM 1776 CA ALA A1043 54.386 20.721 11.550 1.00117.12 C ANISOU 1776 CA ALA A1043 8928 24343 11228 1089 -1689 -3224 C ATOM 1777 C ALA A1043 54.520 19.533 12.501 1.00112.35 C ANISOU 1777 C ALA A1043 7866 23991 10828 1253 -1283 -3005 C ATOM 1778 O ALA A1043 53.541 19.098 13.108 1.00109.38 O ANISOU 1778 O ALA A1043 7153 23441 10967 1416 -1214 -2965 O ATOM 1779 CB ALA A1043 52.930 21.167 11.466 1.00113.86 C ANISOU 1779 CB ALA A1043 8446 23483 11331 1186 -1977 -3334 C ATOM 1780 N ARG A1062 46.945 25.196 5.724 1.00154.36 N ANISOU 1780 N ARG A1062 14371 26381 17897 1378 -5094 -3370 N ATOM 1781 CA ARG A1062 47.989 24.204 5.496 1.00160.41 C ANISOU 1781 CA ARG A1062 15407 27257 18285 1156 -5023 -3591 C ATOM 1782 C ARG A1062 48.728 24.469 4.192 1.00162.77 C ANISOU 1782 C ARG A1062 16422 27445 17978 1010 -5327 -3801 C ATOM 1783 O ARG A1062 49.949 24.336 4.121 1.00150.77 O ANISOU 1783 O ARG A1062 15273 26085 15928 929 -5026 -3954 O ATOM 1784 CB ARG A1062 47.396 22.795 5.477 1.00163.13 C ANISOU 1784 CB ARG A1062 15375 27494 19115 1039 -5260 -3502 C ATOM 1785 CG ARG A1062 46.850 22.332 6.809 1.00152.10 C ANISOU 1785 CG ARG A1062 13279 26225 18287 1189 -4858 -3284 C ATOM 1786 CD ARG A1062 46.334 20.911 6.712 1.00148.95 C ANISOU 1786 CD ARG A1062 12568 25679 18347 1020 -5091 -3204 C ATOM 1787 NE ARG A1062 46.016 20.360 8.022 1.00142.73 N ANISOU 1787 NE ARG A1062 11159 25033 18039 1179 -4601 -3004 N ATOM 1788 CZ ARG A1062 45.581 19.125 8.228 1.00146.56 C ANISOU 1788 CZ ARG A1062 11295 25408 18984 1064 -4644 -2896 C ATOM 1789 NH1 ARG A1062 45.390 18.284 7.224 1.00148.30 N ANISOU 1789 NH1 ARG A1062 11765 25347 19235 745 -5176 -2985 N ATOM 1790 NH2 ARG A1062 45.331 18.723 9.471 1.00151.44 N ANISOU 1790 NH2 ARG A1062 11363 26167 20010 1261 -4129 -2694 N ATOM 1791 N HIS A1063 47.980 24.848 3.162 1.00179.05 N ANISOU 1791 N HIS A1063 18656 29249 20124 997 -5914 -3756 N ATOM 1792 CA HIS A1063 48.536 25.049 1.832 1.00179.34 C ANISOU 1792 CA HIS A1063 19418 29125 19599 886 -6252 -3934 C ATOM 1793 C HIS A1063 48.995 26.479 1.584 1.00170.63 C ANISOU 1793 C HIS A1063 18710 28046 18075 1007 -6089 -3981 C ATOM 1794 O HIS A1063 49.400 26.795 0.461 1.00169.11 O ANISOU 1794 O HIS A1063 19125 27705 17425 962 -6348 -4093 O ATOM 1795 CB HIS A1063 47.510 24.643 0.772 1.00197.51 C ANISOU 1795 CB HIS A1063 21776 31131 22137 758 -7048 -3857 C ATOM 1796 CG HIS A1063 47.027 23.234 0.914 1.00203.89 C ANISOU 1796 CG HIS A1063 22284 31841 23342 551 -7270 -3821 C ATOM 1797 ND1 HIS A1063 47.799 22.145 0.570 1.00209.07 N ANISOU 1797 ND1 HIS A1063 23398 32392 23647 382 -7175 -4028 N ATOM 1798 CD2 HIS A1063 45.854 22.734 1.372 1.00206.97 C ANISOU 1798 CD2 HIS A1063 21980 32199 24462 488 -7539 -3569 C ATOM 1799 CE1 HIS A1063 47.121 21.036 0.806 1.00225.08 C ANISOU 1799 CE1 HIS A1063 25083 34292 26144 196 -7388 -3949 C ATOM 1800 NE2 HIS A1063 45.938 21.366 1.292 1.00219.71 N ANISOU 1800 NE2 HIS A1063 23669 33669 26143 232 -7635 -3666 N ATOM 1801 N GLY A1064 48.942 27.349 2.594 1.00152.62 N ANISOU 1801 N GLY A1064 16173 25906 15910 1156 -5645 -3898 N ATOM 1802 CA GLY A1064 49.408 28.711 2.414 1.00148.06 C ANISOU 1802 CA GLY A1064 16043 25299 14915 1225 -5444 -3955 C ATOM 1803 C GLY A1064 50.903 28.828 2.211 1.00146.65 C ANISOU 1803 C GLY A1064 16364 25278 14078 1041 -5138 -4151 C ATOM 1804 O GLY A1064 51.365 29.814 1.627 1.00146.50 O ANISOU 1804 O GLY A1064 16845 25169 13650 1032 -5112 -4211 O ATOM 1805 N PHE A1065 51.670 27.848 2.687 1.00145.83 N ANISOU 1805 N PHE A1065 16104 25417 13886 909 -4876 -4195 N ATOM 1806 CA PHE A1065 53.114 27.842 2.503 1.00136.29 C ANISOU 1806 CA PHE A1065 15252 24420 12111 752 -4565 -4266 C ATOM 1807 C PHE A1065 53.554 27.150 1.221 1.00137.16 C ANISOU 1807 C PHE A1065 15849 24261 12005 729 -4737 -4251 C ATOM 1808 O PHE A1065 54.641 27.451 0.718 1.00136.21 O ANISOU 1808 O PHE A1065 16159 24123 11473 658 -4477 -4196 O ATOM 1809 CB PHE A1065 53.797 27.165 3.695 1.00128.00 C ANISOU 1809 CB PHE A1065 13788 23762 11083 659 -4103 -4199 C ATOM 1810 CG PHE A1065 53.698 27.946 4.968 1.00124.97 C ANISOU 1810 CG PHE A1065 13156 23555 10774 618 -3780 -4170 C ATOM 1811 CD1 PHE A1065 53.596 29.325 4.940 1.00132.43 C ANISOU 1811 CD1 PHE A1065 14434 24352 11530 592 -3750 -4223 C ATOM 1812 CD2 PHE A1065 53.705 27.304 6.193 1.00120.85 C ANISOU 1812 CD2 PHE A1065 12147 23302 10466 617 -3479 -4088 C ATOM 1813 CE1 PHE A1065 53.505 30.046 6.106 1.00134.57 C ANISOU 1813 CE1 PHE A1065 14633 24702 11794 544 -3421 -4217 C ATOM 1814 CE2 PHE A1065 53.614 28.023 7.366 1.00119.87 C ANISOU 1814 CE2 PHE A1065 11918 23295 10330 579 -3175 -4074 C ATOM 1815 CZ PHE A1065 53.513 29.398 7.321 1.00126.61 C ANISOU 1815 CZ PHE A1065 13185 23960 10962 532 -3143 -4150 C ATOM 1816 N ASP A1066 52.741 26.237 0.684 1.00144.26 N ANISOU 1816 N ASP A1066 16718 24935 13160 770 -5165 -4279 N ATOM 1817 CA ASP A1066 53.131 25.515 -0.523 1.00145.49 C ANISOU 1817 CA ASP A1066 17471 24791 13016 738 -5325 -4304 C ATOM 1818 C ASP A1066 53.329 26.453 -1.707 1.00153.54 C ANISOU 1818 C ASP A1066 19158 25493 13686 751 -5478 -4281 C ATOM 1819 O ASP A1066 54.136 26.162 -2.597 1.00158.59 O ANISOU 1819 O ASP A1066 20389 25972 13895 756 -5363 -4278 O ATOM 1820 CB ASP A1066 52.092 24.446 -0.862 1.00140.68 C ANISOU 1820 CB ASP A1066 16772 23944 12735 686 -5845 -4355 C ATOM 1821 CG ASP A1066 52.378 23.121 -0.184 1.00138.35 C ANISOU 1821 CG ASP A1066 16166 23865 12536 673 -5609 -4408 C ATOM 1822 OD1 ASP A1066 53.434 23.007 0.475 1.00137.84 O ANISOU 1822 OD1 ASP A1066 15977 24123 12273 728 -5005 -4338 O ATOM 1823 OD2 ASP A1066 51.551 22.193 -0.311 1.00127.82 O ANISOU 1823 OD2 ASP A1066 14730 22297 11540 571 -5964 -4422 O ATOM 1824 N ILE A1067 52.604 27.569 -1.744 1.00158.01 N ANISOU 1824 N ILE A1067 19651 25990 14394 805 -5713 -4260 N ATOM 1825 CA ILE A1067 52.780 28.555 -2.804 1.00164.84 C ANISOU 1825 CA ILE A1067 21116 26601 14915 845 -5828 -4233 C ATOM 1826 C ILE A1067 53.805 29.592 -2.360 1.00175.24 C ANISOU 1826 C ILE A1067 22528 28117 15938 823 -5306 -4223 C ATOM 1827 O ILE A1067 54.868 29.730 -2.976 1.00183.26 O ANISOU 1827 O ILE A1067 24010 29069 16552 775 -5036 -4171 O ATOM 1828 CB ILE A1067 51.445 29.223 -3.183 1.00160.58 C ANISOU 1828 CB ILE A1067 20476 25911 14627 963 -6397 -4191 C ATOM 1829 CG1 ILE A1067 50.505 28.208 -3.837 1.00165.94 C ANISOU 1829 CG1 ILE A1067 21143 26350 15558 861 -6988 -4131 C ATOM 1830 CG2 ILE A1067 51.682 30.405 -4.109 1.00166.15 C ANISOU 1830 CG2 ILE A1067 21755 26430 14945 1059 -6431 -4166 C ATOM 1831 CD1 ILE A1067 49.201 28.807 -4.331 1.00168.77 C ANISOU 1831 CD1 ILE A1067 21350 26600 16176 955 -7618 -3981 C ATOM 1832 N LEU A1068 53.497 30.308 -1.279 1.00159.65 N ANISOU 1832 N LEU A1068 20129 26392 14137 841 -5163 -4264 N ATOM 1833 CA LEU A1068 54.341 31.393 -0.772 1.00151.47 C ANISOU 1833 CA LEU A1068 19227 25512 12811 727 -4726 -4271 C ATOM 1834 C LEU A1068 54.742 32.377 -1.869 1.00151.98 C ANISOU 1834 C LEU A1068 19943 25312 12492 747 -4752 -4249 C ATOM 1835 O LEU A1068 53.949 33.227 -2.274 1.00145.87 O ANISOU 1835 O LEU A1068 19349 24381 11696 933 -5036 -4306 O ATOM 1836 CB LEU A1068 55.593 30.834 -0.090 1.00137.83 C ANISOU 1836 CB LEU A1068 17329 24075 10966 507 -4238 -4176 C ATOM 1837 CG LEU A1068 55.462 30.553 1.408 1.00133.07 C ANISOU 1837 CG LEU A1068 16127 23834 10598 423 -4015 -4196 C ATOM 1838 CD1 LEU A1068 56.812 30.202 2.014 1.00137.29 C ANISOU 1838 CD1 LEU A1068 16517 24701 10946 187 -3561 -4036 C ATOM 1839 CD2 LEU A1068 54.841 31.744 2.122 1.00129.82 C ANISOU 1839 CD2 LEU A1068 15685 23465 10176 436 -4003 -4326 C ATOM 1840 N THR A1097 51.466 37.645 0.217 1.00161.52 N ANISOU 1840 N THR A1097 21439 25784 14147 1501 -4198 -4152 N ATOM 1841 CA THR A1097 51.219 36.254 0.573 1.00149.61 C ANISOU 1841 CA THR A1097 19289 24562 12995 1462 -4440 -4142 C ATOM 1842 C THR A1097 51.373 36.046 2.070 1.00156.43 C ANISOU 1842 C THR A1097 19834 25614 13988 1313 -4009 -4189 C ATOM 1843 O THR A1097 50.640 35.265 2.680 1.00161.53 O ANISOU 1843 O THR A1097 19904 26365 15103 1454 -4072 -4084 O ATOM 1844 CB THR A1097 52.181 35.298 -0.159 1.00142.55 C ANISOU 1844 CB THR A1097 18464 23885 11813 1215 -4676 -4269 C ATOM 1845 OG1 THR A1097 52.078 35.497 -1.574 1.00149.18 O ANISOU 1845 OG1 THR A1097 19717 24515 12448 1358 -5062 -4239 O ATOM 1846 CG2 THR A1097 51.846 33.851 0.170 1.00134.53 C ANISOU 1846 CG2 THR A1097 16857 23086 11170 1199 -4901 -4250 C ATOM 1847 N ARG A1098 52.329 36.768 2.656 1.00161.58 N ANISOU 1847 N ARG A1098 20888 26300 14203 999 -3584 -4329 N ATOM 1848 CA ARG A1098 52.696 36.522 4.046 1.00166.09 C ANISOU 1848 CA ARG A1098 21250 27104 14754 762 -3221 -4395 C ATOM 1849 C ARG A1098 51.533 36.785 4.994 1.00166.17 C ANISOU 1849 C ARG A1098 21067 26907 15163 1103 -2967 -4270 C ATOM 1850 O ARG A1098 51.372 36.078 5.993 1.00167.18 O ANISOU 1850 O ARG A1098 20763 27241 15516 1095 -2821 -4246 O ATOM 1851 CB ARG A1098 53.910 37.371 4.423 1.00168.57 C ANISOU 1851 CB ARG A1098 22103 27469 14479 283 -2896 -4539 C ATOM 1852 CG ARG A1098 53.803 38.838 4.038 1.00174.35 C ANISOU 1852 CG ARG A1098 23559 27747 14938 322 -2705 -4569 C ATOM 1853 CD ARG A1098 55.124 39.546 4.292 1.00185.47 C ANISOU 1853 CD ARG A1098 25471 29237 15762 -277 -2474 -4700 C ATOM 1854 NE ARG A1098 55.610 39.302 5.644 1.00187.94 N ANISOU 1854 NE ARG A1098 25648 29832 15927 -667 -2250 -4769 N ATOM 1855 CZ ARG A1098 55.318 40.060 6.692 1.00188.05 C ANISOU 1855 CZ ARG A1098 26074 29587 15787 -756 -1888 -4853 C ATOM 1856 NH1 ARG A1098 54.542 41.126 6.578 1.00191.33 N ANISOU 1856 NH1 ARG A1098 27060 29434 16203 -448 -1636 -4859 N ATOM 1857 NH2 ARG A1098 55.818 39.743 7.883 1.00182.13 N ANISOU 1857 NH2 ARG A1098 25213 29140 14848 -1140 -1750 -4910 N ATOM 1858 N ASN A1099 50.717 37.799 4.705 1.00165.12 N ANISOU 1858 N ASN A1099 20947 30326 11464 1561 2304 -464 N ATOM 1859 CA ASN A1099 49.634 38.166 5.615 1.00162.26 C ANISOU 1859 CA ASN A1099 20599 29734 11317 1483 2071 -410 C ATOM 1860 C ASN A1099 48.720 36.984 5.929 1.00164.36 C ANISOU 1860 C ASN A1099 20736 30012 11702 1511 1754 -924 C ATOM 1861 O ASN A1099 48.628 36.551 7.082 1.00168.56 O ANISOU 1861 O ASN A1099 21172 30272 12603 1348 1683 -1079 O ATOM 1862 CB ASN A1099 48.813 39.320 5.035 1.00162.73 C ANISOU 1862 CB ASN A1099 20836 29891 11106 1613 2003 -46 C ATOM 1863 CG ASN A1099 47.426 39.439 5.667 1.00165.82 C ANISOU 1863 CG ASN A1099 21209 30172 11622 1629 1687 -109 C ATOM 1864 OD1 ASN A1099 46.457 38.856 5.180 1.00170.74 O ANISOU 1864 OD1 ASN A1099 21764 31023 12084 1779 1412 -411 O ATOM 1865 ND2 ASN A1099 47.329 40.207 6.750 1.00165.48 N ANISOU 1865 ND2 ASN A1099 21221 29788 11868 1468 1728 172 N ATOM 1866 N ALA A1100 48.050 36.435 4.913 1.00161.79 N ANISOU 1866 N ALA A1100 20408 29996 11070 1702 1566 -1203 N ATOM 1867 CA ALA A1100 46.857 35.637 5.178 1.00158.35 C ANISOU 1867 CA ALA A1100 19875 29562 10729 1706 1228 -1612 C ATOM 1868 C ALA A1100 47.099 34.446 6.100 1.00166.02 C ANISOU 1868 C ALA A1100 20722 30284 12074 1546 1191 -2026 C ATOM 1869 O ALA A1100 46.691 34.468 7.268 1.00171.44 O ANISOU 1869 O ALA A1100 21353 30685 13100 1385 1098 -2029 O ATOM 1870 CB ALA A1100 46.253 35.154 3.853 1.00140.92 C ANISOU 1870 CB ALA A1100 17671 27751 8123 1917 1058 -1882 C ATOM 1871 N TYR A1101 47.837 33.448 5.618 1.00161.28 N ANISOU 1871 N TYR A1101 20092 29771 11416 1595 1292 -2348 N ATOM 1872 CA TYR A1101 47.907 32.177 6.329 1.00163.70 C ANISOU 1872 CA TYR A1101 20309 29850 12039 1489 1227 -2801 C ATOM 1873 C TYR A1101 48.809 32.273 7.555 1.00168.40 C ANISOU 1873 C TYR A1101 20851 30122 13012 1324 1424 -2639 C ATOM 1874 O TYR A1101 48.467 31.760 8.635 1.00158.38 O ANISOU 1874 O TYR A1101 19518 28567 12093 1179 1318 -2828 O ATOM 1875 CB TYR A1101 48.373 31.104 5.355 1.00152.58 C ANISOU 1875 CB TYR A1101 18916 28633 10425 1627 1277 -3194 C ATOM 1876 CG TYR A1101 47.837 31.364 3.960 1.00150.17 C ANISOU 1876 CG TYR A1101 18676 28730 9651 1814 1175 -3200 C ATOM 1877 CD1 TYR A1101 46.513 31.082 3.637 1.00145.46 C ANISOU 1877 CD1 TYR A1101 18055 28256 8955 1834 857 -3457 C ATOM 1878 CD2 TYR A1101 48.643 31.930 2.980 1.00153.84 C ANISOU 1878 CD2 TYR A1101 19215 29467 9772 1966 1399 -2932 C ATOM 1879 CE1 TYR A1101 46.017 31.336 2.371 1.00158.17 C ANISOU 1879 CE1 TYR A1101 19708 30266 10125 2018 754 -3458 C ATOM 1880 CE2 TYR A1101 48.157 32.182 1.714 1.00149.27 C ANISOU 1880 CE2 TYR A1101 18701 29267 8748 2150 1308 -2925 C ATOM 1881 CZ TYR A1101 46.844 31.885 1.415 1.00159.58 C ANISOU 1881 CZ TYR A1101 19977 30706 9952 2184 980 -3189 C ATOM 1882 OH TYR A1101 46.360 32.140 0.153 1.00164.94 O ANISOU 1882 OH TYR A1101 20703 31794 10173 2381 881 -3181 O ATOM 1883 N ILE A1102 49.952 32.948 7.408 1.00185.07 N ANISOU 1883 N ILE A1102 22979 32281 15058 1334 1714 -2284 N ATOM 1884 CA ILE A1102 50.840 33.195 8.539 1.00194.80 C ANISOU 1884 CA ILE A1102 24138 33247 16631 1167 1906 -2080 C ATOM 1885 C ILE A1102 50.078 33.897 9.655 1.00186.12 C ANISOU 1885 C ILE A1102 23043 31892 15784 994 1773 -1873 C ATOM 1886 O ILE A1102 49.891 33.339 10.741 1.00191.46 O ANISOU 1886 O ILE A1102 23642 32311 16795 866 1688 -2063 O ATOM 1887 CB ILE A1102 52.070 34.003 8.088 1.00196.41 C ANISOU 1887 CB ILE A1102 24354 33576 16696 1177 2229 -1687 C ATOM 1888 CG1 ILE A1102 53.078 33.094 7.384 1.00179.74 C ANISOU 1888 CG1 ILE A1102 22184 31645 14463 1317 2404 -1936 C ATOM 1889 CG2 ILE A1102 52.714 34.721 9.266 1.00190.07 C ANISOU 1889 CG2 ILE A1102 23488 32507 16223 958 2388 -1353 C ATOM 1890 CD1 ILE A1102 54.170 33.831 6.647 1.00173.11 C ANISOU 1890 CD1 ILE A1102 21355 31010 13408 1355 2709 -1589 C ATOM 1891 N GLN A1103 49.588 35.114 9.389 1.00166.72 N ANISOU 1891 N GLN A1103 20690 29495 13161 1005 1754 -1485 N ATOM 1892 CA GLN A1103 48.918 35.886 10.427 1.00166.15 C ANISOU 1892 CA GLN A1103 20643 29174 13312 859 1656 -1249 C ATOM 1893 C GLN A1103 47.752 35.117 11.027 1.00159.87 C ANISOU 1893 C GLN A1103 19780 28272 12693 824 1355 -1616 C ATOM 1894 O GLN A1103 47.503 35.209 12.233 1.00152.55 O ANISOU 1894 O GLN A1103 18811 27073 12080 658 1305 -1583 O ATOM 1895 CB GLN A1103 48.433 37.216 9.857 1.00173.40 C ANISOU 1895 CB GLN A1103 21720 30188 13977 939 1663 -820 C ATOM 1896 CG GLN A1103 48.150 38.256 10.919 1.00177.64 C ANISOU 1896 CG GLN A1103 22323 30428 14745 781 1679 -461 C ATOM 1897 CD GLN A1103 47.182 39.317 10.452 1.00182.83 C ANISOU 1897 CD GLN A1103 23139 31152 15176 913 1574 -158 C ATOM 1898 OE1 GLN A1103 46.530 39.174 9.417 1.00181.38 O ANISOU 1898 OE1 GLN A1103 22979 31260 14679 1122 1429 -264 O ATOM 1899 NE2 GLN A1103 47.077 40.393 11.220 1.00187.08 N ANISOU 1899 NE2 GLN A1103 23791 31419 15873 799 1646 218 N ATOM 1900 N LYS A1104 47.029 34.344 10.210 1.00160.52 N ANISOU 1900 N LYS A1104 19845 28561 12585 957 1156 -1978 N ATOM 1901 CA LYS A1104 45.927 33.552 10.744 1.00158.16 C ANISOU 1901 CA LYS A1104 19467 28151 12476 889 879 -2356 C ATOM 1902 C LYS A1104 46.413 32.558 11.793 1.00154.45 C ANISOU 1902 C LYS A1104 18918 27381 12386 732 929 -2642 C ATOM 1903 O LYS A1104 45.977 32.595 12.950 1.00146.95 O ANISOU 1903 O LYS A1104 17924 26171 11738 572 848 -2637 O ATOM 1904 CB LYS A1104 45.206 32.832 9.607 1.00153.71 C ANISOU 1904 CB LYS A1104 18891 27867 11645 1033 684 -2719 C ATOM 1905 CG LYS A1104 43.912 33.507 9.170 1.00140.69 C ANISOU 1905 CG LYS A1104 17242 26419 9794 1124 447 -2603 C ATOM 1906 CD LYS A1104 43.775 33.521 7.655 1.00131.59 C ANISOU 1906 CD LYS A1104 16133 25670 8195 1343 406 -2653 C ATOM 1907 CE LYS A1104 44.158 32.178 7.062 1.00137.92 C ANISOU 1907 CE LYS A1104 16908 26547 8948 1361 408 -3147 C ATOM 1908 NZ LYS A1104 44.304 32.229 5.584 1.00136.53 N ANISOU 1908 NZ LYS A1104 16793 26767 8315 1576 431 -3163 N ATOM 1909 N TYR A1105 47.314 31.648 11.408 1.00157.74 N ANISOU 1909 N TYR A1105 19321 27826 12788 791 1068 -2893 N ATOM 1910 CA TYR A1105 47.728 30.620 12.363 1.00153.37 C ANISOU 1910 CA TYR A1105 18708 26977 12590 683 1111 -3185 C ATOM 1911 C TYR A1105 48.577 31.202 13.489 1.00138.70 C ANISOU 1911 C TYR A1105 16801 24911 10986 553 1304 -2862 C ATOM 1912 O TYR A1105 48.498 30.741 14.634 1.00133.35 O ANISOU 1912 O TYR A1105 16072 23949 10645 417 1272 -2991 O ATOM 1913 CB TYR A1105 48.471 29.494 11.648 1.00168.10 C ANISOU 1913 CB TYR A1105 20588 28915 14368 817 1218 -3533 C ATOM 1914 CG TYR A1105 47.652 28.229 11.558 1.00175.94 C ANISOU 1914 CG TYR A1105 21602 29787 15460 799 1015 -4064 C ATOM 1915 CD1 TYR A1105 46.546 28.156 10.721 1.00176.54 C ANISOU 1915 CD1 TYR A1105 21702 30059 15316 833 783 -4241 C ATOM 1916 CD2 TYR A1105 47.973 27.112 12.319 1.00174.90 C ANISOU 1916 CD2 TYR A1105 21471 29332 15653 740 1061 -4382 C ATOM 1917 CE1 TYR A1105 45.785 27.004 10.638 1.00176.99 C ANISOU 1917 CE1 TYR A1105 21773 29991 15485 772 602 -4730 C ATOM 1918 CE2 TYR A1105 47.218 25.954 12.242 1.00175.84 C ANISOU 1918 CE2 TYR A1105 21639 29283 15889 692 893 -4860 C ATOM 1919 CZ TYR A1105 46.125 25.907 11.399 1.00177.36 C ANISOU 1919 CZ TYR A1105 21846 29673 15870 689 665 -5036 C ATOM 1920 OH TYR A1105 45.370 24.760 11.317 1.00177.39 O ANISOU 1920 OH TYR A1105 21892 29502 16006 602 505 -5512 O ATOM 1921 N LEU A1106 49.394 32.211 13.185 1.00140.70 N ANISOU 1921 N LEU A1106 17069 25297 11092 577 1510 -2442 N ATOM 1922 CA LEU A1106 50.260 32.792 14.205 1.00130.07 C ANISOU 1922 CA LEU A1106 15660 23769 9990 426 1700 -2134 C ATOM 1923 C LEU A1106 49.454 33.581 15.240 1.00128.15 C ANISOU 1923 C LEU A1106 15440 23315 9935 251 1578 -1915 C ATOM 1924 O LEU A1106 49.789 33.571 16.431 1.00119.52 O ANISOU 1924 O LEU A1106 14280 21985 9149 90 1634 -1862 O ATOM 1925 CB LEU A1106 51.332 33.658 13.538 1.00130.98 C ANISOU 1925 CB LEU A1106 15788 24067 9910 465 1959 -1757 C ATOM 1926 CG LEU A1106 52.615 32.993 13.001 1.00130.40 C ANISOU 1926 CG LEU A1106 15630 24139 9777 577 2180 -1877 C ATOM 1927 CD1 LEU A1106 53.442 32.417 14.150 1.00115.13 C ANISOU 1927 CD1 LEU A1106 13546 21997 8202 481 2285 -1963 C ATOM 1928 CD2 LEU A1106 52.378 31.922 11.920 1.00141.14 C ANISOU 1928 CD2 LEU A1106 17033 25690 10903 793 2100 -2291 C ATOM 1929 N GLN A 301 48.382 34.257 14.813 1.00128.72 N ANISOU 1929 N GLN A 301 15606 23478 9825 296 1412 -1790 N ATOM 1930 CA GLN A 301 47.524 34.960 15.767 1.00125.51 C ANISOU 1930 CA GLN A 301 15228 22877 9584 163 1286 -1605 C ATOM 1931 C GLN A 301 46.835 33.981 16.709 1.00120.25 C ANISOU 1931 C GLN A 301 14481 22004 9205 58 1104 -1984 C ATOM 1932 O GLN A 301 46.660 34.270 17.898 1.00127.33 O ANISOU 1932 O GLN A 301 15359 22660 10359 -109 1092 -1877 O ATOM 1933 CB GLN A 301 46.489 35.809 15.027 1.00131.81 C ANISOU 1933 CB GLN A 301 16132 23844 10108 289 1139 -1412 C ATOM 1934 CG GLN A 301 45.713 36.768 15.910 1.00128.07 C ANISOU 1934 CG GLN A 301 15714 23182 9764 194 1055 -1130 C ATOM 1935 CD GLN A 301 46.435 38.082 16.120 1.00130.73 C ANISOU 1935 CD GLN A 301 16173 23399 10101 122 1289 -615 C ATOM 1936 OE1 GLN A 301 46.529 38.903 15.207 1.00140.46 O ANISOU 1936 OE1 GLN A 301 17533 24770 11065 248 1375 -331 O ATOM 1937 NE2 GLN A 301 46.946 38.291 17.327 1.00120.09 N ANISOU 1937 NE2 GLN A 301 14795 21774 9060 -96 1398 -496 N ATOM 1938 N ALA A 302 46.444 32.814 16.193 1.00120.36 N ANISOU 1938 N ALA A 302 14460 22085 9186 139 970 -2432 N ATOM 1939 CA ALA A 302 45.777 31.816 17.024 1.00118.85 C ANISOU 1939 CA ALA A 302 14214 21655 9288 22 811 -2813 C ATOM 1940 C ALA A 302 46.681 31.328 18.149 1.00120.10 C ANISOU 1940 C ALA A 302 14324 21540 9767 -98 974 -2860 C ATOM 1941 O ALA A 302 46.224 31.130 19.281 1.00122.92 O ANISOU 1941 O ALA A 302 14657 21638 10410 -255 899 -2936 O ATOM 1942 CB ALA A 302 45.319 30.642 16.161 1.00110.40 C ANISOU 1942 CB ALA A 302 13140 20677 8131 114 673 -3282 C ATOM 1943 N ILE A 303 47.963 31.110 17.851 1.00115.96 N ANISOU 1943 N ILE A 303 13776 21084 9199 -16 1200 -2819 N ATOM 1944 CA ILE A 303 48.917 30.676 18.871 1.00109.22 C ANISOU 1944 CA ILE A 303 12847 20019 8631 -90 1366 -2837 C ATOM 1945 C ILE A 303 49.086 31.753 19.940 1.00108.34 C ANISOU 1945 C ILE A 303 12706 19785 8674 -275 1435 -2438 C ATOM 1946 O ILE A 303 49.046 31.481 21.151 1.00110.43 O ANISOU 1946 O ILE A 303 12935 19734 9291 -409 1409 -2466 O ATOM 1947 CB ILE A 303 50.260 30.314 18.207 1.00 99.18 C ANISOU 1947 CB ILE A 303 11528 18907 7248 66 1593 -2841 C ATOM 1948 CG1 ILE A 303 50.178 28.948 17.516 1.00101.31 C ANISOU 1948 CG1 ILE A 303 11841 19178 7473 230 1544 -3317 C ATOM 1949 CG2 ILE A 303 51.403 30.359 19.215 1.00 98.05 C ANISOU 1949 CG2 ILE A 303 11264 18639 7353 -6 1793 -2676 C ATOM 1950 CD1 ILE A 303 51.413 28.594 16.702 1.00109.20 C ANISOU 1950 CD1 ILE A 303 12807 20372 8313 423 1760 -3334 C ATOM 1951 N ASN A 304 49.254 33.002 19.504 1.00108.14 N ANISOU 1951 N ASN A 304 12721 19910 8459 -288 1507 -2027 N ATOM 1952 CA ASN A 304 49.590 34.074 20.434 1.00111.54 C ANISOU 1952 CA ASN A 304 13142 20198 9041 -477 1608 -1628 C ATOM 1953 C ASN A 304 48.423 34.423 21.352 1.00110.35 C ANISOU 1953 C ASN A 304 13053 19775 9100 -608 1408 -1580 C ATOM 1954 O ASN A 304 48.634 34.777 22.518 1.00113.34 O ANISOU 1954 O ASN A 304 13413 19827 9823 -776 1425 -1396 O ATOM 1955 CB ASN A 304 50.058 35.302 19.662 1.00108.03 C ANISOU 1955 CB ASN A 304 12767 19907 8374 -459 1746 -1209 C ATOM 1956 CG ASN A 304 51.425 35.783 20.115 1.00110.01 C ANISOU 1956 CG ASN A 304 12924 20101 8773 -595 1988 -939 C ATOM 1957 OD1 ASN A 304 52.225 35.001 20.636 1.00109.17 O ANISOU 1957 OD1 ASN A 304 12668 19956 8854 -612 2068 -1108 O ATOM 1958 ND2 ASN A 304 51.698 37.068 19.928 1.00114.42 N ANISOU 1958 ND2 ASN A 304 13569 20640 9264 -690 2103 -526 N ATOM 1959 N ASN A 305 47.190 34.372 20.836 1.00105.89 N ANISOU 1959 N ASN A 305 12553 19317 8362 -523 1203 -1724 N ATOM 1960 CA ASN A 305 46.021 34.563 21.692 1.00 99.98 C ANISOU 1960 CA ASN A 305 11835 18282 7873 -622 992 -1709 C ATOM 1961 C ASN A 305 46.013 33.550 22.831 1.00100.19 C ANISOU 1961 C ASN A 305 11792 17922 8353 -741 934 -1956 C ATOM 1962 O ASN A 305 45.734 33.893 23.989 1.00 99.01 O ANISOU 1962 O ASN A 305 11652 17439 8530 -883 888 -1798 O ATOM 1963 CB ASN A 305 44.738 34.450 20.864 1.00102.30 C ANISOU 1963 CB ASN A 305 12149 18829 7890 -496 771 -1901 C ATOM 1964 CG ASN A 305 44.655 35.497 19.763 1.00116.23 C ANISOU 1964 CG ASN A 305 14003 20919 9240 -335 808 -1600 C ATOM 1965 OD1 ASN A 305 45.216 36.590 19.884 1.00116.55 O ANISOU 1965 OD1 ASN A 305 14127 20917 9239 -369 975 -1180 O ATOM 1966 ND2 ASN A 305 43.949 35.171 18.688 1.00117.55 N ANISOU 1966 ND2 ASN A 305 14163 21324 9177 -166 646 -1790 N ATOM 1967 N GLU A 306 46.337 32.296 22.516 1.00 98.91 N ANISOU 1967 N GLU A 306 11581 17793 8205 -671 949 -2339 N ATOM 1968 CA GLU A 306 46.469 31.268 23.542 1.00 97.99 C ANISOU 1968 CA GLU A 306 11429 17299 8504 -751 934 -2553 C ATOM 1969 C GLU A 306 47.561 31.620 24.545 1.00 97.10 C ANISOU 1969 C GLU A 306 11269 16977 8645 -835 1096 -2272 C ATOM 1970 O GLU A 306 47.404 31.396 25.751 1.00 95.42 O ANISOU 1970 O GLU A 306 11049 16407 8798 -949 1048 -2245 O ATOM 1971 CB GLU A 306 46.769 29.920 22.892 1.00 98.74 C ANISOU 1971 CB GLU A 306 11518 17472 8529 -625 965 -2995 C ATOM 1972 CG GLU A 306 46.726 28.737 23.845 1.00 96.82 C ANISOU 1972 CG GLU A 306 11280 16810 8697 -682 943 -3250 C ATOM 1973 CD GLU A 306 45.358 28.092 23.889 1.00101.34 C ANISOU 1973 CD GLU A 306 11892 17236 9377 -775 733 -3568 C ATOM 1974 OE1 GLU A 306 44.402 28.703 23.366 1.00109.45 O ANISOU 1974 OE1 GLU A 306 12908 18486 10192 -804 581 -3541 O ATOM 1975 OE2 GLU A 306 45.241 26.975 24.437 1.00 96.88 O ANISOU 1975 OE2 GLU A 306 11364 16342 9104 -818 728 -3839 O ATOM 1976 N ARG A 307 48.705 32.112 24.059 1.00101.02 N ANISOU 1976 N ARG A 307 11719 17717 8946 -783 1293 -2077 N ATOM 1977 CA ARG A 307 49.769 32.499 24.985 1.00 96.70 C ANISOU 1977 CA ARG A 307 11091 17030 8622 -888 1436 -1820 C ATOM 1978 C ARG A 307 49.296 33.585 25.947 1.00 96.55 C ANISOU 1978 C ARG A 307 11127 16770 8787 -1081 1366 -1500 C ATOM 1979 O ARG A 307 49.579 33.531 27.152 1.00106.95 O ANISOU 1979 O ARG A 307 12404 17808 10425 -1195 1362 -1424 O ATOM 1980 CB ARG A 307 51.004 32.965 24.215 1.00103.02 C ANISOU 1980 CB ARG A 307 11808 18180 9155 -833 1667 -1650 C ATOM 1981 CG ARG A 307 51.739 31.862 23.474 1.00116.79 C ANISOU 1981 CG ARG A 307 13473 20141 10761 -625 1781 -1951 C ATOM 1982 CD ARG A 307 53.076 32.363 22.954 1.00128.43 C ANISOU 1982 CD ARG A 307 14816 21951 12030 -598 2037 -1741 C ATOM 1983 NE ARG A 307 53.941 32.817 24.036 1.00139.64 N ANISOU 1983 NE ARG A 307 16102 23233 13723 -763 2125 -1488 N ATOM 1984 CZ ARG A 307 54.812 32.045 24.672 1.00139.83 C ANISOU 1984 CZ ARG A 307 15971 23197 13962 -695 2192 -1592 C ATOM 1985 NH1 ARG A 307 54.964 30.769 24.357 1.00146.06 N ANISOU 1985 NH1 ARG A 307 16744 24002 14748 -455 2206 -1934 N ATOM 1986 NH2 ARG A 307 55.550 32.567 25.648 1.00137.74 N ANISOU 1986 NH2 ARG A 307 15568 22855 13911 -862 2247 -1352 N ATOM 1987 N LYS A 308 48.570 34.578 25.429 1.00 95.08 N ANISOU 1987 N LYS A 308 11044 16696 8388 -1098 1313 -1312 N ATOM 1988 CA LYS A 308 48.035 35.630 26.290 1.00 95.26 C ANISOU 1988 CA LYS A 308 11151 16474 8570 -1250 1253 -1025 C ATOM 1989 C LYS A 308 47.067 35.058 27.319 1.00 88.68 C ANISOU 1989 C LYS A 308 10328 15308 8059 -1302 1069 -1190 C ATOM 1990 O LYS A 308 47.096 35.443 28.497 1.00 84.10 O ANISOU 1990 O LYS A 308 9762 14443 7749 -1441 1060 -1035 O ATOM 1991 CB LYS A 308 47.338 36.702 25.454 1.00 96.29 C ANISOU 1991 CB LYS A 308 11411 16786 8390 -1193 1229 -810 C ATOM 1992 CG LYS A 308 48.172 37.288 24.334 1.00102.64 C ANISOU 1992 CG LYS A 308 12233 17932 8834 -1133 1424 -625 C ATOM 1993 CD LYS A 308 47.340 38.254 23.509 1.00102.03 C ANISOU 1993 CD LYS A 308 12310 18021 8435 -1028 1382 -413 C ATOM 1994 CE LYS A 308 48.040 38.635 22.218 1.00102.23 C ANISOU 1994 CE LYS A 308 12364 18435 8043 -924 1570 -272 C ATOM 1995 NZ LYS A 308 47.208 39.559 21.399 1.00101.40 N ANISOU 1995 NZ LYS A 308 12429 18486 7613 -777 1523 -42 N ATOM 1996 N ALA A 309 46.194 34.142 26.891 1.00 85.30 N ANISOU 1996 N ALA A 309 9892 14922 7597 -1205 927 -1512 N ATOM 1997 CA ALA A 309 45.248 33.535 27.824 1.00 81.99 C ANISOU 1997 CA ALA A 309 9470 14197 7485 -1276 774 -1677 C ATOM 1998 C ALA A 309 45.972 32.741 28.905 1.00 80.10 C ANISOU 1998 C ALA A 309 9183 13671 7581 -1338 840 -1748 C ATOM 1999 O ALA A 309 45.557 32.742 30.070 1.00 72.44 O ANISOU 1999 O ALA A 309 8230 12398 6897 -1444 782 -1688 O ATOM 2000 CB ALA A 309 44.263 32.643 27.071 1.00 80.13 C ANISOU 2000 CB ALA A 309 9216 14086 7142 -1197 626 -2042 C ATOM 2001 N SER A 310 47.046 32.043 28.530 1.00 89.28 N ANISOU 2001 N SER A 310 10285 14942 8696 -1248 967 -1873 N ATOM 2002 CA SER A 310 47.841 31.309 29.510 1.00 84.87 C ANISOU 2002 CA SER A 310 9673 14152 8422 -1255 1039 -1911 C ATOM 2003 C SER A 310 48.478 32.257 30.513 1.00 73.31 C ANISOU 2003 C SER A 310 8176 12588 7090 -1387 1098 -1572 C ATOM 2004 O SER A 310 48.520 31.966 31.714 1.00 73.52 O ANISOU 2004 O SER A 310 8196 12341 7398 -1447 1070 -1541 O ATOM 2005 CB SER A 310 48.914 30.482 28.803 1.00 89.80 C ANISOU 2005 CB SER A 310 10227 14967 8927 -1088 1178 -2091 C ATOM 2006 OG SER A 310 48.333 29.540 27.921 1.00 88.51 O ANISOU 2006 OG SER A 310 10116 14865 8649 -976 1123 -2450 O ATOM 2007 N LYS A 311 48.978 33.399 30.036 1.00 70.12 N ANISOU 2007 N LYS A 311 7762 12404 6478 -1442 1187 -1319 N ATOM 2008 CA LYS A 311 49.502 34.413 30.946 1.00 76.79 C ANISOU 2008 CA LYS A 311 8595 13145 7438 -1613 1238 -1016 C ATOM 2009 C LYS A 311 48.430 34.870 31.929 1.00 68.90 C ANISOU 2009 C LYS A 311 7707 11839 6632 -1724 1102 -928 C ATOM 2010 O LYS A 311 48.678 34.971 33.136 1.00 65.63 O ANISOU 2010 O LYS A 311 7279 11210 6447 -1827 1090 -838 O ATOM 2011 CB LYS A 311 50.042 35.602 30.152 1.00 81.60 C ANISOU 2011 CB LYS A 311 9217 14006 7782 -1679 1368 -764 C ATOM 2012 CG LYS A 311 50.341 36.830 31.001 1.00 82.04 C ANISOU 2012 CG LYS A 311 9315 13915 7942 -1900 1410 -460 C ATOM 2013 CD LYS A 311 50.707 38.027 30.138 1.00 84.72 C ANISOU 2013 CD LYS A 311 9718 14450 8020 -1978 1554 -203 C ATOM 2014 CE LYS A 311 51.909 37.722 29.261 1.00 91.09 C ANISOU 2014 CE LYS A 311 10366 15607 8638 -1926 1732 -227 C ATOM 2015 NZ LYS A 311 53.078 37.270 30.067 1.00 89.17 N ANISOU 2015 NZ LYS A 311 9912 15379 8589 -2001 1797 -264 N ATOM 2016 N VAL A 312 47.225 35.147 31.426 1.00 61.91 N ANISOU 2016 N VAL A 312 6922 10961 5640 -1687 996 -958 N ATOM 2017 CA VAL A 312 46.156 35.643 32.292 1.00 50.65 C ANISOU 2017 CA VAL A 312 5588 9282 4374 -1766 881 -868 C ATOM 2018 C VAL A 312 45.782 34.597 33.336 1.00 52.61 C ANISOU 2018 C VAL A 312 5804 9263 4924 -1781 803 -1049 C ATOM 2019 O VAL A 312 45.622 34.907 34.523 1.00 59.08 O ANISOU 2019 O VAL A 312 6658 9841 5947 -1880 780 -931 O ATOM 2020 CB VAL A 312 44.935 36.060 31.455 1.00 54.39 C ANISOU 2020 CB VAL A 312 6135 9882 4650 -1682 778 -879 C ATOM 2021 CG1 VAL A 312 43.789 36.491 32.360 1.00 49.85 C ANISOU 2021 CG1 VAL A 312 5626 9066 4247 -1733 666 -805 C ATOM 2022 CG2 VAL A 312 45.312 37.173 30.502 1.00 68.74 C ANISOU 2022 CG2 VAL A 312 8023 11932 6163 -1652 875 -642 C ATOM 2023 N LEU A 313 45.621 33.344 32.904 1.00 57.27 N ANISOU 2023 N LEU A 313 6344 9878 5537 -1685 774 -1342 N ATOM 2024 CA LEU A 313 45.251 32.286 33.838 1.00 54.54 C ANISOU 2024 CA LEU A 313 5996 9249 5480 -1700 727 -1507 C ATOM 2025 C LEU A 313 46.335 32.077 34.884 1.00 58.19 C ANISOU 2025 C LEU A 313 6421 9567 6122 -1719 812 -1398 C ATOM 2026 O LEU A 313 46.034 31.904 36.073 1.00 60.60 O ANISOU 2026 O LEU A 313 6757 9612 6655 -1780 778 -1347 O ATOM 2027 CB LEU A 313 44.972 30.985 33.088 1.00 54.33 C ANISOU 2027 CB LEU A 313 5952 9255 5437 -1605 705 -1855 C ATOM 2028 CG LEU A 313 43.668 30.940 32.291 1.00 57.74 C ANISOU 2028 CG LEU A 313 6394 9799 5746 -1612 576 -2033 C ATOM 2029 CD1 LEU A 313 43.444 29.555 31.707 1.00 62.08 C ANISOU 2029 CD1 LEU A 313 6939 10326 6321 -1562 558 -2420 C ATOM 2030 CD2 LEU A 313 42.493 31.356 33.162 1.00 54.71 C ANISOU 2030 CD2 LEU A 313 6028 9227 5532 -1724 473 -1938 C ATOM 2031 N GLY A 314 47.601 32.087 34.462 1.00 59.29 N ANISOU 2031 N GLY A 314 6478 9905 6145 -1658 924 -1357 N ATOM 2032 CA GLY A 314 48.686 31.980 35.417 1.00 59.77 C ANISOU 2032 CA GLY A 314 6461 9905 6342 -1667 991 -1243 C ATOM 2033 C GLY A 314 48.685 33.115 36.419 1.00 61.01 C ANISOU 2033 C GLY A 314 6647 9963 6571 -1839 964 -983 C ATOM 2034 O GLY A 314 48.887 32.896 37.612 1.00 64.36 O ANISOU 2034 O GLY A 314 7062 10210 7182 -1867 943 -928 O ATOM 2035 N ILE A 315 48.438 34.341 35.950 1.00 61.40 N ANISOU 2035 N ILE A 315 6752 10115 6461 -1945 969 -822 N ATOM 2036 CA ILE A 315 48.416 35.491 36.853 1.00 56.14 C ANISOU 2036 CA ILE A 315 6150 9325 5856 -2116 957 -594 C ATOM 2037 C ILE A 315 47.280 35.365 37.858 1.00 48.09 C ANISOU 2037 C ILE A 315 5233 8013 5025 -2137 850 -612 C ATOM 2038 O ILE A 315 47.450 35.667 39.044 1.00 47.09 O ANISOU 2038 O ILE A 315 5128 7729 5034 -2228 834 -510 O ATOM 2039 CB ILE A 315 48.321 36.803 36.053 1.00 50.72 C ANISOU 2039 CB ILE A 315 5548 8766 4959 -2200 1008 -414 C ATOM 2040 CG1 ILE A 315 49.631 37.069 35.310 1.00 48.34 C ANISOU 2040 CG1 ILE A 315 5131 8745 4492 -2234 1150 -342 C ATOM 2041 CG2 ILE A 315 47.994 37.972 36.973 1.00 46.85 C ANISOU 2041 CG2 ILE A 315 5187 8067 4546 -2362 988 -215 C ATOM 2042 CD1 ILE A 315 49.634 38.362 34.530 1.00 50.41 C ANISOU 2042 CD1 ILE A 315 5498 9111 4545 -2329 1236 -132 C ATOM 2043 N VAL A 316 46.103 34.931 37.405 1.00 50.47 N ANISOU 2043 N VAL A 316 5586 8264 5326 -2061 776 -749 N ATOM 2044 CA VAL A 316 44.975 34.780 38.323 1.00 50.26 C ANISOU 2044 CA VAL A 316 5629 7989 5479 -2088 692 -769 C ATOM 2045 C VAL A 316 45.279 33.713 39.370 1.00 53.48 C ANISOU 2045 C VAL A 316 6002 8209 6108 -2067 698 -849 C ATOM 2046 O VAL A 316 45.147 33.951 40.580 1.00 57.09 O ANISOU 2046 O VAL A 316 6505 8486 6699 -2130 682 -741 O ATOM 2047 CB VAL A 316 43.682 34.466 37.550 1.00 48.29 C ANISOU 2047 CB VAL A 316 5392 7779 5178 -2026 611 -922 C ATOM 2048 CG1 VAL A 316 42.549 34.170 38.523 1.00 54.72 C ANISOU 2048 CG1 VAL A 316 6237 8358 6197 -2064 545 -958 C ATOM 2049 CG2 VAL A 316 43.319 35.622 36.641 1.00 44.57 C ANISOU 2049 CG2 VAL A 316 4972 7492 4469 -2008 598 -794 C ATOM 2050 N PHE A 317 45.715 32.529 38.923 1.00 54.22 N ANISOU 2050 N PHE A 317 6032 8339 6228 -1958 731 -1032 N ATOM 2051 CA PHE A 317 46.077 31.477 39.864 1.00 54.86 C ANISOU 2051 CA PHE A 317 6106 8231 6508 -1897 757 -1084 C ATOM 2052 C PHE A 317 47.144 31.960 40.835 1.00 55.25 C ANISOU 2052 C PHE A 317 6109 8305 6579 -1927 785 -892 C ATOM 2053 O PHE A 317 47.105 31.643 42.029 1.00 57.14 O ANISOU 2053 O PHE A 317 6381 8360 6968 -1924 772 -831 O ATOM 2054 CB PHE A 317 46.584 30.239 39.116 1.00 57.02 C ANISOU 2054 CB PHE A 317 6336 8551 6777 -1745 814 -1299 C ATOM 2055 CG PHE A 317 45.666 29.731 38.031 1.00 53.73 C ANISOU 2055 CG PHE A 317 5952 8159 6305 -1731 779 -1537 C ATOM 2056 CD1 PHE A 317 44.308 29.991 38.052 1.00 57.55 C ANISOU 2056 CD1 PHE A 317 6482 8558 6826 -1835 692 -1574 C ATOM 2057 CD2 PHE A 317 46.181 28.975 36.984 1.00 58.55 C ANISOU 2057 CD2 PHE A 317 6531 8903 6811 -1604 833 -1741 C ATOM 2058 CE1 PHE A 317 43.482 29.517 37.046 1.00 66.33 C ANISOU 2058 CE1 PHE A 317 7591 9743 7869 -1833 641 -1815 C ATOM 2059 CE2 PHE A 317 45.360 28.500 35.980 1.00 59.74 C ANISOU 2059 CE2 PHE A 317 6710 9101 6888 -1602 788 -1993 C ATOM 2060 CZ PHE A 317 44.013 28.769 36.009 1.00 65.98 C ANISOU 2060 CZ PHE A 317 7528 9828 7713 -1726 684 -2033 C ATOM 2061 N PHE A 318 48.104 32.731 40.345 1.00 52.27 N ANISOU 2061 N PHE A 318 5648 8171 6042 -1967 828 -795 N ATOM 2062 CA PHE A 318 49.264 33.059 41.158 1.00 59.07 C ANISOU 2062 CA PHE A 318 6413 9117 6913 -2006 852 -658 C ATOM 2063 C PHE A 318 48.962 34.162 42.160 1.00 55.81 C ANISOU 2063 C PHE A 318 6082 8594 6531 -2183 802 -492 C ATOM 2064 O PHE A 318 49.426 34.110 43.304 1.00 66.59 O ANISOU 2064 O PHE A 318 7418 9909 7975 -2200 777 -422 O ATOM 2065 CB PHE A 318 50.442 33.392 40.243 1.00 79.28 C ANISOU 2065 CB PHE A 318 8825 11996 9301 -2006 935 -636 C ATOM 2066 CG PHE A 318 51.057 32.163 39.614 1.00 90.09 C ANISOU 2066 CG PHE A 318 10091 13480 10658 -1787 999 -798 C ATOM 2067 CD1 PHE A 318 50.844 30.918 40.174 1.00 71.17 C ANISOU 2067 CD1 PHE A 318 7735 10878 8427 -1620 984 -911 C ATOM 2068 CD2 PHE A 318 51.854 32.254 38.471 1.00101.00 C ANISOU 2068 CD2 PHE A 318 11353 15160 11862 -1739 1093 -832 C ATOM 2069 CE1 PHE A 318 51.400 29.788 39.636 1.00 71.10 C ANISOU 2069 CE1 PHE A 318 7670 10928 8418 -1398 1056 -1065 C ATOM 2070 CE2 PHE A 318 52.423 31.106 37.914 1.00 93.04 C ANISOU 2070 CE2 PHE A 318 10263 14251 10838 -1508 1163 -998 C ATOM 2071 CZ PHE A 318 52.194 29.874 38.499 1.00 86.01 C ANISOU 2071 CZ PHE A 318 9432 13123 10123 -1331 1143 -1120 C ATOM 2072 N VAL A 319 48.161 35.148 41.763 1.00 47.83 N ANISOU 2072 N VAL A 319 5184 7542 5447 -2291 786 -431 N ATOM 2073 CA VAL A 319 47.647 36.106 42.732 1.00 41.57 C ANISOU 2073 CA VAL A 319 4514 6583 4700 -2424 745 -304 C ATOM 2074 C VAL A 319 46.836 35.376 43.791 1.00 50.81 C ANISOU 2074 C VAL A 319 5746 7520 6040 -2358 692 -349 C ATOM 2075 O VAL A 319 46.961 35.660 44.987 1.00 50.80 O ANISOU 2075 O VAL A 319 5784 7420 6098 -2417 668 -267 O ATOM 2076 CB VAL A 319 46.826 37.208 42.034 1.00 40.18 C ANISOU 2076 CB VAL A 319 4467 6386 4414 -2491 749 -230 C ATOM 2077 CG1 VAL A 319 46.062 38.051 43.062 1.00 46.46 C ANISOU 2077 CG1 VAL A 319 5417 6961 5274 -2574 713 -130 C ATOM 2078 CG2 VAL A 319 47.741 38.103 41.219 1.00 40.61 C ANISOU 2078 CG2 VAL A 319 4492 6635 4302 -2595 829 -129 C ATOM 2079 N PHE A 320 46.032 34.388 43.378 1.00 52.11 N ANISOU 2079 N PHE A 320 5918 7603 6279 -2245 683 -487 N ATOM 2080 CA PHE A 320 45.226 33.652 44.350 1.00 51.25 C ANISOU 2080 CA PHE A 320 5870 7261 6342 -2205 661 -520 C ATOM 2081 C PHE A 320 46.095 32.951 45.392 1.00 52.45 C ANISOU 2081 C PHE A 320 5984 7365 6579 -2138 678 -479 C ATOM 2082 O PHE A 320 45.884 33.121 46.601 1.00 54.53 O ANISOU 2082 O PHE A 320 6313 7503 6905 -2167 660 -385 O ATOM 2083 CB PHE A 320 44.328 32.637 43.643 1.00 52.46 C ANISOU 2083 CB PHE A 320 6021 7342 6569 -2134 661 -701 C ATOM 2084 CG PHE A 320 43.330 31.977 44.552 1.00 50.55 C ANISOU 2084 CG PHE A 320 5844 6854 6510 -2138 662 -727 C ATOM 2085 CD1 PHE A 320 42.069 32.521 44.721 1.00 49.77 C ANISOU 2085 CD1 PHE A 320 5788 6688 6435 -2208 629 -706 C ATOM 2086 CD2 PHE A 320 43.653 30.819 45.242 1.00 50.13 C ANISOU 2086 CD2 PHE A 320 5806 6640 6599 -2058 710 -755 C ATOM 2087 CE1 PHE A 320 41.145 31.925 45.558 1.00 48.61 C ANISOU 2087 CE1 PHE A 320 5679 6337 6453 -2228 650 -723 C ATOM 2088 CE2 PHE A 320 42.732 30.218 46.081 1.00 52.31 C ANISOU 2088 CE2 PHE A 320 6154 6679 7042 -2079 738 -756 C ATOM 2089 CZ PHE A 320 41.476 30.772 46.238 1.00 51.53 C ANISOU 2089 CZ PHE A 320 6076 6535 6968 -2179 711 -744 C ATOM 2090 N LEU A 321 47.070 32.142 44.949 1.00 64.86 N ANISOU 2090 N LEU A 321 7453 9053 8137 -2019 715 -547 N ATOM 2091 CA LEU A 321 47.832 31.379 45.940 1.00 67.01 C ANISOU 2091 CA LEU A 321 7689 9286 8484 -1899 728 -497 C ATOM 2092 C LEU A 321 48.735 32.295 46.758 1.00 69.07 C ANISOU 2092 C LEU A 321 7882 9708 8655 -1986 687 -351 C ATOM 2093 O LEU A 321 48.893 32.081 47.964 1.00 73.41 O ANISOU 2093 O LEU A 321 8454 10189 9249 -1943 660 -268 O ATOM 2094 CB LEU A 321 48.613 30.212 45.309 1.00 75.71 C ANISOU 2094 CB LEU A 321 8707 10457 9602 -1701 789 -608 C ATOM 2095 CG LEU A 321 49.956 30.259 44.597 1.00 81.41 C ANISOU 2095 CG LEU A 321 9253 11485 10195 -1623 823 -623 C ATOM 2096 CD1 LEU A 321 50.495 28.847 44.249 1.00 90.60 C ANISOU 2096 CD1 LEU A 321 10386 12621 11418 -1360 898 -742 C ATOM 2097 CD2 LEU A 321 49.714 31.061 43.417 1.00 87.52 C ANISOU 2097 CD2 LEU A 321 10010 12401 10841 -1752 830 -671 C ATOM 2098 N ILE A 322 49.271 33.363 46.153 1.00 60.05 N ANISOU 2098 N ILE A 322 6667 8770 7379 -2128 684 -317 N ATOM 2099 CA ILE A 322 50.093 34.296 46.920 1.00 51.30 C ANISOU 2099 CA ILE A 322 5495 7802 6192 -2269 645 -207 C ATOM 2100 C ILE A 322 49.270 34.979 48.008 1.00 49.76 C ANISOU 2100 C ILE A 322 5466 7408 6032 -2381 595 -136 C ATOM 2101 O ILE A 322 49.738 35.148 49.141 1.00 47.91 O ANISOU 2101 O ILE A 322 5214 7209 5781 -2409 545 -76 O ATOM 2102 CB ILE A 322 50.759 35.318 45.980 1.00 40.99 C ANISOU 2102 CB ILE A 322 4104 6717 4752 -2436 683 -185 C ATOM 2103 CG1 ILE A 322 51.915 34.661 45.225 1.00 53.68 C ANISOU 2103 CG1 ILE A 322 5494 8599 6302 -2317 738 -235 C ATOM 2104 CG2 ILE A 322 51.241 36.532 46.757 1.00 40.86 C ANISOU 2104 CG2 ILE A 322 4092 6758 4676 -2668 647 -92 C ATOM 2105 CD1 ILE A 322 52.937 34.004 46.126 1.00 60.91 C ANISOU 2105 CD1 ILE A 322 6242 9663 7240 -2193 704 -214 C ATOM 2106 N MET A 323 48.035 35.381 47.690 1.00 45.45 N ANISOU 2106 N MET A 323 5073 6678 5517 -2429 606 -149 N ATOM 2107 CA MET A 323 47.222 36.101 48.662 1.00 40.87 C ANISOU 2107 CA MET A 323 4651 5920 4957 -2516 577 -85 C ATOM 2108 C MET A 323 46.575 35.195 49.701 1.00 44.79 C ANISOU 2108 C MET A 323 5211 6241 5568 -2392 571 -80 C ATOM 2109 O MET A 323 46.227 35.675 50.786 1.00 43.39 O ANISOU 2109 O MET A 323 5135 5969 5383 -2440 549 -18 O ATOM 2110 CB MET A 323 46.140 36.909 47.947 1.00 35.64 C ANISOU 2110 CB MET A 323 4113 5155 4273 -2578 597 -84 C ATOM 2111 CG MET A 323 46.686 38.008 47.063 1.00 36.38 C ANISOU 2111 CG MET A 323 4206 5376 4240 -2712 624 -41 C ATOM 2112 SD MET A 323 45.391 39.079 46.425 1.00 35.98 S ANISOU 2112 SD MET A 323 4340 5188 4143 -2728 644 8 S ATOM 2113 CE MET A 323 45.041 40.094 47.858 1.00 35.61 C ANISOU 2113 CE MET A 323 4484 4929 4116 -2719 605 75 C ATOM 2114 N TRP A 324 46.392 33.908 49.405 1.00 46.65 N ANISOU 2114 N TRP A 324 5406 6415 5904 -2240 604 -144 N ATOM 2115 CA TRP A 324 45.762 33.023 50.376 1.00 42.88 C ANISOU 2115 CA TRP A 324 5009 5741 5544 -2139 628 -118 C ATOM 2116 C TRP A 324 46.746 32.191 51.186 1.00 48.24 C ANISOU 2116 C TRP A 324 5633 6473 6225 -1992 625 -58 C ATOM 2117 O TRP A 324 46.364 31.678 52.244 1.00 52.97 O ANISOU 2117 O TRP A 324 6320 6926 6879 -1915 646 16 O ATOM 2118 CB TRP A 324 44.767 32.083 49.685 1.00 41.46 C ANISOU 2118 CB TRP A 324 4858 5397 5499 -2083 683 -226 C ATOM 2119 CG TRP A 324 43.371 32.616 49.667 1.00 37.70 C ANISOU 2119 CG TRP A 324 4461 4802 5062 -2178 688 -238 C ATOM 2120 CD1 TRP A 324 42.654 32.998 48.573 1.00 38.98 C ANISOU 2120 CD1 TRP A 324 4601 5007 5203 -2232 674 -326 C ATOM 2121 CD2 TRP A 324 42.527 32.841 50.800 1.00 39.80 C ANISOU 2121 CD2 TRP A 324 4825 4924 5373 -2204 709 -154 C ATOM 2122 NE1 TRP A 324 41.410 33.440 48.954 1.00 38.08 N ANISOU 2122 NE1 TRP A 324 4547 4792 5128 -2281 679 -302 N ATOM 2123 CE2 TRP A 324 41.308 33.354 50.317 1.00 38.87 C ANISOU 2123 CE2 TRP A 324 4723 4771 5275 -2269 710 -200 C ATOM 2124 CE3 TRP A 324 42.682 32.655 52.177 1.00 44.99 C ANISOU 2124 CE3 TRP A 324 5553 5504 6037 -2160 729 -41 C ATOM 2125 CZ2 TRP A 324 40.250 33.684 51.162 1.00 45.36 C ANISOU 2125 CZ2 TRP A 324 5616 5482 6138 -2292 744 -141 C ATOM 2126 CZ3 TRP A 324 41.631 32.984 53.014 1.00 44.17 C ANISOU 2126 CZ3 TRP A 324 5541 5280 5962 -2194 767 17 C ATOM 2127 CH2 TRP A 324 40.432 33.493 52.504 1.00 45.28 C ANISOU 2127 CH2 TRP A 324 5683 5385 6136 -2260 780 -35 C ATOM 2128 N CYS A 325 47.990 32.042 50.727 1.00 46.10 N ANISOU 2128 N CYS A 325 5211 6424 5882 -1932 607 -75 N ATOM 2129 CA CYS A 325 48.965 31.266 51.487 1.00 41.04 C ANISOU 2129 CA CYS A 325 4494 5877 5224 -1748 595 -6 C ATOM 2130 C CYS A 325 49.240 31.801 52.888 1.00 42.23 C ANISOU 2130 C CYS A 325 4666 6099 5281 -1781 523 110 C ATOM 2131 O CYS A 325 49.340 30.976 53.811 1.00 43.88 O ANISOU 2131 O CYS A 325 4918 6247 5510 -1598 532 197 O ATOM 2132 CB CYS A 325 50.270 31.152 50.691 1.00 41.18 C ANISOU 2132 CB CYS A 325 4303 6179 5162 -1680 589 -50 C ATOM 2133 SG CYS A 325 50.293 29.762 49.545 1.00 57.72 S ANISOU 2133 SG CYS A 325 6387 8180 7365 -1459 691 -174 S ATOM 2134 N PRO A 326 49.411 33.112 53.123 1.00 39.47 N ANISOU 2134 N PRO A 326 4303 5875 4819 -1996 456 116 N ATOM 2135 CA PRO A 326 49.717 33.557 54.497 1.00 40.07 C ANISOU 2135 CA PRO A 326 4403 6037 4786 -2025 378 192 C ATOM 2136 C PRO A 326 48.722 33.058 55.533 1.00 39.64 C ANISOU 2136 C PRO A 326 4536 5742 4783 -1920 415 270 C ATOM 2137 O PRO A 326 49.123 32.502 56.566 1.00 40.91 O ANISOU 2137 O PRO A 326 4695 5966 4882 -1762 387 363 O ATOM 2138 CB PRO A 326 49.702 35.086 54.370 1.00 39.53 C ANISOU 2138 CB PRO A 326 4364 6025 4629 -2312 336 147 C ATOM 2139 CG PRO A 326 50.069 35.343 52.966 1.00 39.47 C ANISOU 2139 CG PRO A 326 4248 6109 4639 -2397 374 83 C ATOM 2140 CD PRO A 326 49.428 34.243 52.177 1.00 38.83 C ANISOU 2140 CD PRO A 326 4195 5869 4689 -2217 453 53 C ATOM 2141 N PHE A 327 47.426 33.211 55.258 1.00 39.25 N ANISOU 2141 N PHE A 327 4636 5439 4837 -1991 487 244 N ATOM 2142 CA PHE A 327 46.404 32.779 56.204 1.00 40.19 C ANISOU 2142 CA PHE A 327 4918 5341 5013 -1919 549 320 C ATOM 2143 C PHE A 327 46.491 31.281 56.467 1.00 44.35 C ANISOU 2143 C PHE A 327 5458 5759 5635 -1689 620 392 C ATOM 2144 O PHE A 327 46.431 30.836 57.619 1.00 50.42 O ANISOU 2144 O PHE A 327 6312 6483 6363 -1566 641 516 O ATOM 2145 CB PHE A 327 45.020 33.152 55.673 1.00 43.34 C ANISOU 2145 CB PHE A 327 5416 5533 5517 -2031 617 264 C ATOM 2146 CG PHE A 327 43.890 32.499 56.414 1.00 42.33 C ANISOU 2146 CG PHE A 327 5414 5183 5488 -1963 716 330 C ATOM 2147 CD1 PHE A 327 43.395 33.060 57.578 1.00 45.88 C ANISOU 2147 CD1 PHE A 327 5978 5602 5852 -1985 726 404 C ATOM 2148 CD2 PHE A 327 43.318 31.328 55.944 1.00 40.09 C ANISOU 2148 CD2 PHE A 327 5135 4719 5379 -1893 811 308 C ATOM 2149 CE1 PHE A 327 42.356 32.463 58.264 1.00 52.48 C ANISOU 2149 CE1 PHE A 327 6916 6253 6772 -1929 841 479 C ATOM 2150 CE2 PHE A 327 42.280 30.728 56.625 1.00 42.95 C ANISOU 2150 CE2 PHE A 327 5601 4875 5843 -1869 924 375 C ATOM 2151 CZ PHE A 327 41.797 31.296 57.786 1.00 48.94 C ANISOU 2151 CZ PHE A 327 6457 5626 6511 -1883 944 472 C ATOM 2152 N PHE A 328 46.639 30.485 55.406 1.00 43.33 N ANISOU 2152 N PHE A 328 5265 5575 5623 -1618 668 319 N ATOM 2153 CA PHE A 328 46.617 29.035 55.573 1.00 47.69 C ANISOU 2153 CA PHE A 328 5878 5947 6295 -1404 765 373 C ATOM 2154 C PHE A 328 47.861 28.533 56.292 1.00 46.12 C ANISOU 2154 C PHE A 328 5612 5928 5984 -1173 719 492 C ATOM 2155 O PHE A 328 47.765 27.673 57.177 1.00 49.06 O ANISOU 2155 O PHE A 328 6099 6164 6378 -985 785 632 O ATOM 2156 CB PHE A 328 46.461 28.354 54.218 1.00 46.87 C ANISOU 2156 CB PHE A 328 5741 5734 6335 -1394 827 227 C ATOM 2157 CG PHE A 328 45.035 28.171 53.809 1.00 47.57 C ANISOU 2157 CG PHE A 328 5930 5566 6580 -1531 909 143 C ATOM 2158 CD1 PHE A 328 44.350 27.018 54.152 1.00 46.34 C ANISOU 2158 CD1 PHE A 328 5906 5112 6590 -1463 1037 172 C ATOM 2159 CD2 PHE A 328 44.370 29.160 53.106 1.00 45.46 C ANISOU 2159 CD2 PHE A 328 5620 5361 6289 -1729 863 42 C ATOM 2160 CE1 PHE A 328 43.033 26.847 53.790 1.00 44.02 C ANISOU 2160 CE1 PHE A 328 5665 4619 6443 -1621 1109 78 C ATOM 2161 CE2 PHE A 328 43.053 28.996 52.740 1.00 44.66 C ANISOU 2161 CE2 PHE A 328 5571 5082 6317 -1841 923 -40 C ATOM 2162 CZ PHE A 328 42.383 27.835 53.080 1.00 46.16 C ANISOU 2162 CZ PHE A 328 5856 5006 6678 -1803 1041 -33 C ATOM 2163 N ILE A 329 49.034 29.052 55.927 1.00 43.20 N ANISOU 2163 N ILE A 329 5048 5880 5486 -1175 615 450 N ATOM 2164 CA ILE A 329 50.258 28.663 56.619 1.00 45.38 C ANISOU 2164 CA ILE A 329 5206 6406 5630 -949 548 556 C ATOM 2165 C ILE A 329 50.163 29.036 58.090 1.00 45.86 C ANISOU 2165 C ILE A 329 5345 6535 5547 -937 484 689 C ATOM 2166 O ILE A 329 50.477 28.229 58.972 1.00 47.80 O ANISOU 2166 O ILE A 329 5639 6787 5737 -676 498 841 O ATOM 2167 CB ILE A 329 51.487 29.307 55.955 1.00 45.91 C ANISOU 2167 CB ILE A 329 5007 6854 5581 -1013 447 471 C ATOM 2168 CG1 ILE A 329 51.582 28.898 54.486 1.00 45.69 C ANISOU 2168 CG1 ILE A 329 4913 6778 5670 -997 525 343 C ATOM 2169 CG2 ILE A 329 52.754 28.897 56.682 1.00 48.54 C ANISOU 2169 CG2 ILE A 329 5171 7505 5768 -765 364 575 C ATOM 2170 CD1 ILE A 329 52.681 29.611 53.731 1.00 46.22 C ANISOU 2170 CD1 ILE A 329 4720 7214 5626 -1098 459 263 C ATOM 2171 N THR A 330 49.698 30.256 58.379 1.00 47.01 N ANISOU 2171 N THR A 330 5527 6719 5616 -1200 424 636 N ATOM 2172 CA THR A 330 49.605 30.694 59.766 1.00 46.04 C ANISOU 2172 CA THR A 330 5487 6679 5328 -1201 362 729 C ATOM 2173 C THR A 330 48.618 29.842 60.555 1.00 45.32 C ANISOU 2173 C THR A 330 5620 6292 5307 -1049 491 872 C ATOM 2174 O THR A 330 48.885 29.488 61.706 1.00 48.97 O ANISOU 2174 O THR A 330 6137 6841 5629 -867 470 1019 O ATOM 2175 CB THR A 330 49.220 32.172 59.824 1.00 43.54 C ANISOU 2175 CB THR A 330 5204 6405 4936 -1512 299 618 C ATOM 2176 OG1 THR A 330 50.102 32.925 58.982 1.00 43.51 O ANISOU 2176 OG1 THR A 330 5008 6632 4892 -1681 214 497 O ATOM 2177 CG2 THR A 330 49.329 32.698 61.249 1.00 44.68 C ANISOU 2177 CG2 THR A 330 5417 6693 4868 -1516 214 673 C ATOM 2178 N ASN A 331 47.481 29.483 59.955 1.00 43.96 N ANISOU 2178 N ASN A 331 5572 5788 5344 -1122 631 836 N ATOM 2179 CA ASN A 331 46.491 28.690 60.680 1.00 45.21 C ANISOU 2179 CA ASN A 331 5930 5658 5588 -1026 779 970 C ATOM 2180 C ASN A 331 46.988 27.268 60.935 1.00 54.51 C ANISOU 2180 C ASN A 331 7159 6736 6815 -721 861 1120 C ATOM 2181 O ASN A 331 46.922 26.766 62.070 1.00 60.96 O ANISOU 2181 O ASN A 331 8105 7512 7545 -544 914 1312 O ATOM 2182 CB ASN A 331 45.172 28.671 59.907 1.00 47.71 C ANISOU 2182 CB ASN A 331 6320 5685 6122 -1209 900 869 C ATOM 2183 CG ASN A 331 43.977 28.393 60.800 1.00 60.41 C ANISOU 2183 CG ASN A 331 8105 7066 7780 -1222 1041 984 C ATOM 2184 OD1 ASN A 331 44.123 27.898 61.918 1.00 62.77 O ANISOU 2184 OD1 ASN A 331 8510 7356 7984 -1053 1089 1165 O ATOM 2185 ND2 ASN A 331 42.784 28.710 60.308 1.00 60.06 N ANISOU 2185 ND2 ASN A 331 8081 6864 7873 -1413 1114 888 N ATOM 2186 N ILE A 332 47.495 26.597 59.894 1.00 58.52 N ANISOU 2186 N ILE A 332 7585 7199 7450 -633 884 1041 N ATOM 2187 CA ILE A 332 47.956 25.228 60.090 1.00 54.11 C ANISOU 2187 CA ILE A 332 7107 6500 6952 -315 982 1179 C ATOM 2188 C ILE A 332 49.211 25.187 60.951 1.00 56.46 C ANISOU 2188 C ILE A 332 7303 7139 7009 -43 860 1329 C ATOM 2189 O ILE A 332 49.502 24.152 61.558 1.00 62.13 O ANISOU 2189 O ILE A 332 8134 7758 7713 271 940 1521 O ATOM 2190 CB ILE A 332 48.181 24.496 58.752 1.00 51.80 C ANISOU 2190 CB ILE A 332 6769 6064 6847 -267 1048 1034 C ATOM 2191 CG1 ILE A 332 49.347 25.106 57.975 1.00 60.36 C ANISOU 2191 CG1 ILE A 332 7590 7527 7817 -266 898 907 C ATOM 2192 CG2 ILE A 332 46.905 24.495 57.923 1.00 49.32 C ANISOU 2192 CG2 ILE A 332 6541 5449 6750 -536 1150 872 C ATOM 2193 CD1 ILE A 332 49.639 24.396 56.670 1.00 64.69 C ANISOU 2193 CD1 ILE A 332 8092 7974 8512 -188 968 759 C ATOM 2194 N LEU A 333 49.949 26.297 61.054 1.00 54.64 N ANISOU 2194 N LEU A 333 6865 7314 6581 -158 671 1251 N ATOM 2195 CA LEU A 333 51.072 26.356 61.980 1.00 61.06 C ANISOU 2195 CA LEU A 333 7551 8511 7137 64 529 1374 C ATOM 2196 C LEU A 333 50.618 26.668 63.400 1.00 63.35 C ANISOU 2196 C LEU A 333 7988 8836 7245 74 507 1518 C ATOM 2197 O LEU A 333 51.253 26.222 64.362 1.00 70.31 O ANISOU 2197 O LEU A 333 8867 9915 7933 363 454 1697 O ATOM 2198 CB LEU A 333 52.085 27.396 61.500 1.00 56.09 C ANISOU 2198 CB LEU A 333 6621 8315 6377 -102 341 1210 C ATOM 2199 CG LEU A 333 53.458 27.394 62.170 1.00 60.01 C ANISOU 2199 CG LEU A 333 6886 9293 6622 120 173 1287 C ATOM 2200 CD1 LEU A 333 54.078 26.007 62.116 1.00 67.22 C ANISOU 2200 CD1 LEU A 333 7789 10179 7572 570 248 1445 C ATOM 2201 CD2 LEU A 333 54.368 28.417 61.506 1.00 55.93 C ANISOU 2201 CD2 LEU A 333 6058 9165 6027 -120 24 1098 C ATOM 2202 N SER A 334 49.531 27.429 63.548 1.00 59.94 N ANISOU 2202 N SER A 334 7682 8238 6853 -213 549 1444 N ATOM 2203 CA SER A 334 48.946 27.656 64.863 1.00 61.63 C ANISOU 2203 CA SER A 334 8068 8444 6906 -195 569 1576 C ATOM 2204 C SER A 334 48.376 26.370 65.440 1.00 64.62 C ANISOU 2204 C SER A 334 8678 8509 7366 61 769 1817 C ATOM 2205 O SER A 334 48.292 26.223 66.664 1.00 73.27 O ANISOU 2205 O SER A 334 9898 9675 8265 219 785 2003 O ATOM 2206 CB SER A 334 47.857 28.727 64.778 1.00 55.72 C ANISOU 2206 CB SER A 334 7400 7567 6205 -534 597 1434 C ATOM 2207 OG SER A 334 47.162 28.849 66.005 1.00 52.68 O ANISOU 2207 OG SER A 334 7198 7137 5679 -500 659 1560 O ATOM 2208 N VAL A 335 47.964 25.437 64.582 1.00 65.79 N ANISOU 2208 N VAL A 335 8901 8301 7794 93 934 1815 N ATOM 2209 CA VAL A 335 47.550 24.132 65.095 1.00 72.91 C ANISOU 2209 CA VAL A 335 10039 8873 8791 336 1142 2051 C ATOM 2210 C VAL A 335 48.672 23.093 65.084 1.00 83.91 C ANISOU 2210 C VAL A 335 11411 10325 10147 735 1136 2196 C ATOM 2211 O VAL A 335 48.563 22.077 65.786 1.00 84.96 O ANISOU 2211 O VAL A 335 11758 10247 10277 1010 1288 2450 O ATOM 2212 CB VAL A 335 46.331 23.581 64.335 1.00 65.56 C ANISOU 2212 CB VAL A 335 9251 7466 8194 139 1359 1977 C ATOM 2213 CG1 VAL A 335 45.061 24.263 64.818 1.00 63.76 C ANISOU 2213 CG1 VAL A 335 9110 7143 7974 -131 1433 1960 C ATOM 2214 CG2 VAL A 335 46.505 23.783 62.862 1.00 65.52 C ANISOU 2214 CG2 VAL A 335 9082 7449 8364 -27 1300 1713 C ATOM 2215 N LEU A 336 49.749 23.314 64.318 1.00 94.25 N ANISOU 2215 N LEU A 336 12472 11915 11422 791 981 2055 N ATOM 2216 CA LEU A 336 50.899 22.415 64.393 1.00 97.42 C ANISOU 2216 CA LEU A 336 12816 12451 11748 1217 960 2198 C ATOM 2217 C LEU A 336 51.525 22.440 65.779 1.00 99.48 C ANISOU 2217 C LEU A 336 13070 13052 11678 1504 849 2434 C ATOM 2218 O LEU A 336 52.070 21.429 66.235 1.00107.06 O ANISOU 2218 O LEU A 336 14117 13989 12572 1930 909 2670 O ATOM 2219 CB LEU A 336 51.938 22.783 63.328 1.00115.39 C ANISOU 2219 CB LEU A 336 14780 15038 14025 1199 812 1989 C ATOM 2220 CG LEU A 336 53.205 21.919 63.201 1.00113.24 C ANISOU 2220 CG LEU A 336 14382 14958 13685 1649 784 2095 C ATOM 2221 CD1 LEU A 336 53.617 21.782 61.742 1.00112.96 C ANISOU 2221 CD1 LEU A 336 14190 14900 13830 1599 806 1873 C ATOM 2222 CD2 LEU A 336 54.366 22.482 64.017 1.00 99.62 C ANISOU 2222 CD2 LEU A 336 12386 13847 11618 1816 544 2169 C ATOM 2223 N CYS A 337 51.461 23.581 66.457 1.00 90.23 N ANISOU 2223 N CYS A 337 11804 12198 10281 1292 688 2372 N ATOM 2224 CA CYS A 337 51.899 23.724 67.842 1.00 98.09 C ANISOU 2224 CA CYS A 337 12807 13536 10927 1512 572 2564 C ATOM 2225 C CYS A 337 50.706 24.241 68.638 1.00105.83 C ANISOU 2225 C CYS A 337 14009 14344 11857 1283 658 2597 C ATOM 2226 O CYS A 337 50.542 25.450 68.814 1.00107.65 O ANISOU 2226 O CYS A 337 14145 14791 11966 982 523 2414 O ATOM 2227 CB CYS A 337 53.105 24.662 67.955 1.00 99.98 C ANISOU 2227 CB CYS A 337 12693 14398 10898 1474 272 2416 C ATOM 2228 SG CYS A 337 52.953 26.224 67.046 1.00 90.63 S ANISOU 2228 SG CYS A 337 11302 13334 9801 902 142 2032 S ATOM 2229 N GLU A 338 49.866 23.318 69.116 1.00118.91 N ANISOU 2229 N GLU A 338 15971 15599 13612 1426 903 2833 N ATOM 2230 CA GLU A 338 48.747 23.720 69.962 1.00120.73 C ANISOU 2230 CA GLU A 338 16403 15697 13773 1253 1012 2898 C ATOM 2231 C GLU A 338 49.238 24.397 71.233 1.00126.40 C ANISOU 2231 C GLU A 338 17076 16889 14062 1364 826 2969 C ATOM 2232 O GLU A 338 48.548 25.263 71.786 1.00123.18 O ANISOU 2232 O GLU A 338 16731 16534 13537 1135 818 2887 O ATOM 2233 CB GLU A 338 47.875 22.507 70.294 1.00130.84 C ANISOU 2233 CB GLU A 338 18004 16485 15223 1403 1327 3171 C ATOM 2234 CG GLU A 338 46.562 22.847 70.988 1.00142.10 C ANISOU 2234 CG GLU A 338 19623 17725 16641 1185 1495 3227 C ATOM 2235 CD GLU A 338 45.591 23.595 70.090 1.00129.77 C ANISOU 2235 CD GLU A 338 17987 15979 15339 738 1531 2938 C ATOM 2236 OE1 GLU A 338 45.774 23.576 68.854 1.00109.00 O ANISOU 2236 OE1 GLU A 338 15220 13246 12949 604 1488 2733 O ATOM 2237 OE2 GLU A 338 44.639 24.203 70.623 1.00125.10 O ANISOU 2237 OE2 GLU A 338 17475 15364 14695 544 1607 2921 O ATOM 2238 N LYS A 339 50.422 24.022 71.703 1.00135.18 N ANISOU 2238 N LYS A 339 18072 18366 14924 1726 673 3106 N ATOM 2239 CA LYS A 339 51.136 24.697 72.776 1.00135.21 C ANISOU 2239 CA LYS A 339 17955 18927 14492 1832 431 3117 C ATOM 2240 C LYS A 339 52.495 25.153 72.250 1.00128.59 C ANISOU 2240 C LYS A 339 16738 18564 13557 1843 148 2923 C ATOM 2241 O LYS A 339 52.806 25.006 71.066 1.00124.41 O ANISOU 2241 O LYS A 339 16058 17919 13293 1759 157 2787 O ATOM 2242 CB LYS A 339 51.291 23.779 73.992 1.00138.58 C ANISOU 2242 CB LYS A 339 18581 19425 14647 2300 505 3501 C ATOM 2243 CG LYS A 339 52.055 22.496 73.704 1.00144.48 C ANISOU 2243 CG LYS A 339 19329 20096 15470 2754 566 3739 C ATOM 2244 CD LYS A 339 52.136 21.612 74.937 1.00147.67 C ANISOU 2244 CD LYS A 339 19972 20542 15592 3235 662 4155 C ATOM 2245 CE LYS A 339 52.907 20.333 74.651 1.00148.19 C ANISOU 2245 CE LYS A 339 20067 20503 15734 3731 736 4406 C ATOM 2246 NZ LYS A 339 52.272 19.533 73.567 1.00144.22 N ANISOU 2246 NZ LYS A 339 19746 19333 15720 3626 1020 4390 N ATOM 2247 N SER A 340 53.302 25.726 73.143 1.00136.47 N ANISOU 2247 N SER A 340 17568 20126 14158 1932 -105 2901 N ATOM 2248 CA SER A 340 54.682 26.146 72.904 1.00135.46 C ANISOU 2248 CA SER A 340 17045 20559 13866 1965 -393 2744 C ATOM 2249 C SER A 340 54.808 27.316 71.936 1.00140.36 C ANISOU 2249 C SER A 340 17439 21243 14647 1465 -505 2365 C ATOM 2250 O SER A 340 55.932 27.761 71.674 1.00151.66 O ANISOU 2250 O SER A 340 18520 23140 15964 1417 -729 2210 O ATOM 2251 CB SER A 340 55.564 24.996 72.389 1.00138.48 C ANISOU 2251 CB SER A 340 17294 20985 14336 2395 -369 2922 C ATOM 2252 OG SER A 340 55.186 24.597 71.083 1.00152.36 O ANISOU 2252 OG SER A 340 19095 22277 16517 2268 -182 2842 O ATOM 2253 N CYS A 341 53.708 27.837 71.404 1.00116.80 N ANISOU 2253 N CYS A 341 14635 17829 11916 1097 -353 2223 N ATOM 2254 CA CYS A 341 53.736 28.914 70.427 1.00103.63 C ANISOU 2254 CA CYS A 341 12802 16157 10415 646 -424 1901 C ATOM 2255 C CYS A 341 53.043 30.150 70.991 1.00 88.08 C ANISOU 2255 C CYS A 341 10963 14182 8323 292 -466 1721 C ATOM 2256 O CYS A 341 52.395 30.106 72.040 1.00 83.38 O ANISOU 2256 O CYS A 341 10598 13530 7551 388 -406 1841 O ATOM 2257 CB CYS A 341 53.082 28.470 69.111 1.00105.66 C ANISOU 2257 CB CYS A 341 13139 15918 11089 542 -212 1872 C ATOM 2258 SG CYS A 341 54.179 27.506 68.035 1.00119.66 S ANISOU 2258 SG CYS A 341 14660 17784 13022 812 -217 1914 S ATOM 2259 N ASN A 342 53.197 31.268 70.282 1.00 79.41 N ANISOU 2259 N ASN A 342 9726 13135 7312 -109 -556 1435 N ATOM 2260 CA ASN A 342 52.655 32.560 70.707 1.00 69.07 C ANISOU 2260 CA ASN A 342 8535 11811 5896 -459 -602 1225 C ATOM 2261 C ASN A 342 51.334 32.775 69.974 1.00 59.64 C ANISOU 2261 C ASN A 342 7565 10081 5014 -659 -377 1186 C ATOM 2262 O ASN A 342 51.291 33.355 68.890 1.00 57.38 O ANISOU 2262 O ASN A 342 7199 9662 4940 -929 -364 1017 O ATOM 2263 CB ASN A 342 53.650 33.681 70.425 1.00 71.52 C ANISOU 2263 CB ASN A 342 8580 12491 6105 -780 -825 945 C ATOM 2264 CG ASN A 342 53.285 34.978 71.122 1.00 66.18 C ANISOU 2264 CG ASN A 342 8044 11855 5246 -1093 -900 726 C ATOM 2265 OD1 ASN A 342 52.110 35.276 71.336 1.00 62.53 O ANISOU 2265 OD1 ASN A 342 7874 11036 4848 -1163 -745 729 O ATOM 2266 ND2 ASN A 342 54.298 35.759 71.481 1.00 72.94 N ANISOU 2266 ND2 ASN A 342 8688 13153 5871 -1285 -1135 522 N ATOM 2267 N GLN A 343 50.244 32.316 70.593 1.00 59.33 N ANISOU 2267 N GLN A 343 7798 9761 4984 -521 -197 1352 N ATOM 2268 CA GLN A 343 48.948 32.309 69.921 1.00 57.93 C ANISOU 2268 CA GLN A 343 7797 9105 5107 -659 26 1346 C ATOM 2269 C GLN A 343 48.396 33.714 69.703 1.00 56.05 C ANISOU 2269 C GLN A 343 7625 8783 4888 -1015 7 1100 C ATOM 2270 O GLN A 343 47.647 33.937 68.743 1.00 59.82 O ANISOU 2270 O GLN A 343 8142 8954 5633 -1180 127 1029 O ATOM 2271 CB GLN A 343 47.952 31.465 70.717 1.00 63.75 C ANISOU 2271 CB GLN A 343 8783 9602 5836 -436 234 1592 C ATOM 2272 CG GLN A 343 48.236 29.970 70.684 1.00 62.84 C ANISOU 2272 CG GLN A 343 8674 9398 5805 -97 332 1858 C ATOM 2273 CD GLN A 343 48.007 29.359 69.312 1.00 59.44 C ANISOU 2273 CD GLN A 343 8189 8644 5753 -152 452 1832 C ATOM 2274 OE1 GLN A 343 48.652 28.379 68.942 1.00 58.38 O ANISOU 2274 OE1 GLN A 343 7981 8503 5698 77 463 1947 O ATOM 2275 NE2 GLN A 343 47.077 29.931 68.555 1.00 60.76 N ANISOU 2275 NE2 GLN A 343 8395 8548 6141 -436 542 1675 N ATOM 2276 N LYS A 344 48.731 34.665 70.579 1.00 56.02 N ANISOU 2276 N LYS A 344 7646 9041 4597 -1125 -137 964 N ATOM 2277 CA LYS A 344 48.246 36.031 70.400 1.00 54.71 C ANISOU 2277 CA LYS A 344 7581 8761 4448 -1447 -142 725 C ATOM 2278 C LYS A 344 48.733 36.607 69.078 1.00 53.03 C ANISOU 2278 C LYS A 344 7200 8507 4443 -1708 -200 558 C ATOM 2279 O LYS A 344 47.954 37.194 68.313 1.00 64.71 O ANISOU 2279 O LYS A 344 8775 9690 6123 -1886 -91 472 O ATOM 2280 CB LYS A 344 48.697 36.904 71.570 1.00 57.37 C ANISOU 2280 CB LYS A 344 7970 9404 4423 -1527 -304 576 C ATOM 2281 CG LYS A 344 47.875 36.721 72.833 1.00 58.69 C ANISOU 2281 CG LYS A 344 8381 9543 4377 -1336 -202 691 C ATOM 2282 CD LYS A 344 48.640 37.188 74.057 1.00 63.15 C ANISOU 2282 CD LYS A 344 8941 10532 4523 -1318 -405 584 C ATOM 2283 CE LYS A 344 49.842 36.294 74.310 1.00 79.00 C ANISOU 2283 CE LYS A 344 10708 12937 6373 -1087 -574 724 C ATOM 2284 NZ LYS A 344 50.636 36.720 75.495 1.00 92.16 N ANISOU 2284 NZ LYS A 344 12329 15087 7603 -1062 -803 610 N ATOM 2285 N LEU A 345 50.021 36.425 68.781 1.00 54.39 N ANISOU 2285 N LEU A 345 7110 8995 4561 -1712 -363 525 N ATOM 2286 CA LEU A 345 50.556 36.875 67.503 1.00 53.13 C ANISOU 2286 CA LEU A 345 6772 8827 4589 -1945 -397 394 C ATOM 2287 C LEU A 345 49.888 36.153 66.342 1.00 54.97 C ANISOU 2287 C LEU A 345 7021 8728 5138 -1863 -223 500 C ATOM 2288 O LEU A 345 49.598 36.765 65.309 1.00 61.38 O ANISOU 2288 O LEU A 345 7837 9358 6128 -2077 -169 394 O ATOM 2289 CB LEU A 345 52.067 36.662 67.456 1.00 55.51 C ANISOU 2289 CB LEU A 345 6751 9575 4764 -1924 -587 364 C ATOM 2290 CG LEU A 345 52.709 37.124 66.148 1.00 54.64 C ANISOU 2290 CG LEU A 345 6435 9499 4828 -2170 -606 238 C ATOM 2291 CD1 LEU A 345 52.874 38.631 66.156 1.00 55.18 C ANISOU 2291 CD1 LEU A 345 6546 9590 4828 -2583 -677 -2 C ATOM 2292 CD2 LEU A 345 54.033 36.424 65.907 1.00 56.69 C ANISOU 2292 CD2 LEU A 345 6347 10161 5034 -2022 -726 288 C ATOM 2293 N MET A 346 49.649 34.847 66.488 1.00 55.91 N ANISOU 2293 N MET A 346 7157 8765 5321 -1554 -131 706 N ATOM 2294 CA MET A 346 49.012 34.087 65.417 1.00 53.16 C ANISOU 2294 CA MET A 346 6828 8102 5268 -1490 31 777 C ATOM 2295 C MET A 346 47.636 34.654 65.092 1.00 53.98 C ANISOU 2295 C MET A 346 7128 7860 5522 -1651 173 721 C ATOM 2296 O MET A 346 47.300 34.862 63.921 1.00 53.19 O ANISOU 2296 O MET A 346 6995 7593 5623 -1783 229 644 O ATOM 2297 CB MET A 346 48.905 32.612 65.807 1.00 50.34 C ANISOU 2297 CB MET A 346 6515 7665 4947 -1147 127 1005 C ATOM 2298 CG MET A 346 50.209 31.991 66.281 1.00 53.86 C ANISOU 2298 CG MET A 346 6784 8470 5212 -904 -8 1099 C ATOM 2299 SD MET A 346 51.494 31.947 65.018 1.00 66.33 S ANISOU 2299 SD MET A 346 8035 10285 6883 -947 -114 987 S ATOM 2300 CE MET A 346 50.880 30.651 63.950 1.00 51.18 C ANISOU 2300 CE MET A 346 6196 7962 5290 -770 98 1086 C ATOM 2301 N GLU A 347 46.832 34.925 66.124 1.00 53.69 N ANISOU 2301 N GLU A 347 7289 7743 5370 -1624 232 760 N ATOM 2302 CA GLU A 347 45.503 35.487 65.900 1.00 51.19 C ANISOU 2302 CA GLU A 347 7137 7136 5176 -1743 371 712 C ATOM 2303 C GLU A 347 45.583 36.875 65.279 1.00 52.54 C ANISOU 2303 C GLU A 347 7310 7298 5353 -2014 305 511 C ATOM 2304 O GLU A 347 44.826 37.194 64.352 1.00 54.69 O ANISOU 2304 O GLU A 347 7614 7355 5812 -2109 393 465 O ATOM 2305 CB GLU A 347 44.723 35.542 67.213 1.00 57.70 C ANISOU 2305 CB GLU A 347 8159 7924 5840 -1642 454 792 C ATOM 2306 CG GLU A 347 43.341 36.161 67.071 1.00 67.36 C ANISOU 2306 CG GLU A 347 9531 8891 7171 -1734 603 743 C ATOM 2307 CD GLU A 347 42.853 36.810 68.353 1.00 75.28 C ANISOU 2307 CD GLU A 347 10723 9941 7939 -1705 636 726 C ATOM 2308 OE1 GLU A 347 43.598 36.787 69.356 1.00 79.13 O ANISOU 2308 OE1 GLU A 347 11231 10669 8165 -1627 530 744 O ATOM 2309 OE2 GLU A 347 41.726 37.349 68.353 1.00 72.76 O ANISOU 2309 OE2 GLU A 347 10524 9441 7681 -1745 766 689 O ATOM 2310 N LYS A 348 46.494 37.718 65.776 1.00 60.77 N ANISOU 2310 N LYS A 348 8325 8577 6190 -2146 152 390 N ATOM 2311 CA LYS A 348 46.599 39.074 65.245 1.00 57.58 C ANISOU 2311 CA LYS A 348 7963 8122 5793 -2425 111 205 C ATOM 2312 C LYS A 348 47.019 39.065 63.778 1.00 54.00 C ANISOU 2312 C LYS A 348 7346 7639 5532 -2538 108 176 C ATOM 2313 O LYS A 348 46.510 39.856 62.975 1.00 58.52 O ANISOU 2313 O LYS A 348 8001 8018 6216 -2686 171 106 O ATOM 2314 CB LYS A 348 47.571 39.896 66.090 1.00 65.64 C ANISOU 2314 CB LYS A 348 8973 9409 6558 -2579 -54 60 C ATOM 2315 CG LYS A 348 47.096 40.134 67.520 1.00 65.62 C ANISOU 2315 CG LYS A 348 9169 9437 6326 -2492 -50 47 C ATOM 2316 CD LYS A 348 45.729 40.803 67.547 1.00 69.69 C ANISOU 2316 CD LYS A 348 9944 9621 6915 -2509 114 16 C ATOM 2317 CE LYS A 348 45.159 40.854 68.957 1.00 67.90 C ANISOU 2317 CE LYS A 348 9910 9429 6460 -2370 154 30 C ATOM 2318 NZ LYS A 348 43.834 41.537 68.997 1.00 65.31 N ANISOU 2318 NZ LYS A 348 9815 8805 6195 -2363 325 -6 N ATOM 2319 N LEU A 349 47.951 38.179 63.409 1.00 49.86 N ANISOU 2319 N LEU A 349 6597 7313 5034 -2444 44 237 N ATOM 2320 CA LEU A 349 48.344 38.052 62.008 1.00 45.25 C ANISOU 2320 CA LEU A 349 5855 6721 4617 -2517 60 215 C ATOM 2321 C LEU A 349 47.205 37.498 61.159 1.00 45.69 C ANISOU 2321 C LEU A 349 5983 6484 4891 -2419 209 280 C ATOM 2322 O LEU A 349 46.949 37.993 60.053 1.00 45.81 O ANISOU 2322 O LEU A 349 5995 6390 5021 -2545 251 222 O ATOM 2323 CB LEU A 349 49.576 37.155 61.881 1.00 45.12 C ANISOU 2323 CB LEU A 349 5580 6999 4566 -2388 -29 265 C ATOM 2324 CG LEU A 349 50.868 37.552 62.596 1.00 47.09 C ANISOU 2324 CG LEU A 349 5662 7634 4595 -2473 -202 197 C ATOM 2325 CD1 LEU A 349 51.960 36.528 62.329 1.00 48.44 C ANISOU 2325 CD1 LEU A 349 5555 8092 4757 -2276 -265 272 C ATOM 2326 CD2 LEU A 349 51.317 38.933 62.182 1.00 47.58 C ANISOU 2326 CD2 LEU A 349 5702 7750 4625 -2838 -254 25 C ATOM 2327 N LEU A 350 46.522 36.462 61.655 1.00 41.77 N ANISOU 2327 N LEU A 350 5550 5872 4449 -2202 292 400 N ATOM 2328 CA LEU A 350 45.420 35.870 60.909 1.00 40.10 C ANISOU 2328 CA LEU A 350 5386 5404 4449 -2138 428 439 C ATOM 2329 C LEU A 350 44.313 36.879 60.652 1.00 42.88 C ANISOU 2329 C LEU A 350 5878 5571 4843 -2268 494 374 C ATOM 2330 O LEU A 350 43.664 36.827 59.604 1.00 47.20 O ANISOU 2330 O LEU A 350 6403 5987 5543 -2295 557 347 O ATOM 2331 CB LEU A 350 44.872 34.654 61.660 1.00 42.46 C ANISOU 2331 CB LEU A 350 5749 5595 4790 -1923 525 584 C ATOM 2332 CG LEU A 350 45.692 33.362 61.626 1.00 42.37 C ANISOU 2332 CG LEU A 350 5628 5663 4808 -1725 515 680 C ATOM 2333 CD1 LEU A 350 45.151 32.350 62.626 1.00 47.09 C ANISOU 2333 CD1 LEU A 350 6352 6134 5408 -1524 625 850 C ATOM 2334 CD2 LEU A 350 45.693 32.771 60.231 1.00 44.01 C ANISOU 2334 CD2 LEU A 350 5733 5771 5219 -1728 560 623 C ATOM 2335 N ASN A 351 44.092 37.810 61.582 1.00 42.34 N ANISOU 2335 N ASN A 351 5956 5504 4628 -2331 478 340 N ATOM 2336 CA ASN A 351 43.026 38.794 61.404 1.00 41.28 C ANISOU 2336 CA ASN A 351 5974 5188 4525 -2407 554 286 C ATOM 2337 C ASN A 351 43.274 39.726 60.227 1.00 39.55 C ANISOU 2337 C ASN A 351 5737 4938 4353 -2573 524 197 C ATOM 2338 O ASN A 351 42.334 40.372 59.759 1.00 40.18 O ANISOU 2338 O ASN A 351 5917 4856 4494 -2586 597 179 O ATOM 2339 CB ASN A 351 42.847 39.607 62.684 1.00 47.05 C ANISOU 2339 CB ASN A 351 6885 5924 5066 -2425 549 249 C ATOM 2340 CG ASN A 351 42.192 38.803 63.790 1.00 57.56 C ANISOU 2340 CG ASN A 351 8278 7239 6351 -2242 633 361 C ATOM 2341 OD1 ASN A 351 41.492 37.827 63.526 1.00 60.33 O ANISOU 2341 OD1 ASN A 351 8576 7492 6855 -2129 737 463 O ATOM 2342 ND2 ASN A 351 42.419 39.209 65.037 1.00 57.50 N ANISOU 2342 ND2 ASN A 351 8391 7332 6124 -2224 597 339 N ATOM 2343 N VAL A 352 44.507 39.798 59.737 1.00 41.00 N ANISOU 2343 N VAL A 352 5788 5288 4504 -2683 429 157 N ATOM 2344 CA VAL A 352 44.841 40.567 58.548 1.00 42.87 C ANISOU 2344 CA VAL A 352 5996 5511 4784 -2842 422 101 C ATOM 2345 C VAL A 352 44.996 39.661 57.331 1.00 41.98 C ANISOU 2345 C VAL A 352 5702 5447 4802 -2772 439 133 C ATOM 2346 O VAL A 352 44.634 40.038 56.215 1.00 40.43 O ANISOU 2346 O VAL A 352 5510 5178 4674 -2789 476 119 O ATOM 2347 CB VAL A 352 46.114 41.420 58.793 1.00 39.16 C ANISOU 2347 CB VAL A 352 5498 5203 4180 -3063 326 17 C ATOM 2348 CG1 VAL A 352 46.312 42.419 57.673 1.00 39.27 C ANISOU 2348 CG1 VAL A 352 5543 5148 4229 -3179 350 -24 C ATOM 2349 CG2 VAL A 352 46.037 42.118 60.134 1.00 40.50 C ANISOU 2349 CG2 VAL A 352 5841 5352 4197 -3121 293 -47 C ATOM 2350 N PHE A 353 45.534 38.460 57.534 1.00 39.71 N ANISOU 2350 N PHE A 353 5267 5283 4537 -2643 410 175 N ATOM 2351 CA PHE A 353 45.691 37.532 56.420 1.00 39.70 C ANISOU 2351 CA PHE A 353 5117 5312 4657 -2560 436 181 C ATOM 2352 C PHE A 353 44.340 37.090 55.877 1.00 42.57 C ANISOU 2352 C PHE A 353 5541 5472 5163 -2475 529 189 C ATOM 2353 O PHE A 353 44.205 36.861 54.667 1.00 48.51 O ANISOU 2353 O PHE A 353 6218 6222 5993 -2475 550 149 O ATOM 2354 CB PHE A 353 46.528 36.314 56.836 1.00 41.40 C ANISOU 2354 CB PHE A 353 5194 5670 4867 -2401 402 229 C ATOM 2355 CG PHE A 353 47.925 36.661 57.303 1.00 41.40 C ANISOU 2355 CG PHE A 353 5066 5946 4716 -2469 292 214 C ATOM 2356 CD1 PHE A 353 48.461 37.919 57.064 1.00 39.27 C ANISOU 2356 CD1 PHE A 353 4787 5775 4360 -2711 243 139 C ATOM 2357 CD2 PHE A 353 48.702 35.730 57.974 1.00 40.34 C ANISOU 2357 CD2 PHE A 353 4819 5982 4527 -2292 241 276 C ATOM 2358 CE1 PHE A 353 49.727 38.240 57.493 1.00 41.11 C ANISOU 2358 CE1 PHE A 353 4871 6288 4461 -2813 139 103 C ATOM 2359 CE2 PHE A 353 49.982 36.049 58.405 1.00 41.97 C ANISOU 2359 CE2 PHE A 353 4863 6502 4580 -2350 123 253 C ATOM 2360 CZ PHE A 353 50.490 37.310 58.161 1.00 42.45 C ANISOU 2360 CZ PHE A 353 4888 6679 4564 -2631 68 153 C ATOM 2361 N VAL A 354 43.330 36.976 56.747 1.00 42.17 N ANISOU 2361 N VAL A 354 5610 5279 5134 -2408 585 232 N ATOM 2362 CA VAL A 354 41.984 36.634 56.296 1.00 38.57 C ANISOU 2362 CA VAL A 354 5178 4665 4812 -2356 673 228 C ATOM 2363 C VAL A 354 41.461 37.699 55.343 1.00 40.23 C ANISOU 2363 C VAL A 354 5423 4849 5015 -2432 671 178 C ATOM 2364 O VAL A 354 40.833 37.391 54.323 1.00 44.86 O ANISOU 2364 O VAL A 354 5937 5416 5692 -2381 687 139 O ATOM 2365 CB VAL A 354 41.040 36.434 57.500 1.00 40.02 C ANISOU 2365 CB VAL A 354 5470 4734 5002 -2283 751 295 C ATOM 2366 CG1 VAL A 354 40.966 37.696 58.357 1.00 42.46 C ANISOU 2366 CG1 VAL A 354 5930 5044 5159 -2337 735 293 C ATOM 2367 CG2 VAL A 354 39.658 36.037 57.029 1.00 44.48 C ANISOU 2367 CG2 VAL A 354 6010 5175 5714 -2252 844 282 C ATOM 2368 N TRP A 355 41.726 38.968 55.644 1.00 34.99 N ANISOU 2368 N TRP A 355 4872 4190 4233 -2494 637 171 N ATOM 2369 CA TRP A 355 41.248 40.021 54.763 1.00 37.98 C ANISOU 2369 CA TRP A 355 5311 4522 4597 -2484 639 150 C ATOM 2370 C TRP A 355 42.084 40.134 53.498 1.00 38.61 C ANISOU 2370 C TRP A 355 5293 4714 4664 -2523 595 125 C ATOM 2371 O TRP A 355 41.560 40.549 52.465 1.00 41.68 O ANISOU 2371 O TRP A 355 5691 5085 5060 -2505 614 127 O ATOM 2372 CB TRP A 355 41.190 41.353 55.505 1.00 41.23 C ANISOU 2372 CB TRP A 355 5921 4846 4900 -2546 649 149 C ATOM 2373 CG TRP A 355 39.824 41.609 56.046 1.00 38.00 C ANISOU 2373 CG TRP A 355 5631 4298 4510 -2476 738 175 C ATOM 2374 CD1 TRP A 355 39.365 41.307 57.295 1.00 37.59 C ANISOU 2374 CD1 TRP A 355 5648 4197 4436 -2455 793 196 C ATOM 2375 CD2 TRP A 355 38.720 42.186 55.340 1.00 36.44 C ANISOU 2375 CD2 TRP A 355 5490 4014 4343 -2422 802 196 C ATOM 2376 NE1 TRP A 355 38.047 41.674 57.415 1.00 38.94 N ANISOU 2376 NE1 TRP A 355 5888 4272 4635 -2339 879 215 N ATOM 2377 CE2 TRP A 355 37.628 42.218 56.229 1.00 42.72 C ANISOU 2377 CE2 TRP A 355 6355 4731 5147 -2318 881 215 C ATOM 2378 CE3 TRP A 355 38.552 42.687 54.046 1.00 35.37 C ANISOU 2378 CE3 TRP A 355 5347 3885 4209 -2425 800 212 C ATOM 2379 CZ2 TRP A 355 36.384 42.731 55.865 1.00 47.28 C ANISOU 2379 CZ2 TRP A 355 6960 5258 5746 -2182 944 237 C ATOM 2380 CZ3 TRP A 355 37.318 43.197 53.686 1.00 38.76 C ANISOU 2380 CZ3 TRP A 355 5822 4258 4646 -2283 853 243 C ATOM 2381 CH2 TRP A 355 36.250 43.215 54.592 1.00 41.57 C ANISOU 2381 CH2 TRP A 355 6217 4554 5022 -2158 920 252 C ATOM 2382 N ILE A 356 43.364 39.762 53.541 1.00 40.55 N ANISOU 2382 N ILE A 356 5436 5096 4874 -2592 547 112 N ATOM 2383 CA ILE A 356 44.121 39.642 52.293 1.00 38.73 C ANISOU 2383 CA ILE A 356 5083 4996 4637 -2621 532 91 C ATOM 2384 C ILE A 356 43.474 38.593 51.392 1.00 37.51 C ANISOU 2384 C ILE A 356 4828 4842 4580 -2542 565 62 C ATOM 2385 O ILE A 356 43.250 38.816 50.191 1.00 40.58 O ANISOU 2385 O ILE A 356 5193 5272 4954 -2547 579 44 O ATOM 2386 CB ILE A 356 45.595 39.304 52.580 1.00 35.30 C ANISOU 2386 CB ILE A 356 4516 4747 4149 -2713 487 81 C ATOM 2387 CG1 ILE A 356 46.273 40.454 53.324 1.00 36.39 C ANISOU 2387 CG1 ILE A 356 4737 4910 4178 -2840 446 74 C ATOM 2388 CG2 ILE A 356 46.330 38.997 51.287 1.00 35.67 C ANISOU 2388 CG2 ILE A 356 4410 4951 4192 -2732 498 59 C ATOM 2389 CD1 ILE A 356 47.724 40.189 53.656 1.00 37.69 C ANISOU 2389 CD1 ILE A 356 4729 5317 4275 -2960 387 55 C ATOM 2390 N GLY A 357 43.147 37.437 51.971 1.00 36.33 N ANISOU 2390 N GLY A 357 4633 4645 4525 -2492 588 53 N ATOM 2391 CA GLY A 357 42.456 36.412 51.207 1.00 36.13 C ANISOU 2391 CA GLY A 357 4528 4587 4611 -2436 625 -8 C ATOM 2392 C GLY A 357 41.119 36.890 50.673 1.00 39.48 C ANISOU 2392 C GLY A 357 4998 4946 5058 -2412 641 -27 C ATOM 2393 O GLY A 357 40.745 36.578 49.539 1.00 46.30 O ANISOU 2393 O GLY A 357 5783 5867 5941 -2401 638 -100 O ATOM 2394 N TYR A 358 40.378 37.647 51.485 1.00 36.27 N ANISOU 2394 N TYR A 358 4706 4441 4632 -2388 656 31 N ATOM 2395 CA TYR A 358 39.116 38.225 51.031 1.00 37.09 C ANISOU 2395 CA TYR A 358 4842 4512 4740 -2380 684 29 C ATOM 2396 C TYR A 358 39.335 39.167 49.853 1.00 41.37 C ANISOU 2396 C TYR A 358 5410 5138 5172 -2403 659 41 C ATOM 2397 O TYR A 358 38.625 39.096 48.843 1.00 45.47 O ANISOU 2397 O TYR A 358 5859 5732 5687 -2341 644 3 O ATOM 2398 CB TYR A 358 38.439 38.978 52.176 1.00 36.93 C ANISOU 2398 CB TYR A 358 4959 4375 4696 -2355 729 94 C ATOM 2399 CG TYR A 358 37.792 38.114 53.232 1.00 40.01 C ANISOU 2399 CG TYR A 358 5324 4691 5186 -2306 784 103 C ATOM 2400 CD1 TYR A 358 37.649 36.745 53.057 1.00 39.93 C ANISOU 2400 CD1 TYR A 358 5186 4681 5305 -2288 798 55 C ATOM 2401 CD2 TYR A 358 37.308 38.678 54.406 1.00 39.50 C ANISOU 2401 CD2 TYR A 358 5387 4542 5081 -2284 841 160 C ATOM 2402 CE1 TYR A 358 37.050 35.961 54.028 1.00 37.89 C ANISOU 2402 CE1 TYR A 358 4925 4331 5142 -2255 874 88 C ATOM 2403 CE2 TYR A 358 36.709 37.906 55.378 1.00 38.97 C ANISOU 2403 CE2 TYR A 358 5302 4418 5087 -2243 916 190 C ATOM 2404 CZ TYR A 358 36.584 36.549 55.186 1.00 38.18 C ANISOU 2404 CZ TYR A 358 5073 4310 5124 -2236 937 165 C ATOM 2405 OH TYR A 358 35.984 35.783 56.157 1.00 42.62 O ANISOU 2405 OH TYR A 358 5636 4793 5762 -2207 1035 218 O ATOM 2406 N VAL A 359 40.321 40.060 49.971 1.00 41.12 N ANISOU 2406 N VAL A 359 5476 5107 5041 -2479 651 94 N ATOM 2407 CA VAL A 359 40.591 41.064 48.946 1.00 39.36 C ANISOU 2407 CA VAL A 359 5320 4928 4707 -2531 662 142 C ATOM 2408 C VAL A 359 41.011 40.403 47.642 1.00 42.19 C ANISOU 2408 C VAL A 359 5526 5461 5043 -2516 638 90 C ATOM 2409 O VAL A 359 40.813 40.968 46.558 1.00 48.81 O ANISOU 2409 O VAL A 359 6390 6370 5787 -2482 645 126 O ATOM 2410 CB VAL A 359 41.650 42.064 49.462 1.00 35.54 C ANISOU 2410 CB VAL A 359 4957 4397 4149 -2600 655 186 C ATOM 2411 CG1 VAL A 359 42.207 42.922 48.336 1.00 37.18 C ANISOU 2411 CG1 VAL A 359 5217 4655 4254 -2682 688 244 C ATOM 2412 CG2 VAL A 359 41.047 42.952 50.535 1.00 35.44 C ANISOU 2412 CG2 VAL A 359 5136 4205 4126 -2583 683 217 C ATOM 2413 N ASN A 360 41.572 39.192 47.714 1.00 41.36 N ANISOU 2413 N ASN A 360 5277 5429 5011 -2516 618 8 N ATOM 2414 CA ASN A 360 41.847 38.465 46.476 1.00 43.03 C ANISOU 2414 CA ASN A 360 5354 5796 5200 -2474 605 -74 C ATOM 2415 C ASN A 360 40.606 38.346 45.597 1.00 47.86 C ANISOU 2415 C ASN A 360 5934 6450 5802 -2376 582 -130 C ATOM 2416 O ASN A 360 40.714 38.362 44.365 1.00 54.38 O ANISOU 2416 O ASN A 360 6707 7429 6525 -2343 569 -165 O ATOM 2417 CB ASN A 360 42.389 37.068 46.764 1.00 42.67 C ANISOU 2417 CB ASN A 360 5187 5768 5259 -2442 601 -167 C ATOM 2418 CG ASN A 360 42.348 36.177 45.537 1.00 51.23 C ANISOU 2418 CG ASN A 360 6157 6970 6340 -2374 594 -298 C ATOM 2419 OD1 ASN A 360 41.401 35.415 45.341 1.00 62.35 O ANISOU 2419 OD1 ASN A 360 7527 8327 7836 -2324 583 -402 O ATOM 2420 ND2 ASN A 360 43.360 36.294 44.686 1.00 54.11 N ANISOU 2420 ND2 ASN A 360 6461 7502 6594 -2386 608 -304 N ATOM 2421 N SER A 361 39.424 38.241 46.204 1.00 46.02 N ANISOU 2421 N SER A 361 5714 6114 5656 -2327 577 -140 N ATOM 2422 CA SER A 361 38.170 38.095 45.464 1.00 51.19 C ANISOU 2422 CA SER A 361 6292 6852 6306 -2240 542 -207 C ATOM 2423 C SER A 361 37.752 39.366 44.724 1.00 48.89 C ANISOU 2423 C SER A 361 6084 6639 5852 -2161 530 -103 C ATOM 2424 O SER A 361 36.643 39.409 44.175 1.00 58.47 O ANISOU 2424 O SER A 361 7226 7957 7035 -2057 488 -137 O ATOM 2425 CB SER A 361 37.055 37.652 46.412 1.00 47.27 C ANISOU 2425 CB SER A 361 5760 6245 5954 -2222 559 -236 C ATOM 2426 OG SER A 361 37.374 36.413 47.021 1.00 46.70 O ANISOU 2426 OG SER A 361 5633 6081 6030 -2280 586 -314 O ATOM 2427 N GLY A 362 38.564 40.415 44.668 1.00 42.23 N ANISOU 2427 N GLY A 362 5390 5755 4900 -2203 570 28 N ATOM 2428 CA GLY A 362 38.196 41.586 43.897 1.00 47.50 C ANISOU 2428 CA GLY A 362 6171 6465 5411 -2111 582 151 C ATOM 2429 C GLY A 362 39.264 42.028 42.917 1.00 53.36 C ANISOU 2429 C GLY A 362 6961 7307 6005 -2168 615 219 C ATOM 2430 O GLY A 362 39.251 43.169 42.447 1.00 54.61 O ANISOU 2430 O GLY A 362 7279 7437 6033 -2128 663 370 O ATOM 2431 N ILE A 363 40.193 41.135 42.599 1.00 52.47 N ANISOU 2431 N ILE A 363 6718 7306 5911 -2252 608 119 N ATOM 2432 CA ILE A 363 41.381 41.501 41.837 1.00 50.92 C ANISOU 2432 CA ILE A 363 6542 7218 5589 -2335 666 183 C ATOM 2433 C ILE A 363 41.288 40.924 40.431 1.00 48.48 C ANISOU 2433 C ILE A 363 6111 7160 5148 -2233 635 100 C ATOM 2434 O ILE A 363 41.756 41.531 39.460 1.00 51.30 O ANISOU 2434 O ILE A 363 6519 7643 5328 -2226 688 200 O ATOM 2435 CB ILE A 363 42.653 41.034 42.573 1.00 46.80 C ANISOU 2435 CB ILE A 363 5952 6671 5159 -2491 693 141 C ATOM 2436 CG1 ILE A 363 42.951 41.979 43.740 1.00 41.04 C ANISOU 2436 CG1 ILE A 363 5376 5738 4478 -2623 730 244 C ATOM 2437 CG2 ILE A 363 43.843 40.938 41.623 1.00 49.18 C ANISOU 2437 CG2 ILE A 363 6167 7173 5344 -2552 746 147 C ATOM 2438 CD1 ILE A 363 44.271 41.720 44.413 1.00 40.90 C ANISOU 2438 CD1 ILE A 363 5279 5753 4507 -2783 744 218 C ATOM 2439 N ASN A 364 40.664 39.752 40.316 1.00 46.27 N ANISOU 2439 N ASN A 364 5681 6952 4947 -2161 558 -87 N ATOM 2440 CA ASN A 364 40.490 39.125 39.007 1.00 51.73 C ANISOU 2440 CA ASN A 364 6259 7890 5507 -2068 514 -216 C ATOM 2441 C ASN A 364 39.812 40.037 37.985 1.00 52.75 C ANISOU 2441 C ASN A 364 6455 8174 5413 -1935 492 -104 C ATOM 2442 O ASN A 364 40.258 40.047 36.822 1.00 53.17 O ANISOU 2442 O ASN A 364 6488 8446 5270 -1887 509 -107 O ATOM 2443 CB ASN A 364 39.711 37.809 39.159 1.00 54.03 C ANISOU 2443 CB ASN A 364 6405 8182 5942 -2042 435 -452 C ATOM 2444 CG ASN A 364 40.242 36.937 40.280 1.00 61.53 C ANISOU 2444 CG ASN A 364 7325 8939 7115 -2136 468 -521 C ATOM 2445 OD1 ASN A 364 41.441 36.917 40.561 1.00 61.56 O ANISOU 2445 OD1 ASN A 364 7344 8917 7128 -2196 529 -470 O ATOM 2446 ND2 ASN A 364 39.343 36.204 40.928 1.00 64.01 N ANISOU 2446 ND2 ASN A 364 7586 9133 7601 -2144 433 -629 N ATOM 2447 N PRO A 365 38.758 40.797 38.318 1.00 50.75 N ANISOU 2447 N PRO A 365 6283 7842 5159 -1844 462 2 N ATOM 2448 CA PRO A 365 38.236 41.760 37.333 1.00 52.17 C ANISOU 2448 CA PRO A 365 6550 8171 5099 -1676 454 154 C ATOM 2449 C PRO A 365 39.282 42.757 36.863 1.00 52.04 C ANISOU 2449 C PRO A 365 6715 8128 4930 -1725 581 371 C ATOM 2450 O PRO A 365 39.279 43.141 35.687 1.00 55.94 O ANISOU 2450 O PRO A 365 7244 8827 5182 -1606 593 459 O ATOM 2451 CB PRO A 365 37.089 42.443 38.089 1.00 47.89 C ANISOU 2451 CB PRO A 365 6082 7484 4629 -1569 430 250 C ATOM 2452 CG PRO A 365 36.641 41.439 39.075 1.00 45.90 C ANISOU 2452 CG PRO A 365 5683 7139 4618 -1655 379 62 C ATOM 2453 CD PRO A 365 37.889 40.721 39.508 1.00 47.75 C ANISOU 2453 CD PRO A 365 5897 7272 4972 -1848 433 -20 C ATOM 2454 N LEU A 366 40.192 43.179 37.744 1.00 50.55 N ANISOU 2454 N LEU A 366 6635 7707 4865 -1909 680 457 N ATOM 2455 CA LEU A 366 41.255 44.077 37.309 1.00 47.48 C ANISOU 2455 CA LEU A 366 6393 7293 4352 -2015 816 645 C ATOM 2456 C LEU A 366 42.234 43.373 36.379 1.00 48.98 C ANISOU 2456 C LEU A 366 6436 7742 4431 -2066 848 560 C ATOM 2457 O LEU A 366 42.765 43.999 35.457 1.00 49.09 O ANISOU 2457 O LEU A 366 6533 7871 4247 -2065 949 712 O ATOM 2458 CB LEU A 366 41.991 44.657 38.514 1.00 48.63 C ANISOU 2458 CB LEU A 366 6660 7157 4660 -2234 899 715 C ATOM 2459 CG LEU A 366 42.838 45.886 38.186 1.00 54.49 C ANISOU 2459 CG LEU A 366 7607 7802 5293 -2371 1056 936 C ATOM 2460 CD1 LEU A 366 41.954 46.998 37.641 1.00 62.34 C ANISOU 2460 CD1 LEU A 366 8842 8704 6138 -2183 1100 1146 C ATOM 2461 CD2 LEU A 366 43.611 46.357 39.406 1.00 52.89 C ANISOU 2461 CD2 LEU A 366 7489 7353 5254 -2629 1116 948 C ATOM 2462 N VAL A 367 42.483 42.080 36.599 1.00 48.13 N ANISOU 2462 N VAL A 367 6125 7720 4443 -2097 782 327 N ATOM 2463 CA VAL A 367 43.300 41.314 35.662 1.00 47.97 C ANISOU 2463 CA VAL A 367 5962 7958 4307 -2093 812 215 C ATOM 2464 C VAL A 367 42.640 41.288 34.289 1.00 54.57 C ANISOU 2464 C VAL A 367 6787 9060 4886 -1900 767 196 C ATOM 2465 O VAL A 367 43.300 41.493 33.260 1.00 57.35 O ANISOU 2465 O VAL A 367 7147 9624 5020 -1877 853 265 O ATOM 2466 CB VAL A 367 43.542 39.891 36.199 1.00 45.04 C ANISOU 2466 CB VAL A 367 5409 7580 4125 -2119 751 -37 C ATOM 2467 CG1 VAL A 367 44.384 39.091 35.220 1.00 46.34 C ANISOU 2467 CG1 VAL A 367 5441 8001 4165 -2080 795 -169 C ATOM 2468 CG2 VAL A 367 44.206 39.945 37.563 1.00 43.48 C ANISOU 2468 CG2 VAL A 367 5218 7162 4141 -2279 785 2 C ATOM 2469 N TYR A 368 41.325 41.047 34.252 1.00 53.42 N ANISOU 2469 N TYR A 368 6612 8939 4746 -1758 632 103 N ATOM 2470 CA TYR A 368 40.613 41.074 32.977 1.00 49.97 C ANISOU 2470 CA TYR A 368 6150 8798 4039 -1562 560 78 C ATOM 2471 C TYR A 368 40.721 42.445 32.324 1.00 55.21 C ANISOU 2471 C TYR A 368 7014 9503 4462 -1475 659 394 C ATOM 2472 O TYR A 368 40.945 42.549 31.113 1.00 65.14 O ANISOU 2472 O TYR A 368 8280 11035 5437 -1368 689 440 O ATOM 2473 CB TYR A 368 39.142 40.709 33.171 1.00 52.06 C ANISOU 2473 CB TYR A 368 6322 9095 4364 -1444 395 -60 C ATOM 2474 CG TYR A 368 38.890 39.440 33.947 1.00 56.02 C ANISOU 2474 CG TYR A 368 6663 9488 5136 -1551 320 -340 C ATOM 2475 CD1 TYR A 368 39.793 38.386 33.919 1.00 54.42 C ANISOU 2475 CD1 TYR A 368 6373 9287 5017 -1654 358 -529 C ATOM 2476 CD2 TYR A 368 37.740 39.296 34.711 1.00 53.75 C ANISOU 2476 CD2 TYR A 368 6316 9091 5017 -1536 230 -401 C ATOM 2477 CE1 TYR A 368 39.558 37.229 34.633 1.00 53.42 C ANISOU 2477 CE1 TYR A 368 6138 9019 5139 -1737 312 -759 C ATOM 2478 CE2 TYR A 368 37.497 38.146 35.426 1.00 47.84 C ANISOU 2478 CE2 TYR A 368 5441 8221 4516 -1648 189 -630 C ATOM 2479 CZ TYR A 368 38.407 37.115 35.384 1.00 51.22 C ANISOU 2479 CZ TYR A 368 5817 8615 5027 -1748 232 -803 C ATOM 2480 OH TYR A 368 38.163 35.967 36.099 1.00 59.38 O ANISOU 2480 OH TYR A 368 6762 9488 6310 -1846 211 -1008 O ATOM 2481 N THR A 369 40.569 43.509 33.114 1.00 54.25 N ANISOU 2481 N THR A 369 7077 9097 4438 -1514 724 617 N ATOM 2482 CA THR A 369 40.658 44.859 32.565 1.00 53.62 C ANISOU 2482 CA THR A 369 7239 8981 4154 -1436 844 937 C ATOM 2483 C THR A 369 42.041 45.126 31.988 1.00 55.03 C ANISOU 2483 C THR A 369 7470 9223 4216 -1591 1021 1056 C ATOM 2484 O THR A 369 42.171 45.747 30.927 1.00 62.10 O ANISOU 2484 O THR A 369 8483 10278 4835 -1482 1110 1250 O ATOM 2485 CB THR A 369 40.328 45.889 33.643 1.00 52.94 C ANISOU 2485 CB THR A 369 7365 8518 4233 -1477 899 1116 C ATOM 2486 OG1 THR A 369 39.220 45.426 34.423 1.00 56.33 O ANISOU 2486 OG1 THR A 369 7688 8885 4829 -1387 752 961 O ATOM 2487 CG2 THR A 369 39.963 47.216 33.007 1.00 55.72 C ANISOU 2487 CG2 THR A 369 7986 8820 4364 -1297 993 1434 C ATOM 2488 N LEU A 370 43.086 44.663 32.676 1.00 57.07 N ANISOU 2488 N LEU A 370 7631 9383 4671 -1836 1081 951 N ATOM 2489 CA LEU A 370 44.456 44.889 32.235 1.00 61.45 C ANISOU 2489 CA LEU A 370 8185 10022 5142 -2010 1257 1050 C ATOM 2490 C LEU A 370 44.860 44.005 31.063 1.00 66.39 C ANISOU 2490 C LEU A 370 8634 11034 5558 -1910 1256 910 C ATOM 2491 O LEU A 370 45.829 44.332 30.369 1.00 69.62 O ANISOU 2491 O LEU A 370 9056 11589 5806 -1989 1422 1038 O ATOM 2492 CB LEU A 370 45.428 44.664 33.398 1.00 57.22 C ANISOU 2492 CB LEU A 370 7563 9304 4874 -2284 1301 972 C ATOM 2493 CG LEU A 370 45.388 45.657 34.561 1.00 52.13 C ANISOU 2493 CG LEU A 370 7109 8286 4412 -2450 1344 1110 C ATOM 2494 CD1 LEU A 370 46.180 45.126 35.741 1.00 50.24 C ANISOU 2494 CD1 LEU A 370 6723 7950 4417 -2668 1322 960 C ATOM 2495 CD2 LEU A 370 45.925 47.007 34.129 1.00 54.78 C ANISOU 2495 CD2 LEU A 370 7681 8512 4620 -2578 1542 1401 C ATOM 2496 N PHE A 371 44.149 42.897 30.819 1.00 65.63 N ANISOU 2496 N PHE A 371 8377 11106 5456 -1752 1087 640 N ATOM 2497 CA PHE A 371 44.552 41.976 29.760 1.00 63.03 C ANISOU 2497 CA PHE A 371 7892 11123 4934 -1660 1086 456 C ATOM 2498 C PHE A 371 43.406 41.593 28.826 1.00 66.79 C ANISOU 2498 C PHE A 371 8336 11855 5185 -1411 930 324 C ATOM 2499 O PHE A 371 43.474 40.543 28.179 1.00 72.57 O ANISOU 2499 O PHE A 371 8920 12830 5821 -1338 870 58 O ATOM 2500 CB PHE A 371 45.180 40.715 30.358 1.00 58.78 C ANISOU 2500 CB PHE A 371 7152 10558 4623 -1758 1057 175 C ATOM 2501 CG PHE A 371 46.434 40.976 31.136 1.00 57.76 C ANISOU 2501 CG PHE A 371 6995 10287 4664 -1981 1197 277 C ATOM 2502 CD1 PHE A 371 47.662 41.034 30.497 1.00 73.81 C ANISOU 2502 CD1 PHE A 371 8955 12534 6557 -2046 1366 341 C ATOM 2503 CD2 PHE A 371 46.388 41.166 32.505 1.00 54.24 C ANISOU 2503 CD2 PHE A 371 6576 9530 4502 -2125 1161 303 C ATOM 2504 CE1 PHE A 371 48.822 41.276 31.210 1.00 66.72 C ANISOU 2504 CE1 PHE A 371 7985 11555 5809 -2265 1484 422 C ATOM 2505 CE2 PHE A 371 47.542 41.408 33.223 1.00 60.67 C ANISOU 2505 CE2 PHE A 371 7341 10261 5451 -2336 1267 377 C ATOM 2506 CZ PHE A 371 48.761 41.463 32.574 1.00 61.70 C ANISOU 2506 CZ PHE A 371 7372 10621 5450 -2412 1423 434 C ATOM 2507 N ASN A 372 42.362 42.413 28.728 1.00 63.27 N ANISOU 2507 N ASN A 372 8022 11375 4642 -1270 861 492 N ATOM 2508 CA ASN A 372 41.280 42.149 27.782 1.00 64.40 C ANISOU 2508 CA ASN A 372 8110 11829 4529 -1022 700 385 C ATOM 2509 C ASN A 372 40.689 43.471 27.324 1.00 74.18 C ANISOU 2509 C ASN A 372 9557 13093 5535 -836 732 730 C ATOM 2510 O ASN A 372 40.208 44.253 28.149 1.00 75.81 O ANISOU 2510 O ASN A 372 9894 13007 5902 -841 739 907 O ATOM 2511 CB ASN A 372 40.192 41.267 28.402 1.00 69.55 C ANISOU 2511 CB ASN A 372 8598 12433 5393 -1006 490 91 C ATOM 2512 CG ASN A 372 40.495 39.786 28.279 1.00 77.87 C ANISOU 2512 CG ASN A 372 9457 13594 6538 -1084 428 -295 C ATOM 2513 OD1 ASN A 372 40.921 39.314 27.225 1.00 84.45 O ANISOU 2513 OD1 ASN A 372 10239 14722 7128 -1014 446 -422 O ATOM 2514 ND2 ASN A 372 40.275 39.044 29.359 1.00 78.77 N ANISOU 2514 ND2 ASN A 372 9479 13457 6994 -1219 369 -482 N ATOM 2515 N LYS A 373 40.727 43.718 26.012 1.00 84.94 N ANISOU 2515 N LYS A 373 10967 14801 6505 -650 761 831 N ATOM 2516 CA LYS A 373 40.010 44.863 25.461 1.00 86.77 C ANISOU 2516 CA LYS A 373 11393 15103 6471 -400 767 1155 C ATOM 2517 C LYS A 373 38.508 44.704 25.640 1.00 87.50 C ANISOU 2517 C LYS A 373 11379 15293 6574 -191 523 1033 C ATOM 2518 O LYS A 373 37.799 45.689 25.877 1.00 87.14 O ANISOU 2518 O LYS A 373 11491 15116 6503 -22 521 1294 O ATOM 2519 CB LYS A 373 40.348 45.046 23.981 1.00 85.42 C ANISOU 2519 CB LYS A 373 11280 15333 5841 -221 840 1277 C ATOM 2520 CG LYS A 373 41.554 45.927 23.711 1.00 86.33 C ANISOU 2520 CG LYS A 373 11614 15322 5866 -347 1138 1619 C ATOM 2521 CD LYS A 373 41.264 46.897 22.576 1.00 94.16 C ANISOU 2521 CD LYS A 373 12825 16532 6418 -63 1220 1976 C ATOM 2522 CE LYS A 373 42.506 47.668 22.173 1.00 93.09 C ANISOU 2522 CE LYS A 373 12896 16224 6249 -215 1525 2266 C ATOM 2523 NZ LYS A 373 43.526 46.771 21.567 1.00 96.90 N ANISOU 2523 NZ LYS A 373 13190 16948 6677 -334 1592 2035 N ATOM 2524 N ILE A 374 38.005 43.472 25.531 1.00 81.79 N ANISOU 2524 N ILE A 374 10388 14797 5891 -200 325 634 N ATOM 2525 CA ILE A 374 36.569 43.242 25.662 1.00 81.92 C ANISOU 2525 CA ILE A 374 10247 14961 5917 -36 90 487 C ATOM 2526 C ILE A 374 36.096 43.626 27.057 1.00 79.93 C ANISOU 2526 C ILE A 374 10034 14299 6037 -123 96 566 C ATOM 2527 O ILE A 374 35.173 44.432 27.216 1.00 79.40 O ANISOU 2527 O ILE A 374 10033 14218 5919 89 45 760 O ATOM 2528 CB ILE A 374 36.229 41.776 25.340 1.00 86.63 C ANISOU 2528 CB ILE A 374 10555 15831 6531 -108 -97 9 C ATOM 2529 CG1 ILE A 374 37.049 41.288 24.145 1.00 84.61 C ANISOU 2529 CG1 ILE A 374 10291 15893 5965 -87 -47 -108 C ATOM 2530 CG2 ILE A 374 34.740 41.626 25.065 1.00 91.51 C ANISOU 2530 CG2 ILE A 374 10982 16759 7029 88 -347 -133 C ATOM 2531 CD1 ILE A 374 36.885 39.811 23.856 1.00 94.16 C ANISOU 2531 CD1 ILE A 374 11265 17300 7212 -188 -195 -606 C ATOM 2532 N TYR A 375 36.747 43.081 28.089 1.00 76.72 N ANISOU 2532 N TYR A 375 9597 13563 5992 -411 169 429 N ATOM 2533 CA TYR A 375 36.332 43.365 29.460 1.00 76.71 C ANISOU 2533 CA TYR A 375 9630 13187 6329 -502 178 478 C ATOM 2534 C TYR A 375 36.544 44.832 29.817 1.00 79.66 C ANISOU 2534 C TYR A 375 10305 13274 6687 -439 341 878 C ATOM 2535 O TYR A 375 35.710 45.433 30.497 1.00 81.22 O ANISOU 2535 O TYR A 375 10567 13304 6991 -328 313 990 O ATOM 2536 CB TYR A 375 37.081 42.467 30.446 1.00 72.06 C ANISOU 2536 CB TYR A 375 8959 12334 6087 -805 226 266 C ATOM 2537 CG TYR A 375 36.534 41.059 30.565 1.00 67.96 C ANISOU 2537 CG TYR A 375 8175 11939 5708 -879 69 -126 C ATOM 2538 CD1 TYR A 375 35.301 40.818 31.156 1.00 65.55 C ANISOU 2538 CD1 TYR A 375 7732 11620 5553 -841 -64 -240 C ATOM 2539 CD2 TYR A 375 37.265 39.971 30.108 1.00 75.91 C ANISOU 2539 CD2 TYR A 375 9076 13059 6708 -994 74 -382 C ATOM 2540 CE1 TYR A 375 34.804 39.531 31.273 1.00 68.73 C ANISOU 2540 CE1 TYR A 375 7906 12107 6103 -951 -185 -597 C ATOM 2541 CE2 TYR A 375 36.779 38.683 30.221 1.00 69.89 C ANISOU 2541 CE2 TYR A 375 8113 12353 6090 -1077 -48 -745 C ATOM 2542 CZ TYR A 375 35.550 38.469 30.804 1.00 71.65 C ANISOU 2542 CZ TYR A 375 8209 12545 6471 -1075 -175 -850 C ATOM 2543 OH TYR A 375 35.067 37.185 30.915 1.00 77.68 O ANISOU 2543 OH TYR A 375 8783 13339 7392 -1198 -276 -1211 O ATOM 2544 N ARG A 376 37.654 45.424 29.375 1.00 75.77 N ANISOU 2544 N ARG A 376 10007 12713 6069 -515 527 1092 N ATOM 2545 CA ARG A 376 37.940 46.816 29.717 1.00 79.13 C ANISOU 2545 CA ARG A 376 10753 12813 6502 -506 708 1459 C ATOM 2546 C ARG A 376 36.935 47.766 29.070 1.00 85.94 C ANISOU 2546 C ARG A 376 11764 13796 7093 -138 675 1719 C ATOM 2547 O ARG A 376 36.356 48.636 29.743 1.00 97.81 O ANISOU 2547 O ARG A 376 13444 15022 8697 -29 711 1901 O ATOM 2548 CB ARG A 376 39.370 47.158 29.297 1.00 81.88 C ANISOU 2548 CB ARG A 376 11241 13101 6769 -705 925 1613 C ATOM 2549 CG ARG A 376 39.829 48.561 29.651 1.00 92.75 C ANISOU 2549 CG ARG A 376 12962 14101 8178 -779 1143 1970 C ATOM 2550 CD ARG A 376 41.343 48.699 29.524 1.00 80.79 C ANISOU 2550 CD ARG A 376 11505 12510 6683 -1087 1354 2046 C ATOM 2551 NE ARG A 376 41.808 48.595 28.145 1.00 82.32 N ANISOU 2551 NE ARG A 376 11678 13063 6536 -993 1428 2132 N ATOM 2552 CZ ARG A 376 42.288 47.488 27.593 1.00 81.45 C ANISOU 2552 CZ ARG A 376 11310 13289 6347 -1035 1372 1884 C ATOM 2553 NH1 ARG A 376 42.369 46.355 28.271 1.00 75.62 N ANISOU 2553 NH1 ARG A 376 10321 12560 5853 -1163 1242 1542 N ATOM 2554 NH2 ARG A 376 42.699 47.520 26.328 1.00 88.59 N ANISOU 2554 NH2 ARG A 376 12231 14520 6910 -930 1462 1988 N ATOM 2555 N ARG A 377 36.720 47.615 27.759 1.00 85.11 N ANISOU 2555 N ARG A 377 11597 14117 6624 83 608 1741 N ATOM 2556 CA ARG A 377 35.747 48.448 27.064 1.00 86.99 C ANISOU 2556 CA ARG A 377 11952 14541 6561 483 555 1992 C ATOM 2557 C ARG A 377 34.352 48.234 27.630 1.00 85.72 C ANISOU 2557 C ARG A 377 11602 14454 6514 670 346 1849 C ATOM 2558 O ARG A 377 33.589 49.196 27.804 1.00 83.01 O ANISOU 2558 O ARG A 377 11421 14004 6116 946 361 2101 O ATOM 2559 CB ARG A 377 35.777 48.147 25.565 1.00 85.78 C ANISOU 2559 CB ARG A 377 11718 14902 5973 678 490 1987 C ATOM 2560 CG ARG A 377 35.040 49.163 24.708 1.00 95.02 C ANISOU 2560 CG ARG A 377 13071 16270 6762 1112 484 2336 C ATOM 2561 CD ARG A 377 35.706 50.528 24.785 1.00 97.04 C ANISOU 2561 CD ARG A 377 13764 16112 6996 1115 780 2796 C ATOM 2562 NE ARG A 377 34.802 51.549 25.300 1.00101.65 N ANISOU 2562 NE ARG A 377 14552 16442 7628 1390 792 3054 N ATOM 2563 CZ ARG A 377 35.145 52.811 25.524 1.00103.56 C ANISOU 2563 CZ ARG A 377 15209 16245 7893 1424 1040 3444 C ATOM 2564 NH1 ARG A 377 36.374 53.245 25.292 1.00 98.90 N ANISOU 2564 NH1 ARG A 377 14856 15414 7307 1157 1294 3618 N ATOM 2565 NH2 ARG A 377 34.234 53.658 25.993 1.00109.36 N ANISOU 2565 NH2 ARG A 377 16120 16763 8669 1718 1038 3643 N ATOM 2566 N ALA A 378 34.002 46.977 27.926 1.00 95.12 N ANISOU 2566 N ALA A 378 12453 15820 7867 526 165 1448 N ATOM 2567 CA ALA A 378 32.768 46.688 28.641 1.00 95.52 C ANISOU 2567 CA ALA A 378 12294 15905 8093 618 -4 1288 C ATOM 2568 C ALA A 378 32.679 47.531 29.902 1.00 97.19 C ANISOU 2568 C ALA A 378 12719 15626 8584 585 130 1479 C ATOM 2569 O ALA A 378 31.869 48.451 29.973 1.00 97.65 O ANISOU 2569 O ALA A 378 12897 15652 8555 888 133 1709 O ATOM 2570 CB ALA A 378 32.690 45.197 28.973 1.00100.42 C ANISOU 2570 CB ALA A 378 12581 16644 8930 355 -146 841 C ATOM 2571 N PHE A 379 33.608 47.324 30.840 1.00 88.69 N ANISOU 2571 N PHE A 379 11726 14164 7808 240 260 1412 N ATOM 2572 CA PHE A 379 33.547 47.988 32.141 1.00 78.56 C ANISOU 2572 CA PHE A 379 10624 12426 6800 168 371 1525 C ATOM 2573 C PHE A 379 33.347 49.492 31.990 1.00 78.67 C ANISOU 2573 C PHE A 379 10994 12234 6663 430 510 1914 C ATOM 2574 O PHE A 379 32.489 50.086 32.656 1.00 69.96 O ANISOU 2574 O PHE A 379 9965 10972 5644 623 509 2005 O ATOM 2575 CB PHE A 379 34.823 47.707 32.942 1.00 68.98 C ANISOU 2575 CB PHE A 379 9492 10875 5842 -231 506 1446 C ATOM 2576 CG PHE A 379 34.976 46.275 33.393 1.00 59.52 C ANISOU 2576 CG PHE A 379 7992 9768 4855 -468 397 1087 C ATOM 2577 CD1 PHE A 379 34.096 45.288 32.978 1.00 63.09 C ANISOU 2577 CD1 PHE A 379 8137 10571 5264 -377 205 835 C ATOM 2578 CD2 PHE A 379 36.005 45.923 34.252 1.00 53.49 C ANISOU 2578 CD2 PHE A 379 7259 8733 4332 -785 491 1002 C ATOM 2579 CE1 PHE A 379 34.254 43.980 33.393 1.00 66.26 C ANISOU 2579 CE1 PHE A 379 8307 10997 5873 -603 133 516 C ATOM 2580 CE2 PHE A 379 36.160 44.618 34.677 1.00 53.71 C ANISOU 2580 CE2 PHE A 379 7044 8813 4548 -968 408 703 C ATOM 2581 CZ PHE A 379 35.283 43.646 34.249 1.00 60.09 C ANISOU 2581 CZ PHE A 379 7587 9918 5328 -880 241 464 C ATOM 2582 N SER A 380 34.108 50.121 31.089 1.00 89.78 N ANISOU 2582 N SER A 380 12634 13643 7837 460 644 2156 N ATOM 2583 CA SER A 380 33.973 51.567 30.905 1.00 87.38 C ANISOU 2583 CA SER A 380 12719 13092 7391 704 808 2551 C ATOM 2584 C SER A 380 32.582 51.938 30.394 1.00 91.33 C ANISOU 2584 C SER A 380 13162 13879 7660 1200 671 2673 C ATOM 2585 O SER A 380 31.911 52.819 30.958 1.00 95.11 O ANISOU 2585 O SER A 380 13835 14107 8196 1434 730 2853 O ATOM 2586 CB SER A 380 35.050 52.079 29.948 1.00 80.20 C ANISOU 2586 CB SER A 380 12050 12166 6258 626 990 2793 C ATOM 2587 OG SER A 380 34.846 51.588 28.636 1.00 76.62 O ANISOU 2587 OG SER A 380 11418 12233 5460 827 870 2772 O ATOM 2588 N ASN A 381 32.129 51.274 29.323 1.00 89.85 N ANISOU 2588 N ASN A 381 12701 14240 7197 1381 485 2565 N ATOM 2589 CA ASN A 381 30.838 51.615 28.732 1.00 95.26 C ANISOU 2589 CA ASN A 381 13291 15286 7616 1870 334 2681 C ATOM 2590 C ASN A 381 29.683 51.276 29.670 1.00 94.35 C ANISOU 2590 C ASN A 381 12910 15211 7726 1958 184 2480 C ATOM 2591 O ASN A 381 28.670 51.978 29.689 1.00 96.36 O ANISOU 2591 O ASN A 381 13201 15538 7875 2365 148 2661 O ATOM 2592 CB ASN A 381 30.672 50.905 27.388 1.00 97.83 C ANISOU 2592 CB ASN A 381 13358 16230 7584 2000 150 2561 C ATOM 2593 CG ASN A 381 31.602 51.453 26.319 1.00 97.82 C ANISOU 2593 CG ASN A 381 13644 16253 7270 2042 314 2844 C ATOM 2594 OD1 ASN A 381 32.004 52.616 26.367 1.00102.60 O ANISOU 2594 OD1 ASN A 381 14662 16483 7840 2129 546 3223 O ATOM 2595 ND2 ASN A 381 31.941 50.618 25.344 1.00 96.04 N ANISOU 2595 ND2 ASN A 381 13214 16465 6812 1974 209 2657 N ATOM 2596 N TYR A 382 29.806 50.188 30.432 1.00 88.90 N ANISOU 2596 N TYR A 382 11947 14494 7336 1600 105 2117 N ATOM 2597 CA TYR A 382 28.795 49.829 31.419 1.00 89.45 C ANISOU 2597 CA TYR A 382 11772 14568 7647 1626 1 1929 C ATOM 2598 C TYR A 382 28.715 50.867 32.526 1.00 91.67 C ANISOU 2598 C TYR A 382 12367 14336 8126 1697 185 2143 C ATOM 2599 O TYR A 382 27.618 51.246 32.952 1.00105.13 O ANISOU 2599 O TYR A 382 13997 16096 9853 1993 141 2193 O ATOM 2600 CB TYR A 382 29.104 48.458 32.018 1.00 76.61 C ANISOU 2600 CB TYR A 382 9854 12949 6305 1198 -77 1531 C ATOM 2601 CG TYR A 382 28.979 47.304 31.058 1.00 77.11 C ANISOU 2601 CG TYR A 382 9576 13510 6215 1124 -275 1243 C ATOM 2602 CD1 TYR A 382 28.267 47.429 29.871 1.00 85.98 C ANISOU 2602 CD1 TYR A 382 10559 15140 6970 1458 -434 1289 C ATOM 2603 CD2 TYR A 382 29.566 46.082 31.345 1.00 78.27 C ANISOU 2603 CD2 TYR A 382 9549 13619 6572 734 -305 916 C ATOM 2604 CE1 TYR A 382 28.152 46.367 28.998 1.00 93.98 C ANISOU 2604 CE1 TYR A 382 11267 16611 7829 1373 -622 987 C ATOM 2605 CE2 TYR A 382 29.456 45.021 30.482 1.00 85.98 C ANISOU 2605 CE2 TYR A 382 10245 15007 7415 660 -473 625 C ATOM 2606 CZ TYR A 382 28.749 45.166 29.311 1.00 95.07 C ANISOU 2606 CZ TYR A 382 11261 16661 8201 964 -634 646 C ATOM 2607 OH TYR A 382 28.642 44.101 28.453 1.00101.39 O ANISOU 2607 OH TYR A 382 11790 17877 8857 872 -807 319 O ATOM 2608 N LEU A 383 29.867 51.327 33.018 1.00 88.24 N ANISOU 2608 N LEU A 383 12274 13416 7838 1424 395 2251 N ATOM 2609 CA LEU A 383 29.864 52.327 34.079 1.00 86.59 C ANISOU 2609 CA LEU A 383 12397 12694 7811 1458 576 2421 C ATOM 2610 C LEU A 383 29.212 53.620 33.612 1.00 98.84 C ANISOU 2610 C LEU A 383 14236 14188 9132 1945 656 2782 C ATOM 2611 O LEU A 383 28.321 54.156 34.281 1.00108.25 O ANISOU 2611 O LEU A 383 15476 15258 10395 2214 677 2846 O ATOM 2612 CB LEU A 383 31.291 52.580 34.561 1.00 77.99 C ANISOU 2612 CB LEU A 383 11602 11144 6886 1045 771 2453 C ATOM 2613 CG LEU A 383 31.814 51.599 35.610 1.00 68.13 C ANISOU 2613 CG LEU A 383 10160 9775 5950 620 740 2139 C ATOM 2614 CD1 LEU A 383 33.329 51.597 35.633 1.00 61.33 C ANISOU 2614 CD1 LEU A 383 9470 8676 5158 225 876 2146 C ATOM 2615 CD2 LEU A 383 31.261 51.963 36.977 1.00 69.59 C ANISOU 2615 CD2 LEU A 383 10428 9645 6366 647 794 2103 C ATOM 2616 N ARG A 384 29.634 54.135 32.455 1.00 98.69 N ANISOU 2616 N ARG A 384 14417 14260 8820 2090 716 3034 N ATOM 2617 CA ARG A 384 29.097 55.426 32.027 1.00106.85 C ANISOU 2617 CA ARG A 384 15790 15177 9631 2571 825 3423 C ATOM 2618 C ARG A 384 27.669 55.313 31.494 1.00111.80 C ANISOU 2618 C ARG A 384 16113 16337 10030 3086 611 3440 C ATOM 2619 O ARG A 384 26.832 56.178 31.773 1.00118.15 O ANISOU 2619 O ARG A 384 17073 17025 10795 3506 664 3646 O ATOM 2620 CB ARG A 384 30.013 56.061 30.980 1.00112.81 C ANISOU 2620 CB ARG A 384 16887 15839 10136 2567 987 3727 C ATOM 2621 CG ARG A 384 30.276 55.195 29.772 1.00110.52 C ANISOU 2621 CG ARG A 384 16310 16102 9582 2523 832 3626 C ATOM 2622 CD ARG A 384 31.014 55.967 28.702 1.00109.57 C ANISOU 2622 CD ARG A 384 16549 15917 9164 2612 1015 3989 C ATOM 2623 NE ARG A 384 31.009 55.246 27.437 1.00116.03 N ANISOU 2623 NE ARG A 384 17096 17345 9644 2707 849 3921 N ATOM 2624 CZ ARG A 384 29.968 55.182 26.619 1.00138.86 C ANISOU 2624 CZ ARG A 384 19772 20730 12259 3143 644 3938 C ATOM 2625 NH1 ARG A 384 28.825 55.787 26.904 1.00134.63 N ANISOU 2625 NH1 ARG A 384 19241 20187 11727 3559 584 4051 N ATOM 2626 NH2 ARG A 384 30.072 54.489 25.488 1.00150.45 N ANISOU 2626 NH2 ARG A 384 20990 22708 13468 3149 494 3803 N ATOM 2627 N CYS A 385 27.372 54.255 30.737 1.00110.35 N ANISOU 2627 N CYS A 385 15488 16747 9692 3065 370 3212 N ATOM 2628 CA CYS A 385 26.078 54.130 30.072 1.00117.64 C ANISOU 2628 CA CYS A 385 16086 18263 10351 3533 144 3216 C ATOM 2629 C CYS A 385 24.956 53.845 31.064 1.00129.11 C ANISOU 2629 C CYS A 385 17228 19800 12028 3632 39 3020 C ATOM 2630 O CYS A 385 23.857 54.397 30.937 1.00142.78 O ANISOU 2630 O CYS A 385 18883 21764 13605 4130 -26 3175 O ATOM 2631 CB CYS A 385 26.153 53.030 29.011 1.00110.70 C ANISOU 2631 CB CYS A 385 14828 17983 9251 3414 -83 2974 C ATOM 2632 SG CYS A 385 24.561 52.438 28.388 1.00123.62 S ANISOU 2632 SG CYS A 385 15889 20441 10639 3808 -434 2789 S ATOM 2633 N ASN A 386 25.208 52.983 32.052 1.00121.40 N ANISOU 2633 N ASN A 386 16061 18659 11405 3181 30 2692 N ATOM 2634 CA ASN A 386 24.155 52.603 32.989 1.00124.34 C ANISOU 2634 CA ASN A 386 16107 19146 11991 3234 -57 2492 C ATOM 2635 C ASN A 386 23.850 53.698 34.003 1.00133.06 C ANISOU 2635 C ASN A 386 17540 19776 13241 3463 145 2707 C ATOM 2636 O ASN A 386 22.697 53.838 34.425 1.00141.04 O ANISOU 2636 O ASN A 386 18333 20982 14274 3776 87 2694 O ATOM 2637 CB ASN A 386 24.533 51.309 33.713 1.00126.51 C ANISOU 2637 CB ASN A 386 16102 19383 12582 2689 -113 2096 C ATOM 2638 CG ASN A 386 24.252 50.072 32.881 1.00123.61 C ANISOU 2638 CG ASN A 386 15270 19593 12104 2550 -361 1795 C ATOM 2639 OD1 ASN A 386 24.205 50.131 31.652 1.00117.47 O ANISOU 2639 OD1 ASN A 386 14445 19195 10994 2753 -476 1870 O ATOM 2640 ND2 ASN A 386 24.052 48.943 33.551 1.00136.77 N ANISOU 2640 ND2 ASN A 386 16606 21322 14040 2204 -438 1448 N ATOM 2641 N TYR A 387 24.850 54.474 34.410 1.00137.47 N ANISOU 2641 N TYR A 387 18606 19729 13899 3308 384 2889 N ATOM 2642 CA TYR A 387 24.628 55.545 35.376 1.00139.08 C ANISOU 2642 CA TYR A 387 19174 19432 14237 3505 591 3067 C ATOM 2643 C TYR A 387 25.379 56.819 35.001 1.00145.45 C ANISOU 2643 C TYR A 387 20586 19760 14917 3630 823 3433 C ATOM 2644 O TYR A 387 24.941 57.924 35.327 1.00155.96 O ANISOU 2644 O TYR A 387 22255 20779 16224 4001 977 3674 O ATOM 2645 CB TYR A 387 25.036 55.096 36.781 1.00139.48 C ANISOU 2645 CB TYR A 387 19220 19119 14657 3066 673 2814 C ATOM 2646 CG TYR A 387 23.907 54.480 37.577 1.00144.41 C ANISOU 2646 CG TYR A 387 19424 20013 15431 3150 565 2590 C ATOM 2647 CD1 TYR A 387 22.801 55.237 37.944 1.00138.43 C ANISOU 2647 CD1 TYR A 387 18689 19281 14629 3638 613 2730 C ATOM 2648 CD2 TYR A 387 23.950 53.149 37.971 1.00146.93 C ANISOU 2648 CD2 TYR A 387 19335 20552 15940 2748 436 2249 C ATOM 2649 CE1 TYR A 387 21.766 54.684 38.672 1.00131.98 C ANISOU 2649 CE1 TYR A 387 17463 18737 13945 3706 535 2533 C ATOM 2650 CE2 TYR A 387 22.919 52.587 38.702 1.00140.14 C ANISOU 2650 CE2 TYR A 387 18094 19930 15223 2796 364 2060 C ATOM 2651 CZ TYR A 387 21.830 53.360 39.050 1.00132.52 C ANISOU 2651 CZ TYR A 387 17127 19020 14205 3266 415 2202 C ATOM 2652 OH TYR A 387 20.800 52.810 39.777 1.00129.04 O ANISOU 2652 OH TYR A 387 16282 18843 13903 3307 363 2020 O TER 2653 TYR A 387 HETATM 2654 C1 A1L A1201 37.779 29.638 53.715 1.00 46.97 C HETATM 2655 C2 A1L A1201 37.609 30.116 57.076 1.00 47.96 C HETATM 2656 C3 A1L A1201 38.497 31.676 55.324 1.00 44.77 C HETATM 2657 C4 A1L A1201 38.397 32.743 56.412 1.00 43.60 C HETATM 2658 C5 A1L A1201 37.423 31.274 58.043 1.00 46.46 C HETATM 2659 C6 A1L A1201 38.468 29.288 52.411 1.00 42.43 C HETATM 2660 N1 A1L A1201 37.228 32.508 57.275 1.00 46.26 N HETATM 2661 N2 A1L A1201 39.037 27.092 54.287 1.00 45.53 N HETATM 2662 O1 A1L A1201 35.716 22.591 57.041 1.00 61.94 O HETATM 2663 C7 A1L A1201 39.303 28.156 55.038 1.00 48.33 C HETATM 2664 C8 A1L A1201 39.653 25.814 54.582 1.00 52.46 C HETATM 2665 C9 A1L A1201 38.611 24.948 55.245 1.00 54.58 C HETATM 2666 C10 A1L A1201 38.658 24.730 56.617 1.00 54.66 C HETATM 2667 C11 A1L A1201 37.691 23.938 57.227 1.00 58.27 C HETATM 2668 C12 A1L A1201 36.679 23.373 56.459 1.00 62.29 C HETATM 2669 C13 A1L A1201 36.633 23.598 55.088 1.00 60.29 C HETATM 2670 C14 A1L A1201 37.598 24.388 54.478 1.00 57.09 C HETATM 2671 C15 A1L A1201 34.934 21.741 56.207 1.00 60.50 C HETATM 2672 N A1L A1201 38.600 29.279 54.875 1.00 46.96 N HETATM 2673 C A1L A1201 38.628 30.289 55.942 1.00 47.19 C HETATM 2674 O A1L A1201 40.172 28.091 55.891 1.00 55.69 O HETATM 2675 C16 A1L A1201 34.960 20.320 56.750 1.00 57.95 C HETATM 2676 C17 A1L A1201 34.803 19.319 55.612 1.00 51.32 C HETATM 2677 C18 A1L A1201 33.859 20.131 57.785 1.00 67.16 C HETATM 2678 C19 A1L A1201 37.521 28.744 57.729 1.00 48.51 C HETATM 2679 C20 A1L A1201 36.384 29.248 56.844 1.00 44.66 C HETATM 2680 C21 A1L A1201 37.913 28.324 51.576 1.00 42.92 C HETATM 2681 C22 A1L A1201 38.536 27.988 50.380 1.00 44.52 C HETATM 2682 C23 A1L A1201 39.721 28.612 50.019 1.00 44.85 C HETATM 2683 C24 A1L A1201 40.280 29.572 50.853 1.00 45.53 C HETATM 2684 C25 A1L A1201 39.657 29.908 52.051 1.00 45.08 C HETATM 2685 C26 A1L A1201 37.072 33.621 58.220 1.00 50.63 C HETATM 2686 F A1L A1201 40.328 28.288 48.863 1.00 46.75 F END